data_6R6F
# 
_entry.id   6R6F 
# 
_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   6R6F         pdb_00006r6f 10.2210/pdb6r6f/pdb 
WWPDB D_1292101504 ?            ?                   
# 
loop_
_pdbx_audit_revision_history.ordinal 
_pdbx_audit_revision_history.data_content_type 
_pdbx_audit_revision_history.major_revision 
_pdbx_audit_revision_history.minor_revision 
_pdbx_audit_revision_history.revision_date 
1 'Structure model' 1 0 2019-12-18 
2 'Structure model' 1 1 2020-03-25 
3 'Structure model' 1 2 2020-04-01 
4 'Structure model' 1 3 2021-10-06 
5 'Structure model' 1 4 2024-01-24 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
loop_
_pdbx_audit_revision_group.ordinal 
_pdbx_audit_revision_group.revision_ordinal 
_pdbx_audit_revision_group.data_content_type 
_pdbx_audit_revision_group.group 
1 2 'Structure model' 'Database references'    
2 3 'Structure model' 'Database references'    
3 4 'Structure model' 'Data collection'        
4 4 'Structure model' 'Database references'    
5 4 'Structure model' 'Structure summary'      
6 5 'Structure model' 'Data collection'        
7 5 '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' citation                      
2 2 'Structure model' citation_author               
3 3 'Structure model' citation                      
4 4 'Structure model' database_2                    
5 4 'Structure model' pdbx_contact_author           
6 4 'Structure model' pdbx_database_proc            
7 5 'Structure model' chem_comp_atom                
8 5 'Structure model' chem_comp_bond                
9 5 'Structure model' pdbx_initial_refinement_model 
# 
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' '_citation.journal_id_ISSN'           
2  2 'Structure model' '_citation.journal_volume'            
3  2 'Structure model' '_citation.page_first'                
4  2 'Structure model' '_citation.page_last'                 
5  2 'Structure model' '_citation.pdbx_database_id_DOI'      
6  2 'Structure model' '_citation.pdbx_database_id_PubMed'   
7  2 'Structure model' '_citation.title'                     
8  2 'Structure model' '_citation.year'                      
9  3 'Structure model' '_citation.journal_id_ISSN'           
10 3 'Structure model' '_citation.page_first'                
11 3 'Structure model' '_citation.page_last'                 
12 3 'Structure model' '_citation.title'                     
13 4 'Structure model' '_database_2.pdbx_DOI'                
14 4 'Structure model' '_database_2.pdbx_database_accession' 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        6R6F 
_pdbx_database_status.recvd_initial_deposition_date   2019-03-27 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBE 
_pdbx_database_status.process_site                    PDBE 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
_pdbx_database_status.status_code_nmr_data            ? 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Smirnov, A.'  1 ? 
'Manakova, E.' 2 ? 
'Grazulis, S.' 3 ? 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   FR 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            Eur.J.Med.Chem. 
_citation.journal_id_ASTM           EJMCA5 
_citation.journal_id_CSD            0493 
_citation.journal_id_ISSN           0223-5234 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            185 
_citation.language                  ? 
_citation.page_first                111825 
_citation.page_last                 111825 
_citation.title                     
'Halogenated and di-substituted benzenesulfonamides as selective inhibitors of carbonic anhydrase isoforms.' 
_citation.year                      2020 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1016/j.ejmech.2019.111825 
_citation.pdbx_database_id_PubMed   31740053 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Zaksauskas, A.'   1  ? 
primary 'Capkauskaite, E.' 2  ? 
primary 'Jezepcikas, L.'   3  ? 
primary 'Linkuviene, V.'   4  ? 
primary 'Paketuryte, V.'   5  ? 
primary 'Smirnov, A.'      6  ? 
primary 'Leitans, J.'      7  ? 
primary 'Kazaks, A.'       8  ? 
primary 'Dvinskis, E.'     9  ? 
primary 'Manakova, E.'     10 ? 
primary 'Grazulis, S.'     11 ? 
primary 'Tars, K.'         12 ? 
primary 'Matulis, D.'      13 ? 
# 
loop_
_entity.id 
_entity.type 
_entity.src_method 
_entity.pdbx_description 
_entity.formula_weight 
_entity.pdbx_number_of_molecules 
_entity.pdbx_ec 
_entity.pdbx_mutation 
_entity.pdbx_fragment 
_entity.details 
1 polymer     man 'Carbonic anhydrase 2'                                                         29289.062 1   4.2.1.1 ? 
'human carbonic anhydrase II' ? 
2 non-polymer syn 'ZINC ION'                                                                     65.409    1   ?       
'4-chloro-2-cyclohexylsulfanyl-N-(2-hydroxyethyl)-5-sulfamoyl-benzamide' ?                             ? 
3 non-polymer syn '4-chloranyl-2-cyclohexylsulfanyl-~{N}-(2-hydroxyethyl)-5-sulfamoyl-benzamide' 392.921   1   ?       ? Zn ? 
4 non-polymer syn 'DIMETHYL SULFOXIDE'                                                           78.133    1   ?       ? 
'Dimethyl sulfoxide'          ? 
5 water       nat water                                                                          18.015    340 ?       ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'Carbonate dehydratase II,Carbonic anhydrase C,CAC,Carbonic anhydrase II,CA-II' 
# 
_entity_poly.entity_id                      1 
_entity_poly.type                           'polypeptide(L)' 
_entity_poly.nstd_linkage                   no 
_entity_poly.nstd_monomer                   no 
_entity_poly.pdbx_seq_one_letter_code       
;MSHHWGYGKHNGPEHWHKDFPIAKGERQSPVDIDTHTAKYDPSLKPLSVSYDQATSLRILNNGHAFNVEFDDSQDKAVLK
GGPLDGTYRLIQFHFHWGSLDGQGSEHTVDKKKYAAELHLVHWNTKYGDFGKAVQQPDGLAVLGIFLKVGSAKPGLQKVV
DVLDSIKTKGKSADFTNFDPRGLLPESLDYWTYPGSLTTPPLLECVTWIVLKEPISVSSEQVLKFRKLNFNGEGEPEELM
VDNWRPAQPLKNRQIKASFK
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MSHHWGYGKHNGPEHWHKDFPIAKGERQSPVDIDTHTAKYDPSLKPLSVSYDQATSLRILNNGHAFNVEFDDSQDKAVLK
GGPLDGTYRLIQFHFHWGSLDGQGSEHTVDKKKYAAELHLVHWNTKYGDFGKAVQQPDGLAVLGIFLKVGSAKPGLQKVV
DVLDSIKTKGKSADFTNFDPRGLLPESLDYWTYPGSLTTPPLLECVTWIVLKEPISVSSEQVLKFRKLNFNGEGEPEELM
VDNWRPAQPLKNRQIKASFK
;
_entity_poly.pdbx_strand_id                 A 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 'ZINC ION'                                                                     ZN  
3 '4-chloranyl-2-cyclohexylsulfanyl-~{N}-(2-hydroxyethyl)-5-sulfamoyl-benzamide' EA3 
4 'DIMETHYL SULFOXIDE'                                                           DMS 
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   HIS n 
1 4   HIS n 
1 5   TRP n 
1 6   GLY n 
1 7   TYR n 
1 8   GLY n 
1 9   LYS n 
1 10  HIS n 
1 11  ASN n 
1 12  GLY n 
1 13  PRO n 
1 14  GLU n 
1 15  HIS n 
1 16  TRP n 
1 17  HIS n 
1 18  LYS n 
1 19  ASP n 
1 20  PHE n 
1 21  PRO n 
1 22  ILE n 
1 23  ALA n 
1 24  LYS n 
1 25  GLY n 
1 26  GLU n 
1 27  ARG n 
1 28  GLN n 
1 29  SER n 
1 30  PRO n 
1 31  VAL n 
1 32  ASP n 
1 33  ILE n 
1 34  ASP n 
1 35  THR n 
1 36  HIS n 
1 37  THR n 
1 38  ALA n 
1 39  LYS n 
1 40  TYR n 
1 41  ASP n 
1 42  PRO n 
1 43  SER n 
1 44  LEU n 
1 45  LYS n 
1 46  PRO n 
1 47  LEU n 
1 48  SER n 
1 49  VAL n 
1 50  SER n 
1 51  TYR n 
1 52  ASP n 
1 53  GLN n 
1 54  ALA n 
1 55  THR n 
1 56  SER n 
1 57  LEU n 
1 58  ARG n 
1 59  ILE n 
1 60  LEU n 
1 61  ASN n 
1 62  ASN n 
1 63  GLY n 
1 64  HIS n 
1 65  ALA n 
1 66  PHE n 
1 67  ASN n 
1 68  VAL n 
1 69  GLU n 
1 70  PHE n 
1 71  ASP n 
1 72  ASP n 
1 73  SER n 
1 74  GLN n 
1 75  ASP n 
1 76  LYS n 
1 77  ALA n 
1 78  VAL n 
1 79  LEU n 
1 80  LYS n 
1 81  GLY n 
1 82  GLY n 
1 83  PRO n 
1 84  LEU n 
1 85  ASP n 
1 86  GLY n 
1 87  THR n 
1 88  TYR n 
1 89  ARG n 
1 90  LEU n 
1 91  ILE n 
1 92  GLN n 
1 93  PHE n 
1 94  HIS n 
1 95  PHE n 
1 96  HIS n 
1 97  TRP n 
1 98  GLY n 
1 99  SER n 
1 100 LEU n 
1 101 ASP n 
1 102 GLY n 
1 103 GLN n 
1 104 GLY n 
1 105 SER n 
1 106 GLU n 
1 107 HIS n 
1 108 THR n 
1 109 VAL n 
1 110 ASP n 
1 111 LYS n 
1 112 LYS n 
1 113 LYS n 
1 114 TYR n 
1 115 ALA n 
1 116 ALA n 
1 117 GLU n 
1 118 LEU n 
1 119 HIS n 
1 120 LEU n 
1 121 VAL n 
1 122 HIS n 
1 123 TRP n 
1 124 ASN n 
1 125 THR n 
1 126 LYS n 
1 127 TYR n 
1 128 GLY n 
1 129 ASP n 
1 130 PHE n 
1 131 GLY n 
1 132 LYS n 
1 133 ALA n 
1 134 VAL n 
1 135 GLN n 
1 136 GLN n 
1 137 PRO n 
1 138 ASP n 
1 139 GLY n 
1 140 LEU n 
1 141 ALA n 
1 142 VAL n 
1 143 LEU n 
1 144 GLY n 
1 145 ILE n 
1 146 PHE n 
1 147 LEU n 
1 148 LYS n 
1 149 VAL n 
1 150 GLY n 
1 151 SER n 
1 152 ALA n 
1 153 LYS n 
1 154 PRO n 
1 155 GLY n 
1 156 LEU n 
1 157 GLN n 
1 158 LYS n 
1 159 VAL n 
1 160 VAL n 
1 161 ASP n 
1 162 VAL n 
1 163 LEU n 
1 164 ASP n 
1 165 SER n 
1 166 ILE n 
1 167 LYS n 
1 168 THR n 
1 169 LYS n 
1 170 GLY n 
1 171 LYS n 
1 172 SER n 
1 173 ALA n 
1 174 ASP n 
1 175 PHE n 
1 176 THR n 
1 177 ASN n 
1 178 PHE n 
1 179 ASP n 
1 180 PRO n 
1 181 ARG n 
1 182 GLY n 
1 183 LEU n 
1 184 LEU n 
1 185 PRO n 
1 186 GLU n 
1 187 SER n 
1 188 LEU n 
1 189 ASP n 
1 190 TYR n 
1 191 TRP n 
1 192 THR n 
1 193 TYR n 
1 194 PRO n 
1 195 GLY n 
1 196 SER n 
1 197 LEU n 
1 198 THR n 
1 199 THR n 
1 200 PRO n 
1 201 PRO n 
1 202 LEU n 
1 203 LEU n 
1 204 GLU n 
1 205 CYS n 
1 206 VAL n 
1 207 THR n 
1 208 TRP n 
1 209 ILE n 
1 210 VAL n 
1 211 LEU n 
1 212 LYS n 
1 213 GLU n 
1 214 PRO n 
1 215 ILE n 
1 216 SER n 
1 217 VAL n 
1 218 SER n 
1 219 SER n 
1 220 GLU n 
1 221 GLN n 
1 222 VAL n 
1 223 LEU n 
1 224 LYS n 
1 225 PHE n 
1 226 ARG n 
1 227 LYS n 
1 228 LEU n 
1 229 ASN n 
1 230 PHE n 
1 231 ASN n 
1 232 GLY n 
1 233 GLU n 
1 234 GLY n 
1 235 GLU n 
1 236 PRO n 
1 237 GLU n 
1 238 GLU n 
1 239 LEU n 
1 240 MET n 
1 241 VAL n 
1 242 ASP n 
1 243 ASN n 
1 244 TRP n 
1 245 ARG n 
1 246 PRO n 
1 247 ALA n 
1 248 GLN n 
1 249 PRO n 
1 250 LEU n 
1 251 LYS n 
1 252 ASN n 
1 253 ARG n 
1 254 GLN n 
1 255 ILE n 
1 256 LYS n 
1 257 ALA n 
1 258 SER n 
1 259 PHE n 
1 260 LYS n 
# 
_entity_src_gen.entity_id                          1 
_entity_src_gen.pdbx_src_id                        1 
_entity_src_gen.pdbx_alt_source_flag               sample 
_entity_src_gen.pdbx_seq_type                      'Biological sequence' 
_entity_src_gen.pdbx_beg_seq_num                   1 
_entity_src_gen.pdbx_end_seq_num                   260 
_entity_src_gen.gene_src_common_name               Human 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 CA2 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    ? 
_entity_src_gen.gene_src_tissue                    ? 
_entity_src_gen.gene_src_tissue_fraction           ? 
_entity_src_gen.gene_src_details                   ? 
_entity_src_gen.pdbx_gene_src_fragment             ? 
_entity_src_gen.pdbx_gene_src_scientific_name      'Homo sapiens' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     9606 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     469008 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               'BL21(DE3)' 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          plasmid 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       pET15b 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
ALA 'L-peptide linking' y ALANINE                                                                        ? 'C3 H7 N O2'          
89.093  
ARG 'L-peptide linking' y ARGININE                                                                       ? 'C6 H15 N4 O2 1'      
175.209 
ASN 'L-peptide linking' y ASPARAGINE                                                                     ? 'C4 H8 N2 O3'         
132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID'                                                                ? 'C4 H7 N O4'          
133.103 
CYS 'L-peptide linking' y CYSTEINE                                                                       ? 'C3 H7 N O2 S'        
121.158 
DMS non-polymer         . 'DIMETHYL SULFOXIDE'                                                           ? 'C2 H6 O S'           
78.133  
EA3 non-polymer         . '4-chloranyl-2-cyclohexylsulfanyl-~{N}-(2-hydroxyethyl)-5-sulfamoyl-benzamide' ? 'C15 H21 Cl N2 O4 S2' 
392.921 
GLN 'L-peptide linking' y GLUTAMINE                                                                      ? 'C5 H10 N2 O3'        
146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID'                                                                ? 'C5 H9 N O4'          
147.129 
GLY 'peptide linking'   y GLYCINE                                                                        ? 'C2 H5 N O2'          
75.067  
HIS 'L-peptide linking' y HISTIDINE                                                                      ? 'C6 H10 N3 O2 1'      
156.162 
HOH non-polymer         . WATER                                                                          ? 'H2 O'                
18.015  
ILE 'L-peptide linking' y ISOLEUCINE                                                                     ? 'C6 H13 N O2'         
131.173 
LEU 'L-peptide linking' y LEUCINE                                                                        ? 'C6 H13 N O2'         
131.173 
LYS 'L-peptide linking' y LYSINE                                                                         ? 'C6 H15 N2 O2 1'      
147.195 
MET 'L-peptide linking' y METHIONINE                                                                     ? 'C5 H11 N O2 S'       
149.211 
PHE 'L-peptide linking' y PHENYLALANINE                                                                  ? 'C9 H11 N O2'         
165.189 
PRO 'L-peptide linking' y PROLINE                                                                        ? 'C5 H9 N O2'          
115.130 
SER 'L-peptide linking' y SERINE                                                                         ? 'C3 H7 N O3'          
105.093 
THR 'L-peptide linking' y THREONINE                                                                      ? 'C4 H9 N O3'          
119.119 
TRP 'L-peptide linking' y TRYPTOPHAN                                                                     ? 'C11 H12 N2 O2'       
204.225 
TYR 'L-peptide linking' y TYROSINE                                                                       ? 'C9 H11 N O3'         
181.189 
VAL 'L-peptide linking' y VALINE                                                                         ? 'C5 H11 N O2'         
117.146 
ZN  non-polymer         . 'ZINC ION'                                                                     ? 'Zn 2'                
65.409  
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   MET 1   1   ?   ?   ?   A . n 
A 1 2   SER 2   2   ?   ?   ?   A . n 
A 1 3   HIS 3   3   3   HIS HIS A . n 
A 1 4   HIS 4   4   4   HIS HIS A . n 
A 1 5   TRP 5   5   5   TRP TRP A . n 
A 1 6   GLY 6   6   6   GLY GLY A . n 
A 1 7   TYR 7   7   7   TYR TYR A . n 
A 1 8   GLY 8   8   8   GLY GLY A . n 
A 1 9   LYS 9   9   9   LYS LYS A . n 
A 1 10  HIS 10  10  10  HIS HIS A . n 
A 1 11  ASN 11  11  11  ASN ASN A . n 
A 1 12  GLY 12  12  12  GLY GLY A . n 
A 1 13  PRO 13  13  13  PRO PRO A . n 
A 1 14  GLU 14  14  14  GLU GLU A . n 
A 1 15  HIS 15  15  15  HIS HIS A . n 
A 1 16  TRP 16  16  16  TRP TRP A . n 
A 1 17  HIS 17  17  17  HIS HIS A . n 
A 1 18  LYS 18  18  18  LYS LYS A . n 
A 1 19  ASP 19  19  19  ASP ASP A . n 
A 1 20  PHE 20  20  20  PHE PHE A . n 
A 1 21  PRO 21  21  21  PRO PRO A . n 
A 1 22  ILE 22  22  22  ILE ILE A . n 
A 1 23  ALA 23  23  23  ALA ALA A . n 
A 1 24  LYS 24  24  24  LYS LYS A . n 
A 1 25  GLY 25  25  25  GLY GLY A . n 
A 1 26  GLU 26  26  26  GLU GLU A . n 
A 1 27  ARG 27  27  27  ARG ARG A . n 
A 1 28  GLN 28  28  28  GLN GLN A . n 
A 1 29  SER 29  29  29  SER SER A . n 
A 1 30  PRO 30  30  30  PRO PRO A . n 
A 1 31  VAL 31  31  31  VAL VAL A . n 
A 1 32  ASP 32  32  32  ASP ASP A . n 
A 1 33  ILE 33  33  33  ILE ILE A . n 
A 1 34  ASP 34  34  34  ASP ASP A . n 
A 1 35  THR 35  35  35  THR THR A . n 
A 1 36  HIS 36  36  36  HIS HIS A . n 
A 1 37  THR 37  37  37  THR THR A . n 
A 1 38  ALA 38  38  38  ALA ALA A . n 
A 1 39  LYS 39  39  39  LYS LYS A . n 
A 1 40  TYR 40  40  40  TYR TYR A . n 
A 1 41  ASP 41  41  41  ASP ASP A . n 
A 1 42  PRO 42  42  42  PRO PRO A . n 
A 1 43  SER 43  43  43  SER SER A . n 
A 1 44  LEU 44  44  44  LEU LEU A . n 
A 1 45  LYS 45  45  45  LYS LYS A . n 
A 1 46  PRO 46  46  46  PRO PRO A . n 
A 1 47  LEU 47  47  47  LEU LEU A . n 
A 1 48  SER 48  48  48  SER SER A . n 
A 1 49  VAL 49  49  49  VAL VAL A . n 
A 1 50  SER 50  50  50  SER SER A . n 
A 1 51  TYR 51  51  51  TYR TYR A . n 
A 1 52  ASP 52  52  52  ASP ASP A . n 
A 1 53  GLN 53  53  53  GLN GLN A . n 
A 1 54  ALA 54  54  54  ALA ALA A . n 
A 1 55  THR 55  55  55  THR THR A . n 
A 1 56  SER 56  56  56  SER SER A . n 
A 1 57  LEU 57  57  57  LEU LEU A . n 
A 1 58  ARG 58  58  58  ARG ARG A . n 
A 1 59  ILE 59  59  59  ILE ILE A . n 
A 1 60  LEU 60  60  60  LEU LEU A . n 
A 1 61  ASN 61  61  61  ASN ASN A . n 
A 1 62  ASN 62  62  62  ASN ASN A . n 
A 1 63  GLY 63  63  63  GLY GLY A . n 
A 1 64  HIS 64  64  64  HIS HIS A . n 
A 1 65  ALA 65  65  65  ALA ALA A . n 
A 1 66  PHE 66  66  66  PHE PHE A . n 
A 1 67  ASN 67  67  67  ASN ASN A . n 
A 1 68  VAL 68  68  68  VAL VAL A . n 
A 1 69  GLU 69  69  69  GLU GLU A . n 
A 1 70  PHE 70  70  70  PHE PHE A . n 
A 1 71  ASP 71  71  71  ASP ASP A . n 
A 1 72  ASP 72  72  72  ASP ASP A . n 
A 1 73  SER 73  73  73  SER SER A . n 
A 1 74  GLN 74  74  74  GLN GLN A . n 
A 1 75  ASP 75  75  75  ASP ASP A . n 
A 1 76  LYS 76  76  76  LYS LYS A . n 
A 1 77  ALA 77  77  77  ALA ALA A . n 
A 1 78  VAL 78  78  78  VAL VAL A . n 
A 1 79  LEU 79  79  79  LEU LEU A . n 
A 1 80  LYS 80  80  80  LYS LYS A . n 
A 1 81  GLY 81  81  81  GLY GLY A . n 
A 1 82  GLY 82  82  82  GLY GLY A . n 
A 1 83  PRO 83  83  83  PRO PRO A . n 
A 1 84  LEU 84  84  84  LEU LEU A . n 
A 1 85  ASP 85  85  85  ASP ASP A . n 
A 1 86  GLY 86  86  86  GLY GLY A . n 
A 1 87  THR 87  87  87  THR THR A . n 
A 1 88  TYR 88  88  88  TYR TYR A . n 
A 1 89  ARG 89  89  89  ARG ARG A . n 
A 1 90  LEU 90  90  90  LEU LEU A . n 
A 1 91  ILE 91  91  91  ILE ILE A . n 
A 1 92  GLN 92  92  92  GLN GLN A . n 
A 1 93  PHE 93  93  93  PHE PHE A . n 
A 1 94  HIS 94  94  94  HIS HIS A . n 
A 1 95  PHE 95  95  95  PHE PHE A . n 
A 1 96  HIS 96  96  96  HIS HIS A . n 
A 1 97  TRP 97  97  97  TRP TRP A . n 
A 1 98  GLY 98  98  98  GLY GLY A . n 
A 1 99  SER 99  99  99  SER SER A . n 
A 1 100 LEU 100 100 100 LEU LEU A . n 
A 1 101 ASP 101 101 101 ASP ASP A . n 
A 1 102 GLY 102 102 102 GLY GLY A . n 
A 1 103 GLN 103 103 103 GLN GLN A . n 
A 1 104 GLY 104 104 104 GLY GLY A . n 
A 1 105 SER 105 105 105 SER SER A . n 
A 1 106 GLU 106 106 106 GLU GLU A . n 
A 1 107 HIS 107 107 107 HIS HIS A . n 
A 1 108 THR 108 108 108 THR THR A . n 
A 1 109 VAL 109 109 109 VAL VAL A . n 
A 1 110 ASP 110 110 110 ASP ASP A . n 
A 1 111 LYS 111 111 111 LYS LYS A . n 
A 1 112 LYS 112 112 112 LYS LYS A . n 
A 1 113 LYS 113 113 113 LYS LYS A . n 
A 1 114 TYR 114 114 114 TYR TYR A . n 
A 1 115 ALA 115 115 115 ALA ALA A . n 
A 1 116 ALA 116 116 116 ALA ALA A . n 
A 1 117 GLU 117 117 117 GLU GLU A . n 
A 1 118 LEU 118 118 118 LEU LEU A . n 
A 1 119 HIS 119 119 119 HIS HIS A . n 
A 1 120 LEU 120 120 120 LEU LEU A . n 
A 1 121 VAL 121 121 121 VAL VAL A . n 
A 1 122 HIS 122 122 122 HIS HIS A . n 
A 1 123 TRP 123 123 123 TRP TRP A . n 
A 1 124 ASN 124 124 124 ASN ASN A . n 
A 1 125 THR 125 125 125 THR THR A . n 
A 1 126 LYS 126 127 127 LYS LYS A . n 
A 1 127 TYR 127 128 128 TYR TYR A . n 
A 1 128 GLY 128 129 129 GLY GLY A . n 
A 1 129 ASP 129 130 130 ASP ASP A . n 
A 1 130 PHE 130 131 131 PHE PHE A . n 
A 1 131 GLY 131 132 132 GLY GLY A . n 
A 1 132 LYS 132 133 133 LYS LYS A . n 
A 1 133 ALA 133 134 134 ALA ALA A . n 
A 1 134 VAL 134 135 135 VAL VAL A . n 
A 1 135 GLN 135 136 136 GLN GLN A . n 
A 1 136 GLN 136 137 137 GLN GLN A . n 
A 1 137 PRO 137 138 138 PRO PRO A . n 
A 1 138 ASP 138 139 139 ASP ASP A . n 
A 1 139 GLY 139 140 140 GLY GLY A . n 
A 1 140 LEU 140 141 141 LEU LEU A . n 
A 1 141 ALA 141 142 142 ALA ALA A . n 
A 1 142 VAL 142 143 143 VAL VAL A . n 
A 1 143 LEU 143 144 144 LEU LEU A . n 
A 1 144 GLY 144 145 145 GLY GLY A . n 
A 1 145 ILE 145 146 146 ILE ILE A . n 
A 1 146 PHE 146 147 147 PHE PHE A . n 
A 1 147 LEU 147 148 148 LEU LEU A . n 
A 1 148 LYS 148 149 149 LYS LYS A . n 
A 1 149 VAL 149 150 150 VAL VAL A . n 
A 1 150 GLY 150 151 151 GLY GLY A . n 
A 1 151 SER 151 152 152 SER SER A . n 
A 1 152 ALA 152 153 153 ALA ALA A . n 
A 1 153 LYS 153 154 154 LYS LYS A . n 
A 1 154 PRO 154 155 155 PRO PRO A . n 
A 1 155 GLY 155 156 156 GLY GLY A . n 
A 1 156 LEU 156 157 157 LEU LEU A . n 
A 1 157 GLN 157 158 158 GLN GLN A . n 
A 1 158 LYS 158 159 159 LYS LYS A . n 
A 1 159 VAL 159 160 160 VAL VAL A . n 
A 1 160 VAL 160 161 161 VAL VAL A . n 
A 1 161 ASP 161 162 162 ASP ASP A . n 
A 1 162 VAL 162 163 163 VAL VAL A . n 
A 1 163 LEU 163 164 164 LEU LEU A . n 
A 1 164 ASP 164 165 165 ASP ASP A . n 
A 1 165 SER 165 166 166 SER SER A . n 
A 1 166 ILE 166 167 167 ILE ILE A . n 
A 1 167 LYS 167 168 168 LYS LYS A . n 
A 1 168 THR 168 169 169 THR THR A . n 
A 1 169 LYS 169 170 170 LYS LYS A . n 
A 1 170 GLY 170 171 171 GLY GLY A . n 
A 1 171 LYS 171 172 172 LYS LYS A . n 
A 1 172 SER 172 173 173 SER SER A . n 
A 1 173 ALA 173 174 174 ALA ALA A . n 
A 1 174 ASP 174 175 175 ASP ASP A . n 
A 1 175 PHE 175 176 176 PHE PHE A . n 
A 1 176 THR 176 177 177 THR THR A . n 
A 1 177 ASN 177 178 178 ASN ASN A . n 
A 1 178 PHE 178 179 179 PHE PHE A . n 
A 1 179 ASP 179 180 180 ASP ASP A . n 
A 1 180 PRO 180 181 181 PRO PRO A . n 
A 1 181 ARG 181 182 182 ARG ARG A . n 
A 1 182 GLY 182 183 183 GLY GLY A . n 
A 1 183 LEU 183 184 184 LEU LEU A . n 
A 1 184 LEU 184 185 185 LEU LEU A . n 
A 1 185 PRO 185 186 186 PRO PRO A . n 
A 1 186 GLU 186 187 187 GLU GLU A . n 
A 1 187 SER 187 188 188 SER SER A . n 
A 1 188 LEU 188 189 189 LEU LEU A . n 
A 1 189 ASP 189 190 190 ASP ASP A . n 
A 1 190 TYR 190 191 191 TYR TYR A . n 
A 1 191 TRP 191 192 192 TRP TRP A . n 
A 1 192 THR 192 193 193 THR THR A . n 
A 1 193 TYR 193 194 194 TYR TYR A . n 
A 1 194 PRO 194 195 195 PRO PRO A . n 
A 1 195 GLY 195 196 196 GLY GLY A . n 
A 1 196 SER 196 197 197 SER SER A . n 
A 1 197 LEU 197 198 198 LEU LEU A . n 
A 1 198 THR 198 199 199 THR THR A . n 
A 1 199 THR 199 200 200 THR THR A . n 
A 1 200 PRO 200 201 201 PRO PRO A . n 
A 1 201 PRO 201 202 202 PRO PRO A . n 
A 1 202 LEU 202 203 203 LEU LEU A . n 
A 1 203 LEU 203 204 204 LEU LEU A . n 
A 1 204 GLU 204 205 205 GLU GLU A . n 
A 1 205 CYS 205 206 206 CYS CYS A . n 
A 1 206 VAL 206 207 207 VAL VAL A . n 
A 1 207 THR 207 208 208 THR THR A . n 
A 1 208 TRP 208 209 209 TRP TRP A . n 
A 1 209 ILE 209 210 210 ILE ILE A . n 
A 1 210 VAL 210 211 211 VAL VAL A . n 
A 1 211 LEU 211 212 212 LEU LEU A . n 
A 1 212 LYS 212 213 213 LYS LYS A . n 
A 1 213 GLU 213 214 214 GLU GLU A . n 
A 1 214 PRO 214 215 215 PRO PRO A . n 
A 1 215 ILE 215 216 216 ILE ILE A . n 
A 1 216 SER 216 217 217 SER SER A . n 
A 1 217 VAL 217 218 218 VAL VAL A . n 
A 1 218 SER 218 219 219 SER SER A . n 
A 1 219 SER 219 220 220 SER SER A . n 
A 1 220 GLU 220 221 221 GLU GLU A . n 
A 1 221 GLN 221 222 222 GLN GLN A . n 
A 1 222 VAL 222 223 223 VAL VAL A . n 
A 1 223 LEU 223 224 224 LEU LEU A . n 
A 1 224 LYS 224 225 225 LYS LYS A . n 
A 1 225 PHE 225 226 226 PHE PHE A . n 
A 1 226 ARG 226 227 227 ARG ARG A . n 
A 1 227 LYS 227 228 228 LYS LYS A . n 
A 1 228 LEU 228 229 229 LEU LEU A . n 
A 1 229 ASN 229 230 230 ASN ASN A . n 
A 1 230 PHE 230 231 231 PHE PHE A . n 
A 1 231 ASN 231 232 232 ASN ASN A . n 
A 1 232 GLY 232 233 233 GLY GLY A . n 
A 1 233 GLU 233 234 234 GLU GLU A . n 
A 1 234 GLY 234 235 235 GLY GLY A . n 
A 1 235 GLU 235 236 236 GLU GLU A . n 
A 1 236 PRO 236 237 237 PRO PRO A . n 
A 1 237 GLU 237 238 238 GLU GLU A . n 
A 1 238 GLU 238 239 239 GLU GLU A . n 
A 1 239 LEU 239 240 240 LEU LEU A . n 
A 1 240 MET 240 241 241 MET MET A . n 
A 1 241 VAL 241 242 242 VAL VAL A . n 
A 1 242 ASP 242 243 243 ASP ASP A . n 
A 1 243 ASN 243 244 244 ASN ASN A . n 
A 1 244 TRP 244 245 245 TRP TRP A . n 
A 1 245 ARG 245 246 246 ARG ARG A . n 
A 1 246 PRO 246 247 247 PRO PRO A . n 
A 1 247 ALA 247 248 248 ALA ALA A . n 
A 1 248 GLN 248 249 249 GLN GLN A . n 
A 1 249 PRO 249 250 250 PRO PRO A . n 
A 1 250 LEU 250 251 251 LEU LEU A . n 
A 1 251 LYS 251 252 252 LYS LYS A . n 
A 1 252 ASN 252 253 253 ASN ASN A . n 
A 1 253 ARG 253 254 254 ARG ARG A . n 
A 1 254 GLN 254 255 255 GLN GLN A . n 
A 1 255 ILE 255 256 256 ILE ILE A . n 
A 1 256 LYS 256 257 257 LYS LYS A . n 
A 1 257 ALA 257 258 258 ALA ALA A . n 
A 1 258 SER 258 259 259 SER SER A . n 
A 1 259 PHE 259 260 260 PHE PHE A . n 
A 1 260 LYS 260 261 261 LYS LYS A . n 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
B 2 ZN  1   301 1   ZN  ZN  A . 
C 3 EA3 1   302 1   EA3 EA3 A . 
D 4 DMS 1   303 1   DMS DMS A . 
E 5 HOH 1   401 132 HOH HOH A . 
E 5 HOH 2   402 301 HOH HOH A . 
E 5 HOH 3   403 329 HOH HOH A . 
E 5 HOH 4   404 140 HOH HOH A . 
E 5 HOH 5   405 336 HOH HOH A . 
E 5 HOH 6   406 204 HOH HOH A . 
E 5 HOH 7   407 71  HOH HOH A . 
E 5 HOH 8   408 263 HOH HOH A . 
E 5 HOH 9   409 303 HOH HOH A . 
E 5 HOH 10  410 269 HOH HOH A . 
E 5 HOH 11  411 170 HOH HOH A . 
E 5 HOH 12  412 175 HOH HOH A . 
E 5 HOH 13  413 333 HOH HOH A . 
E 5 HOH 14  414 260 HOH HOH A . 
E 5 HOH 15  415 37  HOH HOH A . 
E 5 HOH 16  416 127 HOH HOH A . 
E 5 HOH 17  417 334 HOH HOH A . 
E 5 HOH 18  418 304 HOH HOH A . 
E 5 HOH 19  419 69  HOH HOH A . 
E 5 HOH 20  420 299 HOH HOH A . 
E 5 HOH 21  421 29  HOH HOH A . 
E 5 HOH 22  422 261 HOH HOH A . 
E 5 HOH 23  423 211 HOH HOH A . 
E 5 HOH 24  424 196 HOH HOH A . 
E 5 HOH 25  425 111 HOH HOH A . 
E 5 HOH 26  426 117 HOH HOH A . 
E 5 HOH 27  427 6   HOH HOH A . 
E 5 HOH 28  428 51  HOH HOH A . 
E 5 HOH 29  429 239 HOH HOH A . 
E 5 HOH 30  430 210 HOH HOH A . 
E 5 HOH 31  431 293 HOH HOH A . 
E 5 HOH 32  432 142 HOH HOH A . 
E 5 HOH 33  433 231 HOH HOH A . 
E 5 HOH 34  434 332 HOH HOH A . 
E 5 HOH 35  435 247 HOH HOH A . 
E 5 HOH 36  436 31  HOH HOH A . 
E 5 HOH 37  437 291 HOH HOH A . 
E 5 HOH 38  438 3   HOH HOH A . 
E 5 HOH 39  439 82  HOH HOH A . 
E 5 HOH 40  440 186 HOH HOH A . 
E 5 HOH 41  441 255 HOH HOH A . 
E 5 HOH 42  442 324 HOH HOH A . 
E 5 HOH 43  443 148 HOH HOH A . 
E 5 HOH 44  444 222 HOH HOH A . 
E 5 HOH 45  445 159 HOH HOH A . 
E 5 HOH 46  446 289 HOH HOH A . 
E 5 HOH 47  447 179 HOH HOH A . 
E 5 HOH 48  448 237 HOH HOH A . 
E 5 HOH 49  449 12  HOH HOH A . 
E 5 HOH 50  450 75  HOH HOH A . 
E 5 HOH 51  451 114 HOH HOH A . 
E 5 HOH 52  452 66  HOH HOH A . 
E 5 HOH 53  453 74  HOH HOH A . 
E 5 HOH 54  454 128 HOH HOH A . 
E 5 HOH 55  455 220 HOH HOH A . 
E 5 HOH 56  456 250 HOH HOH A . 
E 5 HOH 57  457 23  HOH HOH A . 
E 5 HOH 58  458 30  HOH HOH A . 
E 5 HOH 59  459 95  HOH HOH A . 
E 5 HOH 60  460 227 HOH HOH A . 
E 5 HOH 61  461 242 HOH HOH A . 
E 5 HOH 62  462 49  HOH HOH A . 
E 5 HOH 63  463 290 HOH HOH A . 
E 5 HOH 64  464 22  HOH HOH A . 
E 5 HOH 65  465 216 HOH HOH A . 
E 5 HOH 66  466 202 HOH HOH A . 
E 5 HOH 67  467 15  HOH HOH A . 
E 5 HOH 68  468 48  HOH HOH A . 
E 5 HOH 69  469 60  HOH HOH A . 
E 5 HOH 70  470 24  HOH HOH A . 
E 5 HOH 71  471 158 HOH HOH A . 
E 5 HOH 72  472 320 HOH HOH A . 
E 5 HOH 73  473 14  HOH HOH A . 
E 5 HOH 74  474 28  HOH HOH A . 
E 5 HOH 75  475 124 HOH HOH A . 
E 5 HOH 76  476 121 HOH HOH A . 
E 5 HOH 77  477 136 HOH HOH A . 
E 5 HOH 78  478 257 HOH HOH A . 
E 5 HOH 79  479 1   HOH HOH A . 
E 5 HOH 80  480 77  HOH HOH A . 
E 5 HOH 81  481 287 HOH HOH A . 
E 5 HOH 82  482 92  HOH HOH A . 
E 5 HOH 83  483 150 HOH HOH A . 
E 5 HOH 84  484 154 HOH HOH A . 
E 5 HOH 85  485 335 HOH HOH A . 
E 5 HOH 86  486 164 HOH HOH A . 
E 5 HOH 87  487 266 HOH HOH A . 
E 5 HOH 88  488 80  HOH HOH A . 
E 5 HOH 89  489 94  HOH HOH A . 
E 5 HOH 90  490 214 HOH HOH A . 
E 5 HOH 91  491 99  HOH HOH A . 
E 5 HOH 92  492 102 HOH HOH A . 
E 5 HOH 93  493 141 HOH HOH A . 
E 5 HOH 94  494 273 HOH HOH A . 
E 5 HOH 95  495 39  HOH HOH A . 
E 5 HOH 96  496 104 HOH HOH A . 
E 5 HOH 97  497 5   HOH HOH A . 
E 5 HOH 98  498 309 HOH HOH A . 
E 5 HOH 99  499 96  HOH HOH A . 
E 5 HOH 100 500 152 HOH HOH A . 
E 5 HOH 101 501 18  HOH HOH A . 
E 5 HOH 102 502 144 HOH HOH A . 
E 5 HOH 103 503 73  HOH HOH A . 
E 5 HOH 104 504 32  HOH HOH A . 
E 5 HOH 105 505 52  HOH HOH A . 
E 5 HOH 106 506 233 HOH HOH A . 
E 5 HOH 107 507 248 HOH HOH A . 
E 5 HOH 108 508 125 HOH HOH A . 
E 5 HOH 109 509 108 HOH HOH A . 
E 5 HOH 110 510 312 HOH HOH A . 
E 5 HOH 111 511 41  HOH HOH A . 
E 5 HOH 112 512 83  HOH HOH A . 
E 5 HOH 113 513 81  HOH HOH A . 
E 5 HOH 114 514 38  HOH HOH A . 
E 5 HOH 115 515 47  HOH HOH A . 
E 5 HOH 116 516 337 HOH HOH A . 
E 5 HOH 117 517 84  HOH HOH A . 
E 5 HOH 118 518 172 HOH HOH A . 
E 5 HOH 119 519 8   HOH HOH A . 
E 5 HOH 120 520 230 HOH HOH A . 
E 5 HOH 121 521 4   HOH HOH A . 
E 5 HOH 122 522 35  HOH HOH A . 
E 5 HOH 123 523 43  HOH HOH A . 
E 5 HOH 124 524 10  HOH HOH A . 
E 5 HOH 125 525 17  HOH HOH A . 
E 5 HOH 126 526 53  HOH HOH A . 
E 5 HOH 127 527 184 HOH HOH A . 
E 5 HOH 128 528 112 HOH HOH A . 
E 5 HOH 129 529 11  HOH HOH A . 
E 5 HOH 130 530 93  HOH HOH A . 
E 5 HOH 131 531 103 HOH HOH A . 
E 5 HOH 132 532 113 HOH HOH A . 
E 5 HOH 133 533 13  HOH HOH A . 
E 5 HOH 134 534 318 HOH HOH A . 
E 5 HOH 135 535 62  HOH HOH A . 
E 5 HOH 136 536 308 HOH HOH A . 
E 5 HOH 137 537 64  HOH HOH A . 
E 5 HOH 138 538 317 HOH HOH A . 
E 5 HOH 139 539 218 HOH HOH A . 
E 5 HOH 140 540 63  HOH HOH A . 
E 5 HOH 141 541 72  HOH HOH A . 
E 5 HOH 142 542 87  HOH HOH A . 
E 5 HOH 143 543 122 HOH HOH A . 
E 5 HOH 144 544 207 HOH HOH A . 
E 5 HOH 145 545 50  HOH HOH A . 
E 5 HOH 146 546 65  HOH HOH A . 
E 5 HOH 147 547 183 HOH HOH A . 
E 5 HOH 148 548 286 HOH HOH A . 
E 5 HOH 149 549 26  HOH HOH A . 
E 5 HOH 150 550 168 HOH HOH A . 
E 5 HOH 151 551 221 HOH HOH A . 
E 5 HOH 152 552 42  HOH HOH A . 
E 5 HOH 153 553 85  HOH HOH A . 
E 5 HOH 154 554 55  HOH HOH A . 
E 5 HOH 155 555 45  HOH HOH A . 
E 5 HOH 156 556 131 HOH HOH A . 
E 5 HOH 157 557 109 HOH HOH A . 
E 5 HOH 158 558 67  HOH HOH A . 
E 5 HOH 159 559 34  HOH HOH A . 
E 5 HOH 160 560 115 HOH HOH A . 
E 5 HOH 161 561 296 HOH HOH A . 
E 5 HOH 162 562 224 HOH HOH A . 
E 5 HOH 163 563 78  HOH HOH A . 
E 5 HOH 164 564 200 HOH HOH A . 
E 5 HOH 165 565 267 HOH HOH A . 
E 5 HOH 166 566 130 HOH HOH A . 
E 5 HOH 167 567 280 HOH HOH A . 
E 5 HOH 168 568 56  HOH HOH A . 
E 5 HOH 169 569 68  HOH HOH A . 
E 5 HOH 170 570 25  HOH HOH A . 
E 5 HOH 171 571 162 HOH HOH A . 
E 5 HOH 172 572 58  HOH HOH A . 
E 5 HOH 173 573 97  HOH HOH A . 
E 5 HOH 174 574 340 HOH HOH A . 
E 5 HOH 175 575 126 HOH HOH A . 
E 5 HOH 176 576 256 HOH HOH A . 
E 5 HOH 177 577 7   HOH HOH A . 
E 5 HOH 178 578 59  HOH HOH A . 
E 5 HOH 179 579 182 HOH HOH A . 
E 5 HOH 180 580 149 HOH HOH A . 
E 5 HOH 181 581 339 HOH HOH A . 
E 5 HOH 182 582 138 HOH HOH A . 
E 5 HOH 183 583 33  HOH HOH A . 
E 5 HOH 184 584 323 HOH HOH A . 
E 5 HOH 185 585 278 HOH HOH A . 
E 5 HOH 186 586 118 HOH HOH A . 
E 5 HOH 187 587 61  HOH HOH A . 
E 5 HOH 188 588 86  HOH HOH A . 
E 5 HOH 189 589 185 HOH HOH A . 
E 5 HOH 190 590 225 HOH HOH A . 
E 5 HOH 191 591 203 HOH HOH A . 
E 5 HOH 192 592 300 HOH HOH A . 
E 5 HOH 193 593 234 HOH HOH A . 
E 5 HOH 194 594 90  HOH HOH A . 
E 5 HOH 195 595 133 HOH HOH A . 
E 5 HOH 196 596 199 HOH HOH A . 
E 5 HOH 197 597 21  HOH HOH A . 
E 5 HOH 198 598 107 HOH HOH A . 
E 5 HOH 199 599 137 HOH HOH A . 
E 5 HOH 200 600 147 HOH HOH A . 
E 5 HOH 201 601 145 HOH HOH A . 
E 5 HOH 202 602 246 HOH HOH A . 
E 5 HOH 203 603 274 HOH HOH A . 
E 5 HOH 204 604 2   HOH HOH A . 
E 5 HOH 205 605 161 HOH HOH A . 
E 5 HOH 206 606 265 HOH HOH A . 
E 5 HOH 207 607 244 HOH HOH A . 
E 5 HOH 208 608 171 HOH HOH A . 
E 5 HOH 209 609 36  HOH HOH A . 
E 5 HOH 210 610 165 HOH HOH A . 
E 5 HOH 211 611 326 HOH HOH A . 
E 5 HOH 212 612 139 HOH HOH A . 
E 5 HOH 213 613 167 HOH HOH A . 
E 5 HOH 214 614 9   HOH HOH A . 
E 5 HOH 215 615 325 HOH HOH A . 
E 5 HOH 216 616 123 HOH HOH A . 
E 5 HOH 217 617 258 HOH HOH A . 
E 5 HOH 218 618 54  HOH HOH A . 
E 5 HOH 219 619 120 HOH HOH A . 
E 5 HOH 220 620 19  HOH HOH A . 
E 5 HOH 221 621 110 HOH HOH A . 
E 5 HOH 222 622 100 HOH HOH A . 
E 5 HOH 223 623 178 HOH HOH A . 
E 5 HOH 224 624 277 HOH HOH A . 
E 5 HOH 225 625 16  HOH HOH A . 
E 5 HOH 226 626 89  HOH HOH A . 
E 5 HOH 227 627 173 HOH HOH A . 
E 5 HOH 228 628 302 HOH HOH A . 
E 5 HOH 229 629 157 HOH HOH A . 
E 5 HOH 230 630 249 HOH HOH A . 
E 5 HOH 231 631 151 HOH HOH A . 
E 5 HOH 232 632 254 HOH HOH A . 
E 5 HOH 233 633 294 HOH HOH A . 
E 5 HOH 234 634 44  HOH HOH A . 
E 5 HOH 235 635 181 HOH HOH A . 
E 5 HOH 236 636 281 HOH HOH A . 
E 5 HOH 237 637 288 HOH HOH A . 
E 5 HOH 238 638 268 HOH HOH A . 
E 5 HOH 239 639 135 HOH HOH A . 
E 5 HOH 240 640 174 HOH HOH A . 
E 5 HOH 241 641 134 HOH HOH A . 
E 5 HOH 242 642 160 HOH HOH A . 
E 5 HOH 243 643 226 HOH HOH A . 
E 5 HOH 244 644 252 HOH HOH A . 
E 5 HOH 245 645 20  HOH HOH A . 
E 5 HOH 246 646 155 HOH HOH A . 
E 5 HOH 247 647 321 HOH HOH A . 
E 5 HOH 248 648 57  HOH HOH A . 
E 5 HOH 249 649 253 HOH HOH A . 
E 5 HOH 250 650 241 HOH HOH A . 
E 5 HOH 251 651 46  HOH HOH A . 
E 5 HOH 252 652 217 HOH HOH A . 
E 5 HOH 253 653 206 HOH HOH A . 
E 5 HOH 254 654 282 HOH HOH A . 
E 5 HOH 255 655 292 HOH HOH A . 
E 5 HOH 256 656 180 HOH HOH A . 
E 5 HOH 257 657 146 HOH HOH A . 
E 5 HOH 258 658 315 HOH HOH A . 
E 5 HOH 259 659 314 HOH HOH A . 
E 5 HOH 260 660 262 HOH HOH A . 
E 5 HOH 261 661 156 HOH HOH A . 
E 5 HOH 262 662 201 HOH HOH A . 
E 5 HOH 263 663 236 HOH HOH A . 
E 5 HOH 264 664 189 HOH HOH A . 
E 5 HOH 265 665 98  HOH HOH A . 
E 5 HOH 266 666 229 HOH HOH A . 
E 5 HOH 267 667 298 HOH HOH A . 
E 5 HOH 268 668 295 HOH HOH A . 
E 5 HOH 269 669 190 HOH HOH A . 
E 5 HOH 270 670 215 HOH HOH A . 
E 5 HOH 271 671 205 HOH HOH A . 
E 5 HOH 272 672 208 HOH HOH A . 
E 5 HOH 273 673 27  HOH HOH A . 
E 5 HOH 274 674 88  HOH HOH A . 
E 5 HOH 275 675 177 HOH HOH A . 
E 5 HOH 276 676 240 HOH HOH A . 
E 5 HOH 277 677 166 HOH HOH A . 
E 5 HOH 278 678 76  HOH HOH A . 
E 5 HOH 279 679 40  HOH HOH A . 
E 5 HOH 280 680 310 HOH HOH A . 
E 5 HOH 281 681 331 HOH HOH A . 
E 5 HOH 282 682 271 HOH HOH A . 
E 5 HOH 283 683 195 HOH HOH A . 
E 5 HOH 284 684 212 HOH HOH A . 
E 5 HOH 285 685 188 HOH HOH A . 
E 5 HOH 286 686 91  HOH HOH A . 
E 5 HOH 287 687 193 HOH HOH A . 
E 5 HOH 288 688 106 HOH HOH A . 
E 5 HOH 289 689 129 HOH HOH A . 
E 5 HOH 290 690 192 HOH HOH A . 
E 5 HOH 291 691 116 HOH HOH A . 
E 5 HOH 292 692 285 HOH HOH A . 
E 5 HOH 293 693 119 HOH HOH A . 
E 5 HOH 294 694 284 HOH HOH A . 
E 5 HOH 295 695 153 HOH HOH A . 
E 5 HOH 296 696 105 HOH HOH A . 
E 5 HOH 297 697 330 HOH HOH A . 
E 5 HOH 298 698 70  HOH HOH A . 
E 5 HOH 299 699 327 HOH HOH A . 
E 5 HOH 300 700 270 HOH HOH A . 
E 5 HOH 301 701 101 HOH HOH A . 
E 5 HOH 302 702 272 HOH HOH A . 
E 5 HOH 303 703 219 HOH HOH A . 
E 5 HOH 304 704 197 HOH HOH A . 
E 5 HOH 305 705 235 HOH HOH A . 
E 5 HOH 306 706 187 HOH HOH A . 
E 5 HOH 307 707 338 HOH HOH A . 
E 5 HOH 308 708 275 HOH HOH A . 
E 5 HOH 309 709 169 HOH HOH A . 
E 5 HOH 310 710 305 HOH HOH A . 
E 5 HOH 311 711 279 HOH HOH A . 
E 5 HOH 312 712 79  HOH HOH A . 
E 5 HOH 313 713 251 HOH HOH A . 
E 5 HOH 314 714 311 HOH HOH A . 
E 5 HOH 315 715 328 HOH HOH A . 
E 5 HOH 316 716 213 HOH HOH A . 
E 5 HOH 317 717 243 HOH HOH A . 
E 5 HOH 318 718 228 HOH HOH A . 
E 5 HOH 319 719 209 HOH HOH A . 
E 5 HOH 320 720 259 HOH HOH A . 
E 5 HOH 321 721 176 HOH HOH A . 
E 5 HOH 322 722 191 HOH HOH A . 
E 5 HOH 323 723 232 HOH HOH A . 
E 5 HOH 324 724 283 HOH HOH A . 
E 5 HOH 325 725 306 HOH HOH A . 
E 5 HOH 326 726 276 HOH HOH A . 
E 5 HOH 327 727 198 HOH HOH A . 
E 5 HOH 328 728 322 HOH HOH A . 
E 5 HOH 329 729 264 HOH HOH A . 
E 5 HOH 330 730 163 HOH HOH A . 
E 5 HOH 331 731 245 HOH HOH A . 
E 5 HOH 332 732 238 HOH HOH A . 
E 5 HOH 333 733 143 HOH HOH A . 
E 5 HOH 334 734 297 HOH HOH A . 
E 5 HOH 335 735 223 HOH HOH A . 
E 5 HOH 336 736 316 HOH HOH A . 
E 5 HOH 337 737 319 HOH HOH A . 
E 5 HOH 338 738 307 HOH HOH A . 
E 5 HOH 339 739 313 HOH HOH A . 
E 5 HOH 340 740 194 HOH HOH A . 
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1 1 Y 1 A LYS 261 ? CG ? A LYS 260 CG 
2 1 Y 1 A LYS 261 ? CD ? A LYS 260 CD 
3 1 Y 1 A LYS 261 ? CE ? A LYS 260 CE 
4 1 Y 1 A LYS 261 ? NZ ? A LYS 260 NZ 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement        ? ? ? ? ? ? ? ? ? ? ? REFMAC      ? ? ? .    1 
? 'data extraction' ? ? ? ? ? ? ? ? ? ? ? PDB_EXTRACT ? ? ? 3.10 2 
? 'data reduction'  ? ? ? ? ? ? ? ? ? ? ? MOSFLM      ? ? ? .    3 
? 'data scaling'    ? ? ? ? ? ? ? ? ? ? ? SCALA       ? ? ? .    4 
? phasing           ? ? ? ? ? ? ? ? ? ? ? MOLREP      ? ? ? .    5 
? 'model building'  ? ? ? ? ? ? ? ? ? ? ? Coot        ? ? ? .    6 
# 
_cell.angle_alpha                  90.000 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   104.190 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.000 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     6R6F 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     42.308 
_cell.length_a_esd                 ? 
_cell.length_b                     41.749 
_cell.length_b_esd                 ? 
_cell.length_c                     72.323 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        2 
_cell.reciprocal_angle_alpha       ? 
_cell.reciprocal_angle_beta        ? 
_cell.reciprocal_angle_gamma       ? 
_cell.reciprocal_angle_alpha_esd   ? 
_cell.reciprocal_angle_beta_esd    ? 
_cell.reciprocal_angle_gamma_esd   ? 
_cell.reciprocal_length_a          ? 
_cell.reciprocal_length_b          ? 
_cell.reciprocal_length_c          ? 
_cell.reciprocal_length_a_esd      ? 
_cell.reciprocal_length_b_esd      ? 
_cell.reciprocal_length_c_esd      ? 
_cell.pdbx_unique_axis             ? 
# 
_symmetry.entry_id                         6R6F 
_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                   6R6F 
_exptl.crystals_number            2 
_exptl.details                    ? 
_exptl.method                     'X-RAY DIFFRACTION' 
_exptl.method_details             ? 
# 
_exptl_crystal.colour                      ? 
_exptl_crystal.density_diffrn              ? 
_exptl_crystal.density_Matthews            2.11 
_exptl_crystal.density_method              ? 
_exptl_crystal.density_percent_sol         41.82 
_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 sodium bicine (pH 9), 0.2M ammonium sulfate and 2M sodium malonate (pH 7)' 
_exptl_crystal_grow.pdbx_pH_range   ? 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS PILATUS 6M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2015-06-24 
_diffrn_detector.pdbx_frequency               ? 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   1.01000 
_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        1.01000 
_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                         6R6F 
_reflns.data_reduction_details           ? 
_reflns.data_reduction_method            ? 
_reflns.d_resolution_high                1.200 
_reflns.d_resolution_low                 41.017 
_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                       71118 
_reflns.number_obs                       71118 
_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             93.200 
_reflns.R_free_details                   ? 
_reflns.Rmerge_F_all                     ? 
_reflns.Rmerge_F_obs                     ? 
_reflns.Friedel_coverage                 ? 
_reflns.number_gt                        ? 
_reflns.threshold_expression             ? 
_reflns.pdbx_redundancy                  6.000 
_reflns.pdbx_Rmerge_I_obs                ? 
_reflns.pdbx_Rmerge_I_all                ? 
_reflns.pdbx_Rsym_value                  0.118 
_reflns.pdbx_netI_over_av_sigmaI         2.431 
_reflns.pdbx_netI_over_sigmaI            6.700 
_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                  0.133 
_reflns.pdbx_Rpim_I_all                  0.053 
_reflns.pdbx_d_opt                       ? 
_reflns.pdbx_number_measured_all         427545 
_reflns.pdbx_diffrn_id                   1 
_reflns.pdbx_ordinal                     1 
_reflns.pdbx_CC_half                     ? 
_reflns.pdbx_R_split                     ? 
_reflns.pdbx_CC_star                     ? 
# 
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 
_reflns_shell.pdbx_CC_star 
1.200 1.260  ? 1.5 ? ? ? ? 10016 90.200 ? ? ? ? 0.434 ? ? ? ? ? ? ? ? 6.100 0.434 ? ? ? 0.511 0.204 ? 1  1 ? ? ? 
1.260 1.340  ? 1.9 ? ? ? ? 9656  92.400 ? ? ? ? 0.336 ? ? ? ? ? ? ? ? 6.000 0.336 ? ? ? 0.397 0.160 ? 2  1 ? ? ? 
1.340 1.430  ? 2.4 ? ? ? ? 9092  92.100 ? ? ? ? 0.258 ? ? ? ? ? ? ? ? 6.000 0.258 ? ? ? 0.303 0.122 ? 3  1 ? ? ? 
1.430 1.550  ? 3.1 ? ? ? ? 8559  92.900 ? ? ? ? 0.189 ? ? ? ? ? ? ? ? 5.700 0.189 ? ? ? 0.222 0.091 ? 4  1 ? ? ? 
1.550 1.700  ? 3.5 ? ? ? ? 7870  92.900 ? ? ? ? 0.154 ? ? ? ? ? ? ? ? 6.000 0.154 ? ? ? 0.178 0.071 ? 5  1 ? ? ? 
1.700 1.900  ? 3.6 ? ? ? ? 7323  95.400 ? ? ? ? 0.140 ? ? ? ? ? ? ? ? 6.200 0.140 ? ? ? 0.159 0.063 ? 6  1 ? ? ? 
1.900 2.190  ? 3.7 ? ? ? ? 6531  96.100 ? ? ? ? 0.131 ? ? ? ? ? ? ? ? 6.100 0.131 ? ? ? 0.146 0.058 ? 7  1 ? ? ? 
2.190 2.680  ? 4.2 ? ? ? ? 5469  95.600 ? ? ? ? 0.117 ? ? ? ? ? ? ? ? 6.100 0.117 ? ? ? 0.132 0.052 ? 8  1 ? ? ? 
2.680 3.790  ? 4.7 ? ? ? ? 4281  95.700 ? ? ? ? 0.103 ? ? ? ? ? ? ? ? 5.800 0.103 ? ? ? 0.115 0.047 ? 9  1 ? ? ? 
3.790 41.017 ? 5.6 ? ? ? ? 2321  92.400 ? ? ? ? 0.090 ? ? ? ? ? ? ? ? 6.000 0.090 ? ? ? 0.101 0.040 ? 10 1 ? ? ? 
# 
_refine.aniso_B[1][1]                            0.0600 
_refine.aniso_B[1][2]                            -0.0000 
_refine.aniso_B[1][3]                            -0.1500 
_refine.aniso_B[2][2]                            -0.2300 
_refine.aniso_B[2][3]                            0.0000 
_refine.aniso_B[3][3]                            0.2200 
_refine.B_iso_max                                123.110 
_refine.B_iso_mean                               19.0325 
_refine.B_iso_min                                6.820 
_refine.correlation_coeff_Fo_to_Fc               0.9800 
_refine.correlation_coeff_Fo_to_Fc_free          0.9580 
_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                                 6R6F 
_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                            1.2000 
_refine.ls_d_res_low                             32.1600 
_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                     71102 
_refine.ls_number_reflns_R_free                  4509 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    92.7300 
_refine.ls_percent_reflns_R_free                 6.3000 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1490 
_refine.ls_R_factor_R_free                       0.1850 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1457 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    ? 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          0.000 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               THROUGHOUT 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      3HLJ 
_refine.pdbx_stereochemistry_target_values       ? 
_refine.pdbx_R_Free_selection_details            RANDOM 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       0.0440 
_refine.pdbx_overall_ESU_R_Free                  0.0450 
_refine.pdbx_solvent_vdw_probe_radii             1.4000 
_refine.pdbx_solvent_ion_probe_radii             0.8000 
_refine.pdbx_solvent_shrinkage_radii             0.8000 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 ? 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_diffrn_id                           1 
_refine.overall_SU_B                             ? 
_refine.overall_SU_ML                            ? 
_refine.overall_SU_R_Cruickshank_DPI             0.0437 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       1.2000 
_refine_hist.d_res_low                        32.1600 
_refine_hist.number_atoms_solvent             340 
_refine_hist.number_atoms_total               2428 
_refine_hist.number_reflns_all                ? 
_refine_hist.number_reflns_obs                ? 
_refine_hist.number_reflns_R_free             ? 
_refine_hist.number_reflns_R_work             ? 
_refine_hist.R_factor_all                     ? 
_refine_hist.R_factor_obs                     ? 
_refine_hist.R_factor_R_free                  ? 
_refine_hist.R_factor_R_work                  ? 
_refine_hist.pdbx_number_residues_total       ? 
_refine_hist.pdbx_B_iso_mean_ligand           ? 
_refine_hist.pdbx_B_iso_mean_solvent          ? 
_refine_hist.pdbx_number_atoms_protein        2059 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         29 
_refine_hist.pdbx_number_atoms_lipid          ? 
_refine_hist.pdbx_number_atoms_carb           ? 
_refine_hist.pdbx_pseudo_atom_details         ? 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.criterion 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.number 
_refine_ls_restr.rejects 
_refine_ls_restr.type 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' ? 0.019  0.012  2233 ? r_bond_refined_d       ? ? 
'X-RAY DIFFRACTION' ? 2.049  1.650  3045 ? r_angle_refined_deg    ? ? 
'X-RAY DIFFRACTION' ? 7.094  5.000  276  ? r_dihedral_angle_1_deg ? ? 
'X-RAY DIFFRACTION' ? 32.722 23.853 109  ? r_dihedral_angle_2_deg ? ? 
'X-RAY DIFFRACTION' ? 14.152 15.000 369  ? r_dihedral_angle_3_deg ? ? 
'X-RAY DIFFRACTION' ? 21.373 15.000 7    ? r_dihedral_angle_4_deg ? ? 
'X-RAY DIFFRACTION' ? 0.141  0.200  269  ? r_chiral_restr         ? ? 
'X-RAY DIFFRACTION' ? 0.014  0.020  1759 ? r_gen_planes_refined   ? ? 
'X-RAY DIFFRACTION' ? 2.712  1.423  1080 ? r_mcbond_it            ? ? 
'X-RAY DIFFRACTION' ? 3.522  2.133  1364 ? r_mcangle_it           ? ? 
'X-RAY DIFFRACTION' ? 5.211  1.798  1153 ? r_scbond_it            ? ? 
'X-RAY DIFFRACTION' ? 5.936  3.000  2233 ? r_rigid_bond_restr     ? ? 
'X-RAY DIFFRACTION' ? 33.191 5.000  206  ? r_sphericity_free      ? ? 
'X-RAY DIFFRACTION' ? 18.493 5.000  2296 ? r_sphericity_bonded    ? ? 
# 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.d_res_high                       1.2000 
_refine_ls_shell.d_res_low                        1.2310 
_refine_ls_shell.number_reflns_all                ? 
_refine_ls_shell.number_reflns_obs                ? 
_refine_ls_shell.number_reflns_R_free             ? 
_refine_ls_shell.number_reflns_R_work             5021 
_refine_ls_shell.percent_reflns_obs               89.1700 
_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                  ? 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.R_factor_R_work                  0.3330 
_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                     6R6F 
_struct.title                        
;Crystal structure of human carbonic anhydrase isozyme II with 4-chloro-2-cyclohexylsulfanyl-N-(2-hydroxyethyl)-5-sulfamoyl-benzamide
;
_struct.pdbx_model_details           ? 
_struct.pdbx_formula_weight          ? 
_struct.pdbx_formula_weight_method   ? 
_struct.pdbx_model_type_details      ? 
_struct.pdbx_CASP_flag               N 
# 
_struct_keywords.entry_id        6R6F 
_struct_keywords.text            
'drug design, carbonic anhydrase, benzenesulfonamide, metal binding protein, lyase-lyase inhibitor complex, lyase' 
_struct_keywords.pdbx_keywords   LYASE 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 2 ? 
C N N 3 ? 
D N N 4 ? 
E N N 5 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    CAH2_HUMAN 
_struct_ref.pdbx_db_accession          P00918 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;MSHHWGYGKHNGPEHWHKDFPIAKGERQSPVDIDTHTAKYDPSLKPLSVSYDQATSLRILNNGHAFNVEFDDSQDKAVLK
GGPLDGTYRLIQFHFHWGSLDGQGSEHTVDKKKYAAELHLVHWNTKYGDFGKAVQQPDGLAVLGIFLKVGSAKPGLQKVV
DVLDSIKTKGKSADFTNFDPRGLLPESLDYWTYPGSLTTPPLLECVTWIVLKEPISVSSEQVLKFRKLNFNGEGEPEELM
VDNWRPAQPLKNRQIKASFK
;
_struct_ref.pdbx_align_begin           1 
# 
_struct_ref_seq.align_id                      1 
_struct_ref_seq.ref_id                        1 
_struct_ref_seq.pdbx_PDB_id_code              6R6F 
_struct_ref_seq.pdbx_strand_id                A 
_struct_ref_seq.seq_align_beg                 1 
_struct_ref_seq.pdbx_seq_align_beg_ins_code   ? 
_struct_ref_seq.seq_align_end                 260 
_struct_ref_seq.pdbx_seq_align_end_ins_code   ? 
_struct_ref_seq.pdbx_db_accession             P00918 
_struct_ref_seq.db_align_beg                  1 
_struct_ref_seq.pdbx_db_align_beg_ins_code    ? 
_struct_ref_seq.db_align_end                  260 
_struct_ref_seq.pdbx_db_align_end_ins_code    ? 
_struct_ref_seq.pdbx_auth_seq_align_beg       1 
_struct_ref_seq.pdbx_auth_seq_align_end       261 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_and_software_defined_assembly 
_pdbx_struct_assembly.method_details       PISA 
_pdbx_struct_assembly.oligomeric_details   monomeric 
_pdbx_struct_assembly.oligomeric_count     1 
# 
loop_
_pdbx_struct_assembly_prop.biol_id 
_pdbx_struct_assembly_prop.type 
_pdbx_struct_assembly_prop.value 
_pdbx_struct_assembly_prop.details 
1 'ABSA (A^2)' 230   ? 
1 MORE         2     ? 
1 'SSA (A^2)'  11710 ? 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   none 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1 AA1 GLY A 12  ? ASP A 19  ? GLY A 12  ASP A 19  5 ? 8 
HELX_P HELX_P2 AA2 PHE A 20  ? GLY A 25  ? PHE A 20  GLY A 25  5 ? 6 
HELX_P HELX_P3 AA3 LYS A 126 ? GLY A 128 ? LYS A 127 GLY A 129 5 ? 3 
HELX_P HELX_P4 AA4 ASP A 129 ? VAL A 134 ? ASP A 130 VAL A 135 1 ? 6 
HELX_P HELX_P5 AA5 LYS A 153 ? GLY A 155 ? LYS A 154 GLY A 156 5 ? 3 
HELX_P HELX_P6 AA6 LEU A 156 ? LEU A 163 ? LEU A 157 LEU A 164 1 ? 8 
HELX_P HELX_P7 AA7 ASP A 164 ? LYS A 167 ? ASP A 165 LYS A 168 5 ? 4 
HELX_P HELX_P8 AA8 ASP A 179 ? LEU A 184 ? ASP A 180 LEU A 185 5 ? 6 
HELX_P HELX_P9 AA9 SER A 218 ? ARG A 226 ? SER A 219 ARG A 227 1 ? 9 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
metalc1 metalc ? ? A HIS 94  NE2 ? ? ? 1_555 B ZN  . ZN ? ? A HIS 94  A ZN  301 1_555 ? ? ? ? ? ? ? 2.063 ? ? 
metalc2 metalc ? ? A HIS 96  NE2 ? ? ? 1_555 B ZN  . ZN ? ? A HIS 96  A ZN  301 1_555 ? ? ? ? ? ? ? 2.044 ? ? 
metalc3 metalc ? ? A HIS 119 ND1 ? ? ? 1_555 B ZN  . ZN ? ? A HIS 119 A ZN  301 1_555 ? ? ? ? ? ? ? 2.027 ? ? 
metalc4 metalc ? ? B ZN  .   ZN  ? ? ? 1_555 C EA3 . N1 ? ? A ZN  301 A EA3 302 1_555 ? ? ? ? ? ? ? 1.993 ? ? 
# 
_struct_conn_type.id          metalc 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
loop_
_pdbx_struct_conn_angle.id 
_pdbx_struct_conn_angle.ptnr1_label_atom_id 
_pdbx_struct_conn_angle.ptnr1_label_alt_id 
_pdbx_struct_conn_angle.ptnr1_label_asym_id 
_pdbx_struct_conn_angle.ptnr1_label_comp_id 
_pdbx_struct_conn_angle.ptnr1_label_seq_id 
_pdbx_struct_conn_angle.ptnr1_auth_atom_id 
_pdbx_struct_conn_angle.ptnr1_auth_asym_id 
_pdbx_struct_conn_angle.ptnr1_auth_comp_id 
_pdbx_struct_conn_angle.ptnr1_auth_seq_id 
_pdbx_struct_conn_angle.ptnr1_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr1_symmetry 
_pdbx_struct_conn_angle.ptnr2_label_atom_id 
_pdbx_struct_conn_angle.ptnr2_label_alt_id 
_pdbx_struct_conn_angle.ptnr2_label_asym_id 
_pdbx_struct_conn_angle.ptnr2_label_comp_id 
_pdbx_struct_conn_angle.ptnr2_label_seq_id 
_pdbx_struct_conn_angle.ptnr2_auth_atom_id 
_pdbx_struct_conn_angle.ptnr2_auth_asym_id 
_pdbx_struct_conn_angle.ptnr2_auth_comp_id 
_pdbx_struct_conn_angle.ptnr2_auth_seq_id 
_pdbx_struct_conn_angle.ptnr2_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr2_symmetry 
_pdbx_struct_conn_angle.ptnr3_label_atom_id 
_pdbx_struct_conn_angle.ptnr3_label_alt_id 
_pdbx_struct_conn_angle.ptnr3_label_asym_id 
_pdbx_struct_conn_angle.ptnr3_label_comp_id 
_pdbx_struct_conn_angle.ptnr3_label_seq_id 
_pdbx_struct_conn_angle.ptnr3_auth_atom_id 
_pdbx_struct_conn_angle.ptnr3_auth_asym_id 
_pdbx_struct_conn_angle.ptnr3_auth_comp_id 
_pdbx_struct_conn_angle.ptnr3_auth_seq_id 
_pdbx_struct_conn_angle.ptnr3_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr3_symmetry 
_pdbx_struct_conn_angle.value 
_pdbx_struct_conn_angle.value_esd 
1 NE2 ? A HIS 94  ? A HIS 94  ? 1_555 ZN ? B ZN . ? A ZN 301 ? 1_555 NE2 ? A HIS 96  ? A HIS 96  ? 1_555 102.7 ? 
2 NE2 ? A HIS 94  ? A HIS 94  ? 1_555 ZN ? B ZN . ? A ZN 301 ? 1_555 ND1 ? A HIS 119 ? A HIS 119 ? 1_555 113.0 ? 
3 NE2 ? A HIS 96  ? A HIS 96  ? 1_555 ZN ? B ZN . ? A ZN 301 ? 1_555 ND1 ? A HIS 119 ? A HIS 119 ? 1_555 98.7  ? 
4 NE2 ? A HIS 94  ? A HIS 94  ? 1_555 ZN ? B ZN . ? A ZN 301 ? 1_555 N1  ? C EA3 .   ? A EA3 302 ? 1_555 110.1 ? 
5 NE2 ? A HIS 96  ? A HIS 96  ? 1_555 ZN ? B ZN . ? A ZN 301 ? 1_555 N1  ? C EA3 .   ? A EA3 302 ? 1_555 113.8 ? 
6 ND1 ? A HIS 119 ? A HIS 119 ? 1_555 ZN ? B ZN . ? A ZN 301 ? 1_555 N1  ? C EA3 .   ? A EA3 302 ? 1_555 117.2 ? 
# 
loop_
_struct_mon_prot_cis.pdbx_id 
_struct_mon_prot_cis.label_comp_id 
_struct_mon_prot_cis.label_seq_id 
_struct_mon_prot_cis.label_asym_id 
_struct_mon_prot_cis.label_alt_id 
_struct_mon_prot_cis.pdbx_PDB_ins_code 
_struct_mon_prot_cis.auth_comp_id 
_struct_mon_prot_cis.auth_seq_id 
_struct_mon_prot_cis.auth_asym_id 
_struct_mon_prot_cis.pdbx_label_comp_id_2 
_struct_mon_prot_cis.pdbx_label_seq_id_2 
_struct_mon_prot_cis.pdbx_label_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_ins_code_2 
_struct_mon_prot_cis.pdbx_auth_comp_id_2 
_struct_mon_prot_cis.pdbx_auth_seq_id_2 
_struct_mon_prot_cis.pdbx_auth_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_model_num 
_struct_mon_prot_cis.pdbx_omega_angle 
1 SER 29  A . ? SER 29  A PRO 30  A ? PRO 30  A 1 -4.23 
2 PRO 200 A . ? PRO 201 A PRO 201 A ? PRO 202 A 1 5.52  
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 2  ? 
AA2 ? 10 ? 
AA3 ? 6  ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2  ? parallel      
AA2 1 2  ? parallel      
AA2 2 3  ? anti-parallel 
AA2 3 4  ? anti-parallel 
AA2 4 5  ? parallel      
AA2 5 6  ? anti-parallel 
AA2 6 7  ? anti-parallel 
AA2 7 8  ? anti-parallel 
AA2 8 9  ? anti-parallel 
AA2 9 10 ? anti-parallel 
AA3 1 2  ? anti-parallel 
AA3 2 3  ? anti-parallel 
AA3 3 4  ? anti-parallel 
AA3 4 5  ? anti-parallel 
AA3 5 6  ? parallel      
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1  ASP A 32  ? ILE A 33  ? ASP A 32  ILE A 33  
AA1 2  THR A 108 ? VAL A 109 ? THR A 108 VAL A 109 
AA2 1  LYS A 39  ? TYR A 40  ? LYS A 39  TYR A 40  
AA2 2  LYS A 256 ? ALA A 257 ? LYS A 257 ALA A 258 
AA2 3  TYR A 190 ? GLY A 195 ? TYR A 191 GLY A 196 
AA2 4  VAL A 206 ? LEU A 211 ? VAL A 207 LEU A 212 
AA2 5  LEU A 140 ? VAL A 149 ? LEU A 141 VAL A 150 
AA2 6  ALA A 116 ? ASN A 124 ? ALA A 116 ASN A 124 
AA2 7  TYR A 88  ? TRP A 97  ? TYR A 88  TRP A 97  
AA2 8  PHE A 66  ? PHE A 70  ? PHE A 66  PHE A 70  
AA2 9  SER A 56  ? ASN A 61  ? SER A 56  ASN A 61  
AA2 10 SER A 172 ? ASP A 174 ? SER A 173 ASP A 175 
AA3 1  LEU A 47  ? SER A 50  ? LEU A 47  SER A 50  
AA3 2  VAL A 78  ? GLY A 81  ? VAL A 78  GLY A 81  
AA3 3  TYR A 88  ? TRP A 97  ? TYR A 88  TRP A 97  
AA3 4  ALA A 116 ? ASN A 124 ? ALA A 116 ASN A 124 
AA3 5  LEU A 140 ? VAL A 149 ? LEU A 141 VAL A 150 
AA3 6  ILE A 215 ? VAL A 217 ? ILE A 216 VAL A 218 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2  N ILE A 33  ? N ILE A 33  O THR A 108 ? O THR A 108 
AA2 1 2  N LYS A 39  ? N LYS A 39  O ALA A 257 ? O ALA A 258 
AA2 2 3  O LYS A 256 ? O LYS A 257 N THR A 192 ? N THR A 193 
AA2 3 4  N GLY A 195 ? N GLY A 196 O VAL A 206 ? O VAL A 207 
AA2 4 5  O LEU A 211 ? O LEU A 212 N GLY A 144 ? N GLY A 145 
AA2 5 6  O ILE A 145 ? O ILE A 146 N LEU A 118 ? N LEU A 118 
AA2 6 7  O HIS A 119 ? O HIS A 119 N HIS A 94  ? N HIS A 94  
AA2 7 8  O PHE A 93  ? O PHE A 93  N VAL A 68  ? N VAL A 68  
AA2 8 9  O GLU A 69  ? O GLU A 69  N LEU A 57  ? N LEU A 57  
AA2 9 10 N ILE A 59  ? N ILE A 59  O ALA A 173 ? O ALA A 174 
AA3 1 2  N SER A 48  ? N SER A 48  O LYS A 80  ? O LYS A 80  
AA3 2 3  N LEU A 79  ? N LEU A 79  O TYR A 88  ? O TYR A 88  
AA3 3 4  N HIS A 94  ? N HIS A 94  O HIS A 119 ? O HIS A 119 
AA3 4 5  N LEU A 118 ? N LEU A 118 O ILE A 145 ? O ILE A 146 
AA3 5 6  N PHE A 146 ? N PHE A 147 O ILE A 215 ? O ILE A 216 
# 
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 EA3 302 ? 15 'binding site for residue EA3 A 302' 
AC3 Software A DMS 303 ? 6  'binding site for residue DMS A 303' 
# 
loop_
_struct_site_gen.id 
_struct_site_gen.site_id 
_struct_site_gen.pdbx_num_res 
_struct_site_gen.label_comp_id 
_struct_site_gen.label_asym_id 
_struct_site_gen.label_seq_id 
_struct_site_gen.pdbx_auth_ins_code 
_struct_site_gen.auth_comp_id 
_struct_site_gen.auth_asym_id 
_struct_site_gen.auth_seq_id 
_struct_site_gen.label_atom_id 
_struct_site_gen.label_alt_id 
_struct_site_gen.symmetry 
_struct_site_gen.details 
1  AC1 4  HIS A 94  ? HIS A 94  . ? 1_555 ? 
2  AC1 4  HIS A 96  ? HIS A 96  . ? 1_555 ? 
3  AC1 4  HIS A 119 ? HIS A 119 . ? 1_555 ? 
4  AC1 4  EA3 C .   ? EA3 A 302 . ? 1_555 ? 
5  AC2 15 TRP A 5   ? TRP A 5   . ? 1_555 ? 
6  AC2 15 GLN A 92  ? GLN A 92  . ? 1_555 ? 
7  AC2 15 HIS A 94  ? HIS A 94  . ? 1_555 ? 
8  AC2 15 HIS A 96  ? HIS A 96  . ? 1_555 ? 
9  AC2 15 HIS A 119 ? HIS A 119 . ? 1_555 ? 
10 AC2 15 VAL A 142 ? VAL A 143 . ? 1_555 ? 
11 AC2 15 LEU A 197 ? LEU A 198 . ? 1_555 ? 
12 AC2 15 THR A 198 ? THR A 199 . ? 1_555 ? 
13 AC2 15 THR A 199 ? THR A 200 . ? 1_555 ? 
14 AC2 15 TRP A 208 ? TRP A 209 . ? 1_555 ? 
15 AC2 15 ZN  B .   ? ZN  A 301 . ? 1_555 ? 
16 AC2 15 HOH E .   ? HOH A 416 . ? 1_555 ? 
17 AC2 15 HOH E .   ? HOH A 504 . ? 1_555 ? 
18 AC2 15 HOH E .   ? HOH A 521 . ? 1_555 ? 
19 AC2 15 HOH E .   ? HOH A 579 . ? 1_555 ? 
20 AC3 6  TYR A 7   ? TYR A 7   . ? 1_555 ? 
21 AC3 6  ASP A 242 ? ASP A 243 . ? 1_555 ? 
22 AC3 6  TRP A 244 ? TRP A 245 . ? 1_555 ? 
23 AC3 6  PRO A 246 ? PRO A 247 . ? 1_555 ? 
24 AC3 6  HOH E .   ? HOH A 647 . ? 1_555 ? 
25 AC3 6  HOH E .   ? HOH A 660 . ? 1_555 ? 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 ARG A 27  ? ? -141.70 54.29   
2 1 LYS A 76  ? ? -121.25 -76.05  
3 1 LYS A 111 ? ? 74.65   -5.82   
4 1 PHE A 176 ? ? -152.07 70.59   
5 1 ASN A 244 ? ? -99.89  49.67   
6 1 LYS A 252 ? ? 57.40   -140.91 
# 
_phasing.method   MR 
# 
loop_
_pdbx_distant_solvent_atoms.id 
_pdbx_distant_solvent_atoms.PDB_model_num 
_pdbx_distant_solvent_atoms.auth_atom_id 
_pdbx_distant_solvent_atoms.label_alt_id 
_pdbx_distant_solvent_atoms.auth_asym_id 
_pdbx_distant_solvent_atoms.auth_comp_id 
_pdbx_distant_solvent_atoms.auth_seq_id 
_pdbx_distant_solvent_atoms.PDB_ins_code 
_pdbx_distant_solvent_atoms.neighbor_macromolecule_distance 
_pdbx_distant_solvent_atoms.neighbor_ligand_distance 
1 1 O ? A HOH 738 ? 5.82 . 
2 1 O ? A HOH 739 ? 5.95 . 
3 1 O ? A HOH 740 ? 6.45 . 
# 
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 
# 
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  
DMS S    S  N N 88  
DMS O    O  N N 89  
DMS C1   C  N N 90  
DMS C2   C  N N 91  
DMS H11  H  N N 92  
DMS H12  H  N N 93  
DMS H13  H  N N 94  
DMS H21  H  N N 95  
DMS H22  H  N N 96  
DMS H23  H  N N 97  
EA3 O13  O  N N 98  
EA3 C12  C  N N 99  
EA3 N14  N  N N 100 
EA3 C15  C  N N 101 
EA3 C16  C  N N 102 
EA3 O17  O  N N 103 
EA3 C9   C  Y N 104 
EA3 C10  C  Y N 105 
EA3 C3   C  Y N 106 
EA3 S2   S  N N 107 
EA3 O4   O  N N 108 
EA3 O5   O  N N 109 
EA3 N1   N  N N 110 
EA3 C8   C  Y N 111 
EA3 C7   C  Y N 112 
EA3 C6   C  Y N 113 
EA3 CL1  CL N N 114 
EA3 S18  S  N N 115 
EA3 C19  C  N N 116 
EA3 C24  C  N N 117 
EA3 C23  C  N N 118 
EA3 C22  C  N N 119 
EA3 C21  C  N N 120 
EA3 C20  C  N N 121 
EA3 H1   H  N N 122 
EA3 H2   H  N N 123 
EA3 H3   H  N N 124 
EA3 H4   H  N N 125 
EA3 H5   H  N N 126 
EA3 H6   H  N N 127 
EA3 H7   H  N N 128 
EA3 H8   H  N N 129 
EA3 H9   H  N N 130 
EA3 H10  H  N N 131 
EA3 H11  H  N N 132 
EA3 H12  H  N N 133 
EA3 H13  H  N N 134 
EA3 H14  H  N N 135 
EA3 H15  H  N N 136 
EA3 H16  H  N N 137 
EA3 H17  H  N N 138 
EA3 H18  H  N N 139 
EA3 H19  H  N N 140 
EA3 H20  H  N N 141 
EA3 H21  H  N N 142 
GLN N    N  N N 143 
GLN CA   C  N S 144 
GLN C    C  N N 145 
GLN O    O  N N 146 
GLN CB   C  N N 147 
GLN CG   C  N N 148 
GLN CD   C  N N 149 
GLN OE1  O  N N 150 
GLN NE2  N  N N 151 
GLN OXT  O  N N 152 
GLN H    H  N N 153 
GLN H2   H  N N 154 
GLN HA   H  N N 155 
GLN HB2  H  N N 156 
GLN HB3  H  N N 157 
GLN HG2  H  N N 158 
GLN HG3  H  N N 159 
GLN HE21 H  N N 160 
GLN HE22 H  N N 161 
GLN HXT  H  N N 162 
GLU N    N  N N 163 
GLU CA   C  N S 164 
GLU C    C  N N 165 
GLU O    O  N N 166 
GLU CB   C  N N 167 
GLU CG   C  N N 168 
GLU CD   C  N N 169 
GLU OE1  O  N N 170 
GLU OE2  O  N N 171 
GLU OXT  O  N N 172 
GLU H    H  N N 173 
GLU H2   H  N N 174 
GLU HA   H  N N 175 
GLU HB2  H  N N 176 
GLU HB3  H  N N 177 
GLU HG2  H  N N 178 
GLU HG3  H  N N 179 
GLU HE2  H  N N 180 
GLU HXT  H  N N 181 
GLY N    N  N N 182 
GLY CA   C  N N 183 
GLY C    C  N N 184 
GLY O    O  N N 185 
GLY OXT  O  N N 186 
GLY H    H  N N 187 
GLY H2   H  N N 188 
GLY HA2  H  N N 189 
GLY HA3  H  N N 190 
GLY HXT  H  N N 191 
HIS N    N  N N 192 
HIS CA   C  N S 193 
HIS C    C  N N 194 
HIS O    O  N N 195 
HIS CB   C  N N 196 
HIS CG   C  Y N 197 
HIS ND1  N  Y N 198 
HIS CD2  C  Y N 199 
HIS CE1  C  Y N 200 
HIS NE2  N  Y N 201 
HIS OXT  O  N N 202 
HIS H    H  N N 203 
HIS H2   H  N N 204 
HIS HA   H  N N 205 
HIS HB2  H  N N 206 
HIS HB3  H  N N 207 
HIS HD1  H  N N 208 
HIS HD2  H  N N 209 
HIS HE1  H  N N 210 
HIS HE2  H  N N 211 
HIS HXT  H  N N 212 
HOH O    O  N N 213 
HOH H1   H  N N 214 
HOH H2   H  N N 215 
ILE N    N  N N 216 
ILE CA   C  N S 217 
ILE C    C  N N 218 
ILE O    O  N N 219 
ILE CB   C  N S 220 
ILE CG1  C  N N 221 
ILE CG2  C  N N 222 
ILE CD1  C  N N 223 
ILE OXT  O  N N 224 
ILE H    H  N N 225 
ILE H2   H  N N 226 
ILE HA   H  N N 227 
ILE HB   H  N N 228 
ILE HG12 H  N N 229 
ILE HG13 H  N N 230 
ILE HG21 H  N N 231 
ILE HG22 H  N N 232 
ILE HG23 H  N N 233 
ILE HD11 H  N N 234 
ILE HD12 H  N N 235 
ILE HD13 H  N N 236 
ILE HXT  H  N N 237 
LEU N    N  N N 238 
LEU CA   C  N S 239 
LEU C    C  N N 240 
LEU O    O  N N 241 
LEU CB   C  N N 242 
LEU CG   C  N N 243 
LEU CD1  C  N N 244 
LEU CD2  C  N N 245 
LEU OXT  O  N N 246 
LEU H    H  N N 247 
LEU H2   H  N N 248 
LEU HA   H  N N 249 
LEU HB2  H  N N 250 
LEU HB3  H  N N 251 
LEU HG   H  N N 252 
LEU HD11 H  N N 253 
LEU HD12 H  N N 254 
LEU HD13 H  N N 255 
LEU HD21 H  N N 256 
LEU HD22 H  N N 257 
LEU HD23 H  N N 258 
LEU HXT  H  N N 259 
LYS N    N  N N 260 
LYS CA   C  N S 261 
LYS C    C  N N 262 
LYS O    O  N N 263 
LYS CB   C  N N 264 
LYS CG   C  N N 265 
LYS CD   C  N N 266 
LYS CE   C  N N 267 
LYS NZ   N  N N 268 
LYS OXT  O  N N 269 
LYS H    H  N N 270 
LYS H2   H  N N 271 
LYS HA   H  N N 272 
LYS HB2  H  N N 273 
LYS HB3  H  N N 274 
LYS HG2  H  N N 275 
LYS HG3  H  N N 276 
LYS HD2  H  N N 277 
LYS HD3  H  N N 278 
LYS HE2  H  N N 279 
LYS HE3  H  N N 280 
LYS HZ1  H  N N 281 
LYS HZ2  H  N N 282 
LYS HZ3  H  N N 283 
LYS HXT  H  N N 284 
MET N    N  N N 285 
MET CA   C  N S 286 
MET C    C  N N 287 
MET O    O  N N 288 
MET CB   C  N N 289 
MET CG   C  N N 290 
MET SD   S  N N 291 
MET CE   C  N N 292 
MET OXT  O  N N 293 
MET H    H  N N 294 
MET H2   H  N N 295 
MET HA   H  N N 296 
MET HB2  H  N N 297 
MET HB3  H  N N 298 
MET HG2  H  N N 299 
MET HG3  H  N N 300 
MET HE1  H  N N 301 
MET HE2  H  N N 302 
MET HE3  H  N N 303 
MET HXT  H  N N 304 
PHE N    N  N N 305 
PHE CA   C  N S 306 
PHE C    C  N N 307 
PHE O    O  N N 308 
PHE CB   C  N N 309 
PHE CG   C  Y N 310 
PHE CD1  C  Y N 311 
PHE CD2  C  Y N 312 
PHE CE1  C  Y N 313 
PHE CE2  C  Y N 314 
PHE CZ   C  Y N 315 
PHE OXT  O  N N 316 
PHE H    H  N N 317 
PHE H2   H  N N 318 
PHE HA   H  N N 319 
PHE HB2  H  N N 320 
PHE HB3  H  N N 321 
PHE HD1  H  N N 322 
PHE HD2  H  N N 323 
PHE HE1  H  N N 324 
PHE HE2  H  N N 325 
PHE HZ   H  N N 326 
PHE HXT  H  N N 327 
PRO N    N  N N 328 
PRO CA   C  N S 329 
PRO C    C  N N 330 
PRO O    O  N N 331 
PRO CB   C  N N 332 
PRO CG   C  N N 333 
PRO CD   C  N N 334 
PRO OXT  O  N N 335 
PRO H    H  N N 336 
PRO HA   H  N N 337 
PRO HB2  H  N N 338 
PRO HB3  H  N N 339 
PRO HG2  H  N N 340 
PRO HG3  H  N N 341 
PRO HD2  H  N N 342 
PRO HD3  H  N N 343 
PRO HXT  H  N N 344 
SER N    N  N N 345 
SER CA   C  N S 346 
SER C    C  N N 347 
SER O    O  N N 348 
SER CB   C  N N 349 
SER OG   O  N N 350 
SER OXT  O  N N 351 
SER H    H  N N 352 
SER H2   H  N N 353 
SER HA   H  N N 354 
SER HB2  H  N N 355 
SER HB3  H  N N 356 
SER HG   H  N N 357 
SER HXT  H  N N 358 
THR N    N  N N 359 
THR CA   C  N S 360 
THR C    C  N N 361 
THR O    O  N N 362 
THR CB   C  N R 363 
THR OG1  O  N N 364 
THR CG2  C  N N 365 
THR OXT  O  N N 366 
THR H    H  N N 367 
THR H2   H  N N 368 
THR HA   H  N N 369 
THR HB   H  N N 370 
THR HG1  H  N N 371 
THR HG21 H  N N 372 
THR HG22 H  N N 373 
THR HG23 H  N N 374 
THR HXT  H  N N 375 
TRP N    N  N N 376 
TRP CA   C  N S 377 
TRP C    C  N N 378 
TRP O    O  N N 379 
TRP CB   C  N N 380 
TRP CG   C  Y N 381 
TRP CD1  C  Y N 382 
TRP CD2  C  Y N 383 
TRP NE1  N  Y N 384 
TRP CE2  C  Y N 385 
TRP CE3  C  Y N 386 
TRP CZ2  C  Y N 387 
TRP CZ3  C  Y N 388 
TRP CH2  C  Y N 389 
TRP OXT  O  N N 390 
TRP H    H  N N 391 
TRP H2   H  N N 392 
TRP HA   H  N N 393 
TRP HB2  H  N N 394 
TRP HB3  H  N N 395 
TRP HD1  H  N N 396 
TRP HE1  H  N N 397 
TRP HE3  H  N N 398 
TRP HZ2  H  N N 399 
TRP HZ3  H  N N 400 
TRP HH2  H  N N 401 
TRP HXT  H  N N 402 
TYR N    N  N N 403 
TYR CA   C  N S 404 
TYR C    C  N N 405 
TYR O    O  N N 406 
TYR CB   C  N N 407 
TYR CG   C  Y N 408 
TYR CD1  C  Y N 409 
TYR CD2  C  Y N 410 
TYR CE1  C  Y N 411 
TYR CE2  C  Y N 412 
TYR CZ   C  Y N 413 
TYR OH   O  N N 414 
TYR OXT  O  N N 415 
TYR H    H  N N 416 
TYR H2   H  N N 417 
TYR HA   H  N N 418 
TYR HB2  H  N N 419 
TYR HB3  H  N N 420 
TYR HD1  H  N N 421 
TYR HD2  H  N N 422 
TYR HE1  H  N N 423 
TYR HE2  H  N N 424 
TYR HH   H  N N 425 
TYR HXT  H  N N 426 
VAL N    N  N N 427 
VAL CA   C  N S 428 
VAL C    C  N N 429 
VAL O    O  N N 430 
VAL CB   C  N N 431 
VAL CG1  C  N N 432 
VAL CG2  C  N N 433 
VAL OXT  O  N N 434 
VAL H    H  N N 435 
VAL H2   H  N N 436 
VAL HA   H  N N 437 
VAL HB   H  N N 438 
VAL HG11 H  N N 439 
VAL HG12 H  N N 440 
VAL HG13 H  N N 441 
VAL HG21 H  N N 442 
VAL HG22 H  N N 443 
VAL HG23 H  N N 444 
VAL HXT  H  N N 445 
ZN  ZN   ZN N N 446 
# 
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  
DMS S   O    doub N N 83  
DMS S   C1   sing N N 84  
DMS S   C2   sing N N 85  
DMS C1  H11  sing N N 86  
DMS C1  H12  sing N N 87  
DMS C1  H13  sing N N 88  
DMS C2  H21  sing N N 89  
DMS C2  H22  sing N N 90  
DMS C2  H23  sing N N 91  
EA3 C16 O17  sing N N 92  
EA3 C16 C15  sing N N 93  
EA3 C15 N14  sing N N 94  
EA3 O13 C12  doub N N 95  
EA3 C20 C21  sing N N 96  
EA3 C20 C19  sing N N 97  
EA3 C21 C22  sing N N 98  
EA3 C12 N14  sing N N 99  
EA3 C12 C9   sing N N 100 
EA3 C19 S18  sing N N 101 
EA3 C19 C24  sing N N 102 
EA3 S18 C8   sing N N 103 
EA3 C22 C23  sing N N 104 
EA3 C9  C8   doub Y N 105 
EA3 C9  C10  sing Y N 106 
EA3 C8  C7   sing Y N 107 
EA3 C24 C23  sing N N 108 
EA3 C10 C3   doub Y N 109 
EA3 C7  C6   doub Y N 110 
EA3 C3  C6   sing Y N 111 
EA3 C3  S2   sing N N 112 
EA3 C6  CL1  sing N N 113 
EA3 N1  S2   sing N N 114 
EA3 O4  S2   doub N N 115 
EA3 S2  O5   doub N N 116 
EA3 N14 H1   sing N N 117 
EA3 C15 H2   sing N N 118 
EA3 C15 H3   sing N N 119 
EA3 C16 H4   sing N N 120 
EA3 C16 H5   sing N N 121 
EA3 O17 H6   sing N N 122 
EA3 C10 H7   sing N N 123 
EA3 N1  H8   sing N N 124 
EA3 N1  H9   sing N N 125 
EA3 C7  H10  sing N N 126 
EA3 C19 H11  sing N N 127 
EA3 C24 H12  sing N N 128 
EA3 C24 H13  sing N N 129 
EA3 C23 H14  sing N N 130 
EA3 C23 H15  sing N N 131 
EA3 C22 H16  sing N N 132 
EA3 C22 H17  sing N N 133 
EA3 C21 H18  sing N N 134 
EA3 C21 H19  sing N N 135 
EA3 C20 H20  sing N N 136 
EA3 C20 H21  sing N N 137 
GLN N   CA   sing N N 138 
GLN N   H    sing N N 139 
GLN N   H2   sing N N 140 
GLN CA  C    sing N N 141 
GLN CA  CB   sing N N 142 
GLN CA  HA   sing N N 143 
GLN C   O    doub N N 144 
GLN C   OXT  sing N N 145 
GLN CB  CG   sing N N 146 
GLN CB  HB2  sing N N 147 
GLN CB  HB3  sing N N 148 
GLN CG  CD   sing N N 149 
GLN CG  HG2  sing N N 150 
GLN CG  HG3  sing N N 151 
GLN CD  OE1  doub N N 152 
GLN CD  NE2  sing N N 153 
GLN NE2 HE21 sing N N 154 
GLN NE2 HE22 sing N N 155 
GLN OXT HXT  sing N N 156 
GLU N   CA   sing N N 157 
GLU N   H    sing N N 158 
GLU N   H2   sing N N 159 
GLU CA  C    sing N N 160 
GLU CA  CB   sing N N 161 
GLU CA  HA   sing N N 162 
GLU C   O    doub N N 163 
GLU C   OXT  sing N N 164 
GLU CB  CG   sing N N 165 
GLU CB  HB2  sing N N 166 
GLU CB  HB3  sing N N 167 
GLU CG  CD   sing N N 168 
GLU CG  HG2  sing N N 169 
GLU CG  HG3  sing N N 170 
GLU CD  OE1  doub N N 171 
GLU CD  OE2  sing N N 172 
GLU OE2 HE2  sing N N 173 
GLU OXT HXT  sing N N 174 
GLY N   CA   sing N N 175 
GLY N   H    sing N N 176 
GLY N   H2   sing N N 177 
GLY CA  C    sing N N 178 
GLY CA  HA2  sing N N 179 
GLY CA  HA3  sing N N 180 
GLY C   O    doub N N 181 
GLY C   OXT  sing N N 182 
GLY OXT HXT  sing N N 183 
HIS N   CA   sing N N 184 
HIS N   H    sing N N 185 
HIS N   H2   sing N N 186 
HIS CA  C    sing N N 187 
HIS CA  CB   sing N N 188 
HIS CA  HA   sing N N 189 
HIS C   O    doub N N 190 
HIS C   OXT  sing N N 191 
HIS CB  CG   sing N N 192 
HIS CB  HB2  sing N N 193 
HIS CB  HB3  sing N N 194 
HIS CG  ND1  sing Y N 195 
HIS CG  CD2  doub Y N 196 
HIS ND1 CE1  doub Y N 197 
HIS ND1 HD1  sing N N 198 
HIS CD2 NE2  sing Y N 199 
HIS CD2 HD2  sing N N 200 
HIS CE1 NE2  sing Y N 201 
HIS CE1 HE1  sing N N 202 
HIS NE2 HE2  sing N N 203 
HIS OXT HXT  sing N N 204 
HOH O   H1   sing N N 205 
HOH O   H2   sing N N 206 
ILE N   CA   sing N N 207 
ILE N   H    sing N N 208 
ILE N   H2   sing N N 209 
ILE CA  C    sing N N 210 
ILE CA  CB   sing N N 211 
ILE CA  HA   sing N N 212 
ILE C   O    doub N N 213 
ILE C   OXT  sing N N 214 
ILE CB  CG1  sing N N 215 
ILE CB  CG2  sing N N 216 
ILE CB  HB   sing N N 217 
ILE CG1 CD1  sing N N 218 
ILE CG1 HG12 sing N N 219 
ILE CG1 HG13 sing N N 220 
ILE CG2 HG21 sing N N 221 
ILE CG2 HG22 sing N N 222 
ILE CG2 HG23 sing N N 223 
ILE CD1 HD11 sing N N 224 
ILE CD1 HD12 sing N N 225 
ILE CD1 HD13 sing N N 226 
ILE OXT HXT  sing N N 227 
LEU N   CA   sing N N 228 
LEU N   H    sing N N 229 
LEU N   H2   sing N N 230 
LEU CA  C    sing N N 231 
LEU CA  CB   sing N N 232 
LEU CA  HA   sing N N 233 
LEU C   O    doub N N 234 
LEU C   OXT  sing N N 235 
LEU CB  CG   sing N N 236 
LEU CB  HB2  sing N N 237 
LEU CB  HB3  sing N N 238 
LEU CG  CD1  sing N N 239 
LEU CG  CD2  sing N N 240 
LEU CG  HG   sing N N 241 
LEU CD1 HD11 sing N N 242 
LEU CD1 HD12 sing N N 243 
LEU CD1 HD13 sing N N 244 
LEU CD2 HD21 sing N N 245 
LEU CD2 HD22 sing N N 246 
LEU CD2 HD23 sing N N 247 
LEU OXT HXT  sing N N 248 
LYS N   CA   sing N N 249 
LYS N   H    sing N N 250 
LYS N   H2   sing N N 251 
LYS CA  C    sing N N 252 
LYS CA  CB   sing N N 253 
LYS CA  HA   sing N N 254 
LYS C   O    doub N N 255 
LYS C   OXT  sing N N 256 
LYS CB  CG   sing N N 257 
LYS CB  HB2  sing N N 258 
LYS CB  HB3  sing N N 259 
LYS CG  CD   sing N N 260 
LYS CG  HG2  sing N N 261 
LYS CG  HG3  sing N N 262 
LYS CD  CE   sing N N 263 
LYS CD  HD2  sing N N 264 
LYS CD  HD3  sing N N 265 
LYS CE  NZ   sing N N 266 
LYS CE  HE2  sing N N 267 
LYS CE  HE3  sing N N 268 
LYS NZ  HZ1  sing N N 269 
LYS NZ  HZ2  sing N N 270 
LYS NZ  HZ3  sing N N 271 
LYS OXT HXT  sing N N 272 
MET N   CA   sing N N 273 
MET N   H    sing N N 274 
MET N   H2   sing N N 275 
MET CA  C    sing N N 276 
MET CA  CB   sing N N 277 
MET CA  HA   sing N N 278 
MET C   O    doub N N 279 
MET C   OXT  sing N N 280 
MET CB  CG   sing N N 281 
MET CB  HB2  sing N N 282 
MET CB  HB3  sing N N 283 
MET CG  SD   sing N N 284 
MET CG  HG2  sing N N 285 
MET CG  HG3  sing N N 286 
MET SD  CE   sing N N 287 
MET CE  HE1  sing N N 288 
MET CE  HE2  sing N N 289 
MET CE  HE3  sing N N 290 
MET OXT HXT  sing N N 291 
PHE N   CA   sing N N 292 
PHE N   H    sing N N 293 
PHE N   H2   sing N N 294 
PHE CA  C    sing N N 295 
PHE CA  CB   sing N N 296 
PHE CA  HA   sing N N 297 
PHE C   O    doub N N 298 
PHE C   OXT  sing N N 299 
PHE CB  CG   sing N N 300 
PHE CB  HB2  sing N N 301 
PHE CB  HB3  sing N N 302 
PHE CG  CD1  doub Y N 303 
PHE CG  CD2  sing Y N 304 
PHE CD1 CE1  sing Y N 305 
PHE CD1 HD1  sing N N 306 
PHE CD2 CE2  doub Y N 307 
PHE CD2 HD2  sing N N 308 
PHE CE1 CZ   doub Y N 309 
PHE CE1 HE1  sing N N 310 
PHE CE2 CZ   sing Y N 311 
PHE CE2 HE2  sing N N 312 
PHE CZ  HZ   sing N N 313 
PHE OXT HXT  sing N N 314 
PRO N   CA   sing N N 315 
PRO N   CD   sing N N 316 
PRO N   H    sing N N 317 
PRO CA  C    sing N N 318 
PRO CA  CB   sing N N 319 
PRO CA  HA   sing N N 320 
PRO C   O    doub N N 321 
PRO C   OXT  sing N N 322 
PRO CB  CG   sing N N 323 
PRO CB  HB2  sing N N 324 
PRO CB  HB3  sing N N 325 
PRO CG  CD   sing N N 326 
PRO CG  HG2  sing N N 327 
PRO CG  HG3  sing N N 328 
PRO CD  HD2  sing N N 329 
PRO CD  HD3  sing N N 330 
PRO OXT HXT  sing N N 331 
SER N   CA   sing N N 332 
SER N   H    sing N N 333 
SER N   H2   sing N N 334 
SER CA  C    sing N N 335 
SER CA  CB   sing N N 336 
SER CA  HA   sing N N 337 
SER C   O    doub N N 338 
SER C   OXT  sing N N 339 
SER CB  OG   sing N N 340 
SER CB  HB2  sing N N 341 
SER CB  HB3  sing N N 342 
SER OG  HG   sing N N 343 
SER OXT HXT  sing N N 344 
THR N   CA   sing N N 345 
THR N   H    sing N N 346 
THR N   H2   sing N N 347 
THR CA  C    sing N N 348 
THR CA  CB   sing N N 349 
THR CA  HA   sing N N 350 
THR C   O    doub N N 351 
THR C   OXT  sing N N 352 
THR CB  OG1  sing N N 353 
THR CB  CG2  sing N N 354 
THR CB  HB   sing N N 355 
THR OG1 HG1  sing N N 356 
THR CG2 HG21 sing N N 357 
THR CG2 HG22 sing N N 358 
THR CG2 HG23 sing N N 359 
THR OXT HXT  sing N N 360 
TRP N   CA   sing N N 361 
TRP N   H    sing N N 362 
TRP N   H2   sing N N 363 
TRP CA  C    sing N N 364 
TRP CA  CB   sing N N 365 
TRP CA  HA   sing N N 366 
TRP C   O    doub N N 367 
TRP C   OXT  sing N N 368 
TRP CB  CG   sing N N 369 
TRP CB  HB2  sing N N 370 
TRP CB  HB3  sing N N 371 
TRP CG  CD1  doub Y N 372 
TRP CG  CD2  sing Y N 373 
TRP CD1 NE1  sing Y N 374 
TRP CD1 HD1  sing N N 375 
TRP CD2 CE2  doub Y N 376 
TRP CD2 CE3  sing Y N 377 
TRP NE1 CE2  sing Y N 378 
TRP NE1 HE1  sing N N 379 
TRP CE2 CZ2  sing Y N 380 
TRP CE3 CZ3  doub Y N 381 
TRP CE3 HE3  sing N N 382 
TRP CZ2 CH2  doub Y N 383 
TRP CZ2 HZ2  sing N N 384 
TRP CZ3 CH2  sing Y N 385 
TRP CZ3 HZ3  sing N N 386 
TRP CH2 HH2  sing N N 387 
TRP OXT HXT  sing N N 388 
TYR N   CA   sing N N 389 
TYR N   H    sing N N 390 
TYR N   H2   sing N N 391 
TYR CA  C    sing N N 392 
TYR CA  CB   sing N N 393 
TYR CA  HA   sing N N 394 
TYR C   O    doub N N 395 
TYR C   OXT  sing N N 396 
TYR CB  CG   sing N N 397 
TYR CB  HB2  sing N N 398 
TYR CB  HB3  sing N N 399 
TYR CG  CD1  doub Y N 400 
TYR CG  CD2  sing Y N 401 
TYR CD1 CE1  sing Y N 402 
TYR CD1 HD1  sing N N 403 
TYR CD2 CE2  doub Y N 404 
TYR CD2 HD2  sing N N 405 
TYR CE1 CZ   doub Y N 406 
TYR CE1 HE1  sing N N 407 
TYR CE2 CZ   sing Y N 408 
TYR CE2 HE2  sing N N 409 
TYR CZ  OH   sing N N 410 
TYR OH  HH   sing N N 411 
TYR OXT HXT  sing N N 412 
VAL N   CA   sing N N 413 
VAL N   H    sing N N 414 
VAL N   H2   sing N N 415 
VAL CA  C    sing N N 416 
VAL CA  CB   sing N N 417 
VAL CA  HA   sing N N 418 
VAL C   O    doub N N 419 
VAL C   OXT  sing N N 420 
VAL CB  CG1  sing N N 421 
VAL CB  CG2  sing N N 422 
VAL CB  HB   sing N N 423 
VAL CG1 HG11 sing N N 424 
VAL CG1 HG12 sing N N 425 
VAL CG1 HG13 sing N N 426 
VAL CG2 HG21 sing N N 427 
VAL CG2 HG22 sing N N 428 
VAL CG2 HG23 sing N N 429 
VAL OXT HXT  sing N N 430 
# 
_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   3HLJ 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    6R6F 
_atom_sites.fract_transf_matrix[1][1]   0.023636 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.005976 
_atom_sites.fract_transf_matrix[2][1]   -0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.023953 
_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]   0.014262 
_atom_sites.fract_transf_vector[1]      0.000000 
_atom_sites.fract_transf_vector[2]      0.000000 
_atom_sites.fract_transf_vector[3]      0.000000 
# 
loop_
_atom_type.symbol 
C  
CL 
N  
O  
S  
ZN 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N  N   . HIS A 1 3   ? 14.272  -2.383  8.072   1.00 68.55  ? 3   HIS A N   1 
ATOM   2    C  CA  . HIS A 1 3   ? 13.705  -0.974  7.901   1.00 69.43  ? 3   HIS A CA  1 
ATOM   3    C  C   . HIS A 1 3   ? 12.468  -0.782  8.787   1.00 52.81  ? 3   HIS A C   1 
ATOM   4    O  O   . HIS A 1 3   ? 12.612  -0.696  10.015  1.00 52.61  ? 3   HIS A O   1 
ATOM   5    C  CB  . HIS A 1 3   ? 13.641  -0.499  6.417   1.00 70.28  ? 3   HIS A CB  1 
ATOM   6    C  CG  . HIS A 1 3   ? 12.920  0.803   6.120   1.00 113.17 ? 3   HIS A CG  1 
ATOM   7    N  ND1 . HIS A 1 3   ? 11.554  0.875   5.735   1.00 119.36 ? 3   HIS A ND1 1 
ATOM   8    C  CD2 . HIS A 1 3   ? 13.372  2.098   6.090   1.00 108.02 ? 3   HIS A CD2 1 
ATOM   9    C  CE1 . HIS A 1 3   ? 11.208  2.139   5.501   1.00 111.26 ? 3   HIS A CE1 1 
ATOM   10   N  NE2 . HIS A 1 3   ? 12.312  2.914   5.712   1.00 123.11 ? 3   HIS A NE2 1 
ATOM   11   N  N   . HIS A 1 4   ? 11.270  -0.731  8.165   1.00 39.48  ? 4   HIS A N   1 
ATOM   12   C  CA  . HIS A 1 4   ? 10.127  -0.112  8.821   1.00 31.25  ? 4   HIS A CA  1 
ATOM   13   C  C   . HIS A 1 4   ? 9.328   -1.185  9.536   1.00 20.58  ? 4   HIS A C   1 
ATOM   14   O  O   . HIS A 1 4   ? 9.465   -2.381  9.237   1.00 25.00  ? 4   HIS A O   1 
ATOM   15   C  CB  . HIS A 1 4   ? 9.234   0.656   7.838   1.00 31.30  ? 4   HIS A CB  1 
ATOM   16   C  CG  . HIS A 1 4   ? 8.728   1.905   8.468   1.00 36.71  ? 4   HIS A CG  1 
ATOM   17   N  ND1 . HIS A 1 4   ? 9.445   2.547   9.480   1.00 40.36  ? 4   HIS A ND1 1 
ATOM   18   C  CD2 . HIS A 1 4   ? 7.572   2.595   8.294   1.00 53.12  ? 4   HIS A CD2 1 
ATOM   19   C  CE1 . HIS A 1 4   ? 8.779   3.629   9.858   1.00 64.62  ? 4   HIS A CE1 1 
ATOM   20   N  NE2 . HIS A 1 4   ? 7.615   3.679   9.145   1.00 75.57  ? 4   HIS A NE2 1 
ATOM   21   N  N   . TRP A 1 5   ? 8.450   -0.743  10.443  1.00 18.39  ? 5   TRP A N   1 
ATOM   22   C  CA  . TRP A 1 5   ? 7.766   -1.687  11.315  1.00 15.07  ? 5   TRP A CA  1 
ATOM   23   C  C   . TRP A 1 5   ? 6.721   -2.443  10.529  1.00 14.88  ? 5   TRP A C   1 
ATOM   24   O  O   . TRP A 1 5   ? 6.173   -1.973  9.535   1.00 15.15  ? 5   TRP A O   1 
ATOM   25   C  CB  . TRP A 1 5   ? 7.156   -0.963  12.532  1.00 15.97  ? 5   TRP A CB  1 
ATOM   26   C  CG  . TRP A 1 5   ? 5.962   -0.099  12.217  1.00 14.22  ? 5   TRP A CG  1 
ATOM   27   C  CD1 . TRP A 1 5   ? 5.942   1.230   11.894  1.00 16.19  ? 5   TRP A CD1 1 
ATOM   28   C  CD2 . TRP A 1 5   ? 4.578   -0.549  12.181  1.00 12.08  ? 5   TRP A CD2 1 
ATOM   29   N  NE1 . TRP A 1 5   ? 4.657   1.668   11.707  1.00 14.36  ? 5   TRP A NE1 1 
ATOM   30   C  CE2 . TRP A 1 5   ? 3.788   0.589   11.837  1.00 13.12  ? 5   TRP A CE2 1 
ATOM   31   C  CE3 . TRP A 1 5   ? 3.928   -1.804  12.402  1.00 12.25  ? 5   TRP A CE3 1 
ATOM   32   C  CZ2 . TRP A 1 5   ? 2.406   0.536   11.698  1.00 13.95  ? 5   TRP A CZ2 1 
ATOM   33   C  CZ3 . TRP A 1 5   ? 2.541   -1.867  12.277  1.00 13.62  ? 5   TRP A CZ3 1 
ATOM   34   C  CH2 . TRP A 1 5   ? 1.787   -0.686  11.964  1.00 13.35  ? 5   TRP A CH2 1 
ATOM   35   N  N   . GLY A 1 6   ? 6.430   -3.644  11.012  1.00 12.81  ? 6   GLY A N   1 
ATOM   36   C  CA  . GLY A 1 6   ? 5.378   -4.449  10.390  1.00 13.18  ? 6   GLY A CA  1 
ATOM   37   C  C   . GLY A 1 6   ? 5.058   -5.620  11.313  1.00 12.48  ? 6   GLY A C   1 
ATOM   38   O  O   . GLY A 1 6   ? 5.075   -5.464  12.544  1.00 13.27  ? 6   GLY A O   1 
ATOM   39   N  N   . TYR A 1 7   ? 4.756   -6.774  10.709  1.00 14.49  ? 7   TYR A N   1 
ATOM   40   C  CA  . TYR A 1 7   ? 4.280   -7.911  11.476  1.00 15.53  ? 7   TYR A CA  1 
ATOM   41   C  C   . TYR A 1 7   ? 5.088   -9.174  11.126  1.00 27.45  ? 7   TYR A C   1 
ATOM   42   O  O   . TYR A 1 7   ? 4.764   -10.286 11.629  1.00 44.91  ? 7   TYR A O   1 
ATOM   43   C  CB  . TYR A 1 7   ? 2.773   -8.206  11.261  1.00 15.62  ? 7   TYR A CB  1 
ATOM   44   C  CG  . TYR A 1 7   ? 1.925   -7.090  11.826  1.00 11.80  ? 7   TYR A CG  1 
ATOM   45   C  CD1 . TYR A 1 7   ? 1.540   -7.121  13.171  1.00 11.27  ? 7   TYR A CD1 1 
ATOM   46   C  CD2 . TYR A 1 7   ? 1.477   -6.059  10.993  1.00 11.00  ? 7   TYR A CD2 1 
ATOM   47   C  CE1 . TYR A 1 7   ? 0.768   -6.056  13.652  1.00 9.76   ? 7   TYR A CE1 1 
ATOM   48   C  CE2 . TYR A 1 7   ? 0.679   -5.030  11.486  1.00 9.63   ? 7   TYR A CE2 1 
ATOM   49   C  CZ  . TYR A 1 7   ? 0.292   -5.039  12.834  1.00 9.68   ? 7   TYR A CZ  1 
ATOM   50   O  OH  . TYR A 1 7   ? -0.518  -4.048  13.312  1.00 9.85   ? 7   TYR A OH  1 
ATOM   51   N  N   . GLY A 1 8   ? 6.129   -8.960  10.278  1.00 21.25  ? 8   GLY A N   1 
ATOM   52   C  CA  . GLY A 1 8   ? 6.884   -10.020 9.616   1.00 24.39  ? 8   GLY A CA  1 
ATOM   53   C  C   . GLY A 1 8   ? 7.906   -10.595 10.577  1.00 29.53  ? 8   GLY A C   1 
ATOM   54   O  O   . GLY A 1 8   ? 7.937   -10.258 11.765  1.00 32.31  ? 8   GLY A O   1 
ATOM   55   N  N   . LYS A 1 9   ? 8.821   -11.403 10.001  1.00 31.45  ? 9   LYS A N   1 
ATOM   56   C  CA  . LYS A 1 9   ? 9.795   -12.197 10.747  1.00 27.78  ? 9   LYS A CA  1 
ATOM   57   C  C   . LYS A 1 9   ? 10.698  -11.295 11.603  1.00 31.44  ? 9   LYS A C   1 
ATOM   58   O  O   . LYS A 1 9   ? 11.136  -11.676 12.688  1.00 45.86  ? 9   LYS A O   1 
ATOM   59   C  CB  . LYS A 1 9   ? 10.597  -13.162 9.834   1.00 42.95  ? 9   LYS A CB  1 
ATOM   60   C  CG  . LYS A 1 9   ? 10.207  -14.637 9.719   1.00 44.18  ? 9   LYS A CG  1 
ATOM   61   C  CD  . LYS A 1 9   ? 8.797   -14.856 9.315   1.00 73.48  ? 9   LYS A CD  1 
ATOM   62   C  CE  . LYS A 1 9   ? 8.629   -15.477 7.937   1.00 85.54  ? 9   LYS A CE  1 
ATOM   63   N  NZ  . LYS A 1 9   ? 7.201   -15.673 7.562   1.00 92.68  ? 9   LYS A NZ  1 
ATOM   64   N  N   . HIS A 1 10  ? 11.020  -10.108 11.061  1.00 23.75  ? 10  HIS A N   1 
ATOM   65   C  CA  . HIS A 1 10  ? 12.171  -9.278  11.443  1.00 21.17  ? 10  HIS A CA  1 
ATOM   66   C  C   . HIS A 1 10  ? 11.769  -7.866  11.923  1.00 19.67  ? 10  HIS A C   1 
ATOM   67   O  O   . HIS A 1 10  ? 12.654  -7.086  12.349  1.00 21.85  ? 10  HIS A O   1 
ATOM   68   C  CB  . HIS A 1 10  ? 13.190  -9.174  10.234  1.00 22.60  ? 10  HIS A CB  1 
ATOM   69   C  CG  . HIS A 1 10  ? 13.729  -10.514 9.805   1.00 24.43  ? 10  HIS A CG  1 
ATOM   70   N  ND1 . HIS A 1 10  ? 14.782  -11.147 10.509  1.00 28.89  ? 10  HIS A ND1 1 
ATOM   71   C  CD2 . HIS A 1 10  ? 13.335  -11.388 8.827   1.00 23.46  ? 10  HIS A CD2 1 
ATOM   72   C  CE1 . HIS A 1 10  ? 15.020  -12.352 10.000  1.00 21.81  ? 10  HIS A CE1 1 
ATOM   73   N  NE2 . HIS A 1 10  ? 14.166  -12.507 8.914   1.00 30.24  ? 10  HIS A NE2 1 
ATOM   74   N  N   . ASN A 1 11  ? 10.477  -7.476  11.810  1.00 18.31  ? 11  ASN A N   1 
ATOM   75   C  CA  . ASN A 1 11  ? 10.086  -6.098  12.114  1.00 17.63  ? 11  ASN A CA  1 
ATOM   76   C  C   . ASN A 1 11  ? 8.793   -6.076  12.924  1.00 15.78  ? 11  ASN A C   1 
ATOM   77   O  O   . ASN A 1 11  ? 8.139   -5.022  12.972  1.00 15.99  ? 11  ASN A O   1 
ATOM   78   C  CB  . ASN A 1 11  ? 9.885   -5.305  10.803  1.00 15.86  ? 11  ASN A CB  1 
ATOM   79   C  CG  . ASN A 1 11  ? 8.819   -5.870  9.871   1.00 16.63  ? 11  ASN A CG  1 
ATOM   80   O  OD1 . ASN A 1 11  ? 8.204   -6.885  10.204  1.00 18.32  ? 11  ASN A OD1 1 
ATOM   81   N  ND2 . ASN A 1 11  ? 8.597   -5.265  8.709   1.00 19.91  ? 11  ASN A ND2 1 
ATOM   82   N  N   . GLY A 1 12  ? 8.451   -7.226  13.529  1.00 14.00  ? 12  GLY A N   1 
ATOM   83   C  CA  . GLY A 1 12  ? 7.160   -7.384  14.190  1.00 15.53  ? 12  GLY A CA  1 
ATOM   84   C  C   . GLY A 1 12  ? 7.139   -6.802  15.593  1.00 14.69  ? 12  GLY A C   1 
ATOM   85   O  O   . GLY A 1 12  ? 8.077   -6.081  16.017  1.00 14.09  ? 12  GLY A O   1 
ATOM   86   N  N   . PRO A 1 13  ? 6.064   -7.072  16.355  1.00 12.34  ? 13  PRO A N   1 
ATOM   87   C  CA  . PRO A 1 13  ? 5.842   -6.458  17.671  1.00 13.08  ? 13  PRO A CA  1 
ATOM   88   C  C   . PRO A 1 13  ? 6.984   -6.473  18.682  1.00 13.02  ? 13  PRO A C   1 
ATOM   89   O  O   . PRO A 1 13  ? 7.118   -5.525  19.448  1.00 14.10  ? 13  PRO A O   1 
ATOM   90   C  CB  . PRO A 1 13  ? 4.628   -7.265  18.205  1.00 13.10  ? 13  PRO A CB  1 
ATOM   91   C  CG  . PRO A 1 13  ? 3.811   -7.503  16.924  1.00 12.87  ? 13  PRO A CG  1 
ATOM   92   C  CD  . PRO A 1 13  ? 4.875   -7.828  15.882  1.00 13.00  ? 13  PRO A CD  1 
ATOM   93   N  N   A GLU A 1 14  ? 7.832   -7.511  18.615  0.50 13.05  ? 14  GLU A N   1 
ATOM   94   N  N   B GLU A 1 14  ? 7.841   -7.522  18.712  0.50 13.34  ? 14  GLU A N   1 
ATOM   95   C  CA  A GLU A 1 14  ? 8.880   -7.657  19.605  0.50 15.56  ? 14  GLU A CA  1 
ATOM   96   C  CA  B GLU A 1 14  ? 8.895   -7.539  19.725  0.50 17.94  ? 14  GLU A CA  1 
ATOM   97   C  C   A GLU A 1 14  ? 10.029  -6.672  19.291  0.50 13.82  ? 14  GLU A C   1 
ATOM   98   C  C   B GLU A 1 14  ? 10.028  -6.561  19.335  0.50 14.68  ? 14  GLU A C   1 
ATOM   99   O  O   A GLU A 1 14  ? 10.931  -6.518  20.134  0.50 15.78  ? 14  GLU A O   1 
ATOM   100  O  O   B GLU A 1 14  ? 10.941  -6.319  20.147  0.50 17.10  ? 14  GLU A O   1 
ATOM   101  C  CB  A GLU A 1 14  ? 9.242   -9.142  19.657  0.50 15.78  ? 14  GLU A CB  1 
ATOM   102  C  CB  B GLU A 1 14  ? 9.417   -8.959  19.971  0.50 21.68  ? 14  GLU A CB  1 
ATOM   103  C  CG  A GLU A 1 14  ? 9.874   -9.651  18.387  0.50 15.01  ? 14  GLU A CG  1 
ATOM   104  C  CG  B GLU A 1 14  ? 8.339   -10.012 20.255  0.50 23.66  ? 14  GLU A CG  1 
ATOM   105  C  CD  A GLU A 1 14  ? 9.108   -10.201 17.178  0.50 14.23  ? 14  GLU A CD  1 
ATOM   106  C  CD  B GLU A 1 14  ? 7.412   -9.834  21.452  0.50 26.45  ? 14  GLU A CD  1 
ATOM   107  O  OE1 A GLU A 1 14  ? 7.942   -9.802  16.988  0.50 12.87  ? 14  GLU A OE1 1 
ATOM   108  O  OE1 B GLU A 1 14  ? 7.916   -9.830  22.593  0.50 32.33  ? 14  GLU A OE1 1 
ATOM   109  O  OE2 A GLU A 1 14  ? 9.685   -11.023 16.438  0.50 17.35  ? 14  GLU A OE2 1 
ATOM   110  O  OE2 B GLU A 1 14  ? 6.191   -9.701  21.237  0.50 26.49  ? 14  GLU A OE2 1 
ATOM   111  N  N   . HIS A 1 15  ? 10.023  -6.053  18.078  1.00 13.01  ? 15  HIS A N   1 
ATOM   112  C  CA  . HIS A 1 15  ? 11.018  -5.056  17.687  1.00 13.64  ? 15  HIS A CA  1 
ATOM   113  C  C   . HIS A 1 15  ? 10.569  -3.596  17.899  1.00 14.10  ? 15  HIS A C   1 
ATOM   114  O  O   . HIS A 1 15  ? 11.401  -2.642  17.774  1.00 14.18  ? 15  HIS A O   1 
ATOM   115  C  CB  . HIS A 1 15  ? 11.330  -5.236  16.199  1.00 13.71  ? 15  HIS A CB  1 
ATOM   116  C  CG  . HIS A 1 15  ? 12.016  -6.557  15.962  1.00 17.54  ? 15  HIS A CG  1 
ATOM   117  N  ND1 . HIS A 1 15  ? 13.414  -6.702  16.130  1.00 22.57  ? 15  HIS A ND1 1 
ATOM   118  C  CD2 . HIS A 1 15  ? 11.526  -7.782  15.577  1.00 16.99  ? 15  HIS A CD2 1 
ATOM   119  C  CE1 . HIS A 1 15  ? 13.730  -7.953  15.847  1.00 24.91  ? 15  HIS A CE1 1 
ATOM   120  N  NE2 . HIS A 1 15  ? 12.629  -8.622  15.468  1.00 22.54  ? 15  HIS A NE2 1 
ATOM   121  N  N   . TRP A 1 16  ? 9.251   -3.327  18.047  1.00 12.73  ? 16  TRP A N   1 
ATOM   122  C  CA  . TRP A 1 16  ? 8.726   -1.960  17.953  1.00 12.49  ? 16  TRP A CA  1 
ATOM   123  C  C   . TRP A 1 16  ? 9.296   -1.016  19.007  1.00 11.95  ? 16  TRP A C   1 
ATOM   124  O  O   . TRP A 1 16  ? 9.453   0.210   18.731  1.00 12.54  ? 16  TRP A O   1 
ATOM   125  C  CB  . TRP A 1 16  ? 7.191   -2.014  18.107  1.00 11.59  ? 16  TRP A CB  1 
ATOM   126  C  CG  . TRP A 1 16  ? 6.511   -2.709  16.941  1.00 11.32  ? 16  TRP A CG  1 
ATOM   127  C  CD1 . TRP A 1 16  ? 7.063   -3.188  15.754  1.00 10.95  ? 16  TRP A CD1 1 
ATOM   128  C  CD2 . TRP A 1 16  ? 5.081   -3.027  16.891  1.00 11.21  ? 16  TRP A CD2 1 
ATOM   129  N  NE1 . TRP A 1 16  ? 6.059   -3.767  14.987  1.00 11.51  ? 16  TRP A NE1 1 
ATOM   130  C  CE2 . TRP A 1 16  ? 4.844   -3.655  15.639  1.00 11.24  ? 16  TRP A CE2 1 
ATOM   131  C  CE3 . TRP A 1 16  ? 4.020   -2.779  17.778  1.00 11.10  ? 16  TRP A CE3 1 
ATOM   132  C  CZ2 . TRP A 1 16  ? 3.590   -4.101  15.225  1.00 10.80  ? 16  TRP A CZ2 1 
ATOM   133  C  CZ3 . TRP A 1 16  ? 2.770   -3.214  17.381  1.00 11.25  ? 16  TRP A CZ3 1 
ATOM   134  C  CH2 . TRP A 1 16  ? 2.548   -3.840  16.137  1.00 11.03  ? 16  TRP A CH2 1 
ATOM   135  N  N   . HIS A 1 17  ? 9.697   -1.563  20.189  1.00 12.17  ? 17  HIS A N   1 
ATOM   136  C  CA  . HIS A 1 17  ? 10.215  -0.710  21.231  1.00 13.18  ? 17  HIS A CA  1 
ATOM   137  C  C   . HIS A 1 17  ? 11.444  0.094   20.809  1.00 15.37  ? 17  HIS A C   1 
ATOM   138  O  O   . HIS A 1 17  ? 11.703  1.137   21.431  1.00 14.96  ? 17  HIS A O   1 
ATOM   139  C  CB  . HIS A 1 17  ? 10.508  -1.447  22.532  1.00 13.73  ? 17  HIS A CB  1 
ATOM   140  C  CG  . HIS A 1 17  ? 11.661  -2.398  22.365  1.00 14.30  ? 17  HIS A CG  1 
ATOM   141  N  ND1 . HIS A 1 17  ? 12.915  -2.062  22.889  1.00 17.27  ? 17  HIS A ND1 1 
ATOM   142  C  CD2 . HIS A 1 17  ? 11.809  -3.601  21.746  1.00 15.94  ? 17  HIS A CD2 1 
ATOM   143  C  CE1 . HIS A 1 17  ? 13.776  -3.014  22.581  1.00 20.81  ? 17  HIS A CE1 1 
ATOM   144  N  NE2 . HIS A 1 17  ? 13.129  -3.984  21.916  1.00 18.54  ? 17  HIS A NE2 1 
ATOM   145  N  N   . LYS A 1 18  ? 12.227  -0.419  19.848  1.00 14.69  ? 18  LYS A N   1 
ATOM   146  C  CA  . LYS A 1 18  ? 13.465  0.312   19.545  1.00 18.12  ? 18  LYS A CA  1 
ATOM   147  C  C   . LYS A 1 18  ? 13.159  1.674   18.887  1.00 18.89  ? 18  LYS A C   1 
ATOM   148  O  O   . LYS A 1 18  ? 13.847  2.665   19.140  1.00 23.02  ? 18  LYS A O   1 
ATOM   149  C  CB  . LYS A 1 18  ? 14.322  -0.583  18.635  1.00 17.25  ? 18  LYS A CB  1 
ATOM   150  C  CG  . LYS A 1 18  ? 14.945  -1.785  19.345  1.00 17.70  ? 18  LYS A CG  1 
ATOM   151  C  CD  . LYS A 1 18  ? 15.611  -2.752  18.404  1.00 17.46  ? 18  LYS A CD  1 
ATOM   152  C  CE  . LYS A 1 18  ? 14.656  -3.714  17.706  1.00 16.28  ? 18  LYS A CE  1 
ATOM   153  N  NZ  . LYS A 1 18  ? 15.322  -4.547  16.644  1.00 17.59  ? 18  LYS A NZ  1 
ATOM   154  N  N   . ASP A 1 19  ? 12.137  1.754   18.003  1.00 16.14  ? 19  ASP A N   1 
ATOM   155  C  CA  . ASP A 1 19  ? 11.714  3.032   17.435  1.00 16.98  ? 19  ASP A CA  1 
ATOM   156  C  C   . ASP A 1 19  ? 10.701  3.788   18.305  1.00 16.75  ? 19  ASP A C   1 
ATOM   157  O  O   . ASP A 1 19  ? 10.613  5.022   18.225  1.00 16.36  ? 19  ASP A O   1 
ATOM   158  C  CB  . ASP A 1 19  ? 11.204  2.914   15.995  1.00 20.70  ? 19  ASP A CB  1 
ATOM   159  C  CG  . ASP A 1 19  ? 12.338  2.901   14.940  1.00 29.57  ? 19  ASP A CG  1 
ATOM   160  O  OD1 . ASP A 1 19  ? 13.444  3.407   15.229  1.00 33.05  ? 19  ASP A OD1 1 
ATOM   161  O  OD2 . ASP A 1 19  ? 12.081  2.449   13.817  1.00 46.76  ? 19  ASP A OD2 1 
ATOM   162  N  N   . PHE A 1 20  ? 9.947   3.020   19.112  1.00 14.23  ? 20  PHE A N   1 
ATOM   163  C  CA  . PHE A 1 20  ? 8.818   3.573   19.869  1.00 12.91  ? 20  PHE A CA  1 
ATOM   164  C  C   . PHE A 1 20  ? 8.921   3.078   21.311  1.00 13.38  ? 20  PHE A C   1 
ATOM   165  O  O   . PHE A 1 20  ? 8.310   2.089   21.718  1.00 12.86  ? 20  PHE A O   1 
ATOM   166  C  CB  . PHE A 1 20  ? 7.499   3.124   19.241  1.00 14.59  ? 20  PHE A CB  1 
ATOM   167  C  CG  . PHE A 1 20  ? 7.421   3.549   17.797  1.00 15.75  ? 20  PHE A CG  1 
ATOM   168  C  CD1 . PHE A 1 20  ? 7.100   4.875   17.468  1.00 18.90  ? 20  PHE A CD1 1 
ATOM   169  C  CD2 . PHE A 1 20  ? 7.743   2.639   16.754  1.00 18.25  ? 20  PHE A CD2 1 
ATOM   170  C  CE1 . PHE A 1 20  ? 7.072   5.281   16.124  1.00 20.20  ? 20  PHE A CE1 1 
ATOM   171  C  CE2 . PHE A 1 20  ? 7.735   3.045   15.415  1.00 19.40  ? 20  PHE A CE2 1 
ATOM   172  C  CZ  . PHE A 1 20  ? 7.355   4.356   15.117  1.00 19.42  ? 20  PHE A CZ  1 
ATOM   173  N  N   . PRO A 1 21  ? 9.794   3.682   22.134  1.00 14.63  ? 21  PRO A N   1 
ATOM   174  C  CA  . PRO A 1 21  ? 10.040  3.158   23.485  1.00 15.80  ? 21  PRO A CA  1 
ATOM   175  C  C   . PRO A 1 21  ? 8.799   3.058   24.388  1.00 13.42  ? 21  PRO A C   1 
ATOM   176  O  O   . PRO A 1 21  ? 8.814   2.275   25.340  1.00 13.36  ? 21  PRO A O   1 
ATOM   177  C  CB  . PRO A 1 21  ? 11.133  4.118   24.088  1.00 18.19  ? 21  PRO A CB  1 
ATOM   178  C  CG  . PRO A 1 21  ? 11.336  5.208   23.049  1.00 22.99  ? 21  PRO A CG  1 
ATOM   179  C  CD  . PRO A 1 21  ? 10.778  4.738   21.736  1.00 15.45  ? 21  PRO A CD  1 
ATOM   180  N  N   . ILE A 1 22  ? 7.738   3.855   24.092  1.00 12.85  ? 22  ILE A N   1 
ATOM   181  C  CA  . ILE A 1 22  ? 6.465   3.720   24.807  1.00 12.51  ? 22  ILE A CA  1 
ATOM   182  C  C   . ILE A 1 22  ? 5.855   2.325   24.652  1.00 11.17  ? 22  ILE A C   1 
ATOM   183  O  O   . ILE A 1 22  ? 4.952   1.972   25.421  1.00 12.15  ? 22  ILE A O   1 
ATOM   184  C  CB  . ILE A 1 22  ? 5.481   4.828   24.340  1.00 12.21  ? 22  ILE A CB  1 
ATOM   185  C  CG1 . ILE A 1 22  ? 4.414   5.162   25.363  1.00 13.18  ? 22  ILE A CG1 1 
ATOM   186  C  CG2 . ILE A 1 22  ? 4.883   4.529   22.955  1.00 12.40  ? 22  ILE A CG2 1 
ATOM   187  C  CD1 . ILE A 1 22  ? 3.473   6.306   24.983  1.00 17.44  ? 22  ILE A CD1 1 
ATOM   188  N  N   . ALA A 1 23  ? 6.407   1.473   23.734  1.00 11.19  ? 23  ALA A N   1 
ATOM   189  C  CA  . ALA A 1 23  ? 5.934   0.085   23.626  1.00 11.73  ? 23  ALA A CA  1 
ATOM   190  C  C   . ALA A 1 23  ? 5.975   -0.628  24.980  1.00 11.63  ? 23  ALA A C   1 
ATOM   191  O  O   . ALA A 1 23  ? 5.268   -1.611  25.151  1.00 11.83  ? 23  ALA A O   1 
ATOM   192  C  CB  . ALA A 1 23  ? 6.749   -0.689  22.570  1.00 11.99  ? 23  ALA A CB  1 
ATOM   193  N  N   . LYS A 1 24  ? 6.881   -0.223  25.866  1.00 12.60  ? 24  LYS A N   1 
ATOM   194  C  CA  . LYS A 1 24  ? 7.088   -0.832  27.178  1.00 13.07  ? 24  LYS A CA  1 
ATOM   195  C  C   . LYS A 1 24  ? 6.508   0.085   28.267  1.00 15.15  ? 24  LYS A C   1 
ATOM   196  O  O   . LYS A 1 24  ? 6.913   -0.034  29.438  1.00 17.54  ? 24  LYS A O   1 
ATOM   197  C  CB  . LYS A 1 24  ? 8.572   -1.125  27.425  1.00 15.13  ? 24  LYS A CB  1 
ATOM   198  C  CG  . LYS A 1 24  ? 9.192   -2.140  26.470  1.00 15.37  ? 24  LYS A CG  1 
ATOM   199  C  CD  . LYS A 1 24  ? 10.627  -2.356  26.984  1.00 20.61  ? 24  LYS A CD  1 
ATOM   200  C  CE  . LYS A 1 24  ? 11.533  -3.164  26.097  1.00 27.85  ? 24  LYS A CE  1 
ATOM   201  N  NZ  . LYS A 1 24  ? 10.925  -4.482  25.820  1.00 29.32  ? 24  LYS A NZ  1 
ATOM   202  N  N   . GLY A 1 25  ? 5.462   0.884   27.896  1.00 13.55  ? 25  GLY A N   1 
ATOM   203  C  CA  . GLY A 1 25  ? 4.895   1.870   28.823  1.00 14.41  ? 25  GLY A CA  1 
ATOM   204  C  C   . GLY A 1 25  ? 3.892   1.255   29.801  1.00 12.05  ? 25  GLY A C   1 
ATOM   205  O  O   . GLY A 1 25  ? 3.712   0.040   29.941  1.00 13.88  ? 25  GLY A O   1 
ATOM   206  N  N   . GLU A 1 26  ? 3.230   2.173   30.508  1.00 13.40  ? 26  GLU A N   1 
ATOM   207  C  CA  . GLU A 1 26  ? 2.365   1.781   31.595  1.00 15.00  ? 26  GLU A CA  1 
ATOM   208  C  C   . GLU A 1 26  ? 0.899   1.603   31.203  1.00 13.06  ? 26  GLU A C   1 
ATOM   209  O  O   . GLU A 1 26  ? 0.145   1.105   32.030  1.00 15.07  ? 26  GLU A O   1 
ATOM   210  C  CB  . GLU A 1 26  ? 2.397   2.853   32.694  1.00 18.28  ? 26  GLU A CB  1 
ATOM   211  C  CG  . GLU A 1 26  ? 3.844   3.081   33.260  1.00 19.84  ? 26  GLU A CG  1 
ATOM   212  C  CD  . GLU A 1 26  ? 4.500   1.861   33.910  1.00 25.26  ? 26  GLU A CD  1 
ATOM   213  O  OE1 . GLU A 1 26  ? 3.797   1.132   34.700  1.00 30.86  ? 26  GLU A OE1 1 
ATOM   214  O  OE2 . GLU A 1 26  ? 5.688   1.580   33.587  1.00 31.70  ? 26  GLU A OE2 1 
ATOM   215  N  N   . ARG A 1 27  ? 0.506   1.944   29.978  1.00 11.19  ? 27  ARG A N   1 
ATOM   216  C  CA  . ARG A 1 27  ? -0.895  1.746   29.584  1.00 10.57  ? 27  ARG A CA  1 
ATOM   217  C  C   . ARG A 1 27  ? -0.961  1.274   28.123  1.00 8.79   ? 27  ARG A C   1 
ATOM   218  O  O   . ARG A 1 27  ? -1.671  1.837   27.292  1.00 9.17   ? 27  ARG A O   1 
ATOM   219  C  CB  . ARG A 1 27  ? -1.803  2.967   29.883  1.00 11.91  ? 27  ARG A CB  1 
ATOM   220  C  CG  . ARG A 1 27  ? -1.373  4.303   29.302  1.00 13.90  ? 27  ARG A CG  1 
ATOM   221  C  CD  . ARG A 1 27  ? -2.416  5.416   29.571  1.00 16.32  ? 27  ARG A CD  1 
ATOM   222  N  NE  . ARG A 1 27  ? -3.574  5.381   28.612  1.00 15.05  ? 27  ARG A NE  1 
ATOM   223  C  CZ  . ARG A 1 27  ? -4.512  6.296   28.544  1.00 12.17  ? 27  ARG A CZ  1 
ATOM   224  N  NH1 . ARG A 1 27  ? -4.540  7.321   29.400  1.00 14.46  ? 27  ARG A NH1 1 
ATOM   225  N  NH2 . ARG A 1 27  ? -5.497  6.153   27.681  1.00 14.51  ? 27  ARG A NH2 1 
ATOM   226  N  N   . GLN A 1 28  ? -0.223  0.175   27.843  1.00 9.12   ? 28  GLN A N   1 
ATOM   227  C  CA  . GLN A 1 28  ? -0.197  -0.342  26.463  1.00 8.55   ? 28  GLN A CA  1 
ATOM   228  C  C   . GLN A 1 28  ? -1.355  -1.320  26.189  1.00 7.49   ? 28  GLN A C   1 
ATOM   229  O  O   . GLN A 1 28  ? -1.904  -2.021  27.078  1.00 9.12   ? 28  GLN A O   1 
ATOM   230  C  CB  . GLN A 1 28  ? 1.138   -1.077  26.235  1.00 9.01   ? 28  GLN A CB  1 
ATOM   231  C  CG  . GLN A 1 28  ? 2.268   0.001   26.158  1.00 9.76   ? 28  GLN A CG  1 
ATOM   232  C  CD  . GLN A 1 28  ? 2.216   0.793   24.871  1.00 9.99   ? 28  GLN A CD  1 
ATOM   233  O  OE1 . GLN A 1 28  ? 2.381   0.210   23.790  1.00 9.56   ? 28  GLN A OE1 1 
ATOM   234  N  NE2 . GLN A 1 28  ? 1.864   2.073   24.972  1.00 9.34   ? 28  GLN A NE2 1 
ATOM   235  N  N   . SER A 1 29  ? -1.732  -1.409  24.890  1.00 7.85   ? 29  SER A N   1 
ATOM   236  C  CA  . SER A 1 29  ? -2.797  -2.294  24.436  1.00 7.94   ? 29  SER A CA  1 
ATOM   237  C  C   . SER A 1 29  ? -2.255  -3.198  23.333  1.00 7.27   ? 29  SER A C   1 
ATOM   238  O  O   . SER A 1 29  ? -1.296  -2.784  22.631  1.00 8.84   ? 29  SER A O   1 
ATOM   239  C  CB  . SER A 1 29  ? -3.948  -1.405  23.852  1.00 7.75   ? 29  SER A CB  1 
ATOM   240  O  OG  . SER A 1 29  ? -4.573  -0.686  24.933  1.00 7.61   ? 29  SER A OG  1 
ATOM   241  N  N   . PRO A 1 30  ? -2.917  -4.342  23.044  1.00 7.58   ? 30  PRO A N   1 
ATOM   242  C  CA  . PRO A 1 30  ? -4.094  -4.878  23.750  1.00 8.81   ? 30  PRO A CA  1 
ATOM   243  C  C   . PRO A 1 30  ? -3.695  -5.529  25.063  1.00 7.91   ? 30  PRO A C   1 
ATOM   244  O  O   . PRO A 1 30  ? -2.495  -5.577  25.449  1.00 8.63   ? 30  PRO A O   1 
ATOM   245  C  CB  . PRO A 1 30  ? -4.598  -5.908  22.733  1.00 8.50   ? 30  PRO A CB  1 
ATOM   246  C  CG  . PRO A 1 30  ? -3.307  -6.488  22.155  1.00 7.71   ? 30  PRO A CG  1 
ATOM   247  C  CD  . PRO A 1 30  ? -2.404  -5.275  22.012  1.00 7.56   ? 30  PRO A CD  1 
ATOM   248  N  N   . VAL A 1 31  ? -4.669  -6.130  25.765  1.00 8.59   ? 31  VAL A N   1 
ATOM   249  C  CA  . VAL A 1 31  ? -4.485  -6.843  27.031  1.00 8.35   ? 31  VAL A CA  1 
ATOM   250  C  C   . VAL A 1 31  ? -5.394  -8.056  26.998  1.00 8.73   ? 31  VAL A C   1 
ATOM   251  O  O   . VAL A 1 31  ? -6.344  -8.134  26.218  1.00 8.92   ? 31  VAL A O   1 
ATOM   252  C  CB  . VAL A 1 31  ? -4.796  -5.988  28.273  1.00 9.41   ? 31  VAL A CB  1 
ATOM   253  C  CG1 . VAL A 1 31  ? -3.838  -4.785  28.329  1.00 10.34  ? 31  VAL A CG1 1 
ATOM   254  C  CG2 . VAL A 1 31  ? -6.268  -5.486  28.311  1.00 9.81   ? 31  VAL A CG2 1 
ATOM   255  N  N   . ASP A 1 32  ? -5.029  -9.071  27.812  1.00 9.38   ? 32  ASP A N   1 
ATOM   256  C  CA  . ASP A 1 32  ? -5.972  -10.147 28.133  1.00 8.67   ? 32  ASP A CA  1 
ATOM   257  C  C   . ASP A 1 32  ? -7.007  -9.622  29.128  1.00 10.02  ? 32  ASP A C   1 
ATOM   258  O  O   . ASP A 1 32  ? -6.689  -8.975  30.123  1.00 10.74  ? 32  ASP A O   1 
ATOM   259  C  CB  . ASP A 1 32  ? -5.202  -11.331 28.733  1.00 9.99   ? 32  ASP A CB  1 
ATOM   260  C  CG  . ASP A 1 32  ? -6.149  -12.507 29.028  1.00 9.80   ? 32  ASP A CG  1 
ATOM   261  O  OD1 . ASP A 1 32  ? -6.840  -12.987 28.073  1.00 9.96   ? 32  ASP A OD1 1 
ATOM   262  O  OD2 . ASP A 1 32  ? -6.186  -12.946 30.229  1.00 12.45  ? 32  ASP A OD2 1 
ATOM   263  N  N   . ILE A 1 33  ? -8.274  -9.983  28.810  1.00 9.06   ? 33  ILE A N   1 
ATOM   264  C  CA  . ILE A 1 33  ? -9.388  -9.603  29.701  1.00 9.82   ? 33  ILE A CA  1 
ATOM   265  C  C   . ILE A 1 33  ? -9.677  -10.847 30.549  1.00 10.35  ? 33  ILE A C   1 
ATOM   266  O  O   . ILE A 1 33  ? -10.212 -11.856 30.063  1.00 10.83  ? 33  ILE A O   1 
ATOM   267  C  CB  . ILE A 1 33  ? -10.618 -9.190  28.861  1.00 9.98   ? 33  ILE A CB  1 
ATOM   268  C  CG1 . ILE A 1 33  ? -10.263 -7.914  28.067  1.00 9.88   ? 33  ILE A CG1 1 
ATOM   269  C  CG2 . ILE A 1 33  ? -11.858 -8.952  29.767  1.00 11.29  ? 33  ILE A CG2 1 
ATOM   270  C  CD1 . ILE A 1 33  ? -11.285 -7.584  26.931  1.00 11.91  ? 33  ILE A CD1 1 
ATOM   271  N  N   A ASP A 1 34  ? -9.299  -10.767 31.835  0.50 10.88  ? 34  ASP A N   1 
ATOM   272  N  N   B ASP A 1 34  ? -9.290  -10.762 31.834  0.50 10.47  ? 34  ASP A N   1 
ATOM   273  C  CA  A ASP A 1 34  ? -9.595  -11.851 32.774  0.50 13.44  ? 34  ASP A CA  1 
ATOM   274  C  CA  B ASP A 1 34  ? -9.620  -11.815 32.798  0.50 12.55  ? 34  ASP A CA  1 
ATOM   275  C  C   A ASP A 1 34  ? -11.016 -11.622 33.304  0.50 13.16  ? 34  ASP A C   1 
ATOM   276  C  C   B ASP A 1 34  ? -11.058 -11.553 33.257  0.50 12.30  ? 34  ASP A C   1 
ATOM   277  O  O   A ASP A 1 34  ? -11.251 -10.733 34.147  0.50 17.42  ? 34  ASP A O   1 
ATOM   278  O  O   B ASP A 1 34  ? -11.356 -10.564 33.968  0.50 13.48  ? 34  ASP A O   1 
ATOM   279  C  CB  A ASP A 1 34  ? -8.550  -11.867 33.901  0.50 14.67  ? 34  ASP A CB  1 
ATOM   280  C  CB  B ASP A 1 34  ? -8.576  -11.833 33.929  0.50 13.34  ? 34  ASP A CB  1 
ATOM   281  C  CG  A ASP A 1 34  ? -8.697  -13.114 34.772  0.50 16.90  ? 34  ASP A CG  1 
ATOM   282  C  CG  B ASP A 1 34  ? -8.871  -12.861 35.032  0.50 15.11  ? 34  ASP A CG  1 
ATOM   283  O  OD1 A ASP A 1 34  ? -8.271  -14.170 34.310  0.50 18.96  ? 34  ASP A OD1 1 
ATOM   284  O  OD1 B ASP A 1 34  ? -10.071 -13.300 35.172  0.50 15.22  ? 34  ASP A OD1 1 
ATOM   285  O  OD2 A ASP A 1 34  ? -9.283  -13.038 35.896  0.50 20.34  ? 34  ASP A OD2 1 
ATOM   286  O  OD2 B ASP A 1 34  ? -7.904  -13.213 35.773  0.50 17.06  ? 34  ASP A OD2 1 
ATOM   287  N  N   . THR A 1 35  ? -11.976 -12.416 32.810  1.00 13.13  ? 35  THR A N   1 
ATOM   288  C  CA  . THR A 1 35  ? -13.407 -12.125 33.005  1.00 15.07  ? 35  THR A CA  1 
ATOM   289  C  C   . THR A 1 35  ? -13.823 -12.308 34.459  1.00 16.79  ? 35  THR A C   1 
ATOM   290  O  O   . THR A 1 35  ? -14.775 -11.645 34.904  1.00 19.22  ? 35  THR A O   1 
ATOM   291  C  CB  . THR A 1 35  ? -14.300 -13.069 32.176  1.00 17.35  ? 35  THR A CB  1 
ATOM   292  O  OG1 . THR A 1 35  ? -14.158 -14.432 32.654  1.00 15.91  ? 35  THR A OG1 1 
ATOM   293  C  CG2 . THR A 1 35  ? -13.997 -12.937 30.696  1.00 16.46  ? 35  THR A CG2 1 
ATOM   294  N  N   . HIS A 1 36  ? -13.086 -13.119 35.211  1.00 15.61  ? 36  HIS A N   1 
ATOM   295  C  CA  . HIS A 1 36  ? -13.367 -13.309 36.627  1.00 16.91  ? 36  HIS A CA  1 
ATOM   296  C  C   . HIS A 1 36  ? -12.904 -12.148 37.497  1.00 18.86  ? 36  HIS A C   1 
ATOM   297  O  O   . HIS A 1 36  ? -13.586 -11.894 38.507  1.00 20.71  ? 36  HIS A O   1 
ATOM   298  C  CB  . HIS A 1 36  ? -12.783 -14.618 37.131  1.00 20.31  ? 36  HIS A CB  1 
ATOM   299  C  CG  . HIS A 1 36  ? -13.559 -15.752 36.548  1.00 26.29  ? 36  HIS A CG  1 
ATOM   300  N  ND1 . HIS A 1 36  ? -14.909 -15.957 36.880  1.00 27.36  ? 36  HIS A ND1 1 
ATOM   301  C  CD2 . HIS A 1 36  ? -13.232 -16.627 35.549  1.00 26.92  ? 36  HIS A CD2 1 
ATOM   302  C  CE1 . HIS A 1 36  ? -15.331 -17.003 36.175  1.00 44.83  ? 36  HIS A CE1 1 
ATOM   303  N  NE2 . HIS A 1 36  ? -14.311 -17.441 35.351  1.00 35.49  ? 36  HIS A NE2 1 
ATOM   304  N  N   . THR A 1 37  ? -11.867 -11.387 37.036  1.00 19.33  ? 37  THR A N   1 
ATOM   305  C  CA  . THR A 1 37  ? -11.284 -10.255 37.763  1.00 20.29  ? 37  THR A CA  1 
ATOM   306  C  C   . THR A 1 37  ? -11.888 -8.896  37.386  1.00 18.62  ? 37  THR A C   1 
ATOM   307  O  O   . THR A 1 37  ? -11.841 -7.965  38.196  1.00 22.91  ? 37  THR A O   1 
ATOM   308  C  CB  . THR A 1 37  ? -9.777  -10.225 37.583  1.00 25.67  ? 37  THR A CB  1 
ATOM   309  O  OG1 . THR A 1 37  ? -9.386  -11.474 38.176  1.00 26.62  ? 37  THR A OG1 1 
ATOM   310  C  CG2 . THR A 1 37  ? -9.171  -9.052  38.319  1.00 25.60  ? 37  THR A CG2 1 
ATOM   311  N  N   . ALA A 1 38  ? -12.417 -8.767  36.176  1.00 16.07  ? 38  ALA A N   1 
ATOM   312  C  CA  . ALA A 1 38  ? -13.077 -7.536  35.755  1.00 15.08  ? 38  ALA A CA  1 
ATOM   313  C  C   . ALA A 1 38  ? -14.278 -7.300  36.661  1.00 17.67  ? 38  ALA A C   1 
ATOM   314  O  O   . ALA A 1 38  ? -15.106 -8.206  36.887  1.00 22.39  ? 38  ALA A O   1 
ATOM   315  C  CB  . ALA A 1 38  ? -13.524 -7.665  34.313  1.00 14.96  ? 38  ALA A CB  1 
ATOM   316  N  N   A LYS A 1 39  ? -14.372 -6.099  37.229  0.50 16.87  ? 39  LYS A N   1 
ATOM   317  N  N   B LYS A 1 39  ? -14.372 -6.062  37.145  0.50 18.23  ? 39  LYS A N   1 
ATOM   318  C  CA  A LYS A 1 39  ? -15.466 -5.852  38.169  0.50 17.32  ? 39  LYS A CA  1 
ATOM   319  C  CA  B LYS A 1 39  ? -15.430 -5.722  38.091  0.50 20.60  ? 39  LYS A CA  1 
ATOM   320  C  C   A LYS A 1 39  ? -16.563 -5.013  37.512  0.50 16.07  ? 39  LYS A C   1 
ATOM   321  C  C   B LYS A 1 39  ? -16.590 -5.004  37.407  0.50 18.18  ? 39  LYS A C   1 
ATOM   322  O  O   A LYS A 1 39  ? -16.298 -3.999  36.830  0.50 15.84  ? 39  LYS A O   1 
ATOM   323  O  O   B LYS A 1 39  ? -16.403 -4.005  36.691  0.50 14.54  ? 39  LYS A O   1 
ATOM   324  C  CB  A LYS A 1 39  ? -14.995 -5.336  39.537  0.50 16.77  ? 39  LYS A CB  1 
ATOM   325  C  CB  B LYS A 1 39  ? -14.934 -4.856  39.252  0.50 23.67  ? 39  LYS A CB  1 
ATOM   326  C  CG  A LYS A 1 39  ? -16.060 -5.276  40.644  0.50 19.77  ? 39  LYS A CG  1 
ATOM   327  C  CG  B LYS A 1 39  ? -15.885 -4.894  40.440  0.50 27.55  ? 39  LYS A CG  1 
ATOM   328  C  CD  A LYS A 1 39  ? -16.662 -6.602  41.021  0.50 21.28  ? 39  LYS A CD  1 
ATOM   329  C  CD  B LYS A 1 39  ? -15.416 -4.244  41.699  0.50 18.54  ? 39  LYS A CD  1 
ATOM   330  C  CE  A LYS A 1 39  ? -16.695 -7.572  39.863  0.50 21.23  ? 39  LYS A CE  1 
ATOM   331  C  CE  B LYS A 1 39  ? -16.385 -4.581  42.810  0.50 18.94  ? 39  LYS A CE  1 
ATOM   332  N  NZ  A LYS A 1 39  ? -18.073 -7.916  39.439  0.50 21.88  ? 39  LYS A NZ  1 
ATOM   333  N  NZ  B LYS A 1 39  ? -16.341 -3.556  43.864  0.50 24.99  ? 39  LYS A NZ  1 
ATOM   334  N  N   . TYR A 1 40  ? -17.794 -5.498  37.719  1.00 19.74  ? 40  TYR A N   1 
ATOM   335  C  CA  . TYR A 1 40  ? -18.983 -4.796  37.329  1.00 17.78  ? 40  TYR A CA  1 
ATOM   336  C  C   . TYR A 1 40  ? -18.965 -3.411  37.969  1.00 15.01  ? 40  TYR A C   1 
ATOM   337  O  O   . TYR A 1 40  ? -18.768 -3.233  39.203  1.00 17.42  ? 40  TYR A O   1 
ATOM   338  C  CB  . TYR A 1 40  ? -20.224 -5.584  37.783  1.00 21.73  ? 40  TYR A CB  1 
ATOM   339  C  CG  . TYR A 1 40  ? -21.459 -4.736  37.643  1.00 28.52  ? 40  TYR A CG  1 
ATOM   340  C  CD1 . TYR A 1 40  ? -21.868 -4.283  36.379  1.00 24.60  ? 40  TYR A CD1 1 
ATOM   341  C  CD2 . TYR A 1 40  ? -22.253 -4.426  38.750  1.00 36.39  ? 40  TYR A CD2 1 
ATOM   342  C  CE1 . TYR A 1 40  ? -23.009 -3.504  36.220  1.00 29.31  ? 40  TYR A CE1 1 
ATOM   343  C  CE2 . TYR A 1 40  ? -23.408 -3.673  38.595  1.00 34.11  ? 40  TYR A CE2 1 
ATOM   344  C  CZ  . TYR A 1 40  ? -23.782 -3.204  37.344  1.00 31.55  ? 40  TYR A CZ  1 
ATOM   345  O  OH  . TYR A 1 40  ? -24.925 -2.456  37.214  1.00 42.73  ? 40  TYR A OH  1 
ATOM   346  N  N   . ASP A 1 41  ? -19.177 -2.406  37.122  1.00 16.65  ? 41  ASP A N   1 
ATOM   347  C  CA  . ASP A 1 41  ? -19.162 -1.013  37.581  1.00 17.45  ? 41  ASP A CA  1 
ATOM   348  C  C   . ASP A 1 41  ? -20.524 -0.331  37.397  1.00 22.41  ? 41  ASP A C   1 
ATOM   349  O  O   . ASP A 1 41  ? -20.853 0.094   36.278  1.00 21.02  ? 41  ASP A O   1 
ATOM   350  C  CB  . ASP A 1 41  ? -18.072 -0.178  36.885  1.00 18.88  ? 41  ASP A CB  1 
ATOM   351  C  CG  . ASP A 1 41  ? -17.981 1.241   37.424  1.00 20.80  ? 41  ASP A CG  1 
ATOM   352  O  OD1 . ASP A 1 41  ? -18.871 1.633   38.247  1.00 22.76  ? 41  ASP A OD1 1 
ATOM   353  O  OD2 . ASP A 1 41  ? -17.036 1.966   37.016  1.00 23.58  ? 41  ASP A OD2 1 
ATOM   354  N  N   . PRO A 1 42  ? -21.354 -0.235  38.476  1.00 26.90  ? 42  PRO A N   1 
ATOM   355  C  CA  . PRO A 1 42  ? -22.733 0.259   38.317  1.00 27.92  ? 42  PRO A CA  1 
ATOM   356  C  C   . PRO A 1 42  ? -22.755 1.729   37.862  1.00 25.68  ? 42  PRO A C   1 
ATOM   357  O  O   . PRO A 1 42  ? -23.814 2.263   37.464  1.00 35.65  ? 42  PRO A O   1 
ATOM   358  C  CB  . PRO A 1 42  ? -23.397 -0.018  39.690  1.00 29.96  ? 42  PRO A CB  1 
ATOM   359  C  CG  . PRO A 1 42  ? -22.283 -0.231  40.646  1.00 35.51  ? 42  PRO A CG  1 
ATOM   360  C  CD  . PRO A 1 42  ? -21.045 -0.670  39.864  1.00 36.85  ? 42  PRO A CD  1 
ATOM   361  N  N   . SER A 1 43  ? -21.627 2.443   38.026  1.00 24.30  ? 43  SER A N   1 
ATOM   362  C  CA  . SER A 1 43  ? -21.563 3.837   37.583  1.00 27.29  ? 43  SER A CA  1 
ATOM   363  C  C   . SER A 1 43  ? -21.298 4.012   36.078  1.00 26.53  ? 43  SER A C   1 
ATOM   364  O  O   . SER A 1 43  ? -21.375 5.135   35.582  1.00 32.17  ? 43  SER A O   1 
ATOM   365  C  CB  . SER A 1 43  ? -20.542 4.615   38.351  1.00 29.71  ? 43  SER A CB  1 
ATOM   366  O  OG  . SER A 1 43  ? -19.233 4.245   37.915  1.00 30.36  ? 43  SER A OG  1 
ATOM   367  N  N   . LEU A 1 44  ? -20.991 2.955   35.317  1.00 22.72  ? 44  LEU A N   1 
ATOM   368  C  CA  . LEU A 1 44  ? -20.871 3.146   33.868  1.00 23.52  ? 44  LEU A CA  1 
ATOM   369  C  C   . LEU A 1 44  ? -22.260 3.331   33.259  1.00 32.25  ? 44  LEU A C   1 
ATOM   370  O  O   . LEU A 1 44  ? -23.257 2.775   33.740  1.00 35.07  ? 44  LEU A O   1 
ATOM   371  C  CB  . LEU A 1 44  ? -20.239 1.911   33.240  1.00 21.00  ? 44  LEU A CB  1 
ATOM   372  C  CG  . LEU A 1 44  ? -18.776 1.656   33.536  1.00 17.38  ? 44  LEU A CG  1 
ATOM   373  C  CD1 . LEU A 1 44  ? -18.440 0.223   33.117  1.00 19.09  ? 44  LEU A CD1 1 
ATOM   374  C  CD2 . LEU A 1 44  ? -17.904 2.693   32.856  1.00 17.99  ? 44  LEU A CD2 1 
ATOM   375  N  N   . LYS A 1 45  ? -22.303 4.028   32.120  1.00 30.75  ? 45  LYS A N   1 
ATOM   376  C  CA  . LYS A 1 45  ? -23.556 4.136   31.362  1.00 35.94  ? 45  LYS A CA  1 
ATOM   377  C  C   . LYS A 1 45  ? -23.597 3.174   30.179  1.00 40.12  ? 45  LYS A C   1 
ATOM   378  O  O   . LYS A 1 45  ? -22.608 2.443   29.899  1.00 43.47  ? 45  LYS A O   1 
ATOM   379  C  CB  . LYS A 1 45  ? -23.864 5.577   31.060  1.00 31.98  ? 45  LYS A CB  1 
ATOM   380  C  CG  . LYS A 1 45  ? -23.524 6.487   32.217  1.00 36.24  ? 45  LYS A CG  1 
ATOM   381  C  CD  . LYS A 1 45  ? -23.958 7.893   31.982  1.00 51.37  ? 45  LYS A CD  1 
ATOM   382  C  CE  . LYS A 1 45  ? -23.810 8.348   30.533  1.00 80.69  ? 45  LYS A CE  1 
ATOM   383  N  NZ  . LYS A 1 45  ? -24.861 9.318   30.131  1.00 78.27  ? 45  LYS A NZ  1 
ATOM   384  N  N   . PRO A 1 46  ? -24.839 2.975   29.638  1.00 35.73  ? 46  PRO A N   1 
ATOM   385  C  CA  . PRO A 1 46  ? -25.049 2.238   28.402  1.00 35.75  ? 46  PRO A CA  1 
ATOM   386  C  C   . PRO A 1 46  ? -24.240 3.066   27.428  1.00 20.85  ? 46  PRO A C   1 
ATOM   387  O  O   . PRO A 1 46  ? -24.161 4.304   27.468  1.00 22.98  ? 46  PRO A O   1 
ATOM   388  C  CB  . PRO A 1 46  ? -26.588 2.300   28.095  1.00 42.29  ? 46  PRO A CB  1 
ATOM   389  C  CG  . PRO A 1 46  ? -27.165 3.259   29.137  1.00 54.55  ? 46  PRO A CG  1 
ATOM   390  C  CD  . PRO A 1 46  ? -26.105 3.421   30.220  1.00 42.35  ? 46  PRO A CD  1 
ATOM   391  N  N   . LEU A 1 47  ? -23.736 2.299   26.490  1.00 25.42  ? 47  LEU A N   1 
ATOM   392  C  CA  . LEU A 1 47  ? -23.038 3.005   25.472  1.00 20.76  ? 47  LEU A CA  1 
ATOM   393  C  C   . LEU A 1 47  ? -24.061 3.654   24.527  1.00 21.74  ? 47  LEU A C   1 
ATOM   394  O  O   . LEU A 1 47  ? -25.113 3.060   24.312  1.00 25.22  ? 47  LEU A O   1 
ATOM   395  C  CB  . LEU A 1 47  ? -22.309 1.880   24.775  1.00 30.39  ? 47  LEU A CB  1 
ATOM   396  C  CG  . LEU A 1 47  ? -21.142 2.201   23.901  1.00 31.27  ? 47  LEU A CG  1 
ATOM   397  C  CD1 . LEU A 1 47  ? -20.107 3.070   24.671  1.00 27.93  ? 47  LEU A CD1 1 
ATOM   398  C  CD2 . LEU A 1 47  ? -20.620 0.838   23.450  1.00 31.29  ? 47  LEU A CD2 1 
ATOM   399  N  N   . SER A 1 48  ? -23.722 4.793   23.938  1.00 14.48  ? 48  SER A N   1 
ATOM   400  C  CA  . SER A 1 48  ? -24.538 5.393   22.887  1.00 14.81  ? 48  SER A CA  1 
ATOM   401  C  C   . SER A 1 48  ? -23.757 5.360   21.578  1.00 13.93  ? 48  SER A C   1 
ATOM   402  O  O   . SER A 1 48  ? -22.781 6.133   21.401  1.00 13.75  ? 48  SER A O   1 
ATOM   403  C  CB  . SER A 1 48  ? -24.974 6.843   23.300  1.00 16.85  ? 48  SER A CB  1 
ATOM   404  O  OG  . SER A 1 48  ? -25.550 7.461   22.194  1.00 18.23  ? 48  SER A OG  1 
ATOM   405  N  N   . VAL A 1 49  ? -24.193 4.534   20.634  1.00 14.87  ? 49  VAL A N   1 
ATOM   406  C  CA  . VAL A 1 49  ? -23.575 4.399   19.312  1.00 16.60  ? 49  VAL A CA  1 
ATOM   407  C  C   . VAL A 1 49  ? -24.547 5.014   18.309  1.00 16.33  ? 49  VAL A C   1 
ATOM   408  O  O   . VAL A 1 49  ? -25.608 4.432   18.078  1.00 20.52  ? 49  VAL A O   1 
ATOM   409  C  CB  . VAL A 1 49  ? -23.278 2.918   19.000  1.00 17.44  ? 49  VAL A CB  1 
ATOM   410  C  CG1 . VAL A 1 49  ? -22.575 2.801   17.664  1.00 26.52  ? 49  VAL A CG1 1 
ATOM   411  C  CG2 . VAL A 1 49  ? -22.496 2.230   20.135  1.00 20.30  ? 49  VAL A CG2 1 
ATOM   412  N  N   . SER A 1 50  ? -24.222 6.192   17.769  1.00 15.26  ? 50  SER A N   1 
ATOM   413  C  CA  . SER A 1 50  ? -25.149 6.883   16.869  1.00 16.88  ? 50  SER A CA  1 
ATOM   414  C  C   . SER A 1 50  ? -24.579 6.942   15.476  1.00 16.66  ? 50  SER A C   1 
ATOM   415  O  O   . SER A 1 50  ? -23.883 7.907   15.164  1.00 18.76  ? 50  SER A O   1 
ATOM   416  C  CB  . SER A 1 50  ? -25.560 8.321   17.326  1.00 27.01  ? 50  SER A CB  1 
ATOM   417  O  OG  . SER A 1 50  ? -26.026 8.275   18.670  1.00 38.00  ? 50  SER A OG  1 
ATOM   418  N  N   . TYR A 1 51  ? -24.847 5.930   14.651  1.00 18.46  ? 51  TYR A N   1 
ATOM   419  C  CA  . TYR A 1 51  ? -24.221 5.787   13.329  1.00 17.36  ? 51  TYR A CA  1 
ATOM   420  C  C   . TYR A 1 51  ? -25.175 6.018   12.143  1.00 21.74  ? 51  TYR A C   1 
ATOM   421  O  O   . TYR A 1 51  ? -24.781 5.818   10.972  1.00 21.41  ? 51  TYR A O   1 
ATOM   422  C  CB  . TYR A 1 51  ? -23.583 4.393   13.192  1.00 15.63  ? 51  TYR A CB  1 
ATOM   423  C  CG  . TYR A 1 51  ? -22.303 4.138   13.988  1.00 15.15  ? 51  TYR A CG  1 
ATOM   424  C  CD1 . TYR A 1 51  ? -21.600 5.164   14.638  1.00 13.47  ? 51  TYR A CD1 1 
ATOM   425  C  CD2 . TYR A 1 51  ? -21.804 2.829   14.043  1.00 13.23  ? 51  TYR A CD2 1 
ATOM   426  C  CE1 . TYR A 1 51  ? -20.420 4.862   15.318  1.00 12.38  ? 51  TYR A CE1 1 
ATOM   427  C  CE2 . TYR A 1 51  ? -20.639 2.514   14.711  1.00 13.25  ? 51  TYR A CE2 1 
ATOM   428  C  CZ  . TYR A 1 51  ? -19.906 3.551   15.307  1.00 12.33  ? 51  TYR A CZ  1 
ATOM   429  O  OH  . TYR A 1 51  ? -18.749 3.210   15.980  1.00 11.97  ? 51  TYR A OH  1 
ATOM   430  N  N   . ASP A 1 52  ? -26.414 6.426   12.425  1.00 24.24  ? 52  ASP A N   1 
ATOM   431  C  CA  . ASP A 1 52  ? -27.453 6.701   11.418  1.00 26.72  ? 52  ASP A CA  1 
ATOM   432  C  C   . ASP A 1 52  ? -27.016 7.659   10.300  1.00 22.57  ? 52  ASP A C   1 
ATOM   433  O  O   . ASP A 1 52  ? -27.411 7.456   9.155   1.00 29.21  ? 52  ASP A O   1 
ATOM   434  C  CB  . ASP A 1 52  ? -28.709 7.231   12.110  1.00 36.45  ? 52  ASP A CB  1 
ATOM   435  C  CG  . ASP A 1 52  ? -28.472 8.048   13.404  1.00 56.09  ? 52  ASP A CG  1 
ATOM   436  O  OD1 . ASP A 1 52  ? -27.781 7.553   14.410  1.00 68.40  ? 52  ASP A OD1 1 
ATOM   437  O  OD2 . ASP A 1 52  ? -29.030 9.189   13.444  1.00 100.84 ? 52  ASP A OD2 1 
ATOM   438  N  N   . GLN A 1 53  ? -26.229 8.705   10.605  1.00 21.06  ? 53  GLN A N   1 
ATOM   439  C  CA  . GLN A 1 53  ? -25.784 9.637   9.565   1.00 22.45  ? 53  GLN A CA  1 
ATOM   440  C  C   . GLN A 1 53  ? -24.334 9.406   9.102   1.00 19.70  ? 53  GLN A C   1 
ATOM   441  O  O   . GLN A 1 53  ? -23.727 10.309  8.471   1.00 20.99  ? 53  GLN A O   1 
ATOM   442  C  CB  . GLN A 1 53  ? -25.904 11.081  10.070  1.00 33.44  ? 53  GLN A CB  1 
ATOM   443  C  CG  . GLN A 1 53  ? -27.297 11.434  10.582  1.00 44.19  ? 53  GLN A CG  1 
ATOM   444  C  CD  . GLN A 1 53  ? -28.182 11.790  9.421   1.00 62.55  ? 53  GLN A CD  1 
ATOM   445  O  OE1 . GLN A 1 53  ? -27.715 11.890  8.280   1.00 80.25  ? 53  GLN A OE1 1 
ATOM   446  N  NE2 . GLN A 1 53  ? -29.459 11.995  9.713   1.00 68.78  ? 53  GLN A NE2 1 
ATOM   447  N  N   . ALA A 1 54  ? -23.767 8.221   9.398   1.00 17.96  ? 54  ALA A N   1 
ATOM   448  C  CA  . ALA A 1 54  ? -22.385 7.896   9.006   1.00 16.10  ? 54  ALA A CA  1 
ATOM   449  C  C   . ALA A 1 54  ? -22.241 8.011   7.484   1.00 17.65  ? 54  ALA A C   1 
ATOM   450  O  O   . ALA A 1 54  ? -23.104 7.509   6.738   1.00 27.82  ? 54  ALA A O   1 
ATOM   451  C  CB  . ALA A 1 54  ? -21.962 6.513   9.481   1.00 18.66  ? 54  ALA A CB  1 
ATOM   452  N  N   . THR A 1 55  ? -21.213 8.740   7.045   1.00 16.41  ? 55  THR A N   1 
ATOM   453  C  CA  . THR A 1 55  ? -20.905 8.907   5.620   1.00 19.58  ? 55  THR A CA  1 
ATOM   454  C  C   . THR A 1 55  ? -19.548 8.270   5.310   1.00 15.48  ? 55  THR A C   1 
ATOM   455  O  O   . THR A 1 55  ? -18.529 8.911   5.562   1.00 15.41  ? 55  THR A O   1 
ATOM   456  C  CB  . THR A 1 55  ? -20.733 10.395  5.199   1.00 26.44  ? 55  THR A CB  1 
ATOM   457  O  OG1 . THR A 1 55  ? -21.902 11.145  5.477   1.00 31.21  ? 55  THR A OG1 1 
ATOM   458  C  CG2 . THR A 1 55  ? -20.537 10.475  3.701   1.00 26.60  ? 55  THR A CG2 1 
ATOM   459  N  N   . SER A 1 56  ? -19.527 7.032   4.826   1.00 16.49  ? 56  SER A N   1 
ATOM   460  C  CA  . SER A 1 56  ? -18.264 6.429   4.393   1.00 17.90  ? 56  SER A CA  1 
ATOM   461  C  C   . SER A 1 56  ? -17.767 7.113   3.098   1.00 19.29  ? 56  SER A C   1 
ATOM   462  O  O   . SER A 1 56  ? -18.583 7.586   2.296   1.00 22.23  ? 56  SER A O   1 
ATOM   463  C  CB  . SER A 1 56  ? -18.302 4.885   4.241   1.00 18.73  ? 56  SER A CB  1 
ATOM   464  O  OG  . SER A 1 56  ? -19.182 4.476   3.160   1.00 18.52  ? 56  SER A OG  1 
ATOM   465  N  N   . LEU A 1 57  ? -16.451 7.135   2.875   1.00 17.90  ? 57  LEU A N   1 
ATOM   466  C  CA  . LEU A 1 57  ? -15.961 7.743   1.647   1.00 20.18  ? 57  LEU A CA  1 
ATOM   467  C  C   . LEU A 1 57  ? -15.133 6.772   0.796   1.00 18.21  ? 57  LEU A C   1 
ATOM   468  O  O   . LEU A 1 57  ? -15.209 6.776   -0.433  1.00 18.75  ? 57  LEU A O   1 
ATOM   469  C  CB  . LEU A 1 57  ? -15.125 8.948   2.068   1.00 23.20  ? 57  LEU A CB  1 
ATOM   470  C  CG  . LEU A 1 57  ? -16.013 10.087  2.582   1.00 26.41  ? 57  LEU A CG  1 
ATOM   471  C  CD1 . LEU A 1 57  ? -15.144 11.205  3.156   1.00 30.28  ? 57  LEU A CD1 1 
ATOM   472  C  CD2 . LEU A 1 57  ? -16.982 10.618  1.483   1.00 34.70  ? 57  LEU A CD2 1 
ATOM   473  N  N   . ARG A 1 58  ? -14.244 6.000   1.432   1.00 15.90  ? 58  ARG A N   1 
ATOM   474  C  CA  . ARG A 1 58  ? -13.201 5.309   0.684   1.00 15.13  ? 58  ARG A CA  1 
ATOM   475  C  C   . ARG A 1 58  ? -12.647 4.163   1.526   1.00 13.92  ? 58  ARG A C   1 
ATOM   476  O  O   . ARG A 1 58  ? -12.741 4.182   2.767   1.00 16.46  ? 58  ARG A O   1 
ATOM   477  C  CB  . ARG A 1 58  ? -12.060 6.328   0.537   1.00 17.13  ? 58  ARG A CB  1 
ATOM   478  C  CG  . ARG A 1 58  ? -11.163 6.069   -0.664  1.00 19.85  ? 58  ARG A CG  1 
ATOM   479  C  CD  . ARG A 1 58  ? -10.019 7.059   -0.743  1.00 20.40  ? 58  ARG A CD  1 
ATOM   480  N  NE  . ARG A 1 58  ? -9.182  7.037   0.447   1.00 18.43  ? 58  ARG A NE  1 
ATOM   481  C  CZ  . ARG A 1 58  ? -7.875  7.265   0.438   1.00 15.77  ? 58  ARG A CZ  1 
ATOM   482  N  NH1 . ARG A 1 58  ? -7.254  7.552   -0.712  1.00 18.28  ? 58  ARG A NH1 1 
ATOM   483  N  NH2 . ARG A 1 58  ? -7.166  7.239   1.578   1.00 16.48  ? 58  ARG A NH2 1 
ATOM   484  N  N   . ILE A 1 59  ? -12.038 3.185   0.850   1.00 15.83  ? 59  ILE A N   1 
ATOM   485  C  CA  . ILE A 1 59  ? -11.370 2.068   1.521   1.00 13.88  ? 59  ILE A CA  1 
ATOM   486  C  C   . ILE A 1 59  ? -9.932  2.069   1.022   1.00 13.07  ? 59  ILE A C   1 
ATOM   487  O  O   . ILE A 1 59  ? -9.666  2.247   -0.177  1.00 15.44  ? 59  ILE A O   1 
ATOM   488  C  CB  . ILE A 1 59  ? -12.124 0.732   1.292   1.00 15.13  ? 59  ILE A CB  1 
ATOM   489  C  CG1 . ILE A 1 59  ? -11.579 -0.399  2.188   1.00 14.24  ? 59  ILE A CG1 1 
ATOM   490  C  CG2 . ILE A 1 59  ? -12.152 0.368   -0.212  1.00 15.02  ? 59  ILE A CG2 1 
ATOM   491  C  CD1 . ILE A 1 59  ? -12.415 -1.674  2.152   1.00 15.34  ? 59  ILE A CD1 1 
ATOM   492  N  N   . LEU A 1 60  ? -8.954  1.883   1.933   1.00 12.62  ? 60  LEU A N   1 
ATOM   493  C  CA  . LEU A 1 60  ? -7.534  2.033   1.662   1.00 13.16  ? 60  LEU A CA  1 
ATOM   494  C  C   . LEU A 1 60  ? -6.759  0.841   2.236   1.00 13.44  ? 60  LEU A C   1 
ATOM   495  O  O   . LEU A 1 60  ? -6.940  0.487   3.399   1.00 11.66  ? 60  LEU A O   1 
ATOM   496  C  CB  . LEU A 1 60  ? -7.037  3.334   2.328   1.00 14.93  ? 60  LEU A CB  1 
ATOM   497  C  CG  . LEU A 1 60  ? -5.520  3.475   2.293   1.00 13.09  ? 60  LEU A CG  1 
ATOM   498  C  CD1 . LEU A 1 60  ? -5.044  3.760   0.833   1.00 15.70  ? 60  LEU A CD1 1 
ATOM   499  C  CD2 . LEU A 1 60  ? -5.013  4.570   3.246   1.00 15.60  ? 60  LEU A CD2 1 
ATOM   500  N  N   . ASN A 1 61  ? -5.926  0.206   1.409   1.00 11.86  ? 61  ASN A N   1 
ATOM   501  C  CA  . ASN A 1 61  ? -4.929  -0.760  1.863   1.00 12.08  ? 61  ASN A CA  1 
ATOM   502  C  C   . ASN A 1 61  ? -3.666  0.034   2.244   1.00 11.87  ? 61  ASN A C   1 
ATOM   503  O  O   . ASN A 1 61  ? -2.996  0.603   1.357   1.00 14.49  ? 61  ASN A O   1 
ATOM   504  C  CB  . ASN A 1 61  ? -4.627  -1.856  0.803   1.00 12.95  ? 61  ASN A CB  1 
ATOM   505  C  CG  . ASN A 1 61  ? -3.548  -2.834  1.226   1.00 13.60  ? 61  ASN A CG  1 
ATOM   506  O  OD1 . ASN A 1 61  ? -2.669  -2.562  2.091   1.00 13.98  ? 61  ASN A OD1 1 
ATOM   507  N  ND2 . ASN A 1 61  ? -3.558  -4.057  0.673   1.00 13.23  ? 61  ASN A ND2 1 
ATOM   508  N  N   . ASN A 1 62  ? -3.327  0.098   3.571   1.00 11.96  ? 62  ASN A N   1 
ATOM   509  C  CA  . ASN A 1 62  ? -2.228  0.975   3.994   1.00 13.68  ? 62  ASN A CA  1 
ATOM   510  C  C   . ASN A 1 62  ? -0.969  0.137   4.254   1.00 13.41  ? 62  ASN A C   1 
ATOM   511  O  O   . ASN A 1 62  ? 0.071   0.666   4.756   1.00 15.79  ? 62  ASN A O   1 
ATOM   512  C  CB  . ASN A 1 62  ? -2.626  1.818   5.226   1.00 13.71  ? 62  ASN A CB  1 
ATOM   513  C  CG  . ASN A 1 62  ? -2.950  0.929   6.426   1.00 12.67  ? 62  ASN A CG  1 
ATOM   514  O  OD1 . ASN A 1 62  ? -2.464  -0.207  6.549   1.00 13.18  ? 62  ASN A OD1 1 
ATOM   515  N  ND2 . ASN A 1 62  ? -3.763  1.466   7.320   1.00 17.88  ? 62  ASN A ND2 1 
ATOM   516  N  N   . GLY A 1 63  ? -0.958  -1.173  3.852   1.00 13.16  ? 63  GLY A N   1 
ATOM   517  C  CA  . GLY A 1 63  ? 0.205   -2.021  4.045   1.00 12.63  ? 63  GLY A CA  1 
ATOM   518  C  C   . GLY A 1 63  ? 0.289   -2.717  5.428   1.00 11.93  ? 63  GLY A C   1 
ATOM   519  O  O   . GLY A 1 63  ? 1.163   -3.586  5.653   1.00 12.94  ? 63  GLY A O   1 
ATOM   520  N  N   . HIS A 1 64  ? -0.652  -2.365  6.337   1.00 11.97  ? 64  HIS A N   1 
ATOM   521  C  CA  . HIS A 1 64  ? -0.760  -2.970  7.681   1.00 12.34  ? 64  HIS A CA  1 
ATOM   522  C  C   . HIS A 1 64  ? -2.127  -3.632  7.845   1.00 11.38  ? 64  HIS A C   1 
ATOM   523  O  O   . HIS A 1 64  ? -2.190  -4.738  8.395   1.00 16.45  ? 64  HIS A O   1 
ATOM   524  C  CB  . HIS A 1 64  ? -0.522  -1.931  8.798   1.00 12.38  ? 64  HIS A CB  1 
ATOM   525  C  CG  . HIS A 1 64  ? 0.800   -1.269  8.670   1.00 11.89  ? 64  HIS A CG  1 
ATOM   526  N  ND1 . HIS A 1 64  ? 2.027   -1.983  8.870   1.00 14.07  ? 64  HIS A ND1 1 
ATOM   527  C  CD2 . HIS A 1 64  ? 1.135   -0.002  8.378   1.00 13.93  ? 64  HIS A CD2 1 
ATOM   528  C  CE1 . HIS A 1 64  ? 3.053   -1.130  8.722   1.00 14.50  ? 64  HIS A CE1 1 
ATOM   529  N  NE2 . HIS A 1 64  ? 2.530   0.104   8.425   1.00 15.98  ? 64  HIS A NE2 1 
ATOM   530  N  N   . ALA A 1 65  ? -3.169  -2.970  7.348   1.00 11.19  ? 65  ALA A N   1 
ATOM   531  C  CA  . ALA A 1 65  ? -4.508  -3.494  7.327   1.00 11.73  ? 65  ALA A CA  1 
ATOM   532  C  C   . ALA A 1 65  ? -5.241  -2.730  6.213   1.00 10.54  ? 65  ALA A C   1 
ATOM   533  O  O   . ALA A 1 65  ? -4.567  -2.046  5.411   1.00 13.07  ? 65  ALA A O   1 
ATOM   534  C  CB  . ALA A 1 65  ? -5.159  -3.291  8.718   1.00 11.55  ? 65  ALA A CB  1 
ATOM   535  N  N   . PHE A 1 66  ? -6.585  -2.749  6.210   1.00 10.09  ? 66  PHE A N   1 
ATOM   536  C  CA  . PHE A 1 66  ? -7.340  -1.840  5.365   1.00 11.93  ? 66  PHE A CA  1 
ATOM   537  C  C   . PHE A 1 66  ? -8.257  -0.955  6.202   1.00 10.92  ? 66  PHE A C   1 
ATOM   538  O  O   . PHE A 1 66  ? -8.851  -1.433  7.182   1.00 11.11  ? 66  PHE A O   1 
ATOM   539  C  CB  . PHE A 1 66  ? -8.107  -2.548  4.225   1.00 12.26  ? 66  PHE A CB  1 
ATOM   540  C  CG  . PHE A 1 66  ? -9.198  -3.482  4.702   1.00 11.79  ? 66  PHE A CG  1 
ATOM   541  C  CD1 . PHE A 1 66  ? -10.448 -2.976  5.027   1.00 11.54  ? 66  PHE A CD1 1 
ATOM   542  C  CD2 . PHE A 1 66  ? -8.947  -4.847  4.884   1.00 12.55  ? 66  PHE A CD2 1 
ATOM   543  C  CE1 . PHE A 1 66  ? -11.427 -3.838  5.513   1.00 11.47  ? 66  PHE A CE1 1 
ATOM   544  C  CE2 . PHE A 1 66  ? -9.925  -5.717  5.374   1.00 11.83  ? 66  PHE A CE2 1 
ATOM   545  C  CZ  . PHE A 1 66  ? -11.179 -5.190  5.692   1.00 13.36  ? 66  PHE A CZ  1 
ATOM   546  N  N   . ASN A 1 67  ? -8.341  0.333   5.845   1.00 11.76  ? 67  ASN A N   1 
ATOM   547  C  CA  . ASN A 1 67  ? -9.241  1.266   6.537   1.00 11.44  ? 67  ASN A CA  1 
ATOM   548  C  C   . ASN A 1 67  ? -10.479 1.619   5.715   1.00 13.13  ? 67  ASN A C   1 
ATOM   549  O  O   . ASN A 1 67  ? -10.351 1.990   4.539   1.00 13.55  ? 67  ASN A O   1 
ATOM   550  C  CB  . ASN A 1 67  ? -8.581  2.604   6.795   1.00 11.54  ? 67  ASN A CB  1 
ATOM   551  C  CG  . ASN A 1 67  ? -7.443  2.540   7.770   1.00 11.74  ? 67  ASN A CG  1 
ATOM   552  O  OD1 . ASN A 1 67  ? -7.378  1.583   8.595   1.00 13.33  ? 67  ASN A OD1 1 
ATOM   553  N  ND2 . ASN A 1 67  ? -6.577  3.556   7.753   1.00 14.57  ? 67  ASN A ND2 1 
ATOM   554  N  N   . VAL A 1 68  ? -11.658 1.541   6.336   1.00 12.08  ? 68  VAL A N   1 
ATOM   555  C  CA  . VAL A 1 68  ? -12.879 2.152   5.790   1.00 12.08  ? 68  VAL A CA  1 
ATOM   556  C  C   . VAL A 1 68  ? -12.987 3.560   6.400   1.00 12.48  ? 68  VAL A C   1 
ATOM   557  O  O   . VAL A 1 68  ? -13.049 3.684   7.646   1.00 13.18  ? 68  VAL A O   1 
ATOM   558  C  CB  . VAL A 1 68  ? -14.133 1.283   5.957   1.00 14.41  ? 68  VAL A CB  1 
ATOM   559  C  CG1 . VAL A 1 68  ? -15.394 2.055   5.528   1.00 14.79  ? 68  VAL A CG1 1 
ATOM   560  C  CG2 . VAL A 1 68  ? -13.950 -0.047  5.210   1.00 13.13  ? 68  VAL A CG2 1 
ATOM   561  N  N   . GLU A 1 69  ? -12.914 4.592   5.546   1.00 14.12  ? 69  GLU A N   1 
ATOM   562  C  CA  . GLU A 1 69  ? -12.785 5.971   6.039   1.00 13.19  ? 69  GLU A CA  1 
ATOM   563  C  C   . GLU A 1 69  ? -14.155 6.656   5.987   1.00 13.00  ? 69  GLU A C   1 
ATOM   564  O  O   . GLU A 1 69  ? -14.951 6.431   5.024   1.00 15.89  ? 69  GLU A O   1 
ATOM   565  C  CB  . GLU A 1 69  ? -11.888 6.779   5.094   1.00 14.52  ? 69  GLU A CB  1 
ATOM   566  C  CG  . GLU A 1 69  ? -10.465 6.198   5.137   1.00 15.95  ? 69  GLU A CG  1 
ATOM   567  C  CD  . GLU A 1 69  ? -9.638  6.663   3.921   1.00 18.53  ? 69  GLU A CD  1 
ATOM   568  O  OE1 . GLU A 1 69  ? -10.164 7.417   3.040   1.00 17.06  ? 69  GLU A OE1 1 
ATOM   569  O  OE2 . GLU A 1 69  ? -8.439  6.272   3.829   1.00 16.47  ? 69  GLU A OE2 1 
ATOM   570  N  N   . PHE A 1 70  ? -14.383 7.595   6.947   1.00 13.74  ? 70  PHE A N   1 
ATOM   571  C  CA  . PHE A 1 70  ? -15.637 8.357   7.042   1.00 13.67  ? 70  PHE A CA  1 
ATOM   572  C  C   . PHE A 1 70  ? -15.378 9.859   6.935   1.00 15.23  ? 70  PHE A C   1 
ATOM   573  O  O   . PHE A 1 70  ? -14.314 10.352  7.348   1.00 14.54  ? 70  PHE A O   1 
ATOM   574  C  CB  . PHE A 1 70  ? -16.338 8.018   8.378   1.00 12.89  ? 70  PHE A CB  1 
ATOM   575  C  CG  . PHE A 1 70  ? -16.870 6.588   8.390   1.00 12.36  ? 70  PHE A CG  1 
ATOM   576  C  CD1 . PHE A 1 70  ? -16.025 5.481   8.586   1.00 13.43  ? 70  PHE A CD1 1 
ATOM   577  C  CD2 . PHE A 1 70  ? -18.194 6.338   8.060   1.00 12.68  ? 70  PHE A CD2 1 
ATOM   578  C  CE1 . PHE A 1 70  ? -16.511 4.181   8.522   1.00 13.96  ? 70  PHE A CE1 1 
ATOM   579  C  CE2 . PHE A 1 70  ? -18.696 5.030   8.035   1.00 15.14  ? 70  PHE A CE2 1 
ATOM   580  C  CZ  . PHE A 1 70  ? -17.832 3.946   8.202   1.00 14.48  ? 70  PHE A CZ  1 
ATOM   581  N  N   . ASP A 1 71  ? -16.425 10.604  6.496   1.00 17.35  ? 71  ASP A N   1 
ATOM   582  C  CA  . ASP A 1 71  ? -16.379 12.052  6.590   1.00 18.21  ? 71  ASP A CA  1 
ATOM   583  C  C   . ASP A 1 71  ? -16.576 12.436  8.069   1.00 15.43  ? 71  ASP A C   1 
ATOM   584  O  O   . ASP A 1 71  ? -17.686 12.312  8.615   1.00 19.22  ? 71  ASP A O   1 
ATOM   585  C  CB  . ASP A 1 71  ? -17.523 12.634  5.752   1.00 22.53  ? 71  ASP A CB  1 
ATOM   586  C  CG  . ASP A 1 71  ? -17.671 14.139  5.964   1.00 27.01  ? 71  ASP A CG  1 
ATOM   587  O  OD1 . ASP A 1 71  ? -16.781 14.776  6.556   1.00 27.02  ? 71  ASP A OD1 1 
ATOM   588  O  OD2 . ASP A 1 71  ? -18.647 14.674  5.529   1.00 36.46  ? 71  ASP A OD2 1 
ATOM   589  N  N   . ASP A 1 72  ? -15.542 12.945  8.716   1.00 15.50  ? 72  ASP A N   1 
ATOM   590  C  CA  . ASP A 1 72  ? -15.626 13.371  10.112  1.00 16.49  ? 72  ASP A CA  1 
ATOM   591  C  C   . ASP A 1 72  ? -15.536 14.905  10.183  1.00 21.96  ? 72  ASP A C   1 
ATOM   592  O  O   . ASP A 1 72  ? -15.135 15.447  11.210  1.00 24.61  ? 72  ASP A O   1 
ATOM   593  C  CB  . ASP A 1 72  ? -14.497 12.718  10.926  1.00 17.11  ? 72  ASP A CB  1 
ATOM   594  C  CG  . ASP A 1 72  ? -13.079 13.151  10.555  1.00 22.10  ? 72  ASP A CG  1 
ATOM   595  O  OD1 . ASP A 1 72  ? -12.871 13.711  9.443   1.00 27.51  ? 72  ASP A OD1 1 
ATOM   596  O  OD2 . ASP A 1 72  ? -12.187 12.884  11.323  1.00 21.04  ? 72  ASP A OD2 1 
ATOM   597  N  N   . SER A 1 73  ? -15.873 15.599  9.083   1.00 20.94  ? 73  SER A N   1 
ATOM   598  C  CA  . SER A 1 73  ? -15.765 17.071  9.084   1.00 25.09  ? 73  SER A CA  1 
ATOM   599  C  C   . SER A 1 73  ? -16.989 17.728  9.756   1.00 32.12  ? 73  SER A C   1 
ATOM   600  O  O   . SER A 1 73  ? -17.041 18.984  9.904   1.00 33.53  ? 73  SER A O   1 
ATOM   601  C  CB  . SER A 1 73  ? -15.566 17.610  7.681   1.00 29.56  ? 73  SER A CB  1 
ATOM   602  O  OG  . SER A 1 73  ? -16.807 17.529  6.971   1.00 24.34  ? 73  SER A OG  1 
ATOM   603  N  N   . GLN A 1 74  ? -17.995 16.898  10.111  1.00 33.20  ? 74  GLN A N   1 
ATOM   604  C  CA  . GLN A 1 74  ? -19.152 17.341  10.899  1.00 32.61  ? 74  GLN A CA  1 
ATOM   605  C  C   . GLN A 1 74  ? -19.525 16.261  11.903  1.00 26.28  ? 74  GLN A C   1 
ATOM   606  O  O   . GLN A 1 74  ? -19.065 15.131  11.726  1.00 22.38  ? 74  GLN A O   1 
ATOM   607  C  CB  . GLN A 1 74  ? -20.381 17.439  9.997   1.00 39.22  ? 74  GLN A CB  1 
ATOM   608  C  CG  . GLN A 1 74  ? -20.465 18.787  9.337   1.00 39.62  ? 74  GLN A CG  1 
ATOM   609  C  CD  . GLN A 1 74  ? -21.865 18.958  8.822   1.00 53.74  ? 74  GLN A CD  1 
ATOM   610  O  OE1 . GLN A 1 74  ? -22.708 19.587  9.477   1.00 67.44  ? 74  GLN A OE1 1 
ATOM   611  N  NE2 . GLN A 1 74  ? -22.115 18.356  7.659   1.00 45.89  ? 74  GLN A NE2 1 
ATOM   612  N  N   . ASP A 1 75  ? -20.341 16.605  12.929  1.00 33.47  ? 75  ASP A N   1 
ATOM   613  C  CA  . ASP A 1 75  ? -20.840 15.598  13.861  1.00 33.97  ? 75  ASP A CA  1 
ATOM   614  C  C   . ASP A 1 75  ? -21.906 14.788  13.158  1.00 36.87  ? 75  ASP A C   1 
ATOM   615  O  O   . ASP A 1 75  ? -23.053 15.234  13.021  1.00 60.58  ? 75  ASP A O   1 
ATOM   616  C  CB  . ASP A 1 75  ? -21.520 16.143  15.126  1.00 40.86  ? 75  ASP A CB  1 
ATOM   617  C  CG  . ASP A 1 75  ? -20.647 16.148  16.390  1.00 47.45  ? 75  ASP A CG  1 
ATOM   618  O  OD1 . ASP A 1 75  ? -19.662 15.324  16.508  1.00 42.76  ? 75  ASP A OD1 1 
ATOM   619  O  OD2 . ASP A 1 75  ? -20.966 16.949  17.301  1.00 58.49  ? 75  ASP A OD2 1 
ATOM   620  N  N   . LYS A 1 76  ? -21.508 13.602  12.705  1.00 24.35  ? 76  LYS A N   1 
ATOM   621  C  CA  . LYS A 1 76  ? -22.438 12.674  12.077  1.00 29.59  ? 76  LYS A CA  1 
ATOM   622  C  C   . LYS A 1 76  ? -22.447 11.359  12.859  1.00 35.29  ? 76  LYS A C   1 
ATOM   623  O  O   . LYS A 1 76  ? -23.383 11.100  13.610  1.00 44.38  ? 76  LYS A O   1 
ATOM   624  C  CB  . LYS A 1 76  ? -22.053 12.488  10.605  1.00 30.88  ? 76  LYS A CB  1 
ATOM   625  C  CG  . LYS A 1 76  ? -22.267 13.732  9.722   1.00 39.30  ? 76  LYS A CG  1 
ATOM   626  C  CD  . LYS A 1 76  ? -21.771 13.481  8.326   1.00 50.75  ? 76  LYS A CD  1 
ATOM   627  C  CE  . LYS A 1 76  ? -22.388 14.355  7.251   1.00 52.62  ? 76  LYS A CE  1 
ATOM   628  N  NZ  . LYS A 1 76  ? -21.521 14.353  6.054   1.00 43.38  ? 76  LYS A NZ  1 
ATOM   629  N  N   . ALA A 1 77  ? -21.413 10.538  12.692  1.00 25.30  ? 77  ALA A N   1 
ATOM   630  C  CA  . ALA A 1 77  ? -21.416 9.243   13.374  1.00 18.47  ? 77  ALA A CA  1 
ATOM   631  C  C   . ALA A 1 77  ? -20.628 9.442   14.682  1.00 17.76  ? 77  ALA A C   1 
ATOM   632  O  O   . ALA A 1 77  ? -19.403 9.719   14.620  1.00 21.49  ? 77  ALA A O   1 
ATOM   633  C  CB  . ALA A 1 77  ? -20.723 8.237   12.485  1.00 22.68  ? 77  ALA A CB  1 
ATOM   634  N  N   . VAL A 1 78  ? -21.268 9.308   15.864  1.00 15.36  ? 78  VAL A N   1 
ATOM   635  C  CA  . VAL A 1 78  ? -20.587 9.617   17.126  1.00 15.83  ? 78  VAL A CA  1 
ATOM   636  C  C   . VAL A 1 78  ? -20.848 8.542   18.189  1.00 14.39  ? 78  VAL A C   1 
ATOM   637  O  O   . VAL A 1 78  ? -21.870 7.834   18.241  1.00 15.48  ? 78  VAL A O   1 
ATOM   638  C  CB  . VAL A 1 78  ? -20.965 11.015  17.638  1.00 20.91  ? 78  VAL A CB  1 
ATOM   639  C  CG1 . VAL A 1 78  ? -20.688 12.126  16.634  1.00 25.69  ? 78  VAL A CG1 1 
ATOM   640  C  CG2 . VAL A 1 78  ? -22.409 11.043  18.080  1.00 23.08  ? 78  VAL A CG2 1 
ATOM   641  N  N   . LEU A 1 79  ? -19.838 8.387   19.036  1.00 12.30  ? 79  LEU A N   1 
ATOM   642  C  CA  . LEU A 1 79  ? -19.867 7.476   20.191  1.00 12.39  ? 79  LEU A CA  1 
ATOM   643  C  C   . LEU A 1 79  ? -19.854 8.355   21.448  1.00 11.97  ? 79  LEU A C   1 
ATOM   644  O  O   . LEU A 1 79  ? -19.036 9.311   21.535  1.00 13.95  ? 79  LEU A O   1 
ATOM   645  C  CB  . LEU A 1 79  ? -18.645 6.548   20.084  1.00 13.70  ? 79  LEU A CB  1 
ATOM   646  C  CG  . LEU A 1 79  ? -18.469 5.542   21.203  1.00 12.88  ? 79  LEU A CG  1 
ATOM   647  C  CD1 . LEU A 1 79  ? -19.558 4.483   21.105  1.00 17.39  ? 79  LEU A CD1 1 
ATOM   648  C  CD2 . LEU A 1 79  ? -17.095 4.851   21.140  1.00 13.12  ? 79  LEU A CD2 1 
ATOM   649  N  N   A LYS A 1 80  ? -20.664 7.995   22.439  0.50 12.26  ? 80  LYS A N   1 
ATOM   650  N  N   B LYS A 1 80  ? -20.781 8.090   22.378  0.50 12.81  ? 80  LYS A N   1 
ATOM   651  C  CA  A LYS A 1 80  ? -20.637 8.710   23.703  0.50 13.79  ? 80  LYS A CA  1 
ATOM   652  C  CA  B LYS A 1 80  ? -20.901 8.828   23.632  0.50 13.93  ? 80  LYS A CA  1 
ATOM   653  C  C   A LYS A 1 80  ? -21.273 7.821   24.758  0.50 13.86  ? 80  LYS A C   1 
ATOM   654  C  C   B LYS A 1 80  ? -21.306 7.853   24.734  0.50 13.27  ? 80  LYS A C   1 
ATOM   655  O  O   A LYS A 1 80  ? -21.679 6.689   24.460  0.50 14.12  ? 80  LYS A O   1 
ATOM   656  O  O   B LYS A 1 80  ? -21.567 6.676   24.449  0.50 13.11  ? 80  LYS A O   1 
ATOM   657  C  CB  A LYS A 1 80  ? -21.362 10.059  23.606  0.50 16.21  ? 80  LYS A CB  1 
ATOM   658  C  CB  B LYS A 1 80  ? -21.919 9.983   23.585  0.50 17.41  ? 80  LYS A CB  1 
ATOM   659  C  CG  A LYS A 1 80  ? -22.851 9.912   23.348  0.50 14.68  ? 80  LYS A CG  1 
ATOM   660  C  CG  B LYS A 1 80  ? -21.976 10.833  22.328  0.50 19.39  ? 80  LYS A CG  1 
ATOM   661  C  CD  A LYS A 1 80  ? -23.499 11.245  22.971  0.50 18.60  ? 80  LYS A CD  1 
ATOM   662  C  CD  B LYS A 1 80  ? -23.060 11.908  22.494  0.50 22.15  ? 80  LYS A CD  1 
ATOM   663  C  CE  A LYS A 1 80  ? -22.764 11.951  21.841  0.50 31.72  ? 80  LYS A CE  1 
ATOM   664  C  CE  B LYS A 1 80  ? -23.989 11.630  23.659  0.50 20.15  ? 80  LYS A CE  1 
ATOM   665  N  NZ  A LYS A 1 80  ? -23.359 13.243  21.374  0.50 39.19  ? 80  LYS A NZ  1 
ATOM   666  N  NZ  B LYS A 1 80  ? -25.268 10.990  23.235  0.50 27.98  ? 80  LYS A NZ  1 
ATOM   667  N  N   . GLY A 1 81  ? -21.330 8.335   25.992  1.00 13.72  ? 81  GLY A N   1 
ATOM   668  C  CA  . GLY A 1 81  ? -21.833 7.518   27.093  1.00 14.18  ? 81  GLY A CA  1 
ATOM   669  C  C   . GLY A 1 81  ? -20.842 6.412   27.417  1.00 15.74  ? 81  GLY A C   1 
ATOM   670  O  O   . GLY A 1 81  ? -19.641 6.586   27.178  1.00 15.72  ? 81  GLY A O   1 
ATOM   671  N  N   . GLY A 1 82  ? -21.358 5.360   28.078  1.00 16.92  ? 82  GLY A N   1 
ATOM   672  C  CA  . GLY A 1 82  ? -20.416 4.369   28.573  1.00 22.41  ? 82  GLY A CA  1 
ATOM   673  C  C   . GLY A 1 82  ? -19.481 5.001   29.599  1.00 19.58  ? 82  GLY A C   1 
ATOM   674  O  O   . GLY A 1 82  ? -19.926 5.756   30.478  1.00 23.28  ? 82  GLY A O   1 
ATOM   675  N  N   . PRO A 1 83  ? -18.130 4.771   29.454  1.00 14.95  ? 83  PRO A N   1 
ATOM   676  C  CA  . PRO A 1 83  ? -17.152 5.426   30.306  1.00 17.04  ? 83  PRO A CA  1 
ATOM   677  C  C   . PRO A 1 83  ? -16.754 6.849   29.868  1.00 15.02  ? 83  PRO A C   1 
ATOM   678  O  O   . PRO A 1 83  ? -15.925 7.476   30.503  1.00 18.96  ? 83  PRO A O   1 
ATOM   679  C  CB  . PRO A 1 83  ? -15.950 4.458   30.168  1.00 17.67  ? 83  PRO A CB  1 
ATOM   680  C  CG  . PRO A 1 83  ? -15.997 4.031   28.704  1.00 13.88  ? 83  PRO A CG  1 
ATOM   681  C  CD  . PRO A 1 83  ? -17.498 3.891   28.442  1.00 12.51  ? 83  PRO A CD  1 
ATOM   682  N  N   . LEU A 1 84  ? -17.306 7.321   28.735  1.00 13.84  ? 84  LEU A N   1 
ATOM   683  C  CA  . LEU A 1 84  ? -16.753 8.507   28.090  1.00 12.86  ? 84  LEU A CA  1 
ATOM   684  C  C   . LEU A 1 84  ? -17.421 9.785   28.617  1.00 17.54  ? 84  LEU A C   1 
ATOM   685  O  O   . LEU A 1 84  ? -18.631 9.802   28.937  1.00 18.80  ? 84  LEU A O   1 
ATOM   686  C  CB  . LEU A 1 84  ? -17.087 8.445   26.610  1.00 11.54  ? 84  LEU A CB  1 
ATOM   687  C  CG  . LEU A 1 84  ? -16.508 7.200   25.900  1.00 11.27  ? 84  LEU A CG  1 
ATOM   688  C  CD1 . LEU A 1 84  ? -16.998 7.128   24.447  1.00 12.91  ? 84  LEU A CD1 1 
ATOM   689  C  CD2 . LEU A 1 84  ? -14.968 7.204   25.988  1.00 11.83  ? 84  LEU A CD2 1 
ATOM   690  N  N   . ASP A 1 85  ? -16.652 10.885  28.618  1.00 18.29  ? 85  ASP A N   1 
ATOM   691  C  CA  . ASP A 1 85  ? -17.234 12.222  28.799  1.00 21.16  ? 85  ASP A CA  1 
ATOM   692  C  C   . ASP A 1 85  ? -17.163 12.927  27.447  1.00 22.67  ? 85  ASP A C   1 
ATOM   693  O  O   . ASP A 1 85  ? -16.122 12.930  26.766  1.00 29.32  ? 85  ASP A O   1 
ATOM   694  C  CB  . ASP A 1 85  ? -16.431 13.095  29.772  1.00 34.17  ? 85  ASP A CB  1 
ATOM   695  C  CG  . ASP A 1 85  ? -16.525 12.600  31.196  1.00 56.01  ? 85  ASP A CG  1 
ATOM   696  O  OD1 . ASP A 1 85  ? -17.574 11.969  31.525  1.00 84.24  ? 85  ASP A OD1 1 
ATOM   697  O  OD2 . ASP A 1 85  ? -15.560 12.843  31.970  1.00 83.34  ? 85  ASP A OD2 1 
ATOM   698  N  N   . GLY A 1 86  ? -18.243 13.593  27.069  1.00 30.72  ? 86  GLY A N   1 
ATOM   699  C  CA  . GLY A 1 86  ? -18.208 14.248  25.772  1.00 27.24  ? 86  GLY A CA  1 
ATOM   700  C  C   . GLY A 1 86  ? -18.429 13.282  24.595  1.00 23.23  ? 86  GLY A C   1 
ATOM   701  O  O   . GLY A 1 86  ? -18.971 12.150  24.728  1.00 28.25  ? 86  GLY A O   1 
ATOM   702  N  N   . THR A 1 87  ? -18.072 13.818  23.421  1.00 16.55  ? 87  THR A N   1 
ATOM   703  C  CA  . THR A 1 87  ? -18.538 13.325  22.132  1.00 19.05  ? 87  THR A CA  1 
ATOM   704  C  C   . THR A 1 87  ? -17.314 12.899  21.307  1.00 13.76  ? 87  THR A C   1 
ATOM   705  O  O   . THR A 1 87  ? -16.381 13.695  21.163  1.00 14.49  ? 87  THR A O   1 
ATOM   706  C  CB  . THR A 1 87  ? -19.266 14.474  21.396  1.00 26.09  ? 87  THR A CB  1 
ATOM   707  O  OG1 . THR A 1 87  ? -20.430 14.742  22.167  1.00 32.07  ? 87  THR A OG1 1 
ATOM   708  C  CG2 . THR A 1 87  ? -19.590 14.108  19.947  1.00 28.17  ? 87  THR A CG2 1 
ATOM   709  N  N   . TYR A 1 88  ? -17.370 11.694  20.752  1.00 12.10  ? 88  TYR A N   1 
ATOM   710  C  CA  . TYR A 1 88  ? -16.282 11.153  19.943  1.00 10.63  ? 88  TYR A CA  1 
ATOM   711  C  C   . TYR A 1 88  ? -16.770 10.857  18.546  1.00 11.05  ? 88  TYR A C   1 
ATOM   712  O  O   . TYR A 1 88  ? -17.731 10.086  18.403  1.00 15.09  ? 88  TYR A O   1 
ATOM   713  C  CB  . TYR A 1 88  ? -15.658 9.937   20.597  1.00 10.23  ? 88  TYR A CB  1 
ATOM   714  C  CG  . TYR A 1 88  ? -14.905 10.141  21.886  1.00 10.08  ? 88  TYR A CG  1 
ATOM   715  C  CD1 . TYR A 1 88  ? -15.547 10.506  23.068  1.00 11.17  ? 88  TYR A CD1 1 
ATOM   716  C  CD2 . TYR A 1 88  ? -13.502 9.976   21.913  1.00 9.87   ? 88  TYR A CD2 1 
ATOM   717  C  CE1 . TYR A 1 88  ? -14.830 10.680  24.241  1.00 11.38  ? 88  TYR A CE1 1 
ATOM   718  C  CE2 . TYR A 1 88  ? -12.775 10.075  23.104  1.00 9.69   ? 88  TYR A CE2 1 
ATOM   719  C  CZ  . TYR A 1 88  ? -13.458 10.442  24.272  1.00 10.06  ? 88  TYR A CZ  1 
ATOM   720  O  OH  . TYR A 1 88  ? -12.762 10.562  25.451  1.00 10.88  ? 88  TYR A OH  1 
ATOM   721  N  N   . ARG A 1 89  ? -16.055 11.371  17.523  1.00 10.94  ? 89  ARG A N   1 
ATOM   722  C  CA  . ARG A 1 89  ? -16.523 11.222  16.122  1.00 11.13  ? 89  ARG A CA  1 
ATOM   723  C  C   . ARG A 1 89  ? -15.800 10.070  15.414  1.00 10.31  ? 89  ARG A C   1 
ATOM   724  O  O   . ARG A 1 89  ? -14.582 9.959   15.510  1.00 9.87   ? 89  ARG A O   1 
ATOM   725  C  CB  . ARG A 1 89  ? -16.066 12.508  15.395  1.00 14.72  ? 89  ARG A CB  1 
ATOM   726  C  CG  . ARG A 1 89  ? -16.950 12.870  14.224  1.00 23.69  ? 89  ARG A CG  1 
ATOM   727  C  CD  . ARG A 1 89  ? -16.570 14.290  13.815  1.00 23.00  ? 89  ARG A CD  1 
ATOM   728  N  NE  . ARG A 1 89  ? -17.331 15.288  14.541  1.00 21.85  ? 89  ARG A NE  1 
ATOM   729  C  CZ  . ARG A 1 89  ? -17.130 16.607  14.389  1.00 24.55  ? 89  ARG A CZ  1 
ATOM   730  N  NH1 . ARG A 1 89  ? -16.285 17.092  13.468  1.00 27.61  ? 89  ARG A NH1 1 
ATOM   731  N  NH2 . ARG A 1 89  ? -17.885 17.464  15.076  1.00 31.62  ? 89  ARG A NH2 1 
ATOM   732  N  N   . LEU A 1 90  ? -16.595 9.237   14.713  1.00 10.15  ? 90  LEU A N   1 
ATOM   733  C  CA  . LEU A 1 90  ? -15.994 8.137   13.952  1.00 9.92   ? 90  LEU A CA  1 
ATOM   734  C  C   . LEU A 1 90  ? -15.160 8.723   12.812  1.00 10.98  ? 90  LEU A C   1 
ATOM   735  O  O   . LEU A 1 90  ? -15.654 9.450   11.967  1.00 12.04  ? 90  LEU A O   1 
ATOM   736  C  CB  . LEU A 1 90  ? -17.134 7.259   13.408  1.00 10.09  ? 90  LEU A CB  1 
ATOM   737  C  CG  . LEU A 1 90  ? -16.688 6.054   12.542  1.00 11.02  ? 90  LEU A CG  1 
ATOM   738  C  CD1 . LEU A 1 90  ? -15.917 4.968   13.357  1.00 12.18  ? 90  LEU A CD1 1 
ATOM   739  C  CD2 . LEU A 1 90  ? -17.958 5.374   11.970  1.00 13.16  ? 90  LEU A CD2 1 
ATOM   740  N  N   . ILE A 1 91  ? -13.923 8.231   12.717  1.00 9.11   ? 91  ILE A N   1 
ATOM   741  C  CA  . ILE A 1 91  ? -13.038 8.593   11.614  1.00 9.33   ? 91  ILE A CA  1 
ATOM   742  C  C   . ILE A 1 91  ? -12.743 7.401   10.681  1.00 10.37  ? 91  ILE A C   1 
ATOM   743  O  O   . ILE A 1 91  ? -12.678 7.573   9.462   1.00 10.18  ? 91  ILE A O   1 
ATOM   744  C  CB  . ILE A 1 91  ? -11.718 9.278   12.105  1.00 11.80  ? 91  ILE A CB  1 
ATOM   745  C  CG1 . ILE A 1 91  ? -10.764 9.591   10.930  1.00 13.59  ? 91  ILE A CG1 1 
ATOM   746  C  CG2 . ILE A 1 91  ? -10.952 8.396   13.164  1.00 11.30  ? 91  ILE A CG2 1 
ATOM   747  C  CD1 . ILE A 1 91  ? -9.594  10.462  11.333  1.00 15.52  ? 91  ILE A CD1 1 
ATOM   748  N  N   . GLN A 1 92  ? -12.625 6.155   11.223  1.00 10.00  ? 92  GLN A N   1 
ATOM   749  C  CA  . GLN A 1 92  ? -12.268 5.024   10.361  1.00 9.97   ? 92  GLN A CA  1 
ATOM   750  C  C   . GLN A 1 92  ? -12.590 3.752   11.132  1.00 8.89   ? 92  GLN A C   1 
ATOM   751  O  O   . GLN A 1 92  ? -12.578 3.781   12.392  1.00 9.60   ? 92  GLN A O   1 
ATOM   752  C  CB  . GLN A 1 92  ? -10.796 4.995   9.859   1.00 10.71  ? 92  GLN A CB  1 
ATOM   753  C  CG  . GLN A 1 92  ? -9.770  5.111   11.029  1.00 11.44  ? 92  GLN A CG  1 
ATOM   754  C  CD  . GLN A 1 92  ? -8.927  3.843   11.186  1.00 9.56   ? 92  GLN A CD  1 
ATOM   755  O  OE1 . GLN A 1 92  ? -9.480  2.731   11.292  1.00 10.31  ? 92  GLN A OE1 1 
ATOM   756  N  NE2 . GLN A 1 92  ? -7.617  4.091   11.330  1.00 11.69  ? 92  GLN A NE2 1 
ATOM   757  N  N   . PHE A 1 93  ? -12.732 2.628   10.417  1.00 9.26   ? 93  PHE A N   1 
ATOM   758  C  CA  . PHE A 1 93  ? -12.570 1.323   11.052  1.00 9.34   ? 93  PHE A CA  1 
ATOM   759  C  C   . PHE A 1 93  ? -11.592 0.448   10.248  1.00 9.35   ? 93  PHE A C   1 
ATOM   760  O  O   . PHE A 1 93  ? -11.388 0.624   9.024   1.00 10.30  ? 93  PHE A O   1 
ATOM   761  C  CB  . PHE A 1 93  ? -13.901 0.595   11.274  1.00 10.30  ? 93  PHE A CB  1 
ATOM   762  C  CG  . PHE A 1 93  ? -14.674 0.098   10.064  1.00 10.83  ? 93  PHE A CG  1 
ATOM   763  C  CD1 . PHE A 1 93  ? -14.267 -1.070  9.407   1.00 10.59  ? 93  PHE A CD1 1 
ATOM   764  C  CD2 . PHE A 1 93  ? -15.829 0.777   9.655   1.00 12.19  ? 93  PHE A CD2 1 
ATOM   765  C  CE1 . PHE A 1 93  ? -14.989 -1.516  8.288   1.00 11.57  ? 93  PHE A CE1 1 
ATOM   766  C  CE2 . PHE A 1 93  ? -16.553 0.322   8.540   1.00 14.13  ? 93  PHE A CE2 1 
ATOM   767  C  CZ  . PHE A 1 93  ? -16.147 -0.838  7.905   1.00 15.09  ? 93  PHE A CZ  1 
ATOM   768  N  N   . HIS A 1 94  ? -11.043 -0.588  10.921  1.00 7.62   ? 94  HIS A N   1 
ATOM   769  C  CA  . HIS A 1 94  ? -10.164 -1.573  10.287  1.00 7.91   ? 94  HIS A CA  1 
ATOM   770  C  C   . HIS A 1 94  ? -10.267 -2.844  11.118  1.00 7.70   ? 94  HIS A C   1 
ATOM   771  O  O   . HIS A 1 94  ? -10.869 -2.829  12.210  1.00 8.46   ? 94  HIS A O   1 
ATOM   772  C  CB  . HIS A 1 94  ? -8.697  -1.016  10.211  1.00 8.70   ? 94  HIS A CB  1 
ATOM   773  C  CG  . HIS A 1 94  ? -8.173  -0.762  11.600  1.00 8.02   ? 94  HIS A CG  1 
ATOM   774  N  ND1 . HIS A 1 94  ? -8.369  0.455   12.271  1.00 8.27   ? 94  HIS A ND1 1 
ATOM   775  C  CD2 . HIS A 1 94  ? -7.575  -1.605  12.484  1.00 8.13   ? 94  HIS A CD2 1 
ATOM   776  C  CE1 . HIS A 1 94  ? -7.892  0.361   13.510  1.00 8.10   ? 94  HIS A CE1 1 
ATOM   777  N  NE2 . HIS A 1 94  ? -7.391  -0.945  13.651  1.00 7.60   ? 94  HIS A NE2 1 
ATOM   778  N  N   . PHE A 1 95  ? -9.557  -3.884  10.667  1.00 8.00   ? 95  PHE A N   1 
ATOM   779  C  CA  . PHE A 1 95  ? -9.560  -5.193  11.366  1.00 9.05   ? 95  PHE A CA  1 
ATOM   780  C  C   . PHE A 1 95  ? -8.117  -5.658  11.593  1.00 8.64   ? 95  PHE A C   1 
ATOM   781  O  O   . PHE A 1 95  ? -7.196  -5.187  10.892  1.00 8.99   ? 95  PHE A O   1 
ATOM   782  C  CB  . PHE A 1 95  ? -10.291 -6.291  10.568  1.00 9.49   ? 95  PHE A CB  1 
ATOM   783  C  CG  . PHE A 1 95  ? -11.750 -5.999  10.242  1.00 8.73   ? 95  PHE A CG  1 
ATOM   784  C  CD1 . PHE A 1 95  ? -12.036 -5.199  9.152   1.00 10.67  ? 95  PHE A CD1 1 
ATOM   785  C  CD2 . PHE A 1 95  ? -12.770 -6.670  10.914  1.00 10.05  ? 95  PHE A CD2 1 
ATOM   786  C  CE1 . PHE A 1 95  ? -13.361 -4.975  8.773   1.00 10.71  ? 95  PHE A CE1 1 
ATOM   787  C  CE2 . PHE A 1 95  ? -14.089 -6.457  10.540  1.00 11.11  ? 95  PHE A CE2 1 
ATOM   788  C  CZ  . PHE A 1 95  ? -14.386 -5.588  9.486   1.00 11.59  ? 95  PHE A CZ  1 
ATOM   789  N  N   . HIS A 1 96  ? -7.954  -6.621  12.499  1.00 7.90   ? 96  HIS A N   1 
ATOM   790  C  CA  . HIS A 1 96  ? -6.747  -7.448  12.665  1.00 7.82   ? 96  HIS A CA  1 
ATOM   791  C  C   . HIS A 1 96  ? -7.205  -8.893  12.569  1.00 8.20   ? 96  HIS A C   1 
ATOM   792  O  O   . HIS A 1 96  ? -8.276  -9.270  13.056  1.00 8.62   ? 96  HIS A O   1 
ATOM   793  C  CB  . HIS A 1 96  ? -6.100  -7.249  14.061  1.00 8.38   ? 96  HIS A CB  1 
ATOM   794  C  CG  . HIS A 1 96  ? -5.783  -5.783  14.289  1.00 8.04   ? 96  HIS A CG  1 
ATOM   795  N  ND1 . HIS A 1 96  ? -4.552  -5.137  14.049  1.00 9.37   ? 96  HIS A ND1 1 
ATOM   796  C  CD2 . HIS A 1 96  ? -6.624  -4.772  14.704  1.00 7.30   ? 96  HIS A CD2 1 
ATOM   797  C  CE1 . HIS A 1 96  ? -4.673  -3.834  14.317  1.00 9.10   ? 96  HIS A CE1 1 
ATOM   798  N  NE2 . HIS A 1 96  ? -5.886  -3.559  14.743  1.00 8.20   ? 96  HIS A NE2 1 
ATOM   799  N  N   . TRP A 1 97  ? -6.417  -9.783  11.910  1.00 7.71   ? 97  TRP A N   1 
ATOM   800  C  CA  . TRP A 1 97  ? -6.860  -11.167 11.711  1.00 8.97   ? 97  TRP A CA  1 
ATOM   801  C  C   . TRP A 1 97  ? -5.660  -12.087 11.551  1.00 8.89   ? 97  TRP A C   1 
ATOM   802  O  O   . TRP A 1 97  ? -4.490  -11.633 11.480  1.00 9.20   ? 97  TRP A O   1 
ATOM   803  C  CB  . TRP A 1 97  ? -7.796  -11.264 10.476  1.00 9.50   ? 97  TRP A CB  1 
ATOM   804  C  CG  . TRP A 1 97  ? -7.152  -10.892 9.155   1.00 9.69   ? 97  TRP A CG  1 
ATOM   805  C  CD1 . TRP A 1 97  ? -6.453  -11.700 8.281   1.00 9.02   ? 97  TRP A CD1 1 
ATOM   806  C  CD2 . TRP A 1 97  ? -7.063  -9.554  8.577   1.00 9.48   ? 97  TRP A CD2 1 
ATOM   807  N  NE1 . TRP A 1 97  ? -6.014  -10.986 7.194   1.00 10.59  ? 97  TRP A NE1 1 
ATOM   808  C  CE2 . TRP A 1 97  ? -6.402  -9.666  7.329   1.00 9.99   ? 97  TRP A CE2 1 
ATOM   809  C  CE3 . TRP A 1 97  ? -7.582  -8.275  8.974   1.00 8.99   ? 97  TRP A CE3 1 
ATOM   810  C  CZ2 . TRP A 1 97  ? -6.165  -8.559  6.475   1.00 11.02  ? 97  TRP A CZ2 1 
ATOM   811  C  CZ3 . TRP A 1 97  ? -7.301  -7.170  8.153   1.00 10.78  ? 97  TRP A CZ3 1 
ATOM   812  C  CH2 . TRP A 1 97  ? -6.659  -7.327  6.897   1.00 11.51  ? 97  TRP A CH2 1 
ATOM   813  N  N   . GLY A 1 98  ? -5.990  -13.374 11.558  1.00 8.84   ? 98  GLY A N   1 
ATOM   814  C  CA  . GLY A 1 98  ? -4.932  -14.383 11.609  1.00 9.81   ? 98  GLY A CA  1 
ATOM   815  C  C   . GLY A 1 98  ? -4.725  -15.115 10.293  1.00 8.71   ? 98  GLY A C   1 
ATOM   816  O  O   . GLY A 1 98  ? -5.459  -14.974 9.330   1.00 10.67  ? 98  GLY A O   1 
ATOM   817  N  N   . SER A 1 99  ? -3.738  -16.015 10.298  1.00 9.81   ? 99  SER A N   1 
ATOM   818  C  CA  . SER A 1 99  ? -3.504  -16.947 9.189   1.00 11.73  ? 99  SER A CA  1 
ATOM   819  C  C   . SER A 1 99  ? -4.415  -18.185 9.292   1.00 12.17  ? 99  SER A C   1 
ATOM   820  O  O   . SER A 1 99  ? -4.596  -18.849 8.256   1.00 15.40  ? 99  SER A O   1 
ATOM   821  C  CB  . SER A 1 99  ? -2.048  -17.395 9.148   1.00 12.53  ? 99  SER A CB  1 
ATOM   822  O  OG  . SER A 1 99  ? -1.614  -17.823 10.425  1.00 13.54  ? 99  SER A OG  1 
ATOM   823  N  N   . LEU A 1 100 ? -4.919  -18.465 10.510  1.00 11.40  ? 100 LEU A N   1 
ATOM   824  C  CA  . LEU A 1 100 ? -5.848  -19.571 10.762  1.00 13.10  ? 100 LEU A CA  1 
ATOM   825  C  C   . LEU A 1 100 ? -6.886  -19.057 11.754  1.00 12.63  ? 100 LEU A C   1 
ATOM   826  O  O   . LEU A 1 100 ? -6.720  -18.040 12.417  1.00 11.62  ? 100 LEU A O   1 
ATOM   827  C  CB  . LEU A 1 100 ? -5.103  -20.795 11.316  1.00 17.07  ? 100 LEU A CB  1 
ATOM   828  C  CG  . LEU A 1 100 ? -4.334  -21.593 10.256  1.00 22.90  ? 100 LEU A CG  1 
ATOM   829  C  CD1 . LEU A 1 100 ? -3.695  -22.823 10.836  1.00 26.21  ? 100 LEU A CD1 1 
ATOM   830  C  CD2 . LEU A 1 100 ? -5.199  -21.955 9.028   1.00 25.87  ? 100 LEU A CD2 1 
ATOM   831  N  N   . ASP A 1 101 ? -7.986  -19.806 11.883  1.00 11.64  ? 101 ASP A N   1 
ATOM   832  C  CA  . ASP A 1 101 ? -9.112  -19.261 12.644  1.00 12.04  ? 101 ASP A CA  1 
ATOM   833  C  C   . ASP A 1 101 ? -8.808  -19.225 14.151  1.00 11.76  ? 101 ASP A C   1 
ATOM   834  O  O   . ASP A 1 101 ? -9.436  -18.462 14.875  1.00 14.21  ? 101 ASP A O   1 
ATOM   835  C  CB  . ASP A 1 101 ? -10.395 -20.114 12.528  1.00 15.62  ? 101 ASP A CB  1 
ATOM   836  C  CG  . ASP A 1 101 ? -10.956 -20.213 11.110  1.00 16.00  ? 101 ASP A CG  1 
ATOM   837  O  OD1 . ASP A 1 101 ? -10.534 -19.422 10.219  1.00 16.62  ? 101 ASP A OD1 1 
ATOM   838  O  OD2 . ASP A 1 101 ? -11.859 -21.066 10.901  1.00 20.36  ? 101 ASP A OD2 1 
ATOM   839  N  N   . GLY A 1 102 ? -7.805  -19.959 14.602  1.00 12.59  ? 102 GLY A N   1 
ATOM   840  C  CA  . GLY A 1 102 ? -7.501  -19.987 16.056  1.00 13.29  ? 102 GLY A CA  1 
ATOM   841  C  C   . GLY A 1 102 ? -6.646  -18.805 16.560  1.00 10.81  ? 102 GLY A C   1 
ATOM   842  O  O   . GLY A 1 102 ? -6.245  -18.792 17.734  1.00 12.46  ? 102 GLY A O   1 
ATOM   843  N  N   . GLN A 1 103 ? -6.352  -17.791 15.722  1.00 10.89  ? 103 GLN A N   1 
ATOM   844  C  CA  . GLN A 1 103 ? -5.642  -16.588 16.167  1.00 9.99   ? 103 GLN A CA  1 
ATOM   845  C  C   . GLN A 1 103 ? -6.063  -15.440 15.266  1.00 10.28  ? 103 GLN A C   1 
ATOM   846  O  O   . GLN A 1 103 ? -6.611  -15.655 14.176  1.00 10.52  ? 103 GLN A O   1 
ATOM   847  C  CB  . GLN A 1 103 ? -4.119  -16.824 16.205  1.00 11.65  ? 103 GLN A CB  1 
ATOM   848  C  CG  . GLN A 1 103 ? -3.550  -17.101 14.790  1.00 12.98  ? 103 GLN A CG  1 
ATOM   849  C  CD  . GLN A 1 103 ? -2.094  -17.507 14.945  1.00 16.45  ? 103 GLN A CD  1 
ATOM   850  O  OE1 . GLN A 1 103 ? -1.681  -18.156 15.929  1.00 23.10  ? 103 GLN A OE1 1 
ATOM   851  N  NE2 . GLN A 1 103 ? -1.272  -17.100 13.999  1.00 14.57  ? 103 GLN A NE2 1 
ATOM   852  N  N   . GLY A 1 104 ? -5.739  -14.209 15.710  1.00 9.66   ? 104 GLY A N   1 
ATOM   853  C  CA  . GLY A 1 104 ? -6.038  -13.024 14.901  1.00 9.15   ? 104 GLY A CA  1 
ATOM   854  C  C   . GLY A 1 104 ? -6.483  -11.825 15.737  1.00 8.57   ? 104 GLY A C   1 
ATOM   855  O  O   . GLY A 1 104 ? -6.187  -10.694 15.370  1.00 9.45   ? 104 GLY A O   1 
ATOM   856  N  N   . SER A 1 105 ? -7.209  -12.070 16.890  1.00 8.35   ? 105 SER A N   1 
ATOM   857  C  CA  . SER A 1 105 ? -7.602  -10.925 17.708  1.00 7.81   ? 105 SER A CA  1 
ATOM   858  C  C   . SER A 1 105 ? -6.362  -10.374 18.465  1.00 7.62   ? 105 SER A C   1 
ATOM   859  O  O   . SER A 1 105 ? -5.368  -11.095 18.686  1.00 9.24   ? 105 SER A O   1 
ATOM   860  C  CB  . SER A 1 105 ? -8.732  -11.315 18.645  1.00 9.56   ? 105 SER A CB  1 
ATOM   861  O  OG  . SER A 1 105 ? -8.366  -12.264 19.685  1.00 8.86   ? 105 SER A OG  1 
ATOM   862  N  N   . GLU A 1 106 ? -6.566  -9.129  18.901  1.00 7.49   ? 106 GLU A N   1 
ATOM   863  C  CA  . GLU A 1 106 ? -5.523  -8.448  19.672  1.00 8.48   ? 106 GLU A CA  1 
ATOM   864  C  C   . GLU A 1 106 ? -5.851  -8.627  21.166  1.00 8.02   ? 106 GLU A C   1 
ATOM   865  O  O   . GLU A 1 106 ? -5.064  -9.160  21.931  1.00 8.41   ? 106 GLU A O   1 
ATOM   866  C  CB  . GLU A 1 106 ? -5.434  -6.964  19.240  1.00 8.28   ? 106 GLU A CB  1 
ATOM   867  C  CG  . GLU A 1 106 ? -4.946  -6.847  17.780  1.00 9.09   ? 106 GLU A CG  1 
ATOM   868  C  CD  . GLU A 1 106 ? -4.292  -5.519  17.463  1.00 8.47   ? 106 GLU A CD  1 
ATOM   869  O  OE1 . GLU A 1 106 ? -4.978  -4.444  17.739  1.00 8.26   ? 106 GLU A OE1 1 
ATOM   870  O  OE2 . GLU A 1 106 ? -3.130  -5.544  16.962  1.00 9.36   ? 106 GLU A OE2 1 
ATOM   871  N  N   . HIS A 1 107 ? -7.041  -8.137  21.587  1.00 8.49   ? 107 HIS A N   1 
ATOM   872  C  CA  . HIS A 1 107 ? -7.528  -8.542  22.900  1.00 7.37   ? 107 HIS A CA  1 
ATOM   873  C  C   . HIS A 1 107 ? -7.800  -10.044 22.919  1.00 8.68   ? 107 HIS A C   1 
ATOM   874  O  O   . HIS A 1 107 ? -8.164  -10.621 21.899  1.00 7.80   ? 107 HIS A O   1 
ATOM   875  C  CB  . HIS A 1 107 ? -8.798  -7.700  23.242  1.00 7.54   ? 107 HIS A CB  1 
ATOM   876  C  CG  . HIS A 1 107 ? -8.433  -6.257  23.417  1.00 7.92   ? 107 HIS A CG  1 
ATOM   877  N  ND1 . HIS A 1 107 ? -8.500  -5.349  22.355  1.00 7.44   ? 107 HIS A ND1 1 
ATOM   878  C  CD2 . HIS A 1 107 ? -7.981  -5.555  24.499  1.00 8.03   ? 107 HIS A CD2 1 
ATOM   879  C  CE1 . HIS A 1 107 ? -8.052  -4.123  22.783  1.00 7.98   ? 107 HIS A CE1 1 
ATOM   880  N  NE2 . HIS A 1 107 ? -7.707  -4.236  24.119  1.00 7.34   ? 107 HIS A NE2 1 
ATOM   881  N  N   . THR A 1 108 ? -7.656  -10.598 24.136  1.00 8.62   ? 108 THR A N   1 
ATOM   882  C  CA  . THR A 1 108 ? -8.047  -11.994 24.373  1.00 8.40   ? 108 THR A CA  1 
ATOM   883  C  C   . THR A 1 108 ? -8.974  -12.014 25.588  1.00 7.57   ? 108 THR A C   1 
ATOM   884  O  O   . THR A 1 108 ? -9.042  -11.033 26.379  1.00 8.42   ? 108 THR A O   1 
ATOM   885  C  CB  . THR A 1 108 ? -6.812  -12.882 24.561  1.00 8.78   ? 108 THR A CB  1 
ATOM   886  O  OG1 . THR A 1 108 ? -5.982  -12.421 25.633  1.00 9.15   ? 108 THR A OG1 1 
ATOM   887  C  CG2 . THR A 1 108 ? -5.998  -12.980 23.274  1.00 9.58   ? 108 THR A CG2 1 
ATOM   888  N  N   . VAL A 1 109 ? -9.776  -13.101 25.726  1.00 8.64   ? 109 VAL A N   1 
ATOM   889  C  CA  . VAL A 1 109 ? -10.763 -13.249 26.802  1.00 9.43   ? 109 VAL A CA  1 
ATOM   890  C  C   . VAL A 1 109 ? -10.435 -14.530 27.561  1.00 9.73   ? 109 VAL A C   1 
ATOM   891  O  O   . VAL A 1 109 ? -10.572 -15.632 26.997  1.00 10.37  ? 109 VAL A O   1 
ATOM   892  C  CB  . VAL A 1 109 ? -12.208 -13.239 26.247  1.00 10.38  ? 109 VAL A CB  1 
ATOM   893  C  CG1 . VAL A 1 109 ? -13.213 -13.344 27.428  1.00 10.79  ? 109 VAL A CG1 1 
ATOM   894  C  CG2 . VAL A 1 109 ? -12.477 -11.901 25.492  1.00 11.78  ? 109 VAL A CG2 1 
ATOM   895  N  N   . ASP A 1 110 ? -9.920  -14.400 28.797  1.00 10.10  ? 110 ASP A N   1 
ATOM   896  C  CA  . ASP A 1 110 ? -9.437  -15.594 29.500  1.00 11.28  ? 110 ASP A CA  1 
ATOM   897  C  C   . ASP A 1 110 ? -8.472  -16.389 28.608  1.00 11.88  ? 110 ASP A C   1 
ATOM   898  O  O   . ASP A 1 110 ? -8.517  -17.623 28.559  1.00 12.29  ? 110 ASP A O   1 
ATOM   899  C  CB  . ASP A 1 110 ? -10.582 -16.476 30.016  1.00 12.38  ? 110 ASP A CB  1 
ATOM   900  C  CG  . ASP A 1 110 ? -11.431 -15.712 31.021  1.00 13.06  ? 110 ASP A CG  1 
ATOM   901  O  OD1 . ASP A 1 110 ? -10.901 -14.795 31.662  1.00 13.84  ? 110 ASP A OD1 1 
ATOM   902  O  OD2 . ASP A 1 110 ? -12.599 -16.068 31.117  1.00 15.84  ? 110 ASP A OD2 1 
ATOM   903  N  N   . LYS A 1 111 ? -7.580  -15.646 27.917  1.00 10.56  ? 111 LYS A N   1 
ATOM   904  C  CA  . LYS A 1 111 ? -6.545  -16.208 27.038  1.00 12.59  ? 111 LYS A CA  1 
ATOM   905  C  C   . LYS A 1 111 ? -7.103  -16.729 25.699  1.00 11.33  ? 111 LYS A C   1 
ATOM   906  O  O   . LYS A 1 111 ? -6.330  -17.117 24.817  1.00 13.00  ? 111 LYS A O   1 
ATOM   907  C  CB  . LYS A 1 111 ? -5.632  -17.262 27.713  1.00 14.57  ? 111 LYS A CB  1 
ATOM   908  C  CG  . LYS A 1 111 ? -4.886  -16.699 28.939  1.00 16.68  ? 111 LYS A CG  1 
ATOM   909  C  CD  . LYS A 1 111 ? -4.002  -15.459 28.573  1.00 18.21  ? 111 LYS A CD  1 
ATOM   910  C  CE  . LYS A 1 111 ? -3.138  -14.822 29.679  1.00 20.82  ? 111 LYS A CE  1 
ATOM   911  N  NZ  . LYS A 1 111 ? -2.159  -15.754 30.248  1.00 23.66  ? 111 LYS A NZ  1 
ATOM   912  N  N   . LYS A 1 112 ? -8.425  -16.754 25.473  1.00 9.54   ? 112 LYS A N   1 
ATOM   913  C  CA  . LYS A 1 112 ? -8.986  -17.120 24.183  1.00 10.52  ? 112 LYS A CA  1 
ATOM   914  C  C   . LYS A 1 112 ? -8.680  -16.054 23.124  1.00 10.39  ? 112 LYS A C   1 
ATOM   915  O  O   . LYS A 1 112 ? -8.962  -14.866 23.332  1.00 9.53   ? 112 LYS A O   1 
ATOM   916  C  CB  . LYS A 1 112 ? -10.525 -17.275 24.301  1.00 11.71  ? 112 LYS A CB  1 
ATOM   917  C  CG  . LYS A 1 112 ? -11.175 -17.658 22.958  1.00 13.61  ? 112 LYS A CG  1 
ATOM   918  C  CD  . LYS A 1 112 ? -12.690 -17.547 23.016  1.00 15.65  ? 112 LYS A CD  1 
ATOM   919  C  CE  . LYS A 1 112 ? -13.314 -17.803 21.656  1.00 15.82  ? 112 LYS A CE  1 
ATOM   920  N  NZ  . LYS A 1 112 ? -13.075 -19.200 21.208  1.00 15.56  ? 112 LYS A NZ  1 
ATOM   921  N  N   A LYS A 1 113 ? -8.164  -16.560 22.005  0.50 10.27  ? 113 LYS A N   1 
ATOM   922  N  N   B LYS A 1 113 ? -8.149  -16.513 21.986  0.50 10.09  ? 113 LYS A N   1 
ATOM   923  C  CA  A LYS A 1 113 ? -7.984  -15.788 20.778  0.50 10.90  ? 113 LYS A CA  1 
ATOM   924  C  CA  B LYS A 1 113 ? -7.919  -15.685 20.798  0.50 10.46  ? 113 LYS A CA  1 
ATOM   925  C  C   A LYS A 1 113 ? -9.180  -15.997 19.857  0.50 11.58  ? 113 LYS A C   1 
ATOM   926  C  C   B LYS A 1 113 ? -9.002  -15.948 19.746  0.50 9.34   ? 113 LYS A C   1 
ATOM   927  O  O   A LYS A 1 113 ? -9.645  -17.142 19.682  0.50 11.50  ? 113 LYS A O   1 
ATOM   928  O  O   B LYS A 1 113 ? -9.278  -17.117 19.408  0.50 11.66  ? 113 LYS A O   1 
ATOM   929  C  CB  A LYS A 1 113 ? -6.727  -16.272 20.021  0.50 11.04  ? 113 LYS A CB  1 
ATOM   930  C  CB  B LYS A 1 113 ? -6.563  -16.035 20.140  0.50 9.46   ? 113 LYS A CB  1 
ATOM   931  C  CG  A LYS A 1 113 ? -5.433  -16.074 20.798  0.50 11.54  ? 113 LYS A CG  1 
ATOM   932  C  CG  B LYS A 1 113 ? -5.327  -15.622 20.936  0.50 9.35   ? 113 LYS A CG  1 
ATOM   933  C  CD  A LYS A 1 113 ? -4.235  -16.643 20.078  0.50 11.03  ? 113 LYS A CD  1 
ATOM   934  C  CD  B LYS A 1 113 ? -4.062  -16.211 20.334  0.50 10.57  ? 113 LYS A CD  1 
ATOM   935  C  CE  A LYS A 1 113 ? -2.981  -16.028 20.672  0.50 12.90  ? 113 LYS A CE  1 
ATOM   936  C  CE  B LYS A 1 113 ? -2.804  -15.649 20.984  0.50 13.03  ? 113 LYS A CE  1 
ATOM   937  N  NZ  A LYS A 1 113 ? -2.543  -16.704 21.921  0.50 11.88  ? 113 LYS A NZ  1 
ATOM   938  N  NZ  B LYS A 1 113 ? -1.652  -16.556 20.737  0.50 17.75  ? 113 LYS A NZ  1 
ATOM   939  N  N   . TYR A 1 114 ? -9.727  -14.874 19.354  1.00 9.36   ? 114 TYR A N   1 
ATOM   940  C  CA  . TYR A 1 114 ? -10.701 -14.937 18.299  1.00 8.54   ? 114 TYR A CA  1 
ATOM   941  C  C   . TYR A 1 114 ? -10.012 -14.941 16.930  1.00 8.98   ? 114 TYR A C   1 
ATOM   942  O  O   . TYR A 1 114 ? -8.831  -14.550 16.804  1.00 9.72   ? 114 TYR A O   1 
ATOM   943  C  CB  . TYR A 1 114 ? -11.749 -13.803 18.439  1.00 8.86   ? 114 TYR A CB  1 
ATOM   944  C  CG  . TYR A 1 114 ? -12.738 -13.992 19.561  1.00 9.18   ? 114 TYR A CG  1 
ATOM   945  C  CD1 . TYR A 1 114 ? -12.471 -13.523 20.837  1.00 11.30  ? 114 TYR A CD1 1 
ATOM   946  C  CD2 . TYR A 1 114 ? -13.943 -14.642 19.351  1.00 10.32  ? 114 TYR A CD2 1 
ATOM   947  C  CE1 . TYR A 1 114 ? -13.374 -13.692 21.873  1.00 12.83  ? 114 TYR A CE1 1 
ATOM   948  C  CE2 . TYR A 1 114 ? -14.857 -14.820 20.376  1.00 13.90  ? 114 TYR A CE2 1 
ATOM   949  C  CZ  . TYR A 1 114 ? -14.572 -14.344 21.642  1.00 13.73  ? 114 TYR A CZ  1 
ATOM   950  O  OH  . TYR A 1 114 ? -15.467 -14.515 22.658  1.00 18.69  ? 114 TYR A OH  1 
ATOM   951  N  N   . ALA A 1 115 ? -10.798 -15.218 15.885  1.00 9.32   ? 115 ALA A N   1 
ATOM   952  C  CA  . ALA A 1 115 ? -10.273 -15.213 14.508  1.00 9.35   ? 115 ALA A CA  1 
ATOM   953  C  C   . ALA A 1 115 ? -9.888  -13.807 14.043  1.00 9.58   ? 115 ALA A C   1 
ATOM   954  O  O   . ALA A 1 115 ? -9.065  -13.673 13.123  1.00 9.82   ? 115 ALA A O   1 
ATOM   955  C  CB  . ALA A 1 115 ? -11.284 -15.906 13.581  1.00 10.49  ? 115 ALA A CB  1 
ATOM   956  N  N   . ALA A 1 116 ? -10.588 -12.752 14.534  1.00 8.84   ? 116 ALA A N   1 
ATOM   957  C  CA  . ALA A 1 116 ? -10.263 -11.390 14.074  1.00 8.54   ? 116 ALA A CA  1 
ATOM   958  C  C   . ALA A 1 116 ? -10.883 -10.436 15.094  1.00 8.34   ? 116 ALA A C   1 
ATOM   959  O  O   . ALA A 1 116 ? -11.612 -10.865 16.013  1.00 8.67   ? 116 ALA A O   1 
ATOM   960  C  CB  . ALA A 1 116 ? -10.829 -11.156 12.639  1.00 8.82   ? 116 ALA A CB  1 
ATOM   961  N  N   . GLU A 1 117 ? -10.517 -9.163  14.940  1.00 8.09   ? 117 GLU A N   1 
ATOM   962  C  CA  . GLU A 1 117 ? -11.061 -8.105  15.804  1.00 8.47   ? 117 GLU A CA  1 
ATOM   963  C  C   . GLU A 1 117 ? -11.213 -6.851  14.958  1.00 8.00   ? 117 GLU A C   1 
ATOM   964  O  O   . GLU A 1 117 ? -10.302 -6.425  14.204  1.00 9.03   ? 117 GLU A O   1 
ATOM   965  C  CB  . GLU A 1 117 ? -10.056 -7.845  16.969  1.00 7.85   ? 117 GLU A CB  1 
ATOM   966  C  CG  . GLU A 1 117 ? -10.601 -6.875  18.040  1.00 7.21   ? 117 GLU A CG  1 
ATOM   967  C  CD  . GLU A 1 117 ? -9.677  -6.830  19.282  1.00 6.98   ? 117 GLU A CD  1 
ATOM   968  O  OE1 . GLU A 1 117 ? -8.989  -7.866  19.541  1.00 8.45   ? 117 GLU A OE1 1 
ATOM   969  O  OE2 . GLU A 1 117 ? -9.616  -5.723  19.931  1.00 8.59   ? 117 GLU A OE2 1 
ATOM   970  N  N   . LEU A 1 118 ? -12.415 -6.240  15.055  1.00 8.26   ? 118 LEU A N   1 
ATOM   971  C  CA  . LEU A 1 118 ? -12.763 -4.980  14.381  1.00 8.57   ? 118 LEU A CA  1 
ATOM   972  C  C   . LEU A 1 118 ? -12.563 -3.818  15.368  1.00 6.95   ? 118 LEU A C   1 
ATOM   973  O  O   . LEU A 1 118 ? -12.961 -3.881  16.537  1.00 7.73   ? 118 LEU A O   1 
ATOM   974  C  CB  . LEU A 1 118 ? -14.270 -5.101  13.985  1.00 8.37   ? 118 LEU A CB  1 
ATOM   975  C  CG  . LEU A 1 118 ? -15.022 -3.792  13.642  1.00 9.36   ? 118 LEU A CG  1 
ATOM   976  C  CD1 . LEU A 1 118 ? -14.416 -3.130  12.364  1.00 9.42   ? 118 LEU A CD1 1 
ATOM   977  C  CD2 . LEU A 1 118 ? -16.506 -4.150  13.374  1.00 10.82  ? 118 LEU A CD2 1 
ATOM   978  N  N   . HIS A 1 119 ? -11.917 -2.759  14.862  1.00 7.54   ? 119 HIS A N   1 
ATOM   979  C  CA  . HIS A 1 119 ? -11.673 -1.530  15.620  1.00 8.39   ? 119 HIS A CA  1 
ATOM   980  C  C   . HIS A 1 119 ? -12.332 -0.321  14.949  1.00 7.30   ? 119 HIS A C   1 
ATOM   981  O  O   . HIS A 1 119 ? -11.956 0.044   13.819  1.00 8.98   ? 119 HIS A O   1 
ATOM   982  C  CB  . HIS A 1 119 ? -10.157 -1.242  15.765  1.00 7.76   ? 119 HIS A CB  1 
ATOM   983  C  CG  . HIS A 1 119 ? -9.514  -2.264  16.635  1.00 7.93   ? 119 HIS A CG  1 
ATOM   984  N  ND1 . HIS A 1 119 ? -8.112  -2.497  16.602  1.00 7.66   ? 119 HIS A ND1 1 
ATOM   985  C  CD2 . HIS A 1 119 ? -10.078 -3.074  17.628  1.00 7.12   ? 119 HIS A CD2 1 
ATOM   986  C  CE1 . HIS A 1 119 ? -7.812  -3.424  17.490  1.00 7.70   ? 119 HIS A CE1 1 
ATOM   987  N  NE2 . HIS A 1 119 ? -8.978  -3.781  18.170  1.00 7.56   ? 119 HIS A NE2 1 
ATOM   988  N  N   . LEU A 1 120 ? -13.360 0.251   15.603  1.00 7.63   ? 120 LEU A N   1 
ATOM   989  C  CA  . LEU A 1 120 ? -14.028 1.487   15.152  1.00 8.96   ? 120 LEU A CA  1 
ATOM   990  C  C   . LEU A 1 120 ? -13.397 2.645   15.940  1.00 7.52   ? 120 LEU A C   1 
ATOM   991  O  O   . LEU A 1 120 ? -13.532 2.708   17.165  1.00 7.73   ? 120 LEU A O   1 
ATOM   992  C  CB  . LEU A 1 120 ? -15.558 1.393   15.353  1.00 10.04  ? 120 LEU A CB  1 
ATOM   993  C  CG  . LEU A 1 120 ? -16.209 0.311   14.476  1.00 10.89  ? 120 LEU A CG  1 
ATOM   994  C  CD1 . LEU A 1 120 ? -17.068 -0.630  15.330  1.00 11.11  ? 120 LEU A CD1 1 
ATOM   995  C  CD2 . LEU A 1 120 ? -17.055 0.968   13.416  1.00 12.36  ? 120 LEU A CD2 1 
ATOM   996  N  N   . VAL A 1 121 ? -12.637 3.501   15.241  1.00 8.30   ? 121 VAL A N   1 
ATOM   997  C  CA  . VAL A 1 121 ? -11.794 4.533   15.854  1.00 8.32   ? 121 VAL A CA  1 
ATOM   998  C  C   . VAL A 1 121 ? -12.527 5.872   15.867  1.00 8.52   ? 121 VAL A C   1 
ATOM   999  O  O   . VAL A 1 121 ? -12.974 6.334   14.802  1.00 9.46   ? 121 VAL A O   1 
ATOM   1000 C  CB  . VAL A 1 121 ? -10.452 4.626   15.065  1.00 9.08   ? 121 VAL A CB  1 
ATOM   1001 C  CG1 . VAL A 1 121 ? -9.502  5.705   15.654  1.00 9.90   ? 121 VAL A CG1 1 
ATOM   1002 C  CG2 . VAL A 1 121 ? -9.717  3.271   14.971  1.00 9.51   ? 121 VAL A CG2 1 
ATOM   1003 N  N   . HIS A 1 122 ? -12.529 6.492   17.043  1.00 8.01   ? 122 HIS A N   1 
ATOM   1004 C  CA  . HIS A 1 122 ? -13.259 7.768   17.220  1.00 8.60   ? 122 HIS A CA  1 
ATOM   1005 C  C   . HIS A 1 122 ? -12.342 8.766   17.925  1.00 9.77   ? 122 HIS A C   1 
ATOM   1006 O  O   . HIS A 1 122 ? -11.606 8.381   18.819  1.00 9.46   ? 122 HIS A O   1 
ATOM   1007 C  CB  . HIS A 1 122 ? -14.568 7.597   18.076  1.00 9.14   ? 122 HIS A CB  1 
ATOM   1008 C  CG  . HIS A 1 122 ? -15.478 6.470   17.689  1.00 8.74   ? 122 HIS A CG  1 
ATOM   1009 N  ND1 . HIS A 1 122 ? -15.112 5.128   17.950  1.00 8.12   ? 122 HIS A ND1 1 
ATOM   1010 C  CD2 . HIS A 1 122 ? -16.649 6.441   17.005  1.00 9.25   ? 122 HIS A CD2 1 
ATOM   1011 C  CE1 . HIS A 1 122 ? -16.110 4.326   17.514  1.00 8.94   ? 122 HIS A CE1 1 
ATOM   1012 N  NE2 . HIS A 1 122 ? -17.129 5.131   16.959  1.00 9.71   ? 122 HIS A NE2 1 
ATOM   1013 N  N   . TRP A 1 123 ? -12.486 10.077  17.632  1.00 9.06   ? 123 TRP A N   1 
ATOM   1014 C  CA  . TRP A 1 123 ? -11.676 11.080  18.311  1.00 8.79   ? 123 TRP A CA  1 
ATOM   1015 C  C   . TRP A 1 123 ? -12.545 12.123  19.048  1.00 8.87   ? 123 TRP A C   1 
ATOM   1016 O  O   . TRP A 1 123 ? -13.689 12.474  18.623  1.00 10.06  ? 123 TRP A O   1 
ATOM   1017 C  CB  . TRP A 1 123 ? -10.719 11.827  17.351  1.00 10.91  ? 123 TRP A CB  1 
ATOM   1018 C  CG  . TRP A 1 123 ? -11.352 12.479  16.142  1.00 11.23  ? 123 TRP A CG  1 
ATOM   1019 C  CD1 . TRP A 1 123 ? -11.631 11.880  14.928  1.00 13.26  ? 123 TRP A CD1 1 
ATOM   1020 C  CD2 . TRP A 1 123 ? -11.804 13.846  16.030  1.00 12.26  ? 123 TRP A CD2 1 
ATOM   1021 N  NE1 . TRP A 1 123 ? -12.191 12.785  14.060  1.00 12.60  ? 123 TRP A NE1 1 
ATOM   1022 C  CE2 . TRP A 1 123 ? -12.284 14.006  14.699  1.00 13.14  ? 123 TRP A CE2 1 
ATOM   1023 C  CE3 . TRP A 1 123 ? -11.720 14.964  16.874  1.00 13.79  ? 123 TRP A CE3 1 
ATOM   1024 C  CZ2 . TRP A 1 123 ? -12.766 15.220  14.224  1.00 15.41  ? 123 TRP A CZ2 1 
ATOM   1025 C  CZ3 . TRP A 1 123 ? -12.190 16.175  16.399  1.00 16.07  ? 123 TRP A CZ3 1 
ATOM   1026 C  CH2 . TRP A 1 123 ? -12.693 16.286  15.086  1.00 16.94  ? 123 TRP A CH2 1 
ATOM   1027 N  N   . ASN A 1 124 ? -11.994 12.562  20.201  1.00 9.63   ? 124 ASN A N   1 
ATOM   1028 C  CA  . ASN A 1 124 ? -12.754 13.470  21.069  1.00 9.51   ? 124 ASN A CA  1 
ATOM   1029 C  C   . ASN A 1 124 ? -12.831 14.876  20.469  1.00 10.93  ? 124 ASN A C   1 
ATOM   1030 O  O   . ASN A 1 124 ? -11.818 15.586  20.270  1.00 10.97  ? 124 ASN A O   1 
ATOM   1031 C  CB  . ASN A 1 124 ? -11.977 13.495  22.405  1.00 9.85   ? 124 ASN A CB  1 
ATOM   1032 C  CG  . ASN A 1 124 ? -12.742 14.160  23.515  1.00 11.54  ? 124 ASN A CG  1 
ATOM   1033 O  OD1 . ASN A 1 124 ? -13.594 15.060  23.277  1.00 11.54  ? 124 ASN A OD1 1 
ATOM   1034 N  ND2 . ASN A 1 124 ? -12.471 13.701  24.748  1.00 12.00  ? 124 ASN A ND2 1 
ATOM   1035 N  N   . THR A 1 125 ? -14.091 15.312  20.229  1.00 12.08  ? 125 THR A N   1 
ATOM   1036 C  CA  . THR A 1 125 ? -14.272 16.595  19.533  1.00 13.90  ? 125 THR A CA  1 
ATOM   1037 C  C   . THR A 1 125 ? -13.829 17.813  20.394  1.00 13.18  ? 125 THR A C   1 
ATOM   1038 O  O   . THR A 1 125 ? -13.615 18.923  19.770  1.00 14.49  ? 125 THR A O   1 
ATOM   1039 C  CB  . THR A 1 125 ? -15.718 16.722  19.016  1.00 18.67  ? 125 THR A CB  1 
ATOM   1040 O  OG1 . THR A 1 125 ? -16.560 16.783  20.180  1.00 19.98  ? 125 THR A OG1 1 
ATOM   1041 C  CG2 . THR A 1 125 ? -16.136 15.585  18.106  1.00 20.23  ? 125 THR A CG2 1 
ATOM   1042 N  N   . LYS A 1 126 ? -13.585 17.643  21.704  1.00 12.03  ? 127 LYS A N   1 
ATOM   1043 C  CA  . LYS A 1 126 ? -13.064 18.822  22.442  1.00 14.08  ? 127 LYS A CA  1 
ATOM   1044 C  C   . LYS A 1 126 ? -11.653 19.226  21.981  1.00 13.01  ? 127 LYS A C   1 
ATOM   1045 O  O   . LYS A 1 126 ? -11.201 20.315  22.374  1.00 15.04  ? 127 LYS A O   1 
ATOM   1046 C  CB  . LYS A 1 126 ? -13.071 18.543  23.950  1.00 13.25  ? 127 LYS A CB  1 
ATOM   1047 C  CG  . LYS A 1 126 ? -12.000 17.620  24.488  1.00 15.39  ? 127 LYS A CG  1 
ATOM   1048 C  CD  . LYS A 1 126 ? -12.154 17.230  25.994  1.00 19.17  ? 127 LYS A CD  1 
ATOM   1049 C  CE  . LYS A 1 126 ? -11.682 18.368  26.888  1.00 24.91  ? 127 LYS A CE  1 
ATOM   1050 N  NZ  . LYS A 1 126 ? -11.895 18.027  28.335  1.00 35.66  ? 127 LYS A NZ  1 
ATOM   1051 N  N   . TYR A 1 127 ? -10.910 18.346  21.244  1.00 11.62  ? 128 TYR A N   1 
ATOM   1052 C  CA  . TYR A 1 127 ? -9.565  18.699  20.800  1.00 10.82  ? 128 TYR A CA  1 
ATOM   1053 C  C   . TYR A 1 127 ? -9.534  19.109  19.321  1.00 12.87  ? 128 TYR A C   1 
ATOM   1054 O  O   . TYR A 1 127 ? -8.416  19.368  18.787  1.00 12.21  ? 128 TYR A O   1 
ATOM   1055 C  CB  . TYR A 1 127 ? -8.619  17.489  21.032  1.00 11.96  ? 128 TYR A CB  1 
ATOM   1056 C  CG  . TYR A 1 127 ? -8.534  17.135  22.501  1.00 11.12  ? 128 TYR A CG  1 
ATOM   1057 C  CD1 . TYR A 1 127 ? -8.176  18.112  23.456  1.00 11.61  ? 128 TYR A CD1 1 
ATOM   1058 C  CD2 . TYR A 1 127 ? -8.884  15.862  22.950  1.00 11.19  ? 128 TYR A CD2 1 
ATOM   1059 C  CE1 . TYR A 1 127 ? -8.102  17.779  24.811  1.00 12.56  ? 128 TYR A CE1 1 
ATOM   1060 C  CE2 . TYR A 1 127 ? -8.849  15.533  24.312  1.00 12.39  ? 128 TYR A CE2 1 
ATOM   1061 C  CZ  . TYR A 1 127 ? -8.434  16.503  25.223  1.00 13.13  ? 128 TYR A CZ  1 
ATOM   1062 O  OH  . TYR A 1 127 ? -8.453  16.252  26.566  1.00 14.62  ? 128 TYR A OH  1 
ATOM   1063 N  N   . GLY A 1 128 ? -10.721 19.189  18.649  1.00 12.64  ? 129 GLY A N   1 
ATOM   1064 C  CA  . GLY A 1 128 ? -10.749 19.899  17.362  1.00 12.53  ? 129 GLY A CA  1 
ATOM   1065 C  C   . GLY A 1 128 ? -10.375 19.047  16.150  1.00 11.75  ? 129 GLY A C   1 
ATOM   1066 O  O   . GLY A 1 128 ? -11.038 19.179  15.084  1.00 13.99  ? 129 GLY A O   1 
ATOM   1067 N  N   . ASP A 1 129 ? -9.297  18.234  16.233  1.00 13.13  ? 130 ASP A N   1 
ATOM   1068 C  CA  . ASP A 1 129 ? -8.902  17.380  15.112  1.00 14.78  ? 130 ASP A CA  1 
ATOM   1069 C  C   . ASP A 1 129 ? -8.283  16.084  15.657  1.00 14.19  ? 130 ASP A C   1 
ATOM   1070 O  O   . ASP A 1 129 ? -7.799  16.064  16.819  1.00 14.03  ? 130 ASP A O   1 
ATOM   1071 C  CB  . ASP A 1 129 ? -8.055  18.116  14.031  1.00 14.22  ? 130 ASP A CB  1 
ATOM   1072 C  CG  . ASP A 1 129 ? -6.617  18.514  14.383  1.00 19.82  ? 130 ASP A CG  1 
ATOM   1073 O  OD1 . ASP A 1 129 ? -5.760  17.660  14.735  1.00 17.98  ? 130 ASP A OD1 1 
ATOM   1074 O  OD2 . ASP A 1 129 ? -6.243  19.676  14.252  1.00 19.98  ? 130 ASP A OD2 1 
ATOM   1075 N  N   . PHE A 1 130 ? -8.158  15.083  14.761  1.00 13.23  ? 131 PHE A N   1 
ATOM   1076 C  CA  . PHE A 1 130 ? -7.593  13.796  15.162  1.00 12.21  ? 131 PHE A CA  1 
ATOM   1077 C  C   . PHE A 1 130 ? -6.125  13.927  15.624  1.00 11.10  ? 131 PHE A C   1 
ATOM   1078 O  O   . PHE A 1 130 ? -5.715  13.294  16.607  1.00 11.40  ? 131 PHE A O   1 
ATOM   1079 C  CB  . PHE A 1 130 ? -7.766  12.830  13.995  1.00 11.85  ? 131 PHE A CB  1 
ATOM   1080 C  CG  . PHE A 1 130 ? -7.194  11.467  14.257  1.00 10.60  ? 131 PHE A CG  1 
ATOM   1081 C  CD1 . PHE A 1 130 ? -5.842  11.191  14.033  1.00 14.74  ? 131 PHE A CD1 1 
ATOM   1082 C  CD2 . PHE A 1 130 ? -7.956  10.438  14.807  1.00 11.57  ? 131 PHE A CD2 1 
ATOM   1083 C  CE1 . PHE A 1 130 ? -5.310  9.928   14.253  1.00 17.06  ? 131 PHE A CE1 1 
ATOM   1084 C  CE2 . PHE A 1 130 ? -7.419  9.200   15.087  1.00 13.01  ? 131 PHE A CE2 1 
ATOM   1085 C  CZ  . PHE A 1 130 ? -6.123  8.913   14.751  1.00 15.18  ? 131 PHE A CZ  1 
ATOM   1086 N  N   . GLY A 1 131 ? -5.306  14.708  14.865  1.00 12.47  ? 132 GLY A N   1 
ATOM   1087 C  CA  . GLY A 1 131 ? -3.896  14.836  15.200  1.00 14.09  ? 132 GLY A CA  1 
ATOM   1088 C  C   . GLY A 1 131 ? -3.643  15.483  16.558  1.00 12.55  ? 132 GLY A C   1 
ATOM   1089 O  O   . GLY A 1 131 ? -2.659  15.150  17.264  1.00 13.95  ? 132 GLY A O   1 
ATOM   1090 N  N   . LYS A 1 132 ? -4.514  16.423  16.962  1.00 12.29  ? 133 LYS A N   1 
ATOM   1091 C  CA  . LYS A 1 132 ? -4.389  17.001  18.317  1.00 11.69  ? 133 LYS A CA  1 
ATOM   1092 C  C   . LYS A 1 132 ? -4.925  15.972  19.338  1.00 10.32  ? 133 LYS A C   1 
ATOM   1093 O  O   . LYS A 1 132 ? -4.362  15.866  20.470  1.00 12.38  ? 133 LYS A O   1 
ATOM   1094 C  CB  . LYS A 1 132 ? -5.218  18.295  18.411  1.00 11.33  ? 133 LYS A CB  1 
ATOM   1095 C  CG  . LYS A 1 132 ? -4.537  19.493  17.720  1.00 14.06  ? 133 LYS A CG  1 
ATOM   1096 C  CD  . LYS A 1 132 ? -3.278  19.998  18.486  1.00 20.47  ? 133 LYS A CD  1 
ATOM   1097 C  CE  . LYS A 1 132 ? -2.666  21.213  17.778  1.00 26.18  ? 133 LYS A CE  1 
ATOM   1098 N  NZ  . LYS A 1 132 ? -1.786  21.990  18.678  1.00 40.71  ? 133 LYS A NZ  1 
ATOM   1099 N  N   . ALA A 1 133 ? -5.998  15.220  18.999  1.00 10.06  ? 134 ALA A N   1 
ATOM   1100 C  CA  . ALA A 1 133 ? -6.593  14.275  19.944  1.00 10.39  ? 134 ALA A CA  1 
ATOM   1101 C  C   . ALA A 1 133 ? -5.588  13.184  20.356  1.00 9.61   ? 134 ALA A C   1 
ATOM   1102 O  O   . ALA A 1 133 ? -5.557  12.769  21.524  1.00 10.04  ? 134 ALA A O   1 
ATOM   1103 C  CB  . ALA A 1 133 ? -7.875  13.674  19.335  1.00 9.69   ? 134 ALA A CB  1 
ATOM   1104 N  N   . VAL A 1 134 ? -4.766  12.676  19.426  1.00 10.57  ? 135 VAL A N   1 
ATOM   1105 C  CA  . VAL A 1 134 ? -3.865  11.548  19.777  1.00 11.83  ? 135 VAL A CA  1 
ATOM   1106 C  C   . VAL A 1 134 ? -2.760  11.974  20.744  1.00 11.05  ? 135 VAL A C   1 
ATOM   1107 O  O   . VAL A 1 134 ? -2.078  11.109  21.295  1.00 12.20  ? 135 VAL A O   1 
ATOM   1108 C  CB  . VAL A 1 134 ? -3.259  10.840  18.549  1.00 12.45  ? 135 VAL A CB  1 
ATOM   1109 C  CG1 . VAL A 1 134 ? -4.353  10.211  17.712  1.00 13.56  ? 135 VAL A CG1 1 
ATOM   1110 C  CG2 . VAL A 1 134 ? -2.313  11.757  17.749  1.00 12.72  ? 135 VAL A CG2 1 
ATOM   1111 N  N   . GLN A 1 135 ? -2.621  13.328  20.959  1.00 11.64  ? 136 GLN A N   1 
ATOM   1112 C  CA  . GLN A 1 135 ? -1.668  13.825  21.942  1.00 12.47  ? 136 GLN A CA  1 
ATOM   1113 C  C   . GLN A 1 135 ? -2.218  13.931  23.363  1.00 11.45  ? 136 GLN A C   1 
ATOM   1114 O  O   . GLN A 1 135 ? -1.545  14.443  24.261  1.00 13.45  ? 136 GLN A O   1 
ATOM   1115 C  CB  . GLN A 1 135 ? -1.145  15.201  21.454  1.00 13.14  ? 136 GLN A CB  1 
ATOM   1116 C  CG  . GLN A 1 135 ? -0.446  15.113  20.088  1.00 15.66  ? 136 GLN A CG  1 
ATOM   1117 C  CD  . GLN A 1 135 ? -0.006  16.490  19.617  1.00 21.34  ? 136 GLN A CD  1 
ATOM   1118 O  OE1 . GLN A 1 135 ? 0.811   17.165  20.270  1.00 26.96  ? 136 GLN A OE1 1 
ATOM   1119 N  NE2 . GLN A 1 135 ? -0.565  16.934  18.483  1.00 21.07  ? 136 GLN A NE2 1 
ATOM   1120 N  N   . GLN A 1 136 ? -3.442  13.398  23.552  1.00 9.93   ? 137 GLN A N   1 
ATOM   1121 C  CA  . GLN A 1 136 ? -4.133  13.582  24.845  1.00 10.42  ? 137 GLN A CA  1 
ATOM   1122 C  C   . GLN A 1 136 ? -4.525  12.230  25.455  1.00 10.74  ? 137 GLN A C   1 
ATOM   1123 O  O   . GLN A 1 136 ? -4.927  11.317  24.696  1.00 10.69  ? 137 GLN A O   1 
ATOM   1124 C  CB  . GLN A 1 136 ? -5.406  14.427  24.652  1.00 11.52  ? 137 GLN A CB  1 
ATOM   1125 C  CG  . GLN A 1 136 ? -5.101  15.813  24.005  1.00 14.26  ? 137 GLN A CG  1 
ATOM   1126 C  CD  . GLN A 1 136 ? -4.346  16.723  24.949  1.00 15.84  ? 137 GLN A CD  1 
ATOM   1127 O  OE1 . GLN A 1 136 ? -4.337  16.479  26.142  1.00 23.90  ? 137 GLN A OE1 1 
ATOM   1128 N  NE2 . GLN A 1 136 ? -3.668  17.704  24.422  1.00 24.76  ? 137 GLN A NE2 1 
ATOM   1129 N  N   . PRO A 1 137 ? -4.511  12.088  26.819  1.00 10.84  ? 138 PRO A N   1 
ATOM   1130 C  CA  . PRO A 1 137 ? -4.812  10.794  27.417  1.00 10.62  ? 138 PRO A CA  1 
ATOM   1131 C  C   . PRO A 1 137 ? -6.238  10.291  27.147  1.00 10.27  ? 138 PRO A C   1 
ATOM   1132 O  O   . PRO A 1 137 ? -6.484  9.067   27.148  1.00 13.05  ? 138 PRO A O   1 
ATOM   1133 C  CB  . PRO A 1 137 ? -4.542  10.949  28.931  1.00 13.25  ? 138 PRO A CB  1 
ATOM   1134 C  CG  . PRO A 1 137 ? -3.846  12.261  29.065  1.00 20.51  ? 138 PRO A CG  1 
ATOM   1135 C  CD  . PRO A 1 137 ? -4.024  13.086  27.809  1.00 14.21  ? 138 PRO A CD  1 
ATOM   1136 N  N   . ASP A 1 138 ? -7.154  11.264  26.900  1.00 9.74   ? 139 ASP A N   1 
ATOM   1137 C  CA  . ASP A 1 138 ? -8.580  10.980  26.613  1.00 10.16  ? 139 ASP A CA  1 
ATOM   1138 C  C   . ASP A 1 138 ? -8.901  11.412  25.187  1.00 9.57   ? 139 ASP A C   1 
ATOM   1139 O  O   . ASP A 1 138 ? -10.025 11.818  24.874  1.00 9.99   ? 139 ASP A O   1 
ATOM   1140 C  CB  . ASP A 1 138 ? -9.528  11.602  27.627  1.00 12.52  ? 139 ASP A CB  1 
ATOM   1141 C  CG  . ASP A 1 138 ? -9.409  13.118  27.693  1.00 12.34  ? 139 ASP A CG  1 
ATOM   1142 O  OD1 . ASP A 1 138 ? -8.461  13.708  27.087  1.00 12.85  ? 139 ASP A OD1 1 
ATOM   1143 O  OD2 . ASP A 1 138 ? -10.281 13.748  28.379  1.00 15.67  ? 139 ASP A OD2 1 
ATOM   1144 N  N   . GLY A 1 139 ? -7.943  11.268  24.260  1.00 9.57   ? 140 GLY A N   1 
ATOM   1145 C  CA  . GLY A 1 139 ? -8.143  11.740  22.886  1.00 10.03  ? 140 GLY A CA  1 
ATOM   1146 C  C   . GLY A 1 139 ? -9.008  10.840  22.023  1.00 9.02   ? 140 GLY A C   1 
ATOM   1147 O  O   . GLY A 1 139 ? -9.688  11.354  21.139  1.00 9.12   ? 140 GLY A O   1 
ATOM   1148 N  N   . LEU A 1 140 ? -8.833  9.504   22.167  1.00 8.99   ? 141 LEU A N   1 
ATOM   1149 C  CA  . LEU A 1 140 ? -9.553  8.600   21.273  1.00 8.24   ? 141 LEU A CA  1 
ATOM   1150 C  C   . LEU A 1 140 ? -10.377 7.617   22.088  1.00 8.26   ? 141 LEU A C   1 
ATOM   1151 O  O   . LEU A 1 140 ? -10.102 7.329   23.270  1.00 8.79   ? 141 LEU A O   1 
ATOM   1152 C  CB  . LEU A 1 140 ? -8.554  7.725   20.487  1.00 8.14   ? 141 LEU A CB  1 
ATOM   1153 C  CG  . LEU A 1 140 ? -7.625  8.439   19.499  1.00 9.71   ? 141 LEU A CG  1 
ATOM   1154 C  CD1 . LEU A 1 140 ? -6.890  7.373   18.683  1.00 9.72   ? 141 LEU A CD1 1 
ATOM   1155 C  CD2 . LEU A 1 140 ? -8.264  9.507   18.633  1.00 11.22  ? 141 LEU A CD2 1 
ATOM   1156 N  N   . ALA A 1 141 ? -11.419 7.063   21.429  1.00 8.31   ? 142 ALA A N   1 
ATOM   1157 C  CA  . ALA A 1 141 ? -12.195 5.923   21.962  1.00 8.06   ? 142 ALA A CA  1 
ATOM   1158 C  C   . ALA A 1 141 ? -12.276 4.922   20.824  1.00 8.82   ? 142 ALA A C   1 
ATOM   1159 O  O   . ALA A 1 141 ? -12.693 5.268   19.708  1.00 8.67   ? 142 ALA A O   1 
ATOM   1160 C  CB  . ALA A 1 141 ? -13.592 6.384   22.406  1.00 9.98   ? 142 ALA A CB  1 
ATOM   1161 N  N   . VAL A 1 142 ? -11.923 3.648   21.132  1.00 8.04   ? 143 VAL A N   1 
ATOM   1162 C  CA  . VAL A 1 142 ? -11.998 2.591   20.140  1.00 8.14   ? 143 VAL A CA  1 
ATOM   1163 C  C   . VAL A 1 142 ? -13.017 1.545   20.621  1.00 7.56   ? 143 VAL A C   1 
ATOM   1164 O  O   . VAL A 1 142 ? -12.918 1.086   21.772  1.00 7.94   ? 143 VAL A O   1 
ATOM   1165 C  CB  . VAL A 1 142 ? -10.652 1.922   19.795  1.00 9.17   ? 143 VAL A CB  1 
ATOM   1166 C  CG1 . VAL A 1 142 ? -10.802 0.869   18.689  1.00 10.22  ? 143 VAL A CG1 1 
ATOM   1167 C  CG2 . VAL A 1 142 ? -9.654  3.005   19.366  1.00 8.88   ? 143 VAL A CG2 1 
ATOM   1168 N  N   . LEU A 1 143 ? -14.017 1.314   19.762  1.00 7.68   ? 144 LEU A N   1 
ATOM   1169 C  CA  . LEU A 1 143 ? -14.960 0.240   19.985  1.00 7.84   ? 144 LEU A CA  1 
ATOM   1170 C  C   . LEU A 1 143 ? -14.362 -1.000  19.303  1.00 8.43   ? 144 LEU A C   1 
ATOM   1171 O  O   . LEU A 1 143 ? -14.252 -1.065  18.077  1.00 9.12   ? 144 LEU A O   1 
ATOM   1172 C  CB  . LEU A 1 143 ? -16.333 0.684   19.408  1.00 9.94   ? 144 LEU A CB  1 
ATOM   1173 C  CG  . LEU A 1 143 ? -17.471 -0.322  19.582  1.00 11.15  ? 144 LEU A CG  1 
ATOM   1174 C  CD1 . LEU A 1 143 ? -17.679 -0.577  21.091  1.00 14.44  ? 144 LEU A CD1 1 
ATOM   1175 C  CD2 . LEU A 1 143 ? -18.743 0.238   18.943  1.00 12.00  ? 144 LEU A CD2 1 
ATOM   1176 N  N   . GLY A 1 144 ? -14.059 -2.031  20.126  1.00 7.66   ? 145 GLY A N   1 
ATOM   1177 C  CA  . GLY A 1 144 ? -13.507 -3.283  19.650  1.00 7.07   ? 145 GLY A CA  1 
ATOM   1178 C  C   . GLY A 1 144 ? -14.560 -4.395  19.647  1.00 7.35   ? 145 GLY A C   1 
ATOM   1179 O  O   . GLY A 1 144 ? -15.280 -4.560  20.628  1.00 8.25   ? 145 GLY A O   1 
ATOM   1180 N  N   . ILE A 1 145 ? -14.570 -5.186  18.548  1.00 8.04   ? 146 ILE A N   1 
ATOM   1181 C  CA  . ILE A 1 145 ? -15.603 -6.224  18.383  1.00 7.43   ? 146 ILE A CA  1 
ATOM   1182 C  C   . ILE A 1 145 ? -14.859 -7.463  17.894  1.00 7.94   ? 146 ILE A C   1 
ATOM   1183 O  O   . ILE A 1 145 ? -14.179 -7.428  16.839  1.00 9.08   ? 146 ILE A O   1 
ATOM   1184 C  CB  . ILE A 1 145 ? -16.693 -5.732  17.375  1.00 8.17   ? 146 ILE A CB  1 
ATOM   1185 C  CG1 . ILE A 1 145 ? -17.364 -4.467  17.907  1.00 10.00  ? 146 ILE A CG1 1 
ATOM   1186 C  CG2 . ILE A 1 145 ? -17.699 -6.867  17.136  1.00 10.04  ? 146 ILE A CG2 1 
ATOM   1187 C  CD1 . ILE A 1 145 ? -18.446 -3.826  16.980  1.00 10.84  ? 146 ILE A CD1 1 
ATOM   1188 N  N   . PHE A 1 146 ? -15.103 -8.595  18.548  1.00 8.23   ? 147 PHE A N   1 
ATOM   1189 C  CA  . PHE A 1 146 ? -14.448 -9.848  18.163  1.00 8.47   ? 147 PHE A CA  1 
ATOM   1190 C  C   . PHE A 1 146 ? -15.226 -10.488 17.016  1.00 9.52   ? 147 PHE A C   1 
ATOM   1191 O  O   . PHE A 1 146 ? -16.442 -10.332 16.937  1.00 9.60   ? 147 PHE A O   1 
ATOM   1192 C  CB  . PHE A 1 146 ? -14.496 -10.796 19.363  1.00 9.45   ? 147 PHE A CB  1 
ATOM   1193 C  CG  . PHE A 1 146 ? -13.604 -10.371 20.509  1.00 8.54   ? 147 PHE A CG  1 
ATOM   1194 C  CD1 . PHE A 1 146 ? -12.252 -10.127 20.328  1.00 8.92   ? 147 PHE A CD1 1 
ATOM   1195 C  CD2 . PHE A 1 146 ? -14.156 -10.096 21.771  1.00 9.43   ? 147 PHE A CD2 1 
ATOM   1196 C  CE1 . PHE A 1 146 ? -11.421 -9.794  21.390  1.00 9.03   ? 147 PHE A CE1 1 
ATOM   1197 C  CE2 . PHE A 1 146 ? -13.339 -9.726  22.829  1.00 9.65   ? 147 PHE A CE2 1 
ATOM   1198 C  CZ  . PHE A 1 146 ? -11.971 -9.564  22.648  1.00 9.05   ? 147 PHE A CZ  1 
ATOM   1199 N  N   . LEU A 1 147 ? -14.494 -11.206 16.144  1.00 8.87   ? 148 LEU A N   1 
ATOM   1200 C  CA  . LEU A 1 147 ? -15.110 -12.010 15.088  1.00 9.54   ? 148 LEU A CA  1 
ATOM   1201 C  C   . LEU A 1 147 ? -14.749 -13.485 15.291  1.00 9.21   ? 148 LEU A C   1 
ATOM   1202 O  O   . LEU A 1 147 ? -13.605 -13.836 15.553  1.00 9.58   ? 148 LEU A O   1 
ATOM   1203 C  CB  . LEU A 1 147 ? -14.530 -11.647 13.699  1.00 10.24  ? 148 LEU A CB  1 
ATOM   1204 C  CG  . LEU A 1 147 ? -15.040 -10.373 13.023  1.00 10.64  ? 148 LEU A CG  1 
ATOM   1205 C  CD1 . LEU A 1 147 ? -14.785 -9.078  13.846  1.00 11.91  ? 148 LEU A CD1 1 
ATOM   1206 C  CD2 . LEU A 1 147 ? -14.401 -10.204 11.598  1.00 11.93  ? 148 LEU A CD2 1 
ATOM   1207 N  N   . LYS A 1 148 ? -15.793 -14.365 15.221  1.00 9.63   ? 149 LYS A N   1 
ATOM   1208 C  CA  . LYS A 1 148 ? -15.612 -15.819 15.186  1.00 10.94  ? 149 LYS A CA  1 
ATOM   1209 C  C   . LYS A 1 148 ? -16.106 -16.296 13.828  1.00 11.15  ? 149 LYS A C   1 
ATOM   1210 O  O   . LYS A 1 148 ? -16.922 -15.643 13.194  1.00 12.46  ? 149 LYS A O   1 
ATOM   1211 C  CB  . LYS A 1 148 ? -16.372 -16.517 16.339  1.00 11.93  ? 149 LYS A CB  1 
ATOM   1212 C  CG  . LYS A 1 148 ? -17.896 -16.382 16.278  1.00 13.20  ? 149 LYS A CG  1 
ATOM   1213 C  CD  . LYS A 1 148 ? -18.524 -17.098 17.468  1.00 19.61  ? 149 LYS A CD  1 
ATOM   1214 C  CE  . LYS A 1 148 ? -20.021 -17.095 17.375  1.00 24.18  ? 149 LYS A CE  1 
ATOM   1215 N  NZ  . LYS A 1 148 ? -20.570 -18.050 18.388  1.00 42.87  ? 149 LYS A NZ  1 
ATOM   1216 N  N   . VAL A 1 149 ? -15.657 -17.505 13.459  1.00 11.71  ? 150 VAL A N   1 
ATOM   1217 C  CA  . VAL A 1 149 ? -16.033 -18.065 12.150  1.00 12.71  ? 150 VAL A CA  1 
ATOM   1218 C  C   . VAL A 1 149 ? -17.222 -19.019 12.318  1.00 13.55  ? 150 VAL A C   1 
ATOM   1219 O  O   . VAL A 1 149 ? -17.167 -20.014 13.080  1.00 17.10  ? 150 VAL A O   1 
ATOM   1220 C  CB  . VAL A 1 149 ? -14.797 -18.772 11.514  1.00 13.93  ? 150 VAL A CB  1 
ATOM   1221 C  CG1 . VAL A 1 149 ? -15.150 -19.472 10.167  1.00 20.75  ? 150 VAL A CG1 1 
ATOM   1222 C  CG2 . VAL A 1 149 ? -13.705 -17.717 11.219  1.00 15.09  ? 150 VAL A CG2 1 
ATOM   1223 N  N   . GLY A 1 150 ? -18.281 -18.733 11.561  1.00 12.70  ? 151 GLY A N   1 
ATOM   1224 C  CA  . GLY A 1 150 ? -19.501 -19.540 11.663  1.00 16.14  ? 151 GLY A CA  1 
ATOM   1225 C  C   . GLY A 1 150 ? -20.408 -19.141 10.511  1.00 14.53  ? 151 GLY A C   1 
ATOM   1226 O  O   . GLY A 1 150 ? -19.990 -19.270 9.341   1.00 16.55  ? 151 GLY A O   1 
ATOM   1227 N  N   A SER A 1 151 ? -21.580 -18.564 10.828  0.50 15.97  ? 152 SER A N   1 
ATOM   1228 N  N   B SER A 1 151 ? -21.593 -18.597 10.834  0.50 15.99  ? 152 SER A N   1 
ATOM   1229 C  CA  A SER A 1 151 ? -22.504 -18.060 9.816   0.50 16.00  ? 152 SER A CA  1 
ATOM   1230 C  CA  B SER A 1 151 ? -22.488 -18.033 9.830   0.50 16.40  ? 152 SER A CA  1 
ATOM   1231 C  C   A SER A 1 151 ? -21.972 -16.739 9.246   0.50 14.05  ? 152 SER A C   1 
ATOM   1232 C  C   B SER A 1 151 ? -21.823 -16.806 9.196   0.50 15.96  ? 152 SER A C   1 
ATOM   1233 O  O   A SER A 1 151 ? -21.324 -15.974 9.964   0.50 13.99  ? 152 SER A O   1 
ATOM   1234 O  O   B SER A 1 151 ? -20.957 -16.183 9.823   0.50 15.34  ? 152 SER A O   1 
ATOM   1235 C  CB  A SER A 1 151 ? -23.863 -17.854 10.409  0.50 21.37  ? 152 SER A CB  1 
ATOM   1236 C  CB  B SER A 1 151 ? -23.799 -17.647 10.457  0.50 19.18  ? 152 SER A CB  1 
ATOM   1237 O  OG  A SER A 1 151 ? -23.842 -16.805 11.364  0.50 23.77  ? 152 SER A OG  1 
ATOM   1238 O  OG  B SER A 1 151 ? -24.469 -18.785 10.989  0.50 19.39  ? 152 SER A OG  1 
ATOM   1239 N  N   . ALA A 1 152 ? -22.189 -16.487 7.937   1.00 15.66  ? 153 ALA A N   1 
ATOM   1240 C  CA  . ALA A 1 152 ? -21.796 -15.212 7.321   1.00 16.87  ? 153 ALA A CA  1 
ATOM   1241 C  C   . ALA A 1 152 ? -22.477 -13.993 8.009   1.00 14.95  ? 153 ALA A C   1 
ATOM   1242 O  O   . ALA A 1 152 ? -23.616 -14.032 8.535   1.00 17.70  ? 153 ALA A O   1 
ATOM   1243 C  CB  . ALA A 1 152 ? -22.144 -15.211 5.829   1.00 15.89  ? 153 ALA A CB  1 
ATOM   1244 N  N   . LYS A 1 153 ? -21.733 -12.867 7.992   1.00 15.55  ? 154 LYS A N   1 
ATOM   1245 C  CA  . LYS A 1 153 ? -22.256 -11.586 8.426   1.00 16.32  ? 154 LYS A CA  1 
ATOM   1246 C  C   . LYS A 1 153 ? -22.692 -10.818 7.177   1.00 15.88  ? 154 LYS A C   1 
ATOM   1247 O  O   . LYS A 1 153 ? -21.859 -10.331 6.393   1.00 14.78  ? 154 LYS A O   1 
ATOM   1248 C  CB  . LYS A 1 153 ? -21.174 -10.806 9.179   1.00 14.42  ? 154 LYS A CB  1 
ATOM   1249 C  CG  . LYS A 1 153 ? -21.724 -9.607  9.923   1.00 16.85  ? 154 LYS A CG  1 
ATOM   1250 C  CD  . LYS A 1 153 ? -22.506 -9.967  11.190  1.00 21.47  ? 154 LYS A CD  1 
ATOM   1251 C  CE  . LYS A 1 153 ? -22.725 -8.741  12.055  1.00 24.15  ? 154 LYS A CE  1 
ATOM   1252 N  NZ  . LYS A 1 153 ? -23.726 -9.111  13.062  1.00 30.96  ? 154 LYS A NZ  1 
ATOM   1253 N  N   . PRO A 1 154 ? -24.024 -10.704 6.905   1.00 17.92  ? 155 PRO A N   1 
ATOM   1254 C  CA  . PRO A 1 154 ? -24.463 -10.057 5.669   1.00 20.23  ? 155 PRO A CA  1 
ATOM   1255 C  C   . PRO A 1 154 ? -23.872 -8.642  5.500   1.00 17.82  ? 155 PRO A C   1 
ATOM   1256 O  O   . PRO A 1 154 ? -23.478 -8.221  4.392   1.00 20.03  ? 155 PRO A O   1 
ATOM   1257 C  CB  . PRO A 1 154 ? -26.014 -10.024 5.807   1.00 22.35  ? 155 PRO A CB  1 
ATOM   1258 C  CG  . PRO A 1 154 ? -26.328 -11.195 6.758   1.00 27.86  ? 155 PRO A CG  1 
ATOM   1259 C  CD  . PRO A 1 154 ? -25.161 -11.200 7.726   1.00 24.08  ? 155 PRO A CD  1 
ATOM   1260 N  N   . GLY A 1 155 ? -23.812 -7.915  6.624   1.00 18.30  ? 156 GLY A N   1 
ATOM   1261 C  CA  . GLY A 1 155 ? -23.344 -6.541  6.603   1.00 20.72  ? 156 GLY A CA  1 
ATOM   1262 C  C   . GLY A 1 155 ? -21.871 -6.318  6.260   1.00 17.52  ? 156 GLY A C   1 
ATOM   1263 O  O   . GLY A 1 155 ? -21.455 -5.186  6.009   1.00 20.86  ? 156 GLY A O   1 
ATOM   1264 N  N   . LEU A 1 156 ? -21.092 -7.413  6.328   1.00 16.47  ? 157 LEU A N   1 
ATOM   1265 C  CA  . LEU A 1 156 ? -19.664 -7.390  5.984   1.00 15.14  ? 157 LEU A CA  1 
ATOM   1266 C  C   . LEU A 1 156 ? -19.422 -7.627  4.484   1.00 17.77  ? 157 LEU A C   1 
ATOM   1267 O  O   . LEU A 1 156 ? -18.336 -7.281  3.999   1.00 15.95  ? 157 LEU A O   1 
ATOM   1268 C  CB  . LEU A 1 156 ? -18.948 -8.456  6.808   1.00 15.38  ? 157 LEU A CB  1 
ATOM   1269 C  CG  . LEU A 1 156 ? -17.415 -8.547  6.691   1.00 14.96  ? 157 LEU A CG  1 
ATOM   1270 C  CD1 . LEU A 1 156 ? -16.665 -7.216  7.010   1.00 16.02  ? 157 LEU A CD1 1 
ATOM   1271 C  CD2 . LEU A 1 156 ? -16.897 -9.668  7.578   1.00 14.22  ? 157 LEU A CD2 1 
ATOM   1272 N  N   . GLN A 1 157 ? -20.417 -8.165  3.737   1.00 17.27  ? 158 GLN A N   1 
ATOM   1273 C  CA  . GLN A 1 157 ? -20.133 -8.652  2.389   1.00 18.04  ? 158 GLN A CA  1 
ATOM   1274 C  C   . GLN A 1 157 ? -19.676 -7.496  1.486   1.00 15.60  ? 158 GLN A C   1 
ATOM   1275 O  O   . GLN A 1 157 ? -18.824 -7.742  0.638   1.00 16.09  ? 158 GLN A O   1 
ATOM   1276 C  CB  . GLN A 1 157 ? -21.291 -9.478  1.806   1.00 20.73  ? 158 GLN A CB  1 
ATOM   1277 C  CG  . GLN A 1 157 ? -20.840 -10.286 0.555   1.00 18.83  ? 158 GLN A CG  1 
ATOM   1278 C  CD  . GLN A 1 157 ? -19.757 -11.326 0.779   1.00 18.20  ? 158 GLN A CD  1 
ATOM   1279 O  OE1 . GLN A 1 157 ? -19.669 -11.952 1.863   1.00 21.55  ? 158 GLN A OE1 1 
ATOM   1280 N  NE2 . GLN A 1 157 ? -18.945 -11.549 -0.267  1.00 20.48  ? 158 GLN A NE2 1 
ATOM   1281 N  N   . LYS A 1 158 ? -20.263 -6.271  1.600   1.00 17.63  ? 159 LYS A N   1 
ATOM   1282 C  CA  . LYS A 1 158 ? -19.824 -5.146  0.735   1.00 18.57  ? 159 LYS A CA  1 
ATOM   1283 C  C   . LYS A 1 158 ? -18.319 -4.881  0.905   1.00 15.27  ? 159 LYS A C   1 
ATOM   1284 O  O   . LYS A 1 158 ? -17.623 -4.575  -0.046  1.00 16.93  ? 159 LYS A O   1 
ATOM   1285 C  CB  . LYS A 1 158 ? -20.695 -3.891  0.876   1.00 21.45  ? 159 LYS A CB  1 
ATOM   1286 C  CG  . LYS A 1 158 ? -20.200 -2.611  0.219   1.00 41.45  ? 159 LYS A CG  1 
ATOM   1287 C  CD  . LYS A 1 158 ? -21.045 -2.030  -0.934  1.00 70.41  ? 159 LYS A CD  1 
ATOM   1288 C  CE  . LYS A 1 158 ? -20.509 -0.741  -1.551  1.00 76.67  ? 159 LYS A CE  1 
ATOM   1289 N  NZ  . LYS A 1 158 ? -21.287 0.463   -1.152  1.00 73.97  ? 159 LYS A NZ  1 
ATOM   1290 N  N   . VAL A 1 159 ? -17.819 -5.042  2.142   1.00 16.13  ? 160 VAL A N   1 
ATOM   1291 C  CA  . VAL A 1 159 ? -16.394 -4.857  2.396   1.00 14.00  ? 160 VAL A CA  1 
ATOM   1292 C  C   . VAL A 1 159 ? -15.596 -5.999  1.739   1.00 14.21  ? 160 VAL A C   1 
ATOM   1293 O  O   . VAL A 1 159 ? -14.642 -5.761  0.951   1.00 14.58  ? 160 VAL A O   1 
ATOM   1294 C  CB  . VAL A 1 159 ? -16.101 -4.823  3.898   1.00 14.51  ? 160 VAL A CB  1 
ATOM   1295 C  CG1 . VAL A 1 159 ? -14.594 -4.883  4.175   1.00 16.09  ? 160 VAL A CG1 1 
ATOM   1296 C  CG2 . VAL A 1 159 ? -16.683 -3.586  4.551   1.00 17.51  ? 160 VAL A CG2 1 
ATOM   1297 N  N   . VAL A 1 160 ? -16.026 -7.235  1.974   1.00 13.72  ? 161 VAL A N   1 
ATOM   1298 C  CA  . VAL A 1 160 ? -15.372 -8.417  1.387   1.00 16.72  ? 161 VAL A CA  1 
ATOM   1299 C  C   . VAL A 1 160 ? -15.226 -8.276  -0.144  1.00 16.62  ? 161 VAL A C   1 
ATOM   1300 O  O   . VAL A 1 160 ? -14.176 -8.538  -0.761  1.00 16.68  ? 161 VAL A O   1 
ATOM   1301 C  CB  . VAL A 1 160 ? -16.091 -9.747  1.874   1.00 18.32  ? 161 VAL A CB  1 
ATOM   1302 C  CG1 . VAL A 1 160 ? -15.726 -11.021 1.098   1.00 23.17  ? 161 VAL A CG1 1 
ATOM   1303 C  CG2 . VAL A 1 160 ? -15.789 -9.951  3.362   1.00 20.27  ? 161 VAL A CG2 1 
ATOM   1304 N  N   . ASP A 1 161 ? -16.276 -7.794  -0.785  1.00 17.88  ? 162 ASP A N   1 
ATOM   1305 C  CA  . ASP A 1 161 ? -16.275 -7.856  -2.240  1.00 19.76  ? 162 ASP A CA  1 
ATOM   1306 C  C   . ASP A 1 161 ? -15.407 -6.776  -2.878  1.00 21.68  ? 162 ASP A C   1 
ATOM   1307 O  O   . ASP A 1 161 ? -15.041 -6.897  -4.061  1.00 25.74  ? 162 ASP A O   1 
ATOM   1308 C  CB  . ASP A 1 161 ? -17.708 -7.817  -2.684  1.00 24.22  ? 162 ASP A CB  1 
ATOM   1309 C  CG  . ASP A 1 161 ? -18.372 -9.194  -2.653  1.00 23.39  ? 162 ASP A CG  1 
ATOM   1310 O  OD1 . ASP A 1 161 ? -17.617 -10.311 -2.727  1.00 26.54  ? 162 ASP A OD1 1 
ATOM   1311 O  OD2 . ASP A 1 161 ? -19.613 -9.189  -2.491  1.00 28.30  ? 162 ASP A OD2 1 
ATOM   1312 N  N   . VAL A 1 162 ? -15.054 -5.716  -2.130  1.00 17.70  ? 163 VAL A N   1 
ATOM   1313 C  CA  . VAL A 1 162 ? -14.190 -4.678  -2.699  1.00 17.05  ? 163 VAL A CA  1 
ATOM   1314 C  C   . VAL A 1 162 ? -12.688 -4.993  -2.523  1.00 15.44  ? 163 VAL A C   1 
ATOM   1315 O  O   . VAL A 1 162 ? -11.831 -4.304  -3.084  1.00 16.65  ? 163 VAL A O   1 
ATOM   1316 C  CB  . VAL A 1 162 ? -14.565 -3.284  -2.153  1.00 20.35  ? 163 VAL A CB  1 
ATOM   1317 C  CG1 . VAL A 1 162 ? -14.174 -3.075  -0.697  1.00 21.38  ? 163 VAL A CG1 1 
ATOM   1318 C  CG2 . VAL A 1 162 ? -14.151 -2.137  -3.050  1.00 23.85  ? 163 VAL A CG2 1 
ATOM   1319 N  N   . LEU A 1 163 ? -12.339 -5.979  -1.659  1.00 17.27  ? 164 LEU A N   1 
ATOM   1320 C  CA  . LEU A 1 163 ? -10.941 -6.256  -1.319  1.00 15.27  ? 164 LEU A CA  1 
ATOM   1321 C  C   . LEU A 1 163 ? -10.080 -6.646  -2.531  1.00 18.70  ? 164 LEU A C   1 
ATOM   1322 O  O   . LEU A 1 163 ? -8.875  -6.303  -2.576  1.00 17.88  ? 164 LEU A O   1 
ATOM   1323 C  CB  . LEU A 1 163 ? -10.813 -7.342  -0.238  1.00 15.71  ? 164 LEU A CB  1 
ATOM   1324 C  CG  . LEU A 1 163 ? -11.471 -6.963  1.095   1.00 15.05  ? 164 LEU A CG  1 
ATOM   1325 C  CD1 . LEU A 1 163 ? -11.258 -8.117  2.119   1.00 16.08  ? 164 LEU A CD1 1 
ATOM   1326 C  CD2 . LEU A 1 163 ? -10.914 -5.603  1.624   1.00 14.68  ? 164 LEU A CD2 1 
ATOM   1327 N  N   . ASP A 1 164 ? -10.682 -7.295  -3.545  1.00 20.74  ? 165 ASP A N   1 
ATOM   1328 C  CA  . ASP A 1 164 ? -9.825  -7.670  -4.686  1.00 23.48  ? 165 ASP A CA  1 
ATOM   1329 C  C   . ASP A 1 164 ? -9.357  -6.401  -5.439  1.00 22.54  ? 165 ASP A C   1 
ATOM   1330 O  O   . ASP A 1 164 ? -8.384  -6.466  -6.216  1.00 27.30  ? 165 ASP A O   1 
ATOM   1331 C  CB  . ASP A 1 164 ? -10.434 -8.786  -5.555  1.00 37.48  ? 165 ASP A CB  1 
ATOM   1332 C  CG  . ASP A 1 164 ? -11.813 -8.434  -6.068  1.00 75.77  ? 165 ASP A CG  1 
ATOM   1333 O  OD1 . ASP A 1 164 ? -12.173 -7.222  -6.025  1.00 71.66  ? 165 ASP A OD1 1 
ATOM   1334 O  OD2 . ASP A 1 164 ? -12.536 -9.383  -6.489  1.00 101.44 ? 165 ASP A OD2 1 
ATOM   1335 N  N   . SER A 1 165 ? -10.033 -5.249  -5.228  1.00 18.70  ? 166 SER A N   1 
ATOM   1336 C  CA  . SER A 1 165 ? -9.640  -4.001  -5.896  1.00 20.07  ? 166 SER A CA  1 
ATOM   1337 C  C   . SER A 1 165 ? -8.558  -3.198  -5.144  1.00 18.43  ? 166 SER A C   1 
ATOM   1338 O  O   . SER A 1 165 ? -8.078  -2.150  -5.622  1.00 17.58  ? 166 SER A O   1 
ATOM   1339 C  CB  . SER A 1 165 ? -10.858 -3.131  -6.248  1.00 21.86  ? 166 SER A CB  1 
ATOM   1340 O  OG  . SER A 1 165 ? -11.334 -2.452  -5.098  1.00 23.70  ? 166 SER A OG  1 
ATOM   1341 N  N   . ILE A 1 166 ? -8.247  -3.625  -3.911  1.00 15.91  ? 167 ILE A N   1 
ATOM   1342 C  CA  . ILE A 1 166 ? -7.253  -2.958  -3.103  1.00 15.84  ? 167 ILE A CA  1 
ATOM   1343 C  C   . ILE A 1 166 ? -6.264  -3.991  -2.557  1.00 14.62  ? 167 ILE A C   1 
ATOM   1344 O  O   . ILE A 1 166 ? -5.890  -3.983  -1.369  1.00 14.16  ? 167 ILE A O   1 
ATOM   1345 C  CB  . ILE A 1 166 ? -7.916  -2.093  -1.977  1.00 15.92  ? 167 ILE A CB  1 
ATOM   1346 C  CG1 . ILE A 1 166 ? -8.802  -2.902  -0.988  1.00 16.65  ? 167 ILE A CG1 1 
ATOM   1347 C  CG2 . ILE A 1 166 ? -8.649  -0.853  -2.540  1.00 15.98  ? 167 ILE A CG2 1 
ATOM   1348 C  CD1 . ILE A 1 166 ? -8.732  -2.320  0.438   1.00 14.74  ? 167 ILE A CD1 1 
ATOM   1349 N  N   . LYS A 1 167 ? -5.848  -4.916  -3.424  1.00 13.82  ? 168 LYS A N   1 
ATOM   1350 C  CA  . LYS A 1 167 ? -5.060  -6.075  -3.003  1.00 14.43  ? 168 LYS A CA  1 
ATOM   1351 C  C   . LYS A 1 167 ? -3.739  -5.675  -2.301  1.00 13.48  ? 168 LYS A C   1 
ATOM   1352 O  O   . LYS A 1 167 ? -3.308  -6.290  -1.307  1.00 13.73  ? 168 LYS A O   1 
ATOM   1353 C  CB  . LYS A 1 167 ? -4.776  -7.027  -4.174  1.00 15.32  ? 168 LYS A CB  1 
ATOM   1354 C  CG  . LYS A 1 167 ? -3.975  -8.258  -3.762  1.00 17.77  ? 168 LYS A CG  1 
ATOM   1355 C  CD  . LYS A 1 167 ? -3.580  -9.109  -5.002  1.00 24.17  ? 168 LYS A CD  1 
ATOM   1356 C  CE  . LYS A 1 167 ? -2.996  -10.443 -4.594  1.00 27.59  ? 168 LYS A CE  1 
ATOM   1357 N  NZ  . LYS A 1 167 ? -2.713  -11.325 -5.770  1.00 38.51  ? 168 LYS A NZ  1 
ATOM   1358 N  N   . THR A 1 168 ? -3.085  -4.591  -2.824  1.00 14.42  ? 169 THR A N   1 
ATOM   1359 C  CA  . THR A 1 168 ? -1.716  -4.318  -2.433  1.00 13.38  ? 169 THR A CA  1 
ATOM   1360 C  C   . THR A 1 168 ? -1.659  -2.914  -1.767  1.00 13.18  ? 169 THR A C   1 
ATOM   1361 O  O   . THR A 1 168 ? -2.492  -2.013  -1.969  1.00 15.25  ? 169 THR A O   1 
ATOM   1362 C  CB  . THR A 1 168 ? -0.749  -4.395  -3.648  1.00 15.31  ? 169 THR A CB  1 
ATOM   1363 O  OG1 . THR A 1 168 ? -1.276  -3.601  -4.727  1.00 18.77  ? 169 THR A OG1 1 
ATOM   1364 C  CG2 . THR A 1 168 ? -0.563  -5.836  -4.104  1.00 16.23  ? 169 THR A CG2 1 
ATOM   1365 N  N   . LYS A 1 169 ? -0.585  -2.719  -1.030  1.00 16.31  ? 170 LYS A N   1 
ATOM   1366 C  CA  . LYS A 1 169 ? -0.301  -1.506  -0.276  1.00 15.50  ? 170 LYS A CA  1 
ATOM   1367 C  C   . LYS A 1 169 ? -0.380  -0.231  -1.126  1.00 14.43  ? 170 LYS A C   1 
ATOM   1368 O  O   . LYS A 1 169 ? 0.231   -0.180  -2.207  1.00 18.98  ? 170 LYS A O   1 
ATOM   1369 C  CB  . LYS A 1 169 ? 1.092   -1.664  0.364   1.00 16.13  ? 170 LYS A CB  1 
ATOM   1370 C  CG  . LYS A 1 169 ? 1.561   -0.417  1.106   1.00 17.45  ? 170 LYS A CG  1 
ATOM   1371 C  CD  . LYS A 1 169 ? 2.917   -0.653  1.794   1.00 16.84  ? 170 LYS A CD  1 
ATOM   1372 C  CE  . LYS A 1 169 ? 4.022   -1.119  0.855   1.00 29.44  ? 170 LYS A CE  1 
ATOM   1373 N  NZ  . LYS A 1 169 ? 5.364   -0.886  1.472   1.00 51.06  ? 170 LYS A NZ  1 
ATOM   1374 N  N   . GLY A 1 170 ? -1.160  0.761   -0.660  1.00 15.39  ? 171 GLY A N   1 
ATOM   1375 C  CA  . GLY A 1 170 ? -1.280  2.048   -1.350  1.00 17.12  ? 171 GLY A CA  1 
ATOM   1376 C  C   . GLY A 1 170 ? -2.458  2.106   -2.336  1.00 17.99  ? 171 GLY A C   1 
ATOM   1377 O  O   . GLY A 1 170 ? -2.740  3.210   -2.862  1.00 20.31  ? 171 GLY A O   1 
ATOM   1378 N  N   . LYS A 1 171 ? -3.149  0.990   -2.566  1.00 15.58  ? 172 LYS A N   1 
ATOM   1379 C  CA  . LYS A 1 171 ? -4.351  1.011   -3.407  1.00 15.57  ? 172 LYS A CA  1 
ATOM   1380 C  C   . LYS A 1 171 ? -5.550  1.485   -2.563  1.00 14.56  ? 172 LYS A C   1 
ATOM   1381 O  O   . LYS A 1 171 ? -5.719  1.078   -1.400  1.00 16.09  ? 172 LYS A O   1 
ATOM   1382 C  CB  . LYS A 1 171 ? -4.588  -0.377  -4.017  1.00 16.85  ? 172 LYS A CB  1 
ATOM   1383 C  CG  . LYS A 1 171 ? -3.610  -0.719  -5.135  1.00 23.80  ? 172 LYS A CG  1 
ATOM   1384 C  CD  . LYS A 1 171 ? -4.058  -1.822  -6.074  1.00 31.13  ? 172 LYS A CD  1 
ATOM   1385 C  CE  . LYS A 1 171 ? -5.114  -1.404  -7.086  1.00 41.22  ? 172 LYS A CE  1 
ATOM   1386 N  NZ  . LYS A 1 171 ? -5.612  -2.560  -7.897  1.00 32.62  ? 172 LYS A NZ  1 
ATOM   1387 N  N   . SER A 1 172 ? -6.476  2.223   -3.160  1.00 16.87  ? 173 SER A N   1 
ATOM   1388 C  CA  . SER A 1 172 ? -7.698  2.742   -2.552  1.00 17.47  ? 173 SER A CA  1 
ATOM   1389 C  C   . SER A 1 172 ? -8.864  2.597   -3.546  1.00 18.03  ? 173 SER A C   1 
ATOM   1390 O  O   . SER A 1 172 ? -8.649  2.508   -4.801  1.00 19.08  ? 173 SER A O   1 
ATOM   1391 C  CB  . SER A 1 172 ? -7.540  4.212   -2.013  1.00 19.34  ? 173 SER A CB  1 
ATOM   1392 O  OG  . SER A 1 172 ? -7.330  5.157   -3.095  1.00 22.01  ? 173 SER A OG  1 
ATOM   1393 N  N   . ALA A 1 173 ? -10.096 2.631   -3.012  1.00 20.61  ? 174 ALA A N   1 
ATOM   1394 C  CA  . ALA A 1 173 ? -11.300 2.563   -3.852  1.00 22.42  ? 174 ALA A CA  1 
ATOM   1395 C  C   . ALA A 1 173 ? -12.400 3.414   -3.228  1.00 21.17  ? 174 ALA A C   1 
ATOM   1396 O  O   . ALA A 1 173 ? -12.524 3.485   -2.009  1.00 16.18  ? 174 ALA A O   1 
ATOM   1397 C  CB  . ALA A 1 173 ? -11.737 1.113   -4.092  1.00 21.46  ? 174 ALA A CB  1 
ATOM   1398 N  N   . ASP A 1 174 ? -13.250 4.027   -4.041  1.00 21.21  ? 175 ASP A N   1 
ATOM   1399 C  CA  . ASP A 1 174 ? -14.441 4.691   -3.543  1.00 22.78  ? 175 ASP A CA  1 
ATOM   1400 C  C   . ASP A 1 174 ? -15.255 3.661   -2.759  1.00 21.62  ? 175 ASP A C   1 
ATOM   1401 O  O   . ASP A 1 174 ? -15.299 2.464   -3.121  1.00 24.13  ? 175 ASP A O   1 
ATOM   1402 C  CB  . ASP A 1 174 ? -15.269 5.277   -4.722  1.00 25.26  ? 175 ASP A CB  1 
ATOM   1403 C  CG  . ASP A 1 174 ? -14.592 6.492   -5.371  1.00 43.53  ? 175 ASP A CG  1 
ATOM   1404 O  OD1 . ASP A 1 174 ? -14.128 7.408   -4.629  1.00 66.18  ? 175 ASP A OD1 1 
ATOM   1405 O  OD2 . ASP A 1 174 ? -14.582 6.573   -6.636  1.00 52.25  ? 175 ASP A OD2 1 
ATOM   1406 N  N   . PHE A 1 175 ? -15.821 4.139   -1.624  1.00 19.27  ? 176 PHE A N   1 
ATOM   1407 C  CA  . PHE A 1 175 ? -16.555 3.223   -0.753  1.00 19.33  ? 176 PHE A CA  1 
ATOM   1408 C  C   . PHE A 1 175 ? -17.606 4.049   -0.026  1.00 18.27  ? 176 PHE A C   1 
ATOM   1409 O  O   . PHE A 1 175 ? -17.473 4.263   1.182   1.00 24.74  ? 176 PHE A O   1 
ATOM   1410 C  CB  . PHE A 1 175 ? -15.606 2.457   0.184   1.00 20.39  ? 176 PHE A CB  1 
ATOM   1411 C  CG  . PHE A 1 175 ? -16.210 1.176   0.734   1.00 18.59  ? 176 PHE A CG  1 
ATOM   1412 C  CD1 . PHE A 1 175 ? -16.437 0.068   -0.086  1.00 21.67  ? 176 PHE A CD1 1 
ATOM   1413 C  CD2 . PHE A 1 175 ? -16.503 1.039   2.093   1.00 18.90  ? 176 PHE A CD2 1 
ATOM   1414 C  CE1 . PHE A 1 175 ? -17.019 -1.093  0.412   1.00 23.97  ? 176 PHE A CE1 1 
ATOM   1415 C  CE2 . PHE A 1 175 ? -17.074 -0.153  2.605   1.00 16.76  ? 176 PHE A CE2 1 
ATOM   1416 C  CZ  . PHE A 1 175 ? -17.308 -1.225  1.768   1.00 19.85  ? 176 PHE A CZ  1 
ATOM   1417 N  N   . THR A 1 176 ? -18.626 4.499   -0.749  1.00 17.54  ? 177 THR A N   1 
ATOM   1418 C  CA  . THR A 1 176 ? -19.627 5.386   -0.180  1.00 17.23  ? 177 THR A CA  1 
ATOM   1419 C  C   . THR A 1 176 ? -20.801 4.526   0.279   1.00 15.32  ? 177 THR A C   1 
ATOM   1420 O  O   . THR A 1 176 ? -20.994 3.380   -0.191  1.00 17.35  ? 177 THR A O   1 
ATOM   1421 C  CB  . THR A 1 176 ? -20.010 6.462   -1.233  1.00 21.54  ? 177 THR A CB  1 
ATOM   1422 O  OG1 . THR A 1 176 ? -20.302 5.819   -2.476  1.00 30.66  ? 177 THR A OG1 1 
ATOM   1423 C  CG2 . THR A 1 176 ? -18.937 7.493   -1.517  1.00 26.74  ? 177 THR A CG2 1 
ATOM   1424 N  N   . ASN A 1 177 ? -21.622 5.126   1.163   1.00 15.89  ? 178 ASN A N   1 
ATOM   1425 C  CA  . ASN A 1 177 ? -22.896 4.562   1.583   1.00 18.85  ? 178 ASN A CA  1 
ATOM   1426 C  C   . ASN A 1 177 ? -22.716 3.226   2.297   1.00 17.12  ? 178 ASN A C   1 
ATOM   1427 O  O   . ASN A 1 177 ? -23.619 2.408   2.273   1.00 21.71  ? 178 ASN A O   1 
ATOM   1428 C  CB  . ASN A 1 177 ? -23.868 4.508   0.397   1.00 20.79  ? 178 ASN A CB  1 
ATOM   1429 C  CG  . ASN A 1 177 ? -24.076 5.914   -0.196  1.00 20.95  ? 178 ASN A CG  1 
ATOM   1430 O  OD1 . ASN A 1 177 ? -24.731 6.771   0.400   1.00 25.13  ? 178 ASN A OD1 1 
ATOM   1431 N  ND2 . ASN A 1 177 ? -23.510 6.214   -1.366  1.00 23.05  ? 178 ASN A ND2 1 
ATOM   1432 N  N   . PHE A 1 178 ? -21.589 3.000   2.985   1.00 16.61  ? 179 PHE A N   1 
ATOM   1433 C  CA  . PHE A 1 178 ? -21.501 1.768   3.754   1.00 16.88  ? 179 PHE A CA  1 
ATOM   1434 C  C   . PHE A 1 178 ? -21.985 2.045   5.180   1.00 15.03  ? 179 PHE A C   1 
ATOM   1435 O  O   . PHE A 1 178 ? -21.561 3.019   5.800   1.00 15.89  ? 179 PHE A O   1 
ATOM   1436 C  CB  . PHE A 1 178 ? -20.073 1.230   3.810   1.00 15.84  ? 179 PHE A CB  1 
ATOM   1437 C  CG  . PHE A 1 178 ? -19.966 -0.015  4.664   1.00 16.00  ? 179 PHE A CG  1 
ATOM   1438 C  CD1 . PHE A 1 178 ? -20.308 -1.251  4.131   1.00 17.38  ? 179 PHE A CD1 1 
ATOM   1439 C  CD2 . PHE A 1 178 ? -19.537 0.050   6.007   1.00 17.42  ? 179 PHE A CD2 1 
ATOM   1440 C  CE1 . PHE A 1 178 ? -20.256 -2.405  4.934   1.00 20.36  ? 179 PHE A CE1 1 
ATOM   1441 C  CE2 . PHE A 1 178 ? -19.493 -1.121  6.781   1.00 15.39  ? 179 PHE A CE2 1 
ATOM   1442 C  CZ  . PHE A 1 178 ? -19.863 -2.344  6.272   1.00 17.38  ? 179 PHE A CZ  1 
ATOM   1443 N  N   . ASP A 1 179 ? -22.853 1.180   5.707   1.00 15.31  ? 180 ASP A N   1 
ATOM   1444 C  CA  . ASP A 1 179 ? -23.499 1.429   6.991   1.00 14.68  ? 180 ASP A CA  1 
ATOM   1445 C  C   . ASP A 1 179 ? -22.826 0.570   8.073   1.00 14.29  ? 180 ASP A C   1 
ATOM   1446 O  O   . ASP A 1 179 ? -23.054 -0.666  8.128   1.00 14.72  ? 180 ASP A O   1 
ATOM   1447 C  CB  . ASP A 1 179 ? -24.991 1.103   6.869   1.00 17.24  ? 180 ASP A CB  1 
ATOM   1448 C  CG  . ASP A 1 179 ? -25.748 1.384   8.174   1.00 17.56  ? 180 ASP A CG  1 
ATOM   1449 O  OD1 . ASP A 1 179 ? -25.119 1.745   9.240   1.00 16.62  ? 180 ASP A OD1 1 
ATOM   1450 O  OD2 . ASP A 1 179 ? -27.004 1.283   8.141   1.00 25.65  ? 180 ASP A OD2 1 
ATOM   1451 N  N   . PRO A 1 180 ? -22.005 1.157   8.999   1.00 13.19  ? 181 PRO A N   1 
ATOM   1452 C  CA  . PRO A 1 180 ? -21.270 0.311   9.971   1.00 14.18  ? 181 PRO A CA  1 
ATOM   1453 C  C   . PRO A 1 180 ? -22.185 -0.339  11.011  1.00 12.89  ? 181 PRO A C   1 
ATOM   1454 O  O   . PRO A 1 180 ? -21.719 -1.205  11.758  1.00 12.76  ? 181 PRO A O   1 
ATOM   1455 C  CB  . PRO A 1 180 ? -20.251 1.319   10.548  1.00 14.53  ? 181 PRO A CB  1 
ATOM   1456 C  CG  . PRO A 1 180 ? -20.966 2.685   10.434  1.00 14.39  ? 181 PRO A CG  1 
ATOM   1457 C  CD  . PRO A 1 180 ? -21.675 2.595   9.093   1.00 13.94  ? 181 PRO A CD  1 
ATOM   1458 N  N   . ARG A 1 181 ? -23.457 0.109   11.109  1.00 12.18  ? 182 ARG A N   1 
ATOM   1459 C  CA  . ARG A 1 181 ? -24.390 -0.547  12.059  1.00 13.05  ? 182 ARG A CA  1 
ATOM   1460 C  C   . ARG A 1 181 ? -24.504 -2.038  11.739  1.00 14.53  ? 182 ARG A C   1 
ATOM   1461 O  O   . ARG A 1 181 ? -24.876 -2.813  12.616  1.00 16.62  ? 182 ARG A O   1 
ATOM   1462 C  CB  . ARG A 1 181 ? -25.782 0.111   11.985  1.00 13.81  ? 182 ARG A CB  1 
ATOM   1463 C  CG  . ARG A 1 181 ? -25.773 1.549   12.533  1.00 15.90  ? 182 ARG A CG  1 
ATOM   1464 C  CD  . ARG A 1 181 ? -27.101 2.237   12.469  1.00 19.85  ? 182 ARG A CD  1 
ATOM   1465 N  NE  . ARG A 1 181 ? -27.468 2.416   11.052  1.00 19.18  ? 182 ARG A NE  1 
ATOM   1466 C  CZ  . ARG A 1 181 ? -28.539 3.133   10.679  1.00 23.49  ? 182 ARG A CZ  1 
ATOM   1467 N  NH1 . ARG A 1 181 ? -29.329 3.669   11.614  1.00 28.43  ? 182 ARG A NH1 1 
ATOM   1468 N  NH2 . ARG A 1 181 ? -28.815 3.288   9.395   1.00 25.75  ? 182 ARG A NH2 1 
ATOM   1469 N  N   . GLY A 1 182 ? -24.252 -2.450  10.458  1.00 14.74  ? 183 GLY A N   1 
ATOM   1470 C  CA  . GLY A 1 182 ? -24.363 -3.868  10.096  1.00 14.80  ? 183 GLY A CA  1 
ATOM   1471 C  C   . GLY A 1 182 ? -23.205 -4.728  10.600  1.00 15.40  ? 183 GLY A C   1 
ATOM   1472 O  O   . GLY A 1 182 ? -23.192 -5.931  10.316  1.00 19.49  ? 183 GLY A O   1 
ATOM   1473 N  N   . LEU A 1 183 ? -22.228 -4.151  11.360  1.00 13.81  ? 184 LEU A N   1 
ATOM   1474 C  CA  . LEU A 1 183 ? -21.082 -4.935  11.888  1.00 12.73  ? 184 LEU A CA  1 
ATOM   1475 C  C   . LEU A 1 183 ? -21.237 -5.092  13.394  1.00 14.43  ? 184 LEU A C   1 
ATOM   1476 O  O   . LEU A 1 183 ? -20.340 -5.633  14.029  1.00 13.46  ? 184 LEU A O   1 
ATOM   1477 C  CB  . LEU A 1 183 ? -19.760 -4.196  11.566  1.00 13.16  ? 184 LEU A CB  1 
ATOM   1478 C  CG  . LEU A 1 183 ? -19.541 -4.069  10.050  1.00 13.74  ? 184 LEU A CG  1 
ATOM   1479 C  CD1 . LEU A 1 183 ? -18.266 -3.302  9.780   1.00 17.79  ? 184 LEU A CD1 1 
ATOM   1480 C  CD2 . LEU A 1 183 ? -19.422 -5.424  9.371   1.00 19.27  ? 184 LEU A CD2 1 
ATOM   1481 N  N   . LEU A 1 184 ? -22.330 -4.543  13.958  1.00 13.81  ? 185 LEU A N   1 
ATOM   1482 C  CA  . LEU A 1 184 ? -22.481 -4.600  15.434  1.00 13.93  ? 185 LEU A CA  1 
ATOM   1483 C  C   . LEU A 1 184 ? -23.156 -5.925  15.848  1.00 17.68  ? 185 LEU A C   1 
ATOM   1484 O  O   . LEU A 1 184 ? -24.039 -6.430  15.154  1.00 25.34  ? 185 LEU A O   1 
ATOM   1485 C  CB  . LEU A 1 184 ? -23.346 -3.412  15.965  1.00 12.83  ? 185 LEU A CB  1 
ATOM   1486 C  CG  . LEU A 1 184 ? -22.822 -2.014  15.578  1.00 13.12  ? 185 LEU A CG  1 
ATOM   1487 C  CD1 . LEU A 1 184 ? -23.757 -0.863  16.006  1.00 15.44  ? 185 LEU A CD1 1 
ATOM   1488 C  CD2 . LEU A 1 184 ? -21.422 -1.817  16.103  1.00 15.28  ? 185 LEU A CD2 1 
ATOM   1489 N  N   . PRO A 1 185 ? -22.838 -6.486  17.041  1.00 12.35  ? 186 PRO A N   1 
ATOM   1490 C  CA  . PRO A 1 185 ? -23.579 -7.640  17.571  1.00 13.68  ? 186 PRO A CA  1 
ATOM   1491 C  C   . PRO A 1 185 ? -24.864 -7.096  18.194  1.00 14.02  ? 186 PRO A C   1 
ATOM   1492 O  O   . PRO A 1 185 ? -25.120 -5.879  18.294  1.00 15.60  ? 186 PRO A O   1 
ATOM   1493 C  CB  . PRO A 1 185 ? -22.609 -8.196  18.612  1.00 12.64  ? 186 PRO A CB  1 
ATOM   1494 C  CG  . PRO A 1 185 ? -21.999 -6.935  19.148  1.00 10.98  ? 186 PRO A CG  1 
ATOM   1495 C  CD  . PRO A 1 185 ? -21.765 -6.041  17.920  1.00 11.43  ? 186 PRO A CD  1 
ATOM   1496 N  N   . GLU A 1 186 ? -25.710 -8.034  18.673  1.00 14.26  ? 187 GLU A N   1 
ATOM   1497 C  CA  . GLU A 1 186 ? -26.964 -7.650  19.251  1.00 15.35  ? 187 GLU A CA  1 
ATOM   1498 C  C   . GLU A 1 186 ? -26.747 -6.910  20.574  1.00 14.01  ? 187 GLU A C   1 
ATOM   1499 O  O   . GLU A 1 186 ? -27.360 -5.842  20.782  1.00 16.10  ? 187 GLU A O   1 
ATOM   1500 C  CB  . GLU A 1 186 ? -27.672 -8.993  19.437  1.00 20.69  ? 187 GLU A CB  1 
ATOM   1501 C  CG  . GLU A 1 186 ? -28.802 -8.922  20.357  1.00 24.35  ? 187 GLU A CG  1 
ATOM   1502 C  CD  . GLU A 1 186 ? -29.550 -10.251 20.527  1.00 22.77  ? 187 GLU A CD  1 
ATOM   1503 O  OE1 . GLU A 1 186 ? -29.419 -11.113 19.645  1.00 28.12  ? 187 GLU A OE1 1 
ATOM   1504 O  OE2 . GLU A 1 186 ? -30.278 -10.360 21.576  1.00 37.74  ? 187 GLU A OE2 1 
ATOM   1505 N  N   . SER A 1 187 ? -25.891 -7.427  21.483  1.00 12.51  ? 188 SER A N   1 
ATOM   1506 C  CA  . SER A 1 187 ? -25.693 -6.793  22.799  1.00 14.14  ? 188 SER A CA  1 
ATOM   1507 C  C   . SER A 1 187 ? -24.551 -5.740  22.774  1.00 13.36  ? 188 SER A C   1 
ATOM   1508 O  O   . SER A 1 187 ? -23.526 -5.995  22.118  1.00 13.87  ? 188 SER A O   1 
ATOM   1509 C  CB  . SER A 1 187 ? -25.339 -7.830  23.816  1.00 14.63  ? 188 SER A CB  1 
ATOM   1510 O  OG  . SER A 1 187 ? -25.062 -7.223  25.053  1.00 14.09  ? 188 SER A OG  1 
ATOM   1511 N  N   . LEU A 1 188 ? -24.719 -4.623  23.495  1.00 12.75  ? 189 LEU A N   1 
ATOM   1512 C  CA  . LEU A 1 188 ? -23.648 -3.629  23.703  1.00 12.92  ? 189 LEU A CA  1 
ATOM   1513 C  C   . LEU A 1 188 ? -22.973 -3.758  25.085  1.00 11.64  ? 189 LEU A C   1 
ATOM   1514 O  O   . LEU A 1 188 ? -22.296 -2.858  25.565  1.00 14.13  ? 189 LEU A O   1 
ATOM   1515 C  CB  . LEU A 1 188 ? -24.177 -2.197  23.509  1.00 15.64  ? 189 LEU A CB  1 
ATOM   1516 C  CG  . LEU A 1 188 ? -24.621 -1.801  22.091  1.00 16.82  ? 189 LEU A CG  1 
ATOM   1517 C  CD1 . LEU A 1 188 ? -25.195 -0.365  22.058  1.00 20.89  ? 189 LEU A CD1 1 
ATOM   1518 C  CD2 . LEU A 1 188 ? -23.514 -2.030  21.052  1.00 19.77  ? 189 LEU A CD2 1 
ATOM   1519 N  N   . ASP A 1 189 ? -23.124 -4.921  25.749  1.00 11.99  ? 190 ASP A N   1 
ATOM   1520 C  CA  . ASP A 1 189 ? -22.385 -5.200  26.980  1.00 12.63  ? 190 ASP A CA  1 
ATOM   1521 C  C   . ASP A 1 189 ? -20.868 -5.119  26.666  1.00 11.14  ? 190 ASP A C   1 
ATOM   1522 O  O   . ASP A 1 189 ? -20.430 -5.639  25.620  1.00 9.97   ? 190 ASP A O   1 
ATOM   1523 C  CB  . ASP A 1 189 ? -22.666 -6.623  27.508  1.00 14.98  ? 190 ASP A CB  1 
ATOM   1524 C  CG  . ASP A 1 189 ? -24.008 -6.809  28.216  1.00 18.75  ? 190 ASP A CG  1 
ATOM   1525 O  OD1 . ASP A 1 189 ? -24.698 -5.758  28.442  1.00 21.40  ? 190 ASP A OD1 1 
ATOM   1526 O  OD2 . ASP A 1 189 ? -24.405 -7.988  28.519  1.00 27.04  ? 190 ASP A OD2 1 
ATOM   1527 N  N   . TYR A 1 190 ? -20.101 -4.496  27.566  1.00 10.29  ? 191 TYR A N   1 
ATOM   1528 C  CA  . TYR A 1 190 ? -18.699 -4.257  27.230  1.00 9.92   ? 191 TYR A CA  1 
ATOM   1529 C  C   . TYR A 1 190 ? -17.798 -4.296  28.458  1.00 9.36   ? 191 TYR A C   1 
ATOM   1530 O  O   . TYR A 1 190 ? -18.225 -4.172  29.614  1.00 10.23  ? 191 TYR A O   1 
ATOM   1531 C  CB  . TYR A 1 190 ? -18.521 -2.882  26.533  1.00 10.14  ? 191 TYR A CB  1 
ATOM   1532 C  CG  . TYR A 1 190 ? -18.901 -1.687  27.374  1.00 10.39  ? 191 TYR A CG  1 
ATOM   1533 C  CD1 . TYR A 1 190 ? -17.953 -1.063  28.225  1.00 10.46  ? 191 TYR A CD1 1 
ATOM   1534 C  CD2 . TYR A 1 190 ? -20.199 -1.124  27.344  1.00 11.43  ? 191 TYR A CD2 1 
ATOM   1535 C  CE1 . TYR A 1 190 ? -18.330 -0.002  29.073  1.00 10.77  ? 191 TYR A CE1 1 
ATOM   1536 C  CE2 . TYR A 1 190 ? -20.575 -0.048  28.164  1.00 10.80  ? 191 TYR A CE2 1 
ATOM   1537 C  CZ  . TYR A 1 190 ? -19.626 0.531   29.005  1.00 12.22  ? 191 TYR A CZ  1 
ATOM   1538 O  OH  . TYR A 1 190 ? -20.004 1.564   29.839  1.00 12.27  ? 191 TYR A OH  1 
ATOM   1539 N  N   . TRP A 1 191 ? -16.497 -4.426  28.177  1.00 9.01   ? 192 TRP A N   1 
ATOM   1540 C  CA  . TRP A 1 191 ? -15.407 -4.158  29.125  1.00 8.06   ? 192 TRP A CA  1 
ATOM   1541 C  C   . TRP A 1 191 ? -14.710 -2.870  28.706  1.00 7.56   ? 192 TRP A C   1 
ATOM   1542 O  O   . TRP A 1 191 ? -14.609 -2.542  27.518  1.00 9.08   ? 192 TRP A O   1 
ATOM   1543 C  CB  . TRP A 1 191 ? -14.371 -5.303  29.142  1.00 8.71   ? 192 TRP A CB  1 
ATOM   1544 C  CG  . TRP A 1 191 ? -14.913 -6.633  29.592  1.00 9.01   ? 192 TRP A CG  1 
ATOM   1545 C  CD1 . TRP A 1 191 ? -15.158 -7.058  30.875  1.00 10.32  ? 192 TRP A CD1 1 
ATOM   1546 C  CD2 . TRP A 1 191 ? -15.187 -7.787  28.750  1.00 9.22   ? 192 TRP A CD2 1 
ATOM   1547 N  NE1 . TRP A 1 191 ? -15.587 -8.372  30.881  1.00 11.43  ? 192 TRP A NE1 1 
ATOM   1548 C  CE2 . TRP A 1 191 ? -15.649 -8.837  29.585  1.00 10.85  ? 192 TRP A CE2 1 
ATOM   1549 C  CE3 . TRP A 1 191 ? -15.086 -7.989  27.371  1.00 9.82   ? 192 TRP A CE3 1 
ATOM   1550 C  CZ2 . TRP A 1 191 ? -15.891 -10.124 29.087  1.00 11.79  ? 192 TRP A CZ2 1 
ATOM   1551 C  CZ3 . TRP A 1 191 ? -15.325 -9.270  26.872  1.00 11.17  ? 192 TRP A CZ3 1 
ATOM   1552 C  CH2 . TRP A 1 191 ? -15.787 -10.293 27.717  1.00 12.35  ? 192 TRP A CH2 1 
ATOM   1553 N  N   . THR A 1 192 ? -14.123 -2.137  29.671  1.00 7.90   ? 193 THR A N   1 
ATOM   1554 C  CA  . THR A 1 192 ? -13.401 -0.888  29.334  1.00 8.30   ? 193 THR A CA  1 
ATOM   1555 C  C   . THR A 1 192 ? -12.181 -0.748  30.236  1.00 8.29   ? 193 THR A C   1 
ATOM   1556 O  O   . THR A 1 192 ? -12.162 -1.085  31.418  1.00 9.10   ? 193 THR A O   1 
ATOM   1557 C  CB  . THR A 1 192 ? -14.354 0.328   29.406  1.00 8.86   ? 193 THR A CB  1 
ATOM   1558 O  OG1 . THR A 1 192 ? -13.654 1.536   29.057  1.00 8.65   ? 193 THR A OG1 1 
ATOM   1559 C  CG2 . THR A 1 192 ? -14.940 0.561   30.809  1.00 10.19  ? 193 THR A CG2 1 
ATOM   1560 N  N   . TYR A 1 193 ? -11.147 -0.116  29.655  1.00 8.51   ? 194 TYR A N   1 
ATOM   1561 C  CA  . TYR A 1 193 ? -9.902  0.141   30.355  1.00 8.15   ? 194 TYR A CA  1 
ATOM   1562 C  C   . TYR A 1 193 ? -9.154  1.244   29.594  1.00 7.61   ? 194 TYR A C   1 
ATOM   1563 O  O   . TYR A 1 193 ? -9.351  1.411   28.369  1.00 8.22   ? 194 TYR A O   1 
ATOM   1564 C  CB  . TYR A 1 193 ? -9.050  -1.136  30.542  1.00 8.46   ? 194 TYR A CB  1 
ATOM   1565 C  CG  . TYR A 1 193 ? -8.359  -1.635  29.284  1.00 8.61   ? 194 TYR A CG  1 
ATOM   1566 C  CD1 . TYR A 1 193 ? -9.063  -2.334  28.279  1.00 8.74   ? 194 TYR A CD1 1 
ATOM   1567 C  CD2 . TYR A 1 193 ? -7.041  -1.244  29.051  1.00 8.21   ? 194 TYR A CD2 1 
ATOM   1568 C  CE1 . TYR A 1 193 ? -8.399  -2.698  27.080  1.00 8.34   ? 194 TYR A CE1 1 
ATOM   1569 C  CE2 . TYR A 1 193 ? -6.360  -1.581  27.866  1.00 9.54   ? 194 TYR A CE2 1 
ATOM   1570 C  CZ  . TYR A 1 193 ? -7.066  -2.272  26.886  1.00 8.62   ? 194 TYR A CZ  1 
ATOM   1571 O  OH  . TYR A 1 193 ? -6.417  -2.607  25.699  1.00 7.58   ? 194 TYR A OH  1 
ATOM   1572 N  N   . PRO A 1 194 ? -8.189  1.922   30.252  1.00 7.92   ? 195 PRO A N   1 
ATOM   1573 C  CA  . PRO A 1 194 ? -7.349  2.942   29.580  1.00 8.50   ? 195 PRO A CA  1 
ATOM   1574 C  C   . PRO A 1 194 ? -6.152  2.264   28.901  1.00 8.35   ? 195 PRO A C   1 
ATOM   1575 O  O   . PRO A 1 194 ? -5.410  1.509   29.555  1.00 8.82   ? 195 PRO A O   1 
ATOM   1576 C  CB  . PRO A 1 194 ? -6.877  3.855   30.744  1.00 10.48  ? 195 PRO A CB  1 
ATOM   1577 C  CG  . PRO A 1 194 ? -6.826  2.917   31.957  1.00 10.54  ? 195 PRO A CG  1 
ATOM   1578 C  CD  . PRO A 1 194 ? -8.010  1.930   31.738  1.00 9.09   ? 195 PRO A CD  1 
ATOM   1579 N  N   . GLY A 1 195 ? -5.901  2.603   27.610  1.00 7.57   ? 196 GLY A N   1 
ATOM   1580 C  CA  . GLY A 1 195 ? -4.818  1.935   26.880  1.00 8.86   ? 196 GLY A CA  1 
ATOM   1581 C  C   . GLY A 1 195 ? -4.234  2.844   25.820  1.00 8.15   ? 196 GLY A C   1 
ATOM   1582 O  O   . GLY A 1 195 ? -4.118  4.085   25.956  1.00 8.25   ? 196 GLY A O   1 
ATOM   1583 N  N   . SER A 1 196 ? -3.830  2.163   24.724  1.00 7.52   ? 197 SER A N   1 
ATOM   1584 C  CA  . SER A 1 196 ? -2.988  2.820   23.716  1.00 8.21   ? 197 SER A CA  1 
ATOM   1585 C  C   . SER A 1 196 ? -3.432  2.420   22.306  1.00 6.82   ? 197 SER A C   1 
ATOM   1586 O  O   . SER A 1 196 ? -4.212  1.459   22.145  1.00 7.69   ? 197 SER A O   1 
ATOM   1587 C  CB  . SER A 1 196 ? -1.531  2.405   23.930  1.00 9.31   ? 197 SER A CB  1 
ATOM   1588 O  OG  . SER A 1 196 ? -1.289  1.059   23.476  1.00 8.33   ? 197 SER A OG  1 
ATOM   1589 N  N   . LEU A 1 197 ? -2.879  3.096   21.307  1.00 7.76   ? 198 LEU A N   1 
ATOM   1590 C  CA  . LEU A 1 197 ? -2.898  2.482   19.982  1.00 7.72   ? 198 LEU A CA  1 
ATOM   1591 C  C   . LEU A 1 197 ? -2.193  1.134   20.030  1.00 8.12   ? 198 LEU A C   1 
ATOM   1592 O  O   . LEU A 1 197 ? -1.185  0.964   20.731  1.00 7.92   ? 198 LEU A O   1 
ATOM   1593 C  CB  . LEU A 1 197 ? -2.147  3.359   18.967  1.00 9.19   ? 198 LEU A CB  1 
ATOM   1594 C  CG  . LEU A 1 197 ? -2.368  4.884   18.953  1.00 10.90  ? 198 LEU A CG  1 
ATOM   1595 C  CD1 . LEU A 1 197 ? -1.443  5.516   17.889  1.00 12.01  ? 198 LEU A CD1 1 
ATOM   1596 C  CD2 . LEU A 1 197 ? -3.766  5.391   18.703  1.00 12.35  ? 198 LEU A CD2 1 
ATOM   1597 N  N   . THR A 1 198 ? -2.718  0.156   19.242  1.00 7.83   ? 199 THR A N   1 
ATOM   1598 C  CA  . THR A 1 198 ? -1.988  -1.127  19.128  1.00 8.09   ? 199 THR A CA  1 
ATOM   1599 C  C   . THR A 1 198 ? -0.985  -1.224  17.989  1.00 7.57   ? 199 THR A C   1 
ATOM   1600 O  O   . THR A 1 198 ? -0.311  -2.248  17.847  1.00 8.16   ? 199 THR A O   1 
ATOM   1601 C  CB  . THR A 1 198 ? -2.985  -2.293  19.011  1.00 7.46   ? 199 THR A CB  1 
ATOM   1602 O  OG1 . THR A 1 198 ? -3.560  -2.229  17.695  1.00 7.87   ? 199 THR A OG1 1 
ATOM   1603 C  CG2 . THR A 1 198 ? -4.022  -2.321  20.141  1.00 8.09   ? 199 THR A CG2 1 
ATOM   1604 N  N   . THR A 1 199 ? -0.825  -0.108  17.253  1.00 8.41   ? 200 THR A N   1 
ATOM   1605 C  CA  . THR A 1 199 ? 0.174   -0.007  16.188  1.00 8.81   ? 200 THR A CA  1 
ATOM   1606 C  C   . THR A 1 199 ? 1.100   1.168   16.545  1.00 8.80   ? 200 THR A C   1 
ATOM   1607 O  O   . THR A 1 199 ? 0.626   2.161   17.183  1.00 9.34   ? 200 THR A O   1 
ATOM   1608 C  CB  . THR A 1 199 ? -0.438  0.292   14.813  1.00 9.29   ? 200 THR A CB  1 
ATOM   1609 O  OG1 . THR A 1 199 ? -1.146  1.552   14.844  1.00 10.97  ? 200 THR A OG1 1 
ATOM   1610 C  CG2 . THR A 1 199 ? -1.381  -0.807  14.420  1.00 9.48   ? 200 THR A CG2 1 
ATOM   1611 N  N   . PRO A 1 200 ? 2.386   1.156   16.099  1.00 8.95   ? 201 PRO A N   1 
ATOM   1612 C  CA  . PRO A 1 200 ? 3.225   2.394   16.183  1.00 10.02  ? 201 PRO A CA  1 
ATOM   1613 C  C   . PRO A 1 200 ? 2.364   3.565   15.680  1.00 11.49  ? 201 PRO A C   1 
ATOM   1614 O  O   . PRO A 1 200 ? 1.636   3.424   14.652  1.00 12.45  ? 201 PRO A O   1 
ATOM   1615 C  CB  . PRO A 1 200 ? 4.350   2.003   15.237  1.00 12.50  ? 201 PRO A CB  1 
ATOM   1616 C  CG  . PRO A 1 200 ? 4.539   0.519   15.556  1.00 12.59  ? 201 PRO A CG  1 
ATOM   1617 C  CD  . PRO A 1 200 ? 3.110   -0.018  15.486  1.00 11.48  ? 201 PRO A CD  1 
ATOM   1618 N  N   . PRO A 1 201 ? 2.428   4.771   16.289  1.00 10.90  ? 202 PRO A N   1 
ATOM   1619 C  CA  . PRO A 1 201 ? 3.378   5.103   17.372  1.00 11.43  ? 202 PRO A CA  1 
ATOM   1620 C  C   . PRO A 1 201 ? 2.983   4.734   18.807  1.00 9.35   ? 202 PRO A C   1 
ATOM   1621 O  O   . PRO A 1 201 ? 3.674   5.103   19.752  1.00 10.72  ? 202 PRO A O   1 
ATOM   1622 C  CB  . PRO A 1 201 ? 3.454   6.647   17.226  1.00 13.61  ? 202 PRO A CB  1 
ATOM   1623 C  CG  . PRO A 1 201 ? 2.026   7.049   16.745  1.00 14.07  ? 202 PRO A CG  1 
ATOM   1624 C  CD  . PRO A 1 201 ? 1.676   5.943   15.763  1.00 13.24  ? 202 PRO A CD  1 
ATOM   1625 N  N   . LEU A 1 202 ? 1.956   3.870   18.980  1.00 8.94   ? 203 LEU A N   1 
ATOM   1626 C  CA  . LEU A 1 202 ? 1.656   3.250   20.292  1.00 9.17   ? 203 LEU A CA  1 
ATOM   1627 C  C   . LEU A 1 202 ? 1.266   4.288   21.354  1.00 9.28   ? 203 LEU A C   1 
ATOM   1628 O  O   . LEU A 1 202 ? 1.439   4.029   22.585  1.00 9.48   ? 203 LEU A O   1 
ATOM   1629 C  CB  . LEU A 1 202 ? 2.800   2.306   20.775  1.00 9.00   ? 203 LEU A CB  1 
ATOM   1630 C  CG  . LEU A 1 202 ? 3.121   1.154   19.796  1.00 8.66   ? 203 LEU A CG  1 
ATOM   1631 C  CD1 . LEU A 1 202 ? 4.424   0.437   20.241  1.00 11.43  ? 203 LEU A CD1 1 
ATOM   1632 C  CD2 . LEU A 1 202 ? 1.989   0.122   19.739  1.00 9.34   ? 203 LEU A CD2 1 
ATOM   1633 N  N   . LEU A 1 203 ? 0.742   5.447   20.895  1.00 9.23   ? 204 LEU A N   1 
ATOM   1634 C  CA  . LEU A 1 203 ? 0.436   6.559   21.831  1.00 9.74   ? 204 LEU A CA  1 
ATOM   1635 C  C   . LEU A 1 203 ? -0.601  6.150   22.873  1.00 9.04   ? 204 LEU A C   1 
ATOM   1636 O  O   . LEU A 1 203 ? -1.581  5.412   22.554  1.00 8.99   ? 204 LEU A O   1 
ATOM   1637 C  CB  . LEU A 1 203 ? -0.079  7.787   21.052  1.00 9.62   ? 204 LEU A CB  1 
ATOM   1638 C  CG  . LEU A 1 203 ? 0.957   8.374   20.079  1.00 12.31  ? 204 LEU A CG  1 
ATOM   1639 C  CD1 . LEU A 1 203 ? 0.335   9.418   19.135  1.00 14.24  ? 204 LEU A CD1 1 
ATOM   1640 C  CD2 . LEU A 1 203 ? 2.202   8.932   20.803  1.00 17.16  ? 204 LEU A CD2 1 
ATOM   1641 N  N   . GLU A 1 204 ? -0.430  6.606   24.117  1.00 10.95  ? 205 GLU A N   1 
ATOM   1642 C  CA  . GLU A 1 204 ? -1.296  6.207   25.234  1.00 9.36   ? 205 GLU A CA  1 
ATOM   1643 C  C   . GLU A 1 204 ? -2.463  7.203   25.344  1.00 9.48   ? 205 GLU A C   1 
ATOM   1644 O  O   . GLU A 1 204 ? -2.600  7.991   26.301  1.00 11.62  ? 205 GLU A O   1 
ATOM   1645 C  CB  . GLU A 1 204 ? -0.444  6.041   26.501  1.00 10.06  ? 205 GLU A CB  1 
ATOM   1646 C  CG  . GLU A 1 204 ? 0.487   4.848   26.332  1.00 10.47  ? 205 GLU A CG  1 
ATOM   1647 C  CD  . GLU A 1 204 ? 1.369   4.569   27.552  1.00 10.57  ? 205 GLU A CD  1 
ATOM   1648 O  OE1 . GLU A 1 204 ? 1.714   5.516   28.326  1.00 13.06  ? 205 GLU A OE1 1 
ATOM   1649 O  OE2 . GLU A 1 204 ? 1.786   3.374   27.679  1.00 10.93  ? 205 GLU A OE2 1 
ATOM   1650 N  N   . CYS A 1 205 ? -3.343  7.127   24.339  1.00 8.01   ? 206 CYS A N   1 
ATOM   1651 C  CA  . CYS A 1 205 ? -4.415  8.136   24.142  1.00 8.74   ? 206 CYS A CA  1 
ATOM   1652 C  C   . CYS A 1 205 ? -5.804  7.517   23.981  1.00 8.15   ? 206 CYS A C   1 
ATOM   1653 O  O   . CYS A 1 205 ? -6.721  8.257   23.559  1.00 9.27   ? 206 CYS A O   1 
ATOM   1654 C  CB  . CYS A 1 205 ? -4.094  9.021   22.913  1.00 10.50  ? 206 CYS A CB  1 
ATOM   1655 S  SG  . CYS A 1 205 ? -4.010  8.034   21.356  1.00 10.50  ? 206 CYS A SG  1 
ATOM   1656 N  N   . VAL A 1 206 ? -5.968  6.220   24.323  1.00 7.91   ? 207 VAL A N   1 
ATOM   1657 C  CA  . VAL A 1 206 ? -7.189  5.487   23.959  1.00 8.26   ? 207 VAL A CA  1 
ATOM   1658 C  C   . VAL A 1 206 ? -7.973  5.000   25.186  1.00 8.96   ? 207 VAL A C   1 
ATOM   1659 O  O   . VAL A 1 206 ? -7.402  4.381   26.076  1.00 9.59   ? 207 VAL A O   1 
ATOM   1660 C  CB  . VAL A 1 206 ? -6.890  4.240   23.077  1.00 8.37   ? 207 VAL A CB  1 
ATOM   1661 C  CG1 . VAL A 1 206 ? -8.230  3.552   22.711  1.00 8.28   ? 207 VAL A CG1 1 
ATOM   1662 C  CG2 . VAL A 1 206 ? -6.109  4.645   21.778  1.00 9.33   ? 207 VAL A CG2 1 
ATOM   1663 N  N   . THR A 1 207 ? -9.308  5.352   25.203  1.00 8.10   ? 208 THR A N   1 
ATOM   1664 C  CA  . THR A 1 207 ? -10.238 4.608   26.077  1.00 8.48   ? 208 THR A CA  1 
ATOM   1665 C  C   . THR A 1 207 ? -10.781 3.444   25.254  1.00 7.45   ? 208 THR A C   1 
ATOM   1666 O  O   . THR A 1 207 ? -11.414 3.637   24.212  1.00 7.97   ? 208 THR A O   1 
ATOM   1667 C  CB  . THR A 1 207 ? -11.406 5.500   26.554  1.00 8.77   ? 208 THR A CB  1 
ATOM   1668 O  OG1 . THR A 1 207 ? -10.869 6.660   27.243  1.00 9.46   ? 208 THR A OG1 1 
ATOM   1669 C  CG2 . THR A 1 207 ? -12.305 4.672   27.463  1.00 10.14  ? 208 THR A CG2 1 
ATOM   1670 N  N   . TRP A 1 208 ? -10.416 2.213   25.679  1.00 7.77   ? 209 TRP A N   1 
ATOM   1671 C  CA  . TRP A 1 208 ? -10.908 0.986   25.026  1.00 7.06   ? 209 TRP A CA  1 
ATOM   1672 C  C   . TRP A 1 208 ? -12.279 0.562   25.537  1.00 6.94   ? 209 TRP A C   1 
ATOM   1673 O  O   . TRP A 1 208 ? -12.494 0.506   26.741  1.00 7.23   ? 209 TRP A O   1 
ATOM   1674 C  CB  . TRP A 1 208 ? -9.842  -0.165  25.218  1.00 7.41   ? 209 TRP A CB  1 
ATOM   1675 C  CG  . TRP A 1 208 ? -8.707  -0.060  24.245  1.00 7.22   ? 209 TRP A CG  1 
ATOM   1676 C  CD1 . TRP A 1 208 ? -7.495  0.601   24.437  1.00 8.14   ? 209 TRP A CD1 1 
ATOM   1677 C  CD2 . TRP A 1 208 ? -8.763  -0.434  22.856  1.00 7.31   ? 209 TRP A CD2 1 
ATOM   1678 N  NE1 . TRP A 1 208 ? -6.780  0.569   23.231  1.00 7.91   ? 209 TRP A NE1 1 
ATOM   1679 C  CE2 . TRP A 1 208 ? -7.535  -0.028  22.258  1.00 7.52   ? 209 TRP A CE2 1 
ATOM   1680 C  CE3 . TRP A 1 208 ? -9.734  -1.118  22.093  1.00 8.46   ? 209 TRP A CE3 1 
ATOM   1681 C  CZ2 . TRP A 1 208 ? -7.270  -0.293  20.896  1.00 8.52   ? 209 TRP A CZ2 1 
ATOM   1682 C  CZ3 . TRP A 1 208 ? -9.473  -1.409  20.758  1.00 8.61   ? 209 TRP A CZ3 1 
ATOM   1683 C  CH2 . TRP A 1 208 ? -8.249  -0.988  20.180  1.00 8.12   ? 209 TRP A CH2 1 
ATOM   1684 N  N   . ILE A 1 209 ? -13.147 0.245   24.577  1.00 6.93   ? 210 ILE A N   1 
ATOM   1685 C  CA  . ILE A 1 209 ? -14.476 -0.288  24.888  1.00 7.32   ? 210 ILE A CA  1 
ATOM   1686 C  C   . ILE A 1 209 ? -14.590 -1.565  24.068  1.00 7.87   ? 210 ILE A C   1 
ATOM   1687 O  O   . ILE A 1 209 ? -14.747 -1.495  22.817  1.00 8.47   ? 210 ILE A O   1 
ATOM   1688 C  CB  . ILE A 1 209 ? -15.569 0.748   24.549  1.00 8.45   ? 210 ILE A CB  1 
ATOM   1689 C  CG1 . ILE A 1 209 ? -15.336 2.020   25.376  1.00 10.13  ? 210 ILE A CG1 1 
ATOM   1690 C  CG2 . ILE A 1 209 ? -16.975 0.125   24.788  1.00 9.43   ? 210 ILE A CG2 1 
ATOM   1691 C  CD1 . ILE A 1 209 ? -16.182 3.212   24.913  1.00 11.83  ? 210 ILE A CD1 1 
ATOM   1692 N  N   . VAL A 1 210 ? -14.503 -2.746  24.708  1.00 8.00   ? 211 VAL A N   1 
ATOM   1693 C  CA  . VAL A 1 210 ? -14.465 -4.031  23.992  1.00 7.36   ? 211 VAL A CA  1 
ATOM   1694 C  C   . VAL A 1 210 ? -15.766 -4.782  24.241  1.00 7.29   ? 211 VAL A C   1 
ATOM   1695 O  O   . VAL A 1 210 ? -16.137 -5.067  25.394  1.00 8.06   ? 211 VAL A O   1 
ATOM   1696 C  CB  . VAL A 1 210 ? -13.269 -4.886  24.418  1.00 8.35   ? 211 VAL A CB  1 
ATOM   1697 C  CG1 . VAL A 1 210 ? -13.267 -6.230  23.697  1.00 9.06   ? 211 VAL A CG1 1 
ATOM   1698 C  CG2 . VAL A 1 210 ? -11.938 -4.116  24.185  1.00 8.64   ? 211 VAL A CG2 1 
ATOM   1699 N  N   . LEU A 1 211 ? -16.552 -5.012  23.178  1.00 8.49   ? 212 LEU A N   1 
ATOM   1700 C  CA  . LEU A 1 211 ? -17.842 -5.688  23.346  1.00 8.83   ? 212 LEU A CA  1 
ATOM   1701 C  C   . LEU A 1 211 ? -17.652 -7.162  23.706  1.00 9.05   ? 212 LEU A C   1 
ATOM   1702 O  O   . LEU A 1 211 ? -16.776 -7.879  23.159  1.00 8.76   ? 212 LEU A O   1 
ATOM   1703 C  CB  . LEU A 1 211 ? -18.654 -5.566  22.045  1.00 9.50   ? 212 LEU A CB  1 
ATOM   1704 C  CG  . LEU A 1 211 ? -19.058 -4.131  21.652  1.00 9.81   ? 212 LEU A CG  1 
ATOM   1705 C  CD1 . LEU A 1 211 ? -20.087 -4.223  20.473  1.00 13.23  ? 212 LEU A CD1 1 
ATOM   1706 C  CD2 . LEU A 1 211 ? -19.596 -3.293  22.829  1.00 11.51  ? 212 LEU A CD2 1 
ATOM   1707 N  N   . LYS A 1 212 ? -18.490 -7.683  24.600  1.00 9.74   ? 213 LYS A N   1 
ATOM   1708 C  CA  . LYS A 1 212 ? -18.431 -9.074  25.016  1.00 10.80  ? 213 LYS A CA  1 
ATOM   1709 C  C   . LYS A 1 212 ? -18.918 -10.053 23.942  1.00 9.89   ? 213 LYS A C   1 
ATOM   1710 O  O   . LYS A 1 212 ? -18.373 -11.147 23.797  1.00 11.29  ? 213 LYS A O   1 
ATOM   1711 C  CB  . LYS A 1 212 ? -19.235 -9.245  26.324  1.00 12.24  ? 213 LYS A CB  1 
ATOM   1712 C  CG  . LYS A 1 212 ? -19.420 -10.717 26.749  1.00 14.80  ? 213 LYS A CG  1 
ATOM   1713 C  CD  . LYS A 1 212 ? -20.052 -10.911 28.116  1.00 19.45  ? 213 LYS A CD  1 
ATOM   1714 C  CE  . LYS A 1 212 ? -20.212 -12.379 28.487  1.00 23.40  ? 213 LYS A CE  1 
ATOM   1715 N  NZ  . LYS A 1 212 ? -20.701 -12.595 29.875  1.00 40.58  ? 213 LYS A NZ  1 
ATOM   1716 N  N   A GLU A 1 213 ? -19.941 -9.649  23.176  0.50 9.53   ? 214 GLU A N   1 
ATOM   1717 N  N   B GLU A 1 213 ? -19.963 -9.672  23.199  0.50 9.68   ? 214 GLU A N   1 
ATOM   1718 C  CA  A GLU A 1 213 ? -20.591 -10.545 22.214  0.50 11.24  ? 214 GLU A CA  1 
ATOM   1719 C  CA  B GLU A 1 213 ? -20.560 -10.614 22.250  0.50 11.02  ? 214 GLU A CA  1 
ATOM   1720 C  C   A GLU A 1 213 ? -19.871 -10.467 20.865  0.50 10.07  ? 214 GLU A C   1 
ATOM   1721 C  C   B GLU A 1 213 ? -19.861 -10.477 20.894  0.50 9.99   ? 214 GLU A C   1 
ATOM   1722 O  O   A GLU A 1 213 ? -19.786 -9.380  20.260  0.50 10.77  ? 214 GLU A O   1 
ATOM   1723 O  O   B GLU A 1 213 ? -19.769 -9.368  20.332  0.50 10.09  ? 214 GLU A O   1 
ATOM   1724 C  CB  A GLU A 1 213 ? -22.026 -10.058 21.936  0.50 10.87  ? 214 GLU A CB  1 
ATOM   1725 C  CB  B GLU A 1 213 ? -22.054 -10.315 22.028  0.50 11.69  ? 214 GLU A CB  1 
ATOM   1726 C  CG  A GLU A 1 213 ? -22.789 -10.969 20.978  0.50 12.79  ? 214 GLU A CG  1 
ATOM   1727 C  CG  B GLU A 1 213 ? -22.702 -11.359 21.127  0.50 13.14  ? 214 GLU A CG  1 
ATOM   1728 C  CD  A GLU A 1 213 ? -24.234 -10.532 20.758  0.50 11.86  ? 214 GLU A CD  1 
ATOM   1729 C  CD  B GLU A 1 213 ? -24.190 -11.199 20.871  0.50 13.06  ? 214 GLU A CD  1 
ATOM   1730 O  OE1 A GLU A 1 213 ? -24.755 -10.674 19.598  0.50 16.73  ? 214 GLU A OE1 1 
ATOM   1731 O  OE1 B GLU A 1 213 ? -24.766 -10.104 21.154  0.50 12.36  ? 214 GLU A OE1 1 
ATOM   1732 O  OE2 A GLU A 1 213 ? -24.854 -10.059 21.737  0.50 12.44  ? 214 GLU A OE2 1 
ATOM   1733 O  OE2 B GLU A 1 213 ? -24.810 -12.188 20.420  0.50 17.05  ? 214 GLU A OE2 1 
ATOM   1734 N  N   . PRO A 1 214 ? -19.243 -11.570 20.385  1.00 10.33  ? 215 PRO A N   1 
ATOM   1735 C  CA  . PRO A 1 214 ? -18.604 -11.543 19.082  1.00 9.68   ? 215 PRO A CA  1 
ATOM   1736 C  C   . PRO A 1 214 ? -19.648 -11.464 17.976  1.00 10.76  ? 215 PRO A C   1 
ATOM   1737 O  O   . PRO A 1 214 ? -20.814 -11.906 18.147  1.00 13.03  ? 215 PRO A O   1 
ATOM   1738 C  CB  . PRO A 1 214 ? -17.805 -12.881 19.005  1.00 11.13  ? 215 PRO A CB  1 
ATOM   1739 C  CG  . PRO A 1 214 ? -18.552 -13.792 19.946  1.00 15.83  ? 215 PRO A CG  1 
ATOM   1740 C  CD  . PRO A 1 214 ? -19.225 -12.939 21.013  1.00 12.75  ? 215 PRO A CD  1 
ATOM   1741 N  N   . ILE A 1 215 ? -19.198 -11.037 16.773  1.00 10.39  ? 216 ILE A N   1 
ATOM   1742 C  CA  . ILE A 1 215 ? -20.038 -11.274 15.593  1.00 11.72  ? 216 ILE A CA  1 
ATOM   1743 C  C   . ILE A 1 215 ? -19.507 -12.539 14.899  1.00 11.30  ? 216 ILE A C   1 
ATOM   1744 O  O   . ILE A 1 215 ? -18.333 -12.939 15.057  1.00 11.85  ? 216 ILE A O   1 
ATOM   1745 C  CB  . ILE A 1 215 ? -20.044 -10.059 14.629  1.00 11.50  ? 216 ILE A CB  1 
ATOM   1746 C  CG1 . ILE A 1 215 ? -18.624 -9.662  14.161  1.00 12.30  ? 216 ILE A CG1 1 
ATOM   1747 C  CG2 . ILE A 1 215 ? -20.801 -8.874  15.294  1.00 13.16  ? 216 ILE A CG2 1 
ATOM   1748 C  CD1 . ILE A 1 215 ? -18.604 -8.695  12.943  1.00 13.45  ? 216 ILE A CD1 1 
ATOM   1749 N  N   A SER A 1 216 ? -20.386 -13.203 14.152  0.50 12.12  ? 217 SER A N   1 
ATOM   1750 N  N   B SER A 1 216 ? -20.403 -13.213 14.171  0.50 11.64  ? 217 SER A N   1 
ATOM   1751 C  CA  A SER A 1 216 ? -19.966 -14.361 13.378  0.50 11.95  ? 217 SER A CA  1 
ATOM   1752 C  CA  B SER A 1 216 ? -20.005 -14.333 13.328  0.50 11.40  ? 217 SER A CA  1 
ATOM   1753 C  C   A SER A 1 216 ? -19.819 -13.970 11.895  0.50 12.02  ? 217 SER A C   1 
ATOM   1754 C  C   B SER A 1 216 ? -19.768 -13.857 11.885  0.50 11.09  ? 217 SER A C   1 
ATOM   1755 O  O   A SER A 1 216 ? -20.724 -13.312 11.348  0.50 13.57  ? 217 SER A O   1 
ATOM   1756 O  O   B SER A 1 216 ? -20.578 -13.073 11.349  0.50 13.13  ? 217 SER A O   1 
ATOM   1757 C  CB  A SER A 1 216 ? -21.019 -15.438 13.551  0.50 15.49  ? 217 SER A CB  1 
ATOM   1758 C  CB  B SER A 1 216 ? -21.093 -15.408 13.340  0.50 12.01  ? 217 SER A CB  1 
ATOM   1759 O  OG  A SER A 1 216 ? -20.800 -16.504 12.657  0.50 20.90  ? 217 SER A OG  1 
ATOM   1760 O  OG  B SER A 1 216 ? -21.033 -16.178 14.532  0.50 14.36  ? 217 SER A OG  1 
ATOM   1761 N  N   . VAL A 1 217 ? -18.699 -14.399 11.269  1.00 10.77  ? 218 VAL A N   1 
ATOM   1762 C  CA  . VAL A 1 217 ? -18.432 -14.200 9.852   1.00 11.32  ? 218 VAL A CA  1 
ATOM   1763 C  C   . VAL A 1 217 ? -18.186 -15.586 9.270   1.00 11.75  ? 218 VAL A C   1 
ATOM   1764 O  O   . VAL A 1 217 ? -17.831 -16.535 9.976   1.00 12.59  ? 218 VAL A O   1 
ATOM   1765 C  CB  . VAL A 1 217 ? -17.213 -13.247 9.633   1.00 12.49  ? 218 VAL A CB  1 
ATOM   1766 C  CG1 . VAL A 1 217 ? -17.461 -11.912 10.324  1.00 13.23  ? 218 VAL A CG1 1 
ATOM   1767 C  CG2 . VAL A 1 217 ? -15.925 -13.892 10.133  1.00 12.72  ? 218 VAL A CG2 1 
ATOM   1768 N  N   . SER A 1 218 ? -18.338 -15.742 7.939   1.00 12.70  ? 219 SER A N   1 
ATOM   1769 C  CA  . SER A 1 218 ? -18.166 -17.111 7.415   1.00 13.62  ? 219 SER A CA  1 
ATOM   1770 C  C   . SER A 1 218 ? -16.705 -17.381 7.081   1.00 12.93  ? 219 SER A C   1 
ATOM   1771 O  O   . SER A 1 218 ? -15.870 -16.438 6.971   1.00 12.94  ? 219 SER A O   1 
ATOM   1772 C  CB  . SER A 1 218 ? -19.017 -17.312 6.169   1.00 13.33  ? 219 SER A CB  1 
ATOM   1773 O  OG  . SER A 1 218 ? -18.485 -16.434 5.138   1.00 15.48  ? 219 SER A OG  1 
ATOM   1774 N  N   A SER A 1 219 ? -16.368 -18.659 6.966   0.50 14.00  ? 220 SER A N   1 
ATOM   1775 N  N   B SER A 1 219 ? -16.373 -18.664 6.964   0.50 13.74  ? 220 SER A N   1 
ATOM   1776 C  CA  A SER A 1 219 ? -15.025 -19.034 6.542   0.50 16.37  ? 220 SER A CA  1 
ATOM   1777 C  CA  B SER A 1 219 ? -15.038 -19.064 6.535   0.50 16.10  ? 220 SER A CA  1 
ATOM   1778 C  C   A SER A 1 219 ? -14.649 -18.360 5.215   0.50 15.97  ? 220 SER A C   1 
ATOM   1779 C  C   B SER A 1 219 ? -14.651 -18.381 5.214   0.50 15.78  ? 220 SER A C   1 
ATOM   1780 O  O   A SER A 1 219 ? -13.528 -17.855 5.047   0.50 16.45  ? 220 SER A O   1 
ATOM   1781 O  O   B SER A 1 219 ? -13.529 -17.875 5.057   0.50 16.39  ? 220 SER A O   1 
ATOM   1782 C  CB  A SER A 1 219 ? -14.875 -20.545 6.502   0.50 18.99  ? 220 SER A CB  1 
ATOM   1783 C  CB  B SER A 1 219 ? -14.899 -20.587 6.505   0.50 17.12  ? 220 SER A CB  1 
ATOM   1784 O  OG  A SER A 1 219 ? -15.632 -21.085 5.429   0.50 16.67  ? 220 SER A OG  1 
ATOM   1785 O  OG  B SER A 1 219 ? -13.543 -20.981 6.342   0.50 16.41  ? 220 SER A OG  1 
ATOM   1786 N  N   . GLU A 1 220 ? -15.608 -18.280 4.269   1.00 14.58  ? 221 GLU A N   1 
ATOM   1787 C  CA  . GLU A 1 220 ? -15.342 -17.674 2.965   1.00 16.42  ? 221 GLU A CA  1 
ATOM   1788 C  C   . GLU A 1 220 ? -15.022 -16.162 3.113   1.00 15.38  ? 221 GLU A C   1 
ATOM   1789 O  O   . GLU A 1 220 ? -14.156 -15.618 2.383   1.00 16.54  ? 221 GLU A O   1 
ATOM   1790 C  CB  . GLU A 1 220 ? -16.528 -17.816 2.009   1.00 17.39  ? 221 GLU A CB  1 
ATOM   1791 C  CG  . GLU A 1 220 ? -16.774 -19.290 1.593   1.00 26.95  ? 221 GLU A CG  1 
ATOM   1792 C  CD  . GLU A 1 220 ? -17.750 -20.059 2.497   1.00 30.61  ? 221 GLU A CD  1 
ATOM   1793 O  OE1 . GLU A 1 220 ? -18.114 -19.594 3.621   1.00 24.77  ? 221 GLU A OE1 1 
ATOM   1794 O  OE2 . GLU A 1 220 ? -18.150 -21.159 2.106   1.00 41.70  ? 221 GLU A OE2 1 
ATOM   1795 N  N   . GLN A 1 221 ? -15.711 -15.463 4.049   1.00 13.43  ? 222 GLN A N   1 
ATOM   1796 C  CA  . GLN A 1 221 ? -15.443 -14.035 4.259   1.00 13.38  ? 222 GLN A CA  1 
ATOM   1797 C  C   . GLN A 1 221 ? -14.013 -13.798 4.773   1.00 13.66  ? 222 GLN A C   1 
ATOM   1798 O  O   . GLN A 1 221 ? -13.276 -12.946 4.248   1.00 13.83  ? 222 GLN A O   1 
ATOM   1799 C  CB  . GLN A 1 221 ? -16.498 -13.413 5.191   1.00 14.46  ? 222 GLN A CB  1 
ATOM   1800 C  CG  . GLN A 1 221 ? -17.867 -13.320 4.520   1.00 12.99  ? 222 GLN A CG  1 
ATOM   1801 C  CD  . GLN A 1 221 ? -18.984 -12.757 5.394   1.00 13.49  ? 222 GLN A CD  1 
ATOM   1802 O  OE1 . GLN A 1 221 ? -19.090 -13.088 6.563   1.00 12.67  ? 222 GLN A OE1 1 
ATOM   1803 N  NE2 . GLN A 1 221 ? -19.811 -11.877 4.811   1.00 13.92  ? 222 GLN A NE2 1 
ATOM   1804 N  N   . VAL A 1 222 ? -13.606 -14.529 5.819   1.00 14.00  ? 223 VAL A N   1 
ATOM   1805 C  CA  . VAL A 1 222 ? -12.268 -14.332 6.404   1.00 13.89  ? 223 VAL A CA  1 
ATOM   1806 C  C   . VAL A 1 222 ? -11.172 -14.805 5.430   1.00 15.86  ? 223 VAL A C   1 
ATOM   1807 O  O   . VAL A 1 222 ? -10.071 -14.210 5.382   1.00 14.75  ? 223 VAL A O   1 
ATOM   1808 C  CB  . VAL A 1 222 ? -12.170 -14.915 7.840   1.00 17.61  ? 223 VAL A CB  1 
ATOM   1809 C  CG1 . VAL A 1 222 ? -12.146 -16.420 7.808   1.00 20.00  ? 223 VAL A CG1 1 
ATOM   1810 C  CG2 . VAL A 1 222 ? -10.920 -14.401 8.590   1.00 20.26  ? 223 VAL A CG2 1 
ATOM   1811 N  N   . LEU A 1 223 ? -11.459 -15.837 4.607   1.00 14.89  ? 224 LEU A N   1 
ATOM   1812 C  CA  . LEU A 1 223 ? -10.505 -16.270 3.585   1.00 17.09  ? 224 LEU A CA  1 
ATOM   1813 C  C   . LEU A 1 223 ? -10.181 -15.129 2.602   1.00 17.83  ? 224 LEU A C   1 
ATOM   1814 O  O   . LEU A 1 223 ? -9.004  -14.982 2.217   1.00 17.10  ? 224 LEU A O   1 
ATOM   1815 C  CB  . LEU A 1 223 ? -10.971 -17.569 2.911   1.00 22.54  ? 224 LEU A CB  1 
ATOM   1816 C  CG  . LEU A 1 223 ? -10.714 -18.841 3.758   1.00 27.01  ? 224 LEU A CG  1 
ATOM   1817 C  CD1 . LEU A 1 223 ? -11.537 -20.083 3.310   1.00 32.40  ? 224 LEU A CD1 1 
ATOM   1818 C  CD2 . LEU A 1 223 ? -9.222  -19.167 3.921   1.00 31.83  ? 224 LEU A CD2 1 
ATOM   1819 N  N   . LYS A 1 224 ? -11.176 -14.241 2.295   1.00 15.93  ? 225 LYS A N   1 
ATOM   1820 C  CA  . LYS A 1 224 ? -10.924 -13.080 1.439   1.00 16.92  ? 225 LYS A CA  1 
ATOM   1821 C  C   . LYS A 1 224 ? -10.002 -12.061 2.135   1.00 14.24  ? 225 LYS A C   1 
ATOM   1822 O  O   . LYS A 1 224 ? -9.170  -11.430 1.472   1.00 14.74  ? 225 LYS A O   1 
ATOM   1823 C  CB  . LYS A 1 224 ? -12.230 -12.546 0.826   1.00 21.05  ? 225 LYS A CB  1 
ATOM   1824 C  CG  . LYS A 1 224 ? -12.814 -13.454 -0.277  1.00 27.24  ? 225 LYS A CG  1 
ATOM   1825 C  CD  . LYS A 1 224 ? -14.116 -12.983 -0.940  1.00 42.06  ? 225 LYS A CD  1 
ATOM   1826 C  CE  . LYS A 1 224 ? -14.404 -13.726 -2.253  1.00 56.49  ? 225 LYS A CE  1 
ATOM   1827 N  NZ  . LYS A 1 224 ? -15.786 -14.266 -2.461  1.00 35.28  ? 225 LYS A NZ  1 
ATOM   1828 N  N   . PHE A 1 225 ? -10.159 -11.833 3.456   1.00 13.03  ? 226 PHE A N   1 
ATOM   1829 C  CA  . PHE A 1 225 ? -9.190  -10.971 4.144   1.00 12.49  ? 226 PHE A CA  1 
ATOM   1830 C  C   . PHE A 1 225 ? -7.758  -11.496 3.927   1.00 12.39  ? 226 PHE A C   1 
ATOM   1831 O  O   . PHE A 1 225 ? -6.797  -10.706 3.733   1.00 12.28  ? 226 PHE A O   1 
ATOM   1832 C  CB  . PHE A 1 225 ? -9.445  -10.992 5.664   1.00 13.98  ? 226 PHE A CB  1 
ATOM   1833 C  CG  . PHE A 1 225 ? -10.611 -10.144 6.165   1.00 12.94  ? 226 PHE A CG  1 
ATOM   1834 C  CD1 . PHE A 1 225 ? -11.755 -9.869  5.422   1.00 18.31  ? 226 PHE A CD1 1 
ATOM   1835 C  CD2 . PHE A 1 225 ? -10.658 -9.808  7.518   1.00 20.07  ? 226 PHE A CD2 1 
ATOM   1836 C  CE1 . PHE A 1 225 ? -12.813 -9.119  5.938   1.00 16.54  ? 226 PHE A CE1 1 
ATOM   1837 C  CE2 . PHE A 1 225 ? -11.692 -9.035  8.048   1.00 20.94  ? 226 PHE A CE2 1 
ATOM   1838 C  CZ  . PHE A 1 225 ? -12.770 -8.709  7.252   1.00 15.45  ? 226 PHE A CZ  1 
ATOM   1839 N  N   . ARG A 1 226 ? -7.576  -12.823 3.999   1.00 12.77  ? 227 ARG A N   1 
ATOM   1840 C  CA  . ARG A 1 226 ? -6.255  -13.448 4.007   1.00 12.31  ? 227 ARG A CA  1 
ATOM   1841 C  C   . ARG A 1 226 ? -5.645  -13.412 2.595   1.00 14.18  ? 227 ARG A C   1 
ATOM   1842 O  O   . ARG A 1 226 ? -4.531  -13.904 2.439   1.00 14.47  ? 227 ARG A O   1 
ATOM   1843 C  CB  . ARG A 1 226 ? -6.386  -14.888 4.539   1.00 12.59  ? 227 ARG A CB  1 
ATOM   1844 C  CG  . ARG A 1 226 ? -6.843  -14.985 5.997   1.00 12.71  ? 227 ARG A CG  1 
ATOM   1845 C  CD  . ARG A 1 226 ? -6.839  -16.462 6.446   1.00 15.74  ? 227 ARG A CD  1 
ATOM   1846 N  NE  . ARG A 1 226 ? -7.367  -16.572 7.831   1.00 14.27  ? 227 ARG A NE  1 
ATOM   1847 C  CZ  . ARG A 1 226 ? -8.274  -17.456 8.255   1.00 13.82  ? 227 ARG A CZ  1 
ATOM   1848 N  NH1 . ARG A 1 226 ? -8.728  -18.428 7.437   1.00 17.28  ? 227 ARG A NH1 1 
ATOM   1849 N  NH2 . ARG A 1 226 ? -8.720  -17.358 9.491   1.00 14.62  ? 227 ARG A NH2 1 
ATOM   1850 N  N   . LYS A 1 227 ? -6.397  -12.996 1.561   1.00 12.45  ? 228 LYS A N   1 
ATOM   1851 C  CA  . LYS A 1 227 ? -5.873  -12.843 0.198   1.00 14.51  ? 228 LYS A CA  1 
ATOM   1852 C  C   . LYS A 1 227 ? -5.239  -11.470 -0.053  1.00 13.37  ? 228 LYS A C   1 
ATOM   1853 O  O   . LYS A 1 227 ? -4.550  -11.279 -1.085  1.00 15.09  ? 228 LYS A O   1 
ATOM   1854 C  CB  . LYS A 1 227 ? -6.957  -13.117 -0.864  1.00 15.90  ? 228 LYS A CB  1 
ATOM   1855 C  CG  . LYS A 1 227 ? -7.396  -14.590 -0.897  1.00 21.79  ? 228 LYS A CG  1 
ATOM   1856 C  CD  . LYS A 1 227 ? -8.381  -14.912 -2.039  1.00 35.61  ? 228 LYS A CD  1 
ATOM   1857 C  CE  . LYS A 1 227 ? -8.825  -16.369 -2.027  1.00 45.78  ? 228 LYS A CE  1 
ATOM   1858 N  NZ  . LYS A 1 227 ? -9.750  -16.640 -3.154  1.00 69.27  ? 228 LYS A NZ  1 
ATOM   1859 N  N   . LEU A 1 228 ? -5.488  -10.516 0.871   1.00 12.25  ? 229 LEU A N   1 
ATOM   1860 C  CA  . LEU A 1 228 ? -4.861  -9.216  0.747   1.00 13.13  ? 229 LEU A CA  1 
ATOM   1861 C  C   . LEU A 1 228 ? -3.343  -9.380  0.899   1.00 12.99  ? 229 LEU A C   1 
ATOM   1862 O  O   . LEU A 1 228 ? -2.791  -10.432 1.306   1.00 12.91  ? 229 LEU A O   1 
ATOM   1863 C  CB  . LEU A 1 228 ? -5.419  -8.330  1.860   1.00 12.76  ? 229 LEU A CB  1 
ATOM   1864 C  CG  . LEU A 1 228 ? -6.823  -7.794  1.620   1.00 13.90  ? 229 LEU A CG  1 
ATOM   1865 C  CD1 . LEU A 1 228 ? -7.255  -7.205  2.959   1.00 13.99  ? 229 LEU A CD1 1 
ATOM   1866 C  CD2 . LEU A 1 228 ? -6.857  -6.690  0.549   1.00 15.40  ? 229 LEU A CD2 1 
ATOM   1867 N  N   . ASN A 1 229 ? -2.623  -8.319  0.490   1.00 13.64  ? 230 ASN A N   1 
ATOM   1868 C  CA  . ASN A 1 229 ? -1.166  -8.298  0.553   1.00 13.24  ? 230 ASN A CA  1 
ATOM   1869 C  C   . ASN A 1 229 ? -0.625  -7.124  1.391   1.00 13.11  ? 230 ASN A C   1 
ATOM   1870 O  O   . ASN A 1 229 ? -1.155  -6.018  1.328   1.00 13.20  ? 230 ASN A O   1 
ATOM   1871 C  CB  . ASN A 1 229 ? -0.545  -8.120  -0.856  1.00 15.13  ? 230 ASN A CB  1 
ATOM   1872 C  CG  . ASN A 1 229 ? -0.543  -9.340  -1.776  1.00 15.43  ? 230 ASN A CG  1 
ATOM   1873 O  OD1 . ASN A 1 229 ? -0.016  -9.184  -2.888  1.00 17.89  ? 230 ASN A OD1 1 
ATOM   1874 N  ND2 . ASN A 1 229 ? -1.182  -10.468 -1.439  1.00 15.03  ? 230 ASN A ND2 1 
ATOM   1875 N  N   . PHE A 1 230 ? 0.469   -7.423  2.144   1.00 12.80  ? 231 PHE A N   1 
ATOM   1876 C  CA  . PHE A 1 230 ? 1.238   -6.375  2.837   1.00 14.11  ? 231 PHE A CA  1 
ATOM   1877 C  C   . PHE A 1 230 ? 2.115   -5.602  1.863   1.00 14.85  ? 231 PHE A C   1 
ATOM   1878 O  O   . PHE A 1 230 ? 2.380   -4.410  2.068   1.00 15.65  ? 231 PHE A O   1 
ATOM   1879 C  CB  . PHE A 1 230 ? 2.212   -6.974  3.853   1.00 14.05  ? 231 PHE A CB  1 
ATOM   1880 C  CG  . PHE A 1 230 ? 1.623   -7.563  5.130   1.00 13.42  ? 231 PHE A CG  1 
ATOM   1881 C  CD1 . PHE A 1 230 ? 0.840   -6.775  5.986   1.00 14.08  ? 231 PHE A CD1 1 
ATOM   1882 C  CD2 . PHE A 1 230 ? 2.007   -8.838  5.555   1.00 13.30  ? 231 PHE A CD2 1 
ATOM   1883 C  CE1 . PHE A 1 230 ? 0.363   -7.291  7.188   1.00 13.04  ? 231 PHE A CE1 1 
ATOM   1884 C  CE2 . PHE A 1 230 ? 1.502   -9.367  6.736   1.00 13.14  ? 231 PHE A CE2 1 
ATOM   1885 C  CZ  . PHE A 1 230 ? 0.777   -8.562  7.578   1.00 12.62  ? 231 PHE A CZ  1 
ATOM   1886 N  N   . ASN A 1 231 ? 2.605   -6.290  0.809   1.00 15.63  ? 232 ASN A N   1 
ATOM   1887 C  CA  . ASN A 1 231 ? 3.490   -5.667  -0.186  1.00 14.90  ? 232 ASN A CA  1 
ATOM   1888 C  C   . ASN A 1 231 ? 2.701   -4.744  -1.131  1.00 16.47  ? 232 ASN A C   1 
ATOM   1889 O  O   . ASN A 1 231 ? 1.474   -4.863  -1.284  1.00 15.90  ? 232 ASN A O   1 
ATOM   1890 C  CB  . ASN A 1 231 ? 4.168   -6.771  -1.014  1.00 16.94  ? 232 ASN A CB  1 
ATOM   1891 C  CG  . ASN A 1 231 ? 3.136   -7.734  -1.570  1.00 16.37  ? 232 ASN A CG  1 
ATOM   1892 O  OD1 . ASN A 1 231 ? 2.602   -8.577  -0.819  1.00 17.71  ? 232 ASN A OD1 1 
ATOM   1893 N  ND2 . ASN A 1 231 ? 2.811   -7.642  -2.864  1.00 20.41  ? 232 ASN A ND2 1 
ATOM   1894 N  N   . GLY A 1 232 ? 3.476   -3.851  -1.838  1.00 17.49  ? 233 GLY A N   1 
ATOM   1895 C  CA  . GLY A 1 232 ? 2.962   -3.063  -2.956  1.00 17.99  ? 233 GLY A CA  1 
ATOM   1896 C  C   . GLY A 1 232 ? 2.859   -3.868  -4.262  1.00 15.94  ? 233 GLY A C   1 
ATOM   1897 O  O   . GLY A 1 232 ? 3.387   -4.999  -4.383  1.00 18.60  ? 233 GLY A O   1 
ATOM   1898 N  N   . GLU A 1 233 ? 2.130   -3.280  -5.218  1.00 16.95  ? 234 GLU A N   1 
ATOM   1899 C  CA  . GLU A 1 233 ? 2.047   -3.813  -6.576  1.00 19.33  ? 234 GLU A CA  1 
ATOM   1900 C  C   . GLU A 1 233 ? 3.408   -4.182  -7.166  1.00 20.82  ? 234 GLU A C   1 
ATOM   1901 O  O   . GLU A 1 233 ? 4.400   -3.459  -7.029  1.00 21.85  ? 234 GLU A O   1 
ATOM   1902 C  CB  . GLU A 1 233 ? 1.214   -2.918  -7.491  1.00 19.71  ? 234 GLU A CB  1 
ATOM   1903 C  CG  . GLU A 1 233 ? 0.995   -3.487  -8.886  1.00 18.99  ? 234 GLU A CG  1 
ATOM   1904 C  CD  . GLU A 1 233 ? 0.216   -2.581  -9.824  1.00 29.81  ? 234 GLU A CD  1 
ATOM   1905 O  OE1 . GLU A 1 233 ? -0.041  -1.422  -9.445  1.00 27.10  ? 234 GLU A OE1 1 
ATOM   1906 O  OE2 . GLU A 1 233 ? -0.131  -3.038  -10.932 1.00 27.00  ? 234 GLU A OE2 1 
ATOM   1907 N  N   . GLY A 1 234 ? 3.434   -5.368  -7.796  1.00 23.96  ? 235 GLY A N   1 
ATOM   1908 C  CA  . GLY A 1 234 ? 4.590   -5.931  -8.472  1.00 30.24  ? 235 GLY A CA  1 
ATOM   1909 C  C   . GLY A 1 234 ? 5.747   -6.390  -7.573  1.00 37.00  ? 235 GLY A C   1 
ATOM   1910 O  O   . GLY A 1 234 ? 6.770   -6.816  -8.113  1.00 48.15  ? 235 GLY A O   1 
ATOM   1911 N  N   . GLU A 1 235 ? 5.618   -6.329  -6.237  1.00 20.26  ? 236 GLU A N   1 
ATOM   1912 C  CA  . GLU A 1 235 ? 6.657   -6.828  -5.317  1.00 17.99  ? 236 GLU A CA  1 
ATOM   1913 C  C   . GLU A 1 235 ? 6.317   -8.267  -4.899  1.00 22.26  ? 236 GLU A C   1 
ATOM   1914 O  O   . GLU A 1 235 ? 5.184   -8.738  -5.103  1.00 24.44  ? 236 GLU A O   1 
ATOM   1915 C  CB  . GLU A 1 235 ? 6.611   -5.994  -4.026  1.00 20.94  ? 236 GLU A CB  1 
ATOM   1916 C  CG  . GLU A 1 235 ? 7.122   -4.557  -4.254  1.00 23.41  ? 236 GLU A CG  1 
ATOM   1917 C  CD  . GLU A 1 235 ? 6.919   -3.653  -3.054  1.00 33.60  ? 236 GLU A CD  1 
ATOM   1918 O  OE1 . GLU A 1 235 ? 6.350   -4.117  -2.023  1.00 26.09  ? 236 GLU A OE1 1 
ATOM   1919 O  OE2 . GLU A 1 235 ? 7.274   -2.461  -3.189  1.00 41.43  ? 236 GLU A OE2 1 
ATOM   1920 N  N   . PRO A 1 236 ? 7.259   -9.069  -4.363  1.00 23.28  ? 237 PRO A N   1 
ATOM   1921 C  CA  . PRO A 1 236 ? 6.999   -10.483 -4.007  1.00 24.24  ? 237 PRO A CA  1 
ATOM   1922 C  C   . PRO A 1 236 ? 5.865   -10.573 -2.978  1.00 20.98  ? 237 PRO A C   1 
ATOM   1923 O  O   . PRO A 1 236 ? 5.681   -9.687  -2.115  1.00 19.29  ? 237 PRO A O   1 
ATOM   1924 C  CB  . PRO A 1 236 ? 8.326   -10.970 -3.388  1.00 27.65  ? 237 PRO A CB  1 
ATOM   1925 C  CG  . PRO A 1 236 ? 9.361   -10.122 -4.179  1.00 33.29  ? 237 PRO A CG  1 
ATOM   1926 C  CD  . PRO A 1 236 ? 8.695   -8.735  -4.183  1.00 23.97  ? 237 PRO A CD  1 
ATOM   1927 N  N   . GLU A 1 237 ? 5.004   -11.608 -3.133  1.00 18.22  ? 238 GLU A N   1 
ATOM   1928 C  CA  . GLU A 1 237 ? 3.744   -11.595 -2.411  1.00 19.22  ? 238 GLU A CA  1 
ATOM   1929 C  C   . GLU A 1 237 ? 3.976   -11.973 -0.957  1.00 16.94  ? 238 GLU A C   1 
ATOM   1930 O  O   . GLU A 1 237 ? 4.545   -13.022 -0.683  1.00 18.37  ? 238 GLU A O   1 
ATOM   1931 C  CB  . GLU A 1 237 ? 2.728   -12.548 -3.047  1.00 17.79  ? 238 GLU A CB  1 
ATOM   1932 C  CG  . GLU A 1 237 ? 1.389   -12.510 -2.290  1.00 20.44  ? 238 GLU A CG  1 
ATOM   1933 C  CD  . GLU A 1 237 ? 0.305   -13.187 -3.135  1.00 20.61  ? 238 GLU A CD  1 
ATOM   1934 O  OE1 . GLU A 1 237 ? 0.675   -14.203 -3.848  1.00 32.80  ? 238 GLU A OE1 1 
ATOM   1935 O  OE2 . GLU A 1 237 ? -0.853  -12.710 -3.164  1.00 17.53  ? 238 GLU A OE2 1 
ATOM   1936 N  N   . GLU A 1 238 ? 3.475   -11.110 -0.066  1.00 15.74  ? 239 GLU A N   1 
ATOM   1937 C  CA  . GLU A 1 238 ? 3.456   -11.364 1.370   1.00 17.76  ? 239 GLU A CA  1 
ATOM   1938 C  C   . GLU A 1 238 ? 2.008   -11.242 1.803   1.00 14.08  ? 239 GLU A C   1 
ATOM   1939 O  O   . GLU A 1 238 ? 1.448   -10.131 1.849   1.00 16.33  ? 239 GLU A O   1 
ATOM   1940 C  CB  . GLU A 1 238 ? 4.144   -10.203 2.102   1.00 20.42  ? 239 GLU A CB  1 
ATOM   1941 C  CG  . GLU A 1 238 ? 5.422   -10.579 2.823   1.00 37.01  ? 239 GLU A CG  1 
ATOM   1942 C  CD  . GLU A 1 238 ? 6.779   -10.651 2.090   1.00 54.98  ? 239 GLU A CD  1 
ATOM   1943 O  OE1 . GLU A 1 238 ? 6.783   -10.507 0.836   1.00 90.93  ? 239 GLU A OE1 1 
ATOM   1944 O  OE2 . GLU A 1 238 ? 7.871   -10.827 2.785   1.00 60.48  ? 239 GLU A OE2 1 
ATOM   1945 N  N   . LEU A 1 239 ? 1.325   -12.413 2.065   1.00 14.12  ? 240 LEU A N   1 
ATOM   1946 C  CA  . LEU A 1 239 ? -0.088  -12.332 2.398   1.00 13.80  ? 240 LEU A CA  1 
ATOM   1947 C  C   . LEU A 1 239 ? -0.249  -11.512 3.687   1.00 10.87  ? 240 LEU A C   1 
ATOM   1948 O  O   . LEU A 1 239 ? 0.519   -11.704 4.666   1.00 12.68  ? 240 LEU A O   1 
ATOM   1949 C  CB  . LEU A 1 239 ? -0.666  -13.768 2.611   1.00 13.83  ? 240 LEU A CB  1 
ATOM   1950 C  CG  . LEU A 1 239 ? -0.610  -14.638 1.347   1.00 15.69  ? 240 LEU A CG  1 
ATOM   1951 C  CD1 . LEU A 1 239 ? -1.099  -16.012 1.762   1.00 18.73  ? 240 LEU A CD1 1 
ATOM   1952 C  CD2 . LEU A 1 239 ? -1.517  -14.033 0.294   1.00 14.42  ? 240 LEU A CD2 1 
ATOM   1953 N  N   . MET A 1 240 ? -1.275  -10.651 3.678   1.00 11.85  ? 241 MET A N   1 
ATOM   1954 C  CA  . MET A 1 240 ? -1.644  -9.865  4.839   1.00 12.06  ? 241 MET A CA  1 
ATOM   1955 C  C   . MET A 1 240 ? -2.421  -10.786 5.788   1.00 10.80  ? 241 MET A C   1 
ATOM   1956 O  O   . MET A 1 240 ? -3.631  -10.956 5.657   1.00 11.84  ? 241 MET A O   1 
ATOM   1957 C  CB  . MET A 1 240 ? -2.519  -8.664  4.421   1.00 12.39  ? 241 MET A CB  1 
ATOM   1958 C  CG  . MET A 1 240 ? -2.821  -7.622  5.596   1.00 11.98  ? 241 MET A CG  1 
ATOM   1959 S  SD  . MET A 1 240 ? -3.826  -6.243  5.020   1.00 12.90  ? 241 MET A SD  1 
ATOM   1960 C  CE  . MET A 1 240 ? -2.498  -5.165  4.414   1.00 13.73  ? 241 MET A CE  1 
ATOM   1961 N  N   . VAL A 1 241 ? -1.663  -11.406 6.705   1.00 11.41  ? 242 VAL A N   1 
ATOM   1962 C  CA  . VAL A 1 241 ? -2.234  -12.309 7.739   1.00 11.06  ? 242 VAL A CA  1 
ATOM   1963 C  C   . VAL A 1 241 ? -1.420  -12.083 9.029   1.00 10.32  ? 242 VAL A C   1 
ATOM   1964 O  O   . VAL A 1 241 ? -0.268  -11.630 8.973   1.00 10.77  ? 242 VAL A O   1 
ATOM   1965 C  CB  . VAL A 1 241 ? -2.193  -13.833 7.372   1.00 11.93  ? 242 VAL A CB  1 
ATOM   1966 C  CG1 . VAL A 1 241 ? -3.099  -14.140 6.195   1.00 11.83  ? 242 VAL A CG1 1 
ATOM   1967 C  CG2 . VAL A 1 241 ? -0.754  -14.348 7.113   1.00 12.69  ? 242 VAL A CG2 1 
ATOM   1968 N  N   . ASP A 1 242 ? -2.054  -12.349 10.201  1.00 10.00  ? 243 ASP A N   1 
ATOM   1969 C  CA  . ASP A 1 242 ? -1.319  -12.212 11.466  1.00 9.70   ? 243 ASP A CA  1 
ATOM   1970 C  C   . ASP A 1 242 ? -0.838  -10.766 11.676  1.00 9.55   ? 243 ASP A C   1 
ATOM   1971 O  O   . ASP A 1 242 ? 0.275   -10.552 12.190  1.00 10.32  ? 243 ASP A O   1 
ATOM   1972 C  CB  . ASP A 1 242 ? -0.198  -13.280 11.663  1.00 9.99   ? 243 ASP A CB  1 
ATOM   1973 C  CG  . ASP A 1 242 ? -0.827  -14.660 11.743  1.00 10.42  ? 243 ASP A CG  1 
ATOM   1974 O  OD1 . ASP A 1 242 ? -1.855  -14.848 12.437  1.00 10.87  ? 243 ASP A OD1 1 
ATOM   1975 O  OD2 . ASP A 1 242 ? -0.259  -15.594 11.157  1.00 12.19  ? 243 ASP A OD2 1 
ATOM   1976 N  N   . ASN A 1 243 ? -1.758  -9.799  11.418  1.00 9.13   ? 244 ASN A N   1 
ATOM   1977 C  CA  . ASN A 1 243 ? -1.403  -8.370  11.604  1.00 9.60   ? 244 ASN A CA  1 
ATOM   1978 C  C   . ASN A 1 243 ? -1.964  -7.895  12.951  1.00 8.48   ? 244 ASN A C   1 
ATOM   1979 O  O   . ASN A 1 243 ? -2.641  -6.863  13.051  1.00 9.37   ? 244 ASN A O   1 
ATOM   1980 C  CB  . ASN A 1 243 ? -1.964  -7.493  10.473  1.00 9.95   ? 244 ASN A CB  1 
ATOM   1981 C  CG  . ASN A 1 243 ? -3.462  -7.656  10.228  1.00 10.46  ? 244 ASN A CG  1 
ATOM   1982 O  OD1 . ASN A 1 243 ? -4.116  -8.526  10.815  1.00 9.97   ? 244 ASN A OD1 1 
ATOM   1983 N  ND2 . ASN A 1 243 ? -4.031  -6.825  9.387   1.00 15.06  ? 244 ASN A ND2 1 
ATOM   1984 N  N   . TRP A 1 244 ? -1.690  -8.680  14.032  1.00 9.44   ? 245 TRP A N   1 
ATOM   1985 C  CA  . TRP A 1 244 ? -2.135  -8.423  15.407  1.00 8.66   ? 245 TRP A CA  1 
ATOM   1986 C  C   . TRP A 1 244 ? -0.937  -8.299  16.340  1.00 8.44   ? 245 TRP A C   1 
ATOM   1987 O  O   . TRP A 1 244 ? 0.047   -9.050  16.199  1.00 9.79   ? 245 TRP A O   1 
ATOM   1988 C  CB  . TRP A 1 244 ? -3.121  -9.523  15.866  1.00 8.82   ? 245 TRP A CB  1 
ATOM   1989 C  CG  . TRP A 1 244 ? -2.642  -10.956 15.719  1.00 8.69   ? 245 TRP A CG  1 
ATOM   1990 C  CD1 . TRP A 1 244 ? -2.771  -11.706 14.593  1.00 9.14   ? 245 TRP A CD1 1 
ATOM   1991 C  CD2 . TRP A 1 244 ? -2.034  -11.797 16.706  1.00 8.50   ? 245 TRP A CD2 1 
ATOM   1992 N  NE1 . TRP A 1 244 ? -2.240  -12.979 14.795  1.00 9.40   ? 245 TRP A NE1 1 
ATOM   1993 C  CE2 . TRP A 1 244 ? -1.766  -13.045 16.091  1.00 9.12   ? 245 TRP A CE2 1 
ATOM   1994 C  CE3 . TRP A 1 244 ? -1.710  -11.648 18.074  1.00 10.12  ? 245 TRP A CE3 1 
ATOM   1995 C  CZ2 . TRP A 1 244 ? -1.167  -14.118 16.784  1.00 10.53  ? 245 TRP A CZ2 1 
ATOM   1996 C  CZ3 . TRP A 1 244 ? -1.121  -12.686 18.755  1.00 11.56  ? 245 TRP A CZ3 1 
ATOM   1997 C  CH2 . TRP A 1 244 ? -0.861  -13.940 18.133  1.00 11.01  ? 245 TRP A CH2 1 
ATOM   1998 N  N   . ARG A 1 245 ? -1.064  -7.381  17.301  1.00 8.59   ? 246 ARG A N   1 
ATOM   1999 C  CA  . ARG A 1 245 ? -0.102  -7.280  18.404  1.00 9.94   ? 246 ARG A CA  1 
ATOM   2000 C  C   . ARG A 1 245 ? -0.589  -8.183  19.565  1.00 9.52   ? 246 ARG A C   1 
ATOM   2001 O  O   . ARG A 1 245 ? -1.790  -8.200  19.872  1.00 9.93   ? 246 ARG A O   1 
ATOM   2002 C  CB  . ARG A 1 245 ? -0.053  -5.808  18.906  1.00 9.57   ? 246 ARG A CB  1 
ATOM   2003 C  CG  . ARG A 1 245 ? 1.103   -5.576  19.888  1.00 9.48   ? 246 ARG A CG  1 
ATOM   2004 C  CD  . ARG A 1 245 ? 0.976   -4.216  20.565  1.00 9.78   ? 246 ARG A CD  1 
ATOM   2005 N  NE  . ARG A 1 245 ? 2.235   -3.915  21.267  1.00 9.62   ? 246 ARG A NE  1 
ATOM   2006 C  CZ  . ARG A 1 245 ? 2.439   -2.927  22.115  1.00 9.50   ? 246 ARG A CZ  1 
ATOM   2007 N  NH1 . ARG A 1 245 ? 1.457   -2.111  22.514  1.00 9.49   ? 246 ARG A NH1 1 
ATOM   2008 N  NH2 . ARG A 1 245 ? 3.680   -2.688  22.606  1.00 10.53  ? 246 ARG A NH2 1 
ATOM   2009 N  N   A PRO A 1 246 ? 0.302   -9.031  20.147  0.50 9.41   ? 247 PRO A N   1 
ATOM   2010 N  N   B PRO A 1 246 ? 0.324   -8.935  20.217  0.50 9.28   ? 247 PRO A N   1 
ATOM   2011 C  CA  A PRO A 1 246 ? -0.111  -9.836  21.302  0.50 8.99   ? 247 PRO A CA  1 
ATOM   2012 C  CA  B PRO A 1 246 ? -0.153  -9.815  21.284  0.50 9.12   ? 247 PRO A CA  1 
ATOM   2013 C  C   A PRO A 1 246 ? -0.485  -8.979  22.538  0.50 9.31   ? 247 PRO A C   1 
ATOM   2014 C  C   B PRO A 1 246 ? -0.480  -8.980  22.545  0.50 9.59   ? 247 PRO A C   1 
ATOM   2015 O  O   A PRO A 1 246 ? -0.128  -7.789  22.649  0.50 9.66   ? 247 PRO A O   1 
ATOM   2016 O  O   B PRO A 1 246 ? -0.098  -7.799  22.669  0.50 9.78   ? 247 PRO A O   1 
ATOM   2017 C  CB  A PRO A 1 246 ? 1.154   -10.708 21.597  0.50 10.40  ? 247 PRO A CB  1 
ATOM   2018 C  CB  B PRO A 1 246 ? 1.047   -10.779 21.480  0.50 11.42  ? 247 PRO A CB  1 
ATOM   2019 C  CG  A PRO A 1 246 ? 1.956   -10.728 20.291  0.50 10.68  ? 247 PRO A CG  1 
ATOM   2020 C  CG  B PRO A 1 246 ? 2.267   -9.978  21.035  0.50 13.18  ? 247 PRO A CG  1 
ATOM   2021 C  CD  A PRO A 1 246 ? 1.694   -9.351  19.704  0.50 10.23  ? 247 PRO A CD  1 
ATOM   2022 C  CD  B PRO A 1 246 ? 1.798   -9.004  19.968  0.50 11.25  ? 247 PRO A CD  1 
ATOM   2023 N  N   . ALA A 1 247 ? -1.114  -9.641  23.509  1.00 9.46   ? 248 ALA A N   1 
ATOM   2024 C  CA  . ALA A 1 247 ? -1.483  -8.983  24.768  1.00 9.16   ? 248 ALA A CA  1 
ATOM   2025 C  C   . ALA A 1 247 ? -0.245  -8.478  25.508  1.00 9.57   ? 248 ALA A C   1 
ATOM   2026 O  O   . ALA A 1 247 ? 0.796   -9.200  25.544  1.00 10.98  ? 248 ALA A O   1 
ATOM   2027 C  CB  . ALA A 1 247 ? -2.248  -10.003 25.627  1.00 11.31  ? 248 ALA A CB  1 
ATOM   2028 N  N   . GLN A 1 248 ? -0.396  -7.278  26.100  1.00 9.18   ? 249 GLN A N   1 
ATOM   2029 C  CA  . GLN A 1 248 ? 0.673   -6.593  26.833  1.00 9.99   ? 249 GLN A CA  1 
ATOM   2030 C  C   . GLN A 1 248 ? 0.361   -6.614  28.333  1.00 11.19  ? 249 GLN A C   1 
ATOM   2031 O  O   . GLN A 1 248 ? -0.814  -6.811  28.771  1.00 12.23  ? 249 GLN A O   1 
ATOM   2032 C  CB  . GLN A 1 248 ? 0.800   -5.154  26.303  1.00 10.62  ? 249 GLN A CB  1 
ATOM   2033 C  CG  . GLN A 1 248 ? 1.079   -5.087  24.810  1.00 10.02  ? 249 GLN A CG  1 
ATOM   2034 C  CD  . GLN A 1 248 ? 2.381   -5.789  24.512  1.00 11.58  ? 249 GLN A CD  1 
ATOM   2035 O  OE1 . GLN A 1 248 ? 3.417   -5.469  25.133  1.00 13.32  ? 249 GLN A OE1 1 
ATOM   2036 N  NE2 . GLN A 1 248 ? 2.371   -6.693  23.531  1.00 11.95  ? 249 GLN A NE2 1 
ATOM   2037 N  N   . PRO A 1 249 ? 1.362   -6.321  29.185  1.00 11.76  ? 250 PRO A N   1 
ATOM   2038 C  CA  . PRO A 1 249 ? 1.143   -6.379  30.635  1.00 13.90  ? 250 PRO A CA  1 
ATOM   2039 C  C   . PRO A 1 249 ? 0.076   -5.358  31.083  1.00 11.69  ? 250 PRO A C   1 
ATOM   2040 O  O   . PRO A 1 249 ? 0.117   -4.161  30.714  1.00 11.55  ? 250 PRO A O   1 
ATOM   2041 C  CB  . PRO A 1 249 ? 2.535   -5.957  31.148  1.00 15.64  ? 250 PRO A CB  1 
ATOM   2042 C  CG  . PRO A 1 249 ? 3.496   -6.461  30.135  1.00 15.43  ? 250 PRO A CG  1 
ATOM   2043 C  CD  . PRO A 1 249 ? 2.793   -6.097  28.832  1.00 15.44  ? 250 PRO A CD  1 
ATOM   2044 N  N   . LEU A 1 250 ? -0.836  -5.837  31.963  1.00 12.27  ? 251 LEU A N   1 
ATOM   2045 C  CA  . LEU A 1 250 ? -1.924  -4.956  32.415  1.00 12.30  ? 251 LEU A CA  1 
ATOM   2046 C  C   . LEU A 1 250 ? -1.352  -3.837  33.334  1.00 12.64  ? 251 LEU A C   1 
ATOM   2047 O  O   . LEU A 1 250 ? -1.914  -2.730  33.425  1.00 12.17  ? 251 LEU A O   1 
ATOM   2048 C  CB  . LEU A 1 250 ? -2.986  -5.828  33.106  1.00 13.19  ? 251 LEU A CB  1 
ATOM   2049 C  CG  . LEU A 1 250 ? -4.232  -5.049  33.532  1.00 14.11  ? 251 LEU A CG  1 
ATOM   2050 C  CD1 . LEU A 1 250 ? -4.960  -4.432  32.296  1.00 14.19  ? 251 LEU A CD1 1 
ATOM   2051 C  CD2 . LEU A 1 250 ? -5.133  -5.998  34.359  1.00 16.85  ? 251 LEU A CD2 1 
ATOM   2052 N  N   . LYS A 1 251 ? -0.298  -4.140  34.114  1.00 13.30  ? 252 LYS A N   1 
ATOM   2053 C  CA  . LYS A 1 251 ? 0.304   -3.145  35.003  1.00 15.16  ? 252 LYS A CA  1 
ATOM   2054 C  C   . LYS A 1 251 ? -0.751  -2.593  35.977  1.00 17.37  ? 252 LYS A C   1 
ATOM   2055 O  O   . LYS A 1 251 ? -1.532  -3.364  36.549  1.00 18.82  ? 252 LYS A O   1 
ATOM   2056 C  CB  . LYS A 1 251 ? 1.102   -2.103  34.226  1.00 16.54  ? 252 LYS A CB  1 
ATOM   2057 C  CG  . LYS A 1 251 ? 2.253   -2.806  33.515  1.00 21.41  ? 252 LYS A CG  1 
ATOM   2058 C  CD  . LYS A 1 251 ? 3.376   -1.938  33.139  1.00 29.02  ? 252 LYS A CD  1 
ATOM   2059 C  CE  . LYS A 1 251 ? 4.571   -2.764  32.784  1.00 32.41  ? 252 LYS A CE  1 
ATOM   2060 N  NZ  . LYS A 1 251 ? 5.136   -2.014  31.640  1.00 37.25  ? 252 LYS A NZ  1 
ATOM   2061 N  N   . ASN A 1 252 ? -0.678  -1.292  36.235  1.00 16.26  ? 253 ASN A N   1 
ATOM   2062 C  CA  . ASN A 1 252 ? -1.486  -0.748  37.297  1.00 23.72  ? 253 ASN A CA  1 
ATOM   2063 C  C   . ASN A 1 252 ? -2.820  -0.299  36.682  1.00 25.36  ? 253 ASN A C   1 
ATOM   2064 O  O   . ASN A 1 252 ? -3.021  0.971   36.692  1.00 24.59  ? 253 ASN A O   1 
ATOM   2065 C  CB  . ASN A 1 252 ? -0.741  0.414   37.993  1.00 34.64  ? 253 ASN A CB  1 
ATOM   2066 C  CG  . ASN A 1 252 ? -1.387  0.903   39.285  1.00 41.81  ? 253 ASN A CG  1 
ATOM   2067 O  OD1 . ASN A 1 252 ? -1.523  0.131   40.242  1.00 71.73  ? 253 ASN A OD1 1 
ATOM   2068 N  ND2 . ASN A 1 252 ? -1.770  2.189   39.334  1.00 39.22  ? 253 ASN A ND2 1 
ATOM   2069 N  N   . ARG A 1 253 ? -3.627  -1.300  36.114  1.00 15.75  ? 254 ARG A N   1 
ATOM   2070 C  CA  . ARG A 1 253 ? -4.917  -0.974  35.526  1.00 11.44  ? 254 ARG A CA  1 
ATOM   2071 C  C   . ARG A 1 253 ? -6.020  -1.920  35.983  1.00 13.40  ? 254 ARG A C   1 
ATOM   2072 O  O   . ARG A 1 253 ? -5.732  -3.079  36.286  1.00 18.33  ? 254 ARG A O   1 
ATOM   2073 C  CB  . ARG A 1 253 ? -4.844  -0.919  33.978  1.00 11.56  ? 254 ARG A CB  1 
ATOM   2074 C  CG  . ARG A 1 253 ? -3.956  0.236   33.513  1.00 10.93  ? 254 ARG A CG  1 
ATOM   2075 C  CD  . ARG A 1 253 ? -3.841  0.186   31.996  1.00 10.71  ? 254 ARG A CD  1 
ATOM   2076 N  NE  . ARG A 1 253 ? -3.003  -0.959  31.555  1.00 9.80   ? 254 ARG A NE  1 
ATOM   2077 C  CZ  . ARG A 1 253 ? -2.738  -1.224  30.251  1.00 9.52   ? 254 ARG A CZ  1 
ATOM   2078 N  NH1 . ARG A 1 253 ? -3.367  -0.555  29.270  1.00 9.80   ? 254 ARG A NH1 1 
ATOM   2079 N  NH2 . ARG A 1 253 ? -1.931  -2.240  29.912  1.00 9.00   ? 254 ARG A NH2 1 
ATOM   2080 N  N   . GLN A 1 254 ? -7.257  -1.371  35.981  1.00 12.50  ? 255 GLN A N   1 
ATOM   2081 C  CA  . GLN A 1 254 ? -8.460  -2.160  36.228  1.00 14.70  ? 255 GLN A CA  1 
ATOM   2082 C  C   . GLN A 1 254 ? -9.283  -2.196  34.950  1.00 14.72  ? 255 GLN A C   1 
ATOM   2083 O  O   . GLN A 1 254 ? -9.491  -1.155  34.279  1.00 16.19  ? 255 GLN A O   1 
ATOM   2084 C  CB  . GLN A 1 254 ? -9.274  -1.637  37.425  1.00 18.72  ? 255 GLN A CB  1 
ATOM   2085 C  CG  . GLN A 1 254 ? -8.489  -1.897  38.732  1.00 25.85  ? 255 GLN A CG  1 
ATOM   2086 C  CD  . GLN A 1 254 ? -9.376  -1.815  39.943  1.00 36.76  ? 255 GLN A CD  1 
ATOM   2087 O  OE1 . GLN A 1 254 ? -10.231 -0.934  40.035  1.00 49.86  ? 255 GLN A OE1 1 
ATOM   2088 N  NE2 . GLN A 1 254 ? -9.223  -2.729  40.903  1.00 37.81  ? 255 GLN A NE2 1 
ATOM   2089 N  N   . ILE A 1 255 ? -9.771  -3.402  34.656  1.00 11.02  ? 256 ILE A N   1 
ATOM   2090 C  CA  . ILE A 1 255 ? -10.739 -3.528  33.558  1.00 11.37  ? 256 ILE A CA  1 
ATOM   2091 C  C   . ILE A 1 255 ? -12.128 -3.580  34.204  1.00 11.33  ? 256 ILE A C   1 
ATOM   2092 O  O   . ILE A 1 255 ? -12.388 -4.362  35.172  1.00 11.90  ? 256 ILE A O   1 
ATOM   2093 C  CB  . ILE A 1 255 ? -10.475 -4.833  32.761  1.00 11.60  ? 256 ILE A CB  1 
ATOM   2094 C  CG1 . ILE A 1 255 ? -9.036  -4.798  32.172  1.00 12.68  ? 256 ILE A CG1 1 
ATOM   2095 C  CG2 . ILE A 1 255 ? -11.508 -4.996  31.638  1.00 13.10  ? 256 ILE A CG2 1 
ATOM   2096 C  CD1 . ILE A 1 255 ? -8.698  -6.020  31.339  1.00 13.46  ? 256 ILE A CD1 1 
ATOM   2097 N  N   . LYS A 1 256 ? -13.056 -2.735  33.713  1.00 10.14  ? 257 LYS A N   1 
ATOM   2098 C  CA  . LYS A 1 256 ? -14.405 -2.616  34.322  1.00 10.08  ? 257 LYS A CA  1 
ATOM   2099 C  C   . LYS A 1 256 ? -15.415 -3.205  33.360  1.00 9.84   ? 257 LYS A C   1 
ATOM   2100 O  O   . LYS A 1 256 ? -15.240 -3.091  32.141  1.00 11.98  ? 257 LYS A O   1 
ATOM   2101 C  CB  . LYS A 1 256 ? -14.771 -1.137  34.630  1.00 12.27  ? 257 LYS A CB  1 
ATOM   2102 C  CG  . LYS A 1 256 ? -13.757 -0.577  35.660  1.00 15.66  ? 257 LYS A CG  1 
ATOM   2103 C  CD  . LYS A 1 256 ? -13.916 0.804   36.042  1.00 22.72  ? 257 LYS A CD  1 
ATOM   2104 C  CE  . LYS A 1 256 ? -12.878 1.246   37.062  1.00 32.65  ? 257 LYS A CE  1 
ATOM   2105 N  NZ  . LYS A 1 256 ? -12.862 2.741   37.213  1.00 35.67  ? 257 LYS A NZ  1 
ATOM   2106 N  N   . ALA A 1 257 ? -16.418 -3.906  33.902  1.00 10.66  ? 258 ALA A N   1 
ATOM   2107 C  CA  . ALA A 1 257 ? -17.506 -4.500  33.135  1.00 11.41  ? 258 ALA A CA  1 
ATOM   2108 C  C   . ALA A 1 257 ? -18.754 -3.627  33.232  1.00 10.47  ? 258 ALA A C   1 
ATOM   2109 O  O   . ALA A 1 257 ? -19.122 -3.192  34.341  1.00 12.43  ? 258 ALA A O   1 
ATOM   2110 C  CB  . ALA A 1 257 ? -17.734 -5.937  33.594  1.00 13.56  ? 258 ALA A CB  1 
ATOM   2111 N  N   . SER A 1 258 ? -19.504 -3.485  32.114  1.00 11.23  ? 259 SER A N   1 
ATOM   2112 C  CA  . SER A 1 258 ? -20.763 -2.712  32.107  1.00 12.99  ? 259 SER A CA  1 
ATOM   2113 C  C   . SER A 1 258 ? -21.955 -3.570  32.566  1.00 13.86  ? 259 SER A C   1 
ATOM   2114 O  O   . SER A 1 258 ? -23.063 -2.991  32.658  1.00 17.45  ? 259 SER A O   1 
ATOM   2115 C  CB  . SER A 1 258 ? -21.024 -2.224  30.695  1.00 14.77  ? 259 SER A CB  1 
ATOM   2116 O  OG  . SER A 1 258 ? -21.469 -3.297  29.840  1.00 12.16  ? 259 SER A OG  1 
ATOM   2117 N  N   . PHE A 1 259 ? -21.739 -4.871  32.808  1.00 13.66  ? 260 PHE A N   1 
ATOM   2118 C  CA  . PHE A 1 259 ? -22.812 -5.856  32.997  1.00 15.92  ? 260 PHE A CA  1 
ATOM   2119 C  C   . PHE A 1 259 ? -22.503 -6.758  34.185  1.00 22.40  ? 260 PHE A C   1 
ATOM   2120 O  O   . PHE A 1 259 ? -21.334 -6.906  34.600  1.00 20.77  ? 260 PHE A O   1 
ATOM   2121 C  CB  . PHE A 1 259 ? -22.958 -6.754  31.749  1.00 15.82  ? 260 PHE A CB  1 
ATOM   2122 C  CG  . PHE A 1 259 ? -21.667 -7.494  31.413  1.00 15.73  ? 260 PHE A CG  1 
ATOM   2123 C  CD1 . PHE A 1 259 ? -20.673 -6.859  30.649  1.00 13.25  ? 260 PHE A CD1 1 
ATOM   2124 C  CD2 . PHE A 1 259 ? -21.410 -8.778  31.934  1.00 19.34  ? 260 PHE A CD2 1 
ATOM   2125 C  CE1 . PHE A 1 259 ? -19.456 -7.485  30.437  1.00 14.45  ? 260 PHE A CE1 1 
ATOM   2126 C  CE2 . PHE A 1 259 ? -20.170 -9.385  31.717  1.00 21.48  ? 260 PHE A CE2 1 
ATOM   2127 C  CZ  . PHE A 1 259 ? -19.217 -8.762  30.932  1.00 18.34  ? 260 PHE A CZ  1 
ATOM   2128 N  N   . LYS A 1 260 ? -23.605 -7.370  34.655  1.00 33.57  ? 261 LYS A N   1 
ATOM   2129 C  CA  . LYS A 1 260 ? -23.702 -8.399  35.727  1.00 41.10  ? 261 LYS A CA  1 
ATOM   2130 C  C   . LYS A 1 260 ? -23.989 -7.796  37.109  1.00 53.88  ? 261 LYS A C   1 
ATOM   2131 O  O   . LYS A 1 260 ? -24.836 -6.937  37.364  0.01 61.14  ? 261 LYS A O   1 
ATOM   2132 C  CB  . LYS A 1 260 ? -22.423 -9.242  35.767  1.00 48.79  ? 261 LYS A CB  1 
ATOM   2133 O  OXT . LYS A 1 260 ? -23.275 -8.218  37.988  1.00 76.00  ? 261 LYS A OXT 1 
HETATM 2134 ZN ZN  . ZN  B 2 .   ? -6.656  -1.779  15.389  1.00 7.57   ? 301 ZN  A ZN  1 
HETATM 2135 O  O13 . EA3 C 3 .   ? -4.732  2.758   11.405  1.00 10.75  ? 302 EA3 A O13 1 
HETATM 2136 C  C12 . EA3 C 3 .   ? -4.023  2.610   12.443  1.00 10.08  ? 302 EA3 A C12 1 
HETATM 2137 N  N14 . EA3 C 3 .   ? -2.838  2.013   12.461  1.00 11.11  ? 302 EA3 A N14 1 
HETATM 2138 C  C15 . EA3 C 3 .   ? -2.166  1.548   11.170  1.00 14.28  ? 302 EA3 A C15 1 
HETATM 2139 C  C16 . EA3 C 3 .   ? -0.736  2.057   11.086  1.00 19.45  ? 302 EA3 A C16 1 
HETATM 2140 O  O17 . EA3 C 3 .   ? -0.651  3.438   11.137  1.00 21.84  ? 302 EA3 A O17 1 
HETATM 2141 C  C9  . EA3 C 3 .   ? -4.567  2.929   13.759  1.00 9.63   ? 302 EA3 A C9  1 
HETATM 2142 C  C10 . EA3 C 3 .   ? -4.903  1.882   14.665  1.00 8.07   ? 302 EA3 A C10 1 
HETATM 2143 C  C3  . EA3 C 3 .   ? -5.503  2.111   15.878  1.00 8.05   ? 302 EA3 A C3  1 
HETATM 2144 S  S2  . EA3 C 3 .   ? -5.942  0.747   16.942  1.00 8.10   ? 302 EA3 A S2  1 
HETATM 2145 O  O4  . EA3 C 3 .   ? -7.455  0.720   16.902  1.00 8.49   ? 302 EA3 A O4  1 
HETATM 2146 O  O5  . EA3 C 3 .   ? -5.289  0.964   18.258  1.00 7.60   ? 302 EA3 A O5  1 
HETATM 2147 N  N1  . EA3 C 3 .   ? -5.304  -0.567  16.210  1.00 7.14   ? 302 EA3 A N1  1 
HETATM 2148 C  C8  . EA3 C 3 .   ? -5.037  4.216   14.103  1.00 8.65   ? 302 EA3 A C8  1 
HETATM 2149 C  C7  . EA3 C 3 .   ? -5.633  4.504   15.317  1.00 9.17   ? 302 EA3 A C7  1 
HETATM 2150 C  C6  . EA3 C 3 .   ? -5.926  3.419   16.186  1.00 9.13   ? 302 EA3 A C6  1 
HETATM 2151 CL CL1 . EA3 C 3 .   ? -6.774  3.816   17.646  1.00 9.34   ? 302 EA3 A CL1 1 
HETATM 2152 S  S18 . EA3 C 3 .   ? -4.726  5.654   13.004  1.00 11.36  ? 302 EA3 A S18 1 
HETATM 2153 C  C19 . EA3 C 3 .   ? -2.916  5.740   12.881  1.00 21.84  ? 302 EA3 A C19 1 
HETATM 2154 C  C24 . EA3 C 3 .   ? -2.297  5.890   14.291  1.00 25.67  ? 302 EA3 A C24 1 
HETATM 2155 C  C23 . EA3 C 3 .   ? -1.944  7.328   14.639  1.00 21.84  ? 302 EA3 A C23 1 
HETATM 2156 C  C22 . EA3 C 3 .   ? -1.372  8.154   13.415  1.00 22.32  ? 302 EA3 A C22 1 
HETATM 2157 C  C21 . EA3 C 3 .   ? -2.442  8.109   12.287  1.00 22.49  ? 302 EA3 A C21 1 
HETATM 2158 C  C20 . EA3 C 3 .   ? -2.487  6.698   11.759  1.00 19.65  ? 302 EA3 A C20 1 
HETATM 2159 S  S   . DMS D 4 .   ? 1.414   -11.754 15.121  1.00 31.02  ? 303 DMS A S   1 
HETATM 2160 O  O   . DMS D 4 .   ? 2.470   -10.884 14.252  1.00 43.46  ? 303 DMS A O   1 
HETATM 2161 C  C1  . DMS D 4 .   ? 1.827   -11.609 16.852  1.00 36.40  ? 303 DMS A C1  1 
HETATM 2162 C  C2  . DMS D 4 .   ? 1.906   -13.492 14.781  1.00 34.93  ? 303 DMS A C2  1 
HETATM 2163 O  O   . HOH E 5 .   ? 12.503  -0.168  12.155  1.00 47.03  ? 401 HOH A O   1 
HETATM 2164 O  O   . HOH E 5 .   ? -25.860 -10.993 17.620  1.00 29.59  ? 402 HOH A O   1 
HETATM 2165 O  O   . HOH E 5 .   ? -21.061 -7.389  -2.036  1.00 40.93  ? 403 HOH A O   1 
HETATM 2166 O  O   . HOH E 5 .   ? -11.039 -15.404 34.404  1.00 28.32  ? 404 HOH A O   1 
HETATM 2167 O  O   . HOH E 5 .   ? -10.693 -5.823  38.477  1.00 35.36  ? 405 HOH A O   1 
HETATM 2168 O  O   . HOH E 5 .   ? -6.429  -11.537 36.786  1.00 37.59  ? 406 HOH A O   1 
HETATM 2169 O  O   . HOH E 5 .   ? 4.444   -2.667  29.369  1.00 24.52  ? 407 HOH A O   1 
HETATM 2170 O  O   . HOH E 5 .   ? 15.118  -7.217  12.463  1.00 42.98  ? 408 HOH A O   1 
HETATM 2171 O  O   . HOH E 5 .   ? -10.519 3.372   37.685  1.00 43.35  ? 409 HOH A O   1 
HETATM 2172 O  O   . HOH E 5 .   ? -15.611 -1.164  43.801  1.00 37.50  ? 410 HOH A O   1 
HETATM 2173 O  O   . HOH E 5 .   ? -0.698  -17.665 18.235  1.00 33.39  ? 411 HOH A O   1 
HETATM 2174 O  O   . HOH E 5 .   ? -24.124 8.710   20.339  1.00 21.42  ? 412 HOH A O   1 
HETATM 2175 O  O   . HOH E 5 .   ? 9.784   7.434   17.897  1.00 52.95  ? 413 HOH A O   1 
HETATM 2176 O  O   . HOH E 5 .   ? -15.836 3.704   35.544  1.00 32.23  ? 414 HOH A O   1 
HETATM 2177 O  O   . HOH E 5 .   ? -6.319  -4.926  -6.399  1.00 23.24  ? 415 HOH A O   1 
HETATM 2178 O  O   . HOH E 5 .   ? 1.368   4.610   12.246  1.00 20.42  ? 416 HOH A O   1 
HETATM 2179 O  O   . HOH E 5 .   ? -19.532 -21.143 5.145   1.00 27.57  ? 417 HOH A O   1 
HETATM 2180 O  O   . HOH E 5 .   ? -12.222 4.411   35.332  1.00 42.82  ? 418 HOH A O   1 
HETATM 2181 O  O   . HOH E 5 .   ? -7.142  5.889   6.046   1.00 16.14  ? 419 HOH A O   1 
HETATM 2182 O  O   . HOH E 5 .   ? -18.964 17.721  18.766  1.00 39.71  ? 420 HOH A O   1 
HETATM 2183 O  O   . HOH E 5 .   ? -8.743  -3.913  7.956   1.00 9.68   ? 421 HOH A O   1 
HETATM 2184 O  O   . HOH E 5 .   ? 0.384   -9.808  -5.382  1.00 37.67  ? 422 HOH A O   1 
HETATM 2185 O  O   . HOH E 5 .   ? 5.405   -11.099 19.177  1.00 29.85  ? 423 HOH A O   1 
HETATM 2186 O  O   . HOH E 5 .   ? 11.450  -7.230  22.599  1.00 26.77  ? 424 HOH A O   1 
HETATM 2187 O  O   . HOH E 5 .   ? -25.521 9.616   13.303  1.00 27.94  ? 425 HOH A O   1 
HETATM 2188 O  O   . HOH E 5 .   ? -9.898  1.579   39.331  1.00 31.97  ? 426 HOH A O   1 
HETATM 2189 O  O   . HOH E 5 .   ? -1.189  -4.102  15.858  1.00 9.59   ? 427 HOH A O   1 
HETATM 2190 O  O   . HOH E 5 .   ? -20.062 -17.056 3.120   1.00 22.97  ? 428 HOH A O   1 
HETATM 2191 O  O   . HOH E 5 .   ? 6.553   -7.816  -10.550 1.00 31.56  ? 429 HOH A O   1 
HETATM 2192 O  O   . HOH E 5 .   ? -25.893 -15.360 8.265   1.00 37.90  ? 430 HOH A O   1 
HETATM 2193 O  O   . HOH E 5 .   ? 4.762   -1.338  -5.481  1.00 34.64  ? 431 HOH A O   1 
HETATM 2194 O  O   . HOH E 5 .   ? -12.348 12.536  29.515  1.00 35.77  ? 432 HOH A O   1 
HETATM 2195 O  O   . HOH E 5 .   ? -3.206  18.157  14.221  1.00 31.22  ? 433 HOH A O   1 
HETATM 2196 O  O   . HOH E 5 .   ? -25.976 -5.643  13.522  1.00 40.77  ? 434 HOH A O   1 
HETATM 2197 O  O   . HOH E 5 .   ? 2.646   -14.787 -5.528  1.00 42.49  ? 435 HOH A O   1 
HETATM 2198 O  O   . HOH E 5 .   ? -4.836  -12.072 32.344  1.00 20.38  ? 436 HOH A O   1 
HETATM 2199 O  O   . HOH E 5 .   ? -24.049 -3.090  29.235  1.00 35.60  ? 437 HOH A O   1 
HETATM 2200 O  O   . HOH E 5 .   ? -10.611 8.733   25.599  1.00 9.82   ? 438 HOH A O   1 
HETATM 2201 O  O   . HOH E 5 .   ? -1.408  9.051   28.433  1.00 30.54  ? 439 HOH A O   1 
HETATM 2202 O  O   . HOH E 5 .   ? -23.270 0.326   34.797  1.00 35.80  ? 440 HOH A O   1 
HETATM 2203 O  O   . HOH E 5 .   ? 0.521   7.142   30.073  1.00 51.11  ? 441 HOH A O   1 
HETATM 2204 O  O   . HOH E 5 .   ? -25.833 -0.928  35.217  1.00 34.57  ? 442 HOH A O   1 
HETATM 2205 O  O   . HOH E 5 .   ? -17.726 6.333   38.636  1.00 33.91  ? 443 HOH A O   1 
HETATM 2206 O  O   . HOH E 5 .   ? 11.586  -0.527  16.146  1.00 29.55  ? 444 HOH A O   1 
HETATM 2207 O  O   . HOH E 5 .   ? -7.747  -4.899  40.369  1.00 28.50  ? 445 HOH A O   1 
HETATM 2208 O  O   . HOH E 5 .   ? -27.150 -8.067  26.505  1.00 50.14  ? 446 HOH A O   1 
HETATM 2209 O  O   . HOH E 5 .   ? -1.900  -4.890  -7.002  1.00 27.81  ? 447 HOH A O   1 
HETATM 2210 O  O   . HOH E 5 .   ? 6.116   -11.325 15.731  1.00 34.79  ? 448 HOH A O   1 
HETATM 2211 O  O   . HOH E 5 .   ? 3.682   5.001   30.086  1.00 16.94  ? 449 HOH A O   1 
HETATM 2212 O  O   . HOH E 5 .   ? -10.414 -18.489 17.391  1.00 12.56  ? 450 HOH A O   1 
HETATM 2213 O  O   . HOH E 5 .   ? -11.072 -19.941 7.631   1.00 29.24  ? 451 HOH A O   1 
HETATM 2214 O  O   . HOH E 5 .   ? -21.239 7.775   1.886   1.00 20.82  ? 452 HOH A O   1 
HETATM 2215 O  O   . HOH E 5 .   ? -0.152  1.049   34.709  1.00 28.85  ? 453 HOH A O   1 
HETATM 2216 O  O   . HOH E 5 .   ? -2.912  -19.860 6.408   1.00 31.28  ? 454 HOH A O   1 
HETATM 2217 O  O   . HOH E 5 .   ? -27.912 6.248   21.713  1.00 26.43  ? 455 HOH A O   1 
HETATM 2218 O  O   . HOH E 5 .   ? 4.744   -3.655  3.128   1.00 28.90  ? 456 HOH A O   1 
HETATM 2219 O  O   . HOH E 5 .   ? -6.708  21.232  19.731  1.00 13.45  ? 457 HOH A O   1 
HETATM 2220 O  O   . HOH E 5 .   ? -18.024 10.606  11.368  1.00 19.76  ? 458 HOH A O   1 
HETATM 2221 O  O   . HOH E 5 .   ? 2.478   -13.456 5.308   1.00 22.78  ? 459 HOH A O   1 
HETATM 2222 O  O   . HOH E 5 .   ? -12.095 9.311   2.963   1.00 27.72  ? 460 HOH A O   1 
HETATM 2223 O  O   . HOH E 5 .   ? -2.482  -19.382 21.519  1.00 31.03  ? 461 HOH A O   1 
HETATM 2224 O  O   . HOH E 5 .   ? -13.837 14.280  27.331  1.00 26.25  ? 462 HOH A O   1 
HETATM 2225 O  O   . HOH E 5 .   ? -27.267 -5.599  27.573  1.00 36.31  ? 463 HOH A O   1 
HETATM 2226 O  O   . HOH E 5 .   ? -8.033  -15.641 11.560  1.00 11.41  ? 464 HOH A O   1 
HETATM 2227 O  O   . HOH E 5 .   ? -26.324 -7.834  30.437  1.00 36.27  ? 465 HOH A O   1 
HETATM 2228 O  O   . HOH E 5 .   ? -13.114 -22.324 8.844   1.00 34.08  ? 466 HOH A O   1 
HETATM 2229 O  O   . HOH E 5 .   ? -3.540  -11.242 21.075  1.00 10.86  ? 467 HOH A O   1 
HETATM 2230 O  O   . HOH E 5 .   ? -9.079  5.958   29.169  1.00 17.57  ? 468 HOH A O   1 
HETATM 2231 O  O   . HOH E 5 .   ? -10.592 -19.721 20.219  1.00 16.39  ? 469 HOH A O   1 
HETATM 2232 O  O   . HOH E 5 .   ? 4.139   -3.456  26.822  1.00 20.49  ? 470 HOH A O   1 
HETATM 2233 O  O   . HOH E 5 .   ? -15.439 19.675  13.259  1.00 22.66  ? 471 HOH A O   1 
HETATM 2234 O  O   . HOH E 5 .   ? 10.553  -1.470  4.770   1.00 57.18  ? 472 HOH A O   1 
HETATM 2235 O  O   . HOH E 5 .   ? -2.553  -8.836  29.326  1.00 11.95  ? 473 HOH A O   1 
HETATM 2236 O  O   . HOH E 5 .   ? 0.098   -1.245  -4.718  1.00 18.48  ? 474 HOH A O   1 
HETATM 2237 O  O   . HOH E 5 .   ? -8.637  -15.576 36.922  1.00 26.64  ? 475 HOH A O   1 
HETATM 2238 O  O   . HOH E 5 .   ? -16.913 18.522  22.252  1.00 52.40  ? 476 HOH A O   1 
HETATM 2239 O  O   . HOH E 5 .   ? -0.325  14.127  16.284  1.00 22.31  ? 477 HOH A O   1 
HETATM 2240 O  O   . HOH E 5 .   ? -21.846 -14.373 18.700  1.00 37.57  ? 478 HOH A O   1 
HETATM 2241 O  O   . HOH E 5 .   ? -17.091 -8.528  20.525  1.00 9.44   ? 479 HOH A O   1 
HETATM 2242 O  O   . HOH E 5 .   ? -17.346 -16.447 22.207  1.00 22.53  ? 480 HOH A O   1 
HETATM 2243 O  O   . HOH E 5 .   ? -25.864 -9.165  11.359  1.00 37.17  ? 481 HOH A O   1 
HETATM 2244 O  O   . HOH E 5 .   ? -23.449 -13.533 11.349  1.00 22.66  ? 482 HOH A O   1 
HETATM 2245 O  O   . HOH E 5 .   ? -3.477  18.152  21.685  1.00 23.11  ? 483 HOH A O   1 
HETATM 2246 O  O   . HOH E 5 .   ? 3.811   4.158   10.950  1.00 29.11  ? 484 HOH A O   1 
HETATM 2247 O  O   . HOH E 5 .   ? -17.924 -22.488 5.946   1.00 27.30  ? 485 HOH A O   1 
HETATM 2248 O  O   . HOH E 5 .   ? -20.636 8.458   30.228  1.00 26.07  ? 486 HOH A O   1 
HETATM 2249 O  O   . HOH E 5 .   ? 6.002   -2.928  6.974   1.00 36.43  ? 487 HOH A O   1 
HETATM 2250 O  O   . HOH E 5 .   ? -20.311 10.887  26.758  1.00 20.29  ? 488 HOH A O   1 
HETATM 2251 O  O   . HOH E 5 .   ? -2.649  -18.249 31.273  1.00 26.19  ? 489 HOH A O   1 
HETATM 2252 O  O   . HOH E 5 .   ? -13.056 -9.216  -3.170  1.00 33.58  ? 490 HOH A O   1 
HETATM 2253 O  O   . HOH E 5 .   ? 8.567   3.026   27.967  1.00 34.17  ? 491 HOH A O   1 
HETATM 2254 O  O   . HOH E 5 .   ? 1.816   -15.976 9.401   1.00 26.92  ? 492 HOH A O   1 
HETATM 2255 O  O   . HOH E 5 .   ? -6.827  -15.097 31.810  1.00 24.88  ? 493 HOH A O   1 
HETATM 2256 O  O   . HOH E 5 .   ? 11.295  -3.949  7.918   1.00 39.56  ? 494 HOH A O   1 
HETATM 2257 O  O   . HOH E 5 .   ? -16.106 -12.473 24.604  1.00 13.33  ? 495 HOH A O   1 
HETATM 2258 O  O   . HOH E 5 .   ? -18.504 -3.969  -2.580  1.00 23.97  ? 496 HOH A O   1 
HETATM 2259 O  O   . HOH E 5 .   ? -4.481  -13.662 18.240  1.00 9.69   ? 497 HOH A O   1 
HETATM 2260 O  O   . HOH E 5 .   ? -16.744 -11.327 36.801  1.00 59.61  ? 498 HOH A O   1 
HETATM 2261 O  O   . HOH E 5 .   ? -26.225 3.430   15.589  1.00 26.48  ? 499 HOH A O   1 
HETATM 2262 O  O   . HOH E 5 .   ? 1.193   -11.906 25.219  1.00 28.62  ? 500 HOH A O   1 
HETATM 2263 O  O   . HOH E 5 .   ? -3.533  -13.276 -2.687  1.00 22.24  ? 501 HOH A O   1 
HETATM 2264 O  O   . HOH E 5 .   ? -8.582  0.388   -6.570  1.00 33.91  ? 502 HOH A O   1 
HETATM 2265 O  O   . HOH E 5 .   ? -4.261  -8.605  31.385  1.00 18.38  ? 503 HOH A O   1 
HETATM 2266 O  O   . HOH E 5 .   ? -5.150  0.319   9.628   1.00 15.78  ? 504 HOH A O   1 
HETATM 2267 O  O   . HOH E 5 .   ? 5.088   -7.524  22.533  1.00 23.34  ? 505 HOH A O   1 
HETATM 2268 O  O   . HOH E 5 .   ? -18.522 -12.738 -3.692  1.00 24.52  ? 506 HOH A O   1 
HETATM 2269 O  O   . HOH E 5 .   ? -23.343 -11.343 17.174  1.00 32.64  ? 507 HOH A O   1 
HETATM 2270 O  O   . HOH E 5 .   ? -7.387  -17.142 1.600   1.00 25.82  ? 508 HOH A O   1 
HETATM 2271 O  O   . HOH E 5 .   ? 15.371  -2.748  14.539  1.00 26.06  ? 509 HOH A O   1 
HETATM 2272 O  O   . HOH E 5 .   ? 7.064   -4.077  -7.825  1.00 42.28  ? 510 HOH A O   1 
HETATM 2273 O  O   . HOH E 5 .   ? 2.779   0.907   -2.255  1.00 35.66  ? 511 HOH A O   1 
HETATM 2274 O  O   . HOH E 5 .   ? -0.466  10.827  23.531  1.00 17.29  ? 512 HOH A O   1 
HETATM 2275 O  O   . HOH E 5 .   ? -19.929 -4.299  41.484  1.00 32.46  ? 513 HOH A O   1 
HETATM 2276 O  O   . HOH E 5 .   ? -13.822 10.515  28.019  1.00 16.65  ? 514 HOH A O   1 
HETATM 2277 O  O   . HOH E 5 .   ? -17.990 -20.792 8.155   1.00 17.80  ? 515 HOH A O   1 
HETATM 2278 O  O   . HOH E 5 .   ? -12.317 -3.827  37.901  1.00 32.84  ? 516 HOH A O   1 
HETATM 2279 O  O   . HOH E 5 .   ? -22.879 -6.003  2.820   1.00 26.46  ? 517 HOH A O   1 
HETATM 2280 O  O   . HOH E 5 .   ? 4.093   2.407   8.363   1.00 43.79  ? 518 HOH A O   1 
HETATM 2281 O  O   . HOH E 5 .   ? -3.771  -16.049 24.543  1.00 14.06  ? 519 HOH A O   1 
HETATM 2282 O  O   . HOH E 5 .   ? 9.743   1.858   12.417  1.00 37.54  ? 520 HOH A O   1 
HETATM 2283 O  O   . HOH E 5 .   ? -4.624  4.803   9.512   1.00 15.98  ? 521 HOH A O   1 
HETATM 2284 O  O   . HOH E 5 .   ? -2.531  -3.285  11.538  1.00 14.68  ? 522 HOH A O   1 
HETATM 2285 O  O   . HOH E 5 .   ? 2.719   -4.485  7.787   1.00 18.78  ? 523 HOH A O   1 
HETATM 2286 O  O   . HOH E 5 .   ? -3.384  -13.394 25.335  1.00 11.81  ? 524 HOH A O   1 
HETATM 2287 O  O   . HOH E 5 .   ? 8.624   -4.004  21.240  1.00 15.07  ? 525 HOH A O   1 
HETATM 2288 O  O   . HOH E 5 .   ? -10.812 8.520   7.614   1.00 16.58  ? 526 HOH A O   1 
HETATM 2289 O  O   . HOH E 5 .   ? -22.925 -15.040 16.241  1.00 36.58  ? 527 HOH A O   1 
HETATM 2290 O  O   . HOH E 5 .   ? -26.310 2.763   21.061  1.00 19.84  ? 528 HOH A O   1 
HETATM 2291 O  O   . HOH E 5 .   ? -22.031 5.596   4.825   1.00 18.79  ? 529 HOH A O   1 
HETATM 2292 O  O   . HOH E 5 .   ? -23.234 -3.188  6.936   1.00 22.82  ? 530 HOH A O   1 
HETATM 2293 O  O   . HOH E 5 .   ? -16.169 16.036  23.765  1.00 21.72  ? 531 HOH A O   1 
HETATM 2294 O  O   . HOH E 5 .   ? -16.485 -15.972 32.892  1.00 31.53  ? 532 HOH A O   1 
HETATM 2295 O  O   . HOH E 5 .   ? -21.682 -7.320  23.760  1.00 12.50  ? 533 HOH A O   1 
HETATM 2296 O  O   . HOH E 5 .   ? -12.468 10.839  5.293   1.00 54.73  ? 534 HOH A O   1 
HETATM 2297 O  O   . HOH E 5 .   ? -14.828 20.382  17.703  1.00 17.55  ? 535 HOH A O   1 
HETATM 2298 O  O   . HOH E 5 .   ? -1.175  18.307  16.113  1.00 41.59  ? 536 HOH A O   1 
HETATM 2299 O  O   . HOH E 5 .   ? -14.638 -18.848 18.901  1.00 14.79  ? 537 HOH A O   1 
HETATM 2300 O  O   . HOH E 5 .   ? -6.721  14.912  28.938  1.00 45.73  ? 538 HOH A O   1 
HETATM 2301 O  O   . HOH E 5 .   ? 9.209   -5.675  -7.295  1.00 42.88  ? 539 HOH A O   1 
HETATM 2302 O  O   . HOH E 5 .   ? -19.363 10.071  8.938   1.00 15.82  ? 540 HOH A O   1 
HETATM 2303 O  O   . HOH E 5 .   ? 5.508   7.086   20.554  1.00 18.03  ? 541 HOH A O   1 
HETATM 2304 O  O   . HOH E 5 .   ? 2.501   -11.638 9.495   1.00 21.34  ? 542 HOH A O   1 
HETATM 2305 O  O   . HOH E 5 .   ? -6.730  -5.294  37.724  1.00 18.00  ? 543 HOH A O   1 
HETATM 2306 O  O   . HOH E 5 .   ? -18.887 -21.186 14.989  1.00 32.92  ? 544 HOH A O   1 
HETATM 2307 O  O   . HOH E 5 .   ? -24.965 -7.839  9.223   1.00 21.90  ? 545 HOH A O   1 
HETATM 2308 O  O   . HOH E 5 .   ? -23.919 -0.830  4.031   1.00 25.61  ? 546 HOH A O   1 
HETATM 2309 O  O   . HOH E 5 .   ? -13.661 20.219  15.253  1.00 20.33  ? 547 HOH A O   1 
HETATM 2310 O  O   . HOH E 5 .   ? 2.134   8.294   28.004  1.00 59.74  ? 548 HOH A O   1 
HETATM 2311 O  O   . HOH E 5 .   ? 4.905   -5.031  21.143  1.00 12.86  ? 549 HOH A O   1 
HETATM 2312 O  O   . HOH E 5 .   ? -16.748 -1.448  40.078  1.00 48.80  ? 550 HOH A O   1 
HETATM 2313 O  O   . HOH E 5 .   ? 7.654   -8.193  -0.731  1.00 32.21  ? 551 HOH A O   1 
HETATM 2314 O  O   . HOH E 5 .   ? 4.267   -6.803  7.911   1.00 20.62  ? 552 HOH A O   1 
HETATM 2315 O  O   . HOH E 5 .   ? 13.477  0.078   24.673  1.00 22.50  ? 553 HOH A O   1 
HETATM 2316 O  O   . HOH E 5 .   ? -9.296  -10.282 -1.125  1.00 24.05  ? 554 HOH A O   1 
HETATM 2317 O  O   . HOH E 5 .   ? -7.480  -8.747  32.845  1.00 17.42  ? 555 HOH A O   1 
HETATM 2318 O  O   . HOH E 5 .   ? -15.771 8.880   -2.262  1.00 28.21  ? 556 HOH A O   1 
HETATM 2319 O  O   . HOH E 5 .   ? -24.112 -1.077  26.843  1.00 29.59  ? 557 HOH A O   1 
HETATM 2320 O  O   . HOH E 5 .   ? -13.483 -18.768 14.801  1.00 15.94  ? 558 HOH A O   1 
HETATM 2321 O  O   . HOH E 5 .   ? -13.017 -17.090 26.832  1.00 14.36  ? 559 HOH A O   1 
HETATM 2322 O  O   . HOH E 5 .   ? -22.277 -18.693 13.733  1.00 26.44  ? 560 HOH A O   1 
HETATM 2323 O  O   . HOH E 5 .   ? -12.673 -2.284  39.424  1.00 52.37  ? 561 HOH A O   1 
HETATM 2324 O  O   . HOH E 5 .   ? 6.054   -0.436  -1.573  1.00 47.98  ? 562 HOH A O   1 
HETATM 2325 O  O   . HOH E 5 .   ? 11.274  0.919   25.911  1.00 26.65  ? 563 HOH A O   1 
HETATM 2326 O  O   . HOH E 5 .   ? -23.884 -0.241  1.207   1.00 37.85  ? 564 HOH A O   1 
HETATM 2327 O  O   . HOH E 5 .   ? -13.649 -16.692 -0.229  1.00 44.30  ? 565 HOH A O   1 
HETATM 2328 O  O   . HOH E 5 .   ? -10.543 21.032  25.075  1.00 22.87  ? 566 HOH A O   1 
HETATM 2329 O  O   . HOH E 5 .   ? -9.559  13.543  10.370  1.00 29.55  ? 567 HOH A O   1 
HETATM 2330 O  O   . HOH E 5 .   ? -16.403 -10.101 33.105  1.00 16.97  ? 568 HOH A O   1 
HETATM 2331 O  O   . HOH E 5 .   ? -7.174  1.429   35.311  1.00 26.53  ? 569 HOH A O   1 
HETATM 2332 O  O   . HOH E 5 .   ? -12.051 2.739   31.126  1.00 15.76  ? 570 HOH A O   1 
HETATM 2333 O  O   . HOH E 5 .   ? 1.497   -6.330  34.650  1.00 25.66  ? 571 HOH A O   1 
HETATM 2334 O  O   . HOH E 5 .   ? -3.461  3.954   40.861  1.00 21.22  ? 572 HOH A O   1 
HETATM 2335 O  O   . HOH E 5 .   ? -8.573  -22.324 10.607  1.00 22.05  ? 573 HOH A O   1 
HETATM 2336 O  O   . HOH E 5 .   ? -4.760  -16.328 0.894   1.00 34.56  ? 574 HOH A O   1 
HETATM 2337 O  O   . HOH E 5 .   ? 13.948  1.979   23.038  1.00 24.60  ? 575 HOH A O   1 
HETATM 2338 O  O   . HOH E 5 .   ? -5.356  -13.615 34.467  1.00 49.53  ? 576 HOH A O   1 
HETATM 2339 O  O   . HOH E 5 .   ? 1.217   -1.525  29.688  1.00 14.78  ? 577 HOH A O   1 
HETATM 2340 O  O   . HOH E 5 .   ? -12.829 8.005   28.893  1.00 24.42  ? 578 HOH A O   1 
HETATM 2341 O  O   . HOH E 5 .   ? -0.637  4.070   8.309   1.00 42.47  ? 579 HOH A O   1 
HETATM 2342 O  O   . HOH E 5 .   ? 6.599   -6.047  6.760   1.00 29.75  ? 580 HOH A O   1 
HETATM 2343 O  O   . HOH E 5 .   ? 1.599   2.271   36.217  1.00 39.62  ? 581 HOH A O   1 
HETATM 2344 O  O   . HOH E 5 .   ? -0.746  -8.628  32.774  1.00 24.02  ? 582 HOH A O   1 
HETATM 2345 O  O   . HOH E 5 .   ? 1.404   8.838   24.455  1.00 18.23  ? 583 HOH A O   1 
HETATM 2346 O  O   . HOH E 5 .   ? -16.172 -10.059 38.867  1.00 49.13  ? 584 HOH A O   1 
HETATM 2347 O  O   . HOH E 5 .   ? -25.899 8.166   6.203   1.00 39.17  ? 585 HOH A O   1 
HETATM 2348 O  O   . HOH E 5 .   ? -11.166 1.174   33.711  1.00 23.27  ? 586 HOH A O   1 
HETATM 2349 O  O   . HOH E 5 .   ? -9.531  15.399  12.198  1.00 25.36  ? 587 HOH A O   1 
HETATM 2350 O  O   . HOH E 5 .   ? -23.503 -0.140  32.166  1.00 36.26  ? 588 HOH A O   1 
HETATM 2351 O  O   . HOH E 5 .   ? -11.821 -3.003  42.237  1.00 40.20  ? 589 HOH A O   1 
HETATM 2352 O  O   . HOH E 5 .   ? -25.674 -9.951  15.089  1.00 41.52  ? 590 HOH A O   1 
HETATM 2353 O  O   . HOH E 5 .   ? 13.151  -5.974  24.620  1.00 24.67  ? 591 HOH A O   1 
HETATM 2354 O  O   . HOH E 5 .   ? -17.854 4.587   -3.707  1.00 40.28  ? 592 HOH A O   1 
HETATM 2355 O  O   . HOH E 5 .   ? 10.213  -8.855  8.512   1.00 31.35  ? 593 HOH A O   1 
HETATM 2356 O  O   . HOH E 5 .   ? -9.110  -5.804  36.250  1.00 18.48  ? 594 HOH A O   1 
HETATM 2357 O  O   . HOH E 5 .   ? -12.650 13.318  32.224  1.00 33.49  ? 595 HOH A O   1 
HETATM 2358 O  O   . HOH E 5 .   ? -8.646  -20.119 26.969  1.00 23.15  ? 596 HOH A O   1 
HETATM 2359 O  O   . HOH E 5 .   ? -23.068 -11.913 14.230  1.00 22.33  ? 597 HOH A O   1 
HETATM 2360 O  O   . HOH E 5 .   ? -7.259  -8.782  -2.357  1.00 27.51  ? 598 HOH A O   1 
HETATM 2361 O  O   . HOH E 5 .   ? -7.557  8.130   29.756  1.00 37.13  ? 599 HOH A O   1 
HETATM 2362 O  O   . HOH E 5 .   ? -20.510 14.068  28.933  1.00 38.77  ? 600 HOH A O   1 
HETATM 2363 O  O   . HOH E 5 .   ? 13.970  5.639   19.072  1.00 35.86  ? 601 HOH A O   1 
HETATM 2364 O  O   . HOH E 5 .   ? -13.630 -0.915  -6.212  1.00 29.29  ? 602 HOH A O   1 
HETATM 2365 O  O   . HOH E 5 .   ? 3.992   -2.699  5.360   1.00 58.56  ? 603 HOH A O   1 
HETATM 2366 O  O   . HOH E 5 .   ? -6.609  6.634   10.137  1.00 14.94  ? 604 HOH A O   1 
HETATM 2367 O  O   . HOH E 5 .   ? -6.226  -19.996 24.036  1.00 25.23  ? 605 HOH A O   1 
HETATM 2368 O  O   . HOH E 5 .   ? -6.532  -19.693 5.850   1.00 38.58  ? 606 HOH A O   1 
HETATM 2369 O  O   . HOH E 5 .   ? -15.006 6.143   33.017  1.00 33.45  ? 607 HOH A O   1 
HETATM 2370 O  O   . HOH E 5 .   ? -12.467 -18.688 32.556  1.00 30.65  ? 608 HOH A O   1 
HETATM 2371 O  O   . HOH E 5 .   ? -8.135  -19.548 21.842  1.00 15.95  ? 609 HOH A O   1 
HETATM 2372 O  O   . HOH E 5 .   ? -12.754 3.483   -6.950  1.00 31.66  ? 610 HOH A O   1 
HETATM 2373 O  O   . HOH E 5 .   ? -21.686 19.861  17.381  1.00 53.35  ? 611 HOH A O   1 
HETATM 2374 O  O   . HOH E 5 .   ? -11.127 17.997  12.323  1.00 27.44  ? 612 HOH A O   1 
HETATM 2375 O  O   . HOH E 5 .   ? -21.414 -20.041 6.803   1.00 27.77  ? 613 HOH A O   1 
HETATM 2376 O  O   . HOH E 5 .   ? -2.079  -12.454 23.017  1.00 10.50  ? 614 HOH A O   1 
HETATM 2377 O  O   . HOH E 5 .   ? -21.608 19.628  12.285  1.00 51.27  ? 615 HOH A O   1 
HETATM 2378 O  O   . HOH E 5 .   ? 8.638   -4.783  23.875  1.00 23.35  ? 616 HOH A O   1 
HETATM 2379 O  O   . HOH E 5 .   ? -6.890  -8.932  -7.113  1.00 46.26  ? 617 HOH A O   1 
HETATM 2380 O  O   . HOH E 5 .   ? 4.910   -13.419 -5.567  1.00 23.46  ? 618 HOH A O   1 
HETATM 2381 O  O   . HOH E 5 .   ? -24.877 4.572   8.157   1.00 33.25  ? 619 HOH A O   1 
HETATM 2382 O  O   . HOH E 5 .   ? 7.735   6.025   21.964  1.00 15.23  ? 620 HOH A O   1 
HETATM 2383 O  O   . HOH E 5 .   ? -19.513 2.986   -3.260  1.00 36.99  ? 621 HOH A O   1 
HETATM 2384 O  O   . HOH E 5 .   ? -5.715  15.446  11.938  1.00 29.88  ? 622 HOH A O   1 
HETATM 2385 O  O   . HOH E 5 .   ? 2.757   -14.908 0.933   1.00 38.00  ? 623 HOH A O   1 
HETATM 2386 O  O   . HOH E 5 .   ? -3.271  -15.168 33.044  1.00 43.59  ? 624 HOH A O   1 
HETATM 2387 O  O   . HOH E 5 .   ? -9.582  -8.084  34.349  1.00 23.05  ? 625 HOH A O   1 
HETATM 2388 O  O   . HOH E 5 .   ? -0.117  -14.414 22.351  1.00 20.87  ? 626 HOH A O   1 
HETATM 2389 O  O   . HOH E 5 .   ? -5.421  3.137   -5.941  1.00 37.09  ? 627 HOH A O   1 
HETATM 2390 O  O   . HOH E 5 .   ? 7.594   -1.382  -6.098  1.00 38.37  ? 628 HOH A O   1 
HETATM 2391 O  O   . HOH E 5 .   ? 1.782   -17.791 13.976  1.00 38.97  ? 629 HOH A O   1 
HETATM 2392 O  O   . HOH E 5 .   ? -25.325 11.172  19.643  1.00 31.66  ? 630 HOH A O   1 
HETATM 2393 O  O   . HOH E 5 .   ? -3.014  4.532   7.317   1.00 34.07  ? 631 HOH A O   1 
HETATM 2394 O  O   . HOH E 5 .   ? 5.828   -13.237 11.261  1.00 48.12  ? 632 HOH A O   1 
HETATM 2395 O  O   . HOH E 5 .   ? 4.695   -11.262 -6.966  1.00 40.89  ? 633 HOH A O   1 
HETATM 2396 O  O   . HOH E 5 .   ? -1.572  11.216  25.948  1.00 26.35  ? 634 HOH A O   1 
HETATM 2397 O  O   . HOH E 5 .   ? -24.787 -10.062 2.137   1.00 38.08  ? 635 HOH A O   1 
HETATM 2398 O  O   . HOH E 5 .   ? -10.113 6.014   -4.410  1.00 37.87  ? 636 HOH A O   1 
HETATM 2399 O  O   . HOH E 5 .   ? -5.236  -12.990 -4.728  1.00 42.23  ? 637 HOH A O   1 
HETATM 2400 O  O   . HOH E 5 .   ? -19.480 17.561  23.353  1.00 54.71  ? 638 HOH A O   1 
HETATM 2401 O  O   . HOH E 5 .   ? 0.492   19.950  17.703  1.00 50.45  ? 639 HOH A O   1 
HETATM 2402 O  O   . HOH E 5 .   ? -23.412 -10.852 29.709  1.00 50.37  ? 640 HOH A O   1 
HETATM 2403 O  O   . HOH E 5 .   ? 0.365   0.422   -6.810  1.00 29.18  ? 641 HOH A O   1 
HETATM 2404 O  O   . HOH E 5 .   ? 1.467   -15.971 -1.232  1.00 35.71  ? 642 HOH A O   1 
HETATM 2405 O  O   . HOH E 5 .   ? 10.216  -2.682  13.912  1.00 28.72  ? 643 HOH A O   1 
HETATM 2406 O  O   . HOH E 5 .   ? -3.712  -17.002 3.110   1.00 45.53  ? 644 HOH A O   1 
HETATM 2407 O  O   . HOH E 5 .   ? -12.910 -17.407 17.096  1.00 12.48  ? 645 HOH A O   1 
HETATM 2408 O  O   . HOH E 5 .   ? -0.553  -2.978  39.780  1.00 47.85  ? 646 HOH A O   1 
HETATM 2409 O  O   . HOH E 5 .   ? 4.139   -10.986 17.104  1.00 53.39  ? 647 HOH A O   1 
HETATM 2410 O  O   . HOH E 5 .   ? -18.077 -12.132 31.834  1.00 27.90  ? 648 HOH A O   1 
HETATM 2411 O  O   . HOH E 5 .   ? -11.252 11.651  7.265   1.00 40.32  ? 649 HOH A O   1 
HETATM 2412 O  O   . HOH E 5 .   ? -17.849 -8.972  35.134  1.00 41.37  ? 650 HOH A O   1 
HETATM 2413 O  O   . HOH E 5 .   ? -4.205  -1.031  12.004  1.00 15.44  ? 651 HOH A O   1 
HETATM 2414 O  O   . HOH E 5 .   ? 5.751   -8.143  3.185   1.00 31.59  ? 652 HOH A O   1 
HETATM 2415 O  O   . HOH E 5 .   ? -31.649 5.484   13.406  1.00 41.27  ? 653 HOH A O   1 
HETATM 2416 O  O   . HOH E 5 .   ? -4.017  -20.530 14.962  1.00 25.95  ? 654 HOH A O   1 
HETATM 2417 O  O   . HOH E 5 .   ? -22.713 -9.755  25.502  1.00 21.80  ? 655 HOH A O   1 
HETATM 2418 O  O   . HOH E 5 .   ? 14.815  0.147   15.366  1.00 78.23  ? 656 HOH A O   1 
HETATM 2419 O  O   . HOH E 5 .   ? -25.968 4.245   4.202   1.00 38.66  ? 657 HOH A O   1 
HETATM 2420 O  O   . HOH E 5 .   ? -17.599 5.625   35.062  1.00 49.80  ? 658 HOH A O   1 
HETATM 2421 O  O   . HOH E 5 .   ? -17.357 -0.340  -3.986  1.00 64.31  ? 659 HOH A O   1 
HETATM 2422 O  O   . HOH E 5 .   ? 3.202   -14.255 13.049  1.00 52.43  ? 660 HOH A O   1 
HETATM 2423 O  O   . HOH E 5 .   ? -15.381 -16.449 25.774  1.00 33.88  ? 661 HOH A O   1 
HETATM 2424 O  O   . HOH E 5 .   ? 11.899  -6.682  7.928   1.00 30.85  ? 662 HOH A O   1 
HETATM 2425 O  O   . HOH E 5 .   ? -24.953 8.914   26.341  1.00 47.42  ? 663 HOH A O   1 
HETATM 2426 O  O   . HOH E 5 .   ? -8.286  -17.787 35.183  1.00 24.97  ? 664 HOH A O   1 
HETATM 2427 O  O   . HOH E 5 .   ? -17.796 20.214  17.625  1.00 24.98  ? 665 HOH A O   1 
HETATM 2428 O  O   . HOH E 5 .   ? -9.353  -22.372 8.186   1.00 45.05  ? 666 HOH A O   1 
HETATM 2429 O  O   . HOH E 5 .   ? -11.508 -0.270  43.549  1.00 34.28  ? 667 HOH A O   1 
HETATM 2430 O  O   . HOH E 5 .   ? 5.025   -13.179 3.858   1.00 50.57  ? 668 HOH A O   1 
HETATM 2431 O  O   . HOH E 5 .   ? 15.286  -4.104  25.221  1.00 22.28  ? 669 HOH A O   1 
HETATM 2432 O  O   . HOH E 5 .   ? 6.952   -10.717 -8.168  1.00 30.94  ? 670 HOH A O   1 
HETATM 2433 O  O   . HOH E 5 .   ? 2.927   -13.861 8.257   1.00 31.37  ? 671 HOH A O   1 
HETATM 2434 O  O   . HOH E 5 .   ? -4.938  -9.724  33.615  1.00 28.72  ? 672 HOH A O   1 
HETATM 2435 O  O   . HOH E 5 .   ? -10.576 5.011   31.121  1.00 23.41  ? 673 HOH A O   1 
HETATM 2436 O  O   . HOH E 5 .   ? -1.416  -13.177 27.269  1.00 24.14  ? 674 HOH A O   1 
HETATM 2437 O  O   . HOH E 5 .   ? 6.674   -5.182  27.464  1.00 33.52  ? 675 HOH A O   1 
HETATM 2438 O  O   . HOH E 5 .   ? -14.999 21.348  23.184  1.00 29.64  ? 676 HOH A O   1 
HETATM 2439 O  O   . HOH E 5 .   ? -1.352  -13.343 33.389  1.00 27.50  ? 677 HOH A O   1 
HETATM 2440 O  O   . HOH E 5 .   ? -16.928 -18.310 20.342  1.00 23.54  ? 678 HOH A O   1 
HETATM 2441 O  O   . HOH E 5 .   ? -1.881  -17.587 25.836  1.00 25.54  ? 679 HOH A O   1 
HETATM 2442 O  O   . HOH E 5 .   ? -2.979  14.945  11.531  1.00 31.36  ? 680 HOH A O   1 
HETATM 2443 O  O   . HOH E 5 .   ? -10.873 -11.315 -2.905  1.00 47.10  ? 681 HOH A O   1 
HETATM 2444 O  O   . HOH E 5 .   ? -16.572 -18.060 24.342  1.00 37.68  ? 682 HOH A O   1 
HETATM 2445 O  O   . HOH E 5 .   ? -0.254  -7.112  -7.626  1.00 41.62  ? 683 HOH A O   1 
HETATM 2446 O  O   . HOH E 5 .   ? -5.230  -14.171 38.709  1.00 30.53  ? 684 HOH A O   1 
HETATM 2447 O  O   . HOH E 5 .   ? -16.880 -14.110 26.484  1.00 19.57  ? 685 HOH A O   1 
HETATM 2448 O  O   . HOH E 5 .   ? 1.827   12.553  22.768  1.00 25.61  ? 686 HOH A O   1 
HETATM 2449 O  O   . HOH E 5 .   ? -2.760  12.198  12.733  1.00 32.85  ? 687 HOH A O   1 
HETATM 2450 O  O   . HOH E 5 .   ? -14.046 3.752   33.337  1.00 28.05  ? 688 HOH A O   1 
HETATM 2451 O  O   . HOH E 5 .   ? -22.373 -12.540 25.065  1.00 31.76  ? 689 HOH A O   1 
HETATM 2452 O  O   . HOH E 5 .   ? -6.362  -9.326  35.960  1.00 47.17  ? 690 HOH A O   1 
HETATM 2453 O  O   . HOH E 5 .   ? 15.393  -1.478  26.225  1.00 27.26  ? 691 HOH A O   1 
HETATM 2454 O  O   . HOH E 5 .   ? -4.849  20.620  21.641  1.00 23.03  ? 692 HOH A O   1 
HETATM 2455 O  O   . HOH E 5 .   ? -25.945 -3.494  6.714   1.00 49.84  ? 693 HOH A O   1 
HETATM 2456 O  O   . HOH E 5 .   ? -16.165 17.277  26.562  1.00 39.94  ? 694 HOH A O   1 
HETATM 2457 O  O   . HOH E 5 .   ? -2.094  -11.791 31.827  1.00 28.01  ? 695 HOH A O   1 
HETATM 2458 O  O   . HOH E 5 .   ? 1.947   -14.267 20.400  1.00 31.13  ? 696 HOH A O   1 
HETATM 2459 O  O   . HOH E 5 .   ? -20.419 -5.117  -3.554  1.00 50.00  ? 697 HOH A O   1 
HETATM 2460 O  O   . HOH E 5 .   ? -8.271  7.545   7.985   1.00 19.84  ? 698 HOH A O   1 
HETATM 2461 O  O   . HOH E 5 .   ? -1.774  -17.708 5.100   1.00 39.55  ? 699 HOH A O   1 
HETATM 2462 O  O   . HOH E 5 .   ? -21.377 -20.728 15.001  1.00 45.61  ? 700 HOH A O   1 
HETATM 2463 O  O   . HOH E 5 .   ? -7.181  17.048  10.614  1.00 20.75  ? 701 HOH A O   1 
HETATM 2464 O  O   . HOH E 5 .   ? 1.620   -9.978  31.627  1.00 50.24  ? 702 HOH A O   1 
HETATM 2465 O  O   . HOH E 5 .   ? 3.264   6.537   32.332  1.00 49.62  ? 703 HOH A O   1 
HETATM 2466 O  O   . HOH E 5 .   ? -0.819  -17.762 -1.679  1.00 32.40  ? 704 HOH A O   1 
HETATM 2467 O  O   . HOH E 5 .   ? -11.899 10.686  0.600   1.00 33.70  ? 705 HOH A O   1 
HETATM 2468 O  O   . HOH E 5 .   ? -12.770 21.906  26.370  1.00 24.13  ? 706 HOH A O   1 
HETATM 2469 O  O   . HOH E 5 .   ? 2.242   12.962  20.205  1.00 44.34  ? 707 HOH A O   1 
HETATM 2470 O  O   . HOH E 5 .   ? 6.239   -5.783  3.795   1.00 45.44  ? 708 HOH A O   1 
HETATM 2471 O  O   . HOH E 5 .   ? -7.364  -10.427 -4.463  1.00 28.86  ? 709 HOH A O   1 
HETATM 2472 O  O   . HOH E 5 .   ? 3.344   2.775   -0.065  1.00 41.03  ? 710 HOH A O   1 
HETATM 2473 O  O   . HOH E 5 .   ? -12.904 13.714  4.615   1.00 51.89  ? 711 HOH A O   1 
HETATM 2474 O  O   . HOH E 5 .   ? -1.212  -11.245 29.254  1.00 17.07  ? 712 HOH A O   1 
HETATM 2475 O  O   . HOH E 5 .   ? -3.888  -15.844 -2.114  1.00 33.39  ? 713 HOH A O   1 
HETATM 2476 O  O   . HOH E 5 .   ? -0.529  7.266   8.669   1.00 48.67  ? 714 HOH A O   1 
HETATM 2477 O  O   . HOH E 5 .   ? 1.523   12.951  17.648  1.00 35.72  ? 715 HOH A O   1 
HETATM 2478 O  O   . HOH E 5 .   ? 6.418   8.681   18.790  1.00 52.70  ? 716 HOH A O   1 
HETATM 2479 O  O   . HOH E 5 .   ? -19.727 -15.258 26.236  1.00 36.25  ? 717 HOH A O   1 
HETATM 2480 O  O   . HOH E 5 .   ? -11.193 9.570   30.809  1.00 39.85  ? 718 HOH A O   1 
HETATM 2481 O  O   . HOH E 5 .   ? -18.440 2.552   -6.516  1.00 37.99  ? 719 HOH A O   1 
HETATM 2482 O  O   . HOH E 5 .   ? 10.331  -5.656  -4.944  1.00 47.48  ? 720 HOH A O   1 
HETATM 2483 O  O   . HOH E 5 .   ? 6.434   5.262   29.118  1.00 41.82  ? 721 HOH A O   1 
HETATM 2484 O  O   . HOH E 5 .   ? -0.641  12.075  14.327  1.00 29.73  ? 722 HOH A O   1 
HETATM 2485 O  O   . HOH E 5 .   ? -20.035 -15.675 22.725  1.00 36.40  ? 723 HOH A O   1 
HETATM 2486 O  O   . HOH E 5 .   ? -3.364  -20.178 26.875  1.00 47.12  ? 724 HOH A O   1 
HETATM 2487 O  O   . HOH E 5 .   ? -1.610  16.693  12.615  1.00 34.63  ? 725 HOH A O   1 
HETATM 2488 O  O   . HOH E 5 .   ? -0.604  6.291   32.420  1.00 40.34  ? 726 HOH A O   1 
HETATM 2489 O  O   . HOH E 5 .   ? -5.822  -18.508 3.610   1.00 36.77  ? 727 HOH A O   1 
HETATM 2490 O  O   . HOH E 5 .   ? 11.771  0.238   28.939  1.00 46.91  ? 728 HOH A O   1 
HETATM 2491 O  O   . HOH E 5 .   ? -6.190  8.790   11.205  1.00 40.20  ? 729 HOH A O   1 
HETATM 2492 O  O   . HOH E 5 .   ? 5.527   9.103   21.936  1.00 40.47  ? 730 HOH A O   1 
HETATM 2493 O  O   . HOH E 5 .   ? 1.334   -16.635 4.992   1.00 50.90  ? 731 HOH A O   1 
HETATM 2494 O  O   . HOH E 5 .   ? 14.585  4.433   24.176  1.00 39.19  ? 732 HOH A O   1 
HETATM 2495 O  O   . HOH E 5 .   ? 3.901   9.552   23.804  1.00 50.20  ? 733 HOH A O   1 
HETATM 2496 O  O   . HOH E 5 .   ? -28.139 -1.468  28.532  1.00 41.05  ? 734 HOH A O   1 
HETATM 2497 O  O   . HOH E 5 .   ? -3.866  10.800  11.207  1.00 51.97  ? 735 HOH A O   1 
HETATM 2498 O  O   . HOH E 5 .   ? 2.672   12.344  27.284  1.00 58.90  ? 736 HOH A O   1 
HETATM 2499 O  O   . HOH E 5 .   ? -9.022  9.121   -6.771  1.00 40.93  ? 737 HOH A O   1 
HETATM 2500 O  O   . HOH E 5 .   ? -29.631 -10.113 5.447   1.00 42.98  ? 738 HOH A O   1 
HETATM 2501 O  O   . HOH E 5 .   ? 12.207  -7.193  -1.632  1.00 64.20  ? 739 HOH A O   1 
HETATM 2502 O  O   . HOH E 5 .   ? 5.223   11.304  20.622  1.00 54.02  ? 740 HOH A O   1 
# 
loop_
_atom_site_anisotrop.id 
_atom_site_anisotrop.type_symbol 
_atom_site_anisotrop.pdbx_label_atom_id 
_atom_site_anisotrop.pdbx_label_alt_id 
_atom_site_anisotrop.pdbx_label_comp_id 
_atom_site_anisotrop.pdbx_label_asym_id 
_atom_site_anisotrop.pdbx_label_seq_id 
_atom_site_anisotrop.pdbx_PDB_ins_code 
_atom_site_anisotrop.U[1][1] 
_atom_site_anisotrop.U[2][2] 
_atom_site_anisotrop.U[3][3] 
_atom_site_anisotrop.U[1][2] 
_atom_site_anisotrop.U[1][3] 
_atom_site_anisotrop.U[2][3] 
_atom_site_anisotrop.pdbx_auth_seq_id 
_atom_site_anisotrop.pdbx_auth_comp_id 
_atom_site_anisotrop.pdbx_auth_asym_id 
_atom_site_anisotrop.pdbx_auth_atom_id 
1    N  N   . HIS A 3   ? 0.3313 0.8835 1.3899 -0.0416 0.1789  -0.5154 3   HIS A N   
2    C  CA  . HIS A 3   ? 0.6111 0.9939 1.0330 0.1451  0.2544  -0.4955 3   HIS A CA  
3    C  C   . HIS A 3   ? 0.6280 0.9568 0.4216 0.0069  0.1328  -0.0450 3   HIS A C   
4    O  O   . HIS A 3   ? 0.7556 0.7941 0.4491 -0.2192 -0.1338 -0.2171 3   HIS A O   
5    C  CB  . HIS A 3   ? 0.3927 1.2200 1.0577 0.2317  -0.1586 -0.5569 3   HIS A CB  
6    C  CG  . HIS A 3   ? 1.8208 1.5781 0.9009 0.6078  -0.3165 0.0599  3   HIS A CG  
7    N  ND1 . HIS A 3   ? 1.8882 2.0786 0.5683 -0.5830 -0.2171 0.4872  3   HIS A ND1 
8    C  CD2 . HIS A 3   ? 2.0384 1.6311 0.4348 -0.2218 -0.1251 0.6496  3   HIS A CD2 
9    C  CE1 . HIS A 3   ? 2.3115 1.6525 0.2634 0.0054  0.0203  0.5610  3   HIS A CE1 
10   N  NE2 . HIS A 3   ? 2.5833 1.0114 1.0828 -0.3942 -0.6018 0.7626  3   HIS A NE2 
11   N  N   . HIS A 4   ? 0.4306 0.5464 0.5229 -0.0631 0.2450  0.0864  4   HIS A N   
12   C  CA  . HIS A 4   ? 0.2351 0.4244 0.5278 -0.0861 0.1406  0.1656  4   HIS A CA  
13   C  C   . HIS A 4   ? 0.1435 0.3282 0.3102 -0.0362 0.0846  0.0700  4   HIS A C   
14   O  O   . HIS A 4   ? 0.2822 0.3615 0.3062 0.0354  0.1348  0.0534  4   HIS A O   
15   C  CB  . HIS A 4   ? 0.1944 0.3413 0.6534 0.0209  0.2136  0.1691  4   HIS A CB  
16   C  CG  . HIS A 4   ? 0.4327 0.3450 0.6171 0.0810  0.2477  0.1946  4   HIS A CG  
17   N  ND1 . HIS A 4   ? 0.1829 0.5780 0.7727 0.0086  0.0221  0.2200  4   HIS A ND1 
18   C  CD2 . HIS A 4   ? 0.6136 0.7817 0.6232 0.2557  -0.1145 0.3379  4   HIS A CD2 
19   C  CE1 . HIS A 4   ? 0.8350 0.4480 1.1722 0.0527  0.0451  0.2337  4   HIS A CE1 
20   N  NE2 . HIS A 4   ? 0.9934 0.8253 1.0525 0.1148  -0.0383 0.2667  4   HIS A NE2 
21   N  N   . TRP A 5   ? 0.1321 0.2616 0.3049 -0.0422 0.0741  0.0352  5   TRP A N   
22   C  CA  . TRP A 5   ? 0.1367 0.2114 0.2244 -0.0239 0.0609  -0.0021 5   TRP A CA  
23   C  C   . TRP A 5   ? 0.1004 0.1982 0.2667 0.0058  0.0752  -0.0179 5   TRP A C   
24   O  O   . TRP A 5   ? 0.1235 0.2068 0.2455 -0.0272 0.0828  0.0237  5   TRP A O   
25   C  CB  . TRP A 5   ? 0.0731 0.2310 0.3025 -0.0387 0.0837  -0.0477 5   TRP A CB  
26   C  CG  . TRP A 5   ? 0.1402 0.2035 0.1966 -0.0352 0.0662  -0.0048 5   TRP A CG  
27   C  CD1 . TRP A 5   ? 0.1847 0.2174 0.2132 -0.0189 0.0351  0.0253  5   TRP A CD1 
28   C  CD2 . TRP A 5   ? 0.1084 0.1860 0.1644 0.0001  0.0570  -0.0333 5   TRP A CD2 
29   N  NE1 . TRP A 5   ? 0.1755 0.2068 0.1630 0.0156  0.0756  0.0446  5   TRP A NE1 
30   C  CE2 . TRP A 5   ? 0.1596 0.1903 0.1485 0.0149  0.0425  -0.0013 5   TRP A CE2 
31   C  CE3 . TRP A 5   ? 0.1183 0.1852 0.1619 0.0058  0.0367  -0.0190 5   TRP A CE3 
32   C  CZ2 . TRP A 5   ? 0.1819 0.2219 0.1264 0.0212  0.0106  0.0142  5   TRP A CZ2 
33   C  CZ3 . TRP A 5   ? 0.1222 0.2407 0.1546 0.0465  0.0285  -0.0926 5   TRP A CZ3 
34   C  CH2 . TRP A 5   ? 0.1470 0.2211 0.1392 0.0398  0.0595  -0.0541 5   TRP A CH2 
35   N  N   . GLY A 6   ? 0.1086 0.1756 0.2023 0.0130  0.0886  -0.0284 6   GLY A N   
36   C  CA  . GLY A 6   ? 0.1414 0.1671 0.1921 -0.0078 0.0664  -0.0245 6   GLY A CA  
37   C  C   . GLY A 6   ? 0.1027 0.1806 0.1905 0.0254  0.0811  -0.0078 6   GLY A C   
38   O  O   . GLY A 6   ? 0.1275 0.1867 0.1899 0.0351  0.0785  0.0023  6   GLY A O   
39   N  N   . TYR A 7   ? 0.1522 0.1751 0.2231 0.0022  0.0972  -0.0017 7   TYR A N   
40   C  CA  . TYR A 7   ? 0.0978 0.1546 0.3376 0.0333  0.1374  0.0288  7   TYR A CA  
41   C  C   . TYR A 7   ? 0.1375 0.2630 0.6425 0.0892  0.2022  -0.0395 7   TYR A C   
42   O  O   . TYR A 7   ? 0.2819 0.1604 1.2641 0.0396  0.4037  0.0407  7   TYR A O   
43   C  CB  . TYR A 7   ? 0.0889 0.1723 0.3321 0.0214  0.1197  -0.0025 7   TYR A CB  
44   C  CG  . TYR A 7   ? 0.0895 0.1769 0.1817 0.0216  0.0609  -0.0182 7   TYR A CG  
45   C  CD1 . TYR A 7   ? 0.0754 0.1669 0.1859 0.0048  0.0439  -0.0279 7   TYR A CD1 
46   C  CD2 . TYR A 7   ? 0.0874 0.1571 0.1734 0.0042  0.0697  -0.0225 7   TYR A CD2 
47   C  CE1 . TYR A 7   ? 0.0774 0.1479 0.1454 -0.0067 0.0478  -0.0093 7   TYR A CE1 
48   C  CE2 . TYR A 7   ? 0.0740 0.1485 0.1435 0.0015  0.0425  -0.0070 7   TYR A CE2 
49   C  CZ  . TYR A 7   ? 0.0622 0.1575 0.1479 -0.0110 0.0442  -0.0063 7   TYR A CZ  
50   O  OH  . TYR A 7   ? 0.0773 0.1626 0.1342 -0.0029 0.0430  -0.0051 7   TYR A OH  
51   N  N   . GLY A 8   ? 0.1152 0.2208 0.4712 0.0399  0.1267  -0.0588 8   GLY A N   
52   C  CA  . GLY A 8   ? 0.2409 0.2208 0.4650 0.0864  0.1473  -0.0106 8   GLY A CA  
53   C  C   . GLY A 8   ? 0.1647 0.3741 0.5831 0.0599  0.1080  0.0070  8   GLY A C   
54   O  O   . GLY A 8   ? 0.3680 0.3479 0.5115 0.1435  0.2634  0.1901  8   GLY A O   
55   N  N   . LYS A 9   ? 0.2170 0.2723 0.7058 0.1370  0.0758  0.0851  9   LYS A N   
56   C  CA  . LYS A 9   ? 0.1793 0.2888 0.5874 0.0403  0.0651  0.1411  9   LYS A CA  
57   C  C   . LYS A 9   ? 0.4565 0.3221 0.4158 0.0220  -0.0103 0.0974  9   LYS A C   
58   O  O   . LYS A 9   ? 0.3834 0.7957 0.5633 0.1507  -0.0467 0.4045  9   LYS A O   
59   C  CB  . LYS A 9   ? 0.3382 0.3679 0.9259 0.1966  0.1795  0.0423  9   LYS A CB  
60   C  CG  . LYS A 9   ? 0.3909 0.4634 0.8244 -0.0025 0.0041  0.0021  9   LYS A CG  
61   C  CD  . LYS A 9   ? 0.6781 0.9178 1.1960 -0.5044 -0.3194 0.0110  9   LYS A CD  
62   C  CE  . LYS A 9   ? 1.2333 1.0682 0.9486 -0.3957 -0.1732 0.3315  9   LYS A CE  
63   N  NZ  . LYS A 9   ? 1.3813 0.7341 1.4059 -0.4990 -0.5618 0.4134  9   LYS A NZ  
64   N  N   . HIS A 10  ? 0.1905 0.2476 0.4644 0.0741  0.2002  0.0234  10  HIS A N   
65   C  CA  . HIS A 10  ? 0.1661 0.3343 0.3039 0.1181  0.1458  0.0089  10  HIS A CA  
66   C  C   . HIS A 10  ? 0.1903 0.2780 0.2790 0.0806  0.1307  0.0648  10  HIS A C   
67   O  O   . HIS A 10  ? 0.1267 0.3977 0.3059 0.1165  0.0652  -0.0425 10  HIS A O   
68   C  CB  . HIS A 10  ? 0.1799 0.3164 0.3622 0.1081  0.1960  0.0322  10  HIS A CB  
69   C  CG  . HIS A 10  ? 0.2660 0.2966 0.3657 0.0152  0.1767  -0.0474 10  HIS A CG  
70   N  ND1 . HIS A 10  ? 0.3066 0.4011 0.3899 0.0675  0.1701  0.0194  10  HIS A ND1 
71   C  CD2 . HIS A 10  ? 0.2317 0.3525 0.3072 0.0977  0.0868  -0.0134 10  HIS A CD2 
72   C  CE1 . HIS A 10  ? 0.1553 0.3017 0.3717 0.0546  0.1643  0.0833  10  HIS A CE1 
73   N  NE2 . HIS A 10  ? 0.3010 0.3398 0.5083 0.1245  0.1117  -0.0873 10  HIS A NE2 
74   N  N   . ASN A 11  ? 0.1895 0.2618 0.2443 0.0768  0.1239  0.0307  11  ASN A N   
75   C  CA  . ASN A 11  ? 0.1743 0.2615 0.2339 0.0702  0.1481  0.0178  11  ASN A CA  
76   C  C   . ASN A 11  ? 0.1470 0.2391 0.2134 0.0495  0.1217  0.0489  11  ASN A C   
77   O  O   . ASN A 11  ? 0.1326 0.2449 0.2300 0.0663  0.1020  0.0412  11  ASN A O   
78   C  CB  . ASN A 11  ? 0.1176 0.2441 0.2408 0.0387  0.1267  0.0238  11  ASN A CB  
79   C  CG  . ASN A 11  ? 0.2049 0.1928 0.2341 0.0421  0.0967  -0.0022 11  ASN A CG  
80   O  OD1 . ASN A 11  ? 0.1517 0.2236 0.3206 0.0146  0.0983  0.0225  11  ASN A OD1 
81   N  ND2 . ASN A 11  ? 0.2843 0.2151 0.2570 0.0523  0.0717  0.0278  11  ASN A ND2 
82   N  N   . GLY A 12  ? 0.1101 0.2089 0.2129 0.0343  0.1065  0.0092  12  GLY A N   
83   C  CA  . GLY A 12  ? 0.0996 0.3017 0.1888 0.0605  0.0965  0.0067  12  GLY A CA  
84   C  C   . GLY A 12  ? 0.0883 0.2825 0.1874 0.0353  0.0580  0.0423  12  GLY A C   
85   O  O   . GLY A 12  ? 0.0646 0.2412 0.2297 0.0440  0.0828  0.0342  12  GLY A O   
86   N  N   . PRO A 13  ? 0.0838 0.1888 0.1960 0.0261  0.0659  0.0131  13  PRO A N   
87   C  CA  . PRO A 13  ? 0.0988 0.1869 0.2111 -0.0087 0.0606  -0.0019 13  PRO A CA  
88   C  C   . PRO A 13  ? 0.1312 0.1725 0.1909 0.0171  0.0758  0.0179  13  PRO A C   
89   O  O   . PRO A 13  ? 0.1216 0.2082 0.2057 -0.0047 0.0603  -0.0103 13  PRO A O   
90   C  CB  . PRO A 13  ? 0.1522 0.1587 0.1866 -0.0274 0.0851  0.0111  13  PRO A CB  
91   C  CG  . PRO A 13  ? 0.0977 0.1953 0.1959 0.0320  0.0929  -0.0139 13  PRO A CG  
92   C  CD  . PRO A 13  ? 0.0842 0.2429 0.1669 0.0407  0.0694  -0.0199 13  PRO A CD  
93   N  N   A GLU A 14  ? 0.1181 0.1732 0.2043 0.0168  0.0700  0.0139  14  GLU A N   
94   N  N   B GLU A 14  ? 0.1025 0.1490 0.2551 -0.0068 0.1082  0.0303  14  GLU A N   
95   C  CA  A GLU A 14  ? 0.1684 0.1992 0.2236 0.0543  0.0454  0.0193  14  GLU A CA  
96   C  CA  B GLU A 14  ? 0.1808 0.2075 0.2930 0.0306  0.0595  0.0249  14  GLU A CA  
97   C  C   A GLU A 14  ? 0.1271 0.1680 0.2301 0.0926  0.0469  0.0067  14  GLU A C   
98   C  C   B GLU A 14  ? 0.1569 0.1664 0.2343 0.0686  0.0718  0.0082  14  GLU A C   
99   O  O   A GLU A 14  ? 0.1068 0.2574 0.2352 0.0666  0.0561  0.0378  14  GLU A O   
100  O  O   B GLU A 14  ? 0.1614 0.2164 0.2721 0.1016  0.0507  0.0022  14  GLU A O   
101  C  CB  A GLU A 14  ? 0.2025 0.2082 0.1885 0.0710  0.0350  -0.0294 14  GLU A CB  
102  C  CB  B GLU A 14  ? 0.2681 0.1856 0.3700 0.0037  0.0453  0.0230  14  GLU A CB  
103  C  CG  A GLU A 14  ? 0.1504 0.2427 0.1770 0.0737  0.0380  -0.0042 14  GLU A CG  
104  C  CG  B GLU A 14  ? 0.2592 0.2108 0.4289 -0.0386 0.0315  -0.0091 14  GLU A CG  
105  C  CD  A GLU A 14  ? 0.1192 0.2000 0.2215 0.0635  -0.0122 0.0257  14  GLU A CD  
106  C  CD  B GLU A 14  ? 0.2372 0.4550 0.3127 0.0107  -0.0795 -0.0455 14  GLU A CD  
107  O  OE1 A GLU A 14  ? 0.1442 0.1770 0.1678 0.1040  -0.0356 -0.0714 14  GLU A OE1 
108  O  OE1 B GLU A 14  ? 0.3413 0.4262 0.4608 0.0355  -0.2489 -0.0600 14  GLU A OE1 
109  O  OE2 A GLU A 14  ? 0.3735 0.1181 0.1676 0.0551  0.0089  -0.0113 14  GLU A OE2 
110  O  OE2 B GLU A 14  ? 0.2878 0.3725 0.3463 0.0935  -0.1705 -0.1291 14  GLU A OE2 
111  N  N   . HIS A 15  ? 0.0696 0.1931 0.2315 0.0497  0.0754  0.0168  15  HIS A N   
112  C  CA  . HIS A 15  ? 0.1280 0.1605 0.2298 0.0328  0.0419  -0.0060 15  HIS A CA  
113  C  C   . HIS A 15  ? 0.0882 0.1876 0.2599 0.0597  0.0558  -0.0092 15  HIS A C   
114  O  O   . HIS A 15  ? 0.0463 0.2062 0.2861 0.0435  0.0574  0.0059  15  HIS A O   
115  C  CB  . HIS A 15  ? 0.1007 0.2035 0.2167 0.0691  0.0629  0.0099  15  HIS A CB  
116  C  CG  . HIS A 15  ? 0.1938 0.2519 0.2208 0.1447  0.0679  0.0263  15  HIS A CG  
117  N  ND1 . HIS A 15  ? 0.2088 0.3363 0.3125 0.1843  -0.0190 -0.0493 15  HIS A ND1 
118  C  CD2 . HIS A 15  ? 0.2197 0.2321 0.1937 0.1318  0.0837  0.0337  15  HIS A CD2 
119  C  CE1 . HIS A 15  ? 0.2931 0.3399 0.3134 0.1701  -0.0190 -0.0866 15  HIS A CE1 
120  N  NE2 . HIS A 15  ? 0.2770 0.2696 0.3098 0.1820  0.0556  -0.0487 15  HIS A NE2 
121  N  N   . TRP A 16  ? 0.0804 0.2062 0.1971 0.0502  0.0452  -0.0018 16  TRP A N   
122  C  CA  . TRP A 16  ? 0.0343 0.1859 0.2544 0.0177  0.0309  -0.0158 16  TRP A CA  
123  C  C   . TRP A 16  ? 0.0549 0.2029 0.1962 0.0257  0.0326  0.0077  16  TRP A C   
124  O  O   . TRP A 16  ? 0.0694 0.1808 0.2264 0.0010  0.0062  -0.0024 16  TRP A O   
125  C  CB  . TRP A 16  ? 0.0346 0.1953 0.2103 -0.0003 0.0311  -0.0059 16  TRP A CB  
126  C  CG  . TRP A 16  ? 0.0538 0.2093 0.1671 0.0083  0.0226  0.0052  16  TRP A CG  
127  C  CD1 . TRP A 16  ? 0.0515 0.1862 0.1784 0.0020  0.0527  0.0162  16  TRP A CD1 
128  C  CD2 . TRP A 16  ? 0.0603 0.1806 0.1847 -0.0089 0.0420  0.0067  16  TRP A CD2 
129  N  NE1 . TRP A 16  ? 0.0569 0.2007 0.1797 0.0319  0.0412  -0.0086 16  TRP A NE1 
130  C  CE2 . TRP A 16  ? 0.0548 0.1975 0.1745 0.0163  0.0421  -0.0006 16  TRP A CE2 
131  C  CE3 . TRP A 16  ? 0.0779 0.1500 0.1938 0.0150  0.0471  0.0020  16  TRP A CE3 
132  C  CZ2 . TRP A 16  ? 0.0664 0.1691 0.1748 -0.0055 0.0603  0.0006  16  TRP A CZ2 
133  C  CZ3 . TRP A 16  ? 0.0624 0.1820 0.1831 -0.0019 0.0732  -0.0184 16  TRP A CZ3 
134  C  CH2 . TRP A 16  ? 0.0765 0.1698 0.1727 0.0348  0.0536  -0.0050 16  TRP A CH2 
135  N  N   . HIS A 17  ? 0.0422 0.2165 0.2038 0.0475  0.0225  -0.0138 17  HIS A N   
136  C  CA  . HIS A 17  ? 0.0761 0.2110 0.2136 -0.0071 0.0179  0.0150  17  HIS A CA  
137  C  C   . HIS A 17  ? 0.0856 0.2437 0.2547 -0.0267 0.0236  0.0113  17  HIS A C   
138  O  O   . HIS A 17  ? 0.0697 0.2323 0.2664 -0.0070 -0.0018 0.0165  17  HIS A O   
139  C  CB  . HIS A 17  ? 0.1091 0.1998 0.2129 0.0453  -0.0050 0.0225  17  HIS A CB  
140  C  CG  . HIS A 17  ? 0.0897 0.2235 0.2300 0.0390  0.0032  0.0505  17  HIS A CG  
141  N  ND1 . HIS A 17  ? 0.0974 0.2637 0.2949 0.0114  0.0010  0.0560  17  HIS A ND1 
142  C  CD2 . HIS A 17  ? 0.1254 0.2224 0.2576 0.0768  0.0212  0.0879  17  HIS A CD2 
143  C  CE1 . HIS A 17  ? 0.1526 0.3597 0.2784 0.1049  -0.0078 0.0322  17  HIS A CE1 
144  N  NE2 . HIS A 17  ? 0.1332 0.3258 0.2456 0.0979  0.0289  0.1026  17  HIS A NE2 
145  N  N   . LYS A 18  ? 0.0603 0.2381 0.2595 0.0100  0.0187  0.0226  18  LYS A N   
146  C  CA  . LYS A 18  ? 0.0840 0.3080 0.2965 0.0015  0.0731  0.0611  18  LYS A CA  
147  C  C   . LYS A 18  ? 0.0849 0.2537 0.3792 -0.0223 0.0204  0.0425  18  LYS A C   
148  O  O   . LYS A 18  ? 0.0642 0.3035 0.5071 -0.0447 -0.0392 0.0697  18  LYS A O   
149  C  CB  . LYS A 18  ? 0.0732 0.3035 0.2787 -0.0013 0.0178  0.0502  18  LYS A CB  
150  C  CG  . LYS A 18  ? 0.1000 0.3184 0.2540 0.0536  0.0730  0.0559  18  LYS A CG  
151  C  CD  . LYS A 18  ? 0.1147 0.3183 0.2305 0.0407  0.0210  0.0258  18  LYS A CD  
152  C  CE  . LYS A 18  ? 0.1235 0.2346 0.2604 0.1043  0.0052  0.0480  18  LYS A CE  
153  N  NZ  . LYS A 18  ? 0.0921 0.2915 0.2847 0.0906  0.0612  0.0458  18  LYS A NZ  
154  N  N   . ASP A 19  ? 0.0652 0.2468 0.3011 -0.0016 0.0527  0.0268  19  ASP A N   
155  C  CA  . ASP A 19  ? 0.1235 0.2222 0.2995 -0.0132 0.0675  0.0029  19  ASP A CA  
156  C  C   . ASP A 19  ? 0.0718 0.2054 0.3594 -0.0063 0.0685  0.0331  19  ASP A C   
157  O  O   . ASP A 19  ? 0.1095 0.1881 0.3239 -0.0261 0.0265  0.0438  19  ASP A O   
158  C  CB  . ASP A 19  ? 0.1212 0.4023 0.2631 -0.0223 0.0670  0.0216  19  ASP A CB  
159  C  CG  . ASP A 19  ? 0.0846 0.6371 0.4017 -0.0125 0.1044  -0.0398 19  ASP A CG  
160  O  OD1 . ASP A 19  ? 0.1626 0.6807 0.4124 -0.1210 0.1530  -0.0601 19  ASP A OD1 
161  O  OD2 . ASP A 19  ? 0.5131 0.7419 0.5218 -0.1821 0.1846  -0.1722 19  ASP A OD2 
162  N  N   . PHE A 20  ? 0.0682 0.2183 0.2538 -0.0121 0.0500  0.0072  20  PHE A N   
163  C  CA  . PHE A 20  ? 0.0525 0.1952 0.2427 -0.0128 0.0513  0.0171  20  PHE A CA  
164  C  C   . PHE A 20  ? 0.0632 0.2127 0.2323 -0.0189 0.0438  0.0092  20  PHE A C   
165  O  O   . PHE A 20  ? 0.0734 0.2002 0.2150 -0.0254 0.0341  0.0178  20  PHE A O   
166  C  CB  . PHE A 20  ? 0.1027 0.2203 0.2312 -0.0392 0.0145  0.0308  20  PHE A CB  
167  C  CG  . PHE A 20  ? 0.0806 0.2911 0.2268 -0.0692 0.0343  0.0422  20  PHE A CG  
168  C  CD1 . PHE A 20  ? 0.1321 0.3069 0.2791 -0.0785 -0.0071 0.0694  20  PHE A CD1 
169  C  CD2 . PHE A 20  ? 0.1492 0.2843 0.2598 -0.0330 0.0100  0.0467  20  PHE A CD2 
170  C  CE1 . PHE A 20  ? 0.1517 0.3463 0.2696 -0.0550 0.0215  0.0921  20  PHE A CE1 
171  C  CE2 . PHE A 20  ? 0.1269 0.3678 0.2423 -0.0148 0.0201  0.0228  20  PHE A CE2 
172  C  CZ  . PHE A 20  ? 0.0851 0.3623 0.2904 -0.0801 0.0292  0.0937  20  PHE A CZ  
173  N  N   . PRO A 21  ? 0.0516 0.2276 0.2766 -0.0352 0.0407  0.0144  21  PRO A N   
174  C  CA  . PRO A 21  ? 0.0704 0.2727 0.2570 -0.0726 0.0096  0.0328  21  PRO A CA  
175  C  C   . PRO A 21  ? 0.0824 0.1974 0.2300 -0.0445 0.0048  0.0153  21  PRO A C   
176  O  O   . PRO A 21  ? 0.0815 0.2064 0.2197 0.0032  -0.0067 0.0050  21  PRO A O   
177  C  CB  . PRO A 21  ? 0.1152 0.3078 0.2683 -0.0947 0.0000  0.0171  21  PRO A CB  
178  C  CG  . PRO A 21  ? 0.2540 0.2973 0.3224 -0.1428 -0.0208 0.0270  21  PRO A CG  
179  C  CD  . PRO A 21  ? 0.1014 0.2262 0.2593 -0.0581 0.0244  0.0467  21  PRO A CD  
180  N  N   . ILE A 22  ? 0.0533 0.2139 0.2208 -0.0227 0.0114  -0.0194 22  ILE A N   
181  C  CA  . ILE A 22  ? 0.0661 0.1967 0.2124 -0.0139 0.0145  0.0027  22  ILE A CA  
182  C  C   . ILE A 22  ? 0.0524 0.1932 0.1788 -0.0162 0.0127  0.0137  22  ILE A C   
183  O  O   . ILE A 22  ? 0.0503 0.2240 0.1870 -0.0159 0.0252  -0.0071 22  ILE A O   
184  C  CB  . ILE A 22  ? 0.0795 0.1977 0.1866 0.0042  -0.0019 -0.0198 22  ILE A CB  
185  C  CG1 . ILE A 22  ? 0.0943 0.1874 0.2192 -0.0263 0.0258  -0.0534 22  ILE A CG1 
186  C  CG2 . ILE A 22  ? 0.0712 0.1769 0.2230 -0.0313 -0.0242 0.0138  22  ILE A CG2 
187  C  CD1 . ILE A 22  ? 0.1490 0.2088 0.3047 -0.0422 0.0421  0.0140  22  ILE A CD1 
188  N  N   . ALA A 23  ? 0.0545 0.1779 0.1928 -0.0078 0.0200  0.0040  23  ALA A N   
189  C  CA  . ALA A 23  ? 0.0707 0.1812 0.1935 -0.0091 0.0326  -0.0073 23  ALA A CA  
190  C  C   . ALA A 23  ? 0.0572 0.1984 0.1862 0.0122  0.0283  -0.0232 23  ALA A C   
191  O  O   . ALA A 23  ? 0.0828 0.1863 0.1802 0.0004  0.0310  -0.0064 23  ALA A O   
192  C  CB  . ALA A 23  ? 0.0675 0.2013 0.1867 0.0124  0.0286  0.0034  23  ALA A CB  
193  N  N   . LYS A 24  ? 0.0901 0.2178 0.1708 0.0178  0.0132  -0.0230 24  LYS A N   
194  C  CA  . LYS A 24  ? 0.0813 0.2361 0.1791 0.0087  0.0008  -0.0109 24  LYS A CA  
195  C  C   . LYS A 24  ? 0.1046 0.2691 0.2018 0.0046  0.0109  -0.0087 24  LYS A C   
196  O  O   . LYS A 24  ? 0.1373 0.3024 0.2269 -0.0210 -0.0323 0.0272  24  LYS A O   
197  C  CB  . LYS A 24  ? 0.1072 0.2567 0.2111 0.0425  -0.0141 0.0261  24  LYS A CB  
198  C  CG  . LYS A 24  ? 0.1095 0.2541 0.2205 0.0325  0.0018  0.0125  24  LYS A CG  
199  C  CD  . LYS A 24  ? 0.1061 0.3533 0.3235 0.0458  0.0034  0.0678  24  LYS A CD  
200  C  CE  . LYS A 24  ? 0.2954 0.4498 0.3130 0.0033  0.0726  -0.0248 24  LYS A CE  
201  N  NZ  . LYS A 24  ? 0.1386 0.4679 0.5075 0.0277  -0.0018 0.0006  24  LYS A NZ  
202  N  N   . GLY A 25  ? 0.0811 0.2477 0.1859 -0.0031 0.0207  -0.0100 25  GLY A N   
203  C  CA  . GLY A 25  ? 0.0806 0.2719 0.1951 -0.0097 0.0129  -0.0317 25  GLY A CA  
204  C  C   . GLY A 25  ? 0.0709 0.2226 0.1643 0.0218  -0.0198 -0.0114 25  GLY A C   
205  O  O   . GLY A 25  ? 0.1075 0.2492 0.1705 0.0149  -0.0214 -0.0107 25  GLY A O   
206  N  N   . GLU A 26  ? 0.0941 0.2761 0.1391 -0.0072 -0.0097 -0.0524 26  GLU A N   
207  C  CA  . GLU A 26  ? 0.1091 0.3207 0.1402 -0.0390 -0.0183 -0.0276 26  GLU A CA  
208  C  C   . GLU A 26  ? 0.0906 0.2554 0.1504 -0.0088 -0.0082 0.0031  26  GLU A C   
209  O  O   . GLU A 26  ? 0.1481 0.2864 0.1380 -0.0429 -0.0156 0.0187  26  GLU A O   
210  C  CB  . GLU A 26  ? 0.1244 0.3834 0.1869 -0.0438 -0.0476 -0.0979 26  GLU A CB  
211  C  CG  . GLU A 26  ? 0.0952 0.4493 0.2095 -0.0177 -0.0255 -0.0295 26  GLU A CG  
212  C  CD  . GLU A 26  ? 0.2016 0.4983 0.2600 -0.0198 -0.1417 -0.0049 26  GLU A CD  
213  O  OE1 . GLU A 26  ? 0.3190 0.5482 0.3053 -0.0609 -0.1228 -0.0068 26  GLU A OE1 
214  O  OE2 . GLU A 26  ? 0.2454 0.5908 0.3684 0.0772  -0.0883 0.0529  26  GLU A OE2 
215  N  N   . ARG A 27  ? 0.1009 0.1757 0.1483 -0.0117 -0.0086 -0.0017 27  ARG A N   
216  C  CA  . ARG A 27  ? 0.0867 0.1830 0.1319 0.0008  0.0133  -0.0269 27  ARG A CA  
217  C  C   . ARG A 27  ? 0.0598 0.1630 0.1109 0.0006  0.0367  -0.0005 27  ARG A C   
218  O  O   . ARG A 27  ? 0.0718 0.1464 0.1304 -0.0004 0.0054  -0.0082 27  ARG A O   
219  C  CB  . ARG A 27  ? 0.1630 0.1655 0.1239 0.0051  0.0044  -0.0262 27  ARG A CB  
220  C  CG  . ARG A 27  ? 0.1429 0.1815 0.2036 -0.0188 0.0150  -0.0122 27  ARG A CG  
221  C  CD  . ARG A 27  ? 0.2039 0.2355 0.1806 0.0423  -0.0029 -0.0018 27  ARG A CD  
222  N  NE  . ARG A 27  ? 0.2061 0.2002 0.1654 0.0049  0.0317  -0.0055 27  ARG A NE  
223  C  CZ  . ARG A 27  ? 0.1522 0.1981 0.1122 -0.0088 0.0395  0.0128  27  ARG A CZ  
224  N  NH1 . ARG A 27  ? 0.1689 0.2362 0.1445 0.0084  0.0263  -0.0555 27  ARG A NH1 
225  N  NH2 . ARG A 27  ? 0.1738 0.2233 0.1540 -0.0289 0.0165  -0.0311 27  ARG A NH2 
226  N  N   . GLN A 28  ? 0.0613 0.1596 0.1256 -0.0110 0.0333  -0.0226 28  GLN A N   
227  C  CA  . GLN A 28  ? 0.0497 0.1468 0.1284 -0.0057 0.0306  -0.0253 28  GLN A CA  
228  C  C   . GLN A 28  ? 0.0359 0.1190 0.1294 0.0075  0.0253  -0.0036 28  GLN A C   
229  O  O   . GLN A 28  ? 0.0745 0.1582 0.1138 -0.0013 0.0274  -0.0011 28  GLN A O   
230  C  CB  . GLN A 28  ? 0.0553 0.1486 0.1385 0.0071  0.0326  -0.0189 28  GLN A CB  
231  C  CG  . GLN A 28  ? 0.0641 0.1457 0.1608 0.0133  0.0273  -0.0133 28  GLN A CG  
232  C  CD  . GLN A 28  ? 0.0684 0.1694 0.1418 -0.0162 0.0229  -0.0265 28  GLN A CD  
233  O  OE1 . GLN A 28  ? 0.0675 0.1596 0.1359 -0.0075 0.0292  -0.0036 28  GLN A OE1 
234  N  NE2 . GLN A 28  ? 0.0567 0.1526 0.1454 -0.0102 0.0021  -0.0138 28  GLN A NE2 
235  N  N   . SER A 29  ? 0.0480 0.1312 0.1190 0.0114  0.0226  -0.0095 29  SER A N   
236  C  CA  . SER A 29  ? 0.0445 0.1171 0.1402 0.0136  0.0225  -0.0117 29  SER A CA  
237  C  C   . SER A 29  ? 0.0436 0.1195 0.1129 0.0078  0.0223  0.0062  29  SER A C   
238  O  O   . SER A 29  ? 0.0558 0.1507 0.1292 0.0053  0.0405  0.0006  29  SER A O   
239  C  CB  . SER A 29  ? 0.0300 0.1447 0.1197 0.0105  0.0233  -0.0159 29  SER A CB  
240  O  OG  . SER A 29  ? 0.0434 0.1253 0.1201 -0.0026 0.0290  -0.0145 29  SER A OG  
241  N  N   . PRO A 30  ? 0.0415 0.1320 0.1146 0.0062  0.0193  0.0063  30  PRO A N   
242  C  CA  . PRO A 30  ? 0.0560 0.1472 0.1313 -0.0377 0.0064  0.0185  30  PRO A CA  
243  C  C   . PRO A 30  ? 0.0560 0.1251 0.1192 0.0181  0.0359  0.0107  30  PRO A C   
244  O  O   . PRO A 30  ? 0.0714 0.1522 0.1043 0.0091  0.0186  -0.0078 30  PRO A O   
245  C  CB  . PRO A 30  ? 0.0707 0.1228 0.1295 0.0089  0.0343  -0.0110 30  PRO A CB  
246  C  CG  . PRO A 30  ? 0.0545 0.1276 0.1110 0.0005  0.0217  -0.0149 30  PRO A CG  
247  C  CD  . PRO A 30  ? 0.0427 0.1323 0.1122 0.0041  0.0403  -0.0094 30  PRO A CD  
248  N  N   . VAL A 31  ? 0.0774 0.1335 0.1156 0.0033  0.0344  0.0190  31  VAL A N   
249  C  CA  . VAL A 31  ? 0.0684 0.1421 0.1066 0.0062  0.0509  0.0151  31  VAL A CA  
250  C  C   . VAL A 31  ? 0.0838 0.1457 0.1018 0.0117  0.0253  0.0013  31  VAL A C   
251  O  O   . VAL A 31  ? 0.0779 0.1386 0.1225 0.0019  0.0100  0.0089  31  VAL A O   
252  C  CB  . VAL A 31  ? 0.0833 0.1393 0.1348 0.0168  0.0273  -0.0100 31  VAL A CB  
253  C  CG1 . VAL A 31  ? 0.0691 0.1794 0.1441 -0.0153 0.0214  -0.0174 31  VAL A CG1 
254  C  CG2 . VAL A 31  ? 0.0741 0.1385 0.1600 0.0113  0.0359  -0.0110 31  VAL A CG2 
255  N  N   . ASP A 32  ? 0.0960 0.1402 0.1203 0.0050  0.0095  0.0203  32  ASP A N   
256  C  CA  . ASP A 32  ? 0.0765 0.1141 0.1388 0.0196  0.0397  -0.0008 32  ASP A CA  
257  C  C   . ASP A 32  ? 0.0971 0.1597 0.1237 0.0164  0.0381  -0.0164 32  ASP A C   
258  O  O   . ASP A 32  ? 0.0983 0.1752 0.1344 0.0212  0.0334  -0.0203 32  ASP A O   
259  C  CB  . ASP A 32  ? 0.0933 0.1318 0.1546 0.0211  0.0245  0.0131  32  ASP A CB  
260  C  CG  . ASP A 32  ? 0.1084 0.1342 0.1298 0.0391  0.0494  -0.0055 32  ASP A CG  
261  O  OD1 . ASP A 32  ? 0.1079 0.1515 0.1190 0.0171  0.0223  0.0069  32  ASP A OD1 
262  O  OD2 . ASP A 32  ? 0.1658 0.1747 0.1324 -0.0185 0.0154  0.0228  32  ASP A OD2 
263  N  N   . ILE A 33  ? 0.0750 0.1479 0.1213 0.0190  0.0477  -0.0038 33  ILE A N   
264  C  CA  . ILE A 33  ? 0.1097 0.1447 0.1187 0.0350  0.0651  0.0055  33  ILE A CA  
265  C  C   . ILE A 33  ? 0.1352 0.1407 0.1174 0.0273  0.0596  0.0042  33  ILE A C   
266  O  O   . ILE A 33  ? 0.1239 0.1659 0.1217 0.0095  0.0461  0.0075  33  ILE A O   
267  C  CB  . ILE A 33  ? 0.0865 0.1564 0.1364 0.0089  0.0629  0.0200  33  ILE A CB  
268  C  CG1 . ILE A 33  ? 0.0812 0.1542 0.1400 -0.0065 0.0238  0.0265  33  ILE A CG1 
269  C  CG2 . ILE A 33  ? 0.0960 0.1985 0.1342 0.0270  0.0593  -0.0009 33  ILE A CG2 
270  C  CD1 . ILE A 33  ? 0.0933 0.1905 0.1687 0.0100  0.0136  0.0286  33  ILE A CD1 
271  N  N   A ASP A 34  ? 0.1428 0.1622 0.1084 0.0376  0.0579  0.0037  34  ASP A N   
272  N  N   B ASP A 34  ? 0.1323 0.1551 0.1102 0.0364  0.0527  0.0064  34  ASP A N   
273  C  CA  A ASP A 34  ? 0.1985 0.1909 0.1210 0.0220  0.0691  0.0210  34  ASP A CA  
274  C  CA  B ASP A 34  ? 0.1683 0.1860 0.1223 0.0167  0.0488  0.0264  34  ASP A CA  
275  C  C   A ASP A 34  ? 0.2025 0.1751 0.1224 0.0286  0.0779  0.0361  34  ASP A C   
276  C  C   B ASP A 34  ? 0.1881 0.1562 0.1226 0.0427  0.0712  0.0359  34  ASP A C   
277  O  O   A ASP A 34  ? 0.3021 0.2359 0.1239 0.0559  0.0702  0.0022  34  ASP A O   
278  O  O   B ASP A 34  ? 0.2010 0.1694 0.1417 0.0864  0.0912  0.0377  34  ASP A O   
279  C  CB  A ASP A 34  ? 0.2247 0.1987 0.1339 0.0465  0.0499  0.0378  34  ASP A CB  
280  C  CB  B ASP A 34  ? 0.1999 0.1831 0.1237 0.0177  0.0286  0.0386  34  ASP A CB  
281  C  CG  A ASP A 34  ? 0.2804 0.1698 0.1921 0.0399  0.0510  0.0305  34  ASP A CG  
282  C  CG  B ASP A 34  ? 0.1949 0.2122 0.1668 -0.0115 0.0337  0.0629  34  ASP A CG  
283  O  OD1 A ASP A 34  ? 0.3105 0.1872 0.2228 0.0829  0.0791  0.0604  34  ASP A OD1 
284  O  OD1 B ASP A 34  ? 0.2111 0.2697 0.0974 -0.0309 0.0715  0.0407  34  ASP A OD1 
285  O  OD2 A ASP A 34  ? 0.3090 0.2438 0.2200 0.0905  0.0767  -0.0113 34  ASP A OD2 
286  O  OD2 B ASP A 34  ? 0.1982 0.2670 0.1831 0.0039  0.0230  0.0629  34  ASP A OD2 
287  N  N   . THR A 35  ? 0.1629 0.1799 0.1562 0.0433  0.0683  0.0315  35  THR A N   
288  C  CA  . THR A 35  ? 0.1806 0.2088 0.1831 0.0838  0.0885  0.0146  35  THR A CA  
289  C  C   . THR A 35  ? 0.2600 0.2027 0.1751 0.0798  0.0746  0.0060  35  THR A C   
290  O  O   . THR A 35  ? 0.2681 0.2529 0.2093 0.1023  0.1110  0.0591  35  THR A O   
291  C  CB  . THR A 35  ? 0.2255 0.2400 0.1938 0.0612  0.0268  0.0441  35  THR A CB  
292  O  OG1 . THR A 35  ? 0.1824 0.2201 0.2020 -0.0044 0.0818  0.0452  35  THR A OG1 
293  C  CG2 . THR A 35  ? 0.1880 0.2606 0.1768 0.0392  0.0299  0.0081  35  THR A CG2 
294  N  N   . HIS A 36  ? 0.2208 0.2280 0.1442 0.0516  0.0995  0.0399  36  HIS A N   
295  C  CA  . HIS A 36  ? 0.2876 0.1971 0.1578 0.0118  0.1177  0.0429  36  HIS A CA  
296  C  C   . HIS A 36  ? 0.3618 0.2552 0.0995 0.0425  0.0500  0.0411  36  HIS A C   
297  O  O   . HIS A 36  ? 0.3006 0.3553 0.1311 0.0387  0.0477  -0.0013 36  HIS A O   
298  C  CB  . HIS A 36  ? 0.3759 0.2061 0.1895 0.0195  0.0677  0.0486  36  HIS A CB  
299  C  CG  . HIS A 36  ? 0.5158 0.1971 0.2860 0.0423  0.0473  0.0256  36  HIS A CG  
300  N  ND1 . HIS A 36  ? 0.5096 0.2881 0.2419 -0.0587 -0.1047 0.0281  36  HIS A ND1 
301  C  CD2 . HIS A 36  ? 0.6089 0.2372 0.1766 0.1220  -0.0685 0.0247  36  HIS A CD2 
302  C  CE1 . HIS A 36  ? 0.7788 0.4657 0.4589 -0.0543 -0.1597 -0.1424 36  HIS A CE1 
303  N  NE2 . HIS A 36  ? 0.8243 0.1784 0.3456 0.1209  -0.1064 0.0111  36  HIS A NE2 
304  N  N   . THR A 37  ? 0.3793 0.2102 0.1447 0.0675  0.0971  0.0373  37  THR A N   
305  C  CA  . THR A 37  ? 0.4117 0.2172 0.1418 0.0747  0.0648  0.0367  37  THR A CA  
306  C  C   . THR A 37  ? 0.3155 0.2237 0.1683 0.0559  0.0495  0.0201  37  THR A C   
307  O  O   . THR A 37  ? 0.4527 0.2488 0.1691 0.0964  -0.0217 0.0011  37  THR A O   
308  C  CB  . THR A 37  ? 0.3572 0.2104 0.4079 0.1045  -0.0864 0.0148  37  THR A CB  
309  O  OG1 . THR A 37  ? 0.3402 0.2405 0.4308 0.0876  0.0072  0.0598  37  THR A OG1 
310  C  CG2 . THR A 37  ? 0.4128 0.3124 0.2476 0.1557  -0.0617 -0.0505 37  THR A CG2 
311  N  N   . ALA A 38  ? 0.2519 0.2143 0.1445 0.0558  0.0650  0.0250  38  ALA A N   
312  C  CA  . ALA A 38  ? 0.2350 0.2147 0.1231 0.0976  0.0604  -0.0085 38  ALA A CA  
313  C  C   . ALA A 38  ? 0.2179 0.2124 0.2409 0.0550  0.1016  0.0038  38  ALA A C   
314  O  O   . ALA A 38  ? 0.2474 0.2452 0.3581 0.0419  0.1592  0.0143  38  ALA A O   
315  C  CB  . ALA A 38  ? 0.2359 0.1784 0.1540 0.0363  0.0240  0.0003  38  ALA A CB  
316  N  N   A LYS A 39  ? 0.2670 0.2327 0.1411 0.0563  0.0993  0.0076  39  LYS A N   
317  N  N   B LYS A 39  ? 0.2454 0.2309 0.2165 0.1100  0.0429  -0.0111 39  LYS A N   
318  C  CA  A LYS A 39  ? 0.2539 0.2909 0.1134 0.0669  0.0873  0.0179  39  LYS A CA  
319  C  CA  B LYS A 39  ? 0.1953 0.3310 0.2563 0.1242  0.0436  -0.0041 39  LYS A CA  
320  C  C   A LYS A 39  ? 0.2014 0.2806 0.1284 0.0514  0.0958  -0.0179 39  LYS A C   
321  C  C   B LYS A 39  ? 0.1650 0.3144 0.2111 0.0450  0.0091  -0.0065 39  LYS A C   
322  O  O   A LYS A 39  ? 0.1490 0.2860 0.1668 0.0455  0.0797  0.0206  39  LYS A O   
323  O  O   B LYS A 39  ? 0.0969 0.3007 0.1547 0.0264  0.0141  -0.0201 39  LYS A O   
324  C  CB  A LYS A 39  ? 0.2330 0.2858 0.1181 0.0936  0.0707  0.0200  39  LYS A CB  
325  C  CB  B LYS A 39  ? 0.1520 0.4685 0.2789 0.1486  -0.0433 -0.0286 39  LYS A CB  
326  C  CG  A LYS A 39  ? 0.2325 0.3261 0.1924 0.0495  0.1100  0.0774  39  LYS A CG  
327  C  CG  B LYS A 39  ? 0.2800 0.5521 0.2147 0.1125  -0.0414 -0.0413 39  LYS A CG  
328  C  CD  A LYS A 39  ? 0.2363 0.2979 0.2744 0.0081  0.0509  0.0155  39  LYS A CD  
329  C  CD  B LYS A 39  ? 0.1468 0.3886 0.1689 0.0335  -0.0266 0.0548  39  LYS A CD  
330  C  CE  A LYS A 39  ? 0.3231 0.3306 0.1529 -0.0155 0.0498  0.0625  39  LYS A CE  
331  C  CE  B LYS A 39  ? 0.1723 0.3534 0.1938 0.0406  -0.0141 0.0990  39  LYS A CE  
332  N  NZ  A LYS A 39  ? 0.3098 0.2662 0.2552 -0.0363 0.1456  0.0600  39  LYS A NZ  
333  N  NZ  B LYS A 39  ? 0.2655 0.3670 0.3169 0.0234  -0.0974 0.0531  39  LYS A NZ  
334  N  N   . TYR A 40  ? 0.2404 0.3363 0.1733 -0.0133 0.0567  0.0167  40  TYR A N   
335  C  CA  . TYR A 40  ? 0.1651 0.3064 0.2039 -0.0359 0.1256  -0.0230 40  TYR A CA  
336  C  C   . TYR A 40  ? 0.1161 0.2946 0.1594 -0.0091 0.0413  -0.0203 40  TYR A C   
337  O  O   . TYR A 40  ? 0.1708 0.3560 0.1349 0.0343  0.0473  -0.0263 40  TYR A O   
338  C  CB  . TYR A 40  ? 0.1914 0.4188 0.2156 -0.1067 0.1022  -0.0103 40  TYR A CB  
339  C  CG  . TYR A 40  ? 0.2613 0.5274 0.2948 -0.0639 0.0273  0.0034  40  TYR A CG  
340  C  CD1 . TYR A 40  ? 0.2013 0.5023 0.2310 -0.1694 0.0452  -0.0260 40  TYR A CD1 
341  C  CD2 . TYR A 40  ? 0.3223 0.6827 0.3778 0.0156  0.0990  0.0179  40  TYR A CD2 
342  C  CE1 . TYR A 40  ? 0.1859 0.7312 0.1966 -0.1216 0.0427  0.0637  40  TYR A CE1 
343  C  CE2 . TYR A 40  ? 0.3537 0.7577 0.1847 0.0341  0.1115  0.0468  40  TYR A CE2 
344  C  CZ  . TYR A 40  ? 0.2092 0.7755 0.2141 0.0431  -0.0147 -0.0070 40  TYR A CZ  
345  O  OH  . TYR A 40  ? 0.2020 1.1047 0.3166 0.1322  0.0356  -0.0632 40  TYR A OH  
346  N  N   . ASP A 41  ? 0.1400 0.3055 0.1870 0.0447  0.0637  -0.0084 41  ASP A N   
347  C  CA  . ASP A 41  ? 0.1754 0.2827 0.2049 0.0780  0.0356  0.0019  41  ASP A CA  
348  C  C   . ASP A 41  ? 0.2230 0.4268 0.2014 0.1678  0.0744  0.0091  41  ASP A C   
349  O  O   . ASP A 41  ? 0.1975 0.4251 0.1759 0.1157  0.0495  -0.0129 41  ASP A O   
350  C  CB  . ASP A 41  ? 0.2147 0.2449 0.2575 -0.0036 -0.0044 -0.0032 41  ASP A CB  
351  C  CG  . ASP A 41  ? 0.2352 0.3011 0.2541 0.0344  -0.0102 -0.0538 41  ASP A CG  
352  O  OD1 . ASP A 41  ? 0.2975 0.3202 0.2470 0.0955  -0.0086 -0.0969 41  ASP A OD1 
353  O  OD2 . ASP A 41  ? 0.2415 0.3236 0.3310 -0.0612 -0.0352 -0.0449 41  ASP A OD2 
354  N  N   . PRO A 42  ? 0.1862 0.6107 0.2251 0.2009  0.0934  0.0526  42  PRO A N   
355  C  CA  . PRO A 42  ? 0.1763 0.5897 0.2946 0.1617  0.0767  0.1158  42  PRO A CA  
356  C  C   . PRO A 42  ? 0.2238 0.5008 0.2509 0.1761  0.1072  0.0390  42  PRO A C   
357  O  O   . PRO A 42  ? 0.2497 0.7271 0.3776 0.2476  0.0800  0.0655  42  PRO A O   
358  C  CB  . PRO A 42  ? 0.2109 0.6685 0.2591 0.1206  0.1265  0.0474  42  PRO A CB  
359  C  CG  . PRO A 42  ? 0.1917 0.8769 0.2807 0.0819  0.1105  0.0086  42  PRO A CG  
360  C  CD  . PRO A 42  ? 0.3692 0.8500 0.1808 0.3243  0.1060  0.0726  42  PRO A CD  
361  N  N   . SER A 43  ? 0.2269 0.4728 0.2233 0.1292  0.0072  -0.0384 43  SER A N   
362  C  CA  . SER A 43  ? 0.3844 0.3896 0.2630 0.1118  -0.0660 -0.0872 43  SER A CA  
363  C  C   . SER A 43  ? 0.3314 0.4040 0.2726 0.0946  -0.0097 -0.0889 43  SER A C   
364  O  O   . SER A 43  ? 0.4678 0.3916 0.3628 0.1683  0.1114  -0.0838 43  SER A O   
365  C  CB  . SER A 43  ? 0.3247 0.3456 0.4584 0.1848  -0.1225 -0.1581 43  SER A CB  
366  O  OG  . SER A 43  ? 0.3799 0.3658 0.4080 0.1513  -0.1054 -0.1071 43  SER A OG  
367  N  N   . LEU A 44  ? 0.2215 0.4398 0.2017 0.0890  0.0054  -0.0728 44  LEU A N   
368  C  CA  . LEU A 44  ? 0.1835 0.5304 0.1798 0.0477  0.0121  -0.0436 44  LEU A CA  
369  C  C   . LEU A 44  ? 0.2002 0.7477 0.2774 0.0189  0.0087  0.1152  44  LEU A C   
370  O  O   . LEU A 44  ? 0.2778 0.8492 0.2055 -0.0619 0.0067  0.1252  44  LEU A O   
371  C  CB  . LEU A 44  ? 0.1322 0.4828 0.1829 -0.0328 0.0150  -0.0693 44  LEU A CB  
372  C  CG  . LEU A 44  ? 0.1367 0.3389 0.1845 -0.0385 0.0255  -0.0074 44  LEU A CG  
373  C  CD1 . LEU A 44  ? 0.2179 0.3457 0.1618 -0.0306 0.0785  -0.0307 44  LEU A CD1 
374  C  CD2 . LEU A 44  ? 0.1294 0.3269 0.2271 -0.0211 0.0132  0.0308  44  LEU A CD2 
375  N  N   . LYS A 45  ? 0.1216 0.7755 0.2713 0.0680  0.0268  0.1359  45  LYS A N   
376  C  CA  . LYS A 45  ? 0.2690 0.5301 0.5665 0.0697  -0.1922 0.0703  45  LYS A CA  
377  C  C   . LYS A 45  ? 0.2946 0.8158 0.4138 -0.0710 -0.0983 0.0809  45  LYS A C   
378  O  O   . LYS A 45  ? 0.1723 1.1229 0.3565 -0.1175 0.0572  -0.0719 45  LYS A O   
379  C  CB  . LYS A 45  ? 0.3430 0.5762 0.2960 0.2811  0.0900  0.0568  45  LYS A CB  
380  C  CG  . LYS A 45  ? 0.2551 0.6890 0.4327 0.1662  -0.1005 0.0157  45  LYS A CG  
381  C  CD  . LYS A 45  ? 0.4273 0.4374 1.0872 -0.2188 -0.1576 0.1488  45  LYS A CD  
382  C  CE  . LYS A 45  ? 1.0465 1.0767 0.9428 0.5072  0.2582  -0.2982 45  LYS A CE  
383  N  NZ  . LYS A 45  ? 0.5121 0.9724 1.4895 0.2011  -0.3386 0.2100  45  LYS A NZ  
384  N  N   . PRO A 46  ? 0.1375 0.8694 0.3506 0.0308  0.0513  0.0826  46  PRO A N   
385  C  CA  . PRO A 46  ? 0.1535 1.0045 0.2002 -0.1238 0.0299  0.2088  46  PRO A CA  
386  C  C   . PRO A 46  ? 0.1176 0.4433 0.2314 -0.0639 0.0106  0.0375  46  PRO A C   
387  O  O   . PRO A 46  ? 0.1396 0.4162 0.3173 -0.0690 -0.0529 0.0770  46  PRO A O   
388  C  CB  . PRO A 46  ? 0.1867 1.0969 0.3231 0.0157  -0.0403 -0.0756 46  PRO A CB  
389  C  CG  . PRO A 46  ? 0.2544 1.3899 0.4285 0.2103  -0.0079 -0.1481 46  PRO A CG  
390  C  CD  . PRO A 46  ? 0.3622 0.9212 0.3258 0.4756  -0.0478 -0.0723 46  PRO A CD  
391  N  N   . LEU A 47  ? 0.2142 0.4446 0.3069 -0.0451 0.0655  0.1181  47  LEU A N   
392  C  CA  . LEU A 47  ? 0.0736 0.4575 0.2578 -0.0834 0.0061  0.1088  47  LEU A CA  
393  C  C   . LEU A 47  ? 0.1452 0.3204 0.3603 -0.1032 -0.0647 0.1307  47  LEU A C   
394  O  O   . LEU A 47  ? 0.1237 0.3883 0.4461 -0.1263 -0.0537 0.1834  47  LEU A O   
395  C  CB  . LEU A 47  ? 0.3314 0.4001 0.4233 0.0517  -0.1130 0.1307  47  LEU A CB  
396  C  CG  . LEU A 47  ? 0.2339 0.4178 0.5365 -0.0150 -0.0893 -0.0222 47  LEU A CG  
397  C  CD1 . LEU A 47  ? 0.1661 0.4028 0.4922 -0.0021 -0.0414 0.0192  47  LEU A CD1 
398  C  CD2 . LEU A 47  ? 0.1955 0.3065 0.6869 -0.0864 -0.1507 0.0353  47  LEU A CD2 
399  N  N   . SER A 48  ? 0.1090 0.2280 0.2132 -0.0113 0.0074  0.0491  48  SER A N   
400  C  CA  . SER A 48  ? 0.1067 0.2400 0.2159 0.0099  0.0253  0.0237  48  SER A CA  
401  C  C   . SER A 48  ? 0.1101 0.2205 0.1987 -0.0188 0.0171  0.0311  48  SER A C   
402  O  O   . SER A 48  ? 0.0867 0.2131 0.2226 -0.0279 0.0424  -0.0117 48  SER A O   
403  C  CB  . SER A 48  ? 0.1065 0.2606 0.2730 0.0322  0.0148  0.0080  48  SER A CB  
404  O  OG  . SER A 48  ? 0.1225 0.2676 0.3025 0.0223  0.0397  0.0421  48  SER A OG  
405  N  N   . VAL A 49  ? 0.1197 0.2203 0.2249 -0.0261 0.0219  0.0206  49  VAL A N   
406  C  CA  . VAL A 49  ? 0.1658 0.2391 0.2258 -0.0478 0.0122  0.0076  49  VAL A CA  
407  C  C   . VAL A 49  ? 0.1230 0.2570 0.2402 -0.0646 -0.0033 0.0137  49  VAL A C   
408  O  O   . VAL A 49  ? 0.1389 0.3492 0.2915 -0.1228 0.0143  0.0190  49  VAL A O   
409  C  CB  . VAL A 49  ? 0.1650 0.2578 0.2400 -0.0499 0.0325  -0.0395 49  VAL A CB  
410  C  CG1 . VAL A 49  ? 0.3747 0.3121 0.3209 -0.0423 0.1719  -0.0553 49  VAL A CG1 
411  C  CG2 . VAL A 49  ? 0.1704 0.2591 0.3417 -0.0528 0.0254  0.0184  49  VAL A CG2 
412  N  N   . SER A 50  ? 0.1262 0.2273 0.2264 -0.0497 0.0074  0.0075  50  SER A N   
413  C  CA  . SER A 50  ? 0.1137 0.2549 0.2727 -0.0395 0.0302  0.0263  50  SER A CA  
414  C  C   . SER A 50  ? 0.0847 0.2984 0.2498 0.0065  0.0048  0.0525  50  SER A C   
415  O  O   . SER A 50  ? 0.1676 0.2407 0.3043 -0.0219 -0.0220 0.0600  50  SER A O   
416  C  CB  . SER A 50  ? 0.3295 0.2896 0.4073 0.0073  0.1316  -0.0211 50  SER A CB  
417  O  OG  . SER A 50  ? 0.3536 0.6484 0.4417 0.0087  0.0803  -0.2440 50  SER A OG  
418  N  N   . TYR A 51  ? 0.1258 0.2547 0.3209 -0.0384 0.0011  0.0158  51  TYR A N   
419  C  CA  . TYR A 51  ? 0.1493 0.2645 0.2459 -0.0120 -0.0436 0.0242  51  TYR A CA  
420  C  C   . TYR A 51  ? 0.1572 0.3361 0.3325 0.0207  -0.0702 0.0650  51  TYR A C   
421  O  O   . TYR A 51  ? 0.1949 0.3568 0.2615 -0.0535 -0.0617 0.0637  51  TYR A O   
422  C  CB  . TYR A 51  ? 0.0955 0.2662 0.2319 -0.0126 -0.0286 0.0150  51  TYR A CB  
423  C  CG  . TYR A 51  ? 0.1163 0.2481 0.2113 -0.0341 -0.0386 0.0203  51  TYR A CG  
424  C  CD1 . TYR A 51  ? 0.0951 0.2080 0.2086 -0.0414 0.0026  0.0406  51  TYR A CD1 
425  C  CD2 . TYR A 51  ? 0.1025 0.2345 0.1658 -0.0373 0.0185  0.0303  51  TYR A CD2 
426  C  CE1 . TYR A 51  ? 0.0802 0.1817 0.2082 -0.0159 0.0162  0.0355  51  TYR A CE1 
427  C  CE2 . TYR A 51  ? 0.1147 0.2080 0.1806 -0.0535 0.0087  0.0317  51  TYR A CE2 
428  C  CZ  . TYR A 51  ? 0.1201 0.1903 0.1578 -0.0249 0.0023  0.0216  51  TYR A CZ  
429  O  OH  . TYR A 51  ? 0.0995 0.1830 0.1723 -0.0231 0.0100  0.0109  51  TYR A OH  
430  N  N   . ASP A 52  ? 0.1129 0.4561 0.3521 -0.0416 -0.0590 0.1382  52  ASP A N   
431  C  CA  . ASP A 52  ? 0.1513 0.5098 0.3540 -0.0467 -0.0662 0.1854  52  ASP A CA  
432  C  C   . ASP A 52  ? 0.2068 0.3637 0.2868 -0.0162 -0.0624 0.0863  52  ASP A C   
433  O  O   . ASP A 52  ? 0.2602 0.5268 0.3227 -0.0194 -0.0951 0.0983  52  ASP A O   
434  C  CB  . ASP A 52  ? 0.2711 0.6365 0.4773 -0.0064 0.1081  0.1588  52  ASP A CB  
435  C  CG  . ASP A 52  ? 0.2177 1.0590 0.8545 -0.0247 0.2209  -0.1274 52  ASP A CG  
436  O  OD1 . ASP A 52  ? 0.3580 1.2460 0.9948 0.0417  -0.2165 -0.3687 52  ASP A OD1 
437  O  OD2 . ASP A 52  ? 0.6973 1.4644 1.6695 0.3838  0.4401  0.1636  52  ASP A OD2 
438  N  N   . GLN A 53  ? 0.1438 0.3219 0.3345 -0.0025 -0.0104 0.0640  53  GLN A N   
439  C  CA  . GLN A 53  ? 0.1993 0.2964 0.3571 -0.0148 -0.0042 0.0460  53  GLN A CA  
440  C  C   . GLN A 53  ? 0.2021 0.2533 0.2931 0.0526  -0.0414 -0.0012 53  GLN A C   
441  O  O   . GLN A 53  ? 0.2011 0.3205 0.2760 0.0313  -0.0120 0.0370  53  GLN A O   
442  C  CB  . GLN A 53  ? 0.4627 0.3317 0.4763 0.1949  -0.0105 0.0050  53  GLN A CB  
443  C  CG  . GLN A 53  ? 0.5140 0.4515 0.7134 0.0732  0.1832  0.1053  53  GLN A CG  
444  C  CD  . GLN A 53  ? 0.6792 0.8338 0.8638 0.1117  -0.0228 -0.0815 53  GLN A CD  
445  O  OE1 . GLN A 53  ? 0.8911 1.2206 0.9375 0.4105  0.0728  -0.1304 53  GLN A OE1 
446  N  NE2 . GLN A 53  ? 0.6452 1.0954 0.8726 0.0019  -0.1661 -0.3643 53  GLN A NE2 
447  N  N   . ALA A 54  ? 0.1683 0.2244 0.2896 0.0130  0.0000  0.0111  54  ALA A N   
448  C  CA  . ALA A 54  ? 0.1630 0.2383 0.2104 0.0406  -0.0030 -0.0053 54  ALA A CA  
449  C  C   . ALA A 54  ? 0.1998 0.2581 0.2127 -0.0093 0.0185  -0.0611 54  ALA A C   
450  O  O   . ALA A 54  ? 0.2575 0.4416 0.3578 -0.0390 -0.0633 -0.1597 54  ALA A O   
451  C  CB  . ALA A 54  ? 0.2286 0.1773 0.3030 0.0354  0.0501  -0.0198 54  ALA A CB  
452  N  N   . THR A 55  ? 0.1544 0.2381 0.2308 0.0449  0.0220  0.0357  55  THR A N   
453  C  CA  . THR A 55  ? 0.2359 0.2799 0.2280 0.0877  0.0304  0.0328  55  THR A CA  
454  C  C   . THR A 55  ? 0.1741 0.2685 0.1454 0.0287  0.0072  0.0429  55  THR A C   
455  O  O   . THR A 55  ? 0.1641 0.2258 0.1955 0.0414  0.0140  0.0690  55  THR A O   
456  C  CB  . THR A 55  ? 0.3478 0.3193 0.3375 0.0807  0.0231  0.1273  55  THR A CB  
457  O  OG1 . THR A 55  ? 0.4146 0.2731 0.4983 0.0961  -0.0456 -0.0190 55  THR A OG1 
458  C  CG2 . THR A 55  ? 0.3316 0.3550 0.3241 0.1286  0.0232  0.1595  55  THR A CG2 
459  N  N   . SER A 56  ? 0.1939 0.2509 0.1817 0.0449  -0.0454 0.0212  56  SER A N   
460  C  CA  . SER A 56  ? 0.2538 0.2556 0.1709 0.0450  0.0297  0.0361  56  SER A CA  
461  C  C   . SER A 56  ? 0.2804 0.2740 0.1786 0.0902  0.0359  0.0538  56  SER A C   
462  O  O   . SER A 56  ? 0.3384 0.3458 0.1605 0.1242  -0.0153 0.0390  56  SER A O   
463  C  CB  . SER A 56  ? 0.2911 0.2451 0.1752 0.0336  -0.0715 0.0457  56  SER A CB  
464  O  OG  . SER A 56  ? 0.2572 0.2738 0.1725 0.0294  -0.0438 0.0263  56  SER A OG  
465  N  N   . LEU A 57  ? 0.2653 0.2406 0.1744 0.0897  0.0520  0.0647  57  LEU A N   
466  C  CA  . LEU A 57  ? 0.3055 0.2418 0.2193 0.0859  0.0873  0.0647  57  LEU A CA  
467  C  C   . LEU A 57  ? 0.2908 0.2337 0.1673 0.0913  0.0731  0.0734  57  LEU A C   
468  O  O   . LEU A 57  ? 0.3003 0.2578 0.1544 0.0502  0.0110  0.0514  57  LEU A O   
469  C  CB  . LEU A 57  ? 0.4160 0.1946 0.2709 -0.0047 0.1020  0.0697  57  LEU A CB  
470  C  CG  . LEU A 57  ? 0.3961 0.2098 0.3976 0.0119  0.0316  0.0499  57  LEU A CG  
471  C  CD1 . LEU A 57  ? 0.3982 0.2979 0.4543 -0.1415 0.1215  0.0513  57  LEU A CD1 
472  C  CD2 . LEU A 57  ? 0.6338 0.2340 0.4505 0.1236  -0.0725 0.0932  57  LEU A CD2 
473  N  N   . ARG A 58  ? 0.2212 0.2267 0.1562 0.0517  0.0200  0.0381  58  ARG A N   
474  C  CA  . ARG A 58  ? 0.2185 0.1932 0.1630 0.0414  0.0361  0.0409  58  ARG A CA  
475  C  C   . ARG A 58  ? 0.2057 0.1716 0.1517 -0.0083 0.0253  0.0377  58  ARG A C   
476  O  O   . ARG A 58  ? 0.2970 0.1946 0.1338 0.0366  0.0458  0.0257  58  ARG A O   
477  C  CB  . ARG A 58  ? 0.2647 0.2213 0.1648 0.0190  0.0275  0.0290  58  ARG A CB  
478  C  CG  . ARG A 58  ? 0.1795 0.3098 0.2648 -0.0760 0.0508  0.0604  58  ARG A CG  
479  C  CD  . ARG A 58  ? 0.2469 0.2984 0.2298 -0.1116 -0.0195 0.0206  58  ARG A CD  
480  N  NE  . ARG A 58  ? 0.2237 0.2289 0.2476 -0.0450 -0.0326 0.0249  58  ARG A NE  
481  C  CZ  . ARG A 58  ? 0.2285 0.2187 0.1520 -0.0566 0.0132  0.0221  58  ARG A CZ  
482  N  NH1 . ARG A 58  ? 0.2681 0.2389 0.1874 -0.0416 0.0413  0.0421  58  ARG A NH1 
483  N  NH2 . ARG A 58  ? 0.2060 0.2100 0.2100 -0.0428 0.0023  0.0337  58  ARG A NH2 
484  N  N   . ILE A 59  ? 0.2930 0.1758 0.1324 0.0160  0.0076  0.0051  59  ILE A N   
485  C  CA  . ILE A 59  ? 0.1909 0.1806 0.1558 -0.0025 0.0274  0.0223  59  ILE A CA  
486  C  C   . ILE A 59  ? 0.1662 0.2080 0.1223 -0.0601 0.0222  0.0414  59  ILE A C   
487  O  O   . ILE A 59  ? 0.2430 0.2398 0.1037 0.0034  0.0192  0.0326  59  ILE A O   
488  C  CB  . ILE A 59  ? 0.2509 0.1883 0.1353 -0.0377 -0.0293 0.0265  59  ILE A CB  
489  C  CG1 . ILE A 59  ? 0.2224 0.1845 0.1339 -0.0177 0.0052  0.0270  59  ILE A CG1 
490  C  CG2 . ILE A 59  ? 0.2398 0.2039 0.1269 -0.0013 -0.0205 0.0177  59  ILE A CG2 
491  C  CD1 . ILE A 59  ? 0.2230 0.1885 0.1712 -0.0298 -0.0089 0.0599  59  ILE A CD1 
492  N  N   . LEU A 60  ? 0.1878 0.1630 0.1287 -0.0114 0.0097  0.0053  60  LEU A N   
493  C  CA  . LEU A 60  ? 0.1901 0.1887 0.1214 -0.0055 -0.0012 0.0331  60  LEU A CA  
494  C  C   . LEU A 60  ? 0.2030 0.1932 0.1143 0.0249  0.0203  -0.0063 60  LEU A C   
495  O  O   . LEU A 60  ? 0.1461 0.1781 0.1189 -0.0072 0.0306  0.0150  60  LEU A O   
496  C  CB  . LEU A 60  ? 0.1781 0.1863 0.2027 -0.0364 0.0197  0.0179  60  LEU A CB  
497  C  CG  . LEU A 60  ? 0.1736 0.1636 0.1603 -0.0223 0.0116  0.0207  60  LEU A CG  
498  C  CD1 . LEU A 60  ? 0.2517 0.1944 0.1506 -0.0431 0.0283  0.0097  60  LEU A CD1 
499  C  CD2 . LEU A 60  ? 0.2508 0.1521 0.1899 -0.0128 -0.0049 0.0109  60  LEU A CD2 
500  N  N   . ASN A 61  ? 0.1877 0.1579 0.1049 -0.0207 0.0369  -0.0024 61  ASN A N   
501  C  CA  . ASN A 61  ? 0.1540 0.1763 0.1286 -0.0127 0.0412  -0.0189 61  ASN A CA  
502  C  C   . ASN A 61  ? 0.1562 0.1659 0.1287 -0.0200 0.0401  -0.0106 61  ASN A C   
503  O  O   . ASN A 61  ? 0.2580 0.1647 0.1279 -0.0411 0.0428  0.0161  61  ASN A O   
504  C  CB  . ASN A 61  ? 0.2025 0.1457 0.1436 -0.0179 0.0561  -0.0105 61  ASN A CB  
505  C  CG  . ASN A 61  ? 0.2279 0.1697 0.1190 -0.0143 0.0399  -0.0279 61  ASN A CG  
506  O  OD1 . ASN A 61  ? 0.2321 0.1601 0.1391 -0.0597 0.0567  0.0144  61  ASN A OD1 
507  N  ND2 . ASN A 61  ? 0.2411 0.1558 0.1056 -0.0461 0.0864  -0.0105 61  ASN A ND2 
508  N  N   . ASN A 62  ? 0.1945 0.1301 0.1297 -0.0469 0.0446  -0.0041 62  ASN A N   
509  C  CA  . ASN A 62  ? 0.1820 0.1931 0.1446 -0.0454 0.0339  -0.0102 62  ASN A CA  
510  C  C   . ASN A 62  ? 0.1860 0.1996 0.1238 -0.0545 0.0562  0.0134  62  ASN A C   
511  O  O   . ASN A 62  ? 0.2329 0.2141 0.1531 -0.0945 0.0727  0.0073  62  ASN A O   
512  C  CB  . ASN A 62  ? 0.2210 0.1720 0.1280 -0.0425 0.0168  0.0020  62  ASN A CB  
513  C  CG  . ASN A 62  ? 0.1957 0.1502 0.1353 -0.0195 0.0410  -0.0040 62  ASN A CG  
514  O  OD1 . ASN A 62  ? 0.1787 0.1529 0.1690 -0.0175 0.0580  0.0206  62  ASN A OD1 
515  N  ND2 . ASN A 62  ? 0.3166 0.2086 0.1540 0.0497  0.0623  -0.0267 62  ASN A ND2 
516  N  N   . GLY A 63  ? 0.1974 0.1870 0.1154 -0.0380 0.0549  0.0256  63  GLY A N   
517  C  CA  . GLY A 63  ? 0.1461 0.1898 0.1438 -0.0358 0.0893  0.0192  63  GLY A CA  
518  C  C   . GLY A 63  ? 0.1514 0.1538 0.1482 -0.0278 0.0528  -0.0034 63  GLY A C   
519  O  O   . GLY A 63  ? 0.1582 0.1733 0.1603 -0.0104 0.0595  0.0073  63  GLY A O   
520  N  N   . HIS A 64  ? 0.1413 0.1855 0.1279 -0.0377 0.0488  0.0010  64  HIS A N   
521  C  CA  . HIS A 64  ? 0.1382 0.1805 0.1500 -0.0480 0.0625  0.0189  64  HIS A CA  
522  C  C   . HIS A 64  ? 0.1156 0.1690 0.1478 -0.0417 0.0259  0.0320  64  HIS A C   
523  O  O   . HIS A 64  ? 0.1098 0.2169 0.2983 -0.0268 0.0214  0.1158  64  HIS A O   
524  C  CB  . HIS A 64  ? 0.1350 0.1905 0.1447 -0.0661 0.0290  0.0132  64  HIS A CB  
525  C  CG  . HIS A 64  ? 0.1267 0.1806 0.1446 -0.0401 0.0296  -0.0052 64  HIS A CG  
526  N  ND1 . HIS A 64  ? 0.1287 0.2394 0.1664 -0.0403 0.0411  -0.0052 64  HIS A ND1 
527  C  CD2 . HIS A 64  ? 0.1701 0.2086 0.1503 -0.0792 0.0576  -0.0344 64  HIS A CD2 
528  C  CE1 . HIS A 64  ? 0.1206 0.2353 0.1949 -0.0450 0.0757  -0.0397 64  HIS A CE1 
529  N  NE2 . HIS A 64  ? 0.1571 0.2220 0.2278 -0.0766 0.0499  -0.0273 64  HIS A NE2 
530  N  N   . ALA A 65  ? 0.1287 0.1687 0.1276 -0.0237 0.0324  0.0027  65  ALA A N   
531  C  CA  . ALA A 65  ? 0.1366 0.1736 0.1355 -0.0350 0.0421  0.0311  65  ALA A CA  
532  C  C   . ALA A 65  ? 0.1260 0.1592 0.1152 -0.0280 0.0257  -0.0006 65  ALA A C   
533  O  O   . ALA A 65  ? 0.1719 0.1944 0.1304 -0.0444 0.0410  0.0280  65  ALA A O   
534  C  CB  . ALA A 65  ? 0.1326 0.1745 0.1318 -0.0298 0.0458  0.0298  65  ALA A CB  
535  N  N   . PHE A 66  ? 0.1183 0.1414 0.1237 -0.0245 0.0239  -0.0033 66  PHE A N   
536  C  CA  . PHE A 66  ? 0.1738 0.1578 0.1215 0.0047  0.0291  -0.0055 66  PHE A CA  
537  C  C   . PHE A 66  ? 0.1698 0.1554 0.0897 -0.0099 0.0204  -0.0044 66  PHE A C   
538  O  O   . PHE A 66  ? 0.1661 0.1569 0.0989 -0.0055 0.0256  0.0094  66  PHE A O   
539  C  CB  . PHE A 66  ? 0.1457 0.1920 0.1279 -0.0271 0.0194  0.0074  66  PHE A CB  
540  C  CG  . PHE A 66  ? 0.1743 0.1637 0.1097 -0.0196 0.0265  -0.0048 66  PHE A CG  
541  C  CD1 . PHE A 66  ? 0.1669 0.1741 0.0973 -0.0115 0.0227  -0.0020 66  PHE A CD1 
542  C  CD2 . PHE A 66  ? 0.1860 0.1718 0.1190 -0.0109 0.0341  -0.0095 66  PHE A CD2 
543  C  CE1 . PHE A 66  ? 0.1188 0.2006 0.1163 -0.0002 0.0097  0.0089  66  PHE A CE1 
544  C  CE2 . PHE A 66  ? 0.1921 0.1244 0.1331 -0.0128 0.0088  -0.0041 66  PHE A CE2 
545  C  CZ  . PHE A 66  ? 0.1969 0.1869 0.1239 -0.0129 0.0037  0.0073  66  PHE A CZ  
546  N  N   . ASN A 67  ? 0.1985 0.1482 0.1000 0.0062  0.0244  0.0027  67  ASN A N   
547  C  CA  . ASN A 67  ? 0.1791 0.1445 0.1111 -0.0116 0.0311  0.0074  67  ASN A CA  
548  C  C   . ASN A 67  ? 0.1992 0.1632 0.1366 0.0054  0.0389  0.0541  67  ASN A C   
549  O  O   . ASN A 67  ? 0.2254 0.1858 0.1034 -0.0042 0.0279  0.0264  67  ASN A O   
550  C  CB  . ASN A 67  ? 0.1665 0.1574 0.1147 -0.0197 0.0446  0.0059  67  ASN A CB  
551  C  CG  . ASN A 67  ? 0.1454 0.1504 0.1502 -0.0362 0.0496  0.0002  67  ASN A CG  
552  O  OD1 . ASN A 67  ? 0.1659 0.1705 0.1698 -0.0364 0.0106  0.0163  67  ASN A OD1 
553  N  ND2 . ASN A 67  ? 0.1465 0.1758 0.2314 -0.0476 0.0370  0.0003  67  ASN A ND2 
554  N  N   . VAL A 68  ? 0.1608 0.1489 0.1492 0.0220  0.0176  0.0248  68  VAL A N   
555  C  CA  . VAL A 68  ? 0.1952 0.1493 0.1144 0.0522  0.0159  0.0263  68  VAL A CA  
556  C  C   . VAL A 68  ? 0.1716 0.1641 0.1381 0.0372  -0.0005 0.0137  68  VAL A C   
557  O  O   . VAL A 68  ? 0.2074 0.1709 0.1223 0.0451  0.0034  0.0111  68  VAL A O   
558  C  CB  . VAL A 68  ? 0.1982 0.1528 0.1964 0.0466  -0.0031 0.0197  68  VAL A CB  
559  C  CG1 . VAL A 68  ? 0.1302 0.2141 0.2177 0.0161  -0.0006 0.0019  68  VAL A CG1 
560  C  CG2 . VAL A 68  ? 0.1776 0.1835 0.1375 0.0483  0.0082  0.0000  68  VAL A CG2 
561  N  N   . GLU A 69  ? 0.2341 0.1544 0.1479 0.0403  0.0317  0.0296  69  GLU A N   
562  C  CA  . GLU A 69  ? 0.1845 0.1784 0.1380 0.0267  0.0543  0.0330  69  GLU A CA  
563  C  C   . GLU A 69  ? 0.1834 0.1490 0.1615 0.0368  0.0194  0.0318  69  GLU A C   
564  O  O   . GLU A 69  ? 0.2448 0.1969 0.1621 0.0293  -0.0009 0.0135  69  GLU A O   
565  C  CB  . GLU A 69  ? 0.1492 0.2102 0.1923 0.0039  0.0524  0.0403  69  GLU A CB  
566  C  CG  . GLU A 69  ? 0.1757 0.2336 0.1967 0.0359  0.0743  0.0368  69  GLU A CG  
567  C  CD  . GLU A 69  ? 0.1802 0.2762 0.2477 0.0036  0.0570  0.0949  69  GLU A CD  
568  O  OE1 . GLU A 69  ? 0.2237 0.2294 0.1952 0.0111  0.0414  0.0423  69  GLU A OE1 
569  O  OE2 . GLU A 69  ? 0.1488 0.2251 0.2518 -0.0192 0.0593  0.0031  69  GLU A OE2 
570  N  N   . PHE A 70  ? 0.2016 0.1848 0.1357 0.0270  0.0322  0.0245  70  PHE A N   
571  C  CA  . PHE A 70  ? 0.1874 0.1694 0.1623 0.0323  0.0233  0.0557  70  PHE A CA  
572  C  C   . PHE A 70  ? 0.2043 0.1967 0.1776 0.0223  0.0218  0.0193  70  PHE A C   
573  O  O   . PHE A 70  ? 0.1924 0.1648 0.1949 0.0247  0.0252  0.0377  70  PHE A O   
574  C  CB  . PHE A 70  ? 0.1669 0.1831 0.1398 0.0070  0.0093  0.0411  70  PHE A CB  
575  C  CG  . PHE A 70  ? 0.1490 0.1714 0.1493 0.0172  0.0129  0.0293  70  PHE A CG  
576  C  CD1 . PHE A 70  ? 0.1849 0.1802 0.1450 0.0275  0.0017  0.0418  70  PHE A CD1 
577  C  CD2 . PHE A 70  ? 0.1366 0.2064 0.1388 0.0163  0.0255  0.0391  70  PHE A CD2 
578  C  CE1 . PHE A 70  ? 0.2002 0.1845 0.1456 0.0362  0.0040  0.0307  70  PHE A CE1 
579  C  CE2 . PHE A 70  ? 0.1817 0.1903 0.2031 0.0221  0.0050  0.0331  70  PHE A CE2 
580  C  CZ  . PHE A 70  ? 0.1960 0.2194 0.1346 0.0462  0.0135  -0.0109 70  PHE A CZ  
581  N  N   . ASP A 71  ? 0.2770 0.1766 0.2056 0.0497  -0.0214 0.0469  71  ASP A N   
582  C  CA  . ASP A 71  ? 0.2547 0.1949 0.2423 0.0523  -0.0309 0.0420  71  ASP A CA  
583  C  C   . ASP A 71  ? 0.1694 0.1429 0.2739 -0.0163 0.0154  0.0097  71  ASP A C   
584  O  O   . ASP A 71  ? 0.1683 0.1985 0.3636 -0.0223 0.0666  0.0131  71  ASP A O   
585  C  CB  . ASP A 71  ? 0.3601 0.2006 0.2954 0.0174  -0.1277 0.0803  71  ASP A CB  
586  C  CG  . ASP A 71  ? 0.4093 0.2276 0.3891 0.0970  -0.1527 0.0606  71  ASP A CG  
587  O  OD1 . ASP A 71  ? 0.3187 0.2072 0.5008 0.0907  -0.0851 0.0927  71  ASP A OD1 
588  O  OD2 . ASP A 71  ? 0.3753 0.2463 0.7637 0.0677  -0.1951 0.1213  71  ASP A OD2 
589  N  N   . ASP A 72  ? 0.1461 0.1641 0.2785 0.0104  -0.0208 0.0321  72  ASP A N   
590  C  CA  . ASP A 72  ? 0.1551 0.1682 0.3033 -0.0400 -0.0043 0.0026  72  ASP A CA  
591  C  C   . ASP A 72  ? 0.2973 0.1770 0.3601 -0.0275 0.0400  0.0321  72  ASP A C   
592  O  O   . ASP A 72  ? 0.3658 0.1729 0.3963 -0.0497 0.0046  0.0033  72  ASP A O   
593  C  CB  . ASP A 72  ? 0.2204 0.2060 0.2238 -0.0128 0.0356  0.0873  72  ASP A CB  
594  C  CG  . ASP A 72  ? 0.2251 0.3531 0.2614 -0.0111 0.0116  0.1293  72  ASP A CG  
595  O  OD1 . ASP A 72  ? 0.2193 0.5303 0.2958 -0.0265 0.0309  0.2066  72  ASP A OD1 
596  O  OD2 . ASP A 72  ? 0.1835 0.4140 0.2020 -0.0420 0.0232  0.0960  72  ASP A OD2 
597  N  N   . SER A 73  ? 0.2448 0.1632 0.3876 -0.0223 0.0432  0.0686  73  SER A N   
598  C  CA  . SER A 73  ? 0.4811 0.1759 0.2964 -0.0306 0.0945  0.0447  73  SER A CA  
599  C  C   . SER A 73  ? 0.6248 0.1747 0.4211 -0.0006 0.1753  -0.0217 73  SER A C   
600  O  O   . SER A 73  ? 0.7480 0.1741 0.3519 0.0684  0.0912  -0.0054 73  SER A O   
601  C  CB  . SER A 73  ? 0.5199 0.3228 0.2804 -0.0740 0.0119  0.0765  73  SER A CB  
602  O  OG  . SER A 73  ? 0.4001 0.2169 0.3078 0.0537  0.0456  0.0666  73  SER A OG  
603  N  N   . GLN A 74  ? 0.5197 0.1727 0.5689 0.0256  0.1943  -0.0157 74  GLN A N   
604  C  CA  . GLN A 74  ? 0.3574 0.2296 0.6520 0.0373  0.0914  0.0377  74  GLN A CA  
605  C  C   . GLN A 74  ? 0.3699 0.3574 0.2712 0.0192  0.0026  -0.0781 74  GLN A C   
606  O  O   . GLN A 74  ? 0.2708 0.2588 0.3206 -0.0064 -0.0844 -0.0041 74  GLN A O   
607  C  CB  . GLN A 74  ? 0.4782 0.4016 0.6103 0.2883  0.0618  0.0064  74  GLN A CB  
608  C  CG  . GLN A 74  ? 0.2798 0.5192 0.7064 0.1778  0.0873  0.0864  74  GLN A CG  
609  C  CD  . GLN A 74  ? 0.5167 0.6725 0.8525 0.1145  -0.3587 0.0992  74  GLN A CD  
610  O  OE1 . GLN A 74  ? 0.9680 0.7802 0.8143 -0.3088 0.1236  -0.0414 74  GLN A OE1 
611  N  NE2 . GLN A 74  ? 0.5190 0.2550 0.9697 0.0769  -0.1718 -0.0274 74  GLN A NE2 
612  N  N   . ASP A 75  ? 0.3856 0.5899 0.2962 0.0196  0.0409  -0.1214 75  ASP A N   
613  C  CA  . ASP A 75  ? 0.3281 0.5972 0.3653 -0.1717 -0.0126 -0.0992 75  ASP A CA  
614  C  C   . ASP A 75  ? 0.4244 0.3677 0.6087 -0.0939 -0.0810 -0.1720 75  ASP A C   
615  O  O   . ASP A 75  ? 0.5445 0.8283 0.9289 0.0493  -0.2207 -0.1038 75  ASP A O   
616  C  CB  . ASP A 75  ? 0.3877 0.6966 0.4682 -0.0370 -0.0831 -0.2979 75  ASP A CB  
617  C  CG  . ASP A 75  ? 0.7093 0.7846 0.3091 0.0417  0.0044  -0.0965 75  ASP A CG  
618  O  OD1 . ASP A 75  ? 0.3294 0.9447 0.3504 -0.1676 0.0297  0.0050  75  ASP A OD1 
619  O  OD2 . ASP A 75  ? 0.8704 0.8005 0.5513 -0.0206 0.3702  -0.1401 75  ASP A OD2 
620  N  N   . LYS A 76  ? 0.3365 0.2536 0.3352 -0.0455 -0.1231 0.0780  76  LYS A N   
621  C  CA  . LYS A 76  ? 0.4426 0.2346 0.4471 -0.1017 -0.1092 0.0638  76  LYS A CA  
622  C  C   . LYS A 76  ? 0.5204 0.2591 0.5612 0.0886  -0.0038 0.1236  76  LYS A C   
623  O  O   . LYS A 76  ? 0.4571 0.4709 0.7580 -0.0070 -0.0358 0.1132  76  LYS A O   
624  C  CB  . LYS A 76  ? 0.4860 0.2979 0.3895 -0.1372 -0.1575 0.1483  76  LYS A CB  
625  C  CG  . LYS A 76  ? 0.8214 0.2018 0.4699 -0.0697 -0.1099 0.1032  76  LYS A CG  
626  C  CD  . LYS A 76  ? 1.0259 0.4350 0.4672 -0.2347 -0.0717 0.1481  76  LYS A CD  
627  C  CE  . LYS A 76  ? 1.0039 0.5985 0.3968 -0.0312 0.1831  0.1576  76  LYS A CE  
628  N  NZ  . LYS A 76  ? 0.5650 0.4818 0.6014 0.2222  0.2232  0.3071  76  LYS A NZ  
629  N  N   . ALA A 77  ? 0.3119 0.3052 0.3440 0.0234  -0.0994 0.1050  77  ALA A N   
630  C  CA  . ALA A 77  ? 0.1641 0.2615 0.2762 -0.0416 -0.0609 0.0460  77  ALA A CA  
631  C  C   . ALA A 77  ? 0.1154 0.2851 0.2743 0.0005  -0.0586 0.0627  77  ALA A C   
632  O  O   . ALA A 77  ? 0.1198 0.3193 0.3775 -0.0144 -0.0550 -0.0199 77  ALA A O   
633  C  CB  . ALA A 77  ? 0.2466 0.3475 0.2678 0.0102  -0.0687 -0.0104 77  ALA A CB  
634  N  N   . VAL A 78  ? 0.1490 0.2032 0.2314 -0.0026 -0.0499 0.0342  78  VAL A N   
635  C  CA  . VAL A 78  ? 0.1867 0.1930 0.2219 0.0141  -0.0439 0.0345  78  VAL A CA  
636  C  C   . VAL A 78  ? 0.1254 0.2027 0.2185 -0.0127 -0.0306 0.0178  78  VAL A C   
637  O  O   . VAL A 78  ? 0.1104 0.1870 0.2908 -0.0070 -0.0356 0.0082  78  VAL A O   
638  C  CB  . VAL A 78  ? 0.2147 0.2953 0.2845 0.0688  -0.0185 -0.0122 78  VAL A CB  
639  C  CG1 . VAL A 78  ? 0.3877 0.2321 0.3563 0.0614  -0.1419 0.0559  78  VAL A CG1 
640  C  CG2 . VAL A 78  ? 0.2170 0.3396 0.3202 0.0283  0.0369  -0.0178 78  VAL A CG2 
641  N  N   . LEU A 79  ? 0.1055 0.1709 0.1910 0.0111  -0.0050 0.0097  79  LEU A N   
642  C  CA  . LEU A 79  ? 0.0889 0.1748 0.2071 -0.0010 0.0301  0.0095  79  LEU A CA  
643  C  C   . LEU A 79  ? 0.0980 0.1830 0.1736 -0.0057 0.0277  0.0173  79  LEU A C   
644  O  O   . LEU A 79  ? 0.1177 0.1916 0.2208 -0.0154 0.0381  -0.0271 79  LEU A O   
645  C  CB  . LEU A 79  ? 0.1025 0.1775 0.2405 0.0093  0.0240  0.0311  79  LEU A CB  
646  C  CG  . LEU A 79  ? 0.0978 0.1957 0.1960 0.0027  0.0355  0.0146  79  LEU A CG  
647  C  CD1 . LEU A 79  ? 0.0867 0.2042 0.3696 0.0081  0.0646  0.0745  79  LEU A CD1 
648  C  CD2 . LEU A 79  ? 0.1082 0.1568 0.2336 0.0147  0.0491  0.0241  79  LEU A CD2 
649  N  N   A LYS A 80  ? 0.0903 0.1935 0.1819 0.0176  0.0447  0.0051  80  LYS A N   
650  N  N   B LYS A 80  ? 0.0885 0.2111 0.1872 0.0016  0.0355  0.0083  80  LYS A N   
651  C  CA  A LYS A 80  ? 0.1276 0.2141 0.1822 0.0160  0.0602  0.0083  80  LYS A CA  
652  C  CA  B LYS A 80  ? 0.1155 0.2099 0.2039 -0.0005 0.0458  0.0049  80  LYS A CA  
653  C  C   A LYS A 80  ? 0.0908 0.2168 0.2190 -0.0139 0.0754  -0.0087 80  LYS A C   
654  C  C   B LYS A 80  ? 0.0707 0.2158 0.2177 -0.0139 0.0578  -0.0022 80  LYS A C   
655  O  O   A LYS A 80  ? 0.1393 0.1919 0.2052 0.0033  0.0248  0.0189  80  LYS A O   
656  O  O   B LYS A 80  ? 0.0817 0.2091 0.2072 -0.0107 0.0223  0.0154  80  LYS A O   
657  C  CB  A LYS A 80  ? 0.1581 0.2308 0.2271 0.0313  0.0791  0.0203  80  LYS A CB  
658  C  CB  B LYS A 80  ? 0.1894 0.1949 0.2772 0.0245  0.0600  0.0583  80  LYS A CB  
659  C  CG  A LYS A 80  ? 0.1357 0.2017 0.2201 0.0835  0.1111  0.0075  80  LYS A CG  
660  C  CG  B LYS A 80  ? 0.1996 0.2108 0.3265 0.0015  0.0591  0.0942  80  LYS A CG  
661  C  CD  A LYS A 80  ? 0.1578 0.2499 0.2990 0.1106  0.1424  0.0429  80  LYS A CD  
662  C  CD  B LYS A 80  ? 0.1615 0.2820 0.3980 0.0055  0.1024  0.1453  80  LYS A CD  
663  C  CE  A LYS A 80  ? 0.4571 0.4669 0.2814 -0.0173 0.1311  0.1142  80  LYS A CE  
664  C  CE  B LYS A 80  ? 0.0719 0.2153 0.4783 0.0487  0.1357  0.0973  80  LYS A CE  
665  N  NZ  A LYS A 80  ? 0.5632 0.4631 0.4627 0.0745  0.2530  0.0447  80  LYS A NZ  
666  N  NZ  B LYS A 80  ? 0.1212 0.2586 0.6833 0.0080  0.0583  0.0438  80  LYS A NZ  
667  N  N   . GLY A 81  ? 0.1226 0.1878 0.2109 0.0107  0.0692  -0.0037 81  GLY A N   
668  C  CA  . GLY A 81  ? 0.0955 0.1888 0.2544 0.0310  0.0776  0.0333  81  GLY A CA  
669  C  C   . GLY A 81  ? 0.1086 0.1806 0.3086 0.0400  0.0772  0.0080  81  GLY A C   
670  O  O   . GLY A 81  ? 0.1306 0.1939 0.2725 -0.0070 0.0599  0.0110  81  GLY A O   
671  N  N   . GLY A 82  ? 0.0776 0.2059 0.3595 0.0258  0.0686  0.0432  82  GLY A N   
672  C  CA  . GLY A 82  ? 0.1837 0.2206 0.4472 0.0464  0.0642  0.1018  82  GLY A CA  
673  C  C   . GLY A 82  ? 0.1547 0.2572 0.3322 0.0955  0.1231  0.0505  82  GLY A C   
674  O  O   . GLY A 82  ? 0.2164 0.3765 0.2918 0.1699  0.1268  0.0505  82  GLY A O   
675  N  N   . PRO A 83  ? 0.1264 0.2014 0.2404 0.0354  0.0738  0.0361  83  PRO A N   
676  C  CA  . PRO A 83  ? 0.1859 0.2486 0.2129 0.0833  0.0355  -0.0081 83  PRO A CA  
677  C  C   . PRO A 83  ? 0.1447 0.2152 0.2106 0.0807  0.0395  -0.0402 83  PRO A C   
678  O  O   . PRO A 83  ? 0.1909 0.3137 0.2158 0.0666  0.0134  -0.0450 83  PRO A O   
679  C  CB  . PRO A 83  ? 0.1891 0.2588 0.2233 0.0879  0.0158  -0.0262 83  PRO A CB  
680  C  CG  . PRO A 83  ? 0.1030 0.2114 0.2128 0.0069  0.0305  -0.0201 83  PRO A CG  
681  C  CD  . PRO A 83  ? 0.0648 0.1639 0.2465 0.0250  0.0609  0.0186  83  PRO A CD  
682  N  N   . LEU A 84  ? 0.1436 0.1736 0.2088 0.0507  0.0347  -0.0166 84  LEU A N   
683  C  CA  . LEU A 84  ? 0.1411 0.1515 0.1957 0.0322  0.0446  -0.0498 84  LEU A CA  
684  C  C   . LEU A 84  ? 0.1468 0.2122 0.3074 0.0952  0.0282  -0.0663 84  LEU A C   
685  O  O   . LEU A 84  ? 0.1463 0.2325 0.3355 0.0756  0.0363  -0.1124 84  LEU A O   
686  C  CB  . LEU A 84  ? 0.0970 0.1553 0.1859 0.0278  0.0543  -0.0184 84  LEU A CB  
687  C  CG  . LEU A 84  ? 0.0715 0.1569 0.1998 0.0364  0.0439  -0.0206 84  LEU A CG  
688  C  CD1 . LEU A 84  ? 0.1357 0.1540 0.2007 0.0161  0.0344  -0.0255 84  LEU A CD1 
689  C  CD2 . LEU A 84  ? 0.0740 0.1781 0.1971 0.0219  0.0565  -0.0365 84  LEU A CD2 
690  N  N   . ASP A 85  ? 0.2384 0.1865 0.2700 0.0366  0.0666  -0.0824 85  ASP A N   
691  C  CA  . ASP A 85  ? 0.2247 0.1834 0.3959 0.0336  0.0878  -0.0479 85  ASP A CA  
692  C  C   . ASP A 85  ? 0.2276 0.1565 0.4772 0.0400  0.1232  0.0044  85  ASP A C   
693  O  O   . ASP A 85  ? 0.3040 0.2843 0.5256 0.0368  0.1941  -0.1306 85  ASP A O   
694  C  CB  . ASP A 85  ? 0.3779 0.3909 0.5296 -0.0044 0.1514  -0.2778 85  ASP A CB  
695  C  CG  . ASP A 85  ? 0.8390 0.7043 0.5850 0.1407  0.1385  -0.2570 85  ASP A CG  
696  O  OD1 . ASP A 85  ? 1.0784 1.6025 0.5200 -0.3514 -0.0691 -0.4228 85  ASP A OD1 
697  O  OD2 . ASP A 85  ? 0.4294 1.3719 1.3651 -0.0750 0.0089  0.0776  85  ASP A OD2 
698  N  N   . GLY A 86  ? 0.2917 0.2840 0.5914 0.0523  0.0244  -0.0249 86  GLY A N   
699  C  CA  . GLY A 86  ? 0.3080 0.3231 0.4037 -0.0226 0.0441  -0.1345 86  GLY A CA  
700  C  C   . GLY A 86  ? 0.3104 0.3147 0.2576 -0.0584 0.0388  -0.0381 86  GLY A C   
701  O  O   . GLY A 86  ? 0.4272 0.3374 0.3086 -0.1213 0.0660  -0.0199 86  GLY A O   
702  N  N   . THR A 87  ? 0.1571 0.2220 0.2495 0.0480  0.0408  -0.0326 87  THR A N   
703  C  CA  . THR A 87  ? 0.1612 0.3182 0.2444 0.0608  0.0579  -0.0584 87  THR A CA  
704  C  C   . THR A 87  ? 0.0910 0.1860 0.2456 0.0218  0.0219  -0.0552 87  THR A C   
705  O  O   . THR A 87  ? 0.1099 0.1493 0.2915 0.0091  0.0200  -0.0375 87  THR A O   
706  C  CB  . THR A 87  ? 0.1890 0.5316 0.2706 0.2647  -0.0301 -0.0991 87  THR A CB  
707  O  OG1 . THR A 87  ? 0.2660 0.6238 0.3286 0.2070  0.0156  -0.1518 87  THR A OG1 
708  C  CG2 . THR A 87  ? 0.2867 0.4963 0.2874 0.1912  -0.0669 -0.0561 87  THR A CG2 
709  N  N   . TYR A 88  ? 0.0731 0.1641 0.2224 0.0150  0.0299  -0.0244 88  TYR A N   
710  C  CA  . TYR A 88  ? 0.0765 0.1321 0.1953 0.0140  0.0280  -0.0157 88  TYR A CA  
711  C  C   . TYR A 88  ? 0.0585 0.1603 0.2011 0.0259  -0.0017 0.0156  88  TYR A C   
712  O  O   . TYR A 88  ? 0.1056 0.2111 0.2567 -0.0313 -0.0138 0.0266  88  TYR A O   
713  C  CB  . TYR A 88  ? 0.0891 0.1237 0.1758 -0.0038 0.0287  0.0025  88  TYR A CB  
714  C  CG  . TYR A 88  ? 0.0849 0.1233 0.1745 -0.0006 0.0295  -0.0046 88  TYR A CG  
715  C  CD1 . TYR A 88  ? 0.1083 0.1445 0.1716 0.0082  0.0290  -0.0068 88  TYR A CD1 
716  C  CD2 . TYR A 88  ? 0.0837 0.1018 0.1895 0.0037  -0.0055 0.0250  88  TYR A CD2 
717  C  CE1 . TYR A 88  ? 0.1049 0.1608 0.1664 -0.0040 0.0534  -0.0068 88  TYR A CE1 
718  C  CE2 . TYR A 88  ? 0.0797 0.1257 0.1626 -0.0084 0.0317  0.0065  88  TYR A CE2 
719  C  CZ  . TYR A 88  ? 0.1055 0.1028 0.1741 -0.0141 0.0230  -0.0148 88  TYR A CZ  
720  O  OH  . TYR A 88  ? 0.1154 0.1309 0.1669 0.0001  0.0386  -0.0153 88  TYR A OH  
721  N  N   . ARG A 89  ? 0.1252 0.1131 0.1773 0.0312  0.0131  -0.0053 89  ARG A N   
722  C  CA  . ARG A 89  ? 0.1273 0.1110 0.1844 0.0070  -0.0027 0.0135  89  ARG A CA  
723  C  C   . ARG A 89  ? 0.0905 0.1508 0.1502 0.0092  0.0076  0.0209  89  ARG A C   
724  O  O   . ARG A 89  ? 0.0818 0.1386 0.1547 0.0008  0.0094  0.0077  89  ARG A O   
725  C  CB  . ARG A 89  ? 0.1610 0.1459 0.2525 -0.0251 -0.0255 0.0491  89  ARG A CB  
726  C  CG  . ARG A 89  ? 0.3465 0.2669 0.2867 -0.0381 -0.0626 0.1095  89  ARG A CG  
727  C  CD  . ARG A 89  ? 0.2391 0.2193 0.4156 0.0603  0.0211  0.1057  89  ARG A CD  
728  N  NE  . ARG A 89  ? 0.3529 0.2290 0.2481 0.0544  -0.0888 0.0485  89  ARG A NE  
729  C  CZ  . ARG A 89  ? 0.4338 0.2218 0.2770 0.0652  -0.0330 0.0932  89  ARG A CZ  
730  N  NH1 . ARG A 89  ? 0.4764 0.2586 0.3141 0.1047  0.0450  0.1137  89  ARG A NH1 
731  N  NH2 . ARG A 89  ? 0.4560 0.3257 0.4196 0.1551  -0.0858 0.0118  89  ARG A NH2 
732  N  N   . LEU A 90  ? 0.1046 0.1229 0.1583 0.0013  0.0024  0.0103  90  LEU A N   
733  C  CA  . LEU A 90  ? 0.0908 0.1287 0.1571 -0.0114 0.0309  0.0185  90  LEU A CA  
734  C  C   . LEU A 90  ? 0.0996 0.1762 0.1413 0.0030  0.0313  0.0369  90  LEU A C   
735  O  O   . LEU A 90  ? 0.1258 0.1816 0.1502 0.0189  0.0446  0.0440  90  LEU A O   
736  C  CB  . LEU A 90  ? 0.0804 0.1314 0.1716 -0.0042 0.0208  0.0106  90  LEU A CB  
737  C  CG  . LEU A 90  ? 0.1165 0.1580 0.1443 -0.0013 0.0016  0.0013  90  LEU A CG  
738  C  CD1 . LEU A 90  ? 0.1459 0.1515 0.1654 0.0172  0.0211  0.0012  90  LEU A CD1 
739  C  CD2 . LEU A 90  ? 0.1278 0.1877 0.1847 -0.0299 -0.0008 0.0000  90  LEU A CD2 
740  N  N   . ILE A 91  ? 0.1007 0.1168 0.1286 0.0000  0.0414  0.0098  91  ILE A N   
741  C  CA  . ILE A 91  ? 0.0986 0.1263 0.1295 0.0122  0.0447  0.0153  91  ILE A CA  
742  C  C   . ILE A 91  ? 0.1420 0.1237 0.1284 0.0290  0.0423  0.0145  91  ILE A C   
743  O  O   . ILE A 91  ? 0.1254 0.1357 0.1256 -0.0084 0.0413  0.0288  91  ILE A O   
744  C  CB  . ILE A 91  ? 0.1332 0.1894 0.1256 -0.0329 0.0259  0.0220  91  ILE A CB  
745  C  CG1 . ILE A 91  ? 0.1386 0.2183 0.1596 -0.0648 0.0491  0.0138  91  ILE A CG1 
746  C  CG2 . ILE A 91  ? 0.1304 0.1610 0.1378 -0.0006 0.0279  0.0083  91  ILE A CG2 
747  C  CD1 . ILE A 91  ? 0.1399 0.2667 0.1829 -0.0824 0.0705  -0.0033 91  ILE A CD1 
748  N  N   . GLN A 92  ? 0.1341 0.1165 0.1295 -0.0012 0.0139  0.0113  92  GLN A N   
749  C  CA  . GLN A 92  ? 0.1204 0.1129 0.1454 0.0096  0.0458  0.0228  92  GLN A CA  
750  C  C   . GLN A 92  ? 0.1120 0.1102 0.1156 0.0016  0.0431  0.0165  92  GLN A C   
751  O  O   . GLN A 92  ? 0.1389 0.1135 0.1120 -0.0098 0.0313  -0.0024 92  GLN A O   
752  C  CB  . GLN A 92  ? 0.1248 0.1500 0.1321 -0.0067 0.0346  0.0161  92  GLN A CB  
753  C  CG  . GLN A 92  ? 0.1181 0.1438 0.1729 0.0049  0.0125  0.0053  92  GLN A CG  
754  C  CD  . GLN A 92  ? 0.1293 0.1395 0.0944 -0.0040 0.0205  0.0096  92  GLN A CD  
755  O  OE1 . GLN A 92  ? 0.1267 0.1263 0.1388 -0.0042 0.0318  0.0043  92  GLN A OE1 
756  N  NE2 . GLN A 92  ? 0.1346 0.1659 0.1435 -0.0074 0.0269  0.0030  92  GLN A NE2 
757  N  N   . PHE A 93  ? 0.1330 0.1278 0.0910 0.0096  0.0234  0.0106  93  PHE A N   
758  C  CA  . PHE A 93  ? 0.1323 0.1079 0.1145 -0.0177 0.0149  0.0099  93  PHE A CA  
759  C  C   . PHE A 93  ? 0.1427 0.1176 0.0950 -0.0079 0.0073  0.0024  93  PHE A C   
760  O  O   . PHE A 93  ? 0.1569 0.1373 0.0970 -0.0079 0.0174  0.0212  93  PHE A O   
761  C  CB  . PHE A 93  ? 0.1393 0.1214 0.1305 -0.0296 -0.0100 0.0205  93  PHE A CB  
762  C  CG  . PHE A 93  ? 0.1360 0.1377 0.1377 -0.0029 -0.0152 0.0048  93  PHE A CG  
763  C  CD1 . PHE A 93  ? 0.1219 0.1533 0.1269 0.0044  0.0034  0.0049  93  PHE A CD1 
764  C  CD2 . PHE A 93  ? 0.1569 0.1723 0.1338 0.0110  -0.0216 0.0347  93  PHE A CD2 
765  C  CE1 . PHE A 93  ? 0.1391 0.1432 0.1572 0.0129  -0.0227 -0.0023 93  PHE A CE1 
766  C  CE2 . PHE A 93  ? 0.2018 0.1644 0.1705 0.0381  -0.0381 -0.0055 93  PHE A CE2 
767  C  CZ  . PHE A 93  ? 0.2197 0.2175 0.1360 0.0702  -0.0388 -0.0062 93  PHE A CZ  
768  N  N   . HIS A 94  ? 0.0869 0.1025 0.1000 -0.0103 0.0118  0.0021  94  HIS A N   
769  C  CA  . HIS A 94  ? 0.1059 0.0966 0.0980 -0.0120 0.0131  0.0065  94  HIS A CA  
770  C  C   . HIS A 94  ? 0.1056 0.1146 0.0725 -0.0212 0.0102  0.0179  94  HIS A C   
771  O  O   . HIS A 94  ? 0.1009 0.1278 0.0926 0.0068  0.0290  0.0176  94  HIS A O   
772  C  CB  . HIS A 94  ? 0.1014 0.1224 0.1065 -0.0059 0.0207  0.0050  94  HIS A CB  
773  C  CG  . HIS A 94  ? 0.0811 0.1190 0.1044 -0.0055 0.0230  0.0060  94  HIS A CG  
774  N  ND1 . HIS A 94  ? 0.0953 0.1097 0.1090 -0.0093 0.0281  0.0216  94  HIS A ND1 
775  C  CD2 . HIS A 94  ? 0.0741 0.1518 0.0831 -0.0093 0.0238  0.0074  94  HIS A CD2 
776  C  CE1 . HIS A 94  ? 0.0829 0.1154 0.1093 -0.0196 0.0257  0.0066  94  HIS A CE1 
777  N  NE2 . HIS A 94  ? 0.0452 0.1903 0.0530 -0.0063 0.0059  0.0457  94  HIS A NE2 
778  N  N   . PHE A 95  ? 0.0934 0.1012 0.1092 -0.0168 0.0042  0.0035  95  PHE A N   
779  C  CA  . PHE A 95  ? 0.1077 0.1237 0.1126 -0.0283 0.0071  0.0203  95  PHE A CA  
780  C  C   . PHE A 95  ? 0.1072 0.1250 0.0960 0.0002  0.0279  0.0082  95  PHE A C   
781  O  O   . PHE A 95  ? 0.0858 0.1323 0.1234 -0.0025 0.0254  0.0069  95  PHE A O   
782  C  CB  . PHE A 95  ? 0.1145 0.1339 0.1119 -0.0023 0.0066  -0.0047 95  PHE A CB  
783  C  CG  . PHE A 95  ? 0.0993 0.1370 0.0953 -0.0207 0.0089  0.0004  95  PHE A CG  
784  C  CD1 . PHE A 95  ? 0.1280 0.1474 0.1298 -0.0047 0.0053  0.0122  95  PHE A CD1 
785  C  CD2 . PHE A 95  ? 0.1040 0.1375 0.1402 -0.0345 0.0170  0.0021  95  PHE A CD2 
786  C  CE1 . PHE A 95  ? 0.1282 0.1643 0.1144 -0.0041 0.0022  0.0114  95  PHE A CE1 
787  C  CE2 . PHE A 95  ? 0.1174 0.1662 0.1382 -0.0121 0.0228  -0.0027 95  PHE A CE2 
788  C  CZ  . PHE A 95  ? 0.1164 0.1751 0.1490 -0.0142 0.0128  -0.0244 95  PHE A CZ  
789  N  N   . HIS A 96  ? 0.0874 0.0991 0.1136 -0.0113 0.0117  -0.0024 96  HIS A N   
790  C  CA  . HIS A 96  ? 0.0973 0.0869 0.1129 -0.0024 0.0220  -0.0044 96  HIS A CA  
791  C  C   . HIS A 96  ? 0.0759 0.1052 0.1306 -0.0268 0.0260  0.0082  96  HIS A C   
792  O  O   . HIS A 96  ? 0.0961 0.1219 0.1097 -0.0354 0.0313  0.0116  96  HIS A O   
793  C  CB  . HIS A 96  ? 0.0903 0.1076 0.1205 0.0011  0.0239  -0.0209 96  HIS A CB  
794  C  CG  . HIS A 96  ? 0.0894 0.1052 0.1108 -0.0024 0.0278  0.0003  96  HIS A CG  
795  N  ND1 . HIS A 96  ? 0.0942 0.1075 0.1544 -0.0025 0.0386  -0.0043 96  HIS A ND1 
796  C  CD2 . HIS A 96  ? 0.0551 0.1172 0.1050 -0.0037 0.0221  0.0020  96  HIS A CD2 
797  C  CE1 . HIS A 96  ? 0.1012 0.1145 0.1300 0.0129  0.0366  -0.0051 96  HIS A CE1 
798  N  NE2 . HIS A 96  ? 0.1070 0.1014 0.1030 -0.0003 0.0516  -0.0216 96  HIS A NE2 
799  N  N   . TRP A 97  ? 0.0763 0.1104 0.1063 -0.0254 0.0355  0.0030  97  TRP A N   
800  C  CA  . TRP A 97  ? 0.1062 0.0930 0.1417 -0.0036 0.0182  0.0001  97  TRP A CA  
801  C  C   . TRP A 97  ? 0.1095 0.1131 0.1151 -0.0073 0.0200  0.0044  97  TRP A C   
802  O  O   . TRP A 97  ? 0.1054 0.1128 0.1313 -0.0050 0.0290  -0.0108 97  TRP A O   
803  C  CB  . TRP A 97  ? 0.1342 0.1057 0.1208 -0.0355 0.0218  0.0032  97  TRP A CB  
804  C  CG  . TRP A 97  ? 0.1252 0.1279 0.1149 -0.0280 0.0267  -0.0214 97  TRP A CG  
805  C  CD1 . TRP A 97  ? 0.1119 0.1348 0.0962 -0.0168 0.0288  -0.0013 97  TRP A CD1 
806  C  CD2 . TRP A 97  ? 0.1248 0.1371 0.0980 -0.0127 0.0161  -0.0084 97  TRP A CD2 
807  N  NE1 . TRP A 97  ? 0.1585 0.1400 0.1040 -0.0104 0.0432  0.0044  97  TRP A NE1 
808  C  CE2 . TRP A 97  ? 0.1522 0.1274 0.0996 -0.0149 0.0298  -0.0037 97  TRP A CE2 
809  C  CE3 . TRP A 97  ? 0.0996 0.1298 0.1118 -0.0177 0.0109  0.0002  97  TRP A CE3 
810  C  CZ2 . TRP A 97  ? 0.1436 0.1553 0.1197 -0.0002 0.0324  0.0148  97  TRP A CZ2 
811  C  CZ3 . TRP A 97  ? 0.1456 0.1528 0.1111 -0.0190 0.0127  0.0132  97  TRP A CZ3 
812  C  CH2 . TRP A 97  ? 0.1666 0.1453 0.1254 -0.0009 0.0406  0.0048  97  TRP A CH2 
813  N  N   . GLY A 98  ? 0.1247 0.0977 0.1133 0.0017  0.0529  -0.0022 98  GLY A N   
814  C  CA  . GLY A 98  ? 0.1207 0.1375 0.1147 0.0082  0.0537  -0.0089 98  GLY A CA  
815  C  C   . GLY A 98  ? 0.1107 0.0960 0.1244 -0.0223 0.0465  -0.0127 98  GLY A C   
816  O  O   . GLY A 98  ? 0.1447 0.1287 0.1322 0.0013  0.0308  -0.0036 98  GLY A O   
817  N  N   . SER A 99  ? 0.1301 0.1111 0.1314 0.0075  0.0502  -0.0128 99  SER A N   
818  C  CA  . SER A 99  ? 0.1647 0.1216 0.1594 0.0146  0.0579  -0.0288 99  SER A CA  
819  C  C   . SER A 99  ? 0.1571 0.1550 0.1504 0.0000  0.0471  -0.0171 99  SER A C   
820  O  O   . SER A 99  ? 0.2685 0.1730 0.1436 -0.0496 0.0460  -0.0188 99  SER A O   
821  C  CB  . SER A 99  ? 0.1612 0.1309 0.1838 0.0290  0.0335  -0.0100 99  SER A CB  
822  O  OG  . SER A 99  ? 0.1629 0.1526 0.1987 0.0120  0.0230  -0.0087 99  SER A OG  
823  N  N   . LEU A 100 ? 0.1540 0.1321 0.1468 0.0011  0.0348  0.0033  100 LEU A N   
824  C  CA  . LEU A 100 ? 0.1547 0.1266 0.2164 0.0044  0.0651  -0.0158 100 LEU A CA  
825  C  C   . LEU A 100 ? 0.1574 0.1421 0.1804 -0.0241 0.0576  -0.0100 100 LEU A C   
826  O  O   . LEU A 100 ? 0.1479 0.1309 0.1626 -0.0215 0.0317  -0.0092 100 LEU A O   
827  C  CB  . LEU A 100 ? 0.2189 0.1903 0.2391 0.0117  0.0947  0.0479  100 LEU A CB  
828  C  CG  . LEU A 100 ? 0.3371 0.2724 0.2606 0.0493  0.1710  0.0709  100 LEU A CG  
829  C  CD1 . LEU A 100 ? 0.3959 0.2330 0.3670 0.0794  0.0908  -0.0158 100 LEU A CD1 
830  C  CD2 . LEU A 100 ? 0.3613 0.2301 0.3914 0.0906  0.1513  -0.0611 100 LEU A CD2 
831  N  N   . ASP A 101 ? 0.1099 0.1219 0.2106 -0.0017 0.0079  0.0173  101 ASP A N   
832  C  CA  . ASP A 101 ? 0.1322 0.1479 0.1773 -0.0200 0.0221  0.0194  101 ASP A CA  
833  C  C   . ASP A 101 ? 0.1287 0.1443 0.1738 -0.0324 0.0150  0.0229  101 ASP A C   
834  O  O   . ASP A 101 ? 0.1804 0.1522 0.2072 -0.0082 0.0621  0.0380  101 ASP A O   
835  C  CB  . ASP A 101 ? 0.1504 0.2011 0.2420 -0.0627 -0.0132 0.0683  101 ASP A CB  
836  C  CG  . ASP A 101 ? 0.1696 0.1808 0.2576 -0.0502 -0.0189 0.0464  101 ASP A CG  
837  O  OD1 . ASP A 101 ? 0.2041 0.1927 0.2348 -0.0670 0.0029  0.0385  101 ASP A OD1 
838  O  OD2 . ASP A 101 ? 0.2237 0.2448 0.3050 -0.1169 -0.0141 0.0587  101 ASP A OD2 
839  N  N   . GLY A 102 ? 0.1441 0.1360 0.1982 -0.0241 0.0215  0.0344  102 GLY A N   
840  C  CA  . GLY A 102 ? 0.1957 0.1315 0.1777 -0.0244 0.0392  0.0372  102 GLY A CA  
841  C  C   . GLY A 102 ? 0.1091 0.1328 0.1689 0.0141  0.0550  0.0133  102 GLY A C   
842  O  O   . GLY A 102 ? 0.1508 0.1453 0.1775 0.0061  0.0461  0.0200  102 GLY A O   
843  N  N   . GLN A 103 ? 0.1086 0.1589 0.1463 -0.0053 0.0367  0.0223  103 GLN A N   
844  C  CA  . GLN A 103 ? 0.0962 0.1356 0.1475 0.0069  0.0133  0.0132  103 GLN A CA  
845  C  C   . GLN A 103 ? 0.1254 0.1305 0.1346 0.0043  0.0361  0.0111  103 GLN A C   
846  O  O   . GLN A 103 ? 0.1445 0.1242 0.1311 0.0019  0.0403  0.0001  103 GLN A O   
847  C  CB  . GLN A 103 ? 0.0932 0.1714 0.1780 0.0106  0.0541  0.0121  103 GLN A CB  
848  C  CG  . GLN A 103 ? 0.1264 0.1773 0.1894 0.0520  0.0752  0.0106  103 GLN A CG  
849  C  CD  . GLN A 103 ? 0.1449 0.1874 0.2927 0.0617  0.0988  0.0930  103 GLN A CD  
850  O  OE1 . GLN A 103 ? 0.1863 0.3121 0.3792 0.1376  0.1368  0.1439  103 GLN A OE1 
851  N  NE2 . GLN A 103 ? 0.1445 0.2011 0.2079 0.0379  0.0801  0.0402  103 GLN A NE2 
852  N  N   . GLY A 104 ? 0.1248 0.1234 0.1187 0.0120  0.0408  0.0088  104 GLY A N   
853  C  CA  . GLY A 104 ? 0.0946 0.1434 0.1095 0.0158  0.0337  -0.0072 104 GLY A CA  
854  C  C   . GLY A 104 ? 0.0898 0.1216 0.1143 -0.0034 0.0276  0.0020  104 GLY A C   
855  O  O   . GLY A 104 ? 0.1003 0.1275 0.1314 -0.0118 0.0326  0.0116  104 GLY A O   
856  N  N   . SER A 105 ? 0.0943 0.1185 0.1045 0.0031  0.0317  0.0041  105 SER A N   
857  C  CA  . SER A 105 ? 0.0811 0.1062 0.1093 -0.0086 0.0348  0.0033  105 SER A CA  
858  C  C   . SER A 105 ? 0.0680 0.1285 0.0928 -0.0100 0.0525  -0.0024 105 SER A C   
859  O  O   . SER A 105 ? 0.1000 0.1243 0.1268 -0.0093 0.0333  -0.0035 105 SER A O   
860  C  CB  . SER A 105 ? 0.0837 0.1586 0.1208 -0.0207 0.0337  0.0162  105 SER A CB  
861  O  OG  . SER A 105 ? 0.0897 0.1141 0.1330 -0.0108 0.0313  0.0042  105 SER A OG  
862  N  N   . GLU A 106 ? 0.0686 0.1102 0.1058 -0.0092 0.0336  0.0051  106 GLU A N   
863  C  CA  . GLU A 106 ? 0.0987 0.1219 0.1014 -0.0135 0.0136  0.0024  106 GLU A CA  
864  C  C   . GLU A 106 ? 0.0903 0.0989 0.1153 0.0086  0.0122  0.0013  106 GLU A C   
865  O  O   . GLU A 106 ? 0.0741 0.1258 0.1197 0.0055  0.0267  0.0089  106 GLU A O   
866  C  CB  . GLU A 106 ? 0.0949 0.1217 0.0980 -0.0102 0.0326  -0.0029 106 GLU A CB  
867  C  CG  . GLU A 106 ? 0.0960 0.1395 0.1097 -0.0158 0.0510  0.0124  106 GLU A CG  
868  C  CD  . GLU A 106 ? 0.0788 0.1429 0.1002 -0.0111 0.0401  0.0029  106 GLU A CD  
869  O  OE1 . GLU A 106 ? 0.0516 0.1521 0.1101 -0.0171 0.0474  -0.0068 106 GLU A OE1 
870  O  OE2 . GLU A 106 ? 0.0725 0.1425 0.1405 0.0031  0.0416  -0.0125 106 GLU A OE2 
871  N  N   . HIS A 107 ? 0.1034 0.1031 0.1161 0.0147  0.0319  -0.0031 107 HIS A N   
872  C  CA  . HIS A 107 ? 0.0806 0.1032 0.0962 0.0257  0.0217  0.0008  107 HIS A CA  
873  C  C   . HIS A 107 ? 0.0779 0.1324 0.1192 0.0046  0.0345  -0.0003 107 HIS A C   
874  O  O   . HIS A 107 ? 0.0657 0.1100 0.1206 0.0021  0.0362  0.0006  107 HIS A O   
875  C  CB  . HIS A 107 ? 0.0749 0.0895 0.1220 0.0138  0.0385  0.0168  107 HIS A CB  
876  C  CG  . HIS A 107 ? 0.0650 0.1080 0.1280 -0.0073 0.0343  0.0025  107 HIS A CG  
877  N  ND1 . HIS A 107 ? 0.0533 0.1113 0.1179 0.0166  0.0342  -0.0042 107 HIS A ND1 
878  C  CD2 . HIS A 107 ? 0.0464 0.1086 0.1499 0.0100  0.0285  -0.0134 107 HIS A CD2 
879  C  CE1 . HIS A 107 ? 0.0630 0.1224 0.1178 0.0111  0.0294  -0.0116 107 HIS A CE1 
880  N  NE2 . HIS A 107 ? 0.0618 0.1037 0.1134 -0.0023 0.0186  -0.0405 107 HIS A NE2 
881  N  N   . THR A 108 ? 0.0766 0.1307 0.1203 -0.0008 0.0373  0.0075  108 THR A N   
882  C  CA  . THR A 108 ? 0.0718 0.1243 0.1231 0.0055  0.0482  0.0044  108 THR A CA  
883  C  C   . THR A 108 ? 0.0804 0.1064 0.1009 0.0052  0.0283  0.0108  108 THR A C   
884  O  O   . THR A 108 ? 0.0901 0.1239 0.1057 0.0013  0.0251  0.0048  108 THR A O   
885  C  CB  . THR A 108 ? 0.0693 0.1506 0.1138 0.0170  0.0406  -0.0052 108 THR A CB  
886  O  OG1 . THR A 108 ? 0.0849 0.1411 0.1216 0.0315  0.0286  0.0036  108 THR A OG1 
887  C  CG2 . THR A 108 ? 0.1083 0.1443 0.1113 0.0129  0.0557  0.0027  108 THR A CG2 
888  N  N   . VAL A 109 ? 0.0941 0.1221 0.1120 -0.0110 0.0436  0.0040  109 VAL A N   
889  C  CA  . VAL A 109 ? 0.0923 0.1511 0.1147 -0.0027 0.0422  0.0192  109 VAL A CA  
890  C  C   . VAL A 109 ? 0.1058 0.1362 0.1276 -0.0111 0.0343  0.0179  109 VAL A C   
891  O  O   . VAL A 109 ? 0.1235 0.1300 0.1404 0.0024  0.0422  0.0060  109 VAL A O   
892  C  CB  . VAL A 109 ? 0.0812 0.1608 0.1524 -0.0075 0.0458  0.0228  109 VAL A CB  
893  C  CG1 . VAL A 109 ? 0.0973 0.1497 0.1629 0.0017  0.0627  0.0325  109 VAL A CG1 
894  C  CG2 . VAL A 109 ? 0.1143 0.1560 0.1773 0.0144  0.0050  0.0219  109 VAL A CG2 
895  N  N   . ASP A 110 ? 0.1342 0.1396 0.1098 0.0255  0.0475  0.0085  110 ASP A N   
896  C  CA  . ASP A 110 ? 0.1321 0.1306 0.1658 0.0143  0.0400  0.0204  110 ASP A CA  
897  C  C   . ASP A 110 ? 0.1441 0.1378 0.1691 0.0146  0.0345  0.0008  110 ASP A C   
898  O  O   . ASP A 110 ? 0.1801 0.1543 0.1324 0.0182  0.0442  0.0344  110 ASP A O   
899  C  CB  . ASP A 110 ? 0.1446 0.1653 0.1605 0.0108  0.0594  0.0313  110 ASP A CB  
900  C  CG  . ASP A 110 ? 0.1773 0.1775 0.1414 0.0055  0.0455  0.0233  110 ASP A CG  
901  O  OD1 . ASP A 110 ? 0.1885 0.1766 0.1608 0.0131  0.0699  0.0103  110 ASP A OD1 
902  O  OD2 . ASP A 110 ? 0.1704 0.2415 0.1898 0.0159  0.0762  0.0229  110 ASP A OD2 
903  N  N   . LYS A 111 ? 0.1129 0.1508 0.1371 0.0398  0.0212  0.0208  111 LYS A N   
904  C  CA  . LYS A 111 ? 0.1234 0.1938 0.1611 0.0522  0.0174  -0.0017 111 LYS A CA  
905  C  C   . LYS A 111 ? 0.1342 0.1589 0.1374 0.0353  0.0373  0.0154  111 LYS A C   
906  O  O   . LYS A 111 ? 0.1571 0.1845 0.1520 0.0501  0.0518  0.0104  111 LYS A O   
907  C  CB  . LYS A 111 ? 0.1727 0.1935 0.1874 0.0511  -0.0159 0.0011  111 LYS A CB  
908  C  CG  . LYS A 111 ? 0.2400 0.2005 0.1934 0.0754  -0.0515 0.0043  111 LYS A CG  
909  C  CD  . LYS A 111 ? 0.1657 0.2833 0.2427 0.0331  -0.0161 -0.0115 111 LYS A CD  
910  C  CE  . LYS A 111 ? 0.1920 0.3244 0.2746 0.0599  -0.0519 0.0041  111 LYS A CE  
911  N  NZ  . LYS A 111 ? 0.1898 0.3263 0.3830 0.0441  -0.0394 0.0741  111 LYS A NZ  
912  N  N   . LYS A 112 ? 0.1186 0.1316 0.1120 0.0055  0.0453  0.0163  112 LYS A N   
913  C  CA  . LYS A 112 ? 0.1225 0.1486 0.1286 0.0043  0.0366  0.0070  112 LYS A CA  
914  C  C   . LYS A 112 ? 0.1287 0.1428 0.1232 0.0082  0.0394  0.0002  112 LYS A C   
915  O  O   . LYS A 112 ? 0.1009 0.1225 0.1386 -0.0018 0.0314  0.0036  112 LYS A O   
916  C  CB  . LYS A 112 ? 0.1307 0.1729 0.1411 -0.0241 0.0399  -0.0052 112 LYS A CB  
917  C  CG  . LYS A 112 ? 0.1413 0.2340 0.1418 -0.0603 0.0457  -0.0125 112 LYS A CG  
918  C  CD  . LYS A 112 ? 0.1395 0.2370 0.2182 -0.0050 -0.0006 -0.0109 112 LYS A CD  
919  C  CE  . LYS A 112 ? 0.1845 0.1917 0.2246 -0.0221 0.0160  -0.0030 112 LYS A CE  
920  N  NZ  . LYS A 112 ? 0.2181 0.1565 0.2165 -0.0276 0.0278  0.0197  112 LYS A NZ  
921  N  N   A LYS A 113 ? 0.0967 0.1776 0.1158 0.0064  0.0438  0.0078  113 LYS A N   
922  N  N   B LYS A 113 ? 0.1013 0.1576 0.1244 0.0189  0.0408  0.0047  113 LYS A N   
923  C  CA  A LYS A 113 ? 0.1046 0.1766 0.1330 0.0057  0.0569  0.0218  113 LYS A CA  
924  C  CA  B LYS A 113 ? 0.1000 0.1693 0.1282 0.0179  0.0482  0.0142  113 LYS A CA  
925  C  C   A LYS A 113 ? 0.1352 0.1538 0.1511 0.0155  0.0245  0.0348  113 LYS A C   
926  C  C   B LYS A 113 ? 0.0797 0.1264 0.1486 0.0058  0.0499  0.0153  113 LYS A C   
927  O  O   A LYS A 113 ? 0.1159 0.1443 0.1768 0.0198  0.0295  0.0352  113 LYS A O   
928  O  O   B LYS A 113 ? 0.1391 0.1335 0.1704 0.0091  0.0395  -0.0053 113 LYS A O   
929  C  CB  A LYS A 113 ? 0.1118 0.1737 0.1339 0.0189  0.0465  -0.0117 113 LYS A CB  
930  C  CB  B LYS A 113 ? 0.0879 0.1176 0.1538 0.0286  0.0309  -0.0104 113 LYS A CB  
931  C  CG  A LYS A 113 ? 0.0980 0.1809 0.1594 0.0200  0.0521  -0.0043 113 LYS A CG  
932  C  CG  B LYS A 113 ? 0.0845 0.1090 0.1619 0.0444  0.0285  -0.0378 113 LYS A CG  
933  C  CD  A LYS A 113 ? 0.1098 0.1626 0.1465 0.0168  0.0456  -0.0322 113 LYS A CD  
934  C  CD  B LYS A 113 ? 0.0650 0.1590 0.1777 0.0381  0.0333  -0.0272 113 LYS A CD  
935  C  CE  A LYS A 113 ? 0.1083 0.1985 0.1831 0.0226  0.0399  -0.0334 113 LYS A CE  
936  C  CE  B LYS A 113 ? 0.0777 0.2208 0.1964 -0.0159 0.0551  -0.0436 113 LYS A CE  
937  N  NZ  A LYS A 113 ? 0.0558 0.2424 0.1529 0.0181  0.0216  -0.0533 113 LYS A NZ  
938  N  NZ  B LYS A 113 ? 0.1517 0.1912 0.3316 0.0245  0.0299  -0.0455 113 LYS A NZ  
939  N  N   . TYR A 114 ? 0.0935 0.1267 0.1355 0.0087  0.0450  0.0171  114 TYR A N   
940  C  CA  . TYR A 114 ? 0.0801 0.1025 0.1417 -0.0021 0.0380  0.0226  114 TYR A CA  
941  C  C   . TYR A 114 ? 0.1196 0.0845 0.1370 0.0012  0.0261  0.0000  114 TYR A C   
942  O  O   . TYR A 114 ? 0.1091 0.1220 0.1384 -0.0067 0.0367  0.0016  114 TYR A O   
943  C  CB  . TYR A 114 ? 0.0685 0.1179 0.1500 0.0033  0.0419  0.0078  114 TYR A CB  
944  C  CG  . TYR A 114 ? 0.0881 0.1122 0.1486 0.0001  0.0376  0.0089  114 TYR A CG  
945  C  CD1 . TYR A 114 ? 0.1315 0.1303 0.1676 0.0239  0.0364  0.0114  114 TYR A CD1 
946  C  CD2 . TYR A 114 ? 0.1061 0.1259 0.1601 -0.0143 0.0271  0.0130  114 TYR A CD2 
947  C  CE1 . TYR A 114 ? 0.1872 0.1543 0.1461 0.0109  0.0538  0.0075  114 TYR A CE1 
948  C  CE2 . TYR A 114 ? 0.1896 0.1704 0.1679 -0.0200 0.0710  0.0125  114 TYR A CE2 
949  C  CZ  . TYR A 114 ? 0.1955 0.1605 0.1658 -0.0017 0.0893  0.0077  114 TYR A CZ  
950  O  OH  . TYR A 114 ? 0.2343 0.2398 0.2359 0.0240  0.1533  0.0111  114 TYR A OH  
951  N  N   . ALA A 115 ? 0.1011 0.1146 0.1386 -0.0185 0.0227  -0.0097 115 ALA A N   
952  C  CA  . ALA A 115 ? 0.1181 0.1093 0.1279 -0.0277 0.0293  -0.0006 115 ALA A CA  
953  C  C   . ALA A 115 ? 0.1382 0.1165 0.1091 -0.0201 0.0335  0.0329  115 ALA A C   
954  O  O   . ALA A 115 ? 0.1143 0.1140 0.1449 -0.0100 0.0391  0.0005  115 ALA A O   
955  C  CB  . ALA A 115 ? 0.1319 0.1165 0.1500 -0.0049 0.0212  -0.0170 115 ALA A CB  
956  N  N   . ALA A 116 ? 0.0989 0.1089 0.1280 -0.0251 0.0214  -0.0023 116 ALA A N   
957  C  CA  . ALA A 116 ? 0.1004 0.1088 0.1154 -0.0397 0.0332  -0.0065 116 ALA A CA  
958  C  C   . ALA A 116 ? 0.0865 0.1110 0.1194 -0.0240 0.0228  0.0051  116 ALA A C   
959  O  O   . ALA A 116 ? 0.0865 0.1089 0.1338 -0.0052 0.0317  0.0103  116 ALA A O   
960  C  CB  . ALA A 116 ? 0.1016 0.1014 0.1320 -0.0160 0.0200  0.0084  116 ALA A CB  
961  N  N   . GLU A 117 ? 0.0867 0.1029 0.1179 -0.0036 0.0153  0.0002  117 GLU A N   
962  C  CA  . GLU A 117 ? 0.0881 0.1071 0.1267 0.0175  0.0108  0.0006  117 GLU A CA  
963  C  C   . GLU A 117 ? 0.0952 0.1025 0.1059 -0.0100 0.0194  0.0034  117 GLU A C   
964  O  O   . GLU A 117 ? 0.0807 0.1431 0.1190 -0.0109 0.0250  0.0099  117 GLU A O   
965  C  CB  . GLU A 117 ? 0.0612 0.1279 0.1090 0.0020  0.0294  -0.0066 117 GLU A CB  
966  C  CG  . GLU A 117 ? 0.0786 0.0961 0.0993 -0.0058 0.0103  0.0020  117 GLU A CG  
967  C  CD  . GLU A 117 ? 0.0488 0.1146 0.1018 -0.0196 0.0396  0.0114  117 GLU A CD  
968  O  OE1 . GLU A 117 ? 0.0715 0.1248 0.1247 0.0072  0.0188  -0.0195 117 GLU A OE1 
969  O  OE2 . GLU A 117 ? 0.0939 0.1239 0.1084 0.0039  0.0134  -0.0046 117 GLU A OE2 
970  N  N   . LEU A 118 ? 0.0961 0.1115 0.1063 0.0067  0.0035  -0.0057 118 LEU A N   
971  C  CA  . LEU A 118 ? 0.0903 0.1216 0.1138 -0.0109 -0.0033 -0.0087 118 LEU A CA  
972  C  C   . LEU A 118 ? 0.0564 0.1154 0.0921 -0.0037 0.0080  -0.0023 118 LEU A C   
973  O  O   . LEU A 118 ? 0.0689 0.1324 0.0921 -0.0059 0.0216  0.0030  118 LEU A O   
974  C  CB  . LEU A 118 ? 0.0810 0.1252 0.1117 -0.0223 -0.0018 0.0052  118 LEU A CB  
975  C  CG  . LEU A 118 ? 0.0838 0.1463 0.1253 -0.0223 -0.0006 0.0099  118 LEU A CG  
976  C  CD1 . LEU A 118 ? 0.0914 0.1349 0.1315 -0.0139 0.0005  0.0218  118 LEU A CD1 
977  C  CD2 . LEU A 118 ? 0.0845 0.1783 0.1483 -0.0150 -0.0217 0.0179  118 LEU A CD2 
978  N  N   . HIS A 119 ? 0.0791 0.1032 0.1041 -0.0098 -0.0006 0.0095  119 HIS A N   
979  C  CA  . HIS A 119 ? 0.0725 0.1332 0.1129 -0.0030 -0.0006 0.0002  119 HIS A CA  
980  C  C   . HIS A 119 ? 0.0618 0.1064 0.1090 -0.0013 0.0126  0.0009  119 HIS A C   
981  O  O   . HIS A 119 ? 0.1064 0.1292 0.1055 0.0027  0.0205  0.0060  119 HIS A O   
982  C  CB  . HIS A 119 ? 0.0534 0.1280 0.1133 0.0127  0.0221  -0.0036 119 HIS A CB  
983  C  CG  . HIS A 119 ? 0.0636 0.1210 0.1167 -0.0086 0.0178  0.0136  119 HIS A CG  
984  N  ND1 . HIS A 119 ? 0.0677 0.1411 0.0822 -0.0201 0.0383  -0.0035 119 HIS A ND1 
985  C  CD2 . HIS A 119 ? 0.0482 0.1119 0.1104 -0.0266 0.0176  -0.0012 119 HIS A CD2 
986  C  CE1 . HIS A 119 ? 0.0767 0.1288 0.0869 -0.0089 0.0332  0.0003  119 HIS A CE1 
987  N  NE2 . HIS A 119 ? 0.0549 0.1043 0.1278 -0.0199 0.0082  0.0179  119 HIS A NE2 
988  N  N   . LEU A 120 ? 0.0536 0.1014 0.1349 -0.0042 0.0260  0.0036  120 LEU A N   
989  C  CA  . LEU A 120 ? 0.0891 0.1305 0.1208 -0.0011 -0.0049 0.0029  120 LEU A CA  
990  C  C   . LEU A 120 ? 0.0673 0.1007 0.1177 0.0155  0.0111  0.0042  120 LEU A C   
991  O  O   . LEU A 120 ? 0.0747 0.1113 0.1077 -0.0088 0.0168  0.0074  120 LEU A O   
992  C  CB  . LEU A 120 ? 0.0901 0.1328 0.1583 -0.0042 -0.0167 0.0137  120 LEU A CB  
993  C  CG  . LEU A 120 ? 0.1172 0.1479 0.1486 -0.0414 -0.0283 0.0285  120 LEU A CG  
994  C  CD1 . LEU A 120 ? 0.1119 0.1550 0.1551 -0.0455 0.0044  0.0094  120 LEU A CD1 
995  C  CD2 . LEU A 120 ? 0.1176 0.1734 0.1784 0.0070  -0.0260 0.0127  120 LEU A CD2 
996  N  N   . VAL A 121 ? 0.0691 0.1199 0.1260 -0.0105 0.0151  0.0036  121 VAL A N   
997  C  CA  . VAL A 121 ? 0.1059 0.1077 0.1025 -0.0109 0.0361  0.0077  121 VAL A CA  
998  C  C   . VAL A 121 ? 0.0759 0.1095 0.1382 -0.0035 0.0402  0.0049  121 VAL A C   
999  O  O   . VAL A 121 ? 0.0955 0.1205 0.1436 0.0010  0.0201  0.0072  121 VAL A O   
1000 C  CB  . VAL A 121 ? 0.0856 0.1268 0.1324 -0.0102 0.0307  0.0133  121 VAL A CB  
1001 C  CG1 . VAL A 121 ? 0.0761 0.1313 0.1687 -0.0223 0.0210  0.0189  121 VAL A CG1 
1002 C  CG2 . VAL A 121 ? 0.0734 0.1411 0.1468 0.0197  0.0526  0.0143  121 VAL A CG2 
1003 N  N   . HIS A 122 ? 0.0682 0.0971 0.1389 -0.0124 0.0430  -0.0002 122 HIS A N   
1004 C  CA  . HIS A 122 ? 0.0682 0.1025 0.1558 -0.0179 0.0331  0.0048  122 HIS A CA  
1005 C  C   . HIS A 122 ? 0.1063 0.1136 0.1511 -0.0111 -0.0001 0.0036  122 HIS A C   
1006 O  O   . HIS A 122 ? 0.1048 0.1086 0.1459 -0.0144 0.0074  0.0144  122 HIS A O   
1007 C  CB  . HIS A 122 ? 0.0606 0.1418 0.1447 -0.0062 0.0280  0.0073  122 HIS A CB  
1008 C  CG  . HIS A 122 ? 0.0712 0.1177 0.1431 0.0011  0.0155  -0.0091 122 HIS A CG  
1009 N  ND1 . HIS A 122 ? 0.0466 0.1201 0.1418 0.0135  0.0355  -0.0015 122 HIS A ND1 
1010 C  CD2 . HIS A 122 ? 0.0725 0.1332 0.1456 -0.0066 0.0157  0.0167  122 HIS A CD2 
1011 C  CE1 . HIS A 122 ? 0.0650 0.1315 0.1429 0.0013  0.0442  -0.0011 122 HIS A CE1 
1012 N  NE2 . HIS A 122 ? 0.0736 0.1459 0.1493 -0.0162 0.0238  0.0272  122 HIS A NE2 
1013 N  N   . TRP A 123 ? 0.1016 0.0971 0.1454 -0.0032 0.0142  -0.0064 123 TRP A N   
1014 C  CA  . TRP A 123 ? 0.0837 0.1188 0.1314 -0.0070 0.0140  0.0059  123 TRP A CA  
1015 C  C   . TRP A 123 ? 0.0917 0.0914 0.1540 -0.0105 0.0242  0.0198  123 TRP A C   
1016 O  O   . TRP A 123 ? 0.0937 0.1364 0.1522 -0.0052 0.0027  0.0109  123 TRP A O   
1017 C  CB  . TRP A 123 ? 0.0939 0.1729 0.1478 -0.0403 0.0237  0.0170  123 TRP A CB  
1018 C  CG  . TRP A 123 ? 0.1049 0.1533 0.1683 -0.0281 0.0242  0.0116  123 TRP A CG  
1019 C  CD1 . TRP A 123 ? 0.1720 0.1625 0.1693 -0.0487 -0.0009 0.0367  123 TRP A CD1 
1020 C  CD2 . TRP A 123 ? 0.1883 0.1418 0.1357 -0.0326 0.0272  0.0079  123 TRP A CD2 
1021 N  NE1 . TRP A 123 ? 0.1587 0.1338 0.1863 -0.0311 -0.0048 0.0185  123 TRP A NE1 
1022 C  CE2 . TRP A 123 ? 0.1971 0.1266 0.1754 -0.0356 -0.0073 0.0272  123 TRP A CE2 
1023 C  CE3 . TRP A 123 ? 0.2181 0.1262 0.1798 -0.0483 0.0315  0.0154  123 TRP A CE3 
1024 C  CZ2 . TRP A 123 ? 0.2488 0.1334 0.2032 0.0122  0.0214  -0.0020 123 TRP A CZ2 
1025 C  CZ3 . TRP A 123 ? 0.2678 0.1312 0.2114 -0.0434 -0.0079 0.0012  123 TRP A CZ3 
1026 C  CH2 . TRP A 123 ? 0.3103 0.1257 0.2075 -0.0403 -0.0001 0.0201  123 TRP A CH2 
1027 N  N   . ASN A 124 ? 0.1095 0.0865 0.1698 0.0043  0.0144  -0.0199 124 ASN A N   
1028 C  CA  . ASN A 124 ? 0.1045 0.0926 0.1641 0.0049  0.0139  -0.0109 124 ASN A CA  
1029 C  C   . ASN A 124 ? 0.1156 0.1110 0.1885 0.0200  0.0103  -0.0069 124 ASN A C   
1030 O  O   . ASN A 124 ? 0.1210 0.1223 0.1734 0.0010  0.0239  -0.0079 124 ASN A O   
1031 C  CB  . ASN A 124 ? 0.0986 0.1266 0.1490 -0.0021 0.0311  -0.0153 124 ASN A CB  
1032 C  CG  . ASN A 124 ? 0.1289 0.1345 0.1750 0.0172  0.0331  -0.0172 124 ASN A CG  
1033 O  OD1 . ASN A 124 ? 0.1004 0.1287 0.2095 0.0174  0.0394  -0.0122 124 ASN A OD1 
1034 N  ND2 . ASN A 124 ? 0.1781 0.1363 0.1413 -0.0001 0.0311  -0.0145 124 ASN A ND2 
1035 N  N   . THR A 125 ? 0.1185 0.1181 0.2224 0.0303  -0.0094 -0.0086 125 THR A N   
1036 C  CA  . THR A 125 ? 0.1544 0.1225 0.2514 0.0301  -0.0140 -0.0166 125 THR A CA  
1037 C  C   . THR A 125 ? 0.1429 0.1286 0.2292 0.0187  0.0436  -0.0364 125 THR A C   
1038 O  O   . THR A 125 ? 0.1508 0.1384 0.2612 0.0093  0.0196  0.0118  125 THR A O   
1039 C  CB  . THR A 125 ? 0.2084 0.2023 0.2988 0.0482  -0.0897 0.0019  125 THR A CB  
1040 O  OG1 . THR A 125 ? 0.1738 0.2077 0.3776 0.0802  -0.0176 -0.0269 125 THR A OG1 
1041 C  CG2 . THR A 125 ? 0.2507 0.2011 0.3167 0.0197  -0.1039 -0.0303 125 THR A CG2 
1042 N  N   . LYS A 126 ? 0.1460 0.1407 0.1702 0.0215  0.0469  -0.0066 127 LYS A N   
1043 C  CA  . LYS A 126 ? 0.1820 0.1400 0.2128 -0.0329 0.0546  -0.0072 127 LYS A CA  
1044 C  C   . LYS A 126 ? 0.1895 0.1104 0.1942 -0.0121 0.0666  0.0245  127 LYS A C   
1045 O  O   . LYS A 126 ? 0.2243 0.1311 0.2160 -0.0279 0.0646  -0.0205 127 LYS A O   
1046 C  CB  . LYS A 126 ? 0.1564 0.1586 0.1884 -0.0098 0.0527  -0.0227 127 LYS A CB  
1047 C  CG  . LYS A 126 ? 0.2010 0.1921 0.1916 0.0086  0.0410  0.0055  127 LYS A CG  
1048 C  CD  . LYS A 126 ? 0.2695 0.2771 0.1816 -0.1010 0.0943  -0.0185 127 LYS A CD  
1049 C  CE  . LYS A 126 ? 0.4452 0.2649 0.2365 -0.0719 0.1379  -0.0378 127 LYS A CE  
1050 N  NZ  . LYS A 126 ? 0.6667 0.4261 0.2621 -0.0254 0.0136  0.0964  127 LYS A NZ  
1051 N  N   . TYR A 127 ? 0.1350 0.1406 0.1659 -0.0044 0.0442  -0.0060 128 TYR A N   
1052 C  CA  . TYR A 127 ? 0.1409 0.1162 0.1540 0.0016  0.0531  -0.0037 128 TYR A CA  
1053 C  C   . TYR A 127 ? 0.1845 0.1391 0.1653 0.0210  0.0325  -0.0071 128 TYR A C   
1054 O  O   . TYR A 127 ? 0.1601 0.1502 0.1536 0.0079  0.0303  -0.0039 128 TYR A O   
1055 C  CB  . TYR A 127 ? 0.1635 0.1140 0.1769 -0.0051 0.0519  -0.0064 128 TYR A CB  
1056 C  CG  . TYR A 127 ? 0.1353 0.1261 0.1610 -0.0038 0.0384  -0.0147 128 TYR A CG  
1057 C  CD1 . TYR A 127 ? 0.1297 0.1515 0.1597 -0.0070 0.0266  -0.0135 128 TYR A CD1 
1058 C  CD2 . TYR A 127 ? 0.1314 0.1414 0.1524 -0.0150 0.0476  0.0029  128 TYR A CD2 
1059 C  CE1 . TYR A 127 ? 0.1432 0.1625 0.1714 -0.0168 0.0195  0.0075  128 TYR A CE1 
1060 C  CE2 . TYR A 127 ? 0.1311 0.2002 0.1393 0.0022  0.0170  -0.0082 128 TYR A CE2 
1061 C  CZ  . TYR A 127 ? 0.1855 0.1604 0.1531 0.0067  0.0510  0.0011  128 TYR A CZ  
1062 O  OH  . TYR A 127 ? 0.2371 0.1687 0.1496 0.0181  0.0325  -0.0308 128 TYR A OH  
1063 N  N   . GLY A 128 ? 0.1816 0.1345 0.1640 0.0006  0.0335  -0.0018 129 GLY A N   
1064 C  CA  . GLY A 128 ? 0.1759 0.1399 0.1600 0.0019  0.0548  0.0199  129 GLY A CA  
1065 C  C   . GLY A 128 ? 0.1734 0.1118 0.1611 -0.0127 0.0302  0.0116  129 GLY A C   
1066 O  O   . GLY A 128 ? 0.2221 0.1348 0.1745 0.0106  -0.0040 0.0054  129 GLY A O   
1067 N  N   . ASP A 129 ? 0.2217 0.1239 0.1533 0.0302  0.0165  -0.0075 130 ASP A N   
1068 C  CA  . ASP A 129 ? 0.2544 0.1472 0.1599 0.0342  0.0521  -0.0128 130 ASP A CA  
1069 C  C   . ASP A 129 ? 0.2456 0.1483 0.1452 0.0330  0.0104  -0.0076 130 ASP A C   
1070 O  O   . ASP A 129 ? 0.2473 0.1482 0.1375 0.0259  0.0227  -0.0075 130 ASP A O   
1071 C  CB  . ASP A 129 ? 0.2354 0.1633 0.1416 0.0561  0.0480  0.0174  130 ASP A CB  
1072 C  CG  . ASP A 129 ? 0.2348 0.1385 0.3796 0.0756  0.0856  -0.0612 130 ASP A CG  
1073 O  OD1 . ASP A 129 ? 0.2948 0.1913 0.1971 0.0177  0.0295  0.0129  130 ASP A OD1 
1074 O  OD2 . ASP A 129 ? 0.1908 0.2006 0.3677 0.0520  0.0948  0.0397  130 ASP A OD2 
1075 N  N   . PHE A 130 ? 0.2141 0.1513 0.1373 0.0159  0.0303  -0.0094 131 PHE A N   
1076 C  CA  . PHE A 130 ? 0.1781 0.1533 0.1323 0.0080  0.0208  -0.0171 131 PHE A CA  
1077 C  C   . PHE A 130 ? 0.1696 0.1298 0.1222 -0.0068 0.0313  0.0029  131 PHE A C   
1078 O  O   . PHE A 130 ? 0.1596 0.1410 0.1327 -0.0346 0.0259  0.0069  131 PHE A O   
1079 C  CB  . PHE A 130 ? 0.1497 0.1529 0.1474 0.0089  0.0133  -0.0356 131 PHE A CB  
1080 C  CG  . PHE A 130 ? 0.1266 0.1393 0.1368 -0.0017 0.0440  -0.0149 131 PHE A CG  
1081 C  CD1 . PHE A 130 ? 0.1549 0.1732 0.2321 0.0100  0.0734  -0.0222 131 PHE A CD1 
1082 C  CD2 . PHE A 130 ? 0.1421 0.1535 0.1439 -0.0121 0.0458  -0.0092 131 PHE A CD2 
1083 C  CE1 . PHE A 130 ? 0.1934 0.2014 0.2535 0.0288  0.0671  0.0195  131 PHE A CE1 
1084 C  CE2 . PHE A 130 ? 0.1589 0.1569 0.1786 0.0010  0.0234  -0.0244 131 PHE A CE2 
1085 C  CZ  . PHE A 130 ? 0.2030 0.1610 0.2127 0.0400  0.0474  -0.0037 131 PHE A CZ  
1086 N  N   . GLY A 131 ? 0.1912 0.1529 0.1297 -0.0266 0.0584  0.0016  132 GLY A N   
1087 C  CA  . GLY A 131 ? 0.1872 0.1948 0.1532 -0.0487 0.0394  0.0006  132 GLY A CA  
1088 C  C   . GLY A 131 ? 0.1729 0.1623 0.1417 -0.0407 0.0702  0.0151  132 GLY A C   
1089 O  O   . GLY A 131 ? 0.1597 0.1594 0.2107 -0.0203 0.0693  -0.0140 132 GLY A O   
1090 N  N   . LYS A 132 ? 0.1601 0.1375 0.1691 -0.0344 0.0610  0.0190  133 LYS A N   
1091 C  CA  . LYS A 132 ? 0.1407 0.1590 0.1443 -0.0136 0.0574  0.0229  133 LYS A CA  
1092 C  C   . LYS A 132 ? 0.1128 0.1172 0.1623 -0.0266 0.0380  0.0122  133 LYS A C   
1093 O  O   . LYS A 132 ? 0.1650 0.1526 0.1529 -0.0496 0.0174  0.0155  133 LYS A O   
1094 C  CB  . LYS A 132 ? 0.1158 0.1362 0.1784 -0.0155 0.0373  0.0136  133 LYS A CB  
1095 C  CG  . LYS A 132 ? 0.1578 0.1651 0.2111 -0.0484 0.0295  0.0272  133 LYS A CG  
1096 C  CD  . LYS A 132 ? 0.1877 0.2384 0.3515 -0.0987 0.0333  0.0307  133 LYS A CD  
1097 C  CE  . LYS A 132 ? 0.2671 0.1405 0.5870 -0.0851 -0.1001 0.1056  133 LYS A CE  
1098 N  NZ  . LYS A 132 ? 0.5233 0.5583 0.4651 -0.1692 -0.0449 -0.0068 133 LYS A NZ  
1099 N  N   . ALA A 133 ? 0.1073 0.1342 0.1405 -0.0329 0.0569  -0.0063 134 ALA A N   
1100 C  CA  . ALA A 133 ? 0.1045 0.1393 0.1508 -0.0406 0.0416  0.0060  134 ALA A CA  
1101 C  C   . ALA A 133 ? 0.0991 0.1326 0.1332 -0.0345 0.0495  0.0008  134 ALA A C   
1102 O  O   . ALA A 133 ? 0.1009 0.1375 0.1429 -0.0111 0.0317  0.0071  134 ALA A O   
1103 C  CB  . ALA A 133 ? 0.0885 0.1611 0.1185 -0.0311 0.0337  -0.0001 134 ALA A CB  
1104 N  N   . VAL A 134 ? 0.1180 0.1342 0.1493 -0.0386 0.0549  -0.0018 135 VAL A N   
1105 C  CA  . VAL A 134 ? 0.1167 0.1720 0.1608 -0.0029 0.0261  -0.0201 135 VAL A CA  
1106 C  C   . VAL A 134 ? 0.1225 0.1726 0.1246 -0.0243 0.0499  0.0107  135 VAL A C   
1107 O  O   . VAL A 134 ? 0.1344 0.1794 0.1497 -0.0303 0.0429  0.0159  135 VAL A O   
1108 C  CB  . VAL A 134 ? 0.1378 0.1866 0.1483 -0.0562 0.0579  -0.0079 135 VAL A CB  
1109 C  CG1 . VAL A 134 ? 0.1522 0.2043 0.1586 -0.0133 0.0060  -0.0186 135 VAL A CG1 
1110 C  CG2 . VAL A 134 ? 0.1461 0.1700 0.1671 -0.0636 0.0612  -0.0154 135 VAL A CG2 
1111 N  N   . GLN A 135 ? 0.1349 0.1707 0.1368 -0.0501 0.0513  0.0026  136 GLN A N   
1112 C  CA  . GLN A 135 ? 0.1407 0.1719 0.1610 -0.0485 0.0401  -0.0119 136 GLN A CA  
1113 C  C   . GLN A 135 ? 0.1102 0.1666 0.1581 -0.0606 0.0154  0.0031  136 GLN A C   
1114 O  O   . GLN A 135 ? 0.1176 0.2326 0.1607 -0.0695 0.0059  0.0005  136 GLN A O   
1115 C  CB  . GLN A 135 ? 0.1353 0.1856 0.1784 -0.0657 0.0424  -0.0033 136 GLN A CB  
1116 C  CG  . GLN A 135 ? 0.2000 0.2177 0.1773 -0.0745 0.0574  0.0419  136 GLN A CG  
1117 C  CD  . GLN A 135 ? 0.2409 0.2606 0.3094 -0.1212 0.0515  0.0414  136 GLN A CD  
1118 O  OE1 . GLN A 135 ? 0.2503 0.3308 0.4431 -0.0947 -0.0429 0.0286  136 GLN A OE1 
1119 N  NE2 . GLN A 135 ? 0.1841 0.2767 0.3397 -0.0414 0.0741  0.0961  136 GLN A NE2 
1120 N  N   . GLN A 136 ? 0.0989 0.1381 0.1402 -0.0402 0.0425  0.0113  137 GLN A N   
1121 C  CA  . GLN A 136 ? 0.1064 0.1610 0.1287 -0.0302 0.0168  -0.0155 137 GLN A CA  
1122 C  C   . GLN A 136 ? 0.0838 0.1787 0.1454 -0.0302 0.0400  -0.0044 137 GLN A C   
1123 O  O   . GLN A 136 ? 0.1169 0.1532 0.1362 0.0108  0.0128  -0.0055 137 GLN A O   
1124 C  CB  . GLN A 136 ? 0.1403 0.1797 0.1177 0.0140  0.0475  0.0027  137 GLN A CB  
1125 C  CG  . GLN A 136 ? 0.1770 0.1995 0.1655 0.0270  0.0539  0.0111  137 GLN A CG  
1126 C  CD  . GLN A 136 ? 0.1353 0.1575 0.3091 0.0238  0.0295  0.0147  137 GLN A CD  
1127 O  OE1 . GLN A 136 ? 0.3395 0.2280 0.3406 0.0487  -0.0906 -0.0776 137 GLN A OE1 
1128 N  NE2 . GLN A 136 ? 0.2666 0.2409 0.4332 -0.0580 -0.0325 0.0942  137 GLN A NE2 
1129 N  N   . PRO A 137 ? 0.1141 0.1632 0.1342 -0.0279 0.0414  -0.0031 138 PRO A N   
1130 C  CA  . PRO A 137 ? 0.1134 0.1557 0.1346 -0.0113 0.0216  0.0073  138 PRO A CA  
1131 C  C   . PRO A 137 ? 0.1111 0.1629 0.1164 -0.0164 0.0361  0.0057  138 PRO A C   
1132 O  O   . PRO A 137 ? 0.1502 0.1569 0.1885 -0.0050 0.0111  0.0166  138 PRO A O   
1133 C  CB  . PRO A 137 ? 0.1896 0.1876 0.1262 0.0068  0.0406  -0.0057 138 PRO A CB  
1134 C  CG  . PRO A 137 ? 0.3612 0.2684 0.1496 -0.1018 0.0195  0.0111  138 PRO A CG  
1135 C  CD  . PRO A 137 ? 0.1507 0.2289 0.1605 -0.0443 -0.0106 -0.0204 138 PRO A CD  
1136 N  N   . ASP A 138 ? 0.0879 0.1716 0.1106 -0.0072 0.0307  -0.0049 139 ASP A N   
1137 C  CA  . ASP A 138 ? 0.0943 0.1705 0.1213 -0.0050 0.0240  -0.0129 139 ASP A CA  
1138 C  C   . ASP A 138 ? 0.1003 0.1459 0.1174 -0.0236 0.0253  -0.0077 139 ASP A C   
1139 O  O   . ASP A 138 ? 0.0910 0.1337 0.1549 -0.0113 0.0358  0.0049  139 ASP A O   
1140 C  CB  . ASP A 138 ? 0.1708 0.1698 0.1350 0.0178  0.0589  -0.0159 139 ASP A CB  
1141 C  CG  . ASP A 138 ? 0.1174 0.1960 0.1553 0.0204  0.0279  -0.0267 139 ASP A CG  
1142 O  OD1 . ASP A 138 ? 0.1468 0.1658 0.1757 0.0211  0.0337  -0.0166 139 ASP A OD1 
1143 O  OD2 . ASP A 138 ? 0.1711 0.2319 0.1921 0.0545  0.0567  -0.0487 139 ASP A OD2 
1144 N  N   . GLY A 139 ? 0.1120 0.1375 0.1142 -0.0047 0.0388  -0.0035 140 GLY A N   
1145 C  CA  . GLY A 139 ? 0.1335 0.1307 0.1170 0.0027  0.0064  -0.0081 140 GLY A CA  
1146 C  C   . GLY A 139 ? 0.0585 0.1395 0.1447 -0.0050 0.0215  0.0031  140 GLY A C   
1147 O  O   . GLY A 139 ? 0.0803 0.1156 0.1506 -0.0027 0.0158  0.0104  140 GLY A O   
1148 N  N   . LEU A 140 ? 0.0781 0.1203 0.1432 0.0033  0.0136  -0.0081 141 LEU A N   
1149 C  CA  . LEU A 140 ? 0.0402 0.1180 0.1547 -0.0046 0.0200  -0.0114 141 LEU A CA  
1150 C  C   . LEU A 140 ? 0.0817 0.0942 0.1380 0.0047  0.0282  -0.0168 141 LEU A C   
1151 O  O   . LEU A 140 ? 0.0886 0.1064 0.1389 -0.0105 0.0219  -0.0005 141 LEU A O   
1152 C  CB  . LEU A 140 ? 0.0653 0.0951 0.1489 -0.0106 0.0329  -0.0071 141 LEU A CB  
1153 C  CG  . LEU A 140 ? 0.0849 0.1120 0.1720 0.0012  0.0541  0.0046  141 LEU A CG  
1154 C  CD1 . LEU A 140 ? 0.0831 0.1362 0.1500 0.0059  0.0660  -0.0051 141 LEU A CD1 
1155 C  CD2 . LEU A 140 ? 0.1204 0.1270 0.1788 0.0186  0.0655  0.0172  141 LEU A CD2 
1156 N  N   . ALA A 141 ? 0.0788 0.1037 0.1332 -0.0107 0.0447  -0.0042 142 ALA A N   
1157 C  CA  . ALA A 141 ? 0.0643 0.1050 0.1368 -0.0098 0.0480  -0.0062 142 ALA A CA  
1158 C  C   . ALA A 141 ? 0.0750 0.1210 0.1389 -0.0029 0.0055  -0.0076 142 ALA A C   
1159 O  O   . ALA A 141 ? 0.0682 0.1274 0.1339 -0.0104 0.0260  0.0160  142 ALA A O   
1160 C  CB  . ALA A 141 ? 0.0632 0.1373 0.1787 -0.0017 0.0491  -0.0214 142 ALA A CB  
1161 N  N   . VAL A 142 ? 0.0752 0.1081 0.1219 -0.0009 0.0187  -0.0008 143 VAL A N   
1162 C  CA  . VAL A 142 ? 0.0833 0.1098 0.1161 0.0005  0.0368  0.0017  143 VAL A CA  
1163 C  C   . VAL A 142 ? 0.0777 0.0962 0.1133 0.0117  0.0347  -0.0097 143 VAL A C   
1164 O  O   . VAL A 142 ? 0.0743 0.1279 0.0995 -0.0052 0.0376  0.0027  143 VAL A O   
1165 C  CB  . VAL A 142 ? 0.0682 0.1232 0.1569 0.0033  0.0236  0.0013  143 VAL A CB  
1166 C  CG1 . VAL A 142 ? 0.1086 0.1597 0.1201 0.0443  0.0085  -0.0126 143 VAL A CG1 
1167 C  CG2 . VAL A 142 ? 0.0287 0.1644 0.1442 0.0067  0.0463  0.0135  143 VAL A CG2 
1168 N  N   . LEU A 143 ? 0.0639 0.1081 0.1197 -0.0054 0.0234  0.0006  144 LEU A N   
1169 C  CA  . LEU A 143 ? 0.0680 0.1124 0.1174 -0.0033 0.0347  0.0127  144 LEU A CA  
1170 C  C   . LEU A 143 ? 0.0973 0.1264 0.0966 -0.0053 0.0214  -0.0084 144 LEU A C   
1171 O  O   . LEU A 143 ? 0.1199 0.1270 0.0996 -0.0093 0.0253  0.0021  144 LEU A O   
1172 C  CB  . LEU A 143 ? 0.0941 0.1485 0.1350 -0.0097 0.0181  0.0283  144 LEU A CB  
1173 C  CG  . LEU A 143 ? 0.0976 0.1521 0.1741 -0.0217 0.0237  0.0350  144 LEU A CG  
1174 C  CD1 . LEU A 143 ? 0.1215 0.2507 0.1763 -0.0271 0.0245  0.0405  144 LEU A CD1 
1175 C  CD2 . LEU A 143 ? 0.0908 0.2059 0.1594 -0.0153 0.0116  0.0204  144 LEU A CD2 
1176 N  N   . GLY A 144 ? 0.0533 0.1229 0.1147 -0.0087 0.0189  -0.0027 145 GLY A N   
1177 C  CA  . GLY A 144 ? 0.0449 0.1053 0.1185 -0.0132 0.0546  0.0209  145 GLY A CA  
1178 C  C   . GLY A 144 ? 0.0549 0.1133 0.1111 -0.0199 0.0289  0.0293  145 GLY A C   
1179 O  O   . GLY A 144 ? 0.0810 0.1405 0.0917 -0.0280 0.0268  0.0204  145 GLY A O   
1180 N  N   . ILE A 145 ? 0.0818 0.1109 0.1129 -0.0250 0.0355  0.0158  146 ILE A N   
1181 C  CA  . ILE A 145 ? 0.0578 0.0979 0.1264 -0.0100 0.0283  0.0233  146 ILE A CA  
1182 C  C   . ILE A 145 ? 0.0662 0.1174 0.1180 -0.0122 0.0111  -0.0079 146 ILE A C   
1183 O  O   . ILE A 145 ? 0.0941 0.1359 0.1151 -0.0115 0.0173  -0.0046 146 ILE A O   
1184 C  CB  . ILE A 145 ? 0.0427 0.1328 0.1350 -0.0058 0.0270  0.0193  146 ILE A CB  
1185 C  CG1 . ILE A 145 ? 0.0718 0.1350 0.1729 0.0016  -0.0064 0.0093  146 ILE A CG1 
1186 C  CG2 . ILE A 145 ? 0.0648 0.1367 0.1799 -0.0035 0.0122  0.0047  146 ILE A CG2 
1187 C  CD1 . ILE A 145 ? 0.1204 0.1497 0.1416 -0.0190 -0.0153 0.0314  146 ILE A CD1 
1188 N  N   . PHE A 146 ? 0.0732 0.1162 0.1232 -0.0029 0.0252  0.0048  147 PHE A N   
1189 C  CA  . PHE A 146 ? 0.0691 0.1247 0.1278 0.0072  0.0125  0.0000  147 PHE A CA  
1190 C  C   . PHE A 146 ? 0.0837 0.1319 0.1461 -0.0117 0.0117  -0.0089 147 PHE A C   
1191 O  O   . PHE A 146 ? 0.0861 0.1472 0.1315 -0.0021 0.0148  -0.0075 147 PHE A O   
1192 C  CB  . PHE A 146 ? 0.1005 0.1416 0.1169 -0.0001 0.0013  0.0102  147 PHE A CB  
1193 C  CG  . PHE A 146 ? 0.0876 0.1070 0.1297 -0.0118 0.0025  0.0074  147 PHE A CG  
1194 C  CD1 . PHE A 146 ? 0.0837 0.1068 0.1483 -0.0039 0.0041  0.0047  147 PHE A CD1 
1195 C  CD2 . PHE A 146 ? 0.1199 0.1198 0.1186 0.0037  0.0052  0.0188  147 PHE A CD2 
1196 C  CE1 . PHE A 146 ? 0.0921 0.1174 0.1335 0.0158  0.0058  0.0006  147 PHE A CE1 
1197 C  CE2 . PHE A 146 ? 0.0926 0.1204 0.1536 -0.0178 0.0002  0.0292  147 PHE A CE2 
1198 C  CZ  . PHE A 146 ? 0.1023 0.1131 0.1283 -0.0283 0.0106  0.0237  147 PHE A CZ  
1199 N  N   . LEU A 147 ? 0.0973 0.1273 0.1125 -0.0179 0.0272  -0.0061 148 LEU A N   
1200 C  CA  . LEU A 147 ? 0.1213 0.1259 0.1151 -0.0058 0.0087  -0.0013 148 LEU A CA  
1201 C  C   . LEU A 147 ? 0.1102 0.1235 0.1164 -0.0145 0.0267  -0.0037 148 LEU A C   
1202 O  O   . LEU A 147 ? 0.1046 0.1188 0.1407 -0.0172 0.0190  0.0055  148 LEU A O   
1203 C  CB  . LEU A 147 ? 0.1241 0.1346 0.1304 -0.0204 0.0144  0.0147  148 LEU A CB  
1204 C  CG  . LEU A 147 ? 0.1486 0.1331 0.1226 -0.0102 -0.0015 0.0049  148 LEU A CG  
1205 C  CD1 . LEU A 147 ? 0.2062 0.1273 0.1189 -0.0579 0.0066  0.0114  148 LEU A CD1 
1206 C  CD2 . LEU A 147 ? 0.1673 0.1680 0.1180 -0.0257 0.0021  0.0142  148 LEU A CD2 
1207 N  N   . LYS A 148 ? 0.1081 0.1086 0.1493 -0.0135 0.0151  -0.0141 149 LYS A N   
1208 C  CA  . LYS A 148 ? 0.1377 0.1174 0.1605 0.0038  0.0099  0.0018  149 LYS A CA  
1209 C  C   . LYS A 148 ? 0.1178 0.1364 0.1691 0.0020  0.0158  0.0066  149 LYS A C   
1210 O  O   . LYS A 148 ? 0.1381 0.1684 0.1668 0.0054  0.0075  0.0072  149 LYS A O   
1211 C  CB  . LYS A 148 ? 0.1346 0.1827 0.1357 -0.0277 0.0022  -0.0006 149 LYS A CB  
1212 C  CG  . LYS A 148 ? 0.1328 0.1554 0.2131 -0.0103 0.0629  0.0100  149 LYS A CG  
1213 C  CD  . LYS A 148 ? 0.2115 0.2746 0.2588 -0.0251 0.1077  0.0491  149 LYS A CD  
1214 C  CE  . LYS A 148 ? 0.2179 0.4327 0.2679 -0.0247 0.1165  0.0857  149 LYS A CE  
1215 N  NZ  . LYS A 148 ? 0.4735 0.5435 0.6118 -0.1059 0.2703  0.2242  149 LYS A NZ  
1216 N  N   . VAL A 149 ? 0.1322 0.1134 0.1993 -0.0265 -0.0102 -0.0179 150 VAL A N   
1217 C  CA  . VAL A 149 ? 0.1289 0.1429 0.2111 -0.0177 -0.0031 -0.0314 150 VAL A CA  
1218 C  C   . VAL A 149 ? 0.1648 0.1632 0.1867 -0.0451 0.0197  -0.0081 150 VAL A C   
1219 O  O   . VAL A 149 ? 0.2312 0.2018 0.2168 -0.0608 -0.0292 0.0248  150 VAL A O   
1220 C  CB  . VAL A 149 ? 0.1560 0.1833 0.1899 0.0100  0.0030  -0.0196 150 VAL A CB  
1221 C  CG1 . VAL A 149 ? 0.2477 0.3234 0.2171 0.0261  0.0156  -0.0886 150 VAL A CG1 
1222 C  CG2 . VAL A 149 ? 0.1156 0.2402 0.2172 -0.0041 0.0608  -0.0337 150 VAL A CG2 
1223 N  N   . GLY A 150 ? 0.1303 0.1504 0.2016 -0.0397 0.0063  -0.0251 151 GLY A N   
1224 C  CA  . GLY A 150 ? 0.1874 0.1802 0.2452 -0.0893 -0.0351 0.0188  151 GLY A CA  
1225 C  C   . GLY A 150 ? 0.1604 0.1678 0.2239 -0.0678 -0.0302 -0.0093 151 GLY A C   
1226 O  O   . GLY A 150 ? 0.2214 0.1824 0.2250 -0.0743 -0.0340 -0.0197 151 GLY A O   
1227 N  N   A SER A 151 ? 0.1799 0.2036 0.2232 -0.0644 0.0058  -0.0057 152 SER A N   
1228 N  N   B SER A 151 ? 0.1763 0.1971 0.2341 -0.0653 0.0041  0.0046  152 SER A N   
1229 C  CA  A SER A 151 ? 0.1500 0.2452 0.2125 -0.0752 0.0071  -0.0181 152 SER A CA  
1230 C  CA  B SER A 151 ? 0.1587 0.2436 0.2210 -0.0493 0.0097  -0.0089 152 SER A CA  
1231 C  C   A SER A 151 ? 0.1676 0.1813 0.1849 -0.0333 0.0106  -0.0600 152 SER A C   
1232 C  C   B SER A 151 ? 0.1910 0.1989 0.2164 -0.0122 -0.0074 -0.0031 152 SER A C   
1233 O  O   A SER A 151 ? 0.1314 0.2201 0.1801 -0.0508 0.0052  -0.0502 152 SER A O   
1234 O  O   B SER A 151 ? 0.2149 0.2358 0.1320 -0.0137 0.0021  -0.0188 152 SER A O   
1235 C  CB  A SER A 151 ? 0.1741 0.3532 0.2848 -0.0851 0.0537  -0.0207 152 SER A CB  
1236 C  CB  B SER A 151 ? 0.1775 0.2662 0.2852 -0.0748 0.0548  -0.0354 152 SER A CB  
1237 O  OG  A SER A 151 ? 0.1949 0.4362 0.2721 -0.1370 0.0486  -0.0419 152 SER A OG  
1238 O  OG  B SER A 151 ? 0.1492 0.3231 0.2645 -0.0752 0.0288  0.0229  152 SER A OG  
1239 N  N   . ALA A 152 ? 0.1921 0.2108 0.1920 -0.0042 -0.0075 -0.0131 153 ALA A N   
1240 C  CA  . ALA A 152 ? 0.2570 0.2164 0.1675 -0.0147 -0.0155 -0.0201 153 ALA A CA  
1241 C  C   . ALA A 152 ? 0.1538 0.2455 0.1687 -0.0308 0.0055  -0.0237 153 ALA A C   
1242 O  O   . ALA A 152 ? 0.1626 0.2601 0.2495 -0.0204 0.0195  -0.0332 153 ALA A O   
1243 C  CB  . ALA A 152 ? 0.2292 0.2017 0.1727 -0.0332 -0.0290 -0.0130 153 ALA A CB  
1244 N  N   . LYS A 153 ? 0.2025 0.1756 0.2125 -0.0121 -0.0347 -0.0109 154 LYS A N   
1245 C  CA  . LYS A 153 ? 0.1892 0.2188 0.2118 0.0060  -0.0043 0.0150  154 LYS A CA  
1246 C  C   . LYS A 153 ? 0.1666 0.2054 0.2312 0.0061  -0.0055 0.0066  154 LYS A C   
1247 O  O   . LYS A 153 ? 0.1744 0.2086 0.1786 -0.0166 -0.0436 -0.0096 154 LYS A O   
1248 C  CB  . LYS A 153 ? 0.1761 0.1845 0.1874 0.0097  -0.0058 0.0124  154 LYS A CB  
1249 C  CG  . LYS A 153 ? 0.2113 0.1884 0.2404 -0.0341 -0.0311 -0.0092 154 LYS A CG  
1250 C  CD  . LYS A 153 ? 0.3782 0.2430 0.1944 -0.0043 -0.0143 -0.0279 154 LYS A CD  
1251 C  CE  . LYS A 153 ? 0.4480 0.2584 0.2111 0.0381  0.0337  0.0166  154 LYS A CE  
1252 N  NZ  . LYS A 153 ? 0.3328 0.6189 0.2244 0.0078  -0.0038 0.1278  154 LYS A NZ  
1253 N  N   . PRO A 154 ? 0.1683 0.2559 0.2568 -0.0111 -0.0277 0.0423  155 PRO A N   
1254 C  CA  . PRO A 154 ? 0.1357 0.2830 0.3499 -0.0357 -0.0819 0.1026  155 PRO A CA  
1255 C  C   . PRO A 154 ? 0.1872 0.2614 0.2286 -0.0161 -0.0554 0.0641  155 PRO A C   
1256 O  O   . PRO A 154 ? 0.2231 0.3006 0.2372 -0.0491 -0.0785 0.0790  155 PRO A O   
1257 C  CB  . PRO A 154 ? 0.1353 0.3545 0.3592 -0.0497 -0.0263 0.0639  155 PRO A CB  
1258 C  CG  . PRO A 154 ? 0.1802 0.4483 0.4299 -0.0115 -0.0074 0.1381  155 PRO A CG  
1259 C  CD  . PRO A 154 ? 0.1841 0.4067 0.3242 -0.0487 0.0139  0.0480  155 PRO A CD  
1260 N  N   . GLY A 155 ? 0.1744 0.2487 0.2721 0.0403  -0.0337 0.0140  156 GLY A N   
1261 C  CA  . GLY A 155 ? 0.2002 0.2606 0.3262 0.0413  -0.0201 0.0296  156 GLY A CA  
1262 C  C   . GLY A 155 ? 0.2136 0.2229 0.2290 0.0000  -0.0237 0.0429  156 GLY A C   
1263 O  O   . GLY A 155 ? 0.2230 0.2210 0.3484 0.0234  -0.0006 0.0475  156 GLY A O   
1264 N  N   . LEU A 156 ? 0.1736 0.2633 0.1888 0.0172  -0.0083 0.0212  157 LEU A N   
1265 C  CA  . LEU A 156 ? 0.1714 0.2250 0.1788 -0.0102 -0.0379 -0.0147 157 LEU A CA  
1266 C  C   . LEU A 156 ? 0.1939 0.2797 0.2014 -0.0201 -0.0313 -0.0348 157 LEU A C   
1267 O  O   . LEU A 156 ? 0.2002 0.2365 0.1693 -0.0113 -0.0292 0.0081  157 LEU A O   
1268 C  CB  . LEU A 156 ? 0.1654 0.2365 0.1823 -0.0058 -0.0392 0.0038  157 LEU A CB  
1269 C  CG  . LEU A 156 ? 0.1493 0.2149 0.2041 -0.0691 -0.0483 0.0239  157 LEU A CG  
1270 C  CD1 . LEU A 156 ? 0.2113 0.1720 0.2251 -0.0487 -0.0671 -0.0070 157 LEU A CD1 
1271 C  CD2 . LEU A 156 ? 0.1134 0.2091 0.2178 0.0203  -0.0157 0.0082  157 LEU A CD2 
1272 N  N   . GLN A 157 ? 0.2027 0.3019 0.1515 -0.0677 -0.0193 0.0085  158 GLN A N   
1273 C  CA  . GLN A 157 ? 0.2232 0.3080 0.1542 -0.0925 -0.0097 0.0100  158 GLN A CA  
1274 C  C   . GLN A 157 ? 0.1637 0.2870 0.1418 -0.0768 -0.0245 0.0032  158 GLN A C   
1275 O  O   . GLN A 157 ? 0.2077 0.2547 0.1490 -0.0401 -0.0253 -0.0145 158 GLN A O   
1276 C  CB  . GLN A 157 ? 0.2885 0.3066 0.1923 -0.0976 -0.0441 -0.0313 158 GLN A CB  
1277 C  CG  . GLN A 157 ? 0.2591 0.2358 0.2206 -0.0156 -0.0483 -0.0133 158 GLN A CG  
1278 C  CD  . GLN A 157 ? 0.2718 0.2390 0.1806 0.0098  0.0069  -0.0105 158 GLN A CD  
1279 O  OE1 . GLN A 157 ? 0.3649 0.2825 0.1714 -0.0428 -0.0172 0.0058  158 GLN A OE1 
1280 N  NE2 . GLN A 157 ? 0.3439 0.2540 0.1804 -0.0833 0.0136  -0.0559 158 GLN A NE2 
1281 N  N   . LYS A 158 ? 0.2014 0.2853 0.1829 -0.0521 -0.0502 0.0105  159 LYS A N   
1282 C  CA  . LYS A 158 ? 0.2186 0.2872 0.1999 -0.0440 -0.0477 0.0074  159 LYS A CA  
1283 C  C   . LYS A 158 ? 0.1935 0.2298 0.1565 0.0064  -0.0156 0.0099  159 LYS A C   
1284 O  O   . LYS A 158 ? 0.2280 0.2596 0.1554 -0.0597 -0.0231 0.0129  159 LYS A O   
1285 C  CB  . LYS A 158 ? 0.2402 0.3252 0.2495 0.0162  -0.0178 0.0161  159 LYS A CB  
1286 C  CG  . LYS A 158 ? 0.7274 0.5660 0.2814 -0.0850 -0.0468 0.1816  159 LYS A CG  
1287 C  CD  . LYS A 158 ? 0.9225 0.8141 0.9388 0.1495  -0.3509 0.3402  159 LYS A CD  
1288 C  CE  . LYS A 158 ? 1.0125 0.6161 1.2844 0.1222  -0.2675 0.3028  159 LYS A CE  
1289 N  NZ  . LYS A 158 ? 0.4540 0.5205 1.8360 -0.0790 -0.2795 0.2360  159 LYS A NZ  
1290 N  N   . VAL A 159 ? 0.2337 0.2068 0.1725 0.0016  -0.0522 -0.0171 160 VAL A N   
1291 C  CA  . VAL A 159 ? 0.2183 0.1756 0.1378 -0.0226 -0.0273 -0.0229 160 VAL A CA  
1292 C  C   . VAL A 159 ? 0.2237 0.2017 0.1145 -0.0285 0.0023  -0.0247 160 VAL A C   
1293 O  O   . VAL A 159 ? 0.2025 0.1982 0.1532 -0.0122 -0.0222 0.0020  160 VAL A O   
1294 C  CB  . VAL A 159 ? 0.2174 0.2195 0.1143 0.0264  0.0049  0.0002  160 VAL A CB  
1295 C  CG1 . VAL A 159 ? 0.1957 0.2680 0.1474 -0.0343 -0.0130 0.0061  160 VAL A CG1 
1296 C  CG2 . VAL A 159 ? 0.2738 0.2084 0.1831 0.0553  -0.0450 -0.0408 160 VAL A CG2 
1297 N  N   . VAL A 160 ? 0.2121 0.1590 0.1502 0.0085  -0.0266 -0.0041 161 VAL A N   
1298 C  CA  . VAL A 160 ? 0.2702 0.2018 0.1632 0.0179  0.0190  -0.0234 161 VAL A CA  
1299 C  C   . VAL A 160 ? 0.2443 0.2125 0.1747 -0.0115 0.0115  0.0094  161 VAL A C   
1300 O  O   . VAL A 160 ? 0.2586 0.1949 0.1801 -0.0347 0.0290  -0.0077 161 VAL A O   
1301 C  CB  . VAL A 160 ? 0.3201 0.1978 0.1781 0.0067  0.0510  0.0052  161 VAL A CB  
1302 C  CG1 . VAL A 160 ? 0.2964 0.2728 0.3111 -0.0136 -0.0603 -0.0854 161 VAL A CG1 
1303 C  CG2 . VAL A 160 ? 0.3788 0.2169 0.1745 0.0546  0.0243  -0.0086 161 VAL A CG2 
1304 N  N   . ASP A 161 ? 0.2868 0.2366 0.1558 -0.0644 -0.0450 0.0055  162 ASP A N   
1305 C  CA  . ASP A 161 ? 0.3310 0.2782 0.1414 -0.0700 0.0353  -0.0005 162 ASP A CA  
1306 C  C   . ASP A 161 ? 0.3884 0.2868 0.1486 -0.0917 -0.0149 0.0005  162 ASP A C   
1307 O  O   . ASP A 161 ? 0.4302 0.3657 0.1820 -0.1691 0.0647  -0.0356 162 ASP A O   
1308 C  CB  . ASP A 161 ? 0.4385 0.2958 0.1859 -0.0892 -0.0443 0.0379  162 ASP A CB  
1309 C  CG  . ASP A 161 ? 0.4025 0.2757 0.2104 -0.0637 -0.0501 0.0052  162 ASP A CG  
1310 O  OD1 . ASP A 161 ? 0.3202 0.3241 0.3641 -0.0816 0.0063  -0.0584 162 ASP A OD1 
1311 O  OD2 . ASP A 161 ? 0.3895 0.4196 0.2663 -0.0166 -0.0255 -0.0573 162 ASP A OD2 
1312 N  N   . VAL A 162 ? 0.2846 0.2205 0.1676 -0.0305 -0.0471 0.0089  163 VAL A N   
1313 C  CA  . VAL A 162 ? 0.2492 0.2231 0.1757 0.0085  -0.0260 0.0158  163 VAL A CA  
1314 C  C   . VAL A 162 ? 0.2316 0.1914 0.1637 -0.0201 -0.0048 -0.0009 163 VAL A C   
1315 O  O   . VAL A 162 ? 0.2754 0.2036 0.1535 -0.0510 0.0061  0.0013  163 VAL A O   
1316 C  CB  . VAL A 162 ? 0.3296 0.2009 0.2427 -0.0121 -0.0293 -0.0066 163 VAL A CB  
1317 C  CG1 . VAL A 162 ? 0.2630 0.2667 0.2825 0.0201  -0.0624 -0.0686 163 VAL A CG1 
1318 C  CG2 . VAL A 162 ? 0.3319 0.2940 0.2802 -0.0760 0.0487  0.0010  163 VAL A CG2 
1319 N  N   . LEU A 163 ? 0.2866 0.2132 0.1564 0.0149  -0.0436 -0.0244 164 LEU A N   
1320 C  CA  . LEU A 163 ? 0.2125 0.2233 0.1442 -0.0373 -0.0013 0.0029  164 LEU A CA  
1321 C  C   . LEU A 163 ? 0.3371 0.2016 0.1718 -0.0232 0.0347  -0.0390 164 LEU A C   
1322 O  O   . LEU A 163 ? 0.3134 0.2171 0.1486 0.0182  0.0398  0.0020  164 LEU A O   
1323 C  CB  . LEU A 163 ? 0.2337 0.2131 0.1500 -0.0324 0.0299  -0.0021 164 LEU A CB  
1324 C  CG  . LEU A 163 ? 0.2309 0.2039 0.1368 -0.0528 0.0092  0.0117  164 LEU A CG  
1325 C  CD1 . LEU A 163 ? 0.2097 0.2068 0.1945 0.0034  0.0198  0.0378  164 LEU A CD1 
1326 C  CD2 . LEU A 163 ? 0.2387 0.1806 0.1384 0.0106  -0.0181 0.0060  164 LEU A CD2 
1327 N  N   . ASP A 164 ? 0.3941 0.2501 0.1439 -0.0322 0.0353  -0.0293 165 ASP A N   
1328 C  CA  . ASP A 164 ? 0.4285 0.3243 0.1392 -0.0613 0.0550  -0.0392 165 ASP A CA  
1329 C  C   . ASP A 164 ? 0.3928 0.2915 0.1720 -0.0251 0.0378  -0.0403 165 ASP A C   
1330 O  O   . ASP A 164 ? 0.4656 0.3497 0.2218 0.0791  0.0826  -0.0596 165 ASP A O   
1331 C  CB  . ASP A 164 ? 0.5753 0.5865 0.2621 -0.2099 0.0609  -0.1894 165 ASP A CB  
1332 C  CG  . ASP A 164 ? 0.8679 1.3420 0.6689 -0.1395 -0.2588 0.0635  165 ASP A CG  
1333 O  OD1 . ASP A 164 ? 1.1385 1.3089 0.2754 -0.7243 0.1031  0.0526  165 ASP A OD1 
1334 O  OD2 . ASP A 164 ? 1.9535 1.0245 0.8761 -0.4447 -0.4107 -0.2535 165 ASP A OD2 
1335 N  N   . SER A 165 ? 0.3143 0.2269 0.1694 -0.0405 -0.0037 -0.0168 166 SER A N   
1336 C  CA  . SER A 165 ? 0.3854 0.2454 0.1318 -0.0220 -0.0192 -0.0116 166 SER A CA  
1337 C  C   . SER A 165 ? 0.2760 0.3061 0.1180 -0.0491 0.0380  0.0285  166 SER A C   
1338 O  O   . SER A 165 ? 0.2637 0.2809 0.1233 -0.0197 0.0305  0.0243  166 SER A O   
1339 C  CB  . SER A 165 ? 0.3197 0.3562 0.1546 0.0085  0.0674  0.0416  166 SER A CB  
1340 O  OG  . SER A 165 ? 0.3921 0.3108 0.1975 0.0451  -0.0068 0.0277  166 SER A OG  
1341 N  N   . ILE A 166 ? 0.2928 0.1896 0.1222 -0.0301 0.0116  0.0031  167 ILE A N   
1342 C  CA  . ILE A 166 ? 0.2276 0.2469 0.1272 -0.0233 0.0313  -0.0145 167 ILE A CA  
1343 C  C   . ILE A 166 ? 0.2474 0.1830 0.1251 -0.0243 0.0390  -0.0304 167 ILE A C   
1344 O  O   . ILE A 166 ? 0.2363 0.1754 0.1262 -0.0358 0.0399  -0.0077 167 ILE A O   
1345 C  CB  . ILE A 166 ? 0.2817 0.1829 0.1400 -0.0261 0.0526  -0.0051 167 ILE A CB  
1346 C  CG1 . ILE A 166 ? 0.3192 0.1963 0.1171 -0.0520 0.0713  -0.0151 167 ILE A CG1 
1347 C  CG2 . ILE A 166 ? 0.2662 0.1784 0.1626 -0.0152 0.0173  0.0094  167 ILE A CG2 
1348 C  CD1 . ILE A 166 ? 0.2433 0.1939 0.1230 0.0039  0.0650  -0.0218 167 ILE A CD1 
1349 N  N   . LYS A 167 ? 0.2010 0.1777 0.1463 -0.0203 0.0607  -0.0125 168 LYS A N   
1350 C  CA  . LYS A 167 ? 0.2106 0.1992 0.1382 0.0086  0.0482  -0.0321 168 LYS A CA  
1351 C  C   . LYS A 167 ? 0.2143 0.1870 0.1107 -0.0155 0.0805  -0.0027 168 LYS A C   
1352 O  O   . LYS A 167 ? 0.2376 0.1539 0.1300 -0.0177 0.0575  -0.0100 168 LYS A O   
1353 C  CB  . LYS A 167 ? 0.2715 0.1786 0.1320 -0.0071 0.0201  -0.0417 168 LYS A CB  
1354 C  CG  . LYS A 167 ? 0.3100 0.2043 0.1608 0.0076  0.0307  -0.0253 168 LYS A CG  
1355 C  CD  . LYS A 167 ? 0.4388 0.2548 0.2249 0.0326  -0.0321 -0.1094 168 LYS A CD  
1356 C  CE  . LYS A 167 ? 0.5163 0.2483 0.2837 0.0061  -0.0162 -0.0723 168 LYS A CE  
1357 N  NZ  . LYS A 167 ? 0.6939 0.4772 0.2921 -0.0086 0.0715  -0.1447 168 LYS A NZ  
1358 N  N   . THR A 168 ? 0.2395 0.1773 0.1310 -0.0453 0.0428  0.0081  169 THR A N   
1359 C  CA  . THR A 168 ? 0.2190 0.1622 0.1273 -0.0625 0.0713  -0.0100 169 THR A CA  
1360 C  C   . THR A 168 ? 0.2020 0.1675 0.1313 -0.0303 0.0967  -0.0113 169 THR A C   
1361 O  O   . THR A 168 ? 0.2652 0.1678 0.1464 -0.0383 0.0757  -0.0016 169 THR A O   
1362 C  CB  . THR A 168 ? 0.2370 0.1901 0.1547 -0.0392 0.0882  -0.0005 169 THR A CB  
1363 O  OG1 . THR A 168 ? 0.3146 0.2562 0.1424 -0.0600 0.0895  0.0254  169 THR A OG1 
1364 C  CG2 . THR A 168 ? 0.2341 0.1819 0.2007 0.0135  0.0775  -0.0043 169 THR A CG2 
1365 N  N   . LYS A 169 ? 0.2649 0.2204 0.1342 -0.0982 0.0685  -0.0204 170 LYS A N   
1366 C  CA  . LYS A 169 ? 0.2626 0.1833 0.1432 -0.0440 0.0606  0.0069  170 LYS A CA  
1367 C  C   . LYS A 169 ? 0.2038 0.2062 0.1382 -0.0364 0.0804  0.0299  170 LYS A C   
1368 O  O   . LYS A 169 ? 0.3404 0.2343 0.1463 -0.0923 0.1304  0.0006  170 LYS A O   
1369 C  CB  . LYS A 169 ? 0.2517 0.2456 0.1155 -0.0462 0.0497  -0.0068 170 LYS A CB  
1370 C  CG  . LYS A 169 ? 0.2583 0.2448 0.1601 -0.0584 0.0189  0.0184  170 LYS A CG  
1371 C  CD  . LYS A 169 ? 0.1845 0.2811 0.1744 -0.0690 0.0789  0.0073  170 LYS A CD  
1372 C  CE  . LYS A 169 ? 0.3085 0.5078 0.3022 -0.0012 0.1423  -0.0580 170 LYS A CE  
1373 N  NZ  . LYS A 169 ? 0.4656 0.8567 0.6176 -0.1056 -0.1020 0.1460  170 LYS A NZ  
1374 N  N   . GLY A 170 ? 0.2885 0.1486 0.1478 -0.0296 0.0423  0.0050  171 GLY A N   
1375 C  CA  . GLY A 170 ? 0.2445 0.1998 0.2059 -0.0198 0.0182  0.0655  171 GLY A CA  
1376 C  C   . GLY A 170 ? 0.2849 0.2269 0.1719 -0.0506 0.0168  0.0476  171 GLY A C   
1377 O  O   . GLY A 170 ? 0.3455 0.2075 0.2185 -0.0463 0.0023  0.0705  171 GLY A O   
1378 N  N   . LYS A 171 ? 0.2665 0.1892 0.1360 -0.0439 0.0416  0.0274  172 LYS A N   
1379 C  CA  . LYS A 171 ? 0.2077 0.2143 0.1697 -0.0374 0.0894  0.0250  172 LYS A CA  
1380 C  C   . LYS A 171 ? 0.1784 0.2521 0.1226 0.0057  0.0385  0.0340  172 LYS A C   
1381 O  O   . LYS A 171 ? 0.2615 0.2222 0.1275 -0.0406 0.0491  0.0267  172 LYS A O   
1382 C  CB  . LYS A 171 ? 0.2504 0.2200 0.1698 0.0002  0.0209  -0.0167 172 LYS A CB  
1383 C  CG  . LYS A 171 ? 0.2487 0.3126 0.3429 0.0212  0.0558  -0.1509 172 LYS A CG  
1384 C  CD  . LYS A 171 ? 0.4362 0.4323 0.3144 0.0106  -0.0190 -0.1905 172 LYS A CD  
1385 C  CE  . LYS A 171 ? 0.6827 0.4688 0.4147 -0.0745 -0.2259 -0.1008 172 LYS A CE  
1386 N  NZ  . LYS A 171 ? 0.6808 0.3035 0.2552 -0.0938 0.0994  -0.0358 172 LYS A NZ  
1387 N  N   . SER A 172 ? 0.2646 0.2613 0.1149 0.0357  0.0380  0.0228  173 SER A N   
1388 C  CA  . SER A 172 ? 0.2819 0.2353 0.1465 0.0534  0.0425  -0.0196 173 SER A CA  
1389 C  C   . SER A 172 ? 0.3100 0.2467 0.1283 0.0215  0.0741  0.0206  173 SER A C   
1390 O  O   . SER A 172 ? 0.2790 0.3407 0.1050 0.0478  0.0511  0.0262  173 SER A O   
1391 C  CB  . SER A 172 ? 0.3254 0.2404 0.1691 -0.0232 0.0902  0.0032  173 SER A CB  
1392 O  OG  . SER A 172 ? 0.3419 0.2871 0.2072 0.0678  0.0800  0.0682  173 SER A OG  
1393 N  N   . ALA A 173 ? 0.2725 0.3629 0.1474 0.0491  0.0427  0.0133  174 ALA A N   
1394 C  CA  . ALA A 173 ? 0.2738 0.3878 0.1903 0.0937  0.0434  0.0375  174 ALA A CA  
1395 C  C   . ALA A 173 ? 0.2481 0.4088 0.1472 0.1162  -0.0249 -0.0247 174 ALA A C   
1396 O  O   . ALA A 173 ? 0.2221 0.2624 0.1304 0.0403  -0.0040 0.0163  174 ALA A O   
1397 C  CB  . ALA A 173 ? 0.2964 0.3475 0.1715 0.0829  -0.0047 -0.0003 174 ALA A CB  
1398 N  N   . ASP A 174 ? 0.3080 0.3598 0.1377 0.1355  0.0229  0.0577  175 ASP A N   
1399 C  CA  . ASP A 174 ? 0.3222 0.3830 0.1601 0.1509  0.0230  0.0599  175 ASP A CA  
1400 C  C   . ASP A 174 ? 0.3087 0.3376 0.1751 0.1574  0.0347  0.0063  175 ASP A C   
1401 O  O   . ASP A 174 ? 0.3601 0.3700 0.1867 0.1079  -0.0114 -0.0416 175 ASP A O   
1402 C  CB  . ASP A 174 ? 0.3571 0.4302 0.1723 0.1736  0.0359  0.1077  175 ASP A CB  
1403 C  CG  . ASP A 174 ? 0.8649 0.5488 0.2402 0.0303  -0.0564 0.2259  175 ASP A CG  
1404 O  OD1 . ASP A 174 ? 1.3767 0.6580 0.4798 0.0753  -0.2874 0.0038  175 ASP A OD1 
1405 O  OD2 . ASP A 174 ? 1.0201 0.6898 0.2753 0.0489  0.1429  0.1849  175 ASP A OD2 
1406 N  N   . PHE A 175 ? 0.2688 0.3119 0.1514 0.0860  0.0420  0.0222  176 PHE A N   
1407 C  CA  . PHE A 175 ? 0.2752 0.2437 0.2157 0.0551  0.0043  0.0320  176 PHE A CA  
1408 C  C   . PHE A 175 ? 0.1878 0.2678 0.2384 0.0243  0.0113  0.0480  176 PHE A C   
1409 O  O   . PHE A 175 ? 0.3468 0.3266 0.2666 0.1527  -0.1024 -0.0339 176 PHE A O   
1410 C  CB  . PHE A 175 ? 0.3253 0.2194 0.2300 0.0365  -0.0261 0.0403  176 PHE A CB  
1411 C  CG  . PHE A 175 ? 0.3039 0.2096 0.1928 0.0306  0.0342  0.0260  176 PHE A CG  
1412 C  CD1 . PHE A 175 ? 0.3941 0.2637 0.1654 0.0126  -0.0075 0.0138  176 PHE A CD1 
1413 C  CD2 . PHE A 175 ? 0.2825 0.2534 0.1823 0.0250  -0.0158 0.0341  176 PHE A CD2 
1414 C  CE1 . PHE A 175 ? 0.4996 0.2032 0.2081 0.0529  0.0192  0.0009  176 PHE A CE1 
1415 C  CE2 . PHE A 175 ? 0.2136 0.1996 0.2237 0.0644  -0.0154 0.0240  176 PHE A CE2 
1416 C  CZ  . PHE A 175 ? 0.3267 0.2271 0.2003 0.0464  -0.0095 0.0094  176 PHE A CZ  
1417 N  N   . THR A 176 ? 0.2682 0.2455 0.1526 0.0607  0.0001  0.0489  177 THR A N   
1418 C  CA  . THR A 176 ? 0.2264 0.2554 0.1727 0.0392  0.0078  0.0845  177 THR A CA  
1419 C  C   . THR A 176 ? 0.2304 0.2082 0.1435 0.0298  -0.0243 0.0457  177 THR A C   
1420 O  O   . THR A 176 ? 0.3036 0.1995 0.1560 0.0268  -0.0234 0.0370  177 THR A O   
1421 C  CB  . THR A 176 ? 0.2869 0.2958 0.2359 -0.0061 -0.0860 0.1214  177 THR A CB  
1422 O  OG1 . THR A 176 ? 0.5590 0.4370 0.1687 0.1159  -0.0274 0.1071  177 THR A OG1 
1423 C  CG2 . THR A 176 ? 0.3763 0.2814 0.3582 -0.0357 -0.0554 0.1713  177 THR A CG2 
1424 N  N   . ASN A 177 ? 0.2311 0.2170 0.1557 0.0250  -0.0356 0.0200  178 ASN A N   
1425 C  CA  . ASN A 177 ? 0.2727 0.2415 0.2020 -0.0647 -0.0433 0.0838  178 ASN A CA  
1426 C  C   . ASN A 177 ? 0.2719 0.2089 0.1698 -0.0422 -0.0380 0.0355  178 ASN A C   
1427 O  O   . ASN A 177 ? 0.2740 0.2776 0.2732 -0.0519 -0.0951 0.1112  178 ASN A O   
1428 C  CB  . ASN A 177 ? 0.2468 0.2869 0.2562 -0.0147 -0.0761 0.1074  178 ASN A CB  
1429 C  CG  . ASN A 177 ? 0.2456 0.3278 0.2224 0.0800  -0.0226 0.1073  178 ASN A CG  
1430 O  OD1 . ASN A 177 ? 0.2427 0.3169 0.3953 0.0933  -0.0051 0.0591  178 ASN A OD1 
1431 N  ND2 . ASN A 177 ? 0.2333 0.4382 0.2043 -0.0070 -0.0629 0.1408  178 ASN A ND2 
1432 N  N   . PHE A 178 ? 0.2712 0.2267 0.1332 -0.0042 0.0013  0.0502  179 PHE A N   
1433 C  CA  . PHE A 178 ? 0.2622 0.2370 0.1423 0.0302  -0.0157 0.0509  179 PHE A CA  
1434 C  C   . PHE A 178 ? 0.2028 0.2139 0.1544 0.0207  -0.0215 0.0275  179 PHE A C   
1435 O  O   . PHE A 178 ? 0.2329 0.2391 0.1316 -0.0266 -0.0147 0.0070  179 PHE A O   
1436 C  CB  . PHE A 178 ? 0.2443 0.2258 0.1319 0.0047  0.0053  0.0473  179 PHE A CB  
1437 C  CG  . PHE A 178 ? 0.2258 0.2407 0.1414 0.0063  -0.0008 0.0603  179 PHE A CG  
1438 C  CD1 . PHE A 178 ? 0.2469 0.2389 0.1744 0.0098  0.0042  0.0260  179 PHE A CD1 
1439 C  CD2 . PHE A 178 ? 0.2340 0.3043 0.1234 0.0310  0.0152  0.0592  179 PHE A CD2 
1440 C  CE1 . PHE A 178 ? 0.3353 0.2790 0.1592 0.0205  0.0053  0.0204  179 PHE A CE1 
1441 C  CE2 . PHE A 178 ? 0.1783 0.2661 0.1405 0.0344  -0.0143 0.0324  179 PHE A CE2 
1442 C  CZ  . PHE A 178 ? 0.2297 0.2791 0.1517 0.0518  0.0088  0.0268  179 PHE A CZ  
1443 N  N   . ASP A 179 ? 0.1704 0.2558 0.1553 0.0295  -0.0376 0.0254  180 ASP A N   
1444 C  CA  . ASP A 179 ? 0.1520 0.2542 0.1514 0.0186  -0.0175 0.0225  180 ASP A CA  
1445 C  C   . ASP A 179 ? 0.1504 0.2226 0.1698 0.0178  -0.0133 0.0157  180 ASP A C   
1446 O  O   . ASP A 179 ? 0.1653 0.2207 0.1734 -0.0157 -0.0212 0.0154  180 ASP A O   
1447 C  CB  . ASP A 179 ? 0.1477 0.3256 0.1817 0.0207  -0.0085 0.0476  180 ASP A CB  
1448 C  CG  . ASP A 179 ? 0.1450 0.3281 0.1939 0.0250  -0.0115 0.0247  180 ASP A CG  
1449 O  OD1 . ASP A 179 ? 0.1887 0.2402 0.2025 0.0051  -0.0369 0.0179  180 ASP A OD1 
1450 O  OD2 . ASP A 179 ? 0.1506 0.5647 0.2594 -0.0089 -0.0425 -0.0580 180 ASP A OD2 
1451 N  N   . PRO A 180 ? 0.1327 0.1784 0.1899 0.0037  -0.0148 0.0161  181 PRO A N   
1452 C  CA  . PRO A 180 ? 0.1225 0.2543 0.1618 -0.0279 -0.0192 0.0319  181 PRO A CA  
1453 C  C   . PRO A 180 ? 0.1247 0.2068 0.1582 0.0027  -0.0081 0.0095  181 PRO A C   
1454 O  O   . PRO A 180 ? 0.1310 0.2032 0.1504 0.0038  0.0095  0.0276  181 PRO A O   
1455 C  CB  . PRO A 180 ? 0.1640 0.1977 0.1902 -0.0337 -0.0048 0.0149  181 PRO A CB  
1456 C  CG  . PRO A 180 ? 0.1845 0.2079 0.1543 -0.0223 -0.0221 0.0271  181 PRO A CG  
1457 C  CD  . PRO A 180 ? 0.1675 0.1880 0.1740 0.0132  -0.0381 0.0230  181 PRO A CD  
1458 N  N   . ARG A 181 ? 0.1161 0.1949 0.1517 0.0044  0.0094  0.0113  182 ARG A N   
1459 C  CA  . ARG A 181 ? 0.1046 0.2092 0.1822 0.0005  0.0065  0.0294  182 ARG A CA  
1460 C  C   . ARG A 181 ? 0.1417 0.2246 0.1858 -0.0054 -0.0245 0.0463  182 ARG A C   
1461 O  O   . ARG A 181 ? 0.1510 0.2625 0.2178 -0.0154 -0.0047 0.0801  182 ARG A O   
1462 C  CB  . ARG A 181 ? 0.0874 0.2328 0.2043 -0.0130 -0.0153 0.0301  182 ARG A CB  
1463 C  CG  . ARG A 181 ? 0.1488 0.2287 0.2264 0.0038  0.0316  0.0249  182 ARG A CG  
1464 C  CD  . ARG A 181 ? 0.2172 0.2730 0.2638 0.0813  0.0504  0.0392  182 ARG A CD  
1465 N  NE  . ARG A 181 ? 0.1507 0.2861 0.2919 -0.0161 -0.0185 0.0658  182 ARG A NE  
1466 C  CZ  . ARG A 181 ? 0.1860 0.4129 0.2938 0.0681  0.0111  0.0531  182 ARG A CZ  
1467 N  NH1 . ARG A 181 ? 0.2368 0.4305 0.4129 0.1099  0.0024  -0.0218 182 ARG A NH1 
1468 N  NH2 . ARG A 181 ? 0.1932 0.4670 0.3182 0.0877  -0.0060 0.0944  182 ARG A NH2 
1469 N  N   . GLY A 182 ? 0.1465 0.2233 0.1901 -0.0006 -0.0370 0.0184  183 GLY A N   
1470 C  CA  . GLY A 182 ? 0.1482 0.2038 0.2103 -0.0211 -0.0370 0.0305  183 GLY A CA  
1471 C  C   . GLY A 182 ? 0.1576 0.2253 0.2023 0.0057  -0.0290 0.0152  183 GLY A C   
1472 O  O   . GLY A 182 ? 0.2468 0.1977 0.2961 -0.0005 -0.1237 0.0027  183 GLY A O   
1473 N  N   . LEU A 183 ? 0.1508 0.2229 0.1508 -0.0044 -0.0220 -0.0066 184 LEU A N   
1474 C  CA  . LEU A 183 ? 0.1395 0.1867 0.1574 -0.0046 -0.0061 0.0026  184 LEU A CA  
1475 C  C   . LEU A 183 ? 0.1766 0.2133 0.1583 -0.0097 -0.0504 -0.0118 184 LEU A C   
1476 O  O   . LEU A 183 ? 0.1235 0.2111 0.1769 -0.0121 -0.0159 0.0267  184 LEU A O   
1477 C  CB  . LEU A 183 ? 0.1475 0.1888 0.1635 0.0258  0.0051  0.0226  184 LEU A CB  
1478 C  CG  . LEU A 183 ? 0.1769 0.1949 0.1502 0.0318  0.0111  0.0113  184 LEU A CG  
1479 C  CD1 . LEU A 183 ? 0.2078 0.3087 0.1594 0.0062  0.0157  0.0373  184 LEU A CD1 
1480 C  CD2 . LEU A 183 ? 0.3076 0.2601 0.1644 0.0568  -0.0110 -0.0217 184 LEU A CD2 
1481 N  N   . LEU A 184 ? 0.1601 0.1845 0.1802 -0.0003 -0.0109 0.0189  185 LEU A N   
1482 C  CA  . LEU A 184 ? 0.1439 0.1817 0.2036 -0.0401 -0.0135 0.0453  185 LEU A CA  
1483 C  C   . LEU A 184 ? 0.2031 0.2023 0.2662 -0.0690 -0.0893 0.0718  185 LEU A C   
1484 O  O   . LEU A 184 ? 0.3198 0.3077 0.3353 -0.1652 -0.2013 0.1468  185 LEU A O   
1485 C  CB  . LEU A 184 ? 0.0982 0.1948 0.1942 -0.0350 -0.0075 0.0498  185 LEU A CB  
1486 C  CG  . LEU A 184 ? 0.0845 0.1863 0.2276 -0.0156 -0.0109 0.0223  185 LEU A CG  
1487 C  CD1 . LEU A 184 ? 0.1377 0.2551 0.1938 0.0315  -0.0089 -0.0047 185 LEU A CD1 
1488 C  CD2 . LEU A 184 ? 0.1185 0.2151 0.2470 -0.0258 -0.0583 0.0097  185 LEU A CD2 
1489 N  N   . PRO A 185 ? 0.0718 0.1910 0.2064 -0.0309 -0.0084 0.0446  186 PRO A N   
1490 C  CA  . PRO A 185 ? 0.1342 0.1852 0.2002 -0.0368 -0.0126 0.0405  186 PRO A CA  
1491 C  C   . PRO A 185 ? 0.1018 0.1995 0.2312 -0.0401 -0.0168 0.0443  186 PRO A C   
1492 O  O   . PRO A 185 ? 0.0562 0.1980 0.3384 -0.0149 -0.0273 0.0553  186 PRO A O   
1493 C  CB  . PRO A 185 ? 0.0770 0.1680 0.2352 -0.0196 -0.0004 0.0472  186 PRO A CB  
1494 C  CG  . PRO A 185 ? 0.0578 0.1959 0.1635 -0.0032 0.0035  0.0219  186 PRO A CG  
1495 C  CD  . PRO A 185 ? 0.1002 0.1752 0.1587 0.0170  -0.0098 0.0036  186 PRO A CD  
1496 N  N   . GLU A 186 ? 0.1353 0.1946 0.2116 -0.0557 0.0025  0.0257  187 GLU A N   
1497 C  CA  . GLU A 186 ? 0.1074 0.2495 0.2262 -0.0622 0.0002  0.0640  187 GLU A CA  
1498 C  C   . GLU A 186 ? 0.0822 0.1963 0.2540 -0.0322 0.0034  0.0596  187 GLU A C   
1499 O  O   . GLU A 186 ? 0.0980 0.2284 0.2854 0.0053  -0.0078 0.0601  187 GLU A O   
1500 C  CB  . GLU A 186 ? 0.1496 0.2452 0.3913 -0.0784 -0.0392 0.0757  187 GLU A CB  
1501 C  CG  . GLU A 186 ? 0.1567 0.3245 0.4439 -0.0241 -0.0194 0.0363  187 GLU A CG  
1502 C  CD  . GLU A 186 ? 0.1143 0.3717 0.3790 -0.0298 -0.0500 0.0565  187 GLU A CD  
1503 O  OE1 . GLU A 186 ? 0.1870 0.2364 0.6449 -0.0908 0.0672  -0.0370 187 GLU A OE1 
1504 O  OE2 . GLU A 186 ? 0.3050 0.4677 0.6610 0.0141  0.1967  0.1899  187 GLU A OE2 
1505 N  N   . SER A 187 ? 0.0273 0.2256 0.2225 -0.0395 0.0068  0.0425  188 SER A N   
1506 C  CA  . SER A 187 ? 0.0962 0.2018 0.2390 -0.0390 0.0132  0.0344  188 SER A CA  
1507 C  C   . SER A 187 ? 0.1040 0.2053 0.1984 -0.0356 0.0185  0.0170  188 SER A C   
1508 O  O   . SER A 187 ? 0.1128 0.2248 0.1895 -0.0329 0.0353  0.0034  188 SER A O   
1509 C  CB  . SER A 187 ? 0.1044 0.2465 0.2050 -0.0258 -0.0008 0.0295  188 SER A CB  
1510 O  OG  . SER A 187 ? 0.0844 0.2189 0.2321 -0.0367 0.0042  0.0357  188 SER A OG  
1511 N  N   . LEU A 188 ? 0.0853 0.1781 0.2211 0.0019  -0.0027 0.0185  189 LEU A N   
1512 C  CA  . LEU A 188 ? 0.0634 0.2010 0.2264 -0.0002 0.0173  0.0076  189 LEU A CA  
1513 C  C   . LEU A 188 ? 0.0607 0.1779 0.2036 0.0197  0.0362  -0.0122 189 LEU A C   
1514 O  O   . LEU A 188 ? 0.1221 0.2075 0.2073 -0.0122 -0.0051 0.0000  189 LEU A O   
1515 C  CB  . LEU A 188 ? 0.1124 0.1946 0.2870 -0.0153 0.0084  0.0310  189 LEU A CB  
1516 C  CG  . LEU A 188 ? 0.0932 0.2407 0.3050 0.0350  0.0172  0.0234  189 LEU A CG  
1517 C  CD1 . LEU A 188 ? 0.1364 0.2300 0.4273 0.0350  0.0239  0.0603  189 LEU A CD1 
1518 C  CD2 . LEU A 188 ? 0.1092 0.3574 0.2847 0.0276  0.0250  0.0462  189 LEU A CD2 
1519 N  N   . ASP A 189 ? 0.0593 0.2064 0.1899 0.0140  0.0341  -0.0065 190 ASP A N   
1520 C  CA  . ASP A 189 ? 0.0612 0.2297 0.1888 -0.0430 0.0132  0.0334  190 ASP A CA  
1521 C  C   . ASP A 189 ? 0.0664 0.1712 0.1854 -0.0034 0.0247  -0.0226 190 ASP A C   
1522 O  O   . ASP A 189 ? 0.0765 0.1641 0.1381 -0.0252 0.0163  0.0000  190 ASP A O   
1523 C  CB  . ASP A 189 ? 0.1181 0.2712 0.1799 -0.1032 0.0115  0.0542  190 ASP A CB  
1524 C  CG  . ASP A 189 ? 0.1712 0.3501 0.1909 -0.1271 0.0522  0.0022  190 ASP A CG  
1525 O  OD1 . ASP A 189 ? 0.1311 0.4541 0.2278 -0.0678 0.0784  0.0006  190 ASP A OD1 
1526 O  OD2 . ASP A 189 ? 0.2143 0.4538 0.3592 -0.2024 0.0177  0.0956  190 ASP A OD2 
1527 N  N   . TYR A 190 ? 0.0560 0.1884 0.1465 -0.0088 0.0275  0.0082  191 TYR A N   
1528 C  CA  . TYR A 190 ? 0.0588 0.1715 0.1465 -0.0206 0.0205  0.0193  191 TYR A CA  
1529 C  C   . TYR A 190 ? 0.0831 0.1565 0.1158 -0.0126 0.0270  0.0195  191 TYR A C   
1530 O  O   . TYR A 190 ? 0.0989 0.1773 0.1126 -0.0226 0.0359  0.0135  191 TYR A O   
1531 C  CB  . TYR A 190 ? 0.0851 0.1593 0.1407 -0.0163 0.0502  0.0173  191 TYR A CB  
1532 C  CG  . TYR A 190 ? 0.0917 0.1666 0.1364 0.0078  0.0339  0.0042  191 TYR A CG  
1533 C  CD1 . TYR A 190 ? 0.0933 0.1427 0.1614 -0.0339 0.0499  0.0132  191 TYR A CD1 
1534 C  CD2 . TYR A 190 ? 0.0959 0.1729 0.1651 0.0153  0.0441  0.0221  191 TYR A CD2 
1535 C  CE1 . TYR A 190 ? 0.0989 0.1429 0.1673 -0.0126 0.0335  0.0131  191 TYR A CE1 
1536 C  CE2 . TYR A 190 ? 0.0710 0.1808 0.1583 0.0108  0.0292  0.0185  191 TYR A CE2 
1537 C  CZ  . TYR A 190 ? 0.1275 0.1697 0.1669 -0.0048 0.0170  0.0173  191 TYR A CZ  
1538 O  OH  . TYR A 190 ? 0.1012 0.1769 0.1881 0.0119  0.0160  -0.0010 191 TYR A OH  
1539 N  N   . TRP A 191 ? 0.0776 0.1384 0.1265 -0.0143 0.0196  0.0027  192 TRP A N   
1540 C  CA  . TRP A 191 ? 0.0572 0.1349 0.1143 -0.0027 0.0300  0.0274  192 TRP A CA  
1541 C  C   . TRP A 191 ? 0.0425 0.1344 0.1104 0.0044  0.0453  0.0098  192 TRP A C   
1542 O  O   . TRP A 191 ? 0.0944 0.1500 0.1005 -0.0207 0.0417  0.0073  192 TRP A O   
1543 C  CB  . TRP A 191 ? 0.0503 0.1402 0.1403 -0.0033 0.0480  0.0038  192 TRP A CB  
1544 C  CG  . TRP A 191 ? 0.0657 0.1459 0.1307 -0.0005 0.0387  0.0130  192 TRP A CG  
1545 C  CD1 . TRP A 191 ? 0.1117 0.1500 0.1304 0.0004  0.0205  0.0196  192 TRP A CD1 
1546 C  CD2 . TRP A 191 ? 0.0603 0.1554 0.1346 0.0136  0.0192  0.0100  192 TRP A CD2 
1547 N  NE1 . TRP A 191 ? 0.1396 0.1386 0.1558 0.0086  0.0444  0.0186  192 TRP A NE1 
1548 C  CE2 . TRP A 191 ? 0.1158 0.1249 0.1716 0.0152  0.0325  0.0093  192 TRP A CE2 
1549 C  CE3 . TRP A 191 ? 0.0768 0.1590 0.1371 0.0043  0.0092  0.0122  192 TRP A CE3 
1550 C  CZ2 . TRP A 191 ? 0.1102 0.1450 0.1924 0.0026  -0.0119 0.0170  192 TRP A CZ2 
1551 C  CZ3 . TRP A 191 ? 0.0574 0.1683 0.1988 -0.0020 0.0061  -0.0126 192 TRP A CZ3 
1552 C  CH2 . TRP A 191 ? 0.1028 0.1640 0.2025 0.0010  -0.0021 -0.0161 192 TRP A CH2 
1553 N  N   . THR A 192 ? 0.0586 0.1471 0.0944 -0.0004 0.0368  0.0104  193 THR A N   
1554 C  CA  . THR A 192 ? 0.0564 0.1434 0.1156 -0.0093 0.0527  0.0131  193 THR A CA  
1555 C  C   . THR A 192 ? 0.0838 0.1195 0.1118 -0.0027 0.0427  0.0199  193 THR A C   
1556 O  O   . THR A 192 ? 0.0784 0.1599 0.1073 0.0111  0.0413  0.0151  193 THR A O   
1557 C  CB  . THR A 192 ? 0.0935 0.1335 0.1095 0.0021  0.0677  0.0089  193 THR A CB  
1558 O  OG1 . THR A 192 ? 0.0648 0.1386 0.1253 -0.0013 0.0405  0.0030  193 THR A OG1 
1559 C  CG2 . THR A 192 ? 0.1016 0.1662 0.1194 0.0135  0.0750  0.0008  193 THR A CG2 
1560 N  N   . TYR A 193 ? 0.0662 0.1500 0.1068 -0.0124 0.0256  0.0136  194 TYR A N   
1561 C  CA  . TYR A 193 ? 0.0371 0.1493 0.1231 -0.0031 0.0308  0.0013  194 TYR A CA  
1562 C  C   . TYR A 193 ? 0.0696 0.1084 0.1111 0.0092  0.0290  -0.0086 194 TYR A C   
1563 O  O   . TYR A 193 ? 0.0807 0.1244 0.1070 0.0050  0.0315  -0.0027 194 TYR A O   
1564 C  CB  . TYR A 193 ? 0.0743 0.1272 0.1199 -0.0082 0.0321  -0.0055 194 TYR A CB  
1565 C  CG  . TYR A 193 ? 0.0664 0.1388 0.1217 0.0020  0.0149  -0.0104 194 TYR A CG  
1566 C  CD1 . TYR A 193 ? 0.0855 0.1307 0.1156 0.0154  0.0118  -0.0116 194 TYR A CD1 
1567 C  CD2 . TYR A 193 ? 0.0621 0.1270 0.1226 0.0043  -0.0044 -0.0114 194 TYR A CD2 
1568 C  CE1 . TYR A 193 ? 0.0774 0.1256 0.1140 -0.0073 0.0278  0.0160  194 TYR A CE1 
1569 C  CE2 . TYR A 193 ? 0.1073 0.1322 0.1231 0.0051  0.0095  -0.0321 194 TYR A CE2 
1570 C  CZ  . TYR A 193 ? 0.0779 0.1461 0.1034 -0.0105 0.0258  -0.0092 194 TYR A CZ  
1571 O  OH  . TYR A 193 ? 0.0513 0.1344 0.1023 -0.0057 0.0216  -0.0063 194 TYR A OH  
1572 N  N   . PRO A 194 ? 0.0797 0.1208 0.1003 0.0075  0.0190  -0.0082 195 PRO A N   
1573 C  CA  . PRO A 194 ? 0.0646 0.1224 0.1360 0.0086  0.0208  -0.0026 195 PRO A CA  
1574 C  C   . PRO A 194 ? 0.0781 0.1348 0.1045 0.0089  0.0137  -0.0151 195 PRO A C   
1575 O  O   . PRO A 194 ? 0.0706 0.1504 0.1140 0.0146  0.0212  -0.0005 195 PRO A O   
1576 C  CB  . PRO A 194 ? 0.0826 0.2000 0.1154 -0.0097 0.0166  -0.0103 195 PRO A CB  
1577 C  CG  . PRO A 194 ? 0.1053 0.1666 0.1284 -0.0117 0.0248  -0.0120 195 PRO A CG  
1578 C  CD  . PRO A 194 ? 0.0939 0.1497 0.1016 0.0034  0.0436  -0.0080 195 PRO A CD  
1579 N  N   . GLY A 195 ? 0.0520 0.1312 0.1046 0.0059  0.0356  -0.0037 196 GLY A N   
1580 C  CA  . GLY A 195 ? 0.0580 0.1641 0.1144 0.0210  0.0472  0.0122  196 GLY A CA  
1581 C  C   . GLY A 195 ? 0.0662 0.1284 0.1149 -0.0021 0.0257  -0.0038 196 GLY A C   
1582 O  O   . GLY A 195 ? 0.0798 0.1212 0.1122 0.0077  0.0245  -0.0086 196 GLY A O   
1583 N  N   . SER A 196 ? 0.0534 0.1317 0.1005 -0.0033 0.0100  -0.0055 197 SER A N   
1584 C  CA  . SER A 196 ? 0.0531 0.1248 0.1339 -0.0204 0.0182  0.0049  197 SER A CA  
1585 C  C   . SER A 196 ? 0.0291 0.1122 0.1180 0.0143  0.0363  0.0009  197 SER A C   
1586 O  O   . SER A 196 ? 0.0481 0.1208 0.1233 -0.0023 0.0322  -0.0027 197 SER A O   
1587 C  CB  . SER A 196 ? 0.0732 0.1464 0.1339 0.0232  0.0117  -0.0134 197 SER A CB  
1588 O  OG  . SER A 196 ? 0.0549 0.1382 0.1232 0.0154  0.0207  -0.0120 197 SER A OG  
1589 N  N   . LEU A 197 ? 0.0734 0.1174 0.1041 0.0006  0.0383  -0.0044 198 LEU A N   
1590 C  CA  . LEU A 197 ? 0.0416 0.1403 0.1113 -0.0196 0.0473  -0.0166 198 LEU A CA  
1591 C  C   . LEU A 197 ? 0.0551 0.1500 0.1032 -0.0052 0.0291  -0.0036 198 LEU A C   
1592 O  O   . LEU A 197 ? 0.0594 0.1353 0.1059 -0.0016 0.0267  -0.0149 198 LEU A O   
1593 C  CB  . LEU A 197 ? 0.0436 0.1472 0.1583 -0.0104 0.0354  0.0234  198 LEU A CB  
1594 C  CG  . LEU A 197 ? 0.0889 0.1575 0.1679 -0.0092 0.0431  0.0272  198 LEU A CG  
1595 C  CD1 . LEU A 197 ? 0.0955 0.1873 0.1733 -0.0084 0.0445  0.0445  198 LEU A CD1 
1596 C  CD2 . LEU A 197 ? 0.0870 0.1754 0.2070 -0.0110 0.0387  0.0315  198 LEU A CD2 
1597 N  N   . THR A 198 ? 0.0502 0.1304 0.1170 -0.0006 0.0400  -0.0122 199 THR A N   
1598 C  CA  . THR A 198 ? 0.0437 0.1283 0.1353 -0.0076 0.0409  -0.0135 199 THR A CA  
1599 C  C   . THR A 198 ? 0.0619 0.1228 0.1031 -0.0049 0.0297  -0.0087 199 THR A C   
1600 O  O   . THR A 198 ? 0.0459 0.1362 0.1280 -0.0010 0.0294  0.0050  199 THR A O   
1601 C  CB  . THR A 198 ? 0.0530 0.1156 0.1150 -0.0130 0.0446  0.0057  199 THR A CB  
1602 O  OG1 . THR A 198 ? 0.0607 0.1177 0.1206 -0.0052 0.0354  0.0012  199 THR A OG1 
1603 C  CG2 . THR A 198 ? 0.0542 0.1296 0.1234 0.0052  0.0471  -0.0031 199 THR A CG2 
1604 N  N   . THR A 199 ? 0.0804 0.1282 0.1108 -0.0129 0.0421  -0.0027 200 THR A N   
1605 C  CA  . THR A 199 ? 0.0838 0.1346 0.1164 -0.0157 0.0447  -0.0042 200 THR A CA  
1606 C  C   . THR A 199 ? 0.0463 0.1625 0.1257 -0.0208 0.0447  0.0022  200 THR A C   
1607 O  O   . THR A 199 ? 0.0651 0.1569 0.1327 -0.0129 0.0326  -0.0076 200 THR A O   
1608 C  CB  . THR A 199 ? 0.0776 0.1490 0.1262 -0.0089 0.0412  -0.0096 200 THR A CB  
1609 O  OG1 . THR A 199 ? 0.1198 0.1423 0.1546 -0.0038 0.0106  -0.0167 200 THR A OG1 
1610 C  CG2 . THR A 199 ? 0.0811 0.1468 0.1323 0.0043  0.0211  -0.0268 200 THR A CG2 
1611 N  N   . PRO A 200 ? 0.0530 0.1601 0.1269 -0.0150 0.0548  0.0027  201 PRO A N   
1612 C  CA  . PRO A 200 ? 0.0400 0.1766 0.1641 -0.0264 0.0207  0.0016  201 PRO A CA  
1613 C  C   . PRO A 200 ? 0.1144 0.1700 0.1522 -0.0131 0.0391  -0.0048 201 PRO A C   
1614 O  O   . PRO A 200 ? 0.1317 0.1995 0.1418 -0.0111 0.0199  -0.0023 201 PRO A O   
1615 C  CB  . PRO A 200 ? 0.0655 0.1932 0.2161 0.0038  0.0329  -0.0521 201 PRO A CB  
1616 C  CG  . PRO A 200 ? 0.0844 0.1928 0.2009 -0.0106 0.0369  -0.0475 201 PRO A CG  
1617 C  CD  . PRO A 200 ? 0.0630 0.1980 0.1751 0.0168  0.0370  -0.0408 201 PRO A CD  
1618 N  N   . PRO A 201 ? 0.0865 0.1657 0.1619 -0.0278 0.0297  -0.0074 202 PRO A N   
1619 C  CA  . PRO A 201 ? 0.1244 0.1658 0.1441 -0.0330 0.0149  0.0276  202 PRO A CA  
1620 C  C   . PRO A 201 ? 0.0576 0.1468 0.1508 -0.0058 0.0323  0.0096  202 PRO A C   
1621 O  O   . PRO A 201 ? 0.0635 0.1730 0.1708 -0.0308 0.0267  -0.0092 202 PRO A O   
1622 C  CB  . PRO A 201 ? 0.1399 0.1686 0.2086 -0.0491 0.0451  0.0249  202 PRO A CB  
1623 C  CG  . PRO A 201 ? 0.1556 0.1676 0.2114 -0.0009 0.0178  -0.0184 202 PRO A CG  
1624 C  CD  . PRO A 201 ? 0.1698 0.1973 0.1360 -0.0019 0.0421  0.0002  202 PRO A CD  
1625 N  N   . LEU A 202 ? 0.0506 0.1363 0.1526 -0.0087 0.0331  0.0137  203 LEU A N   
1626 C  CA  . LEU A 202 ? 0.0558 0.1583 0.1341 0.0055  0.0424  0.0031  203 LEU A CA  
1627 C  C   . LEU A 202 ? 0.0423 0.1443 0.1659 -0.0105 0.0357  -0.0070 203 LEU A C   
1628 O  O   . LEU A 202 ? 0.0582 0.1483 0.1536 -0.0111 0.0255  -0.0118 203 LEU A O   
1629 C  CB  . LEU A 202 ? 0.0540 0.1508 0.1368 0.0046  0.0219  -0.0089 203 LEU A CB  
1630 C  CG  . LEU A 202 ? 0.0283 0.1526 0.1482 0.0001  0.0531  -0.0013 203 LEU A CG  
1631 C  CD1 . LEU A 202 ? 0.0346 0.1863 0.2135 0.0177  0.0452  -0.0127 203 LEU A CD1 
1632 C  CD2 . LEU A 202 ? 0.0443 0.1416 0.1690 -0.0002 0.0447  -0.0026 203 LEU A CD2 
1633 N  N   . LEU A 203 ? 0.0515 0.1490 0.1502 0.0008  0.0262  -0.0052 204 LEU A N   
1634 C  CA  . LEU A 203 ? 0.0722 0.1567 0.1410 -0.0093 0.0433  0.0015  204 LEU A CA  
1635 C  C   . LEU A 203 ? 0.0812 0.1272 0.1349 -0.0151 0.0348  0.0019  204 LEU A C   
1636 O  O   . LEU A 203 ? 0.0719 0.1400 0.1297 -0.0106 0.0322  -0.0216 204 LEU A O   
1637 C  CB  . LEU A 203 ? 0.0790 0.1254 0.1612 -0.0182 0.0297  0.0128  204 LEU A CB  
1638 C  CG  . LEU A 203 ? 0.1183 0.1544 0.1949 -0.0241 0.0502  0.0219  204 LEU A CG  
1639 C  CD1 . LEU A 203 ? 0.1068 0.1802 0.2541 0.0069  0.0624  0.0418  204 LEU A CD1 
1640 C  CD2 . LEU A 203 ? 0.1081 0.2327 0.3112 -0.0919 0.0869  0.0091  204 LEU A CD2 
1641 N  N   . GLU A 204 ? 0.0862 0.1840 0.1456 -0.0270 0.0436  -0.0267 205 GLU A N   
1642 C  CA  . GLU A 204 ? 0.0633 0.1661 0.1263 -0.0084 0.0251  0.0002  205 GLU A CA  
1643 C  C   . GLU A 204 ? 0.0686 0.1486 0.1429 -0.0065 0.0241  -0.0196 205 GLU A C   
1644 O  O   . GLU A 204 ? 0.1065 0.1919 0.1431 0.0080  0.0103  -0.0300 205 GLU A O   
1645 C  CB  . GLU A 204 ? 0.0793 0.1479 0.1550 0.0022  -0.0010 -0.0207 205 GLU A CB  
1646 C  CG  . GLU A 204 ? 0.0727 0.1745 0.1507 0.0221  0.0192  -0.0093 205 GLU A CG  
1647 C  CD  . GLU A 204 ? 0.0718 0.1668 0.1630 -0.0176 0.0050  -0.0179 205 GLU A CD  
1648 O  OE1 . GLU A 204 ? 0.1213 0.1730 0.2017 -0.0013 -0.0212 -0.0355 205 GLU A OE1 
1649 O  OE2 . GLU A 204 ? 0.0812 0.1698 0.1641 0.0009  -0.0139 -0.0156 205 GLU A OE2 
1650 N  N   . CYS A 205 ? 0.0538 0.1086 0.1418 -0.0283 0.0245  -0.0100 206 CYS A N   
1651 C  CA  . CYS A 205 ? 0.0709 0.1120 0.1490 -0.0139 0.0363  -0.0082 206 CYS A CA  
1652 C  C   . CYS A 205 ? 0.0844 0.1205 0.1047 -0.0188 0.0308  -0.0046 206 CYS A C   
1653 O  O   . CYS A 205 ? 0.0914 0.1235 0.1371 -0.0068 0.0120  0.0113  206 CYS A O   
1654 C  CB  . CYS A 205 ? 0.0961 0.1533 0.1495 -0.0088 0.0658  -0.0118 206 CYS A CB  
1655 S  SG  . CYS A 205 ? 0.1120 0.1493 0.1375 -0.0094 0.0274  -0.0040 206 CYS A SG  
1656 N  N   . VAL A 206 ? 0.0675 0.1225 0.1107 -0.0073 0.0260  0.0008  207 VAL A N   
1657 C  CA  . VAL A 206 ? 0.0671 0.1234 0.1232 -0.0039 0.0225  0.0042  207 VAL A CA  
1658 C  C   . VAL A 206 ? 0.0639 0.1244 0.1518 0.0107  0.0315  0.0177  207 VAL A C   
1659 O  O   . VAL A 206 ? 0.0715 0.1497 0.1432 -0.0046 0.0161  0.0148  207 VAL A O   
1660 C  CB  . VAL A 206 ? 0.0616 0.1196 0.1370 -0.0194 0.0446  -0.0012 207 VAL A CB  
1661 C  CG1 . VAL A 206 ? 0.0488 0.1445 0.1210 -0.0043 0.0408  -0.0179 207 VAL A CG1 
1662 C  CG2 . VAL A 206 ? 0.0829 0.1565 0.1149 -0.0032 0.0418  -0.0037 207 VAL A CG2 
1663 N  N   . THR A 207 ? 0.0522 0.1059 0.1495 -0.0062 0.0347  -0.0084 208 THR A N   
1664 C  CA  . THR A 207 ? 0.0739 0.1180 0.1302 -0.0097 0.0222  0.0005  208 THR A CA  
1665 C  C   . THR A 207 ? 0.0330 0.1183 0.1316 -0.0118 0.0337  0.0043  208 THR A C   
1666 O  O   . THR A 207 ? 0.0519 0.1239 0.1270 0.0027  0.0262  0.0051  208 THR A O   
1667 C  CB  . THR A 207 ? 0.0727 0.1229 0.1374 -0.0004 0.0146  0.0128  208 THR A CB  
1668 O  OG1 . THR A 207 ? 0.0810 0.1381 0.1404 -0.0042 0.0283  -0.0174 208 THR A OG1 
1669 C  CG2 . THR A 207 ? 0.0949 0.1511 0.1393 -0.0173 0.0226  0.0171  208 THR A CG2 
1670 N  N   . TRP A 208 ? 0.0723 0.1133 0.1095 0.0033  0.0254  -0.0117 209 TRP A N   
1671 C  CA  . TRP A 208 ? 0.0488 0.1100 0.1093 -0.0081 0.0314  -0.0058 209 TRP A CA  
1672 C  C   . TRP A 208 ? 0.0387 0.1146 0.1102 0.0206  0.0433  -0.0018 209 TRP A C   
1673 O  O   . TRP A 208 ? 0.0507 0.1274 0.0964 0.0021  0.0277  0.0021  209 TRP A O   
1674 C  CB  . TRP A 208 ? 0.0427 0.1454 0.0934 0.0137  0.0341  -0.0066 209 TRP A CB  
1675 C  CG  . TRP A 208 ? 0.0366 0.1259 0.1118 0.0067  0.0381  0.0003  209 TRP A CG  
1676 C  CD1 . TRP A 208 ? 0.0521 0.1359 0.1214 0.0005  0.0187  -0.0083 209 TRP A CD1 
1677 C  CD2 . TRP A 208 ? 0.0454 0.0993 0.1331 0.0005  0.0268  -0.0205 209 TRP A CD2 
1678 N  NE1 . TRP A 208 ? 0.0538 0.1289 0.1178 0.0137  0.0291  -0.0151 209 TRP A NE1 
1679 C  CE2 . TRP A 208 ? 0.0628 0.1086 0.1142 -0.0031 0.0330  -0.0099 209 TRP A CE2 
1680 C  CE3 . TRP A 208 ? 0.0781 0.1270 0.1162 -0.0043 0.0185  -0.0111 209 TRP A CE3 
1681 C  CZ2 . TRP A 208 ? 0.0759 0.1301 0.1174 0.0348  0.0223  -0.0238 209 TRP A CZ2 
1682 C  CZ3 . TRP A 208 ? 0.1023 0.1250 0.1000 -0.0143 0.0336  0.0196  209 TRP A CZ3 
1683 C  CH2 . TRP A 208 ? 0.0933 0.1097 0.1056 -0.0084 0.0257  0.0128  209 TRP A CH2 
1684 N  N   . ILE A 209 ? 0.0372 0.1138 0.1122 -0.0032 0.0373  0.0065  210 ILE A N   
1685 C  CA  . ILE A 209 ? 0.0527 0.1145 0.1108 -0.0231 0.0363  0.0053  210 ILE A CA  
1686 C  C   . ILE A 209 ? 0.0801 0.1129 0.1058 -0.0153 0.0341  -0.0041 210 ILE A C   
1687 O  O   . ILE A 209 ? 0.0851 0.1317 0.1050 -0.0116 0.0273  0.0020  210 ILE A O   
1688 C  CB  . ILE A 209 ? 0.0675 0.1084 0.1450 -0.0114 0.0367  0.0151  210 ILE A CB  
1689 C  CG1 . ILE A 209 ? 0.0696 0.1356 0.1797 0.0298  0.0228  -0.0189 210 ILE A CG1 
1690 C  CG2 . ILE A 209 ? 0.0429 0.1625 0.1528 -0.0073 0.0152  0.0077  210 ILE A CG2 
1691 C  CD1 . ILE A 209 ? 0.0653 0.1551 0.2289 0.0239  0.0240  0.0157  210 ILE A CD1 
1692 N  N   . VAL A 210 ? 0.0727 0.1156 0.1156 -0.0091 0.0245  0.0091  211 VAL A N   
1693 C  CA  . VAL A 210 ? 0.0599 0.1070 0.1126 -0.0052 0.0288  0.0173  211 VAL A CA  
1694 C  C   . VAL A 210 ? 0.0617 0.0986 0.1165 0.0021  0.0232  0.0166  211 VAL A C   
1695 O  O   . VAL A 210 ? 0.0768 0.1235 0.1059 -0.0044 0.0313  0.0125  211 VAL A O   
1696 C  CB  . VAL A 210 ? 0.0594 0.1192 0.1386 -0.0021 0.0286  0.0166  211 VAL A CB  
1697 C  CG1 . VAL A 210 ? 0.0916 0.1274 0.1253 0.0044  0.0226  0.0143  211 VAL A CG1 
1698 C  CG2 . VAL A 210 ? 0.0731 0.1214 0.1338 -0.0106 0.0427  0.0116  211 VAL A CG2 
1699 N  N   . LEU A 211 ? 0.0489 0.1359 0.1377 -0.0054 0.0074  0.0099  212 LEU A N   
1700 C  CA  . LEU A 211 ? 0.0666 0.1274 0.1413 -0.0172 0.0210  -0.0089 212 LEU A CA  
1701 C  C   . LEU A 211 ? 0.0584 0.1427 0.1428 -0.0141 0.0203  0.0255  212 LEU A C   
1702 O  O   . LEU A 211 ? 0.0539 0.1441 0.1349 -0.0176 0.0293  0.0073  212 LEU A O   
1703 C  CB  . LEU A 211 ? 0.0469 0.1449 0.1691 -0.0205 0.0059  0.0215  212 LEU A CB  
1704 C  CG  . LEU A 211 ? 0.0838 0.1443 0.1447 -0.0308 0.0082  0.0215  212 LEU A CG  
1705 C  CD1 . LEU A 211 ? 0.1036 0.2151 0.1838 -0.0144 -0.0291 0.0140  212 LEU A CD1 
1706 C  CD2 . LEU A 211 ? 0.0953 0.2031 0.1388 -0.0175 0.0335  0.0134  212 LEU A CD2 
1707 N  N   . LYS A 212 ? 0.0702 0.1664 0.1332 -0.0236 0.0196  0.0309  213 LYS A N   
1708 C  CA  . LYS A 212 ? 0.1328 0.1625 0.1151 -0.0226 0.0036  0.0340  213 LYS A CA  
1709 C  C   . LYS A 212 ? 0.0908 0.1486 0.1363 -0.0330 0.0135  0.0403  213 LYS A C   
1710 O  O   . LYS A 212 ? 0.1029 0.1551 0.1709 -0.0159 -0.0054 0.0087  213 LYS A O   
1711 C  CB  . LYS A 212 ? 0.1402 0.1762 0.1486 -0.0530 0.0346  0.0078  213 LYS A CB  
1712 C  CG  . LYS A 212 ? 0.2007 0.1876 0.1740 -0.0069 0.0141  0.0309  213 LYS A CG  
1713 C  CD  . LYS A 212 ? 0.3044 0.2377 0.1969 -0.0819 0.0636  0.0198  213 LYS A CD  
1714 C  CE  . LYS A 212 ? 0.3847 0.2631 0.2414 -0.0403 0.0392  0.0624  213 LYS A CE  
1715 N  NZ  . LYS A 212 ? 0.6888 0.5242 0.3290 -0.1896 0.1499  0.0780  213 LYS A NZ  
1716 N  N   A GLU A 213 ? 0.0707 0.1436 0.1477 -0.0183 0.0178  0.0215  214 GLU A N   
1717 N  N   B GLU A 213 ? 0.0776 0.1446 0.1456 -0.0122 0.0179  0.0254  214 GLU A N   
1718 C  CA  A GLU A 213 ? 0.0820 0.1917 0.1532 -0.0313 0.0190  0.0051  214 GLU A CA  
1719 C  CA  B GLU A 213 ? 0.0750 0.1888 0.1547 -0.0212 0.0134  0.0114  214 GLU A CA  
1720 C  C   A GLU A 213 ? 0.0847 0.1454 0.1526 -0.0385 0.0178  -0.0097 214 GLU A C   
1721 C  C   B GLU A 213 ? 0.0815 0.1463 0.1517 -0.0359 0.0114  -0.0095 214 GLU A C   
1722 O  O   A GLU A 213 ? 0.0917 0.1524 0.1650 -0.0108 0.0093  0.0089  214 GLU A O   
1723 O  O   B GLU A 213 ? 0.0818 0.1525 0.1490 -0.0129 0.0061  0.0044  214 GLU A O   
1724 C  CB  A GLU A 213 ? 0.0740 0.1856 0.1535 -0.0392 0.0304  0.0133  214 GLU A CB  
1725 C  CB  B GLU A 213 ? 0.0914 0.1766 0.1762 -0.0042 -0.0093 0.0282  214 GLU A CB  
1726 C  CG  A GLU A 213 ? 0.1254 0.1664 0.1941 -0.0456 -0.0003 0.0195  214 GLU A CG  
1727 C  CG  B GLU A 213 ? 0.0919 0.1849 0.2225 -0.0133 -0.0171 0.0159  214 GLU A CG  
1728 C  CD  A GLU A 213 ? 0.1267 0.1359 0.1878 -0.0527 0.0171  -0.0336 214 GLU A CD  
1729 C  CD  B GLU A 213 ? 0.0895 0.1532 0.2536 -0.0357 -0.0013 0.0457  214 GLU A CD  
1730 O  OE1 A GLU A 213 ? 0.2085 0.2247 0.2025 -0.0978 -0.0142 -0.0179 214 GLU A OE1 
1731 O  OE1 B GLU A 213 ? 0.0962 0.1998 0.1734 -0.0122 -0.0013 0.0044  214 GLU A OE1 
1732 O  OE2 A GLU A 213 ? 0.0980 0.1873 0.1874 -0.0563 0.0337  -0.0212 214 GLU A OE2 
1733 O  OE2 B GLU A 213 ? 0.1407 0.1696 0.3375 -0.0317 -0.0337 -0.0105 214 GLU A OE2 
1734 N  N   . PRO A 214 ? 0.1115 0.1364 0.1447 -0.0223 0.0190  0.0061  215 PRO A N   
1735 C  CA  . PRO A 214 ? 0.0648 0.1623 0.1405 -0.0124 0.0192  0.0040  215 PRO A CA  
1736 C  C   . PRO A 214 ? 0.1086 0.1428 0.1575 -0.0248 0.0053  -0.0011 215 PRO A C   
1737 O  O   . PRO A 214 ? 0.1226 0.1948 0.1777 -0.0570 -0.0003 0.0055  215 PRO A O   
1738 C  CB  . PRO A 214 ? 0.1262 0.1350 0.1617 -0.0046 0.0055  0.0215  215 PRO A CB  
1739 C  CG  . PRO A 214 ? 0.1740 0.1977 0.2296 0.0252  0.1154  0.0215  215 PRO A CG  
1740 C  CD  . PRO A 214 ? 0.1658 0.1327 0.1860 -0.0305 0.0644  0.0043  215 PRO A CD  
1741 N  N   . ILE A 215 ? 0.1127 0.1429 0.1391 -0.0086 0.0037  0.0050  216 ILE A N   
1742 C  CA  . ILE A 215 ? 0.1368 0.1504 0.1579 0.0065  -0.0077 -0.0143 216 ILE A CA  
1743 C  C   . ILE A 215 ? 0.1059 0.1549 0.1686 -0.0027 0.0168  -0.0051 216 ILE A C   
1744 O  O   . ILE A 215 ? 0.1181 0.1490 0.1831 -0.0092 -0.0041 0.0031  216 ILE A O   
1745 C  CB  . ILE A 215 ? 0.1215 0.1385 0.1770 0.0005  0.0096  -0.0046 216 ILE A CB  
1746 C  CG1 . ILE A 215 ? 0.1338 0.1626 0.1708 -0.0081 0.0183  0.0189  216 ILE A CG1 
1747 C  CG2 . ILE A 215 ? 0.1549 0.1363 0.2086 0.0413  0.0109  -0.0047 216 ILE A CG2 
1748 C  CD1 . ILE A 215 ? 0.1878 0.1543 0.1690 -0.0174 -0.0100 0.0140  216 ILE A CD1 
1749 N  N   A SER A 216 ? 0.1174 0.1507 0.1923 0.0047  0.0041  -0.0259 217 SER A N   
1750 N  N   B SER A 216 ? 0.1132 0.1482 0.1808 0.0111  0.0058  -0.0275 217 SER A N   
1751 C  CA  A SER A 216 ? 0.1174 0.1429 0.1937 -0.0006 0.0085  -0.0136 217 SER A CA  
1752 C  CA  B SER A 216 ? 0.1132 0.1493 0.1708 -0.0018 0.0044  -0.0227 217 SER A CA  
1753 C  C   A SER A 216 ? 0.1059 0.1604 0.1903 -0.0048 -0.0016 -0.0141 217 SER A C   
1754 C  C   B SER A 216 ? 0.1167 0.1553 0.1493 -0.0039 -0.0198 -0.0395 217 SER A C   
1755 O  O   A SER A 216 ? 0.1077 0.1974 0.2104 -0.0198 -0.0162 0.0042  217 SER A O   
1756 O  O   B SER A 216 ? 0.1529 0.1658 0.1802 0.0059  -0.0240 -0.0342 217 SER A O   
1757 C  CB  A SER A 216 ? 0.2117 0.1723 0.2043 -0.0457 0.0836  0.0343  217 SER A CB  
1758 C  CB  B SER A 216 ? 0.1841 0.1359 0.1362 -0.0346 0.0447  -0.0319 217 SER A CB  
1759 O  OG  A SER A 216 ? 0.3522 0.2441 0.1977 -0.0590 0.0312  -0.0119 217 SER A OG  
1760 O  OG  B SER A 216 ? 0.1378 0.2501 0.1576 -0.0559 -0.0005 0.0158  217 SER A OG  
1761 N  N   . VAL A 217 ? 0.1168 0.1407 0.1518 -0.0225 0.0071  -0.0280 218 VAL A N   
1762 C  CA  . VAL A 217 ? 0.1367 0.1286 0.1648 0.0025  0.0064  -0.0070 218 VAL A CA  
1763 C  C   . VAL A 217 ? 0.1386 0.1564 0.1515 -0.0087 -0.0122 -0.0255 218 VAL A C   
1764 O  O   . VAL A 217 ? 0.1636 0.1619 0.1529 -0.0490 -0.0240 -0.0041 218 VAL A O   
1765 C  CB  . VAL A 217 ? 0.1306 0.1386 0.2052 -0.0157 -0.0104 -0.0240 218 VAL A CB  
1766 C  CG1 . VAL A 217 ? 0.1650 0.1452 0.1924 0.0168  -0.0070 -0.0221 218 VAL A CG1 
1767 C  CG2 . VAL A 217 ? 0.1201 0.1251 0.2380 -0.0245 -0.0118 -0.0141 218 VAL A CG2 
1768 N  N   . SER A 218 ? 0.1669 0.1607 0.1547 -0.0181 -0.0139 -0.0397 219 SER A N   
1769 C  CA  . SER A 218 ? 0.1729 0.1575 0.1869 0.0017  -0.0113 -0.0472 219 SER A CA  
1770 C  C   . SER A 218 ? 0.1635 0.1452 0.1826 -0.0188 -0.0242 -0.0326 219 SER A C   
1771 O  O   . SER A 218 ? 0.1564 0.1474 0.1876 -0.0225 0.0068  -0.0366 219 SER A O   
1772 C  CB  . SER A 218 ? 0.1964 0.1391 0.1708 -0.0175 -0.0050 -0.0205 219 SER A CB  
1773 O  OG  . SER A 218 ? 0.2179 0.1971 0.1729 -0.0636 -0.0138 -0.0064 219 SER A OG  
1774 N  N   A SER A 219 ? 0.2080 0.1438 0.1802 -0.0131 0.0012  -0.0380 220 SER A N   
1775 N  N   B SER A 219 ? 0.1956 0.1464 0.1802 -0.0107 0.0034  -0.0380 220 SER A N   
1776 C  CA  A SER A 219 ? 0.2354 0.1623 0.2240 0.0239  -0.0091 -0.0295 220 SER A CA  
1777 C  CA  B SER A 219 ? 0.2239 0.1689 0.2190 0.0314  -0.0067 -0.0295 220 SER A CA  
1778 C  C   A SER A 219 ? 0.2208 0.1474 0.2386 -0.0245 0.0107  -0.0460 220 SER A C   
1779 C  C   B SER A 219 ? 0.2125 0.1481 0.2389 -0.0208 0.0150  -0.0445 220 SER A C   
1780 O  O   A SER A 219 ? 0.2177 0.1371 0.2700 -0.0243 0.0162  -0.0165 220 SER A O   
1781 O  O   B SER A 219 ? 0.2118 0.1386 0.2722 -0.0236 0.0189  -0.0179 220 SER A O   
1782 C  CB  A SER A 219 ? 0.2752 0.1454 0.3011 -0.0288 0.0036  -0.0265 220 SER A CB  
1783 C  CB  B SER A 219 ? 0.1974 0.1594 0.2935 0.0160  0.0183  -0.0369 220 SER A CB  
1784 O  OG  A SER A 219 ? 0.2239 0.1418 0.2674 0.0168  0.0163  -0.0147 220 SER A OG  
1785 O  OG  B SER A 219 ? 0.1835 0.1781 0.2619 0.0030  0.0320  0.0032  220 SER A OG  
1786 N  N   . GLU A 220 ? 0.1973 0.1705 0.1860 -0.0230 0.0420  -0.0329 221 GLU A N   
1787 C  CA  . GLU A 220 ? 0.2620 0.1756 0.1863 -0.0305 0.0122  -0.0005 221 GLU A CA  
1788 C  C   . GLU A 220 ? 0.2459 0.1888 0.1493 -0.0332 0.0226  -0.0038 221 GLU A C   
1789 O  O   . GLU A 220 ? 0.2222 0.2068 0.1992 -0.0216 0.0482  -0.0216 221 GLU A O   
1790 C  CB  . GLU A 220 ? 0.2797 0.1923 0.1887 -0.0553 0.0178  -0.0234 221 GLU A CB  
1791 C  CG  . GLU A 220 ? 0.5388 0.2580 0.2269 -0.1271 -0.0029 -0.0771 221 GLU A CG  
1792 C  CD  . GLU A 220 ? 0.4656 0.3442 0.3532 -0.1518 0.0882  -0.1488 221 GLU A CD  
1793 O  OE1 . GLU A 220 ? 0.4126 0.2386 0.2900 -0.1088 0.0340  -0.1112 221 GLU A OE1 
1794 O  OE2 . GLU A 220 ? 0.5602 0.4942 0.5299 -0.2861 0.1600  -0.2728 221 GLU A OE2 
1795 N  N   . GLN A 221 ? 0.1715 0.1639 0.1748 -0.0083 -0.0067 -0.0103 222 GLN A N   
1796 C  CA  . GLN A 221 ? 0.1544 0.1720 0.1820 -0.0278 0.0307  -0.0054 222 GLN A CA  
1797 C  C   . GLN A 221 ? 0.1576 0.1797 0.1817 -0.0094 0.0140  0.0004  222 GLN A C   
1798 O  O   . GLN A 221 ? 0.1869 0.1690 0.1697 -0.0197 0.0234  -0.0013 222 GLN A O   
1799 C  CB  . GLN A 221 ? 0.1813 0.2129 0.1553 -0.0242 0.0055  -0.0401 222 GLN A CB  
1800 C  CG  . GLN A 221 ? 0.1773 0.1835 0.1326 -0.0239 0.0121  0.0069  222 GLN A CG  
1801 C  CD  . GLN A 221 ? 0.1993 0.1605 0.1526 -0.0074 0.0209  -0.0022 222 GLN A CD  
1802 O  OE1 . GLN A 221 ? 0.1388 0.1874 0.1551 0.0070  0.0093  0.0024  222 GLN A OE1 
1803 N  NE2 . GLN A 221 ? 0.1439 0.2007 0.1841 -0.0396 -0.0108 0.0037  222 GLN A NE2 
1804 N  N   . VAL A 222 ? 0.1763 0.1615 0.1938 -0.0035 0.0011  -0.0057 223 VAL A N   
1805 C  CA  . VAL A 222 ? 0.1811 0.1831 0.1633 -0.0120 0.0166  0.0034  223 VAL A CA  
1806 C  C   . VAL A 222 ? 0.2118 0.1784 0.2124 -0.0232 0.0390  -0.0245 223 VAL A C   
1807 O  O   . VAL A 222 ? 0.2099 0.1687 0.1816 -0.0226 0.0365  0.0151  223 VAL A O   
1808 C  CB  . VAL A 222 ? 0.2556 0.2122 0.2011 -0.0198 -0.0471 0.0478  223 VAL A CB  
1809 C  CG1 . VAL A 222 ? 0.2673 0.2213 0.2712 -0.0546 -0.0111 0.0066  223 VAL A CG1 
1810 C  CG2 . VAL A 222 ? 0.2605 0.2280 0.2812 -0.0416 -0.0425 -0.0048 223 VAL A CG2 
1811 N  N   . LEU A 223 ? 0.1914 0.1898 0.1844 0.0145  0.0199  -0.0126 224 LEU A N   
1812 C  CA  . LEU A 223 ? 0.2433 0.1621 0.2438 -0.0063 0.0790  -0.0322 224 LEU A CA  
1813 C  C   . LEU A 223 ? 0.2467 0.2296 0.2013 -0.0172 0.0476  -0.0138 224 LEU A C   
1814 O  O   . LEU A 223 ? 0.2056 0.2124 0.2319 -0.0061 0.0604  -0.0200 224 LEU A O   
1815 C  CB  . LEU A 223 ? 0.3402 0.1985 0.3175 -0.0584 0.0749  -0.0717 224 LEU A CB  
1816 C  CG  . LEU A 223 ? 0.3050 0.2237 0.4975 0.0314  -0.0114 -0.0823 224 LEU A CG  
1817 C  CD1 . LEU A 223 ? 0.2713 0.4275 0.5323 -0.0784 -0.0025 -0.1430 224 LEU A CD1 
1818 C  CD2 . LEU A 223 ? 0.2336 0.3098 0.6661 0.0258  0.1274  -0.1584 224 LEU A CD2 
1819 N  N   . LYS A 224 ? 0.2072 0.2262 0.1718 -0.0278 0.0122  -0.0279 225 LYS A N   
1820 C  CA  . LYS A 224 ? 0.2068 0.2644 0.1716 -0.0308 0.0081  -0.0147 225 LYS A CA  
1821 C  C   . LYS A 224 ? 0.1574 0.2416 0.1421 -0.0153 0.0158  0.0055  225 LYS A C   
1822 O  O   . LYS A 224 ? 0.2050 0.2210 0.1339 -0.0111 0.0330  -0.0006 225 LYS A O   
1823 C  CB  . LYS A 224 ? 0.2935 0.3222 0.1841 0.0282  -0.0392 -0.0031 225 LYS A CB  
1824 C  CG  . LYS A 224 ? 0.3252 0.5143 0.1955 -0.0637 -0.0544 -0.0592 225 LYS A CG  
1825 C  CD  . LYS A 224 ? 0.3697 0.7336 0.4949 -0.0663 -0.1740 -0.1838 225 LYS A CD  
1826 C  CE  . LYS A 224 ? 0.4949 1.0414 0.6102 -0.1365 -0.2392 -0.3407 225 LYS A CE  
1827 N  NZ  . LYS A 224 ? 0.2845 0.4840 0.5721 0.0622  0.0398  -0.2241 225 LYS A NZ  
1828 N  N   . PHE A 225 ? 0.1676 0.1919 0.1353 -0.0013 0.0347  -0.0114 226 PHE A N   
1829 C  CA  . PHE A 225 ? 0.1658 0.1578 0.1510 -0.0068 0.0567  0.0081  226 PHE A CA  
1830 C  C   . PHE A 225 ? 0.1885 0.1511 0.1311 0.0035  0.0590  -0.0027 226 PHE A C   
1831 O  O   . PHE A 225 ? 0.1867 0.1377 0.1423 -0.0111 0.0574  -0.0086 226 PHE A O   
1832 C  CB  . PHE A 225 ? 0.2057 0.1762 0.1490 0.0036  0.0697  -0.0116 226 PHE A CB  
1833 C  CG  . PHE A 225 ? 0.1629 0.1478 0.1811 -0.0335 0.0469  -0.0231 226 PHE A CG  
1834 C  CD1 . PHE A 225 ? 0.2401 0.2761 0.1795 0.0871  0.0353  -0.0122 226 PHE A CD1 
1835 C  CD2 . PHE A 225 ? 0.1815 0.3037 0.2772 0.0151  -0.0179 -0.1767 226 PHE A CD2 
1836 C  CE1 . PHE A 225 ? 0.2199 0.1981 0.2103 0.0322  0.0554  -0.0075 226 PHE A CE1 
1837 C  CE2 . PHE A 225 ? 0.1447 0.3380 0.3129 0.0282  0.0013  -0.1629 226 PHE A CE2 
1838 C  CZ  . PHE A 225 ? 0.1560 0.1993 0.2318 -0.0562 0.0179  -0.0298 226 PHE A CZ  
1839 N  N   . ARG A 226 ? 0.1953 0.1478 0.1421 0.0082  0.0504  0.0059  227 ARG A N   
1840 C  CA  . ARG A 226 ? 0.1562 0.1528 0.1587 -0.0113 0.0486  0.0102  227 ARG A CA  
1841 C  C   . ARG A 226 ? 0.2139 0.1547 0.1702 -0.0137 0.0513  0.0121  227 ARG A C   
1842 O  O   . ARG A 226 ? 0.2036 0.1790 0.1673 -0.0193 0.0507  -0.0021 227 ARG A O   
1843 C  CB  . ARG A 226 ? 0.1680 0.1472 0.1628 0.0211  0.0525  0.0258  227 ARG A CB  
1844 C  CG  . ARG A 226 ? 0.1860 0.1632 0.1338 -0.0102 0.0295  0.0284  227 ARG A CG  
1845 C  CD  . ARG A 226 ? 0.2622 0.1507 0.1852 -0.0331 0.0555  0.0047  227 ARG A CD  
1846 N  NE  . ARG A 226 ? 0.2416 0.1377 0.1629 -0.0518 0.0170  0.0089  227 ARG A NE  
1847 C  CZ  . ARG A 226 ? 0.2129 0.1542 0.1580 -0.0408 0.0212  -0.0127 227 ARG A CZ  
1848 N  NH1 . ARG A 226 ? 0.2634 0.1709 0.2222 -0.0630 -0.0187 -0.0270 227 ARG A NH1 
1849 N  NH2 . ARG A 226 ? 0.2070 0.1716 0.1769 -0.0595 0.0640  0.0088  227 ARG A NH2 
1850 N  N   . LYS A 227 ? 0.1957 0.1368 0.1404 -0.0210 0.0366  -0.0242 228 LYS A N   
1851 C  CA  . LYS A 227 ? 0.2414 0.1781 0.1318 -0.0635 0.0479  -0.0427 228 LYS A CA  
1852 C  C   . LYS A 227 ? 0.2125 0.1750 0.1203 -0.0230 0.0430  -0.0160 228 LYS A C   
1853 O  O   . LYS A 227 ? 0.2592 0.1967 0.1174 -0.0392 0.0493  -0.0190 228 LYS A O   
1854 C  CB  . LYS A 227 ? 0.2605 0.1930 0.1507 -0.0402 0.0282  -0.0208 228 LYS A CB  
1855 C  CG  . LYS A 227 ? 0.3112 0.2600 0.2566 -0.1235 0.0231  -0.0399 228 LYS A CG  
1856 C  CD  . LYS A 227 ? 0.3419 0.5577 0.4536 -0.1365 -0.0634 -0.2277 228 LYS A CD  
1857 C  CE  . LYS A 227 ? 0.5107 0.5424 0.6865 -0.0531 -0.0699 -0.4034 228 LYS A CE  
1858 N  NZ  . LYS A 227 ? 0.8726 1.1956 0.5638 -0.3854 -0.0998 -0.3622 228 LYS A NZ  
1859 N  N   . LEU A 228 ? 0.1752 0.1511 0.1389 -0.0237 0.0563  -0.0226 229 LEU A N   
1860 C  CA  . LEU A 228 ? 0.1971 0.1508 0.1508 -0.0184 0.0372  -0.0148 229 LEU A CA  
1861 C  C   . LEU A 228 ? 0.2181 0.1644 0.1111 -0.0289 0.0588  -0.0172 229 LEU A C   
1862 O  O   . LEU A 228 ? 0.2258 0.1443 0.1206 -0.0037 0.0677  -0.0201 229 LEU A O   
1863 C  CB  . LEU A 228 ? 0.2107 0.1438 0.1305 -0.0385 0.0566  -0.0038 229 LEU A CB  
1864 C  CG  . LEU A 228 ? 0.2014 0.1960 0.1307 -0.0260 0.0532  0.0094  229 LEU A CG  
1865 C  CD1 . LEU A 228 ? 0.2183 0.1799 0.1332 -0.0447 0.0362  -0.0280 229 LEU A CD1 
1866 C  CD2 . LEU A 228 ? 0.2194 0.2049 0.1608 0.0023  0.0421  0.0289  229 LEU A CD2 
1867 N  N   . ASN A 229 ? 0.2122 0.1788 0.1271 -0.0522 0.0672  -0.0173 230 ASN A N   
1868 C  CA  . ASN A 229 ? 0.1892 0.2089 0.1050 -0.0309 0.0506  -0.0151 230 ASN A CA  
1869 C  C   . ASN A 229 ? 0.1995 0.1860 0.1124 -0.0233 0.0701  -0.0027 230 ASN A C   
1870 O  O   . ASN A 229 ? 0.1801 0.1812 0.1404 -0.0234 0.0600  -0.0018 230 ASN A O   
1871 C  CB  . ASN A 229 ? 0.2764 0.1942 0.1041 -0.0238 0.0780  -0.0201 230 ASN A CB  
1872 C  CG  . ASN A 229 ? 0.2431 0.2115 0.1317 -0.0234 0.0820  -0.0355 230 ASN A CG  
1873 O  OD1 . ASN A 229 ? 0.3316 0.2046 0.1436 -0.0518 0.0995  -0.0330 230 ASN A OD1 
1874 N  ND2 . ASN A 229 ? 0.2699 0.1773 0.1235 -0.0103 0.0458  -0.0065 230 ASN A ND2 
1875 N  N   . PHE A 230 ? 0.1428 0.2111 0.1323 -0.0573 0.0722  -0.0151 231 PHE A N   
1876 C  CA  . PHE A 230 ? 0.1723 0.1964 0.1673 -0.0666 0.0539  0.0173  231 PHE A CA  
1877 C  C   . PHE A 230 ? 0.2347 0.1669 0.1626 -0.0304 0.0872  0.0137  231 PHE A C   
1878 O  O   . PHE A 230 ? 0.2355 0.1859 0.1730 -0.0873 0.0710  0.0143  231 PHE A O   
1879 C  CB  . PHE A 230 ? 0.1963 0.1999 0.1377 -0.0529 0.0739  0.0015  231 PHE A CB  
1880 C  CG  . PHE A 230 ? 0.1953 0.1777 0.1368 -0.0617 0.0891  -0.0215 231 PHE A CG  
1881 C  CD1 . PHE A 230 ? 0.2039 0.1895 0.1413 -0.0216 0.0774  -0.0043 231 PHE A CD1 
1882 C  CD2 . PHE A 230 ? 0.1741 0.1865 0.1449 -0.0467 0.0850  -0.0197 231 PHE A CD2 
1883 C  CE1 . PHE A 230 ? 0.1867 0.1723 0.1364 -0.0436 0.0589  0.0025  231 PHE A CE1 
1884 C  CE2 . PHE A 230 ? 0.2061 0.1641 0.1289 -0.0278 0.0449  0.0044  231 PHE A CE2 
1885 C  CZ  . PHE A 230 ? 0.1395 0.2030 0.1368 -0.0464 0.0462  -0.0044 231 PHE A CZ  
1886 N  N   . ASN A 231 ? 0.2321 0.2246 0.1373 -0.0207 0.1090  0.0083  232 ASN A N   
1887 C  CA  . ASN A 231 ? 0.1902 0.1729 0.2030 -0.0500 0.1130  -0.0179 232 ASN A CA  
1888 C  C   . ASN A 231 ? 0.2114 0.2466 0.1676 -0.0307 0.1174  -0.0120 232 ASN A C   
1889 O  O   . ASN A 231 ? 0.2431 0.1982 0.1628 -0.0018 0.0864  -0.0108 232 ASN A O   
1890 C  CB  . ASN A 231 ? 0.2207 0.2157 0.2071 -0.0234 0.1221  -0.0421 232 ASN A CB  
1891 C  CG  . ASN A 231 ? 0.2488 0.1811 0.1921 -0.0319 0.1216  -0.0133 232 ASN A CG  
1892 O  OD1 . ASN A 231 ? 0.2827 0.1870 0.2032 -0.0414 0.1432  -0.0110 232 ASN A OD1 
1893 N  ND2 . ASN A 231 ? 0.3716 0.2250 0.1788 -0.0316 0.0990  -0.0424 232 ASN A ND2 
1894 N  N   . GLY A 232 ? 0.2617 0.2231 0.1795 -0.0092 0.1379  -0.0002 233 GLY A N   
1895 C  CA  . GLY A 232 ? 0.2721 0.2132 0.1982 -0.0141 0.1366  -0.0063 233 GLY A CA  
1896 C  C   . GLY A 232 ? 0.2221 0.2018 0.1817 -0.0009 0.0700  0.0065  233 GLY A C   
1897 O  O   . GLY A 232 ? 0.2487 0.2384 0.2197 0.0310  0.1253  0.0179  233 GLY A O   
1898 N  N   . GLU A 233 ? 0.2271 0.2456 0.1714 -0.0549 0.0700  0.0267  234 GLU A N   
1899 C  CA  . GLU A 233 ? 0.2965 0.2570 0.1806 0.0153  0.0508  -0.0157 234 GLU A CA  
1900 C  C   . GLU A 233 ? 0.3177 0.2470 0.2262 0.0384  0.0692  -0.0053 234 GLU A C   
1901 O  O   . GLU A 233 ? 0.3515 0.2899 0.1887 -0.0387 0.1506  -0.0083 234 GLU A O   
1902 C  CB  . GLU A 233 ? 0.2982 0.2697 0.1808 -0.0173 0.0615  0.0429  234 GLU A CB  
1903 C  CG  . GLU A 233 ? 0.2613 0.2519 0.2082 -0.0700 0.0575  0.0229  234 GLU A CG  
1904 C  CD  . GLU A 233 ? 0.4900 0.3910 0.2517 0.1302  -0.0379 -0.0929 234 GLU A CD  
1905 O  OE1 . GLU A 233 ? 0.4767 0.3220 0.2311 -0.0223 0.0433  -0.0105 234 GLU A OE1 
1906 O  OE2 . GLU A 233 ? 0.3609 0.4323 0.2328 -0.0468 -0.0025 -0.0619 234 GLU A OE2 
1907 N  N   . GLY A 234 ? 0.3905 0.2970 0.2229 0.0666  0.1183  -0.0348 235 GLY A N   
1908 C  CA  . GLY A 234 ? 0.4382 0.4545 0.2563 0.2379  0.0434  -0.0820 235 GLY A CA  
1909 C  C   . GLY A 234 ? 0.4896 0.7128 0.2034 0.1657  0.0428  0.1256  235 GLY A C   
1910 O  O   . GLY A 234 ? 0.6170 0.9358 0.2768 0.2213  0.1914  -0.0035 235 GLY A O   
1911 N  N   . GLU A 235 ? 0.2991 0.2462 0.2246 0.0268  0.0847  -0.0010 236 GLU A N   
1912 C  CA  . GLU A 235 ? 0.2436 0.2046 0.2353 0.0519  0.0598  -0.0251 236 GLU A CA  
1913 C  C   . GLU A 235 ? 0.3047 0.2676 0.2735 0.0168  0.1635  0.0021  236 GLU A C   
1914 O  O   . GLU A 235 ? 0.3523 0.2910 0.2853 0.0179  0.1771  0.0318  236 GLU A O   
1915 C  CB  . GLU A 235 ? 0.3192 0.2052 0.2712 0.0208  0.0851  -0.0195 236 GLU A CB  
1916 C  CG  . GLU A 235 ? 0.3005 0.2021 0.3868 0.0055  0.1491  0.0021  236 GLU A CG  
1917 C  CD  . GLU A 235 ? 0.5475 0.3071 0.4219 -0.1539 0.2669  -0.0312 236 GLU A CD  
1918 O  OE1 . GLU A 235 ? 0.2912 0.2726 0.4276 -0.0815 0.1964  -0.0174 236 GLU A OE1 
1919 O  OE2 . GLU A 235 ? 0.6563 0.3719 0.5457 -0.2649 0.2208  -0.0383 236 GLU A OE2 
1920 N  N   . PRO A 236 ? 0.2319 0.2757 0.3768 -0.0073 0.1672  0.0589  237 PRO A N   
1921 C  CA  . PRO A 236 ? 0.3070 0.2557 0.3582 -0.0266 0.2609  -0.0107 237 PRO A CA  
1922 C  C   . PRO A 236 ? 0.3007 0.2669 0.2297 -0.0881 0.1947  -0.0425 237 PRO A C   
1923 O  O   . PRO A 236 ? 0.2938 0.2255 0.2136 -0.0304 0.1502  -0.0331 237 PRO A O   
1924 C  CB  . PRO A 236 ? 0.3069 0.2757 0.4679 0.0066  0.2929  0.0289  237 PRO A CB  
1925 C  CG  . PRO A 236 ? 0.3730 0.2953 0.5965 0.0135  0.2366  0.2181  237 PRO A CG  
1926 C  CD  . PRO A 236 ? 0.2086 0.2827 0.4194 -0.0168 0.1482  0.0785  237 PRO A CD  
1927 N  N   . GLU A 237 ? 0.2634 0.1793 0.2495 -0.0190 0.1350  -0.0132 238 GLU A N   
1928 C  CA  . GLU A 237 ? 0.3073 0.2690 0.1539 -0.0514 0.1649  -0.0165 238 GLU A CA  
1929 C  C   . GLU A 237 ? 0.2258 0.2120 0.2057 -0.0124 0.1173  -0.0162 238 GLU A C   
1930 O  O   . GLU A 237 ? 0.2584 0.2371 0.2023 0.0193  0.0894  -0.0303 238 GLU A O   
1931 C  CB  . GLU A 237 ? 0.2547 0.1691 0.2521 0.0469  0.0729  -0.0413 238 GLU A CB  
1932 C  CG  . GLU A 237 ? 0.2609 0.2684 0.2473 -0.0436 0.0608  -0.0819 238 GLU A CG  
1933 C  CD  . GLU A 237 ? 0.2651 0.2646 0.2535 -0.0061 0.0412  -0.0660 238 GLU A CD  
1934 O  OE1 . GLU A 237 ? 0.3604 0.4079 0.4781 0.1012  -0.0402 -0.2398 238 GLU A OE1 
1935 O  OE2 . GLU A 237 ? 0.2714 0.2161 0.1784 0.0013  0.0410  -0.0478 238 GLU A OE2 
1936 N  N   . GLU A 238 ? 0.2276 0.2120 0.1586 -0.0573 0.1106  -0.0414 239 GLU A N   
1937 C  CA  . GLU A 238 ? 0.2168 0.2943 0.1636 -0.0497 0.1062  -0.0564 239 GLU A CA  
1938 C  C   . GLU A 238 ? 0.2074 0.1975 0.1298 -0.0326 0.0993  -0.0333 239 GLU A C   
1939 O  O   . GLU A 238 ? 0.2665 0.1722 0.1816 -0.0201 0.0881  -0.0239 239 GLU A O   
1940 C  CB  . GLU A 238 ? 0.2057 0.3352 0.2350 -0.1005 0.0833  -0.0435 239 GLU A CB  
1941 C  CG  . GLU A 238 ? 0.2265 0.5210 0.6585 0.1745  0.1137  -0.0913 239 GLU A CG  
1942 C  CD  . GLU A 238 ? 0.4415 0.9596 0.6879 -0.0059 0.3368  -0.0710 239 GLU A CD  
1943 O  OE1 . GLU A 238 ? 1.4974 1.2614 0.6961 -0.0880 -0.0182 -0.1579 239 GLU A OE1 
1944 O  OE2 . GLU A 238 ? 0.7145 1.1788 0.4045 0.0875  0.0117  -0.3439 239 GLU A OE2 
1945 N  N   . LEU A 239 ? 0.1964 0.1960 0.1439 -0.0179 0.0708  -0.0027 240 LEU A N   
1946 C  CA  . LEU A 239 ? 0.1748 0.2091 0.1404 -0.0598 0.0863  -0.0269 240 LEU A CA  
1947 C  C   . LEU A 239 ? 0.1459 0.1352 0.1321 -0.0051 0.0771  0.0122  240 LEU A C   
1948 O  O   . LEU A 239 ? 0.1585 0.1860 0.1371 -0.0276 0.0723  -0.0032 240 LEU A O   
1949 C  CB  . LEU A 239 ? 0.1985 0.1607 0.1662 0.0023  0.0441  -0.0082 240 LEU A CB  
1950 C  CG  . LEU A 239 ? 0.1964 0.1981 0.2016 0.0048  0.0237  -0.0507 240 LEU A CG  
1951 C  CD1 . LEU A 239 ? 0.2075 0.1411 0.3628 0.0460  0.0113  -0.0508 240 LEU A CD1 
1952 C  CD2 . LEU A 239 ? 0.1694 0.2043 0.1740 0.0229  0.0633  -0.0668 240 LEU A CD2 
1953 N  N   . MET A 240 ? 0.1569 0.1416 0.1517 0.0035  0.0922  -0.0073 241 MET A N   
1954 C  CA  . MET A 240 ? 0.1780 0.1669 0.1133 -0.0145 0.0903  -0.0025 241 MET A CA  
1955 C  C   . MET A 240 ? 0.1362 0.1632 0.1108 -0.0488 0.0525  -0.0172 241 MET A C   
1956 O  O   . MET A 240 ? 0.1327 0.1847 0.1323 -0.0339 0.0519  -0.0079 241 MET A O   
1957 C  CB  . MET A 240 ? 0.1838 0.1608 0.1260 -0.0093 0.0599  -0.0111 241 MET A CB  
1958 C  CG  . MET A 240 ? 0.1251 0.2014 0.1286 -0.0016 0.0695  -0.0275 241 MET A CG  
1959 S  SD  . MET A 240 ? 0.1842 0.1571 0.1489 -0.0189 0.0670  0.0018  241 MET A SD  
1960 C  CE  . MET A 240 ? 0.2358 0.1544 0.1314 -0.0605 0.0672  0.0129  241 MET A CE  
1961 N  N   . VAL A 241 ? 0.1551 0.1544 0.1239 -0.0216 0.0631  0.0013  242 VAL A N   
1962 C  CA  . VAL A 241 ? 0.1558 0.1341 0.1302 -0.0159 0.0595  -0.0096 242 VAL A CA  
1963 C  C   . VAL A 241 ? 0.1268 0.1303 0.1349 0.0012  0.0593  -0.0130 242 VAL A C   
1964 O  O   . VAL A 241 ? 0.1303 0.1508 0.1280 -0.0301 0.0661  -0.0223 242 VAL A O   
1965 C  CB  . VAL A 241 ? 0.1596 0.1302 0.1632 -0.0051 0.0257  -0.0083 242 VAL A CB  
1966 C  CG1 . VAL A 241 ? 0.1599 0.1483 0.1413 -0.0351 0.0348  -0.0229 242 VAL A CG1 
1967 C  CG2 . VAL A 241 ? 0.1835 0.1414 0.1569 0.0193  0.0306  -0.0099 242 VAL A CG2 
1968 N  N   . ASP A 242 ? 0.1306 0.1332 0.1161 0.0004  0.0572  -0.0026 243 ASP A N   
1969 C  CA  . ASP A 242 ? 0.1068 0.1131 0.1485 0.0064  0.0405  0.0013  243 ASP A CA  
1970 C  C   . ASP A 242 ? 0.1111 0.1353 0.1165 -0.0124 0.0434  -0.0087 243 ASP A C   
1971 O  O   . ASP A 242 ? 0.0926 0.1533 0.1463 -0.0026 0.0395  -0.0220 243 ASP A O   
1972 C  CB  . ASP A 242 ? 0.0879 0.1414 0.1502 -0.0022 0.0449  0.0006  243 ASP A CB  
1973 C  CG  . ASP A 242 ? 0.1280 0.1296 0.1385 0.0142  0.0629  0.0075  243 ASP A CG  
1974 O  OD1 . ASP A 242 ? 0.1219 0.1429 0.1479 0.0023  0.0539  0.0064  243 ASP A OD1 
1975 O  OD2 . ASP A 242 ? 0.1344 0.1483 0.1804 0.0155  0.0684  -0.0182 243 ASP A OD2 
1976 N  N   . ASN A 243 ? 0.1169 0.1208 0.1092 -0.0037 0.0545  0.0006  244 ASN A N   
1977 C  CA  . ASN A 243 ? 0.1305 0.1235 0.1106 -0.0122 0.0300  -0.0121 244 ASN A CA  
1978 C  C   . ASN A 243 ? 0.0736 0.1217 0.1267 -0.0055 0.0292  -0.0140 244 ASN A C   
1979 O  O   . ASN A 243 ? 0.1146 0.1297 0.1116 0.0140  0.0440  -0.0037 244 ASN A O   
1980 C  CB  . ASN A 243 ? 0.0985 0.1635 0.1161 -0.0055 0.0422  -0.0043 244 ASN A CB  
1981 C  CG  . ASN A 243 ? 0.1089 0.1599 0.1285 -0.0320 0.0406  -0.0001 244 ASN A CG  
1982 O  OD1 . ASN A 243 ? 0.1009 0.1402 0.1377 -0.0082 0.0381  0.0060  244 ASN A OD1 
1983 N  ND2 . ASN A 243 ? 0.1601 0.1831 0.2290 -0.0377 0.0117  0.0609  244 ASN A ND2 
1984 N  N   . TRP A 244 ? 0.1261 0.1225 0.1102 -0.0086 0.0436  -0.0027 245 TRP A N   
1985 C  CA  . TRP A 244 ? 0.0743 0.1393 0.1154 -0.0072 0.0354  -0.0253 245 TRP A CA  
1986 C  C   . TRP A 244 ? 0.0752 0.1421 0.1032 -0.0016 0.0431  0.0036  245 TRP A C   
1987 O  O   . TRP A 244 ? 0.0921 0.1386 0.1410 0.0100  0.0438  -0.0143 245 TRP A O   
1988 C  CB  . TRP A 244 ? 0.0853 0.1177 0.1320 0.0057  0.0515  -0.0186 245 TRP A CB  
1989 C  CG  . TRP A 244 ? 0.0725 0.1289 0.1287 0.0002  0.0471  0.0019  245 TRP A CG  
1990 C  CD1 . TRP A 244 ? 0.0693 0.1453 0.1328 0.0005  0.0528  -0.0129 245 TRP A CD1 
1991 C  CD2 . TRP A 244 ? 0.0621 0.1339 0.1268 -0.0061 0.0474  -0.0040 245 TRP A CD2 
1992 N  NE1 . TRP A 244 ? 0.0894 0.1348 0.1328 0.0080  0.0357  -0.0036 245 TRP A NE1 
1993 C  CE2 . TRP A 244 ? 0.0867 0.1188 0.1410 0.0005  0.0384  0.0152  245 TRP A CE2 
1994 C  CE3 . TRP A 244 ? 0.1068 0.1569 0.1208 -0.0054 0.0436  0.0147  245 TRP A CE3 
1995 C  CZ2 . TRP A 244 ? 0.1037 0.1507 0.1457 0.0161  0.0494  0.0187  245 TRP A CZ2 
1996 C  CZ3 . TRP A 244 ? 0.1160 0.1553 0.1680 0.0160  0.0480  0.0239  245 TRP A CZ3 
1997 C  CH2 . TRP A 244 ? 0.1189 0.1562 0.1432 -0.0163 0.0458  0.0238  245 TRP A CH2 
1998 N  N   . ARG A 245 ? 0.0870 0.1355 0.1037 -0.0127 0.0335  -0.0047 246 ARG A N   
1999 C  CA  . ARG A 245 ? 0.1127 0.1441 0.1210 0.0174  0.0122  0.0017  246 ARG A CA  
2000 C  C   . ARG A 245 ? 0.0713 0.1553 0.1352 0.0138  0.0147  -0.0025 246 ARG A C   
2001 O  O   . ARG A 245 ? 0.0784 0.1461 0.1526 0.0025  0.0221  -0.0163 246 ARG A O   
2002 C  CB  . ARG A 245 ? 0.0921 0.1249 0.1468 -0.0160 0.0006  0.0039  246 ARG A CB  
2003 C  CG  . ARG A 245 ? 0.0613 0.1605 0.1382 0.0220  0.0179  -0.0216 246 ARG A CG  
2004 C  CD  . ARG A 245 ? 0.0691 0.1525 0.1499 -0.0023 0.0087  -0.0086 246 ARG A CD  
2005 N  NE  . ARG A 245 ? 0.0655 0.1705 0.1293 -0.0098 0.0268  -0.0195 246 ARG A NE  
2006 C  CZ  . ARG A 245 ? 0.0653 0.1608 0.1349 -0.0084 0.0308  -0.0133 246 ARG A CZ  
2007 N  NH1 . ARG A 245 ? 0.0748 0.1507 0.1349 -0.0015 0.0439  -0.0037 246 ARG A NH1 
2008 N  NH2 . ARG A 245 ? 0.0534 0.1805 0.1661 -0.0187 0.0386  -0.0098 246 ARG A NH2 
2009 N  N   A PRO A 246 ? 0.0739 0.1342 0.1495 0.0245  0.0322  -0.0004 247 PRO A N   
2010 N  N   B PRO A 246 ? 0.0758 0.1143 0.1625 0.0221  0.0378  0.0085  247 PRO A N   
2011 C  CA  A PRO A 246 ? 0.0572 0.1315 0.1526 0.0223  0.0474  -0.0043 247 PRO A CA  
2012 C  CA  B PRO A 246 ? 0.0682 0.1201 0.1583 0.0144  0.0436  0.0048  247 PRO A CA  
2013 C  C   A PRO A 246 ? 0.0806 0.1585 0.1146 0.0359  0.0300  0.0136  247 PRO A C   
2014 C  C   B PRO A 246 ? 0.0844 0.1556 0.1244 0.0319  0.0281  0.0208  247 PRO A C   
2015 O  O   A PRO A 246 ? 0.0883 0.1542 0.1244 0.0345  0.0416  0.0013  247 PRO A O   
2016 O  O   B PRO A 246 ? 0.0937 0.1504 0.1276 0.0334  0.0396  0.0027  247 PRO A O   
2017 C  CB  A PRO A 246 ? 0.0935 0.1580 0.1434 0.0534  0.0392  -0.0129 247 PRO A CB  
2018 C  CB  B PRO A 246 ? 0.1185 0.1364 0.1788 0.0461  0.0378  0.0071  247 PRO A CB  
2019 C  CG  A PRO A 246 ? 0.1059 0.1614 0.1384 0.0283  0.0406  -0.0162 247 PRO A CG  
2020 C  CG  B PRO A 246 ? 0.0946 0.1769 0.2293 0.0395  0.0082  0.0230  247 PRO A CG  
2021 C  CD  A PRO A 246 ? 0.0960 0.1788 0.1137 0.0550  0.0364  -0.0337 247 PRO A CD  
2022 C  CD  B PRO A 246 ? 0.0745 0.1996 0.1533 0.0414  0.0290  -0.0092 247 PRO A CD  
2023 N  N   . ALA A 247 ? 0.0776 0.1493 0.1326 0.0189  0.0489  0.0026  248 ALA A N   
2024 C  CA  . ALA A 247 ? 0.0703 0.1594 0.1181 0.0071  0.0399  -0.0036 248 ALA A CA  
2025 C  C   . ALA A 247 ? 0.0745 0.1650 0.1242 0.0137  0.0310  0.0111  248 ALA A C   
2026 O  O   . ALA A 247 ? 0.0955 0.1720 0.1497 0.0283  0.0230  0.0198  248 ALA A O   
2027 C  CB  . ALA A 247 ? 0.1179 0.1471 0.1646 -0.0099 0.0166  0.0086  248 ALA A CB  
2028 N  N   . GLN A 248 ? 0.0759 0.1543 0.1187 -0.0006 0.0285  0.0168  249 GLN A N   
2029 C  CA  . GLN A 248 ? 0.0849 0.1669 0.1277 0.0208  0.0049  0.0000  249 GLN A CA  
2030 C  C   . GLN A 248 ? 0.1155 0.1751 0.1346 0.0107  0.0072  0.0125  249 GLN A C   
2031 O  O   . GLN A 248 ? 0.1242 0.1995 0.1407 0.0008  0.0215  0.0122  249 GLN A O   
2032 C  CB  . GLN A 248 ? 0.1093 0.1580 0.1363 -0.0038 0.0075  -0.0044 249 GLN A CB  
2033 C  CG  . GLN A 248 ? 0.0928 0.1461 0.1416 0.0100  0.0147  0.0044  249 GLN A CG  
2034 C  CD  . GLN A 248 ? 0.0786 0.2192 0.1421 0.0019  0.0220  -0.0079 249 GLN A CD  
2035 O  OE1 . GLN A 248 ? 0.0883 0.2328 0.1849 -0.0129 0.0036  -0.0066 249 GLN A OE1 
2036 N  NE2 . GLN A 248 ? 0.1072 0.2028 0.1439 -0.0020 0.0094  -0.0148 249 GLN A NE2 
2037 N  N   . PRO A 249 ? 0.0944 0.2075 0.1447 0.0293  0.0098  -0.0067 250 PRO A N   
2038 C  CA  . PRO A 249 ? 0.1192 0.2566 0.1522 0.0551  0.0248  0.0032  250 PRO A CA  
2039 C  C   . PRO A 249 ? 0.1260 0.2050 0.1131 0.0347  -0.0032 -0.0059 250 PRO A C   
2040 O  O   . PRO A 249 ? 0.0937 0.2179 0.1271 0.0292  0.0100  0.0038  250 PRO A O   
2041 C  CB  . PRO A 249 ? 0.1298 0.3026 0.1619 0.0998  -0.0283 -0.0545 250 PRO A CB  
2042 C  CG  . PRO A 249 ? 0.1137 0.3227 0.1497 0.0398  0.0108  0.0068  250 PRO A CG  
2043 C  CD  . PRO A 249 ? 0.0795 0.3248 0.1823 0.0211  -0.0190 0.0194  250 PRO A CD  
2044 N  N   . LEU A 250 ? 0.1237 0.2054 0.1370 0.0469  0.0171  0.0038  251 LEU A N   
2045 C  CA  . LEU A 250 ? 0.1171 0.1856 0.1646 0.0175  0.0262  -0.0178 251 LEU A CA  
2046 C  C   . LEU A 250 ? 0.1511 0.1921 0.1368 0.0277  -0.0002 -0.0018 251 LEU A C   
2047 O  O   . LEU A 250 ? 0.1134 0.1844 0.1644 0.0253  0.0085  0.0006  251 LEU A O   
2048 C  CB  . LEU A 250 ? 0.1314 0.1824 0.1873 0.0244  0.0242  0.0068  251 LEU A CB  
2049 C  CG  . LEU A 250 ? 0.1059 0.2204 0.2099 0.0089  0.0547  0.0450  251 LEU A CG  
2050 C  CD1 . LEU A 250 ? 0.1393 0.2190 0.1806 0.0102  -0.0091 -0.0221 251 LEU A CD1 
2051 C  CD2 . LEU A 250 ? 0.1856 0.2050 0.2494 -0.0598 0.0738  0.0049  251 LEU A CD2 
2052 N  N   . LYS A 251 ? 0.1413 0.2163 0.1478 0.0496  -0.0032 -0.0129 252 LYS A N   
2053 C  CA  . LYS A 251 ? 0.1669 0.2339 0.1752 0.0524  -0.0043 -0.0111 252 LYS A CA  
2054 C  C   . LYS A 251 ? 0.1590 0.2654 0.2354 0.0801  0.0013  -0.0077 252 LYS A C   
2055 O  O   . LYS A 251 ? 0.1928 0.3219 0.2002 0.0144  0.0189  -0.0006 252 LYS A O   
2056 C  CB  . LYS A 251 ? 0.1612 0.2436 0.2235 0.0092  -0.0104 -0.0314 252 LYS A CB  
2057 C  CG  . LYS A 251 ? 0.2311 0.3348 0.2476 -0.0233 0.1037  -0.0648 252 LYS A CG  
2058 C  CD  . LYS A 251 ? 0.2850 0.4712 0.3465 -0.1164 0.1131  -0.0932 252 LYS A CD  
2059 C  CE  . LYS A 251 ? 0.2838 0.4813 0.4664 -0.1377 0.2256  -0.1463 252 LYS A CE  
2060 N  NZ  . LYS A 251 ? 0.3718 0.6735 0.3700 0.1886  0.0482  0.0758  252 LYS A NZ  
2061 N  N   . ASN A 252 ? 0.1644 0.2865 0.1666 0.0661  -0.0331 -0.0699 253 ASN A N   
2062 C  CA  . ASN A 252 ? 0.1344 0.4896 0.2772 0.0932  -0.0257 -0.1544 253 ASN A CA  
2063 C  C   . ASN A 252 ? 0.2020 0.3640 0.3975 0.1213  -0.0922 -0.1237 253 ASN A C   
2064 O  O   . ASN A 252 ? 0.2534 0.3075 0.3735 0.0591  -0.0296 -0.0892 253 ASN A O   
2065 C  CB  . ASN A 252 ? 0.2535 0.6739 0.3888 0.0265  -0.1051 -0.3087 253 ASN A CB  
2066 C  CG  . ASN A 252 ? 0.6251 0.5917 0.3717 0.2608  -0.0557 -0.1948 253 ASN A CG  
2067 O  OD1 . ASN A 252 ? 1.3279 0.7531 0.6442 0.2171  -0.1197 0.0981  253 ASN A OD1 
2068 N  ND2 . ASN A 252 ? 0.2593 0.5313 0.6994 0.1146  -0.1998 -0.1458 253 ASN A ND2 
2069 N  N   . ARG A 253 ? 0.1005 0.3322 0.1659 0.0233  0.0305  0.0006  254 ARG A N   
2070 C  CA  . ARG A 253 ? 0.1138 0.1939 0.1271 0.0009  0.0218  -0.0087 254 ARG A CA  
2071 C  C   . ARG A 253 ? 0.1592 0.1716 0.1784 0.0140  0.0597  -0.0150 254 ARG A C   
2072 O  O   . ARG A 253 ? 0.2190 0.1993 0.2781 0.0490  0.1193  0.0465  254 ARG A O   
2073 C  CB  . ARG A 253 ? 0.1425 0.1683 0.1285 0.0187  0.0608  -0.0099 254 ARG A CB  
2074 C  CG  . ARG A 253 ? 0.1414 0.1522 0.1217 0.0023  0.0477  -0.0212 254 ARG A CG  
2075 C  CD  . ARG A 253 ? 0.1279 0.1671 0.1120 0.0384  0.0334  -0.0143 254 ARG A CD  
2076 N  NE  . ARG A 253 ? 0.0886 0.1518 0.1317 0.0089  0.0139  -0.0237 254 ARG A NE  
2077 C  CZ  . ARG A 253 ? 0.0861 0.1423 0.1335 0.0017  0.0033  -0.0119 254 ARG A CZ  
2078 N  NH1 . ARG A 253 ? 0.0677 0.1619 0.1425 0.0107  -0.0080 -0.0013 254 ARG A NH1 
2079 N  NH2 . ARG A 253 ? 0.0743 0.1348 0.1330 0.0063  0.0158  0.0150  254 ARG A NH2 
2080 N  N   . GLN A 254 ? 0.1302 0.2165 0.1282 0.0146  0.0241  -0.0370 255 GLN A N   
2081 C  CA  . GLN A 254 ? 0.1289 0.2817 0.1479 0.0043  -0.0062 -0.0649 255 GLN A CA  
2082 C  C   . GLN A 254 ? 0.1508 0.2282 0.1804 -0.0041 -0.0375 0.0050  255 GLN A C   
2083 O  O   . GLN A 254 ? 0.2013 0.2158 0.1982 -0.0232 -0.0369 0.0242  255 GLN A O   
2084 C  CB  . GLN A 254 ? 0.1830 0.4000 0.1284 -0.0083 0.0261  -0.0743 255 GLN A CB  
2085 C  CG  . GLN A 254 ? 0.2946 0.5344 0.1532 0.1249  0.0350  -0.0624 255 GLN A CG  
2086 C  CD  . GLN A 254 ? 0.5026 0.6133 0.2806 0.0261  0.2276  0.1905  255 GLN A CD  
2087 O  OE1 . GLN A 254 ? 0.6172 0.4182 0.8591 -0.1266 0.3617  -0.0440 255 GLN A OE1 
2088 N  NE2 . GLN A 254 ? 0.5896 0.5246 0.3223 0.0776  0.2017  0.1571  255 GLN A NE2 
2089 N  N   . ILE A 255 ? 0.1021 0.1833 0.1332 -0.0013 0.0359  -0.0081 256 ILE A N   
2090 C  CA  . ILE A 255 ? 0.1041 0.1869 0.1407 0.0218  0.0290  -0.0210 256 ILE A CA  
2091 C  C   . ILE A 255 ? 0.1313 0.1694 0.1296 0.0030  0.0496  0.0196  256 ILE A C   
2092 O  O   . ILE A 255 ? 0.1204 0.1849 0.1470 0.0228  0.0602  0.0411  256 ILE A O   
2093 C  CB  . ILE A 255 ? 0.0889 0.1996 0.1521 0.0375  0.0132  -0.0300 256 ILE A CB  
2094 C  CG1 . ILE A 255 ? 0.1076 0.1823 0.1917 0.0418  0.0447  -0.0179 256 ILE A CG1 
2095 C  CG2 . ILE A 255 ? 0.1289 0.2016 0.1671 0.0348  -0.0065 -0.0441 256 ILE A CG2 
2096 C  CD1 . ILE A 255 ? 0.1311 0.2074 0.1730 -0.0089 0.0670  -0.0553 256 ILE A CD1 
2097 N  N   . LYS A 256 ? 0.0812 0.1854 0.1188 0.0009  0.0431  0.0029  257 LYS A N   
2098 C  CA  . LYS A 256 ? 0.0835 0.1856 0.1138 0.0097  0.0446  0.0020  257 LYS A CA  
2099 C  C   . LYS A 256 ? 0.0750 0.1757 0.1230 0.0013  0.0379  0.0147  257 LYS A C   
2100 O  O   . LYS A 256 ? 0.1206 0.2269 0.1076 -0.0291 0.0368  0.0139  257 LYS A O   
2101 C  CB  . LYS A 256 ? 0.1149 0.1802 0.1711 -0.0037 0.0553  -0.0025 257 LYS A CB  
2102 C  CG  . LYS A 256 ? 0.1892 0.1917 0.2140 -0.0339 0.0342  -0.0381 257 LYS A CG  
2103 C  CD  . LYS A 256 ? 0.2738 0.2193 0.3701 -0.0161 0.0325  -0.0730 257 LYS A CD  
2104 C  CE  . LYS A 256 ? 0.3948 0.4078 0.4378 -0.1782 0.0054  -0.0877 257 LYS A CE  
2105 N  NZ  . LYS A 256 ? 0.3231 0.3921 0.6401 -0.0608 0.0715  -0.0895 257 LYS A NZ  
2106 N  N   . ALA A 257 ? 0.0878 0.1981 0.1192 -0.0126 0.0527  0.0039  258 ALA A N   
2107 C  CA  . ALA A 257 ? 0.0914 0.1852 0.1568 -0.0137 0.0425  -0.0015 258 ALA A CA  
2108 C  C   . ALA A 257 ? 0.1067 0.1547 0.1362 -0.0223 0.0381  -0.0036 258 ALA A C   
2109 O  O   . ALA A 257 ? 0.1072 0.2353 0.1298 -0.0265 0.0556  -0.0264 258 ALA A O   
2110 C  CB  . ALA A 257 ? 0.1169 0.2078 0.1906 -0.0587 0.0819  -0.0039 258 ALA A CB  
2111 N  N   . SER A 258 ? 0.1038 0.1751 0.1478 -0.0210 0.0376  0.0175  259 SER A N   
2112 C  CA  . SER A 258 ? 0.0933 0.2143 0.1860 -0.0142 0.0692  0.0309  259 SER A CA  
2113 C  C   . SER A 258 ? 0.1071 0.2492 0.1702 -0.0351 0.0846  0.0009  259 SER A C   
2114 O  O   . SER A 258 ? 0.0901 0.3705 0.2021 -0.0062 0.0919  0.0155  259 SER A O   
2115 C  CB  . SER A 258 ? 0.1558 0.2016 0.2036 -0.0248 0.0167  0.0367  259 SER A CB  
2116 O  OG  . SER A 258 ? 0.1102 0.2038 0.1482 0.0115  0.0515  0.0175  259 SER A OG  
2117 N  N   . PHE A 259 ? 0.0949 0.2461 0.1781 -0.0509 0.0445  0.0176  260 PHE A N   
2118 C  CA  . PHE A 259 ? 0.1338 0.2617 0.2095 -0.0697 0.0407  0.0403  260 PHE A CA  
2119 C  C   . PHE A 259 ? 0.2588 0.4131 0.1790 -0.1033 -0.0001 0.0659  260 PHE A C   
2120 O  O   . PHE A 259 ? 0.2294 0.3516 0.2082 -0.0739 0.0039  0.0895  260 PHE A O   
2121 C  CB  . PHE A 259 ? 0.1207 0.2550 0.2255 -0.0412 0.0192  0.0100  260 PHE A CB  
2122 C  CG  . PHE A 259 ? 0.1279 0.2020 0.2676 -0.0449 0.0317  0.0266  260 PHE A CG  
2123 C  CD1 . PHE A 259 ? 0.1294 0.2129 0.1610 -0.0341 0.0195  -0.0044 260 PHE A CD1 
2124 C  CD2 . PHE A 259 ? 0.1971 0.2175 0.3204 -0.0135 0.0300  0.0158  260 PHE A CD2 
2125 C  CE1 . PHE A 259 ? 0.1443 0.2205 0.1844 -0.0210 0.0431  0.0039  260 PHE A CE1 
2126 C  CE2 . PHE A 259 ? 0.1816 0.2430 0.3917 -0.0233 0.0441  0.1216  260 PHE A CE2 
2127 C  CZ  . PHE A 259 ? 0.1450 0.2663 0.2857 -0.0471 0.0017  0.0848  260 PHE A CZ  
2128 N  N   . LYS A 260 ? 0.3676 0.5110 0.3970 -0.1998 0.0678  0.0579  261 LYS A N   
2129 C  CA  . LYS A 260 ? 0.5797 0.5251 0.4568 -0.0321 -0.0209 0.1451  261 LYS A CA  
2130 C  C   . LYS A 260 ? 0.7478 0.9167 0.3827 -0.4293 -0.0108 0.0787  261 LYS A C   
2131 O  O   . LYS A 260 ? 0.7993 0.9797 0.5439 -0.2815 -0.1049 0.1009  261 LYS A O   
2132 C  CB  . LYS A 260 ? 0.5702 0.5307 0.7528 -0.0594 0.0864  0.0996  261 LYS A CB  
2133 O  OXT . LYS A 260 ? 0.8516 1.3361 0.7000 -0.1453 0.1465  0.4865  261 LYS A OXT 
2134 ZN ZN  . ZN  B .   ? 0.0669 0.1179 0.1028 -0.0100 0.0309  0.0024  301 ZN  A ZN  
2135 O  O13 . EA3 C .   ? 0.1091 0.1658 0.1335 -0.0140 0.0372  0.0025  302 EA3 A O13 
2136 C  C12 . EA3 C .   ? 0.1177 0.1324 0.1328 -0.0283 0.0315  0.0103  302 EA3 A C12 
2137 N  N14 . EA3 C .   ? 0.1050 0.1917 0.1252 -0.0105 0.0413  0.0165  302 EA3 A N14 
2138 C  C15 . EA3 C .   ? 0.1672 0.2298 0.1456 -0.0436 0.0678  -0.0020 302 EA3 A C15 
2139 C  C16 . EA3 C .   ? 0.1942 0.2942 0.2507 -0.0789 0.0839  -0.0186 302 EA3 A C16 
2140 O  O17 . EA3 C .   ? 0.2505 0.2644 0.3149 -0.0524 0.1226  0.0400  302 EA3 A O17 
2141 C  C9  . EA3 C .   ? 0.0923 0.1427 0.1310 -0.0159 0.0147  -0.0065 302 EA3 A C9  
2142 C  C10 . EA3 C .   ? 0.0411 0.1442 0.1214 -0.0186 0.0201  -0.0070 302 EA3 A C10 
2143 C  C3  . EA3 C .   ? 0.0493 0.1382 0.1183 -0.0309 0.0319  0.0055  302 EA3 A C3  
2144 S  S2  . EA3 C .   ? 0.0685 0.1220 0.1172 -0.0003 0.0276  0.0031  302 EA3 A S2  
2145 O  O4  . EA3 C .   ? 0.0643 0.1360 0.1221 -0.0162 0.0195  -0.0110 302 EA3 A O4  
2146 O  O5  . EA3 C .   ? 0.0488 0.1020 0.1377 0.0111  0.0245  -0.0069 302 EA3 A O5  
2147 N  N1  . EA3 C .   ? 0.0258 0.1056 0.1396 -0.0278 0.0392  0.0006  302 EA3 A N1  
2148 C  C8  . EA3 C .   ? 0.0980 0.1163 0.1144 -0.0458 0.0376  0.0080  302 EA3 A C8  
2149 C  C7  . EA3 C .   ? 0.0797 0.1522 0.1165 -0.0348 0.0294  -0.0080 302 EA3 A C7  
2150 C  C6  . EA3 C .   ? 0.0777 0.1557 0.1135 -0.0194 0.0311  -0.0179 302 EA3 A C6  
2151 CL CL1 . EA3 C .   ? 0.0928 0.1222 0.1398 0.0006  0.0361  -0.0118 302 EA3 A CL1 
2152 S  S18 . EA3 C .   ? 0.1513 0.1435 0.1368 -0.0212 0.0282  0.0127  302 EA3 A S18 
2153 C  C19 . EA3 C .   ? 0.1622 0.2998 0.3678 -0.1393 -0.0234 0.1392  302 EA3 A C19 
2154 C  C24 . EA3 C .   ? 0.3051 0.3174 0.3527 -0.1460 -0.0602 0.0369  302 EA3 A C24 
2155 C  C23 . EA3 C .   ? 0.3744 0.2090 0.2466 -0.0209 -0.0083 0.0659  302 EA3 A C23 
2156 C  C22 . EA3 C .   ? 0.2381 0.3104 0.2994 -0.0879 -0.0067 0.0759  302 EA3 A C22 
2157 C  C21 . EA3 C .   ? 0.3583 0.2318 0.2646 -0.0791 -0.0485 0.0582  302 EA3 A C21 
2158 C  C20 . EA3 C .   ? 0.2052 0.2343 0.3071 -0.0840 0.0098  0.0846  302 EA3 A C20 
2159 S  S   . DMS D .   ? 0.2746 0.3947 0.5092 -0.0286 0.0631  -0.0083 303 DMS A S   
2160 O  O   . DMS D .   ? 0.2495 0.4520 0.9496 -0.0811 0.0037  0.2852  303 DMS A O   
2161 C  C1  . DMS D .   ? 0.5016 0.4907 0.3906 -0.1439 0.1912  -0.2777 303 DMS A C1  
2162 C  C2  . DMS D .   ? 0.3565 0.5173 0.4531 0.2287  0.1121  -0.1610 303 DMS A C2  
2163 O  O   . HOH E .   ? 0.4948 0.8728 0.4195 -0.3427 0.1159  0.0558  401 HOH A O   
2164 O  O   . HOH E .   ? 0.2200 0.3813 0.5229 -0.0581 0.0429  0.0391  402 HOH A O   
2165 O  O   . HOH E .   ? 0.8056 0.2913 0.4582 0.0219  -0.2958 -0.0543 403 HOH A O   
2166 O  O   . HOH E .   ? 0.4386 0.2816 0.3557 0.1207  0.0803  -0.0226 404 HOH A O   
2167 O  O   . HOH E .   ? 0.4318 0.5869 0.3248 -0.0205 0.0462  0.0985  405 HOH A O   
2168 O  O   . HOH E .   ? 0.6441 0.2948 0.4894 -0.0181 -0.0504 -0.0270 406 HOH A O   
2169 O  O   . HOH E .   ? 0.3041 0.2782 0.3492 -0.0419 0.1021  -0.0868 407 HOH A O   
2170 O  O   . HOH E .   ? 0.2562 0.6949 0.6819 0.0563  -0.1048 -0.2635 408 HOH A O   
2171 O  O   . HOH E .   ? 0.9603 0.4003 0.2864 -0.1518 0.1237  -0.0455 409 HOH A O   
2172 O  O   . HOH E .   ? 0.4947 0.3551 0.5750 -0.0025 -0.0465 0.0675  410 HOH A O   
2173 O  O   . HOH E .   ? 0.5525 0.2032 0.5129 0.0502  0.0634  0.0746  411 HOH A O   
2174 O  O   . HOH E .   ? 0.1865 0.2636 0.3637 0.0138  0.0011  -0.0033 412 HOH A O   
2175 O  O   . HOH E .   ? 0.4368 0.3422 1.2328 -0.0970 -0.0025 0.0846  413 HOH A O   
2176 O  O   . HOH E .   ? 0.6423 0.2904 0.2918 -0.0493 0.0795  -0.0279 414 HOH A O   
2177 O  O   . HOH E .   ? 0.4596 0.2932 0.1303 0.0245  0.0316  -0.0271 415 HOH A O   
2178 O  O   . HOH E .   ? 0.2276 0.3380 0.2100 0.0250  0.0250  0.0136  416 HOH A O   
2179 O  O   . HOH E .   ? 0.3561 0.2352 0.4563 -0.1118 0.0807  -0.0916 417 HOH A O   
2180 O  O   . HOH E .   ? 0.3381 0.8766 0.4123 0.1517  -0.0939 -0.2692 418 HOH A O   
2181 O  O   . HOH E .   ? 0.1960 0.2132 0.2039 -0.0256 0.0332  0.0223  419 HOH A O   
2182 O  O   . HOH E .   ? 0.3934 0.4509 0.6646 0.0024  -0.1503 -0.0086 420 HOH A O   
2183 O  O   . HOH E .   ? 0.1126 0.1607 0.0944 -0.0151 0.0165  0.0027  421 HOH A O   
2184 O  O   . HOH E .   ? 0.2951 0.8845 0.2518 -0.0776 0.1110  -0.1132 422 HOH A O   
2185 O  O   . HOH E .   ? 0.2308 0.5231 0.3802 -0.0118 0.1210  -0.1081 423 HOH A O   
2186 O  O   . HOH E .   ? 0.5131 0.2974 0.2066 -0.0125 0.0103  0.0290  424 HOH A O   
2187 O  O   . HOH E .   ? 0.3086 0.3592 0.3939 -0.0190 -0.1183 0.0164  425 HOH A O   
2188 O  O   . HOH E .   ? 0.7486 0.2670 0.1993 -0.0893 0.0022  -0.0036 426 HOH A O   
2189 O  O   . HOH E .   ? 0.0889 0.1474 0.1280 0.0009  0.0366  -0.0065 427 HOH A O   
2190 O  O   . HOH E .   ? 0.2784 0.4068 0.1874 -0.1324 -0.0507 0.0471  428 HOH A O   
2191 O  O   . HOH E .   ? 0.4788 0.4383 0.2822 0.0697  0.0829  -0.0989 429 HOH A O   
2192 O  O   . HOH E .   ? 0.2962 0.4314 0.7126 -0.1437 -0.2257 0.1899  430 HOH A O   
2193 O  O   . HOH E .   ? 0.4521 0.5403 0.3236 -0.1377 0.0168  0.1600  431 HOH A O   
2194 O  O   . HOH E .   ? 0.3879 0.4755 0.4957 -0.2315 0.2931  -0.2291 432 HOH A O   
2195 O  O   . HOH E .   ? 0.5825 0.2312 0.3727 -0.0335 0.2152  0.0359  433 HOH A O   
2196 O  O   . HOH E .   ? 0.2002 1.0310 0.3179 0.2051  0.0460  -0.0378 434 HOH A O   
2197 O  O   . HOH E .   ? 0.5189 0.6581 0.4374 0.3449  -0.2076 -0.2678 435 HOH A O   
2198 O  O   . HOH E .   ? 0.3105 0.2978 0.1662 0.0354  -0.0145 0.0134  436 HOH A O   
2199 O  O   . HOH E .   ? 0.1729 0.7806 0.3992 0.1585  -0.0688 -0.2638 437 HOH A O   
2200 O  O   . HOH E .   ? 0.1040 0.1300 0.1389 -0.0192 0.0238  0.0006  438 HOH A O   
2201 O  O   . HOH E .   ? 0.2819 0.4761 0.4023 0.1892  -0.1550 -0.2517 439 HOH A O   
2202 O  O   . HOH E .   ? 0.2114 0.9407 0.2081 0.0310  0.0294  0.0634  440 HOH A O   
2203 O  O   . HOH E .   ? 0.2623 0.8788 0.8008 -0.0336 -0.0329 -0.3035 441 HOH A O   
2204 O  O   . HOH E .   ? 0.1630 0.8292 0.3213 -0.0392 0.0030  0.1162  442 HOH A O   
2205 O  O   . HOH E .   ? 0.4170 0.3287 0.5427 -0.0717 -0.1264 0.1044  443 HOH A O   
2206 O  O   . HOH E .   ? 0.2090 0.5602 0.3535 0.0735  0.1412  0.1309  444 HOH A O   
2207 O  O   . HOH E .   ? 0.4953 0.2649 0.3225 0.1254  0.1641  0.1057  445 HOH A O   
2208 O  O   . HOH E .   ? 0.6741 0.8586 0.3725 -0.5207 0.0982  -0.1119 446 HOH A O   
2209 O  O   . HOH E .   ? 0.4433 0.4160 0.1974 -0.1093 0.0375  0.0366  447 HOH A O   
2210 O  O   . HOH E .   ? 0.2635 0.4931 0.5654 0.0661  -0.1252 -0.0542 448 HOH A O   
2211 O  O   . HOH E .   ? 0.1855 0.2147 0.2434 0.0079  -0.0839 -0.0240 449 HOH A O   
2212 O  O   . HOH E .   ? 0.1084 0.1450 0.2237 -0.0055 0.0344  0.0157  450 HOH A O   
2213 O  O   . HOH E .   ? 0.4260 0.3416 0.3435 -0.0293 -0.0837 -0.0204 451 HOH A O   
2214 O  O   . HOH E .   ? 0.3294 0.2558 0.2059 0.0565  -0.0816 0.0447  452 HOH A O   
2215 O  O   . HOH E .   ? 0.5285 0.3520 0.2154 -0.1144 0.0684  -0.0441 453 HOH A O   
2216 O  O   . HOH E .   ? 0.4608 0.5180 0.2096 0.1791  0.0097  -0.1130 454 HOH A O   
2217 O  O   . HOH E .   ? 0.1066 0.3689 0.5288 0.0179  0.0533  0.1145  455 HOH A O   
2218 O  O   . HOH E .   ? 0.3875 0.3352 0.3753 -0.1350 0.0042  -0.0027 456 HOH A O   
2219 O  O   . HOH E .   ? 0.2060 0.1561 0.1490 0.0201  0.0306  -0.0064 457 HOH A O   
2220 O  O   . HOH E .   ? 0.1876 0.3737 0.1894 0.0173  -0.0185 -0.0013 458 HOH A O   
2221 O  O   . HOH E .   ? 0.2469 0.3965 0.2222 0.0625  0.0622  0.0466  459 HOH A O   
2222 O  O   . HOH E .   ? 0.3413 0.3559 0.3559 -0.0446 -0.0702 0.1141  460 HOH A O   
2223 O  O   . HOH E .   ? 0.2154 0.4136 0.5499 -0.0346 0.0209  -0.1425 461 HOH A O   
2224 O  O   . HOH E .   ? 0.4165 0.3613 0.2196 -0.1265 0.1509  -0.0844 462 HOH A O   
2225 O  O   . HOH E .   ? 0.2655 0.5989 0.5151 0.1052  -0.1390 -0.0473 463 HOH A O   
2226 O  O   . HOH E .   ? 0.1310 0.1454 0.1571 -0.0172 0.0354  0.0015  464 HOH A O   
2227 O  O   . HOH E .   ? 0.2020 0.7464 0.4297 0.0410  0.1551  0.2324  465 HOH A O   
2228 O  O   . HOH E .   ? 0.3692 0.4065 0.5193 -0.0490 -0.2073 0.1326  466 HOH A O   
2229 O  O   . HOH E .   ? 0.1138 0.1665 0.1324 0.0042  0.0257  0.0084  467 HOH A O   
2230 O  O   . HOH E .   ? 0.1578 0.2702 0.2394 0.0153  -0.0136 -0.0008 468 HOH A O   
2231 O  O   . HOH E .   ? 0.2011 0.1880 0.2336 0.0002  0.0160  0.0071  469 HOH A O   
2232 O  O   . HOH E .   ? 0.3210 0.2377 0.2197 -0.0847 -0.0156 -0.0041 470 HOH A O   
2233 O  O   . HOH E .   ? 0.3576 0.2305 0.2728 -0.0339 -0.0068 0.0242  471 HOH A O   
2234 O  O   . HOH E .   ? 0.3219 0.5978 1.2530 0.0826  -0.1112 -0.4277 472 HOH A O   
2235 O  O   . HOH E .   ? 0.0844 0.2082 0.1612 0.0100  0.0053  0.0227  473 HOH A O   
2236 O  O   . HOH E .   ? 0.3319 0.1912 0.1790 -0.0721 0.0721  0.0155  474 HOH A O   
2237 O  O   . HOH E .   ? 0.2591 0.3075 0.4455 -0.0330 -0.0192 0.1747  475 HOH A O   
2238 O  O   . HOH E .   ? 0.2348 1.3204 0.4356 -0.0336 -0.0473 -0.0094 476 HOH A O   
2239 O  O   . HOH E .   ? 0.2504 0.2961 0.3013 0.0068  0.1335  0.0407  477 HOH A O   
2240 O  O   . HOH E .   ? 0.3752 0.2348 0.8174 -0.1079 -0.0321 0.0537  478 HOH A O   
2241 O  O   . HOH E .   ? 0.0761 0.1323 0.1504 -0.0176 0.0381  0.0046  479 HOH A O   
2242 O  O   . HOH E .   ? 0.2915 0.2285 0.3359 0.0006  0.1602  0.0803  480 HOH A O   
2243 O  O   . HOH E .   ? 0.2681 0.6001 0.5442 0.0418  0.1351  0.1075  481 HOH A O   
2244 O  O   . HOH E .   ? 0.2498 0.3664 0.2447 -0.0469 -0.0270 -0.0096 482 HOH A O   
2245 O  O   . HOH E .   ? 0.2258 0.2983 0.3540 -0.0528 0.0712  -0.0479 483 HOH A O   
2246 O  O   . HOH E .   ? 0.4029 0.3071 0.3959 0.0512  0.1492  0.0565  484 HOH A O   
2247 O  O   . HOH E .   ? 0.3520 0.2225 0.4626 -0.0573 0.0116  0.0150  485 HOH A O   
2248 O  O   . HOH E .   ? 0.2690 0.4247 0.2970 0.1322  0.1032  0.0449  486 HOH A O   
2249 O  O   . HOH E .   ? 0.6608 0.4617 0.2618 -0.0493 -0.0884 0.0411  487 HOH A O   
2250 O  O   . HOH E .   ? 0.2017 0.2011 0.3682 0.0277  0.0153  -0.0456 488 HOH A O   
2251 O  O   . HOH E .   ? 0.2604 0.4099 0.3247 -0.0442 0.0084  0.1178  489 HOH A O   
2252 O  O   . HOH E .   ? 0.5202 0.4478 0.3079 -0.1362 0.1173  -0.1761 490 HOH A O   
2253 O  O   . HOH E .   ? 0.2721 0.6164 0.4097 0.0145  0.1042  -0.0175 491 HOH A O   
2254 O  O   . HOH E .   ? 0.3143 0.4570 0.2514 0.1715  0.1119  0.0025  492 HOH A O   
2255 O  O   . HOH E .   ? 0.5070 0.2508 0.1877 -0.1149 0.0270  0.0536  493 HOH A O   
2256 O  O   . HOH E .   ? 0.2861 0.3463 0.8707 0.0049  0.0285  0.1162  494 HOH A O   
2257 O  O   . HOH E .   ? 0.1219 0.1905 0.1939 0.0239  0.0289  0.0044  495 HOH A O   
2258 O  O   . HOH E .   ? 0.3063 0.4115 0.1928 0.0021  -0.0175 0.0381  496 HOH A O   
2259 O  O   . HOH E .   ? 0.0971 0.1421 0.1289 0.0175  0.0347  -0.0048 497 HOH A O   
2260 O  O   . HOH E .   ? 0.7458 0.9494 0.5697 0.3646  0.1890  0.3766  498 HOH A O   
2261 O  O   . HOH E .   ? 0.1504 0.4864 0.3694 -0.0895 -0.0188 0.0183  499 HOH A O   
2262 O  O   . HOH E .   ? 0.3866 0.2791 0.4219 0.1599  -0.0222 -0.0025 500 HOH A O   
2263 O  O   . HOH E .   ? 0.4008 0.2420 0.2021 -0.0069 0.1017  -0.0657 501 HOH A O   
2264 O  O   . HOH E .   ? 0.7831 0.3545 0.1508 0.1291  0.0596  0.0002  502 HOH A O   
2265 O  O   . HOH E .   ? 0.1625 0.3287 0.2073 -0.0333 0.0424  -0.0567 503 HOH A O   
2266 O  O   . HOH E .   ? 0.1562 0.2552 0.1883 -0.0201 -0.0050 0.0467  504 HOH A O   
2267 O  O   . HOH E .   ? 0.2787 0.3651 0.2431 0.1490  0.0661  0.0064  505 HOH A O   
2268 O  O   . HOH E .   ? 0.2806 0.3425 0.3087 -0.0644 -0.0543 -0.0342 506 HOH A O   
2269 O  O   . HOH E .   ? 0.2772 0.5227 0.4404 -0.0631 -0.0760 0.0580  507 HOH A O   
2270 O  O   . HOH E .   ? 0.3450 0.2781 0.3581 -0.0132 0.0055  -0.0192 508 HOH A O   
2271 O  O   . HOH E .   ? 0.1375 0.5650 0.2876 0.0009  -0.0139 0.1323  509 HOH A O   
2272 O  O   . HOH E .   ? 0.6599 0.7072 0.2393 0.1136  0.1400  0.0456  510 HOH A O   
2273 O  O   . HOH E .   ? 0.5086 0.4567 0.3896 -0.0499 0.1596  -0.0594 511 HOH A O   
2274 O  O   . HOH E .   ? 0.1883 0.2151 0.2537 -0.0525 0.0100  -0.0061 512 HOH A O   
2275 O  O   . HOH E .   ? 0.4657 0.5967 0.1709 -0.0281 0.0436  0.0321  513 HOH A O   
2276 O  O   . HOH E .   ? 0.1964 0.2616 0.1744 0.0019  0.0872  -0.0449 514 HOH A O   
2277 O  O   . HOH E .   ? 0.2229 0.1999 0.2537 -0.0765 -0.0013 -0.0187 515 HOH A O   
2278 O  O   . HOH E .   ? 0.4952 0.5400 0.2125 0.0197  0.0710  0.1036  516 HOH A O   
2279 O  O   . HOH E .   ? 0.2122 0.3388 0.4542 0.0082  0.0251  0.1210  517 HOH A O   
2280 O  O   . HOH E .   ? 0.8998 0.4858 0.2781 -0.3206 0.0072  0.0293  518 HOH A O   
2281 O  O   . HOH E .   ? 0.1479 0.1878 0.1985 0.0486  0.0379  0.0098  519 HOH A O   
2282 O  O   . HOH E .   ? 0.3173 0.4810 0.6281 -0.0428 0.1948  -0.0347 520 HOH A O   
2283 O  O   . HOH E .   ? 0.2242 0.2307 0.1522 -0.0130 0.0160  0.0151  521 HOH A O   
2284 O  O   . HOH E .   ? 0.1478 0.2748 0.1350 0.0333  0.0306  0.0059  522 HOH A O   
2285 O  O   . HOH E .   ? 0.1761 0.1838 0.3538 -0.0392 0.0135  0.0099  523 HOH A O   
2286 O  O   . HOH E .   ? 0.1122 0.1848 0.1518 0.0227  0.0217  0.0103  524 HOH A O   
2287 O  O   . HOH E .   ? 0.1237 0.2107 0.2381 -0.0025 0.0164  0.0035  525 HOH A O   
2288 O  O   . HOH E .   ? 0.1719 0.2659 0.1923 -0.0117 -0.0062 -0.0249 526 HOH A O   
2289 O  O   . HOH E .   ? 0.5039 0.3871 0.4987 -0.1211 0.1244  -0.0644 527 HOH A O   
2290 O  O   . HOH E .   ? 0.1934 0.2397 0.3208 -0.0789 0.0239  0.0579  528 HOH A O   
2291 O  O   . HOH E .   ? 0.2713 0.2456 0.1971 -0.0113 -0.0418 0.0183  529 HOH A O   
2292 O  O   . HOH E .   ? 0.2188 0.2454 0.4029 0.0194  0.0206  0.0117  530 HOH A O   
2293 O  O   . HOH E .   ? 0.2564 0.2064 0.3625 0.0608  0.0600  -0.0447 531 HOH A O   
2294 O  O   . HOH E .   ? 0.2630 0.6095 0.3254 -0.1040 -0.0129 0.2149  532 HOH A O   
2295 O  O   . HOH E .   ? 0.0621 0.1770 0.2358 -0.0019 0.0030  -0.0359 533 HOH A O   
2296 O  O   . HOH E .   ? 0.4938 0.5279 1.0579 0.0641  0.3264  -0.2294 534 HOH A O   
2297 O  O   . HOH E .   ? 0.2408 0.2254 0.2007 -0.0035 0.0111  -0.0081 535 HOH A O   
2298 O  O   . HOH E .   ? 0.6722 0.4207 0.4874 -0.0421 0.2731  0.0638  536 HOH A O   
2299 O  O   . HOH E .   ? 0.1802 0.2190 0.1626 -0.0043 0.0273  0.0065  537 HOH A O   
2300 O  O   . HOH E .   ? 0.2978 0.5895 0.8504 0.1518  -0.0368 0.0270  538 HOH A O   
2301 O  O   . HOH E .   ? 0.4494 0.4058 0.7738 0.1238  -0.2701 -0.1244 539 HOH A O   
2302 O  O   . HOH E .   ? 0.1892 0.2106 0.2011 0.0181  -0.0041 0.0145  540 HOH A O   
2303 O  O   . HOH E .   ? 0.1174 0.1935 0.3738 -0.0392 -0.0441 0.0043  541 HOH A O   
2304 O  O   . HOH E .   ? 0.1777 0.3477 0.2855 0.0252  0.0022  0.0419  542 HOH A O   
2305 O  O   . HOH E .   ? 0.1872 0.2816 0.2150 0.0199  0.0299  0.0103  543 HOH A O   
2306 O  O   . HOH E .   ? 0.3462 0.4892 0.4156 -0.1525 -0.0832 0.2192  544 HOH A O   
2307 O  O   . HOH E .   ? 0.2799 0.2651 0.2872 0.0268  0.0368  0.0483  545 HOH A O   
2308 O  O   . HOH E .   ? 0.4899 0.2888 0.1944 -0.1124 -0.0639 0.0046  546 HOH A O   
2309 O  O   . HOH E .   ? 0.3310 0.1759 0.2656 0.0223  -0.0387 -0.0115 547 HOH A O   
2310 O  O   . HOH E .   ? 0.7598 0.7731 0.7367 -0.3208 0.0737  -0.5334 548 HOH A O   
2311 O  O   . HOH E .   ? 0.0747 0.2247 0.1891 0.0221  0.0403  -0.0100 549 HOH A O   
2312 O  O   . HOH E .   ? 0.4242 0.6916 0.7385 -0.1199 -0.3245 0.1240  550 HOH A O   
2313 O  O   . HOH E .   ? 0.2545 0.4072 0.5622 -0.0607 0.1214  0.0482  551 HOH A O   
2314 O  O   . HOH E .   ? 0.3031 0.2330 0.2472 0.0403  0.1098  0.0006  552 HOH A O   
2315 O  O   . HOH E .   ? 0.1443 0.3711 0.3395 -0.0374 -0.0420 0.0229  553 HOH A O   
2316 O  O   . HOH E .   ? 0.4806 0.2582 0.1751 0.1069  0.0902  0.0044  554 HOH A O   
2317 O  O   . HOH E .   ? 0.2596 0.2359 0.1665 -0.0362 0.0044  -0.0078 555 HOH A O   
2318 O  O   . HOH E .   ? 0.3860 0.3643 0.3216 -0.0545 -0.0435 0.1644  556 HOH A O   
2319 O  O   . HOH E .   ? 0.1680 0.6224 0.3339 0.1169  -0.0026 -0.1877 557 HOH A O   
2320 O  O   . HOH E .   ? 0.1768 0.2074 0.2214 0.0179  0.0141  -0.0167 558 HOH A O   
2321 O  O   . HOH E .   ? 0.1567 0.1932 0.1956 -0.0086 0.0628  0.0030  559 HOH A O   
2322 O  O   . HOH E .   ? 0.4479 0.2716 0.2850 -0.0510 0.0501  0.0076  560 HOH A O   
2323 O  O   . HOH E .   ? 0.6427 1.0444 0.3026 -0.3990 0.0719  -0.1215 561 HOH A O   
2324 O  O   . HOH E .   ? 1.0691 0.2800 0.4739 -0.1394 0.3420  -0.0853 562 HOH A O   
2325 O  O   . HOH E .   ? 0.1389 0.4293 0.4444 0.0203  -0.0447 0.1671  563 HOH A O   
2326 O  O   . HOH E .   ? 0.6458 0.4588 0.3337 0.1289  -0.1367 -0.0305 564 HOH A O   
2327 O  O   . HOH E .   ? 0.7222 0.6757 0.2852 -0.0949 0.0766  -0.2218 565 HOH A O   
2328 O  O   . HOH E .   ? 0.3582 0.2946 0.2160 -0.0082 0.0229  -0.0381 566 HOH A O   
2329 O  O   . HOH E .   ? 0.4573 0.3202 0.3453 -0.1312 0.0955  -0.0120 567 HOH A O   
2330 O  O   . HOH E .   ? 0.2237 0.2075 0.2136 0.0176  0.0772  0.0607  568 HOH A O   
2331 O  O   . HOH E .   ? 0.3741 0.2437 0.3902 0.1243  0.1851  0.0757  569 HOH A O   
2332 O  O   . HOH E .   ? 0.1856 0.1959 0.2172 0.0157  0.0113  -0.0635 570 HOH A O   
2333 O  O   . HOH E .   ? 0.3660 0.3844 0.2247 0.2148  0.0054  0.0022  571 HOH A O   
2334 O  O   . HOH E .   ? 0.2273 0.3367 0.2424 0.0792  0.1065  0.0397  572 HOH A O   
2335 O  O   . HOH E .   ? 0.4261 0.1902 0.2215 -0.0622 -0.0313 -0.0135 573 HOH A O   
2336 O  O   . HOH E .   ? 0.4724 0.3414 0.4995 -0.0974 0.0016  -0.0713 574 HOH A O   
2337 O  O   . HOH E .   ? 0.1386 0.3953 0.4008 0.0104  0.0604  0.1015  575 HOH A O   
2338 O  O   . HOH E .   ? 0.4256 1.0990 0.3572 -0.0366 -0.0372 0.2855  576 HOH A O   
2339 O  O   . HOH E .   ? 0.0985 0.2963 0.1666 -0.0216 -0.0287 0.0549  577 HOH A O   
2340 O  O   . HOH E .   ? 0.2776 0.3093 0.3410 0.0861  0.1416  0.0013  578 HOH A O   
2341 O  O   . HOH E .   ? 0.6142 0.5184 0.4809 -0.0906 -0.0680 0.2252  579 HOH A O   
2342 O  O   . HOH E .   ? 0.4262 0.3959 0.3080 0.0178  0.1322  -0.0075 580 HOH A O   
2343 O  O   . HOH E .   ? 0.5047 0.6382 0.3623 -0.1039 0.0565  0.0160  581 HOH A O   
2344 O  O   . HOH E .   ? 0.3768 0.2384 0.2972 0.1007  0.0692  0.0489  582 HOH A O   
2345 O  O   . HOH E .   ? 0.1578 0.2311 0.3039 -0.1005 -0.0004 -0.0366 583 HOH A O   
2346 O  O   . HOH E .   ? 0.5231 0.3209 1.0226 -0.1173 -0.4269 0.1394  584 HOH A O   
2347 O  O   . HOH E .   ? 0.3553 0.5319 0.6009 -0.0823 -0.0820 0.0148  585 HOH A O   
2348 O  O   . HOH E .   ? 0.2551 0.2754 0.3536 0.0024  0.1850  -0.0059 586 HOH A O   
2349 O  O   . HOH E .   ? 0.5148 0.2580 0.1906 0.1785  -0.0793 -0.0198 587 HOH A O   
2350 O  O   . HOH E .   ? 0.6322 0.3695 0.3759 -0.1498 0.3114  -0.0653 588 HOH A O   
2351 O  O   . HOH E .   ? 0.3911 0.9062 0.2300 -0.2430 0.0142  -0.0838 589 HOH A O   
2352 O  O   . HOH E .   ? 0.9081 0.3176 0.3517 0.0778  0.2813  0.0287  590 HOH A O   
2353 O  O   . HOH E .   ? 0.1905 0.3756 0.3713 0.0108  0.0324  0.1418  591 HOH A O   
2354 O  O   . HOH E .   ? 0.2847 0.8315 0.4141 0.2385  -0.0109 0.0961  592 HOH A O   
2355 O  O   . HOH E .   ? 0.1729 0.4290 0.5891 -0.0287 0.1754  0.0073  593 HOH A O   
2356 O  O   . HOH E .   ? 0.2340 0.2243 0.2437 0.0138  0.0174  0.0251  594 HOH A O   
2357 O  O   . HOH E .   ? 0.4334 0.3337 0.5052 -0.1723 0.3019  -0.1362 595 HOH A O   
2358 O  O   . HOH E .   ? 0.3302 0.2341 0.3153 0.0252  -0.0161 -0.0100 596 HOH A O   
2359 O  O   . HOH E .   ? 0.1474 0.3151 0.3860 0.0886  -0.0818 -0.0826 597 HOH A O   
2360 O  O   . HOH E .   ? 0.3078 0.4221 0.3154 0.0010  0.0709  0.0141  598 HOH A O   
2361 O  O   . HOH E .   ? 0.4383 0.3878 0.5848 0.1135  0.3043  0.0839  599 HOH A O   
2362 O  O   . HOH E .   ? 0.4365 0.5256 0.5108 0.0836  0.2410  -0.0027 600 HOH A O   
2363 O  O   . HOH E .   ? 0.3828 0.4608 0.5190 -0.2577 0.1802  -0.0804 601 HOH A O   
2364 O  O   . HOH E .   ? 0.5118 0.3055 0.2956 0.0279  -0.0186 -0.0515 602 HOH A O   
2365 O  O   . HOH E .   ? 0.3810 1.0339 0.8100 -0.1298 0.1811  0.1889  603 HOH A O   
2366 O  O   . HOH E .   ? 0.1651 0.2038 0.1985 -0.0523 -0.0082 0.0326  604 HOH A O   
2367 O  O   . HOH E .   ? 0.3917 0.2633 0.3034 0.1393  -0.0707 -0.0473 605 HOH A O   
2368 O  O   . HOH E .   ? 0.6351 0.2896 0.5410 -0.0724 0.1383  -0.0569 606 HOH A O   
2369 O  O   . HOH E .   ? 0.3810 0.4645 0.4254 0.0903  -0.1142 -0.1178 607 HOH A O   
2370 O  O   . HOH E .   ? 0.3092 0.3869 0.4683 -0.1410 -0.0173 0.1694  608 HOH A O   
2371 O  O   . HOH E .   ? 0.1806 0.1657 0.2597 0.0292  0.0275  -0.0402 609 HOH A O   
2372 O  O   . HOH E .   ? 0.4688 0.5602 0.1741 0.0541  0.0146  0.0282  610 HOH A O   
2373 O  O   . HOH E .   ? 0.4397 0.9811 0.6061 0.3738  0.0496  -0.0381 611 HOH A O   
2374 O  O   . HOH E .   ? 0.4886 0.2896 0.2643 -0.1402 -0.0719 0.0381  612 HOH A O   
2375 O  O   . HOH E .   ? 0.3674 0.3761 0.3118 0.1584  -0.0356 -0.0352 613 HOH A O   
2376 O  O   . HOH E .   ? 0.0973 0.1447 0.1567 0.0212  0.0290  -0.0076 614 HOH A O   
2377 O  O   . HOH E .   ? 0.8991 0.4050 0.6438 -0.3671 0.2163  -0.0678 615 HOH A O   
2378 O  O   . HOH E .   ? 0.2194 0.3806 0.2873 0.0476  -0.0043 0.0227  616 HOH A O   
2379 O  O   . HOH E .   ? 0.7799 0.5317 0.4459 -0.0666 -0.1983 0.0788  617 HOH A O   
2380 O  O   . HOH E .   ? 0.3849 0.2958 0.2106 0.1357  0.0922  -0.0264 618 HOH A O   
2381 O  O   . HOH E .   ? 0.3923 0.3116 0.5596 -0.0677 -0.1180 -0.0446 619 HOH A O   
2382 O  O   . HOH E .   ? 0.0934 0.2160 0.2692 -0.0131 0.0166  0.0078  620 HOH A O   
2383 O  O   . HOH E .   ? 0.5382 0.5299 0.3373 0.2319  -0.1918 -0.1240 621 HOH A O   
2384 O  O   . HOH E .   ? 0.4123 0.4766 0.2465 -0.0453 0.1179  0.1768  622 HOH A O   
2385 O  O   . HOH E .   ? 0.1813 0.2888 0.9737 0.0069  0.1061  -0.0500 623 HOH A O   
2386 O  O   . HOH E .   ? 1.0359 0.3586 0.2619 -0.0828 0.0272  0.0570  624 HOH A O   
2387 O  O   . HOH E .   ? 0.3155 0.2050 0.3554 0.0772  0.1626  0.0911  625 HOH A O   
2388 O  O   . HOH E .   ? 0.2423 0.2348 0.3160 0.1147  0.0447  0.0373  626 HOH A O   
2389 O  O   . HOH E .   ? 0.4455 0.6261 0.3376 0.0607  0.0418  0.0960  627 HOH A O   
2390 O  O   . HOH E .   ? 0.3861 0.3629 0.7088 -0.0671 0.1087  0.0373  628 HOH A O   
2391 O  O   . HOH E .   ? 0.3691 0.5747 0.5369 0.2645  0.1939  0.1752  629 HOH A O   
2392 O  O   . HOH E .   ? 0.3043 0.4428 0.4560 -0.0074 -0.0047 -0.0884 630 HOH A O   
2393 O  O   . HOH E .   ? 0.5123 0.2834 0.4986 -0.0171 0.2600  0.0445  631 HOH A O   
2394 O  O   . HOH E .   ? 0.5107 0.4714 0.8462 -0.1013 -0.0837 0.2317  632 HOH A O   
2395 O  O   . HOH E .   ? 0.5863 0.6436 0.3238 -0.0122 0.1570  0.0759  633 HOH A O   
2396 O  O   . HOH E .   ? 0.1253 0.5862 0.2896 0.1064  0.0572  0.0697  634 HOH A O   
2397 O  O   . HOH E .   ? 0.4336 0.6506 0.3626 -0.0232 -0.0243 -0.2405 635 HOH A O   
2398 O  O   . HOH E .   ? 0.6111 0.4433 0.3843 0.1657  0.0058  0.0427  636 HOH A O   
2399 O  O   . HOH E .   ? 0.6470 0.5949 0.3626 -0.2399 0.0463  0.0079  637 HOH A O   
2400 O  O   . HOH E .   ? 0.5689 0.8800 0.6297 0.3995  -0.0212 -0.2376 638 HOH A O   
2401 O  O   . HOH E .   ? 0.8001 0.3525 0.7644 -0.0348 -0.2458 -0.0651 639 HOH A O   
2402 O  O   . HOH E .   ? 0.5710 0.7845 0.5583 -0.2757 -0.2041 -0.0820 640 HOH A O   
2403 O  O   . HOH E .   ? 0.4747 0.3404 0.2937 -0.1307 0.1398  0.0826  641 HOH A O   
2404 O  O   . HOH E .   ? 0.2806 0.5729 0.5035 0.0904  0.0345  0.2097  642 HOH A O   
2405 O  O   . HOH E .   ? 0.2598 0.3873 0.4442 -0.0372 0.1570  -0.0765 643 HOH A O   
2406 O  O   . HOH E .   ? 0.5194 0.6002 0.6103 -0.0208 0.3193  -0.0977 644 HOH A O   
2407 O  O   . HOH E .   ? 0.1402 0.1567 0.1773 -0.0227 0.0139  -0.0117 645 HOH A O   
2408 O  O   . HOH E .   ? 0.6850 0.9127 0.2204 0.3279  0.0255  0.0171  646 HOH A O   
2409 O  O   . HOH E .   ? 0.3974 0.8554 0.7756 0.2458  -0.0655 -0.2841 647 HOH A O   
2410 O  O   . HOH E .   ? 0.2676 0.3116 0.4807 0.0209  0.1072  0.0231  648 HOH A O   
2411 O  O   . HOH E .   ? 0.3071 0.8445 0.3805 0.0536  0.0805  -0.2538 649 HOH A O   
2412 O  O   . HOH E .   ? 0.8840 0.2825 0.4052 0.0885  0.1144  -0.0288 650 HOH A O   
2413 O  O   . HOH E .   ? 0.1945 0.2057 0.1863 -0.0419 0.0384  0.0156  651 HOH A O   
2414 O  O   . HOH E .   ? 0.2867 0.4012 0.5125 -0.0915 0.0011  -0.0867 652 HOH A O   
2415 O  O   . HOH E .   ? 0.3030 0.5582 0.7069 -0.0774 -0.0111 0.2705  653 HOH A O   
2416 O  O   . HOH E .   ? 0.2416 0.3103 0.4341 -0.0188 0.0615  -0.0343 654 HOH A O   
2417 O  O   . HOH E .   ? 0.1522 0.3616 0.3146 -0.0100 -0.0133 -0.0038 655 HOH A O   
2418 O  O   . HOH E .   ? 0.9237 1.4558 0.5928 0.6540  0.4374  0.4569  656 HOH A O   
2419 O  O   . HOH E .   ? 0.6646 0.4690 0.3352 0.1547  0.0279  0.0996  657 HOH A O   
2420 O  O   . HOH E .   ? 0.6595 0.4624 0.7702 -0.1268 0.0302  -0.2843 658 HOH A O   
2421 O  O   . HOH E .   ? 1.3202 0.6338 0.4893 0.3439  -0.4099 -0.0820 659 HOH A O   
2422 O  O   . HOH E .   ? 0.4679 0.6661 0.8580 0.3057  -0.3265 -0.3960 660 HOH A O   
2423 O  O   . HOH E .   ? 0.3212 0.3491 0.6171 0.0963  -0.1846 -0.0829 661 HOH A O   
2424 O  O   . HOH E .   ? 0.3647 0.3797 0.4276 0.0685  0.2195  -0.0149 662 HOH A O   
2425 O  O   . HOH E .   ? 0.3533 0.8693 0.5790 0.0863  -0.0193 -0.1667 663 HOH A O   
2426 O  O   . HOH E .   ? 0.2748 0.4389 0.2351 -0.0600 0.0354  0.1014  664 HOH A O   
2427 O  O   . HOH E .   ? 0.2949 0.3209 0.3334 -0.0864 -0.0335 0.0780  665 HOH A O   
2428 O  O   . HOH E .   ? 0.8102 0.4244 0.4772 0.1847  0.1694  0.0234  666 HOH A O   
2429 O  O   . HOH E .   ? 0.5051 0.2669 0.5305 -0.0661 -0.1613 0.0717  667 HOH A O   
2430 O  O   . HOH E .   ? 0.4483 0.6803 0.7930 0.1914  0.0197  0.4359  668 HOH A O   
2431 O  O   . HOH E .   ? 0.1164 0.3523 0.3779 0.0842  0.0705  -0.0313 669 HOH A O   
2432 O  O   . HOH E .   ? 0.1826 0.4766 0.5163 0.1111  0.0196  -0.0889 670 HOH A O   
2433 O  O   . HOH E .   ? 0.2304 0.6156 0.3461 -0.0778 0.0234  0.0277  671 HOH A O   
2434 O  O   . HOH E .   ? 0.4215 0.2827 0.3870 0.0027  0.1357  -0.0581 672 HOH A O   
2435 O  O   . HOH E .   ? 0.2882 0.3635 0.2377 -0.0983 -0.0021 0.0271  673 HOH A O   
2436 O  O   . HOH E .   ? 0.3489 0.2420 0.3262 0.0848  -0.1000 -0.0231 674 HOH A O   
2437 O  O   . HOH E .   ? 0.4413 0.4782 0.3541 0.0850  0.0078  0.1004  675 HOH A O   
2438 O  O   . HOH E .   ? 0.3071 0.2988 0.5202 0.1016  0.1974  0.1412  676 HOH A O   
2439 O  O   . HOH E .   ? 0.3895 0.3927 0.2627 -0.0436 0.0274  0.0647  677 HOH A O   
2440 O  O   . HOH E .   ? 0.2135 0.3896 0.2913 -0.0262 0.0506  -0.0217 678 HOH A O   
2441 O  O   . HOH E .   ? 0.2760 0.3729 0.3213 0.1708  0.0144  -0.0269 679 HOH A O   
2442 O  O   . HOH E .   ? 0.4541 0.4348 0.3025 -0.0951 -0.0412 0.1007  680 HOH A O   
2443 O  O   . HOH E .   ? 0.7074 0.3536 0.7284 0.0184  -0.4086 -0.0614 681 HOH A O   
2444 O  O   . HOH E .   ? 0.2942 0.5775 0.5601 -0.1596 -0.0901 0.2457  682 HOH A O   
2445 O  O   . HOH E .   ? 0.8093 0.3763 0.3959 0.1148  0.0983  -0.0456 683 HOH A O   
2446 O  O   . HOH E .   ? 0.3120 0.5874 0.2605 0.0044  0.0366  -0.0731 684 HOH A O   
2447 O  O   . HOH E .   ? 0.1787 0.2690 0.2957 -0.0116 0.0630  0.0215  685 HOH A O   
2448 O  O   . HOH E .   ? 0.2793 0.3075 0.3864 -0.0785 0.0796  0.0156  686 HOH A O   
2449 O  O   . HOH E .   ? 0.2745 0.3269 0.6467 -0.0365 -0.0231 0.0631  687 HOH A O   
2450 O  O   . HOH E .   ? 0.3422 0.4290 0.2947 0.0739  -0.0646 -0.1523 688 HOH A O   
2451 O  O   . HOH E .   ? 0.2129 0.4971 0.4965 -0.1077 0.1203  -0.0150 689 HOH A O   
2452 O  O   . HOH E .   ? 0.4054 0.3467 1.0402 -0.0917 -0.1779 0.0544  690 HOH A O   
2453 O  O   . HOH E .   ? 0.3510 0.4069 0.2780 0.1193  -0.0324 -0.0215 691 HOH A O   
2454 O  O   . HOH E .   ? 0.2645 0.2587 0.3520 -0.0217 -0.0522 0.0214  692 HOH A O   
2455 O  O   . HOH E .   ? 0.5776 0.5434 0.7727 0.0790  -0.2470 -0.0524 693 HOH A O   
2456 O  O   . HOH E .   ? 0.2484 0.7263 0.5430 0.0136  0.0316  -0.3268 694 HOH A O   
2457 O  O   . HOH E .   ? 0.2244 0.5859 0.2540 0.1200  -0.0185 0.0023  695 HOH A O   
2458 O  O   . HOH E .   ? 0.1913 0.3402 0.6513 0.0240  -0.0062 0.0795  696 HOH A O   
2459 O  O   . HOH E .   ? 0.6197 0.7503 0.5295 0.2066  -0.3574 -0.1807 697 HOH A O   
2460 O  O   . HOH E .   ? 0.1946 0.3834 0.1757 0.0023  0.0469  0.0091  698 HOH A O   
2461 O  O   . HOH E .   ? 0.7982 0.2568 0.4479 0.0736  0.0052  -0.0458 699 HOH A O   
2462 O  O   . HOH E .   ? 0.4370 0.3992 0.8967 -0.0703 0.1667  0.1032  700 HOH A O   
2463 O  O   . HOH E .   ? 0.3187 0.2528 0.2169 -0.0318 0.0653  0.0012  701 HOH A O   
2464 O  O   . HOH E .   ? 0.3805 0.2922 1.2361 0.0907  -0.0003 0.0455  702 HOH A O   
2465 O  O   . HOH E .   ? 0.5285 0.9180 0.4389 -0.1178 -0.0834 -0.4320 703 HOH A O   
2466 O  O   . HOH E .   ? 0.6613 0.2763 0.2933 -0.0397 0.0509  -0.0115 704 HOH A O   
2467 O  O   . HOH E .   ? 0.2998 0.5113 0.4694 -0.0749 0.0271  0.1301  705 HOH A O   
2468 O  O   . HOH E .   ? 0.2956 0.1772 0.4441 0.0310  0.1701  0.0006  706 HOH A O   
2469 O  O   . HOH E .   ? 0.8705 0.3978 0.4165 -0.1415 0.0610  -0.0241 707 HOH A O   
2470 O  O   . HOH E .   ? 0.5290 0.3510 0.8467 -0.0038 0.3856  0.0330  708 HOH A O   
2471 O  O   . HOH E .   ? 0.3381 0.3618 0.3967 0.0542  0.0696  -0.0270 709 HOH A O   
2472 O  O   . HOH E .   ? 0.3177 0.5974 0.6440 0.0706  0.1459  0.3255  710 HOH A O   
2473 O  O   . HOH E .   ? 0.9311 0.5210 0.5195 -0.3861 -0.0392 0.0990  711 HOH A O   
2474 O  O   . HOH E .   ? 0.1571 0.2653 0.2258 0.0425  -0.0215 0.0081  712 HOH A O   
2475 O  O   . HOH E .   ? 0.4284 0.2963 0.5440 -0.0809 0.0511  -0.0974 713 HOH A O   
2476 O  O   . HOH E .   ? 0.6359 0.7491 0.4641 -0.3292 -0.0636 0.1194  714 HOH A O   
2477 O  O   . HOH E .   ? 0.3007 0.4665 0.5901 -0.0816 -0.0491 0.1674  715 HOH A O   
2478 O  O   . HOH E .   ? 0.7160 0.6228 0.6635 -0.2490 -0.2405 0.2606  716 HOH A O   
2479 O  O   . HOH E .   ? 0.4034 0.3001 0.6736 0.0748  0.1253  0.0032  717 HOH A O   
2480 O  O   . HOH E .   ? 0.3951 0.4038 0.7153 -0.1409 0.1114  -0.0585 718 HOH A O   
2481 O  O   . HOH E .   ? 0.5586 0.4693 0.4156 0.2576  -0.1842 0.0648  719 HOH A O   
2482 O  O   . HOH E .   ? 0.4868 0.4585 0.8586 -0.2315 -0.0952 0.2192  720 HOH A O   
2483 O  O   . HOH E .   ? 0.3835 0.3245 0.8810 -0.1826 -0.2798 0.0576  721 HOH A O   
2484 O  O   . HOH E .   ? 0.3335 0.4762 0.3199 0.1600  0.0506  -0.0284 722 HOH A O   
2485 O  O   . HOH E .   ? 0.3674 0.5590 0.4565 -0.2977 -0.0506 0.2676  723 HOH A O   
2486 O  O   . HOH E .   ? 0.4609 0.5159 0.8133 0.2509  -0.1637 -0.0239 724 HOH A O   
2487 O  O   . HOH E .   ? 0.5840 0.3360 0.3957 0.1054  0.1245  0.0648  725 HOH A O   
2488 O  O   . HOH E .   ? 0.4523 0.7508 0.3295 -0.0528 0.0544  -0.2770 726 HOH A O   
2489 O  O   . HOH E .   ? 0.7126 0.3550 0.3295 0.1472  -0.0083 -0.0417 727 HOH A O   
2490 O  O   . HOH E .   ? 0.6271 0.4974 0.6580 0.0020  -0.3168 -0.1787 728 HOH A O   
2491 O  O   . HOH E .   ? 0.5308 0.5479 0.4487 -0.1360 -0.1542 -0.0408 729 HOH A O   
2492 O  O   . HOH E .   ? 0.4322 0.3519 0.7536 0.0097  -0.1909 -0.1636 730 HOH A O   
2493 O  O   . HOH E .   ? 0.7070 0.6982 0.5287 0.2626  -0.0450 -0.0761 731 HOH A O   
2494 O  O   . HOH E .   ? 0.2595 0.5364 0.6930 0.0468  -0.0130 0.1229  732 HOH A O   
2495 O  O   . HOH E .   ? 0.2762 1.0355 0.5955 -0.1582 -0.0500 0.1861  733 HOH A O   
2496 O  O   . HOH E .   ? 0.2301 0.7843 0.5453 0.1272  0.1018  0.0304  734 HOH A O   
2497 O  O   . HOH E .   ? 1.0064 0.5387 0.4294 -0.2791 0.2392  -0.1546 735 HOH A O   
2498 O  O   . HOH E .   ? 0.5018 0.7882 0.9478 -0.3186 0.0438  0.1527  736 HOH A O   
2499 O  O   . HOH E .   ? 0.5887 0.5486 0.4176 -0.0005 -0.2060 0.1710  737 HOH A O   
2500 O  O   . HOH E .   ? 0.1829 0.8414 0.6089 0.1768  -0.0220 -0.2252 738 HOH A O   
2501 O  O   . HOH E .   ? 1.4045 0.3554 0.6795 -0.1270 -0.1427 -0.0442 739 HOH A O   
2502 O  O   . HOH E .   ? 0.5812 0.3444 1.1269 0.1276  0.0210  -0.0418 740 HOH A O   
# 
