data_5LLC
# 
_entry.id   5LLC 
# 
_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   5LLC         pdb_00005llc 10.2210/pdb5llc/pdb 
WWPDB D_1200000948 ?            ?                   
# 
loop_
_pdbx_audit_revision_history.ordinal 
_pdbx_audit_revision_history.data_content_type 
_pdbx_audit_revision_history.major_revision 
_pdbx_audit_revision_history.minor_revision 
_pdbx_audit_revision_history.revision_date 
1 'Structure model' 1 0 2017-08-16 
2 'Structure model' 1 1 2018-05-16 
3 'Structure model' 1 2 2024-01-10 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
loop_
_pdbx_audit_revision_group.ordinal 
_pdbx_audit_revision_group.revision_ordinal 
_pdbx_audit_revision_group.data_content_type 
_pdbx_audit_revision_group.group 
1 2 'Structure model' 'Data collection'        
2 2 'Structure model' 'Database references'    
3 3 'Structure model' 'Data collection'        
4 3 'Structure model' 'Database references'    
5 3 'Structure model' 'Refinement description' 
# 
loop_
_pdbx_audit_revision_category.ordinal 
_pdbx_audit_revision_category.revision_ordinal 
_pdbx_audit_revision_category.data_content_type 
_pdbx_audit_revision_category.category 
1 2 'Structure model' citation                      
2 2 'Structure model' citation_author               
3 3 'Structure model' chem_comp_atom                
4 3 'Structure model' chem_comp_bond                
5 3 'Structure model' database_2                    
6 3 'Structure model' diffrn_radiation_wavelength   
7 3 '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.country'                   
2  2 'Structure model' '_citation.journal_abbrev'            
3  2 'Structure model' '_citation.journal_id_CSD'            
4  2 'Structure model' '_citation.journal_id_ISSN'           
5  2 'Structure model' '_citation.journal_volume'            
6  2 'Structure model' '_citation.page_first'                
7  2 'Structure model' '_citation.page_last'                 
8  2 'Structure model' '_citation.pdbx_database_id_DOI'      
9  2 'Structure model' '_citation.pdbx_database_id_PubMed'   
10 2 'Structure model' '_citation.title'                     
11 2 'Structure model' '_citation.year'                      
12 3 'Structure model' '_database_2.pdbx_DOI'                
13 3 '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                        5LLC 
_pdbx_database_status.recvd_initial_deposition_date   2016-07-27 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBE 
_pdbx_database_status.process_site                    PDBE 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
_pdbx_database_status.status_code_nmr_data            ? 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
'Manakova, E.' 1 
'Smirnov, A.'  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                   US 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            PeerJ 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            ? 
_citation.journal_id_ISSN           2167-8359 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            6 
_citation.language                  ? 
_citation.page_first                e4412 
_citation.page_last                 e4412 
_citation.title                     
'Crystal structure correlations with the intrinsic thermodynamics of human carbonic anhydrase inhibitor binding.' 
_citation.year                      2018 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.7717/peerj.4412 
_citation.pdbx_database_id_PubMed   29503769 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Smirnov, A.'  1 ? 
primary 'Zubriene, A.' 2 ? 
primary 'Manakova, E.' 3 ? 
primary 'Grazulis, S.' 4 ? 
primary 'Matulis, D.'  5 ? 
# 
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-(1,3-Benzothiazol-2-ylthio)-2,3,5,6-tetra uorobenzenesulfonamide' ? 
3 non-polymer syn 'DIMETHYL SULFOXIDE'                                                                78.133    2   ?       ? Zn ? 
4 non-polymer syn 1,2-ETHANEDIOL                                                                      62.068    4   ?       ? DMS 
? 
5 non-polymer syn '2,3,6-tris(fluoranyl)-5-(methylamino)-4-(2-phenylethylsulfonyl)benzenesulfonamide' 408.416   1   ?       ? EDO 
? 
6 water       nat water                                                                               18.015    302 ?       ? ? ? 
# 
_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 'DIMETHYL SULFOXIDE'                                                                DMS 
4 1,2-ETHANEDIOL                                                                      EDO 
5 '2,3,6-tris(fluoranyl)-5-(methylamino)-4-(2-phenylethylsulfonyl)benzenesulfonamide' V26 
6 water                                                                               HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   MET n 
1 2   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  
EDO non-polymer         . 1,2-ETHANEDIOL                                                                      'ETHYLENE GLYCOL' 
'C2 H6 O2'            62.068  
GLN 'L-peptide linking' y GLUTAMINE                                                                           ?                 
'C5 H10 N2 O3'        146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID'                                                                     ?                 
'C5 H9 N O4'          147.129 
GLY 'peptide linking'   y GLYCINE                                                                             ?                 
'C2 H5 N O2'          75.067  
HIS 'L-peptide linking' y HISTIDINE                                                                           ?                 
'C6 H10 N3 O2 1'      156.162 
HOH non-polymer         . WATER                                                                               ?                 
'H2 O'                18.015  
ILE 'L-peptide linking' y ISOLEUCINE                                                                          ?                 
'C6 H13 N O2'         131.173 
LEU 'L-peptide linking' y LEUCINE                                                                             ?                 
'C6 H13 N O2'         131.173 
LYS 'L-peptide linking' y LYSINE                                                                              ?                 
'C6 H15 N2 O2 1'      147.195 
MET 'L-peptide linking' y METHIONINE                                                                          ?                 
'C5 H11 N O2 S'       149.211 
PHE 'L-peptide linking' y PHENYLALANINE                                                                       ?                 
'C9 H11 N O2'         165.189 
PRO 'L-peptide linking' y PROLINE                                                                             ?                 
'C5 H9 N O2'          115.130 
SER 'L-peptide linking' y SERINE                                                                              ?                 
'C3 H7 N O3'          105.093 
THR 'L-peptide linking' y THREONINE                                                                           ?                 
'C4 H9 N O3'          119.119 
TRP 'L-peptide linking' y TRYPTOPHAN                                                                          ?                 
'C11 H12 N2 O2'       204.225 
TYR 'L-peptide linking' y TYROSINE                                                                            ?                 
'C9 H11 N O3'         181.189 
V26 non-polymer         . '2,3,6-tris(fluoranyl)-5-(methylamino)-4-(2-phenylethylsulfonyl)benzenesulfonamide' ?                 
'C15 H15 F3 N2 O4 S2' 408.416 
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 DMS 1   302 1   DMS DMS A . 
D 3 DMS 1   303 2   DMS DMS A . 
E 4 EDO 1   304 1   EDO EDO A . 
F 4 EDO 1   305 2   EDO EDO A . 
G 4 EDO 1   306 3   EDO EDO A . 
H 4 EDO 1   307 4   EDO EDO A . 
I 5 V26 1   308 1   V26 V26 A . 
J 6 HOH 1   401 235 HOH HOH A . 
J 6 HOH 2   402 172 HOH HOH A . 
J 6 HOH 3   403 298 HOH HOH A . 
J 6 HOH 4   404 300 HOH HOH A . 
J 6 HOH 5   405 290 HOH HOH A . 
J 6 HOH 6   406 214 HOH HOH A . 
J 6 HOH 7   407 135 HOH HOH A . 
J 6 HOH 8   408 133 HOH HOH A . 
J 6 HOH 9   409 222 HOH HOH A . 
J 6 HOH 10  410 275 HOH HOH A . 
J 6 HOH 11  411 111 HOH HOH A . 
J 6 HOH 12  412 233 HOH HOH A . 
J 6 HOH 13  413 9   HOH HOH A . 
J 6 HOH 14  414 77  HOH HOH A . 
J 6 HOH 15  415 49  HOH HOH A . 
J 6 HOH 16  416 203 HOH HOH A . 
J 6 HOH 17  417 194 HOH HOH A . 
J 6 HOH 18  418 168 HOH HOH A . 
J 6 HOH 19  419 167 HOH HOH A . 
J 6 HOH 20  420 255 HOH HOH A . 
J 6 HOH 21  421 171 HOH HOH A . 
J 6 HOH 22  422 18  HOH HOH A . 
J 6 HOH 23  423 297 HOH HOH A . 
J 6 HOH 24  424 38  HOH HOH A . 
J 6 HOH 25  425 160 HOH HOH A . 
J 6 HOH 26  426 228 HOH HOH A . 
J 6 HOH 27  427 302 HOH HOH A . 
J 6 HOH 28  428 97  HOH HOH A . 
J 6 HOH 29  429 102 HOH HOH A . 
J 6 HOH 30  430 159 HOH HOH A . 
J 6 HOH 31  431 118 HOH HOH A . 
J 6 HOH 32  432 76  HOH HOH A . 
J 6 HOH 33  433 90  HOH HOH A . 
J 6 HOH 34  434 122 HOH HOH A . 
J 6 HOH 35  435 157 HOH HOH A . 
J 6 HOH 36  436 262 HOH HOH A . 
J 6 HOH 37  437 81  HOH HOH A . 
J 6 HOH 38  438 232 HOH HOH A . 
J 6 HOH 39  439 94  HOH HOH A . 
J 6 HOH 40  440 250 HOH HOH A . 
J 6 HOH 41  441 13  HOH HOH A . 
J 6 HOH 42  442 20  HOH HOH A . 
J 6 HOH 43  443 45  HOH HOH A . 
J 6 HOH 44  444 225 HOH HOH A . 
J 6 HOH 45  445 84  HOH HOH A . 
J 6 HOH 46  446 151 HOH HOH A . 
J 6 HOH 47  447 113 HOH HOH A . 
J 6 HOH 48  448 249 HOH HOH A . 
J 6 HOH 49  449 164 HOH HOH A . 
J 6 HOH 50  450 3   HOH HOH A . 
J 6 HOH 51  451 121 HOH HOH A . 
J 6 HOH 52  452 87  HOH HOH A . 
J 6 HOH 53  453 21  HOH HOH A . 
J 6 HOH 54  454 288 HOH HOH A . 
J 6 HOH 55  455 141 HOH HOH A . 
J 6 HOH 56  456 23  HOH HOH A . 
J 6 HOH 57  457 128 HOH HOH A . 
J 6 HOH 58  458 231 HOH HOH A . 
J 6 HOH 59  459 119 HOH HOH A . 
J 6 HOH 60  460 54  HOH HOH A . 
J 6 HOH 61  461 31  HOH HOH A . 
J 6 HOH 62  462 179 HOH HOH A . 
J 6 HOH 63  463 67  HOH HOH A . 
J 6 HOH 64  464 5   HOH HOH A . 
J 6 HOH 65  465 279 HOH HOH A . 
J 6 HOH 66  466 192 HOH HOH A . 
J 6 HOH 67  467 185 HOH HOH A . 
J 6 HOH 68  468 7   HOH HOH A . 
J 6 HOH 69  469 163 HOH HOH A . 
J 6 HOH 70  470 204 HOH HOH A . 
J 6 HOH 71  471 116 HOH HOH A . 
J 6 HOH 72  472 109 HOH HOH A . 
J 6 HOH 73  473 205 HOH HOH A . 
J 6 HOH 74  474 127 HOH HOH A . 
J 6 HOH 75  475 93  HOH HOH A . 
J 6 HOH 76  476 181 HOH HOH A . 
J 6 HOH 77  477 69  HOH HOH A . 
J 6 HOH 78  478 30  HOH HOH A . 
J 6 HOH 79  479 158 HOH HOH A . 
J 6 HOH 80  480 43  HOH HOH A . 
J 6 HOH 81  481 79  HOH HOH A . 
J 6 HOH 82  482 200 HOH HOH A . 
J 6 HOH 83  483 125 HOH HOH A . 
J 6 HOH 84  484 145 HOH HOH A . 
J 6 HOH 85  485 57  HOH HOH A . 
J 6 HOH 86  486 2   HOH HOH A . 
J 6 HOH 87  487 1   HOH HOH A . 
J 6 HOH 88  488 11  HOH HOH A . 
J 6 HOH 89  489 202 HOH HOH A . 
J 6 HOH 90  490 59  HOH HOH A . 
J 6 HOH 91  491 34  HOH HOH A . 
J 6 HOH 92  492 51  HOH HOH A . 
J 6 HOH 93  493 234 HOH HOH A . 
J 6 HOH 94  494 56  HOH HOH A . 
J 6 HOH 95  495 190 HOH HOH A . 
J 6 HOH 96  496 10  HOH HOH A . 
J 6 HOH 97  497 223 HOH HOH A . 
J 6 HOH 98  498 106 HOH HOH A . 
J 6 HOH 99  499 120 HOH HOH A . 
J 6 HOH 100 500 8   HOH HOH A . 
J 6 HOH 101 501 47  HOH HOH A . 
J 6 HOH 102 502 46  HOH HOH A . 
J 6 HOH 103 503 24  HOH HOH A . 
J 6 HOH 104 504 15  HOH HOH A . 
J 6 HOH 105 505 98  HOH HOH A . 
J 6 HOH 106 506 148 HOH HOH A . 
J 6 HOH 107 507 26  HOH HOH A . 
J 6 HOH 108 508 178 HOH HOH A . 
J 6 HOH 109 509 170 HOH HOH A . 
J 6 HOH 110 510 99  HOH HOH A . 
J 6 HOH 111 511 39  HOH HOH A . 
J 6 HOH 112 512 19  HOH HOH A . 
J 6 HOH 113 513 6   HOH HOH A . 
J 6 HOH 114 514 36  HOH HOH A . 
J 6 HOH 115 515 65  HOH HOH A . 
J 6 HOH 116 516 283 HOH HOH A . 
J 6 HOH 117 517 60  HOH HOH A . 
J 6 HOH 118 518 266 HOH HOH A . 
J 6 HOH 119 519 115 HOH HOH A . 
J 6 HOH 120 520 42  HOH HOH A . 
J 6 HOH 121 521 152 HOH HOH A . 
J 6 HOH 122 522 41  HOH HOH A . 
J 6 HOH 123 523 74  HOH HOH A . 
J 6 HOH 124 524 91  HOH HOH A . 
J 6 HOH 125 525 110 HOH HOH A . 
J 6 HOH 126 526 184 HOH HOH A . 
J 6 HOH 127 527 33  HOH HOH A . 
J 6 HOH 128 528 73  HOH HOH A . 
J 6 HOH 129 529 138 HOH HOH A . 
J 6 HOH 130 530 187 HOH HOH A . 
J 6 HOH 131 531 22  HOH HOH A . 
J 6 HOH 132 532 63  HOH HOH A . 
J 6 HOH 133 533 206 HOH HOH A . 
J 6 HOH 134 534 260 HOH HOH A . 
J 6 HOH 135 535 117 HOH HOH A . 
J 6 HOH 136 536 92  HOH HOH A . 
J 6 HOH 137 537 89  HOH HOH A . 
J 6 HOH 138 538 230 HOH HOH A . 
J 6 HOH 139 539 124 HOH HOH A . 
J 6 HOH 140 540 28  HOH HOH A . 
J 6 HOH 141 541 294 HOH HOH A . 
J 6 HOH 142 542 229 HOH HOH A . 
J 6 HOH 143 543 72  HOH HOH A . 
J 6 HOH 144 544 61  HOH HOH A . 
J 6 HOH 145 545 103 HOH HOH A . 
J 6 HOH 146 546 25  HOH HOH A . 
J 6 HOH 147 547 105 HOH HOH A . 
J 6 HOH 148 548 143 HOH HOH A . 
J 6 HOH 149 549 29  HOH HOH A . 
J 6 HOH 150 550 142 HOH HOH A . 
J 6 HOH 151 551 112 HOH HOH A . 
J 6 HOH 152 552 53  HOH HOH A . 
J 6 HOH 153 553 12  HOH HOH A . 
J 6 HOH 154 554 75  HOH HOH A . 
J 6 HOH 155 555 299 HOH HOH A . 
J 6 HOH 156 556 227 HOH HOH A . 
J 6 HOH 157 557 114 HOH HOH A . 
J 6 HOH 158 558 207 HOH HOH A . 
J 6 HOH 159 559 35  HOH HOH A . 
J 6 HOH 160 560 32  HOH HOH A . 
J 6 HOH 161 561 62  HOH HOH A . 
J 6 HOH 162 562 139 HOH HOH A . 
J 6 HOH 163 563 55  HOH HOH A . 
J 6 HOH 164 564 242 HOH HOH A . 
J 6 HOH 165 565 180 HOH HOH A . 
J 6 HOH 166 566 291 HOH HOH A . 
J 6 HOH 167 567 198 HOH HOH A . 
J 6 HOH 168 568 68  HOH HOH A . 
J 6 HOH 169 569 199 HOH HOH A . 
J 6 HOH 170 570 27  HOH HOH A . 
J 6 HOH 171 571 146 HOH HOH A . 
J 6 HOH 172 572 40  HOH HOH A . 
J 6 HOH 173 573 131 HOH HOH A . 
J 6 HOH 174 574 226 HOH HOH A . 
J 6 HOH 175 575 263 HOH HOH A . 
J 6 HOH 176 576 85  HOH HOH A . 
J 6 HOH 177 577 14  HOH HOH A . 
J 6 HOH 178 578 191 HOH HOH A . 
J 6 HOH 179 579 169 HOH HOH A . 
J 6 HOH 180 580 104 HOH HOH A . 
J 6 HOH 181 581 64  HOH HOH A . 
J 6 HOH 182 582 153 HOH HOH A . 
J 6 HOH 183 583 4   HOH HOH A . 
J 6 HOH 184 584 189 HOH HOH A . 
J 6 HOH 185 585 101 HOH HOH A . 
J 6 HOH 186 586 161 HOH HOH A . 
J 6 HOH 187 587 16  HOH HOH A . 
J 6 HOH 188 588 108 HOH HOH A . 
J 6 HOH 189 589 280 HOH HOH A . 
J 6 HOH 190 590 155 HOH HOH A . 
J 6 HOH 191 591 147 HOH HOH A . 
J 6 HOH 192 592 86  HOH HOH A . 
J 6 HOH 193 593 140 HOH HOH A . 
J 6 HOH 194 594 281 HOH HOH A . 
J 6 HOH 195 595 150 HOH HOH A . 
J 6 HOH 196 596 137 HOH HOH A . 
J 6 HOH 197 597 209 HOH HOH A . 
J 6 HOH 198 598 134 HOH HOH A . 
J 6 HOH 199 599 52  HOH HOH A . 
J 6 HOH 200 600 259 HOH HOH A . 
J 6 HOH 201 601 188 HOH HOH A . 
J 6 HOH 202 602 278 HOH HOH A . 
J 6 HOH 203 603 100 HOH HOH A . 
J 6 HOH 204 604 284 HOH HOH A . 
J 6 HOH 205 605 96  HOH HOH A . 
J 6 HOH 206 606 165 HOH HOH A . 
J 6 HOH 207 607 208 HOH HOH A . 
J 6 HOH 208 608 243 HOH HOH A . 
J 6 HOH 209 609 162 HOH HOH A . 
J 6 HOH 210 610 88  HOH HOH A . 
J 6 HOH 211 611 175 HOH HOH A . 
J 6 HOH 212 612 83  HOH HOH A . 
J 6 HOH 213 613 123 HOH HOH A . 
J 6 HOH 214 614 95  HOH HOH A . 
J 6 HOH 215 615 144 HOH HOH A . 
J 6 HOH 216 616 173 HOH HOH A . 
J 6 HOH 217 617 174 HOH HOH A . 
J 6 HOH 218 618 292 HOH HOH A . 
J 6 HOH 219 619 252 HOH HOH A . 
J 6 HOH 220 620 156 HOH HOH A . 
J 6 HOH 221 621 58  HOH HOH A . 
J 6 HOH 222 622 287 HOH HOH A . 
J 6 HOH 223 623 17  HOH HOH A . 
J 6 HOH 224 624 296 HOH HOH A . 
J 6 HOH 225 625 295 HOH HOH A . 
J 6 HOH 226 626 257 HOH HOH A . 
J 6 HOH 227 627 224 HOH HOH A . 
J 6 HOH 228 628 271 HOH HOH A . 
J 6 HOH 229 629 261 HOH HOH A . 
J 6 HOH 230 630 240 HOH HOH A . 
J 6 HOH 231 631 196 HOH HOH A . 
J 6 HOH 232 632 177 HOH HOH A . 
J 6 HOH 233 633 285 HOH HOH A . 
J 6 HOH 234 634 130 HOH HOH A . 
J 6 HOH 235 635 244 HOH HOH A . 
J 6 HOH 236 636 301 HOH HOH A . 
J 6 HOH 237 637 71  HOH HOH A . 
J 6 HOH 238 638 274 HOH HOH A . 
J 6 HOH 239 639 265 HOH HOH A . 
J 6 HOH 240 640 70  HOH HOH A . 
J 6 HOH 241 641 210 HOH HOH A . 
J 6 HOH 242 642 264 HOH HOH A . 
J 6 HOH 243 643 277 HOH HOH A . 
J 6 HOH 244 644 239 HOH HOH A . 
J 6 HOH 245 645 282 HOH HOH A . 
J 6 HOH 246 646 107 HOH HOH A . 
J 6 HOH 247 647 241 HOH HOH A . 
J 6 HOH 248 648 293 HOH HOH A . 
J 6 HOH 249 649 154 HOH HOH A . 
J 6 HOH 250 650 273 HOH HOH A . 
J 6 HOH 251 651 276 HOH HOH A . 
J 6 HOH 252 652 267 HOH HOH A . 
J 6 HOH 253 653 254 HOH HOH A . 
J 6 HOH 254 654 166 HOH HOH A . 
J 6 HOH 255 655 66  HOH HOH A . 
J 6 HOH 256 656 149 HOH HOH A . 
J 6 HOH 257 657 289 HOH HOH A . 
J 6 HOH 258 658 270 HOH HOH A . 
J 6 HOH 259 659 182 HOH HOH A . 
J 6 HOH 260 660 213 HOH HOH A . 
J 6 HOH 261 661 132 HOH HOH A . 
J 6 HOH 262 662 211 HOH HOH A . 
J 6 HOH 263 663 183 HOH HOH A . 
J 6 HOH 264 664 176 HOH HOH A . 
J 6 HOH 265 665 253 HOH HOH A . 
J 6 HOH 266 666 268 HOH HOH A . 
J 6 HOH 267 667 48  HOH HOH A . 
J 6 HOH 268 668 251 HOH HOH A . 
J 6 HOH 269 669 258 HOH HOH A . 
J 6 HOH 270 670 219 HOH HOH A . 
J 6 HOH 271 671 215 HOH HOH A . 
J 6 HOH 272 672 186 HOH HOH A . 
J 6 HOH 273 673 126 HOH HOH A . 
J 6 HOH 274 674 216 HOH HOH A . 
J 6 HOH 275 675 37  HOH HOH A . 
J 6 HOH 276 676 212 HOH HOH A . 
J 6 HOH 277 677 44  HOH HOH A . 
J 6 HOH 278 678 80  HOH HOH A . 
J 6 HOH 279 679 256 HOH HOH A . 
J 6 HOH 280 680 221 HOH HOH A . 
J 6 HOH 281 681 201 HOH HOH A . 
J 6 HOH 282 682 217 HOH HOH A . 
J 6 HOH 283 683 129 HOH HOH A . 
J 6 HOH 284 684 218 HOH HOH A . 
J 6 HOH 285 685 247 HOH HOH A . 
J 6 HOH 286 686 269 HOH HOH A . 
J 6 HOH 287 687 82  HOH HOH A . 
J 6 HOH 288 688 195 HOH HOH A . 
J 6 HOH 289 689 248 HOH HOH A . 
J 6 HOH 290 690 236 HOH HOH A . 
J 6 HOH 291 691 50  HOH HOH A . 
J 6 HOH 292 692 272 HOH HOH A . 
J 6 HOH 293 693 220 HOH HOH A . 
J 6 HOH 294 694 246 HOH HOH A . 
J 6 HOH 295 695 238 HOH HOH A . 
J 6 HOH 296 696 286 HOH HOH A . 
J 6 HOH 297 697 136 HOH HOH A . 
J 6 HOH 298 698 197 HOH HOH A . 
J 6 HOH 299 699 245 HOH HOH A . 
J 6 HOH 300 700 237 HOH HOH A . 
J 6 HOH 301 701 78  HOH HOH A . 
J 6 HOH 302 702 193 HOH HOH A . 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement        ? ? ? ? ? ? ? ? ? ? ? REFMAC      ? ? ? 5.6.0117 1 
? 'data scaling'    ? ? ? ? ? ? ? ? ? ? ? SCALA       ? ? ? 3.3.20   2 
? 'data extraction' ? ? ? ? ? ? ? ? ? ? ? PDB_EXTRACT ? ? ? 3.20     3 
? 'data reduction'  ? ? ? ? ? ? ? ? ? ? ? XDS         ? ? ? .        4 
? phasing           ? ? ? ? ? ? ? ? ? ? ? MOLREP      ? ? ? .        5 
# 
_cell.angle_alpha                  90.000 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   104.110 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.000 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     5LLC 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     42.209 
_cell.length_a_esd                 ? 
_cell.length_b                     41.078 
_cell.length_b_esd                 ? 
_cell.length_c                     71.968 
_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                         5LLC 
_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                   5LLC 
_exptl.crystals_number            1 
_exptl.details                    ? 
_exptl.method                     'X-RAY DIFFRACTION' 
_exptl.method_details             ? 
# 
_exptl_crystal.colour                      ? 
_exptl_crystal.density_diffrn              ? 
_exptl_crystal.density_Matthews            2.02 
_exptl_crystal.density_method              ? 
_exptl_crystal.density_percent_sol         38.6 
_exptl_crystal.description                 ? 
_exptl_crystal.F_000                       ? 
_exptl_crystal.id                          1 
_exptl_crystal.preparation                 ? 
_exptl_crystal.size_max                    ? 
_exptl_crystal.size_mid                    ? 
_exptl_crystal.size_min                    ? 
_exptl_crystal.size_rad                    ? 
_exptl_crystal.colour_lustre               ? 
_exptl_crystal.colour_modifier             ? 
_exptl_crystal.colour_primary              ? 
_exptl_crystal.density_meas                ? 
_exptl_crystal.density_meas_esd            ? 
_exptl_crystal.density_meas_gt             ? 
_exptl_crystal.density_meas_lt             ? 
_exptl_crystal.density_meas_temp           ? 
_exptl_crystal.density_meas_temp_esd       ? 
_exptl_crystal.density_meas_temp_gt        ? 
_exptl_crystal.density_meas_temp_lt        ? 
_exptl_crystal.pdbx_crystal_image_url      ? 
_exptl_crystal.pdbx_crystal_image_format   ? 
_exptl_crystal.pdbx_mosaicity              ? 
_exptl_crystal.pdbx_mosaicity_esd          ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, SITTING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              7 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp            291 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    
'Crystallization buffer: 0.1M sodium bicine (pH 9), 0.2 M 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_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS PILATUS3 6M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2012-11-30 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.826606 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.current                     ? 
_diffrn_source.details                     ? 
_diffrn_source.diffrn_id                   1 
_diffrn_source.power                       ? 
_diffrn_source.size                        ? 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.target                      ? 
_diffrn_source.type                        'PETRA III, EMBL c/o DESY BEAMLINE P13 (MX1)' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.826606 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   'P13 (MX1)' 
_diffrn_source.pdbx_synchrotron_site       'PETRA III, EMBL c/o DESY' 
# 
_reflns.B_iso_Wilson_estimate            9.980 
_reflns.entry_id                         5LLC 
_reflns.data_reduction_details           ? 
_reflns.data_reduction_method            ? 
_reflns.d_resolution_high                1.100 
_reflns.d_resolution_low                 69.798 
_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                       ? 
_reflns.number_obs                       95940 
_reflns.observed_criterion               ? 
_reflns.observed_criterion_F_max         ? 
_reflns.observed_criterion_F_min         ? 
_reflns.observed_criterion_I_max         ? 
_reflns.observed_criterion_I_min         ? 
_reflns.observed_criterion_sigma_F       ? 
_reflns.observed_criterion_sigma_I       ? 
_reflns.percent_possible_obs             98.800 
_reflns.R_free_details                   ? 
_reflns.Rmerge_F_all                     ? 
_reflns.Rmerge_F_obs                     ? 
_reflns.Friedel_coverage                 ? 
_reflns.number_gt                        ? 
_reflns.threshold_expression             ? 
_reflns.pdbx_redundancy                  6.700 
_reflns.pdbx_Rmerge_I_obs                ? 
_reflns.pdbx_Rmerge_I_all                ? 
_reflns.pdbx_Rsym_value                  0.038 
_reflns.pdbx_netI_over_av_sigmaI         8.500 
_reflns.pdbx_netI_over_sigmaI            18.400 
_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                  ? 
_reflns.pdbx_Rpim_I_all                  ? 
_reflns.pdbx_d_opt                       ? 
_reflns.pdbx_number_measured_all         ? 
_reflns.pdbx_diffrn_id                   1 
_reflns.pdbx_ordinal                     1 
_reflns.pdbx_CC_half                     ? 
_reflns.pdbx_R_split                     ? 
# 
loop_
_reflns_shell.d_res_high 
_reflns_shell.d_res_low 
_reflns_shell.meanI_over_sigI_all 
_reflns_shell.meanI_over_sigI_obs 
_reflns_shell.number_measured_all 
_reflns_shell.number_measured_obs 
_reflns_shell.number_possible 
_reflns_shell.number_unique_all 
_reflns_shell.number_unique_obs 
_reflns_shell.percent_possible_all 
_reflns_shell.percent_possible_obs 
_reflns_shell.Rmerge_F_all 
_reflns_shell.Rmerge_F_obs 
_reflns_shell.Rmerge_I_all 
_reflns_shell.Rmerge_I_obs 
_reflns_shell.meanI_over_sigI_gt 
_reflns_shell.meanI_over_uI_all 
_reflns_shell.meanI_over_uI_gt 
_reflns_shell.number_measured_gt 
_reflns_shell.number_unique_gt 
_reflns_shell.percent_possible_gt 
_reflns_shell.Rmerge_F_gt 
_reflns_shell.Rmerge_I_gt 
_reflns_shell.pdbx_redundancy 
_reflns_shell.pdbx_Rsym_value 
_reflns_shell.pdbx_chi_squared 
_reflns_shell.pdbx_netI_over_sigmaI_all 
_reflns_shell.pdbx_netI_over_sigmaI_obs 
_reflns_shell.pdbx_Rrim_I_all 
_reflns_shell.pdbx_Rpim_I_all 
_reflns_shell.pdbx_rejects 
_reflns_shell.pdbx_ordinal 
_reflns_shell.pdbx_diffrn_id 
_reflns_shell.pdbx_CC_half 
_reflns_shell.pdbx_R_split 
1.100 1.160  ? 2.900  ? ? ? ? ? 97.900 ? ? ? ? 0.265 ? ? ? ? ? ? ? ? 6.500 ? ? ? ? ? ? ? 1  1 ? ? 
1.160 1.230  ? 4.300  ? ? ? ? ? 98.900 ? ? ? ? 0.183 ? ? ? ? ? ? ? ? 6.600 ? ? ? ? ? ? ? 2  1 ? ? 
1.230 1.310  ? 6.000  ? ? ? ? ? 98.800 ? ? ? ? 0.129 ? ? ? ? ? ? ? ? 6.700 ? ? ? ? ? ? ? 3  1 ? ? 
1.310 1.420  ? 8.200  ? ? ? ? ? 99.200 ? ? ? ? 0.092 ? ? ? ? ? ? ? ? 6.700 ? ? ? ? ? ? ? 4  1 ? ? 
1.420 1.560  ? 11.400 ? ? ? ? ? 98.500 ? ? ? ? 0.064 ? ? ? ? ? ? ? ? 6.700 ? ? ? ? ? ? ? 5  1 ? ? 
1.560 1.740  ? 14.100 ? ? ? ? ? 99.600 ? ? ? ? 0.050 ? ? ? ? ? ? ? ? 6.900 ? ? ? ? ? ? ? 6  1 ? ? 
1.740 2.010  ? 16.000 ? ? ? ? ? 98.600 ? ? ? ? 0.040 ? ? ? ? ? ? ? ? 6.700 ? ? ? ? ? ? ? 7  1 ? ? 
2.010 2.460  ? 18.300 ? ? ? ? ? 99.600 ? ? ? ? 0.036 ? ? ? ? ? ? ? ? 7.000 ? ? ? ? ? ? ? 8  1 ? ? 
2.460 3.480  ? 19.000 ? ? ? ? ? 98.900 ? ? ? ? 0.033 ? ? ? ? ? ? ? ? 6.800 ? ? ? ? ? ? ? 9  1 ? ? 
3.480 69.798 ? 21.800 ? ? ? ? ? 99.400 ? ? ? ? 0.027 ? ? ? ? ? ? ? ? 6.700 ? ? ? ? ? ? ? 10 1 ? ? 
# 
_refine.aniso_B[1][1]                            0.0700 
_refine.aniso_B[1][2]                            0.0000 
_refine.aniso_B[1][3]                            0.0600 
_refine.aniso_B[2][2]                            -0.0700 
_refine.aniso_B[2][3]                            0.0000 
_refine.aniso_B[3][3]                            0.0300 
_refine.B_iso_max                                119.960 
_refine.B_iso_mean                               17.6520 
_refine.B_iso_min                                6.440 
_refine.correlation_coeff_Fo_to_Fc               0.9790 
_refine.correlation_coeff_Fo_to_Fc_free          0.9720 
_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                                 5LLC 
_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                            1.1000 
_refine.ls_d_res_low                             40.9400 
_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                     86284 
_refine.ls_number_reflns_R_free                  9634 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    98.7300 
_refine.ls_percent_reflns_R_free                 10.0000 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1401 
_refine.ls_R_factor_R_free                       0.1611 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1377 
_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                       0.0320 
_refine.pdbx_overall_ESU_R_Free                  0.0320 
_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             0.0317 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.cycle_id                         final 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.d_res_high                       1.1000 
_refine_hist.d_res_low                        40.9400 
_refine_hist.pdbx_number_atoms_ligand         51 
_refine_hist.number_atoms_solvent             302 
_refine_hist.number_atoms_total               2411 
_refine_hist.pdbx_number_residues_total       258 
_refine_hist.pdbx_B_iso_mean_ligand           21.13 
_refine_hist.pdbx_B_iso_mean_solvent          30.20 
_refine_hist.pdbx_number_atoms_protein        2058 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.criterion 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.number 
_refine_ls_restr.rejects 
_refine_ls_restr.type 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' ? 0.024  0.020  2335 ? r_bond_refined_d       ? ? 
'X-RAY DIFFRACTION' ? 2.408  1.965  3184 ? r_angle_refined_deg    ? ? 
'X-RAY DIFFRACTION' ? 6.902  5.000  291  ? r_dihedral_angle_1_deg ? ? 
'X-RAY DIFFRACTION' ? 32.971 24.712 104  ? r_dihedral_angle_2_deg ? ? 
'X-RAY DIFFRACTION' ? 12.622 15.000 387  ? r_dihedral_angle_3_deg ? ? 
'X-RAY DIFFRACTION' ? 21.307 15.000 7    ? r_dihedral_angle_4_deg ? ? 
'X-RAY DIFFRACTION' ? 0.172  0.200  325  ? r_chiral_restr         ? ? 
'X-RAY DIFFRACTION' ? 0.015  0.021  1822 ? r_gen_planes_refined   ? ? 
'X-RAY DIFFRACTION' ? 9.240  3.000  2335 ? r_rigid_bond_restr     ? ? 
'X-RAY DIFFRACTION' ? 28.569 5.000  303  ? r_sphericity_free      ? ? 
'X-RAY DIFFRACTION' ? 14.828 5.000  2259 ? r_sphericity_bonded    ? ? 
# 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.d_res_high                       1.1000 
_refine_ls_shell.d_res_low                        1.1290 
_refine_ls_shell.number_reflns_all                6906 
_refine_ls_shell.number_reflns_obs                ? 
_refine_ls_shell.number_reflns_R_free             707 
_refine_ls_shell.number_reflns_R_work             6199 
_refine_ls_shell.percent_reflns_obs               96.4500 
_refine_ls_shell.percent_reflns_R_free            ? 
_refine_ls_shell.R_factor_all                     ? 
_refine_ls_shell.R_factor_obs                     ? 
_refine_ls_shell.R_factor_R_free                  0.2510 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.R_factor_R_work                  0.2200 
_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                     5LLC 
_struct.title                        
;Crystal structure of human carbonic anhydrase isozyme II with 3-(Methylamino)-2,5,6-trifluoro-4-[(2-phenylethyl)sulfonyl]benzenesulfonamide
;
_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        5LLC 
_struct_keywords.text            
'drug design, carbonic anhydrase, benzenesulfonamide, metal-binding, lyase-lyase inhibitor complex, lyase' 
_struct_keywords.pdbx_keywords   LYASE 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 2 ? 
C N N 3 ? 
D N N 3 ? 
E N N 4 ? 
F N N 4 ? 
G N N 4 ? 
H N N 4 ? 
I N N 5 ? 
J N N 6 ? 
# 
_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              5LLC 
_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              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)' 1100  ? 
1 MORE         11    ? 
1 'SSA (A^2)'  11520 ? 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F,G,H,I,J 
# 
_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 ? ILE A 166 ? ASP A 165 ILE A 167 5 ? 3 
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 ? ? ? ? ? ? ? 2.008 ? ? 
metalc2 metalc ? ? A HIS 96  NE2 ? ? ? 1_555 B ZN  . ZN ? ? A HIS 96  A ZN  301 1_555 ? ? ? ? ? ? ? 2.024 ? ? 
metalc3 metalc ? ? A HIS 119 ND1 ? ? ? 1_555 B ZN  . ZN ? ? A HIS 119 A ZN  301 1_555 ? ? ? ? ? ? ? 2.051 ? ? 
metalc4 metalc ? ? B ZN  .   ZN  ? ? ? 1_555 I V26 . N4 ? ? A ZN  301 A V26 308 1_555 ? ? ? ? ? ? ? 1.936 ? ? 
# 
_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_555 104.4 ? 
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_555 110.7 ? 
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 N4  ? I V26 .   ? A V26 308 ? 1_555 112.2 ? 
5 NE2 ? A HIS 96  ? A HIS 96  ? 1_555 ZN ? B ZN . ? A ZN 301 ? 1_555 N4  ? I V26 .   ? A V26 308 ? 1_555 113.4 ? 
6 ND1 ? A HIS 119 ? A HIS 119 ? 1_555 ZN ? B ZN . ? A ZN 301 ? 1_555 N4  ? I V26 .   ? A V26 308 ? 1_555 116.0 ? 
# 
loop_
_struct_mon_prot_cis.pdbx_id 
_struct_mon_prot_cis.label_comp_id 
_struct_mon_prot_cis.label_seq_id 
_struct_mon_prot_cis.label_asym_id 
_struct_mon_prot_cis.label_alt_id 
_struct_mon_prot_cis.pdbx_PDB_ins_code 
_struct_mon_prot_cis.auth_comp_id 
_struct_mon_prot_cis.auth_seq_id 
_struct_mon_prot_cis.auth_asym_id 
_struct_mon_prot_cis.pdbx_label_comp_id_2 
_struct_mon_prot_cis.pdbx_label_seq_id_2 
_struct_mon_prot_cis.pdbx_label_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_ins_code_2 
_struct_mon_prot_cis.pdbx_auth_comp_id_2 
_struct_mon_prot_cis.pdbx_auth_seq_id_2 
_struct_mon_prot_cis.pdbx_auth_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_model_num 
_struct_mon_prot_cis.pdbx_omega_angle 
1 SER 29  A . ? SER 29  A PRO 30  A ? PRO 30  A 1 -1.82 
2 PRO 200 A . ? PRO 201 A PRO 201 A ? PRO 202 A 1 10.93 
# 
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 ILE A 209 ? O ILE A 210 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 DMS 302 ? 4  'binding site for residue DMS A 302' 
AC3 Software A DMS 303 ? 4  'binding site for residue DMS A 303' 
AC4 Software A EDO 304 ? 4  'binding site for residue EDO A 304' 
AC5 Software A EDO 305 ? 6  'binding site for residue EDO A 305' 
AC6 Software A EDO 306 ? 8  'binding site for residue EDO A 306' 
AC7 Software A EDO 307 ? 2  'binding site for residue EDO A 307' 
AC8 Software A V26 308 ? 17 'binding site for residue V26 A 308' 
# 
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  V26 I .   ? V26 A 308 . ? 1_555 ? 
5  AC2 4  TYR A 7   ? TYR A 7   . ? 1_555 ? 
6  AC2 4  ASP A 242 ? ASP A 243 . ? 1_555 ? 
7  AC2 4  TRP A 244 ? TRP A 245 . ? 1_555 ? 
8  AC2 4  HOH J .   ? HOH A 427 . ? 1_555 ? 
9  AC3 4  ILE A 91  ? ILE A 91  . ? 1_555 ? 
10 AC3 4  PHE A 130 ? PHE A 131 . ? 1_555 ? 
11 AC3 4  V26 I .   ? V26 A 308 . ? 1_555 ? 
12 AC3 4  HOH J .   ? HOH A 538 . ? 1_555 ? 
13 AC4 4  LYS A 148 ? LYS A 149 . ? 1_555 ? 
14 AC4 4  PRO A 214 ? PRO A 215 . ? 1_555 ? 
15 AC4 4  HOH J .   ? HOH A 419 . ? 1_555 ? 
16 AC4 4  HOH J .   ? HOH A 477 . ? 1_555 ? 
17 AC5 6  LEU A 163 ? LEU A 164 . ? 1_555 ? 
18 AC5 6  ASP A 164 ? ASP A 165 . ? 1_555 ? 
19 AC5 6  LYS A 224 ? LYS A 225 . ? 1_555 ? 
20 AC5 6  LYS A 227 ? LYS A 228 . ? 1_555 ? 
21 AC5 6  LEU A 228 ? LEU A 229 . ? 1_555 ? 
22 AC5 6  HOH J .   ? HOH A 414 . ? 1_555 ? 
23 AC6 8  HIS A 17  ? HIS A 17  . ? 1_555 ? 
24 AC6 8  PRO A 21  ? PRO A 21  . ? 1_555 ? 
25 AC6 8  LEU A 47  ? LEU A 47  . ? 1_655 ? 
26 AC6 8  SER A 48  ? SER A 48  . ? 1_655 ? 
27 AC6 8  HOH J .   ? HOH A 423 . ? 1_655 ? 
28 AC6 8  HOH J .   ? HOH A 457 . ? 1_655 ? 
29 AC6 8  HOH J .   ? HOH A 484 . ? 1_655 ? 
30 AC6 8  HOH J .   ? HOH A 687 . ? 1_655 ? 
31 AC7 2  PRO A 246 ? PRO A 247 . ? 1_555 ? 
32 AC7 2  HOH J .   ? HOH A 523 . ? 1_555 ? 
33 AC8 17 ASN A 62  ? ASN A 62  . ? 1_555 ? 
34 AC8 17 HIS A 64  ? HIS A 64  . ? 1_555 ? 
35 AC8 17 ASN A 67  ? ASN A 67  . ? 1_555 ? 
36 AC8 17 GLN A 92  ? GLN A 92  . ? 1_555 ? 
37 AC8 17 HIS A 94  ? HIS A 94  . ? 1_555 ? 
38 AC8 17 HIS A 96  ? HIS A 96  . ? 1_555 ? 
39 AC8 17 HIS A 119 ? HIS A 119 . ? 1_555 ? 
40 AC8 17 VAL A 121 ? VAL A 121 . ? 1_555 ? 
41 AC8 17 PHE A 130 ? PHE A 131 . ? 1_555 ? 
42 AC8 17 LEU A 197 ? LEU A 198 . ? 1_555 ? 
43 AC8 17 THR A 198 ? THR A 199 . ? 1_555 ? 
44 AC8 17 THR A 199 ? THR A 200 . ? 1_555 ? 
45 AC8 17 PRO A 200 ? PRO A 201 . ? 1_555 ? 
46 AC8 17 PRO A 201 ? PRO A 202 . ? 1_555 ? 
47 AC8 17 ZN  B .   ? ZN  A 301 . ? 1_555 ? 
48 AC8 17 DMS D .   ? DMS A 303 . ? 1_555 ? 
49 AC8 17 HOH J .   ? HOH A 575 . ? 1_555 ? 
# 
loop_
_pdbx_validate_close_contact.id 
_pdbx_validate_close_contact.PDB_model_num 
_pdbx_validate_close_contact.auth_atom_id_1 
_pdbx_validate_close_contact.auth_asym_id_1 
_pdbx_validate_close_contact.auth_comp_id_1 
_pdbx_validate_close_contact.auth_seq_id_1 
_pdbx_validate_close_contact.PDB_ins_code_1 
_pdbx_validate_close_contact.label_alt_id_1 
_pdbx_validate_close_contact.auth_atom_id_2 
_pdbx_validate_close_contact.auth_asym_id_2 
_pdbx_validate_close_contact.auth_comp_id_2 
_pdbx_validate_close_contact.auth_seq_id_2 
_pdbx_validate_close_contact.PDB_ins_code_2 
_pdbx_validate_close_contact.label_alt_id_2 
_pdbx_validate_close_contact.dist 
1 1 O  A HOH 412 ? ? O A HOH 475 ? ? 2.04 
2 1 NZ A LYS 213 ? B O A HOH 401 ? ? 2.08 
3 1 O  A HOH 658 ? ? O A HOH 686 ? ? 2.18 
# 
loop_
_pdbx_validate_rmsd_bond.id 
_pdbx_validate_rmsd_bond.PDB_model_num 
_pdbx_validate_rmsd_bond.auth_atom_id_1 
_pdbx_validate_rmsd_bond.auth_asym_id_1 
_pdbx_validate_rmsd_bond.auth_comp_id_1 
_pdbx_validate_rmsd_bond.auth_seq_id_1 
_pdbx_validate_rmsd_bond.PDB_ins_code_1 
_pdbx_validate_rmsd_bond.label_alt_id_1 
_pdbx_validate_rmsd_bond.auth_atom_id_2 
_pdbx_validate_rmsd_bond.auth_asym_id_2 
_pdbx_validate_rmsd_bond.auth_comp_id_2 
_pdbx_validate_rmsd_bond.auth_seq_id_2 
_pdbx_validate_rmsd_bond.PDB_ins_code_2 
_pdbx_validate_rmsd_bond.label_alt_id_2 
_pdbx_validate_rmsd_bond.bond_value 
_pdbx_validate_rmsd_bond.bond_target_value 
_pdbx_validate_rmsd_bond.bond_deviation 
_pdbx_validate_rmsd_bond.bond_standard_deviation 
_pdbx_validate_rmsd_bond.linker_flag 
1 1 CG A HIS 3  ? ? CD2 A HIS 3  ? ? 1.414 1.354 0.060 0.009 N 
2 1 CG A HIS 10 ? B CD2 A HIS 10 ? B 1.408 1.354 0.054 0.009 N 
3 1 CG A HIS 36 ? ? CD2 A HIS 36 ? ? 1.411 1.354 0.057 0.009 N 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 ARG A 27  ? ? -144.01 56.70   
2 1 LYS A 76  ? ? -113.67 -90.10  
3 1 GLU A 106 ? ? -90.83  -60.52  
4 1 LYS A 111 ? ? 73.83   -2.44   
5 1 PHE A 176 ? ? -152.11 67.88   
6 1 ASN A 244 ? ? -94.25  43.99   
7 1 LYS A 252 ? ? 55.40   -140.33 
# 
_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 701 ? 6.07 . 
2 1 O ? A HOH 702 ? 6.54 . 
# 
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  
EDO C1   C  N N 98  
EDO O1   O  N N 99  
EDO C2   C  N N 100 
EDO O2   O  N N 101 
EDO H11  H  N N 102 
EDO H12  H  N N 103 
EDO HO1  H  N N 104 
EDO H21  H  N N 105 
EDO H22  H  N N 106 
EDO HO2  H  N N 107 
GLN N    N  N N 108 
GLN CA   C  N S 109 
GLN C    C  N N 110 
GLN O    O  N N 111 
GLN CB   C  N N 112 
GLN CG   C  N N 113 
GLN CD   C  N N 114 
GLN OE1  O  N N 115 
GLN NE2  N  N N 116 
GLN OXT  O  N N 117 
GLN H    H  N N 118 
GLN H2   H  N N 119 
GLN HA   H  N N 120 
GLN HB2  H  N N 121 
GLN HB3  H  N N 122 
GLN HG2  H  N N 123 
GLN HG3  H  N N 124 
GLN HE21 H  N N 125 
GLN HE22 H  N N 126 
GLN HXT  H  N N 127 
GLU N    N  N N 128 
GLU CA   C  N S 129 
GLU C    C  N N 130 
GLU O    O  N N 131 
GLU CB   C  N N 132 
GLU CG   C  N N 133 
GLU CD   C  N N 134 
GLU OE1  O  N N 135 
GLU OE2  O  N N 136 
GLU OXT  O  N N 137 
GLU H    H  N N 138 
GLU H2   H  N N 139 
GLU HA   H  N N 140 
GLU HB2  H  N N 141 
GLU HB3  H  N N 142 
GLU HG2  H  N N 143 
GLU HG3  H  N N 144 
GLU HE2  H  N N 145 
GLU HXT  H  N N 146 
GLY N    N  N N 147 
GLY CA   C  N N 148 
GLY C    C  N N 149 
GLY O    O  N N 150 
GLY OXT  O  N N 151 
GLY H    H  N N 152 
GLY H2   H  N N 153 
GLY HA2  H  N N 154 
GLY HA3  H  N N 155 
GLY HXT  H  N N 156 
HIS N    N  N N 157 
HIS CA   C  N S 158 
HIS C    C  N N 159 
HIS O    O  N N 160 
HIS CB   C  N N 161 
HIS CG   C  Y N 162 
HIS ND1  N  Y N 163 
HIS CD2  C  Y N 164 
HIS CE1  C  Y N 165 
HIS NE2  N  Y N 166 
HIS OXT  O  N N 167 
HIS H    H  N N 168 
HIS H2   H  N N 169 
HIS HA   H  N N 170 
HIS HB2  H  N N 171 
HIS HB3  H  N N 172 
HIS HD1  H  N N 173 
HIS HD2  H  N N 174 
HIS HE1  H  N N 175 
HIS HE2  H  N N 176 
HIS HXT  H  N N 177 
HOH O    O  N N 178 
HOH H1   H  N N 179 
HOH H2   H  N N 180 
ILE N    N  N N 181 
ILE CA   C  N S 182 
ILE C    C  N N 183 
ILE O    O  N N 184 
ILE CB   C  N S 185 
ILE CG1  C  N N 186 
ILE CG2  C  N N 187 
ILE CD1  C  N N 188 
ILE OXT  O  N N 189 
ILE H    H  N N 190 
ILE H2   H  N N 191 
ILE HA   H  N N 192 
ILE HB   H  N N 193 
ILE HG12 H  N N 194 
ILE HG13 H  N N 195 
ILE HG21 H  N N 196 
ILE HG22 H  N N 197 
ILE HG23 H  N N 198 
ILE HD11 H  N N 199 
ILE HD12 H  N N 200 
ILE HD13 H  N N 201 
ILE HXT  H  N N 202 
LEU N    N  N N 203 
LEU CA   C  N S 204 
LEU C    C  N N 205 
LEU O    O  N N 206 
LEU CB   C  N N 207 
LEU CG   C  N N 208 
LEU CD1  C  N N 209 
LEU CD2  C  N N 210 
LEU OXT  O  N N 211 
LEU H    H  N N 212 
LEU H2   H  N N 213 
LEU HA   H  N N 214 
LEU HB2  H  N N 215 
LEU HB3  H  N N 216 
LEU HG   H  N N 217 
LEU HD11 H  N N 218 
LEU HD12 H  N N 219 
LEU HD13 H  N N 220 
LEU HD21 H  N N 221 
LEU HD22 H  N N 222 
LEU HD23 H  N N 223 
LEU HXT  H  N N 224 
LYS N    N  N N 225 
LYS CA   C  N S 226 
LYS C    C  N N 227 
LYS O    O  N N 228 
LYS CB   C  N N 229 
LYS CG   C  N N 230 
LYS CD   C  N N 231 
LYS CE   C  N N 232 
LYS NZ   N  N N 233 
LYS OXT  O  N N 234 
LYS H    H  N N 235 
LYS H2   H  N N 236 
LYS HA   H  N N 237 
LYS HB2  H  N N 238 
LYS HB3  H  N N 239 
LYS HG2  H  N N 240 
LYS HG3  H  N N 241 
LYS HD2  H  N N 242 
LYS HD3  H  N N 243 
LYS HE2  H  N N 244 
LYS HE3  H  N N 245 
LYS HZ1  H  N N 246 
LYS HZ2  H  N N 247 
LYS HZ3  H  N N 248 
LYS HXT  H  N N 249 
MET N    N  N N 250 
MET CA   C  N S 251 
MET C    C  N N 252 
MET O    O  N N 253 
MET CB   C  N N 254 
MET CG   C  N N 255 
MET SD   S  N N 256 
MET CE   C  N N 257 
MET OXT  O  N N 258 
MET H    H  N N 259 
MET H2   H  N N 260 
MET HA   H  N N 261 
MET HB2  H  N N 262 
MET HB3  H  N N 263 
MET HG2  H  N N 264 
MET HG3  H  N N 265 
MET HE1  H  N N 266 
MET HE2  H  N N 267 
MET HE3  H  N N 268 
MET HXT  H  N N 269 
PHE N    N  N N 270 
PHE CA   C  N S 271 
PHE C    C  N N 272 
PHE O    O  N N 273 
PHE CB   C  N N 274 
PHE CG   C  Y N 275 
PHE CD1  C  Y N 276 
PHE CD2  C  Y N 277 
PHE CE1  C  Y N 278 
PHE CE2  C  Y N 279 
PHE CZ   C  Y N 280 
PHE OXT  O  N N 281 
PHE H    H  N N 282 
PHE H2   H  N N 283 
PHE HA   H  N N 284 
PHE HB2  H  N N 285 
PHE HB3  H  N N 286 
PHE HD1  H  N N 287 
PHE HD2  H  N N 288 
PHE HE1  H  N N 289 
PHE HE2  H  N N 290 
PHE HZ   H  N N 291 
PHE HXT  H  N N 292 
PRO N    N  N N 293 
PRO CA   C  N S 294 
PRO C    C  N N 295 
PRO O    O  N N 296 
PRO CB   C  N N 297 
PRO CG   C  N N 298 
PRO CD   C  N N 299 
PRO OXT  O  N N 300 
PRO H    H  N N 301 
PRO HA   H  N N 302 
PRO HB2  H  N N 303 
PRO HB3  H  N N 304 
PRO HG2  H  N N 305 
PRO HG3  H  N N 306 
PRO HD2  H  N N 307 
PRO HD3  H  N N 308 
PRO HXT  H  N N 309 
SER N    N  N N 310 
SER CA   C  N S 311 
SER C    C  N N 312 
SER O    O  N N 313 
SER CB   C  N N 314 
SER OG   O  N N 315 
SER OXT  O  N N 316 
SER H    H  N N 317 
SER H2   H  N N 318 
SER HA   H  N N 319 
SER HB2  H  N N 320 
SER HB3  H  N N 321 
SER HG   H  N N 322 
SER HXT  H  N N 323 
THR N    N  N N 324 
THR CA   C  N S 325 
THR C    C  N N 326 
THR O    O  N N 327 
THR CB   C  N R 328 
THR OG1  O  N N 329 
THR CG2  C  N N 330 
THR OXT  O  N N 331 
THR H    H  N N 332 
THR H2   H  N N 333 
THR HA   H  N N 334 
THR HB   H  N N 335 
THR HG1  H  N N 336 
THR HG21 H  N N 337 
THR HG22 H  N N 338 
THR HG23 H  N N 339 
THR HXT  H  N N 340 
TRP N    N  N N 341 
TRP CA   C  N S 342 
TRP C    C  N N 343 
TRP O    O  N N 344 
TRP CB   C  N N 345 
TRP CG   C  Y N 346 
TRP CD1  C  Y N 347 
TRP CD2  C  Y N 348 
TRP NE1  N  Y N 349 
TRP CE2  C  Y N 350 
TRP CE3  C  Y N 351 
TRP CZ2  C  Y N 352 
TRP CZ3  C  Y N 353 
TRP CH2  C  Y N 354 
TRP OXT  O  N N 355 
TRP H    H  N N 356 
TRP H2   H  N N 357 
TRP HA   H  N N 358 
TRP HB2  H  N N 359 
TRP HB3  H  N N 360 
TRP HD1  H  N N 361 
TRP HE1  H  N N 362 
TRP HE3  H  N N 363 
TRP HZ2  H  N N 364 
TRP HZ3  H  N N 365 
TRP HH2  H  N N 366 
TRP HXT  H  N N 367 
TYR N    N  N N 368 
TYR CA   C  N S 369 
TYR C    C  N N 370 
TYR O    O  N N 371 
TYR CB   C  N N 372 
TYR CG   C  Y N 373 
TYR CD1  C  Y N 374 
TYR CD2  C  Y N 375 
TYR CE1  C  Y N 376 
TYR CE2  C  Y N 377 
TYR CZ   C  Y N 378 
TYR OH   O  N N 379 
TYR OXT  O  N N 380 
TYR H    H  N N 381 
TYR H2   H  N N 382 
TYR HA   H  N N 383 
TYR HB2  H  N N 384 
TYR HB3  H  N N 385 
TYR HD1  H  N N 386 
TYR HD2  H  N N 387 
TYR HE1  H  N N 388 
TYR HE2  H  N N 389 
TYR HH   H  N N 390 
TYR HXT  H  N N 391 
V26 O16  O  N N 392 
V26 S14  S  N N 393 
V26 O15  O  N N 394 
V26 C8   C  Y N 395 
V26 C7   C  Y N 396 
V26 F12  F  N N 397 
V26 C6   C  Y N 398 
V26 F11  F  N N 399 
V26 C9   C  Y N 400 
V26 N25  N  N N 401 
V26 C26  C  N N 402 
V26 C10  C  Y N 403 
V26 F13  F  N N 404 
V26 C5   C  Y N 405 
V26 S1   S  N N 406 
V26 O3   O  N N 407 
V26 N4   N  N N 408 
V26 O2   O  N N 409 
V26 C17  C  N N 410 
V26 C18  C  N N 411 
V26 C19  C  Y N 412 
V26 C24  C  Y N 413 
V26 C23  C  Y N 414 
V26 C22  C  Y N 415 
V26 C21  C  Y N 416 
V26 C20  C  Y N 417 
V26 H1   H  N N 418 
V26 H2   H  N N 419 
V26 H3   H  N N 420 
V26 H4   H  N N 421 
V26 H5   H  N N 422 
V26 H6   H  N N 423 
V26 H7   H  N N 424 
V26 H8   H  N N 425 
V26 H9   H  N N 426 
V26 H10  H  N N 427 
V26 H11  H  N N 428 
V26 H12  H  N N 429 
V26 H13  H  N N 430 
V26 H14  H  N N 431 
V26 H15  H  N N 432 
VAL N    N  N N 433 
VAL CA   C  N S 434 
VAL C    C  N N 435 
VAL O    O  N N 436 
VAL CB   C  N N 437 
VAL CG1  C  N N 438 
VAL CG2  C  N N 439 
VAL OXT  O  N N 440 
VAL H    H  N N 441 
VAL H2   H  N N 442 
VAL HA   H  N N 443 
VAL HB   H  N N 444 
VAL HG11 H  N N 445 
VAL HG12 H  N N 446 
VAL HG13 H  N N 447 
VAL HG21 H  N N 448 
VAL HG22 H  N N 449 
VAL HG23 H  N N 450 
VAL HXT  H  N N 451 
ZN  ZN   ZN N N 452 
# 
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  
EDO C1  O1   sing N N 92  
EDO C1  C2   sing N N 93  
EDO C1  H11  sing N N 94  
EDO C1  H12  sing N N 95  
EDO O1  HO1  sing N N 96  
EDO C2  O2   sing N N 97  
EDO C2  H21  sing N N 98  
EDO C2  H22  sing N N 99  
EDO O2  HO2  sing N N 100 
GLN N   CA   sing N N 101 
GLN N   H    sing N N 102 
GLN N   H2   sing N N 103 
GLN CA  C    sing N N 104 
GLN CA  CB   sing N N 105 
GLN CA  HA   sing N N 106 
GLN C   O    doub N N 107 
GLN C   OXT  sing N N 108 
GLN CB  CG   sing N N 109 
GLN CB  HB2  sing N N 110 
GLN CB  HB3  sing N N 111 
GLN CG  CD   sing N N 112 
GLN CG  HG2  sing N N 113 
GLN CG  HG3  sing N N 114 
GLN CD  OE1  doub N N 115 
GLN CD  NE2  sing N N 116 
GLN NE2 HE21 sing N N 117 
GLN NE2 HE22 sing N N 118 
GLN OXT HXT  sing N N 119 
GLU N   CA   sing N N 120 
GLU N   H    sing N N 121 
GLU N   H2   sing N N 122 
GLU CA  C    sing N N 123 
GLU CA  CB   sing N N 124 
GLU CA  HA   sing N N 125 
GLU C   O    doub N N 126 
GLU C   OXT  sing N N 127 
GLU CB  CG   sing N N 128 
GLU CB  HB2  sing N N 129 
GLU CB  HB3  sing N N 130 
GLU CG  CD   sing N N 131 
GLU CG  HG2  sing N N 132 
GLU CG  HG3  sing N N 133 
GLU CD  OE1  doub N N 134 
GLU CD  OE2  sing N N 135 
GLU OE2 HE2  sing N N 136 
GLU OXT HXT  sing N N 137 
GLY N   CA   sing N N 138 
GLY N   H    sing N N 139 
GLY N   H2   sing N N 140 
GLY CA  C    sing N N 141 
GLY CA  HA2  sing N N 142 
GLY CA  HA3  sing N N 143 
GLY C   O    doub N N 144 
GLY C   OXT  sing N N 145 
GLY OXT HXT  sing N N 146 
HIS N   CA   sing N N 147 
HIS N   H    sing N N 148 
HIS N   H2   sing N N 149 
HIS CA  C    sing N N 150 
HIS CA  CB   sing N N 151 
HIS CA  HA   sing N N 152 
HIS C   O    doub N N 153 
HIS C   OXT  sing N N 154 
HIS CB  CG   sing N N 155 
HIS CB  HB2  sing N N 156 
HIS CB  HB3  sing N N 157 
HIS CG  ND1  sing Y N 158 
HIS CG  CD2  doub Y N 159 
HIS ND1 CE1  doub Y N 160 
HIS ND1 HD1  sing N N 161 
HIS CD2 NE2  sing Y N 162 
HIS CD2 HD2  sing N N 163 
HIS CE1 NE2  sing Y N 164 
HIS CE1 HE1  sing N N 165 
HIS NE2 HE2  sing N N 166 
HIS OXT HXT  sing N N 167 
HOH O   H1   sing N N 168 
HOH O   H2   sing N N 169 
ILE N   CA   sing N N 170 
ILE N   H    sing N N 171 
ILE N   H2   sing N N 172 
ILE CA  C    sing N N 173 
ILE CA  CB   sing N N 174 
ILE CA  HA   sing N N 175 
ILE C   O    doub N N 176 
ILE C   OXT  sing N N 177 
ILE CB  CG1  sing N N 178 
ILE CB  CG2  sing N N 179 
ILE CB  HB   sing N N 180 
ILE CG1 CD1  sing N N 181 
ILE CG1 HG12 sing N N 182 
ILE CG1 HG13 sing N N 183 
ILE CG2 HG21 sing N N 184 
ILE CG2 HG22 sing N N 185 
ILE CG2 HG23 sing N N 186 
ILE CD1 HD11 sing N N 187 
ILE CD1 HD12 sing N N 188 
ILE CD1 HD13 sing N N 189 
ILE OXT HXT  sing N N 190 
LEU N   CA   sing N N 191 
LEU N   H    sing N N 192 
LEU N   H2   sing N N 193 
LEU CA  C    sing N N 194 
LEU CA  CB   sing N N 195 
LEU CA  HA   sing N N 196 
LEU C   O    doub N N 197 
LEU C   OXT  sing N N 198 
LEU CB  CG   sing N N 199 
LEU CB  HB2  sing N N 200 
LEU CB  HB3  sing N N 201 
LEU CG  CD1  sing N N 202 
LEU CG  CD2  sing N N 203 
LEU CG  HG   sing N N 204 
LEU CD1 HD11 sing N N 205 
LEU CD1 HD12 sing N N 206 
LEU CD1 HD13 sing N N 207 
LEU CD2 HD21 sing N N 208 
LEU CD2 HD22 sing N N 209 
LEU CD2 HD23 sing N N 210 
LEU OXT HXT  sing N N 211 
LYS N   CA   sing N N 212 
LYS N   H    sing N N 213 
LYS N   H2   sing N N 214 
LYS CA  C    sing N N 215 
LYS CA  CB   sing N N 216 
LYS CA  HA   sing N N 217 
LYS C   O    doub N N 218 
LYS C   OXT  sing N N 219 
LYS CB  CG   sing N N 220 
LYS CB  HB2  sing N N 221 
LYS CB  HB3  sing N N 222 
LYS CG  CD   sing N N 223 
LYS CG  HG2  sing N N 224 
LYS CG  HG3  sing N N 225 
LYS CD  CE   sing N N 226 
LYS CD  HD2  sing N N 227 
LYS CD  HD3  sing N N 228 
LYS CE  NZ   sing N N 229 
LYS CE  HE2  sing N N 230 
LYS CE  HE3  sing N N 231 
LYS NZ  HZ1  sing N N 232 
LYS NZ  HZ2  sing N N 233 
LYS NZ  HZ3  sing N N 234 
LYS OXT HXT  sing N N 235 
MET N   CA   sing N N 236 
MET N   H    sing N N 237 
MET N   H2   sing N N 238 
MET CA  C    sing N N 239 
MET CA  CB   sing N N 240 
MET CA  HA   sing N N 241 
MET C   O    doub N N 242 
MET C   OXT  sing N N 243 
MET CB  CG   sing N N 244 
MET CB  HB2  sing N N 245 
MET CB  HB3  sing N N 246 
MET CG  SD   sing N N 247 
MET CG  HG2  sing N N 248 
MET CG  HG3  sing N N 249 
MET SD  CE   sing N N 250 
MET CE  HE1  sing N N 251 
MET CE  HE2  sing N N 252 
MET CE  HE3  sing N N 253 
MET OXT HXT  sing N N 254 
PHE N   CA   sing N N 255 
PHE N   H    sing N N 256 
PHE N   H2   sing N N 257 
PHE CA  C    sing N N 258 
PHE CA  CB   sing N N 259 
PHE CA  HA   sing N N 260 
PHE C   O    doub N N 261 
PHE C   OXT  sing N N 262 
PHE CB  CG   sing N N 263 
PHE CB  HB2  sing N N 264 
PHE CB  HB3  sing N N 265 
PHE CG  CD1  doub Y N 266 
PHE CG  CD2  sing Y N 267 
PHE CD1 CE1  sing Y N 268 
PHE CD1 HD1  sing N N 269 
PHE CD2 CE2  doub Y N 270 
PHE CD2 HD2  sing N N 271 
PHE CE1 CZ   doub Y N 272 
PHE CE1 HE1  sing N N 273 
PHE CE2 CZ   sing Y N 274 
PHE CE2 HE2  sing N N 275 
PHE CZ  HZ   sing N N 276 
PHE OXT HXT  sing N N 277 
PRO N   CA   sing N N 278 
PRO N   CD   sing N N 279 
PRO N   H    sing N N 280 
PRO CA  C    sing N N 281 
PRO CA  CB   sing N N 282 
PRO CA  HA   sing N N 283 
PRO C   O    doub N N 284 
PRO C   OXT  sing N N 285 
PRO CB  CG   sing N N 286 
PRO CB  HB2  sing N N 287 
PRO CB  HB3  sing N N 288 
PRO CG  CD   sing N N 289 
PRO CG  HG2  sing N N 290 
PRO CG  HG3  sing N N 291 
PRO CD  HD2  sing N N 292 
PRO CD  HD3  sing N N 293 
PRO OXT HXT  sing N N 294 
SER N   CA   sing N N 295 
SER N   H    sing N N 296 
SER N   H2   sing N N 297 
SER CA  C    sing N N 298 
SER CA  CB   sing N N 299 
SER CA  HA   sing N N 300 
SER C   O    doub N N 301 
SER C   OXT  sing N N 302 
SER CB  OG   sing N N 303 
SER CB  HB2  sing N N 304 
SER CB  HB3  sing N N 305 
SER OG  HG   sing N N 306 
SER OXT HXT  sing N N 307 
THR N   CA   sing N N 308 
THR N   H    sing N N 309 
THR N   H2   sing N N 310 
THR CA  C    sing N N 311 
THR CA  CB   sing N N 312 
THR CA  HA   sing N N 313 
THR C   O    doub N N 314 
THR C   OXT  sing N N 315 
THR CB  OG1  sing N N 316 
THR CB  CG2  sing N N 317 
THR CB  HB   sing N N 318 
THR OG1 HG1  sing N N 319 
THR CG2 HG21 sing N N 320 
THR CG2 HG22 sing N N 321 
THR CG2 HG23 sing N N 322 
THR OXT HXT  sing N N 323 
TRP N   CA   sing N N 324 
TRP N   H    sing N N 325 
TRP N   H2   sing N N 326 
TRP CA  C    sing N N 327 
TRP CA  CB   sing N N 328 
TRP CA  HA   sing N N 329 
TRP C   O    doub N N 330 
TRP C   OXT  sing N N 331 
TRP CB  CG   sing N N 332 
TRP CB  HB2  sing N N 333 
TRP CB  HB3  sing N N 334 
TRP CG  CD1  doub Y N 335 
TRP CG  CD2  sing Y N 336 
TRP CD1 NE1  sing Y N 337 
TRP CD1 HD1  sing N N 338 
TRP CD2 CE2  doub Y N 339 
TRP CD2 CE3  sing Y N 340 
TRP NE1 CE2  sing Y N 341 
TRP NE1 HE1  sing N N 342 
TRP CE2 CZ2  sing Y N 343 
TRP CE3 CZ3  doub Y N 344 
TRP CE3 HE3  sing N N 345 
TRP CZ2 CH2  doub Y N 346 
TRP CZ2 HZ2  sing N N 347 
TRP CZ3 CH2  sing Y N 348 
TRP CZ3 HZ3  sing N N 349 
TRP CH2 HH2  sing N N 350 
TRP OXT HXT  sing N N 351 
TYR N   CA   sing N N 352 
TYR N   H    sing N N 353 
TYR N   H2   sing N N 354 
TYR CA  C    sing N N 355 
TYR CA  CB   sing N N 356 
TYR CA  HA   sing N N 357 
TYR C   O    doub N N 358 
TYR C   OXT  sing N N 359 
TYR CB  CG   sing N N 360 
TYR CB  HB2  sing N N 361 
TYR CB  HB3  sing N N 362 
TYR CG  CD1  doub Y N 363 
TYR CG  CD2  sing Y N 364 
TYR CD1 CE1  sing Y N 365 
TYR CD1 HD1  sing N N 366 
TYR CD2 CE2  doub Y N 367 
TYR CD2 HD2  sing N N 368 
TYR CE1 CZ   doub Y N 369 
TYR CE1 HE1  sing N N 370 
TYR CE2 CZ   sing Y N 371 
TYR CE2 HE2  sing N N 372 
TYR CZ  OH   sing N N 373 
TYR OH  HH   sing N N 374 
TYR OXT HXT  sing N N 375 
V26 C20 C21  doub Y N 376 
V26 C20 C19  sing Y N 377 
V26 C21 C22  sing Y N 378 
V26 C18 C19  sing N N 379 
V26 C18 C17  sing N N 380 
V26 C19 C24  doub Y N 381 
V26 C22 C23  doub Y N 382 
V26 C24 C23  sing Y N 383 
V26 C17 S14  sing N N 384 
V26 C26 N25  sing N N 385 
V26 O16 S14  doub N N 386 
V26 N25 C9   sing N N 387 
V26 S14 C8   sing N N 388 
V26 S14 O15  doub N N 389 
V26 C9  C8   doub Y N 390 
V26 C9  C10  sing Y N 391 
V26 C8  C7   sing Y N 392 
V26 F13 C10  sing N N 393 
V26 C10 C5   doub Y N 394 
V26 C7  F12  sing N N 395 
V26 C7  C6   doub Y N 396 
V26 C5  C6   sing Y N 397 
V26 C5  S1   sing N N 398 
V26 C6  F11  sing N N 399 
V26 N4  S1   sing N N 400 
V26 O2  S1   doub N N 401 
V26 S1  O3   doub N N 402 
V26 N25 H1   sing N N 403 
V26 C26 H2   sing N N 404 
V26 C26 H3   sing N N 405 
V26 C26 H4   sing N N 406 
V26 N4  H5   sing N N 407 
V26 N4  H6   sing N N 408 
V26 C17 H7   sing N N 409 
V26 C17 H8   sing N N 410 
V26 C18 H9   sing N N 411 
V26 C18 H10  sing N N 412 
V26 C24 H11  sing N N 413 
V26 C23 H12  sing N N 414 
V26 C22 H13  sing N N 415 
V26 C21 H14  sing N N 416 
V26 C20 H15  sing N N 417 
VAL N   CA   sing N N 418 
VAL N   H    sing N N 419 
VAL N   H2   sing N N 420 
VAL CA  C    sing N N 421 
VAL CA  CB   sing N N 422 
VAL CA  HA   sing N N 423 
VAL C   O    doub N N 424 
VAL C   OXT  sing N N 425 
VAL CB  CG1  sing N N 426 
VAL CB  CG2  sing N N 427 
VAL CB  HB   sing N N 428 
VAL CG1 HG11 sing N N 429 
VAL CG1 HG12 sing N N 430 
VAL CG1 HG13 sing N N 431 
VAL CG2 HG21 sing N N 432 
VAL CG2 HG22 sing N N 433 
VAL CG2 HG23 sing N N 434 
VAL OXT HXT  sing N N 435 
# 
_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                    5LLC 
_atom_sites.fract_transf_matrix[1][1]   0.023692 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.005953 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.024344 
_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]   0.014327 
_atom_sites.fract_transf_vector[1]      0.000000 
_atom_sites.fract_transf_vector[2]      0.000000 
_atom_sites.fract_transf_vector[3]      0.000000 
# 
loop_
_atom_type.symbol 
C  
F  
N  
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   ? 13.870  -0.057  6.551   1.00 24.93  ? 3   HIS A N   1 
ATOM   2    C  CA  . HIS A 1 3   ? 13.531  -1.071  7.624   1.00 24.41  ? 3   HIS A CA  1 
ATOM   3    C  C   . HIS A 1 3   ? 12.470  -0.546  8.597   1.00 26.72  ? 3   HIS A C   1 
ATOM   4    O  O   . HIS A 1 3   ? 12.793  -0.329  9.821   1.00 31.60  ? 3   HIS A O   1 
ATOM   5    C  CB  . HIS A 1 3   ? 14.739  -1.469  8.412   1.00 23.43  ? 3   HIS A CB  1 
ATOM   6    C  CG  . HIS A 1 3   ? 14.521  -2.720  9.142   1.00 23.44  ? 3   HIS A CG  1 
ATOM   7    N  ND1 . HIS A 1 3   ? 14.174  -2.761  10.472  1.00 25.65  ? 3   HIS A ND1 1 
ATOM   8    C  CD2 . HIS A 1 3   ? 14.545  -4.057  8.682   1.00 22.87  ? 3   HIS A CD2 1 
ATOM   9    C  CE1 . HIS A 1 3   ? 14.057  -4.045  10.849  1.00 23.62  ? 3   HIS A CE1 1 
ATOM   10   N  NE2 . HIS A 1 3   ? 14.280  -4.843  9.762   1.00 27.72  ? 3   HIS A NE2 1 
ATOM   11   N  N   . HIS A 1 4   ? 11.238  -0.334  8.093   1.00 48.12  ? 4   HIS A N   1 
ATOM   12   C  CA  . HIS A 1 4   ? 10.152  0.199   8.839   1.00 33.17  ? 4   HIS A CA  1 
ATOM   13   C  C   . HIS A 1 4   ? 9.489   -0.963  9.624   1.00 19.32  ? 4   HIS A C   1 
ATOM   14   O  O   . HIS A 1 4   ? 9.658   -2.153  9.326   1.00 18.89  ? 4   HIS A O   1 
ATOM   15   C  CB  . HIS A 1 4   ? 9.196   0.863   7.822   1.00 69.28  ? 4   HIS A CB  1 
ATOM   16   C  CG  . HIS A 1 4   ? 8.564   2.121   8.319   1.00 75.51  ? 4   HIS A CG  1 
ATOM   17   N  ND1 . HIS A 1 4   ? 9.265   3.077   8.983   1.00 91.31  ? 4   HIS A ND1 1 
ATOM   18   C  CD2 . HIS A 1 4   ? 7.240   2.579   8.227   1.00 85.43  ? 4   HIS A CD2 1 
ATOM   19   C  CE1 . HIS A 1 4   ? 8.433   4.093   9.301   1.00 106.51 ? 4   HIS A CE1 1 
ATOM   20   N  NE2 . HIS A 1 4   ? 7.190   3.788   8.830   1.00 119.96 ? 4   HIS A NE2 1 
ATOM   21   N  N   . TRP A 1 5   ? 8.739   -0.607  10.609  1.00 17.19  ? 5   TRP A N   1 
ATOM   22   C  CA  . TRP A 1 5   ? 8.016   -1.545  11.430  1.00 15.08  ? 5   TRP A CA  1 
ATOM   23   C  C   . TRP A 1 5   ? 7.024   -2.304  10.610  1.00 13.64  ? 5   TRP A C   1 
ATOM   24   O  O   . TRP A 1 5   ? 6.494   -1.846  9.580   1.00 15.77  ? 5   TRP A O   1 
ATOM   25   C  CB  . TRP A 1 5   ? 7.333   -0.839  12.598  1.00 13.74  ? 5   TRP A CB  1 
ATOM   26   C  CG  . TRP A 1 5   ? 6.133   -0.029  12.187  1.00 12.94  ? 5   TRP A CG  1 
ATOM   27   C  CD1 . TRP A 1 5   ? 6.101   1.313   11.854  1.00 15.86  ? 5   TRP A CD1 1 
ATOM   28   C  CD2 . TRP A 1 5   ? 4.774   -0.494  12.113  1.00 12.01  ? 5   TRP A CD2 1 
ATOM   29   N  NE1 . TRP A 1 5   ? 4.823   1.719   11.573  1.00 14.44  ? 5   TRP A NE1 1 
ATOM   30   C  CE2 . TRP A 1 5   ? 3.980   0.639   11.691  1.00 13.15  ? 5   TRP A CE2 1 
ATOM   31   C  CE3 . TRP A 1 5   ? 4.169   -1.718  12.361  1.00 11.93  ? 5   TRP A CE3 1 
ATOM   32   C  CZ2 . TRP A 1 5   ? 2.586   0.568   11.560  1.00 14.68  ? 5   TRP A CZ2 1 
ATOM   33   C  CZ3 . TRP A 1 5   ? 2.772   -1.803  12.187  1.00 12.52  ? 5   TRP A CZ3 1 
ATOM   34   C  CH2 . TRP A 1 5   ? 2.007   -0.684  11.796  1.00 14.20  ? 5   TRP A CH2 1 
ATOM   35   N  N   . GLY A 1 6   ? 6.682   -3.512  11.092  1.00 13.94  ? 6   GLY A N   1 
ATOM   36   C  CA  . GLY A 1 6   ? 5.624   -4.313  10.398  1.00 15.18  ? 6   GLY A CA  1 
ATOM   37   C  C   . GLY A 1 6   ? 5.263   -5.472  11.282  1.00 14.22  ? 6   GLY A C   1 
ATOM   38   O  O   . GLY A 1 6   ? 5.282   -5.327  12.516  1.00 13.99  ? 6   GLY A O   1 
ATOM   39   N  N   A TYR A 1 7   ? 4.826   -6.515  10.567  0.50 12.11  ? 7   TYR A N   1 
ATOM   40   N  N   B TYR A 1 7   ? 5.120   -6.718  10.878  0.50 18.01  ? 7   TYR A N   1 
ATOM   41   C  CA  A TYR A 1 7   ? 4.330   -7.768  11.161  0.50 9.80   ? 7   TYR A CA  1 
ATOM   42   C  CA  B TYR A 1 7   ? 4.834   -7.781  11.904  0.50 13.28  ? 7   TYR A CA  1 
ATOM   43   C  C   A TYR A 1 7   ? 5.148   -9.002  10.719  0.50 15.75  ? 7   TYR A C   1 
ATOM   44   C  C   B TYR A 1 7   ? 5.705   -9.076  11.832  0.50 16.06  ? 7   TYR A C   1 
ATOM   45   O  O   A TYR A 1 7   ? 4.556   -10.104 10.481  0.50 16.09  ? 7   TYR A O   1 
ATOM   46   O  O   B TYR A 1 7   ? 5.327   -10.127 12.478  0.50 22.17  ? 7   TYR A O   1 
ATOM   47   C  CB  A TYR A 1 7   ? 2.813   -7.969  11.012  0.50 9.88   ? 7   TYR A CB  1 
ATOM   48   C  CB  B TYR A 1 7   ? 3.395   -8.215  11.674  0.50 13.71  ? 7   TYR A CB  1 
ATOM   49   C  CG  A TYR A 1 7   ? 2.064   -6.886  11.668  0.50 8.07   ? 7   TYR A CG  1 
ATOM   50   C  CG  B TYR A 1 7   ? 2.383   -7.148  12.158  0.50 12.99  ? 7   TYR A CG  1 
ATOM   51   C  CD1 A TYR A 1 7   ? 1.729   -7.002  13.019  0.50 9.07   ? 7   TYR A CD1 1 
ATOM   52   C  CD1 B TYR A 1 7   ? 1.884   -7.186  13.453  0.50 12.23  ? 7   TYR A CD1 1 
ATOM   53   C  CD2 A TYR A 1 7   ? 1.544   -5.838  10.908  0.50 8.61   ? 7   TYR A CD2 1 
ATOM   54   C  CD2 B TYR A 1 7   ? 1.895   -6.160  11.296  0.50 13.26  ? 7   TYR A CD2 1 
ATOM   55   C  CE1 A TYR A 1 7   ? 0.915   -6.026  13.608  0.50 7.89   ? 7   TYR A CE1 1 
ATOM   56   C  CE1 B TYR A 1 7   ? 0.974   -6.186  13.896  0.50 12.11  ? 7   TYR A CE1 1 
ATOM   57   C  CE2 A TYR A 1 7   ? 0.754   -4.862  11.502  0.50 9.01   ? 7   TYR A CE2 1 
ATOM   58   C  CE2 B TYR A 1 7   ? 1.001   -5.155  11.733  0.50 12.91  ? 7   TYR A CE2 1 
ATOM   59   C  CZ  A TYR A 1 7   ? 0.436   -4.979  12.840  0.50 8.54   ? 7   TYR A CZ  1 
ATOM   60   C  CZ  B TYR A 1 7   ? 0.516   -5.209  13.040  0.50 10.82  ? 7   TYR A CZ  1 
ATOM   61   O  OH  A TYR A 1 7   ? -0.351  -4.017  13.367  0.50 9.32   ? 7   TYR A OH  1 
ATOM   62   O  OH  B TYR A 1 7   ? -0.349  -4.219  13.499  0.50 12.50  ? 7   TYR A OH  1 
ATOM   63   N  N   A GLY A 1 8   ? 6.479   -8.845  10.790  0.50 21.17  ? 8   GLY A N   1 
ATOM   64   N  N   B GLY A 1 8   ? 6.801   -9.006  11.096  0.50 20.71  ? 8   GLY A N   1 
ATOM   65   C  CA  A GLY A 1 8   ? 7.452   -9.952  10.774  0.50 23.27  ? 8   GLY A CA  1 
ATOM   66   C  CA  B GLY A 1 8   ? 7.647   -10.154 10.904  0.50 11.82  ? 8   GLY A CA  1 
ATOM   67   C  C   A GLY A 1 8   ? 8.590   -10.143 11.856  0.50 15.73  ? 8   GLY A C   1 
ATOM   68   C  C   B GLY A 1 8   ? 8.703   -10.280 11.970  0.50 26.65  ? 8   GLY A C   1 
ATOM   69   O  O   A GLY A 1 8   ? 8.699   -9.513  12.905  0.50 22.00  ? 8   GLY A O   1 
ATOM   70   O  O   B GLY A 1 8   ? 8.742   -9.519  12.943  0.50 18.43  ? 8   GLY A O   1 
ATOM   71   N  N   A LYS A 1 9   ? 9.446   -11.108 11.613  0.50 16.62  ? 9   LYS A N   1 
ATOM   72   N  N   B LYS A 1 9   ? 9.563   -11.262 11.742  0.50 39.09  ? 9   LYS A N   1 
ATOM   73   C  CA  A LYS A 1 9   ? 10.510  -11.499 12.535  0.50 19.58  ? 9   LYS A CA  1 
ATOM   74   C  CA  B LYS A 1 9   ? 10.610  -11.689 12.642  0.50 33.80  ? 9   LYS A CA  1 
ATOM   75   C  C   A LYS A 1 9   ? 11.463  -10.400 12.895  0.50 17.89  ? 9   LYS A C   1 
ATOM   76   C  C   B LYS A 1 9   ? 11.529  -10.533 12.880  0.50 33.21  ? 9   LYS A C   1 
ATOM   77   O  O   A LYS A 1 9   ? 11.848  -10.332 14.030  0.50 19.01  ? 9   LYS A O   1 
ATOM   78   O  O   B LYS A 1 9   ? 12.013  -10.352 13.985  0.50 47.02  ? 9   LYS A O   1 
ATOM   79   C  CB  A LYS A 1 9   ? 11.382  -12.548 11.956  0.50 22.21  ? 9   LYS A CB  1 
ATOM   80   C  CB  B LYS A 1 9   ? 11.398  -12.824 12.008  0.50 43.82  ? 9   LYS A CB  1 
ATOM   81   C  CG  A LYS A 1 9   ? 12.390  -13.096 12.905  0.50 28.25  ? 9   LYS A CG  1 
ATOM   82   C  CG  B LYS A 1 9   ? 12.670  -13.216 12.743  0.50 52.29  ? 9   LYS A CG  1 
ATOM   83   C  CD  A LYS A 1 9   ? 13.020  -14.332 12.331  0.50 31.71  ? 9   LYS A CD  1 
ATOM   84   C  CD  B LYS A 1 9   ? 12.959  -14.697 12.565  0.50 56.75  ? 9   LYS A CD  1 
ATOM   85   C  CE  A LYS A 1 9   ? 13.068  -15.361 13.414  0.50 43.05  ? 9   LYS A CE  1 
ATOM   86   C  CE  B LYS A 1 9   ? 14.439  -15.048 12.598  0.50 57.67  ? 9   LYS A CE  1 
ATOM   87   N  NZ  A LYS A 1 9   ? 14.491  -15.421 13.817  0.50 55.21  ? 9   LYS A NZ  1 
ATOM   88   N  NZ  B LYS A 1 9   ? 15.050  -15.515 11.302  0.50 49.60  ? 9   LYS A NZ  1 
ATOM   89   N  N   A HIS A 1 10  ? 11.960  -9.655  11.889  0.50 16.35  ? 10  HIS A N   1 
ATOM   90   N  N   B HIS A 1 10  ? 11.728  -9.780  11.795  0.50 23.35  ? 10  HIS A N   1 
ATOM   91   C  CA  A HIS A 1 10  ? 12.920  -8.694  12.160  0.50 12.86  ? 10  HIS A CA  1 
ATOM   92   C  CA  B HIS A 1 10  ? 12.742  -8.832  11.657  0.50 22.22  ? 10  HIS A CA  1 
ATOM   93   C  C   A HIS A 1 10  ? 12.280  -7.380  12.258  0.50 14.02  ? 10  HIS A C   1 
ATOM   94   C  C   B HIS A 1 10  ? 12.228  -7.486  12.068  0.50 19.54  ? 10  HIS A C   1 
ATOM   95   O  O   A HIS A 1 10  ? 12.997  -6.492  12.563  0.50 21.18  ? 10  HIS A O   1 
ATOM   96   O  O   B HIS A 1 10  ? 12.965  -6.681  12.514  0.50 21.99  ? 10  HIS A O   1 
ATOM   97   C  CB  A HIS A 1 10  ? 13.960  -8.687  11.064  0.50 14.08  ? 10  HIS A CB  1 
ATOM   98   C  CB  B HIS A 1 10  ? 13.286  -8.917  10.183  0.50 18.59  ? 10  HIS A CB  1 
ATOM   99   C  CG  A HIS A 1 10  ? 14.551  -10.035 10.820  0.50 12.99  ? 10  HIS A CG  1 
ATOM   100  C  CG  B HIS A 1 10  ? 13.777  -10.334 9.780   0.50 19.72  ? 10  HIS A CG  1 
ATOM   101  N  ND1 A HIS A 1 10  ? 15.562  -10.528 11.548  0.50 16.05  ? 10  HIS A ND1 1 
ATOM   102  N  ND1 B HIS A 1 10  ? 14.698  -10.980 10.472  0.50 21.05  ? 10  HIS A ND1 1 
ATOM   103  C  CD2 A HIS A 1 10  ? 14.179  -10.997 9.947   0.50 15.23  ? 10  HIS A CD2 1 
ATOM   104  C  CD2 B HIS A 1 10  ? 13.420  -11.177 8.710   0.50 18.64  ? 10  HIS A CD2 1 
ATOM   105  C  CE1 A HIS A 1 10  ? 15.833  -11.760 11.117  0.50 14.87  ? 10  HIS A CE1 1 
ATOM   106  C  CE1 B HIS A 1 10  ? 14.938  -12.168 9.933   0.50 25.30  ? 10  HIS A CE1 1 
ATOM   107  N  NE2 A HIS A 1 10  ? 14.996  -12.043 10.117  0.50 15.18  ? 10  HIS A NE2 1 
ATOM   108  N  NE2 B HIS A 1 10  ? 14.188  -12.285 8.815   0.50 21.81  ? 10  HIS A NE2 1 
ATOM   109  N  N   . ASN A 1 11  ? 10.876  -7.264  12.056  1.00 20.41  ? 11  ASN A N   1 
ATOM   110  C  CA  . ASN A 1 11  ? 10.285  -5.931  12.182  1.00 17.17  ? 11  ASN A CA  1 
ATOM   111  C  C   . ASN A 1 11  ? 8.947   -5.926  12.930  1.00 17.60  ? 11  ASN A C   1 
ATOM   112  O  O   . ASN A 1 11  ? 8.337   -4.882  13.050  1.00 16.69  ? 11  ASN A O   1 
ATOM   113  C  CB  . ASN A 1 11  ? 10.090  -5.157  10.882  1.00 16.76  ? 11  ASN A CB  1 
ATOM   114  C  CG  . ASN A 1 11  ? 9.029   -5.772  9.970   1.00 17.58  ? 11  ASN A CG  1 
ATOM   115  O  OD1 . ASN A 1 11  ? 8.402   -6.778  10.305  1.00 21.54  ? 11  ASN A OD1 1 
ATOM   116  N  ND2 . ASN A 1 11  ? 8.799   -5.157  8.833   1.00 19.07  ? 11  ASN A ND2 1 
ATOM   117  N  N   . GLY A 1 12  ? 8.564   -7.052  13.512  1.00 16.75  ? 12  GLY A N   1 
ATOM   118  C  CA  . GLY A 1 12  ? 7.339   -7.240  14.254  1.00 15.51  ? 12  GLY A CA  1 
ATOM   119  C  C   . GLY A 1 12  ? 7.277   -6.660  15.617  1.00 13.68  ? 12  GLY A C   1 
ATOM   120  O  O   . GLY A 1 12  ? 8.207   -5.965  16.057  1.00 14.30  ? 12  GLY A O   1 
ATOM   121  N  N   . PRO A 1 13  ? 6.211   -6.957  16.323  1.00 12.51  ? 13  PRO A N   1 
ATOM   122  C  CA  . PRO A 1 13  ? 5.944   -6.350  17.632  1.00 12.29  ? 13  PRO A CA  1 
ATOM   123  C  C   . PRO A 1 13  ? 7.073   -6.392  18.593  1.00 12.73  ? 13  PRO A C   1 
ATOM   124  O  O   . PRO A 1 13  ? 7.222   -5.422  19.370  1.00 13.42  ? 13  PRO A O   1 
ATOM   125  C  CB  . PRO A 1 13  ? 4.729   -7.133  18.087  1.00 13.39  ? 13  PRO A CB  1 
ATOM   126  C  CG  . PRO A 1 13  ? 3.955   -7.385  16.888  1.00 13.71  ? 13  PRO A CG  1 
ATOM   127  C  CD  . PRO A 1 13  ? 5.029   -7.667  15.825  1.00 14.01  ? 13  PRO A CD  1 
ATOM   128  N  N   . GLU A 1 14  ? 7.897   -7.443  18.632  1.00 14.04  ? 14  GLU A N   1 
ATOM   129  C  CA  . GLU A 1 14  ? 8.987   -7.482  19.590  1.00 16.70  ? 14  GLU A CA  1 
ATOM   130  C  C   . GLU A 1 14  ? 10.119  -6.500  19.282  1.00 15.75  ? 14  GLU A C   1 
ATOM   131  O  O   . GLU A 1 14  ? 10.998  -6.270  20.115  1.00 16.58  ? 14  GLU A O   1 
ATOM   132  C  CB  . GLU A 1 14  ? 9.468   -8.933  19.639  1.00 21.03  ? 14  GLU A CB  1 
ATOM   133  C  CG  . GLU A 1 14  ? 10.029  -9.481  18.321  1.00 23.29  ? 14  GLU A CG  1 
ATOM   134  C  CD  . GLU A 1 14  ? 9.216   -10.030 17.115  1.00 26.60  ? 14  GLU A CD  1 
ATOM   135  O  OE1 . GLU A 1 14  ? 8.049   -9.621  16.939  1.00 22.19  ? 14  GLU A OE1 1 
ATOM   136  O  OE2 . GLU A 1 14  ? 9.768   -10.861 16.364  1.00 26.73  ? 14  GLU A OE2 1 
ATOM   137  N  N   . HIS A 1 15  ? 10.099  -5.929  18.098  1.00 14.02  ? 15  HIS A N   1 
ATOM   138  C  CA  . HIS A 1 15  ? 11.115  -4.920  17.720  1.00 14.07  ? 15  HIS A CA  1 
ATOM   139  C  C   . HIS A 1 15  ? 10.662  -3.461  17.868  1.00 12.57  ? 15  HIS A C   1 
ATOM   140  O  O   . HIS A 1 15  ? 11.510  -2.538  17.813  1.00 14.77  ? 15  HIS A O   1 
ATOM   141  C  CB  . HIS A 1 15  ? 11.483  -5.104  16.263  1.00 15.32  ? 15  HIS A CB  1 
ATOM   142  C  CG  . HIS A 1 15  ? 12.175  -6.362  16.010  1.00 18.33  ? 15  HIS A CG  1 
ATOM   143  N  ND1 . HIS A 1 15  ? 13.568  -6.473  16.100  1.00 20.49  ? 15  HIS A ND1 1 
ATOM   144  C  CD2 . HIS A 1 15  ? 11.690  -7.590  15.626  1.00 19.54  ? 15  HIS A CD2 1 
ATOM   145  C  CE1 . HIS A 1 15  ? 13.899  -7.746  15.835  1.00 24.52  ? 15  HIS A CE1 1 
ATOM   146  N  NE2 . HIS A 1 15  ? 12.803  -8.448  15.538  1.00 22.39  ? 15  HIS A NE2 1 
ATOM   147  N  N   . TRP A 1 16  ? 9.364   -3.252  18.036  1.00 12.00  ? 16  TRP A N   1 
ATOM   148  C  CA  . TRP A 1 16  ? 8.829   -1.885  17.903  1.00 11.57  ? 16  TRP A CA  1 
ATOM   149  C  C   . TRP A 1 16  ? 9.413   -0.946  18.939  1.00 11.56  ? 16  TRP A C   1 
ATOM   150  O  O   . TRP A 1 16  ? 9.514   0.272   18.682  1.00 12.39  ? 16  TRP A O   1 
ATOM   151  C  CB  . TRP A 1 16  ? 7.298   -1.951  18.016  1.00 12.23  ? 16  TRP A CB  1 
ATOM   152  C  CG  . TRP A 1 16  ? 6.589   -2.607  16.860  1.00 10.51  ? 16  TRP A CG  1 
ATOM   153  C  CD1 . TRP A 1 16  ? 7.138   -3.080  15.684  1.00 11.42  ? 16  TRP A CD1 1 
ATOM   154  C  CD2 . TRP A 1 16  ? 5.222   -2.953  16.844  1.00 9.71   ? 16  TRP A CD2 1 
ATOM   155  N  NE1 . TRP A 1 16  ? 6.167   -3.634  14.923  1.00 11.19  ? 16  TRP A NE1 1 
ATOM   156  C  CE2 . TRP A 1 16  ? 5.003   -3.573  15.583  1.00 10.13  ? 16  TRP A CE2 1 
ATOM   157  C  CE3 . TRP A 1 16  ? 4.163   -2.771  17.736  1.00 10.36  ? 16  TRP A CE3 1 
ATOM   158  C  CZ2 . TRP A 1 16  ? 3.721   -4.003  15.194  1.00 10.41  ? 16  TRP A CZ2 1 
ATOM   159  C  CZ3 . TRP A 1 16  ? 2.906   -3.188  17.353  1.00 10.13  ? 16  TRP A CZ3 1 
ATOM   160  C  CH2 . TRP A 1 16  ? 2.687   -3.792  16.108  1.00 10.85  ? 16  TRP A CH2 1 
ATOM   161  N  N   . HIS A 1 17  ? 9.776   -1.465  20.082  1.00 12.20  ? 17  HIS A N   1 
ATOM   162  C  CA  . HIS A 1 17  ? 10.256  -0.601  21.144  1.00 12.92  ? 17  HIS A CA  1 
ATOM   163  C  C   . HIS A 1 17  ? 11.508  0.168   20.774  1.00 14.44  ? 17  HIS A C   1 
ATOM   164  O  O   . HIS A 1 17  ? 11.791  1.237   21.401  1.00 15.36  ? 17  HIS A O   1 
ATOM   165  C  CB  . HIS A 1 17  ? 10.565  -1.345  22.453  1.00 13.62  ? 17  HIS A CB  1 
ATOM   166  C  CG  . HIS A 1 17  ? 11.785  -2.218  22.366  1.00 15.66  ? 17  HIS A CG  1 
ATOM   167  N  ND1 . HIS A 1 17  ? 13.010  -1.848  22.889  1.00 19.10  ? 17  HIS A ND1 1 
ATOM   168  C  CD2 . HIS A 1 17  ? 11.941  -3.407  21.758  1.00 15.80  ? 17  HIS A CD2 1 
ATOM   169  C  CE1 . HIS A 1 17  ? 13.862  -2.770  22.628  1.00 20.94  ? 17  HIS A CE1 1 
ATOM   170  N  NE2 . HIS A 1 17  ? 13.280  -3.733  21.954  1.00 19.02  ? 17  HIS A NE2 1 
ATOM   171  N  N   . LYS A 1 18  ? 12.287  -0.324  19.798  1.00 14.85  ? 18  LYS A N   1 
ATOM   172  C  CA  . LYS A 1 18  ? 13.539  0.407   19.451  1.00 17.27  ? 18  LYS A CA  1 
ATOM   173  C  C   . LYS A 1 18  ? 13.202  1.748   18.823  1.00 17.44  ? 18  LYS A C   1 
ATOM   174  O  O   . LYS A 1 18  ? 13.859  2.783   19.126  1.00 23.05  ? 18  LYS A O   1 
ATOM   175  C  CB  . LYS A 1 18  ? 14.351  -0.462  18.535  1.00 18.70  ? 18  LYS A CB  1 
ATOM   176  C  CG  . LYS A 1 18  ? 14.950  -1.644  19.277  1.00 18.76  ? 18  LYS A CG  1 
ATOM   177  C  CD  . LYS A 1 18  ? 15.691  -2.598  18.296  1.00 18.79  ? 18  LYS A CD  1 
ATOM   178  C  CE  . LYS A 1 18  ? 14.713  -3.616  17.700  1.00 20.36  ? 18  LYS A CE  1 
ATOM   179  N  NZ  . LYS A 1 18  ? 15.351  -4.391  16.568  1.00 20.41  ? 18  LYS A NZ  1 
ATOM   180  N  N   . ASP A 1 19  ? 12.217  1.804   17.922  1.00 17.18  ? 19  ASP A N   1 
ATOM   181  C  CA  . ASP A 1 19  ? 11.761  3.071   17.309  1.00 17.35  ? 19  ASP A CA  1 
ATOM   182  C  C   . ASP A 1 19  ? 10.750  3.819   18.190  1.00 16.69  ? 19  ASP A C   1 
ATOM   183  O  O   . ASP A 1 19  ? 10.646  5.037   18.110  1.00 17.70  ? 19  ASP A O   1 
ATOM   184  C  CB  . ASP A 1 19  ? 11.235  2.837   15.920  1.00 21.52  ? 19  ASP A CB  1 
ATOM   185  C  CG  . ASP A 1 19  ? 12.337  2.838   14.865  1.00 31.80  ? 19  ASP A CG  1 
ATOM   186  O  OD1 . ASP A 1 19  ? 13.372  3.492   15.062  1.00 31.91  ? 19  ASP A OD1 1 
ATOM   187  O  OD2 . ASP A 1 19  ? 12.158  2.139   13.850  1.00 50.26  ? 19  ASP A OD2 1 
ATOM   188  N  N   . PHE A 1 20  ? 9.976   3.092   19.001  1.00 14.55  ? 20  PHE A N   1 
ATOM   189  C  CA  . PHE A 1 20  ? 8.872   3.673   19.716  1.00 13.89  ? 20  PHE A CA  1 
ATOM   190  C  C   . PHE A 1 20  ? 8.982   3.151   21.146  1.00 13.48  ? 20  PHE A C   1 
ATOM   191  O  O   . PHE A 1 20  ? 8.311   2.161   21.514  1.00 13.06  ? 20  PHE A O   1 
ATOM   192  C  CB  . PHE A 1 20  ? 7.564   3.167   19.076  1.00 13.19  ? 20  PHE A CB  1 
ATOM   193  C  CG  . PHE A 1 20  ? 7.457   3.543   17.666  1.00 14.28  ? 20  PHE A CG  1 
ATOM   194  C  CD1 . PHE A 1 20  ? 7.072   4.850   17.330  1.00 16.59  ? 20  PHE A CD1 1 
ATOM   195  C  CD2 . PHE A 1 20  ? 7.861   2.640   16.660  1.00 16.18  ? 20  PHE A CD2 1 
ATOM   196  C  CE1 . PHE A 1 20  ? 7.109   5.225   15.978  1.00 17.26  ? 20  PHE A CE1 1 
ATOM   197  C  CE2 . PHE A 1 20  ? 7.872   3.034   15.318  1.00 18.73  ? 20  PHE A CE2 1 
ATOM   198  C  CZ  . PHE A 1 20  ? 7.444   4.312   14.996  1.00 17.95  ? 20  PHE A CZ  1 
ATOM   199  N  N   . PRO A 1 21  ? 9.836   3.774   21.979  1.00 14.76  ? 21  PRO A N   1 
ATOM   200  C  CA  . PRO A 1 21  ? 10.068  3.258   23.309  1.00 15.31  ? 21  PRO A CA  1 
ATOM   201  C  C   . PRO A 1 21  ? 8.811   3.168   24.219  1.00 13.86  ? 21  PRO A C   1 
ATOM   202  O  O   . PRO A 1 21  ? 8.854   2.389   25.207  1.00 14.05  ? 21  PRO A O   1 
ATOM   203  C  CB  . PRO A 1 21  ? 11.143  4.164   23.923  1.00 17.87  ? 21  PRO A CB  1 
ATOM   204  C  CG  . PRO A 1 21  ? 11.294  5.215   22.946  1.00 25.84  ? 21  PRO A CG  1 
ATOM   205  C  CD  . PRO A 1 21  ? 10.783  4.831   21.621  1.00 17.09  ? 21  PRO A CD  1 
ATOM   206  N  N   A ILE A 1 22  ? 7.764   3.942   23.958  0.50 13.36  ? 22  ILE A N   1 
ATOM   207  N  N   B ILE A 1 22  ? 7.762   3.927   23.933  0.50 13.40  ? 22  ILE A N   1 
ATOM   208  C  CA  A ILE A 1 22  ? 6.529   3.838   24.702  0.50 14.10  ? 22  ILE A CA  1 
ATOM   209  C  CA  B ILE A 1 22  ? 6.506   3.797   24.627  0.50 12.11  ? 22  ILE A CA  1 
ATOM   210  C  C   A ILE A 1 22  ? 5.926   2.422   24.561  0.50 12.06  ? 22  ILE A C   1 
ATOM   211  C  C   B ILE A 1 22  ? 5.914   2.414   24.542  0.50 11.54  ? 22  ILE A C   1 
ATOM   212  O  O   A ILE A 1 22  ? 4.998   2.072   25.307  0.50 12.77  ? 22  ILE A O   1 
ATOM   213  O  O   B ILE A 1 22  ? 4.997   2.071   25.305  0.50 12.75  ? 22  ILE A O   1 
ATOM   214  C  CB  A ILE A 1 22  ? 5.507   4.906   24.218  0.50 13.55  ? 22  ILE A CB  1 
ATOM   215  C  CB  B ILE A 1 22  ? 5.523   4.891   24.177  0.50 11.79  ? 22  ILE A CB  1 
ATOM   216  C  CG1 A ILE A 1 22  ? 4.349   5.141   25.225  0.50 17.17  ? 22  ILE A CG1 1 
ATOM   217  C  CG1 B ILE A 1 22  ? 4.453   5.198   25.244  0.50 12.39  ? 22  ILE A CG1 1 
ATOM   218  C  CG2 A ILE A 1 22  ? 4.962   4.559   22.807  0.50 14.49  ? 22  ILE A CG2 1 
ATOM   219  C  CG2 B ILE A 1 22  ? 4.906   4.539   22.782  0.50 11.24  ? 22  ILE A CG2 1 
ATOM   220  C  CD1 A ILE A 1 22  ? 4.857   5.634   26.550  0.50 22.86  ? 22  ILE A CD1 1 
ATOM   221  C  CD1 B ILE A 1 22  ? 3.552   6.320   24.826  0.50 12.21  ? 22  ILE A CD1 1 
ATOM   222  N  N   . ALA A 1 23  ? 6.438   1.571   23.643  1.00 11.41  ? 23  ALA A N   1 
ATOM   223  C  CA  . ALA A 1 23  ? 6.008   0.200   23.535  1.00 11.26  ? 23  ALA A CA  1 
ATOM   224  C  C   . ALA A 1 23  ? 6.076   -0.520  24.876  1.00 12.33  ? 23  ALA A C   1 
ATOM   225  O  O   . ALA A 1 23  ? 5.361   -1.535  25.058  1.00 12.32  ? 23  ALA A O   1 
ATOM   226  C  CB  . ALA A 1 23  ? 6.825   -0.550  22.513  1.00 11.50  ? 23  ALA A CB  1 
ATOM   227  N  N   . LYS A 1 24  ? 7.021   -0.091  25.765  1.00 12.98  ? 24  LYS A N   1 
ATOM   228  C  CA  . LYS A 1 24  ? 7.181   -0.698  27.080  1.00 13.85  ? 24  LYS A CA  1 
ATOM   229  C  C   . LYS A 1 24  ? 6.545   0.212   28.151  1.00 14.96  ? 24  LYS A C   1 
ATOM   230  O  O   . LYS A 1 24  ? 6.924   0.086   29.342  1.00 16.35  ? 24  LYS A O   1 
ATOM   231  C  CB  . LYS A 1 24  ? 8.668   -0.959  27.391  1.00 15.30  ? 24  LYS A CB  1 
ATOM   232  C  CG  . LYS A 1 24  ? 9.293   -1.930  26.375  1.00 16.86  ? 24  LYS A CG  1 
ATOM   233  C  CD  . LYS A 1 24  ? 10.748  -2.146  26.786  1.00 20.51  ? 24  LYS A CD  1 
ATOM   234  C  CE  . LYS A 1 24  ? 11.491  -3.113  25.893  1.00 23.95  ? 24  LYS A CE  1 
ATOM   235  N  NZ  . LYS A 1 24  ? 11.153  -4.517  26.029  1.00 31.93  ? 24  LYS A NZ  1 
ATOM   236  N  N   . GLY A 1 25  ? 5.564   1.000   27.798  1.00 13.36  ? 25  GLY A N   1 
ATOM   237  C  CA  . GLY A 1 25  ? 4.937   1.999   28.675  1.00 14.62  ? 25  GLY A CA  1 
ATOM   238  C  C   . GLY A 1 25  ? 3.968   1.348   29.666  1.00 13.17  ? 25  GLY A C   1 
ATOM   239  O  O   . GLY A 1 25  ? 3.785   0.129   29.764  1.00 14.06  ? 25  GLY A O   1 
ATOM   240  N  N   . GLU A 1 26  ? 3.325   2.243   30.409  1.00 14.18  ? 26  GLU A N   1 
ATOM   241  C  CA  . GLU A 1 26  ? 2.447   1.868   31.507  1.00 14.86  ? 26  GLU A CA  1 
ATOM   242  C  C   . GLU A 1 26  ? 1.004   1.608   31.116  1.00 12.06  ? 26  GLU A C   1 
ATOM   243  O  O   . GLU A 1 26  ? 0.242   1.110   31.952  1.00 14.16  ? 26  GLU A O   1 
ATOM   244  C  CB  . GLU A 1 26  ? 2.432   2.963   32.601  1.00 19.85  ? 26  GLU A CB  1 
ATOM   245  C  CG  . GLU A 1 26  ? 3.817   3.172   33.180  1.00 22.50  ? 26  GLU A CG  1 
ATOM   246  C  CD  . GLU A 1 26  ? 4.425   1.890   33.773  1.00 28.62  ? 26  GLU A CD  1 
ATOM   247  O  OE1 . GLU A 1 26  ? 3.724   1.204   34.589  1.00 31.29  ? 26  GLU A OE1 1 
ATOM   248  O  OE2 . GLU A 1 26  ? 5.631   1.620   33.461  1.00 34.58  ? 26  GLU A OE2 1 
ATOM   249  N  N   . ARG A 1 27  ? 0.605   1.929   29.885  1.00 10.69  ? 27  ARG A N   1 
ATOM   250  C  CA  . ARG A 1 27  ? -0.798  1.690   29.515  1.00 9.27   ? 27  ARG A CA  1 
ATOM   251  C  C   . ARG A 1 27  ? -0.866  1.250   28.039  1.00 8.55   ? 27  ARG A C   1 
ATOM   252  O  O   . ARG A 1 27  ? -1.539  1.875   27.196  1.00 9.09   ? 27  ARG A O   1 
ATOM   253  C  CB  . ARG A 1 27  ? -1.723  2.898   29.814  1.00 12.33  ? 27  ARG A CB  1 
ATOM   254  C  CG  . ARG A 1 27  ? -1.369  4.218   29.247  1.00 13.52  ? 27  ARG A CG  1 
ATOM   255  C  CD  . ARG A 1 27  ? -2.448  5.257   29.532  1.00 16.03  ? 27  ARG A CD  1 
ATOM   256  N  NE  . ARG A 1 27  ? -3.533  5.233   28.553  1.00 13.47  ? 27  ARG A NE  1 
ATOM   257  C  CZ  . ARG A 1 27  ? -4.417  6.211   28.402  1.00 11.80  ? 27  ARG A CZ  1 
ATOM   258  N  NH1 . ARG A 1 27  ? -4.351  7.293   29.163  1.00 15.75  ? 27  ARG A NH1 1 
ATOM   259  N  NH2 . ARG A 1 27  ? -5.370  6.103   27.485  1.00 12.89  ? 27  ARG A NH2 1 
ATOM   260  N  N   . GLN A 1 28  ? -0.150  0.187   27.746  1.00 8.30   ? 28  GLN A N   1 
ATOM   261  C  CA  . GLN A 1 28  ? -0.115  -0.352  26.386  1.00 8.26   ? 28  GLN A CA  1 
ATOM   262  C  C   . GLN A 1 28  ? -1.277  -1.315  26.134  1.00 7.50   ? 28  GLN A C   1 
ATOM   263  O  O   . GLN A 1 28  ? -1.769  -2.002  27.024  1.00 8.71   ? 28  GLN A O   1 
ATOM   264  C  CB  . GLN A 1 28  ? 1.223   -1.029  26.154  1.00 9.04   ? 28  GLN A CB  1 
ATOM   265  C  CG  . GLN A 1 28  ? 2.369   0.023   26.042  1.00 9.51   ? 28  GLN A CG  1 
ATOM   266  C  CD  . GLN A 1 28  ? 2.269   0.797   24.758  1.00 8.62   ? 28  GLN A CD  1 
ATOM   267  O  OE1 . GLN A 1 28  ? 2.452   0.239   23.666  1.00 8.87   ? 28  GLN A OE1 1 
ATOM   268  N  NE2 . GLN A 1 28  ? 1.939   2.080   24.856  1.00 9.09   ? 28  GLN A NE2 1 
ATOM   269  N  N   . SER A 1 29  ? -1.623  -1.407  24.847  1.00 7.40   ? 29  SER A N   1 
ATOM   270  C  CA  . SER A 1 29  ? -2.676  -2.297  24.356  1.00 7.18   ? 29  SER A CA  1 
ATOM   271  C  C   . SER A 1 29  ? -2.158  -3.165  23.243  1.00 6.79   ? 29  SER A C   1 
ATOM   272  O  O   . SER A 1 29  ? -1.188  -2.803  22.567  1.00 7.77   ? 29  SER A O   1 
ATOM   273  C  CB  . SER A 1 29  ? -3.846  -1.430  23.830  1.00 7.15   ? 29  SER A CB  1 
ATOM   274  O  OG  . SER A 1 29  ? -4.458  -0.708  24.886  1.00 7.30   ? 29  SER A OG  1 
ATOM   275  N  N   . PRO A 1 30  ? -2.809  -4.306  22.972  1.00 6.61   ? 30  PRO A N   1 
ATOM   276  C  CA  . PRO A 1 30  ? -3.980  -4.845  23.674  1.00 6.80   ? 30  PRO A CA  1 
ATOM   277  C  C   . PRO A 1 30  ? -3.562  -5.502  24.980  1.00 6.68   ? 30  PRO A C   1 
ATOM   278  O  O   . PRO A 1 30  ? -2.381  -5.559  25.326  1.00 7.71   ? 30  PRO A O   1 
ATOM   279  C  CB  . PRO A 1 30  ? -4.509  -5.874  22.670  1.00 7.05   ? 30  PRO A CB  1 
ATOM   280  C  CG  . PRO A 1 30  ? -3.229  -6.439  22.068  1.00 7.65   ? 30  PRO A CG  1 
ATOM   281  C  CD  . PRO A 1 30  ? -2.336  -5.197  21.908  1.00 7.06   ? 30  PRO A CD  1 
ATOM   282  N  N   . VAL A 1 31  ? -4.570  -6.047  25.662  1.00 7.58   ? 31  VAL A N   1 
ATOM   283  C  CA  . VAL A 1 31  ? -4.411  -6.815  26.902  1.00 7.49   ? 31  VAL A CA  1 
ATOM   284  C  C   . VAL A 1 31  ? -5.261  -8.033  26.844  1.00 7.65   ? 31  VAL A C   1 
ATOM   285  O  O   . VAL A 1 31  ? -6.255  -8.093  26.080  1.00 8.63   ? 31  VAL A O   1 
ATOM   286  C  CB  . VAL A 1 31  ? -4.711  -5.964  28.168  1.00 8.49   ? 31  VAL A CB  1 
ATOM   287  C  CG1 . VAL A 1 31  ? -3.786  -4.783  28.274  1.00 9.81   ? 31  VAL A CG1 1 
ATOM   288  C  CG2 . VAL A 1 31  ? -6.206  -5.554  28.217  1.00 9.52   ? 31  VAL A CG2 1 
ATOM   289  N  N   . ASP A 1 32  ? -4.975  -9.021  27.693  1.00 8.20   ? 32  ASP A N   1 
ATOM   290  C  CA  . ASP A 1 32  ? -5.864  -10.107 27.983  1.00 8.37   ? 32  ASP A CA  1 
ATOM   291  C  C   . ASP A 1 32  ? -6.933  -9.601  28.974  1.00 8.42   ? 32  ASP A C   1 
ATOM   292  O  O   . ASP A 1 32  ? -6.618  -8.958  29.978  1.00 10.50  ? 32  ASP A O   1 
ATOM   293  C  CB  . ASP A 1 32  ? -5.122  -11.302 28.585  1.00 9.81   ? 32  ASP A CB  1 
ATOM   294  C  CG  . ASP A 1 32  ? -6.061  -12.455 28.865  1.00 10.57  ? 32  ASP A CG  1 
ATOM   295  O  OD1 . ASP A 1 32  ? -6.770  -12.910 27.928  1.00 10.11  ? 32  ASP A OD1 1 
ATOM   296  O  OD2 . ASP A 1 32  ? -6.141  -12.877 30.039  1.00 12.81  ? 32  ASP A OD2 1 
ATOM   297  N  N   . ILE A 1 33  ? -8.185  -9.867  28.690  1.00 8.23   ? 33  ILE A N   1 
ATOM   298  C  CA  . ILE A 1 33  ? -9.298  -9.533  29.535  1.00 9.30   ? 33  ILE A CA  1 
ATOM   299  C  C   . ILE A 1 33  ? -9.593  -10.766 30.371  1.00 9.54   ? 33  ILE A C   1 
ATOM   300  O  O   . ILE A 1 33  ? -10.115 -11.745 29.894  1.00 10.41  ? 33  ILE A O   1 
ATOM   301  C  CB  . ILE A 1 33  ? -10.494 -9.077  28.710  1.00 9.25   ? 33  ILE A CB  1 
ATOM   302  C  CG1 . ILE A 1 33  ? -10.152 -7.870  27.842  1.00 10.45  ? 33  ILE A CG1 1 
ATOM   303  C  CG2 . ILE A 1 33  ? -11.707 -8.813  29.628  1.00 11.99  ? 33  ILE A CG2 1 
ATOM   304  C  CD1 . ILE A 1 33  ? -11.182 -7.584  26.742  1.00 12.38  ? 33  ILE A CD1 1 
ATOM   305  N  N   A ASP A 1 34  ? -9.299  -10.639 31.673  0.50 11.24  ? 34  ASP A N   1 
ATOM   306  N  N   B ASP A 1 34  ? -9.146  -10.766 31.620  0.50 10.91  ? 34  ASP A N   1 
ATOM   307  C  CA  A ASP A 1 34  ? -9.571  -11.647 32.688  0.50 11.85  ? 34  ASP A CA  1 
ATOM   308  C  CA  B ASP A 1 34  ? -9.487  -11.823 32.513  0.50 11.84  ? 34  ASP A CA  1 
ATOM   309  C  C   A ASP A 1 34  ? -11.046 -11.460 33.114  0.50 13.05  ? 34  ASP A C   1 
ATOM   310  C  C   B ASP A 1 34  ? -10.869 -11.485 33.073  0.50 12.30  ? 34  ASP A C   1 
ATOM   311  O  O   A ASP A 1 34  ? -11.469 -10.570 33.819  0.50 12.73  ? 34  ASP A O   1 
ATOM   312  O  O   B ASP A 1 34  ? -10.965 -10.464 33.900  0.50 12.25  ? 34  ASP A O   1 
ATOM   313  C  CB  A ASP A 1 34  ? -8.576  -11.568 33.848  0.50 13.52  ? 34  ASP A CB  1 
ATOM   314  C  CB  B ASP A 1 34  ? -8.466  -11.933 33.608  0.50 13.84  ? 34  ASP A CB  1 
ATOM   315  C  CG  A ASP A 1 34  ? -8.803  -12.671 34.879  0.50 15.69  ? 34  ASP A CG  1 
ATOM   316  C  CG  B ASP A 1 34  ? -8.718  -13.139 34.453  0.50 17.68  ? 34  ASP A CG  1 
ATOM   317  O  OD1 A ASP A 1 34  ? -9.958  -13.149 35.011  0.50 15.90  ? 34  ASP A OD1 1 
ATOM   318  O  OD1 B ASP A 1 34  ? -8.331  -14.224 34.039  0.50 20.54  ? 34  ASP A OD1 1 
ATOM   319  O  OD2 A ASP A 1 34  ? -7.826  -13.029 35.582  0.50 23.28  ? 34  ASP A OD2 1 
ATOM   320  O  OD2 B ASP A 1 34  ? -9.330  -13.017 35.520  0.50 21.81  ? 34  ASP A OD2 1 
ATOM   321  N  N   . THR A 1 35  ? -11.907 -12.251 32.611  1.00 13.96  ? 35  THR A N   1 
ATOM   322  C  CA  . THR A 1 35  ? -13.297 -11.950 32.869  1.00 13.95  ? 35  THR A CA  1 
ATOM   323  C  C   . THR A 1 35  ? -13.707 -12.087 34.277  1.00 12.59  ? 35  THR A C   1 
ATOM   324  O  O   . THR A 1 35  ? -14.624 -11.379 34.745  1.00 16.30  ? 35  THR A O   1 
ATOM   325  C  CB  . THR A 1 35  ? -14.182 -12.823 32.035  1.00 15.13  ? 35  THR A CB  1 
ATOM   326  O  OG1 . THR A 1 35  ? -14.063 -14.155 32.526  1.00 17.42  ? 35  THR A OG1 1 
ATOM   327  C  CG2 . THR A 1 35  ? -13.903 -12.753 30.531  1.00 17.78  ? 35  THR A CG2 1 
ATOM   328  N  N   . HIS A 1 36  ? -13.064 -12.949 35.050  1.00 15.24  ? 36  HIS A N   1 
ATOM   329  C  CA  . HIS A 1 36  ? -13.349 -13.094 36.440  1.00 16.01  ? 36  HIS A CA  1 
ATOM   330  C  C   . HIS A 1 36  ? -12.841 -11.952 37.276  1.00 17.28  ? 36  HIS A C   1 
ATOM   331  O  O   . HIS A 1 36  ? -13.476 -11.627 38.295  1.00 19.05  ? 36  HIS A O   1 
ATOM   332  C  CB  . HIS A 1 36  ? -12.844 -14.510 36.871  1.00 18.45  ? 36  HIS A CB  1 
ATOM   333  C  CG  . HIS A 1 36  ? -13.765 -15.613 36.348  1.00 17.75  ? 36  HIS A CG  1 
ATOM   334  N  ND1 . HIS A 1 36  ? -15.099 -15.690 36.727  1.00 23.15  ? 36  HIS A ND1 1 
ATOM   335  C  CD2 . HIS A 1 36  ? -13.580 -16.593 35.350  1.00 19.27  ? 36  HIS A CD2 1 
ATOM   336  C  CE1 . HIS A 1 36  ? -15.716 -16.706 36.044  1.00 22.61  ? 36  HIS A CE1 1 
ATOM   337  N  NE2 . HIS A 1 36  ? -14.801 -17.256 35.208  1.00 23.32  ? 36  HIS A NE2 1 
ATOM   338  N  N   . THR A 1 37  ? -11.722 -11.316 36.882  1.00 17.39  ? 37  THR A N   1 
ATOM   339  C  CA  . THR A 1 37  ? -11.137 -10.186 37.617  1.00 17.43  ? 37  THR A CA  1 
ATOM   340  C  C   . THR A 1 37  ? -11.704 -8.821  37.205  1.00 17.05  ? 37  THR A C   1 
ATOM   341  O  O   . THR A 1 37  ? -11.597 -7.887  38.009  1.00 20.62  ? 37  THR A O   1 
ATOM   342  C  CB  . THR A 1 37  ? -9.599  -10.205 37.392  1.00 23.36  ? 37  THR A CB  1 
ATOM   343  O  OG1 . THR A 1 37  ? -9.103  -11.369 37.957  1.00 28.03  ? 37  THR A OG1 1 
ATOM   344  C  CG2 . THR A 1 37  ? -8.823  -8.976  38.087  1.00 24.08  ? 37  THR A CG2 1 
ATOM   345  N  N   . ALA A 1 38  ? -12.294 -8.716  36.024  1.00 14.43  ? 38  ALA A N   1 
ATOM   346  C  CA  . ALA A 1 38  ? -12.903 -7.480  35.639  1.00 14.10  ? 38  ALA A CA  1 
ATOM   347  C  C   . ALA A 1 38  ? -13.973 -7.125  36.618  1.00 15.42  ? 38  ALA A C   1 
ATOM   348  O  O   . ALA A 1 38  ? -14.651 -7.958  37.093  1.00 21.58  ? 38  ALA A O   1 
ATOM   349  C  CB  . ALA A 1 38  ? -13.449 -7.608  34.251  1.00 13.89  ? 38  ALA A CB  1 
ATOM   350  N  N   A LYS A 1 39  ? -14.021 -5.848  36.964  0.50 14.95  ? 39  LYS A N   1 
ATOM   351  N  N   B LYS A 1 39  ? -14.083 -5.889  37.076  0.50 15.28  ? 39  LYS A N   1 
ATOM   352  C  CA  A LYS A 1 39  ? -14.893 -5.289  37.997  0.50 14.90  ? 39  LYS A CA  1 
ATOM   353  C  CA  B LYS A 1 39  ? -15.185 -5.657  38.020  0.50 19.33  ? 39  LYS A CA  1 
ATOM   354  C  C   A LYS A 1 39  ? -16.242 -4.834  37.351  0.50 14.20  ? 39  LYS A C   1 
ATOM   355  C  C   B LYS A 1 39  ? -16.278 -4.938  37.335  0.50 15.35  ? 39  LYS A C   1 
ATOM   356  O  O   A LYS A 1 39  ? -16.235 -3.901  36.566  0.50 13.66  ? 39  LYS A O   1 
ATOM   357  O  O   B LYS A 1 39  ? -16.150 -3.942  36.634  0.50 13.69  ? 39  LYS A O   1 
ATOM   358  C  CB  A LYS A 1 39  ? -14.141 -4.110  38.641  0.50 13.80  ? 39  LYS A CB  1 
ATOM   359  C  CB  B LYS A 1 39  ? -14.811 -4.863  39.239  0.50 20.20  ? 39  LYS A CB  1 
ATOM   360  C  CG  A LYS A 1 39  ? -14.909 -3.300  39.713  0.50 15.28  ? 39  LYS A CG  1 
ATOM   361  C  CG  B LYS A 1 39  ? -15.750 -4.867  40.479  0.50 23.97  ? 39  LYS A CG  1 
ATOM   362  C  CD  A LYS A 1 39  ? -15.084 -4.116  40.994  0.50 16.25  ? 39  LYS A CD  1 
ATOM   363  C  CD  B LYS A 1 39  ? -15.239 -3.756  41.408  0.50 27.98  ? 39  LYS A CD  1 
ATOM   364  C  CE  A LYS A 1 39  ? -15.829 -3.245  41.955  0.50 22.46  ? 39  LYS A CE  1 
ATOM   365  C  CE  B LYS A 1 39  ? -16.243 -3.310  42.458  0.50 25.90  ? 39  LYS A CE  1 
ATOM   366  N  NZ  A LYS A 1 39  ? -16.263 -4.165  43.020  0.50 22.86  ? 39  LYS A NZ  1 
ATOM   367  N  NZ  B LYS A 1 39  ? -16.432 -4.551  43.229  0.50 33.18  ? 39  LYS A NZ  1 
ATOM   368  N  N   . TYR A 1 40  ? -17.422 -5.420  37.719  1.00 17.24  ? 40  TYR A N   1 
ATOM   369  C  CA  . TYR A 1 40  ? -18.678 -4.824  37.328  1.00 16.22  ? 40  TYR A CA  1 
ATOM   370  C  C   . TYR A 1 40  ? -18.778 -3.432  37.921  1.00 13.88  ? 40  TYR A C   1 
ATOM   371  O  O   . TYR A 1 40  ? -18.632 -3.268  39.179  1.00 16.74  ? 40  TYR A O   1 
ATOM   372  C  CB  . TYR A 1 40  ? -19.855 -5.716  37.730  1.00 20.69  ? 40  TYR A CB  1 
ATOM   373  C  CG  . TYR A 1 40  ? -21.169 -4.935  37.602  1.00 21.68  ? 40  TYR A CG  1 
ATOM   374  C  CD1 . TYR A 1 40  ? -21.619 -4.489  36.353  1.00 19.90  ? 40  TYR A CD1 1 
ATOM   375  C  CD2 . TYR A 1 40  ? -22.023 -4.729  38.703  1.00 27.54  ? 40  TYR A CD2 1 
ATOM   376  C  CE1 . TYR A 1 40  ? -22.830 -3.783  36.206  1.00 23.49  ? 40  TYR A CE1 1 
ATOM   377  C  CE2 . TYR A 1 40  ? -23.246 -4.045  38.513  1.00 27.93  ? 40  TYR A CE2 1 
ATOM   378  C  CZ  . TYR A 1 40  ? -23.636 -3.570  37.284  1.00 26.73  ? 40  TYR A CZ  1 
ATOM   379  O  OH  . TYR A 1 40  ? -24.820 -2.864  37.147  1.00 36.71  ? 40  TYR A OH  1 
ATOM   380  N  N   . ASP A 1 41  ? -19.041 -2.432  37.124  1.00 14.53  ? 41  ASP A N   1 
ATOM   381  C  CA  . ASP A 1 41  ? -19.101 -1.035  37.582  1.00 14.75  ? 41  ASP A CA  1 
ATOM   382  C  C   . ASP A 1 41  ? -20.511 -0.567  37.311  1.00 16.40  ? 41  ASP A C   1 
ATOM   383  O  O   . ASP A 1 41  ? -20.857 -0.231  36.169  1.00 16.91  ? 41  ASP A O   1 
ATOM   384  C  CB  . ASP A 1 41  ? -18.061 -0.184  36.874  1.00 18.33  ? 41  ASP A CB  1 
ATOM   385  C  CG  . ASP A 1 41  ? -18.033 1.216   37.340  1.00 21.66  ? 41  ASP A CG  1 
ATOM   386  O  OD1 . ASP A 1 41  ? -18.907 1.614   38.135  1.00 21.84  ? 41  ASP A OD1 1 
ATOM   387  O  OD2 . ASP A 1 41  ? -17.058 1.922   37.019  1.00 25.05  ? 41  ASP A OD2 1 
ATOM   388  N  N   . PRO A 1 42  ? -21.388 -0.539  38.348  1.00 21.17  ? 42  PRO A N   1 
ATOM   389  C  CA  . PRO A 1 42  ? -22.742 -0.047  38.149  1.00 21.50  ? 42  PRO A CA  1 
ATOM   390  C  C   . PRO A 1 42  ? -22.787 1.472   37.758  1.00 25.07  ? 42  PRO A C   1 
ATOM   391  O  O   . PRO A 1 42  ? -23.876 1.974   37.382  1.00 36.56  ? 42  PRO A O   1 
ATOM   392  C  CB  . PRO A 1 42  ? -23.411 -0.358  39.484  1.00 31.80  ? 42  PRO A CB  1 
ATOM   393  C  CG  . PRO A 1 42  ? -22.289 -0.156  40.493  1.00 31.61  ? 42  PRO A CG  1 
ATOM   394  C  CD  . PRO A 1 42  ? -21.129 -0.830  39.794  1.00 24.57  ? 42  PRO A CD  1 
ATOM   395  N  N   . SER A 1 43  ? -21.698 2.233   37.912  1.00 25.43  ? 43  SER A N   1 
ATOM   396  C  CA  . SER A 1 43  ? -21.636 3.667   37.441  1.00 25.37  ? 43  SER A CA  1 
ATOM   397  C  C   . SER A 1 43  ? -21.470 3.799   35.884  1.00 22.73  ? 43  SER A C   1 
ATOM   398  O  O   . SER A 1 43  ? -21.683 4.900   35.331  1.00 31.41  ? 43  SER A O   1 
ATOM   399  C  CB  . SER A 1 43  ? -20.529 4.414   38.164  1.00 25.33  ? 43  SER A CB  1 
ATOM   400  O  OG  . SER A 1 43  ? -19.247 4.167   37.682  1.00 30.90  ? 43  SER A OG  1 
ATOM   401  N  N   . LEU A 1 44  ? -21.111 2.708   35.216  1.00 26.62  ? 44  LEU A N   1 
ATOM   402  C  CA  . LEU A 1 44  ? -20.868 2.732   33.763  1.00 19.93  ? 44  LEU A CA  1 
ATOM   403  C  C   . LEU A 1 44  ? -22.235 2.868   33.124  1.00 21.69  ? 44  LEU A C   1 
ATOM   404  O  O   . LEU A 1 44  ? -23.227 2.357   33.564  1.00 27.37  ? 44  LEU A O   1 
ATOM   405  C  CB  . LEU A 1 44  ? -20.168 1.481   33.289  1.00 18.57  ? 44  LEU A CB  1 
ATOM   406  C  CG  . LEU A 1 44  ? -18.699 1.490   33.500  1.00 16.77  ? 44  LEU A CG  1 
ATOM   407  C  CD1 . LEU A 1 44  ? -18.211 0.096   33.094  1.00 17.77  ? 44  LEU A CD1 1 
ATOM   408  C  CD2 . LEU A 1 44  ? -17.978 2.589   32.729  1.00 17.98  ? 44  LEU A CD2 1 
ATOM   409  N  N   . LYS A 1 45  ? -22.294 3.625   32.048  1.00 20.08  ? 45  LYS A N   1 
ATOM   410  C  CA  . LYS A 1 45  ? -23.572 3.901   31.328  1.00 21.04  ? 45  LYS A CA  1 
ATOM   411  C  C   . LYS A 1 45  ? -23.620 2.998   30.115  1.00 18.55  ? 45  LYS A C   1 
ATOM   412  O  O   . LYS A 1 45  ? -22.602 2.520   29.639  1.00 19.23  ? 45  LYS A O   1 
ATOM   413  C  CB  . LYS A 1 45  ? -23.647 5.285   30.856  1.00 20.14  ? 45  LYS A CB  1 
ATOM   414  C  CG  . LYS A 1 45  ? -23.279 6.247   31.933  1.00 25.85  ? 45  LYS A CG  1 
ATOM   415  C  CD  . LYS A 1 45  ? -23.671 7.677   31.565  1.00 35.34  ? 45  LYS A CD  1 
ATOM   416  C  CE  . LYS A 1 45  ? -22.903 8.705   32.403  1.00 45.30  ? 45  LYS A CE  1 
ATOM   417  N  NZ  . LYS A 1 45  ? -23.409 8.746   33.800  1.00 51.25  ? 45  LYS A NZ  1 
ATOM   418  N  N   . PRO A 1 46  ? -24.857 2.779   29.592  1.00 17.58  ? 46  PRO A N   1 
ATOM   419  C  CA  . PRO A 1 46  ? -24.939 2.147   28.244  1.00 17.43  ? 46  PRO A CA  1 
ATOM   420  C  C   . PRO A 1 46  ? -24.131 2.932   27.264  1.00 14.84  ? 46  PRO A C   1 
ATOM   421  O  O   . PRO A 1 46  ? -24.089 4.141   27.320  1.00 16.94  ? 46  PRO A O   1 
ATOM   422  C  CB  . PRO A 1 46  ? -26.441 2.137   27.948  1.00 19.86  ? 46  PRO A CB  1 
ATOM   423  C  CG  . PRO A 1 46  ? -27.146 2.391   29.278  1.00 27.10  ? 46  PRO A CG  1 
ATOM   424  C  CD  . PRO A 1 46  ? -26.157 3.156   30.138  1.00 21.07  ? 46  PRO A CD  1 
ATOM   425  N  N   . LEU A 1 47  ? -23.577 2.183   26.326  1.00 18.20  ? 47  LEU A N   1 
ATOM   426  C  CA  . LEU A 1 47  ? -22.805 2.782   25.261  1.00 15.77  ? 47  LEU A CA  1 
ATOM   427  C  C   . LEU A 1 47  ? -23.882 3.460   24.357  1.00 18.14  ? 47  LEU A C   1 
ATOM   428  O  O   . LEU A 1 47  ? -24.881 2.802   24.104  1.00 23.96  ? 47  LEU A O   1 
ATOM   429  C  CB  . LEU A 1 47  ? -22.056 1.752   24.475  1.00 21.02  ? 47  LEU A CB  1 
ATOM   430  C  CG  . LEU A 1 47  ? -20.937 2.086   23.649  1.00 21.49  ? 47  LEU A CG  1 
ATOM   431  C  CD1 . LEU A 1 47  ? -19.939 2.985   24.488  1.00 24.00  ? 47  LEU A CD1 1 
ATOM   432  C  CD2 . LEU A 1 47  ? -20.352 0.798   23.105  1.00 23.36  ? 47  LEU A CD2 1 
ATOM   433  N  N   . SER A 1 48  ? -23.619 4.652   23.868  1.00 15.14  ? 48  SER A N   1 
ATOM   434  C  CA  . SER A 1 48  ? -24.469 5.306   22.847  1.00 15.25  ? 48  SER A CA  1 
ATOM   435  C  C   . SER A 1 48  ? -23.716 5.347   21.506  1.00 13.98  ? 48  SER A C   1 
ATOM   436  O  O   . SER A 1 48  ? -22.689 6.027   21.395  1.00 15.99  ? 48  SER A O   1 
ATOM   437  C  CB  . SER A 1 48  ? -24.839 6.713   23.305  1.00 17.39  ? 48  SER A CB  1 
ATOM   438  O  OG  . SER A 1 48  ? -25.465 7.428   22.274  1.00 20.20  ? 48  SER A OG  1 
ATOM   439  N  N   . VAL A 1 49  ? -24.123 4.534   20.600  1.00 15.00  ? 49  VAL A N   1 
ATOM   440  C  CA  . VAL A 1 49  ? -23.555 4.460   19.304  1.00 16.20  ? 49  VAL A CA  1 
ATOM   441  C  C   . VAL A 1 49  ? -24.541 5.028   18.285  1.00 16.58  ? 49  VAL A C   1 
ATOM   442  O  O   . VAL A 1 49  ? -25.598 4.477   18.098  1.00 21.24  ? 49  VAL A O   1 
ATOM   443  C  CB  . VAL A 1 49  ? -23.298 2.967   18.919  1.00 19.30  ? 49  VAL A CB  1 
ATOM   444  C  CG1 . VAL A 1 49  ? -22.635 2.918   17.540  1.00 24.68  ? 49  VAL A CG1 1 
ATOM   445  C  CG2 . VAL A 1 49  ? -22.480 2.231   19.951  1.00 23.05  ? 49  VAL A CG2 1 
ATOM   446  N  N   . SER A 1 50  ? -24.214 6.135   17.681  1.00 16.16  ? 50  SER A N   1 
ATOM   447  C  CA  . SER A 1 50  ? -25.148 6.846   16.819  1.00 19.34  ? 50  SER A CA  1 
ATOM   448  C  C   . SER A 1 50  ? -24.537 6.929   15.476  1.00 18.15  ? 50  SER A C   1 
ATOM   449  O  O   . SER A 1 50  ? -23.830 7.895   15.154  1.00 19.32  ? 50  SER A O   1 
ATOM   450  C  CB  . SER A 1 50  ? -25.554 8.218   17.396  1.00 22.41  ? 50  SER A CB  1 
ATOM   451  O  OG  . SER A 1 50  ? -26.242 8.012   18.639  1.00 25.46  ? 50  SER A OG  1 
ATOM   452  N  N   . TYR A 1 51  ? -24.823 5.970   14.631  1.00 17.80  ? 51  TYR A N   1 
ATOM   453  C  CA  . TYR A 1 51  ? -24.227 5.842   13.348  1.00 16.32  ? 51  TYR A CA  1 
ATOM   454  C  C   . TYR A 1 51  ? -25.181 6.060   12.189  1.00 18.89  ? 51  TYR A C   1 
ATOM   455  O  O   . TYR A 1 51  ? -24.791 5.924   11.037  1.00 19.44  ? 51  TYR A O   1 
ATOM   456  C  CB  . TYR A 1 51  ? -23.541 4.458   13.130  1.00 16.36  ? 51  TYR A CB  1 
ATOM   457  C  CG  . TYR A 1 51  ? -22.290 4.153   13.908  1.00 14.10  ? 51  TYR A CG  1 
ATOM   458  C  CD1 . TYR A 1 51  ? -21.532 5.176   14.545  1.00 14.94  ? 51  TYR A CD1 1 
ATOM   459  C  CD2 . TYR A 1 51  ? -21.852 2.862   14.043  1.00 13.72  ? 51  TYR A CD2 1 
ATOM   460  C  CE1 . TYR A 1 51  ? -20.356 4.850   15.217  1.00 12.40  ? 51  TYR A CE1 1 
ATOM   461  C  CE2 . TYR A 1 51  ? -20.641 2.543   14.681  1.00 12.38  ? 51  TYR A CE2 1 
ATOM   462  C  CZ  . TYR A 1 51  ? -19.911 3.546   15.331  1.00 12.05  ? 51  TYR A CZ  1 
ATOM   463  O  OH  . TYR A 1 51  ? -18.770 3.202   15.959  1.00 12.66  ? 51  TYR A OH  1 
ATOM   464  N  N   . ASP A 1 52  ? -26.414 6.453   12.450  1.00 22.22  ? 52  ASP A N   1 
ATOM   465  C  CA  . ASP A 1 52  ? -27.419 6.699   11.387  1.00 22.78  ? 52  ASP A CA  1 
ATOM   466  C  C   . ASP A 1 52  ? -27.018 7.683   10.286  1.00 22.51  ? 52  ASP A C   1 
ATOM   467  O  O   . ASP A 1 52  ? -27.441 7.524   9.148   1.00 25.53  ? 52  ASP A O   1 
ATOM   468  C  CB  . ASP A 1 52  ? -28.753 7.136   11.993  1.00 26.79  ? 52  ASP A CB  1 
ATOM   469  C  CG  . ASP A 1 52  ? -28.582 8.200   13.114  1.00 31.97  ? 52  ASP A CG  1 
ATOM   470  O  OD1 . ASP A 1 52  ? -27.854 7.982   14.166  1.00 40.73  ? 52  ASP A OD1 1 
ATOM   471  O  OD2 . ASP A 1 52  ? -29.206 9.259   12.930  1.00 50.81  ? 52  ASP A OD2 1 
ATOM   472  N  N   . GLN A 1 53  ? -26.201 8.665   10.615  1.00 22.60  ? 53  GLN A N   1 
ATOM   473  C  CA  . GLN A 1 53  ? -25.786 9.634   9.571   1.00 24.73  ? 53  GLN A CA  1 
ATOM   474  C  C   . GLN A 1 53  ? -24.352 9.375   9.080   1.00 18.96  ? 53  GLN A C   1 
ATOM   475  O  O   . GLN A 1 53  ? -23.753 10.211  8.428   1.00 19.49  ? 53  GLN A O   1 
ATOM   476  C  CB  . GLN A 1 53  ? -25.955 11.076  10.090  1.00 29.90  ? 53  GLN A CB  1 
ATOM   477  C  CG  . GLN A 1 53  ? -27.353 11.418  10.617  1.00 46.27  ? 53  GLN A CG  1 
ATOM   478  C  CD  . GLN A 1 53  ? -28.384 11.467  9.524   1.00 58.82  ? 53  GLN A CD  1 
ATOM   479  O  OE1 . GLN A 1 53  ? -28.052 11.554  8.343   1.00 64.83  ? 53  GLN A OE1 1 
ATOM   480  N  NE2 . GLN A 1 53  ? -29.654 11.434  9.906   1.00 84.64  ? 53  GLN A NE2 1 
ATOM   481  N  N   . ALA A 1 54  ? -23.771 8.249   9.430   1.00 18.40  ? 54  ALA A N   1 
ATOM   482  C  CA  . ALA A 1 54  ? -22.402 8.034   9.041   1.00 16.72  ? 54  ALA A CA  1 
ATOM   483  C  C   . ALA A 1 54  ? -22.267 8.071   7.542   1.00 17.25  ? 54  ALA A C   1 
ATOM   484  O  O   . ALA A 1 54  ? -23.093 7.487   6.811   1.00 23.59  ? 54  ALA A O   1 
ATOM   485  C  CB  . ALA A 1 54  ? -21.882 6.669   9.539   1.00 19.84  ? 54  ALA A CB  1 
ATOM   486  N  N   A THR A 1 55  ? -21.198 8.716   7.061   0.50 14.67  ? 55  THR A N   1 
ATOM   487  N  N   B THR A 1 55  ? -21.215 8.728   7.057   0.50 14.65  ? 55  THR A N   1 
ATOM   488  C  CA  A THR A 1 55  ? -20.947 8.894   5.650   0.50 15.79  ? 55  THR A CA  1 
ATOM   489  C  CA  B THR A 1 55  ? -20.993 8.882   5.633   0.50 15.91  ? 55  THR A CA  1 
ATOM   490  C  C   A THR A 1 55  ? -19.573 8.355   5.324   0.50 13.88  ? 55  THR A C   1 
ATOM   491  C  C   B THR A 1 55  ? -19.597 8.359   5.304   0.50 13.94  ? 55  THR A C   1 
ATOM   492  O  O   A THR A 1 55  ? -18.536 8.983   5.579   0.50 14.27  ? 55  THR A O   1 
ATOM   493  O  O   B THR A 1 55  ? -18.579 8.973   5.560   0.50 14.39  ? 55  THR A O   1 
ATOM   494  C  CB  A THR A 1 55  ? -20.921 10.367  5.169   0.50 21.84  ? 55  THR A CB  1 
ATOM   495  C  CB  B THR A 1 55  ? -21.298 10.325  5.101   0.50 21.48  ? 55  THR A CB  1 
ATOM   496  O  OG1 A THR A 1 55  ? -22.102 11.097  5.546   0.50 28.31  ? 55  THR A OG1 1 
ATOM   497  O  OG1 B THR A 1 55  ? -20.483 11.266  5.761   0.50 30.10  ? 55  THR A OG1 1 
ATOM   498  C  CG2 A THR A 1 55  ? -20.753 10.328  3.657   0.50 22.34  ? 55  THR A CG2 1 
ATOM   499  C  CG2 B THR A 1 55  ? -22.737 10.748  5.371   0.50 29.11  ? 55  THR A CG2 1 
ATOM   500  N  N   . SER A 1 56  ? -19.586 7.133   4.820   1.00 14.48  ? 56  SER A N   1 
ATOM   501  C  CA  . SER A 1 56  ? -18.354 6.570   4.376   1.00 14.27  ? 56  SER A CA  1 
ATOM   502  C  C   . SER A 1 56  ? -17.939 7.203   3.114   1.00 14.12  ? 56  SER A C   1 
ATOM   503  O  O   . SER A 1 56  ? -18.658 7.665   2.305   1.00 17.42  ? 56  SER A O   1 
ATOM   504  C  CB  . SER A 1 56  ? -18.336 5.013   4.214   1.00 15.62  ? 56  SER A CB  1 
ATOM   505  O  OG  . SER A 1 56  ? -19.159 4.661   3.091   1.00 16.30  ? 56  SER A OG  1 
ATOM   506  N  N   . LEU A 1 57  ? -16.650 7.245   2.916   1.00 13.18  ? 57  LEU A N   1 
ATOM   507  C  CA  . LEU A 1 57  ? -16.088 7.847   1.718   1.00 15.49  ? 57  LEU A CA  1 
ATOM   508  C  C   . LEU A 1 57  ? -15.213 6.895   0.862   1.00 14.53  ? 57  LEU A C   1 
ATOM   509  O  O   . LEU A 1 57  ? -15.238 6.924   -0.366  1.00 16.45  ? 57  LEU A O   1 
ATOM   510  C  CB  . LEU A 1 57  ? -15.176 8.961   2.121   1.00 20.01  ? 57  LEU A CB  1 
ATOM   511  C  CG  . LEU A 1 57  ? -15.778 10.282  2.725   1.00 28.05  ? 57  LEU A CG  1 
ATOM   512  C  CD1 . LEU A 1 57  ? -14.738 11.296  3.257   1.00 30.58  ? 57  LEU A CD1 1 
ATOM   513  C  CD2 . LEU A 1 57  ? -16.747 10.884  1.711   1.00 40.68  ? 57  LEU A CD2 1 
ATOM   514  N  N   . ARG A 1 58  ? -14.354 6.161   1.526   1.00 14.15  ? 58  ARG A N   1 
ATOM   515  C  CA  . ARG A 1 58  ? -13.348 5.446   0.763   1.00 14.66  ? 58  ARG A CA  1 
ATOM   516  C  C   . ARG A 1 58  ? -12.765 4.283   1.582   1.00 12.69  ? 58  ARG A C   1 
ATOM   517  O  O   . ARG A 1 58  ? -12.875 4.260   2.776   1.00 13.77  ? 58  ARG A O   1 
ATOM   518  C  CB  . ARG A 1 58  ? -12.197 6.430   0.566   1.00 16.65  ? 58  ARG A CB  1 
ATOM   519  C  CG  . ARG A 1 58  ? -11.109 6.094   -0.300  1.00 20.69  ? 58  ARG A CG  1 
ATOM   520  C  CD  . ARG A 1 58  ? -10.126 7.228   -0.523  1.00 23.21  ? 58  ARG A CD  1 
ATOM   521  N  NE  . ARG A 1 58  ? -9.222  7.259   0.617   1.00 19.10  ? 58  ARG A NE  1 
ATOM   522  C  CZ  . ARG A 1 58  ? -7.912  7.467   0.565   1.00 17.63  ? 58  ARG A CZ  1 
ATOM   523  N  NH1 . ARG A 1 58  ? -7.297  7.688   -0.587  1.00 19.25  ? 58  ARG A NH1 1 
ATOM   524  N  NH2 . ARG A 1 58  ? -7.212  7.443   1.688   1.00 18.30  ? 58  ARG A NH2 1 
ATOM   525  N  N   . ILE A 1 59  ? -12.150 3.328   0.890   1.00 13.33  ? 59  ILE A N   1 
ATOM   526  C  CA  . ILE A 1 59  ? -11.468 2.225   1.537   1.00 12.90  ? 59  ILE A CA  1 
ATOM   527  C  C   . ILE A 1 59  ? -10.048 2.234   1.016   1.00 12.30  ? 59  ILE A C   1 
ATOM   528  O  O   . ILE A 1 59  ? -9.758  2.415   -0.206  1.00 15.64  ? 59  ILE A O   1 
ATOM   529  C  CB  . ILE A 1 59  ? -12.193 0.909   1.301   1.00 13.44  ? 59  ILE A CB  1 
ATOM   530  C  CG1 . ILE A 1 59  ? -11.573 -0.204  2.175   1.00 13.03  ? 59  ILE A CG1 1 
ATOM   531  C  CG2 . ILE A 1 59  ? -12.152 0.454   -0.216  1.00 15.94  ? 59  ILE A CG2 1 
ATOM   532  C  CD1 . ILE A 1 59  ? -12.390 -1.472  2.091   1.00 14.81  ? 59  ILE A CD1 1 
ATOM   533  N  N   . LEU A 1 60  ? -9.087  2.057   1.935   1.00 12.29  ? 60  LEU A N   1 
ATOM   534  C  CA  . LEU A 1 60  ? -7.753  2.163   1.691   1.00 11.94  ? 60  LEU A CA  1 
ATOM   535  C  C   . LEU A 1 60  ? -6.891  0.991   2.235   1.00 11.48  ? 60  LEU A C   1 
ATOM   536  O  O   . LEU A 1 60  ? -7.047  0.661   3.398   1.00 12.16  ? 60  LEU A O   1 
ATOM   537  C  CB  . LEU A 1 60  ? -7.128  3.493   2.345   1.00 13.40  ? 60  LEU A CB  1 
ATOM   538  C  CG  . LEU A 1 60  ? -5.643  3.636   2.255   1.00 14.60  ? 60  LEU A CG  1 
ATOM   539  C  CD1 . LEU A 1 60  ? -5.064  3.927   0.848   1.00 16.14  ? 60  LEU A CD1 1 
ATOM   540  C  CD2 . LEU A 1 60  ? -5.143  4.753   3.230   1.00 16.32  ? 60  LEU A CD2 1 
ATOM   541  N  N   . ASN A 1 61  ? -5.969  0.410   1.451   1.00 11.81  ? 61  ASN A N   1 
ATOM   542  C  CA  . ASN A 1 61  ? -4.981  -0.511  1.918   1.00 12.08  ? 61  ASN A CA  1 
ATOM   543  C  C   . ASN A 1 61  ? -3.715  0.306   2.299   1.00 12.05  ? 61  ASN A C   1 
ATOM   544  O  O   . ASN A 1 61  ? -3.152  0.897   1.429   1.00 13.51  ? 61  ASN A O   1 
ATOM   545  C  CB  . ASN A 1 61  ? -4.657  -1.565  0.841   1.00 13.73  ? 61  ASN A CB  1 
ATOM   546  C  CG  . ASN A 1 61  ? -3.543  -2.505  1.252   1.00 12.25  ? 61  ASN A CG  1 
ATOM   547  O  OD1 . ASN A 1 61  ? -2.709  -2.254  2.133   1.00 13.43  ? 61  ASN A OD1 1 
ATOM   548  N  ND2 . ASN A 1 61  ? -3.518  -3.712  0.654   1.00 13.91  ? 61  ASN A ND2 1 
ATOM   549  N  N   . ASN A 1 62  ? -3.486  0.446   3.594   1.00 12.65  ? 62  ASN A N   1 
ATOM   550  C  CA  . ASN A 1 62  ? -2.455  1.308   4.074   1.00 13.72  ? 62  ASN A CA  1 
ATOM   551  C  C   . ASN A 1 62  ? -1.149  0.559   4.259   1.00 13.27  ? 62  ASN A C   1 
ATOM   552  O  O   . ASN A 1 62  ? -0.151  1.075   4.814   1.00 17.07  ? 62  ASN A O   1 
ATOM   553  C  CB  . ASN A 1 62  ? -2.790  2.125   5.328   1.00 13.79  ? 62  ASN A CB  1 
ATOM   554  C  CG  . ASN A 1 62  ? -2.849  1.251   6.537   1.00 12.81  ? 62  ASN A CG  1 
ATOM   555  O  OD1 . ASN A 1 62  ? -2.652  0.009   6.501   1.00 13.98  ? 62  ASN A OD1 1 
ATOM   556  N  ND2 . ASN A 1 62  ? -2.999  1.874   7.661   1.00 15.19  ? 62  ASN A ND2 1 
ATOM   557  N  N   . GLY A 1 63  ? -1.082  -0.720  3.833   1.00 13.46  ? 63  GLY A N   1 
ATOM   558  C  CA  . GLY A 1 63  ? 0.046   -1.503  4.019   1.00 13.98  ? 63  GLY A CA  1 
ATOM   559  C  C   . GLY A 1 63  ? 0.073   -2.452  5.183   1.00 14.81  ? 63  GLY A C   1 
ATOM   560  O  O   . GLY A 1 63  ? 0.906   -3.347  5.264   1.00 18.29  ? 63  GLY A O   1 
ATOM   561  N  N   . HIS A 1 64  ? -0.813  -2.286  6.100   1.00 13.59  ? 64  HIS A N   1 
ATOM   562  C  CA  . HIS A 1 64  ? -0.995  -3.295  7.163   1.00 15.93  ? 64  HIS A CA  1 
ATOM   563  C  C   . HIS A 1 64  ? -2.378  -3.504  7.598   1.00 13.12  ? 64  HIS A C   1 
ATOM   564  O  O   . HIS A 1 64  ? -2.565  -4.376  8.519   1.00 14.70  ? 64  HIS A O   1 
ATOM   565  C  CB  . HIS A 1 64  ? -0.099  -2.986  8.303   1.00 16.24  ? 64  HIS A CB  1 
ATOM   566  C  CG  . HIS A 1 64  ? -0.376  -1.673  8.892   1.00 13.29  ? 64  HIS A CG  1 
ATOM   567  N  ND1 . HIS A 1 64  ? -1.197  -1.419  9.912   1.00 14.04  ? 64  HIS A ND1 1 
ATOM   568  C  CD2 . HIS A 1 64  ? 0.217   -0.446  8.564   1.00 16.51  ? 64  HIS A CD2 1 
ATOM   569  C  CE1 . HIS A 1 64  ? -1.177  -0.092  10.181  1.00 14.64  ? 64  HIS A CE1 1 
ATOM   570  N  NE2 . HIS A 1 64  ? -0.290  0.483   9.366   1.00 16.33  ? 64  HIS A NE2 1 
ATOM   571  N  N   . ALA A 1 65  ? -3.344  -2.838  7.039   1.00 12.21  ? 65  ALA A N   1 
ATOM   572  C  CA  . ALA A 1 65  ? -4.754  -3.085  7.243   1.00 12.58  ? 65  ALA A CA  1 
ATOM   573  C  C   . ALA A 1 65  ? -5.474  -2.530  6.042   1.00 11.94  ? 65  ALA A C   1 
ATOM   574  O  O   . ALA A 1 65  ? -4.849  -1.805  5.211   1.00 13.46  ? 65  ALA A O   1 
ATOM   575  C  CB  . ALA A 1 65  ? -5.255  -2.413  8.545   1.00 17.78  ? 65  ALA A CB  1 
ATOM   576  N  N   . PHE A 1 66  ? -6.771  -2.728  5.956   1.00 13.22  ? 66  PHE A N   1 
ATOM   577  C  CA  . PHE A 1 66  ? -7.602  -1.861  5.122   1.00 14.46  ? 66  PHE A CA  1 
ATOM   578  C  C   . PHE A 1 66  ? -8.490  -0.983  5.994   1.00 13.67  ? 66  PHE A C   1 
ATOM   579  O  O   . PHE A 1 66  ? -8.983  -1.407  7.047   1.00 14.44  ? 66  PHE A O   1 
ATOM   580  C  CB  . PHE A 1 66  ? -8.448  -2.713  4.115   1.00 16.28  ? 66  PHE A CB  1 
ATOM   581  C  CG  . PHE A 1 66  ? -9.404  -3.654  4.752   1.00 15.25  ? 66  PHE A CG  1 
ATOM   582  C  CD1 . PHE A 1 66  ? -10.659 -3.203  5.093   1.00 17.40  ? 66  PHE A CD1 1 
ATOM   583  C  CD2 . PHE A 1 66  ? -9.061  -4.987  4.983   1.00 15.28  ? 66  PHE A CD2 1 
ATOM   584  C  CE1 . PHE A 1 66  ? -11.550 -4.033  5.657   1.00 19.84  ? 66  PHE A CE1 1 
ATOM   585  C  CE2 . PHE A 1 66  ? -9.987  -5.870  5.559   1.00 18.02  ? 66  PHE A CE2 1 
ATOM   586  C  CZ  . PHE A 1 66  ? -11.284 -5.361  5.870   1.00 17.07  ? 66  PHE A CZ  1 
ATOM   587  N  N   . ASN A 1 67  ? -8.589  0.315   5.623   1.00 15.62  ? 67  ASN A N   1 
ATOM   588  C  CA  . ASN A 1 67  ? -9.263  1.254   6.423   1.00 12.73  ? 67  ASN A CA  1 
ATOM   589  C  C   . ASN A 1 67  ? -10.571 1.749   5.692   1.00 10.54  ? 67  ASN A C   1 
ATOM   590  O  O   . ASN A 1 67  ? -10.415 2.217   4.536   1.00 13.06  ? 67  ASN A O   1 
ATOM   591  C  CB  . ASN A 1 67  ? -8.386  2.444   6.688   1.00 16.27  ? 67  ASN A CB  1 
ATOM   592  C  CG  . ASN A 1 67  ? -7.085  2.116   7.396   1.00 21.44  ? 67  ASN A CG  1 
ATOM   593  O  OD1 . ASN A 1 67  ? -7.028  1.342   8.365   1.00 13.27  ? 67  ASN A OD1 1 
ATOM   594  N  ND2 . ASN A 1 67  ? -6.016  2.935   7.094   1.00 28.88  ? 67  ASN A ND2 1 
ATOM   595  N  N   . VAL A 1 68  ? -11.716 1.676   6.297   1.00 10.92  ? 68  VAL A N   1 
ATOM   596  C  CA  . VAL A 1 68  ? -12.929 2.266   5.735   1.00 10.90  ? 68  VAL A CA  1 
ATOM   597  C  C   . VAL A 1 68  ? -12.987 3.648   6.398   1.00 11.45  ? 68  VAL A C   1 
ATOM   598  O  O   . VAL A 1 68  ? -13.111 3.737   7.627   1.00 10.98  ? 68  VAL A O   1 
ATOM   599  C  CB  . VAL A 1 68  ? -14.169 1.448   5.933   1.00 12.00  ? 68  VAL A CB  1 
ATOM   600  C  CG1 . VAL A 1 68  ? -15.400 2.213   5.499   1.00 14.42  ? 68  VAL A CG1 1 
ATOM   601  C  CG2 . VAL A 1 68  ? -13.992 0.131   5.161   1.00 14.25  ? 68  VAL A CG2 1 
ATOM   602  N  N   . GLU A 1 69  ? -12.894 4.716   5.632   1.00 12.64  ? 69  GLU A N   1 
ATOM   603  C  CA  . GLU A 1 69  ? -12.790 6.088   6.110   1.00 12.26  ? 69  GLU A CA  1 
ATOM   604  C  C   . GLU A 1 69  ? -14.169 6.781   6.030   1.00 12.56  ? 69  GLU A C   1 
ATOM   605  O  O   . GLU A 1 69  ? -14.958 6.542   5.071   1.00 14.47  ? 69  GLU A O   1 
ATOM   606  C  CB  . GLU A 1 69  ? -11.946 6.822   5.181   1.00 14.79  ? 69  GLU A CB  1 
ATOM   607  C  CG  . GLU A 1 69  ? -10.608 6.320   5.262   1.00 15.30  ? 69  GLU A CG  1 
ATOM   608  C  CD  . GLU A 1 69  ? -9.730  6.768   4.076   1.00 18.91  ? 69  GLU A CD  1 
ATOM   609  O  OE1 . GLU A 1 69  ? -10.251 7.454   3.114   1.00 19.35  ? 69  GLU A OE1 1 
ATOM   610  O  OE2 . GLU A 1 69  ? -8.523  6.468   3.995   1.00 18.39  ? 69  GLU A OE2 1 
ATOM   611  N  N   . PHE A 1 70  ? -14.435 7.637   7.006   1.00 12.48  ? 70  PHE A N   1 
ATOM   612  C  CA  . PHE A 1 70  ? -15.669 8.376   7.059   1.00 13.11  ? 70  PHE A CA  1 
ATOM   613  C  C   . PHE A 1 70  ? -15.399 9.863   6.976   1.00 13.14  ? 70  PHE A C   1 
ATOM   614  O  O   . PHE A 1 70  ? -14.333 10.347  7.385   1.00 14.37  ? 70  PHE A O   1 
ATOM   615  C  CB  . PHE A 1 70  ? -16.375 8.040   8.357   1.00 13.05  ? 70  PHE A CB  1 
ATOM   616  C  CG  . PHE A 1 70  ? -16.953 6.641   8.330   1.00 12.20  ? 70  PHE A CG  1 
ATOM   617  C  CD1 . PHE A 1 70  ? -16.100 5.529   8.547   1.00 13.15  ? 70  PHE A CD1 1 
ATOM   618  C  CD2 . PHE A 1 70  ? -18.261 6.418   8.003   1.00 12.21  ? 70  PHE A CD2 1 
ATOM   619  C  CE1 . PHE A 1 70  ? -16.626 4.260   8.406   1.00 13.93  ? 70  PHE A CE1 1 
ATOM   620  C  CE2 . PHE A 1 70  ? -18.787 5.135   7.859   1.00 12.73  ? 70  PHE A CE2 1 
ATOM   621  C  CZ  . PHE A 1 70  ? -17.940 4.038   8.100   1.00 14.11  ? 70  PHE A CZ  1 
ATOM   622  N  N   . ASP A 1 71  ? -16.387 10.602  6.521   1.00 16.90  ? 71  ASP A N   1 
ATOM   623  C  CA  . ASP A 1 71  ? -16.269 12.043  6.577   1.00 17.59  ? 71  ASP A CA  1 
ATOM   624  C  C   . ASP A 1 71  ? -16.576 12.416  8.003   1.00 16.32  ? 71  ASP A C   1 
ATOM   625  O  O   . ASP A 1 71  ? -17.679 12.234  8.481   1.00 23.66  ? 71  ASP A O   1 
ATOM   626  C  CB  . ASP A 1 71  ? -17.354 12.615  5.731   1.00 24.10  ? 71  ASP A CB  1 
ATOM   627  C  CG  . ASP A 1 71  ? -17.546 14.114  5.937   1.00 28.51  ? 71  ASP A CG  1 
ATOM   628  O  OD1 . ASP A 1 71  ? -16.683 14.764  6.464   1.00 26.45  ? 71  ASP A OD1 1 
ATOM   629  O  OD2 . ASP A 1 71  ? -18.630 14.677  5.571   1.00 39.20  ? 71  ASP A OD2 1 
ATOM   630  N  N   . ASP A 1 72  ? -15.564 12.922  8.683   1.00 14.66  ? 72  ASP A N   1 
ATOM   631  C  CA  . ASP A 1 72  ? -15.663 13.327  10.056  1.00 15.26  ? 72  ASP A CA  1 
ATOM   632  C  C   . ASP A 1 72  ? -15.624 14.841  10.221  1.00 18.73  ? 72  ASP A C   1 
ATOM   633  O  O   . ASP A 1 72  ? -15.221 15.361  11.255  1.00 20.26  ? 72  ASP A O   1 
ATOM   634  C  CB  . ASP A 1 72  ? -14.595 12.671  10.918  1.00 15.00  ? 72  ASP A CB  1 
ATOM   635  C  CG  . ASP A 1 72  ? -13.201 13.178  10.552  1.00 15.21  ? 72  ASP A CG  1 
ATOM   636  O  OD1 . ASP A 1 72  ? -13.044 13.797  9.462   1.00 17.68  ? 72  ASP A OD1 1 
ATOM   637  O  OD2 . ASP A 1 72  ? -12.248 12.987  11.343  1.00 16.19  ? 72  ASP A OD2 1 
ATOM   638  N  N   . SER A 1 73  ? -16.106 15.555  9.220   1.00 19.24  ? 73  SER A N   1 
ATOM   639  C  CA  . SER A 1 73  ? -16.022 17.059  9.281   1.00 21.15  ? 73  SER A CA  1 
ATOM   640  C  C   . SER A 1 73  ? -17.376 17.623  9.842   1.00 19.72  ? 73  SER A C   1 
ATOM   641  O  O   . SER A 1 73  ? -17.434 18.845  10.056  1.00 18.09  ? 73  SER A O   1 
ATOM   642  C  CB  . SER A 1 73  ? -15.669 17.541  7.887   1.00 26.74  ? 73  SER A CB  1 
ATOM   643  O  OG  . SER A 1 73  ? -16.843 17.411  7.156   1.00 22.34  ? 73  SER A OG  1 
ATOM   644  N  N   . GLN A 1 74  ? -18.382 16.785  10.164  1.00 21.51  ? 74  GLN A N   1 
ATOM   645  C  CA  . GLN A 1 74  ? -19.576 17.232  10.808  1.00 24.54  ? 74  GLN A CA  1 
ATOM   646  C  C   . GLN A 1 74  ? -19.843 16.263  11.900  1.00 23.48  ? 74  GLN A C   1 
ATOM   647  O  O   . GLN A 1 74  ? -19.299 15.130  11.925  1.00 19.02  ? 74  GLN A O   1 
ATOM   648  C  CB  . GLN A 1 74  ? -20.803 17.252  9.835   1.00 29.05  ? 74  GLN A CB  1 
ATOM   649  C  CG  . GLN A 1 74  ? -20.638 18.278  8.718   1.00 32.05  ? 74  GLN A CG  1 
ATOM   650  C  CD  . GLN A 1 74  ? -21.782 18.144  7.694   1.00 34.58  ? 74  GLN A CD  1 
ATOM   651  O  OE1 . GLN A 1 74  ? -22.932 17.984  8.073   1.00 57.89  ? 74  GLN A OE1 1 
ATOM   652  N  NE2 . GLN A 1 74  ? -21.464 18.278  6.392   1.00 49.79  ? 74  GLN A NE2 1 
ATOM   653  N  N   . ASP A 1 75  ? -20.835 16.683  12.694  1.00 26.37  ? 75  ASP A N   1 
ATOM   654  C  CA  . ASP A 1 75  ? -21.257 16.001  13.809  1.00 23.29  ? 75  ASP A CA  1 
ATOM   655  C  C   . ASP A 1 75  ? -22.236 14.873  13.311  1.00 27.68  ? 75  ASP A C   1 
ATOM   656  O  O   . ASP A 1 75  ? -23.493 15.065  13.322  1.00 36.83  ? 75  ASP A O   1 
ATOM   657  C  CB  . ASP A 1 75  ? -21.895 16.999  14.779  1.00 31.30  ? 75  ASP A CB  1 
ATOM   658  C  CG  . ASP A 1 75  ? -22.492 16.321  15.945  1.00 38.36  ? 75  ASP A CG  1 
ATOM   659  O  OD1 . ASP A 1 75  ? -22.239 15.076  16.103  1.00 32.96  ? 75  ASP A OD1 1 
ATOM   660  O  OD2 . ASP A 1 75  ? -23.213 17.012  16.710  1.00 72.98  ? 75  ASP A OD2 1 
ATOM   661  N  N   . LYS A 1 76  ? -21.695 13.729  12.913  1.00 20.47  ? 76  LYS A N   1 
ATOM   662  C  CA  . LYS A 1 76  ? -22.514 12.650  12.335  1.00 27.09  ? 76  LYS A CA  1 
ATOM   663  C  C   . LYS A 1 76  ? -22.548 11.413  13.230  1.00 37.65  ? 76  LYS A C   1 
ATOM   664  O  O   . LYS A 1 76  ? -23.394 11.252  14.153  1.00 48.83  ? 76  LYS A O   1 
ATOM   665  C  CB  . LYS A 1 76  ? -22.066 12.417  10.882  1.00 25.21  ? 76  LYS A CB  1 
ATOM   666  C  CG  . LYS A 1 76  ? -22.424 13.632  10.015  1.00 34.14  ? 76  LYS A CG  1 
ATOM   667  C  CD  . LYS A 1 76  ? -22.109 13.346  8.557   1.00 39.97  ? 76  LYS A CD  1 
ATOM   668  C  CE  . LYS A 1 76  ? -22.356 14.508  7.605   1.00 40.73  ? 76  LYS A CE  1 
ATOM   669  N  NZ  . LYS A 1 76  ? -21.828 14.176  6.255   1.00 37.58  ? 76  LYS A NZ  1 
ATOM   670  N  N   . ALA A 1 77  ? -21.598 10.564  12.971  1.00 25.97  ? 77  ALA A N   1 
ATOM   671  C  CA  . ALA A 1 77  ? -21.431 9.255   13.557  1.00 19.48  ? 77  ALA A CA  1 
ATOM   672  C  C   . ALA A 1 77  ? -20.661 9.443   14.879  1.00 16.33  ? 77  ALA A C   1 
ATOM   673  O  O   . ALA A 1 77  ? -19.481 9.687   14.871  1.00 25.03  ? 77  ALA A O   1 
ATOM   674  C  CB  . ALA A 1 77  ? -20.634 8.480   12.492  1.00 21.26  ? 77  ALA A CB  1 
ATOM   675  N  N   . VAL A 1 78  ? -21.326 9.305   15.980  1.00 15.96  ? 78  VAL A N   1 
ATOM   676  C  CA  . VAL A 1 78  ? -20.651 9.579   17.238  1.00 16.17  ? 78  VAL A CA  1 
ATOM   677  C  C   . VAL A 1 78  ? -20.874 8.458   18.256  1.00 14.15  ? 78  VAL A C   1 
ATOM   678  O  O   . VAL A 1 78  ? -21.935 7.792   18.310  1.00 15.68  ? 78  VAL A O   1 
ATOM   679  C  CB  . VAL A 1 78  ? -20.909 10.944  17.824  1.00 22.42  ? 78  VAL A CB  1 
ATOM   680  C  CG1 . VAL A 1 78  ? -20.772 12.080  16.864  1.00 27.74  ? 78  VAL A CG1 1 
ATOM   681  C  CG2 . VAL A 1 78  ? -22.272 10.900  18.227  1.00 22.38  ? 78  VAL A CG2 1 
ATOM   682  N  N   . LEU A 1 79  ? -19.843 8.306   19.076  1.00 11.96  ? 79  LEU A N   1 
ATOM   683  C  CA  . LEU A 1 79  ? -19.843 7.451   20.224  1.00 12.23  ? 79  LEU A CA  1 
ATOM   684  C  C   . LEU A 1 79  ? -19.826 8.267   21.484  1.00 12.19  ? 79  LEU A C   1 
ATOM   685  O  O   . LEU A 1 79  ? -18.987 9.214   21.583  1.00 13.60  ? 79  LEU A O   1 
ATOM   686  C  CB  . LEU A 1 79  ? -18.578 6.529   20.127  1.00 12.55  ? 79  LEU A CB  1 
ATOM   687  C  CG  . LEU A 1 79  ? -18.471 5.510   21.186  1.00 13.25  ? 79  LEU A CG  1 
ATOM   688  C  CD1 . LEU A 1 79  ? -19.541 4.418   20.998  1.00 18.04  ? 79  LEU A CD1 1 
ATOM   689  C  CD2 . LEU A 1 79  ? -17.106 4.817   21.082  1.00 13.74  ? 79  LEU A CD2 1 
ATOM   690  N  N   . LYS A 1 80  ? -20.703 7.936   22.416  1.00 13.31  ? 80  LYS A N   1 
ATOM   691  C  CA  . LYS A 1 80  ? -20.735 8.646   23.718  1.00 14.51  ? 80  LYS A CA  1 
ATOM   692  C  C   . LYS A 1 80  ? -21.249 7.727   24.791  1.00 13.26  ? 80  LYS A C   1 
ATOM   693  O  O   . LYS A 1 80  ? -21.555 6.543   24.472  1.00 14.01  ? 80  LYS A O   1 
ATOM   694  C  CB  . LYS A 1 80  ? -21.457 9.991   23.681  1.00 18.63  ? 80  LYS A CB  1 
ATOM   695  C  CG  . LYS A 1 80  ? -22.857 9.747   23.438  1.00 18.89  ? 80  LYS A CG  1 
ATOM   696  C  CD  . LYS A 1 80  ? -23.241 10.907  22.601  1.00 38.93  ? 80  LYS A CD  1 
ATOM   697  C  CE  . LYS A 1 80  ? -23.295 12.118  23.470  1.00 39.89  ? 80  LYS A CE  1 
ATOM   698  N  NZ  . LYS A 1 80  ? -24.550 11.922  24.213  1.00 83.01  ? 80  LYS A NZ  1 
ATOM   699  N  N   . GLY A 1 81  ? -21.372 8.211   25.998  1.00 14.99  ? 81  GLY A N   1 
ATOM   700  C  CA  . GLY A 1 81  ? -21.823 7.378   27.081  1.00 15.71  ? 81  GLY A CA  1 
ATOM   701  C  C   . GLY A 1 81  ? -20.838 6.322   27.367  1.00 15.11  ? 81  GLY A C   1 
ATOM   702  O  O   . GLY A 1 81  ? -19.628 6.502   27.179  1.00 14.57  ? 81  GLY A O   1 
ATOM   703  N  N   . GLY A 1 82  ? -21.281 5.215   27.949  1.00 19.46  ? 82  GLY A N   1 
ATOM   704  C  CA  . GLY A 1 82  ? -20.368 4.188   28.346  1.00 21.78  ? 82  GLY A CA  1 
ATOM   705  C  C   . GLY A 1 82  ? -19.480 4.810   29.437  1.00 18.96  ? 82  GLY A C   1 
ATOM   706  O  O   . GLY A 1 82  ? -19.934 5.535   30.317  1.00 25.52  ? 82  GLY A O   1 
ATOM   707  N  N   . PRO A 1 83  ? -18.143 4.602   29.334  1.00 16.40  ? 83  PRO A N   1 
ATOM   708  C  CA  . PRO A 1 83  ? -17.243 5.213   30.234  1.00 16.35  ? 83  PRO A CA  1 
ATOM   709  C  C   . PRO A 1 83  ? -16.830 6.618   29.834  1.00 16.74  ? 83  PRO A C   1 
ATOM   710  O  O   . PRO A 1 83  ? -16.023 7.186   30.521  1.00 18.81  ? 83  PRO A O   1 
ATOM   711  C  CB  . PRO A 1 83  ? -15.954 4.315   30.072  1.00 16.80  ? 83  PRO A CB  1 
ATOM   712  C  CG  . PRO A 1 83  ? -15.966 3.962   28.617  1.00 15.50  ? 83  PRO A CG  1 
ATOM   713  C  CD  . PRO A 1 83  ? -17.463 3.795   28.317  1.00 15.65  ? 83  PRO A CD  1 
ATOM   714  N  N   . LEU A 1 84  ? -17.321 7.134   28.719  1.00 13.96  ? 84  LEU A N   1 
ATOM   715  C  CA  . LEU A 1 84  ? -16.747 8.347   28.104  1.00 13.83  ? 84  LEU A CA  1 
ATOM   716  C  C   . LEU A 1 84  ? -17.374 9.593   28.666  1.00 15.44  ? 84  LEU A C   1 
ATOM   717  O  O   . LEU A 1 84  ? -18.545 9.634   28.955  1.00 16.79  ? 84  LEU A O   1 
ATOM   718  C  CB  . LEU A 1 84  ? -17.001 8.320   26.647  1.00 12.41  ? 84  LEU A CB  1 
ATOM   719  C  CG  . LEU A 1 84  ? -16.434 7.107   25.914  1.00 11.88  ? 84  LEU A CG  1 
ATOM   720  C  CD1 . LEU A 1 84  ? -16.960 7.018   24.472  1.00 13.35  ? 84  LEU A CD1 1 
ATOM   721  C  CD2 . LEU A 1 84  ? -14.900 7.051   26.018  1.00 11.99  ? 84  LEU A CD2 1 
ATOM   722  N  N   . ASP A 1 85  ? -16.549 10.641  28.746  1.00 16.95  ? 85  ASP A N   1 
ATOM   723  C  CA  . ASP A 1 85  ? -17.022 11.944  29.192  1.00 19.06  ? 85  ASP A CA  1 
ATOM   724  C  C   . ASP A 1 85  ? -17.430 12.887  28.088  1.00 21.85  ? 85  ASP A C   1 
ATOM   725  O  O   . ASP A 1 85  ? -18.143 13.861  28.350  1.00 40.84  ? 85  ASP A O   1 
ATOM   726  C  CB  . ASP A 1 85  ? -16.035 12.655  30.094  1.00 21.72  ? 85  ASP A CB  1 
ATOM   727  C  CG  . ASP A 1 85  ? -16.146 12.172  31.562  1.00 25.16  ? 85  ASP A CG  1 
ATOM   728  O  OD1 . ASP A 1 85  ? -17.240 11.637  31.992  1.00 37.08  ? 85  ASP A OD1 1 
ATOM   729  O  OD2 . ASP A 1 85  ? -15.135 12.330  32.319  1.00 30.06  ? 85  ASP A OD2 1 
ATOM   730  N  N   . GLY A 1 86  ? -16.995 12.638  26.864  1.00 28.83  ? 86  GLY A N   1 
ATOM   731  C  CA  . GLY A 1 86  ? -17.419 13.559  25.854  1.00 32.74  ? 86  GLY A CA  1 
ATOM   732  C  C   . GLY A 1 86  ? -18.295 12.983  24.781  1.00 23.97  ? 86  GLY A C   1 
ATOM   733  O  O   . GLY A 1 86  ? -19.072 12.085  24.938  1.00 27.87  ? 86  GLY A O   1 
ATOM   734  N  N   A THR A 1 87  ? -17.995 13.601  23.626  0.50 18.57  ? 87  THR A N   1 
ATOM   735  N  N   B THR A 1 87  ? -18.141 13.576  23.633  0.50 14.78  ? 87  THR A N   1 
ATOM   736  C  CA  A THR A 1 87  ? -18.431 13.109  22.292  0.50 18.69  ? 87  THR A CA  1 
ATOM   737  C  CA  B THR A 1 87  ? -18.526 12.902  22.439  0.50 12.88  ? 87  THR A CA  1 
ATOM   738  C  C   A THR A 1 87  ? -17.280 12.782  21.379  0.50 14.58  ? 87  THR A C   1 
ATOM   739  C  C   B THR A 1 87  ? -17.270 12.673  21.620  0.50 10.80  ? 87  THR A C   1 
ATOM   740  O  O   A THR A 1 87  ? -16.384 13.587  21.135  0.50 12.85  ? 87  THR A O   1 
ATOM   741  O  O   B THR A 1 87  ? -16.311 13.490  21.641  0.50 10.88  ? 87  THR A O   1 
ATOM   742  C  CB  A THR A 1 87  ? -19.327 14.113  21.546  0.50 21.34  ? 87  THR A CB  1 
ATOM   743  C  CB  B THR A 1 87  ? -19.527 13.763  21.681  0.50 15.40  ? 87  THR A CB  1 
ATOM   744  O  OG1 A THR A 1 87  ? -20.470 14.422  22.331  0.50 27.30  ? 87  THR A OG1 1 
ATOM   745  O  OG1 B THR A 1 87  ? -18.937 15.055  21.483  0.50 13.36  ? 87  THR A OG1 1 
ATOM   746  C  CG2 A THR A 1 87  ? -19.782 13.541  20.203  0.50 20.62  ? 87  THR A CG2 1 
ATOM   747  C  CG2 B THR A 1 87  ? -20.865 13.929  22.453  0.50 16.81  ? 87  THR A CG2 1 
ATOM   748  N  N   . TYR A 1 88  ? -17.325 11.566  20.894  1.00 11.62  ? 88  TYR A N   1 
ATOM   749  C  CA  . TYR A 1 88  ? -16.224 11.074  20.048  1.00 10.84  ? 88  TYR A CA  1 
ATOM   750  C  C   . TYR A 1 88  ? -16.782 10.773  18.676  1.00 10.80  ? 88  TYR A C   1 
ATOM   751  O  O   . TYR A 1 88  ? -17.766 10.091  18.495  1.00 14.13  ? 88  TYR A O   1 
ATOM   752  C  CB  . TYR A 1 88  ? -15.574 9.856   20.621  1.00 11.04  ? 88  TYR A CB  1 
ATOM   753  C  CG  . TYR A 1 88  ? -14.835 10.047  21.936  1.00 9.59   ? 88  TYR A CG  1 
ATOM   754  C  CD1 . TYR A 1 88  ? -15.468 10.375  23.138  1.00 11.06  ? 88  TYR A CD1 1 
ATOM   755  C  CD2 . TYR A 1 88  ? -13.454 9.901   21.947  1.00 9.06   ? 88  TYR A CD2 1 
ATOM   756  C  CE1 . TYR A 1 88  ? -14.748 10.549  24.332  1.00 10.67  ? 88  TYR A CE1 1 
ATOM   757  C  CE2 . TYR A 1 88  ? -12.730 10.008  23.159  1.00 9.20   ? 88  TYR A CE2 1 
ATOM   758  C  CZ  . TYR A 1 88  ? -13.389 10.323  24.338  1.00 9.74   ? 88  TYR A CZ  1 
ATOM   759  O  OH  . TYR A 1 88  ? -12.672 10.402  25.499  1.00 10.23  ? 88  TYR A OH  1 
ATOM   760  N  N   . ARG A 1 89  ? -16.131 11.290  17.672  1.00 10.46  ? 89  ARG A N   1 
ATOM   761  C  CA  . ARG A 1 89  ? -16.560 11.177  16.277  1.00 11.30  ? 89  ARG A CA  1 
ATOM   762  C  C   . ARG A 1 89  ? -15.830 10.081  15.533  1.00 8.41   ? 89  ARG A C   1 
ATOM   763  O  O   . ARG A 1 89  ? -14.607 9.954   15.580  1.00 8.72   ? 89  ARG A O   1 
ATOM   764  C  CB  . ARG A 1 89  ? -16.218 12.505  15.558  1.00 14.53  ? 89  ARG A CB  1 
ATOM   765  C  CG  . ARG A 1 89  ? -17.108 12.580  14.331  1.00 15.15  ? 89  ARG A CG  1 
ATOM   766  C  CD  . ARG A 1 89  ? -16.940 13.958  13.715  1.00 16.81  ? 89  ARG A CD  1 
ATOM   767  N  NE  . ARG A 1 89  ? -17.535 14.978  14.573  1.00 16.58  ? 89  ARG A NE  1 
ATOM   768  C  CZ  . ARG A 1 89  ? -17.398 16.288  14.398  1.00 14.63  ? 89  ARG A CZ  1 
ATOM   769  N  NH1 . ARG A 1 89  ? -16.670 16.756  13.392  1.00 19.57  ? 89  ARG A NH1 1 
ATOM   770  N  NH2 . ARG A 1 89  ? -17.989 17.130  15.235  1.00 17.69  ? 89  ARG A NH2 1 
ATOM   771  N  N   . LEU A 1 90  ? -16.614 9.247   14.819  1.00 9.66   ? 90  LEU A N   1 
ATOM   772  C  CA  . LEU A 1 90  ? -16.056 8.158   14.000  1.00 10.06  ? 90  LEU A CA  1 
ATOM   773  C  C   . LEU A 1 90  ? -15.213 8.720   12.880  1.00 9.76   ? 90  LEU A C   1 
ATOM   774  O  O   . LEU A 1 90  ? -15.704 9.556   12.077  1.00 11.82  ? 90  LEU A O   1 
ATOM   775  C  CB  . LEU A 1 90  ? -17.189 7.313   13.429  1.00 11.01  ? 90  LEU A CB  1 
ATOM   776  C  CG  . LEU A 1 90  ? -16.764 6.143   12.518  1.00 11.35  ? 90  LEU A CG  1 
ATOM   777  C  CD1 . LEU A 1 90  ? -16.042 5.055   13.316  1.00 12.59  ? 90  LEU A CD1 1 
ATOM   778  C  CD2 . LEU A 1 90  ? -18.013 5.507   11.916  1.00 14.35  ? 90  LEU A CD2 1 
ATOM   779  N  N   . ILE A 1 91  ? -13.995 8.256   12.747  1.00 9.35   ? 91  ILE A N   1 
ATOM   780  C  CA  . ILE A 1 91  ? -13.142 8.612   11.652  1.00 9.51   ? 91  ILE A CA  1 
ATOM   781  C  C   . ILE A 1 91  ? -12.920 7.452   10.682  1.00 8.95   ? 91  ILE A C   1 
ATOM   782  O  O   . ILE A 1 91  ? -12.848 7.649   9.461   1.00 10.20  ? 91  ILE A O   1 
ATOM   783  C  CB  . ILE A 1 91  ? -11.807 9.245   12.119  1.00 10.81  ? 91  ILE A CB  1 
ATOM   784  C  CG1 . ILE A 1 91  ? -10.931 9.678   10.918  1.00 13.29  ? 91  ILE A CG1 1 
ATOM   785  C  CG2 . ILE A 1 91  ? -11.033 8.372   13.078  1.00 10.97  ? 91  ILE A CG2 1 
ATOM   786  C  CD1 . ILE A 1 91  ? -9.795  10.592  11.302  1.00 15.27  ? 91  ILE A CD1 1 
ATOM   787  N  N   . GLN A 1 92  ? -12.752 6.216   11.187  1.00 9.14   ? 92  GLN A N   1 
ATOM   788  C  CA  . GLN A 1 92  ? -12.496 5.081   10.321  1.00 9.14   ? 92  GLN A CA  1 
ATOM   789  C  C   . GLN A 1 92  ? -12.688 3.810   11.076  1.00 8.94   ? 92  GLN A C   1 
ATOM   790  O  O   . GLN A 1 92  ? -12.763 3.823   12.315  1.00 9.16   ? 92  GLN A O   1 
ATOM   791  C  CB  . GLN A 1 92  ? -11.104 5.155   9.779   1.00 10.59  ? 92  GLN A CB  1 
ATOM   792  C  CG  . GLN A 1 92  ? -9.949  5.058   10.809  1.00 11.13  ? 92  GLN A CG  1 
ATOM   793  C  CD  . GLN A 1 92  ? -9.299  3.700   10.728  1.00 11.15  ? 92  GLN A CD  1 
ATOM   794  O  OE1 . GLN A 1 92  ? -9.715  2.742   11.369  1.00 10.70  ? 92  GLN A OE1 1 
ATOM   795  N  NE2 . GLN A 1 92  ? -8.339  3.516   9.801   1.00 13.50  ? 92  GLN A NE2 1 
ATOM   796  N  N   . PHE A 1 93  ? -12.785 2.683   10.358  1.00 8.76   ? 93  PHE A N   1 
ATOM   797  C  CA  . PHE A 1 93  ? -12.634 1.405   10.980  1.00 8.50   ? 93  PHE A CA  1 
ATOM   798  C  C   . PHE A 1 93  ? -11.652 0.573   10.183  1.00 8.04   ? 93  PHE A C   1 
ATOM   799  O  O   . PHE A 1 93  ? -11.388 0.787   8.983   1.00 9.72   ? 93  PHE A O   1 
ATOM   800  C  CB  . PHE A 1 93  ? -13.949 0.679   11.237  1.00 9.31   ? 93  PHE A CB  1 
ATOM   801  C  CG  . PHE A 1 93  ? -14.681 0.196   10.009  1.00 9.39   ? 93  PHE A CG  1 
ATOM   802  C  CD1 . PHE A 1 93  ? -14.322 -0.946  9.331   1.00 9.81   ? 93  PHE A CD1 1 
ATOM   803  C  CD2 . PHE A 1 93  ? -15.836 0.875   9.581   1.00 10.64  ? 93  PHE A CD2 1 
ATOM   804  C  CE1 . PHE A 1 93  ? -15.053 -1.402  8.231   1.00 11.23  ? 93  PHE A CE1 1 
ATOM   805  C  CE2 . PHE A 1 93  ? -16.561 0.408   8.478   1.00 11.63  ? 93  PHE A CE2 1 
ATOM   806  C  CZ  . PHE A 1 93  ? -16.175 -0.710  7.808   1.00 12.27  ? 93  PHE A CZ  1 
ATOM   807  N  N   . HIS A 1 94  ? -11.117 -0.459  10.865  1.00 8.58   ? 94  HIS A N   1 
ATOM   808  C  CA  . HIS A 1 94  ? -10.185 -1.429  10.270  1.00 8.14   ? 94  HIS A CA  1 
ATOM   809  C  C   . HIS A 1 94  ? -10.288 -2.694  11.101  1.00 7.80   ? 94  HIS A C   1 
ATOM   810  O  O   . HIS A 1 94  ? -10.903 -2.735  12.145  1.00 8.09   ? 94  HIS A O   1 
ATOM   811  C  CB  . HIS A 1 94  ? -8.754  -0.922  10.180  1.00 8.67   ? 94  HIS A CB  1 
ATOM   812  C  CG  . HIS A 1 94  ? -8.189  -0.636  11.545  1.00 8.11   ? 94  HIS A CG  1 
ATOM   813  N  ND1 . HIS A 1 94  ? -8.382  0.538   12.215  1.00 7.99   ? 94  HIS A ND1 1 
ATOM   814  C  CD2 . HIS A 1 94  ? -7.552  -1.465  12.442  1.00 7.75   ? 94  HIS A CD2 1 
ATOM   815  C  CE1 . HIS A 1 94  ? -7.878  0.417   13.441  1.00 8.05   ? 94  HIS A CE1 1 
ATOM   816  N  NE2 . HIS A 1 94  ? -7.360  -0.796  13.606  1.00 7.81   ? 94  HIS A NE2 1 
ATOM   817  N  N   . PHE A 1 95  ? -9.581  -3.729  10.628  1.00 7.93   ? 95  PHE A N   1 
ATOM   818  C  CA  . PHE A 1 95  ? -9.512  -5.030  11.305  1.00 8.20   ? 95  PHE A CA  1 
ATOM   819  C  C   . PHE A 1 95  ? -8.070  -5.448  11.491  1.00 7.67   ? 95  PHE A C   1 
ATOM   820  O  O   . PHE A 1 95  ? -7.170  -4.964  10.825  1.00 8.71   ? 95  PHE A O   1 
ATOM   821  C  CB  . PHE A 1 95  ? -10.220 -6.111  10.445  1.00 8.62   ? 95  PHE A CB  1 
ATOM   822  C  CG  . PHE A 1 95  ? -11.683 -5.867  10.172  1.00 8.73   ? 95  PHE A CG  1 
ATOM   823  C  CD1 . PHE A 1 95  ? -12.066 -4.990  9.162   1.00 9.72   ? 95  PHE A CD1 1 
ATOM   824  C  CD2 . PHE A 1 95  ? -12.684 -6.544  10.873  1.00 9.51   ? 95  PHE A CD2 1 
ATOM   825  C  CE1 . PHE A 1 95  ? -13.403 -4.820  8.844   1.00 10.95  ? 95  PHE A CE1 1 
ATOM   826  C  CE2 . PHE A 1 95  ? -14.036 -6.398  10.542  1.00 10.14  ? 95  PHE A CE2 1 
ATOM   827  C  CZ  . PHE A 1 95  ? -14.399 -5.499  9.526   1.00 10.61  ? 95  PHE A CZ  1 
ATOM   828  N  N   . HIS A 1 96  ? -7.909  -6.433  12.384  1.00 7.46   ? 96  HIS A N   1 
ATOM   829  C  CA  . HIS A 1 96  ? -6.713  -7.225  12.542  1.00 7.97   ? 96  HIS A CA  1 
ATOM   830  C  C   . HIS A 1 96  ? -7.151  -8.684  12.436  1.00 7.82   ? 96  HIS A C   1 
ATOM   831  O  O   . HIS A 1 96  ? -8.229  -9.030  12.925  1.00 8.09   ? 96  HIS A O   1 
ATOM   832  C  CB  . HIS A 1 96  ? -6.032  -7.001  13.934  1.00 8.03   ? 96  HIS A CB  1 
ATOM   833  C  CG  . HIS A 1 96  ? -5.736  -5.551  14.199  1.00 7.62   ? 96  HIS A CG  1 
ATOM   834  N  ND1 . HIS A 1 96  ? -4.516  -4.993  14.042  1.00 8.29   ? 96  HIS A ND1 1 
ATOM   835  C  CD2 . HIS A 1 96  ? -6.554  -4.523  14.598  1.00 7.28   ? 96  HIS A CD2 1 
ATOM   836  C  CE1 . HIS A 1 96  ? -4.585  -3.686  14.330  1.00 8.21   ? 96  HIS A CE1 1 
ATOM   837  N  NE2 . HIS A 1 96  ? -5.806  -3.367  14.667  1.00 7.42   ? 96  HIS A NE2 1 
ATOM   838  N  N   . TRP A 1 97  ? -6.344  -9.523  11.801  1.00 7.75   ? 97  TRP A N   1 
ATOM   839  C  CA  . TRP A 1 97  ? -6.737  -10.907 11.599  1.00 8.26   ? 97  TRP A CA  1 
ATOM   840  C  C   . TRP A 1 97  ? -5.542  -11.798 11.466  1.00 8.08   ? 97  TRP A C   1 
ATOM   841  O  O   . TRP A 1 97  ? -4.381  -11.386 11.391  1.00 8.67   ? 97  TRP A O   1 
ATOM   842  C  CB  . TRP A 1 97  ? -7.676  -11.037 10.364  1.00 9.03   ? 97  TRP A CB  1 
ATOM   843  C  CG  . TRP A 1 97  ? -7.014  -10.657 9.082   1.00 8.73   ? 97  TRP A CG  1 
ATOM   844  C  CD1 . TRP A 1 97  ? -6.317  -11.462 8.232   1.00 9.84   ? 97  TRP A CD1 1 
ATOM   845  C  CD2 . TRP A 1 97  ? -6.946  -9.338  8.512   1.00 9.23   ? 97  TRP A CD2 1 
ATOM   846  N  NE1 . TRP A 1 97  ? -5.894  -10.746 7.131   1.00 10.38  ? 97  TRP A NE1 1 
ATOM   847  C  CE2 . TRP A 1 97  ? -6.224  -9.447  7.288   1.00 10.06  ? 97  TRP A CE2 1 
ATOM   848  C  CE3 . TRP A 1 97  ? -7.435  -8.051  8.909   1.00 9.06   ? 97  TRP A CE3 1 
ATOM   849  C  CZ2 . TRP A 1 97  ? -6.034  -8.338  6.457   1.00 10.49  ? 97  TRP A CZ2 1 
ATOM   850  C  CZ3 . TRP A 1 97  ? -7.173  -6.975  8.108   1.00 10.41  ? 97  TRP A CZ3 1 
ATOM   851  C  CH2 . TRP A 1 97  ? -6.513  -7.116  6.882   1.00 11.31  ? 97  TRP A CH2 1 
ATOM   852  N  N   . GLY A 1 98  ? -5.837  -13.129 11.446  1.00 8.97   ? 98  GLY A N   1 
ATOM   853  C  CA  . GLY A 1 98  ? -4.794  -14.128 11.494  1.00 9.05   ? 98  GLY A CA  1 
ATOM   854  C  C   . GLY A 1 98  ? -4.598  -14.829 10.157  1.00 9.41   ? 98  GLY A C   1 
ATOM   855  O  O   . GLY A 1 98  ? -5.310  -14.672 9.192   1.00 10.62  ? 98  GLY A O   1 
ATOM   856  N  N   . SER A 1 99  ? -3.544  -15.700 10.185  1.00 10.86  ? 99  SER A N   1 
ATOM   857  C  CA  . SER A 1 99  ? -3.310  -16.628 9.075   1.00 11.30  ? 99  SER A CA  1 
ATOM   858  C  C   . SER A 1 99  ? -4.215  -17.856 9.168   1.00 12.36  ? 99  SER A C   1 
ATOM   859  O  O   . SER A 1 99  ? -4.299  -18.590 8.195   1.00 15.92  ? 99  SER A O   1 
ATOM   860  C  CB  . SER A 1 99  ? -1.877  -16.998 9.075   1.00 13.63  ? 99  SER A CB  1 
ATOM   861  O  OG  . SER A 1 99  ? -1.441  -17.496 10.329  1.00 12.98  ? 99  SER A OG  1 
ATOM   862  N  N   . LEU A 1 100 ? -4.833  -18.102 10.320  1.00 12.28  ? 100 LEU A N   1 
ATOM   863  C  CA  . LEU A 1 100 ? -5.617  -19.281 10.673  1.00 14.19  ? 100 LEU A CA  1 
ATOM   864  C  C   . LEU A 1 100 ? -6.733  -18.799 11.518  1.00 12.29  ? 100 LEU A C   1 
ATOM   865  O  O   . LEU A 1 100 ? -6.595  -17.780 12.204  1.00 12.15  ? 100 LEU A O   1 
ATOM   866  C  CB  . LEU A 1 100 ? -4.802  -20.237 11.663  1.00 20.81  ? 100 LEU A CB  1 
ATOM   867  C  CG  . LEU A 1 100 ? -3.442  -20.615 11.138  1.00 21.19  ? 100 LEU A CG  1 
ATOM   868  C  CD1 . LEU A 1 100 ? -2.391  -20.984 12.179  1.00 28.63  ? 100 LEU A CD1 1 
ATOM   869  C  CD2 . LEU A 1 100 ? -3.694  -21.650 10.062  1.00 35.22  ? 100 LEU A CD2 1 
ATOM   870  N  N   . ASP A 1 101 ? -7.840  -19.548 11.586  1.00 12.41  ? 101 ASP A N   1 
ATOM   871  C  CA  . ASP A 1 101 ? -9.015  -19.086 12.344  1.00 12.03  ? 101 ASP A CA  1 
ATOM   872  C  C   . ASP A 1 101 ? -8.721  -19.012 13.826  1.00 11.47  ? 101 ASP A C   1 
ATOM   873  O  O   . ASP A 1 101 ? -9.397  -18.296 14.519  1.00 13.51  ? 101 ASP A O   1 
ATOM   874  C  CB  . ASP A 1 101 ? -10.207 -19.987 12.111  1.00 13.52  ? 101 ASP A CB  1 
ATOM   875  C  CG  . ASP A 1 101 ? -10.676 -20.078 10.684  1.00 15.93  ? 101 ASP A CG  1 
ATOM   876  O  OD1 . ASP A 1 101 ? -10.435 -19.162 9.855   1.00 15.30  ? 101 ASP A OD1 1 
ATOM   877  O  OD2 . ASP A 1 101 ? -11.509 -20.969 10.427  1.00 20.59  ? 101 ASP A OD2 1 
ATOM   878  N  N   . GLY A 1 102 ? -7.722  -19.778 14.312  1.00 12.74  ? 102 GLY A N   1 
ATOM   879  C  CA  . GLY A 1 102 ? -7.402  -19.803 15.720  1.00 13.04  ? 102 GLY A CA  1 
ATOM   880  C  C   . GLY A 1 102 ? -6.623  -18.621 16.281  1.00 11.46  ? 102 GLY A C   1 
ATOM   881  O  O   . GLY A 1 102 ? -6.249  -18.625 17.463  1.00 12.30  ? 102 GLY A O   1 
ATOM   882  N  N   . GLN A 1 103 ? -6.323  -17.609 15.480  1.00 10.55  ? 103 GLN A N   1 
ATOM   883  C  CA  . GLN A 1 103 ? -5.630  -16.427 15.977  1.00 9.68   ? 103 GLN A CA  1 
ATOM   884  C  C   . GLN A 1 103 ? -6.032  -15.258 15.086  1.00 8.59   ? 103 GLN A C   1 
ATOM   885  O  O   . GLN A 1 103 ? -6.551  -15.450 13.993  1.00 9.48   ? 103 GLN A O   1 
ATOM   886  C  CB  . GLN A 1 103 ? -4.121  -16.598 15.997  1.00 10.60  ? 103 GLN A CB  1 
ATOM   887  C  CG  . GLN A 1 103 ? -3.528  -16.830 14.599  1.00 11.77  ? 103 GLN A CG  1 
ATOM   888  C  CD  . GLN A 1 103 ? -2.138  -17.395 14.705  1.00 15.20  ? 103 GLN A CD  1 
ATOM   889  O  OE1 . GLN A 1 103 ? -1.919  -18.317 15.475  1.00 24.72  ? 103 GLN A OE1 1 
ATOM   890  N  NE2 . GLN A 1 103 ? -1.230  -16.934 13.911  1.00 14.30  ? 103 GLN A NE2 1 
ATOM   891  N  N   . GLY A 1 104 ? -5.719  -14.040 15.555  1.00 8.12   ? 104 GLY A N   1 
ATOM   892  C  CA  . GLY A 1 104 ? -6.006  -12.863 14.770  1.00 7.91   ? 104 GLY A CA  1 
ATOM   893  C  C   . GLY A 1 104 ? -6.446  -11.667 15.596  1.00 7.84   ? 104 GLY A C   1 
ATOM   894  O  O   . GLY A 1 104 ? -6.179  -10.530 15.227  1.00 8.45   ? 104 GLY A O   1 
ATOM   895  N  N   . SER A 1 105 ? -7.144  -11.916 16.729  1.00 7.78   ? 105 SER A N   1 
ATOM   896  C  CA  . SER A 1 105 ? -7.530  -10.806 17.579  1.00 7.66   ? 105 SER A CA  1 
ATOM   897  C  C   . SER A 1 105 ? -6.334  -10.249 18.313  1.00 7.43   ? 105 SER A C   1 
ATOM   898  O  O   . SER A 1 105 ? -5.306  -10.920 18.530  1.00 8.50   ? 105 SER A O   1 
ATOM   899  C  CB  . SER A 1 105 ? -8.695  -11.157 18.521  1.00 7.58   ? 105 SER A CB  1 
ATOM   900  O  OG  . SER A 1 105 ? -8.319  -12.126 19.473  1.00 8.01   ? 105 SER A OG  1 
ATOM   901  N  N   . GLU A 1 106 ? -6.481  -8.996  18.710  1.00 7.27   ? 106 GLU A N   1 
ATOM   902  C  CA  . GLU A 1 106 ? -5.444  -8.298  19.549  1.00 7.25   ? 106 GLU A CA  1 
ATOM   903  C  C   . GLU A 1 106 ? -5.774  -8.507  21.011  1.00 7.06   ? 106 GLU A C   1 
ATOM   904  O  O   . GLU A 1 106 ? -4.990  -9.086  21.788  1.00 7.74   ? 106 GLU A O   1 
ATOM   905  C  CB  . GLU A 1 106 ? -5.392  -6.819  19.112  1.00 7.24   ? 106 GLU A CB  1 
ATOM   906  C  CG  . GLU A 1 106 ? -5.030  -6.661  17.674  1.00 9.03   ? 106 GLU A CG  1 
ATOM   907  C  CD  . GLU A 1 106 ? -4.254  -5.418  17.401  1.00 7.51   ? 106 GLU A CD  1 
ATOM   908  O  OE1 . GLU A 1 106 ? -4.861  -4.318  17.595  1.00 8.17   ? 106 GLU A OE1 1 
ATOM   909  O  OE2 . GLU A 1 106 ? -3.087  -5.510  17.056  1.00 9.19   ? 106 GLU A OE2 1 
ATOM   910  N  N   . HIS A 1 107 ? -6.955  -8.043  21.444  1.00 6.95   ? 107 HIS A N   1 
ATOM   911  C  CA  . HIS A 1 107 ? -7.414  -8.434  22.748  1.00 6.85   ? 107 HIS A CA  1 
ATOM   912  C  C   . HIS A 1 107 ? -7.712  -9.949  22.764  1.00 6.63   ? 107 HIS A C   1 
ATOM   913  O  O   . HIS A 1 107 ? -8.053  -10.551 21.747  1.00 7.46   ? 107 HIS A O   1 
ATOM   914  C  CB  . HIS A 1 107 ? -8.671  -7.629  23.146  1.00 7.16   ? 107 HIS A CB  1 
ATOM   915  C  CG  . HIS A 1 107 ? -8.367  -6.184  23.296  1.00 6.85   ? 107 HIS A CG  1 
ATOM   916  N  ND1 . HIS A 1 107 ? -8.410  -5.287  22.257  1.00 7.36   ? 107 HIS A ND1 1 
ATOM   917  C  CD2 . HIS A 1 107 ? -7.897  -5.481  24.374  1.00 7.05   ? 107 HIS A CD2 1 
ATOM   918  C  CE1 . HIS A 1 107 ? -7.944  -4.088  22.721  1.00 7.65   ? 107 HIS A CE1 1 
ATOM   919  N  NE2 . HIS A 1 107 ? -7.651  -4.178  24.003  1.00 7.22   ? 107 HIS A NE2 1 
ATOM   920  N  N   . THR A 1 108 ? -7.599  -10.515 23.975  1.00 7.33   ? 108 THR A N   1 
ATOM   921  C  CA  . THR A 1 108 ? -7.960  -11.883 24.210  1.00 7.52   ? 108 THR A CA  1 
ATOM   922  C  C   . THR A 1 108 ? -8.931  -11.884 25.420  1.00 7.66   ? 108 THR A C   1 
ATOM   923  O  O   . THR A 1 108 ? -8.953  -10.932 26.199  1.00 8.34   ? 108 THR A O   1 
ATOM   924  C  CB  . THR A 1 108 ? -6.748  -12.797 24.430  1.00 8.36   ? 108 THR A CB  1 
ATOM   925  O  OG1 . THR A 1 108 ? -5.932  -12.315 25.484  1.00 8.99   ? 108 THR A OG1 1 
ATOM   926  C  CG2 . THR A 1 108 ? -5.932  -12.878 23.145  1.00 9.50   ? 108 THR A CG2 1 
ATOM   927  N  N   . VAL A 1 109 ? -9.683  -12.973 25.567  1.00 8.43   ? 109 VAL A N   1 
ATOM   928  C  CA  . VAL A 1 109 ? -10.698 -13.055 26.659  1.00 8.81   ? 109 VAL A CA  1 
ATOM   929  C  C   . VAL A 1 109 ? -10.368 -14.345 27.395  1.00 9.28   ? 109 VAL A C   1 
ATOM   930  O  O   . VAL A 1 109 ? -10.542 -15.449 26.819  1.00 9.74   ? 109 VAL A O   1 
ATOM   931  C  CB  . VAL A 1 109 ? -12.112 -13.079 26.087  1.00 9.90   ? 109 VAL A CB  1 
ATOM   932  C  CG1 . VAL A 1 109 ? -13.141 -13.205 27.230  1.00 11.64  ? 109 VAL A CG1 1 
ATOM   933  C  CG2 . VAL A 1 109 ? -12.400 -11.799 25.277  1.00 10.57  ? 109 VAL A CG2 1 
ATOM   934  N  N   . ASP A 1 110 ? -9.864  -14.247 28.624  1.00 9.88   ? 110 ASP A N   1 
ATOM   935  C  CA  . ASP A 1 110 ? -9.397  -15.478 29.315  1.00 11.39  ? 110 ASP A CA  1 
ATOM   936  C  C   . ASP A 1 110 ? -8.473  -16.288 28.452  1.00 10.60  ? 110 ASP A C   1 
ATOM   937  O  O   . ASP A 1 110 ? -8.529  -17.522 28.381  1.00 11.46  ? 110 ASP A O   1 
ATOM   938  C  CB  . ASP A 1 110 ? -10.574 -16.312 29.817  1.00 13.50  ? 110 ASP A CB  1 
ATOM   939  C  CG  . ASP A 1 110 ? -11.418 -15.542 30.859  1.00 14.79  ? 110 ASP A CG  1 
ATOM   940  O  OD1 . ASP A 1 110 ? -10.866 -14.658 31.548  1.00 14.81  ? 110 ASP A OD1 1 
ATOM   941  O  OD2 . ASP A 1 110 ? -12.619 -15.842 30.945  1.00 17.00  ? 110 ASP A OD2 1 
ATOM   942  N  N   . LYS A 1 111 ? -7.575  -15.569 27.762  1.00 9.45   ? 111 LYS A N   1 
ATOM   943  C  CA  . LYS A 1 111 ? -6.557  -16.098 26.869  1.00 10.28  ? 111 LYS A CA  1 
ATOM   944  C  C   . LYS A 1 111 ? -7.121  -16.603 25.522  1.00 9.90   ? 111 LYS A C   1 
ATOM   945  O  O   . LYS A 1 111 ? -6.312  -16.964 24.644  1.00 11.08  ? 111 LYS A O   1 
ATOM   946  C  CB  . LYS A 1 111 ? -5.620  -17.159 27.496  1.00 12.32  ? 111 LYS A CB  1 
ATOM   947  C  CG  . LYS A 1 111 ? -4.934  -16.649 28.747  1.00 16.89  ? 111 LYS A CG  1 
ATOM   948  C  CD  . LYS A 1 111 ? -4.017  -15.421 28.494  1.00 19.13  ? 111 LYS A CD  1 
ATOM   949  C  CE  . LYS A 1 111 ? -3.235  -14.801 29.693  1.00 24.17  ? 111 LYS A CE  1 
ATOM   950  N  NZ  . LYS A 1 111 ? -1.996  -15.534 29.812  1.00 25.33  ? 111 LYS A NZ  1 
ATOM   951  N  N   . LYS A 1 112 ? -8.415  -16.571 25.302  1.00 9.48   ? 112 LYS A N   1 
ATOM   952  C  CA  . LYS A 1 112 ? -8.971  -16.962 24.025  1.00 10.22  ? 112 LYS A CA  1 
ATOM   953  C  C   . LYS A 1 112 ? -8.644  -15.916 22.963  1.00 9.46   ? 112 LYS A C   1 
ATOM   954  O  O   . LYS A 1 112 ? -8.900  -14.722 23.163  1.00 9.35   ? 112 LYS A O   1 
ATOM   955  C  CB  . LYS A 1 112 ? -10.511 -17.067 24.104  1.00 12.12  ? 112 LYS A CB  1 
ATOM   956  C  CG  . LYS A 1 112 ? -11.179 -17.438 22.773  1.00 12.58  ? 112 LYS A CG  1 
ATOM   957  C  CD  . LYS A 1 112 ? -12.717 -17.435 22.880  1.00 16.06  ? 112 LYS A CD  1 
ATOM   958  C  CE  . LYS A 1 112 ? -13.277 -17.567 21.520  1.00 16.56  ? 112 LYS A CE  1 
ATOM   959  N  NZ  . LYS A 1 112 ? -13.175 -18.884 21.030  1.00 18.32  ? 112 LYS A NZ  1 
ATOM   960  N  N   A LYS A 1 113 ? -8.122  -16.395 21.824  0.50 9.46   ? 113 LYS A N   1 
ATOM   961  N  N   B LYS A 1 113 ? -8.122  -16.393 21.823  0.50 9.60   ? 113 LYS A N   1 
ATOM   962  C  CA  A LYS A 1 113 ? -7.926  -15.593 20.631  0.50 9.38   ? 113 LYS A CA  1 
ATOM   963  C  CA  B LYS A 1 113 ? -7.924  -15.590 20.629  0.50 9.68   ? 113 LYS A CA  1 
ATOM   964  C  C   A LYS A 1 113 ? -9.066  -15.813 19.663  0.50 8.94   ? 113 LYS A C   1 
ATOM   965  C  C   B LYS A 1 113 ? -9.062  -15.811 19.658  0.50 8.99   ? 113 LYS A C   1 
ATOM   966  O  O   A LYS A 1 113 ? -9.427  -16.953 19.372  0.50 12.62  ? 113 LYS A O   1 
ATOM   967  O  O   B LYS A 1 113 ? -9.417  -16.957 19.362  0.50 10.38  ? 113 LYS A O   1 
ATOM   968  C  CB  A LYS A 1 113 ? -6.623  -15.998 19.951  0.50 9.16   ? 113 LYS A CB  1 
ATOM   969  C  CB  B LYS A 1 113 ? -6.620  -15.995 19.951  0.50 10.51  ? 113 LYS A CB  1 
ATOM   970  C  CG  A LYS A 1 113 ? -5.370  -15.716 20.739  0.50 10.22  ? 113 LYS A CG  1 
ATOM   971  C  CG  B LYS A 1 113 ? -5.375  -15.665 20.734  0.50 12.06  ? 113 LYS A CG  1 
ATOM   972  C  CD  A LYS A 1 113 ? -4.149  -16.280 20.053  0.50 11.46  ? 113 LYS A CD  1 
ATOM   973  C  CD  B LYS A 1 113 ? -4.108  -16.237 20.126  0.50 13.41  ? 113 LYS A CD  1 
ATOM   974  C  CE  A LYS A 1 113 ? -2.837  -15.796 20.617  0.50 14.01  ? 113 LYS A CE  1 
ATOM   975  C  CE  B LYS A 1 113 ? -2.899  -15.657 20.881  0.50 18.27  ? 113 LYS A CE  1 
ATOM   976  N  NZ  A LYS A 1 113 ? -2.545  -16.437 21.883  0.50 14.58  ? 113 LYS A NZ  1 
ATOM   977  N  NZ  B LYS A 1 113 ? -1.644  -16.425 20.798  0.50 19.42  ? 113 LYS A NZ  1 
ATOM   978  N  N   . TYR A 1 114 ? -9.635  -14.735 19.131  1.00 8.67   ? 114 TYR A N   1 
ATOM   979  C  CA  . TYR A 1 114 ? -10.627 -14.774 18.119  1.00 9.03   ? 114 TYR A CA  1 
ATOM   980  C  C   . TYR A 1 114 ? -9.940  -14.718 16.728  1.00 7.94   ? 114 TYR A C   1 
ATOM   981  O  O   . TYR A 1 114 ? -8.748  -14.419 16.607  1.00 8.65   ? 114 TYR A O   1 
ATOM   982  C  CB  . TYR A 1 114 ? -11.673 -13.674 18.260  1.00 8.69   ? 114 TYR A CB  1 
ATOM   983  C  CG  . TYR A 1 114 ? -12.646 -13.895 19.395  1.00 8.56   ? 114 TYR A CG  1 
ATOM   984  C  CD1 . TYR A 1 114 ? -12.347 -13.493 20.695  1.00 10.26  ? 114 TYR A CD1 1 
ATOM   985  C  CD2 . TYR A 1 114 ? -13.863 -14.508 19.168  1.00 9.89   ? 114 TYR A CD2 1 
ATOM   986  C  CE1 . TYR A 1 114 ? -13.243 -13.686 21.729  1.00 12.77  ? 114 TYR A CE1 1 
ATOM   987  C  CE2 . TYR A 1 114 ? -14.762 -14.710 20.198  1.00 12.75  ? 114 TYR A CE2 1 
ATOM   988  C  CZ  . TYR A 1 114 ? -14.443 -14.298 21.477  1.00 13.80  ? 114 TYR A CZ  1 
ATOM   989  O  OH  . TYR A 1 114 ? -15.319 -14.486 22.524  1.00 19.94  ? 114 TYR A OH  1 
ATOM   990  N  N   . ALA A 1 115 ? -10.683 -15.021 15.666  1.00 8.56   ? 115 ALA A N   1 
ATOM   991  C  CA  . ALA A 1 115 ? -10.169 -15.025 14.302  1.00 8.48   ? 115 ALA A CA  1 
ATOM   992  C  C   . ALA A 1 115 ? -9.796  -13.624 13.804  1.00 8.37   ? 115 ALA A C   1 
ATOM   993  O  O   . ALA A 1 115 ? -8.941  -13.489 12.942  1.00 9.14   ? 115 ALA A O   1 
ATOM   994  C  CB  . ALA A 1 115 ? -11.202 -15.654 13.364  1.00 10.35  ? 115 ALA A CB  1 
ATOM   995  N  N   . ALA A 1 116 ? -10.449 -12.606 14.363  1.00 8.17   ? 116 ALA A N   1 
ATOM   996  C  CA  . ALA A 1 116 ? -10.186 -11.235 13.911  1.00 8.03   ? 116 ALA A CA  1 
ATOM   997  C  C   . ALA A 1 116 ? -10.771 -10.306 14.957  1.00 7.59   ? 116 ALA A C   1 
ATOM   998  O  O   . ALA A 1 116 ? -11.505 -10.700 15.854  1.00 7.89   ? 116 ALA A O   1 
ATOM   999  C  CB  . ALA A 1 116 ? -10.721 -10.959 12.500  1.00 9.18   ? 116 ALA A CB  1 
ATOM   1000 N  N   . GLU A 1 117 ? -10.438 -9.008  14.788  1.00 7.60   ? 117 GLU A N   1 
ATOM   1001 C  CA  . GLU A 1 117 ? -10.984 -7.970  15.658  1.00 7.41   ? 117 GLU A CA  1 
ATOM   1002 C  C   . GLU A 1 117 ? -11.162 -6.718  14.828  1.00 7.24   ? 117 GLU A C   1 
ATOM   1003 O  O   . GLU A 1 117 ? -10.251 -6.299  14.080  1.00 8.98   ? 117 GLU A O   1 
ATOM   1004 C  CB  . GLU A 1 117 ? -9.998  -7.714  16.833  1.00 8.07   ? 117 GLU A CB  1 
ATOM   1005 C  CG  . GLU A 1 117 ? -10.463 -6.777  17.879  1.00 8.00   ? 117 GLU A CG  1 
ATOM   1006 C  CD  . GLU A 1 117 ? -9.544  -6.692  19.102  1.00 7.37   ? 117 GLU A CD  1 
ATOM   1007 O  OE1 . GLU A 1 117 ? -8.896  -7.736  19.421  1.00 8.41   ? 117 GLU A OE1 1 
ATOM   1008 O  OE2 . GLU A 1 117 ? -9.462  -5.624  19.754  1.00 8.76   ? 117 GLU A OE2 1 
ATOM   1009 N  N   . LEU A 1 118 ? -12.343 -6.131  14.947  1.00 7.50   ? 118 LEU A N   1 
ATOM   1010 C  CA  . LEU A 1 118 ? -12.759 -4.902  14.288  1.00 7.18   ? 118 LEU A CA  1 
ATOM   1011 C  C   . LEU A 1 118 ? -12.498 -3.750  15.288  1.00 6.87   ? 118 LEU A C   1 
ATOM   1012 O  O   . LEU A 1 118 ? -12.905 -3.829  16.444  1.00 7.20   ? 118 LEU A O   1 
ATOM   1013 C  CB  . LEU A 1 118 ? -14.242 -5.014  13.972  1.00 8.27   ? 118 LEU A CB  1 
ATOM   1014 C  CG  . LEU A 1 118 ? -14.976 -3.723  13.593  1.00 9.03   ? 118 LEU A CG  1 
ATOM   1015 C  CD1 . LEU A 1 118 ? -14.418 -3.032  12.373  1.00 9.60   ? 118 LEU A CD1 1 
ATOM   1016 C  CD2 . LEU A 1 118 ? -16.468 -4.062  13.390  1.00 10.70  ? 118 LEU A CD2 1 
ATOM   1017 N  N   . HIS A 1 119 ? -11.886 -2.685  14.787  1.00 6.74   ? 119 HIS A N   1 
ATOM   1018 C  CA  . HIS A 1 119 ? -11.637 -1.460  15.555  1.00 6.72   ? 119 HIS A CA  1 
ATOM   1019 C  C   . HIS A 1 119 ? -12.381 -0.304  14.877  1.00 7.04   ? 119 HIS A C   1 
ATOM   1020 O  O   . HIS A 1 119 ? -12.002 0.077   13.755  1.00 7.57   ? 119 HIS A O   1 
ATOM   1021 C  CB  . HIS A 1 119 ? -10.163 -1.158  15.628  1.00 7.21   ? 119 HIS A CB  1 
ATOM   1022 C  CG  . HIS A 1 119 ? -9.414  -2.125  16.508  1.00 7.00   ? 119 HIS A CG  1 
ATOM   1023 N  ND1 . HIS A 1 119 ? -8.066  -2.314  16.496  1.00 6.66   ? 119 HIS A ND1 1 
ATOM   1024 C  CD2 . HIS A 1 119 ? -9.935  -2.958  17.466  1.00 7.08   ? 119 HIS A CD2 1 
ATOM   1025 C  CE1 . HIS A 1 119 ? -7.779  -3.222  17.400  1.00 7.77   ? 119 HIS A CE1 1 
ATOM   1026 N  NE2 . HIS A 1 119 ? -8.880  -3.629  18.004  1.00 7.09   ? 119 HIS A NE2 1 
ATOM   1027 N  N   . LEU A 1 120 ? -13.384 0.250   15.551  1.00 7.05   ? 120 LEU A N   1 
ATOM   1028 C  CA  . LEU A 1 120 ? -14.073 1.459   15.122  1.00 7.69   ? 120 LEU A CA  1 
ATOM   1029 C  C   . LEU A 1 120 ? -13.451 2.596   15.894  1.00 7.00   ? 120 LEU A C   1 
ATOM   1030 O  O   . LEU A 1 120 ? -13.534 2.642   17.127  1.00 6.92   ? 120 LEU A O   1 
ATOM   1031 C  CB  . LEU A 1 120 ? -15.549 1.338   15.360  1.00 8.42   ? 120 LEU A CB  1 
ATOM   1032 C  CG  . LEU A 1 120 ? -16.292 0.306   14.468  1.00 9.20   ? 120 LEU A CG  1 
ATOM   1033 C  CD1 . LEU A 1 120 ? -17.221 -0.536  15.270  1.00 15.25  ? 120 LEU A CD1 1 
ATOM   1034 C  CD2 . LEU A 1 120 ? -17.026 1.031   13.346  1.00 11.76  ? 120 LEU A CD2 1 
ATOM   1035 N  N   . VAL A 1 121 ? -12.787 3.520   15.184  1.00 7.86   ? 121 VAL A N   1 
ATOM   1036 C  CA  . VAL A 1 121 ? -11.917 4.517   15.808  1.00 7.49   ? 121 VAL A CA  1 
ATOM   1037 C  C   . VAL A 1 121 ? -12.610 5.874   15.833  1.00 7.46   ? 121 VAL A C   1 
ATOM   1038 O  O   . VAL A 1 121 ? -13.059 6.364   14.794  1.00 8.30   ? 121 VAL A O   1 
ATOM   1039 C  CB  . VAL A 1 121 ? -10.613 4.611   15.015  1.00 8.08   ? 121 VAL A CB  1 
ATOM   1040 C  CG1 . VAL A 1 121 ? -9.644  5.628   15.613  1.00 8.94   ? 121 VAL A CG1 1 
ATOM   1041 C  CG2 . VAL A 1 121 ? -9.950  3.219   14.879  1.00 8.84   ? 121 VAL A CG2 1 
ATOM   1042 N  N   . HIS A 1 122 ? -12.631 6.494   17.020  1.00 7.24   ? 122 HIS A N   1 
ATOM   1043 C  CA  . HIS A 1 122 ? -13.328 7.748   17.240  1.00 8.10   ? 122 HIS A CA  1 
ATOM   1044 C  C   . HIS A 1 122 ? -12.420 8.732   17.977  1.00 7.91   ? 122 HIS A C   1 
ATOM   1045 O  O   . HIS A 1 122 ? -11.698 8.305   18.875  1.00 8.71   ? 122 HIS A O   1 
ATOM   1046 C  CB  . HIS A 1 122 ? -14.582 7.571   18.062  1.00 8.43   ? 122 HIS A CB  1 
ATOM   1047 C  CG  . HIS A 1 122 ? -15.443 6.422   17.667  1.00 8.11   ? 122 HIS A CG  1 
ATOM   1048 N  ND1 . HIS A 1 122 ? -15.136 5.120   17.948  1.00 8.17   ? 122 HIS A ND1 1 
ATOM   1049 C  CD2 . HIS A 1 122 ? -16.688 6.367   17.050  1.00 8.88   ? 122 HIS A CD2 1 
ATOM   1050 C  CE1 . HIS A 1 122 ? -16.124 4.336   17.509  1.00 9.42   ? 122 HIS A CE1 1 
ATOM   1051 N  NE2 . HIS A 1 122 ? -17.105 5.051   16.947  1.00 9.41   ? 122 HIS A NE2 1 
ATOM   1052 N  N   . TRP A 1 123 ? -12.491 10.014  17.637  1.00 8.05   ? 123 TRP A N   1 
ATOM   1053 C  CA  . TRP A 1 123 ? -11.676 11.033  18.328  1.00 7.95   ? 123 TRP A CA  1 
ATOM   1054 C  C   . TRP A 1 123 ? -12.549 11.985  19.084  1.00 8.23   ? 123 TRP A C   1 
ATOM   1055 O  O   . TRP A 1 123 ? -13.683 12.333  18.690  1.00 9.07   ? 123 TRP A O   1 
ATOM   1056 C  CB  . TRP A 1 123 ? -10.720 11.786  17.352  1.00 9.31   ? 123 TRP A CB  1 
ATOM   1057 C  CG  . TRP A 1 123 ? -11.415 12.398  16.151  1.00 9.94   ? 123 TRP A CG  1 
ATOM   1058 C  CD1 . TRP A 1 123 ? -11.616 11.796  14.937  1.00 10.61  ? 123 TRP A CD1 1 
ATOM   1059 C  CD2 . TRP A 1 123 ? -11.924 13.730  16.033  1.00 10.27  ? 123 TRP A CD2 1 
ATOM   1060 N  NE1 . TRP A 1 123 ? -12.267 12.632  14.085  1.00 11.58  ? 123 TRP A NE1 1 
ATOM   1061 C  CE2 . TRP A 1 123 ? -12.436 13.862  14.712  1.00 11.66  ? 123 TRP A CE2 1 
ATOM   1062 C  CE3 . TRP A 1 123 ? -12.013 14.833  16.904  1.00 11.31  ? 123 TRP A CE3 1 
ATOM   1063 C  CZ2 . TRP A 1 123 ? -13.052 15.039  14.254  1.00 13.11  ? 123 TRP A CZ2 1 
ATOM   1064 C  CZ3 . TRP A 1 123 ? -12.573 16.013  16.432  1.00 13.08  ? 123 TRP A CZ3 1 
ATOM   1065 C  CH2 . TRP A 1 123 ? -13.041 16.087  15.124  1.00 14.09  ? 123 TRP A CH2 1 
ATOM   1066 N  N   . ASN A 1 124 ? -12.009 12.444  20.210  1.00 8.91   ? 124 ASN A N   1 
ATOM   1067 C  CA  . ASN A 1 124 ? -12.713 13.339  21.122  1.00 9.01   ? 124 ASN A CA  1 
ATOM   1068 C  C   . ASN A 1 124 ? -12.864 14.721  20.534  1.00 9.18   ? 124 ASN A C   1 
ATOM   1069 O  O   . ASN A 1 124 ? -11.855 15.388  20.234  1.00 9.55   ? 124 ASN A O   1 
ATOM   1070 C  CB  . ASN A 1 124 ? -11.904 13.392  22.414  1.00 9.91   ? 124 ASN A CB  1 
ATOM   1071 C  CG  . ASN A 1 124 ? -12.628 13.987  23.562  1.00 10.45  ? 124 ASN A CG  1 
ATOM   1072 O  OD1 . ASN A 1 124 ? -13.504 14.863  23.369  1.00 11.53  ? 124 ASN A OD1 1 
ATOM   1073 N  ND2 . ASN A 1 124 ? -12.355 13.516  24.774  1.00 11.68  ? 124 ASN A ND2 1 
ATOM   1074 N  N   . THR A 1 125 ? -14.135 15.132  20.351  1.00 10.30  ? 125 THR A N   1 
ATOM   1075 C  CA  . THR A 1 125 ? -14.384 16.387  19.672  1.00 11.89  ? 125 THR A CA  1 
ATOM   1076 C  C   . THR A 1 125 ? -13.787 17.603  20.415  1.00 13.00  ? 125 THR A C   1 
ATOM   1077 O  O   . THR A 1 125 ? -13.631 18.636  19.800  1.00 14.37  ? 125 THR A O   1 
ATOM   1078 C  CB  . THR A 1 125 ? -15.927 16.558  19.356  1.00 14.74  ? 125 THR A CB  1 
ATOM   1079 O  OG1 . THR A 1 125 ? -16.631 16.547  20.589  1.00 19.79  ? 125 THR A OG1 1 
ATOM   1080 C  CG2 . THR A 1 125 ? -16.378 15.474  18.360  1.00 17.47  ? 125 THR A CG2 1 
ATOM   1081 N  N   . LYS A 1 126 ? -13.478 17.468  21.724  1.00 12.44  ? 127 LYS A N   1 
ATOM   1082 C  CA  . LYS A 1 126 ? -12.930 18.585  22.413  1.00 14.42  ? 127 LYS A CA  1 
ATOM   1083 C  C   . LYS A 1 126 ? -11.507 18.938  21.908  1.00 12.20  ? 127 LYS A C   1 
ATOM   1084 O  O   . LYS A 1 126 ? -11.023 20.016  22.268  1.00 14.69  ? 127 LYS A O   1 
ATOM   1085 C  CB  . LYS A 1 126 ? -13.021 18.346  23.897  1.00 16.38  ? 127 LYS A CB  1 
ATOM   1086 C  CG  . LYS A 1 126 ? -11.906 17.535  24.409  1.00 16.30  ? 127 LYS A CG  1 
ATOM   1087 C  CD  . LYS A 1 126 ? -12.394 17.275  25.800  1.00 23.84  ? 127 LYS A CD  1 
ATOM   1088 C  CE  . LYS A 1 126 ? -11.461 16.506  26.584  1.00 26.62  ? 127 LYS A CE  1 
ATOM   1089 N  NZ  . LYS A 1 126 ? -10.678 17.475  27.361  1.00 46.21  ? 127 LYS A NZ  1 
ATOM   1090 N  N   . TYR A 1 127 ? -10.868 18.085  21.094  1.00 11.00  ? 128 TYR A N   1 
ATOM   1091 C  CA  . TYR A 1 127 ? -9.502  18.335  20.563  1.00 10.79  ? 128 TYR A CA  1 
ATOM   1092 C  C   . TYR A 1 127 ? -9.523  18.715  19.097  1.00 10.47  ? 128 TYR A C   1 
ATOM   1093 O  O   . TYR A 1 127 ? -8.461  18.963  18.530  1.00 11.72  ? 128 TYR A O   1 
ATOM   1094 C  CB  . TYR A 1 127 ? -8.574  17.171  20.855  1.00 11.84  ? 128 TYR A CB  1 
ATOM   1095 C  CG  . TYR A 1 127 ? -8.433  16.874  22.290  1.00 10.80  ? 128 TYR A CG  1 
ATOM   1096 C  CD1 . TYR A 1 127 ? -8.072  17.893  23.221  1.00 12.26  ? 128 TYR A CD1 1 
ATOM   1097 C  CD2 . TYR A 1 127 ? -8.771  15.621  22.807  1.00 10.66  ? 128 TYR A CD2 1 
ATOM   1098 C  CE1 . TYR A 1 127 ? -8.003  17.601  24.570  1.00 13.18  ? 128 TYR A CE1 1 
ATOM   1099 C  CE2 . TYR A 1 127 ? -8.697  15.342  24.163  1.00 10.93  ? 128 TYR A CE2 1 
ATOM   1100 C  CZ  . TYR A 1 127 ? -8.314  16.339  25.043  1.00 12.65  ? 128 TYR A CZ  1 
ATOM   1101 O  OH  . TYR A 1 127 ? -8.241  16.128  26.386  1.00 14.04  ? 128 TYR A OH  1 
ATOM   1102 N  N   . GLY A 1 128 ? -10.708 18.799  18.482  1.00 10.89  ? 129 GLY A N   1 
ATOM   1103 C  CA  . GLY A 1 128 ? -10.807 19.441  17.170  1.00 12.34  ? 129 GLY A CA  1 
ATOM   1104 C  C   . GLY A 1 128 ? -10.500 18.605  15.959  1.00 11.51  ? 129 GLY A C   1 
ATOM   1105 O  O   . GLY A 1 128 ? -11.117 18.750  14.908  1.00 13.86  ? 129 GLY A O   1 
ATOM   1106 N  N   . ASP A 1 129 ? -9.486  17.751  16.049  1.00 12.25  ? 130 ASP A N   1 
ATOM   1107 C  CA  . ASP A 1 129 ? -9.234  16.808  14.977  1.00 13.77  ? 130 ASP A CA  1 
ATOM   1108 C  C   . ASP A 1 129 ? -8.441  15.604  15.524  1.00 12.38  ? 130 ASP A C   1 
ATOM   1109 O  O   . ASP A 1 129 ? -7.965  15.607  16.670  1.00 13.35  ? 130 ASP A O   1 
ATOM   1110 C  CB  . ASP A 1 129 ? -8.642  17.430  13.786  1.00 16.03  ? 130 ASP A CB  1 
ATOM   1111 C  CG  . ASP A 1 129 ? -7.275  17.884  13.988  1.00 15.12  ? 130 ASP A CG  1 
ATOM   1112 O  OD1 . ASP A 1 129 ? -6.654  17.596  14.993  1.00 19.80  ? 130 ASP A OD1 1 
ATOM   1113 O  OD2 . ASP A 1 129 ? -6.740  18.594  13.089  1.00 19.37  ? 130 ASP A OD2 1 
ATOM   1114 N  N   . PHE A 1 130 ? -8.302  14.598  14.676  1.00 12.14  ? 131 PHE A N   1 
ATOM   1115 C  CA  . PHE A 1 130 ? -7.668  13.342  15.105  1.00 10.99  ? 131 PHE A CA  1 
ATOM   1116 C  C   . PHE A 1 130 ? -6.209  13.534  15.477  1.00 10.83  ? 131 PHE A C   1 
ATOM   1117 O  O   . PHE A 1 130 ? -5.725  12.995  16.468  1.00 10.77  ? 131 PHE A O   1 
ATOM   1118 C  CB  . PHE A 1 130 ? -7.776  12.343  13.937  1.00 11.81  ? 131 PHE A CB  1 
ATOM   1119 C  CG  . PHE A 1 130 ? -7.121  11.035  14.214  1.00 10.63  ? 131 PHE A CG  1 
ATOM   1120 C  CD1 . PHE A 1 130 ? -7.798  10.002  14.825  1.00 11.18  ? 131 PHE A CD1 1 
ATOM   1121 C  CD2 . PHE A 1 130 ? -5.800  10.797  13.905  1.00 12.80  ? 131 PHE A CD2 1 
ATOM   1122 C  CE1 . PHE A 1 130 ? -7.185  8.775   15.064  1.00 12.39  ? 131 PHE A CE1 1 
ATOM   1123 C  CE2 . PHE A 1 130 ? -5.206  9.575   14.104  1.00 14.53  ? 131 PHE A CE2 1 
ATOM   1124 C  CZ  . PHE A 1 130 ? -5.907  8.548   14.706  1.00 13.60  ? 131 PHE A CZ  1 
ATOM   1125 N  N   . GLY A 1 131 ? -5.469  14.344  14.694  1.00 13.00  ? 132 GLY A N   1 
ATOM   1126 C  CA  . GLY A 1 131 ? -4.034  14.477  14.942  1.00 14.13  ? 132 GLY A CA  1 
ATOM   1127 C  C   . GLY A 1 131 ? -3.734  15.154  16.291  1.00 13.32  ? 132 GLY A C   1 
ATOM   1128 O  O   . GLY A 1 131 ? -2.723  14.848  16.964  1.00 14.86  ? 132 GLY A O   1 
ATOM   1129 N  N   . LYS A 1 132 ? -4.583  16.093  16.693  1.00 12.41  ? 133 LYS A N   1 
ATOM   1130 C  CA  . LYS A 1 132 ? -4.409  16.655  18.037  1.00 12.15  ? 133 LYS A CA  1 
ATOM   1131 C  C   . LYS A 1 132 ? -4.885  15.679  19.113  1.00 11.44  ? 133 LYS A C   1 
ATOM   1132 O  O   . LYS A 1 132 ? -4.324  15.621  20.219  1.00 11.42  ? 133 LYS A O   1 
ATOM   1133 C  CB  . LYS A 1 132 ? -5.133  18.008  18.136  1.00 12.56  ? 133 LYS A CB  1 
ATOM   1134 C  CG  . LYS A 1 132 ? -4.479  19.129  17.319  1.00 16.94  ? 133 LYS A CG  1 
ATOM   1135 C  CD  . LYS A 1 132 ? -3.170  19.523  18.023  1.00 28.62  ? 133 LYS A CD  1 
ATOM   1136 C  CE  . LYS A 1 132 ? -2.621  20.843  17.609  1.00 31.01  ? 133 LYS A CE  1 
ATOM   1137 N  NZ  . LYS A 1 132 ? -1.478  21.220  18.500  1.00 45.00  ? 133 LYS A NZ  1 
ATOM   1138 N  N   . ALA A 1 133 ? -5.976  14.958  18.828  1.00 10.53  ? 134 ALA A N   1 
ATOM   1139 C  CA  . ALA A 1 133 ? -6.518  14.036  19.814  1.00 9.91   ? 134 ALA A CA  1 
ATOM   1140 C  C   . ALA A 1 133 ? -5.519  12.973  20.232  1.00 9.22   ? 134 ALA A C   1 
ATOM   1141 O  O   . ALA A 1 133 ? -5.505  12.597  21.394  1.00 10.01  ? 134 ALA A O   1 
ATOM   1142 C  CB  . ALA A 1 133 ? -7.789  13.409  19.284  1.00 9.91   ? 134 ALA A CB  1 
ATOM   1143 N  N   . VAL A 1 134 ? -4.738  12.450  19.308  1.00 9.89   ? 135 VAL A N   1 
ATOM   1144 C  CA  . VAL A 1 134 ? -3.798  11.330  19.694  1.00 10.19  ? 135 VAL A CA  1 
ATOM   1145 C  C   . VAL A 1 134 ? -2.708  11.789  20.612  1.00 9.89   ? 135 VAL A C   1 
ATOM   1146 O  O   . VAL A 1 134 ? -2.022  10.940  21.179  1.00 10.92  ? 135 VAL A O   1 
ATOM   1147 C  CB  . VAL A 1 134 ? -3.216  10.623  18.491  1.00 11.36  ? 135 VAL A CB  1 
ATOM   1148 C  CG1 . VAL A 1 134 ? -4.286  9.945   17.673  1.00 13.45  ? 135 VAL A CG1 1 
ATOM   1149 C  CG2 . VAL A 1 134 ? -2.350  11.523  17.626  1.00 12.71  ? 135 VAL A CG2 1 
ATOM   1150 N  N   A GLN A 1 135 ? -2.572  13.115  20.792  0.50 11.21  ? 136 GLN A N   1 
ATOM   1151 N  N   B GLN A 1 135 ? -2.573  13.109  20.840  0.50 10.96  ? 136 GLN A N   1 
ATOM   1152 C  CA  A GLN A 1 135 ? -1.607  13.657  21.741  0.50 12.08  ? 136 GLN A CA  1 
ATOM   1153 C  CA  B GLN A 1 135 ? -1.591  13.621  21.804  0.50 11.67  ? 136 GLN A CA  1 
ATOM   1154 C  C   A GLN A 1 135 ? -2.192  13.866  23.141  0.50 10.26  ? 136 GLN A C   1 
ATOM   1155 C  C   B GLN A 1 135 ? -2.100  13.687  23.234  0.50 11.46  ? 136 GLN A C   1 
ATOM   1156 O  O   A GLN A 1 135 ? -1.577  14.553  23.983  0.50 11.42  ? 136 GLN A O   1 
ATOM   1157 O  O   B GLN A 1 135 ? -1.352  14.087  24.178  0.50 13.35  ? 136 GLN A O   1 
ATOM   1158 C  CB  A GLN A 1 135 ? -1.005  14.988  21.178  0.50 14.70  ? 136 GLN A CB  1 
ATOM   1159 C  CB  B GLN A 1 135 ? -1.096  15.015  21.321  0.50 13.45  ? 136 GLN A CB  1 
ATOM   1160 C  CG  A GLN A 1 135 ? -0.345  14.803  19.810  0.50 17.50  ? 136 GLN A CG  1 
ATOM   1161 C  CG  B GLN A 1 135 ? -0.501  14.889  19.935  0.50 14.86  ? 136 GLN A CG  1 
ATOM   1162 C  CD  A GLN A 1 135 ? 0.891   13.903  19.839  0.50 25.05  ? 136 GLN A CD  1 
ATOM   1163 C  CD  B GLN A 1 135 ? -0.020  16.185  19.379  0.50 15.95  ? 136 GLN A CD  1 
ATOM   1164 O  OE1 A GLN A 1 135 ? 1.633   13.847  20.829  0.50 26.23  ? 136 GLN A OE1 1 
ATOM   1165 O  OE1 B GLN A 1 135 ? -0.490  16.618  18.337  0.50 17.49  ? 136 GLN A OE1 1 
ATOM   1166 N  NE2 A GLN A 1 135 ? 1.126   13.186  18.726  0.50 27.53  ? 136 GLN A NE2 1 
ATOM   1167 N  NE2 B GLN A 1 135 ? 0.878   16.828  20.067  0.50 19.43  ? 136 GLN A NE2 1 
ATOM   1168 N  N   . GLN A 1 136 ? -3.351  13.293  23.418  1.00 10.46  ? 137 GLN A N   1 
ATOM   1169 C  CA  . GLN A 1 136 ? -4.046  13.484  24.675  1.00 9.90   ? 137 GLN A CA  1 
ATOM   1170 C  C   . GLN A 1 136 ? -4.391  12.158  25.299  1.00 9.52   ? 137 GLN A C   1 
ATOM   1171 O  O   . GLN A 1 136 ? -4.748  11.222  24.593  1.00 10.24  ? 137 GLN A O   1 
ATOM   1172 C  CB  . GLN A 1 136 ? -5.325  14.295  24.494  1.00 11.35  ? 137 GLN A CB  1 
ATOM   1173 C  CG  . GLN A 1 136 ? -5.118  15.576  23.721  1.00 15.30  ? 137 GLN A CG  1 
ATOM   1174 C  CD  . GLN A 1 136 ? -4.220  16.543  24.420  1.00 19.96  ? 137 GLN A CD  1 
ATOM   1175 O  OE1 . GLN A 1 136 ? -4.032  16.501  25.597  1.00 20.82  ? 137 GLN A OE1 1 
ATOM   1176 N  NE2 . GLN A 1 136 ? -3.590  17.372  23.640  1.00 33.95  ? 137 GLN A NE2 1 
ATOM   1177 N  N   A PRO A 1 137 ? -4.477  12.066  26.647  0.50 9.84   ? 138 PRO A N   1 
ATOM   1178 N  N   B PRO A 1 137 ? -4.370  12.078  26.665  0.50 10.53  ? 138 PRO A N   1 
ATOM   1179 C  CA  A PRO A 1 137 ? -4.712  10.765  27.297  0.50 10.47  ? 138 PRO A CA  1 
ATOM   1180 C  CA  B PRO A 1 137 ? -4.624  10.773  27.292  0.50 10.89  ? 138 PRO A CA  1 
ATOM   1181 C  C   A PRO A 1 137 ? -6.132  10.279  27.113  0.50 10.64  ? 138 PRO A C   1 
ATOM   1182 C  C   B PRO A 1 137 ? -6.060  10.289  27.105  0.50 10.82  ? 138 PRO A C   1 
ATOM   1183 O  O   A PRO A 1 137 ? -6.379  9.073   27.248  0.50 14.35  ? 138 PRO A O   1 
ATOM   1184 O  O   B PRO A 1 137 ? -6.277  9.075   27.247  0.50 14.59  ? 138 PRO A O   1 
ATOM   1185 C  CB  A PRO A 1 137 ? -4.432  11.022  28.755  0.50 14.50  ? 138 PRO A CB  1 
ATOM   1186 C  CB  B PRO A 1 137 ? -4.349  11.012  28.762  0.50 14.94  ? 138 PRO A CB  1 
ATOM   1187 C  CG  A PRO A 1 137 ? -4.445  12.483  28.890  0.50 17.14  ? 138 PRO A CG  1 
ATOM   1188 C  CG  B PRO A 1 137 ? -3.366  12.089  28.811  0.50 21.50  ? 138 PRO A CG  1 
ATOM   1189 C  CD  A PRO A 1 137 ? -4.052  13.090  27.601  0.50 11.96  ? 138 PRO A CD  1 
ATOM   1190 C  CD  B PRO A 1 137 ? -3.719  13.021  27.664  0.50 14.91  ? 138 PRO A CD  1 
ATOM   1191 N  N   . ASP A 1 138 ? -7.043  11.195  26.819  1.00 10.14  ? 139 ASP A N   1 
ATOM   1192 C  CA  . ASP A 1 138 ? -8.446  10.901  26.529  1.00 10.27  ? 139 ASP A CA  1 
ATOM   1193 C  C   . ASP A 1 138 ? -8.778  11.283  25.101  1.00 9.37   ? 139 ASP A C   1 
ATOM   1194 O  O   . ASP A 1 138 ? -9.912  11.699  24.836  1.00 10.16  ? 139 ASP A O   1 
ATOM   1195 C  CB  . ASP A 1 138 ? -9.385  11.534  27.528  1.00 12.40  ? 139 ASP A CB  1 
ATOM   1196 C  CG  . ASP A 1 138 ? -9.291  13.016  27.552  1.00 13.10  ? 139 ASP A CG  1 
ATOM   1197 O  OD1 . ASP A 1 138 ? -8.362  13.579  26.960  1.00 13.19  ? 139 ASP A OD1 1 
ATOM   1198 O  OD2 . ASP A 1 138 ? -10.152 13.595  28.230  1.00 16.45  ? 139 ASP A OD2 1 
ATOM   1199 N  N   . GLY A 1 139 ? -7.825  11.142  24.194  1.00 8.54   ? 140 GLY A N   1 
ATOM   1200 C  CA  . GLY A 1 139 ? -8.075  11.605  22.834  1.00 8.74   ? 140 GLY A CA  1 
ATOM   1201 C  C   . GLY A 1 139 ? -8.935  10.716  21.971  1.00 7.60   ? 140 GLY A C   1 
ATOM   1202 O  O   . GLY A 1 139 ? -9.660  11.232  21.102  1.00 8.43   ? 140 GLY A O   1 
ATOM   1203 N  N   . LEU A 1 140 ? -8.826  9.395   22.121  1.00 7.45   ? 141 LEU A N   1 
ATOM   1204 C  CA  . LEU A 1 140 ? -9.522  8.449   21.256  1.00 7.40   ? 141 LEU A CA  1 
ATOM   1205 C  C   . LEU A 1 140 ? -10.362 7.523   22.085  1.00 7.17   ? 141 LEU A C   1 
ATOM   1206 O  O   . LEU A 1 140 ? -10.091 7.222   23.257  1.00 7.56   ? 141 LEU A O   1 
ATOM   1207 C  CB  . LEU A 1 140 ? -8.583  7.573   20.447  1.00 7.97   ? 141 LEU A CB  1 
ATOM   1208 C  CG  . LEU A 1 140 ? -7.676  8.265   19.436  1.00 9.72   ? 141 LEU A CG  1 
ATOM   1209 C  CD1 . LEU A 1 140 ? -6.968  7.174   18.602  1.00 9.87   ? 141 LEU A CD1 1 
ATOM   1210 C  CD2 . LEU A 1 140 ? -8.304  9.308   18.565  1.00 11.07  ? 141 LEU A CD2 1 
ATOM   1211 N  N   . ALA A 1 141 ? -11.435 7.029   21.452  1.00 7.44   ? 142 ALA A N   1 
ATOM   1212 C  CA  . ALA A 1 141 ? -12.244 5.885   21.974  1.00 7.75   ? 142 ALA A CA  1 
ATOM   1213 C  C   . ALA A 1 141 ? -12.277 4.889   20.831  1.00 7.04   ? 142 ALA A C   1 
ATOM   1214 O  O   . ALA A 1 141 ? -12.728 5.242   19.715  1.00 8.34   ? 142 ALA A O   1 
ATOM   1215 C  CB  . ALA A 1 141 ? -13.619 6.332   22.383  1.00 9.16   ? 142 ALA A CB  1 
ATOM   1216 N  N   . VAL A 1 142 ? -11.801 3.668   21.080  1.00 6.93   ? 143 VAL A N   1 
ATOM   1217 C  CA  . VAL A 1 142 ? -11.818 2.628   20.062  1.00 7.00   ? 143 VAL A CA  1 
ATOM   1218 C  C   . VAL A 1 142 ? -12.770 1.569   20.561  1.00 6.69   ? 143 VAL A C   1 
ATOM   1219 O  O   . VAL A 1 142 ? -12.636 1.045   21.673  1.00 7.36   ? 143 VAL A O   1 
ATOM   1220 C  CB  . VAL A 1 142 ? -10.444 2.083   19.695  1.00 7.41   ? 143 VAL A CB  1 
ATOM   1221 C  CG1 . VAL A 1 142 ? -10.602 1.064   18.592  1.00 8.64   ? 143 VAL A CG1 1 
ATOM   1222 C  CG2 . VAL A 1 142 ? -9.516  3.217   19.257  1.00 8.89   ? 143 VAL A CG2 1 
ATOM   1223 N  N   . LEU A 1 143 ? -13.784 1.287   19.723  1.00 7.07   ? 144 LEU A N   1 
ATOM   1224 C  CA  . LEU A 1 143 ? -14.749 0.226   19.986  1.00 7.52   ? 144 LEU A CA  1 
ATOM   1225 C  C   . LEU A 1 143 ? -14.215 -1.017  19.288  1.00 7.42   ? 144 LEU A C   1 
ATOM   1226 O  O   . LEU A 1 143 ? -14.073 -1.045  18.062  1.00 8.58   ? 144 LEU A O   1 
ATOM   1227 C  CB  . LEU A 1 143 ? -16.107 0.687   19.418  1.00 9.64   ? 144 LEU A CB  1 
ATOM   1228 C  CG  . LEU A 1 143 ? -17.244 -0.262  19.564  1.00 11.20  ? 144 LEU A CG  1 
ATOM   1229 C  CD1 . LEU A 1 143 ? -17.478 -0.610  21.009  1.00 13.54  ? 144 LEU A CD1 1 
ATOM   1230 C  CD2 . LEU A 1 143 ? -18.526 0.290   18.938  1.00 12.59  ? 144 LEU A CD2 1 
ATOM   1231 N  N   . GLY A 1 144 ? -13.908 -2.030  20.085  1.00 7.17   ? 145 GLY A N   1 
ATOM   1232 C  CA  . GLY A 1 144 ? -13.354 -3.291  19.583  1.00 7.60   ? 145 GLY A CA  1 
ATOM   1233 C  C   . GLY A 1 144 ? -14.423 -4.382  19.593  1.00 6.98   ? 145 GLY A C   1 
ATOM   1234 O  O   . GLY A 1 144 ? -15.145 -4.531  20.599  1.00 8.27   ? 145 GLY A O   1 
ATOM   1235 N  N   . ILE A 1 145 ? -14.494 -5.107  18.493  1.00 6.87   ? 146 ILE A N   1 
ATOM   1236 C  CA  . ILE A 1 145 ? -15.499 -6.155  18.303  1.00 7.27   ? 146 ILE A CA  1 
ATOM   1237 C  C   . ILE A 1 145 ? -14.781 -7.389  17.798  1.00 7.11   ? 146 ILE A C   1 
ATOM   1238 O  O   . ILE A 1 145 ? -14.101 -7.335  16.777  1.00 8.10   ? 146 ILE A O   1 
ATOM   1239 C  CB  . ILE A 1 145 ? -16.633 -5.678  17.330  1.00 8.87   ? 146 ILE A CB  1 
ATOM   1240 C  CG1 . ILE A 1 145 ? -17.250 -4.385  17.872  1.00 10.37  ? 146 ILE A CG1 1 
ATOM   1241 C  CG2 . ILE A 1 145 ? -17.636 -6.811  17.133  1.00 10.91  ? 146 ILE A CG2 1 
ATOM   1242 C  CD1 . ILE A 1 145 ? -18.302 -3.789  16.970  1.00 10.43  ? 146 ILE A CD1 1 
ATOM   1243 N  N   . PHE A 1 146 ? -14.980 -8.492  18.482  1.00 7.15   ? 147 PHE A N   1 
ATOM   1244 C  CA  . PHE A 1 146 ? -14.368 -9.764  18.055  1.00 7.65   ? 147 PHE A CA  1 
ATOM   1245 C  C   . PHE A 1 146 ? -15.141 -10.381 16.901  1.00 7.55   ? 147 PHE A C   1 
ATOM   1246 O  O   . PHE A 1 146 ? -16.369 -10.254 16.829  1.00 8.70   ? 147 PHE A O   1 
ATOM   1247 C  CB  . PHE A 1 146 ? -14.371 -10.741 19.234  1.00 7.84   ? 147 PHE A CB  1 
ATOM   1248 C  CG  . PHE A 1 146 ? -13.509 -10.260 20.377  1.00 7.24   ? 147 PHE A CG  1 
ATOM   1249 C  CD1 . PHE A 1 146 ? -12.134 -10.092 20.194  1.00 7.78   ? 147 PHE A CD1 1 
ATOM   1250 C  CD2 . PHE A 1 146 ? -14.028 -10.029 21.617  1.00 8.03   ? 147 PHE A CD2 1 
ATOM   1251 C  CE1 . PHE A 1 146 ? -11.314 -9.701  21.270  1.00 8.79   ? 147 PHE A CE1 1 
ATOM   1252 C  CE2 . PHE A 1 146 ? -13.241 -9.646  22.690  1.00 8.40   ? 147 PHE A CE2 1 
ATOM   1253 C  CZ  . PHE A 1 146 ? -11.869 -9.482  22.517  1.00 8.17   ? 147 PHE A CZ  1 
ATOM   1254 N  N   . LEU A 1 147 ? -14.405 -11.088 16.038  1.00 8.09   ? 148 LEU A N   1 
ATOM   1255 C  CA  . LEU A 1 147 ? -14.999 -11.878 14.951  1.00 8.51   ? 148 LEU A CA  1 
ATOM   1256 C  C   . LEU A 1 147 ? -14.681 -13.349 15.199  1.00 8.18   ? 148 LEU A C   1 
ATOM   1257 O  O   . LEU A 1 147 ? -13.504 -13.699 15.379  1.00 8.89   ? 148 LEU A O   1 
ATOM   1258 C  CB  . LEU A 1 147 ? -14.420 -11.500 13.594  1.00 9.40   ? 148 LEU A CB  1 
ATOM   1259 C  CG  . LEU A 1 147 ? -14.972 -10.229 12.912  1.00 9.84   ? 148 LEU A CG  1 
ATOM   1260 C  CD1 . LEU A 1 147 ? -14.743 -8.987  13.768  1.00 11.17  ? 148 LEU A CD1 1 
ATOM   1261 C  CD2 . LEU A 1 147 ? -14.363 -10.049 11.528  1.00 11.11  ? 148 LEU A CD2 1 
ATOM   1262 N  N   . LYS A 1 148 ? -15.700 -14.177 15.129  1.00 9.58   ? 149 LYS A N   1 
ATOM   1263 C  CA  . LYS A 1 148 ? -15.561 -15.648 15.086  1.00 10.00  ? 149 LYS A CA  1 
ATOM   1264 C  C   . LYS A 1 148 ? -16.046 -16.135 13.730  1.00 10.86  ? 149 LYS A C   1 
ATOM   1265 O  O   . LYS A 1 148 ? -16.851 -15.486 13.065  1.00 11.66  ? 149 LYS A O   1 
ATOM   1266 C  CB  . LYS A 1 148 ? -16.271 -16.303 16.249  1.00 11.65  ? 149 LYS A CB  1 
ATOM   1267 C  CG  . LYS A 1 148 ? -17.767 -16.157 16.221  1.00 13.28  ? 149 LYS A CG  1 
ATOM   1268 C  CD  . LYS A 1 148 ? -18.403 -16.882 17.420  1.00 20.79  ? 149 LYS A CD  1 
ATOM   1269 C  CE  . LYS A 1 148 ? -19.887 -16.903 17.276  1.00 28.69  ? 149 LYS A CE  1 
ATOM   1270 N  NZ  . LYS A 1 148 ? -20.437 -17.787 18.350  1.00 39.39  ? 149 LYS A NZ  1 
ATOM   1271 N  N   . VAL A 1 149 ? -15.560 -17.300 13.327  1.00 11.26  ? 150 VAL A N   1 
ATOM   1272 C  CA  . VAL A 1 149 ? -15.934 -17.885 12.038  1.00 11.20  ? 150 VAL A CA  1 
ATOM   1273 C  C   . VAL A 1 149 ? -17.137 -18.793 12.236  1.00 11.80  ? 150 VAL A C   1 
ATOM   1274 O  O   . VAL A 1 149 ? -17.092 -19.743 13.020  1.00 13.03  ? 150 VAL A O   1 
ATOM   1275 C  CB  . VAL A 1 149 ? -14.734 -18.625 11.427  1.00 11.86  ? 150 VAL A CB  1 
ATOM   1276 C  CG1 . VAL A 1 149 ? -15.115 -19.406 10.199  1.00 13.45  ? 150 VAL A CG1 1 
ATOM   1277 C  CG2 . VAL A 1 149 ? -13.640 -17.638 11.129  1.00 13.88  ? 150 VAL A CG2 1 
ATOM   1278 N  N   . GLY A 1 150 ? -18.157 -18.533 11.484  1.00 12.06  ? 151 GLY A N   1 
ATOM   1279 C  CA  . GLY A 1 150 ? -19.404 -19.338 11.511  1.00 13.30  ? 151 GLY A CA  1 
ATOM   1280 C  C   . GLY A 1 150 ? -20.305 -18.876 10.420  1.00 13.57  ? 151 GLY A C   1 
ATOM   1281 O  O   . GLY A 1 150 ? -19.942 -18.925 9.247   1.00 14.22  ? 151 GLY A O   1 
ATOM   1282 N  N   A SER A 1 151 ? -21.509 -18.409 10.727  0.50 14.00  ? 152 SER A N   1 
ATOM   1283 N  N   B SER A 1 151 ? -21.485 -18.373 10.782  0.50 15.48  ? 152 SER A N   1 
ATOM   1284 C  CA  A SER A 1 151 ? -22.395 -17.879 9.704   0.50 15.97  ? 152 SER A CA  1 
ATOM   1285 C  CA  B SER A 1 151 ? -22.318 -17.728 9.789   0.50 14.82  ? 152 SER A CA  1 
ATOM   1286 C  C   A SER A 1 151 ? -21.890 -16.525 9.218   0.50 12.66  ? 152 SER A C   1 
ATOM   1287 C  C   B SER A 1 151 ? -21.662 -16.533 9.133   0.50 14.62  ? 152 SER A C   1 
ATOM   1288 O  O   A SER A 1 151 ? -21.266 -15.775 10.000  0.50 11.65  ? 152 SER A O   1 
ATOM   1289 O  O   B SER A 1 151 ? -20.774 -15.875 9.690   0.50 11.46  ? 152 SER A O   1 
ATOM   1290 C  CB  A SER A 1 151 ? -23.739 -17.688 10.354  0.50 18.15  ? 152 SER A CB  1 
ATOM   1291 C  CB  B SER A 1 151 ? -23.721 -17.407 10.335  0.50 20.89  ? 152 SER A CB  1 
ATOM   1292 O  OG  A SER A 1 151 ? -23.650 -16.580 11.238  0.50 21.67  ? 152 SER A OG  1 
ATOM   1293 O  OG  B SER A 1 151 ? -24.301 -18.549 10.945  0.50 22.02  ? 152 SER A OG  1 
ATOM   1294 N  N   . ALA A 1 152 ? -22.074 -16.231 7.909   1.00 15.00  ? 153 ALA A N   1 
ATOM   1295 C  CA  . ALA A 1 152 ? -21.696 -14.998 7.320   1.00 13.99  ? 153 ALA A CA  1 
ATOM   1296 C  C   . ALA A 1 152 ? -22.368 -13.797 8.015   1.00 12.77  ? 153 ALA A C   1 
ATOM   1297 O  O   . ALA A 1 152 ? -23.482 -13.837 8.521   1.00 15.40  ? 153 ALA A O   1 
ATOM   1298 C  CB  . ALA A 1 152 ? -22.059 -14.979 5.827   1.00 17.02  ? 153 ALA A CB  1 
ATOM   1299 N  N   . LYS A 1 153 ? -21.619 -12.652 7.923   1.00 14.14  ? 154 LYS A N   1 
ATOM   1300 C  CA  . LYS A 1 153 ? -22.116 -11.357 8.401   1.00 14.51  ? 154 LYS A CA  1 
ATOM   1301 C  C   . LYS A 1 153 ? -22.591 -10.589 7.086   1.00 13.56  ? 154 LYS A C   1 
ATOM   1302 O  O   . LYS A 1 153 ? -21.727 -10.145 6.335   1.00 13.27  ? 154 LYS A O   1 
ATOM   1303 C  CB  . LYS A 1 153 ? -21.056 -10.595 9.144   1.00 14.96  ? 154 LYS A CB  1 
ATOM   1304 C  CG  . LYS A 1 153 ? -21.632 -9.358  9.783   1.00 18.22  ? 154 LYS A CG  1 
ATOM   1305 C  CD  . LYS A 1 153 ? -22.436 -9.716  11.013  1.00 20.85  ? 154 LYS A CD  1 
ATOM   1306 C  CE  . LYS A 1 153 ? -22.469 -8.539  11.959  1.00 21.22  ? 154 LYS A CE  1 
ATOM   1307 N  NZ  . LYS A 1 153 ? -23.447 -8.841  13.033  1.00 20.88  ? 154 LYS A NZ  1 
ATOM   1308 N  N   . PRO A 1 154 ? -23.899 -10.491 6.862   1.00 14.93  ? 155 PRO A N   1 
ATOM   1309 C  CA  . PRO A 1 154 ? -24.269 -9.919  5.547   1.00 15.45  ? 155 PRO A CA  1 
ATOM   1310 C  C   . PRO A 1 154 ? -23.799 -8.486  5.429   1.00 15.52  ? 155 PRO A C   1 
ATOM   1311 O  O   . PRO A 1 154 ? -23.396 -8.103  4.320   1.00 16.57  ? 155 PRO A O   1 
ATOM   1312 C  CB  . PRO A 1 154 ? -25.819 -9.996  5.594   1.00 17.23  ? 155 PRO A CB  1 
ATOM   1313 C  CG  . PRO A 1 154 ? -26.066 -11.159 6.533   1.00 20.33  ? 155 PRO A CG  1 
ATOM   1314 C  CD  . PRO A 1 154 ? -25.082 -11.069 7.620   1.00 17.09  ? 155 PRO A CD  1 
ATOM   1315 N  N   . GLY A 1 155 ? -23.761 -7.720  6.543   1.00 15.20  ? 156 GLY A N   1 
ATOM   1316 C  CA  . GLY A 1 155 ? -23.384 -6.331  6.474   1.00 15.82  ? 156 GLY A CA  1 
ATOM   1317 C  C   . GLY A 1 155 ? -21.912 -6.142  6.275   1.00 15.16  ? 156 GLY A C   1 
ATOM   1318 O  O   . GLY A 1 155 ? -21.488 -5.001  6.095   1.00 18.54  ? 156 GLY A O   1 
ATOM   1319 N  N   . LEU A 1 156 ? -21.149 -7.206  6.295   1.00 14.30  ? 157 LEU A N   1 
ATOM   1320 C  CA  . LEU A 1 156 ? -19.751 -7.170  5.966   1.00 13.32  ? 157 LEU A CA  1 
ATOM   1321 C  C   . LEU A 1 156 ? -19.440 -7.387  4.497   1.00 13.68  ? 157 LEU A C   1 
ATOM   1322 O  O   . LEU A 1 156 ? -18.352 -7.079  4.007   1.00 13.33  ? 157 LEU A O   1 
ATOM   1323 C  CB  . LEU A 1 156 ? -18.933 -8.197  6.819   1.00 13.12  ? 157 LEU A CB  1 
ATOM   1324 C  CG  . LEU A 1 156 ? -17.406 -8.296  6.645   1.00 13.16  ? 157 LEU A CG  1 
ATOM   1325 C  CD1 . LEU A 1 156 ? -16.656 -7.040  7.000   1.00 15.62  ? 157 LEU A CD1 1 
ATOM   1326 C  CD2 . LEU A 1 156 ? -16.880 -9.515  7.480   1.00 14.95  ? 157 LEU A CD2 1 
ATOM   1327 N  N   . GLN A 1 157 ? -20.324 -7.987  3.723   1.00 13.95  ? 158 GLN A N   1 
ATOM   1328 C  CA  . GLN A 1 157 ? -19.975 -8.445  2.379   1.00 15.76  ? 158 GLN A CA  1 
ATOM   1329 C  C   . GLN A 1 157 ? -19.618 -7.304  1.475   1.00 14.75  ? 158 GLN A C   1 
ATOM   1330 O  O   . GLN A 1 157 ? -18.788 -7.508  0.626   1.00 14.71  ? 158 GLN A O   1 
ATOM   1331 C  CB  . GLN A 1 157 ? -21.116 -9.293  1.820   1.00 17.69  ? 158 GLN A CB  1 
ATOM   1332 C  CG  . GLN A 1 157 ? -20.696 -10.009 0.529   1.00 17.47  ? 158 GLN A CG  1 
ATOM   1333 C  CD  . GLN A 1 157 ? -19.531 -11.016 0.748   1.00 16.49  ? 158 GLN A CD  1 
ATOM   1334 O  OE1 . GLN A 1 157 ? -19.375 -11.569 1.849   1.00 17.29  ? 158 GLN A OE1 1 
ATOM   1335 N  NE2 . GLN A 1 157 ? -18.713 -11.250 -0.318  1.00 18.95  ? 158 GLN A NE2 1 
ATOM   1336 N  N   . LYS A 1 158 ? -20.218 -6.093  1.582   1.00 15.83  ? 159 LYS A N   1 
ATOM   1337 C  CA  . LYS A 1 158 ? -19.795 -5.019  0.677   1.00 15.28  ? 159 LYS A CA  1 
ATOM   1338 C  C   . LYS A 1 158 ? -18.292 -4.681  0.851   1.00 14.47  ? 159 LYS A C   1 
ATOM   1339 O  O   . LYS A 1 158 ? -17.656 -4.316  -0.112  1.00 16.71  ? 159 LYS A O   1 
ATOM   1340 C  CB  . LYS A 1 158 ? -20.667 -3.797  0.918   1.00 17.10  ? 159 LYS A CB  1 
ATOM   1341 C  CG  . LYS A 1 158 ? -22.060 -3.889  0.289   1.00 24.11  ? 159 LYS A CG  1 
ATOM   1342 C  CD  . LYS A 1 158 ? -22.686 -2.471  0.073   1.00 36.98  ? 159 LYS A CD  1 
ATOM   1343 C  CE  . LYS A 1 158 ? -22.629 -1.332  1.174   1.00 49.25  ? 159 LYS A CE  1 
ATOM   1344 N  NZ  . LYS A 1 158 ? -23.640 -0.132  1.065   1.00 38.80  ? 159 LYS A NZ  1 
ATOM   1345 N  N   . VAL A 1 159 ? -17.784 -4.830  2.078   1.00 14.73  ? 160 VAL A N   1 
ATOM   1346 C  CA  . VAL A 1 159 ? -16.367 -4.602  2.328   1.00 14.44  ? 160 VAL A CA  1 
ATOM   1347 C  C   . VAL A 1 159 ? -15.581 -5.705  1.688   1.00 14.23  ? 160 VAL A C   1 
ATOM   1348 O  O   . VAL A 1 159 ? -14.665 -5.455  0.956   1.00 15.23  ? 160 VAL A O   1 
ATOM   1349 C  CB  . VAL A 1 159 ? -16.093 -4.553  3.851   1.00 14.32  ? 160 VAL A CB  1 
ATOM   1350 C  CG1 . VAL A 1 159 ? -14.607 -4.576  4.159   1.00 16.92  ? 160 VAL A CG1 1 
ATOM   1351 C  CG2 . VAL A 1 159 ? -16.704 -3.363  4.444   1.00 17.32  ? 160 VAL A CG2 1 
ATOM   1352 N  N   . VAL A 1 160 ? -15.963 -6.965  1.930   1.00 14.40  ? 161 VAL A N   1 
ATOM   1353 C  CA  . VAL A 1 160 ? -15.253 -8.086  1.360   1.00 14.68  ? 161 VAL A CA  1 
ATOM   1354 C  C   . VAL A 1 160 ? -15.182 -7.997  -0.127  1.00 16.01  ? 161 VAL A C   1 
ATOM   1355 O  O   . VAL A 1 160 ? -14.159 -8.275  -0.696  1.00 16.28  ? 161 VAL A O   1 
ATOM   1356 C  CB  . VAL A 1 160 ? -15.993 -9.471  1.787   1.00 16.68  ? 161 VAL A CB  1 
ATOM   1357 C  CG1 . VAL A 1 160 ? -15.460 -10.668 1.016   1.00 20.40  ? 161 VAL A CG1 1 
ATOM   1358 C  CG2 . VAL A 1 160 ? -15.833 -9.628  3.305   1.00 16.47  ? 161 VAL A CG2 1 
ATOM   1359 N  N   . ASP A 1 161 ? -16.260 -7.591  -0.774  1.00 16.74  ? 162 ASP A N   1 
ATOM   1360 C  CA  . ASP A 1 161 ? -16.241 -7.621  -2.248  1.00 18.10  ? 162 ASP A CA  1 
ATOM   1361 C  C   . ASP A 1 161 ? -15.370 -6.564  -2.870  1.00 21.11  ? 162 ASP A C   1 
ATOM   1362 O  O   . ASP A 1 161 ? -14.969 -6.751  -3.986  1.00 25.01  ? 162 ASP A O   1 
ATOM   1363 C  CB  . ASP A 1 161 ? -17.645 -7.507  -2.657  1.00 22.98  ? 162 ASP A CB  1 
ATOM   1364 C  CG  . ASP A 1 161 ? -18.331 -8.867  -2.654  1.00 23.12  ? 162 ASP A CG  1 
ATOM   1365 O  OD1 . ASP A 1 161 ? -17.607 -9.917  -2.719  1.00 29.88  ? 162 ASP A OD1 1 
ATOM   1366 O  OD2 . ASP A 1 161 ? -19.551 -8.847  -2.480  1.00 33.15  ? 162 ASP A OD2 1 
ATOM   1367 N  N   . VAL A 1 162 ? -15.004 -5.487  -2.165  1.00 18.95  ? 163 VAL A N   1 
ATOM   1368 C  CA  . VAL A 1 162 ? -14.223 -4.418  -2.751  1.00 18.74  ? 163 VAL A CA  1 
ATOM   1369 C  C   . VAL A 1 162 ? -12.723 -4.733  -2.507  1.00 16.91  ? 163 VAL A C   1 
ATOM   1370 O  O   . VAL A 1 162 ? -11.822 -4.098  -3.067  1.00 17.58  ? 163 VAL A O   1 
ATOM   1371 C  CB  . VAL A 1 162 ? -14.670 -3.041  -2.148  1.00 19.89  ? 163 VAL A CB  1 
ATOM   1372 C  CG1 . VAL A 1 162 ? -14.092 -2.827  -0.805  1.00 20.95  ? 163 VAL A CG1 1 
ATOM   1373 C  CG2 . VAL A 1 162 ? -14.322 -1.826  -3.015  1.00 22.84  ? 163 VAL A CG2 1 
ATOM   1374 N  N   . LEU A 1 163 ? -12.435 -5.746  -1.676  1.00 16.99  ? 164 LEU A N   1 
ATOM   1375 C  CA  . LEU A 1 163 ? -11.023 -5.977  -1.379  1.00 14.91  ? 164 LEU A CA  1 
ATOM   1376 C  C   . LEU A 1 163 ? -10.149 -6.340  -2.528  1.00 16.85  ? 164 LEU A C   1 
ATOM   1377 O  O   . LEU A 1 163 ? -8.949  -6.008  -2.567  1.00 16.78  ? 164 LEU A O   1 
ATOM   1378 C  CB  . LEU A 1 163 ? -10.774 -7.011  -0.261  1.00 14.69  ? 164 LEU A CB  1 
ATOM   1379 C  CG  . LEU A 1 163 ? -11.435 -6.682  1.085   1.00 13.79  ? 164 LEU A CG  1 
ATOM   1380 C  CD1 . LEU A 1 163 ? -11.183 -7.822  2.090   1.00 15.96  ? 164 LEU A CD1 1 
ATOM   1381 C  CD2 . LEU A 1 163 ? -10.920 -5.362  1.637   1.00 14.66  ? 164 LEU A CD2 1 
ATOM   1382 N  N   . ASP A 1 164 ? -10.700 -6.999  -3.551  1.00 18.56  ? 165 ASP A N   1 
ATOM   1383 C  CA  . ASP A 1 164 ? -9.868  -7.329  -4.716  1.00 24.68  ? 165 ASP A CA  1 
ATOM   1384 C  C   . ASP A 1 164 ? -9.423  -6.058  -5.436  1.00 21.75  ? 165 ASP A C   1 
ATOM   1385 O  O   . ASP A 1 164 ? -8.496  -6.192  -6.250  1.00 25.91  ? 165 ASP A O   1 
ATOM   1386 C  CB  . ASP A 1 164 ? -10.649 -8.225  -5.644  1.00 30.42  ? 165 ASP A CB  1 
ATOM   1387 C  CG  . ASP A 1 164 ? -11.724 -7.463  -6.386  1.00 36.48  ? 165 ASP A CG  1 
ATOM   1388 O  OD1 . ASP A 1 164 ? -12.553 -6.777  -5.757  1.00 57.91  ? 165 ASP A OD1 1 
ATOM   1389 O  OD2 . ASP A 1 164 ? -11.753 -7.561  -7.659  1.00 69.76  ? 165 ASP A OD2 1 
ATOM   1390 N  N   . SER A 1 165 ? -10.095 -4.898  -5.219  1.00 19.76  ? 166 SER A N   1 
ATOM   1391 C  CA  . SER A 1 165 ? -9.723  -3.651  -5.916  1.00 20.07  ? 166 SER A CA  1 
ATOM   1392 C  C   . SER A 1 165 ? -8.644  -2.893  -5.106  1.00 17.23  ? 166 SER A C   1 
ATOM   1393 O  O   . SER A 1 165 ? -8.074  -1.895  -5.636  1.00 19.82  ? 166 SER A O   1 
ATOM   1394 C  CB  . SER A 1 165 ? -10.989 -2.813  -6.214  1.00 21.27  ? 166 SER A CB  1 
ATOM   1395 O  OG  . SER A 1 165 ? -11.344 -2.219  -5.007  1.00 22.76  ? 166 SER A OG  1 
ATOM   1396 N  N   . ILE A 1 166 ? -8.310  -3.358  -3.897  1.00 15.02  ? 167 ILE A N   1 
ATOM   1397 C  CA  . ILE A 1 166 ? -7.306  -2.670  -3.082  1.00 14.67  ? 167 ILE A CA  1 
ATOM   1398 C  C   . ILE A 1 166 ? -6.249  -3.670  -2.547  1.00 14.17  ? 167 ILE A C   1 
ATOM   1399 O  O   . ILE A 1 166 ? -5.856  -3.680  -1.375  1.00 14.73  ? 167 ILE A O   1 
ATOM   1400 C  CB  . ILE A 1 166 ? -7.911  -1.805  -1.932  1.00 14.40  ? 167 ILE A CB  1 
ATOM   1401 C  CG1 . ILE A 1 166 ? -8.775  -2.683  -1.013  1.00 14.58  ? 167 ILE A CG1 1 
ATOM   1402 C  CG2 . ILE A 1 166 ? -8.654  -0.663  -2.521  1.00 16.67  ? 167 ILE A CG2 1 
ATOM   1403 C  CD1 . ILE A 1 166 ? -8.794  -2.084  0.354   1.00 16.45  ? 167 ILE A CD1 1 
ATOM   1404 N  N   . LYS A 1 167 ? -5.860  -4.575  -3.455  1.00 14.88  ? 168 LYS A N   1 
ATOM   1405 C  CA  . LYS A 1 167 ? -5.119  -5.712  -3.011  1.00 14.60  ? 168 LYS A CA  1 
ATOM   1406 C  C   . LYS A 1 167 ? -3.796  -5.323  -2.323  1.00 13.41  ? 168 LYS A C   1 
ATOM   1407 O  O   . LYS A 1 167 ? -3.321  -5.960  -1.372  1.00 14.68  ? 168 LYS A O   1 
ATOM   1408 C  CB  . LYS A 1 167 ? -4.783  -6.669  -4.193  1.00 16.11  ? 168 LYS A CB  1 
ATOM   1409 C  CG  . LYS A 1 167 ? -4.011  -7.883  -3.780  1.00 15.39  ? 168 LYS A CG  1 
ATOM   1410 C  CD  . LYS A 1 167 ? -3.819  -8.855  -4.915  1.00 21.73  ? 168 LYS A CD  1 
ATOM   1411 C  CE  . LYS A 1 167 ? -2.963  -10.056 -4.469  1.00 31.02  ? 168 LYS A CE  1 
ATOM   1412 N  NZ  . LYS A 1 167 ? -2.573  -10.957 -5.623  1.00 45.43  ? 168 LYS A NZ  1 
ATOM   1413 N  N   . THR A 1 168 ? -3.170  -4.292  -2.861  1.00 14.30  ? 169 THR A N   1 
ATOM   1414 C  CA  . THR A 1 168 ? -1.827  -3.952  -2.492  1.00 14.18  ? 169 THR A CA  1 
ATOM   1415 C  C   . THR A 1 168 ? -1.713  -2.504  -1.860  1.00 12.61  ? 169 THR A C   1 
ATOM   1416 O  O   . THR A 1 168 ? -2.609  -1.699  -1.938  1.00 15.43  ? 169 THR A O   1 
ATOM   1417 C  CB  . THR A 1 168 ? -0.828  -4.017  -3.722  1.00 15.93  ? 169 THR A CB  1 
ATOM   1418 O  OG1 . THR A 1 168 ? -1.397  -3.255  -4.787  1.00 17.37  ? 169 THR A OG1 1 
ATOM   1419 C  CG2 . THR A 1 168 ? -0.655  -5.465  -4.195  1.00 18.05  ? 169 THR A CG2 1 
ATOM   1420 N  N   . LYS A 1 169 ? -0.642  -2.420  -1.123  1.00 15.02  ? 170 LYS A N   1 
ATOM   1421 C  CA  . LYS A 1 169 ? -0.374  -1.194  -0.336  1.00 14.46  ? 170 LYS A CA  1 
ATOM   1422 C  C   . LYS A 1 169 ? -0.496  0.117   -1.105  1.00 14.84  ? 170 LYS A C   1 
ATOM   1423 O  O   . LYS A 1 169 ? 0.060   0.188   -2.233  1.00 17.60  ? 170 LYS A O   1 
ATOM   1424 C  CB  . LYS A 1 169 ? 1.004   -1.331  0.261   1.00 15.22  ? 170 LYS A CB  1 
ATOM   1425 C  CG  . LYS A 1 169 ? 1.445   -0.108  1.068   1.00 17.04  ? 170 LYS A CG  1 
ATOM   1426 C  CD  . LYS A 1 169 ? 2.698   -0.305  1.713   1.00 18.77  ? 170 LYS A CD  1 
ATOM   1427 C  CE  . LYS A 1 169 ? 3.902   -0.364  0.782   1.00 31.67  ? 170 LYS A CE  1 
ATOM   1428 N  NZ  . LYS A 1 169 ? 5.076   -0.686  1.643   1.00 51.04  ? 170 LYS A NZ  1 
ATOM   1429 N  N   . GLY A 1 170 ? -1.336  1.038   -0.611  1.00 16.04  ? 171 GLY A N   1 
ATOM   1430 C  CA  . GLY A 1 170 ? -1.515  2.270   -1.293  1.00 16.93  ? 171 GLY A CA  1 
ATOM   1431 C  C   . GLY A 1 170 ? -2.706  2.347   -2.208  1.00 18.09  ? 171 GLY A C   1 
ATOM   1432 O  O   . GLY A 1 170 ? -2.996  3.462   -2.654  1.00 22.21  ? 171 GLY A O   1 
ATOM   1433 N  N   . LYS A 1 171 ? -3.335  1.220   -2.565  1.00 15.81  ? 172 LYS A N   1 
ATOM   1434 C  CA  . LYS A 1 171 ? -4.551  1.252   -3.306  1.00 15.95  ? 172 LYS A CA  1 
ATOM   1435 C  C   . LYS A 1 171 ? -5.730  1.728   -2.490  1.00 15.00  ? 172 LYS A C   1 
ATOM   1436 O  O   . LYS A 1 171 ? -5.891  1.307   -1.341  1.00 14.72  ? 172 LYS A O   1 
ATOM   1437 C  CB  . LYS A 1 171 ? -4.766  -0.063  -3.985  1.00 18.52  ? 172 LYS A CB  1 
ATOM   1438 C  CG  . LYS A 1 171 ? -3.682  -0.494  -4.959  1.00 20.03  ? 172 LYS A CG  1 
ATOM   1439 C  CD  . LYS A 1 171 ? -4.140  -1.617  -5.923  1.00 26.06  ? 172 LYS A CD  1 
ATOM   1440 C  CE  . LYS A 1 171 ? -4.472  -1.262  -7.361  1.00 47.03  ? 172 LYS A CE  1 
ATOM   1441 N  NZ  . LYS A 1 171 ? -5.406  -2.347  -7.886  1.00 48.70  ? 172 LYS A NZ  1 
ATOM   1442 N  N   . SER A 1 172 ? -6.592  2.541   -3.057  1.00 17.16  ? 173 SER A N   1 
ATOM   1443 C  CA  . SER A 1 172 ? -7.870  2.997   -2.542  1.00 17.21  ? 173 SER A CA  1 
ATOM   1444 C  C   . SER A 1 172 ? -9.040  2.786   -3.481  1.00 15.83  ? 173 SER A C   1 
ATOM   1445 O  O   . SER A 1 172 ? -8.806  2.675   -4.684  1.00 20.03  ? 173 SER A O   1 
ATOM   1446 C  CB  . SER A 1 172 ? -7.775  4.434   -2.074  1.00 17.85  ? 173 SER A CB  1 
ATOM   1447 O  OG  . SER A 1 172 ? -7.381  5.297   -3.115  1.00 25.16  ? 173 SER A OG  1 
ATOM   1448 N  N   . ALA A 1 173 ? -10.268 2.777   -3.014  1.00 17.83  ? 174 ALA A N   1 
ATOM   1449 C  CA  . ALA A 1 173 ? -11.417 2.721   -3.845  1.00 19.87  ? 174 ALA A CA  1 
ATOM   1450 C  C   . ALA A 1 173 ? -12.562 3.522   -3.191  1.00 15.10  ? 174 ALA A C   1 
ATOM   1451 O  O   . ALA A 1 173 ? -12.639 3.598   -1.970  1.00 14.90  ? 174 ALA A O   1 
ATOM   1452 C  CB  . ALA A 1 173 ? -11.839 1.267   -4.053  1.00 24.61  ? 174 ALA A CB  1 
ATOM   1453 N  N   . ASP A 1 174 ? -13.326 4.260   -4.005  1.00 18.79  ? 175 ASP A N   1 
ATOM   1454 C  CA  . ASP A 1 174 ? -14.549 4.924   -3.450  1.00 17.94  ? 175 ASP A CA  1 
ATOM   1455 C  C   . ASP A 1 174 ? -15.386 3.858   -2.736  1.00 17.03  ? 175 ASP A C   1 
ATOM   1456 O  O   . ASP A 1 174 ? -15.472 2.660   -3.176  1.00 21.50  ? 175 ASP A O   1 
ATOM   1457 C  CB  . ASP A 1 174 ? -15.342 5.550   -4.583  1.00 26.32  ? 175 ASP A CB  1 
ATOM   1458 C  CG  . ASP A 1 174 ? -14.512 6.513   -5.418  1.00 33.37  ? 175 ASP A CG  1 
ATOM   1459 O  OD1 . ASP A 1 174 ? -13.683 7.277   -4.840  1.00 50.48  ? 175 ASP A OD1 1 
ATOM   1460 O  OD2 . ASP A 1 174 ? -14.675 6.492   -6.664  1.00 26.92  ? 175 ASP A OD2 1 
ATOM   1461 N  N   . PHE A 1 175 ? -15.956 4.315   -1.625  1.00 16.84  ? 176 PHE A N   1 
ATOM   1462 C  CA  . PHE A 1 175 ? -16.678 3.445   -0.743  1.00 16.22  ? 176 PHE A CA  1 
ATOM   1463 C  C   . PHE A 1 175 ? -17.732 4.211   -0.010  1.00 14.62  ? 176 PHE A C   1 
ATOM   1464 O  O   . PHE A 1 175 ? -17.499 4.472   1.139   1.00 17.80  ? 176 PHE A O   1 
ATOM   1465 C  CB  . PHE A 1 175 ? -15.692 2.621   0.094   1.00 16.05  ? 176 PHE A CB  1 
ATOM   1466 C  CG  . PHE A 1 175 ? -16.294 1.347   0.607   1.00 15.94  ? 176 PHE A CG  1 
ATOM   1467 C  CD1 . PHE A 1 175 ? -16.570 0.259   -0.232  1.00 19.36  ? 176 PHE A CD1 1 
ATOM   1468 C  CD2 . PHE A 1 175 ? -16.592 1.237   1.924   1.00 16.23  ? 176 PHE A CD2 1 
ATOM   1469 C  CE1 . PHE A 1 175 ? -17.078 -0.909  0.267   1.00 20.56  ? 176 PHE A CE1 1 
ATOM   1470 C  CE2 . PHE A 1 175 ? -17.118 0.065   2.466   1.00 17.04  ? 176 PHE A CE2 1 
ATOM   1471 C  CZ  . PHE A 1 175 ? -17.405 -0.990  1.606   1.00 19.85  ? 176 PHE A CZ  1 
ATOM   1472 N  N   . THR A 1 176 ? -18.721 4.658   -0.723  1.00 16.61  ? 177 THR A N   1 
ATOM   1473 C  CA  . THR A 1 176 ? -19.804 5.454   -0.179  1.00 15.25  ? 177 THR A CA  1 
ATOM   1474 C  C   . THR A 1 176 ? -20.913 4.612   0.307   1.00 14.97  ? 177 THR A C   1 
ATOM   1475 O  O   . THR A 1 176 ? -21.085 3.441   -0.210  1.00 16.63  ? 177 THR A O   1 
ATOM   1476 C  CB  . THR A 1 176 ? -20.200 6.476   -1.231  1.00 17.40  ? 177 THR A CB  1 
ATOM   1477 O  OG1 . THR A 1 176 ? -20.600 5.789   -2.466  1.00 22.67  ? 177 THR A OG1 1 
ATOM   1478 C  CG2 . THR A 1 176 ? -19.014 7.426   -1.538  1.00 29.86  ? 177 THR A CG2 1 
ATOM   1479 N  N   . ASN A 1 177 ? -21.758 5.160   1.199   1.00 15.41  ? 178 ASN A N   1 
ATOM   1480 C  CA  . ASN A 1 177 ? -23.031 4.590   1.618   1.00 16.86  ? 178 ASN A CA  1 
ATOM   1481 C  C   . ASN A 1 177 ? -22.865 3.261   2.362   1.00 16.34  ? 178 ASN A C   1 
ATOM   1482 O  O   . ASN A 1 177 ? -23.797 2.529   2.412   1.00 22.06  ? 178 ASN A O   1 
ATOM   1483 C  CB  . ASN A 1 177 ? -23.973 4.488   0.435   1.00 17.28  ? 178 ASN A CB  1 
ATOM   1484 C  CG  . ASN A 1 177 ? -24.176 5.874   -0.232  1.00 17.12  ? 178 ASN A CG  1 
ATOM   1485 O  OD1 . ASN A 1 177 ? -24.786 6.740   0.395   1.00 22.21  ? 178 ASN A OD1 1 
ATOM   1486 N  ND2 . ASN A 1 177 ? -23.554 6.102   -1.391  1.00 18.14  ? 178 ASN A ND2 1 
ATOM   1487 N  N   . PHE A 1 178 ? -21.665 3.062   2.952   1.00 15.16  ? 179 PHE A N   1 
ATOM   1488 C  CA  . PHE A 1 178 ? -21.521 1.862   3.776   1.00 15.53  ? 179 PHE A CA  1 
ATOM   1489 C  C   . PHE A 1 178 ? -21.993 2.163   5.188   1.00 13.87  ? 179 PHE A C   1 
ATOM   1490 O  O   . PHE A 1 178 ? -21.573 3.156   5.788   1.00 14.99  ? 179 PHE A O   1 
ATOM   1491 C  CB  . PHE A 1 178 ? -20.088 1.397   3.806   1.00 15.37  ? 179 PHE A CB  1 
ATOM   1492 C  CG  . PHE A 1 178 ? -19.906 0.166   4.665   1.00 14.43  ? 179 PHE A CG  1 
ATOM   1493 C  CD1 . PHE A 1 178 ? -20.362 -1.067  4.175   1.00 16.20  ? 179 PHE A CD1 1 
ATOM   1494 C  CD2 . PHE A 1 178 ? -19.516 0.227   6.004   1.00 13.55  ? 179 PHE A CD2 1 
ATOM   1495 C  CE1 . PHE A 1 178 ? -20.302 -2.211  4.926   1.00 16.31  ? 179 PHE A CE1 1 
ATOM   1496 C  CE2 . PHE A 1 178 ? -19.508 -0.934  6.786   1.00 13.28  ? 179 PHE A CE2 1 
ATOM   1497 C  CZ  . PHE A 1 178 ? -19.886 -2.151  6.262   1.00 14.15  ? 179 PHE A CZ  1 
ATOM   1498 N  N   . ASP A 1 179 ? -22.861 1.293   5.697   1.00 14.97  ? 180 ASP A N   1 
ATOM   1499 C  CA  . ASP A 1 179 ? -23.457 1.534   6.986   1.00 15.52  ? 180 ASP A CA  1 
ATOM   1500 C  C   . ASP A 1 179 ? -22.779 0.650   8.054   1.00 13.11  ? 180 ASP A C   1 
ATOM   1501 O  O   . ASP A 1 179 ? -22.980 -0.577  8.077   1.00 14.00  ? 180 ASP A O   1 
ATOM   1502 C  CB  . ASP A 1 179 ? -24.940 1.202   6.889   1.00 17.95  ? 180 ASP A CB  1 
ATOM   1503 C  CG  . ASP A 1 179 ? -25.704 1.633   8.078   1.00 18.92  ? 180 ASP A CG  1 
ATOM   1504 O  OD1 . ASP A 1 179 ? -25.128 1.764   9.187   1.00 16.74  ? 180 ASP A OD1 1 
ATOM   1505 O  OD2 . ASP A 1 179 ? -26.895 1.878   7.949   1.00 26.16  ? 180 ASP A OD2 1 
ATOM   1506 N  N   . PRO A 1 180 ? -21.988 1.245   8.958   1.00 11.90  ? 181 PRO A N   1 
ATOM   1507 C  CA  . PRO A 1 180 ? -21.265 0.403   9.951   1.00 12.33  ? 181 PRO A CA  1 
ATOM   1508 C  C   . PRO A 1 180 ? -22.185 -0.204  10.985  1.00 12.15  ? 181 PRO A C   1 
ATOM   1509 O  O   . PRO A 1 180 ? -21.732 -1.075  11.720  1.00 12.01  ? 181 PRO A O   1 
ATOM   1510 C  CB  . PRO A 1 180 ? -20.249 1.434   10.529  1.00 13.70  ? 181 PRO A CB  1 
ATOM   1511 C  CG  . PRO A 1 180 ? -20.919 2.754   10.411  1.00 13.69  ? 181 PRO A CG  1 
ATOM   1512 C  CD  . PRO A 1 180 ? -21.637 2.668   9.050   1.00 13.64  ? 181 PRO A CD  1 
ATOM   1513 N  N   . ARG A 1 181 ? -23.467 0.188   11.024  1.00 12.19  ? 182 ARG A N   1 
ATOM   1514 C  CA  . ARG A 1 181 ? -24.398 -0.495  11.996  1.00 13.22  ? 182 ARG A CA  1 
ATOM   1515 C  C   . ARG A 1 181 ? -24.485 -1.963  11.621  1.00 12.96  ? 182 ARG A C   1 
ATOM   1516 O  O   . ARG A 1 181 ? -24.841 -2.775  12.522  1.00 15.14  ? 182 ARG A O   1 
ATOM   1517 C  CB  . ARG A 1 181 ? -25.779 0.143   11.949  1.00 13.91  ? 182 ARG A CB  1 
ATOM   1518 C  CG  . ARG A 1 181 ? -25.749 1.583   12.481  1.00 16.33  ? 182 ARG A CG  1 
ATOM   1519 C  CD  . ARG A 1 181 ? -27.072 2.281   12.442  1.00 19.29  ? 182 ARG A CD  1 
ATOM   1520 N  NE  . ARG A 1 181 ? -27.403 2.568   11.076  1.00 18.67  ? 182 ARG A NE  1 
ATOM   1521 C  CZ  . ARG A 1 181 ? -28.493 3.225   10.721  1.00 22.15  ? 182 ARG A CZ  1 
ATOM   1522 N  NH1 . ARG A 1 181 ? -29.337 3.659   11.638  1.00 28.74  ? 182 ARG A NH1 1 
ATOM   1523 N  NH2 . ARG A 1 181 ? -28.725 3.440   9.429   1.00 26.58  ? 182 ARG A NH2 1 
ATOM   1524 N  N   . GLY A 1 182 ? -24.265 -2.365  10.352  1.00 13.52  ? 183 GLY A N   1 
ATOM   1525 C  CA  . GLY A 1 182 ? -24.280 -3.757  9.972   1.00 15.94  ? 183 GLY A CA  1 
ATOM   1526 C  C   . GLY A 1 182 ? -23.193 -4.603  10.512  1.00 14.81  ? 183 GLY A C   1 
ATOM   1527 O  O   . GLY A 1 182 ? -23.222 -5.785  10.270  1.00 17.44  ? 183 GLY A O   1 
ATOM   1528 N  N   . LEU A 1 183 ? -22.230 -4.027  11.241  1.00 12.96  ? 184 LEU A N   1 
ATOM   1529 C  CA  . LEU A 1 183 ? -21.125 -4.743  11.805  1.00 13.09  ? 184 LEU A CA  1 
ATOM   1530 C  C   . LEU A 1 183 ? -21.263 -4.926  13.309  1.00 12.65  ? 184 LEU A C   1 
ATOM   1531 O  O   . LEU A 1 183 ? -20.308 -5.480  13.918  1.00 14.46  ? 184 LEU A O   1 
ATOM   1532 C  CB  . LEU A 1 183 ? -19.824 -4.024  11.508  1.00 13.27  ? 184 LEU A CB  1 
ATOM   1533 C  CG  . LEU A 1 183 ? -19.558 -3.934  10.005  1.00 14.24  ? 184 LEU A CG  1 
ATOM   1534 C  CD1 . LEU A 1 183 ? -18.305 -3.146  9.851   1.00 17.11  ? 184 LEU A CD1 1 
ATOM   1535 C  CD2 . LEU A 1 183 ? -19.441 -5.260  9.251   1.00 16.90  ? 184 LEU A CD2 1 
ATOM   1536 N  N   . LEU A 1 184 ? -22.349 -4.469  13.919  1.00 13.35  ? 185 LEU A N   1 
ATOM   1537 C  CA  . LEU A 1 184 ? -22.475 -4.515  15.346  1.00 12.86  ? 185 LEU A CA  1 
ATOM   1538 C  C   . LEU A 1 184 ? -23.265 -5.753  15.902  1.00 14.61  ? 185 LEU A C   1 
ATOM   1539 O  O   . LEU A 1 184 ? -24.377 -6.048  15.407  1.00 17.68  ? 185 LEU A O   1 
ATOM   1540 C  CB  . LEU A 1 184 ? -23.247 -3.310  15.886  1.00 12.79  ? 185 LEU A CB  1 
ATOM   1541 C  CG  . LEU A 1 184 ? -22.648 -1.956  15.459  1.00 12.38  ? 185 LEU A CG  1 
ATOM   1542 C  CD1 . LEU A 1 184 ? -23.517 -0.817  15.922  1.00 13.64  ? 185 LEU A CD1 1 
ATOM   1543 C  CD2 . LEU A 1 184 ? -21.230 -1.829  16.016  1.00 14.40  ? 185 LEU A CD2 1 
ATOM   1544 N  N   . PRO A 1 185 ? -22.838 -6.399  16.978  1.00 12.34  ? 186 PRO A N   1 
ATOM   1545 C  CA  . PRO A 1 185 ? -23.569 -7.503  17.539  1.00 13.35  ? 186 PRO A CA  1 
ATOM   1546 C  C   . PRO A 1 185 ? -24.856 -6.944  18.201  1.00 14.03  ? 186 PRO A C   1 
ATOM   1547 O  O   . PRO A 1 185 ? -25.053 -5.735  18.343  1.00 15.93  ? 186 PRO A O   1 
ATOM   1548 C  CB  . PRO A 1 185 ? -22.556 -8.116  18.555  1.00 12.69  ? 186 PRO A CB  1 
ATOM   1549 C  CG  . PRO A 1 185 ? -21.850 -6.883  19.008  1.00 11.77  ? 186 PRO A CG  1 
ATOM   1550 C  CD  . PRO A 1 185 ? -21.669 -5.978  17.798  1.00 11.60  ? 186 PRO A CD  1 
ATOM   1551 N  N   A GLU A 1 186 ? -25.669 -7.886  18.711  0.50 15.30  ? 187 GLU A N   1 
ATOM   1552 N  N   B GLU A 1 186 ? -25.719 -7.880  18.673  0.50 15.48  ? 187 GLU A N   1 
ATOM   1553 C  CA  A GLU A 1 186 ? -26.938 -7.515  19.253  0.50 15.97  ? 187 GLU A CA  1 
ATOM   1554 C  CA  B GLU A 1 186 ? -26.973 -7.483  19.323  0.50 15.79  ? 187 GLU A CA  1 
ATOM   1555 C  C   A GLU A 1 186 ? -26.734 -6.744  20.567  0.50 14.33  ? 187 GLU A C   1 
ATOM   1556 C  C   B GLU A 1 186 ? -26.716 -6.714  20.579  0.50 14.57  ? 187 GLU A C   1 
ATOM   1557 O  O   A GLU A 1 186 ? -27.329 -5.661  20.772  0.50 17.80  ? 187 GLU A O   1 
ATOM   1558 O  O   B GLU A 1 186 ? -27.327 -5.666  20.811  0.50 17.84  ? 187 GLU A O   1 
ATOM   1559 C  CB  A GLU A 1 186 ? -27.611 -8.815  19.486  0.50 21.26  ? 187 GLU A CB  1 
ATOM   1560 C  CB  B GLU A 1 186 ? -27.709 -8.704  19.778  0.50 23.19  ? 187 GLU A CB  1 
ATOM   1561 C  CG  A GLU A 1 186 ? -28.824 -8.677  20.320  0.50 20.54  ? 187 GLU A CG  1 
ATOM   1562 C  CG  B GLU A 1 186 ? -28.435 -9.322  18.658  0.50 20.53  ? 187 GLU A CG  1 
ATOM   1563 C  CD  A GLU A 1 186 ? -29.376 -9.985  20.735  0.50 23.28  ? 187 GLU A CD  1 
ATOM   1564 C  CD  B GLU A 1 186 ? -29.215 -10.543 19.092  0.50 25.37  ? 187 GLU A CD  1 
ATOM   1565 O  OE1 A GLU A 1 186 ? -29.221 -10.959 19.945  0.50 23.22  ? 187 GLU A OE1 1 
ATOM   1566 O  OE1 B GLU A 1 186 ? -29.294 -10.839 20.317  0.50 26.40  ? 187 GLU A OE1 1 
ATOM   1567 O  OE2 A GLU A 1 186 ? -29.985 -9.971  21.829  0.50 29.03  ? 187 GLU A OE2 1 
ATOM   1568 O  OE2 B GLU A 1 186 ? -29.805 -11.212 18.226  0.50 27.66  ? 187 GLU A OE2 1 
ATOM   1569 N  N   . SER A 1 187 ? -25.803 -7.237  21.414  1.00 13.52  ? 188 SER A N   1 
ATOM   1570 C  CA  . SER A 1 187 ? -25.571 -6.634  22.681  1.00 13.71  ? 188 SER A CA  1 
ATOM   1571 C  C   . SER A 1 187 ? -24.440 -5.609  22.677  1.00 13.46  ? 188 SER A C   1 
ATOM   1572 O  O   . SER A 1 187 ? -23.420 -5.869  22.033  1.00 14.20  ? 188 SER A O   1 
ATOM   1573 C  CB  . SER A 1 187 ? -25.173 -7.697  23.696  1.00 14.84  ? 188 SER A CB  1 
ATOM   1574 O  OG  . SER A 1 187 ? -24.894 -7.136  25.001  1.00 15.78  ? 188 SER A OG  1 
ATOM   1575 N  N   . LEU A 1 188 ? -24.602 -4.524  23.409  1.00 12.90  ? 189 LEU A N   1 
ATOM   1576 C  CA  . LEU A 1 188 ? -23.545 -3.535  23.620  1.00 13.90  ? 189 LEU A CA  1 
ATOM   1577 C  C   . LEU A 1 188 ? -22.923 -3.677  24.998  1.00 12.92  ? 189 LEU A C   1 
ATOM   1578 O  O   . LEU A 1 188 ? -22.246 -2.733  25.457  1.00 14.29  ? 189 LEU A O   1 
ATOM   1579 C  CB  . LEU A 1 188 ? -24.050 -2.076  23.354  1.00 15.60  ? 189 LEU A CB  1 
ATOM   1580 C  CG  . LEU A 1 188 ? -24.474 -1.785  21.933  1.00 17.17  ? 189 LEU A CG  1 
ATOM   1581 C  CD1 . LEU A 1 188 ? -24.983 -0.361  21.762  1.00 20.43  ? 189 LEU A CD1 1 
ATOM   1582 C  CD2 . LEU A 1 188 ? -23.375 -2.117  20.946  1.00 21.40  ? 189 LEU A CD2 1 
ATOM   1583 N  N   . ASP A 1 189 ? -23.064 -4.833  25.667  1.00 12.06  ? 190 ASP A N   1 
ATOM   1584 C  CA  . ASP A 1 189 ? -22.302 -5.076  26.877  1.00 11.99  ? 190 ASP A CA  1 
ATOM   1585 C  C   . ASP A 1 189 ? -20.792 -5.038  26.576  1.00 10.49  ? 190 ASP A C   1 
ATOM   1586 O  O   . ASP A 1 189 ? -20.350 -5.548  25.542  1.00 10.31  ? 190 ASP A O   1 
ATOM   1587 C  CB  . ASP A 1 189 ? -22.628 -6.417  27.469  1.00 15.00  ? 190 ASP A CB  1 
ATOM   1588 C  CG  . ASP A 1 189 ? -24.013 -6.501  28.108  1.00 20.97  ? 190 ASP A CG  1 
ATOM   1589 O  OD1 . ASP A 1 189 ? -24.653 -5.444  28.315  1.00 28.67  ? 190 ASP A OD1 1 
ATOM   1590 O  OD2 . ASP A 1 189 ? -24.449 -7.639  28.391  1.00 28.31  ? 190 ASP A OD2 1 
ATOM   1591 N  N   . TYR A 1 190 ? -20.013 -4.453  27.483  1.00 10.11  ? 191 TYR A N   1 
ATOM   1592 C  CA  . TYR A 1 190 ? -18.577 -4.180  27.177  1.00 9.46   ? 191 TYR A CA  1 
ATOM   1593 C  C   . TYR A 1 190 ? -17.719 -4.270  28.407  1.00 8.84   ? 191 TYR A C   1 
ATOM   1594 O  O   . TYR A 1 190 ? -18.149 -4.124  29.570  1.00 9.72   ? 191 TYR A O   1 
ATOM   1595 C  CB  . TYR A 1 190 ? -18.459 -2.800  26.500  1.00 9.77   ? 191 TYR A CB  1 
ATOM   1596 C  CG  . TYR A 1 190 ? -18.833 -1.654  27.359  1.00 9.95   ? 191 TYR A CG  1 
ATOM   1597 C  CD1 . TYR A 1 190 ? -17.905 -1.037  28.216  1.00 10.68  ? 191 TYR A CD1 1 
ATOM   1598 C  CD2 . TYR A 1 190 ? -20.136 -1.124  27.299  1.00 11.24  ? 191 TYR A CD2 1 
ATOM   1599 C  CE1 . TYR A 1 190 ? -18.314 0.031   29.029  1.00 11.36  ? 191 TYR A CE1 1 
ATOM   1600 C  CE2 . TYR A 1 190 ? -20.511 -0.066  28.106  1.00 11.56  ? 191 TYR A CE2 1 
ATOM   1601 C  CZ  . TYR A 1 190 ? -19.613 0.507   28.988  1.00 11.39  ? 191 TYR A CZ  1 
ATOM   1602 O  OH  . TYR A 1 190 ? -19.953 1.519   29.842  1.00 13.18  ? 191 TYR A OH  1 
ATOM   1603 N  N   . TRP A 1 191 ? -16.418 -4.391  28.099  1.00 8.07   ? 192 TRP A N   1 
ATOM   1604 C  CA  . TRP A 1 191 ? -15.323 -4.149  29.039  1.00 8.40   ? 192 TRP A CA  1 
ATOM   1605 C  C   . TRP A 1 191 ? -14.626 -2.849  28.605  1.00 7.82   ? 192 TRP A C   1 
ATOM   1606 O  O   . TRP A 1 191 ? -14.573 -2.508  27.444  1.00 8.75   ? 192 TRP A O   1 
ATOM   1607 C  CB  . TRP A 1 191 ? -14.303 -5.267  29.042  1.00 8.80   ? 192 TRP A CB  1 
ATOM   1608 C  CG  . TRP A 1 191 ? -14.825 -6.593  29.441  1.00 9.00   ? 192 TRP A CG  1 
ATOM   1609 C  CD1 . TRP A 1 191 ? -15.059 -7.011  30.721  1.00 10.22  ? 192 TRP A CD1 1 
ATOM   1610 C  CD2 . TRP A 1 191 ? -15.095 -7.702  28.581  1.00 9.12   ? 192 TRP A CD2 1 
ATOM   1611 N  NE1 . TRP A 1 191 ? -15.476 -8.328  30.704  1.00 10.91  ? 192 TRP A NE1 1 
ATOM   1612 C  CE2 . TRP A 1 191 ? -15.520 -8.780  29.429  1.00 10.51  ? 192 TRP A CE2 1 
ATOM   1613 C  CE3 . TRP A 1 191 ? -14.998 -7.929  27.184  1.00 9.52   ? 192 TRP A CE3 1 
ATOM   1614 C  CZ2 . TRP A 1 191 ? -15.799 -10.031 28.880  1.00 11.16  ? 192 TRP A CZ2 1 
ATOM   1615 C  CZ3 . TRP A 1 191 ? -15.256 -9.196  26.700  1.00 10.59  ? 192 TRP A CZ3 1 
ATOM   1616 C  CH2 . TRP A 1 191 ? -15.670 -10.214 27.551  1.00 11.89  ? 192 TRP A CH2 1 
ATOM   1617 N  N   . THR A 1 192 ? -14.032 -2.147  29.577  1.00 7.95   ? 193 THR A N   1 
ATOM   1618 C  CA  . THR A 1 192 ? -13.302 -0.907  29.251  1.00 8.00   ? 193 THR A CA  1 
ATOM   1619 C  C   . THR A 1 192 ? -12.073 -0.763  30.121  1.00 7.23   ? 193 THR A C   1 
ATOM   1620 O  O   . THR A 1 192 ? -12.058 -1.151  31.294  1.00 8.59   ? 193 THR A O   1 
ATOM   1621 C  CB  . THR A 1 192 ? -14.245 0.305   29.364  1.00 8.38   ? 193 THR A CB  1 
ATOM   1622 O  OG1 . THR A 1 192 ? -13.555 1.492   28.949  1.00 8.61   ? 193 THR A OG1 1 
ATOM   1623 C  CG2 . THR A 1 192 ? -14.780 0.542   30.743  1.00 9.86   ? 193 THR A CG2 1 
ATOM   1624 N  N   . TYR A 1 193 ? -11.015 -0.145  29.549  1.00 7.59   ? 194 TYR A N   1 
ATOM   1625 C  CA  . TYR A 1 193 ? -9.804  0.132   30.262  1.00 7.82   ? 194 TYR A CA  1 
ATOM   1626 C  C   . TYR A 1 193 ? -9.044  1.207   29.472  1.00 7.23   ? 194 TYR A C   1 
ATOM   1627 O  O   . TYR A 1 193 ? -9.239  1.376   28.297  1.00 7.47   ? 194 TYR A O   1 
ATOM   1628 C  CB  . TYR A 1 193 ? -8.967  -1.137  30.470  1.00 8.71   ? 194 TYR A CB  1 
ATOM   1629 C  CG  . TYR A 1 193 ? -8.263  -1.625  29.218  1.00 7.45   ? 194 TYR A CG  1 
ATOM   1630 C  CD1 . TYR A 1 193 ? -8.943  -2.335  28.227  1.00 7.57   ? 194 TYR A CD1 1 
ATOM   1631 C  CD2 . TYR A 1 193 ? -6.964  -1.279  28.985  1.00 7.85   ? 194 TYR A CD2 1 
ATOM   1632 C  CE1 . TYR A 1 193 ? -8.331  -2.687  27.036  1.00 7.72   ? 194 TYR A CE1 1 
ATOM   1633 C  CE2 . TYR A 1 193 ? -6.320  -1.617  27.811  1.00 7.94   ? 194 TYR A CE2 1 
ATOM   1634 C  CZ  . TYR A 1 193 ? -6.998  -2.309  26.808  1.00 7.01   ? 194 TYR A CZ  1 
ATOM   1635 O  OH  . TYR A 1 193 ? -6.341  -2.603  25.649  1.00 7.54   ? 194 TYR A OH  1 
ATOM   1636 N  N   . PRO A 1 194 ? -8.089  1.902   30.168  1.00 7.71   ? 195 PRO A N   1 
ATOM   1637 C  CA  . PRO A 1 194 ? -7.242  2.915   29.477  1.00 7.89   ? 195 PRO A CA  1 
ATOM   1638 C  C   . PRO A 1 194 ? -6.051  2.227   28.819  1.00 7.35   ? 195 PRO A C   1 
ATOM   1639 O  O   . PRO A 1 194 ? -5.328  1.465   29.482  1.00 8.33   ? 195 PRO A O   1 
ATOM   1640 C  CB  . PRO A 1 194 ? -6.787  3.818   30.630  1.00 9.41   ? 195 PRO A CB  1 
ATOM   1641 C  CG  . PRO A 1 194 ? -6.778  2.907   31.828  1.00 9.80   ? 195 PRO A CG  1 
ATOM   1642 C  CD  . PRO A 1 194 ? -7.906  1.935   31.613  1.00 9.87   ? 195 PRO A CD  1 
ATOM   1643 N  N   . GLY A 1 195 ? -5.831  2.526   27.552  1.00 7.23   ? 196 GLY A N   1 
ATOM   1644 C  CA  . GLY A 1 195 ? -4.716  1.915   26.841  1.00 7.37   ? 196 GLY A CA  1 
ATOM   1645 C  C   . GLY A 1 195 ? -4.162  2.769   25.737  1.00 7.16   ? 196 GLY A C   1 
ATOM   1646 O  O   . GLY A 1 195 ? -4.058  4.027   25.892  1.00 7.78   ? 196 GLY A O   1 
ATOM   1647 N  N   . SER A 1 196 ? -3.740  2.139   24.670  1.00 6.81   ? 197 SER A N   1 
ATOM   1648 C  CA  . SER A 1 196 ? -2.912  2.763   23.659  1.00 7.40   ? 197 SER A CA  1 
ATOM   1649 C  C   . SER A 1 196 ? -3.369  2.352   22.266  1.00 6.61   ? 197 SER A C   1 
ATOM   1650 O  O   . SER A 1 196 ? -4.125  1.394   22.077  1.00 7.04   ? 197 SER A O   1 
ATOM   1651 C  CB  . SER A 1 196 ? -1.432  2.373   23.841  1.00 7.90   ? 197 SER A CB  1 
ATOM   1652 O  OG  . SER A 1 196 ? -1.183  1.029   23.404  1.00 7.56   ? 197 SER A OG  1 
ATOM   1653 N  N   . LEU A 1 197 ? -2.823  3.049   21.262  1.00 6.88   ? 198 LEU A N   1 
ATOM   1654 C  CA  . LEU A 1 197 ? -2.778  2.516   19.903  1.00 7.28   ? 198 LEU A CA  1 
ATOM   1655 C  C   . LEU A 1 197 ? -2.055  1.195   19.913  1.00 6.98   ? 198 LEU A C   1 
ATOM   1656 O  O   . LEU A 1 197 ? -1.033  1.023   20.631  1.00 7.70   ? 198 LEU A O   1 
ATOM   1657 C  CB  . LEU A 1 197 ? -2.036  3.516   19.016  1.00 8.21   ? 198 LEU A CB  1 
ATOM   1658 C  CG  . LEU A 1 197 ? -2.600  4.913   18.944  1.00 8.63   ? 198 LEU A CG  1 
ATOM   1659 C  CD1 . LEU A 1 197 ? -1.741  5.811   18.045  1.00 10.65  ? 198 LEU A CD1 1 
ATOM   1660 C  CD2 . LEU A 1 197 ? -4.007  4.948   18.493  1.00 10.05  ? 198 LEU A CD2 1 
ATOM   1661 N  N   . THR A 1 198 ? -2.507  0.222   19.105  1.00 7.14   ? 199 THR A N   1 
ATOM   1662 C  CA  . THR A 1 198 ? -1.861  -1.085  19.095  1.00 8.05   ? 199 THR A CA  1 
ATOM   1663 C  C   . THR A 1 198 ? -0.816  -1.224  17.988  1.00 7.74   ? 199 THR A C   1 
ATOM   1664 O  O   . THR A 1 198 ? -0.230  -2.312  17.845  1.00 9.01   ? 199 THR A O   1 
ATOM   1665 C  CB  . THR A 1 198 ? -2.912  -2.213  18.919  1.00 7.59   ? 199 THR A CB  1 
ATOM   1666 O  OG1 . THR A 1 198 ? -3.469  -2.094  17.622  1.00 7.55   ? 199 THR A OG1 1 
ATOM   1667 C  CG2 . THR A 1 198 ? -3.963  -2.190  20.034  1.00 8.07   ? 199 THR A CG2 1 
ATOM   1668 N  N   . THR A 1 199 ? -0.574  -0.189  17.214  1.00 8.41   ? 200 THR A N   1 
ATOM   1669 C  CA  . THR A 1 199 ? 0.505   -0.149  16.249  1.00 10.07  ? 200 THR A CA  1 
ATOM   1670 C  C   . THR A 1 199 ? 1.308   1.101   16.532  1.00 9.29   ? 200 THR A C   1 
ATOM   1671 O  O   . THR A 1 199 ? 0.810   2.055   17.127  1.00 8.94   ? 200 THR A O   1 
ATOM   1672 C  CB  . THR A 1 199 ? 0.053   -0.107  14.788  1.00 11.13  ? 200 THR A CB  1 
ATOM   1673 O  OG1 . THR A 1 199 ? -0.346  1.147   14.428  1.00 12.97  ? 200 THR A OG1 1 
ATOM   1674 C  CG2 . THR A 1 199 ? -1.078  -1.040  14.430  1.00 11.41  ? 200 THR A CG2 1 
ATOM   1675 N  N   . PRO A 1 200 ? 2.556   1.150   16.055  1.00 9.69   ? 201 PRO A N   1 
ATOM   1676 C  CA  . PRO A 1 200 ? 3.266   2.402   16.065  1.00 10.30  ? 201 PRO A CA  1 
ATOM   1677 C  C   . PRO A 1 200 ? 2.393   3.498   15.501  1.00 10.14  ? 201 PRO A C   1 
ATOM   1678 O  O   . PRO A 1 200 ? 1.711   3.315   14.503  1.00 10.98  ? 201 PRO A O   1 
ATOM   1679 C  CB  . PRO A 1 200 ? 4.482   2.088   15.168  1.00 11.65  ? 201 PRO A CB  1 
ATOM   1680 C  CG  . PRO A 1 200 ? 4.765   0.640   15.478  1.00 11.55  ? 201 PRO A CG  1 
ATOM   1681 C  CD  . PRO A 1 200 ? 3.382   0.073   15.427  1.00 11.41  ? 201 PRO A CD  1 
ATOM   1682 N  N   . PRO A 1 201 ? 2.398   4.684   16.139  1.00 10.07  ? 202 PRO A N   1 
ATOM   1683 C  CA  . PRO A 1 201 ? 3.317   5.133   17.202  1.00 10.86  ? 202 PRO A CA  1 
ATOM   1684 C  C   . PRO A 1 201 ? 2.958   4.741   18.661  1.00 9.77   ? 202 PRO A C   1 
ATOM   1685 O  O   . PRO A 1 201 ? 3.647   5.216   19.560  1.00 10.69  ? 202 PRO A O   1 
ATOM   1686 C  CB  . PRO A 1 201 ? 3.290   6.684   17.025  1.00 12.76  ? 202 PRO A CB  1 
ATOM   1687 C  CG  . PRO A 1 201 ? 1.859   6.952   16.558  1.00 12.80  ? 202 PRO A CG  1 
ATOM   1688 C  CD  . PRO A 1 201 ? 1.566   5.821   15.598  1.00 11.71  ? 202 PRO A CD  1 
ATOM   1689 N  N   . LEU A 1 202 ? 1.956   3.884   18.874  1.00 8.66   ? 203 LEU A N   1 
ATOM   1690 C  CA  . LEU A 1 202 ? 1.735   3.263   20.191  1.00 8.37   ? 203 LEU A CA  1 
ATOM   1691 C  C   . LEU A 1 202 ? 1.370   4.269   21.266  1.00 8.57   ? 203 LEU A C   1 
ATOM   1692 O  O   . LEU A 1 202 ? 1.503   4.017   22.465  1.00 8.69   ? 203 LEU A O   1 
ATOM   1693 C  CB  . LEU A 1 202 ? 2.932   2.384   20.648  1.00 9.22   ? 203 LEU A CB  1 
ATOM   1694 C  CG  . LEU A 1 202 ? 3.224   1.211   19.672  1.00 9.21   ? 203 LEU A CG  1 
ATOM   1695 C  CD1 . LEU A 1 202 ? 4.565   0.571   20.126  1.00 11.41  ? 203 LEU A CD1 1 
ATOM   1696 C  CD2 . LEU A 1 202 ? 2.135   0.140   19.686  1.00 9.60   ? 203 LEU A CD2 1 
ATOM   1697 N  N   . LEU A 1 203 ? 0.791   5.407   20.858  1.00 8.98   ? 204 LEU A N   1 
ATOM   1698 C  CA  . LEU A 1 203 ? 0.467   6.520   21.759  1.00 8.96   ? 204 LEU A CA  1 
ATOM   1699 C  C   . LEU A 1 203 ? -0.559  6.087   22.763  1.00 8.23   ? 204 LEU A C   1 
ATOM   1700 O  O   . LEU A 1 203 ? -1.534  5.361   22.464  1.00 8.51   ? 204 LEU A O   1 
ATOM   1701 C  CB  . LEU A 1 203 ? 0.018   7.712   20.974  1.00 10.31  ? 204 LEU A CB  1 
ATOM   1702 C  CG  . LEU A 1 203 ? 1.035   8.300   20.034  1.00 11.19  ? 204 LEU A CG  1 
ATOM   1703 C  CD1 . LEU A 1 203 ? 0.455   9.365   19.127  1.00 13.60  ? 204 LEU A CD1 1 
ATOM   1704 C  CD2 . LEU A 1 203 ? 2.250   8.896   20.809  1.00 15.38  ? 204 LEU A CD2 1 
ATOM   1705 N  N   . GLU A 1 204 ? -0.405  6.564   23.998  1.00 8.68   ? 205 GLU A N   1 
ATOM   1706 C  CA  . GLU A 1 204 ? -1.253  6.211   25.120  1.00 9.43   ? 205 GLU A CA  1 
ATOM   1707 C  C   . GLU A 1 204 ? -2.453  7.167   25.246  1.00 8.85   ? 205 GLU A C   1 
ATOM   1708 O  O   . GLU A 1 204 ? -2.544  7.941   26.184  1.00 11.13  ? 205 GLU A O   1 
ATOM   1709 C  CB  . GLU A 1 204 ? -0.413  6.058   26.405  1.00 10.07  ? 205 GLU A CB  1 
ATOM   1710 C  CG  . GLU A 1 204 ? 0.503   4.864   26.300  1.00 10.44  ? 205 GLU A CG  1 
ATOM   1711 C  CD  . GLU A 1 204 ? 1.410   4.570   27.464  1.00 10.68  ? 205 GLU A CD  1 
ATOM   1712 O  OE1 . GLU A 1 204 ? 1.733   5.506   28.220  1.00 13.17  ? 205 GLU A OE1 1 
ATOM   1713 O  OE2 . GLU A 1 204 ? 1.827   3.383   27.605  1.00 11.36  ? 205 GLU A OE2 1 
ATOM   1714 N  N   . CYS A 1 205 ? -3.339  7.071   24.287  1.00 8.44   ? 206 CYS A N   1 
ATOM   1715 C  CA  . CYS A 1 205 ? -4.379  8.049   24.049  1.00 8.13   ? 206 CYS A CA  1 
ATOM   1716 C  C   . CYS A 1 205 ? -5.750  7.434   23.963  1.00 8.04   ? 206 CYS A C   1 
ATOM   1717 O  O   . CYS A 1 205 ? -6.695  8.135   23.586  1.00 9.41   ? 206 CYS A O   1 
ATOM   1718 C  CB  . CYS A 1 205 ? -4.096  8.862   22.816  1.00 9.35   ? 206 CYS A CB  1 
ATOM   1719 S  SG  . CYS A 1 205 ? -4.018  7.872   21.279  1.00 9.67   ? 206 CYS A SG  1 
ATOM   1720 N  N   . VAL A 1 206 ? -5.897  6.134   24.232  1.00 7.51   ? 207 VAL A N   1 
ATOM   1721 C  CA  . VAL A 1 206 ? -7.125  5.416   23.898  1.00 7.47   ? 207 VAL A CA  1 
ATOM   1722 C  C   . VAL A 1 206 ? -7.899  4.972   25.152  1.00 7.37   ? 207 VAL A C   1 
ATOM   1723 O  O   . VAL A 1 206 ? -7.348  4.308   26.018  1.00 8.64   ? 207 VAL A O   1 
ATOM   1724 C  CB  . VAL A 1 206 ? -6.864  4.153   23.052  1.00 8.16   ? 207 VAL A CB  1 
ATOM   1725 C  CG1 . VAL A 1 206 ? -8.174  3.472   22.695  1.00 7.78   ? 207 VAL A CG1 1 
ATOM   1726 C  CG2 . VAL A 1 206 ? -6.106  4.525   21.759  1.00 8.67   ? 207 VAL A CG2 1 
ATOM   1727 N  N   . THR A 1 207 ? -9.188  5.280   25.181  1.00 7.04   ? 208 THR A N   1 
ATOM   1728 C  CA  . THR A 1 207 ? -10.149 4.561   26.030  1.00 7.46   ? 208 THR A CA  1 
ATOM   1729 C  C   . THR A 1 207 ? -10.671 3.382   25.204  1.00 7.19   ? 208 THR A C   1 
ATOM   1730 O  O   . THR A 1 207 ? -11.368 3.590   24.181  1.00 7.74   ? 208 THR A O   1 
ATOM   1731 C  CB  . THR A 1 207 ? -11.316 5.428   26.493  1.00 8.50   ? 208 THR A CB  1 
ATOM   1732 O  OG1 . THR A 1 207 ? -10.798 6.539   27.242  1.00 9.43   ? 208 THR A OG1 1 
ATOM   1733 C  CG2 . THR A 1 207 ? -12.253 4.587   27.374  1.00 9.84   ? 208 THR A CG2 1 
ATOM   1734 N  N   . TRP A 1 208 ? -10.318 2.147   25.603  1.00 6.81   ? 209 TRP A N   1 
ATOM   1735 C  CA  . TRP A 1 208 ? -10.757 0.972   24.898  1.00 6.64   ? 209 TRP A CA  1 
ATOM   1736 C  C   . TRP A 1 208 ? -12.130 0.566   25.433  1.00 6.53   ? 209 TRP A C   1 
ATOM   1737 O  O   . TRP A 1 208 ? -12.345 0.519   26.648  1.00 7.46   ? 209 TRP A O   1 
ATOM   1738 C  CB  . TRP A 1 208 ? -9.745  -0.180  25.090  1.00 7.12   ? 209 TRP A CB  1 
ATOM   1739 C  CG  . TRP A 1 208 ? -8.626  -0.062  24.143  1.00 6.46   ? 209 TRP A CG  1 
ATOM   1740 C  CD1 . TRP A 1 208 ? -7.386  0.506   24.338  1.00 7.40   ? 209 TRP A CD1 1 
ATOM   1741 C  CD2 . TRP A 1 208 ? -8.697  -0.451  22.771  1.00 6.44   ? 209 TRP A CD2 1 
ATOM   1742 N  NE1 . TRP A 1 208 ? -6.695  0.523   23.167  1.00 7.80   ? 209 TRP A NE1 1 
ATOM   1743 C  CE2 . TRP A 1 208 ? -7.438  -0.070  22.174  1.00 7.13   ? 209 TRP A CE2 1 
ATOM   1744 C  CE3 . TRP A 1 208 ? -9.660  -1.074  21.967  1.00 6.75   ? 209 TRP A CE3 1 
ATOM   1745 C  CZ2 . TRP A 1 208 ? -7.184  -0.286  20.815  1.00 8.03   ? 209 TRP A CZ2 1 
ATOM   1746 C  CZ3 . TRP A 1 208 ? -9.382  -1.315  20.651  1.00 7.98   ? 209 TRP A CZ3 1 
ATOM   1747 C  CH2 . TRP A 1 208 ? -8.180  -0.909  20.080  1.00 8.48   ? 209 TRP A CH2 1 
ATOM   1748 N  N   . ILE A 1 209 ? -13.035 0.208   24.501  1.00 6.64   ? 210 ILE A N   1 
ATOM   1749 C  CA  . ILE A 1 209 ? -14.356 -0.312  24.810  1.00 6.96   ? 210 ILE A CA  1 
ATOM   1750 C  C   . ILE A 1 209 ? -14.484 -1.568  23.976  1.00 6.76   ? 210 ILE A C   1 
ATOM   1751 O  O   . ILE A 1 209 ? -14.561 -1.482  22.752  1.00 8.16   ? 210 ILE A O   1 
ATOM   1752 C  CB  . ILE A 1 209 ? -15.443 0.716   24.470  1.00 7.81   ? 210 ILE A CB  1 
ATOM   1753 C  CG1 . ILE A 1 209 ? -15.224 1.985   25.300  1.00 9.57   ? 210 ILE A CG1 1 
ATOM   1754 C  CG2 . ILE A 1 209 ? -16.815 0.091   24.721  1.00 9.54   ? 210 ILE A CG2 1 
ATOM   1755 C  CD1 . ILE A 1 209 ? -16.043 3.188   24.828  1.00 11.66  ? 210 ILE A CD1 1 
ATOM   1756 N  N   . VAL A 1 210 ? -14.406 -2.737  24.628  1.00 6.84   ? 211 VAL A N   1 
ATOM   1757 C  CA  . VAL A 1 210 ? -14.396 -4.026  23.924  1.00 6.74   ? 211 VAL A CA  1 
ATOM   1758 C  C   . VAL A 1 210 ? -15.698 -4.720  24.181  1.00 7.18   ? 211 VAL A C   1 
ATOM   1759 O  O   . VAL A 1 210 ? -16.030 -5.008  25.330  1.00 7.72   ? 211 VAL A O   1 
ATOM   1760 C  CB  . VAL A 1 210 ? -13.175 -4.877  24.362  1.00 7.87   ? 211 VAL A CB  1 
ATOM   1761 C  CG1 . VAL A 1 210 ? -13.193 -6.232  23.667  1.00 9.29   ? 211 VAL A CG1 1 
ATOM   1762 C  CG2 . VAL A 1 210 ? -11.871 -4.123  24.078  1.00 9.37   ? 211 VAL A CG2 1 
ATOM   1763 N  N   . LEU A 1 211 ? -16.456 -5.004  23.120  1.00 7.76   ? 212 LEU A N   1 
ATOM   1764 C  CA  . LEU A 1 211 ? -17.748 -5.657  23.286  1.00 8.47   ? 212 LEU A CA  1 
ATOM   1765 C  C   . LEU A 1 211 ? -17.560 -7.146  23.655  1.00 8.11   ? 212 LEU A C   1 
ATOM   1766 O  O   . LEU A 1 211 ? -16.707 -7.837  23.124  1.00 8.64   ? 212 LEU A O   1 
ATOM   1767 C  CB  . LEU A 1 211 ? -18.568 -5.546  21.981  1.00 9.35   ? 212 LEU A CB  1 
ATOM   1768 C  CG  . LEU A 1 211 ? -18.947 -4.120  21.589  1.00 9.94   ? 212 LEU A CG  1 
ATOM   1769 C  CD1 . LEU A 1 211 ? -19.971 -4.196  20.414  1.00 12.20  ? 212 LEU A CD1 1 
ATOM   1770 C  CD2 . LEU A 1 211 ? -19.482 -3.296  22.740  1.00 11.45  ? 212 LEU A CD2 1 
ATOM   1771 N  N   A LYS A 1 212 ? -18.435 -7.599  24.564  0.50 9.32   ? 213 LYS A N   1 
ATOM   1772 N  N   B LYS A 1 212 ? -18.435 -7.598  24.564  0.50 9.33   ? 213 LYS A N   1 
ATOM   1773 C  CA  A LYS A 1 212 ? -18.390 -8.999  24.960  0.50 10.12  ? 213 LYS A CA  1 
ATOM   1774 C  CA  B LYS A 1 212 ? -18.391 -8.992  24.961  0.50 10.12  ? 213 LYS A CA  1 
ATOM   1775 C  C   A LYS A 1 212 ? -18.874 -9.925  23.869  0.50 9.32   ? 213 LYS A C   1 
ATOM   1776 C  C   B LYS A 1 212 ? -18.874 -9.923  23.870  0.50 9.32   ? 213 LYS A C   1 
ATOM   1777 O  O   A LYS A 1 212 ? -18.336 -11.036 23.748  0.50 11.65  ? 213 LYS A O   1 
ATOM   1778 O  O   B LYS A 1 212 ? -18.336 -11.035 23.748  0.50 11.65  ? 213 LYS A O   1 
ATOM   1779 C  CB  A LYS A 1 212 ? -19.190 -9.221  26.233  0.50 12.95  ? 213 LYS A CB  1 
ATOM   1780 C  CB  B LYS A 1 212 ? -19.181 -9.224  26.239  0.50 12.97  ? 213 LYS A CB  1 
ATOM   1781 C  CG  A LYS A 1 212 ? -19.288 -10.682 26.683  0.50 16.64  ? 213 LYS A CG  1 
ATOM   1782 C  CG  B LYS A 1 212 ? -19.294 -10.717 26.561  0.50 16.63  ? 213 LYS A CG  1 
ATOM   1783 C  CD  A LYS A 1 212 ? -20.123 -10.811 27.926  0.50 23.77  ? 213 LYS A CD  1 
ATOM   1784 C  CD  B LYS A 1 212 ? -19.775 -11.069 27.937  0.50 20.18  ? 213 LYS A CD  1 
ATOM   1785 C  CE  A LYS A 1 212 ? -20.054 -12.180 28.550  0.50 27.26  ? 213 LYS A CE  1 
ATOM   1786 C  CE  B LYS A 1 212 ? -21.051 -10.305 28.271  0.50 29.64  ? 213 LYS A CE  1 
ATOM   1787 N  NZ  A LYS A 1 212 ? -21.102 -12.298 29.610  0.50 34.46  ? 213 LYS A NZ  1 
ATOM   1788 N  NZ  B LYS A 1 212 ? -22.149 -10.088 27.304  0.50 31.44  ? 213 LYS A NZ  1 
ATOM   1789 N  N   . GLU A 1 213 ? -19.879 -9.534  23.105  1.00 9.15   ? 214 GLU A N   1 
ATOM   1790 C  CA  . GLU A 1 213 ? -20.499 -10.439 22.115  1.00 9.78   ? 214 GLU A CA  1 
ATOM   1791 C  C   . GLU A 1 213 ? -19.737 -10.314 20.818  1.00 9.12   ? 214 GLU A C   1 
ATOM   1792 O  O   . GLU A 1 213 ? -19.657 -9.230  20.239  1.00 9.65   ? 214 GLU A O   1 
ATOM   1793 C  CB  . GLU A 1 213 ? -21.937 -10.078 21.888  1.00 10.48  ? 214 GLU A CB  1 
ATOM   1794 C  CG  . GLU A 1 213 ? -22.622 -11.024 20.940  1.00 13.31  ? 214 GLU A CG  1 
ATOM   1795 C  CD  . GLU A 1 213 ? -24.082 -10.791 20.726  1.00 17.18  ? 214 GLU A CD  1 
ATOM   1796 O  OE1 . GLU A 1 213 ? -24.702 -9.942  21.364  1.00 17.22  ? 214 GLU A OE1 1 
ATOM   1797 O  OE2 . GLU A 1 213 ? -24.614 -11.569 19.922  1.00 33.36  ? 214 GLU A OE2 1 
ATOM   1798 N  N   . PRO A 1 214 ? -19.143 -11.415 20.304  1.00 9.63   ? 215 PRO A N   1 
ATOM   1799 C  CA  . PRO A 1 214 ? -18.519 -11.381 18.975  1.00 10.00  ? 215 PRO A CA  1 
ATOM   1800 C  C   . PRO A 1 214 ? -19.550 -11.317 17.874  1.00 9.58   ? 215 PRO A C   1 
ATOM   1801 O  O   . PRO A 1 214 ? -20.703 -11.731 18.071  1.00 12.45  ? 215 PRO A O   1 
ATOM   1802 C  CB  . PRO A 1 214 ? -17.746 -12.705 18.910  1.00 10.72  ? 215 PRO A CB  1 
ATOM   1803 C  CG  . PRO A 1 214 ? -18.630 -13.648 19.715  1.00 15.43  ? 215 PRO A CG  1 
ATOM   1804 C  CD  . PRO A 1 214 ? -19.091 -12.780 20.899  1.00 11.78  ? 215 PRO A CD  1 
ATOM   1805 N  N   . ILE A 1 215 ? -19.119 -10.885 16.715  1.00 9.85   ? 216 ILE A N   1 
ATOM   1806 C  CA  . ILE A 1 215 ? -19.926 -11.097 15.489  1.00 10.45  ? 216 ILE A CA  1 
ATOM   1807 C  C   . ILE A 1 215 ? -19.401 -12.379 14.818  1.00 9.90   ? 216 ILE A C   1 
ATOM   1808 O  O   . ILE A 1 215 ? -18.226 -12.718 14.925  1.00 11.33  ? 216 ILE A O   1 
ATOM   1809 C  CB  . ILE A 1 215 ? -19.950 -9.905  14.572  1.00 10.75  ? 216 ILE A CB  1 
ATOM   1810 C  CG1 . ILE A 1 215 ? -18.563 -9.517  14.060  1.00 11.91  ? 216 ILE A CG1 1 
ATOM   1811 C  CG2 . ILE A 1 215 ? -20.630 -8.708  15.246  1.00 13.58  ? 216 ILE A CG2 1 
ATOM   1812 C  CD1 . ILE A 1 215 ? -18.546 -8.541  12.875  1.00 15.06  ? 216 ILE A CD1 1 
ATOM   1813 N  N   A SER A 1 216 ? -20.322 -13.091 14.170  0.50 10.79  ? 217 SER A N   1 
ATOM   1814 N  N   B SER A 1 216 ? -20.237 -12.985 13.990  0.50 11.50  ? 217 SER A N   1 
ATOM   1815 C  CA  A SER A 1 216 ? -19.980 -14.170 13.227  0.50 11.16  ? 217 SER A CA  1 
ATOM   1816 C  CA  B SER A 1 216 ? -19.810 -14.168 13.289  0.50 11.91  ? 217 SER A CA  1 
ATOM   1817 C  C   A SER A 1 216 ? -19.711 -13.690 11.807  0.50 10.48  ? 217 SER A C   1 
ATOM   1818 C  C   B SER A 1 216 ? -19.728 -13.773 11.838  0.50 11.38  ? 217 SER A C   1 
ATOM   1819 O  O   A SER A 1 216 ? -20.491 -12.903 11.251  0.50 11.74  ? 217 SER A O   1 
ATOM   1820 O  O   B SER A 1 216 ? -20.641 -13.079 11.319  0.50 12.96  ? 217 SER A O   1 
ATOM   1821 C  CB  A SER A 1 216 ? -21.088 -15.231 13.240  0.50 13.03  ? 217 SER A CB  1 
ATOM   1822 C  CB  B SER A 1 216 ? -20.828 -15.292 13.518  0.50 17.20  ? 217 SER A CB  1 
ATOM   1823 O  OG  A SER A 1 216 ? -21.071 -15.875 14.509  0.50 12.78  ? 217 SER A OG  1 
ATOM   1824 O  OG  B SER A 1 216 ? -20.613 -16.368 12.632  0.50 19.51  ? 217 SER A OG  1 
ATOM   1825 N  N   . VAL A 1 217 ? -18.610 -14.172 11.217  1.00 11.06  ? 218 VAL A N   1 
ATOM   1826 C  CA  . VAL A 1 217 ? -18.350 -13.985 9.774   1.00 11.69  ? 218 VAL A CA  1 
ATOM   1827 C  C   . VAL A 1 217 ? -18.114 -15.340 9.183   1.00 10.81  ? 218 VAL A C   1 
ATOM   1828 O  O   . VAL A 1 217 ? -17.739 -16.299 9.903   1.00 12.05  ? 218 VAL A O   1 
ATOM   1829 C  CB  . VAL A 1 217 ? -17.147 -13.051 9.570   1.00 12.23  ? 218 VAL A CB  1 
ATOM   1830 C  CG1 . VAL A 1 217 ? -17.439 -11.712 10.230  1.00 13.29  ? 218 VAL A CG1 1 
ATOM   1831 C  CG2 . VAL A 1 217 ? -15.876 -13.667 10.085  1.00 13.98  ? 218 VAL A CG2 1 
ATOM   1832 N  N   . SER A 1 218 ? -18.261 -15.499 7.903   1.00 11.59  ? 219 SER A N   1 
ATOM   1833 C  CA  . SER A 1 218 ? -18.034 -16.841 7.333   1.00 12.48  ? 219 SER A CA  1 
ATOM   1834 C  C   . SER A 1 218 ? -16.559 -17.067 7.054   1.00 11.54  ? 219 SER A C   1 
ATOM   1835 O  O   . SER A 1 218 ? -15.728 -16.130 6.920   1.00 12.29  ? 219 SER A O   1 
ATOM   1836 C  CB  . SER A 1 218 ? -18.816 -16.993 6.044   1.00 13.19  ? 219 SER A CB  1 
ATOM   1837 O  OG  . SER A 1 218 ? -18.306 -16.148 5.054   1.00 14.73  ? 219 SER A OG  1 
ATOM   1838 N  N   A SER A 1 219 ? -16.208 -18.342 6.880   0.50 13.20  ? 220 SER A N   1 
ATOM   1839 N  N   B SER A 1 219 ? -16.266 -18.340 6.895   0.50 12.77  ? 220 SER A N   1 
ATOM   1840 C  CA  A SER A 1 219 ? -14.814 -18.674 6.488   0.50 12.47  ? 220 SER A CA  1 
ATOM   1841 C  CA  B SER A 1 219 ? -14.912 -18.696 6.582   0.50 13.51  ? 220 SER A CA  1 
ATOM   1842 C  C   A SER A 1 219 ? -14.479 -18.002 5.192   0.50 13.71  ? 220 SER A C   1 
ATOM   1843 C  C   B SER A 1 219 ? -14.523 -18.044 5.252   0.50 14.15  ? 220 SER A C   1 
ATOM   1844 O  O   A SER A 1 219 ? -13.362 -17.516 5.003   0.50 14.13  ? 220 SER A O   1 
ATOM   1845 O  O   B SER A 1 219 ? -13.394 -17.588 5.126   0.50 14.72  ? 220 SER A O   1 
ATOM   1846 C  CB  A SER A 1 219 ? -14.679 -20.164 6.272   0.50 14.21  ? 220 SER A CB  1 
ATOM   1847 C  CB  B SER A 1 219 ? -14.813 -20.198 6.536   0.50 15.34  ? 220 SER A CB  1 
ATOM   1848 O  OG  A SER A 1 219 ? -15.712 -20.739 5.503   0.50 15.00  ? 220 SER A OG  1 
ATOM   1849 O  OG  B SER A 1 219 ? -13.484 -20.575 6.217   0.50 16.35  ? 220 SER A OG  1 
ATOM   1850 N  N   . GLU A 1 220 ? -15.435 -17.920 4.273   1.00 13.53  ? 221 GLU A N   1 
ATOM   1851 C  CA  . GLU A 1 220 ? -15.103 -17.303 3.016   1.00 15.72  ? 221 GLU A CA  1 
ATOM   1852 C  C   . GLU A 1 220 ? -14.846 -15.810 3.165   1.00 13.29  ? 221 GLU A C   1 
ATOM   1853 O  O   . GLU A 1 220 ? -13.992 -15.281 2.438   1.00 15.97  ? 221 GLU A O   1 
ATOM   1854 C  CB  . GLU A 1 220 ? -16.214 -17.474 2.007   1.00 18.06  ? 221 GLU A CB  1 
ATOM   1855 C  CG  . GLU A 1 220 ? -16.390 -18.959 1.587   1.00 23.13  ? 221 GLU A CG  1 
ATOM   1856 C  CD  . GLU A 1 220 ? -17.315 -19.768 2.516   1.00 25.83  ? 221 GLU A CD  1 
ATOM   1857 O  OE1 . GLU A 1 220 ? -17.790 -19.313 3.568   1.00 24.81  ? 221 GLU A OE1 1 
ATOM   1858 O  OE2 . GLU A 1 220 ? -17.542 -20.962 2.219   1.00 62.12  ? 221 GLU A OE2 1 
ATOM   1859 N  N   . GLN A 1 221 ? -15.539 -15.145 4.047   1.00 13.09  ? 222 GLN A N   1 
ATOM   1860 C  CA  . GLN A 1 221 ? -15.298 -13.715 4.284   1.00 12.80  ? 222 GLN A CA  1 
ATOM   1861 C  C   . GLN A 1 221 ? -13.884 -13.491 4.829   1.00 11.77  ? 222 GLN A C   1 
ATOM   1862 O  O   . GLN A 1 221 ? -13.124 -12.644 4.319   1.00 13.69  ? 222 GLN A O   1 
ATOM   1863 C  CB  . GLN A 1 221 ? -16.365 -13.156 5.193   1.00 13.09  ? 222 GLN A CB  1 
ATOM   1864 C  CG  . GLN A 1 221 ? -17.733 -13.023 4.528   1.00 13.22  ? 222 GLN A CG  1 
ATOM   1865 C  CD  . GLN A 1 221 ? -18.854 -12.502 5.390   1.00 13.03  ? 222 GLN A CD  1 
ATOM   1866 O  OE1 . GLN A 1 221 ? -18.982 -12.867 6.561   1.00 12.50  ? 222 GLN A OE1 1 
ATOM   1867 N  NE2 . GLN A 1 221 ? -19.670 -11.598 4.806   1.00 13.61  ? 222 GLN A NE2 1 
ATOM   1868 N  N   . VAL A 1 222 ? -13.471 -14.244 5.861   1.00 12.66  ? 223 VAL A N   1 
ATOM   1869 C  CA  . VAL A 1 222 ? -12.120 -14.011 6.431   1.00 13.78  ? 223 VAL A CA  1 
ATOM   1870 C  C   . VAL A 1 222 ? -11.086 -14.487 5.455   1.00 13.17  ? 223 VAL A C   1 
ATOM   1871 O  O   . VAL A 1 222 ? -9.981  -13.893 5.368   1.00 13.53  ? 223 VAL A O   1 
ATOM   1872 C  CB  . VAL A 1 222 ? -11.994 -14.567 7.852   1.00 15.58  ? 223 VAL A CB  1 
ATOM   1873 C  CG1 . VAL A 1 222 ? -11.963 -16.075 7.894   1.00 19.04  ? 223 VAL A CG1 1 
ATOM   1874 C  CG2 . VAL A 1 222 ? -10.792 -13.989 8.579   1.00 18.84  ? 223 VAL A CG2 1 
ATOM   1875 N  N   . LEU A 1 223 ? -11.376 -15.484 4.651   1.00 13.95  ? 224 LEU A N   1 
ATOM   1876 C  CA  . LEU A 1 223 ? -10.418 -15.889 3.666   1.00 16.74  ? 224 LEU A CA  1 
ATOM   1877 C  C   . LEU A 1 223 ? -10.092 -14.789 2.698   1.00 14.89  ? 224 LEU A C   1 
ATOM   1878 O  O   . LEU A 1 223 ? -8.924  -14.620 2.257   1.00 16.00  ? 224 LEU A O   1 
ATOM   1879 C  CB  . LEU A 1 223 ? -10.865 -17.164 2.936   1.00 19.07  ? 224 LEU A CB  1 
ATOM   1880 C  CG  . LEU A 1 223 ? -10.645 -18.484 3.679   1.00 21.80  ? 224 LEU A CG  1 
ATOM   1881 C  CD1 . LEU A 1 223 ? -11.582 -19.541 3.091   1.00 24.76  ? 224 LEU A CD1 1 
ATOM   1882 C  CD2 . LEU A 1 223 ? -9.171  -18.893 3.659   1.00 27.19  ? 224 LEU A CD2 1 
ATOM   1883 N  N   . LYS A 1 224 ? -11.034 -13.921 2.367   1.00 14.19  ? 225 LYS A N   1 
ATOM   1884 C  CA  . LYS A 1 224 ? -10.781 -12.835 1.459   1.00 15.26  ? 225 LYS A CA  1 
ATOM   1885 C  C   . LYS A 1 224 ? -9.934  -11.764 2.143   1.00 13.46  ? 225 LYS A C   1 
ATOM   1886 O  O   . LYS A 1 224 ? -9.149  -11.109 1.467   1.00 14.39  ? 225 LYS A O   1 
ATOM   1887 C  CB  . LYS A 1 224 ? -12.084 -12.319 0.899   1.00 17.65  ? 225 LYS A CB  1 
ATOM   1888 C  CG  . LYS A 1 224 ? -12.598 -13.332 -0.158  1.00 21.20  ? 225 LYS A CG  1 
ATOM   1889 C  CD  . LYS A 1 224 ? -13.740 -12.894 -1.024  1.00 31.73  ? 225 LYS A CD  1 
ATOM   1890 C  CE  . LYS A 1 224 ? -14.318 -14.014 -1.926  1.00 36.75  ? 225 LYS A CE  1 
ATOM   1891 N  NZ  . LYS A 1 224 ? -15.343 -13.322 -2.743  1.00 79.71  ? 225 LYS A NZ  1 
ATOM   1892 N  N   . PHE A 1 225 ? -10.009 -11.565 3.455   1.00 12.51  ? 226 PHE A N   1 
ATOM   1893 C  CA  . PHE A 1 225 ? -9.109  -10.653 4.144   1.00 12.74  ? 226 PHE A CA  1 
ATOM   1894 C  C   . PHE A 1 225 ? -7.662  -11.129 3.918   1.00 12.47  ? 226 PHE A C   1 
ATOM   1895 O  O   . PHE A 1 225 ? -6.728  -10.348 3.719   1.00 12.55  ? 226 PHE A O   1 
ATOM   1896 C  CB  . PHE A 1 225 ? -9.299  -10.726 5.667   1.00 11.70  ? 226 PHE A CB  1 
ATOM   1897 C  CG  . PHE A 1 225 ? -10.513 -10.004 6.238   1.00 12.14  ? 226 PHE A CG  1 
ATOM   1898 C  CD1 . PHE A 1 225 ? -11.608 -9.638  5.474   1.00 14.67  ? 226 PHE A CD1 1 
ATOM   1899 C  CD2 . PHE A 1 225 ? -10.545 -9.752  7.599   1.00 14.12  ? 226 PHE A CD2 1 
ATOM   1900 C  CE1 . PHE A 1 225 ? -12.699 -9.008  6.074   1.00 16.69  ? 226 PHE A CE1 1 
ATOM   1901 C  CE2 . PHE A 1 225 ? -11.634 -9.130  8.196   1.00 15.10  ? 226 PHE A CE2 1 
ATOM   1902 C  CZ  . PHE A 1 225 ? -12.718 -8.761  7.434   1.00 16.78  ? 226 PHE A CZ  1 
ATOM   1903 N  N   . ARG A 1 226 ? -7.478  -12.451 3.964   1.00 12.35  ? 227 ARG A N   1 
ATOM   1904 C  CA  . ARG A 1 226 ? -6.155  -13.035 3.902   1.00 13.21  ? 227 ARG A CA  1 
ATOM   1905 C  C   . ARG A 1 226 ? -5.542  -13.046 2.501   1.00 14.19  ? 227 ARG A C   1 
ATOM   1906 O  O   . ARG A 1 226 ? -4.394  -13.459 2.368   1.00 14.61  ? 227 ARG A O   1 
ATOM   1907 C  CB  . ARG A 1 226 ? -6.159  -14.512 4.436   1.00 13.86  ? 227 ARG A CB  1 
ATOM   1908 C  CG  . ARG A 1 226 ? -6.639  -14.625 5.870   1.00 13.07  ? 227 ARG A CG  1 
ATOM   1909 C  CD  . ARG A 1 226 ? -6.526  -16.054 6.355   1.00 14.46  ? 227 ARG A CD  1 
ATOM   1910 N  NE  . ARG A 1 226 ? -7.110  -16.242 7.652   1.00 12.63  ? 227 ARG A NE  1 
ATOM   1911 C  CZ  . ARG A 1 226 ? -8.072  -17.112 7.963   1.00 14.42  ? 227 ARG A CZ  1 
ATOM   1912 N  NH1 . ARG A 1 226 ? -8.499  -17.981 7.057   1.00 17.27  ? 227 ARG A NH1 1 
ATOM   1913 N  NH2 . ARG A 1 226 ? -8.626  -17.071 9.159   1.00 14.58  ? 227 ARG A NH2 1 
ATOM   1914 N  N   . LYS A 1 227 ? -6.288  -12.593 1.491   1.00 14.09  ? 228 LYS A N   1 
ATOM   1915 C  CA  . LYS A 1 227 ? -5.755  -12.475 0.125   1.00 15.71  ? 228 LYS A CA  1 
ATOM   1916 C  C   . LYS A 1 227 ? -5.141  -11.077 -0.123  1.00 14.09  ? 228 LYS A C   1 
ATOM   1917 O  O   . LYS A 1 227 ? -4.511  -10.844 -1.153  1.00 16.58  ? 228 LYS A O   1 
ATOM   1918 C  CB  . LYS A 1 227 ? -6.892  -12.728 -0.869  1.00 16.81  ? 228 LYS A CB  1 
ATOM   1919 C  CG  . LYS A 1 227 ? -7.279  -14.177 -0.921  1.00 20.17  ? 228 LYS A CG  1 
ATOM   1920 C  CD  . LYS A 1 227 ? -8.384  -14.301 -1.931  1.00 28.79  ? 228 LYS A CD  1 
ATOM   1921 C  CE  . LYS A 1 227 ? -7.922  -14.307 -3.381  1.00 36.19  ? 228 LYS A CE  1 
ATOM   1922 N  NZ  . LYS A 1 227 ? -8.778  -15.106 -4.319  1.00 56.42  ? 228 LYS A NZ  1 
ATOM   1923 N  N   . LEU A 1 228 ? -5.347  -10.143 0.802   1.00 13.60  ? 229 LEU A N   1 
ATOM   1924 C  CA  . LEU A 1 228 ? -4.761  -8.848  0.719   1.00 13.63  ? 229 LEU A CA  1 
ATOM   1925 C  C   . LEU A 1 228 ? -3.265  -8.990  0.833   1.00 14.19  ? 229 LEU A C   1 
ATOM   1926 O  O   . LEU A 1 228 ? -2.690  -10.065 1.266   1.00 13.49  ? 229 LEU A O   1 
ATOM   1927 C  CB  . LEU A 1 228 ? -5.287  -7.860  1.796   1.00 14.19  ? 229 LEU A CB  1 
ATOM   1928 C  CG  . LEU A 1 228 ? -6.724  -7.448  1.577   1.00 14.40  ? 229 LEU A CG  1 
ATOM   1929 C  CD1 . LEU A 1 228 ? -7.191  -6.837  2.879   1.00 15.33  ? 229 LEU A CD1 1 
ATOM   1930 C  CD2 . LEU A 1 228 ? -6.835  -6.456  0.438   1.00 17.48  ? 229 LEU A CD2 1 
ATOM   1931 N  N   . ASN A 1 229 ? -2.539  -7.951  0.466   1.00 13.77  ? 230 ASN A N   1 
ATOM   1932 C  CA  . ASN A 1 229 ? -1.114  -7.994  0.500   1.00 13.49  ? 230 ASN A CA  1 
ATOM   1933 C  C   . ASN A 1 229 ? -0.529  -6.758  1.304   1.00 13.56  ? 230 ASN A C   1 
ATOM   1934 O  O   . ASN A 1 229 ? -1.046  -5.631  1.256   1.00 14.74  ? 230 ASN A O   1 
ATOM   1935 C  CB  . ASN A 1 229 ? -0.506  -7.788  -0.925  1.00 14.57  ? 230 ASN A CB  1 
ATOM   1936 C  CG  . ASN A 1 229 ? -0.538  -8.974  -1.852  1.00 15.88  ? 230 ASN A CG  1 
ATOM   1937 O  OD1 . ASN A 1 229 ? -0.021  -8.803  -2.968  1.00 18.64  ? 230 ASN A OD1 1 
ATOM   1938 N  ND2 . ASN A 1 229 ? -1.103  -10.130 -1.459  1.00 16.60  ? 230 ASN A ND2 1 
ATOM   1939 N  N   . PHE A 1 230 ? 0.526   -7.108  2.087   1.00 13.58  ? 231 PHE A N   1 
ATOM   1940 C  CA  . PHE A 1 230 ? 1.292   -6.021  2.772   1.00 12.83  ? 231 PHE A CA  1 
ATOM   1941 C  C   . PHE A 1 230 ? 2.117   -5.232  1.769   1.00 14.69  ? 231 PHE A C   1 
ATOM   1942 O  O   . PHE A 1 230 ? 2.392   -4.062  2.045   1.00 16.03  ? 231 PHE A O   1 
ATOM   1943 C  CB  . PHE A 1 230 ? 2.301   -6.622  3.745   1.00 13.96  ? 231 PHE A CB  1 
ATOM   1944 C  CG  . PHE A 1 230 ? 1.715   -7.219  5.035   1.00 12.93  ? 231 PHE A CG  1 
ATOM   1945 C  CD1 . PHE A 1 230 ? 1.041   -6.450  5.978   1.00 14.93  ? 231 PHE A CD1 1 
ATOM   1946 C  CD2 . PHE A 1 230 ? 2.049   -8.508  5.410   1.00 14.99  ? 231 PHE A CD2 1 
ATOM   1947 C  CE1 . PHE A 1 230 ? 0.614   -7.000  7.175   1.00 14.59  ? 231 PHE A CE1 1 
ATOM   1948 C  CE2 . PHE A 1 230 ? 1.604   -9.067  6.592   1.00 14.31  ? 231 PHE A CE2 1 
ATOM   1949 C  CZ  . PHE A 1 230 ? 0.933   -8.305  7.504   1.00 13.36  ? 231 PHE A CZ  1 
ATOM   1950 N  N   . ASN A 1 231 ? 2.621   -5.867  0.734   1.00 14.24  ? 232 ASN A N   1 
ATOM   1951 C  CA  . ASN A 1 231 ? 3.460   -5.227  -0.287  1.00 15.90  ? 232 ASN A CA  1 
ATOM   1952 C  C   . ASN A 1 231 ? 2.630   -4.377  -1.211  1.00 13.42  ? 232 ASN A C   1 
ATOM   1953 O  O   . ASN A 1 231 ? 1.437   -4.422  -1.393  1.00 15.63  ? 232 ASN A O   1 
ATOM   1954 C  CB  . ASN A 1 231 ? 4.141   -6.308  -1.064  1.00 16.97  ? 232 ASN A CB  1 
ATOM   1955 C  CG  . ASN A 1 231 ? 3.118   -7.240  -1.645  1.00 14.94  ? 232 ASN A CG  1 
ATOM   1956 O  OD1 . ASN A 1 231 ? 2.656   -8.132  -0.941  1.00 17.97  ? 232 ASN A OD1 1 
ATOM   1957 N  ND2 . ASN A 1 231 ? 2.794   -7.105  -2.945  1.00 18.50  ? 232 ASN A ND2 1 
ATOM   1958 N  N   . GLY A 1 232 ? 3.434   -3.479  -1.853  1.00 18.10  ? 233 GLY A N   1 
ATOM   1959 C  CA  . GLY A 1 232 ? 2.825   -2.691  -2.986  1.00 18.14  ? 233 GLY A CA  1 
ATOM   1960 C  C   . GLY A 1 232 ? 2.820   -3.484  -4.307  1.00 16.11  ? 233 GLY A C   1 
ATOM   1961 O  O   . GLY A 1 232 ? 3.504   -4.505  -4.395  1.00 18.86  ? 233 GLY A O   1 
ATOM   1962 N  N   . GLU A 1 233 ? 2.090   -2.970  -5.272  1.00 16.56  ? 234 GLU A N   1 
ATOM   1963 C  CA  . GLU A 1 233 ? 2.007   -3.563  -6.607  1.00 14.97  ? 234 GLU A CA  1 
ATOM   1964 C  C   . GLU A 1 233 ? 3.403   -3.669  -7.202  1.00 17.90  ? 234 GLU A C   1 
ATOM   1965 O  O   . GLU A 1 233 ? 4.196   -2.757  -7.101  1.00 19.74  ? 234 GLU A O   1 
ATOM   1966 C  CB  . GLU A 1 233 ? 1.135   -2.735  -7.510  1.00 17.62  ? 234 GLU A CB  1 
ATOM   1967 C  CG  . GLU A 1 233 ? 0.831   -3.351  -8.854  1.00 19.24  ? 234 GLU A CG  1 
ATOM   1968 C  CD  . GLU A 1 233 ? 0.030   -2.411  -9.734  1.00 25.12  ? 234 GLU A CD  1 
ATOM   1969 O  OE1 . GLU A 1 233 ? -0.278  -1.291  -9.273  1.00 26.04  ? 234 GLU A OE1 1 
ATOM   1970 O  OE2 . GLU A 1 233 ? -0.292  -2.785  -10.881 1.00 26.92  ? 234 GLU A OE2 1 
ATOM   1971 N  N   . GLY A 1 234 ? 3.665   -4.829  -7.827  1.00 21.61  ? 235 GLY A N   1 
ATOM   1972 C  CA  . GLY A 1 234 ? 4.951   -5.025  -8.499  1.00 22.65  ? 235 GLY A CA  1 
ATOM   1973 C  C   . GLY A 1 234 ? 6.084   -5.420  -7.547  1.00 24.52  ? 235 GLY A C   1 
ATOM   1974 O  O   . GLY A 1 234 ? 7.249   -5.507  -7.955  1.00 29.34  ? 235 GLY A O   1 
ATOM   1975 N  N   . GLU A 1 235 ? 5.745   -5.723  -6.288  1.00 21.16  ? 236 GLU A N   1 
ATOM   1976 C  CA  . GLU A 1 235 ? 6.700   -6.300  -5.321  1.00 18.51  ? 236 GLU A CA  1 
ATOM   1977 C  C   . GLU A 1 235 ? 6.349   -7.726  -4.971  1.00 21.71  ? 236 GLU A C   1 
ATOM   1978 O  O   . GLU A 1 235 ? 5.198   -8.184  -5.185  1.00 26.09  ? 236 GLU A O   1 
ATOM   1979 C  CB  . GLU A 1 235 ? 6.663   -5.508  -3.986  1.00 20.86  ? 236 GLU A CB  1 
ATOM   1980 C  CG  . GLU A 1 235 ? 7.141   -4.060  -4.128  1.00 22.75  ? 236 GLU A CG  1 
ATOM   1981 C  CD  . GLU A 1 235 ? 6.905   -3.186  -2.898  1.00 28.64  ? 236 GLU A CD  1 
ATOM   1982 O  OE1 . GLU A 1 235 ? 6.319   -3.667  -1.872  1.00 32.02  ? 236 GLU A OE1 1 
ATOM   1983 O  OE2 . GLU A 1 235 ? 7.333   -2.021  -2.997  1.00 44.85  ? 236 GLU A OE2 1 
ATOM   1984 N  N   . PRO A 1 236 ? 7.333   -8.414  -4.404  1.00 20.52  ? 237 PRO A N   1 
ATOM   1985 C  CA  . PRO A 1 236 ? 7.079   -9.813  -4.082  1.00 21.65  ? 237 PRO A CA  1 
ATOM   1986 C  C   . PRO A 1 236 ? 5.925   -9.952  -3.111  1.00 21.18  ? 237 PRO A C   1 
ATOM   1987 O  O   . PRO A 1 236 ? 5.793   -9.160  -2.150  1.00 21.22  ? 237 PRO A O   1 
ATOM   1988 C  CB  . PRO A 1 236 ? 8.349   -10.207 -3.389  1.00 23.66  ? 237 PRO A CB  1 
ATOM   1989 C  CG  . PRO A 1 236 ? 9.439   -9.378  -4.053  1.00 30.90  ? 237 PRO A CG  1 
ATOM   1990 C  CD  . PRO A 1 236 ? 8.748   -8.060  -4.143  1.00 27.66  ? 237 PRO A CD  1 
ATOM   1991 N  N   . GLU A 1 237 ? 5.062   -10.944 -3.292  1.00 20.57  ? 238 GLU A N   1 
ATOM   1992 C  CA  . GLU A 1 237 ? 3.865   -10.970 -2.545  1.00 19.17  ? 238 GLU A CA  1 
ATOM   1993 C  C   . GLU A 1 237 ? 4.045   -11.418 -1.106  1.00 17.86  ? 238 GLU A C   1 
ATOM   1994 O  O   . GLU A 1 237 ? 4.644   -12.448 -0.857  1.00 16.37  ? 238 GLU A O   1 
ATOM   1995 C  CB  . GLU A 1 237 ? 2.944   -12.014 -3.187  1.00 20.66  ? 238 GLU A CB  1 
ATOM   1996 C  CG  . GLU A 1 237 ? 1.598   -11.969 -2.531  1.00 25.01  ? 238 GLU A CG  1 
ATOM   1997 C  CD  . GLU A 1 237 ? 0.529   -12.768 -3.252  1.00 24.43  ? 238 GLU A CD  1 
ATOM   1998 O  OE1 . GLU A 1 237 ? 0.907   -13.781 -3.920  1.00 52.76  ? 238 GLU A OE1 1 
ATOM   1999 O  OE2 . GLU A 1 237 ? -0.675  -12.381 -3.238  1.00 21.58  ? 238 GLU A OE2 1 
ATOM   2000 N  N   . GLU A 1 238 ? 3.517   -10.669 -0.165  1.00 16.32  ? 239 GLU A N   1 
ATOM   2001 C  CA  . GLU A 1 238 ? 3.449   -10.965 1.257   1.00 15.72  ? 239 GLU A CA  1 
ATOM   2002 C  C   . GLU A 1 238 ? 2.056   -10.888 1.689   1.00 13.96  ? 239 GLU A C   1 
ATOM   2003 O  O   . GLU A 1 238 ? 1.492   -9.778  1.781   1.00 16.68  ? 239 GLU A O   1 
ATOM   2004 C  CB  . GLU A 1 238 ? 4.224   -9.888  2.034   1.00 16.57  ? 239 GLU A CB  1 
ATOM   2005 C  CG  . GLU A 1 238 ? 5.645   -9.707  1.583   1.00 20.41  ? 239 GLU A CG  1 
ATOM   2006 C  CD  . GLU A 1 238 ? 6.402   -8.605  2.318   1.00 31.66  ? 239 GLU A CD  1 
ATOM   2007 O  OE1 . GLU A 1 238 ? 5.851   -7.795  3.121   1.00 31.52  ? 239 GLU A OE1 1 
ATOM   2008 O  OE2 . GLU A 1 238 ? 7.609   -8.658  2.101   1.00 47.76  ? 239 GLU A OE2 1 
ATOM   2009 N  N   . LEU A 1 239 ? 1.412   -12.060 1.952   1.00 14.51  ? 240 LEU A N   1 
ATOM   2010 C  CA  . LEU A 1 239 ? 0.022   -12.014 2.288   1.00 12.55  ? 240 LEU A CA  1 
ATOM   2011 C  C   . LEU A 1 239 ? -0.203  -11.181 3.569   1.00 12.49  ? 240 LEU A C   1 
ATOM   2012 O  O   . LEU A 1 239 ? 0.569   -11.366 4.528   1.00 13.51  ? 240 LEU A O   1 
ATOM   2013 C  CB  . LEU A 1 239 ? -0.496  -13.408 2.512   1.00 13.34  ? 240 LEU A CB  1 
ATOM   2014 C  CG  . LEU A 1 239 ? -0.609  -14.307 1.287   1.00 15.32  ? 240 LEU A CG  1 
ATOM   2015 C  CD1 . LEU A 1 239 ? -1.140  -15.649 1.720   1.00 19.29  ? 240 LEU A CD1 1 
ATOM   2016 C  CD2 . LEU A 1 239 ? -1.391  -13.633 0.162   1.00 16.90  ? 240 LEU A CD2 1 
ATOM   2017 N  N   . MET A 1 240 ? -1.241  -10.366 3.591   1.00 12.60  ? 241 MET A N   1 
ATOM   2018 C  CA  . MET A 1 240 ? -1.596  -9.561  4.768   1.00 12.98  ? 241 MET A CA  1 
ATOM   2019 C  C   . MET A 1 240 ? -2.387  -10.493 5.693   1.00 11.55  ? 241 MET A C   1 
ATOM   2020 O  O   . MET A 1 240 ? -3.549  -10.670 5.615   1.00 12.22  ? 241 MET A O   1 
ATOM   2021 C  CB  . MET A 1 240 ? -2.442  -8.390  4.334   1.00 12.64  ? 241 MET A CB  1 
ATOM   2022 C  CG  . MET A 1 240 ? -2.672  -7.424  5.534   1.00 13.41  ? 241 MET A CG  1 
ATOM   2023 S  SD  . MET A 1 240 ? -3.676  -6.008  5.116   1.00 13.54  ? 241 MET A SD  1 
ATOM   2024 C  CE  . MET A 1 240 ? -2.489  -5.046  4.170   1.00 15.57  ? 241 MET A CE  1 
ATOM   2025 N  N   . VAL A 1 241 ? -1.580  -11.093 6.622   1.00 11.07  ? 242 VAL A N   1 
ATOM   2026 C  CA  . VAL A 1 241 ? -2.084  -12.002 7.703   1.00 10.84  ? 242 VAL A CA  1 
ATOM   2027 C  C   . VAL A 1 241 ? -1.278  -11.757 8.965   1.00 9.99   ? 242 VAL A C   1 
ATOM   2028 O  O   . VAL A 1 241 ? -0.136  -11.324 8.910   1.00 10.80  ? 242 VAL A O   1 
ATOM   2029 C  CB  . VAL A 1 241 ? -1.983  -13.525 7.308   1.00 11.01  ? 242 VAL A CB  1 
ATOM   2030 C  CG1 . VAL A 1 241 ? -2.904  -13.826 6.156   1.00 12.94  ? 242 VAL A CG1 1 
ATOM   2031 C  CG2 . VAL A 1 241 ? -0.554  -13.935 7.046   1.00 12.80  ? 242 VAL A CG2 1 
ATOM   2032 N  N   . ASP A 1 242 ? -1.887  -12.062 10.121  1.00 9.66   ? 243 ASP A N   1 
ATOM   2033 C  CA  . ASP A 1 242 ? -1.196  -11.917 11.401  1.00 9.66   ? 243 ASP A CA  1 
ATOM   2034 C  C   . ASP A 1 242 ? -0.702  -10.491 11.648  1.00 9.05   ? 243 ASP A C   1 
ATOM   2035 O  O   . ASP A 1 242 ? 0.422   -10.273 12.122  1.00 11.10  ? 243 ASP A O   1 
ATOM   2036 C  CB  . ASP A 1 242 ? -0.102  -12.981 11.626  1.00 10.30  ? 243 ASP A CB  1 
ATOM   2037 C  CG  . ASP A 1 242 ? -0.710  -14.384 11.703  1.00 10.26  ? 243 ASP A CG  1 
ATOM   2038 O  OD1 . ASP A 1 242 ? -1.765  -14.551 12.337  1.00 9.80   ? 243 ASP A OD1 1 
ATOM   2039 O  OD2 . ASP A 1 242 ? -0.079  -15.319 11.107  1.00 12.34  ? 243 ASP A OD2 1 
ATOM   2040 N  N   . ASN A 1 243 ? -1.619  -9.566  11.371  1.00 8.89   ? 244 ASN A N   1 
ATOM   2041 C  CA  . ASN A 1 243 ? -1.354  -8.122  11.638  1.00 8.88   ? 244 ASN A CA  1 
ATOM   2042 C  C   . ASN A 1 243 ? -1.877  -7.696  12.984  1.00 8.15   ? 244 ASN A C   1 
ATOM   2043 O  O   . ASN A 1 243 ? -2.487  -6.633  13.119  1.00 10.10  ? 244 ASN A O   1 
ATOM   2044 C  CB  . ASN A 1 243 ? -1.898  -7.273  10.462  1.00 9.14   ? 244 ASN A CB  1 
ATOM   2045 C  CG  . ASN A 1 243 ? -3.333  -7.524  10.179  1.00 9.89   ? 244 ASN A CG  1 
ATOM   2046 O  OD1 . ASN A 1 243 ? -4.010  -8.309  10.827  1.00 10.28  ? 244 ASN A OD1 1 
ATOM   2047 N  ND2 . ASN A 1 243 ? -3.815  -6.958  9.071   1.00 15.03  ? 244 ASN A ND2 1 
ATOM   2048 N  N   . TRP A 1 244 ? -1.649  -8.507  14.004  1.00 8.17   ? 245 TRP A N   1 
ATOM   2049 C  CA  . TRP A 1 244 ? -2.061  -8.263  15.382  1.00 7.90   ? 245 TRP A CA  1 
ATOM   2050 C  C   . TRP A 1 244 ? -0.837  -8.203  16.301  1.00 7.98   ? 245 TRP A C   1 
ATOM   2051 O  O   . TRP A 1 244 ? 0.135   -8.908  16.132  1.00 9.46   ? 245 TRP A O   1 
ATOM   2052 C  CB  . TRP A 1 244 ? -3.046  -9.373  15.857  1.00 8.16   ? 245 TRP A CB  1 
ATOM   2053 C  CG  . TRP A 1 244 ? -2.577  -10.776 15.669  1.00 8.41   ? 245 TRP A CG  1 
ATOM   2054 C  CD1 . TRP A 1 244 ? -2.700  -11.511 14.531  1.00 8.56   ? 245 TRP A CD1 1 
ATOM   2055 C  CD2 . TRP A 1 244 ? -1.946  -11.639 16.634  1.00 8.50   ? 245 TRP A CD2 1 
ATOM   2056 N  NE1 . TRP A 1 244 ? -2.169  -12.771 14.704  1.00 8.82   ? 245 TRP A NE1 1 
ATOM   2057 C  CE2 . TRP A 1 244 ? -1.716  -12.871 15.977  1.00 8.63   ? 245 TRP A CE2 1 
ATOM   2058 C  CE3 . TRP A 1 244 ? -1.621  -11.503 17.990  1.00 9.44   ? 245 TRP A CE3 1 
ATOM   2059 C  CZ2 . TRP A 1 244 ? -1.125  -13.958 16.652  1.00 9.72   ? 245 TRP A CZ2 1 
ATOM   2060 C  CZ3 . TRP A 1 244 ? -1.119  -12.594 18.663  1.00 10.40  ? 245 TRP A CZ3 1 
ATOM   2061 C  CH2 . TRP A 1 244 ? -0.841  -13.796 17.968  1.00 10.64  ? 245 TRP A CH2 1 
ATOM   2062 N  N   . ARG A 1 245 ? -0.970  -7.344  17.304  1.00 8.07   ? 246 ARG A N   1 
ATOM   2063 C  CA  . ARG A 1 245 ? -0.011  -7.239  18.407  1.00 7.93   ? 246 ARG A CA  1 
ATOM   2064 C  C   . ARG A 1 245 ? -0.473  -8.176  19.521  1.00 8.01   ? 246 ARG A C   1 
ATOM   2065 O  O   . ARG A 1 245 ? -1.657  -8.159  19.857  1.00 9.05   ? 246 ARG A O   1 
ATOM   2066 C  CB  . ARG A 1 245 ? 0.079   -5.799  18.899  1.00 8.32   ? 246 ARG A CB  1 
ATOM   2067 C  CG  . ARG A 1 245 ? 1.180   -5.553  19.885  1.00 8.73   ? 246 ARG A CG  1 
ATOM   2068 C  CD  . ARG A 1 245 ? 1.108   -4.210  20.549  1.00 8.62   ? 246 ARG A CD  1 
ATOM   2069 N  NE  . ARG A 1 245 ? 2.341   -3.905  21.248  1.00 9.39   ? 246 ARG A NE  1 
ATOM   2070 C  CZ  . ARG A 1 245 ? 2.552   -2.854  22.048  1.00 8.66   ? 246 ARG A CZ  1 
ATOM   2071 N  NH1 . ARG A 1 245 ? 1.553   -2.093  22.449  1.00 9.24   ? 246 ARG A NH1 1 
ATOM   2072 N  NH2 . ARG A 1 245 ? 3.786   -2.618  22.499  1.00 10.83  ? 246 ARG A NH2 1 
ATOM   2073 N  N   A PRO A 1 246 ? 0.416   -8.953  20.124  0.50 8.38   ? 247 PRO A N   1 
ATOM   2074 N  N   B PRO A 1 246 ? 0.463   -8.939  20.126  0.50 9.01   ? 247 PRO A N   1 
ATOM   2075 C  CA  A PRO A 1 246 ? -0.013  -9.773  21.239  0.50 9.78   ? 247 PRO A CA  1 
ATOM   2076 C  CA  B PRO A 1 246 ? 0.074   -9.769  21.258  0.50 9.66   ? 247 PRO A CA  1 
ATOM   2077 C  C   A PRO A 1 246 ? -0.369  -8.935  22.483  0.50 9.00   ? 247 PRO A C   1 
ATOM   2078 C  C   B PRO A 1 246 ? -0.302  -8.946  22.500  0.50 9.52   ? 247 PRO A C   1 
ATOM   2079 O  O   A PRO A 1 246 ? -0.032  -7.745  22.624  0.50 8.99   ? 247 PRO A O   1 
ATOM   2080 O  O   B PRO A 1 246 ? 0.066   -7.759  22.632  0.50 9.51   ? 247 PRO A O   1 
ATOM   2081 C  CB  A PRO A 1 246 ? 1.177   -10.640 21.507  0.50 12.63  ? 247 PRO A CB  1 
ATOM   2082 C  CB  B PRO A 1 246 ? 1.295   -10.571 21.524  0.50 14.08  ? 247 PRO A CB  1 
ATOM   2083 C  CG  A PRO A 1 246 ? 2.064   -10.611 20.267  0.50 9.82   ? 247 PRO A CG  1 
ATOM   2084 C  CG  B PRO A 1 246 ? 2.411   -9.788  21.046  0.50 16.41  ? 247 PRO A CG  1 
ATOM   2085 C  CD  A PRO A 1 246 ? 1.805   -9.222  19.732  0.50 10.13  ? 247 PRO A CD  1 
ATOM   2086 C  CD  B PRO A 1 246 ? 1.902   -9.062  19.850  0.50 12.34  ? 247 PRO A CD  1 
ATOM   2087 N  N   . ALA A 1 247 ? -1.011  -9.600  23.442  1.00 9.76   ? 248 ALA A N   1 
ATOM   2088 C  CA  . ALA A 1 247 ? -1.364  -8.954  24.703  1.00 9.04   ? 248 ALA A CA  1 
ATOM   2089 C  C   . ALA A 1 247 ? -0.135  -8.475  25.451  1.00 8.95   ? 248 ALA A C   1 
ATOM   2090 O  O   . ALA A 1 247 ? 0.899   -9.117  25.507  1.00 10.81  ? 248 ALA A O   1 
ATOM   2091 C  CB  . ALA A 1 247 ? -2.144  -9.934  25.554  1.00 11.76  ? 248 ALA A CB  1 
ATOM   2092 N  N   . GLN A 1 248 ? -0.272  -7.269  26.029  1.00 8.85   ? 249 GLN A N   1 
ATOM   2093 C  CA  . GLN A 1 248 ? 0.769   -6.539  26.753  1.00 9.40   ? 249 GLN A CA  1 
ATOM   2094 C  C   . GLN A 1 248 ? 0.456   -6.541  28.226  1.00 9.99   ? 249 GLN A C   1 
ATOM   2095 O  O   . GLN A 1 248 ? -0.676  -6.772  28.648  1.00 10.77  ? 249 GLN A O   1 
ATOM   2096 C  CB  . GLN A 1 248 ? 0.807   -5.110  26.212  1.00 10.71  ? 249 GLN A CB  1 
ATOM   2097 C  CG  . GLN A 1 248 ? 1.135   -5.052  24.725  1.00 10.82  ? 249 GLN A CG  1 
ATOM   2098 C  CD  . GLN A 1 248 ? 2.489   -5.706  24.400  1.00 10.97  ? 249 GLN A CD  1 
ATOM   2099 O  OE1 . GLN A 1 248 ? 3.506   -5.360  24.992  1.00 13.89  ? 249 GLN A OE1 1 
ATOM   2100 N  NE2 . GLN A 1 248 ? 2.496   -6.636  23.453  1.00 12.25  ? 249 GLN A NE2 1 
ATOM   2101 N  N   . PRO A 1 249 ? 1.482   -6.251  29.088  1.00 12.26  ? 250 PRO A N   1 
ATOM   2102 C  CA  . PRO A 1 249 ? 1.270   -6.287  30.525  1.00 13.75  ? 250 PRO A CA  1 
ATOM   2103 C  C   . PRO A 1 249 ? 0.192   -5.287  30.974  1.00 11.42  ? 250 PRO A C   1 
ATOM   2104 O  O   . PRO A 1 249 ? 0.211   -4.112  30.613  1.00 12.18  ? 250 PRO A O   1 
ATOM   2105 C  CB  . PRO A 1 249 ? 2.674   -5.890  31.068  1.00 16.40  ? 250 PRO A CB  1 
ATOM   2106 C  CG  . PRO A 1 249 ? 3.615   -6.372  30.036  1.00 19.55  ? 250 PRO A CG  1 
ATOM   2107 C  CD  . PRO A 1 249 ? 2.873   -6.020  28.723  1.00 17.04  ? 250 PRO A CD  1 
ATOM   2108 N  N   . LEU A 1 250 ? -0.666  -5.775  31.843  1.00 12.10  ? 251 LEU A N   1 
ATOM   2109 C  CA  . LEU A 1 250 ? -1.723  -4.922  32.352  1.00 11.88  ? 251 LEU A CA  1 
ATOM   2110 C  C   . LEU A 1 250 ? -1.224  -3.842  33.289  1.00 11.58  ? 251 LEU A C   1 
ATOM   2111 O  O   . LEU A 1 250 ? -1.797  -2.743  33.367  1.00 12.09  ? 251 LEU A O   1 
ATOM   2112 C  CB  . LEU A 1 250 ? -2.783  -5.790  33.089  1.00 14.00  ? 251 LEU A CB  1 
ATOM   2113 C  CG  . LEU A 1 250 ? -4.057  -5.069  33.493  1.00 14.57  ? 251 LEU A CG  1 
ATOM   2114 C  CD1 . LEU A 1 250 ? -4.875  -4.537  32.270  1.00 13.98  ? 251 LEU A CD1 1 
ATOM   2115 C  CD2 . LEU A 1 250 ? -4.952  -6.039  34.265  1.00 19.37  ? 251 LEU A CD2 1 
ATOM   2116 N  N   . LYS A 1 251 ? -0.152  -4.097  34.039  1.00 13.34  ? 252 LYS A N   1 
ATOM   2117 C  CA  . LYS A 1 251 ? 0.520   -3.077  34.893  1.00 13.92  ? 252 LYS A CA  1 
ATOM   2118 C  C   . LYS A 1 251 ? -0.548  -2.505  35.822  1.00 15.45  ? 252 LYS A C   1 
ATOM   2119 O  O   . LYS A 1 251 ? -1.302  -3.335  36.381  1.00 16.94  ? 252 LYS A O   1 
ATOM   2120 C  CB  . LYS A 1 251 ? 1.282   -2.080  34.083  1.00 16.35  ? 252 LYS A CB  1 
ATOM   2121 C  CG  . LYS A 1 251 ? 2.404   -2.738  33.329  1.00 19.24  ? 252 LYS A CG  1 
ATOM   2122 C  CD  . LYS A 1 251 ? 3.380   -1.760  32.699  1.00 19.53  ? 252 LYS A CD  1 
ATOM   2123 C  CE  . LYS A 1 251 ? 4.487   -2.518  32.133  1.00 26.23  ? 252 LYS A CE  1 
ATOM   2124 N  NZ  . LYS A 1 251 ? 5.391   -1.659  31.369  1.00 29.51  ? 252 LYS A NZ  1 
ATOM   2125 N  N   . ASN A 1 252 ? -0.566  -1.229  36.094  1.00 13.58  ? 253 ASN A N   1 
ATOM   2126 C  CA  . ASN A 1 252 ? -1.429  -0.797  37.143  1.00 19.84  ? 253 ASN A CA  1 
ATOM   2127 C  C   . ASN A 1 252 ? -2.753  -0.373  36.525  1.00 19.23  ? 253 ASN A C   1 
ATOM   2128 O  O   . ASN A 1 252 ? -3.060  0.818   36.474  1.00 22.21  ? 253 ASN A O   1 
ATOM   2129 C  CB  . ASN A 1 252 ? -0.697  0.372   37.894  1.00 25.11  ? 253 ASN A CB  1 
ATOM   2130 C  CG  . ASN A 1 252 ? -1.517  0.886   39.045  1.00 31.05  ? 253 ASN A CG  1 
ATOM   2131 O  OD1 . ASN A 1 252 ? -2.111  0.102   39.825  1.00 54.25  ? 253 ASN A OD1 1 
ATOM   2132 N  ND2 . ASN A 1 252 ? -1.495  2.193   39.244  1.00 37.52  ? 253 ASN A ND2 1 
ATOM   2133 N  N   . ARG A 1 253 ? -3.564  -1.397  35.932  1.00 14.67  ? 254 ARG A N   1 
ATOM   2134 C  CA  . ARG A 1 253 ? -4.820  -1.046  35.416  1.00 11.59  ? 254 ARG A CA  1 
ATOM   2135 C  C   . ARG A 1 253 ? -5.909  -1.959  35.861  1.00 12.09  ? 254 ARG A C   1 
ATOM   2136 O  O   . ARG A 1 253 ? -5.657  -3.120  36.117  1.00 18.62  ? 254 ARG A O   1 
ATOM   2137 C  CB  . ARG A 1 253 ? -4.748  -0.968  33.894  1.00 11.09  ? 254 ARG A CB  1 
ATOM   2138 C  CG  . ARG A 1 253 ? -3.850  0.143   33.406  1.00 11.09  ? 254 ARG A CG  1 
ATOM   2139 C  CD  . ARG A 1 253 ? -3.720  0.161   31.877  1.00 10.56  ? 254 ARG A CD  1 
ATOM   2140 N  NE  . ARG A 1 253 ? -2.937  -0.985  31.433  1.00 9.52   ? 254 ARG A NE  1 
ATOM   2141 C  CZ  . ARG A 1 253 ? -2.667  -1.264  30.167  1.00 8.02   ? 254 ARG A CZ  1 
ATOM   2142 N  NH1 . ARG A 1 253 ? -3.265  -0.571  29.173  1.00 8.32   ? 254 ARG A NH1 1 
ATOM   2143 N  NH2 . ARG A 1 253 ? -1.828  -2.232  29.825  1.00 8.97   ? 254 ARG A NH2 1 
ATOM   2144 N  N   . GLN A 1 254 ? -7.113  -1.432  35.906  1.00 12.61  ? 255 GLN A N   1 
ATOM   2145 C  CA  . GLN A 1 254 ? -8.303  -2.213  36.169  1.00 14.71  ? 255 GLN A CA  1 
ATOM   2146 C  C   . GLN A 1 254 ? -9.183  -2.224  34.939  1.00 12.46  ? 255 GLN A C   1 
ATOM   2147 O  O   . GLN A 1 254 ? -9.404  -1.176  34.247  1.00 17.10  ? 255 GLN A O   1 
ATOM   2148 C  CB  . GLN A 1 254 ? -9.070  -1.601  37.293  1.00 19.98  ? 255 GLN A CB  1 
ATOM   2149 C  CG  . GLN A 1 254 ? -8.438  -1.833  38.640  1.00 31.39  ? 255 GLN A CG  1 
ATOM   2150 C  CD  . GLN A 1 254 ? -9.534  -1.738  39.707  1.00 54.49  ? 255 GLN A CD  1 
ATOM   2151 O  OE1 . GLN A 1 254 ? -10.471 -0.894  39.627  1.00 55.10  ? 255 GLN A OE1 1 
ATOM   2152 N  NE2 . GLN A 1 254 ? -9.463  -2.613  40.710  1.00 86.13  ? 255 GLN A NE2 1 
ATOM   2153 N  N   . ILE A 1 255 ? -9.631  -3.392  34.564  1.00 10.74  ? 256 ILE A N   1 
ATOM   2154 C  CA  . ILE A 1 255 ? -10.622 -3.543  33.499  1.00 10.49  ? 256 ILE A CA  1 
ATOM   2155 C  C   . ILE A 1 255 ? -11.995 -3.557  34.176  1.00 10.29  ? 256 ILE A C   1 
ATOM   2156 O  O   . ILE A 1 255 ? -12.225 -4.274  35.144  1.00 11.98  ? 256 ILE A O   1 
ATOM   2157 C  CB  . ILE A 1 255 ? -10.420 -4.785  32.673  1.00 10.44  ? 256 ILE A CB  1 
ATOM   2158 C  CG1 . ILE A 1 255 ? -8.943  -4.796  32.112  1.00 12.05  ? 256 ILE A CG1 1 
ATOM   2159 C  CG2 . ILE A 1 255 ? -11.445 -4.912  31.587  1.00 12.08  ? 256 ILE A CG2 1 
ATOM   2160 C  CD1 . ILE A 1 255 ? -8.610  -5.978  31.264  1.00 14.46  ? 256 ILE A CD1 1 
ATOM   2161 N  N   A LYS A 1 256 ? -12.915 -2.734  33.667  0.50 10.41  ? 257 LYS A N   1 
ATOM   2162 N  N   B LYS A 1 256 ? -12.924 -2.743  33.663  0.50 10.40  ? 257 LYS A N   1 
ATOM   2163 C  CA  A LYS A 1 256 ? -14.265 -2.615  34.218  0.50 10.34  ? 257 LYS A CA  1 
ATOM   2164 C  CA  B LYS A 1 256 ? -14.282 -2.607  34.208  0.50 10.17  ? 257 LYS A CA  1 
ATOM   2165 C  C   A LYS A 1 256 ? -15.252 -3.246  33.247  0.50 10.02  ? 257 LYS A C   1 
ATOM   2166 C  C   B LYS A 1 256 ? -15.267 -3.235  33.245  0.50 10.03  ? 257 LYS A C   1 
ATOM   2167 O  O   A LYS A 1 256 ? -15.045 -3.151  32.045  0.50 12.01  ? 257 LYS A O   1 
ATOM   2168 O  O   B LYS A 1 256 ? -15.054 -3.139  32.029  0.50 12.16  ? 257 LYS A O   1 
ATOM   2169 C  CB  A LYS A 1 256 ? -14.620 -1.157  34.468  0.50 12.28  ? 257 LYS A CB  1 
ATOM   2170 C  CB  B LYS A 1 256 ? -14.590 -1.152  34.513  0.50 12.36  ? 257 LYS A CB  1 
ATOM   2171 C  CG  A LYS A 1 256 ? -13.581 -0.458  35.354  0.50 17.45  ? 257 LYS A CG  1 
ATOM   2172 C  CG  B LYS A 1 256 ? -13.717 -0.643  35.685  0.50 14.68  ? 257 LYS A CG  1 
ATOM   2173 C  CD  A LYS A 1 256 ? -14.063 0.857   35.924  0.50 29.59  ? 257 LYS A CD  1 
ATOM   2174 C  CD  B LYS A 1 256 ? -13.758 0.812   35.902  0.50 18.63  ? 257 LYS A CD  1 
ATOM   2175 C  CE  A LYS A 1 256 ? -12.956 1.512   36.733  0.50 37.04  ? 257 LYS A CE  1 
ATOM   2176 C  CE  B LYS A 1 256 ? -12.586 1.193   36.755  0.50 26.65  ? 257 LYS A CE  1 
ATOM   2177 N  NZ  A LYS A 1 256 ? -12.035 0.458   37.220  0.50 41.60  ? 257 LYS A NZ  1 
ATOM   2178 N  NZ  B LYS A 1 256 ? -12.742 2.613   37.222  0.50 23.08  ? 257 LYS A NZ  1 
ATOM   2179 N  N   . ALA A 1 257 ? -16.290 -3.862  33.781  1.00 10.75  ? 258 ALA A N   1 
ATOM   2180 C  CA  . ALA A 1 257 ? -17.353 -4.463  32.994  1.00 10.99  ? 258 ALA A CA  1 
ATOM   2181 C  C   . ALA A 1 257 ? -18.624 -3.664  33.181  1.00 10.58  ? 258 ALA A C   1 
ATOM   2182 O  O   . ALA A 1 257 ? -18.990 -3.217  34.288  1.00 12.34  ? 258 ALA A O   1 
ATOM   2183 C  CB  . ALA A 1 257 ? -17.610 -5.932  33.426  1.00 13.56  ? 258 ALA A CB  1 
ATOM   2184 N  N   . SER A 1 258 ? -19.370 -3.521  32.082  1.00 10.93  ? 259 SER A N   1 
ATOM   2185 C  CA  . SER A 1 258 ? -20.651 -2.831  32.107  1.00 12.51  ? 259 SER A CA  1 
ATOM   2186 C  C   . SER A 1 258 ? -21.784 -3.732  32.536  1.00 13.67  ? 259 SER A C   1 
ATOM   2187 O  O   . SER A 1 258 ? -22.930 -3.236  32.639  1.00 18.57  ? 259 SER A O   1 
ATOM   2188 C  CB  . SER A 1 258 ? -20.960 -2.265  30.726  1.00 12.91  ? 259 SER A CB  1 
ATOM   2189 O  OG  . SER A 1 258 ? -21.359 -3.286  29.816  1.00 12.16  ? 259 SER A OG  1 
ATOM   2190 N  N   . PHE A 1 259 ? -21.519 -5.025  32.744  1.00 14.27  ? 260 PHE A N   1 
ATOM   2191 C  CA  . PHE A 1 259 ? -22.549 -6.060  32.898  1.00 16.29  ? 260 PHE A CA  1 
ATOM   2192 C  C   . PHE A 1 259 ? -22.096 -6.951  34.035  1.00 19.01  ? 260 PHE A C   1 
ATOM   2193 O  O   . PHE A 1 259 ? -20.881 -7.077  34.338  1.00 20.97  ? 260 PHE A O   1 
ATOM   2194 C  CB  . PHE A 1 259 ? -22.737 -6.828  31.591  1.00 15.90  ? 260 PHE A CB  1 
ATOM   2195 C  CG  . PHE A 1 259 ? -21.488 -7.530  31.170  1.00 14.64  ? 260 PHE A CG  1 
ATOM   2196 C  CD1 . PHE A 1 259 ? -20.496 -6.851  30.479  1.00 13.41  ? 260 PHE A CD1 1 
ATOM   2197 C  CD2 . PHE A 1 259 ? -21.236 -8.816  31.585  1.00 18.81  ? 260 PHE A CD2 1 
ATOM   2198 C  CE1 . PHE A 1 259 ? -19.287 -7.466  30.168  1.00 14.07  ? 260 PHE A CE1 1 
ATOM   2199 C  CE2 . PHE A 1 259 ? -20.040 -9.436  31.261  1.00 20.61  ? 260 PHE A CE2 1 
ATOM   2200 C  CZ  . PHE A 1 259 ? -19.048 -8.797  30.573  1.00 17.23  ? 260 PHE A CZ  1 
ATOM   2201 N  N   . LYS A 1 260 ? -23.118 -7.600  34.581  1.00 30.74  ? 261 LYS A N   1 
ATOM   2202 C  CA  . LYS A 1 260 ? -23.108 -8.732  35.508  1.00 40.36  ? 261 LYS A CA  1 
ATOM   2203 C  C   . LYS A 1 260 ? -22.707 -8.479  36.944  1.00 63.50  ? 261 LYS A C   1 
ATOM   2204 O  O   . LYS A 1 260 ? -23.469 -7.770  37.650  1.00 97.65  ? 261 LYS A O   1 
ATOM   2205 C  CB  . LYS A 1 260 ? -22.558 -10.030 34.874  1.00 40.18  ? 261 LYS A CB  1 
ATOM   2206 C  CG  . LYS A 1 260 ? -23.490 -10.535 33.767  1.00 46.25  ? 261 LYS A CG  1 
ATOM   2207 C  CD  . LYS A 1 260 ? -23.269 -11.999 33.304  1.00 48.91  ? 261 LYS A CD  1 
ATOM   2208 C  CE  . LYS A 1 260 ? -21.947 -12.219 32.540  1.00 47.47  ? 261 LYS A CE  1 
ATOM   2209 N  NZ  . LYS A 1 260 ? -21.621 -13.648 32.178  1.00 60.55  ? 261 LYS A NZ  1 
HETATM 2210 ZN ZN  . ZN  B 2 .   ? -6.582  -1.599  15.274  1.00 7.26   ? 301 ZN  A ZN  1 
HETATM 2211 S  S   . DMS C 3 .   ? 1.445   -11.699 15.007  1.00 21.49  ? 302 DMS A S   1 
HETATM 2212 O  O   . DMS C 3 .   ? 1.984   -13.081 14.616  1.00 28.74  ? 302 DMS A O   1 
HETATM 2213 C  C1  . DMS C 3 .   ? 1.717   -11.525 16.595  1.00 19.87  ? 302 DMS A C1  1 
HETATM 2214 C  C2  . DMS C 3 .   ? 2.559   -10.493 14.619  1.00 21.94  ? 302 DMS A C2  1 
HETATM 2215 S  S   . DMS D 3 .   ? -5.577  7.555   10.821  1.00 30.45  ? 303 DMS A S   1 
HETATM 2216 O  O   . DMS D 3 .   ? -5.221  7.060   9.436   1.00 35.39  ? 303 DMS A O   1 
HETATM 2217 C  C1  . DMS D 3 .   ? -4.370  8.736   11.052  1.00 33.64  ? 303 DMS A C1  1 
HETATM 2218 C  C2  . DMS D 3 .   ? -6.934  8.534   11.049  1.00 27.15  ? 303 DMS A C2  1 
HETATM 2219 C  C1  . EDO E 4 .   ? -19.978 -15.436 22.526  1.00 21.63  ? 304 EDO A C1  1 
HETATM 2220 O  O1  . EDO E 4 .   ? -21.022 -14.510 23.092  1.00 38.80  ? 304 EDO A O1  1 
HETATM 2221 C  C2  . EDO E 4 .   ? -20.323 -16.455 21.437  1.00 40.03  ? 304 EDO A C2  1 
HETATM 2222 O  O2  . EDO E 4 .   ? -21.178 -16.031 20.386  1.00 50.41  ? 304 EDO A O2  1 
HETATM 2223 C  C1  . EDO F 4 .   ? -8.195  -9.585  -1.324  1.00 30.77  ? 305 EDO A C1  1 
HETATM 2224 O  O1  . EDO F 4 .   ? -7.625  -8.692  -2.331  1.00 30.54  ? 305 EDO A O1  1 
HETATM 2225 C  C2  . EDO F 4 .   ? -9.634  -10.176 -1.261  1.00 24.58  ? 305 EDO A C2  1 
HETATM 2226 O  O2  . EDO F 4 .   ? -10.233 -10.706 -2.507  1.00 45.15  ? 305 EDO A O2  1 
HETATM 2227 C  C1  . EDO G 4 .   ? 14.779  2.856   24.012  1.00 30.20  ? 306 EDO A C1  1 
HETATM 2228 O  O1  . EDO G 4 .   ? 14.006  2.152   23.068  1.00 26.20  ? 306 EDO A O1  1 
HETATM 2229 C  C2  . EDO G 4 .   ? 14.606  4.408   24.176  1.00 27.37  ? 306 EDO A C2  1 
HETATM 2230 O  O2  . EDO G 4 .   ? 14.199  5.053   25.443  1.00 30.68  ? 306 EDO A O2  1 
HETATM 2231 C  C1  . EDO H 4 .   ? 3.468   -13.033 22.882  1.00 29.97  ? 307 EDO A C1  1 
HETATM 2232 O  O1  . EDO H 4 .   ? 4.175   -11.810 23.112  1.00 31.09  ? 307 EDO A O1  1 
HETATM 2233 C  C2  . EDO H 4 .   ? 3.418   -13.682 21.469  1.00 31.78  ? 307 EDO A C2  1 
HETATM 2234 O  O2  . EDO H 4 .   ? 2.192   -14.232 20.845  1.00 27.51  ? 307 EDO A O2  1 
HETATM 2235 O  O16 . V26 I 5 .   ? -3.358  6.488   12.808  1.00 15.78  ? 308 V26 A O16 1 
HETATM 2236 S  S14 . V26 I 5 .   ? -2.510  5.609   13.647  1.00 13.05  ? 308 V26 A S14 1 
HETATM 2237 O  O15 . V26 I 5 .   ? -1.743  6.301   14.672  1.00 13.94  ? 308 V26 A O15 1 
HETATM 2238 C  C8  . V26 I 5 .   ? -3.521  4.384   14.439  1.00 11.46  ? 308 V26 A C8  1 
HETATM 2239 C  C7  . V26 I 5 .   ? -2.846  3.443   15.234  1.00 10.69  ? 308 V26 A C7  1 
HETATM 2240 F  F12 . V26 I 5 .   ? -1.534  3.514   15.400  1.00 11.81  ? 308 V26 A F12 1 
HETATM 2241 C  C6  . V26 I 5 .   ? -3.550  2.390   15.830  1.00 9.87   ? 308 V26 A C6  1 
HETATM 2242 F  F11 . V26 I 5 .   ? -2.839  1.474   16.506  1.00 10.43  ? 308 V26 A F11 1 
HETATM 2243 C  C9  . V26 I 5 .   ? -4.918  4.264   14.272  1.00 10.45  ? 308 V26 A C9  1 
HETATM 2244 N  N25 . V26 I 5 .   ? -5.648  5.146   13.504  1.00 12.01  ? 308 V26 A N25 1 
HETATM 2245 C  C26 . V26 I 5 .   ? -6.775  4.722   12.663  1.00 12.65  ? 308 V26 A C26 1 
HETATM 2246 C  C10 . V26 I 5 .   ? -5.565  3.228   14.996  1.00 9.58   ? 308 V26 A C10 1 
HETATM 2247 F  F13 . V26 I 5 .   ? -6.890  3.254   14.942  1.00 11.12  ? 308 V26 A F13 1 
HETATM 2248 C  C5  . V26 I 5 .   ? -4.949  2.268   15.777  1.00 10.75  ? 308 V26 A C5  1 
HETATM 2249 S  S1  . V26 I 5 .   ? -5.732  0.955   16.709  1.00 8.16   ? 308 V26 A S1  1 
HETATM 2250 O  O3  . V26 I 5 .   ? -5.187  1.180   18.042  1.00 8.54   ? 308 V26 A O3  1 
HETATM 2251 N  N4  . V26 I 5 .   ? -5.281  -0.434  16.109  1.00 14.35  ? 308 V26 A N4  1 
HETATM 2252 O  O2  . V26 I 5 .   ? -7.142  1.123   16.509  1.00 8.67   ? 308 V26 A O2  1 
HETATM 2253 C  C17 . V26 I 5 .   ? -1.385  4.712   12.608  1.00 16.59  ? 308 V26 A C17 1 
HETATM 2254 C  C18 . V26 I 5 .   ? -2.014  4.180   11.324  1.00 17.53  ? 308 V26 A C18 1 
HETATM 2255 C  C19 . V26 I 5 .   ? -2.917  3.022   11.462  1.00 15.08  ? 308 V26 A C19 1 
HETATM 2256 C  C24 . V26 I 5 .   ? -2.774  1.962   12.400  1.00 16.58  ? 308 V26 A C24 1 
HETATM 2257 C  C23 . V26 I 5 .   ? -3.656  0.935   12.519  1.00 15.64  ? 308 V26 A C23 1 
HETATM 2258 C  C22 . V26 I 5 .   ? -4.738  0.910   11.617  1.00 16.83  ? 308 V26 A C22 1 
HETATM 2259 C  C21 . V26 I 5 .   ? -4.931  2.007   10.763  1.00 16.59  ? 308 V26 A C21 1 
HETATM 2260 C  C20 . V26 I 5 .   ? -4.069  3.075   10.730  1.00 17.02  ? 308 V26 A C20 1 
HETATM 2261 O  O   . HOH J 6 .   ? -22.644 -9.570  25.349  1.00 22.93  ? 401 HOH A O   1 
HETATM 2262 O  O   . HOH J 6 .   ? -4.271  -1.413  38.032  1.00 27.31  ? 402 HOH A O   1 
HETATM 2263 O  O   . HOH J 6 .   ? -28.276 6.372   15.703  1.00 37.87  ? 403 HOH A O   1 
HETATM 2264 O  O   . HOH J 6 .   ? -14.574 -8.471  -5.526  1.00 37.38  ? 404 HOH A O   1 
HETATM 2265 O  O   . HOH J 6 .   ? -19.426 17.246  5.850   1.00 33.80  ? 405 HOH A O   1 
HETATM 2266 O  O   . HOH J 6 .   ? -3.333  17.985  21.323  1.00 21.09  ? 406 HOH A O   1 
HETATM 2267 O  O   . HOH J 6 .   ? -11.112 -15.115 34.195  1.00 23.79  ? 407 HOH A O   1 
HETATM 2268 O  O   . HOH J 6 .   ? 1.867   12.396  22.769  1.00 26.83  ? 408 HOH A O   1 
HETATM 2269 O  O   . HOH J 6 .   ? 2.690   -14.298 -5.533  1.00 43.52  ? 409 HOH A O   1 
HETATM 2270 O  O   . HOH J 6 .   ? -20.868 -6.784  -2.162  1.00 41.62  ? 410 HOH A O   1 
HETATM 2271 O  O   . HOH J 6 .   ? -25.521 -10.595 17.802  1.00 26.22  ? 411 HOH A O   1 
HETATM 2272 O  O   . HOH J 6 .   ? -17.798 -22.019 6.032   1.00 21.08  ? 412 HOH A O   1 
HETATM 2273 O  O   . HOH J 6 .   ? -1.056  -4.188  15.916  1.00 10.20  ? 413 HOH A O   1 
HETATM 2274 O  O   . HOH J 6 .   ? -7.272  -10.155 -4.371  1.00 38.56  ? 414 HOH A O   1 
HETATM 2275 O  O   . HOH J 6 .   ? 2.641   -11.395 9.420   1.00 20.13  ? 415 HOH A O   1 
HETATM 2276 O  O   . HOH J 6 .   ? -19.376 14.050  9.018   1.00 32.89  ? 416 HOH A O   1 
HETATM 2277 O  O   . HOH J 6 .   ? -15.494 -10.339 37.395  1.00 31.67  ? 417 HOH A O   1 
HETATM 2278 O  O   . HOH J 6 .   ? -5.008  2.184   37.444  1.00 29.37  ? 418 HOH A O   1 
HETATM 2279 O  O   . HOH J 6 .   ? -21.861 -14.167 18.752  1.00 34.35  ? 419 HOH A O   1 
HETATM 2280 O  O   . HOH J 6 .   ? -14.258 -16.531 29.085  1.00 22.56  ? 420 HOH A O   1 
HETATM 2281 O  O   . HOH J 6 .   ? -16.975 -14.107 37.499  1.00 28.81  ? 421 HOH A O   1 
HETATM 2282 O  O   . HOH J 6 .   ? -8.704  -3.823  7.927   1.00 11.55  ? 422 HOH A O   1 
HETATM 2283 O  O   . HOH J 6 .   ? -27.789 6.367   21.858  1.00 26.47  ? 423 HOH A O   1 
HETATM 2284 O  O   . HOH J 6 .   ? -21.204 7.830   1.863   1.00 19.70  ? 424 HOH A O   1 
HETATM 2285 O  O   . HOH J 6 .   ? 1.187   14.589  24.301  1.00 30.00  ? 425 HOH A O   1 
HETATM 2286 O  O   . HOH J 6 .   ? 6.676   -0.371  -1.106  1.00 41.77  ? 426 HOH A O   1 
HETATM 2287 O  O   . HOH J 6 .   ? 3.451   -13.894 12.634  1.00 35.49  ? 427 HOH A O   1 
HETATM 2288 O  O   . HOH J 6 .   ? -22.165 3.735   -2.745  1.00 92.74  ? 428 HOH A O   1 
HETATM 2289 O  O   . HOH J 6 .   ? -12.338 12.548  29.164  1.00 27.17  ? 429 HOH A O   1 
HETATM 2290 O  O   . HOH J 6 .   ? -9.755  1.559   39.096  1.00 29.42  ? 430 HOH A O   1 
HETATM 2291 O  O   . HOH J 6 .   ? -9.057  5.830   29.055  1.00 17.14  ? 431 HOH A O   1 
HETATM 2292 O  O   . HOH J 6 .   ? 4.452   -2.494  29.072  1.00 26.25  ? 432 HOH A O   1 
HETATM 2293 O  O   . HOH J 6 .   ? -12.670 13.121  31.910  1.00 29.42  ? 433 HOH A O   1 
HETATM 2294 O  O   . HOH J 6 .   ? -10.025 15.820  29.629  1.00 30.49  ? 434 HOH A O   1 
HETATM 2295 O  O   . HOH J 6 .   ? -12.155 10.739  5.956   1.00 35.69  ? 435 HOH A O   1 
HETATM 2296 O  O   . HOH J 6 .   ? -6.946  5.782   5.993   1.00 26.52  ? 436 HOH A O   1 
HETATM 2297 O  O   . HOH J 6 .   ? 4.365   -3.417  26.621  1.00 19.83  ? 437 HOH A O   1 
HETATM 2298 O  O   . HOH J 6 .   ? -19.649 14.913  16.616  1.00 26.22  ? 438 HOH A O   1 
HETATM 2299 O  O   . HOH J 6 .   ? -6.359  -4.633  -6.381  1.00 26.34  ? 439 HOH A O   1 
HETATM 2300 O  O   . HOH J 6 .   ? 2.006   8.128   27.937  1.00 34.82  ? 440 HOH A O   1 
HETATM 2301 O  O   . HOH J 6 .   ? -6.676  -20.257 19.511  1.00 12.59  ? 441 HOH A O   1 
HETATM 2302 O  O   . HOH J 6 .   ? 3.720   5.022   29.924  1.00 19.72  ? 442 HOH A O   1 
HETATM 2303 O  O   . HOH J 6 .   ? 0.015   -0.998  -4.735  1.00 18.14  ? 443 HOH A O   1 
HETATM 2304 O  O   . HOH J 6 .   ? -25.218 9.584   13.158  1.00 34.19  ? 444 HOH A O   1 
HETATM 2305 O  O   . HOH J 6 .   ? -22.150 -18.326 13.583  1.00 22.67  ? 445 HOH A O   1 
HETATM 2306 O  O   . HOH J 6 .   ? -25.608 -15.328 7.914   1.00 30.60  ? 446 HOH A O   1 
HETATM 2307 O  O   . HOH J 6 .   ? -13.025 -22.227 8.624   1.00 24.33  ? 447 HOH A O   1 
HETATM 2308 O  O   . HOH J 6 .   ? 0.543   7.126   29.980  1.00 31.95  ? 448 HOH A O   1 
HETATM 2309 O  O   . HOH J 6 .   ? -20.566 8.345   30.144  1.00 28.80  ? 449 HOH A O   1 
HETATM 2310 O  O   . HOH J 6 .   ? -10.542 8.662   25.633  1.00 10.21  ? 450 HOH A O   1 
HETATM 2311 O  O   . HOH J 6 .   ? -24.073 -2.996  29.235  1.00 68.83  ? 451 HOH A O   1 
HETATM 2312 O  O   . HOH J 6 .   ? -1.094  9.247   28.024  1.00 25.73  ? 452 HOH A O   1 
HETATM 2313 O  O   . HOH J 6 .   ? -20.253 10.705  26.913  1.00 18.36  ? 453 HOH A O   1 
HETATM 2314 O  O   . HOH J 6 .   ? -10.214 -12.514 40.116  1.00 26.84  ? 454 HOH A O   1 
HETATM 2315 O  O   . HOH J 6 .   ? 11.811  -0.383  16.233  1.00 23.69  ? 455 HOH A O   1 
HETATM 2316 O  O   . HOH J 6 .   ? -2.337  -3.076  11.801  1.00 13.79  ? 456 HOH A O   1 
HETATM 2317 O  O   . HOH J 6 .   ? -25.861 6.170   27.159  1.00 26.41  ? 457 HOH A O   1 
HETATM 2318 O  O   . HOH J 6 .   ? -2.607  -18.617 6.091   1.00 46.65  ? 458 HOH A O   1 
HETATM 2319 O  O   . HOH J 6 .   ? -8.429  -15.397 36.737  1.00 27.90  ? 459 HOH A O   1 
HETATM 2320 O  O   . HOH J 6 .   ? -15.401 -21.848 13.160  1.00 16.01  ? 460 HOH A O   1 
HETATM 2321 O  O   . HOH J 6 .   ? -24.127 8.630   20.252  1.00 18.80  ? 461 HOH A O   1 
HETATM 2322 O  O   . HOH J 6 .   ? -19.655 -4.230  41.493  1.00 34.40  ? 462 HOH A O   1 
HETATM 2323 O  O   . HOH J 6 .   ? -4.710  -12.015 32.170  1.00 19.92  ? 463 HOH A O   1 
HETATM 2324 O  O   . HOH J 6 .   ? -7.877  -15.398 11.340  1.00 10.93  ? 464 HOH A O   1 
HETATM 2325 O  O   . HOH J 6 .   ? -26.981 -12.848 20.251  1.00 44.84  ? 465 HOH A O   1 
HETATM 2326 O  O   . HOH J 6 .   ? -27.246 -7.587  26.271  1.00 36.29  ? 466 HOH A O   1 
HETATM 2327 O  O   . HOH J 6 .   ? -12.109 9.433   3.141   1.00 26.00  ? 467 HOH A O   1 
HETATM 2328 O  O   . HOH J 6 .   ? -2.453  -8.754  29.196  1.00 11.35  ? 468 HOH A O   1 
HETATM 2329 O  O   . HOH J 6 .   ? -16.524 -15.188 33.041  1.00 44.93  ? 469 HOH A O   1 
HETATM 2330 O  O   . HOH J 6 .   ? -25.670 7.900   6.048   1.00 42.43  ? 470 HOH A O   1 
HETATM 2331 O  O   . HOH J 6 .   ? -10.500 13.230  8.683   1.00 31.70  ? 471 HOH A O   1 
HETATM 2332 O  O   . HOH J 6 .   ? 1.971   -15.673 9.351   1.00 22.31  ? 472 HOH A O   1 
HETATM 2333 O  O   . HOH J 6 .   ? -22.901 -14.660 16.126  1.00 31.10  ? 473 HOH A O   1 
HETATM 2334 O  O   . HOH J 6 .   ? -5.458  3.158   -5.460  1.00 72.39  ? 474 HOH A O   1 
HETATM 2335 O  O   . HOH J 6 .   ? -19.271 -20.812 5.303   1.00 28.34  ? 475 HOH A O   1 
HETATM 2336 O  O   . HOH J 6 .   ? 6.172   -11.230 15.780  1.00 35.38  ? 476 HOH A O   1 
HETATM 2337 O  O   . HOH J 6 .   ? -17.361 -16.234 22.032  1.00 21.58  ? 477 HOH A O   1 
HETATM 2338 O  O   . HOH J 6 .   ? -18.062 10.722  11.332  1.00 18.12  ? 478 HOH A O   1 
HETATM 2339 O  O   . HOH J 6 .   ? -1.966  -4.694  -7.043  1.00 27.21  ? 479 HOH A O   1 
HETATM 2340 O  O   . HOH J 6 .   ? -13.735 10.358  28.020  1.00 17.95  ? 480 HOH A O   1 
HETATM 2341 O  O   . HOH J 6 .   ? -6.960  -14.902 31.688  1.00 24.23  ? 481 HOH A O   1 
HETATM 2342 O  O   . HOH J 6 .   ? -15.029 2.521   38.756  1.00 27.21  ? 482 HOH A O   1 
HETATM 2343 O  O   . HOH J 6 .   ? -8.550  0.662   -6.522  1.00 30.66  ? 483 HOH A O   1 
HETATM 2344 O  O   . HOH J 6 .   ? -26.196 2.792   21.006  1.00 29.57  ? 484 HOH A O   1 
HETATM 2345 O  O   . HOH J 6 .   ? -22.834 -5.906  2.781   1.00 21.55  ? 485 HOH A O   1 
HETATM 2346 O  O   . HOH J 6 .   ? -4.480  -13.496 18.066  1.00 9.54   ? 486 HOH A O   1 
HETATM 2347 O  O   . HOH J 6 .   ? -16.956 -8.430  20.452  1.00 9.34   ? 487 HOH A O   1 
HETATM 2348 O  O   . HOH J 6 .   ? -10.323 -18.284 17.108  1.00 12.58  ? 488 HOH A O   1 
HETATM 2349 O  O   . HOH J 6 .   ? 9.400   7.460   18.489  1.00 41.61  ? 489 HOH A O   1 
HETATM 2350 O  O   . HOH J 6 .   ? -11.019 -19.382 7.174   1.00 25.62  ? 490 HOH A O   1 
HETATM 2351 O  O   . HOH J 6 .   ? 5.537   7.083   20.281  1.00 17.29  ? 491 HOH A O   1 
HETATM 2352 O  O   . HOH J 6 .   ? -14.603 -18.549 18.699  1.00 15.20  ? 492 HOH A O   1 
HETATM 2353 O  O   . HOH J 6 .   ? -13.561 -0.934  -6.019  1.00 35.38  ? 493 HOH A O   1 
HETATM 2354 O  O   . HOH J 6 .   ? -4.217  -8.538  31.264  1.00 20.20  ? 494 HOH A O   1 
HETATM 2355 O  O   . HOH J 6 .   ? -0.901  -6.058  36.536  1.00 28.25  ? 495 HOH A O   1 
HETATM 2356 O  O   . HOH J 6 .   ? -21.539 -7.198  23.675  1.00 12.62  ? 496 HOH A O   1 
HETATM 2357 O  O   . HOH J 6 .   ? 0.827   3.010   9.369   1.00 24.17  ? 497 HOH A O   1 
HETATM 2358 O  O   . HOH J 6 .   ? -6.627  -5.307  37.501  1.00 19.58  ? 498 HOH A O   1 
HETATM 2359 O  O   . HOH J 6 .   ? -23.401 -13.266 11.365  1.00 19.69  ? 499 HOH A O   1 
HETATM 2360 O  O   . HOH J 6 .   ? -3.422  -11.199 20.931  1.00 10.70  ? 500 HOH A O   1 
HETATM 2361 O  O   . HOH J 6 .   ? -16.019 -12.376 24.455  1.00 14.46  ? 501 HOH A O   1 
HETATM 2362 O  O   . HOH J 6 .   ? 1.443   -11.813 25.185  1.00 25.30  ? 502 HOH A O   1 
HETATM 2363 O  O   . HOH J 6 .   ? -16.057 15.854  23.797  1.00 16.63  ? 503 HOH A O   1 
HETATM 2364 O  O   . HOH J 6 .   ? -3.759  -15.916 24.384  1.00 12.70  ? 504 HOH A O   1 
HETATM 2365 O  O   . HOH J 6 .   ? 4.385   -6.518  7.829   1.00 24.56  ? 505 HOH A O   1 
HETATM 2366 O  O   . HOH J 6 .   ? -25.955 -6.325  13.141  1.00 24.16  ? 506 HOH A O   1 
HETATM 2367 O  O   . HOH J 6 .   ? -17.926 -20.405 8.035   1.00 14.47  ? 507 HOH A O   1 
HETATM 2368 O  O   . HOH J 6 .   ? -26.168 -7.646  30.576  1.00 33.91  ? 508 HOH A O   1 
HETATM 2369 O  O   . HOH J 6 .   ? -0.348  13.723  16.043  1.00 26.39  ? 509 HOH A O   1 
HETATM 2370 O  O   . HOH J 6 .   ? -18.600 -3.790  -2.679  1.00 29.54  ? 510 HOH A O   1 
HETATM 2371 O  O   . HOH J 6 .   ? -0.397  10.782  23.439  1.00 16.04  ? 511 HOH A O   1 
HETATM 2372 O  O   . HOH J 6 .   ? -19.397 10.071  8.895   1.00 15.37  ? 512 HOH A O   1 
HETATM 2373 O  O   . HOH J 6 .   ? -3.329  -13.295 25.220  1.00 10.95  ? 513 HOH A O   1 
HETATM 2374 O  O   . HOH J 6 .   ? -22.076 5.714   4.782   1.00 18.73  ? 514 HOH A O   1 
HETATM 2375 O  O   . HOH J 6 .   ? -26.745 -2.583  14.560  1.00 21.02  ? 515 HOH A O   1 
HETATM 2376 O  O   . HOH J 6 .   ? 4.303   4.392   10.939  1.00 32.71  ? 516 HOH A O   1 
HETATM 2377 O  O   . HOH J 6 .   ? -23.348 -3.019  6.753   1.00 21.57  ? 517 HOH A O   1 
HETATM 2378 O  O   . HOH J 6 .   ? -19.991 15.857  19.019  1.00 31.85  ? 518 HOH A O   1 
HETATM 2379 O  O   . HOH J 6 .   ? 13.127  -3.877  13.558  1.00 28.80  ? 519 HOH A O   1 
HETATM 2380 O  O   . HOH J 6 .   ? -24.894 -7.719  9.124   1.00 19.54  ? 520 HOH A O   1 
HETATM 2381 O  O   . HOH J 6 .   ? 2.595   -13.172 5.227   1.00 23.44  ? 521 HOH A O   1 
HETATM 2382 O  O   . HOH J 6 .   ? -4.394  -4.581  10.900  1.00 15.92  ? 522 HOH A O   1 
HETATM 2383 O  O   . HOH J 6 .   ? -0.234  -14.369 22.254  1.00 20.85  ? 523 HOH A O   1 
HETATM 2384 O  O   . HOH J 6 .   ? 13.213  -5.791  24.606  1.00 26.99  ? 524 HOH A O   1 
HETATM 2385 O  O   . HOH J 6 .   ? 7.621   -7.595  -0.699  1.00 29.63  ? 525 HOH A O   1 
HETATM 2386 O  O   . HOH J 6 .   ? 0.436   -19.521 10.851  1.00 31.92  ? 526 HOH A O   1 
HETATM 2387 O  O   . HOH J 6 .   ? -13.365 -18.518 14.592  1.00 15.08  ? 527 HOH A O   1 
HETATM 2388 O  O   . HOH J 6 .   ? -7.169  -16.719 1.612   1.00 21.76  ? 528 HOH A O   1 
HETATM 2389 O  O   . HOH J 6 .   ? -4.572  -15.878 0.947   1.00 29.67  ? 529 HOH A O   1 
HETATM 2390 O  O   . HOH J 6 .   ? -17.222 -7.411  39.698  1.00 32.98  ? 530 HOH A O   1 
HETATM 2391 O  O   . HOH J 6 .   ? 8.711   -3.879  21.193  1.00 15.50  ? 531 HOH A O   1 
HETATM 2392 O  O   . HOH J 6 .   ? -7.384  -8.687  32.673  1.00 17.51  ? 532 HOH A O   1 
HETATM 2393 O  O   . HOH J 6 .   ? 11.394  -3.758  7.793   1.00 31.18  ? 533 HOH A O   1 
HETATM 2394 O  O   . HOH J 6 .   ? -15.761 3.724   35.283  1.00 30.70  ? 534 HOH A O   1 
HETATM 2395 O  O   . HOH J 6 .   ? -23.140 -0.425  34.525  1.00 30.10  ? 535 HOH A O   1 
HETATM 2396 O  O   . HOH J 6 .   ? 1.956   4.295   11.869  1.00 26.76  ? 536 HOH A O   1 
HETATM 2397 O  O   . HOH J 6 .   ? -3.469  -12.938 -2.733  1.00 27.86  ? 537 HOH A O   1 
HETATM 2398 O  O   . HOH J 6 .   ? -7.545  5.858   8.371   1.00 28.04  ? 538 HOH A O   1 
HETATM 2399 O  O   . HOH J 6 .   ? 0.083   -14.266 31.246  1.00 31.27  ? 539 HOH A O   1 
HETATM 2400 O  O   . HOH J 6 .   ? -10.126 14.649  12.194  1.00 17.36  ? 540 HOH A O   1 
HETATM 2401 O  O   . HOH J 6 .   ? 7.036   -2.803  6.975   1.00 33.34  ? 541 HOH A O   1 
HETATM 2402 O  O   . HOH J 6 .   ? 14.089  5.600   19.219  1.00 31.99  ? 542 HOH A O   1 
HETATM 2403 O  O   . HOH J 6 .   ? -3.032  4.705   7.640   1.00 26.22  ? 543 HOH A O   1 
HETATM 2404 O  O   . HOH J 6 .   ? -10.559 -19.456 20.092  1.00 17.79  ? 544 HOH A O   1 
HETATM 2405 O  O   . HOH J 6 .   ? 11.304  1.337   26.178  1.00 24.37  ? 545 HOH A O   1 
HETATM 2406 O  O   . HOH J 6 .   ? -12.998 -16.867 26.708  1.00 14.83  ? 546 HOH A O   1 
HETATM 2407 O  O   . HOH J 6 .   ? -0.218  -20.501 14.848  1.00 38.49  ? 547 HOH A O   1 
HETATM 2408 O  O   . HOH J 6 .   ? -23.319 -11.102 17.164  1.00 27.94  ? 548 HOH A O   1 
HETATM 2409 O  O   . HOH J 6 .   ? -16.352 -9.930  33.016  1.00 17.63  ? 549 HOH A O   1 
HETATM 2410 O  O   . HOH J 6 .   ? -11.709 -3.131  42.372  1.00 28.35  ? 550 HOH A O   1 
HETATM 2411 O  O   . HOH J 6 .   ? -26.181 3.418   15.516  1.00 27.49  ? 551 HOH A O   1 
HETATM 2412 O  O   . HOH J 6 .   ? -9.544  -8.004  34.177  1.00 23.19  ? 552 HOH A O   1 
HETATM 2413 O  O   . HOH J 6 .   ? 5.007   -4.928  21.107  1.00 14.62  ? 553 HOH A O   1 
HETATM 2414 O  O   . HOH J 6 .   ? -8.466  -19.853 26.728  1.00 20.39  ? 554 HOH A O   1 
HETATM 2415 O  O   . HOH J 6 .   ? -6.981  -8.498  -6.998  1.00 33.73  ? 555 HOH A O   1 
HETATM 2416 O  O   . HOH J 6 .   ? -14.756 6.087   32.839  1.00 39.84  ? 556 HOH A O   1 
HETATM 2417 O  O   . HOH J 6 .   ? -6.127  -19.715 23.878  1.00 21.51  ? 557 HOH A O   1 
HETATM 2418 O  O   . HOH J 6 .   ? -25.735 -3.486  32.088  1.00 45.03  ? 558 HOH A O   1 
HETATM 2419 O  O   . HOH J 6 .   ? -23.958 -0.719  26.575  1.00 17.81  ? 559 HOH A O   1 
HETATM 2420 O  O   . HOH J 6 .   ? 1.339   8.809   24.426  1.00 17.17  ? 560 HOH A O   1 
HETATM 2421 O  O   . HOH J 6 .   ? -7.969  -22.197 10.476  1.00 19.79  ? 561 HOH A O   1 
HETATM 2422 O  O   . HOH J 6 .   ? 5.218   -12.745 -5.543  1.00 30.17  ? 562 HOH A O   1 
HETATM 2423 O  O   . HOH J 6 .   ? -11.886 2.740   30.947  1.00 18.63  ? 563 HOH A O   1 
HETATM 2424 O  O   . HOH J 6 .   ? 7.076   -3.663  30.149  1.00 39.52  ? 564 HOH A O   1 
HETATM 2425 O  O   . HOH J 6 .   ? -11.061 1.085   33.522  1.00 22.56  ? 565 HOH A O   1 
HETATM 2426 O  O   . HOH J 6 .   ? -12.736 16.188  7.851   1.00 34.10  ? 566 HOH A O   1 
HETATM 2427 O  O   . HOH J 6 .   ? 3.677   -3.018  4.426   1.00 32.60  ? 567 HOH A O   1 
HETATM 2428 O  O   . HOH J 6 .   ? -12.709 7.900   28.950  1.00 25.08  ? 568 HOH A O   1 
HETATM 2429 O  O   . HOH J 6 .   ? -17.185 -1.027  40.329  1.00 38.77  ? 569 HOH A O   1 
HETATM 2430 O  O   . HOH J 6 .   ? -23.918 -0.793  3.972   1.00 23.80  ? 570 HOH A O   1 
HETATM 2431 O  O   . HOH J 6 .   ? 5.128   -7.377  22.466  1.00 27.16  ? 571 HOH A O   1 
HETATM 2432 O  O   . HOH J 6 .   ? -9.041  -5.845  36.020  1.00 19.24  ? 572 HOH A O   1 
HETATM 2433 O  O   . HOH J 6 .   ? -12.876 -8.912  -3.238  1.00 30.03  ? 573 HOH A O   1 
HETATM 2434 O  O   . HOH J 6 .   ? -21.189 -19.649 6.713   1.00 26.43  ? 574 HOH A O   1 
HETATM 2435 O  O   . HOH J 6 .   ? -0.716  9.033   14.596  1.00 30.94  ? 575 HOH A O   1 
HETATM 2436 O  O   . HOH J 6 .   ? -0.501  -8.574  32.671  1.00 25.15  ? 576 HOH A O   1 
HETATM 2437 O  O   . HOH J 6 .   ? 1.315   -1.544  29.592  1.00 14.26  ? 577 HOH A O   1 
HETATM 2438 O  O   . HOH J 6 .   ? -0.866  -17.421 18.052  1.00 30.88  ? 578 HOH A O   1 
HETATM 2439 O  O   . HOH J 6 .   ? -18.589 19.960  14.770  1.00 23.63  ? 579 HOH A O   1 
HETATM 2440 O  O   . HOH J 6 .   ? 3.693   -1.615  8.745   1.00 24.71  ? 580 HOH A O   1 
HETATM 2441 O  O   . HOH J 6 .   ? -22.943 -11.753 14.075  1.00 22.93  ? 581 HOH A O   1 
HETATM 2442 O  O   . HOH J 6 .   ? 8.188   3.288   27.933  1.00 33.24  ? 582 HOH A O   1 
HETATM 2443 O  O   . HOH J 6 .   ? -2.017  -12.334 22.938  1.00 10.87  ? 583 HOH A O   1 
HETATM 2444 O  O   . HOH J 6 .   ? -27.214 -10.808 22.661  1.00 38.25  ? 584 HOH A O   1 
HETATM 2445 O  O   . HOH J 6 .   ? -5.915  15.252  11.908  1.00 30.68  ? 585 HOH A O   1 
HETATM 2446 O  O   . HOH J 6 .   ? -11.035 9.037   7.566   1.00 29.12  ? 586 HOH A O   1 
HETATM 2447 O  O   . HOH J 6 .   ? -8.093  -19.364 21.705  1.00 14.11  ? 587 HOH A O   1 
HETATM 2448 O  O   . HOH J 6 .   ? -30.785 -7.191  22.532  1.00 32.04  ? 588 HOH A O   1 
HETATM 2449 O  O   . HOH J 6 .   ? -24.792 -11.179 24.071  1.00 35.56  ? 589 HOH A O   1 
HETATM 2450 O  O   . HOH J 6 .   ? -6.912  1.472   35.264  1.00 24.68  ? 590 HOH A O   1 
HETATM 2451 O  O   . HOH J 6 .   ? 2.815   -14.430 0.810   1.00 37.44  ? 591 HOH A O   1 
HETATM 2452 O  O   . HOH J 6 .   ? -13.804 14.118  27.313  1.00 22.67  ? 592 HOH A O   1 
HETATM 2453 O  O   . HOH J 6 .   ? -12.988 3.525   -6.889  1.00 26.58  ? 593 HOH A O   1 
HETATM 2454 O  O   . HOH J 6 .   ? 1.886   -4.237  -12.339 1.00 33.32  ? 594 HOH A O   1 
HETATM 2455 O  O   . HOH J 6 .   ? 9.678   1.951   12.172  1.00 31.22  ? 595 HOH A O   1 
HETATM 2456 O  O   . HOH J 6 .   ? -16.889 19.159  22.080  1.00 52.06  ? 596 HOH A O   1 
HETATM 2457 O  O   . HOH J 6 .   ? -2.322  21.877  21.327  1.00 30.41  ? 597 HOH A O   1 
HETATM 2458 O  O   . HOH J 6 .   ? -15.183 -20.114 22.930  1.00 33.43  ? 598 HOH A O   1 
HETATM 2459 O  O   . HOH J 6 .   ? 7.733   6.067   21.783  1.00 17.35  ? 599 HOH A O   1 
HETATM 2460 O  O   . HOH J 6 .   ? -10.836 -4.956  38.375  1.00 95.49  ? 600 HOH A O   1 
HETATM 2461 O  O   . HOH J 6 .   ? -21.873 19.494  12.100  1.00 31.92  ? 601 HOH A O   1 
HETATM 2462 O  O   . HOH J 6 .   ? -17.048 0.185   -4.071  1.00 43.82  ? 602 HOH A O   1 
HETATM 2463 O  O   . HOH J 6 .   ? -24.710 -9.453  1.898   1.00 25.15  ? 603 HOH A O   1 
HETATM 2464 O  O   . HOH J 6 .   ? 6.655   -5.851  6.748   1.00 34.83  ? 604 HOH A O   1 
HETATM 2465 O  O   . HOH J 6 .   ? -1.441  11.456  25.959  1.00 26.10  ? 605 HOH A O   1 
HETATM 2466 O  O   . HOH J 6 .   ? -18.513 -9.025  34.624  1.00 31.79  ? 606 HOH A O   1 
HETATM 2467 O  O   . HOH J 6 .   ? -21.818 19.678  17.465  1.00 39.29  ? 607 HOH A O   1 
HETATM 2468 O  O   . HOH J 6 .   ? 15.235  -10.272 14.627  1.00 32.48  ? 608 HOH A O   1 
HETATM 2469 O  O   . HOH J 6 .   ? 2.898   -4.204  7.511   1.00 28.25  ? 609 HOH A O   1 
HETATM 2470 O  O   . HOH J 6 .   ? -18.572 3.880   -3.907  1.00 90.48  ? 610 HOH A O   1 
HETATM 2471 O  O   . HOH J 6 .   ? -13.752 -23.026 11.237  1.00 35.54  ? 611 HOH A O   1 
HETATM 2472 O  O   . HOH J 6 .   ? 3.069   1.134   -1.910  1.00 56.90  ? 612 HOH A O   1 
HETATM 2473 O  O   . HOH J 6 .   ? 10.152  -13.408 9.479   1.00 43.19  ? 613 HOH A O   1 
HETATM 2474 O  O   . HOH J 6 .   ? -22.405 -12.329 24.953  1.00 28.74  ? 614 HOH A O   1 
HETATM 2475 O  O   . HOH J 6 .   ? 0.414   0.611   -6.798  1.00 96.02  ? 615 HOH A O   1 
HETATM 2476 O  O   . HOH J 6 .   ? -22.746 15.391  19.427  1.00 41.62  ? 616 HOH A O   1 
HETATM 2477 O  O   . HOH J 6 .   ? -24.442 4.817   7.958   1.00 37.73  ? 617 HOH A O   1 
HETATM 2478 O  O   . HOH J 6 .   ? -7.235  16.693  10.555  1.00 37.41  ? 618 HOH A O   1 
HETATM 2479 O  O   . HOH J 6 .   ? -2.798  -14.899 32.870  1.00 34.66  ? 619 HOH A O   1 
HETATM 2480 O  O   . HOH J 6 .   ? 10.358  -2.592  14.131  1.00 27.19  ? 620 HOH A O   1 
HETATM 2481 O  O   . HOH J 6 .   ? -11.226 -23.646 12.287  1.00 20.42  ? 621 HOH A O   1 
HETATM 2482 O  O   . HOH J 6 .   ? 8.672   2.467   30.763  1.00 44.54  ? 622 HOH A O   1 
HETATM 2483 O  O   . HOH J 6 .   ? -12.810 -17.216 16.852  1.00 13.55  ? 623 HOH A O   1 
HETATM 2484 O  O   . HOH J 6 .   ? 12.058  -6.574  8.080   1.00 27.84  ? 624 HOH A O   1 
HETATM 2485 O  O   . HOH J 6 .   ? 10.315  -8.635  8.369   1.00 25.79  ? 625 HOH A O   1 
HETATM 2486 O  O   . HOH J 6 .   ? -15.226 -16.093 25.403  1.00 37.42  ? 626 HOH A O   1 
HETATM 2487 O  O   . HOH J 6 .   ? -31.675 5.479   13.091  1.00 44.41  ? 627 HOH A O   1 
HETATM 2488 O  O   . HOH J 6 .   ? -3.398  17.548  13.971  1.00 37.95  ? 628 HOH A O   1 
HETATM 2489 O  O   . HOH J 6 .   ? -26.411 4.661   6.222   1.00 43.35  ? 629 HOH A O   1 
HETATM 2490 O  O   . HOH J 6 .   ? 8.709   -4.607  23.795  1.00 24.96  ? 630 HOH A O   1 
HETATM 2491 O  O   . HOH J 6 .   ? -0.143  -3.047  39.595  1.00 54.12  ? 631 HOH A O   1 
HETATM 2492 O  O   . HOH J 6 .   ? -23.799 8.075   3.504   1.00 31.89  ? 632 HOH A O   1 
HETATM 2493 O  O   . HOH J 6 .   ? 5.391   -10.752 18.806  1.00 38.77  ? 633 HOH A O   1 
HETATM 2494 O  O   . HOH J 6 .   ? -25.171 11.138  19.713  1.00 30.37  ? 634 HOH A O   1 
HETATM 2495 O  O   . HOH J 6 .   ? 14.651  0.048   15.105  1.00 37.18  ? 635 HOH A O   1 
HETATM 2496 O  O   . HOH J 6 .   ? -5.696  -12.475 -5.165  1.00 37.58  ? 636 HOH A O   1 
HETATM 2497 O  O   . HOH J 6 .   ? -17.572 -19.415 35.169  1.00 25.49  ? 637 HOH A O   1 
HETATM 2498 O  O   . HOH J 6 .   ? -23.752 -3.460  3.878   1.00 37.76  ? 638 HOH A O   1 
HETATM 2499 O  O   . HOH J 6 .   ? -17.660 19.794  17.570  1.00 24.16  ? 639 HOH A O   1 
HETATM 2500 O  O   . HOH J 6 .   ? -1.350  -13.103 27.146  1.00 24.23  ? 640 HOH A O   1 
HETATM 2501 O  O   . HOH J 6 .   ? -25.016 8.765   26.177  1.00 39.51  ? 641 HOH A O   1 
HETATM 2502 O  O   . HOH J 6 .   ? -1.209  7.467   9.959   1.00 54.76  ? 642 HOH A O   1 
HETATM 2503 O  O   . HOH J 6 .   ? 0.902   3.364   2.017   1.00 34.43  ? 643 HOH A O   1 
HETATM 2504 O  O   . HOH J 6 .   ? -8.717  7.994   8.351   1.00 32.78  ? 644 HOH A O   1 
HETATM 2505 O  O   . HOH J 6 .   ? 2.942   -13.503 8.100   1.00 29.17  ? 645 HOH A O   1 
HETATM 2506 O  O   . HOH J 6 .   ? 15.398  -3.982  25.173  1.00 22.03  ? 646 HOH A O   1 
HETATM 2507 O  O   . HOH J 6 .   ? 6.482   -5.434  27.469  1.00 38.62  ? 647 HOH A O   1 
HETATM 2508 O  O   . HOH J 6 .   ? -21.042 -0.031  -1.927  1.00 38.75  ? 648 HOH A O   1 
HETATM 2509 O  O   . HOH J 6 .   ? -4.806  20.382  21.496  1.00 22.75  ? 649 HOH A O   1 
HETATM 2510 O  O   . HOH J 6 .   ? -16.850 -17.973 20.108  1.00 26.74  ? 650 HOH A O   1 
HETATM 2511 O  O   . HOH J 6 .   ? -27.442 -7.035  7.656   1.00 38.66  ? 651 HOH A O   1 
HETATM 2512 O  O   . HOH J 6 .   ? 0.643   -15.925 24.129  1.00 51.72  ? 652 HOH A O   1 
HETATM 2513 O  O   . HOH J 6 .   ? -17.867 -12.155 31.891  1.00 35.43  ? 653 HOH A O   1 
HETATM 2514 O  O   . HOH J 6 .   ? -10.539 4.927   31.001  1.00 22.42  ? 654 HOH A O   1 
HETATM 2515 O  O   . HOH J 6 .   ? -2.033  -17.526 25.690  1.00 24.86  ? 655 HOH A O   1 
HETATM 2516 O  O   . HOH J 6 .   ? -24.376 13.597  20.554  1.00 34.91  ? 656 HOH A O   1 
HETATM 2517 O  O   . HOH J 6 .   ? -1.399  4.472   2.273   1.00 33.89  ? 657 HOH A O   1 
HETATM 2518 O  O   . HOH J 6 .   ? -9.714  15.703  8.080   1.00 38.21  ? 658 HOH A O   1 
HETATM 2519 O  O   . HOH J 6 .   ? 15.482  -1.238  26.075  1.00 23.50  ? 659 HOH A O   1 
HETATM 2520 O  O   . HOH J 6 .   ? -2.012  -11.813 31.668  1.00 31.74  ? 660 HOH A O   1 
HETATM 2521 O  O   . HOH J 6 .   ? -24.096 -7.025  0.336   1.00 35.08  ? 661 HOH A O   1 
HETATM 2522 O  O   . HOH J 6 .   ? -11.552 0.920   -7.764  1.00 39.84  ? 662 HOH A O   1 
HETATM 2523 O  O   . HOH J 6 .   ? -5.907  -20.823 26.229  1.00 25.87  ? 663 HOH A O   1 
HETATM 2524 O  O   . HOH J 6 .   ? 1.862   -9.777  31.355  1.00 50.47  ? 664 HOH A O   1 
HETATM 2525 O  O   . HOH J 6 .   ? -0.993  -13.210 33.178  1.00 27.29  ? 665 HOH A O   1 
HETATM 2526 O  O   . HOH J 6 .   ? -8.078  14.535  10.468  1.00 34.08  ? 666 HOH A O   1 
HETATM 2527 O  O   . HOH J 6 .   ? -13.736 -21.210 15.152  1.00 17.49  ? 667 HOH A O   1 
HETATM 2528 O  O   . HOH J 6 .   ? 12.407  7.810   20.821  1.00 55.22  ? 668 HOH A O   1 
HETATM 2529 O  O   . HOH J 6 .   ? -10.448 -20.304 25.027  1.00 18.91  ? 669 HOH A O   1 
HETATM 2530 O  O   . HOH J 6 .   ? -14.121 3.549   33.266  1.00 27.93  ? 670 HOH A O   1 
HETATM 2531 O  O   . HOH J 6 .   ? -9.183  3.085   34.848  1.00 26.65  ? 671 HOH A O   1 
HETATM 2532 O  O   . HOH J 6 .   ? -12.315 13.321  4.988   1.00 32.86  ? 672 HOH A O   1 
HETATM 2533 O  O   . HOH J 6 .   ? 1.526   -17.484 7.168   1.00 31.57  ? 673 HOH A O   1 
HETATM 2534 O  O   . HOH J 6 .   ? -11.690 10.850  0.741   1.00 29.58  ? 674 HOH A O   1 
HETATM 2535 O  O   . HOH J 6 .   ? -14.902 -21.114 17.676  1.00 17.61  ? 675 HOH A O   1 
HETATM 2536 O  O   . HOH J 6 .   ? -5.567  -9.398  34.546  1.00 80.94  ? 676 HOH A O   1 
HETATM 2537 O  O   . HOH J 6 .   ? -1.146  -11.182 29.076  1.00 17.69  ? 677 HOH A O   1 
HETATM 2538 O  O   . HOH J 6 .   ? -18.952 14.085  35.314  1.00 32.29  ? 678 HOH A O   1 
HETATM 2539 O  O   . HOH J 6 .   ? -16.530 -14.692 28.806  1.00 36.81  ? 679 HOH A O   1 
HETATM 2540 O  O   . HOH J 6 .   ? 5.868   -14.199 9.050   1.00 39.24  ? 680 HOH A O   1 
HETATM 2541 O  O   . HOH J 6 .   ? -21.207 20.660  14.897  1.00 38.40  ? 681 HOH A O   1 
HETATM 2542 O  O   . HOH J 6 .   ? -16.044 17.344  26.239  1.00 36.52  ? 682 HOH A O   1 
HETATM 2543 O  O   . HOH J 6 .   ? 2.302   -19.879 16.359  1.00 57.71  ? 683 HOH A O   1 
HETATM 2544 O  O   . HOH J 6 .   ? -0.381  -6.999  -7.444  1.00 42.18  ? 684 HOH A O   1 
HETATM 2545 O  O   . HOH J 6 .   ? 6.565   8.518   18.153  1.00 39.02  ? 685 HOH A O   1 
HETATM 2546 O  O   . HOH J 6 .   ? -10.189 15.075  6.049   1.00 34.79  ? 686 HOH A O   1 
HETATM 2547 O  O   . HOH J 6 .   ? -28.665 0.159   24.555  1.00 22.89  ? 687 HOH A O   1 
HETATM 2548 O  O   . HOH J 6 .   ? -3.763  -15.610 -1.941  1.00 37.97  ? 688 HOH A O   1 
HETATM 2549 O  O   . HOH J 6 .   ? 6.352   5.664   29.047  1.00 82.58  ? 689 HOH A O   1 
HETATM 2550 O  O   . HOH J 6 .   ? -1.356  -17.180 4.767   1.00 39.11  ? 690 HOH A O   1 
HETATM 2551 O  O   . HOH J 6 .   ? -12.822 -19.555 26.231  1.00 26.18  ? 691 HOH A O   1 
HETATM 2552 O  O   . HOH J 6 .   ? -6.295  12.228  10.387  1.00 43.68  ? 692 HOH A O   1 
HETATM 2553 O  O   . HOH J 6 .   ? -3.191  -19.916 26.995  1.00 35.21  ? 693 HOH A O   1 
HETATM 2554 O  O   . HOH J 6 .   ? 5.570   9.193   21.821  1.00 35.19  ? 694 HOH A O   1 
HETATM 2555 O  O   . HOH J 6 .   ? -2.708  -9.422  34.623  1.00 43.94  ? 695 HOH A O   1 
HETATM 2556 O  O   . HOH J 6 .   ? 14.274  -1.431  28.528  1.00 31.99  ? 696 HOH A O   1 
HETATM 2557 O  O   . HOH J 6 .   ? -26.511 -11.598 2.212   1.00 27.53  ? 697 HOH A O   1 
HETATM 2558 O  O   . HOH J 6 .   ? 1.310   -21.762 12.982  1.00 46.48  ? 698 HOH A O   1 
HETATM 2559 O  O   . HOH J 6 .   ? 3.877   9.861   23.853  1.00 27.44  ? 699 HOH A O   1 
HETATM 2560 O  O   . HOH J 6 .   ? -2.294  -11.974 34.901  1.00 67.46  ? 700 HOH A O   1 
HETATM 2561 O  O   . HOH J 6 .   ? -0.762  6.539   43.412  1.00 20.34  ? 701 HOH A O   1 
HETATM 2562 O  O   . HOH J 6 .   ? -12.163 13.767  1.844   1.00 35.23  ? 702 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   ? 0.2460 0.3713 0.3299 0.0192  0.0168  -0.0120 3   HIS A N   
2    C  CA  . HIS A 3   ? 0.2465 0.3450 0.3357 0.0267  -0.0035 0.0295  3   HIS A CA  
3    C  C   . HIS A 3   ? 0.3540 0.3568 0.3045 0.0008  0.0899  0.0675  3   HIS A C   
4    O  O   . HIS A 3   ? 0.4108 0.4154 0.3744 -0.0168 -0.0564 -0.0408 3   HIS A O   
5    C  CB  . HIS A 3   ? 0.2857 0.2843 0.3201 -0.0566 -0.0494 0.0320  3   HIS A CB  
6    C  CG  . HIS A 3   ? 0.2782 0.3033 0.3091 -0.0284 -0.0019 0.0116  3   HIS A CG  
7    N  ND1 . HIS A 3   ? 0.3205 0.3198 0.3342 -0.0206 -0.0035 0.0109  3   HIS A ND1 
8    C  CD2 . HIS A 3   ? 0.3007 0.2964 0.2717 -0.0082 -0.0263 -0.0100 3   HIS A CD2 
9    C  CE1 . HIS A 3   ? 0.2839 0.3062 0.3073 -0.0245 -0.0093 -0.0046 3   HIS A CE1 
10   N  NE2 . HIS A 3   ? 0.3396 0.3537 0.3600 0.0008  0.0114  -0.0020 3   HIS A NE2 
11   N  N   . HIS A 4   ? 0.3246 0.6789 0.8246 0.0788  0.1103  0.2522  4   HIS A N   
12   C  CA  . HIS A 4   ? 0.3292 0.3436 0.5871 -0.0329 0.2230  0.1081  4   HIS A CA  
13   C  C   . HIS A 4   ? 0.2143 0.2555 0.2642 -0.0658 0.0737  -0.0081 4   HIS A C   
14   O  O   . HIS A 4   ? 0.2109 0.2471 0.2595 -0.0126 0.0789  0.0141  4   HIS A O   
15   C  CB  . HIS A 4   ? 0.2426 1.1375 1.2520 0.1588  0.1392  0.3176  4   HIS A CB  
16   C  CG  . HIS A 4   ? 0.7860 0.8561 1.2266 0.0165  0.1674  0.2973  4   HIS A CG  
17   N  ND1 . HIS A 4   ? 0.9689 1.0537 1.4464 0.0119  -0.0781 0.4181  4   HIS A ND1 
18   C  CD2 . HIS A 4   ? 0.7228 1.4072 1.1155 -0.0812 -0.3088 0.6927  4   HIS A CD2 
19   C  CE1 . HIS A 4   ? 0.9552 0.9549 2.1366 0.0304  -0.2858 0.4045  4   HIS A CE1 
20   N  NE2 . HIS A 4   ? 0.9046 1.5198 2.1333 0.0666  -0.4386 0.5406  4   HIS A NE2 
21   N  N   . TRP A 5   ? 0.1539 0.2480 0.2511 -0.0285 0.0731  0.0176  5   TRP A N   
22   C  CA  . TRP A 5   ? 0.1466 0.2109 0.2153 -0.0359 0.0509  0.0041  5   TRP A CA  
23   C  C   . TRP A 5   ? 0.1445 0.2050 0.1687 -0.0080 0.0381  0.0122  5   TRP A C   
24   O  O   . TRP A 5   ? 0.1878 0.2125 0.1987 -0.0247 0.0333  -0.0093 5   TRP A O   
25   C  CB  . TRP A 5   ? 0.1261 0.2018 0.1942 -0.0153 0.0153  -0.0099 5   TRP A CB  
26   C  CG  . TRP A 5   ? 0.1572 0.1641 0.1700 -0.0394 0.0368  -0.0021 5   TRP A CG  
27   C  CD1 . TRP A 5   ? 0.2017 0.2011 0.1996 -0.0447 0.0288  0.0024  5   TRP A CD1 
28   C  CD2 . TRP A 5   ? 0.1307 0.1783 0.1473 -0.0015 0.0098  -0.0115 5   TRP A CD2 
29   N  NE1 . TRP A 5   ? 0.1975 0.1704 0.1806 -0.0218 0.0262  0.0175  5   TRP A NE1 
30   C  CE2 . TRP A 5   ? 0.1732 0.1750 0.1513 -0.0046 0.0206  0.0063  5   TRP A CE2 
31   C  CE3 . TRP A 5   ? 0.1341 0.1729 0.1460 -0.0317 0.0263  -0.0271 5   TRP A CE3 
32   C  CZ2 . TRP A 5   ? 0.1854 0.2268 0.1451 0.0181  -0.0055 0.0193  5   TRP A CZ2 
33   C  CZ3 . TRP A 5   ? 0.1525 0.1717 0.1515 -0.0120 0.0099  -0.0406 5   TRP A CZ3 
34   C  CH2 . TRP A 5   ? 0.1909 0.2190 0.1293 0.0077  0.0149  -0.0222 5   TRP A CH2 
35   N  N   . GLY A 6   ? 0.1764 0.1674 0.1859 -0.0038 0.0670  -0.0137 6   GLY A N   
36   C  CA  . GLY A 6   ? 0.1878 0.1820 0.2067 -0.0240 0.0636  -0.0355 6   GLY A CA  
37   C  C   . GLY A 6   ? 0.1616 0.1763 0.2022 -0.0059 0.0769  -0.0281 6   GLY A C   
38   O  O   . GLY A 6   ? 0.1395 0.1820 0.2098 0.0116  0.0445  0.0010  6   GLY A O   
39   N  N   A TYR A 7   ? 0.1653 0.1277 0.1669 0.0244  0.0516  -0.0070 7   TYR A N   
40   N  N   B TYR A 7   ? 0.1488 0.1730 0.3625 -0.0381 0.0996  -0.0480 7   TYR A N   
41   C  CA  A TYR A 7   ? 0.1016 0.1254 0.1451 -0.0046 0.0024  -0.0006 7   TYR A CA  
42   C  CA  B TYR A 7   ? 0.1207 0.1852 0.1985 -0.0010 -0.0062 -0.0668 7   TYR A CA  
43   C  C   A TYR A 7   ? 0.1630 0.1298 0.3055 -0.0243 0.1018  0.0170  7   TYR A C   
44   C  C   B TYR A 7   ? 0.1500 0.2001 0.2601 0.0225  -0.0183 -0.0917 7   TYR A C   
45   O  O   A TYR A 7   ? 0.1278 0.1474 0.3360 0.0199  -0.0111 -0.0043 7   TYR A O   
46   O  O   B TYR A 7   ? 0.1063 0.1464 0.5895 -0.0309 0.1006  -0.1168 7   TYR A O   
47   C  CB  A TYR A 7   ? 0.0828 0.1288 0.1639 0.0156  0.0320  -0.0119 7   TYR A CB  
48   C  CB  B TYR A 7   ? 0.1256 0.1985 0.1967 0.0251  -0.0185 -0.0559 7   TYR A CB  
49   C  CG  A TYR A 7   ? 0.1009 0.0954 0.1102 0.0007  0.0166  0.0035  7   TYR A CG  
50   C  CG  B TYR A 7   ? 0.1484 0.1572 0.1879 -0.0071 0.0148  -0.0278 7   TYR A CG  
51   C  CD1 A TYR A 7   ? 0.1206 0.1219 0.1019 -0.0077 0.0099  -0.0148 7   TYR A CD1 
52   C  CD1 B TYR A 7   ? 0.1084 0.1726 0.1835 -0.0091 0.0211  -0.0130 7   TYR A CD1 
53   C  CD2 A TYR A 7   ? 0.1221 0.0954 0.1095 -0.0057 -0.0162 -0.0204 7   TYR A CD2 
54   C  CD2 B TYR A 7   ? 0.1488 0.2118 0.1431 -0.0006 0.0271  -0.0155 7   TYR A CD2 
55   C  CE1 A TYR A 7   ? 0.0910 0.1036 0.1050 -0.0043 -0.0015 0.0041  7   TYR A CE1 
56   C  CE1 B TYR A 7   ? 0.1230 0.1421 0.1948 -0.0179 0.0098  -0.0099 7   TYR A CE1 
57   C  CE2 A TYR A 7   ? 0.0971 0.1226 0.1226 -0.0121 0.0144  -0.0142 7   TYR A CE2 
58   C  CE2 B TYR A 7   ? 0.1705 0.1923 0.1277 -0.0277 0.0209  -0.0288 7   TYR A CE2 
59   C  CZ  A TYR A 7   ? 0.1076 0.0984 0.1185 -0.0041 0.0125  -0.0051 7   TYR A CZ  
60   C  CZ  B TYR A 7   ? 0.1380 0.1580 0.1149 -0.0273 0.0032  -0.0406 7   TYR A CZ  
61   O  OH  A TYR A 7   ? 0.1325 0.1125 0.1089 0.0000  0.0175  -0.0135 7   TYR A OH  
62   O  OH  B TYR A 7   ? 0.1684 0.1343 0.1722 -0.0136 -0.0077 -0.0222 7   TYR A OH  
63   N  N   A GLY A 8   ? 0.1836 0.1380 0.4826 -0.0190 0.1888  -0.0597 8   GLY A N   
64   N  N   B GLY A 8   ? 0.1870 0.3759 0.2238 0.1120  -0.0293 -0.0262 8   GLY A N   
65   C  CA  A GLY A 8   ? 0.1890 0.2922 0.4029 -0.0148 0.0197  0.0340  8   GLY A CA  
66   C  CA  B GLY A 8   ? 0.0869 0.1984 0.1638 0.0024  -0.0063 -0.0361 8   GLY A CA  
67   C  C   A GLY A 8   ? 0.1592 0.1964 0.2419 -0.0017 0.0535  -0.0471 8   GLY A C   
68   C  C   B GLY A 8   ? 0.3583 0.3996 0.2548 0.1186  -0.0283 -0.0718 8   GLY A C   
69   O  O   A GLY A 8   ? 0.2132 0.2345 0.3883 -0.0454 0.1280  -0.1301 8   GLY A O   
70   O  O   B GLY A 8   ? 0.2186 0.2290 0.2526 0.0348  0.0088  -0.0390 8   GLY A O   
71   N  N   A LYS A 9   ? 0.1208 0.1976 0.3127 -0.0076 0.0231  -0.1010 9   LYS A N   
72   N  N   B LYS A 9   ? 0.4981 0.4214 0.5655 0.1858  -0.1464 0.0732  9   LYS A N   
73   C  CA  A LYS A 9   ? 0.2259 0.2088 0.3090 -0.0177 -0.0024 -0.0013 9   LYS A CA  
74   C  CA  B LYS A 9   ? 0.3614 0.3914 0.5311 0.0688  -0.1365 -0.0697 9   LYS A CA  
75   C  C   A LYS A 9   ? 0.2257 0.2021 0.2516 -0.0189 0.0756  -0.0949 9   LYS A C   
76   C  C   B LYS A 9   ? 0.4022 0.4995 0.3600 -0.0722 0.0068  0.0562  9   LYS A C   
77   O  O   A LYS A 9   ? 0.2249 0.2170 0.2804 -0.0178 0.0784  -0.0118 9   LYS A O   
78   O  O   B LYS A 9   ? 0.5555 0.7702 0.4606 -0.0706 -0.0294 -0.1367 9   LYS A O   
79   C  CB  A LYS A 9   ? 0.1186 0.4287 0.2962 0.0524  -0.0192 -0.0416 9   LYS A CB  
80   C  CB  B LYS A 9   ? 0.5577 0.3310 0.7760 0.0637  0.1010  0.0230  9   LYS A CB  
81   C  CG  A LYS A 9   ? 0.2520 0.3838 0.4375 0.1803  -0.0511 0.0049  9   LYS A CG  
82   C  CG  B LYS A 9   ? 0.7005 0.5576 0.7286 0.2224  0.1655  0.0667  9   LYS A CG  
83   C  CD  A LYS A 9   ? 0.3217 0.3098 0.5734 0.1603  -0.0581 0.0403  9   LYS A CD  
84   C  CD  B LYS A 9   ? 0.6750 0.5590 0.9219 0.2141  -0.0109 0.1520  9   LYS A CD  
85   C  CE  A LYS A 9   ? 0.6452 0.3357 0.6547 0.1524  -0.1125 0.1439  9   LYS A CE  
86   C  CE  B LYS A 9   ? 0.6541 0.6294 0.9075 0.1342  0.0474  0.2777  9   LYS A CE  
87   N  NZ  A LYS A 9   ? 0.7548 0.6653 0.6773 0.0954  -0.2669 0.0031  9   LYS A NZ  
88   N  NZ  B LYS A 9   ? 0.4490 0.3698 1.0656 0.1794  -0.0944 -0.0076 9   LYS A NZ  
89   N  N   A HIS A 10  ? 0.1131 0.2201 0.2881 -0.0007 -0.0241 -0.0844 10  HIS A N   
90   N  N   B HIS A 10  ? 0.2608 0.2136 0.4126 0.1053  0.1220  -0.0208 10  HIS A N   
91   C  CA  A HIS A 10  ? 0.0923 0.2036 0.1926 0.0092  -0.0027 -0.0329 10  HIS A CA  
92   C  CA  B HIS A 10  ? 0.2681 0.2878 0.2883 0.0217  0.1136  -0.0028 10  HIS A CA  
93   C  C   A HIS A 10  ? 0.1702 0.1430 0.2194 0.0049  0.0281  0.0113  10  HIS A C   
94   C  C   B HIS A 10  ? 0.2049 0.3149 0.2225 0.1154  0.0835  -0.0232 10  HIS A C   
95   O  O   A HIS A 10  ? 0.2570 0.2545 0.2930 -0.0082 0.0505  -0.0125 10  HIS A O   
96   O  O   B HIS A 10  ? 0.1633 0.3312 0.3411 0.1121  0.0256  -0.0653 10  HIS A O   
97   C  CB  A HIS A 10  ? 0.1180 0.1906 0.2261 0.0285  0.0209  0.0229  10  HIS A CB  
98   C  CB  B HIS A 10  ? 0.1649 0.2358 0.3057 0.0034  0.1187  -0.0370 10  HIS A CB  
99   C  CG  A HIS A 10  ? 0.1199 0.2085 0.1650 -0.0182 -0.0285 -0.0115 10  HIS A CG  
100  C  CG  B HIS A 10  ? 0.1621 0.2327 0.3543 0.0000  0.0108  -0.0658 10  HIS A CG  
101  N  ND1 A HIS A 10  ? 0.1037 0.1904 0.3158 0.0399  0.0269  0.0135  10  HIS A ND1 
102  N  ND1 B HIS A 10  ? 0.2865 0.2725 0.2405 0.0286  0.0015  -0.0925 10  HIS A ND1 
103  C  CD2 A HIS A 10  ? 0.1612 0.2187 0.1985 -0.0329 0.0505  -0.0648 10  HIS A CD2 
104  C  CD2 B HIS A 10  ? 0.1492 0.2666 0.2925 0.0346  0.0697  -0.0935 10  HIS A CD2 
105  C  CE1 A HIS A 10  ? 0.0763 0.2062 0.2822 0.0408  0.0052  0.0010  10  HIS A CE1 
106  C  CE1 B HIS A 10  ? 0.4053 0.2664 0.2894 0.1552  -0.0434 -0.0278 10  HIS A CE1 
107  N  NE2 A HIS A 10  ? 0.1068 0.2529 0.2169 -0.0164 0.0248  -0.0238 10  HIS A NE2 
108  N  NE2 B HIS A 10  ? 0.2773 0.3526 0.1986 0.0692  0.0727  -0.0750 10  HIS A NE2 
109  N  N   . ASN A 11  ? 0.2027 0.2214 0.3512 0.0728  0.1372  0.0140  11  ASN A N   
110  C  CA  . ASN A 11  ? 0.1597 0.2270 0.2656 0.0544  0.0966  0.0071  11  ASN A CA  
111  C  C   . ASN A 11  ? 0.1720 0.2029 0.2937 0.0461  0.1054  0.0252  11  ASN A C   
112  O  O   . ASN A 11  ? 0.1651 0.2312 0.2377 0.0597  0.0857  0.0263  11  ASN A O   
113  C  CB  . ASN A 11  ? 0.1438 0.2333 0.2598 0.0267  0.0807  0.0289  11  ASN A CB  
114  C  CG  . ASN A 11  ? 0.2169 0.2308 0.2199 0.0198  0.1074  -0.0247 11  ASN A CG  
115  O  OD1 . ASN A 11  ? 0.2338 0.2449 0.3396 -0.0131 0.1120  0.0087  11  ASN A OD1 
116  N  ND2 . ASN A 11  ? 0.2363 0.2423 0.2460 -0.0370 0.0837  -0.0054 11  ASN A ND2 
117  N  N   . GLY A 12  ? 0.1635 0.2230 0.2498 0.0505  0.0925  0.0077  12  GLY A N   
118  C  CA  . GLY A 12  ? 0.1083 0.2445 0.2363 0.0320  0.0610  0.0089  12  GLY A CA  
119  C  C   . GLY A 12  ? 0.1413 0.1645 0.2136 0.0266  0.0612  0.0295  12  GLY A C   
120  O  O   . GLY A 12  ? 0.1206 0.1880 0.2345 0.0384  0.0496  0.0425  12  GLY A O   
121  N  N   . PRO A 13  ? 0.1081 0.1573 0.2098 0.0087  0.0535  0.0031  13  PRO A N   
122  C  CA  . PRO A 13  ? 0.1115 0.1217 0.2334 0.0082  0.0469  0.0015  13  PRO A CA  
123  C  C   . PRO A 13  ? 0.1500 0.1397 0.1937 0.0143  0.0482  0.0008  13  PRO A C   
124  O  O   . PRO A 13  ? 0.1150 0.1723 0.2222 -0.0099 0.0329  -0.0196 13  PRO A O   
125  C  CB  . PRO A 13  ? 0.1422 0.1430 0.2233 -0.0076 0.0617  -0.0326 13  PRO A CB  
126  C  CG  . PRO A 13  ? 0.1465 0.1519 0.2223 -0.0173 0.0627  -0.0237 13  PRO A CG  
127  C  CD  . PRO A 13  ? 0.1457 0.1756 0.2108 0.0019  0.0606  0.0076  13  PRO A CD  
128  N  N   . GLU A 14  ? 0.1748 0.1420 0.2163 0.0266  0.0381  0.0218  14  GLU A N   
129  C  CA  . GLU A 14  ? 0.2228 0.1650 0.2466 0.0456  0.0430  0.0414  14  GLU A CA  
130  C  C   . GLU A 14  ? 0.1525 0.2080 0.2380 0.0824  0.0270  0.0450  14  GLU A C   
131  O  O   . GLU A 14  ? 0.1732 0.1985 0.2583 0.0688  0.0315  0.0619  14  GLU A O   
132  C  CB  . GLU A 14  ? 0.3260 0.1791 0.2937 0.0601  0.0149  0.0227  14  GLU A CB  
133  C  CG  . GLU A 14  ? 0.2019 0.3324 0.3508 0.0860  -0.0816 -0.0326 14  GLU A CG  
134  C  CD  . GLU A 14  ? 0.1947 0.4255 0.3903 0.0263  -0.0476 -0.0562 14  GLU A CD  
135  O  OE1 . GLU A 14  ? 0.2530 0.2820 0.3083 0.0920  -0.0898 -0.1080 14  GLU A OE1 
136  O  OE2 . GLU A 14  ? 0.5501 0.1729 0.2926 -0.0131 0.0749  0.0020  14  GLU A OE2 
137  N  N   . HIS A 15  ? 0.1228 0.1812 0.2284 0.0344  0.0526  0.0237  15  HIS A N   
138  C  CA  . HIS A 15  ? 0.1124 0.1819 0.2401 0.0509  0.0392  0.0167  15  HIS A CA  
139  C  C   . HIS A 15  ? 0.0850 0.1985 0.1940 0.0350  0.0097  0.0094  15  HIS A C   
140  O  O   . HIS A 15  ? 0.0781 0.1819 0.3011 0.0175  0.0307  0.0364  15  HIS A O   
141  C  CB  . HIS A 15  ? 0.0983 0.2088 0.2749 0.0612  0.0421  0.0359  15  HIS A CB  
142  C  CG  . HIS A 15  ? 0.1771 0.2597 0.2598 0.0877  0.0719  0.0680  15  HIS A CG  
143  N  ND1 . HIS A 15  ? 0.1835 0.3219 0.2732 0.1194  0.0507  0.0121  15  HIS A ND1 
144  C  CD2 . HIS A 15  ? 0.2021 0.2587 0.2814 0.1041  0.0737  0.0452  15  HIS A CD2 
145  C  CE1 . HIS A 15  ? 0.3190 0.3587 0.2538 0.1803  -0.0318 -0.0337 15  HIS A CE1 
146  N  NE2 . HIS A 15  ? 0.3037 0.2971 0.2498 0.1736  0.0744  0.0054  15  HIS A NE2 
147  N  N   . TRP A 16  ? 0.0794 0.1563 0.2202 0.0160  0.0186  0.0170  16  TRP A N   
148  C  CA  . TRP A 16  ? 0.0728 0.1430 0.2237 0.0153  0.0083  -0.0044 16  TRP A CA  
149  C  C   . TRP A 16  ? 0.0888 0.1432 0.2069 0.0278  0.0125  0.0270  16  TRP A C   
150  O  O   . TRP A 16  ? 0.0824 0.1472 0.2412 0.0063  -0.0104 0.0207  16  TRP A O   
151  C  CB  . TRP A 16  ? 0.0684 0.1636 0.2325 0.0103  0.0035  -0.0149 16  TRP A CB  
152  C  CG  . TRP A 16  ? 0.0930 0.1333 0.1728 0.0074  0.0132  -0.0006 16  TRP A CG  
153  C  CD1 . TRP A 16  ? 0.1127 0.1579 0.1633 0.0148  0.0232  0.0198  16  TRP A CD1 
154  C  CD2 . TRP A 16  ? 0.0754 0.1156 0.1779 0.0126  0.0238  0.0038  16  TRP A CD2 
155  N  NE1 . TRP A 16  ? 0.0921 0.1501 0.1829 0.0076  0.0261  0.0024  16  TRP A NE1 
156  C  CE2 . TRP A 16  ? 0.0909 0.1256 0.1680 0.0073  0.0331  0.0024  16  TRP A CE2 
157  C  CE3 . TRP A 16  ? 0.0772 0.1231 0.1932 -0.0017 0.0244  -0.0038 16  TRP A CE3 
158  C  CZ2 . TRP A 16  ? 0.1050 0.1106 0.1799 0.0000  0.0403  0.0142  16  TRP A CZ2 
159  C  CZ3 . TRP A 16  ? 0.0775 0.1165 0.1906 0.0005  0.0229  -0.0027 16  TRP A CZ3 
160  C  CH2 . TRP A 16  ? 0.1272 0.1081 0.1765 -0.0015 0.0362  -0.0048 16  TRP A CH2 
161  N  N   . HIS A 17  ? 0.0781 0.1701 0.2151 -0.0041 -0.0024 -0.0062 17  HIS A N   
162  C  CA  . HIS A 17  ? 0.0852 0.1764 0.2291 0.0130  -0.0038 0.0282  17  HIS A CA  
163  C  C   . HIS A 17  ? 0.0782 0.1718 0.2986 0.0066  -0.0008 0.0318  17  HIS A C   
164  O  O   . HIS A 17  ? 0.0816 0.2013 0.3005 -0.0023 -0.0230 0.0272  17  HIS A O   
165  C  CB  . HIS A 17  ? 0.0861 0.1878 0.2434 0.0154  0.0093  0.0223  17  HIS A CB  
166  C  CG  . HIS A 17  ? 0.0901 0.1970 0.3077 0.0142  -0.0212 0.0498  17  HIS A CG  
167  N  ND1 . HIS A 17  ? 0.0834 0.2796 0.3626 -0.0049 -0.0193 0.0690  17  HIS A ND1 
168  C  CD2 . HIS A 17  ? 0.1169 0.1904 0.2930 0.0399  0.0140  0.0628  17  HIS A CD2 
169  C  CE1 . HIS A 17  ? 0.1169 0.3447 0.3339 0.0732  0.0225  0.0866  17  HIS A CE1 
170  N  NE2 . HIS A 17  ? 0.1439 0.2591 0.3195 0.0454  -0.0110 0.1002  17  HIS A NE2 
171  N  N   . LYS A 18  ? 0.0511 0.2011 0.3120 0.0093  -0.0024 0.0337  18  LYS A N   
172  C  CA  . LYS A 18  ? 0.0684 0.2502 0.3375 0.0175  0.0001  0.0934  18  LYS A CA  
173  C  C   . LYS A 18  ? 0.0710 0.2334 0.3580 -0.0174 -0.0121 0.0926  18  LYS A C   
174  O  O   . LYS A 18  ? 0.1305 0.2452 0.5001 -0.0494 -0.0507 0.0979  18  LYS A O   
175  C  CB  . LYS A 18  ? 0.0804 0.2645 0.3655 0.0458  0.0020  0.0952  18  LYS A CB  
176  C  CG  . LYS A 18  ? 0.1036 0.2721 0.3370 0.0340  0.0408  0.0772  18  LYS A CG  
177  C  CD  . LYS A 18  ? 0.1043 0.2700 0.3395 0.0505  0.0362  0.0986  18  LYS A CD  
178  C  CE  . LYS A 18  ? 0.1041 0.2831 0.3864 0.0553  0.0353  0.0907  18  LYS A CE  
179  N  NZ  . LYS A 18  ? 0.0988 0.3670 0.3095 0.1020  0.0390  0.1377  18  LYS A NZ  
180  N  N   . ASP A 19  ? 0.0886 0.2456 0.3184 0.0110  0.0074  0.0661  19  ASP A N   
181  C  CA  . ASP A 19  ? 0.1093 0.2175 0.3325 -0.0019 -0.0049 0.0668  19  ASP A CA  
182  C  C   . ASP A 19  ? 0.1059 0.1943 0.3339 0.0031  0.0111  0.0524  19  ASP A C   
183  O  O   . ASP A 19  ? 0.1372 0.1842 0.3511 -0.0188 0.0060  0.0648  19  ASP A O   
184  C  CB  . ASP A 19  ? 0.1404 0.3838 0.2932 0.0681  -0.0120 0.0217  19  ASP A CB  
185  C  CG  . ASP A 19  ? 0.1216 0.6565 0.4298 -0.0326 0.0491  -0.0098 19  ASP A CG  
186  O  OD1 . ASP A 19  ? 0.1782 0.6011 0.4330 -0.0379 0.0538  0.0597  19  ASP A OD1 
187  O  OD2 . ASP A 19  ? 0.4343 0.8662 0.6092 -0.0520 0.0549  -0.1037 19  ASP A OD2 
188  N  N   . PHE A 20  ? 0.0948 0.1853 0.2728 -0.0286 -0.0176 0.0392  20  PHE A N   
189  C  CA  . PHE A 20  ? 0.0625 0.1737 0.2915 -0.0167 -0.0046 0.0200  20  PHE A CA  
190  C  C   . PHE A 20  ? 0.0706 0.1815 0.2599 -0.0205 -0.0131 0.0109  20  PHE A C   
191  O  O   . PHE A 20  ? 0.1010 0.1467 0.2485 -0.0098 -0.0119 0.0074  20  PHE A O   
192  C  CB  . PHE A 20  ? 0.0769 0.1838 0.2404 -0.0021 -0.0071 0.0174  20  PHE A CB  
193  C  CG  . PHE A 20  ? 0.0697 0.2104 0.2624 -0.0348 -0.0010 0.0379  20  PHE A CG  
194  C  CD1 . PHE A 20  ? 0.1016 0.2410 0.2876 -0.0281 -0.0135 0.0590  20  PHE A CD1 
195  C  CD2 . PHE A 20  ? 0.1045 0.2628 0.2474 -0.0348 0.0096  0.0230  20  PHE A CD2 
196  C  CE1 . PHE A 20  ? 0.1115 0.2702 0.2739 -0.0244 0.0031  0.0559  20  PHE A CE1 
197  C  CE2 . PHE A 20  ? 0.1174 0.3259 0.2682 -0.0199 0.0068  0.0471  20  PHE A CE2 
198  C  CZ  . PHE A 20  ? 0.1009 0.3177 0.2632 -0.0317 0.0071  0.0661  20  PHE A CZ  
199  N  N   . PRO A 21  ? 0.0846 0.2074 0.2687 -0.0244 -0.0218 0.0186  21  PRO A N   
200  C  CA  . PRO A 21  ? 0.0869 0.2150 0.2800 -0.0300 -0.0342 0.0015  21  PRO A CA  
201  C  C   . PRO A 21  ? 0.0939 0.1745 0.2581 -0.0199 -0.0390 -0.0086 21  PRO A C   
202  O  O   . PRO A 21  ? 0.0973 0.1891 0.2473 -0.0223 -0.0443 0.0149  21  PRO A O   
203  C  CB  . PRO A 21  ? 0.1222 0.2401 0.3166 -0.0705 -0.0593 0.0318  21  PRO A CB  
204  C  CG  . PRO A 21  ? 0.3180 0.3004 0.3633 -0.1826 -0.1477 0.0540  21  PRO A CG  
205  C  CD  . PRO A 21  ? 0.1215 0.1949 0.3327 -0.0513 -0.0410 0.0344  21  PRO A CD  
206  N  N   A ILE A 22  ? 0.0806 0.1536 0.2736 -0.0209 -0.0423 -0.0140 22  ILE A N   
207  N  N   B ILE A 22  ? 0.0952 0.1484 0.2653 -0.0196 -0.0502 -0.0149 22  ILE A N   
208  C  CA  A ILE A 22  ? 0.0390 0.1669 0.3298 -0.0099 -0.0292 -0.0120 22  ILE A CA  
209  C  CA  B ILE A 22  ? 0.1104 0.1270 0.2226 -0.0038 -0.0397 -0.0277 22  ILE A CA  
210  C  C   A ILE A 22  ? 0.0838 0.1360 0.2383 0.0006  -0.0222 -0.0293 22  ILE A C   
211  C  C   B ILE A 22  ? 0.0872 0.1221 0.2291 -0.0035 -0.0258 -0.0273 22  ILE A C   
212  O  O   A ILE A 22  ? 0.0864 0.1595 0.2391 -0.0006 -0.0208 -0.0124 22  ILE A O   
213  O  O   B ILE A 22  ? 0.0856 0.1596 0.2391 -0.0013 -0.0208 -0.0116 22  ILE A O   
214  C  CB  A ILE A 22  ? 0.0979 0.1624 0.2545 -0.0136 -0.0324 -0.0175 22  ILE A CB  
215  C  CB  B ILE A 22  ? 0.1133 0.1195 0.2148 -0.0233 -0.0270 -0.0176 22  ILE A CB  
216  C  CG1 A ILE A 22  ? 0.1176 0.2163 0.3183 0.0221  0.0000  -0.0781 22  ILE A CG1 
217  C  CG1 B ILE A 22  ? 0.1225 0.1425 0.2055 -0.0138 -0.0386 -0.0511 22  ILE A CG1 
218  C  CG2 A ILE A 22  ? 0.1007 0.1870 0.2628 -0.0467 -0.0511 -0.0249 22  ILE A CG2 
219  C  CG2 B ILE A 22  ? 0.0921 0.1544 0.1807 -0.0013 -0.0245 -0.0049 22  ILE A CG2 
220  C  CD1 A ILE A 22  ? 0.2417 0.2875 0.3391 -0.0474 -0.0756 -0.0377 22  ILE A CD1 
221  C  CD1 B ILE A 22  ? 0.0966 0.1263 0.2412 -0.0229 -0.0175 -0.0326 22  ILE A CD1 
222  N  N   . ALA A 23  ? 0.0918 0.1347 0.2071 -0.0031 -0.0251 -0.0097 23  ALA A N   
223  C  CA  . ALA A 23  ? 0.0931 0.1305 0.2041 -0.0146 -0.0210 -0.0186 23  ALA A CA  
224  C  C   . ALA A 23  ? 0.0799 0.1605 0.2280 0.0059  -0.0183 -0.0250 23  ALA A C   
225  O  O   . ALA A 23  ? 0.1099 0.1458 0.2120 -0.0142 -0.0086 -0.0146 23  ALA A O   
226  C  CB  . ALA A 23  ? 0.0810 0.1367 0.2190 -0.0010 -0.0313 -0.0114 23  ALA A CB  
227  N  N   . LYS A 24  ? 0.1242 0.1627 0.2061 0.0000  -0.0252 0.0043  24  LYS A N   
228  C  CA  . LYS A 24  ? 0.1167 0.1955 0.2140 -0.0010 -0.0252 0.0057  24  LYS A CA  
229  C  C   . LYS A 24  ? 0.1289 0.2166 0.2228 -0.0161 -0.0603 -0.0049 24  LYS A C   
230  O  O   . LYS A 24  ? 0.1407 0.2541 0.2264 0.0001  -0.0555 -0.0187 24  LYS A O   
231  C  CB  . LYS A 24  ? 0.1172 0.2213 0.2426 0.0324  -0.0313 0.0100  24  LYS A CB  
232  C  CG  . LYS A 24  ? 0.1587 0.2363 0.2456 0.0339  -0.0504 0.0168  24  LYS A CG  
233  C  CD  . LYS A 24  ? 0.1498 0.3223 0.3070 0.0636  0.0030  0.0639  24  LYS A CD  
234  C  CE  . LYS A 24  ? 0.1744 0.3407 0.3946 0.0555  -0.0399 0.0370  24  LYS A CE  
235  N  NZ  . LYS A 24  ? 0.2601 0.3885 0.5644 -0.0210 0.0571  -0.1098 24  LYS A NZ  
236  N  N   . GLY A 25  ? 0.1160 0.1808 0.2106 -0.0130 -0.0317 -0.0225 25  GLY A N   
237  C  CA  . GLY A 25  ? 0.1631 0.1738 0.2186 -0.0362 -0.0142 -0.0498 25  GLY A CA  
238  C  C   . GLY A 25  ? 0.1318 0.1879 0.1803 -0.0083 -0.0571 -0.0270 25  GLY A C   
239  O  O   . GLY A 25  ? 0.1411 0.2164 0.1764 -0.0010 -0.0381 -0.0136 25  GLY A O   
240  N  N   . GLU A 26  ? 0.1313 0.2304 0.1768 0.0044  -0.0615 -0.0450 26  GLU A N   
241  C  CA  . GLU A 26  ? 0.1615 0.2469 0.1562 -0.0054 -0.0524 -0.0522 26  GLU A CA  
242  C  C   . GLU A 26  ? 0.1539 0.1797 0.1246 0.0000  -0.0337 -0.0294 26  GLU A C   
243  O  O   . GLU A 26  ? 0.1978 0.2138 0.1262 -0.0071 -0.0432 -0.0115 26  GLU A O   
244  C  CB  . GLU A 26  ? 0.1959 0.3415 0.2166 -0.0269 -0.0731 -0.1368 26  GLU A CB  
245  C  CG  . GLU A 26  ? 0.2458 0.4241 0.1850 -0.0236 -0.0873 -0.0791 26  GLU A CG  
246  C  CD  . GLU A 26  ? 0.2583 0.5249 0.3041 -0.0348 -0.1359 -0.0364 26  GLU A CD  
247  O  OE1 . GLU A 26  ? 0.3806 0.4581 0.3501 0.0310  -0.0927 -0.0410 26  GLU A OE1 
248  O  OE2 . GLU A 26  ? 0.3087 0.4991 0.5059 0.0441  -0.1336 0.0099  26  GLU A OE2 
249  N  N   . ARG A 27  ? 0.1351 0.1421 0.1288 0.0082  -0.0348 -0.0230 27  ARG A N   
250  C  CA  . ARG A 27  ? 0.1079 0.1246 0.1195 0.0041  -0.0217 -0.0291 27  ARG A CA  
251  C  C   . ARG A 27  ? 0.1134 0.1095 0.1018 -0.0003 -0.0133 -0.0151 27  ARG A C   
252  O  O   . ARG A 27  ? 0.1022 0.1263 0.1169 0.0096  -0.0183 -0.0115 27  ARG A O   
253  C  CB  . ARG A 27  ? 0.1855 0.1539 0.1289 0.0030  -0.0313 -0.0372 27  ARG A CB  
254  C  CG  . ARG A 27  ? 0.1674 0.1785 0.1677 0.0046  -0.0154 -0.0208 27  ARG A CG  
255  C  CD  . ARG A 27  ? 0.2286 0.2286 0.1516 0.0379  -0.0335 -0.0190 27  ARG A CD  
256  N  NE  . ARG A 27  ? 0.2192 0.1476 0.1448 0.0100  -0.0024 -0.0144 27  ARG A NE  
257  C  CZ  . ARG A 27  ? 0.1710 0.1645 0.1128 0.0331  -0.0052 0.0068  27  ARG A CZ  
258  N  NH1 . ARG A 27  ? 0.1976 0.2217 0.1791 0.0401  -0.0137 -0.1134 27  ARG A NH1 
259  N  NH2 . ARG A 27  ? 0.1756 0.1606 0.1532 -0.0060 -0.0044 -0.0306 27  ARG A NH2 
260  N  N   . GLN A 28  ? 0.1030 0.1027 0.1095 0.0017  -0.0311 -0.0221 28  GLN A N   
261  C  CA  . GLN A 28  ? 0.0905 0.1092 0.1142 -0.0114 -0.0179 -0.0186 28  GLN A CA  
262  C  C   . GLN A 28  ? 0.0794 0.1061 0.0993 -0.0035 -0.0071 -0.0088 28  GLN A C   
263  O  O   . GLN A 28  ? 0.1128 0.1186 0.0993 -0.0083 -0.0166 -0.0055 28  GLN A O   
264  C  CB  . GLN A 28  ? 0.0728 0.1380 0.1324 -0.0041 -0.0148 -0.0193 28  GLN A CB  
265  C  CG  . GLN A 28  ? 0.0878 0.1358 0.1377 -0.0037 -0.0131 -0.0204 28  GLN A CG  
266  C  CD  . GLN A 28  ? 0.0851 0.1070 0.1352 -0.0046 -0.0307 -0.0192 28  GLN A CD  
267  O  OE1 . GLN A 28  ? 0.0857 0.1097 0.1414 -0.0141 -0.0087 -0.0179 28  GLN A OE1 
268  N  NE2 . GLN A 28  ? 0.0838 0.1147 0.1468 -0.0059 -0.0142 -0.0194 28  GLN A NE2 
269  N  N   . SER A 29  ? 0.0847 0.0986 0.0976 -0.0015 -0.0142 -0.0136 29  SER A N   
270  C  CA  . SER A 29  ? 0.0751 0.0881 0.1093 -0.0041 -0.0189 -0.0177 29  SER A CA  
271  C  C   . SER A 29  ? 0.0678 0.0870 0.1030 -0.0024 -0.0120 -0.0081 29  SER A C   
272  O  O   . SER A 29  ? 0.0837 0.0948 0.1168 -0.0046 0.0017  -0.0074 29  SER A O   
273  C  CB  . SER A 29  ? 0.0813 0.0856 0.1043 0.0052  -0.0070 -0.0175 29  SER A CB  
274  O  OG  . SER A 29  ? 0.0886 0.0886 0.1000 0.0049  -0.0048 -0.0182 29  SER A OG  
275  N  N   . PRO A 30  ? 0.0745 0.0816 0.0948 0.0030  -0.0105 -0.0065 30  PRO A N   
276  C  CA  . PRO A 30  ? 0.0753 0.0828 0.1004 -0.0037 -0.0085 0.0052  30  PRO A CA  
277  C  C   . PRO A 30  ? 0.0767 0.0839 0.0931 0.0024  0.0001  -0.0094 30  PRO A C   
278  O  O   . PRO A 30  ? 0.0855 0.1050 0.1022 0.0032  -0.0161 -0.0035 30  PRO A O   
279  C  CB  . PRO A 30  ? 0.0750 0.0971 0.0953 0.0041  -0.0100 -0.0198 30  PRO A CB  
280  C  CG  . PRO A 30  ? 0.0803 0.0952 0.1149 -0.0071 0.0010  -0.0065 30  PRO A CG  
281  C  CD  . PRO A 30  ? 0.0780 0.0898 0.1005 -0.0015 0.0035  -0.0168 30  PRO A CD  
282  N  N   . VAL A 31  ? 0.0938 0.0979 0.0961 0.0059  0.0000  0.0087  31  VAL A N   
283  C  CA  . VAL A 31  ? 0.1058 0.0920 0.0869 0.0020  -0.0077 0.0049  31  VAL A CA  
284  C  C   . VAL A 31  ? 0.0912 0.1037 0.0957 0.0168  -0.0041 0.0015  31  VAL A C   
285  O  O   . VAL A 31  ? 0.1089 0.1062 0.1127 0.0024  -0.0089 0.0159  31  VAL A O   
286  C  CB  . VAL A 31  ? 0.1172 0.0978 0.1075 0.0017  -0.0054 -0.0052 31  VAL A CB  
287  C  CG1 . VAL A 31  ? 0.1370 0.1115 0.1240 -0.0080 -0.0031 -0.0082 31  VAL A CG1 
288  C  CG2 . VAL A 31  ? 0.1278 0.1084 0.1254 0.0143  0.0140  -0.0080 31  VAL A CG2 
289  N  N   . ASP A 32  ? 0.1092 0.0974 0.1046 0.0088  -0.0087 0.0081  32  ASP A N   
290  C  CA  . ASP A 32  ? 0.1174 0.0909 0.1095 0.0065  -0.0006 0.0092  32  ASP A CA  
291  C  C   . ASP A 32  ? 0.1208 0.1016 0.0974 0.0086  -0.0113 0.0043  32  ASP A C   
292  O  O   . ASP A 32  ? 0.1256 0.1504 0.1226 -0.0024 -0.0065 -0.0205 32  ASP A O   
293  C  CB  . ASP A 32  ? 0.1582 0.0917 0.1226 0.0183  -0.0120 0.0178  32  ASP A CB  
294  C  CG  . ASP A 32  ? 0.1805 0.1031 0.1181 0.0184  -0.0148 0.0296  32  ASP A CG  
295  O  OD1 . ASP A 32  ? 0.1539 0.1064 0.1235 0.0098  -0.0146 0.0182  32  ASP A OD1 
296  O  OD2 . ASP A 32  ? 0.2236 0.1368 0.1263 -0.0210 -0.0146 0.0308  32  ASP A OD2 
297  N  N   . ILE A 33  ? 0.1149 0.0979 0.0996 0.0086  -0.0024 0.0083  33  ILE A N   
298  C  CA  . ILE A 33  ? 0.1319 0.1199 0.1013 0.0192  0.0081  0.0120  33  ILE A CA  
299  C  C   . ILE A 33  ? 0.1442 0.1111 0.1070 0.0256  0.0227  0.0122  33  ILE A C   
300  O  O   . ILE A 33  ? 0.1641 0.1118 0.1195 0.0111  0.0161  0.0126  33  ILE A O   
301  C  CB  . ILE A 33  ? 0.1147 0.1124 0.1243 0.0129  0.0043  0.0081  33  ILE A CB  
302  C  CG1 . ILE A 33  ? 0.1330 0.1203 0.1439 0.0155  0.0012  0.0348  33  ILE A CG1 
303  C  CG2 . ILE A 33  ? 0.1354 0.1675 0.1527 0.0278  0.0174  -0.0005 33  ILE A CG2 
304  C  CD1 . ILE A 33  ? 0.1377 0.1667 0.1657 0.0094  -0.0167 0.0333  33  ILE A CD1 
305  N  N   A ASP A 34  ? 0.1844 0.1445 0.0983 0.0394  0.0098  0.0359  34  ASP A N   
306  N  N   B ASP A 34  ? 0.1773 0.1383 0.0987 0.0102  0.0146  0.0019  34  ASP A N   
307  C  CA  A ASP A 34  ? 0.2137 0.1283 0.1081 0.0305  0.0294  0.0368  34  ASP A CA  
308  C  CA  B ASP A 34  ? 0.2167 0.1272 0.1057 0.0507  0.0288  0.0297  34  ASP A CA  
309  C  C   A ASP A 34  ? 0.2216 0.1721 0.1018 0.0412  0.0346  0.0318  34  ASP A C   
310  C  C   B ASP A 34  ? 0.2402 0.1370 0.0898 0.0573  0.0478  0.0595  34  ASP A C   
311  O  O   A ASP A 34  ? 0.1887 0.1835 0.1113 0.0186  0.0414  0.0098  34  ASP A O   
312  O  O   B ASP A 34  ? 0.1515 0.1845 0.1292 0.0627  0.0276  0.0283  34  ASP A O   
313  C  CB  A ASP A 34  ? 0.2210 0.1436 0.1492 0.0482  0.0110  0.0102  34  ASP A CB  
314  C  CB  B ASP A 34  ? 0.2948 0.1381 0.0926 0.0763  0.0200  0.0355  34  ASP A CB  
315  C  CG  A ASP A 34  ? 0.2104 0.1940 0.1916 0.0807  0.0219  0.0254  34  ASP A CG  
316  C  CG  B ASP A 34  ? 0.3373 0.1916 0.1429 0.0666  0.0469  0.0575  34  ASP A CG  
317  O  OD1 A ASP A 34  ? 0.2649 0.2085 0.1307 0.0265  0.0023  0.0803  34  ASP A OD1 
318  O  OD1 B ASP A 34  ? 0.3623 0.1947 0.2232 0.1159  0.0599  0.0777  34  ASP A OD1 
319  O  OD2 A ASP A 34  ? 0.3065 0.3346 0.2433 0.0675  -0.0307 0.1449  34  ASP A OD2 
320  O  OD2 B ASP A 34  ? 0.3396 0.2804 0.2088 0.0718  0.0773  -0.0003 34  ASP A OD2 
321  N  N   . THR A 35  ? 0.2258 0.1740 0.1306 0.0505  0.0399  0.0593  35  THR A N   
322  C  CA  . THR A 35  ? 0.2036 0.1871 0.1391 0.0679  0.0375  0.0507  35  THR A CA  
323  C  C   . THR A 35  ? 0.1831 0.1683 0.1270 0.0366  0.0300  0.0355  35  THR A C   
324  O  O   . THR A 35  ? 0.2577 0.1959 0.1656 0.0829  0.0537  0.0625  35  THR A O   
325  C  CB  . THR A 35  ? 0.1856 0.2105 0.1785 0.0403  0.0251  0.0650  35  THR A CB  
326  O  OG1 . THR A 35  ? 0.2348 0.2390 0.1880 0.0434  0.0403  0.0675  35  THR A OG1 
327  C  CG2 . THR A 35  ? 0.2236 0.2682 0.1836 0.0760  0.0533  0.0799  35  THR A CG2 
328  N  N   . HIS A 36  ? 0.2872 0.1588 0.1332 0.0631  0.0417  0.0725  36  HIS A N   
329  C  CA  . HIS A 36  ? 0.3126 0.1811 0.1145 0.0465  0.0275  0.0621  36  HIS A CA  
330  C  C   . HIS A 36  ? 0.3046 0.2428 0.1090 0.0384  0.0240  0.0452  36  HIS A C   
331  O  O   . HIS A 36  ? 0.2700 0.3264 0.1272 0.0846  0.0137  0.0309  36  HIS A O   
332  C  CB  . HIS A 36  ? 0.3621 0.1973 0.1418 0.0458  0.0057  0.0839  36  HIS A CB  
333  C  CG  . HIS A 36  ? 0.3769 0.1396 0.1580 0.0513  -0.0015 0.0472  36  HIS A CG  
334  N  ND1 . HIS A 36  ? 0.4154 0.2827 0.1814 -0.0308 -0.0182 0.0549  36  HIS A ND1 
335  C  CD2 . HIS A 36  ? 0.3508 0.1783 0.2030 0.0724  -0.0579 0.0679  36  HIS A CD2 
336  C  CE1 . HIS A 36  ? 0.3422 0.2601 0.2569 -0.0351 -0.0303 0.0740  36  HIS A CE1 
337  N  NE2 . HIS A 36  ? 0.3454 0.2563 0.2840 0.0458  0.0351  0.0668  36  HIS A NE2 
338  N  N   . THR A 37  ? 0.3222 0.1535 0.1852 0.0529  0.0590  0.0291  37  THR A N   
339  C  CA  . THR A 37  ? 0.2946 0.2189 0.1485 0.0865  0.0524  0.0672  37  THR A CA  
340  C  C   . THR A 37  ? 0.2635 0.2311 0.1532 0.0965  0.0496  0.0151  37  THR A C   
341  O  O   . THR A 37  ? 0.3676 0.2536 0.1622 0.1098  -0.0342 0.0041  37  THR A O   
342  C  CB  . THR A 37  ? 0.2799 0.2073 0.4003 0.0604  -0.0816 0.0698  37  THR A CB  
343  O  OG1 . THR A 37  ? 0.3986 0.2213 0.4449 0.0313  0.0397  0.0996  37  THR A OG1 
344  C  CG2 . THR A 37  ? 0.3920 0.3231 0.1997 0.0864  -0.0364 0.0825  37  THR A CG2 
345  N  N   . ALA A 38  ? 0.2549 0.1754 0.1181 0.0553  0.0329  0.0361  38  ALA A N   
346  C  CA  . ALA A 38  ? 0.2370 0.1801 0.1183 0.0571  0.0395  0.0445  38  ALA A CA  
347  C  C   . ALA A 38  ? 0.2320 0.1797 0.1740 0.0379  0.0675  0.0588  38  ALA A C   
348  O  O   . ALA A 38  ? 0.3562 0.1771 0.2864 0.0461  0.1580  0.0317  38  ALA A O   
349  C  CB  . ALA A 38  ? 0.2070 0.1811 0.1395 0.0395  0.0154  0.0348  38  ALA A CB  
350  N  N   A LYS A 39  ? 0.2416 0.1890 0.1374 0.0612  0.0006  0.0052  39  LYS A N   
351  N  N   B LYS A 39  ? 0.2222 0.2038 0.1542 0.0890  -0.0041 0.0129  39  LYS A N   
352  C  CA  A LYS A 39  ? 0.2585 0.2058 0.1016 0.0640  0.0076  0.0322  39  LYS A CA  
353  C  CA  B LYS A 39  ? 0.2469 0.3123 0.1750 0.1347  0.0024  -0.0379 39  LYS A CA  
354  C  C   A LYS A 39  ? 0.2194 0.2150 0.1052 0.0698  0.0557  0.0329  39  LYS A C   
355  C  C   B LYS A 39  ? 0.2155 0.2347 0.1328 0.0584  0.0197  0.0335  39  LYS A C   
356  O  O   A LYS A 39  ? 0.1900 0.2201 0.1088 0.0340  0.0126  0.0270  39  LYS A O   
357  O  O   B LYS A 39  ? 0.1611 0.2291 0.1300 0.0657  0.0062  0.0397  39  LYS A O   
358  C  CB  A LYS A 39  ? 0.2134 0.2158 0.0952 0.0414  0.0148  0.0077  39  LYS A CB  
359  C  CB  B LYS A 39  ? 0.1764 0.4323 0.1587 0.1274  -0.0724 -0.0234 39  LYS A CB  
360  C  CG  A LYS A 39  ? 0.2158 0.2031 0.1615 0.0372  0.0156  -0.0133 39  LYS A CG  
361  C  CG  B LYS A 39  ? 0.3130 0.4621 0.1356 0.2334  -0.0320 -0.0570 39  LYS A CG  
362  C  CD  A LYS A 39  ? 0.2911 0.1604 0.1660 0.0063  -0.0089 -0.0557 39  LYS A CD  
363  C  CD  B LYS A 39  ? 0.3048 0.5896 0.1685 0.2213  -0.0852 -0.1115 39  LYS A CD  
364  C  CE  A LYS A 39  ? 0.3496 0.3258 0.1777 0.0707  0.1163  0.0005  39  LYS A CE  
365  C  CE  B LYS A 39  ? 0.2746 0.5363 0.1729 0.1410  -0.0395 -0.0143 39  LYS A CE  
366  N  NZ  A LYS A 39  ? 0.2258 0.3065 0.3363 0.0822  -0.0249 0.1636  39  LYS A NZ  
367  N  NZ  B LYS A 39  ? 0.4067 0.6575 0.1962 0.0851  0.0865  0.0710  39  LYS A NZ  
368  N  N   . TYR A 40  ? 0.2730 0.2513 0.1305 0.0397  0.0388  0.0309  40  TYR A N   
369  C  CA  . TYR A 40  ? 0.2312 0.2213 0.1633 0.0153  0.0754  0.0054  40  TYR A CA  
370  C  C   . TYR A 40  ? 0.1626 0.2178 0.1469 -0.0028 0.0236  0.0284  40  TYR A C   
371  O  O   . TYR A 40  ? 0.2257 0.2901 0.1201 0.0467  0.0184  0.0000  40  TYR A O   
372  C  CB  . TYR A 40  ? 0.2695 0.2960 0.2205 -0.0697 0.0890  -0.0068 40  TYR A CB  
373  C  CG  . TYR A 40  ? 0.2804 0.3844 0.1588 -0.0842 0.0784  0.0024  40  TYR A CG  
374  C  CD1 . TYR A 40  ? 0.2293 0.3321 0.1943 -0.0860 0.0247  -0.0120 40  TYR A CD1 
375  C  CD2 . TYR A 40  ? 0.2167 0.6129 0.2167 0.0274  0.0750  0.0700  40  TYR A CD2 
376  C  CE1 . TYR A 40  ? 0.2249 0.4571 0.2106 -0.0709 0.0425  0.0006  40  TYR A CE1 
377  C  CE2 . TYR A 40  ? 0.2752 0.5666 0.2192 0.0434  0.0903  0.0515  40  TYR A CE2 
378  C  CZ  . TYR A 40  ? 0.2283 0.5720 0.2153 -0.0049 0.0423  0.0526  40  TYR A CZ  
379  O  OH  . TYR A 40  ? 0.2540 0.7587 0.3823 0.0702  0.0719  -0.1119 40  TYR A OH  
380  N  N   . ASP A 41  ? 0.1880 0.2043 0.1596 0.0401  0.0315  0.0065  41  ASP A N   
381  C  CA  . ASP A 41  ? 0.1946 0.1843 0.1816 0.0044  0.0225  -0.0068 41  ASP A CA  
382  C  C   . ASP A 41  ? 0.1749 0.2621 0.1860 0.0162  0.0197  -0.0176 41  ASP A C   
383  O  O   . ASP A 41  ? 0.1923 0.2585 0.1916 0.0346  0.0059  -0.0052 41  ASP A O   
384  C  CB  . ASP A 41  ? 0.2001 0.2517 0.2445 -0.0230 -0.0080 -0.0113 41  ASP A CB  
385  C  CG  . ASP A 41  ? 0.2268 0.3030 0.2928 -0.0308 -0.0141 -0.0720 41  ASP A CG  
386  O  OD1 . ASP A 41  ? 0.2973 0.2560 0.2764 0.0193  -0.0187 -0.0710 41  ASP A OD1 
387  O  OD2 . ASP A 41  ? 0.2987 0.3549 0.2980 -0.0908 -0.0701 -0.0116 41  ASP A OD2 
388  N  N   . PRO A 42  ? 0.2345 0.3592 0.2106 0.0920  0.0566  0.0060  42  PRO A N   
389  C  CA  . PRO A 42  ? 0.1957 0.3506 0.2705 0.0524  0.0653  -0.0115 42  PRO A CA  
390  C  C   . PRO A 42  ? 0.3025 0.3780 0.2721 0.1446  0.1026  0.0211  42  PRO A C   
391  O  O   . PRO A 42  ? 0.3274 0.6345 0.4269 0.2520  0.1297  0.0601  42  PRO A O   
392  C  CB  . PRO A 42  ? 0.3111 0.6067 0.2906 0.1370  0.1230  0.0269  42  PRO A CB  
393  C  CG  . PRO A 42  ? 0.3323 0.6430 0.2258 0.1176  0.1215  -0.0172 42  PRO A CG  
394  C  CD  . PRO A 42  ? 0.3393 0.3986 0.1956 0.1125  0.0948  0.0491  42  PRO A CD  
395  N  N   . SER A 43  ? 0.3303 0.3934 0.2424 0.1120  0.0615  0.0088  43  SER A N   
396  C  CA  . SER A 43  ? 0.3332 0.3312 0.2994 0.1013  -0.0513 -0.0553 43  SER A CA  
397  C  C   . SER A 43  ? 0.3375 0.2878 0.2381 0.0754  -0.0548 -0.0592 43  SER A C   
398  O  O   . SER A 43  ? 0.5066 0.3130 0.3738 0.1766  -0.0715 0.0167  43  SER A O   
399  C  CB  . SER A 43  ? 0.3544 0.3838 0.2241 0.0599  -0.0406 -0.1055 43  SER A CB  
400  O  OG  . SER A 43  ? 0.3465 0.3259 0.5018 0.0080  -0.0903 -0.1660 43  SER A OG  
401  N  N   . LEU A 44  ? 0.3934 0.3781 0.2401 0.1057  -0.0098 -0.0979 44  LEU A N   
402  C  CA  . LEU A 44  ? 0.2322 0.2942 0.2309 0.0392  -0.0201 0.0055  44  LEU A CA  
403  C  C   . LEU A 44  ? 0.2040 0.3713 0.2485 -0.0129 -0.0130 0.0041  44  LEU A C   
404  O  O   . LEU A 44  ? 0.2060 0.5224 0.3113 -0.0412 -0.0274 0.0966  44  LEU A O   
405  C  CB  . LEU A 44  ? 0.2073 0.2778 0.2202 -0.0220 0.0133  -0.0210 44  LEU A CB  
406  C  CG  . LEU A 44  ? 0.2134 0.2254 0.1983 -0.0068 -0.0195 0.0438  44  LEU A CG  
407  C  CD1 . LEU A 44  ? 0.2469 0.2069 0.2213 -0.0044 0.0200  0.0148  44  LEU A CD1 
408  C  CD2 . LEU A 44  ? 0.2212 0.2212 0.2406 -0.0130 -0.0003 0.0198  44  LEU A CD2 
409  N  N   . LYS A 45  ? 0.2251 0.2797 0.2581 0.0185  -0.0313 0.0125  45  LYS A N   
410  C  CA  . LYS A 45  ? 0.2337 0.2368 0.3291 0.0559  -0.0450 -0.0318 45  LYS A CA  
411  C  C   . LYS A 45  ? 0.1448 0.2865 0.2732 0.0403  0.0306  -0.0162 45  LYS A C   
412  O  O   . LYS A 45  ? 0.1704 0.2438 0.3163 0.0037  0.0154  -0.0357 45  LYS A O   
413  C  CB  . LYS A 45  ? 0.3048 0.2207 0.2397 0.0979  0.0144  -0.0037 45  LYS A CB  
414  C  CG  . LYS A 45  ? 0.2705 0.4088 0.3027 0.0179  0.0241  -0.0581 45  LYS A CG  
415  C  CD  . LYS A 45  ? 0.5701 0.2757 0.4970 -0.0993 0.0957  -0.0573 45  LYS A CD  
416  C  CE  . LYS A 45  ? 0.7240 0.4089 0.5882 -0.0856 0.1286  -0.1689 45  LYS A CE  
417  N  NZ  . LYS A 45  ? 0.7271 0.5343 0.6858 0.0912  0.3131  -0.1168 45  LYS A NZ  
418  N  N   . PRO A 46  ? 0.1324 0.2779 0.2574 -0.0122 0.0296  0.0200  46  PRO A N   
419  C  CA  . PRO A 46  ? 0.1670 0.2610 0.2340 -0.0074 0.0116  0.0152  46  PRO A CA  
420  C  C   . PRO A 46  ? 0.1271 0.2108 0.2257 0.0120  0.0272  0.0388  46  PRO A C   
421  O  O   . PRO A 46  ? 0.1251 0.2190 0.2994 -0.0041 -0.0107 0.0203  46  PRO A O   
422  C  CB  . PRO A 46  ? 0.1664 0.2998 0.2883 -0.0361 0.0231  -0.0032 46  PRO A CB  
423  C  CG  . PRO A 46  ? 0.1624 0.5281 0.3389 -0.0156 0.0254  -0.0588 46  PRO A CG  
424  C  CD  . PRO A 46  ? 0.1659 0.3097 0.3249 0.0217  0.0233  0.0091  46  PRO A CD  
425  N  N   . LEU A 47  ? 0.1167 0.2681 0.3069 0.0119  0.0108  0.0026  47  LEU A N   
426  C  CA  . LEU A 47  ? 0.1016 0.2302 0.2671 -0.0154 0.0193  -0.0102 47  LEU A CA  
427  C  C   . LEU A 47  ? 0.0781 0.2675 0.3434 -0.0337 -0.0339 0.0876  47  LEU A C   
428  O  O   . LEU A 47  ? 0.1255 0.3274 0.4571 -0.0668 -0.0905 0.1783  47  LEU A O   
429  C  CB  . LEU A 47  ? 0.1870 0.2943 0.3172 0.0957  0.0419  0.0038  47  LEU A CB  
430  C  CG  . LEU A 47  ? 0.1281 0.3589 0.3292 0.0148  -0.0188 -0.0790 47  LEU A CG  
431  C  CD1 . LEU A 47  ? 0.1095 0.2797 0.5224 -0.0610 -0.0292 -0.0190 47  LEU A CD1 
432  C  CD2 . LEU A 47  ? 0.1456 0.3088 0.4329 0.0474  0.0111  -0.1071 47  LEU A CD2 
433  N  N   . SER A 48  ? 0.1235 0.2085 0.2431 -0.0163 0.0034  0.0568  48  SER A N   
434  C  CA  . SER A 48  ? 0.1528 0.2014 0.2251 -0.0031 0.0003  0.0397  48  SER A CA  
435  C  C   . SER A 48  ? 0.1210 0.2003 0.2099 -0.0027 -0.0088 0.0161  48  SER A C   
436  O  O   . SER A 48  ? 0.1304 0.2331 0.2440 -0.0297 0.0062  0.0274  48  SER A O   
437  C  CB  . SER A 48  ? 0.1741 0.2027 0.2840 0.0135  0.0276  0.0423  48  SER A CB  
438  O  OG  . SER A 48  ? 0.1798 0.2728 0.3148 0.0564  0.0340  0.0825  48  SER A OG  
439  N  N   . VAL A 49  ? 0.1482 0.1976 0.2240 -0.0274 0.0098  0.0307  49  VAL A N   
440  C  CA  . VAL A 49  ? 0.1620 0.2041 0.2495 -0.0511 -0.0172 -0.0043 49  VAL A CA  
441  C  C   . VAL A 49  ? 0.1775 0.2195 0.2327 -0.0674 -0.0179 -0.0130 49  VAL A C   
442  O  O   . VAL A 49  ? 0.1891 0.3334 0.2843 -0.1181 -0.0328 -0.0055 49  VAL A O   
443  C  CB  . VAL A 49  ? 0.2522 0.2171 0.2639 -0.0635 0.0509  0.0087  49  VAL A CB  
444  C  CG1 . VAL A 49  ? 0.4187 0.2300 0.2889 -0.0540 0.0520  0.0065  49  VAL A CG1 
445  C  CG2 . VAL A 49  ? 0.2547 0.2316 0.3894 -0.0430 0.0364  0.0300  49  VAL A CG2 
446  N  N   . SER A 50  ? 0.1640 0.2206 0.2293 -0.0333 -0.0088 0.0046  50  SER A N   
447  C  CA  . SER A 50  ? 0.1736 0.2099 0.3514 -0.0068 -0.0282 -0.0003 50  SER A CA  
448  C  C   . SER A 50  ? 0.1402 0.2512 0.2984 -0.0184 -0.0807 0.0055  50  SER A C   
449  O  O   . SER A 50  ? 0.2242 0.2056 0.3041 -0.0447 -0.0662 0.0331  50  SER A O   
450  C  CB  . SER A 50  ? 0.2501 0.2451 0.3560 0.0214  -0.0089 0.0044  50  SER A CB  
451  O  OG  . SER A 50  ? 0.2192 0.3952 0.3531 0.0028  -0.0155 -0.0678 50  SER A OG  
452  N  N   . TYR A 51  ? 0.1589 0.2368 0.2804 -0.0439 -0.0640 0.0500  51  TYR A N   
453  C  CA  . TYR A 51  ? 0.1304 0.1956 0.2940 -0.0147 -0.0751 0.0608  51  TYR A CA  
454  C  C   . TYR A 51  ? 0.1754 0.2529 0.2894 -0.0390 -0.0432 0.0957  51  TYR A C   
455  O  O   . TYR A 51  ? 0.1995 0.2712 0.2678 -0.0082 -0.0784 0.0680  51  TYR A O   
456  C  CB  . TYR A 51  ? 0.1378 0.2237 0.2599 -0.0295 -0.0675 0.0322  51  TYR A CB  
457  C  CG  . TYR A 51  ? 0.1479 0.1943 0.1934 -0.0436 -0.0551 0.0260  51  TYR A CG  
458  C  CD1 . TYR A 51  ? 0.1526 0.1623 0.2526 -0.0189 -0.0461 0.0226  51  TYR A CD1 
459  C  CD2 . TYR A 51  ? 0.1682 0.1631 0.1900 -0.0348 -0.0194 0.0284  51  TYR A CD2 
460  C  CE1 . TYR A 51  ? 0.1451 0.1508 0.1749 -0.0217 -0.0348 0.0287  51  TYR A CE1 
461  C  CE2 . TYR A 51  ? 0.1273 0.1600 0.1829 -0.0375 -0.0253 0.0130  51  TYR A CE2 
462  C  CZ  . TYR A 51  ? 0.1491 0.1360 0.1727 -0.0236 -0.0240 0.0190  51  TYR A CZ  
463  O  OH  . TYR A 51  ? 0.1352 0.1407 0.2048 -0.0162 -0.0516 0.0239  51  TYR A OH  
464  N  N   . ASP A 52  ? 0.1266 0.3152 0.4023 -0.0546 -0.1049 0.1284  52  ASP A N   
465  C  CA  . ASP A 52  ? 0.1511 0.3691 0.3453 -0.0531 -0.0860 0.1592  52  ASP A CA  
466  C  C   . ASP A 52  ? 0.1889 0.3355 0.3309 -0.0147 -0.0965 0.1386  52  ASP A C   
467  O  O   . ASP A 52  ? 0.2788 0.3260 0.3652 -0.0032 -0.1036 0.1023  52  ASP A O   
468  C  CB  . ASP A 52  ? 0.1498 0.4413 0.4268 -0.0098 -0.1054 0.1600  52  ASP A CB  
469  C  CG  . ASP A 52  ? 0.2883 0.4527 0.4738 0.0080  -0.0500 0.1187  52  ASP A CG  
470  O  OD1 . ASP A 52  ? 0.3569 0.6625 0.5281 -0.0174 -0.0513 0.1071  52  ASP A OD1 
471  O  OD2 . ASP A 52  ? 0.6043 0.6414 0.6845 0.1291  -0.0857 0.3061  52  ASP A OD2 
472  N  N   . GLN A 53  ? 0.1640 0.2791 0.4156 0.0126  -0.0379 0.1217  53  GLN A N   
473  C  CA  . GLN A 53  ? 0.2170 0.2782 0.4442 -0.0223 -0.0436 0.1240  53  GLN A CA  
474  C  C   . GLN A 53  ? 0.2269 0.2084 0.2850 -0.0153 -0.0491 0.0639  53  GLN A C   
475  O  O   . GLN A 53  ? 0.2189 0.2111 0.3102 -0.0104 -0.0417 0.0593  53  GLN A O   
476  C  CB  . GLN A 53  ? 0.2547 0.2585 0.6226 0.0450  0.0046  0.1537  53  GLN A CB  
477  C  CG  . GLN A 53  ? 0.2548 0.5404 0.9627 0.0794  0.1259  0.2856  53  GLN A CG  
478  C  CD  . GLN A 53  ? 0.5192 0.7616 0.9542 -0.1608 -0.0339 0.4147  53  GLN A CD  
479  O  OE1 . GLN A 53  ? 0.5852 0.9004 0.9775 0.2763  -0.1568 0.1335  53  GLN A OE1 
480  N  NE2 . GLN A 53  ? 0.5081 1.7565 0.9512 0.3341  -0.1852 0.2639  53  GLN A NE2 
481  N  N   . ALA A 54  ? 0.2096 0.1823 0.3073 -0.0142 -0.0586 0.0450  54  ALA A N   
482  C  CA  . ALA A 54  ? 0.2416 0.1682 0.2252 -0.0049 -0.0628 0.0023  54  ALA A CA  
483  C  C   . ALA A 54  ? 0.2548 0.1805 0.2199 -0.0110 -0.0518 0.0015  54  ALA A C   
484  O  O   . ALA A 54  ? 0.2633 0.3396 0.2936 -0.0804 -0.0659 -0.0524 54  ALA A O   
485  C  CB  . ALA A 54  ? 0.2832 0.1774 0.2930 0.0148  -0.0383 0.0137  54  ALA A CB  
486  N  N   A THR A 55  ? 0.1913 0.1767 0.1894 0.0137  -0.0573 0.0326  55  THR A N   
487  N  N   B THR A 55  ? 0.1897 0.1773 0.1895 0.0136  -0.0575 0.0322  55  THR A N   
488  C  CA  A THR A 55  ? 0.1997 0.2073 0.1929 0.0320  -0.0653 0.0560  55  THR A CA  
489  C  CA  B THR A 55  ? 0.1995 0.2090 0.1957 0.0219  -0.0582 0.0537  55  THR A CA  
490  C  C   A THR A 55  ? 0.2300 0.1528 0.1446 -0.0006 -0.0645 0.0147  55  THR A C   
491  C  C   B THR A 55  ? 0.2318 0.1545 0.1432 -0.0006 -0.0619 0.0159  55  THR A C   
492  O  O   A THR A 55  ? 0.2161 0.1508 0.1753 0.0177  -0.0670 0.0273  55  THR A O   
493  O  O   B THR A 55  ? 0.2143 0.1541 0.1783 0.0206  -0.0617 0.0292  55  THR A O   
494  C  CB  A THR A 55  ? 0.3611 0.2584 0.2104 0.0430  -0.0348 0.0934  55  THR A CB  
495  C  CB  B THR A 55  ? 0.3057 0.2513 0.2592 0.1045  -0.0237 0.0595  55  THR A CB  
496  O  OG1 A THR A 55  ? 0.3237 0.1728 0.5789 0.0423  -0.2459 0.0010  55  THR A OG1 
497  O  OG1 B THR A 55  ? 0.3799 0.2594 0.5042 0.0230  -0.1142 0.0706  55  THR A OG1 
498  C  CG2 A THR A 55  ? 0.3941 0.2695 0.1852 0.1723  -0.0329 0.0835  55  THR A CG2 
499  C  CG2 B THR A 55  ? 0.3654 0.3497 0.3910 0.1744  -0.0132 0.0874  55  THR A CG2 
500  N  N   . SER A 56  ? 0.2398 0.1495 0.1606 0.0280  -0.0816 0.0114  56  SER A N   
501  C  CA  . SER A 56  ? 0.2614 0.1450 0.1356 -0.0093 -0.0679 0.0104  56  SER A CA  
502  C  C   . SER A 56  ? 0.2347 0.1676 0.1340 0.0294  -0.0430 0.0362  56  SER A C   
503  O  O   . SER A 56  ? 0.3109 0.1756 0.1752 0.0496  -0.1052 0.0161  56  SER A O   
504  C  CB  . SER A 56  ? 0.3192 0.1423 0.1319 -0.0100 -0.0929 0.0059  56  SER A CB  
505  O  OG  . SER A 56  ? 0.2990 0.1625 0.1578 -0.0156 -0.1081 0.0210  56  SER A OG  
506  N  N   . LEU A 57  ? 0.2585 0.1248 0.1172 0.0153  -0.0309 0.0326  57  LEU A N   
507  C  CA  . LEU A 57  ? 0.2115 0.1752 0.2020 -0.0076 0.0041  0.0381  57  LEU A CA  
508  C  C   . LEU A 57  ? 0.2635 0.1720 0.1164 0.0066  -0.0251 0.0489  57  LEU A C   
509  O  O   . LEU A 57  ? 0.3041 0.1888 0.1318 0.0230  -0.0447 0.0485  57  LEU A O   
510  C  CB  . LEU A 57  ? 0.3276 0.2424 0.1904 -0.0417 -0.0041 0.0943  57  LEU A CB  
511  C  CG  . LEU A 57  ? 0.6258 0.1739 0.2659 0.0311  -0.1423 -0.0231 57  LEU A CG  
512  C  CD1 . LEU A 57  ? 0.7045 0.2204 0.2370 -0.0804 -0.0366 0.0149  57  LEU A CD1 
513  C  CD2 . LEU A 57  ? 0.9771 0.2894 0.2791 0.1381  -0.2169 -0.0835 57  LEU A CD2 
514  N  N   . ARG A 58  ? 0.2291 0.1682 0.1404 0.0166  -0.0215 0.0373  58  ARG A N   
515  C  CA  . ARG A 58  ? 0.2208 0.1938 0.1422 -0.0087 -0.0412 0.0658  58  ARG A CA  
516  C  C   . ARG A 58  ? 0.2097 0.1630 0.1095 -0.0220 -0.0263 0.0318  58  ARG A C   
517  O  O   . ARG A 58  ? 0.2602 0.1607 0.1023 0.0098  -0.0190 0.0215  58  ARG A O   
518  C  CB  . ARG A 58  ? 0.1699 0.2675 0.1950 0.0049  -0.0194 0.0335  58  ARG A CB  
519  C  CG  . ARG A 58  ? 0.1693 0.2347 0.3820 -0.0322 0.0322  0.1516  58  ARG A CG  
520  C  CD  . ARG A 58  ? 0.3438 0.2633 0.2746 -0.1181 -0.0593 0.0887  58  ARG A CD  
521  N  NE  . ARG A 58  ? 0.2070 0.2853 0.2333 -0.0443 -0.0046 0.0198  58  ARG A NE  
522  C  CZ  . ARG A 58  ? 0.2025 0.2509 0.2166 -0.0099 0.0135  0.0610  58  ARG A CZ  
523  N  NH1 . ARG A 58  ? 0.2645 0.2502 0.2167 -0.0658 0.0320  0.0671  58  ARG A NH1 
524  N  NH2 . ARG A 58  ? 0.2366 0.2091 0.2494 -0.0308 0.0093  0.0684  58  ARG A NH2 
525  N  N   . ILE A 59  ? 0.2363 0.1724 0.0976 0.0109  -0.0261 0.0232  59  ILE A N   
526  C  CA  . ILE A 59  ? 0.2037 0.1676 0.1189 -0.0104 -0.0094 0.0452  59  ILE A CA  
527  C  C   . ILE A 59  ? 0.1882 0.1445 0.1344 0.0034  -0.0449 0.0375  59  ILE A C   
528  O  O   . ILE A 59  ? 0.2615 0.2386 0.0939 0.0303  -0.0183 0.0498  59  ILE A O   
529  C  CB  . ILE A 59  ? 0.2408 0.1538 0.1159 -0.0218 -0.0311 0.0193  59  ILE A CB  
530  C  CG1 . ILE A 59  ? 0.2423 0.1435 0.1090 -0.0230 -0.0383 0.0261  59  ILE A CG1 
531  C  CG2 . ILE A 59  ? 0.3352 0.1668 0.1036 -0.0054 -0.0736 0.0131  59  ILE A CG2 
532  C  CD1 . ILE A 59  ? 0.2699 0.1404 0.1525 -0.0104 -0.0234 0.0023  59  ILE A CD1 
533  N  N   . LEU A 60  ? 0.1527 0.1639 0.1503 -0.0205 -0.0252 0.0131  60  LEU A N   
534  C  CA  . LEU A 60  ? 0.1852 0.1457 0.1225 0.0068  -0.0333 0.0265  60  LEU A CA  
535  C  C   . LEU A 60  ? 0.1770 0.1433 0.1156 -0.0089 -0.0040 0.0136  60  LEU A C   
536  O  O   . LEU A 60  ? 0.2028 0.1474 0.1119 -0.0037 0.0038  0.0199  60  LEU A O   
537  C  CB  . LEU A 60  ? 0.1801 0.1427 0.1861 -0.0167 0.0013  0.0092  60  LEU A CB  
538  C  CG  . LEU A 60  ? 0.2300 0.1305 0.1942 0.0049  -0.0151 0.0348  60  LEU A CG  
539  C  CD1 . LEU A 60  ? 0.2238 0.1909 0.1985 -0.0529 -0.0132 0.0549  60  LEU A CD1 
540  C  CD2 . LEU A 60  ? 0.2337 0.1503 0.2361 -0.0430 -0.0197 0.0159  60  LEU A CD2 
541  N  N   . ASN A 61  ? 0.1943 0.1282 0.1260 -0.0100 0.0035  0.0379  61  ASN A N   
542  C  CA  . ASN A 61  ? 0.1917 0.1559 0.1113 -0.0193 0.0126  -0.0126 61  ASN A CA  
543  C  C   . ASN A 61  ? 0.2043 0.1298 0.1235 -0.0292 0.0099  0.0126  61  ASN A C   
544  O  O   . ASN A 61  ? 0.2098 0.1604 0.1430 -0.0256 0.0137  0.0469  61  ASN A O   
545  C  CB  . ASN A 61  ? 0.2641 0.1351 0.1224 -0.0092 0.0166  0.0258  61  ASN A CB  
546  C  CG  . ASN A 61  ? 0.2028 0.1529 0.1095 -0.0307 0.0057  -0.0063 61  ASN A CG  
547  O  OD1 . ASN A 61  ? 0.2148 0.1596 0.1357 -0.0272 0.0080  0.0129  61  ASN A OD1 
548  N  ND2 . ASN A 61  ? 0.2563 0.1517 0.1206 -0.0229 0.0265  -0.0015 61  ASN A ND2 
549  N  N   . ASN A 62  ? 0.2395 0.1266 0.1143 -0.0370 0.0024  0.0083  62  ASN A N   
550  C  CA  . ASN A 62  ? 0.2182 0.1659 0.1369 -0.0231 -0.0133 0.0192  62  ASN A CA  
551  C  C   . ASN A 62  ? 0.1967 0.1676 0.1397 -0.1001 0.0026  0.0057  62  ASN A C   
552  O  O   . ASN A 62  ? 0.2217 0.2064 0.2204 -0.0656 0.0105  -0.0017 62  ASN A O   
553  C  CB  . ASN A 62  ? 0.2298 0.1379 0.1559 -0.0454 0.0052  0.0148  62  ASN A CB  
554  C  CG  . ASN A 62  ? 0.1875 0.1618 0.1375 -0.0434 -0.0320 -0.0057 62  ASN A CG  
555  O  OD1 . ASN A 62  ? 0.2499 0.1439 0.1369 -0.0487 -0.0109 0.0107  62  ASN A OD1 
556  N  ND2 . ASN A 62  ? 0.2657 0.1634 0.1479 -0.0197 -0.0193 0.0048  62  ASN A ND2 
557  N  N   . GLY A 63  ? 0.2012 0.1766 0.1333 -0.0348 0.0046  0.0187  63  GLY A N   
558  C  CA  . GLY A 63  ? 0.2017 0.1845 0.1447 -0.0741 0.0200  0.0078  63  GLY A CA  
559  C  C   . GLY A 63  ? 0.1946 0.1659 0.2022 -0.0181 0.0206  0.0113  63  GLY A C   
560  O  O   . GLY A 63  ? 0.2155 0.2368 0.2426 -0.0277 0.0535  0.0467  63  GLY A O   
561  N  N   . HIS A 64  ? 0.2104 0.1723 0.1335 -0.0397 0.0261  0.0155  64  HIS A N   
562  C  CA  . HIS A 64  ? 0.2417 0.1879 0.1756 0.0077  0.0390  0.0326  64  HIS A CA  
563  C  C   . HIS A 64  ? 0.2192 0.1233 0.1561 -0.0381 0.0313  0.0051  64  HIS A C   
564  O  O   . HIS A 64  ? 0.2143 0.1629 0.1811 -0.0280 0.0138  0.0447  64  HIS A O   
565  C  CB  . HIS A 64  ? 0.2476 0.2028 0.1666 -0.0348 0.0509  -0.0017 64  HIS A CB  
566  C  CG  . HIS A 64  ? 0.1929 0.1781 0.1341 -0.0289 0.0156  0.0093  64  HIS A CG  
567  N  ND1 . HIS A 64  ? 0.1921 0.1772 0.1641 -0.0060 -0.0046 -0.0263 64  HIS A ND1 
568  C  CD2 . HIS A 64  ? 0.2800 0.2117 0.1354 -0.0375 0.0000  -0.0304 64  HIS A CD2 
569  C  CE1 . HIS A 64  ? 0.1721 0.2180 0.1659 -0.0142 0.0051  -0.0147 64  HIS A CE1 
570  N  NE2 . HIS A 64  ? 0.2170 0.2311 0.1721 -0.0485 0.0027  -0.0197 64  HIS A NE2 
571  N  N   . ALA A 65  ? 0.1990 0.1254 0.1395 -0.0212 0.0138  0.0052  65  ALA A N   
572  C  CA  . ALA A 65  ? 0.1849 0.1656 0.1274 -0.0671 0.0087  -0.0026 65  ALA A CA  
573  C  C   . ALA A 65  ? 0.2394 0.1228 0.0913 -0.0267 0.0152  0.0008  65  ALA A C   
574  O  O   . ALA A 65  ? 0.2273 0.1528 0.1313 -0.0436 0.0247  -0.0021 65  ALA A O   
575  C  CB  . ALA A 65  ? 0.1886 0.3574 0.1296 -0.0461 0.0017  -0.0662 65  ALA A CB  
576  N  N   . PHE A 66  ? 0.2178 0.1498 0.1344 -0.0288 0.0170  0.0126  66  PHE A N   
577  C  CA  . PHE A 66  ? 0.2784 0.1489 0.1219 0.0118  0.0104  0.0348  66  PHE A CA  
578  C  C   . PHE A 66  ? 0.2387 0.1747 0.1059 -0.0241 0.0178  -0.0017 66  PHE A C   
579  O  O   . PHE A 66  ? 0.2698 0.1577 0.1210 -0.0109 0.0197  0.0160  66  PHE A O   
580  C  CB  . PHE A 66  ? 0.2703 0.2444 0.1036 0.0181  -0.0121 0.0111  66  PHE A CB  
581  C  CG  . PHE A 66  ? 0.2524 0.2343 0.0925 -0.0177 -0.0274 -0.0170 66  PHE A CG  
582  C  CD1 . PHE A 66  ? 0.2556 0.3048 0.1007 0.0590  -0.0584 -0.0340 66  PHE A CD1 
583  C  CD2 . PHE A 66  ? 0.2470 0.2151 0.1183 -0.0129 -0.0256 -0.0373 66  PHE A CD2 
584  C  CE1 . PHE A 66  ? 0.2354 0.3332 0.1851 0.0182  -0.0878 -0.0167 66  PHE A CE1 
585  C  CE2 . PHE A 66  ? 0.2879 0.2523 0.1442 -0.0555 -0.0403 -0.0710 66  PHE A CE2 
586  C  CZ  . PHE A 66  ? 0.2474 0.2778 0.1234 -0.0694 -0.0274 -0.0615 66  PHE A CZ  
587  N  N   . ASN A 67  ? 0.2646 0.1836 0.1449 0.0573  0.0277  0.0635  67  ASN A N   
588  C  CA  . ASN A 67  ? 0.2080 0.1665 0.1090 0.0164  0.0099  0.0120  67  ASN A CA  
589  C  C   . ASN A 67  ? 0.1773 0.1238 0.0992 -0.0065 -0.0403 0.0113  67  ASN A C   
590  O  O   . ASN A 67  ? 0.1975 0.1950 0.1037 -0.0173 -0.0211 0.0443  67  ASN A O   
591  C  CB  . ASN A 67  ? 0.1879 0.2822 0.1479 -0.0644 -0.0399 0.0467  67  ASN A CB  
592  C  CG  . ASN A 67  ? 0.2535 0.3731 0.1880 -0.0656 -0.0206 0.0923  67  ASN A CG  
593  O  OD1 . ASN A 67  ? 0.1846 0.1601 0.1592 -0.0375 -0.0276 0.0299  67  ASN A OD1 
594  N  ND2 . ASN A 67  ? 0.3788 0.3662 0.3521 -0.1861 -0.0544 0.1027  67  ASN A ND2 
595  N  N   . VAL A 68  ? 0.1905 0.1304 0.0939 -0.0010 -0.0024 0.0140  68  VAL A N   
596  C  CA  . VAL A 68  ? 0.2001 0.1254 0.0886 0.0164  -0.0335 0.0080  68  VAL A CA  
597  C  C   . VAL A 68  ? 0.2029 0.1348 0.0974 0.0052  -0.0386 0.0161  68  VAL A C   
598  O  O   . VAL A 68  ? 0.2116 0.1054 0.1001 0.0027  -0.0307 0.0131  68  VAL A O   
599  C  CB  . VAL A 68  ? 0.2001 0.1113 0.1444 -0.0178 -0.0280 -0.0010 68  VAL A CB  
600  C  CG1 . VAL A 68  ? 0.2201 0.1856 0.1421 0.0284  -0.0650 -0.0088 68  VAL A CG1 
601  C  CG2 . VAL A 68  ? 0.2311 0.1504 0.1596 -0.0307 -0.0230 -0.0324 68  VAL A CG2 
602  N  N   . GLU A 69  ? 0.2478 0.1257 0.1067 -0.0015 -0.0289 0.0157  69  GLU A N   
603  C  CA  . GLU A 69  ? 0.2356 0.1278 0.1025 0.0010  -0.0148 0.0114  69  GLU A CA  
604  C  C   . GLU A 69  ? 0.2252 0.1501 0.1016 0.0129  -0.0230 0.0403  69  GLU A C   
605  O  O   . GLU A 69  ? 0.2545 0.1405 0.1544 0.0032  -0.0582 0.0153  69  GLU A O   
606  C  CB  . GLU A 69  ? 0.1440 0.1949 0.2231 0.0043  0.0379  -0.0032 69  GLU A CB  
607  C  CG  . GLU A 69  ? 0.1640 0.2239 0.1935 -0.0496 0.0339  0.0310  69  GLU A CG  
608  C  CD  . GLU A 69  ? 0.1845 0.2315 0.3025 0.0286  0.0474  0.0454  69  GLU A CD  
609  O  OE1 . GLU A 69  ? 0.2522 0.2392 0.2438 -0.0196 0.0260  0.0693  69  GLU A OE1 
610  O  OE2 . GLU A 69  ? 0.2076 0.2011 0.2897 -0.0182 0.0237  0.0395  69  GLU A OE2 
611  N  N   . PHE A 70  ? 0.2213 0.1369 0.1156 -0.0026 -0.0289 0.0166  70  PHE A N   
612  C  CA  . PHE A 70  ? 0.2120 0.1133 0.1727 0.0049  -0.0747 0.0240  70  PHE A CA  
613  C  C   . PHE A 70  ? 0.2023 0.1308 0.1659 0.0031  -0.0593 0.0081  70  PHE A C   
614  O  O   . PHE A 70  ? 0.2311 0.1262 0.1886 0.0035  -0.0593 0.0269  70  PHE A O   
615  C  CB  . PHE A 70  ? 0.2318 0.1189 0.1449 0.0003  -0.0568 0.0259  70  PHE A CB  
616  C  CG  . PHE A 70  ? 0.1917 0.1147 0.1571 0.0091  -0.0430 0.0292  70  PHE A CG  
617  C  CD1 . PHE A 70  ? 0.2269 0.1269 0.1458 0.0126  -0.0395 0.0333  70  PHE A CD1 
618  C  CD2 . PHE A 70  ? 0.2018 0.1221 0.1398 0.0136  -0.0627 0.0164  70  PHE A CD2 
619  C  CE1 . PHE A 70  ? 0.2240 0.1348 0.1704 0.0293  -0.0120 0.0450  70  PHE A CE1 
620  C  CE2 . PHE A 70  ? 0.2238 0.1259 0.1339 0.0017  -0.0520 0.0063  70  PHE A CE2 
621  C  CZ  . PHE A 70  ? 0.2524 0.1080 0.1756 0.0161  -0.0287 0.0108  70  PHE A CZ  
622  N  N   . ASP A 71  ? 0.2885 0.1303 0.2231 0.0329  -0.1107 0.0511  71  ASP A N   
623  C  CA  . ASP A 71  ? 0.2730 0.1120 0.2833 0.0175  -0.0807 0.0579  71  ASP A CA  
624  C  C   . ASP A 71  ? 0.2129 0.0860 0.3210 0.0041  -0.0021 0.0032  71  ASP A C   
625  O  O   . ASP A 71  ? 0.2560 0.1947 0.4483 -0.0266 0.0137  -0.0152 71  ASP A O   
626  C  CB  . ASP A 71  ? 0.3467 0.1457 0.4230 0.0100  -0.1907 0.1040  71  ASP A CB  
627  C  CG  . ASP A 71  ? 0.4287 0.1780 0.4765 0.0089  -0.2084 0.1049  71  ASP A CG  
628  O  OD1 . ASP A 71  ? 0.3874 0.1673 0.4503 0.0215  -0.1114 0.1001  71  ASP A OD1 
629  O  OD2 . ASP A 71  ? 0.4503 0.1933 0.8456 0.0059  -0.3300 0.1324  71  ASP A OD2 
630  N  N   . ASP A 72  ? 0.2170 0.0887 0.2509 -0.0024 -0.0197 0.0186  72  ASP A N   
631  C  CA  . ASP A 72  ? 0.2301 0.1030 0.2469 -0.0088 0.0357  0.0087  72  ASP A CA  
632  C  C   . ASP A 72  ? 0.3242 0.1129 0.2743 -0.0265 0.0546  0.0070  72  ASP A C   
633  O  O   . ASP A 72  ? 0.3609 0.1451 0.2635 -0.0388 0.0794  -0.0109 72  ASP A O   
634  C  CB  . ASP A 72  ? 0.2304 0.1377 0.2016 -0.0065 0.0351  0.0274  72  ASP A CB  
635  C  CG  . ASP A 72  ? 0.2554 0.1614 0.1611 0.0066  -0.0126 0.0317  72  ASP A CG  
636  O  OD1 . ASP A 72  ? 0.2239 0.2617 0.1862 -0.0162 -0.0305 0.0610  72  ASP A OD1 
637  O  OD2 . ASP A 72  ? 0.2606 0.1881 0.1662 -0.0204 -0.0183 0.0140  72  ASP A OD2 
638  N  N   . SER A 73  ? 0.2918 0.0882 0.3512 0.0008  0.0372  0.0445  73  SER A N   
639  C  CA  . SER A 73  ? 0.3004 0.1077 0.3953 -0.0216 0.0080  0.0200  73  SER A CA  
640  C  C   . SER A 73  ? 0.2682 0.1133 0.3677 0.0010  0.0698  -0.0113 73  SER A C   
641  O  O   . SER A 73  ? 0.2846 0.1088 0.2939 -0.0071 -0.0048 0.0104  73  SER A O   
642  C  CB  . SER A 73  ? 0.4215 0.1597 0.4347 -0.0306 0.0023  0.0860  73  SER A CB  
643  O  OG  . SER A 73  ? 0.4160 0.1377 0.2950 0.0472  0.0430  0.0394  73  SER A OG  
644  N  N   . GLN A 74  ? 0.2548 0.1176 0.4448 0.0083  0.0500  -0.0109 74  GLN A N   
645  C  CA  . GLN A 74  ? 0.2983 0.1423 0.4916 0.0100  0.0851  0.0282  74  GLN A CA  
646  C  C   . GLN A 74  ? 0.3058 0.1829 0.4034 -0.0377 0.0623  -0.0782 74  GLN A C   
647  O  O   . GLN A 74  ? 0.2725 0.1990 0.2511 -0.0599 -0.0509 0.0195  74  GLN A O   
648  C  CB  . GLN A 74  ? 0.3321 0.1869 0.5848 -0.0335 0.0644  0.0564  74  GLN A CB  
649  C  CG  . GLN A 74  ? 0.3677 0.2383 0.6118 0.0240  0.0612  0.0834  74  GLN A CG  
650  C  CD  . GLN A 74  ? 0.4905 0.2746 0.5483 -0.0280 0.0710  0.1702  74  GLN A CD  
651  O  OE1 . GLN A 74  ? 0.5824 0.6729 0.9441 0.0311  0.2167  0.3811  74  GLN A OE1 
652  N  NE2 . GLN A 74  ? 0.9139 0.4207 0.5569 -0.2468 0.0816  -0.1221 74  GLN A NE2 
653  N  N   . ASP A 75  ? 0.3105 0.2969 0.3946 -0.0929 0.1041  -0.0860 75  ASP A N   
654  C  CA  . ASP A 75  ? 0.2775 0.2128 0.3944 -0.0568 0.0474  -0.0526 75  ASP A CA  
655  C  C   . ASP A 75  ? 0.2424 0.3518 0.4573 -0.0305 0.0306  -0.0904 75  ASP A C   
656  O  O   . ASP A 75  ? 0.2567 0.4122 0.7304 -0.0076 0.0403  -0.0926 75  ASP A O   
657  C  CB  . ASP A 75  ? 0.3817 0.3819 0.4258 -0.0905 0.1284  -0.0777 75  ASP A CB  
658  C  CG  . ASP A 75  ? 0.7232 0.3389 0.3955 -0.1739 -0.1248 0.1706  75  ASP A CG  
659  O  OD1 . ASP A 75  ? 0.2810 0.4211 0.5503 -0.0619 -0.1062 0.1736  75  ASP A OD1 
660  O  OD2 . ASP A 75  ? 1.1921 0.7213 0.8596 0.0960  0.2208  0.1024  75  ASP A OD2 
661  N  N   . LYS A 76  ? 0.2592 0.2217 0.2967 -0.0540 -0.0781 0.0917  76  LYS A N   
662  C  CA  . LYS A 76  ? 0.4648 0.1791 0.3855 -0.0732 -0.0586 0.0428  76  LYS A CA  
663  C  C   . LYS A 76  ? 0.5443 0.2627 0.6236 0.0724  -0.0992 0.2023  76  LYS A C   
664  O  O   . LYS A 76  ? 0.4471 0.7820 0.6262 -0.1586 -0.2637 0.2949  76  LYS A O   
665  C  CB  . LYS A 76  ? 0.3924 0.1700 0.3953 -0.0465 -0.1764 0.0478  76  LYS A CB  
666  C  CG  . LYS A 76  ? 0.6802 0.2573 0.3594 0.0280  -0.2601 0.0110  76  LYS A CG  
667  C  CD  . LYS A 76  ? 0.9963 0.1920 0.3303 -0.1057 -0.2745 0.0208  76  LYS A CD  
668  C  CE  . LYS A 76  ? 0.7512 0.4190 0.3773 -0.0211 -0.2330 0.1149  76  LYS A CE  
669  N  NZ  . LYS A 76  ? 0.6190 0.3206 0.4880 0.0092  -0.0758 0.1604  76  LYS A NZ  
670  N  N   . ALA A 77  ? 0.2771 0.3368 0.3730 0.0758  -0.1712 0.0395  77  ALA A N   
671  C  CA  . ALA A 77  ? 0.2172 0.2716 0.2513 -0.0119 -0.0905 0.0339  77  ALA A CA  
672  C  C   . ALA A 77  ? 0.1402 0.2074 0.2727 -0.0020 -0.0869 0.0021  77  ALA A C   
673  O  O   . ALA A 77  ? 0.1407 0.5217 0.2883 -0.0285 -0.0460 -0.0878 77  ALA A O   
674  C  CB  . ALA A 77  ? 0.3228 0.2504 0.2343 -0.0124 -0.1215 -0.0154 77  ALA A CB  
675  N  N   . VAL A 78  ? 0.1773 0.1817 0.2473 -0.0175 -0.0688 0.0322  78  VAL A N   
676  C  CA  . VAL A 78  ? 0.2169 0.1704 0.2268 0.0054  -0.0597 0.0265  78  VAL A CA  
677  C  C   . VAL A 78  ? 0.1682 0.1393 0.2301 -0.0187 -0.0524 0.0183  78  VAL A C   
678  O  O   . VAL A 78  ? 0.1502 0.1738 0.2717 -0.0281 -0.0557 0.0350  78  VAL A O   
679  C  CB  . VAL A 78  ? 0.3014 0.2099 0.3404 0.0662  -0.0738 -0.0008 78  VAL A CB  
680  C  CG1 . VAL A 78  ? 0.4352 0.1688 0.4498 0.0822  -0.0502 0.0239  78  VAL A CG1 
681  C  CG2 . VAL A 78  ? 0.2788 0.1854 0.3860 0.0379  -0.0529 0.0232  78  VAL A CG2 
682  N  N   . LEU A 79  ? 0.1247 0.1483 0.1810 -0.0082 -0.0245 0.0221  79  LEU A N   
683  C  CA  . LEU A 79  ? 0.1243 0.1544 0.1861 -0.0087 0.0006  0.0201  79  LEU A CA  
684  C  C   . LEU A 79  ? 0.1226 0.1484 0.1920 -0.0008 0.0023  0.0093  79  LEU A C   
685  O  O   . LEU A 79  ? 0.1542 0.1606 0.2020 -0.0159 0.0031  -0.0074 79  LEU A O   
686  C  CB  . LEU A 79  ? 0.1127 0.1644 0.1994 -0.0099 -0.0082 0.0229  79  LEU A CB  
687  C  CG  . LEU A 79  ? 0.1527 0.1606 0.1902 0.0130  0.0027  0.0318  79  LEU A CG  
688  C  CD1 . LEU A 79  ? 0.1481 0.1764 0.3608 0.0020  0.0269  0.0662  79  LEU A CD1 
689  C  CD2 . LEU A 79  ? 0.1307 0.1806 0.2107 0.0230  -0.0151 0.0013  79  LEU A CD2 
690  N  N   . LYS A 80  ? 0.1459 0.1732 0.1862 0.0031  0.0183  0.0066  80  LYS A N   
691  C  CA  . LYS A 80  ? 0.1420 0.1808 0.2284 0.0020  0.0339  0.0207  80  LYS A CA  
692  C  C   . LYS A 80  ? 0.1097 0.1713 0.2228 0.0109  0.0252  0.0206  80  LYS A C   
693  O  O   . LYS A 80  ? 0.1304 0.1624 0.2397 -0.0107 0.0031  0.0315  80  LYS A O   
694  C  CB  . LYS A 80  ? 0.1929 0.2104 0.3044 0.0384  0.0588  0.0159  80  LYS A CB  
695  C  CG  . LYS A 80  ? 0.1886 0.1961 0.3328 0.0465  0.0634  0.0560  80  LYS A CG  
696  C  CD  . LYS A 80  ? 0.5343 0.4072 0.5375 0.0209  -0.1624 0.1600  80  LYS A CD  
697  C  CE  . LYS A 80  ? 0.2839 0.7213 0.5103 0.1976  0.0137  0.0865  80  LYS A CE  
698  N  NZ  . LYS A 80  ? 0.5472 1.3888 1.2180 0.2800  0.3149  0.5644  80  LYS A NZ  
699  N  N   . GLY A 81  ? 0.1687 0.1800 0.2208 0.0260  0.0368  0.0295  81  GLY A N   
700  C  CA  . GLY A 81  ? 0.1660 0.1967 0.2340 0.0394  0.0652  0.0518  81  GLY A CA  
701  C  C   . GLY A 81  ? 0.1370 0.1820 0.2548 0.0227  0.0557  0.0324  81  GLY A C   
702  O  O   . GLY A 81  ? 0.1363 0.1694 0.2477 0.0003  0.0292  -0.0094 81  GLY A O   
703  N  N   . GLY A 82  ? 0.1313 0.2173 0.3906 0.0043  0.0375  0.0741  82  GLY A N   
704  C  CA  . GLY A 82  ? 0.1877 0.1985 0.4412 -0.0093 0.0498  0.0584  82  GLY A CA  
705  C  C   . GLY A 82  ? 0.2141 0.2002 0.3062 0.0439  0.1042  0.0641  82  GLY A C   
706  O  O   . GLY A 82  ? 0.2587 0.3767 0.3341 0.1345  0.1380  0.1288  82  GLY A O   
707  N  N   . PRO A 83  ? 0.1860 0.1491 0.2881 0.0249  0.0667  0.0278  83  PRO A N   
708  C  CA  . PRO A 83  ? 0.2169 0.1691 0.2354 0.0465  0.0445  0.0261  83  PRO A CA  
709  C  C   . PRO A 83  ? 0.1776 0.2334 0.2248 0.0386  0.0065  -0.0104 83  PRO A C   
710  O  O   . PRO A 83  ? 0.2390 0.2545 0.2210 0.0203  -0.0289 0.0071  83  PRO A O   
711  C  CB  . PRO A 83  ? 0.2211 0.1968 0.2205 0.0428  -0.0322 0.0136  83  PRO A CB  
712  C  CG  . PRO A 83  ? 0.1735 0.1847 0.2305 0.0531  0.0175  0.0051  83  PRO A CG  
713  C  CD  . PRO A 83  ? 0.1838 0.1449 0.2657 0.0381  0.0676  0.0248  83  PRO A CD  
714  N  N   . LEU A 84  ? 0.1665 0.1712 0.1925 0.0427  0.0285  0.0085  84  LEU A N   
715  C  CA  . LEU A 84  ? 0.1842 0.1404 0.2008 0.0377  0.0233  -0.0060 84  LEU A CA  
716  C  C   . LEU A 84  ? 0.1639 0.1836 0.2390 0.0505  0.0052  -0.0313 84  LEU A C   
717  O  O   . LEU A 84  ? 0.2040 0.1798 0.2540 0.0438  0.0478  -0.0307 84  LEU A O   
718  C  CB  . LEU A 84  ? 0.1459 0.1298 0.1958 0.0194  0.0289  -0.0076 84  LEU A CB  
719  C  CG  . LEU A 84  ? 0.1266 0.1213 0.2030 0.0178  0.0362  -0.0043 84  LEU A CG  
720  C  CD1 . LEU A 84  ? 0.1497 0.1828 0.1747 0.0124  0.0126  -0.0049 84  LEU A CD1 
721  C  CD2 . LEU A 84  ? 0.1279 0.1250 0.2028 0.0094  0.0281  -0.0146 84  LEU A CD2 
722  N  N   . ASP A 85  ? 0.2492 0.1665 0.2283 0.0267  0.0211  -0.0577 85  ASP A N   
723  C  CA  . ASP A 85  ? 0.3130 0.1606 0.2505 0.0217  0.0463  -0.0317 85  ASP A CA  
724  C  C   . ASP A 85  ? 0.3416 0.1824 0.3062 -0.0013 -0.0463 -0.0829 85  ASP A C   
725  O  O   . ASP A 85  ? 0.3986 0.3140 0.8392 0.1605  0.0908  0.1851  85  ASP A O   
726  C  CB  . ASP A 85  ? 0.3989 0.1669 0.2592 0.0531  0.0304  -0.0351 85  ASP A CB  
727  C  CG  . ASP A 85  ? 0.3388 0.3614 0.2556 -0.0570 0.0410  -0.0196 85  ASP A CG  
728  O  OD1 . ASP A 85  ? 0.3804 0.6603 0.3682 -0.0861 0.0764  0.1315  85  ASP A OD1 
729  O  OD2 . ASP A 85  ? 0.3248 0.3982 0.4190 -0.0269 -0.0681 -0.1058 85  ASP A OD2 
730  N  N   . GLY A 86  ? 0.6741 0.1666 0.2545 0.0159  -0.0031 -0.0662 86  GLY A N   
731  C  CA  . GLY A 86  ? 0.5044 0.4526 0.2869 -0.2099 -0.0590 0.1256  86  GLY A CA  
732  C  C   . GLY A 86  ? 0.3162 0.2961 0.2983 -0.1079 -0.0007 0.0636  86  GLY A C   
733  O  O   . GLY A 86  ? 0.3481 0.3896 0.3213 -0.1876 -0.0148 0.0722  86  GLY A O   
734  N  N   A THR A 87  ? 0.2560 0.1831 0.2666 0.0456  0.0935  -0.0151 87  THR A N   
735  N  N   B THR A 87  ? 0.1955 0.1172 0.2488 -0.0294 -0.0096 -0.0060 87  THR A N   
736  C  CA  A THR A 87  ? 0.1704 0.2261 0.3136 0.0322  0.0219  -0.0322 87  THR A CA  
737  C  CA  B THR A 87  ? 0.1541 0.1183 0.2168 0.0172  0.0423  -0.0305 87  THR A CA  
738  C  C   A THR A 87  ? 0.1297 0.1342 0.2900 0.0239  -0.0135 -0.0414 87  THR A C   
739  C  C   B THR A 87  ? 0.1237 0.1167 0.1697 0.0142  0.0237  0.0189  87  THR A C   
740  O  O   A THR A 87  ? 0.1793 0.0982 0.2108 0.0221  -0.0044 -0.0020 87  THR A O   
741  O  O   B THR A 87  ? 0.1334 0.1242 0.1557 0.0046  0.0280  -0.0098 87  THR A O   
742  C  CB  A THR A 87  ? 0.1816 0.1999 0.4293 0.0186  0.0015  -0.0381 87  THR A CB  
743  C  CB  B THR A 87  ? 0.1577 0.1393 0.2879 0.0487  0.0575  -0.0006 87  THR A CB  
744  O  OG1 A THR A 87  ? 0.1660 0.3371 0.5340 0.0790  -0.0296 -0.1114 87  THR A OG1 
745  O  OG1 B THR A 87  ? 0.1231 0.1754 0.2090 0.0144  -0.0096 0.0458  87  THR A OG1 
746  C  CG2 A THR A 87  ? 0.1486 0.2286 0.4061 0.0252  -0.0003 -0.0310 87  THR A CG2 
747  C  CG2 B THR A 87  ? 0.1960 0.1780 0.2645 0.0335  0.0625  0.0028  87  THR A CG2 
748  N  N   . TYR A 88  ? 0.1283 0.1158 0.1972 0.0182  0.0015  -0.0154 88  TYR A N   
749  C  CA  . TYR A 88  ? 0.1172 0.1239 0.1708 0.0093  -0.0046 -0.0087 88  TYR A CA  
750  C  C   . TYR A 88  ? 0.1140 0.1317 0.1645 0.0089  -0.0076 -0.0028 88  TYR A C   
751  O  O   . TYR A 88  ? 0.1515 0.1881 0.1970 -0.0419 -0.0412 0.0239  88  TYR A O   
752  C  CB  . TYR A 88  ? 0.1482 0.1018 0.1692 0.0109  -0.0142 0.0028  88  TYR A CB  
753  C  CG  . TYR A 88  ? 0.1165 0.0907 0.1570 0.0105  0.0015  -0.0085 88  TYR A CG  
754  C  CD1 . TYR A 88  ? 0.1386 0.1290 0.1525 0.0155  0.0019  -0.0038 88  TYR A CD1 
755  C  CD2 . TYR A 88  ? 0.1273 0.0768 0.1401 0.0144  -0.0046 0.0086  88  TYR A CD2 
756  C  CE1 . TYR A 88  ? 0.1315 0.1176 0.1563 0.0208  0.0126  -0.0152 88  TYR A CE1 
757  C  CE2 . TYR A 88  ? 0.1247 0.0886 0.1362 0.0062  0.0021  -0.0017 88  TYR A CE2 
758  C  CZ  . TYR A 88  ? 0.1368 0.0952 0.1377 0.0043  0.0052  -0.0121 88  TYR A CZ  
759  O  OH  . TYR A 88  ? 0.1344 0.1154 0.1388 0.0007  0.0051  -0.0190 88  TYR A OH  
760  N  N   . ARG A 89  ? 0.1190 0.1194 0.1588 0.0197  -0.0156 -0.0161 89  ARG A N   
761  C  CA  . ARG A 89  ? 0.1515 0.1120 0.1659 0.0156  -0.0344 -0.0054 89  ARG A CA  
762  C  C   . ARG A 89  ? 0.1235 0.0863 0.1095 -0.0060 -0.0197 0.0245  89  ARG A C   
763  O  O   . ARG A 89  ? 0.1180 0.0847 0.1287 0.0028  -0.0172 0.0087  89  ARG A O   
764  C  CB  . ARG A 89  ? 0.2623 0.0681 0.2214 0.0318  -0.0662 0.0199  89  ARG A CB  
765  C  CG  . ARG A 89  ? 0.2565 0.1289 0.1904 0.0026  -0.0222 0.0198  89  ARG A CG  
766  C  CD  . ARG A 89  ? 0.2673 0.1398 0.2315 0.0476  -0.0087 0.0318  89  ARG A CD  
767  N  NE  . ARG A 89  ? 0.2821 0.1331 0.2148 0.0188  -0.0225 0.0317  89  ARG A NE  
768  C  CZ  . ARG A 89  ? 0.2616 0.1304 0.1636 0.0113  0.0027  0.0094  89  ARG A CZ  
769  N  NH1 . ARG A 89  ? 0.2784 0.1897 0.2754 -0.0007 0.0434  0.0615  89  ARG A NH1 
770  N  NH2 . ARG A 89  ? 0.3016 0.1333 0.2372 0.0449  0.0089  0.0137  89  ARG A NH2 
771  N  N   . LEU A 90  ? 0.1318 0.1005 0.1348 -0.0060 -0.0322 0.0215  90  LEU A N   
772  C  CA  . LEU A 90  ? 0.1458 0.1059 0.1304 -0.0113 -0.0331 0.0174  90  LEU A CA  
773  C  C   . LEU A 90  ? 0.1537 0.1110 0.1061 -0.0063 -0.0379 0.0172  90  LEU A C   
774  O  O   . LEU A 90  ? 0.1542 0.1351 0.1597 0.0020  -0.0383 0.0524  90  LEU A O   
775  C  CB  . LEU A 90  ? 0.1574 0.1177 0.1430 -0.0252 -0.0452 0.0152  90  LEU A CB  
776  C  CG  . LEU A 90  ? 0.1621 0.1262 0.1430 -0.0377 -0.0417 0.0015  90  LEU A CG  
777  C  CD1 . LEU A 90  ? 0.2069 0.1101 0.1613 -0.0292 -0.0241 0.0135  90  LEU A CD1 
778  C  CD2 . LEU A 90  ? 0.1805 0.1826 0.1820 -0.0388 -0.0560 -0.0035 90  LEU A CD2 
779  N  N   . ILE A 91  ? 0.1559 0.0847 0.1147 -0.0087 -0.0122 0.0093  91  ILE A N   
780  C  CA  . ILE A 91  ? 0.1577 0.0922 0.1115 -0.0110 -0.0148 0.0078  91  ILE A CA  
781  C  C   . ILE A 91  ? 0.1456 0.0922 0.1019 -0.0147 -0.0231 0.0208  91  ILE A C   
782  O  O   . ILE A 91  ? 0.1942 0.0921 0.1011 -0.0107 -0.0320 0.0175  91  ILE A O   
783  C  CB  . ILE A 91  ? 0.2012 0.0978 0.1116 -0.0263 -0.0077 0.0105  91  ILE A CB  
784  C  CG1 . ILE A 91  ? 0.2098 0.1484 0.1467 -0.0683 -0.0138 0.0041  91  ILE A CG1 
785  C  CG2 . ILE A 91  ? 0.1723 0.1002 0.1441 -0.0105 -0.0166 0.0082  91  ILE A CG2 
786  C  CD1 . ILE A 91  ? 0.2155 0.1747 0.1899 -0.0804 -0.0027 -0.0055 91  ILE A CD1 
787  N  N   . GLN A 92  ? 0.1620 0.0830 0.1022 -0.0086 -0.0243 0.0216  92  GLN A N   
788  C  CA  . GLN A 92  ? 0.1648 0.0838 0.0986 -0.0102 -0.0175 0.0085  92  GLN A CA  
789  C  C   . GLN A 92  ? 0.1501 0.0934 0.0961 -0.0116 -0.0251 0.0104  92  GLN A C   
790  O  O   . GLN A 92  ? 0.1657 0.0868 0.0957 -0.0083 -0.0141 0.0060  92  GLN A O   
791  C  CB  . GLN A 92  ? 0.1818 0.1028 0.1176 -0.0003 -0.0335 0.0135  92  GLN A CB  
792  C  CG  . GLN A 92  ? 0.1733 0.1034 0.1460 -0.0068 -0.0289 0.0167  92  GLN A CG  
793  C  CD  . GLN A 92  ? 0.1519 0.1216 0.1500 -0.0157 -0.0208 0.0207  92  GLN A CD  
794  O  OE1 . GLN A 92  ? 0.1676 0.1020 0.1368 -0.0060 -0.0294 0.0271  92  GLN A OE1 
795  N  NE2 . GLN A 92  ? 0.1873 0.1601 0.1655 -0.0168 -0.0028 0.0120  92  GLN A NE2 
796  N  N   . PHE A 93  ? 0.1649 0.0759 0.0920 0.0001  -0.0212 0.0074  93  PHE A N   
797  C  CA  . PHE A 93  ? 0.1517 0.0780 0.0932 -0.0136 -0.0137 0.0024  93  PHE A CA  
798  C  C   . PHE A 93  ? 0.1412 0.0754 0.0885 -0.0114 -0.0294 0.0114  93  PHE A C   
799  O  O   . PHE A 93  ? 0.1799 0.1041 0.0851 -0.0062 -0.0259 0.0115  93  PHE A O   
800  C  CB  . PHE A 93  ? 0.1571 0.0962 0.1000 -0.0092 -0.0443 0.0104  93  PHE A CB  
801  C  CG  . PHE A 93  ? 0.1600 0.0834 0.1131 -0.0207 -0.0428 0.0245  93  PHE A CG  
802  C  CD1 . PHE A 93  ? 0.1702 0.0987 0.1039 -0.0035 -0.0348 -0.0017 93  PHE A CD1 
803  C  CD2 . PHE A 93  ? 0.1810 0.1092 0.1138 -0.0003 -0.0480 0.0245  93  PHE A CD2 
804  C  CE1 . PHE A 93  ? 0.1747 0.1143 0.1376 0.0027  -0.0573 0.0020  93  PHE A CE1 
805  C  CE2 . PHE A 93  ? 0.1884 0.1208 0.1326 -0.0038 -0.0653 0.0037  93  PHE A CE2 
806  C  CZ  . PHE A 93  ? 0.2161 0.1089 0.1410 0.0020  -0.0807 -0.0048 93  PHE A CZ  
807  N  N   . HIS A 94  ? 0.1527 0.0830 0.0903 -0.0094 -0.0287 0.0097  94  HIS A N   
808  C  CA  . HIS A 94  ? 0.1442 0.0800 0.0848 -0.0068 -0.0197 0.0055  94  HIS A CA  
809  C  C   . HIS A 94  ? 0.1246 0.0908 0.0807 -0.0189 -0.0245 0.0001  94  HIS A C   
810  O  O   . HIS A 94  ? 0.1379 0.0856 0.0837 -0.0137 -0.0097 0.0109  94  HIS A O   
811  C  CB  . HIS A 94  ? 0.1543 0.0939 0.0812 -0.0184 -0.0080 0.0073  94  HIS A CB  
812  C  CG  . HIS A 94  ? 0.1341 0.0834 0.0904 -0.0248 -0.0013 -0.0005 94  HIS A CG  
813  N  ND1 . HIS A 94  ? 0.1325 0.0824 0.0886 -0.0215 -0.0137 0.0068  94  HIS A ND1 
814  C  CD2 . HIS A 94  ? 0.1185 0.0991 0.0766 -0.0183 -0.0103 0.0000  94  HIS A CD2 
815  C  CE1 . HIS A 94  ? 0.1162 0.0908 0.0987 -0.0120 -0.0073 0.0114  94  HIS A CE1 
816  N  NE2 . HIS A 94  ? 0.1204 0.0837 0.0926 -0.0094 -0.0031 0.0020  94  HIS A NE2 
817  N  N   . PHE A 95  ? 0.1270 0.0913 0.0830 -0.0167 -0.0151 0.0054  95  PHE A N   
818  C  CA  . PHE A 95  ? 0.1362 0.0870 0.0882 -0.0057 -0.0160 0.0062  95  PHE A CA  
819  C  C   . PHE A 95  ? 0.1224 0.0834 0.0855 -0.0108 -0.0107 -0.0114 95  PHE A C   
820  O  O   . PHE A 95  ? 0.1252 0.0992 0.1062 -0.0204 -0.0102 0.0131  95  PHE A O   
821  C  CB  . PHE A 95  ? 0.1298 0.0898 0.1077 -0.0087 -0.0219 -0.0063 95  PHE A CB  
822  C  CG  . PHE A 95  ? 0.1557 0.0829 0.0929 -0.0083 -0.0281 -0.0140 95  PHE A CG  
823  C  CD1 . PHE A 95  ? 0.1617 0.0970 0.1104 -0.0100 -0.0384 0.0035  95  PHE A CD1 
824  C  CD2 . PHE A 95  ? 0.1427 0.0986 0.1199 -0.0237 -0.0244 -0.0149 95  PHE A CD2 
825  C  CE1 . PHE A 95  ? 0.1744 0.1162 0.1254 -0.0100 -0.0460 -0.0104 95  PHE A CE1 
826  C  CE2 . PHE A 95  ? 0.1464 0.1124 0.1265 -0.0038 -0.0348 -0.0259 95  PHE A CE2 
827  C  CZ  . PHE A 95  ? 0.1576 0.1243 0.1212 -0.0041 -0.0381 -0.0315 95  PHE A CZ  
828  N  N   . HIS A 96  ? 0.1138 0.0883 0.0812 -0.0074 -0.0175 -0.0049 96  HIS A N   
829  C  CA  . HIS A 96  ? 0.1185 0.0838 0.1004 -0.0043 -0.0057 -0.0008 96  HIS A CA  
830  C  C   . HIS A 96  ? 0.1303 0.0891 0.0776 -0.0051 -0.0017 -0.0103 96  HIS A C   
831  O  O   . HIS A 96  ? 0.1225 0.0859 0.0988 -0.0093 0.0041  -0.0065 96  HIS A O   
832  C  CB  . HIS A 96  ? 0.1198 0.0896 0.0956 -0.0135 -0.0098 -0.0165 96  HIS A CB  
833  C  CG  . HIS A 96  ? 0.1106 0.0922 0.0868 -0.0024 -0.0121 -0.0102 96  HIS A CG  
834  N  ND1 . HIS A 96  ? 0.1156 0.0834 0.1158 -0.0063 -0.0006 -0.0107 96  HIS A ND1 
835  C  CD2 . HIS A 96  ? 0.1093 0.0772 0.0900 -0.0012 -0.0179 -0.0102 96  HIS A CD2 
836  C  CE1 . HIS A 96  ? 0.1195 0.0869 0.1054 -0.0017 -0.0003 -0.0135 96  HIS A CE1 
837  N  NE2 . HIS A 96  ? 0.1099 0.0799 0.0918 0.0000  -0.0074 -0.0092 96  HIS A NE2 
838  N  N   . TRP A 97  ? 0.1307 0.0797 0.0839 -0.0065 -0.0059 -0.0080 97  TRP A N   
839  C  CA  . TRP A 97  ? 0.1323 0.0882 0.0932 -0.0115 -0.0060 -0.0121 97  TRP A CA  
840  C  C   . TRP A 97  ? 0.1215 0.0961 0.0892 -0.0021 0.0082  -0.0089 97  TRP A C   
841  O  O   . TRP A 97  ? 0.1222 0.0935 0.1138 -0.0124 0.0119  -0.0142 97  TRP A O   
842  C  CB  . TRP A 97  ? 0.1573 0.0970 0.0886 -0.0229 -0.0119 -0.0081 97  TRP A CB  
843  C  CG  . TRP A 97  ? 0.1475 0.0908 0.0932 -0.0144 -0.0118 -0.0137 97  TRP A CG  
844  C  CD1 . TRP A 97  ? 0.1661 0.1131 0.0945 -0.0176 -0.0013 -0.0170 97  TRP A CD1 
845  C  CD2 . TRP A 97  ? 0.1627 0.1050 0.0828 -0.0221 -0.0087 -0.0026 97  TRP A CD2 
846  N  NE1 . TRP A 97  ? 0.2005 0.1057 0.0881 -0.0137 0.0074  -0.0147 97  TRP A NE1 
847  C  CE2 . TRP A 97  ? 0.1756 0.1104 0.0958 -0.0333 -0.0035 -0.0102 97  TRP A CE2 
848  C  CE3 . TRP A 97  ? 0.1535 0.1010 0.0898 -0.0017 -0.0272 -0.0005 97  TRP A CE3 
849  C  CZ2 . TRP A 97  ? 0.1849 0.1159 0.0978 -0.0215 -0.0054 -0.0088 97  TRP A CZ2 
850  C  CZ3 . TRP A 97  ? 0.1926 0.1159 0.0869 -0.0093 -0.0153 -0.0026 97  TRP A CZ3 
851  C  CH2 . TRP A 97  ? 0.2184 0.1111 0.1001 -0.0348 -0.0001 -0.0060 97  TRP A CH2 
852  N  N   . GLY A 98  ? 0.1467 0.0883 0.1058 -0.0116 0.0026  -0.0130 98  GLY A N   
853  C  CA  . GLY A 98  ? 0.1325 0.1037 0.1072 -0.0027 -0.0006 -0.0103 98  GLY A CA  
854  C  C   . GLY A 98  ? 0.1493 0.0962 0.1116 -0.0207 0.0071  -0.0105 98  GLY A C   
855  O  O   . GLY A 98  ? 0.1773 0.1115 0.1147 -0.0093 -0.0087 -0.0254 98  GLY A O   
856  N  N   . SER A 99  ? 0.1580 0.1162 0.1386 -0.0093 0.0149  -0.0344 99  SER A N   
857  C  CA  . SER A 99  ? 0.1694 0.1092 0.1504 -0.0154 0.0201  -0.0522 99  SER A CA  
858  C  C   . SER A 99  ? 0.1755 0.1129 0.1810 0.0043  0.0078  -0.0582 99  SER A C   
859  O  O   . SER A 99  ? 0.2786 0.1437 0.1826 -0.0094 -0.0074 -0.0627 99  SER A O   
860  C  CB  . SER A 99  ? 0.1969 0.1333 0.1875 -0.0165 0.0388  -0.0557 99  SER A CB  
861  O  OG  . SER A 99  ? 0.1612 0.1150 0.2169 0.0083  0.0198  -0.0320 99  SER A OG  
862  N  N   . LEU A 100 ? 0.1693 0.1101 0.1871 -0.0074 0.0155  -0.0351 100 LEU A N   
863  C  CA  . LEU A 100 ? 0.2030 0.0850 0.2512 0.0019  0.0340  -0.0297 100 LEU A CA  
864  C  C   . LEU A 100 ? 0.1854 0.0944 0.1871 -0.0195 -0.0032 -0.0082 100 LEU A C   
865  O  O   . LEU A 100 ? 0.1905 0.0869 0.1843 -0.0162 0.0035  -0.0281 100 LEU A O   
866  C  CB  . LEU A 100 ? 0.2948 0.1643 0.3313 0.0540  0.0753  0.0342  100 LEU A CB  
867  C  CG  . LEU A 100 ? 0.2617 0.2628 0.2807 0.0318  0.0021  -0.0132 100 LEU A CG  
868  C  CD1 . LEU A 100 ? 0.2713 0.4334 0.3831 0.1542  0.0238  0.0469  100 LEU A CD1 
869  C  CD2 . LEU A 100 ? 0.5315 0.3206 0.4861 -0.0089 0.1342  -0.1032 100 LEU A CD2 
870  N  N   . ASP A 101 ? 0.1617 0.1055 0.2040 -0.0083 -0.0052 -0.0291 101 ASP A N   
871  C  CA  . ASP A 101 ? 0.1754 0.0982 0.1833 -0.0157 0.0006  -0.0070 101 ASP A CA  
872  C  C   . ASP A 101 ? 0.1659 0.0966 0.1729 -0.0086 0.0109  -0.0076 101 ASP A C   
873  O  O   . ASP A 101 ? 0.2090 0.1327 0.1715 0.0015  0.0204  0.0012  101 ASP A O   
874  C  CB  . ASP A 101 ? 0.1990 0.1176 0.1972 -0.0308 -0.0252 0.0174  101 ASP A CB  
875  C  CG  . ASP A 101 ? 0.2166 0.1482 0.2402 -0.0480 0.0052  -0.0126 101 ASP A CG  
876  O  OD1 . ASP A 101 ? 0.2315 0.1616 0.1882 -0.0384 0.0038  -0.0147 101 ASP A OD1 
877  O  OD2 . ASP A 101 ? 0.2912 0.2100 0.2809 -0.1064 -0.0496 0.0074  101 ASP A OD2 
878  N  N   . GLY A 102 ? 0.1946 0.1020 0.1872 -0.0260 -0.0220 0.0162  102 GLY A N   
879  C  CA  . GLY A 102 ? 0.1938 0.1074 0.1942 -0.0248 -0.0144 0.0324  102 GLY A CA  
880  C  C   . GLY A 102 ? 0.1700 0.1037 0.1617 -0.0043 -0.0037 0.0137  102 GLY A C   
881  O  O   . GLY A 102 ? 0.1926 0.1061 0.1685 -0.0043 0.0057  0.0284  102 GLY A O   
882  N  N   . GLN A 103 ? 0.1703 0.0864 0.1439 -0.0196 0.0114  0.0071  103 GLN A N   
883  C  CA  . GLN A 103 ? 0.1469 0.0904 0.1303 -0.0038 0.0000  0.0100  103 GLN A CA  
884  C  C   . GLN A 103 ? 0.1237 0.0908 0.1115 -0.0046 0.0104  -0.0071 103 GLN A C   
885  O  O   . GLN A 103 ? 0.1527 0.0877 0.1196 -0.0077 0.0003  -0.0073 103 GLN A O   
886  C  CB  . GLN A 103 ? 0.1638 0.0944 0.1445 0.0167  0.0060  0.0037  103 GLN A CB  
887  C  CG  . GLN A 103 ? 0.1576 0.1195 0.1699 0.0185  0.0304  -0.0043 103 GLN A CG  
888  C  CD  . GLN A 103 ? 0.2138 0.1447 0.2188 0.0531  0.0641  0.0366  103 GLN A CD  
889  O  OE1 . GLN A 103 ? 0.2958 0.3080 0.3353 0.1641  0.1298  0.1603  103 GLN A OE1 
890  N  NE2 . GLN A 103 ? 0.1715 0.1440 0.2277 0.0353  0.0200  0.0166  103 GLN A NE2 
891  N  N   . GLY A 104 ? 0.1124 0.0916 0.1045 -0.0035 0.0043  -0.0063 104 GLY A N   
892  C  CA  . GLY A 104 ? 0.1264 0.0842 0.0899 -0.0113 -0.0104 0.0024  104 GLY A CA  
893  C  C   . GLY A 104 ? 0.1088 0.0870 0.1018 -0.0120 -0.0092 -0.0006 104 GLY A C   
894  O  O   . GLY A 104 ? 0.1199 0.0904 0.1106 -0.0107 -0.0027 0.0074  104 GLY A O   
895  N  N   . SER A 105 ? 0.1004 0.0891 0.1061 -0.0082 -0.0070 -0.0093 105 SER A N   
896  C  CA  . SER A 105 ? 0.1110 0.0826 0.0973 -0.0109 -0.0062 -0.0124 105 SER A CA  
897  C  C   . SER A 105 ? 0.0903 0.0882 0.1036 -0.0110 0.0027  -0.0071 105 SER A C   
898  O  O   . SER A 105 ? 0.1149 0.0923 0.1156 -0.0035 -0.0074 -0.0126 105 SER A O   
899  C  CB  . SER A 105 ? 0.0980 0.0803 0.1095 -0.0007 -0.0013 0.0091  105 SER A CB  
900  O  OG  . SER A 105 ? 0.1099 0.0795 0.1147 -0.0049 0.0037  0.0097  105 SER A OG  
901  N  N   . GLU A 106 ? 0.1037 0.0842 0.0879 -0.0087 0.0003  -0.0063 106 GLU A N   
902  C  CA  . GLU A 106 ? 0.1025 0.0825 0.0903 -0.0125 -0.0068 -0.0034 106 GLU A CA  
903  C  C   . GLU A 106 ? 0.0927 0.0718 0.1037 -0.0035 -0.0068 -0.0030 106 GLU A C   
904  O  O   . GLU A 106 ? 0.0987 0.0939 0.1014 0.0019  -0.0089 -0.0007 106 GLU A O   
905  C  CB  . GLU A 106 ? 0.1036 0.0819 0.0894 -0.0086 0.0043  0.0041  106 GLU A CB  
906  C  CG  . GLU A 106 ? 0.1420 0.0974 0.1036 -0.0105 0.0130  -0.0062 106 GLU A CG  
907  C  CD  . GLU A 106 ? 0.0975 0.0881 0.0996 -0.0086 0.0019  0.0013  106 GLU A CD  
908  O  OE1 . GLU A 106 ? 0.0932 0.0942 0.1228 -0.0052 -0.0010 -0.0059 106 GLU A OE1 
909  O  OE2 . GLU A 106 ? 0.1023 0.1136 0.1333 -0.0055 0.0140  -0.0132 106 GLU A OE2 
910  N  N   . HIS A 107 ? 0.0982 0.0745 0.0914 -0.0001 -0.0030 0.0020  107 HIS A N   
911  C  CA  . HIS A 107 ? 0.0965 0.0799 0.0838 -0.0013 -0.0026 0.0027  107 HIS A CA  
912  C  C   . HIS A 107 ? 0.0777 0.0802 0.0939 0.0010  0.0031  0.0043  107 HIS A C   
913  O  O   . HIS A 107 ? 0.1036 0.0829 0.0969 -0.0049 -0.0098 0.0006  107 HIS A O   
914  C  CB  . HIS A 107 ? 0.0974 0.0778 0.0967 0.0024  0.0007  0.0005  107 HIS A CB  
915  C  CG  . HIS A 107 ? 0.0851 0.0863 0.0887 0.0140  -0.0049 -0.0005 107 HIS A CG  
916  N  ND1 . HIS A 107 ? 0.1104 0.0802 0.0887 0.0059  -0.0146 0.0001  107 HIS A ND1 
917  C  CD2 . HIS A 107 ? 0.0843 0.0848 0.0986 0.0119  -0.0104 -0.0027 107 HIS A CD2 
918  C  CE1 . HIS A 107 ? 0.1007 0.0925 0.0974 0.0118  -0.0129 -0.0104 107 HIS A CE1 
919  N  NE2 . HIS A 107 ? 0.0874 0.0905 0.0964 0.0057  -0.0083 -0.0120 107 HIS A NE2 
920  N  N   . THR A 108 ? 0.0992 0.0860 0.0930 -0.0027 -0.0041 0.0111  108 THR A N   
921  C  CA  . THR A 108 ? 0.1143 0.0732 0.0982 0.0000  0.0031  0.0111  108 THR A CA  
922  C  C   . THR A 108 ? 0.1177 0.0776 0.0956 -0.0035 -0.0086 0.0032  108 THR A C   
923  O  O   . THR A 108 ? 0.1104 0.0930 0.1131 0.0082  0.0003  0.0076  108 THR A O   
924  C  CB  . THR A 108 ? 0.1107 0.0892 0.1176 0.0113  -0.0104 0.0035  108 THR A CB  
925  O  OG1 . THR A 108 ? 0.1228 0.0983 0.1203 0.0109  -0.0146 -0.0013 108 THR A OG1 
926  C  CG2 . THR A 108 ? 0.1253 0.1174 0.1183 0.0161  0.0041  -0.0043 108 THR A CG2 
927  N  N   . VAL A 109 ? 0.1160 0.0926 0.1115 0.0000  -0.0057 0.0120  109 VAL A N   
928  C  CA  . VAL A 109 ? 0.1167 0.1032 0.1146 -0.0041 0.0115  0.0165  109 VAL A CA  
929  C  C   . VAL A 109 ? 0.1428 0.0930 0.1167 -0.0070 0.0068  0.0181  109 VAL A C   
930  O  O   . VAL A 109 ? 0.1419 0.1000 0.1280 0.0026  0.0099  0.0245  109 VAL A O   
931  C  CB  . VAL A 109 ? 0.1164 0.1199 0.1396 -0.0074 0.0068  0.0303  109 VAL A CB  
932  C  CG1 . VAL A 109 ? 0.1315 0.1512 0.1594 -0.0043 0.0159  0.0317  109 VAL A CG1 
933  C  CG2 . VAL A 109 ? 0.1309 0.1333 0.1370 0.0115  -0.0097 0.0252  109 VAL A CG2 
934  N  N   . ASP A 110 ? 0.1474 0.1111 0.1167 0.0071  0.0131  0.0282  110 ASP A N   
935  C  CA  . ASP A 110 ? 0.1969 0.1106 0.1251 0.0111  0.0166  0.0388  110 ASP A CA  
936  C  C   . ASP A 110 ? 0.1829 0.1005 0.1192 0.0060  0.0041  0.0272  110 ASP A C   
937  O  O   . ASP A 110 ? 0.1904 0.1046 0.1404 0.0120  0.0062  0.0307  110 ASP A O   
938  C  CB  . ASP A 110 ? 0.2228 0.1289 0.1613 0.0210  0.0472  0.0482  110 ASP A CB  
939  C  CG  . ASP A 110 ? 0.2504 0.1527 0.1586 -0.0024 0.0313  0.0529  110 ASP A CG  
940  O  OD1 . ASP A 110 ? 0.2276 0.1636 0.1712 0.0342  0.0515  0.0465  110 ASP A OD1 
941  O  OD2 . ASP A 110 ? 0.2383 0.2232 0.1842 0.0183  0.0395  0.0392  110 ASP A OD2 
942  N  N   . LYS A 111 ? 0.1396 0.1075 0.1119 0.0135  -0.0031 0.0151  111 LYS A N   
943  C  CA  . LYS A 111 ? 0.1474 0.1048 0.1383 0.0241  -0.0060 0.0210  111 LYS A CA  
944  C  C   . LYS A 111 ? 0.1599 0.0864 0.1298 0.0129  0.0028  0.0043  111 LYS A C   
945  O  O   . LYS A 111 ? 0.1448 0.1313 0.1446 0.0104  0.0063  -0.0031 111 LYS A O   
946  C  CB  . LYS A 111 ? 0.1836 0.1412 0.1431 0.0443  -0.0162 0.0207  111 LYS A CB  
947  C  CG  . LYS A 111 ? 0.2925 0.1922 0.1571 0.1014  -0.0421 0.0035  111 LYS A CG  
948  C  CD  . LYS A 111 ? 0.2307 0.2460 0.2498 0.0485  -0.0851 -0.0386 111 LYS A CD  
949  C  CE  . LYS A 111 ? 0.2987 0.3730 0.2467 0.0791  -0.0634 -0.0511 111 LYS A CE  
950  N  NZ  . LYS A 111 ? 0.2641 0.3615 0.3367 0.0098  -0.0753 0.0644  111 LYS A NZ  
951  N  N   . LYS A 112 ? 0.1419 0.0910 0.1271 0.0049  -0.0070 0.0165  112 LYS A N   
952  C  CA  . LYS A 112 ? 0.1572 0.1013 0.1298 -0.0077 0.0086  0.0017  112 LYS A CA  
953  C  C   . LYS A 112 ? 0.1359 0.0851 0.1384 0.0119  -0.0037 0.0096  112 LYS A C   
954  O  O   . LYS A 112 ? 0.1439 0.0898 0.1216 -0.0035 -0.0041 -0.0030 112 LYS A O   
955  C  CB  . LYS A 112 ? 0.1559 0.1432 0.1614 -0.0267 -0.0023 0.0021  112 LYS A CB  
956  C  CG  . LYS A 112 ? 0.1387 0.1832 0.1560 -0.0251 -0.0120 -0.0127 112 LYS A CG  
957  C  CD  . LYS A 112 ? 0.1577 0.2325 0.2201 -0.0073 -0.0310 0.0216  112 LYS A CD  
958  C  CE  . LYS A 112 ? 0.1961 0.1928 0.2401 -0.0104 -0.0533 -0.0071 112 LYS A CE  
959  N  NZ  . LYS A 112 ? 0.2381 0.2021 0.2556 -0.0207 -0.0540 0.0463  112 LYS A NZ  
960  N  N   A LYS A 113 ? 0.1432 0.1004 0.1158 0.0146  -0.0144 0.0052  113 LYS A N   
961  N  N   B LYS A 113 ? 0.1467 0.1000 0.1177 0.0172  -0.0157 0.0043  113 LYS A N   
962  C  CA  A LYS A 113 ? 0.1391 0.0886 0.1288 0.0100  -0.0013 -0.0005 113 LYS A CA  
963  C  CA  B LYS A 113 ? 0.1424 0.0978 0.1274 0.0118  -0.0175 0.0026  113 LYS A CA  
964  C  C   A LYS A 113 ? 0.1315 0.0733 0.1348 -0.0037 0.0136  0.0140  113 LYS A C   
965  C  C   B LYS A 113 ? 0.1435 0.0800 0.1180 0.0024  -0.0027 -0.0065 113 LYS A C   
966  O  O   A LYS A 113 ? 0.2012 0.0773 0.2009 -0.0153 -0.0419 0.0131  113 LYS A O   
967  O  O   B LYS A 113 ? 0.1634 0.0781 0.1527 0.0010  -0.0340 0.0088  113 LYS A O   
968  C  CB  A LYS A 113 ? 0.1272 0.1099 0.1107 -0.0041 -0.0052 -0.0052 113 LYS A CB  
969  C  CB  B LYS A 113 ? 0.1553 0.1199 0.1242 0.0088  -0.0031 0.0020  113 LYS A CB  
970  C  CG  A LYS A 113 ? 0.1185 0.1102 0.1596 0.0148  -0.0041 -0.0120 113 LYS A CG  
971  C  CG  B LYS A 113 ? 0.1465 0.1938 0.1180 0.0216  0.0046  0.0077  113 LYS A CG  
972  C  CD  A LYS A 113 ? 0.1172 0.1415 0.1767 0.0093  0.0031  -0.0120 113 LYS A CD  
973  C  CD  B LYS A 113 ? 0.1388 0.1635 0.2070 0.0362  -0.0063 0.0041  113 LYS A CD  
974  C  CE  A LYS A 113 ? 0.1587 0.1420 0.2315 -0.0144 -0.0208 0.0303  113 LYS A CE  
975  C  CE  B LYS A 113 ? 0.1571 0.2861 0.2509 0.0298  -0.0133 0.0208  113 LYS A CE  
976  N  NZ  A LYS A 113 ? 0.1172 0.2162 0.2205 0.0229  -0.0329 0.0138  113 LYS A NZ  
977  N  NZ  B LYS A 113 ? 0.1753 0.2610 0.3016 0.0357  -0.0060 0.0035  113 LYS A NZ  
978  N  N   . TYR A 114 ? 0.1280 0.0790 0.1221 0.0001  -0.0046 0.0046  114 TYR A N   
979  C  CA  . TYR A 114 ? 0.1235 0.0917 0.1279 -0.0089 -0.0149 0.0099  114 TYR A CA  
980  C  C   . TYR A 114 ? 0.1120 0.0702 0.1192 -0.0073 -0.0073 -0.0015 114 TYR A C   
981  O  O   . TYR A 114 ? 0.1129 0.0922 0.1234 -0.0035 -0.0024 -0.0046 114 TYR A O   
982  C  CB  . TYR A 114 ? 0.1174 0.0891 0.1237 0.0007  -0.0074 0.0041  114 TYR A CB  
983  C  CG  . TYR A 114 ? 0.1131 0.0850 0.1271 0.0057  -0.0070 0.0171  114 TYR A CG  
984  C  CD1 . TYR A 114 ? 0.1512 0.1095 0.1291 0.0092  -0.0010 0.0060  114 TYR A CD1 
985  C  CD2 . TYR A 114 ? 0.1080 0.0984 0.1691 -0.0013 0.0034  0.0132  114 TYR A CD2 
986  C  CE1 . TYR A 114 ? 0.2189 0.1384 0.1278 0.0253  0.0256  0.0060  114 TYR A CE1 
987  C  CE2 . TYR A 114 ? 0.1336 0.1502 0.2003 0.0110  0.0252  0.0060  114 TYR A CE2 
988  C  CZ  . TYR A 114 ? 0.1797 0.1603 0.1843 -0.0086 0.0441  0.0250  114 TYR A CZ  
989  O  OH  . TYR A 114 ? 0.2928 0.2406 0.2240 0.0253  0.1124  0.0359  114 TYR A OH  
990  N  N   . ALA A 115 ? 0.1235 0.0812 0.1204 -0.0142 -0.0160 -0.0024 115 ALA A N   
991  C  CA  . ALA A 115 ? 0.1309 0.0762 0.1150 -0.0203 -0.0120 -0.0065 115 ALA A CA  
992  C  C   . ALA A 115 ? 0.1351 0.0859 0.0970 -0.0031 -0.0174 -0.0120 115 ALA A C   
993  O  O   . ALA A 115 ? 0.1347 0.0844 0.1279 -0.0109 -0.0015 -0.0063 115 ALA A O   
994  C  CB  . ALA A 115 ? 0.1498 0.1086 0.1345 -0.0166 -0.0168 -0.0142 115 ALA A CB  
995  N  N   . ALA A 116 ? 0.1250 0.0754 0.1098 -0.0068 -0.0063 0.0017  116 ALA A N   
996  C  CA  . ALA A 116 ? 0.1246 0.0816 0.0988 -0.0157 -0.0116 0.0005  116 ALA A CA  
997  C  C   . ALA A 116 ? 0.1150 0.0797 0.0935 -0.0030 -0.0131 0.0031  116 ALA A C   
998  O  O   . ALA A 116 ? 0.1158 0.0838 0.1001 -0.0092 -0.0051 0.0015  116 ALA A O   
999  C  CB  . ALA A 116 ? 0.1468 0.1004 0.1016 -0.0140 -0.0132 0.0015  116 ALA A CB  
1000 N  N   . GLU A 117 ? 0.1199 0.0727 0.0961 -0.0027 -0.0167 -0.0052 117 GLU A N   
1001 C  CA  . GLU A 117 ? 0.1165 0.0767 0.0881 -0.0013 -0.0087 0.0031  117 GLU A CA  
1002 C  C   . GLU A 117 ? 0.1098 0.0864 0.0788 0.0000  -0.0153 0.0005  117 GLU A C   
1003 O  O   . GLU A 117 ? 0.1221 0.1049 0.1142 0.0027  0.0028  0.0272  117 GLU A O   
1004 C  CB  . GLU A 117 ? 0.1235 0.0982 0.0847 0.0010  -0.0116 0.0003  117 GLU A CB  
1005 C  CG  . GLU A 117 ? 0.1111 0.0983 0.0945 -0.0077 -0.0146 -0.0059 117 GLU A CG  
1006 C  CD  . GLU A 117 ? 0.1058 0.0799 0.0940 -0.0044 -0.0068 0.0040  117 GLU A CD  
1007 O  OE1 . GLU A 117 ? 0.1138 0.0992 0.1066 -0.0020 -0.0091 0.0060  117 GLU A OE1 
1008 O  OE2 . GLU A 117 ? 0.1465 0.0966 0.0898 -0.0052 -0.0222 0.0000  117 GLU A OE2 
1009 N  N   . LEU A 118 ? 0.1138 0.0791 0.0918 -0.0073 -0.0228 0.0035  118 LEU A N   
1010 C  CA  . LEU A 118 ? 0.1127 0.0733 0.0868 0.0013  -0.0247 0.0043  118 LEU A CA  
1011 C  C   . LEU A 118 ? 0.1083 0.0645 0.0882 0.0031  -0.0197 0.0054  118 LEU A C   
1012 O  O   . LEU A 118 ? 0.1086 0.0778 0.0870 -0.0057 -0.0104 0.0034  118 LEU A O   
1013 C  CB  . LEU A 118 ? 0.1247 0.0762 0.1133 -0.0120 -0.0318 0.0119  118 LEU A CB  
1014 C  CG  . LEU A 118 ? 0.1308 0.1059 0.1061 -0.0049 -0.0405 0.0179  118 LEU A CG  
1015 C  CD1 . LEU A 118 ? 0.1544 0.0979 0.1122 -0.0102 -0.0452 0.0236  118 LEU A CD1 
1016 C  CD2 . LEU A 118 ? 0.1230 0.1357 0.1476 -0.0068 -0.0423 0.0151  118 LEU A CD2 
1017 N  N   . HIS A 119 ? 0.1115 0.0666 0.0778 -0.0046 -0.0193 0.0013  119 HIS A N   
1018 C  CA  . HIS A 119 ? 0.1070 0.0732 0.0750 -0.0041 -0.0201 0.0068  119 HIS A CA  
1019 C  C   . HIS A 119 ? 0.1077 0.0799 0.0798 -0.0131 -0.0245 0.0104  119 HIS A C   
1020 O  O   . HIS A 119 ? 0.1147 0.0841 0.0888 0.0048  -0.0125 0.0093  119 HIS A O   
1021 C  CB  . HIS A 119 ? 0.1004 0.0851 0.0885 0.0034  -0.0138 0.0060  119 HIS A CB  
1022 C  CG  . HIS A 119 ? 0.1032 0.0808 0.0816 -0.0103 -0.0197 -0.0089 119 HIS A CG  
1023 N  ND1 . HIS A 119 ? 0.0883 0.0859 0.0789 -0.0043 -0.0071 0.0000  119 HIS A ND1 
1024 C  CD2 . HIS A 119 ? 0.0982 0.0819 0.0888 -0.0032 -0.0164 0.0000  119 HIS A CD2 
1025 C  CE1 . HIS A 119 ? 0.1242 0.0905 0.0806 -0.0046 -0.0086 -0.0062 119 HIS A CE1 
1026 N  NE2 . HIS A 119 ? 0.0934 0.0910 0.0850 0.0000  -0.0148 0.0037  119 HIS A NE2 
1027 N  N   . LEU A 120 ? 0.0958 0.0709 0.1009 0.0005  -0.0167 0.0057  120 LEU A N   
1028 C  CA  . LEU A 120 ? 0.1102 0.0738 0.1077 0.0024  -0.0292 0.0030  120 LEU A CA  
1029 C  C   . LEU A 120 ? 0.0987 0.0821 0.0851 0.0065  -0.0148 0.0161  120 LEU A C   
1030 O  O   . LEU A 120 ? 0.0926 0.0776 0.0926 -0.0066 -0.0129 0.0055  120 LEU A O   
1031 C  CB  . LEU A 120 ? 0.1147 0.0789 0.1262 -0.0003 -0.0317 0.0017  120 LEU A CB  
1032 C  CG  . LEU A 120 ? 0.1268 0.0983 0.1246 -0.0115 -0.0390 0.0049  120 LEU A CG  
1033 C  CD1 . LEU A 120 ? 0.2379 0.1727 0.1689 -0.0898 -0.0220 0.0010  120 LEU A CD1 
1034 C  CD2 . LEU A 120 ? 0.1594 0.1510 0.1365 0.0010  -0.0601 -0.0092 120 LEU A CD2 
1035 N  N   . VAL A 121 ? 0.1176 0.0825 0.0983 -0.0082 -0.0174 0.0140  121 VAL A N   
1036 C  CA  . VAL A 121 ? 0.1131 0.0747 0.0965 -0.0051 -0.0107 0.0046  121 VAL A CA  
1037 C  C   . VAL A 121 ? 0.1095 0.0728 0.1009 -0.0063 -0.0074 0.0076  121 VAL A C   
1038 O  O   . VAL A 121 ? 0.1310 0.0815 0.1027 0.0015  -0.0242 0.0131  121 VAL A O   
1039 C  CB  . VAL A 121 ? 0.1190 0.0747 0.1133 0.0041  -0.0088 0.0052  121 VAL A CB  
1040 C  CG1 . VAL A 121 ? 0.1266 0.0913 0.1215 -0.0103 -0.0006 -0.0076 121 VAL A CG1 
1041 C  CG2 . VAL A 121 ? 0.1217 0.0942 0.1199 0.0048  -0.0068 0.0044  121 VAL A CG2 
1042 N  N   . HIS A 122 ? 0.1052 0.0671 0.1027 -0.0034 -0.0148 0.0065  122 HIS A N   
1043 C  CA  . HIS A 122 ? 0.1242 0.0807 0.1027 -0.0006 -0.0171 0.0034  122 HIS A CA  
1044 C  C   . HIS A 122 ? 0.1221 0.0750 0.1032 0.0055  -0.0201 0.0109  122 HIS A C   
1045 O  O   . HIS A 122 ? 0.1319 0.0803 0.1187 -0.0083 -0.0226 0.0122  122 HIS A O   
1046 C  CB  . HIS A 122 ? 0.1136 0.0747 0.1317 0.0051  -0.0121 0.0017  122 HIS A CB  
1047 C  CG  . HIS A 122 ? 0.1019 0.0868 0.1194 0.0080  -0.0035 0.0130  122 HIS A CG  
1048 N  ND1 . HIS A 122 ? 0.1014 0.0860 0.1228 0.0019  -0.0130 0.0206  122 HIS A ND1 
1049 C  CD2 . HIS A 122 ? 0.1093 0.1070 0.1210 -0.0013 -0.0055 0.0052  122 HIS A CD2 
1050 C  CE1 . HIS A 122 ? 0.0961 0.1208 0.1407 0.0065  -0.0102 0.0059  122 HIS A CE1 
1051 N  NE2 . HIS A 122 ? 0.1127 0.1009 0.1437 -0.0070 -0.0207 0.0077  122 HIS A NE2 
1052 N  N   . TRP A 123 ? 0.1138 0.0720 0.1199 -0.0013 -0.0097 0.0001  123 TRP A N   
1053 C  CA  . TRP A 123 ? 0.1190 0.0714 0.1115 -0.0062 -0.0082 -0.0038 123 TRP A CA  
1054 C  C   . TRP A 123 ? 0.1185 0.0754 0.1186 -0.0020 -0.0060 0.0063  123 TRP A C   
1055 O  O   . TRP A 123 ? 0.1140 0.0851 0.1455 0.0044  -0.0162 -0.0052 123 TRP A O   
1056 C  CB  . TRP A 123 ? 0.1299 0.1043 0.1194 -0.0121 -0.0028 0.0003  123 TRP A CB  
1057 C  CG  . TRP A 123 ? 0.1525 0.0920 0.1333 -0.0260 -0.0021 0.0151  123 TRP A CG  
1058 C  CD1 . TRP A 123 ? 0.1828 0.0991 0.1210 -0.0236 -0.0127 0.0097  123 TRP A CD1 
1059 C  CD2 . TRP A 123 ? 0.1819 0.0794 0.1287 -0.0216 -0.0057 0.0103  123 TRP A CD2 
1060 N  NE1 . TRP A 123 ? 0.2223 0.0855 0.1318 -0.0160 -0.0234 0.0078  123 TRP A NE1 
1061 C  CE2 . TRP A 123 ? 0.2264 0.0825 0.1341 -0.0126 -0.0085 0.0062  123 TRP A CE2 
1062 C  CE3 . TRP A 123 ? 0.1984 0.0697 0.1614 -0.0272 0.0119  0.0043  123 TRP A CE3 
1063 C  CZ2 . TRP A 123 ? 0.2648 0.0785 0.1547 -0.0226 -0.0088 0.0201  123 TRP A CZ2 
1064 C  CZ3 . TRP A 123 ? 0.2680 0.0866 0.1421 -0.0252 0.0198  0.0013  123 TRP A CZ3 
1065 C  CH2 . TRP A 123 ? 0.2639 0.0912 0.1800 -0.0052 0.0006  0.0104  123 TRP A CH2 
1066 N  N   . ASN A 124 ? 0.1217 0.0839 0.1326 0.0048  -0.0093 -0.0082 124 ASN A N   
1067 C  CA  . ASN A 124 ? 0.1252 0.0886 0.1283 0.0236  -0.0146 -0.0163 124 ASN A CA  
1068 C  C   . ASN A 124 ? 0.1262 0.0891 0.1334 0.0148  -0.0015 -0.0175 124 ASN A C   
1069 O  O   . ASN A 124 ? 0.1342 0.0936 0.1350 0.0068  0.0012  -0.0001 124 ASN A O   
1070 C  CB  . ASN A 124 ? 0.1537 0.0961 0.1264 0.0126  0.0085  -0.0115 124 ASN A CB  
1071 C  CG  . ASN A 124 ? 0.1571 0.0952 0.1447 0.0043  0.0192  -0.0096 124 ASN A CG  
1072 O  OD1 . ASN A 124 ? 0.1675 0.1097 0.1609 0.0291  0.0197  -0.0092 124 ASN A OD1 
1073 N  ND2 . ASN A 124 ? 0.2001 0.1061 0.1374 0.0060  0.0148  -0.0148 124 ASN A ND2 
1074 N  N   . THR A 125 ? 0.1280 0.0907 0.1723 0.0203  -0.0043 -0.0051 125 THR A N   
1075 C  CA  . THR A 125 ? 0.1546 0.1034 0.1934 0.0248  -0.0092 0.0175  125 THR A CA  
1076 C  C   . THR A 125 ? 0.1837 0.0956 0.2143 0.0372  0.0218  0.0142  125 THR A C   
1077 O  O   . THR A 125 ? 0.2064 0.1071 0.2322 0.0295  -0.0071 0.0261  125 THR A O   
1078 C  CB  . THR A 125 ? 0.1720 0.1305 0.2574 0.0291  -0.0210 0.0394  125 THR A CB  
1079 O  OG1 . THR A 125 ? 0.2215 0.1653 0.3648 0.0658  0.0665  0.0324  125 THR A OG1 
1080 C  CG2 . THR A 125 ? 0.2144 0.1589 0.2903 -0.0185 -0.0776 0.0214  125 THR A CG2 
1081 N  N   . LYS A 126 ? 0.1958 0.0835 0.1932 0.0091  0.0291  -0.0206 127 LYS A N   
1082 C  CA  . LYS A 126 ? 0.2395 0.1108 0.1974 -0.0051 0.0335  -0.0478 127 LYS A CA  
1083 C  C   . LYS A 126 ? 0.2104 0.0800 0.1729 0.0087  0.0109  -0.0185 127 LYS A C   
1084 O  O   . LYS A 126 ? 0.2442 0.1007 0.2133 -0.0138 0.0165  -0.0425 127 LYS A O   
1085 C  CB  . LYS A 126 ? 0.2504 0.1595 0.2125 -0.0066 0.0126  -0.0438 127 LYS A CB  
1086 C  CG  . LYS A 126 ? 0.2117 0.2055 0.2020 -0.0263 0.0030  -0.0353 127 LYS A CG  
1087 C  CD  . LYS A 126 ? 0.3346 0.3389 0.2322 -0.1251 0.0755  -0.1076 127 LYS A CD  
1088 C  CE  . LYS A 126 ? 0.2312 0.2695 0.5108 0.0043  -0.0010 -0.1115 127 LYS A CE  
1089 N  NZ  . LYS A 126 ? 0.3759 0.6861 0.6937 -0.2737 0.2730  -0.4478 127 LYS A NZ  
1090 N  N   . TYR A 127 ? 0.1833 0.0750 0.1594 0.0019  -0.0174 -0.0086 128 TYR A N   
1091 C  CA  . TYR A 127 ? 0.1675 0.0926 0.1500 -0.0043 -0.0248 -0.0098 128 TYR A CA  
1092 C  C   . TYR A 127 ? 0.1640 0.0794 0.1543 -0.0104 -0.0149 -0.0118 128 TYR A C   
1093 O  O   . TYR A 127 ? 0.1771 0.0983 0.1700 -0.0087 -0.0109 0.0000  128 TYR A O   
1094 C  CB  . TYR A 127 ? 0.1911 0.0935 0.1653 -0.0043 -0.0255 -0.0054 128 TYR A CB  
1095 C  CG  . TYR A 127 ? 0.1614 0.0896 0.1591 0.0074  -0.0309 -0.0082 128 TYR A CG  
1096 C  CD1 . TYR A 127 ? 0.1917 0.1027 0.1712 -0.0093 -0.0377 -0.0131 128 TYR A CD1 
1097 C  CD2 . TYR A 127 ? 0.1638 0.0957 0.1455 0.0021  -0.0026 -0.0044 128 TYR A CD2 
1098 C  CE1 . TYR A 127 ? 0.2298 0.1113 0.1592 0.0116  -0.0333 -0.0199 128 TYR A CE1 
1099 C  CE2 . TYR A 127 ? 0.1503 0.1125 0.1523 0.0006  0.0015  -0.0299 128 TYR A CE2 
1100 C  CZ  . TYR A 127 ? 0.2054 0.1212 0.1542 0.0291  -0.0089 -0.0226 128 TYR A CZ  
1101 O  OH  . TYR A 127 ? 0.2473 0.1388 0.1473 0.0275  -0.0269 -0.0324 128 TYR A OH  
1102 N  N   . GLY A 128 ? 0.1578 0.0913 0.1647 -0.0060 -0.0126 0.0093  129 GLY A N   
1103 C  CA  . GLY A 128 ? 0.1960 0.1023 0.1702 -0.0138 -0.0137 0.0220  129 GLY A CA  
1104 C  C   . GLY A 128 ? 0.1960 0.0962 0.1448 0.0019  -0.0233 0.0237  129 GLY A C   
1105 O  O   . GLY A 128 ? 0.2656 0.1039 0.1570 0.0000  -0.0403 0.0199  129 GLY A O   
1106 N  N   . ASP A 129 ? 0.2233 0.1061 0.1360 0.0120  -0.0187 -0.0020 130 ASP A N   
1107 C  CA  . ASP A 129 ? 0.2693 0.1102 0.1437 0.0120  -0.0161 0.0108  130 ASP A CA  
1108 C  C   . ASP A 129 ? 0.2352 0.1071 0.1278 0.0012  -0.0368 0.0066  130 ASP A C   
1109 O  O   . ASP A 129 ? 0.2714 0.1110 0.1250 0.0105  -0.0205 -0.0080 130 ASP A O   
1110 C  CB  . ASP A 129 ? 0.2552 0.1629 0.1908 0.0120  0.0377  0.0167  130 ASP A CB  
1111 C  CG  . ASP A 129 ? 0.2885 0.1243 0.1615 0.0505  0.0307  0.0414  130 ASP A CG  
1112 O  OD1 . ASP A 129 ? 0.3181 0.1787 0.2556 -0.0551 -0.0529 0.0209  130 ASP A OD1 
1113 O  OD2 . ASP A 129 ? 0.3093 0.1620 0.2646 0.0066  0.0795  0.0317  130 ASP A OD2 
1114 N  N   . PHE A 130 ? 0.2433 0.0979 0.1199 -0.0109 -0.0041 0.0015  131 PHE A N   
1115 C  CA  . PHE A 130 ? 0.1902 0.1027 0.1244 -0.0052 -0.0077 0.0006  131 PHE A CA  
1116 C  C   . PHE A 130 ? 0.2037 0.0854 0.1224 -0.0088 0.0305  0.0006  131 PHE A C   
1117 O  O   . PHE A 130 ? 0.1835 0.1067 0.1190 -0.0178 0.0074  0.0035  131 PHE A O   
1118 C  CB  . PHE A 130 ? 0.2096 0.1005 0.1386 -0.0017 -0.0132 -0.0100 131 PHE A CB  
1119 C  CG  . PHE A 130 ? 0.1809 0.1059 0.1168 -0.0118 0.0100  -0.0198 131 PHE A CG  
1120 C  CD1 . PHE A 130 ? 0.1906 0.1189 0.1149 -0.0271 0.0015  -0.0046 131 PHE A CD1 
1121 C  CD2 . PHE A 130 ? 0.2207 0.1146 0.1508 -0.0302 0.0146  -0.0274 131 PHE A CD2 
1122 C  CE1 . PHE A 130 ? 0.2307 0.1066 0.1333 -0.0322 -0.0007 -0.0094 131 PHE A CE1 
1123 C  CE2 . PHE A 130 ? 0.2149 0.1598 0.1771 -0.0066 -0.0060 -0.0152 131 PHE A CE2 
1124 C  CZ  . PHE A 130 ? 0.2406 0.1502 0.1259 -0.0080 -0.0068 -0.0152 131 PHE A CZ  
1125 N  N   . GLY A 131 ? 0.2169 0.1240 0.1527 -0.0305 0.0529  0.0013  132 GLY A N   
1126 C  CA  . GLY A 131 ? 0.2325 0.1448 0.1595 -0.0368 0.0658  0.0073  132 GLY A CA  
1127 C  C   . GLY A 131 ? 0.1747 0.1632 0.1682 -0.0383 0.0386  0.0135  132 GLY A C   
1128 O  O   . GLY A 131 ? 0.1984 0.1281 0.2380 -0.0284 0.0252  -0.0148 132 GLY A O   
1129 N  N   . LYS A 132 ? 0.1774 0.1164 0.1777 -0.0406 0.0264  -0.0071 133 LYS A N   
1130 C  CA  . LYS A 132 ? 0.1886 0.0860 0.1868 -0.0157 0.0062  0.0132  133 LYS A CA  
1131 C  C   . LYS A 132 ? 0.1790 0.1025 0.1532 -0.0397 0.0076  -0.0121 133 LYS A C   
1132 O  O   . LYS A 132 ? 0.1630 0.1210 0.1498 -0.0328 -0.0087 -0.0175 133 LYS A O   
1133 C  CB  . LYS A 132 ? 0.1710 0.1142 0.1918 -0.0184 -0.0017 -0.0070 133 LYS A CB  
1134 C  CG  . LYS A 132 ? 0.2090 0.1308 0.3037 -0.0255 -0.0324 0.0408  133 LYS A CG  
1135 C  CD  . LYS A 132 ? 0.2558 0.1693 0.6621 -0.0425 -0.1001 0.1446  133 LYS A CD  
1136 C  CE  . LYS A 132 ? 0.2442 0.2290 0.7049 -0.0487 0.0182  0.1248  133 LYS A CE  
1137 N  NZ  . LYS A 132 ? 0.5052 0.4149 0.7896 -0.3107 -0.0760 0.1887  133 LYS A NZ  
1138 N  N   . ALA A 133 ? 0.1650 0.0970 0.1379 -0.0403 0.0028  -0.0051 134 ALA A N   
1139 C  CA  . ALA A 133 ? 0.1386 0.1244 0.1131 -0.0234 -0.0006 -0.0087 134 ALA A CA  
1140 C  C   . ALA A 133 ? 0.1352 0.1122 0.1027 -0.0388 -0.0024 0.0003  134 ALA A C   
1141 O  O   . ALA A 133 ? 0.1260 0.1386 0.1158 -0.0186 -0.0068 0.0001  134 ALA A O   
1142 C  CB  . ALA A 133 ? 0.1454 0.1095 0.1217 -0.0324 -0.0157 0.0046  134 ALA A CB  
1143 N  N   . VAL A 134 ? 0.1462 0.1088 0.1208 -0.0274 0.0141  -0.0054 135 VAL A N   
1144 C  CA  . VAL A 134 ? 0.1495 0.1058 0.1318 -0.0166 0.0087  0.0088  135 VAL A CA  
1145 C  C   . VAL A 134 ? 0.1262 0.1255 0.1240 -0.0102 0.0193  -0.0059 135 VAL A C   
1146 O  O   . VAL A 134 ? 0.1451 0.1289 0.1407 -0.0137 0.0063  -0.0040 135 VAL A O   
1147 C  CB  . VAL A 134 ? 0.1665 0.1265 0.1386 -0.0171 0.0155  -0.0208 135 VAL A CB  
1148 C  CG1 . VAL A 134 ? 0.2141 0.1591 0.1378 -0.0244 0.0087  -0.0195 135 VAL A CG1 
1149 C  CG2 . VAL A 134 ? 0.1960 0.1419 0.1450 -0.0189 0.0351  -0.0121 135 VAL A CG2 
1150 N  N   A GLN A 135 ? 0.1541 0.1208 0.1509 -0.0335 0.0222  -0.0167 136 GLN A N   
1151 N  N   B GLN A 135 ? 0.1553 0.1181 0.1430 -0.0305 0.0098  -0.0194 136 GLN A N   
1152 C  CA  A GLN A 135 ? 0.1447 0.1416 0.1724 -0.0296 -0.0097 -0.0119 136 GLN A CA  
1153 C  CA  B GLN A 135 ? 0.1503 0.1348 0.1581 -0.0412 -0.0087 -0.0285 136 GLN A CA  
1154 C  C   A GLN A 135 ? 0.1432 0.0974 0.1490 -0.0166 -0.0295 0.0035  136 GLN A C   
1155 C  C   B GLN A 135 ? 0.1509 0.1217 0.1626 -0.0147 -0.0049 -0.0173 136 GLN A C   
1156 O  O   A GLN A 135 ? 0.1502 0.1269 0.1565 -0.0359 -0.0355 -0.0099 136 GLN A O   
1157 O  O   B GLN A 135 ? 0.1457 0.1471 0.2143 -0.0144 -0.0471 0.0010  136 GLN A O   
1158 C  CB  A GLN A 135 ? 0.1827 0.1622 0.2134 -0.0560 0.0098  -0.0076 136 GLN A CB  
1159 C  CB  B GLN A 135 ? 0.1622 0.1582 0.1906 -0.0564 -0.0019 -0.0107 136 GLN A CB  
1160 C  CG  A GLN A 135 ? 0.2297 0.1773 0.2578 -0.0679 0.0838  0.0571  136 GLN A CG  
1161 C  CG  B GLN A 135 ? 0.2079 0.1837 0.1729 -0.0566 -0.0234 0.0077  136 GLN A CG  
1162 C  CD  A GLN A 135 ? 0.2021 0.3438 0.4056 -0.0366 -0.0657 0.0483  136 GLN A CD  
1163 C  CD  B GLN A 135 ? 0.1465 0.2340 0.2252 -0.0653 0.0197  0.0262  136 GLN A CD  
1164 O  OE1 A GLN A 135 ? 0.1951 0.4212 0.3804 0.0109  -0.0197 -0.0724 136 GLN A OE1 
1165 O  OE1 B GLN A 135 ? 0.2204 0.1837 0.2605 -0.0313 0.0259  0.0493  136 GLN A OE1 
1166 N  NE2 A GLN A 135 ? 0.3159 0.3022 0.4279 -0.1736 0.0461  0.0212  136 GLN A NE2 
1167 N  NE2 B GLN A 135 ? 0.2492 0.2006 0.2882 -0.1071 -0.0217 0.0494  136 GLN A NE2 
1168 N  N   . GLN A 136 ? 0.1368 0.1306 0.1299 -0.0114 -0.0020 -0.0229 137 GLN A N   
1169 C  CA  . GLN A 136 ? 0.1503 0.1171 0.1088 -0.0012 -0.0167 -0.0148 137 GLN A CA  
1170 C  C   . GLN A 136 ? 0.1261 0.1244 0.1113 0.0046  -0.0171 -0.0251 137 GLN A C   
1171 O  O   . GLN A 136 ? 0.1721 0.1183 0.0984 0.0000  -0.0074 -0.0188 137 GLN A O   
1172 C  CB  . GLN A 136 ? 0.1695 0.1110 0.1504 0.0081  -0.0133 -0.0116 137 GLN A CB  
1173 C  CG  . GLN A 136 ? 0.2718 0.1600 0.1492 0.0586  0.0244  0.0027  137 GLN A CG  
1174 C  CD  . GLN A 136 ? 0.2333 0.1554 0.3694 0.0065  0.0526  0.0511  137 GLN A CD  
1175 O  OE1 . GLN A 136 ? 0.3041 0.1474 0.3396 -0.0087 0.0054  -0.0813 137 GLN A OE1 
1176 N  NE2 . GLN A 136 ? 0.3161 0.2863 0.6876 -0.0237 0.0362  0.2320  137 GLN A NE2 
1177 N  N   A PRO A 137 ? 0.1284 0.1377 0.1077 -0.0057 -0.0162 -0.0274 138 PRO A N   
1178 N  N   B PRO A 137 ? 0.1387 0.1466 0.1146 0.0000  -0.0131 -0.0219 138 PRO A N   
1179 C  CA  A PRO A 137 ? 0.1387 0.1614 0.0975 0.0186  -0.0138 0.0098  138 PRO A CA  
1180 C  CA  B PRO A 137 ? 0.1458 0.1655 0.1025 0.0227  -0.0162 0.0132  138 PRO A CA  
1181 C  C   A PRO A 137 ? 0.1588 0.1475 0.0979 0.0208  -0.0186 0.0054  138 PRO A C   
1182 C  C   B PRO A 137 ? 0.1629 0.1490 0.0992 0.0237  -0.0179 0.0076  138 PRO A C   
1183 O  O   A PRO A 137 ? 0.1982 0.1447 0.2022 0.0170  -0.0054 0.0377  138 PRO A O   
1184 O  O   B PRO A 137 ? 0.2029 0.1469 0.2044 0.0193  0.0013  0.0366  138 PRO A O   
1185 C  CB  A PRO A 137 ? 0.2091 0.2308 0.1108 0.0165  -0.0270 0.0038  138 PRO A CB  
1186 C  CB  B PRO A 137 ? 0.2269 0.2247 0.1160 0.0258  -0.0230 -0.0027 138 PRO A CB  
1187 C  CG  A PRO A 137 ? 0.3122 0.2702 0.0688 -0.0211 -0.0758 -0.0494 138 PRO A CG  
1188 C  CG  B PRO A 137 ? 0.3241 0.3355 0.1573 -0.0694 -0.0524 -0.0043 138 PRO A CG  
1189 C  CD  A PRO A 137 ? 0.1383 0.2124 0.1037 -0.0577 -0.0410 -0.0377 138 PRO A CD  
1190 C  CD  B PRO A 137 ? 0.2248 0.2119 0.1298 -0.0372 -0.0174 -0.0406 138 PRO A CD  
1191 N  N   . ASP A 138 ? 0.1315 0.1494 0.1041 0.0051  -0.0111 -0.0151 139 ASP A N   
1192 C  CA  . ASP A 138 ? 0.1456 0.1305 0.1138 0.0043  0.0003  -0.0083 139 ASP A CA  
1193 C  C   . ASP A 138 ? 0.1295 0.1050 0.1216 -0.0010 -0.0003 -0.0048 139 ASP A C   
1194 O  O   . ASP A 138 ? 0.1404 0.1128 0.1327 0.0052  0.0114  -0.0152 139 ASP A O   
1195 C  CB  . ASP A 138 ? 0.1773 0.1635 0.1301 0.0289  0.0164  -0.0152 139 ASP A CB  
1196 C  CG  . ASP A 138 ? 0.1724 0.1967 0.1286 0.0267  0.0186  -0.0456 139 ASP A CG  
1197 O  OD1 . ASP A 138 ? 0.2124 0.1330 0.1556 0.0203  -0.0031 -0.0458 139 ASP A OD1 
1198 O  OD2 . ASP A 138 ? 0.2219 0.2097 0.1932 0.0307  0.0201  -0.0662 139 ASP A OD2 
1199 N  N   . GLY A 139 ? 0.1307 0.0970 0.0966 -0.0043 -0.0003 -0.0141 140 GLY A N   
1200 C  CA  . GLY A 139 ? 0.1351 0.0954 0.1014 -0.0119 -0.0048 -0.0040 140 GLY A CA  
1201 C  C   . GLY A 139 ? 0.1093 0.0852 0.0940 -0.0015 -0.0043 -0.0043 140 GLY A C   
1202 O  O   . GLY A 139 ? 0.1256 0.0844 0.1099 0.0060  -0.0087 0.0024  140 GLY A O   
1203 N  N   . LEU A 140 ? 0.1023 0.0744 0.1062 0.0041  -0.0099 -0.0038 141 LEU A N   
1204 C  CA  . LEU A 140 ? 0.0970 0.0803 0.1037 -0.0017 -0.0115 -0.0055 141 LEU A CA  
1205 C  C   . LEU A 140 ? 0.0879 0.0873 0.0971 0.0035  -0.0044 -0.0077 141 LEU A C   
1206 O  O   . LEU A 140 ? 0.1049 0.0829 0.0996 -0.0017 -0.0109 -0.0015 141 LEU A O   
1207 C  CB  . LEU A 140 ? 0.1122 0.0883 0.1019 0.0048  0.0074  -0.0082 141 LEU A CB  
1208 C  CG  . LEU A 140 ? 0.1217 0.1095 0.1381 0.0230  0.0172  0.0153  141 LEU A CG  
1209 C  CD1 . LEU A 140 ? 0.1115 0.1259 0.1376 0.0187  0.0190  0.0026  141 LEU A CD1 
1210 C  CD2 . LEU A 140 ? 0.1697 0.1031 0.1477 0.0231  0.0175  0.0153  141 LEU A CD2 
1211 N  N   . ALA A 141 ? 0.0903 0.0741 0.1180 -0.0017 -0.0074 0.0015  142 ALA A N   
1212 C  CA  . ALA A 141 ? 0.1027 0.0725 0.1190 -0.0066 -0.0021 0.0052  142 ALA A CA  
1213 C  C   . ALA A 141 ? 0.0948 0.0751 0.0974 -0.0126 -0.0126 0.0135  142 ALA A C   
1214 O  O   . ALA A 141 ? 0.1185 0.0865 0.1118 -0.0024 -0.0206 0.0131  142 ALA A O   
1215 C  CB  . ALA A 141 ? 0.1067 0.1086 0.1328 -0.0143 0.0068  -0.0049 142 ALA A CB  
1216 N  N   . VAL A 142 ? 0.0905 0.0675 0.1052 -0.0027 -0.0093 0.0043  143 VAL A N   
1217 C  CA  . VAL A 142 ? 0.1016 0.0727 0.0913 -0.0063 -0.0127 0.0060  143 VAL A CA  
1218 C  C   . VAL A 142 ? 0.0868 0.0829 0.0842 0.0054  -0.0027 -0.0031 143 VAL A C   
1219 O  O   . VAL A 142 ? 0.1004 0.0914 0.0876 -0.0060 -0.0078 0.0057  143 VAL A O   
1220 C  CB  . VAL A 142 ? 0.0905 0.0978 0.0930 0.0049  -0.0065 0.0035  143 VAL A CB  
1221 C  CG1 . VAL A 142 ? 0.1163 0.1055 0.1062 0.0082  -0.0027 -0.0020 143 VAL A CG1 
1222 C  CG2 . VAL A 142 ? 0.1014 0.1325 0.1036 -0.0138 -0.0107 0.0116  143 VAL A CG2 
1223 N  N   . LEU A 143 ? 0.0913 0.0768 0.1004 -0.0054 -0.0144 0.0049  144 LEU A N   
1224 C  CA  . LEU A 143 ? 0.0769 0.0895 0.1192 -0.0086 -0.0174 0.0012  144 LEU A CA  
1225 C  C   . LEU A 143 ? 0.0913 0.0966 0.0939 -0.0163 -0.0137 0.0083  144 LEU A C   
1226 O  O   . LEU A 143 ? 0.1317 0.0917 0.1023 -0.0070 -0.0063 0.0103  144 LEU A O   
1227 C  CB  . LEU A 143 ? 0.1147 0.1172 0.1342 -0.0099 -0.0167 0.0163  144 LEU A CB  
1228 C  CG  . LEU A 143 ? 0.1133 0.1337 0.1783 -0.0059 -0.0162 0.0154  144 LEU A CG  
1229 C  CD1 . LEU A 143 ? 0.1330 0.1923 0.1888 -0.0359 -0.0208 0.0340  144 LEU A CD1 
1230 C  CD2 . LEU A 143 ? 0.1108 0.1680 0.1993 -0.0013 -0.0212 0.0164  144 LEU A CD2 
1231 N  N   . GLY A 144 ? 0.0971 0.0798 0.0954 -0.0091 -0.0065 0.0107  145 GLY A N   
1232 C  CA  . GLY A 144 ? 0.0940 0.0855 0.1092 -0.0074 -0.0132 -0.0031 145 GLY A CA  
1233 C  C   . GLY A 144 ? 0.0900 0.0835 0.0914 -0.0054 -0.0151 0.0093  145 GLY A C   
1234 O  O   . GLY A 144 ? 0.1119 0.1013 0.1009 -0.0164 0.0023  -0.0046 145 GLY A O   
1235 N  N   . ILE A 145 ? 0.0895 0.0785 0.0929 -0.0077 -0.0161 -0.0015 146 ILE A N   
1236 C  CA  . ILE A 145 ? 0.0825 0.0837 0.1097 -0.0089 -0.0184 0.0076  146 ILE A CA  
1237 C  C   . ILE A 145 ? 0.0952 0.0766 0.0983 -0.0055 -0.0229 0.0028  146 ILE A C   
1238 O  O   . ILE A 145 ? 0.1151 0.0759 0.1165 -0.0141 0.0003  0.0057  146 ILE A O   
1239 C  CB  . ILE A 145 ? 0.1062 0.1018 0.1288 -0.0038 -0.0271 0.0153  146 ILE A CB  
1240 C  CG1 . ILE A 145 ? 0.1295 0.1167 0.1475 0.0214  -0.0447 -0.0068 146 ILE A CG1 
1241 C  CG2 . ILE A 145 ? 0.1068 0.1133 0.1941 -0.0227 -0.0478 0.0115  146 ILE A CG2 
1242 C  CD1 . ILE A 145 ? 0.1122 0.1104 0.1736 0.0105  -0.0351 0.0161  146 ILE A CD1 
1243 N  N   . PHE A 146 ? 0.0997 0.0776 0.0942 -0.0027 -0.0116 0.0082  147 PHE A N   
1244 C  CA  . PHE A 146 ? 0.1125 0.0775 0.1005 0.0023  -0.0254 0.0073  147 PHE A CA  
1245 C  C   . PHE A 146 ? 0.0992 0.0815 0.1061 -0.0120 -0.0105 0.0015  147 PHE A C   
1246 O  O   . PHE A 146 ? 0.1020 0.1027 0.1255 -0.0040 -0.0233 -0.0054 147 PHE A O   
1247 C  CB  . PHE A 146 ? 0.1013 0.0829 0.1133 -0.0142 -0.0131 0.0035  147 PHE A CB  
1248 C  CG  . PHE A 146 ? 0.1066 0.0737 0.0944 -0.0024 -0.0120 0.0109  147 PHE A CG  
1249 C  CD1 . PHE A 146 ? 0.1025 0.0829 0.1102 0.0017  -0.0151 0.0034  147 PHE A CD1 
1250 C  CD2 . PHE A 146 ? 0.1158 0.0782 0.1108 -0.0086 -0.0127 0.0167  147 PHE A CD2 
1251 C  CE1 . PHE A 146 ? 0.1240 0.0934 0.1163 -0.0098 -0.0193 0.0086  147 PHE A CE1 
1252 C  CE2 . PHE A 146 ? 0.1090 0.0927 0.1171 -0.0096 -0.0133 0.0076  147 PHE A CE2 
1253 C  CZ  . PHE A 146 ? 0.1070 0.0923 0.1110 -0.0094 -0.0137 0.0127  147 PHE A CZ  
1254 N  N   . LEU A 147 ? 0.1172 0.0775 0.1128 -0.0098 -0.0124 -0.0026 148 LEU A N   
1255 C  CA  . LEU A 147 ? 0.1324 0.0810 0.1097 -0.0119 -0.0223 -0.0089 148 LEU A CA  
1256 C  C   . LEU A 147 ? 0.1072 0.0932 0.1101 -0.0094 -0.0194 0.0041  148 LEU A C   
1257 O  O   . LEU A 147 ? 0.1292 0.0819 0.1264 -0.0055 -0.0118 -0.0020 148 LEU A O   
1258 C  CB  . LEU A 147 ? 0.1620 0.0918 0.1031 -0.0082 -0.0154 -0.0032 148 LEU A CB  
1259 C  CG  . LEU A 147 ? 0.1764 0.0759 0.1216 -0.0160 -0.0417 -0.0054 148 LEU A CG  
1260 C  CD1 . LEU A 147 ? 0.2021 0.0907 0.1314 -0.0165 -0.0419 -0.0020 148 LEU A CD1 
1261 C  CD2 . LEU A 147 ? 0.1823 0.1163 0.1237 -0.0197 -0.0443 0.0065  148 LEU A CD2 
1262 N  N   . LYS A 148 ? 0.1312 0.0799 0.1527 -0.0135 -0.0329 -0.0028 149 LYS A N   
1263 C  CA  . LYS A 148 ? 0.1483 0.0812 0.1506 -0.0038 -0.0193 -0.0005 149 LYS A CA  
1264 C  C   . LYS A 148 ? 0.1466 0.0988 0.1669 -0.0182 -0.0344 -0.0027 149 LYS A C   
1265 O  O   . LYS A 148 ? 0.1735 0.1189 0.1506 0.0194  -0.0436 -0.0137 149 LYS A O   
1266 C  CB  . LYS A 148 ? 0.1660 0.1212 0.1552 -0.0303 -0.0236 0.0167  149 LYS A CB  
1267 C  CG  . LYS A 148 ? 0.1720 0.1456 0.1867 -0.0368 0.0015  0.0210  149 LYS A CG  
1268 C  CD  . LYS A 148 ? 0.2552 0.2542 0.2804 -0.0570 0.0098  0.0762  149 LYS A CD  
1269 C  CE  . LYS A 148 ? 0.2615 0.4280 0.4004 -0.0710 0.0904  0.0648  149 LYS A CE  
1270 N  NZ  . LYS A 148 ? 0.3909 0.5924 0.5131 -0.2172 0.0645  0.1547  149 LYS A NZ  
1271 N  N   . VAL A 149 ? 0.1655 0.0935 0.1689 -0.0055 -0.0209 -0.0168 150 VAL A N   
1272 C  CA  . VAL A 149 ? 0.1543 0.1058 0.1656 -0.0156 -0.0200 -0.0408 150 VAL A CA  
1273 C  C   . VAL A 149 ? 0.1745 0.1041 0.1696 -0.0184 -0.0263 -0.0006 150 VAL A C   
1274 O  O   . VAL A 149 ? 0.1880 0.1216 0.1852 -0.0179 -0.0370 0.0063  150 VAL A O   
1275 C  CB  . VAL A 149 ? 0.1528 0.1134 0.1843 -0.0052 -0.0262 -0.0185 150 VAL A CB  
1276 C  CG1 . VAL A 149 ? 0.1841 0.1475 0.1792 -0.0121 -0.0173 -0.0445 150 VAL A CG1 
1277 C  CG2 . VAL A 149 ? 0.1668 0.1556 0.2048 -0.0114 -0.0151 -0.0038 150 VAL A CG2 
1278 N  N   . GLY A 150 ? 0.1650 0.1129 0.1803 -0.0291 -0.0397 -0.0103 151 GLY A N   
1279 C  CA  . GLY A 150 ? 0.1604 0.1713 0.1733 -0.0278 -0.0265 0.0076  151 GLY A CA  
1280 C  C   . GLY A 150 ? 0.1886 0.1435 0.1835 -0.0582 -0.0417 0.0024  151 GLY A C   
1281 O  O   . GLY A 150 ? 0.2076 0.1345 0.1981 -0.0362 -0.0282 -0.0193 151 GLY A O   
1282 N  N   A SER A 151 ? 0.1762 0.1453 0.2104 -0.0516 -0.0621 0.0052  152 SER A N   
1283 N  N   B SER A 151 ? 0.1895 0.1589 0.2395 -0.0441 -0.0564 -0.0010 152 SER A N   
1284 C  CA  A SER A 151 ? 0.2016 0.1591 0.2459 -0.0109 -0.0754 0.0315  152 SER A CA  
1285 C  CA  B SER A 151 ? 0.1838 0.1328 0.2462 -0.0513 -0.0873 -0.0283 152 SER A CA  
1286 C  C   A SER A 151 ? 0.1687 0.1244 0.1876 -0.0228 -0.0276 -0.0471 152 SER A C   
1287 C  C   B SER A 151 ? 0.2239 0.1118 0.2198 -0.0179 -0.0926 -0.0109 152 SER A C   
1288 O  O   A SER A 151 ? 0.1400 0.1213 0.1814 -0.0249 -0.0120 -0.0450 152 SER A O   
1289 O  O   B SER A 151 ? 0.1485 0.1368 0.1498 -0.0203 -0.0233 -0.0144 152 SER A O   
1290 C  CB  A SER A 151 ? 0.1455 0.2189 0.3253 0.0104  -0.0982 0.0428  152 SER A CB  
1291 C  CB  B SER A 151 ? 0.2388 0.2046 0.3503 -0.0804 0.0261  -0.0342 152 SER A CB  
1292 O  OG  A SER A 151 ? 0.2058 0.3058 0.3115 -0.0102 0.0051  0.0342  152 SER A OG  
1293 O  OG  B SER A 151 ? 0.1677 0.2606 0.4079 -0.0447 -0.0340 0.1071  152 SER A OG  
1294 N  N   . ALA A 152 ? 0.2390 0.1334 0.1976 -0.0174 -0.0777 -0.0142 153 ALA A N   
1295 C  CA  . ALA A 152 ? 0.2245 0.1391 0.1677 -0.0080 -0.0480 -0.0089 153 ALA A CA  
1296 C  C   . ALA A 152 ? 0.1925 0.1318 0.1606 0.0026  -0.0513 -0.0175 153 ALA A C   
1297 O  O   . ALA A 152 ? 0.2041 0.1542 0.2268 0.0034  -0.0428 -0.0207 153 ALA A O   
1298 C  CB  . ALA A 152 ? 0.3048 0.1604 0.1815 0.0054  -0.0697 -0.0153 153 ALA A CB  
1299 N  N   . LYS A 153 ? 0.2110 0.1343 0.1918 0.0006  -0.0702 -0.0020 154 LYS A N   
1300 C  CA  . LYS A 153 ? 0.2484 0.1251 0.1776 0.0107  -0.0498 -0.0071 154 LYS A CA  
1301 C  C   . LYS A 153 ? 0.1956 0.1342 0.1852 0.0015  -0.0531 -0.0013 154 LYS A C   
1302 O  O   . LYS A 153 ? 0.1825 0.1497 0.1719 -0.0087 -0.0632 -0.0052 154 LYS A O   
1303 C  CB  . LYS A 153 ? 0.2265 0.1318 0.2099 -0.0211 -0.0715 0.0096  154 LYS A CB  
1304 C  CG  . LYS A 153 ? 0.2930 0.1324 0.2666 -0.0054 -0.1142 -0.0270 154 LYS A CG  
1305 C  CD  . LYS A 153 ? 0.4101 0.1569 0.2250 0.0013  -0.1059 -0.0190 154 LYS A CD  
1306 C  CE  . LYS A 153 ? 0.3909 0.1659 0.2492 0.0133  -0.1041 -0.0225 154 LYS A CE  
1307 N  NZ  . LYS A 153 ? 0.2825 0.2169 0.2939 0.0074  -0.0579 -0.0856 154 LYS A NZ  
1308 N  N   . PRO A 154 ? 0.2083 0.1635 0.1950 -0.0046 -0.0802 -0.0001 155 PRO A N   
1309 C  CA  . PRO A 154 ? 0.1934 0.1697 0.2236 -0.0035 -0.0876 -0.0003 155 PRO A CA  
1310 C  C   . PRO A 154 ? 0.2297 0.1777 0.1821 -0.0096 -0.1017 0.0086  155 PRO A C   
1311 O  O   . PRO A 154 ? 0.2427 0.1909 0.1958 -0.0114 -0.1058 0.0060  155 PRO A O   
1312 C  CB  . PRO A 154 ? 0.1868 0.1764 0.2912 -0.0017 -0.0705 -0.0020 155 PRO A CB  
1313 C  CG  . PRO A 154 ? 0.2677 0.2028 0.3019 -0.0038 -0.0892 0.0034  155 PRO A CG  
1314 C  CD  . PRO A 154 ? 0.2087 0.1930 0.2477 -0.0107 -0.0280 0.0181  155 PRO A CD  
1315 N  N   . GLY A 155 ? 0.2172 0.1442 0.2158 0.0121  -0.0852 -0.0023 156 GLY A N   
1316 C  CA  . GLY A 155 ? 0.2354 0.1448 0.2206 -0.0154 -0.0386 -0.0031 156 GLY A CA  
1317 C  C   . GLY A 155 ? 0.2415 0.1384 0.1959 -0.0113 -0.0454 0.0161  156 GLY A C   
1318 O  O   . GLY A 155 ? 0.2446 0.1466 0.3129 -0.0071 -0.0646 0.0303  156 GLY A O   
1319 N  N   . LEU A 156 ? 0.1720 0.1612 0.2101 -0.0087 -0.0615 -0.0188 157 LEU A N   
1320 C  CA  . LEU A 156 ? 0.2492 0.1097 0.1469 -0.0136 -0.0725 -0.0138 157 LEU A CA  
1321 C  C   . LEU A 156 ? 0.2193 0.1252 0.1753 -0.0181 -0.0696 -0.0109 157 LEU A C   
1322 O  O   . LEU A 156 ? 0.2120 0.1365 0.1578 -0.0126 -0.0648 -0.0107 157 LEU A O   
1323 C  CB  . LEU A 156 ? 0.1903 0.1370 0.1710 -0.0322 -0.0729 -0.0027 157 LEU A CB  
1324 C  CG  . LEU A 156 ? 0.1982 0.1599 0.1418 -0.0193 -0.0478 0.0031  157 LEU A CG  
1325 C  CD1 . LEU A 156 ? 0.2398 0.1806 0.1729 -0.0597 -0.0820 -0.0052 157 LEU A CD1 
1326 C  CD2 . LEU A 156 ? 0.2032 0.1776 0.1871 -0.0031 -0.0696 -0.0034 157 LEU A CD2 
1327 N  N   . GLN A 157 ? 0.2301 0.1340 0.1660 -0.0227 -0.0778 0.0008  158 GLN A N   
1328 C  CA  . GLN A 157 ? 0.3045 0.1530 0.1412 -0.0548 -0.0895 -0.0222 158 GLN A CA  
1329 C  C   . GLN A 157 ? 0.2529 0.1583 0.1490 -0.0562 -0.0909 -0.0147 158 GLN A C   
1330 O  O   . GLN A 157 ? 0.2290 0.1581 0.1718 -0.0126 -0.0772 -0.0157 158 GLN A O   
1331 C  CB  . GLN A 157 ? 0.2928 0.1816 0.1976 -0.0709 -0.0760 -0.0198 158 GLN A CB  
1332 C  CG  . GLN A 157 ? 0.3212 0.1615 0.1810 -0.0201 -0.0922 -0.0318 158 GLN A CG  
1333 C  CD  . GLN A 157 ? 0.3066 0.1510 0.1685 -0.0688 -0.0707 -0.0100 158 GLN A CD  
1334 O  OE1 . GLN A 157 ? 0.3407 0.1513 0.1648 -0.0196 -0.0719 -0.0119 158 GLN A OE1 
1335 N  NE2 . GLN A 157 ? 0.3277 0.2113 0.1809 -0.0662 -0.0696 -0.0361 158 GLN A NE2 
1336 N  N   . LYS A 158 ? 0.2731 0.1546 0.1738 -0.0278 -0.1085 -0.0051 159 LYS A N   
1337 C  CA  . LYS A 158 ? 0.2558 0.1525 0.1720 -0.0288 -0.0807 0.0017  159 LYS A CA  
1338 C  C   . LYS A 158 ? 0.2499 0.1590 0.1405 0.0041  -0.0744 -0.0096 159 LYS A C   
1339 O  O   . LYS A 158 ? 0.2829 0.2014 0.1504 -0.0485 -0.0744 0.0085  159 LYS A O   
1340 C  CB  . LYS A 158 ? 0.3062 0.1587 0.1850 -0.0076 -0.0790 0.0129  159 LYS A CB  
1341 C  CG  . LYS A 158 ? 0.3661 0.3066 0.2431 0.0292  -0.0846 0.0601  159 LYS A CG  
1342 C  CD  . LYS A 158 ? 0.5741 0.3749 0.4560 0.1118  -0.1995 -0.0154 159 LYS A CD  
1343 C  CE  . LYS A 158 ? 0.9756 0.4645 0.4311 0.1726  -0.4239 -0.0494 159 LYS A CE  
1344 N  NZ  . LYS A 158 ? 0.7874 0.3274 0.3594 -0.0454 -0.2709 0.0766  159 LYS A NZ  
1345 N  N   . VAL A 159 ? 0.2614 0.1480 0.1500 -0.0204 -0.0910 -0.0074 160 VAL A N   
1346 C  CA  . VAL A 159 ? 0.2566 0.1363 0.1556 -0.0122 -0.0693 -0.0054 160 VAL A CA  
1347 C  C   . VAL A 159 ? 0.2492 0.1479 0.1433 -0.0210 -0.0588 -0.0027 160 VAL A C   
1348 O  O   . VAL A 159 ? 0.2554 0.1591 0.1641 -0.0195 -0.0680 -0.0071 160 VAL A O   
1349 C  CB  . VAL A 159 ? 0.2458 0.1597 0.1386 -0.0366 -0.0694 -0.0181 160 VAL A CB  
1350 C  CG1 . VAL A 159 ? 0.2580 0.2090 0.1758 -0.0456 -0.0590 -0.0020 160 VAL A CG1 
1351 C  CG2 . VAL A 159 ? 0.3052 0.1833 0.1693 0.0127  -0.0874 -0.0403 160 VAL A CG2 
1352 N  N   . VAL A 160 ? 0.2674 0.1430 0.1365 -0.0271 -0.0608 -0.0177 161 VAL A N   
1353 C  CA  . VAL A 160 ? 0.2383 0.1666 0.1527 -0.0010 -0.0452 -0.0060 161 VAL A CA  
1354 C  C   . VAL A 160 ? 0.3098 0.1322 0.1661 0.0035  -0.0432 -0.0359 161 VAL A C   
1355 O  O   . VAL A 160 ? 0.2833 0.1675 0.1676 -0.0289 -0.0368 -0.0265 161 VAL A O   
1356 C  CB  . VAL A 160 ? 0.2944 0.1740 0.1652 0.0087  -0.0143 -0.0098 161 VAL A CB  
1357 C  CG1 . VAL A 160 ? 0.3287 0.1974 0.2489 -0.0573 -0.0485 -0.0505 161 VAL A CG1 
1358 C  CG2 . VAL A 160 ? 0.2666 0.1806 0.1787 0.0054  0.0010  -0.0068 161 VAL A CG2 
1359 N  N   . ASP A 161 ? 0.3052 0.1932 0.1374 -0.0421 -0.0692 -0.0063 162 ASP A N   
1360 C  CA  . ASP A 161 ? 0.3194 0.2229 0.1453 -0.0408 -0.0870 -0.0080 162 ASP A CA  
1361 C  C   . ASP A 161 ? 0.4086 0.2691 0.1244 -0.0522 -0.0828 0.0017  162 ASP A C   
1362 O  O   . ASP A 161 ? 0.4237 0.3467 0.1799 -0.0650 -0.0204 -0.0386 162 ASP A O   
1363 C  CB  . ASP A 161 ? 0.4156 0.2739 0.1835 -0.0573 -0.1090 -0.0449 162 ASP A CB  
1364 C  CG  . ASP A 161 ? 0.4064 0.3305 0.1413 -0.0627 -0.0386 -0.0592 162 ASP A CG  
1365 O  OD1 . ASP A 161 ? 0.4947 0.3203 0.3203 -0.0729 -0.1160 -0.0256 162 ASP A OD1 
1366 O  OD2 . ASP A 161 ? 0.4171 0.5019 0.3406 0.0186  -0.1389 -0.1011 162 ASP A OD2 
1367 N  N   . VAL A 162 ? 0.3828 0.2008 0.1362 -0.0527 -0.1128 0.0100  163 VAL A N   
1368 C  CA  . VAL A 162 ? 0.3280 0.2512 0.1328 -0.0196 -0.0913 0.0137  163 VAL A CA  
1369 C  C   . VAL A 162 ? 0.3397 0.1867 0.1162 -0.0286 -0.0461 0.0293  163 VAL A C   
1370 O  O   . VAL A 162 ? 0.3318 0.2154 0.1206 -0.0238 -0.0303 0.0020  163 VAL A O   
1371 C  CB  . VAL A 162 ? 0.3077 0.2201 0.2279 -0.0197 -0.0483 0.0098  163 VAL A CB  
1372 C  CG1 . VAL A 162 ? 0.3991 0.1650 0.2316 -0.0147 -0.0769 -0.0097 163 VAL A CG1 
1373 C  CG2 . VAL A 162 ? 0.3464 0.2549 0.2664 0.0364  0.0131  0.0615  163 VAL A CG2 
1374 N  N   . LEU A 163 ? 0.2947 0.2031 0.1475 -0.0390 -0.0803 0.0170  164 LEU A N   
1375 C  CA  . LEU A 163 ? 0.2946 0.1483 0.1234 -0.0288 -0.0164 -0.0044 164 LEU A CA  
1376 C  C   . LEU A 163 ? 0.3087 0.1926 0.1389 -0.0209 0.0017  -0.0010 164 LEU A C   
1377 O  O   . LEU A 163 ? 0.3086 0.2143 0.1147 0.0068  0.0143  0.0186  164 LEU A O   
1378 C  CB  . LEU A 163 ? 0.2664 0.1657 0.1261 -0.0243 -0.0212 -0.0144 164 LEU A CB  
1379 C  CG  . LEU A 163 ? 0.2496 0.1528 0.1212 -0.0104 -0.0381 -0.0041 164 LEU A CG  
1380 C  CD1 . LEU A 163 ? 0.2615 0.1765 0.1682 -0.0258 -0.0419 0.0392  164 LEU A CD1 
1381 C  CD2 . LEU A 163 ? 0.2617 0.1876 0.1079 -0.0083 -0.0406 -0.0077 164 LEU A CD2 
1382 N  N   . ASP A 164 ? 0.3841 0.2050 0.1160 -0.0115 -0.0315 -0.0313 165 ASP A N   
1383 C  CA  . ASP A 164 ? 0.5579 0.2226 0.1572 -0.0306 0.0270  -0.0693 165 ASP A CA  
1384 C  C   . ASP A 164 ? 0.3856 0.2907 0.1500 0.0043  -0.0060 -0.0068 165 ASP A C   
1385 O  O   . ASP A 164 ? 0.4889 0.2754 0.2202 0.0529  0.0710  0.0031  165 ASP A O   
1386 C  CB  . ASP A 164 ? 0.6169 0.3262 0.2125 -0.0930 -0.0054 -0.0909 165 ASP A CB  
1387 C  CG  . ASP A 164 ? 0.5131 0.5121 0.3605 -0.2870 -0.0436 -0.0797 165 ASP A CG  
1388 O  OD1 . ASP A 164 ? 0.6592 1.2510 0.2903 -0.0989 -0.0173 -0.2099 165 ASP A OD1 
1389 O  OD2 . ASP A 164 ? 0.8034 1.3806 0.4663 -0.0590 -0.0331 -0.5253 165 ASP A OD2 
1390 N  N   . SER A 165 ? 0.3378 0.2817 0.1312 -0.0197 -0.0432 0.0154  166 SER A N   
1391 C  CA  . SER A 165 ? 0.3657 0.2653 0.1316 0.0115  -0.0344 -0.0035 166 SER A CA  
1392 C  C   . SER A 165 ? 0.3066 0.2358 0.1120 -0.0143 -0.0027 0.0214  166 SER A C   
1393 O  O   . SER A 165 ? 0.3835 0.2390 0.1305 -0.0189 -0.0054 0.0291  166 SER A O   
1394 C  CB  . SER A 165 ? 0.3249 0.2779 0.2053 0.0071  0.0098  0.0223  166 SER A CB  
1395 O  OG  . SER A 165 ? 0.4198 0.2470 0.1976 0.0333  -0.0190 0.0364  166 SER A OG  
1396 N  N   . ILE A 166 ? 0.2395 0.2154 0.1158 -0.0160 -0.0065 0.0049  167 ILE A N   
1397 C  CA  . ILE A 166 ? 0.2509 0.1599 0.1464 -0.0073 -0.0015 0.0233  167 ILE A CA  
1398 C  C   . ILE A 166 ? 0.2442 0.1840 0.1102 -0.0211 0.0020  -0.0227 167 ILE A C   
1399 O  O   . ILE A 166 ? 0.2621 0.1872 0.1101 -0.0255 0.0087  -0.0021 167 ILE A O   
1400 C  CB  . ILE A 166 ? 0.2700 0.1782 0.0988 -0.0057 0.0126  0.0082  167 ILE A CB  
1401 C  CG1 . ILE A 166 ? 0.2531 0.1865 0.1142 0.0052  0.0174  0.0057  167 ILE A CG1 
1402 C  CG2 . ILE A 166 ? 0.3169 0.1732 0.1431 0.0034  -0.0161 0.0313  167 ILE A CG2 
1403 C  CD1 . ILE A 166 ? 0.3141 0.1928 0.1180 -0.0342 0.0077  -0.0196 167 ILE A CD1 
1404 N  N   . LYS A 167 ? 0.2456 0.1802 0.1395 0.0135  0.0165  0.0178  168 LYS A N   
1405 C  CA  . LYS A 167 ? 0.1993 0.2266 0.1287 0.0098  -0.0013 -0.0441 168 LYS A CA  
1406 C  C   . LYS A 167 ? 0.1942 0.1979 0.1174 0.0001  0.0299  0.0239  168 LYS A C   
1407 O  O   . LYS A 167 ? 0.2678 0.1615 0.1281 -0.0219 0.0049  -0.0021 168 LYS A O   
1408 C  CB  . LYS A 167 ? 0.2718 0.1784 0.1616 0.0000  -0.0226 -0.0315 168 LYS A CB  
1409 C  CG  . LYS A 167 ? 0.2090 0.2192 0.1562 -0.0006 0.0142  -0.0271 168 LYS A CG  
1410 C  CD  . LYS A 167 ? 0.3228 0.2818 0.2210 -0.0190 -0.0274 -0.0864 168 LYS A CD  
1411 C  CE  . LYS A 167 ? 0.5006 0.3303 0.3478 0.0465  -0.0265 -0.0639 168 LYS A CE  
1412 N  NZ  . LYS A 167 ? 0.5584 0.5996 0.5680 0.1577  -0.0188 -0.2232 168 LYS A NZ  
1413 N  N   . THR A 168 ? 0.2124 0.1756 0.1553 -0.0071 -0.0032 0.0049  169 THR A N   
1414 C  CA  . THR A 168 ? 0.2161 0.2041 0.1185 -0.0043 0.0381  0.0078  169 THR A CA  
1415 C  C   . THR A 168 ? 0.1773 0.1939 0.1080 -0.0070 0.0063  0.0109  169 THR A C   
1416 O  O   . THR A 168 ? 0.2438 0.1758 0.1664 -0.0080 0.0326  0.0329  169 THR A O   
1417 C  CB  . THR A 168 ? 0.2316 0.2203 0.1535 -0.0153 0.0159  0.0120  169 THR A CB  
1418 O  OG1 . THR A 168 ? 0.2700 0.2551 0.1348 0.0078  0.0324  0.0186  169 THR A OG1 
1419 C  CG2 . THR A 168 ? 0.2928 0.2092 0.1836 -0.0087 0.0612  0.0034  169 THR A CG2 
1420 N  N   . LYS A 169 ? 0.2331 0.1852 0.1520 -0.0428 0.0441  0.0124  170 LYS A N   
1421 C  CA  . LYS A 169 ? 0.2003 0.1709 0.1782 -0.0293 0.0295  0.0024  170 LYS A CA  
1422 C  C   . LYS A 169 ? 0.1895 0.2044 0.1701 -0.0144 0.0482  0.0599  170 LYS A C   
1423 O  O   . LYS A 169 ? 0.2810 0.2222 0.1655 -0.0412 0.0379  0.0236  170 LYS A O   
1424 C  CB  . LYS A 169 ? 0.2275 0.1729 0.1776 -0.0125 0.0524  0.0132  170 LYS A CB  
1425 C  CG  . LYS A 169 ? 0.2387 0.2368 0.1720 -0.0560 -0.0115 0.0432  170 LYS A CG  
1426 C  CD  . LYS A 169 ? 0.2743 0.2259 0.2125 -0.0059 0.0275  0.0162  170 LYS A CD  
1427 C  CE  . LYS A 169 ? 0.2562 0.6333 0.3138 0.0496  0.0276  -0.0793 170 LYS A CE  
1428 N  NZ  . LYS A 169 ? 0.5983 0.8790 0.4618 -0.0203 -0.1544 0.2449  170 LYS A NZ  
1429 N  N   . GLY A 170 ? 0.2621 0.1509 0.1961 -0.0469 0.0392  0.0208  171 GLY A N   
1430 C  CA  . GLY A 170 ? 0.2578 0.1446 0.2408 -0.0146 0.0000  0.0716  171 GLY A CA  
1431 C  C   . GLY A 170 ? 0.2782 0.2106 0.1985 -0.0051 0.0041  0.0777  171 GLY A C   
1432 O  O   . GLY A 170 ? 0.3073 0.2304 0.3058 -0.0469 -0.0218 0.1335  171 GLY A O   
1433 N  N   . LYS A 171 ? 0.2215 0.1718 0.2073 -0.0124 0.0274  0.0672  172 LYS A N   
1434 C  CA  . LYS A 171 ? 0.1991 0.1997 0.2073 -0.0054 0.0013  0.0680  172 LYS A CA  
1435 C  C   . LYS A 171 ? 0.1972 0.2153 0.1572 0.0410  0.0116  0.0310  172 LYS A C   
1436 O  O   . LYS A 171 ? 0.2463 0.1917 0.1210 -0.0027 0.0208  0.0496  172 LYS A O   
1437 C  CB  . LYS A 171 ? 0.3445 0.2151 0.1439 -0.0054 0.0423  0.0351  172 LYS A CB  
1438 C  CG  . LYS A 171 ? 0.2979 0.2399 0.2231 -0.0149 0.0221  0.0066  172 LYS A CG  
1439 C  CD  . LYS A 171 ? 0.4341 0.2646 0.2915 0.0337  -0.0351 -0.0081 172 LYS A CD  
1440 C  CE  . LYS A 171 ? 1.0851 0.3625 0.3395 0.0359  -0.1913 -0.1111 172 LYS A CE  
1441 N  NZ  . LYS A 171 ? 1.2572 0.3195 0.2736 -0.1343 0.2094  -0.0131 172 LYS A NZ  
1442 N  N   . SER A 172 ? 0.2706 0.2116 0.1699 0.0109  -0.0098 0.0922  173 SER A N   
1443 C  CA  . SER A 172 ? 0.1636 0.1953 0.2949 0.0176  0.0030  0.0454  173 SER A CA  
1444 C  C   . SER A 172 ? 0.1758 0.2431 0.1824 0.0326  -0.0342 0.0887  173 SER A C   
1445 O  O   . SER A 172 ? 0.3386 0.3197 0.1027 0.0476  -0.0225 0.0604  173 SER A O   
1446 C  CB  . SER A 172 ? 0.2526 0.2504 0.1754 -0.0054 0.0027  0.0201  173 SER A CB  
1447 O  OG  . SER A 172 ? 0.4765 0.2340 0.2451 0.0120  0.0298  0.1005  173 SER A OG  
1448 N  N   . ALA A 173 ? 0.2126 0.2935 0.1713 0.0798  -0.0241 0.0211  174 ALA A N   
1449 C  CA  . ALA A 173 ? 0.2363 0.3720 0.1465 0.0395  -0.0375 0.0882  174 ALA A CA  
1450 C  C   . ALA A 173 ? 0.1666 0.2533 0.1538 0.0226  -0.0283 0.0456  174 ALA A C   
1451 O  O   . ALA A 173 ? 0.2323 0.2214 0.1124 0.0252  -0.0266 0.0285  174 ALA A O   
1452 C  CB  . ALA A 173 ? 0.4319 0.3364 0.1668 0.0775  -0.0294 -0.0185 174 ALA A CB  
1453 N  N   . ASP A 174 ? 0.2462 0.3353 0.1324 0.0239  -0.0296 0.0908  175 ASP A N   
1454 C  CA  . ASP A 174 ? 0.2391 0.3034 0.1389 0.0303  -0.0023 0.0485  175 ASP A CA  
1455 C  C   . ASP A 174 ? 0.2452 0.2212 0.1805 0.0205  -0.0555 0.0412  175 ASP A C   
1456 O  O   . ASP A 174 ? 0.3360 0.2894 0.1914 0.0197  -0.0231 -0.0171 175 ASP A O   
1457 C  CB  . ASP A 174 ? 0.3226 0.4384 0.2390 0.0935  -0.0427 0.1146  175 ASP A CB  
1458 C  CG  . ASP A 174 ? 0.4754 0.5533 0.2390 0.0309  -0.0373 0.1336  175 ASP A CG  
1459 O  OD1 . ASP A 174 ? 0.6338 0.7917 0.4923 0.0200  -0.3068 -0.0329 175 ASP A OD1 
1460 O  OD2 . ASP A 174 ? 0.3289 0.4463 0.2477 -0.0122 -0.0092 0.0913  175 ASP A OD2 
1461 N  N   . PHE A 175 ? 0.2460 0.2520 0.1416 0.0104  -0.0187 0.0080  176 PHE A N   
1462 C  CA  . PHE A 175 ? 0.2223 0.2304 0.1634 0.0099  -0.0423 0.0531  176 PHE A CA  
1463 C  C   . PHE A 175 ? 0.1837 0.1627 0.2088 0.0115  -0.0573 -0.0115 176 PHE A C   
1464 O  O   . PHE A 175 ? 0.2883 0.2319 0.1562 0.0302  -0.0860 -0.0147 176 PHE A O   
1465 C  CB  . PHE A 175 ? 0.2799 0.1709 0.1591 0.0078  -0.0531 0.0368  176 PHE A CB  
1466 C  CG  . PHE A 175 ? 0.2817 0.1741 0.1498 0.0210  -0.0666 -0.0041 176 PHE A CG  
1467 C  CD1 . PHE A 175 ? 0.3659 0.1904 0.1792 0.0017  -0.0355 -0.0168 176 PHE A CD1 
1468 C  CD2 . PHE A 175 ? 0.2743 0.1784 0.1635 -0.0155 -0.0873 0.0143  176 PHE A CD2 
1469 C  CE1 . PHE A 175 ? 0.3878 0.1947 0.1985 0.0143  -0.0432 0.0083  176 PHE A CE1 
1470 C  CE2 . PHE A 175 ? 0.2979 0.1607 0.1888 0.0063  -0.0909 0.0255  176 PHE A CE2 
1471 C  CZ  . PHE A 175 ? 0.3932 0.1350 0.2257 0.0082  -0.0870 0.0055  176 PHE A CZ  
1472 N  N   . THR A 176 ? 0.2757 0.2323 0.1230 0.0030  -0.0850 0.0280  177 THR A N   
1473 C  CA  . THR A 176 ? 0.2458 0.1793 0.1543 0.0471  -0.0326 0.0310  177 THR A CA  
1474 C  C   . THR A 176 ? 0.2538 0.1797 0.1351 -0.0040 -0.0825 0.0621  177 THR A C   
1475 O  O   . THR A 176 ? 0.3331 0.1488 0.1498 -0.0115 -0.0869 0.0185  177 THR A O   
1476 C  CB  . THR A 176 ? 0.2854 0.1904 0.1853 0.0232  -0.0850 0.0557  177 THR A CB  
1477 O  OG1 . THR A 176 ? 0.4545 0.2504 0.1562 0.0898  -0.1216 0.0241  177 THR A OG1 
1478 C  CG2 . THR A 176 ? 0.3984 0.3102 0.4259 -0.0324 -0.1347 0.1970  177 THR A CG2 
1479 N  N   . ASN A 177 ? 0.2849 0.1838 0.1167 0.0277  -0.0659 0.0124  178 ASN A N   
1480 C  CA  . ASN A 177 ? 0.2597 0.1865 0.1941 -0.0063 -0.0838 0.0524  178 ASN A CA  
1481 C  C   . ASN A 177 ? 0.2750 0.1904 0.1554 -0.0156 -0.0904 0.0421  178 ASN A C   
1482 O  O   . ASN A 177 ? 0.3260 0.2250 0.2871 -0.0480 -0.1416 0.1202  178 ASN A O   
1483 C  CB  . ASN A 177 ? 0.2969 0.1827 0.1770 -0.0043 -0.1039 0.0493  178 ASN A CB  
1484 C  CG  . ASN A 177 ? 0.2628 0.1915 0.1958 0.0041  -0.1036 0.0162  178 ASN A CG  
1485 O  OD1 . ASN A 177 ? 0.3776 0.2171 0.2488 0.0684  -0.0559 0.0551  178 ASN A OD1 
1486 N  ND2 . ASN A 177 ? 0.3240 0.1870 0.1782 0.0093  -0.0973 0.0542  178 ASN A ND2 
1487 N  N   . PHE A 178 ? 0.3014 0.1420 0.1324 0.0062  -0.0837 0.0114  179 PHE A N   
1488 C  CA  . PHE A 178 ? 0.3122 0.1278 0.1499 0.0006  -0.0819 0.0342  179 PHE A CA  
1489 C  C   . PHE A 178 ? 0.2431 0.1494 0.1342 -0.0012 -0.0925 0.0302  179 PHE A C   
1490 O  O   . PHE A 178 ? 0.2825 0.1444 0.1425 -0.0076 -0.0725 0.0114  179 PHE A O   
1491 C  CB  . PHE A 178 ? 0.2984 0.1500 0.1354 -0.0116 -0.0375 0.0309  179 PHE A CB  
1492 C  CG  . PHE A 178 ? 0.2706 0.1337 0.1439 -0.0082 -0.0524 0.0359  179 PHE A CG  
1493 C  CD1 . PHE A 178 ? 0.3054 0.1562 0.1539 -0.0098 -0.0648 0.0242  179 PHE A CD1 
1494 C  CD2 . PHE A 178 ? 0.2329 0.1453 0.1367 -0.0055 -0.0450 0.0315  179 PHE A CD2 
1495 C  CE1 . PHE A 178 ? 0.3129 0.1348 0.1720 -0.0066 -0.0697 0.0184  179 PHE A CE1 
1496 C  CE2 . PHE A 178 ? 0.1959 0.1513 0.1570 -0.0001 -0.0430 0.0342  179 PHE A CE2 
1497 C  CZ  . PHE A 178 ? 0.2484 0.1482 0.1411 0.0070  -0.0544 0.0225  179 PHE A CZ  
1498 N  N   . ASP A 179 ? 0.2513 0.1451 0.1720 0.0026  -0.0847 0.0436  180 ASP A N   
1499 C  CA  . ASP A 179 ? 0.2211 0.1974 0.1710 0.0204  -0.0914 0.0217  180 ASP A CA  
1500 C  C   . ASP A 179 ? 0.1851 0.1542 0.1588 -0.0096 -0.0612 0.0262  180 ASP A C   
1501 O  O   . ASP A 179 ? 0.2261 0.1436 0.1624 -0.0120 -0.0643 0.0066  180 ASP A O   
1502 C  CB  . ASP A 179 ? 0.2108 0.2627 0.2083 -0.0133 -0.1088 0.0397  180 ASP A CB  
1503 C  CG  . ASP A 179 ? 0.2506 0.2424 0.2257 0.0324  -0.0864 0.0390  180 ASP A CG  
1504 O  OD1 . ASP A 179 ? 0.2268 0.1747 0.2344 0.0035  -0.0751 0.0443  180 ASP A OD1 
1505 O  OD2 . ASP A 179 ? 0.2101 0.4255 0.3583 0.0215  -0.1089 0.0339  180 ASP A OD2 
1506 N  N   . PRO A 180 ? 0.1807 0.1206 0.1508 -0.0049 -0.0586 0.0161  181 PRO A N   
1507 C  CA  . PRO A 180 ? 0.1723 0.1326 0.1632 -0.0005 -0.0601 0.0339  181 PRO A CA  
1508 C  C   . PRO A 180 ? 0.1727 0.1483 0.1405 -0.0068 -0.0619 0.0311  181 PRO A C   
1509 O  O   . PRO A 180 ? 0.1683 0.1447 0.1432 -0.0049 -0.0544 0.0274  181 PRO A O   
1510 C  CB  . PRO A 180 ? 0.1800 0.1599 0.1805 -0.0218 -0.0614 0.0181  181 PRO A CB  
1511 C  CG  . PRO A 180 ? 0.2090 0.1556 0.1553 -0.0137 -0.0659 0.0159  181 PRO A CG  
1512 C  CD  . PRO A 180 ? 0.2067 0.1456 0.1659 0.0052  -0.0707 0.0184  181 PRO A CD  
1513 N  N   . ARG A 181 ? 0.1544 0.1585 0.1502 0.0071  -0.0529 0.0203  182 ARG A N   
1514 C  CA  . ARG A 181 ? 0.1643 0.1423 0.1956 -0.0135 -0.0307 0.0182  182 ARG A CA  
1515 C  C   . ARG A 181 ? 0.1432 0.1657 0.1835 0.0076  -0.0741 0.0285  182 ARG A C   
1516 O  O   . ARG A 181 ? 0.1838 0.1613 0.2301 -0.0116 -0.0535 0.0520  182 ARG A O   
1517 C  CB  . ARG A 181 ? 0.1512 0.1678 0.2092 -0.0060 -0.0351 0.0322  182 ARG A CB  
1518 C  CG  . ARG A 181 ? 0.1803 0.1703 0.2696 -0.0187 -0.0089 0.0076  182 ARG A CG  
1519 C  CD  . ARG A 181 ? 0.1580 0.2764 0.2983 0.0197  0.0088  0.0491  182 ARG A CD  
1520 N  NE  . ARG A 181 ? 0.1746 0.2097 0.3252 -0.0082 -0.0074 0.0654  182 ARG A NE  
1521 C  CZ  . ARG A 181 ? 0.1597 0.3330 0.3488 0.0196  0.0359  0.1659  182 ARG A CZ  
1522 N  NH1 . ARG A 181 ? 0.1966 0.4154 0.4797 0.0417  0.0803  0.1676  182 ARG A NH1 
1523 N  NH2 . ARG A 181 ? 0.2614 0.3792 0.3695 0.0515  0.0207  0.1764  182 ARG A NH2 
1524 N  N   . GLY A 182 ? 0.1693 0.1664 0.1780 -0.0074 -0.0803 0.0240  183 GLY A N   
1525 C  CA  . GLY A 182 ? 0.2248 0.1342 0.2466 -0.0326 -0.1172 0.0228  183 GLY A CA  
1526 C  C   . GLY A 182 ? 0.2064 0.1367 0.2196 -0.0098 -0.0838 0.0265  183 GLY A C   
1527 O  O   . GLY A 182 ? 0.2498 0.1391 0.2738 -0.0148 -0.1140 0.0142  183 GLY A O   
1528 N  N   . LEU A 183 ? 0.1984 0.1288 0.1650 -0.0071 -0.0780 0.0183  184 LEU A N   
1529 C  CA  . LEU A 183 ? 0.2000 0.1257 0.1717 0.0073  -0.0698 0.0062  184 LEU A CA  
1530 C  C   . LEU A 183 ? 0.1941 0.1316 0.1547 0.0013  -0.0657 0.0241  184 LEU A C   
1531 O  O   . LEU A 183 ? 0.2123 0.1475 0.1897 0.0060  -0.0639 0.0390  184 LEU A O   
1532 C  CB  . LEU A 183 ? 0.1967 0.1580 0.1492 0.0278  -0.0566 0.0318  184 LEU A CB  
1533 C  CG  . LEU A 183 ? 0.2102 0.1724 0.1580 0.0048  -0.0425 0.0173  184 LEU A CG  
1534 C  CD1 . LEU A 183 ? 0.2255 0.2527 0.1718 0.0403  -0.0346 0.0670  184 LEU A CD1 
1535 C  CD2 . LEU A 183 ? 0.2492 0.1974 0.1955 0.0408  -0.0520 -0.0285 184 LEU A CD2 
1536 N  N   . LEU A 184 ? 0.2031 0.1403 0.1639 0.0124  -0.0557 0.0201  185 LEU A N   
1537 C  CA  . LEU A 184 ? 0.1516 0.1591 0.1780 -0.0326 -0.0562 0.0326  185 LEU A CA  
1538 C  C   . LEU A 184 ? 0.2050 0.1573 0.1928 -0.0640 -0.0781 0.0304  185 LEU A C   
1539 O  O   . LEU A 184 ? 0.2115 0.2175 0.2426 -0.0640 -0.0781 0.0643  185 LEU A O   
1540 C  CB  . LEU A 184 ? 0.1178 0.1641 0.2040 -0.0166 -0.0381 0.0261  185 LEU A CB  
1541 C  CG  . LEU A 184 ? 0.1045 0.1641 0.2016 0.0021  -0.0324 0.0251  185 LEU A CG  
1542 C  CD1 . LEU A 184 ? 0.1203 0.1913 0.2064 0.0115  -0.0046 0.0066  185 LEU A CD1 
1543 C  CD2 . LEU A 184 ? 0.1115 0.1851 0.2506 -0.0297 -0.0436 0.0346  185 LEU A CD2 
1544 N  N   . PRO A 185 ? 0.1474 0.1412 0.1801 -0.0230 -0.0630 0.0353  186 PRO A N   
1545 C  CA  . PRO A 185 ? 0.1876 0.1395 0.1800 -0.0281 -0.0498 0.0485  186 PRO A CA  
1546 C  C   . PRO A 185 ? 0.1201 0.1607 0.2520 -0.0151 -0.0623 0.0403  186 PRO A C   
1547 O  O   . PRO A 185 ? 0.1124 0.1469 0.3457 -0.0055 -0.0573 0.0696  186 PRO A O   
1548 C  CB  . PRO A 185 ? 0.1343 0.1483 0.1994 -0.0124 -0.0381 0.0381  186 PRO A CB  
1549 C  CG  . PRO A 185 ? 0.1150 0.1730 0.1589 0.0146  -0.0310 0.0228  186 PRO A CG  
1550 C  CD  . PRO A 185 ? 0.1212 0.1651 0.1543 0.0083  -0.0272 0.0205  186 PRO A CD  
1551 N  N   A GLU A 186 ? 0.1660 0.1580 0.2572 -0.0478 -0.0767 0.0612  187 GLU A N   
1552 N  N   B GLU A 186 ? 0.1659 0.1638 0.2584 -0.0593 -0.0766 0.0454  187 GLU A N   
1553 C  CA  A GLU A 186 ? 0.1111 0.1977 0.2979 -0.0513 -0.0603 0.0472  187 GLU A CA  
1554 C  CA  B GLU A 186 ? 0.1045 0.1940 0.3012 -0.0516 -0.0509 0.0465  187 GLU A CA  
1555 C  C   A GLU A 186 ? 0.0860 0.1826 0.2757 -0.0163 -0.0351 0.0417  187 GLU A C   
1556 C  C   B GLU A 186 ? 0.0956 0.1817 0.2764 -0.0149 -0.0344 0.0445  187 GLU A C   
1557 O  O   A GLU A 186 ? 0.1162 0.2106 0.3496 0.0237  -0.0430 0.0430  187 GLU A O   
1558 O  O   B GLU A 186 ? 0.1204 0.2100 0.3474 0.0243  -0.0419 0.0472  187 GLU A O   
1559 C  CB  A GLU A 186 ? 0.1755 0.2458 0.3864 -0.1089 -0.1337 0.0728  187 GLU A CB  
1560 C  CB  B GLU A 186 ? 0.2087 0.2410 0.4312 -0.1074 -0.0926 0.1150  187 GLU A CB  
1561 C  CG  A GLU A 186 ? 0.2084 0.2079 0.3641 -0.0087 -0.0965 0.0869  187 GLU A CG  
1562 C  CG  B GLU A 186 ? 0.2145 0.1787 0.3867 -0.0577 -0.0643 0.0644  187 GLU A CG  
1563 C  CD  A GLU A 186 ? 0.2591 0.2221 0.4035 0.0247  -0.0307 0.0727  187 GLU A CD  
1564 C  CD  B GLU A 186 ? 0.1950 0.2666 0.5022 -0.0832 -0.0421 0.0835  187 GLU A CD  
1565 O  OE1 A GLU A 186 ? 0.1172 0.2305 0.5342 -0.0555 -0.0403 0.0135  187 GLU A OE1 
1566 O  OE1 B GLU A 186 ? 0.2813 0.2241 0.4973 -0.0296 -0.0020 0.0890  187 GLU A OE1 
1567 O  OE2 A GLU A 186 ? 0.3188 0.2006 0.5835 0.0403  0.1952  0.1304  187 GLU A OE2 
1568 O  OE2 B GLU A 186 ? 0.1975 0.2115 0.6417 -0.0684 0.0082  -0.0657 187 GLU A OE2 
1569 N  N   . SER A 187 ? 0.0957 0.1683 0.2495 -0.0218 -0.0370 0.0296  188 SER A N   
1570 C  CA  . SER A 187 ? 0.0851 0.1800 0.2559 -0.0143 -0.0046 0.0410  188 SER A CA  
1571 C  C   . SER A 187 ? 0.0820 0.1918 0.2373 -0.0194 -0.0210 0.0286  188 SER A C   
1572 O  O   . SER A 187 ? 0.0926 0.2132 0.2337 -0.0313 -0.0020 -0.0003 188 SER A O   
1573 C  CB  . SER A 187 ? 0.1266 0.2056 0.2315 -0.0357 -0.0083 0.0324  188 SER A CB  
1574 O  OG  . SER A 187 ? 0.1269 0.2170 0.2556 -0.0357 -0.0031 0.0463  188 SER A OG  
1575 N  N   . LEU A 188 ? 0.0996 0.1468 0.2434 -0.0111 -0.0099 0.0155  189 LEU A N   
1576 C  CA  . LEU A 188 ? 0.1070 0.1666 0.2544 -0.0097 -0.0302 0.0331  189 LEU A CA  
1577 C  C   . LEU A 188 ? 0.0983 0.1656 0.2268 -0.0052 0.0001  -0.0032 189 LEU A C   
1578 O  O   . LEU A 188 ? 0.1357 0.1744 0.2327 -0.0189 -0.0071 -0.0129 189 LEU A O   
1579 C  CB  . LEU A 188 ? 0.1359 0.1941 0.2628 -0.0230 -0.0166 0.0359  189 LEU A CB  
1580 C  CG  . LEU A 188 ? 0.1171 0.2055 0.3296 -0.0109 -0.0434 0.0720  189 LEU A CG  
1581 C  CD1 . LEU A 188 ? 0.1835 0.2111 0.3815 -0.0259 -0.0599 0.0856  189 LEU A CD1 
1582 C  CD2 . LEU A 188 ? 0.1260 0.3553 0.3317 -0.0333 -0.0421 0.1180  189 LEU A CD2 
1583 N  N   . ASP A 189 ? 0.0964 0.1699 0.1918 -0.0006 0.0008  -0.0010 190 ASP A N   
1584 C  CA  . ASP A 189 ? 0.0996 0.1923 0.1634 -0.0252 0.0223  -0.0077 190 ASP A CA  
1585 C  C   . ASP A 189 ? 0.1089 0.1378 0.1516 -0.0183 0.0024  -0.0003 190 ASP A C   
1586 O  O   . ASP A 189 ? 0.0993 0.1393 0.1532 -0.0188 0.0038  -0.0052 190 ASP A O   
1587 C  CB  . ASP A 189 ? 0.1492 0.2298 0.1906 -0.0768 0.0243  0.0406  190 ASP A CB  
1588 C  CG  . ASP A 189 ? 0.2023 0.3694 0.2250 -0.0998 0.0065  0.0308  190 ASP A CG  
1589 O  OD1 . ASP A 189 ? 0.1920 0.5318 0.3654 -0.1199 0.1252  -0.0842 190 ASP A OD1 
1590 O  OD2 . ASP A 189 ? 0.2245 0.5706 0.2803 -0.1879 -0.0028 0.1058  190 ASP A OD2 
1591 N  N   . TYR A 190 ? 0.1013 0.1492 0.1336 -0.0121 0.0085  0.0091  191 TYR A N   
1592 C  CA  . TYR A 190 ? 0.0956 0.1358 0.1280 -0.0147 -0.0010 0.0254  191 TYR A CA  
1593 C  C   . TYR A 190 ? 0.0975 0.1169 0.1213 -0.0142 0.0149  0.0131  191 TYR A C   
1594 O  O   . TYR A 190 ? 0.1165 0.1403 0.1122 -0.0088 0.0199  0.0007  191 TYR A O   
1595 C  CB  . TYR A 190 ? 0.1108 0.1280 0.1323 -0.0197 0.0111  0.0107  191 TYR A CB  
1596 C  CG  . TYR A 190 ? 0.1115 0.1313 0.1351 -0.0176 0.0081  0.0171  191 TYR A CG  
1597 C  CD1 . TYR A 190 ? 0.1388 0.1359 0.1310 -0.0163 0.0113  0.0109  191 TYR A CD1 
1598 C  CD2 . TYR A 190 ? 0.1277 0.1428 0.1567 0.0013  0.0119  0.0167  191 TYR A CD2 
1599 C  CE1 . TYR A 190 ? 0.1351 0.1439 0.1525 -0.0133 -0.0015 0.0177  191 TYR A CE1 
1600 C  CE2 . TYR A 190 ? 0.1299 0.1342 0.1748 0.0010  0.0043  0.0153  191 TYR A CE2 
1601 C  CZ  . TYR A 190 ? 0.1416 0.1235 0.1673 0.0046  0.0137  0.0066  191 TYR A CZ  
1602 O  OH  . TYR A 190 ? 0.1724 0.1571 0.1710 0.0147  0.0021  -0.0164 191 TYR A OH  
1603 N  N   . TRP A 191 ? 0.0973 0.1045 0.1049 -0.0076 0.0012  0.0098  192 TRP A N   
1604 C  CA  . TRP A 191 ? 0.1131 0.1000 0.1058 -0.0132 0.0157  0.0111  192 TRP A CA  
1605 C  C   . TRP A 191 ? 0.0976 0.1136 0.0860 0.0021  0.0046  0.0048  192 TRP A C   
1606 O  O   . TRP A 191 ? 0.1178 0.1190 0.0954 -0.0166 0.0043  0.0065  192 TRP A O   
1607 C  CB  . TRP A 191 ? 0.1122 0.1095 0.1124 -0.0027 0.0126  0.0044  192 TRP A CB  
1608 C  CG  . TRP A 191 ? 0.1124 0.1080 0.1213 0.0071  0.0068  0.0115  192 TRP A CG  
1609 C  CD1 . TRP A 191 ? 0.1440 0.1133 0.1308 0.0071  0.0119  0.0208  192 TRP A CD1 
1610 C  CD2 . TRP A 191 ? 0.0929 0.1125 0.1412 0.0089  0.0105  0.0142  192 TRP A CD2 
1611 N  NE1 . TRP A 191 ? 0.1556 0.1198 0.1392 0.0006  0.0142  0.0284  192 TRP A NE1 
1612 C  CE2 . TRP A 191 ? 0.1305 0.1159 0.1528 0.0035  0.0030  0.0148  192 TRP A CE2 
1613 C  CE3 . TRP A 191 ? 0.0879 0.1406 0.1328 0.0057  -0.0041 -0.0131 192 TRP A CE3 
1614 C  CZ2 . TRP A 191 ? 0.1269 0.1095 0.1875 0.0048  -0.0078 0.0198  192 TRP A CZ2 
1615 C  CZ3 . TRP A 191 ? 0.1036 0.1323 0.1664 -0.0030 -0.0093 -0.0093 192 TRP A CZ3 
1616 C  CH2 . TRP A 191 ? 0.1263 0.1339 0.1913 0.0013  -0.0113 -0.0107 192 TRP A CH2 
1617 N  N   . THR A 192 ? 0.1009 0.1036 0.0975 -0.0044 0.0001  0.0098  193 THR A N   
1618 C  CA  . THR A 192 ? 0.1068 0.1079 0.0891 -0.0001 0.0044  0.0044  193 THR A CA  
1619 C  C   . THR A 192 ? 0.0980 0.1013 0.0753 0.0098  -0.0005 0.0012  193 THR A C   
1620 O  O   . THR A 192 ? 0.1128 0.1282 0.0852 -0.0020 0.0031  0.0087  193 THR A O   
1621 C  CB  . THR A 192 ? 0.1080 0.1022 0.1081 0.0046  0.0157  0.0071  193 THR A CB  
1622 O  OG1 . THR A 192 ? 0.1084 0.1050 0.1133 0.0054  0.0074  -0.0027 193 THR A OG1 
1623 C  CG2 . THR A 192 ? 0.1322 0.1261 0.1165 0.0153  0.0192  0.0000  193 THR A CG2 
1624 N  N   . TYR A 193 ? 0.0943 0.1004 0.0935 0.0001  0.0019  -0.0021 194 TYR A N   
1625 C  CA  . TYR A 193 ? 0.0918 0.1080 0.0973 -0.0003 -0.0076 0.0020  194 TYR A CA  
1626 C  C   . TYR A 193 ? 0.0917 0.1045 0.0784 0.0118  -0.0005 -0.0082 194 TYR A C   
1627 O  O   . TYR A 193 ? 0.0953 0.1032 0.0852 0.0043  -0.0094 -0.0048 194 TYR A O   
1628 C  CB  . TYR A 193 ? 0.1356 0.1115 0.0837 0.0131  -0.0071 0.0013  194 TYR A CB  
1629 C  CG  . TYR A 193 ? 0.0958 0.0971 0.0899 0.0041  -0.0125 0.0068  194 TYR A CG  
1630 C  CD1 . TYR A 193 ? 0.0997 0.0922 0.0953 0.0120  -0.0024 0.0085  194 TYR A CD1 
1631 C  CD2 . TYR A 193 ? 0.0964 0.0983 0.1036 0.0130  -0.0203 -0.0054 194 TYR A CD2 
1632 C  CE1 . TYR A 193 ? 0.0974 0.0899 0.1058 0.0118  -0.0065 0.0118  194 TYR A CE1 
1633 C  CE2 . TYR A 193 ? 0.1066 0.0966 0.0984 0.0076  -0.0060 -0.0044 194 TYR A CE2 
1634 C  CZ  . TYR A 193 ? 0.0943 0.0807 0.0913 0.0175  -0.0087 -0.0049 194 TYR A CZ  
1635 O  OH  . TYR A 193 ? 0.0982 0.0925 0.0957 0.0071  -0.0043 -0.0046 194 TYR A OH  
1636 N  N   . PRO A 194 ? 0.0952 0.1111 0.0868 0.0062  -0.0126 -0.0068 195 PRO A N   
1637 C  CA  . PRO A 194 ? 0.1090 0.0935 0.0970 0.0027  -0.0037 -0.0184 195 PRO A CA  
1638 C  C   . PRO A 194 ? 0.0909 0.0961 0.0922 -0.0017 -0.0173 -0.0108 195 PRO A C   
1639 O  O   . PRO A 194 ? 0.1118 0.1172 0.0873 0.0148  -0.0132 -0.0046 195 PRO A O   
1640 C  CB  . PRO A 194 ? 0.1262 0.1217 0.1093 -0.0010 -0.0093 -0.0270 195 PRO A CB  
1641 C  CG  . PRO A 194 ? 0.1298 0.1396 0.1028 -0.0116 -0.0006 -0.0249 195 PRO A CG  
1642 C  CD  . PRO A 194 ? 0.1279 0.1626 0.0842 -0.0116 -0.0063 -0.0099 195 PRO A CD  
1643 N  N   . GLY A 195 ? 0.0935 0.0909 0.0901 0.0062  -0.0089 -0.0121 196 GLY A N   
1644 C  CA  . GLY A 195 ? 0.0958 0.0869 0.0970 0.0049  -0.0027 -0.0118 196 GLY A CA  
1645 C  C   . GLY A 195 ? 0.0939 0.0868 0.0912 -0.0020 -0.0093 -0.0151 196 GLY A C   
1646 O  O   . GLY A 195 ? 0.1048 0.0886 0.1022 -0.0019 -0.0037 -0.0137 196 GLY A O   
1647 N  N   . SER A 196 ? 0.0812 0.0901 0.0872 -0.0015 -0.0080 -0.0098 197 SER A N   
1648 C  CA  . SER A 196 ? 0.0842 0.0958 0.1010 -0.0116 0.0010  -0.0147 197 SER A CA  
1649 C  C   . SER A 196 ? 0.0755 0.0773 0.0979 0.0019  -0.0062 -0.0035 197 SER A C   
1650 O  O   . SER A 196 ? 0.0768 0.0905 0.1000 -0.0048 -0.0054 -0.0100 197 SER A O   
1651 C  CB  . SER A 196 ? 0.0819 0.0969 0.1212 -0.0088 -0.0021 -0.0221 197 SER A CB  
1652 O  OG  . SER A 196 ? 0.0790 0.0879 0.1201 -0.0003 -0.0051 -0.0131 197 SER A OG  
1653 N  N   . LEU A 197 ? 0.0794 0.0859 0.0958 -0.0048 0.0003  -0.0109 198 LEU A N   
1654 C  CA  . LEU A 197 ? 0.0888 0.0891 0.0986 0.0003  0.0020  -0.0041 198 LEU A CA  
1655 C  C   . LEU A 197 ? 0.0723 0.0917 0.1010 -0.0031 0.0103  -0.0057 198 LEU A C   
1656 O  O   . LEU A 197 ? 0.0773 0.0988 0.1162 -0.0046 -0.0030 -0.0164 198 LEU A O   
1657 C  CB  . LEU A 197 ? 0.0998 0.0940 0.1180 -0.0020 0.0121  -0.0055 198 LEU A CB  
1658 C  CG  . LEU A 197 ? 0.1049 0.1034 0.1196 -0.0108 0.0104  0.0030  198 LEU A CG  
1659 C  CD1 . LEU A 197 ? 0.1448 0.1129 0.1469 -0.0299 -0.0046 0.0164  198 LEU A CD1 
1660 C  CD2 . LEU A 197 ? 0.1111 0.1185 0.1521 0.0126  0.0154  0.0255  198 LEU A CD2 
1661 N  N   . THR A 198 ? 0.0895 0.0798 0.1018 -0.0026 -0.0040 -0.0182 199 THR A N   
1662 C  CA  . THR A 198 ? 0.0737 0.0890 0.1430 -0.0087 0.0107  -0.0182 199 THR A CA  
1663 C  C   . THR A 198 ? 0.0693 0.0992 0.1253 -0.0071 -0.0083 -0.0148 199 THR A C   
1664 O  O   . THR A 198 ? 0.0803 0.1079 0.1538 -0.0008 0.0098  -0.0166 199 THR A O   
1665 C  CB  . THR A 198 ? 0.0938 0.0922 0.1022 -0.0108 -0.0012 -0.0109 199 THR A CB  
1666 O  OG1 . THR A 198 ? 0.0978 0.0929 0.0962 -0.0080 -0.0063 0.0043  199 THR A OG1 
1667 C  CG2 . THR A 198 ? 0.0918 0.1052 0.1093 -0.0071 0.0028  -0.0057 199 THR A CG2 
1668 N  N   . THR A 199 ? 0.0904 0.1107 0.1185 -0.0124 0.0161  -0.0160 200 THR A N   
1669 C  CA  . THR A 199 ? 0.1222 0.1203 0.1397 -0.0183 0.0284  -0.0263 200 THR A CA  
1670 C  C   . THR A 199 ? 0.0978 0.1152 0.1398 -0.0197 0.0159  -0.0187 200 THR A C   
1671 O  O   . THR A 199 ? 0.0938 0.1104 0.1356 -0.0170 0.0104  -0.0251 200 THR A O   
1672 C  CB  . THR A 199 ? 0.1404 0.1474 0.1347 -0.0258 0.0148  0.0032  200 THR A CB  
1673 O  OG1 . THR A 199 ? 0.1715 0.1676 0.1536 -0.0388 0.0097  -0.0026 200 THR A OG1 
1674 C  CG2 . THR A 199 ? 0.1336 0.1293 0.1705 -0.0247 0.0044  -0.0273 200 THR A CG2 
1675 N  N   . PRO A 200 ? 0.0992 0.1251 0.1439 -0.0102 0.0229  -0.0093 201 PRO A N   
1676 C  CA  . PRO A 200 ? 0.0904 0.1410 0.1599 -0.0353 0.0168  -0.0071 201 PRO A CA  
1677 C  C   . PRO A 200 ? 0.1020 0.1413 0.1416 -0.0220 0.0251  -0.0156 201 PRO A C   
1678 O  O   . PRO A 200 ? 0.1350 0.1457 0.1365 -0.0309 0.0082  -0.0003 201 PRO A O   
1679 C  CB  . PRO A 200 ? 0.0956 0.1600 0.1870 -0.0160 0.0197  -0.0049 201 PRO A CB  
1680 C  CG  . PRO A 200 ? 0.1158 0.1550 0.1682 -0.0060 0.0186  -0.0116 201 PRO A CG  
1681 C  CD  . PRO A 200 ? 0.1137 0.1430 0.1767 0.0024  0.0217  -0.0353 201 PRO A CD  
1682 N  N   . PRO A 201 ? 0.0956 0.1446 0.1424 -0.0273 0.0137  -0.0020 202 PRO A N   
1683 C  CA  . PRO A 201 ? 0.1190 0.1427 0.1510 -0.0282 0.0132  -0.0103 202 PRO A CA  
1684 C  C   . PRO A 201 ? 0.1019 0.1247 0.1445 -0.0104 -0.0065 -0.0082 202 PRO A C   
1685 O  O   . PRO A 201 ? 0.1113 0.1308 0.1638 -0.0284 0.0041  -0.0115 202 PRO A O   
1686 C  CB  . PRO A 201 ? 0.1541 0.1358 0.1949 -0.0507 0.0108  0.0035  202 PRO A CB  
1687 C  CG  . PRO A 201 ? 0.1537 0.1453 0.1870 -0.0207 0.0052  -0.0052 202 PRO A CG  
1688 C  CD  . PRO A 201 ? 0.1499 0.1312 0.1639 0.0000  0.0010  -0.0060 202 PRO A CD  
1689 N  N   . LEU A 202 ? 0.0873 0.1045 0.1372 -0.0142 0.0114  -0.0092 203 LEU A N   
1690 C  CA  . LEU A 202 ? 0.0822 0.1054 0.1303 -0.0046 0.0032  -0.0205 203 LEU A CA  
1691 C  C   . LEU A 202 ? 0.0820 0.1134 0.1299 -0.0168 0.0080  -0.0043 203 LEU A C   
1692 O  O   . LEU A 202 ? 0.0927 0.1034 0.1339 -0.0068 0.0000  -0.0144 203 LEU A O   
1693 C  CB  . LEU A 202 ? 0.0773 0.1186 0.1543 0.0043  -0.0083 -0.0261 203 LEU A CB  
1694 C  CG  . LEU A 202 ? 0.0794 0.1185 0.1518 0.0024  0.0071  -0.0263 203 LEU A CG  
1695 C  CD1 . LEU A 202 ? 0.0754 0.1460 0.2117 -0.0031 -0.0015 -0.0179 203 LEU A CD1 
1696 C  CD2 . LEU A 202 ? 0.0922 0.1106 0.1618 -0.0085 0.0006  -0.0209 203 LEU A CD2 
1697 N  N   . LEU A 203 ? 0.0958 0.0939 0.1513 -0.0030 0.0032  -0.0163 204 LEU A N   
1698 C  CA  . LEU A 203 ? 0.0974 0.0971 0.1458 -0.0129 0.0003  -0.0197 204 LEU A CA  
1699 C  C   . LEU A 203 ? 0.0935 0.0865 0.1324 -0.0027 -0.0043 -0.0135 204 LEU A C   
1700 O  O   . LEU A 203 ? 0.0975 0.0988 0.1268 -0.0105 -0.0031 -0.0126 204 LEU A O   
1701 C  CB  . LEU A 203 ? 0.1226 0.1030 0.1659 -0.0111 0.0129  0.0063  204 LEU A CB  
1702 C  CG  . LEU A 203 ? 0.1376 0.1190 0.1686 -0.0094 0.0288  -0.0006 204 LEU A CG  
1703 C  CD1 . LEU A 203 ? 0.1833 0.1145 0.2187 0.0063  0.0384  0.0344  204 LEU A CD1 
1704 C  CD2 . LEU A 203 ? 0.1486 0.1737 0.2619 -0.0608 0.0163  -0.0027 204 LEU A CD2 
1705 N  N   . GLU A 204 ? 0.0879 0.1052 0.1365 -0.0074 -0.0051 -0.0192 205 GLU A N   
1706 C  CA  . GLU A 204 ? 0.1208 0.1067 0.1308 -0.0074 -0.0161 -0.0294 205 GLU A CA  
1707 C  C   . GLU A 204 ? 0.0997 0.1020 0.1344 -0.0131 -0.0148 -0.0313 205 GLU A C   
1708 O  O   . GLU A 204 ? 0.1281 0.1509 0.1438 0.0205  -0.0214 -0.0562 205 GLU A O   
1709 C  CB  . GLU A 204 ? 0.1131 0.1282 0.1412 0.0032  -0.0361 -0.0175 205 GLU A CB  
1710 C  CG  . GLU A 204 ? 0.1226 0.1167 0.1572 -0.0013 -0.0307 -0.0263 205 GLU A CG  
1711 C  CD  . GLU A 204 ? 0.1315 0.1295 0.1448 -0.0024 -0.0295 -0.0368 205 GLU A CD  
1712 O  OE1 . GLU A 204 ? 0.1402 0.1576 0.2027 0.0144  -0.0675 -0.0509 205 GLU A OE1 
1713 O  OE2 . GLU A 204 ? 0.1297 0.1358 0.1662 -0.0080 -0.0379 -0.0177 205 GLU A OE2 
1714 N  N   . CYS A 205 ? 0.1034 0.0927 0.1243 -0.0113 -0.0118 -0.0188 206 CYS A N   
1715 C  CA  . CYS A 205 ? 0.0878 0.0904 0.1305 -0.0066 -0.0113 -0.0059 206 CYS A CA  
1716 C  C   . CYS A 205 ? 0.0971 0.0905 0.1176 0.0074  -0.0120 -0.0104 206 CYS A C   
1717 O  O   . CYS A 205 ? 0.1102 0.0887 0.1586 -0.0005 -0.0232 -0.0013 206 CYS A O   
1718 C  CB  . CYS A 205 ? 0.1268 0.1022 0.1261 -0.0174 0.0083  -0.0038 206 CYS A CB  
1719 S  SG  . CYS A 205 ? 0.1398 0.1034 0.1240 -0.0003 -0.0052 -0.0070 206 CYS A SG  
1720 N  N   . VAL A 206 ? 0.0960 0.0780 0.1113 0.0003  -0.0104 -0.0003 207 VAL A N   
1721 C  CA  . VAL A 206 ? 0.0925 0.0878 0.1036 -0.0049 0.0003  -0.0003 207 VAL A CA  
1722 C  C   . VAL A 206 ? 0.0913 0.0773 0.1113 0.0044  -0.0155 -0.0041 207 VAL A C   
1723 O  O   . VAL A 206 ? 0.1067 0.1027 0.1186 0.0094  -0.0103 0.0163  207 VAL A O   
1724 C  CB  . VAL A 206 ? 0.0901 0.0952 0.1244 -0.0038 -0.0049 -0.0031 207 VAL A CB  
1725 C  CG1 . VAL A 206 ? 0.0806 0.0989 0.1159 0.0013  -0.0125 -0.0027 207 VAL A CG1 
1726 C  CG2 . VAL A 206 ? 0.0957 0.1049 0.1287 -0.0001 0.0093  -0.0120 207 VAL A CG2 
1727 N  N   . THR A 207 ? 0.0944 0.0724 0.1005 0.0000  -0.0031 -0.0028 208 THR A N   
1728 C  CA  . THR A 207 ? 0.0944 0.0913 0.0974 0.0037  -0.0007 -0.0063 208 THR A CA  
1729 C  C   . THR A 207 ? 0.0983 0.0878 0.0869 0.0005  -0.0026 0.0030  208 THR A C   
1730 O  O   . THR A 207 ? 0.1018 0.0868 0.1054 0.0096  -0.0142 0.0027  208 THR A O   
1731 C  CB  . THR A 207 ? 0.1216 0.0856 0.1158 0.0028  0.0063  -0.0109 208 THR A CB  
1732 O  OG1 . THR A 207 ? 0.1253 0.1040 0.1290 0.0051  0.0060  -0.0252 208 THR A OG1 
1733 C  CG2 . THR A 207 ? 0.1239 0.1116 0.1381 0.0003  0.0157  -0.0046 208 THR A CG2 
1734 N  N   . TRP A 208 ? 0.0926 0.0747 0.0913 0.0093  -0.0041 0.0010  209 TRP A N   
1735 C  CA  . TRP A 208 ? 0.0808 0.0843 0.0868 0.0054  -0.0046 -0.0087 209 TRP A CA  
1736 C  C   . TRP A 208 ? 0.0856 0.0793 0.0833 0.0088  -0.0038 -0.0041 209 TRP A C   
1737 O  O   . TRP A 208 ? 0.0926 0.1034 0.0873 0.0015  0.0032  0.0031  209 TRP A O   
1738 C  CB  . TRP A 208 ? 0.0900 0.0804 0.1000 0.0076  -0.0091 0.0059  209 TRP A CB  
1739 C  CG  . TRP A 208 ? 0.0715 0.0806 0.0932 0.0125  -0.0046 0.0046  209 TRP A CG  
1740 C  CD1 . TRP A 208 ? 0.0873 0.0837 0.1102 0.0010  -0.0074 0.0041  209 TRP A CD1 
1741 C  CD2 . TRP A 208 ? 0.0710 0.0749 0.0986 0.0082  -0.0071 0.0027  209 TRP A CD2 
1742 N  NE1 . TRP A 208 ? 0.0926 0.0960 0.1077 -0.0081 -0.0003 -0.0035 209 TRP A NE1 
1743 C  CE2 . TRP A 208 ? 0.0887 0.0763 0.1057 0.0140  -0.0074 -0.0032 209 TRP A CE2 
1744 C  CE3 . TRP A 208 ? 0.0900 0.0780 0.0883 0.0065  -0.0118 -0.0010 209 TRP A CE3 
1745 C  CZ2 . TRP A 208 ? 0.0942 0.1034 0.1075 0.0258  0.0054  -0.0015 209 TRP A CZ2 
1746 C  CZ3 . TRP A 208 ? 0.1097 0.0912 0.1022 0.0227  -0.0035 0.0000  209 TRP A CZ3 
1747 C  CH2 . TRP A 208 ? 0.1163 0.0970 0.1088 0.0189  0.0015  0.0015  209 TRP A CH2 
1748 N  N   . ILE A 209 ? 0.0807 0.0851 0.0863 0.0012  -0.0043 0.0027  210 ILE A N   
1749 C  CA  . ILE A 209 ? 0.0728 0.0918 0.0996 -0.0013 0.0007  -0.0008 210 ILE A CA  
1750 C  C   . ILE A 209 ? 0.0711 0.0947 0.0909 -0.0038 -0.0041 0.0049  210 ILE A C   
1751 O  O   . ILE A 209 ? 0.1237 0.0892 0.0967 -0.0017 -0.0087 0.0030  210 ILE A O   
1752 C  CB  . ILE A 209 ? 0.0754 0.0939 0.1275 -0.0007 0.0024  0.0010  210 ILE A CB  
1753 C  CG1 . ILE A 209 ? 0.0894 0.1016 0.1727 0.0088  -0.0017 -0.0167 210 ILE A CG1 
1754 C  CG2 . ILE A 209 ? 0.0759 0.1342 0.1520 0.0118  0.0020  0.0055  210 ILE A CG2 
1755 C  CD1 . ILE A 209 ? 0.1177 0.1088 0.2163 0.0230  -0.0001 0.0109  210 ILE A CD1 
1756 N  N   . VAL A 210 ? 0.0815 0.0813 0.0970 0.0001  -0.0008 0.0060  211 VAL A N   
1757 C  CA  . VAL A 210 ? 0.0794 0.0894 0.0869 -0.0032 -0.0017 0.0028  211 VAL A CA  
1758 C  C   . VAL A 210 ? 0.0918 0.0866 0.0943 0.0057  0.0027  0.0027  211 VAL A C   
1759 O  O   . VAL A 210 ? 0.0973 0.1022 0.0939 -0.0114 0.0024  0.0055  211 VAL A O   
1760 C  CB  . VAL A 210 ? 0.0788 0.0960 0.1244 0.0028  -0.0008 0.0037  211 VAL A CB  
1761 C  CG1 . VAL A 210 ? 0.1176 0.1010 0.1342 0.0043  -0.0010 -0.0020 211 VAL A CG1 
1762 C  CG2 . VAL A 210 ? 0.1079 0.1171 0.1308 -0.0114 0.0078  0.0032  211 VAL A CG2 
1763 N  N   . LEU A 211 ? 0.0800 0.1045 0.1101 -0.0093 -0.0073 0.0063  212 LEU A N   
1764 C  CA  . LEU A 211 ? 0.0806 0.1106 0.1306 -0.0049 -0.0082 0.0021  212 LEU A CA  
1765 C  C   . LEU A 211 ? 0.0803 0.1158 0.1120 -0.0194 -0.0100 0.0041  212 LEU A C   
1766 O  O   . LEU A 211 ? 0.0926 0.1181 0.1176 -0.0125 -0.0038 0.0074  212 LEU A O   
1767 C  CB  . LEU A 211 ? 0.0879 0.1187 0.1483 -0.0200 -0.0239 0.0153  212 LEU A CB  
1768 C  CG  . LEU A 211 ? 0.1034 0.1265 0.1476 -0.0104 -0.0157 0.0163  212 LEU A CG  
1769 C  CD1 . LEU A 211 ? 0.1190 0.1726 0.1717 -0.0287 -0.0454 0.0324  212 LEU A CD1 
1770 C  CD2 . LEU A 211 ? 0.1146 0.1468 0.1735 0.0153  -0.0043 0.0162  212 LEU A CD2 
1771 N  N   A LYS A 212 ? 0.1032 0.1222 0.1286 -0.0280 -0.0020 0.0146  213 LYS A N   
1772 N  N   B LYS A 212 ? 0.1034 0.1222 0.1287 -0.0280 -0.0020 0.0146  213 LYS A N   
1773 C  CA  A LYS A 212 ? 0.1231 0.1234 0.1380 -0.0252 -0.0083 0.0230  213 LYS A CA  
1774 C  CA  B LYS A 212 ? 0.1230 0.1235 0.1381 -0.0252 -0.0085 0.0230  213 LYS A CA  
1775 C  C   A LYS A 212 ? 0.1136 0.1023 0.1380 -0.0122 -0.0068 0.0259  213 LYS A C   
1776 C  C   B LYS A 212 ? 0.1136 0.1023 0.1380 -0.0122 -0.0068 0.0259  213 LYS A C   
1777 O  O   A LYS A 212 ? 0.1350 0.1201 0.1876 -0.0055 -0.0390 0.0260  213 LYS A O   
1778 O  O   B LYS A 212 ? 0.1350 0.1201 0.1876 -0.0054 -0.0388 0.0261  213 LYS A O   
1779 C  CB  A LYS A 212 ? 0.1740 0.1749 0.1430 -0.0714 0.0107  0.0355  213 LYS A CB  
1780 C  CB  B LYS A 212 ? 0.1735 0.1756 0.1436 -0.0697 0.0110  0.0366  213 LYS A CB  
1781 C  CG  A LYS A 212 ? 0.2280 0.1949 0.2092 -0.0406 -0.0006 0.0509  213 LYS A CG  
1782 C  CG  B LYS A 212 ? 0.2243 0.1958 0.2115 -0.0244 0.0078  0.0482  213 LYS A CG  
1783 C  CD  A LYS A 212 ? 0.3630 0.2971 0.2430 -0.1120 0.0599  0.0195  213 LYS A CD  
1784 C  CD  B LYS A 212 ? 0.2843 0.2401 0.2423 -0.0984 0.0480  0.0463  213 LYS A CD  
1785 C  CE  A LYS A 212 ? 0.3888 0.3339 0.3129 -0.1891 0.0560  0.1412  213 LYS A CE  
1786 C  CE  B LYS A 212 ? 0.1982 0.4975 0.4305 -0.1828 0.1362  -0.1129 213 LYS A CE  
1787 N  NZ  A LYS A 212 ? 0.5313 0.4520 0.3260 -0.0957 0.1432  0.0790  213 LYS A NZ  
1788 N  NZ  B LYS A 212 ? 0.5738 0.3217 0.2991 -0.0239 0.0913  0.0505  213 LYS A NZ  
1789 N  N   . GLU A 213 ? 0.0960 0.1194 0.1323 -0.0098 -0.0192 0.0148  214 GLU A N   
1790 C  CA  . GLU A 213 ? 0.1002 0.1198 0.1513 -0.0238 -0.0113 0.0078  214 GLU A CA  
1791 C  C   . GLU A 213 ? 0.0949 0.1023 0.1493 -0.0162 -0.0171 0.0110  214 GLU A C   
1792 O  O   . GLU A 213 ? 0.1084 0.1093 0.1488 -0.0102 -0.0175 0.0247  214 GLU A O   
1793 C  CB  . GLU A 213 ? 0.0899 0.1439 0.1644 -0.0193 -0.0116 0.0244  214 GLU A CB  
1794 C  CG  . GLU A 213 ? 0.1316 0.1633 0.2107 -0.0467 -0.0447 0.0216  214 GLU A CG  
1795 C  CD  . GLU A 213 ? 0.1455 0.2624 0.2448 -0.0861 -0.0500 0.0252  214 GLU A CD  
1796 O  OE1 . GLU A 213 ? 0.1425 0.1871 0.3246 -0.0280 -0.0489 0.0461  214 GLU A OE1 
1797 O  OE2 . GLU A 213 ? 0.1948 0.6528 0.4201 -0.0555 -0.0606 -0.1884 214 GLU A OE2 
1798 N  N   . PRO A 214 ? 0.1250 0.1043 0.1365 -0.0149 -0.0131 0.0114  215 PRO A N   
1799 C  CA  . PRO A 214 ? 0.1203 0.1174 0.1420 -0.0052 -0.0089 0.0041  215 PRO A CA  
1800 C  C   . PRO A 214 ? 0.1158 0.1054 0.1425 -0.0197 -0.0239 -0.0116 215 PRO A C   
1801 O  O   . PRO A 214 ? 0.1352 0.1723 0.1651 -0.0425 -0.0394 0.0142  215 PRO A O   
1802 C  CB  . PRO A 214 ? 0.1257 0.1118 0.1697 -0.0074 -0.0175 -0.0054 215 PRO A CB  
1803 C  CG  . PRO A 214 ? 0.1888 0.1724 0.2249 -0.0230 -0.0008 0.0082  215 PRO A CG  
1804 C  CD  . PRO A 214 ? 0.1612 0.1031 0.1833 -0.0048 0.0141  0.0280  215 PRO A CD  
1805 N  N   . ILE A 215 ? 0.1283 0.1185 0.1273 -0.0073 -0.0322 -0.0113 216 ILE A N   
1806 C  CA  . ILE A 215 ? 0.1418 0.1192 0.1359 -0.0063 -0.0412 -0.0272 216 ILE A CA  
1807 C  C   . ILE A 215 ? 0.1138 0.1137 0.1486 -0.0113 -0.0266 -0.0074 216 ILE A C   
1808 O  O   . ILE A 215 ? 0.1297 0.1154 0.1852 -0.0126 -0.0267 -0.0197 216 ILE A O   
1809 C  CB  . ILE A 215 ? 0.1517 0.1097 0.1469 0.0085  -0.0208 -0.0115 216 ILE A CB  
1810 C  CG1 . ILE A 215 ? 0.1958 0.1201 0.1363 -0.0098 -0.0474 0.0031  216 ILE A CG1 
1811 C  CG2 . ILE A 215 ? 0.2073 0.1255 0.1829 0.0269  -0.0463 -0.0199 216 ILE A CG2 
1812 C  CD1 . ILE A 215 ? 0.2764 0.1439 0.1518 -0.0120 -0.0463 0.0221  216 ILE A CD1 
1813 N  N   A SER A 216 ? 0.1140 0.1361 0.1597 -0.0104 -0.0372 -0.0102 217 SER A N   
1814 N  N   B SER A 216 ? 0.1608 0.1140 0.1617 -0.0024 -0.0482 -0.0307 217 SER A N   
1815 C  CA  A SER A 216 ? 0.1444 0.1324 0.1473 0.0127  -0.0524 -0.0017 217 SER A CA  
1816 C  CA  B SER A 216 ? 0.1740 0.1147 0.1634 -0.0320 -0.0241 -0.0482 217 SER A CA  
1817 C  C   A SER A 216 ? 0.1455 0.0891 0.1635 -0.0162 -0.0441 -0.0186 217 SER A C   
1818 C  C   B SER A 216 ? 0.1564 0.0996 0.1763 -0.0081 -0.0361 -0.0121 217 SER A C   
1819 O  O   A SER A 216 ? 0.1723 0.1212 0.1526 -0.0070 -0.0593 0.0000  217 SER A O   
1820 O  O   B SER A 216 ? 0.1723 0.1494 0.1704 0.0175  -0.0386 -0.0057 217 SER A O   
1821 C  CB  A SER A 216 ? 0.2671 0.0786 0.1493 -0.0216 -0.0155 -0.0271 217 SER A CB  
1822 C  CB  B SER A 216 ? 0.2262 0.1888 0.2384 -0.0776 0.0173  -0.0187 217 SER A CB  
1823 O  OG  A SER A 216 ? 0.1775 0.1519 0.1559 -0.0348 -0.0174 -0.0028 217 SER A OG  
1824 O  OG  B SER A 216 ? 0.2707 0.2164 0.2541 0.0249  -0.0060 -0.0093 217 SER A OG  
1825 N  N   . VAL A 217 ? 0.1528 0.1129 0.1544 -0.0143 -0.0412 -0.0232 218 VAL A N   
1826 C  CA  . VAL A 217 ? 0.1937 0.1129 0.1374 -0.0208 -0.0394 -0.0190 218 VAL A CA  
1827 C  C   . VAL A 217 ? 0.1539 0.1104 0.1463 -0.0199 -0.0390 -0.0086 218 VAL A C   
1828 O  O   . VAL A 217 ? 0.1862 0.1181 0.1533 -0.0205 -0.0375 -0.0121 218 VAL A O   
1829 C  CB  . VAL A 217 ? 0.1817 0.0992 0.1837 -0.0254 -0.0557 -0.0245 218 VAL A CB  
1830 C  CG1 . VAL A 217 ? 0.2201 0.1070 0.1777 -0.0313 -0.0423 -0.0322 218 VAL A CG1 
1831 C  CG2 . VAL A 217 ? 0.1636 0.1354 0.2319 -0.0285 -0.0348 -0.0262 218 VAL A CG2 
1832 N  N   . SER A 218 ? 0.1900 0.1032 0.1472 -0.0179 -0.0410 -0.0263 219 SER A N   
1833 C  CA  . SER A 218 ? 0.1925 0.1093 0.1723 -0.0317 -0.0324 -0.0222 219 SER A CA  
1834 C  C   . SER A 218 ? 0.1852 0.1023 0.1508 -0.0241 -0.0210 -0.0125 219 SER A C   
1835 O  O   . SER A 218 ? 0.1886 0.1146 0.1638 -0.0206 -0.0320 -0.0119 219 SER A O   
1836 C  CB  . SER A 218 ? 0.2182 0.1278 0.1552 -0.0115 -0.0474 -0.0138 219 SER A CB  
1837 O  OG  . SER A 218 ? 0.2634 0.1372 0.1590 -0.0364 -0.0538 -0.0144 219 SER A OG  
1838 N  N   A SER A 219 ? 0.2104 0.1025 0.1887 -0.0194 -0.0315 -0.0046 220 SER A N   
1839 N  N   B SER A 219 ? 0.1967 0.1075 0.1808 -0.0122 -0.0370 -0.0074 220 SER A N   
1840 C  CA  A SER A 219 ? 0.2126 0.0907 0.1703 -0.0373 -0.0394 0.0017  220 SER A CA  
1841 C  CA  B SER A 219 ? 0.2078 0.1281 0.1774 -0.0127 -0.0516 -0.0111 220 SER A CA  
1842 C  C   A SER A 219 ? 0.2213 0.1081 0.1912 -0.0254 -0.0201 -0.0055 220 SER A C   
1843 C  C   B SER A 219 ? 0.2254 0.1169 0.1953 -0.0430 -0.0320 -0.0261 220 SER A C   
1844 O  O   A SER A 219 ? 0.2100 0.0995 0.2270 -0.0120 -0.0093 0.0240  220 SER A O   
1845 O  O   B SER A 219 ? 0.1924 0.1318 0.2347 -0.0088 -0.0051 -0.0361 220 SER A O   
1846 C  CB  A SER A 219 ? 0.2264 0.0807 0.2327 -0.0260 -0.0361 0.0588  220 SER A CB  
1847 C  CB  B SER A 219 ? 0.2198 0.1381 0.2248 -0.0315 -0.0081 -0.0342 220 SER A CB  
1848 O  OG  A SER A 219 ? 0.2383 0.1005 0.2311 0.0120  -0.0197 -0.0105 220 SER A OG  
1849 O  OG  B SER A 219 ? 0.2588 0.1365 0.2258 0.0280  -0.0742 -0.0074 220 SER A OG  
1850 N  N   . GLU A 220 ? 0.2405 0.1149 0.1587 -0.0222 -0.0238 -0.0229 221 GLU A N   
1851 C  CA  . GLU A 220 ? 0.2779 0.1413 0.1776 -0.0373 -0.0277 -0.0274 221 GLU A CA  
1852 C  C   . GLU A 220 ? 0.2369 0.1244 0.1433 -0.0006 -0.0017 -0.0104 221 GLU A C   
1853 O  O   . GLU A 220 ? 0.2782 0.1572 0.1711 0.0034  0.0161  -0.0153 221 GLU A O   
1854 C  CB  . GLU A 220 ? 0.3382 0.1752 0.1726 -0.0326 -0.0337 -0.0513 221 GLU A CB  
1855 C  CG  . GLU A 220 ? 0.4164 0.2075 0.2547 -0.0156 -0.1023 -0.0843 221 GLU A CG  
1856 C  CD  . GLU A 220 ? 0.4560 0.1733 0.3519 -0.0258 -0.0533 -0.1030 221 GLU A CD  
1857 O  OE1 . GLU A 220 ? 0.3679 0.2116 0.3633 -0.1115 -0.0020 -0.0916 221 GLU A OE1 
1858 O  OE2 . GLU A 220 ? 1.3536 0.1855 0.8210 -0.1864 -0.0102 -0.2210 221 GLU A OE2 
1859 N  N   . GLN A 221 ? 0.2187 0.1118 0.1668 -0.0212 -0.0252 -0.0175 222 GLN A N   
1860 C  CA  . GLN A 221 ? 0.2142 0.1045 0.1677 -0.0157 -0.0498 -0.0086 222 GLN A CA  
1861 C  C   . GLN A 221 ? 0.1831 0.1225 0.1414 -0.0119 -0.0115 0.0059  222 GLN A C   
1862 O  O   . GLN A 221 ? 0.2337 0.1456 0.1409 -0.0361 -0.0174 0.0065  222 GLN A O   
1863 C  CB  . GLN A 221 ? 0.2309 0.1155 0.1510 -0.0184 -0.0452 -0.0195 222 GLN A CB  
1864 C  CG  . GLN A 221 ? 0.2273 0.1307 0.1441 -0.0423 -0.0684 -0.0043 222 GLN A CG  
1865 C  CD  . GLN A 221 ? 0.2312 0.1149 0.1486 -0.0137 -0.0299 -0.0275 222 GLN A CD  
1866 O  OE1 . GLN A 221 ? 0.2009 0.1196 0.1544 -0.0092 -0.0366 -0.0066 222 GLN A OE1 
1867 N  NE2 . GLN A 221 ? 0.2152 0.1196 0.1821 -0.0229 -0.0634 0.0027  222 GLN A NE2 
1868 N  N   . VAL A 222 ? 0.2069 0.1222 0.1518 -0.0285 -0.0329 0.0076  223 VAL A N   
1869 C  CA  . VAL A 222 ? 0.2018 0.1551 0.1667 -0.0293 -0.0249 0.0071  223 VAL A CA  
1870 C  C   . VAL A 222 ? 0.1929 0.1280 0.1794 -0.0178 -0.0200 0.0023  223 VAL A C   
1871 O  O   . VAL A 222 ? 0.1969 0.1544 0.1625 -0.0309 -0.0082 0.0003  223 VAL A O   
1872 C  CB  . VAL A 222 ? 0.2081 0.1837 0.2001 -0.0315 -0.0505 0.0445  223 VAL A CB  
1873 C  CG1 . VAL A 222 ? 0.2581 0.1911 0.2742 -0.0590 -0.0458 0.0675  223 VAL A CG1 
1874 C  CG2 . VAL A 222 ? 0.3068 0.1807 0.2283 -0.0644 -0.0943 0.0137  223 VAL A CG2 
1875 N  N   . LEU A 223 ? 0.2012 0.1401 0.1885 -0.0201 -0.0093 -0.0068 224 LEU A N   
1876 C  CA  . LEU A 223 ? 0.2406 0.1395 0.2559 -0.0476 0.0264  0.0006  224 LEU A CA  
1877 C  C   . LEU A 223 ? 0.2336 0.1419 0.1902 -0.0277 0.0082  -0.0357 224 LEU A C   
1878 O  O   . LEU A 223 ? 0.2243 0.1865 0.1969 -0.0262 -0.0015 -0.0260 224 LEU A O   
1879 C  CB  . LEU A 223 ? 0.3030 0.1422 0.2793 -0.0217 0.0397  -0.0331 224 LEU A CB  
1880 C  CG  . LEU A 223 ? 0.3828 0.1784 0.2667 -0.0006 0.0196  -0.0272 224 LEU A CG  
1881 C  CD1 . LEU A 223 ? 0.3472 0.1906 0.4028 -0.0303 -0.0239 -0.0205 224 LEU A CD1 
1882 C  CD2 . LEU A 223 ? 0.3758 0.2969 0.3603 0.0184  -0.0175 -0.1477 224 LEU A CD2 
1883 N  N   . LYS A 224 ? 0.2362 0.1477 0.1553 -0.0099 -0.0164 -0.0205 225 LYS A N   
1884 C  CA  . LYS A 224 ? 0.2395 0.1889 0.1513 -0.0500 0.0032  -0.0217 225 LYS A CA  
1885 C  C   . LYS A 224 ? 0.2383 0.1516 0.1215 -0.0252 -0.0333 0.0109  225 LYS A C   
1886 O  O   . LYS A 224 ? 0.2498 0.1680 0.1289 -0.0386 -0.0032 -0.0214 225 LYS A O   
1887 C  CB  . LYS A 224 ? 0.2481 0.2617 0.1608 -0.0458 -0.0397 0.0076  225 LYS A CB  
1888 C  CG  . LYS A 224 ? 0.2662 0.3125 0.2268 -0.0210 -0.0646 -0.0062 225 LYS A CG  
1889 C  CD  . LYS A 224 ? 0.4296 0.4873 0.2885 0.1209  -0.0891 -0.1808 225 LYS A CD  
1890 C  CE  . LYS A 224 ? 0.4492 0.6370 0.3102 0.1395  -0.1024 -0.2883 225 LYS A CE  
1891 N  NZ  . LYS A 224 ? 0.8004 1.4730 0.7549 0.5562  -0.1709 -0.3059 225 LYS A NZ  
1892 N  N   . PHE A 225 ? 0.2115 0.1413 0.1225 -0.0178 -0.0115 -0.0044 226 PHE A N   
1893 C  CA  . PHE A 225 ? 0.2056 0.1389 0.1395 -0.0285 -0.0060 0.0001  226 PHE A CA  
1894 C  C   . PHE A 225 ? 0.2202 0.1377 0.1156 -0.0401 -0.0063 0.0054  226 PHE A C   
1895 O  O   . PHE A 225 ? 0.2002 0.1573 0.1194 -0.0234 0.0146  -0.0250 226 PHE A O   
1896 C  CB  . PHE A 225 ? 0.2085 0.1198 0.1163 -0.0305 0.0031  0.0048  226 PHE A CB  
1897 C  CG  . PHE A 225 ? 0.1987 0.1224 0.1400 -0.0304 0.0023  -0.0270 226 PHE A CG  
1898 C  CD1 . PHE A 225 ? 0.2337 0.1720 0.1516 -0.0142 -0.0153 -0.0115 226 PHE A CD1 
1899 C  CD2 . PHE A 225 ? 0.2161 0.1724 0.1479 -0.0285 0.0065  -0.0362 226 PHE A CD2 
1900 C  CE1 . PHE A 225 ? 0.2483 0.2018 0.1842 0.0154  -0.0166 -0.0275 226 PHE A CE1 
1901 C  CE2 . PHE A 225 ? 0.2040 0.1818 0.1877 -0.0379 -0.0049 -0.0656 226 PHE A CE2 
1902 C  CZ  . PHE A 225 ? 0.1886 0.2194 0.2294 -0.0353 0.0043  -0.0879 226 PHE A CZ  
1903 N  N   . ARG A 226 ? 0.1999 0.1534 0.1160 -0.0259 -0.0035 -0.0085 227 ARG A N   
1904 C  CA  . ARG A 226 ? 0.2187 0.1686 0.1142 -0.0476 -0.0013 -0.0263 227 ARG A CA  
1905 C  C   . ARG A 226 ? 0.2154 0.1588 0.1645 -0.0237 0.0144  -0.0094 227 ARG A C   
1906 O  O   . ARG A 226 ? 0.2280 0.1763 0.1507 -0.0098 0.0027  -0.0136 227 ARG A O   
1907 C  CB  . ARG A 226 ? 0.2416 0.1398 0.1451 -0.0176 0.0087  0.0148  227 ARG A CB  
1908 C  CG  . ARG A 226 ? 0.2046 0.1562 0.1358 -0.0239 0.0076  0.0035  227 ARG A CG  
1909 C  CD  . ARG A 226 ? 0.2627 0.1421 0.1445 -0.0211 -0.0093 0.0041  227 ARG A CD  
1910 N  NE  . ARG A 226 ? 0.2261 0.1254 0.1282 -0.0392 -0.0179 -0.0107 227 ARG A NE  
1911 C  CZ  . ARG A 226 ? 0.2533 0.1571 0.1375 -0.0483 -0.0205 -0.0357 227 ARG A CZ  
1912 N  NH1 . ARG A 226 ? 0.2885 0.1816 0.1861 -0.0665 -0.0362 -0.0687 227 ARG A NH1 
1913 N  NH2 . ARG A 226 ? 0.2671 0.1321 0.1545 -0.0608 -0.0087 -0.0068 227 ARG A NH2 
1914 N  N   . LYS A 227 ? 0.2462 0.1787 0.1106 -0.0256 0.0024  -0.0130 228 LYS A N   
1915 C  CA  . LYS A 227 ? 0.2847 0.1962 0.1159 -0.0821 0.0087  -0.0472 228 LYS A CA  
1916 C  C   . LYS A 227 ? 0.2474 0.1898 0.0982 -0.0068 0.0110  -0.0291 228 LYS A C   
1917 O  O   . LYS A 227 ? 0.3048 0.2148 0.1102 -0.0353 0.0210  -0.0417 228 LYS A O   
1918 C  CB  . LYS A 227 ? 0.2746 0.2502 0.1137 -0.0483 -0.0038 -0.0337 228 LYS A CB  
1919 C  CG  . LYS A 227 ? 0.3267 0.2574 0.1821 -0.1289 0.0043  -0.0634 228 LYS A CG  
1920 C  CD  . LYS A 227 ? 0.4255 0.4144 0.2538 -0.1733 -0.0375 -0.1243 228 LYS A CD  
1921 C  CE  . LYS A 227 ? 0.4034 0.6432 0.3285 -0.0425 -0.0520 -0.1708 228 LYS A CE  
1922 N  NZ  . LYS A 227 ? 0.6247 0.7397 0.7791 0.0337  -0.3048 -0.3639 228 LYS A NZ  
1923 N  N   . LEU A 228 ? 0.2563 0.1556 0.1045 -0.0445 0.0281  -0.0103 229 LEU A N   
1924 C  CA  . LEU A 228 ? 0.2010 0.1942 0.1225 -0.0299 0.0195  -0.0044 229 LEU A CA  
1925 C  C   . LEU A 228 ? 0.2768 0.1658 0.0966 -0.0401 0.0265  -0.0104 229 LEU A C   
1926 O  O   . LEU A 228 ? 0.2302 0.1660 0.1160 -0.0161 0.0234  -0.0210 229 LEU A O   
1927 C  CB  . LEU A 228 ? 0.2444 0.1933 0.1011 -0.0263 0.0102  -0.0194 229 LEU A CB  
1928 C  CG  . LEU A 228 ? 0.2293 0.2093 0.1086 -0.0249 -0.0153 -0.0076 229 LEU A CG  
1929 C  CD1 . LEU A 228 ? 0.2563 0.1797 0.1464 -0.0272 0.0203  -0.0419 229 LEU A CD1 
1930 C  CD2 . LEU A 228 ? 0.3203 0.2138 0.1297 -0.0164 0.0419  0.0174  229 LEU A CD2 
1931 N  N   . ASN A 229 ? 0.2196 0.1812 0.1224 -0.0337 0.0225  -0.0266 230 ASN A N   
1932 C  CA  . ASN A 229 ? 0.2380 0.1782 0.0961 -0.0091 0.0148  -0.0264 230 ASN A CA  
1933 C  C   . ASN A 229 ? 0.2119 0.2032 0.1000 0.0083  0.0255  0.0100  230 ASN A C   
1934 O  O   . ASN A 229 ? 0.2499 0.1700 0.1400 -0.0120 0.0265  -0.0059 230 ASN A O   
1935 C  CB  . ASN A 229 ? 0.2222 0.2135 0.1176 -0.0293 0.0230  -0.0295 230 ASN A CB  
1936 C  CG  . ASN A 229 ? 0.2872 0.2144 0.1014 -0.0333 0.0083  -0.0300 230 ASN A CG  
1937 O  OD1 . ASN A 229 ? 0.3443 0.2347 0.1290 -0.0175 0.0388  -0.0377 230 ASN A OD1 
1938 N  ND2 . ASN A 229 ? 0.2854 0.1975 0.1476 -0.0395 0.0315  -0.0340 230 ASN A ND2 
1939 N  N   . PHE A 230 ? 0.2266 0.1618 0.1274 -0.0386 0.0384  -0.0219 231 PHE A N   
1940 C  CA  . PHE A 230 ? 0.2081 0.1551 0.1243 -0.0275 0.0057  0.0098  231 PHE A CA  
1941 C  C   . PHE A 230 ? 0.2588 0.1548 0.1441 -0.0395 0.0454  -0.0195 231 PHE A C   
1942 O  O   . PHE A 230 ? 0.2660 0.1914 0.1512 -0.0781 0.0584  -0.0220 231 PHE A O   
1943 C  CB  . PHE A 230 ? 0.2090 0.1615 0.1600 -0.0234 0.0359  -0.0142 231 PHE A CB  
1944 C  CG  . PHE A 230 ? 0.1922 0.1580 0.1412 -0.0231 0.0154  -0.0166 231 PHE A CG  
1945 C  CD1 . PHE A 230 ? 0.2413 0.1979 0.1278 -0.0189 0.0362  -0.0219 231 PHE A CD1 
1946 C  CD2 . PHE A 230 ? 0.2398 0.1898 0.1397 0.0113  0.0208  -0.0233 231 PHE A CD2 
1947 C  CE1 . PHE A 230 ? 0.2309 0.1673 0.1561 -0.0383 0.0582  -0.0304 231 PHE A CE1 
1948 C  CE2 . PHE A 230 ? 0.2383 0.1728 0.1325 -0.0129 0.0109  -0.0230 231 PHE A CE2 
1949 C  CZ  . PHE A 230 ? 0.2022 0.1717 0.1334 -0.0320 -0.0027 -0.0174 231 PHE A CZ  
1950 N  N   . ASN A 231 ? 0.2196 0.1972 0.1243 -0.0414 0.0419  -0.0129 232 ASN A N   
1951 C  CA  . ASN A 231 ? 0.2198 0.2117 0.1722 -0.0288 0.0507  -0.0339 232 ASN A CA  
1952 C  C   . ASN A 231 ? 0.1537 0.2327 0.1235 0.0176  0.0154  0.0054  232 ASN A C   
1953 O  O   . ASN A 231 ? 0.2261 0.2108 0.1570 0.0001  0.0406  -0.0109 232 ASN A O   
1954 C  CB  . ASN A 231 ? 0.2205 0.2184 0.2057 -0.0185 0.0710  0.0046  232 ASN A CB  
1955 C  CG  . ASN A 231 ? 0.2073 0.1845 0.1757 0.0149  0.0425  -0.0071 232 ASN A CG  
1956 O  OD1 . ASN A 231 ? 0.3016 0.2002 0.1809 -0.0478 0.0815  -0.0425 232 ASN A OD1 
1957 N  ND2 . ASN A 231 ? 0.2657 0.2773 0.1600 0.0248  0.0395  -0.0043 232 ASN A ND2 
1958 N  N   . GLY A 232 ? 0.3052 0.2078 0.1746 -0.0153 0.0593  0.0125  233 GLY A N   
1959 C  CA  . GLY A 232 ? 0.2904 0.2392 0.1597 0.0252  0.0685  0.0219  233 GLY A CA  
1960 C  C   . GLY A 232 ? 0.1669 0.2237 0.2213 0.0436  0.0013  0.0263  233 GLY A C   
1961 O  O   . GLY A 232 ? 0.2170 0.3109 0.1886 0.0797  0.0566  0.0649  233 GLY A O   
1962 N  N   . GLU A 233 ? 0.2049 0.2609 0.1633 0.0258  0.0370  0.0043  234 GLU A N   
1963 C  CA  . GLU A 233 ? 0.1835 0.2210 0.1643 0.0223  0.0251  0.0044  234 GLU A CA  
1964 C  C   . GLU A 233 ? 0.2228 0.2695 0.1879 0.0318  0.0329  0.0280  234 GLU A C   
1965 O  O   . GLU A 233 ? 0.2470 0.3102 0.1926 -0.0049 0.0285  0.0461  234 GLU A O   
1966 C  CB  . GLU A 233 ? 0.2709 0.2410 0.1576 0.0560  0.0141  0.0305  234 GLU A CB  
1967 C  CG  . GLU A 233 ? 0.2641 0.2608 0.2062 -0.0454 0.0212  0.0322  234 GLU A CG  
1968 C  CD  . GLU A 233 ? 0.2632 0.4208 0.2702 0.1427  0.0066  -0.0204 234 GLU A CD  
1969 O  OE1 . GLU A 233 ? 0.3562 0.3109 0.3223 0.0847  0.0736  0.0597  234 GLU A OE1 
1970 O  OE2 . GLU A 233 ? 0.3661 0.3472 0.3095 -0.0051 -0.0680 0.0068  234 GLU A OE2 
1971 N  N   . GLY A 234 ? 0.2836 0.3433 0.1940 0.0944  0.0386  -0.0017 235 GLY A N   
1972 C  CA  . GLY A 234 ? 0.2789 0.3885 0.1931 0.0454  0.0399  0.0315  235 GLY A CA  
1973 C  C   . GLY A 234 ? 0.2808 0.4821 0.1686 0.0860  0.0236  0.0346  235 GLY A C   
1974 O  O   . GLY A 234 ? 0.2657 0.6090 0.2398 0.0892  0.0601  0.0342  235 GLY A O   
1975 N  N   . GLU A 235 ? 0.2645 0.3112 0.2280 0.0966  0.0432  0.0252  236 GLU A N   
1976 C  CA  . GLU A 235 ? 0.2358 0.2408 0.2265 0.0529  0.0375  0.0032  236 GLU A CA  
1977 C  C   . GLU A 235 ? 0.2843 0.3210 0.2193 0.0280  0.0885  0.0116  236 GLU A C   
1978 O  O   . GLU A 235 ? 0.3148 0.4189 0.2577 0.0575  0.1391  0.0252  236 GLU A O   
1979 C  CB  . GLU A 235 ? 0.3102 0.2606 0.2215 0.0204  0.0899  0.0250  236 GLU A CB  
1980 C  CG  . GLU A 235 ? 0.2936 0.3048 0.2660 -0.0098 0.0979  0.0037  236 GLU A CG  
1981 C  CD  . GLU A 235 ? 0.4652 0.3120 0.3109 -0.1036 0.1067  -0.0096 236 GLU A CD  
1982 O  OE1 . GLU A 235 ? 0.3999 0.3251 0.4915 -0.0971 0.2150  0.0207  236 GLU A OE1 
1983 O  OE2 . GLU A 235 ? 0.6457 0.3826 0.6757 -0.0865 0.3626  0.1502  236 GLU A OE2 
1984 N  N   . PRO A 236 ? 0.2552 0.3083 0.2161 0.0882  0.1094  0.0662  237 PRO A N   
1985 C  CA  . PRO A 236 ? 0.2470 0.2947 0.2807 0.0710  0.0910  0.0838  237 PRO A CA  
1986 C  C   . PRO A 236 ? 0.3220 0.3119 0.1710 -0.0427 0.1138  -0.0241 237 PRO A C   
1987 O  O   . PRO A 236 ? 0.2849 0.3163 0.2049 -0.0306 0.1018  -0.0296 237 PRO A O   
1988 C  CB  . PRO A 236 ? 0.2226 0.4036 0.2724 0.1032  0.1102  0.0878  237 PRO A CB  
1989 C  CG  . PRO A 236 ? 0.2517 0.4753 0.4471 0.1539  0.1596  0.2614  237 PRO A CG  
1990 C  CD  . PRO A 236 ? 0.2169 0.4785 0.3554 0.1521  0.0234  0.0322  237 PRO A CD  
1991 N  N   . GLU A 237 ? 0.2897 0.2728 0.2190 0.0015  0.0863  -0.0590 238 GLU A N   
1992 C  CA  . GLU A 237 ? 0.2536 0.3048 0.1697 -0.0386 0.0494  -0.0511 238 GLU A CA  
1993 C  C   . GLU A 237 ? 0.2430 0.2163 0.2192 -0.0111 0.0636  -0.0335 238 GLU A C   
1994 O  O   . GLU A 237 ? 0.1942 0.2560 0.1718 0.0089  0.0172  -0.0496 238 GLU A O   
1995 C  CB  . GLU A 237 ? 0.3396 0.2474 0.1977 0.0153  -0.0186 -0.0816 238 GLU A CB  
1996 C  CG  . GLU A 237 ? 0.3715 0.3046 0.2743 -0.0636 0.0205  -0.0857 238 GLU A CG  
1997 C  CD  . GLU A 237 ? 0.3343 0.3611 0.2329 0.0313  0.0223  -0.1278 238 GLU A CD  
1998 O  OE1 . GLU A 237 ? 0.6043 0.5533 0.8470 -0.0201 0.1422  -0.4828 238 GLU A OE1 
1999 O  OE2 . GLU A 237 ? 0.3325 0.2506 0.2369 -0.0348 0.0245  -0.1011 238 GLU A OE2 
2000 N  N   . GLU A 238 ? 0.2377 0.2232 0.1590 -0.0494 0.0439  -0.0430 239 GLU A N   
2001 C  CA  . GLU A 238 ? 0.2026 0.2368 0.1578 -0.0412 0.0494  -0.0322 239 GLU A CA  
2002 C  C   . GLU A 238 ? 0.1859 0.2160 0.1286 -0.0187 0.0524  -0.0286 239 GLU A C   
2003 O  O   . GLU A 238 ? 0.2626 0.1849 0.1862 -0.0120 0.0463  -0.0333 239 GLU A O   
2004 C  CB  . GLU A 238 ? 0.1917 0.2144 0.2232 -0.0070 0.0147  -0.0109 239 GLU A CB  
2005 C  CG  . GLU A 238 ? 0.2343 0.2939 0.2473 0.0637  -0.0348 -0.1049 239 GLU A CG  
2006 C  CD  . GLU A 238 ? 0.3928 0.4703 0.3397 -0.1230 0.1359  -0.1576 239 GLU A CD  
2007 O  OE1 . GLU A 238 ? 0.2965 0.3830 0.5181 -0.0164 0.0408  -0.1362 239 GLU A OE1 
2008 O  OE2 . GLU A 238 ? 0.3806 1.0197 0.4142 -0.3725 0.1083  -0.3274 239 GLU A OE2 
2009 N  N   . LEU A 239 ? 0.2096 0.2047 0.1369 -0.0494 0.0474  -0.0205 240 LEU A N   
2010 C  CA  . LEU A 239 ? 0.1930 0.1481 0.1359 -0.0313 0.0403  -0.0236 240 LEU A CA  
2011 C  C   . LEU A 239 ? 0.2143 0.1671 0.0931 -0.0199 0.0162  0.0054  240 LEU A C   
2012 O  O   . LEU A 239 ? 0.2047 0.1609 0.1476 -0.0164 0.0482  -0.0109 240 LEU A O   
2013 C  CB  . LEU A 239 ? 0.1731 0.1480 0.1858 -0.0120 0.0346  -0.0178 240 LEU A CB  
2014 C  CG  . LEU A 239 ? 0.1676 0.1803 0.2340 -0.0066 0.0063  -0.0582 240 LEU A CG  
2015 C  CD1 . LEU A 239 ? 0.2433 0.1439 0.3457 0.0337  -0.0731 -0.0461 240 LEU A CD1 
2016 C  CD2 . LEU A 239 ? 0.2638 0.1720 0.2061 0.0041  0.0057  -0.0505 240 LEU A CD2 
2017 N  N   . MET A 240 ? 0.2116 0.1425 0.1246 -0.0105 0.0430  -0.0187 241 MET A N   
2018 C  CA  . MET A 240 ? 0.2037 0.1759 0.1134 -0.0087 0.0500  -0.0094 241 MET A CA  
2019 C  C   . MET A 240 ? 0.2036 0.1489 0.0861 -0.0052 0.0181  -0.0201 241 MET A C   
2020 O  O   . MET A 240 ? 0.1837 0.1612 0.1192 -0.0270 0.0214  -0.0076 241 MET A O   
2021 C  CB  . MET A 240 ? 0.2202 0.1353 0.1246 0.0062  0.0368  0.0000  241 MET A CB  
2022 C  CG  . MET A 240 ? 0.2404 0.1577 0.1115 -0.0135 0.0471  -0.0223 241 MET A CG  
2023 S  SD  . MET A 240 ? 0.2424 0.1310 0.1410 -0.0184 0.0432  -0.0136 241 MET A SD  
2024 C  CE  . MET A 240 ? 0.2889 0.1335 0.1688 -0.0289 0.0582  0.0207  241 MET A CE  
2025 N  N   . VAL A 241 ? 0.1836 0.1268 0.1102 -0.0125 0.0237  -0.0225 242 VAL A N   
2026 C  CA  . VAL A 241 ? 0.1849 0.1225 0.1045 -0.0186 0.0277  -0.0157 242 VAL A CA  
2027 C  C   . VAL A 241 ? 0.1570 0.1086 0.1140 -0.0088 0.0146  -0.0219 242 VAL A C   
2028 O  O   . VAL A 241 ? 0.1512 0.1393 0.1199 -0.0176 0.0315  -0.0241 242 VAL A O   
2029 C  CB  . VAL A 241 ? 0.1612 0.1254 0.1315 -0.0126 0.0131  -0.0412 242 VAL A CB  
2030 C  CG1 . VAL A 241 ? 0.2054 0.1545 0.1315 -0.0344 0.0078  -0.0318 242 VAL A CG1 
2031 C  CG2 . VAL A 241 ? 0.2001 0.1368 0.1494 -0.0057 0.0340  -0.0351 242 VAL A CG2 
2032 N  N   . ASP A 242 ? 0.1526 0.1049 0.1095 -0.0120 0.0260  -0.0151 243 ASP A N   
2033 C  CA  . ASP A 242 ? 0.1489 0.1052 0.1131 0.0081  0.0098  -0.0220 243 ASP A CA  
2034 C  C   . ASP A 242 ? 0.1303 0.1074 0.1062 -0.0120 0.0210  -0.0228 243 ASP A C   
2035 O  O   . ASP A 242 ? 0.1492 0.1194 0.1528 -0.0121 0.0049  -0.0300 243 ASP A O   
2036 C  CB  . ASP A 242 ? 0.1500 0.1093 0.1322 -0.0208 0.0086  -0.0096 243 ASP A CB  
2037 C  CG  . ASP A 242 ? 0.1534 0.1074 0.1290 0.0017  0.0010  -0.0286 243 ASP A CG  
2038 O  OD1 . ASP A 242 ? 0.1298 0.0947 0.1480 0.0059  0.0110  -0.0147 243 ASP A OD1 
2039 O  OD2 . ASP A 242 ? 0.1757 0.1203 0.1727 0.0006  0.0351  -0.0423 243 ASP A OD2 
2040 N  N   . ASN A 243 ? 0.1404 0.0835 0.1134 -0.0027 0.0228  -0.0208 244 ASN A N   
2041 C  CA  . ASN A 243 ? 0.1356 0.0876 0.1142 -0.0131 0.0199  -0.0152 244 ASN A CA  
2042 C  C   . ASN A 243 ? 0.1104 0.0926 0.1064 -0.0142 0.0164  -0.0066 244 ASN A C   
2043 O  O   . ASN A 243 ? 0.1547 0.1155 0.1136 0.0203  0.0262  -0.0006 244 ASN A O   
2044 C  CB  . ASN A 243 ? 0.1319 0.1133 0.1016 -0.0266 0.0199  -0.0015 244 ASN A CB  
2045 C  CG  . ASN A 243 ? 0.1533 0.0948 0.1275 -0.0344 0.0126  0.0000  244 ASN A CG  
2046 O  OD1 . ASN A 243 ? 0.1424 0.1071 0.1407 -0.0199 0.0059  0.0078  244 ASN A OD1 
2047 N  ND2 . ASN A 243 ? 0.1993 0.2049 0.1668 -0.0559 -0.0148 0.0640  244 ASN A ND2 
2048 N  N   . TRP A 244 ? 0.1190 0.0930 0.0983 -0.0076 0.0074  -0.0154 245 TRP A N   
2049 C  CA  . TRP A 244 ? 0.0957 0.0997 0.1046 -0.0010 0.0114  -0.0163 245 TRP A CA  
2050 C  C   . TRP A 244 ? 0.1045 0.0949 0.1034 -0.0074 0.0161  -0.0094 245 TRP A C   
2051 O  O   . TRP A 244 ? 0.1098 0.1167 0.1326 0.0157  0.0044  -0.0310 245 TRP A O   
2052 C  CB  . TRP A 244 ? 0.1158 0.0898 0.1045 0.0059  0.0131  -0.0088 245 TRP A CB  
2053 C  CG  . TRP A 244 ? 0.1172 0.0935 0.1088 -0.0057 0.0166  -0.0136 245 TRP A CG  
2054 C  CD1 . TRP A 244 ? 0.1122 0.0874 0.1255 -0.0034 0.0172  -0.0171 245 TRP A CD1 
2055 C  CD2 . TRP A 244 ? 0.1098 0.1007 0.1124 -0.0034 0.0140  -0.0052 245 TRP A CD2 
2056 N  NE1 . TRP A 244 ? 0.1221 0.0948 0.1181 -0.0071 0.0081  -0.0041 245 TRP A NE1 
2057 C  CE2 . TRP A 244 ? 0.1181 0.0929 0.1168 -0.0066 0.0076  -0.0073 245 TRP A CE2 
2058 C  CE3 . TRP A 244 ? 0.1181 0.1189 0.1215 0.0049  0.0055  -0.0071 245 TRP A CE3 
2059 C  CZ2 . TRP A 244 ? 0.1268 0.1070 0.1354 0.0000  0.0097  -0.0074 245 TRP A CZ2 
2060 C  CZ3 . TRP A 244 ? 0.1282 0.1195 0.1473 0.0107  0.0098  0.0068  245 TRP A CZ3 
2061 C  CH2 . TRP A 244 ? 0.1361 0.1163 0.1518 0.0245  -0.0051 -0.0065 245 TRP A CH2 
2062 N  N   . ARG A 245 ? 0.1009 0.1014 0.1041 -0.0028 0.0074  -0.0207 246 ARG A N   
2063 C  CA  . ARG A 245 ? 0.0868 0.1010 0.1134 0.0013  -0.0048 -0.0142 246 ARG A CA  
2064 C  C   . ARG A 245 ? 0.0910 0.1041 0.1089 0.0034  0.0028  -0.0342 246 ARG A C   
2065 O  O   . ARG A 245 ? 0.1002 0.1162 0.1272 -0.0060 0.0081  -0.0188 246 ARG A O   
2066 C  CB  . ARG A 245 ? 0.0912 0.1040 0.1210 -0.0031 0.0017  -0.0249 246 ARG A CB  
2067 C  CG  . ARG A 245 ? 0.0873 0.1045 0.1398 -0.0076 0.0037  -0.0232 246 ARG A CG  
2068 C  CD  . ARG A 245 ? 0.0747 0.1106 0.1421 -0.0143 0.0052  -0.0253 246 ARG A CD  
2069 N  NE  . ARG A 245 ? 0.0898 0.1174 0.1497 -0.0113 0.0098  -0.0368 246 ARG A NE  
2070 C  CZ  . ARG A 245 ? 0.0917 0.1140 0.1233 -0.0147 0.0115  -0.0223 246 ARG A CZ  
2071 N  NH1 . ARG A 245 ? 0.1001 0.1196 0.1309 -0.0195 0.0041  -0.0242 246 ARG A NH1 
2072 N  NH2 . ARG A 245 ? 0.0965 0.1432 0.1715 -0.0299 -0.0054 -0.0212 246 ARG A NH2 
2073 N  N   A PRO A 246 ? 0.1000 0.1054 0.1128 -0.0001 0.0068  -0.0148 247 PRO A N   
2074 N  N   B PRO A 246 ? 0.1162 0.1018 0.1243 0.0068  0.0013  -0.0120 247 PRO A N   
2075 C  CA  A PRO A 246 ? 0.1490 0.1122 0.1104 0.0115  0.0015  -0.0046 247 PRO A CA  
2076 C  CA  B PRO A 246 ? 0.1427 0.1088 0.1154 0.0000  -0.0073 -0.0175 247 PRO A CA  
2077 C  C   A PRO A 246 ? 0.1233 0.0992 0.1194 0.0174  -0.0125 -0.0062 247 PRO A C   
2078 C  C   B PRO A 246 ? 0.1363 0.1050 0.1203 0.0089  -0.0071 -0.0143 247 PRO A C   
2079 O  O   A PRO A 246 ? 0.1062 0.1071 0.1280 0.0040  -0.0082 -0.0143 247 PRO A O   
2080 O  O   B PRO A 246 ? 0.1253 0.1050 0.1308 0.0087  -0.0142 -0.0015 247 PRO A O   
2081 C  CB  A PRO A 246 ? 0.1675 0.1530 0.1592 0.0505  0.0322  -0.0160 247 PRO A CB  
2082 C  CB  B PRO A 246 ? 0.2214 0.1537 0.1597 0.0653  0.0070  0.0277  247 PRO A CB  
2083 C  CG  A PRO A 246 ? 0.1192 0.1238 0.1298 0.0135  -0.0001 0.0143  247 PRO A CG  
2084 C  CG  B PRO A 246 ? 0.2034 0.2081 0.2119 0.0164  -0.0344 0.0087  247 PRO A CG  
2085 C  CD  A PRO A 246 ? 0.1032 0.1147 0.1668 0.0186  0.0041  0.0215  247 PRO A CD  
2086 C  CD  B PRO A 246 ? 0.1256 0.1631 0.1799 0.0267  -0.0019 -0.0037 247 PRO A CD  
2087 N  N   . ALA A 247 ? 0.1387 0.1172 0.1147 0.0120  0.0000  0.0000  248 ALA A N   
2088 C  CA  . ALA A 247 ? 0.1201 0.1122 0.1111 0.0115  -0.0028 -0.0003 248 ALA A CA  
2089 C  C   . ALA A 247 ? 0.1079 0.1213 0.1106 0.0237  -0.0126 0.0005  248 ALA A C   
2090 O  O   . ALA A 247 ? 0.1228 0.1414 0.1465 0.0441  -0.0073 0.0105  248 ALA A O   
2091 C  CB  . ALA A 247 ? 0.1767 0.1336 0.1363 -0.0118 0.0051  0.0015  248 ALA A CB  
2092 N  N   . GLN A 248 ? 0.1013 0.1152 0.1196 0.0113  -0.0159 -0.0037 249 GLN A N   
2093 C  CA  . GLN A 248 ? 0.1002 0.1287 0.1280 0.0111  -0.0263 0.0059  249 GLN A CA  
2094 C  C   . GLN A 248 ? 0.1138 0.1268 0.1387 0.0289  -0.0285 0.0044  249 GLN A C   
2095 O  O   . GLN A 248 ? 0.1383 0.1422 0.1288 0.0142  -0.0162 0.0103  249 GLN A O   
2096 C  CB  . GLN A 248 ? 0.1240 0.1228 0.1600 -0.0094 -0.0337 0.0059  249 GLN A CB  
2097 C  CG  . GLN A 248 ? 0.1350 0.1383 0.1377 -0.0154 -0.0175 0.0132  249 GLN A CG  
2098 C  CD  . GLN A 248 ? 0.0966 0.1588 0.1613 -0.0217 -0.0087 0.0141  249 GLN A CD  
2099 O  OE1 . GLN A 248 ? 0.1145 0.2105 0.2026 -0.0329 -0.0154 -0.0335 249 GLN A OE1 
2100 N  NE2 . GLN A 248 ? 0.1396 0.1651 0.1604 -0.0005 -0.0120 -0.0154 249 GLN A NE2 
2101 N  N   . PRO A 249 ? 0.1412 0.1772 0.1474 0.0485  -0.0408 -0.0094 250 PRO A N   
2102 C  CA  . PRO A 249 ? 0.1801 0.2116 0.1307 0.0665  -0.0469 -0.0082 250 PRO A CA  
2103 C  C   . PRO A 249 ? 0.1524 0.1539 0.1275 0.0384  -0.0335 0.0015  250 PRO A C   
2104 O  O   . PRO A 249 ? 0.1469 0.1658 0.1498 0.0357  -0.0335 0.0196  250 PRO A O   
2105 C  CB  . PRO A 249 ? 0.1792 0.2599 0.1837 0.0617  -0.0659 -0.0366 250 PRO A CB  
2106 C  CG  . PRO A 249 ? 0.2060 0.3571 0.1797 0.0485  -0.0687 -0.0381 250 PRO A CG  
2107 C  CD  . PRO A 249 ? 0.1119 0.3310 0.2043 0.0529  -0.0777 -0.0520 250 PRO A CD  
2108 N  N   . LEU A 250 ? 0.1833 0.1494 0.1269 0.0478  -0.0221 0.0020  251 LEU A N   
2109 C  CA  . LEU A 250 ? 0.1808 0.1421 0.1282 0.0132  -0.0138 0.0015  251 LEU A CA  
2110 C  C   . LEU A 250 ? 0.1596 0.1449 0.1352 0.0335  -0.0293 0.0082  251 LEU A C   
2111 O  O   . LEU A 250 ? 0.1511 0.1562 0.1517 0.0197  -0.0395 0.0031  251 LEU A O   
2112 C  CB  . LEU A 250 ? 0.2222 0.1511 0.1585 0.0162  0.0070  -0.0021 251 LEU A CB  
2113 C  CG  . LEU A 250 ? 0.2169 0.1718 0.1649 -0.0232 0.0263  0.0121  251 LEU A CG  
2114 C  CD1 . LEU A 250 ? 0.1422 0.2226 0.1661 -0.0135 -0.0073 -0.0147 251 LEU A CD1 
2115 C  CD2 . LEU A 250 ? 0.3314 0.2070 0.1975 -0.0763 0.0386  -0.0249 251 LEU A CD2 
2116 N  N   . LYS A 251 ? 0.1792 0.2072 0.1204 0.0632  -0.0427 0.0020  252 LYS A N   
2117 C  CA  . LYS A 251 ? 0.1665 0.2231 0.1393 0.0656  -0.0516 -0.0175 252 LYS A CA  
2118 C  C   . LYS A 251 ? 0.1924 0.1988 0.1955 0.0291  -0.0595 -0.0274 252 LYS A C   
2119 O  O   . LYS A 251 ? 0.2455 0.2189 0.1792 0.0078  0.0049  -0.0178 252 LYS A O   
2120 C  CB  . LYS A 251 ? 0.2370 0.2030 0.1808 -0.0006 -0.0644 -0.0248 252 LYS A CB  
2121 C  CG  . LYS A 251 ? 0.2240 0.2506 0.2562 0.0027  0.0091  -0.0285 252 LYS A CG  
2122 C  CD  . LYS A 251 ? 0.2188 0.2785 0.2446 -0.0006 -0.0151 -0.0344 252 LYS A CD  
2123 C  CE  . LYS A 251 ? 0.1699 0.3223 0.5044 0.0452  0.0487  -0.0197 252 LYS A CE  
2124 N  NZ  . LYS A 251 ? 0.2592 0.3733 0.4887 0.0208  -0.0273 0.0993  252 LYS A NZ  
2125 N  N   . ASN A 252 ? 0.1886 0.1903 0.1368 0.0286  -0.0456 -0.0372 253 ASN A N   
2126 C  CA  . ASN A 252 ? 0.2506 0.3137 0.1894 0.0644  -0.0644 -0.0965 253 ASN A CA  
2127 C  C   . ASN A 252 ? 0.2221 0.2467 0.2619 0.0657  -0.0423 -0.0230 253 ASN A C   
2128 O  O   . ASN A 252 ? 0.3174 0.2857 0.2406 0.0754  -0.0560 -0.0472 253 ASN A O   
2129 C  CB  . ASN A 252 ? 0.2563 0.4114 0.2861 0.0627  -0.0923 -0.1807 253 ASN A CB  
2130 C  CG  . ASN A 252 ? 0.4158 0.4591 0.3048 0.1002  -0.0939 -0.2382 253 ASN A CG  
2131 O  OD1 . ASN A 252 ? 0.8295 0.9010 0.3306 -0.1612 0.0778  -0.1005 253 ASN A OD1 
2132 N  ND2 . ASN A 252 ? 0.4322 0.4614 0.5317 0.0222  -0.0804 -0.2897 253 ASN A ND2 
2133 N  N   . ARG A 253 ? 0.1527 0.2948 0.1097 0.0226  -0.0066 0.0320  254 ARG A N   
2134 C  CA  . ARG A 253 ? 0.1576 0.1758 0.1068 0.0151  -0.0241 -0.0065 254 ARG A CA  
2135 C  C   . ARG A 253 ? 0.1911 0.1576 0.1104 0.0028  0.0070  -0.0131 254 ARG A C   
2136 O  O   . ARG A 253 ? 0.2420 0.1957 0.2696 0.0595  0.0711  0.0711  254 ARG A O   
2137 C  CB  . ARG A 253 ? 0.1546 0.1592 0.1075 0.0212  -0.0113 -0.0099 254 ARG A CB  
2138 C  CG  . ARG A 253 ? 0.1705 0.1388 0.1116 0.0130  -0.0074 -0.0153 254 ARG A CG  
2139 C  CD  . ARG A 253 ? 0.1664 0.1283 0.1066 0.0164  -0.0046 -0.0194 254 ARG A CD  
2140 N  NE  . ARG A 253 ? 0.1342 0.1230 0.1046 0.0147  -0.0154 0.0006  254 ARG A NE  
2141 C  CZ  . ARG A 253 ? 0.1106 0.1049 0.0892 -0.0051 -0.0152 0.0034  254 ARG A CZ  
2142 N  NH1 . ARG A 253 ? 0.1031 0.1152 0.0975 0.0010  -0.0205 -0.0010 254 ARG A NH1 
2143 N  NH2 . ARG A 253 ? 0.1149 0.1178 0.1079 0.0087  -0.0228 -0.0076 254 ARG A NH2 
2144 N  N   . GLN A 254 ? 0.1396 0.1897 0.1494 0.0192  -0.0177 -0.0463 255 GLN A N   
2145 C  CA  . GLN A 254 ? 0.1714 0.2444 0.1429 -0.0098 -0.0103 -0.0513 255 GLN A CA  
2146 C  C   . GLN A 254 ? 0.1712 0.1527 0.1495 0.0228  -0.0152 -0.0105 255 GLN A C   
2147 O  O   . GLN A 254 ? 0.2653 0.1538 0.2305 -0.0124 -0.0702 0.0019  255 GLN A O   
2148 C  CB  . GLN A 254 ? 0.2146 0.3889 0.1553 -0.0094 0.0142  -0.0857 255 GLN A CB  
2149 C  CG  . GLN A 254 ? 0.4621 0.5656 0.1648 0.2113  0.0566  -0.0533 255 GLN A CG  
2150 C  CD  . GLN A 254 ? 0.7109 0.8223 0.5370 -0.0068 0.3811  0.2725  255 GLN A CD  
2151 O  OE1 . GLN A 254 ? 1.0772 0.3816 0.6345 -0.0662 0.4228  -0.0661 255 GLN A OE1 
2152 N  NE2 . GLN A 254 ? 1.5046 1.0040 0.7635 0.6687  0.8019  0.4866  255 GLN A NE2 
2153 N  N   . ILE A 255 ? 0.1491 0.1402 0.1187 0.0105  -0.0087 0.0006  256 ILE A N   
2154 C  CA  . ILE A 255 ? 0.1388 0.1576 0.1022 0.0250  -0.0043 0.0083  256 ILE A CA  
2155 C  C   . ILE A 255 ? 0.1506 0.1345 0.1055 0.0092  0.0119  0.0127  256 ILE A C   
2156 O  O   . ILE A 255 ? 0.1776 0.1497 0.1275 0.0171  0.0199  0.0370  256 ILE A O   
2157 C  CB  . ILE A 255 ? 0.1525 0.1256 0.1183 0.0245  -0.0035 0.0032  256 ILE A CB  
2158 C  CG1 . ILE A 255 ? 0.1620 0.1462 0.1494 0.0234  0.0041  -0.0151 256 ILE A CG1 
2159 C  CG2 . ILE A 255 ? 0.1463 0.1784 0.1342 0.0152  -0.0052 -0.0015 256 ILE A CG2 
2160 C  CD1 . ILE A 255 ? 0.2074 0.1802 0.1616 0.0107  0.0238  -0.0273 256 ILE A CD1 
2161 N  N   A LYS A 256 ? 0.1342 0.1608 0.1005 0.0076  0.0007  0.0220  257 LYS A N   
2162 N  N   B LYS A 256 ? 0.1324 0.1601 0.1025 0.0078  -0.0003 0.0157  257 LYS A N   
2163 C  CA  A LYS A 256 ? 0.1326 0.1517 0.1086 0.0007  0.0127  0.0137  257 LYS A CA  
2164 C  CA  B LYS A 256 ? 0.1321 0.1483 0.1059 0.0038  0.0136  0.0149  257 LYS A CA  
2165 C  C   A LYS A 256 ? 0.1384 0.1488 0.0934 0.0034  0.0119  0.0127  257 LYS A C   
2166 C  C   B LYS A 256 ? 0.1357 0.1519 0.0932 0.0043  0.0142  0.0114  257 LYS A C   
2167 O  O   A LYS A 256 ? 0.1665 0.1902 0.0996 -0.0478 0.0087  0.0157  257 LYS A O   
2168 O  O   B LYS A 256 ? 0.1704 0.1941 0.0975 -0.0529 0.0111  0.0074  257 LYS A O   
2169 C  CB  A LYS A 256 ? 0.1889 0.1671 0.1102 -0.0065 0.0094  -0.0226 257 LYS A CB  
2170 C  CB  B LYS A 256 ? 0.1265 0.1731 0.1696 0.0073  0.0244  -0.0236 257 LYS A CB  
2171 C  CG  A LYS A 256 ? 0.2777 0.2308 0.1544 -0.0606 -0.0136 -0.0231 257 LYS A CG  
2172 C  CG  B LYS A 256 ? 0.1933 0.1471 0.2172 0.0252  0.0274  -0.0482 257 LYS A CG  
2173 C  CD  A LYS A 256 ? 0.4280 0.3370 0.3594 0.0034  -0.0142 -0.0724 257 LYS A CD  
2174 C  CD  B LYS A 256 ? 0.2777 0.1724 0.2574 0.0219  -0.0142 -0.0438 257 LYS A CD  
2175 C  CE  A LYS A 256 ? 0.4772 0.4808 0.4492 -0.0635 -0.0557 -0.0588 257 LYS A CE  
2176 C  CE  B LYS A 256 ? 0.3670 0.3594 0.2861 -0.1031 -0.0187 -0.2048 257 LYS A CE  
2177 N  NZ  A LYS A 256 ? 0.6657 0.5095 0.4053 0.0535  0.0566  0.1040  257 LYS A NZ  
2178 N  NZ  B LYS A 256 ? 0.2721 0.2169 0.3878 -0.0546 -0.0505 -0.0511 257 LYS A NZ  
2179 N  N   . ALA A 257 ? 0.1381 0.1605 0.1097 -0.0020 0.0278  0.0068  258 ALA A N   
2180 C  CA  . ALA A 257 ? 0.1203 0.1624 0.1347 0.0000  0.0027  0.0074  258 ALA A CA  
2181 C  C   . ALA A 257 ? 0.1288 0.1572 0.1158 -0.0211 0.0063  0.0043  258 ALA A C   
2182 O  O   . ALA A 257 ? 0.1524 0.1897 0.1268 0.0062  0.0303  -0.0044 258 ALA A O   
2183 C  CB  . ALA A 257 ? 0.1720 0.1652 0.1780 -0.0082 0.0187  0.0200  258 ALA A CB  
2184 N  N   . SER A 258 ? 0.1217 0.1607 0.1327 -0.0035 0.0196  0.0073  259 SER A N   
2185 C  CA  . SER A 258 ? 0.1435 0.1841 0.1475 0.0031  0.0100  -0.0005 259 SER A CA  
2186 C  C   . SER A 258 ? 0.1149 0.2261 0.1782 -0.0148 0.0467  -0.0105 259 SER A C   
2187 O  O   . SER A 258 ? 0.1703 0.3167 0.2186 0.0229  0.0511  0.0060  259 SER A O   
2188 C  CB  . SER A 258 ? 0.1392 0.1816 0.1695 -0.0010 -0.0068 0.0038  259 SER A CB  
2189 O  OG  . SER A 258 ? 0.1154 0.1904 0.1563 -0.0020 0.0185  -0.0043 259 SER A OG  
2190 N  N   . PHE A 259 ? 0.1571 0.1977 0.1872 -0.0379 0.0518  0.0024  260 PHE A N   
2191 C  CA  . PHE A 259 ? 0.2066 0.1887 0.2236 -0.0586 0.0483  0.0318  260 PHE A CA  
2192 C  C   . PHE A 259 ? 0.2423 0.2549 0.2250 -0.0961 0.0566  0.0236  260 PHE A C   
2193 O  O   . PHE A 259 ? 0.2879 0.2541 0.2548 -0.0687 0.0081  0.0984  260 PHE A O   
2194 C  CB  . PHE A 259 ? 0.1687 0.2038 0.2312 -0.0285 0.0156  0.0008  260 PHE A CB  
2195 C  CG  . PHE A 259 ? 0.1526 0.1939 0.2098 -0.0399 0.0294  0.0082  260 PHE A CG  
2196 C  CD1 . PHE A 259 ? 0.1486 0.1728 0.1879 -0.0270 -0.0074 -0.0116 260 PHE A CD1 
2197 C  CD2 . PHE A 259 ? 0.2354 0.1825 0.2967 -0.0606 0.0264  0.0494  260 PHE A CD2 
2198 C  CE1 . PHE A 259 ? 0.1483 0.1766 0.2097 -0.0238 0.0038  0.0046  260 PHE A CE1 
2199 C  CE2 . PHE A 259 ? 0.2259 0.2416 0.3156 -0.0362 0.0171  0.0496  260 PHE A CE2 
2200 C  CZ  . PHE A 259 ? 0.1981 0.1736 0.2831 -0.0269 0.0081  0.0046  260 PHE A CZ  
2201 N  N   . LYS A 260 ? 0.3558 0.5037 0.3083 -0.1918 0.0353  0.1877  261 LYS A N   
2202 C  CA  . LYS A 260 ? 0.6097 0.5752 0.3486 -0.0684 0.0666  0.2257  261 LYS A CA  
2203 C  C   . LYS A 260 ? 1.0412 1.0169 0.3547 -0.1224 -0.0126 0.1958  261 LYS A C   
2204 O  O   . LYS A 260 ? 1.2194 1.6197 0.8711 0.3194  0.8106  0.8844  261 LYS A O   
2205 C  CB  . LYS A 260 ? 0.6495 0.3828 0.4941 -0.1001 -0.0109 0.1973  261 LYS A CB  
2206 C  CG  . LYS A 260 ? 0.7597 0.3992 0.5982 -0.3079 -0.0204 0.1107  261 LYS A CG  
2207 C  CD  . LYS A 260 ? 0.6779 0.5710 0.6093 -0.2317 0.2391  0.0764  261 LYS A CD  
2208 C  CE  . LYS A 260 ? 0.7714 0.4509 0.5812 0.0776  0.2120  0.2276  261 LYS A CE  
2209 N  NZ  . LYS A 260 ? 1.0767 0.6055 0.6183 0.3668  0.3720  0.2268  261 LYS A NZ  
2210 ZN ZN  . ZN  B .   ? 0.1036 0.0838 0.0885 -0.0054 -0.0120 -0.0052 301 ZN  A ZN  
2211 S  S   . DMS C .   ? 0.2495 0.2882 0.2786 -0.0304 0.0266  -0.0452 302 DMS A S   
2212 O  O   . DMS C .   ? 0.3941 0.3503 0.3476 0.0615  0.0930  -0.1309 302 DMS A O   
2213 C  C1  . DMS C .   ? 0.1913 0.2883 0.2752 0.0034  0.0306  -0.1101 302 DMS A C1  
2214 C  C2  . DMS C .   ? 0.2331 0.2246 0.3759 -0.0098 0.0200  0.0026  302 DMS A C2  
2215 S  S   . DMS D .   ? 0.4010 0.3896 0.3664 0.0000  -0.0007 0.0273  303 DMS A S   
2216 O  O   . DMS D .   ? 0.4362 0.5263 0.3823 0.0174  -0.0264 -0.0621 303 DMS A O   
2217 C  C1  . DMS D .   ? 0.4246 0.4261 0.4276 -0.0311 -0.0019 0.0183  303 DMS A C1  
2218 C  C2  . DMS D .   ? 0.3514 0.3677 0.3125 0.0156  -0.0277 -0.0430 303 DMS A C2  
2219 C  C1  . EDO E .   ? 0.2657 0.2494 0.3065 -0.0685 0.0590  0.0719  304 EDO A C1  
2220 O  O1  . EDO E .   ? 0.5103 0.4986 0.4654 -0.2277 0.2063  -0.0894 304 EDO A O1  
2221 C  C2  . EDO E .   ? 0.6755 0.4214 0.4239 -0.2088 -0.0505 -0.0048 304 EDO A C2  
2222 O  O2  . EDO E .   ? 0.8450 0.5077 0.5625 -0.3104 -0.0979 0.2069  304 EDO A O2  
2223 C  C1  . EDO F .   ? 0.5297 0.3878 0.2516 -0.0098 -0.0278 0.0337  305 EDO A C1  
2224 O  O1  . EDO F .   ? 0.4828 0.4192 0.2583 -0.0052 -0.0057 0.0579  305 EDO A O1  
2225 C  C2  . EDO F .   ? 0.4959 0.2341 0.2038 0.0984  0.0944  0.0621  305 EDO A C2  
2226 O  O2  . EDO F .   ? 0.8101 0.5085 0.3966 0.1385  -0.0031 0.1128  305 EDO A O2  
2227 C  C1  . EDO G .   ? 0.2094 0.2297 0.7084 -0.0675 -0.2058 0.0970  306 EDO A C1  
2228 O  O1  . EDO G .   ? 0.2083 0.3231 0.4638 -0.0001 0.0024  -0.0066 306 EDO A O1  
2229 C  C2  . EDO G .   ? 0.1255 0.3652 0.5490 -0.0394 0.0236  -0.0157 306 EDO A C2  
2230 O  O2  . EDO G .   ? 0.2123 0.5058 0.4474 0.0013  -0.0913 0.0930  306 EDO A O2  
2231 C  C1  . EDO H .   ? 0.4192 0.3478 0.3716 -0.0080 -0.0614 0.0087  307 EDO A C1  
2232 O  O1  . EDO H .   ? 0.3791 0.3691 0.4327 0.0270  -0.0099 0.0148  307 EDO A O1  
2233 C  C2  . EDO H .   ? 0.4478 0.3651 0.3944 -0.0111 -0.0266 -0.0472 307 EDO A C2  
2234 O  O2  . EDO H .   ? 0.3378 0.3226 0.3847 0.0252  0.0173  0.0168  307 EDO A O2  
2235 O  O16 . V26 I .   ? 0.2449 0.1625 0.1917 -0.0500 -0.0445 0.0610  308 V26 A O16 
2236 S  S14 . V26 I .   ? 0.1870 0.1483 0.1605 -0.0434 0.0040  0.0043  308 V26 A S14 
2237 O  O15 . V26 I .   ? 0.1931 0.1588 0.1776 -0.0498 0.0024  0.0138  308 V26 A O15 
2238 C  C8  . V26 I .   ? 0.1647 0.1357 0.1350 -0.0219 -0.0229 0.0077  308 V26 A C8  
2239 C  C7  . V26 I .   ? 0.1453 0.1233 0.1375 -0.0219 0.0015  0.0068  308 V26 A C7  
2240 F  F12 . V26 I .   ? 0.1261 0.1550 0.1676 -0.0248 0.0024  0.0008  308 V26 A F12 
2241 C  C6  . V26 I .   ? 0.1385 0.1104 0.1260 -0.0110 -0.0088 0.0116  308 V26 A C6  
2242 F  F11 . V26 I .   ? 0.1262 0.1237 0.1464 -0.0141 -0.0013 0.0137  308 V26 A F11 
2243 C  C9  . V26 I .   ? 0.1542 0.0982 0.1445 -0.0085 -0.0113 0.0137  308 V26 A C9  
2244 N  N25 . V26 I .   ? 0.1688 0.1243 0.1630 -0.0255 -0.0337 0.0205  308 V26 A N25 
2245 C  C26 . V26 I .   ? 0.1732 0.1627 0.1446 -0.0265 -0.0250 0.0240  308 V26 A C26 
2246 C  C10 . V26 I .   ? 0.1120 0.1143 0.1377 -0.0249 -0.0137 0.0109  308 V26 A C10 
2247 F  F13 . V26 I .   ? 0.1370 0.1281 0.1572 -0.0115 -0.0121 0.0088  308 V26 A F13 
2248 C  C5  . V26 I .   ? 0.1503 0.0992 0.1588 -0.0038 -0.0372 0.0035  308 V26 A C5  
2249 S  S1  . V26 I .   ? 0.1023 0.0962 0.1111 -0.0052 -0.0115 -0.0131 308 V26 A S1  
2250 O  O3  . V26 I .   ? 0.1018 0.1106 0.1120 -0.0003 -0.0162 -0.0208 308 V26 A O3  
2251 N  N4  . V26 I .   ? 0.1189 0.0878 0.3384 -0.0142 -0.0423 -0.0588 308 V26 A N4  
2252 O  O2  . V26 I .   ? 0.1115 0.1023 0.1154 -0.0146 -0.0105 -0.0093 308 V26 A O2  
2253 C  C17 . V26 I .   ? 0.2560 0.1985 0.1758 -0.0577 0.0132  -0.0215 308 V26 A C17 
2254 C  C18 . V26 I .   ? 0.2736 0.2030 0.1891 -0.0724 0.0403  -0.0388 308 V26 A C18 
2255 C  C19 . V26 I .   ? 0.2166 0.1975 0.1588 -0.0425 0.0331  -0.0092 308 V26 A C19 
2256 C  C24 . V26 I .   ? 0.2469 0.1645 0.2182 -0.0381 -0.0318 -0.0201 308 V26 A C24 
2257 C  C23 . V26 I .   ? 0.2049 0.2093 0.1798 -0.0281 -0.0020 0.0098  308 V26 A C23 
2258 C  C22 . V26 I .   ? 0.2412 0.2352 0.1630 -0.0344 -0.0256 -0.0214 308 V26 A C22 
2259 C  C21 . V26 I .   ? 0.1930 0.2930 0.1444 0.0076  -0.0148 -0.0160 308 V26 A C21 
2260 C  C20 . V26 I .   ? 0.2021 0.2359 0.2084 0.0000  0.0173  0.0157  308 V26 A C20 
2261 O  O   . HOH J .   ? 0.2056 0.2818 0.3838 -0.0049 0.0010  -0.0057 401 HOH A O   
2262 O  O   . HOH J .   ? 0.2960 0.5421 0.1994 0.0938  -0.0015 -0.0135 402 HOH A O   
2263 O  O   . HOH J .   ? 0.4427 0.4501 0.5458 -0.0043 -0.1374 0.0601  403 HOH A O   
2264 O  O   . HOH J .   ? 0.5232 0.4176 0.4790 -0.0654 0.0666  -0.0909 404 HOH A O   
2265 O  O   . HOH J .   ? 0.4808 0.3238 0.4797 0.0637  -0.0546 0.0013  405 HOH A O   
2266 O  O   . HOH J .   ? 0.3300 0.1536 0.3176 -0.0388 -0.0940 -0.0124 406 HOH A O   
2267 O  O   . HOH J .   ? 0.3445 0.2890 0.2702 0.0353  0.0324  0.0219  407 HOH A O   
2268 O  O   . HOH J .   ? 0.2753 0.2984 0.4456 -0.0877 0.0098  -0.0030 408 HOH A O   
2269 O  O   . HOH J .   ? 0.5856 0.5673 0.5004 0.2678  -0.2964 -0.2407 409 HOH A O   
2270 O  O   . HOH J .   ? 0.6061 0.4279 0.5472 -0.0573 -0.2743 -0.1124 410 HOH A O   
2271 O  O   . HOH J .   ? 0.3019 0.2401 0.4542 -0.0542 -0.1045 0.0000  411 HOH A O   
2272 O  O   . HOH J .   ? 0.3903 0.1721 0.2384 -0.0289 -0.0215 -0.0190 412 HOH A O   
2273 O  O   . HOH J .   ? 0.1362 0.1208 0.1303 -0.0102 0.0212  -0.0215 413 HOH A O   
2274 O  O   . HOH J .   ? 0.7423 0.3030 0.4196 0.1430  -0.0610 -0.0670 414 HOH A O   
2275 O  O   . HOH J .   ? 0.1976 0.2513 0.3158 0.0222  0.0386  0.0218  415 HOH A O   
2276 O  O   . HOH J .   ? 0.3693 0.2779 0.6022 -0.0675 0.0671  -0.0052 416 HOH A O   
2277 O  O   . HOH J .   ? 0.5891 0.2363 0.3777 0.0397  0.1253  0.0656  417 HOH A O   
2278 O  O   . HOH J .   ? 0.3416 0.2597 0.5145 0.0357  0.0034  -0.1731 418 HOH A O   
2279 O  O   . HOH J .   ? 0.4316 0.2492 0.6241 -0.1749 0.0209  0.0285  419 HOH A O   
2280 O  O   . HOH J .   ? 0.2409 0.3314 0.2847 -0.0307 0.0680  0.0710  420 HOH A O   
2281 O  O   . HOH J .   ? 0.3465 0.4742 0.2741 -0.0461 -0.0136 0.1173  421 HOH A O   
2282 O  O   . HOH J .   ? 0.2069 0.1332 0.0987 -0.0218 -0.0153 0.0052  422 HOH A O   
2283 O  O   . HOH J .   ? 0.1762 0.3774 0.4521 0.0181  -0.0126 0.0267  423 HOH A O   
2284 O  O   . HOH J .   ? 0.3813 0.1483 0.2190 0.0182  -0.1545 0.0140  424 HOH A O   
2285 O  O   . HOH J .   ? 0.2469 0.5249 0.3682 -0.0582 -0.0573 0.0399  425 HOH A O   
2286 O  O   . HOH J .   ? 0.8105 0.3575 0.4187 -0.0885 0.1520  -0.0744 426 HOH A O   
2287 O  O   . HOH J .   ? 0.3819 0.4947 0.4717 0.1054  0.0540  -0.0425 427 HOH A O   
2288 O  O   . HOH J .   ? 1.0492 1.6380 0.8363 0.5187  -0.3353 -0.5916 428 HOH A O   
2289 O  O   . HOH J .   ? 0.3282 0.3867 0.3174 -0.0595 0.1234  -0.1699 429 HOH A O   
2290 O  O   . HOH J .   ? 0.6474 0.2275 0.2428 -0.1191 -0.0031 -0.0740 430 HOH A O   
2291 O  O   . HOH J .   ? 0.2291 0.2067 0.2152 0.0168  -0.0298 -0.0285 431 HOH A O   
2292 O  O   . HOH J .   ? 0.3551 0.3123 0.3296 -0.1042 0.1211  -0.1301 432 HOH A O   
2293 O  O   . HOH J .   ? 0.4280 0.3867 0.3029 -0.1840 0.1465  -0.1526 433 HOH A O   
2294 O  O   . HOH J .   ? 0.5777 0.3181 0.2624 -0.0722 0.1228  -0.0826 434 HOH A O   
2295 O  O   . HOH J .   ? 0.3367 0.4329 0.5863 -0.0353 0.2108  0.0211  435 HOH A O   
2296 O  O   . HOH J .   ? 0.3493 0.3835 0.2750 -0.1369 0.0181  0.1011  436 HOH A O   
2297 O  O   . HOH J .   ? 0.3184 0.1893 0.2456 -0.0851 -0.0381 -0.0052 437 HOH A O   
2298 O  O   . HOH J .   ? 0.2657 0.4805 0.2498 -0.0211 -0.0026 0.0221  438 HOH A O   
2299 O  O   . HOH J .   ? 0.5000 0.3557 0.1449 0.0447  -0.0097 0.0189  439 HOH A O   
2300 O  O   . HOH J .   ? 0.5242 0.2370 0.5616 -0.0907 -0.1099 -0.0912 440 HOH A O   
2301 O  O   . HOH J .   ? 0.1952 0.1280 0.1547 -0.0114 -0.0074 0.0071  441 HOH A O   
2302 O  O   . HOH J .   ? 0.2297 0.2115 0.3080 0.0243  -0.1430 -0.0688 442 HOH A O   
2303 O  O   . HOH J .   ? 0.2395 0.2352 0.2143 0.0008  0.0586  0.0416  443 HOH A O   
2304 O  O   . HOH J .   ? 0.4440 0.3526 0.5023 0.0434  -0.2122 0.0432  444 HOH A O   
2305 O  O   . HOH J .   ? 0.3242 0.2269 0.3102 -0.0559 0.0161  -0.0280 445 HOH A O   
2306 O  O   . HOH J .   ? 0.2911 0.3914 0.4800 -0.0908 -0.1224 -0.0340 446 HOH A O   
2307 O  O   . HOH J .   ? 0.3532 0.2236 0.3476 -0.0012 -0.1247 0.0027  447 HOH A O   
2308 O  O   . HOH J .   ? 0.3662 0.3858 0.4617 0.0362  -0.1094 -0.2179 448 HOH A O   
2309 O  O   . HOH J .   ? 0.3307 0.3923 0.3713 0.0456  0.1309  -0.0331 449 HOH A O   
2310 O  O   . HOH J .   ? 0.1570 0.1081 0.1228 -0.0093 0.0034  -0.0107 450 HOH A O   
2311 O  O   . HOH J .   ? 0.2836 1.7927 0.5389 0.3192  0.1873  -0.1974 451 HOH A O   
2312 O  O   . HOH J .   ? 0.2797 0.3325 0.3652 0.0315  -0.0781 -0.2064 452 HOH A O   
2313 O  O   . HOH J .   ? 0.1969 0.2100 0.2904 0.0227  0.0449  0.0162  453 HOH A O   
2314 O  O   . HOH J .   ? 0.3669 0.2854 0.3675 0.0062  0.0318  0.0535  454 HOH A O   
2315 O  O   . HOH J .   ? 0.2028 0.3124 0.3849 0.0177  0.0288  0.0174  455 HOH A O   
2316 O  O   . HOH J .   ? 0.1571 0.1959 0.1709 -0.0199 0.0065  -0.0057 456 HOH A O   
2317 O  O   . HOH J .   ? 0.1824 0.3616 0.4596 0.0586  -0.0164 -0.0126 457 HOH A O   
2318 O  O   . HOH J .   ? 0.3458 1.0465 0.3799 0.1835  -0.1304 -0.2340 458 HOH A O   
2319 O  O   . HOH J .   ? 0.3774 0.2770 0.4057 -0.0161 -0.0151 0.1871  459 HOH A O   
2320 O  O   . HOH J .   ? 0.2316 0.1474 0.2291 -0.0094 -0.0278 0.0038  460 HOH A O   
2321 O  O   . HOH J .   ? 0.1988 0.2370 0.2782 0.0161  -0.0093 0.0324  461 HOH A O   
2322 O  O   . HOH J .   ? 0.4848 0.6258 0.1961 -0.0954 0.0226  0.0964  462 HOH A O   
2323 O  O   . HOH J .   ? 0.3427 0.2423 0.1718 -0.0348 -0.0570 0.0193  463 HOH A O   
2324 O  O   . HOH J .   ? 0.1671 0.1176 0.1304 -0.0105 0.0085  -0.0200 464 HOH A O   
2325 O  O   . HOH J .   ? 0.3205 0.4347 0.9487 0.0120  -0.1607 -0.0557 465 HOH A O   
2326 O  O   . HOH J .   ? 0.2337 0.5953 0.5494 -0.0790 0.0986  0.0456  466 HOH A O   
2327 O  O   . HOH J .   ? 0.3295 0.2710 0.3871 -0.0447 0.0040  0.0399  467 HOH A O   
2328 O  O   . HOH J .   ? 0.1251 0.1561 0.1500 0.0041  -0.0320 0.0159  468 HOH A O   
2329 O  O   . HOH J .   ? 0.2705 0.8403 0.5963 -0.0456 -0.0092 0.4609  469 HOH A O   
2330 O  O   . HOH J .   ? 0.4945 0.5238 0.5935 0.0276  -0.2773 0.0333  470 HOH A O   
2331 O  O   . HOH J .   ? 0.3429 0.5031 0.3583 0.0984  0.0768  0.0857  471 HOH A O   
2332 O  O   . HOH J .   ? 0.2395 0.3598 0.2483 0.0183  0.0579  -0.0278 472 HOH A O   
2333 O  O   . HOH J .   ? 0.3744 0.4047 0.4025 -0.0055 0.0445  -0.0639 473 HOH A O   
2334 O  O   . HOH J .   ? 1.1040 1.1132 0.5332 0.1749  0.3210  0.2958  474 HOH A O   
2335 O  O   . HOH J .   ? 0.4223 0.2426 0.4117 -0.0992 0.0866  -0.0566 475 HOH A O   
2336 O  O   . HOH J .   ? 0.2760 0.3016 0.7664 -0.0249 -0.1231 0.0230  476 HOH A O   
2337 O  O   . HOH J .   ? 0.2631 0.2419 0.3149 0.0198  0.0434  0.0606  477 HOH A O   
2338 O  O   . HOH J .   ? 0.2336 0.2275 0.2270 -0.0096 -0.0756 0.0434  478 HOH A O   
2339 O  O   . HOH J .   ? 0.4452 0.3264 0.2621 -0.1168 0.0027  -0.0201 479 HOH A O   
2340 O  O   . HOH J .   ? 0.2115 0.2717 0.1988 -0.0259 0.0562  -0.0438 480 HOH A O   
2341 O  O   . HOH J .   ? 0.4922 0.2282 0.2002 -0.0848 -0.0032 0.0718  481 HOH A O   
2342 O  O   . HOH J .   ? 0.2918 0.3883 0.3539 0.0076  0.0259  -0.0852 482 HOH A O   
2343 O  O   . HOH J .   ? 0.7085 0.2664 0.1898 0.1032  0.0237  0.0373  483 HOH A O   
2344 O  O   . HOH J .   ? 0.2524 0.3097 0.5615 -0.1116 -0.0540 0.1150  484 HOH A O   
2345 O  O   . HOH J .   ? 0.2936 0.2380 0.2872 0.0088  -0.0568 0.0331  485 HOH A O   
2346 O  O   . HOH J .   ? 0.1247 0.1061 0.1314 0.0088  -0.0089 -0.0121 486 HOH A O   
2347 O  O   . HOH J .   ? 0.1054 0.1204 0.1288 -0.0149 0.0041  0.0054  487 HOH A O   
2348 O  O   . HOH J .   ? 0.1849 0.1086 0.1844 -0.0141 -0.0178 0.0044  488 HOH A O   
2349 O  O   . HOH J .   ? 0.3691 0.2620 0.9498 0.0055  0.0178  0.0329  489 HOH A O   
2350 O  O   . HOH J .   ? 0.3525 0.3625 0.2584 -0.1222 0.0071  -0.1077 490 HOH A O   
2351 O  O   . HOH J .   ? 0.1586 0.1562 0.3422 -0.0366 -0.0711 0.0035  491 HOH A O   
2352 O  O   . HOH J .   ? 0.1906 0.1827 0.2040 0.0049  -0.0236 0.0154  492 HOH A O   
2353 O  O   . HOH J .   ? 0.6216 0.3609 0.3616 0.1097  0.0478  -0.0217 493 HOH A O   
2354 O  O   . HOH J .   ? 0.2304 0.3428 0.1942 -0.0152 -0.0281 -0.0767 494 HOH A O   
2355 O  O   . HOH J .   ? 0.5831 0.2487 0.2413 0.0379  0.0104  0.0274  495 HOH A O   
2356 O  O   . HOH J .   ? 0.0891 0.1685 0.2217 -0.0031 -0.0111 -0.0337 496 HOH A O   
2357 O  O   . HOH J .   ? 0.2336 0.2667 0.4180 -0.0302 -0.0035 0.0131  497 HOH A O   
2358 O  O   . HOH J .   ? 0.2789 0.2413 0.2238 0.0432  0.0063  0.0239  498 HOH A O   
2359 O  O   . HOH J .   ? 0.2108 0.2675 0.2696 0.0237  -0.0417 0.0093  499 HOH A O   
2360 O  O   . HOH J .   ? 0.1356 0.1492 0.1215 0.0306  0.0027  0.0003  500 HOH A O   
2361 O  O   . HOH J .   ? 0.1536 0.1965 0.1994 0.0197  -0.0185 0.0197  501 HOH A O   
2362 O  O   . HOH J .   ? 0.4589 0.1862 0.3161 0.1265  -0.0675 -0.0405 502 HOH A O   
2363 O  O   . HOH J .   ? 0.2354 0.1491 0.2470 0.0186  0.0151  -0.0266 503 HOH A O   
2364 O  O   . HOH J .   ? 0.1529 0.1332 0.1964 0.0229  0.0070  0.0074  504 HOH A O   
2365 O  O   . HOH J .   ? 0.3713 0.2724 0.2893 0.0006  0.0857  -0.0509 505 HOH A O   
2366 O  O   . HOH J .   ? 0.2311 0.3953 0.2915 0.0267  -0.0399 -0.0294 506 HOH A O   
2367 O  O   . HOH J .   ? 0.2030 0.1340 0.2126 -0.0375 -0.0258 -0.0023 507 HOH A O   
2368 O  O   . HOH J .   ? 0.2793 0.5401 0.4690 -0.0078 0.1216  0.0992  508 HOH A O   
2369 O  O   . HOH J .   ? 0.3043 0.2955 0.4028 -0.0118 0.1096  0.0283  509 HOH A O   
2370 O  O   . HOH J .   ? 0.3974 0.5026 0.2224 -0.0500 -0.1213 0.1054  510 HOH A O   
2371 O  O   . HOH J .   ? 0.2309 0.1736 0.2048 0.0043  -0.0324 -0.0302 511 HOH A O   
2372 O  O   . HOH J .   ? 0.2082 0.1886 0.1870 -0.0149 -0.0522 0.0109  512 HOH A O   
2373 O  O   . HOH J .   ? 0.1336 0.1242 0.1580 0.0179  -0.0136 0.0119  513 HOH A O   
2374 O  O   . HOH J .   ? 0.3374 0.1683 0.2058 -0.0207 -0.1132 0.0164  514 HOH A O   
2375 O  O   . HOH J .   ? 0.1378 0.3777 0.2831 0.0210  -0.0026 0.1376  515 HOH A O   
2376 O  O   . HOH J .   ? 0.4467 0.3937 0.4025 0.0590  0.0688  0.0702  516 HOH A O   
2377 O  O   . HOH J .   ? 0.2876 0.1809 0.3511 -0.0274 -0.0540 -0.0337 517 HOH A O   
2378 O  O   . HOH J .   ? 0.3007 0.3382 0.5712 -0.0028 0.0672  0.0125  518 HOH A O   
2379 O  O   . HOH J .   ? 0.1545 0.5412 0.3984 -0.0441 0.0207  0.0535  519 HOH A O   
2380 O  O   . HOH J .   ? 0.2732 0.1905 0.2785 0.0109  -0.1081 -0.0199 520 HOH A O   
2381 O  O   . HOH J .   ? 0.3763 0.2645 0.2499 0.0427  0.0049  -0.0288 521 HOH A O   
2382 O  O   . HOH J .   ? 0.2125 0.2025 0.1897 -0.0388 0.0017  -0.0111 522 HOH A O   
2383 O  O   . HOH J .   ? 0.2153 0.2194 0.3574 0.0715  -0.0193 -0.0482 523 HOH A O   
2384 O  O   . HOH J .   ? 0.2203 0.3306 0.4746 0.0346  0.0568  0.1251  524 HOH A O   
2385 O  O   . HOH J .   ? 0.3184 0.4517 0.3557 -0.0878 0.0265  -0.0096 525 HOH A O   
2386 O  O   . HOH J .   ? 0.4194 0.2777 0.5156 0.0998  -0.2018 -0.0538 526 HOH A O   
2387 O  O   . HOH J .   ? 0.2366 0.1431 0.1931 0.0027  -0.0219 0.0082  527 HOH A O   
2388 O  O   . HOH J .   ? 0.2998 0.2146 0.3124 -0.0172 -0.0073 -0.0149 528 HOH A O   
2389 O  O   . HOH J .   ? 0.2994 0.2773 0.5508 -0.0414 -0.0092 -0.1072 529 HOH A O   
2390 O  O   . HOH J .   ? 0.5450 0.3842 0.3237 0.0679  0.1289  0.1720  530 HOH A O   
2391 O  O   . HOH J .   ? 0.1248 0.1864 0.2774 -0.0071 0.0044  0.0174  531 HOH A O   
2392 O  O   . HOH J .   ? 0.2689 0.2333 0.1631 0.0020  0.0031  -0.0231 532 HOH A O   
2393 O  O   . HOH J .   ? 0.2570 0.3799 0.5478 -0.0855 0.0549  -0.0149 533 HOH A O   
2394 O  O   . HOH J .   ? 0.4042 0.4621 0.3001 -0.0214 -0.0201 -0.0049 534 HOH A O   
2395 O  O   . HOH J .   ? 0.2782 0.5145 0.3508 -0.0416 -0.0606 0.1444  535 HOH A O   
2396 O  O   . HOH J .   ? 0.4775 0.3147 0.2247 -0.0130 0.0494  0.0951  536 HOH A O   
2397 O  O   . HOH J .   ? 0.4934 0.3316 0.2336 -0.0306 0.0940  -0.1248 537 HOH A O   
2398 O  O   . HOH J .   ? 0.4409 0.2962 0.3282 -0.1023 0.0807  0.0935  538 HOH A O   
2399 O  O   . HOH J .   ? 0.4150 0.2673 0.5058 0.0309  -0.1933 -0.0249 539 HOH A O   
2400 O  O   . HOH J .   ? 0.3027 0.1730 0.1837 0.0051  -0.0326 0.0100  540 HOH A O   
2401 O  O   . HOH J .   ? 0.4420 0.4512 0.3734 0.0027  -0.0078 -0.0467 541 HOH A O   
2402 O  O   . HOH J .   ? 0.2383 0.3476 0.6294 -0.0772 0.1174  0.0272  542 HOH A O   
2403 O  O   . HOH J .   ? 0.5568 0.1853 0.2540 -0.0577 -0.0250 0.0137  543 HOH A O   
2404 O  O   . HOH J .   ? 0.3094 0.1328 0.2336 -0.0164 -0.0024 0.0115  544 HOH A O   
2405 O  O   . HOH J .   ? 0.1467 0.3711 0.4079 0.0197  -0.0274 0.1186  545 HOH A O   
2406 O  O   . HOH J .   ? 0.1695 0.1583 0.2352 -0.0285 0.0298  0.0010  546 HOH A O   
2407 O  O   . HOH J .   ? 0.3820 0.3093 0.7710 0.1451  0.1527  0.0531  547 HOH A O   
2408 O  O   . HOH J .   ? 0.2872 0.4041 0.3701 -0.0824 -0.1242 0.0331  548 HOH A O   
2409 O  O   . HOH J .   ? 0.2471 0.1886 0.2340 0.0375  0.0498  0.1035  549 HOH A O   
2410 O  O   . HOH J .   ? 0.3145 0.4469 0.3158 -0.0763 -0.0340 0.0445  550 HOH A O   
2411 O  O   . HOH J .   ? 0.2587 0.4894 0.2962 -0.1315 -0.0568 0.0060  551 HOH A O   
2412 O  O   . HOH J .   ? 0.3446 0.2088 0.3276 0.0693  0.1275  0.0553  552 HOH A O   
2413 O  O   . HOH J .   ? 0.0974 0.2175 0.2405 0.0103  0.0151  -0.0461 553 HOH A O   
2414 O  O   . HOH J .   ? 0.3064 0.1876 0.2809 -0.0104 -0.0710 -0.0241 554 HOH A O   
2415 O  O   . HOH J .   ? 0.5475 0.3898 0.3440 -0.0010 -0.0027 -0.1040 555 HOH A O   
2416 O  O   . HOH J .   ? 0.5572 0.3260 0.6305 0.1264  0.0299  -0.1363 556 HOH A O   
2417 O  O   . HOH J .   ? 0.3701 0.1607 0.2864 0.0592  -0.0125 -0.0405 557 HOH A O   
2418 O  O   . HOH J .   ? 0.2207 0.7422 0.7479 -0.0851 0.0838  -0.1052 558 HOH A O   
2419 O  O   . HOH J .   ? 0.1844 0.2126 0.2797 -0.0013 -0.0125 -0.0153 559 HOH A O   
2420 O  O   . HOH J .   ? 0.2030 0.1674 0.2820 -0.0590 -0.0434 -0.0340 560 HOH A O   
2421 O  O   . HOH J .   ? 0.3801 0.1569 0.2151 -0.0275 -0.0175 -0.0255 561 HOH A O   
2422 O  O   . HOH J .   ? 0.5019 0.4222 0.2223 0.2565  0.0542  -0.0513 562 HOH A O   
2423 O  O   . HOH J .   ? 0.2481 0.1893 0.2702 0.0121  -0.0710 -0.0767 563 HOH A O   
2424 O  O   . HOH J .   ? 0.4718 0.4600 0.5698 0.1967  0.0179  -0.0258 564 HOH A O   
2425 O  O   . HOH J .   ? 0.3226 0.3256 0.2088 0.0265  0.0313  -0.0230 565 HOH A O   
2426 O  O   . HOH J .   ? 0.4783 0.3076 0.5095 0.0055  0.0454  -0.0010 566 HOH A O   
2427 O  O   . HOH J .   ? 0.3993 0.4470 0.3924 -0.1321 -0.0480 -0.0666 567 HOH A O   
2428 O  O   . HOH J .   ? 0.3161 0.2637 0.3730 0.0780  0.0262  0.0359  568 HOH A O   
2429 O  O   . HOH J .   ? 0.5583 0.4323 0.4824 -0.0305 -0.1914 -0.0965 569 HOH A O   
2430 O  O   . HOH J .   ? 0.4445 0.2117 0.2478 -0.0874 -0.1218 -0.0017 570 HOH A O   
2431 O  O   . HOH J .   ? 0.2996 0.4003 0.3321 0.1324  0.0480  0.0410  571 HOH A O   
2432 O  O   . HOH J .   ? 0.2797 0.2452 0.2061 0.0311  -0.0208 0.0706  572 HOH A O   
2433 O  O   . HOH J .   ? 0.5975 0.2973 0.2460 -0.1396 0.0324  -0.0947 573 HOH A O   
2434 O  O   . HOH J .   ? 0.3490 0.3001 0.3550 -0.0318 -0.0582 -0.0237 574 HOH A O   
2435 O  O   . HOH J .   ? 0.3860 0.2804 0.5092 -0.0837 -0.0003 0.0350  575 HOH A O   
2436 O  O   . HOH J .   ? 0.4485 0.1833 0.3237 0.0859  0.0156  0.0652  576 HOH A O   
2437 O  O   . HOH J .   ? 0.1378 0.2266 0.1773 -0.0094 -0.0516 0.0527  577 HOH A O   
2438 O  O   . HOH J .   ? 0.5271 0.3034 0.3427 0.1123  0.0087  -0.0074 578 HOH A O   
2439 O  O   . HOH J .   ? 0.3481 0.1939 0.3558 0.0203  0.0604  0.0804  579 HOH A O   
2440 O  O   . HOH J .   ? 0.2799 0.3690 0.2897 -0.0549 0.0308  -0.0082 580 HOH A O   
2441 O  O   . HOH J .   ? 0.2240 0.3274 0.3199 0.0980  -0.1001 -0.0745 581 HOH A O   
2442 O  O   . HOH J .   ? 0.3379 0.5820 0.3429 -0.0798 -0.0190 -0.0359 582 HOH A O   
2443 O  O   . HOH J .   ? 0.1317 0.1231 0.1581 0.0178  -0.0098 -0.0074 583 HOH A O   
2444 O  O   . HOH J .   ? 0.3984 0.4593 0.5957 -0.1816 -0.0044 0.1706  584 HOH A O   
2445 O  O   . HOH J .   ? 0.5198 0.4714 0.1744 -0.0250 0.0383  0.0895  585 HOH A O   
2446 O  O   . HOH J .   ? 0.3461 0.5246 0.2354 -0.1437 0.0259  -0.1027 586 HOH A O   
2447 O  O   . HOH J .   ? 0.2280 0.1054 0.2025 0.0049  -0.0074 -0.0099 587 HOH A O   
2448 O  O   . HOH J .   ? 0.5407 0.3610 0.3156 -0.0130 -0.0232 0.0768  588 HOH A O   
2449 O  O   . HOH J .   ? 0.3885 0.4146 0.5482 0.0917  0.1411  0.1450  589 HOH A O   
2450 O  O   . HOH J .   ? 0.3289 0.2125 0.3961 0.0725  0.0549  0.0250  590 HOH A O   
2451 O  O   . HOH J .   ? 0.2041 0.2134 1.0049 0.0423  0.0714  0.0590  591 HOH A O   
2452 O  O   . HOH J .   ? 0.3917 0.2547 0.2151 -0.0820 0.1288  -0.0900 592 HOH A O   
2453 O  O   . HOH J .   ? 0.4016 0.4298 0.1784 0.0697  -0.0588 0.0113  593 HOH A O   
2454 O  O   . HOH J .   ? 0.5752 0.3558 0.3348 -0.1026 0.1004  -0.1228 594 HOH A O   
2455 O  O   . HOH J .   ? 0.2939 0.3407 0.5518 -0.0826 0.1216  -0.0342 595 HOH A O   
2456 O  O   . HOH J .   ? 0.3767 1.0202 0.5810 -0.0494 0.1386  -0.1508 596 HOH A O   
2457 O  O   . HOH J .   ? 0.3508 0.2202 0.5845 0.0261  -0.1138 0.0575  597 HOH A O   
2458 O  O   . HOH J .   ? 0.3626 0.2601 0.6474 0.0667  0.1851  0.0898  598 HOH A O   
2459 O  O   . HOH J .   ? 0.1354 0.1940 0.3296 -0.0131 -0.0241 -0.0153 599 HOH A O   
2460 O  O   . HOH J .   ? 1.2468 1.8199 0.5612 -0.4830 0.1818  -0.0751 600 HOH A O   
2461 O  O   . HOH J .   ? 0.5863 0.2058 0.4208 -0.0329 0.0970  0.0945  601 HOH A O   
2462 O  O   . HOH J .   ? 0.7577 0.3755 0.5317 0.1374  -0.2572 0.0469  602 HOH A O   
2463 O  O   . HOH J .   ? 0.3813 0.3481 0.2259 -0.0821 -0.0921 0.0209  603 HOH A O   
2464 O  O   . HOH J .   ? 0.4237 0.4854 0.4142 0.0511  0.0432  -0.0230 604 HOH A O   
2465 O  O   . HOH J .   ? 0.3005 0.4359 0.2552 0.0816  0.0295  0.0099  605 HOH A O   
2466 O  O   . HOH J .   ? 0.4707 0.2718 0.4652 0.0684  0.2549  0.1033  606 HOH A O   
2467 O  O   . HOH J .   ? 0.5227 0.5382 0.4320 -0.0813 0.0690  -0.0063 607 HOH A O   
2468 O  O   . HOH J .   ? 0.4365 0.3489 0.4485 0.2023  -0.0604 -0.0571 608 HOH A O   
2469 O  O   . HOH J .   ? 0.3346 0.2759 0.4627 0.0256  -0.1054 -0.0535 609 HOH A O   
2470 O  O   . HOH J .   ? 1.1095 1.9763 0.3519 0.3860  0.0088  -0.3946 610 HOH A O   
2471 O  O   . HOH J .   ? 0.5163 0.5412 0.2925 0.3023  -0.0522 0.0023  611 HOH A O   
2472 O  O   . HOH J .   ? 0.6686 0.9707 0.5227 -0.0802 0.0724  0.1416  612 HOH A O   
2473 O  O   . HOH J .   ? 0.6097 0.4675 0.5638 0.2820  0.1438  0.0474  613 HOH A O   
2474 O  O   . HOH J .   ? 0.3490 0.2978 0.4449 -0.0447 0.0026  -0.0098 614 HOH A O   
2475 O  O   . HOH J .   ? 2.4741 0.5928 0.5813 0.3073  -0.0186 0.1771  615 HOH A O   
2476 O  O   . HOH J .   ? 0.3198 0.6638 0.5978 0.0441  0.0738  -0.0071 616 HOH A O   
2477 O  O   . HOH J .   ? 0.5487 0.3022 0.5825 0.0399  -0.2124 -0.0324 617 HOH A O   
2478 O  O   . HOH J .   ? 0.5512 0.5426 0.3274 0.0017  0.0388  -0.0013 618 HOH A O   
2479 O  O   . HOH J .   ? 0.6233 0.3467 0.3471 -0.0179 -0.0221 0.0864  619 HOH A O   
2480 O  O   . HOH J .   ? 0.2377 0.4011 0.3942 -0.0091 0.0364  0.0502  620 HOH A O   
2481 O  O   . HOH J .   ? 0.3353 0.1844 0.2560 -0.0093 -0.0450 0.0083  621 HOH A O   
2482 O  O   . HOH J .   ? 0.5690 0.5217 0.6017 -0.0099 -0.0808 0.0100  622 HOH A O   
2483 O  O   . HOH J .   ? 0.1896 0.1212 0.2037 -0.0176 -0.0428 -0.0088 623 HOH A O   
2484 O  O   . HOH J .   ? 0.3306 0.3341 0.3932 0.0406  0.0595  -0.0615 624 HOH A O   
2485 O  O   . HOH J .   ? 0.3116 0.3384 0.3298 0.0164  0.0452  -0.0732 625 HOH A O   
2486 O  O   . HOH J .   ? 0.4088 0.3813 0.6316 0.1977  -0.2134 -0.1743 626 HOH A O   
2487 O  O   . HOH J .   ? 0.3246 0.6402 0.7225 0.0271  0.0414  0.3046  627 HOH A O   
2488 O  O   . HOH J .   ? 0.7020 0.2653 0.4745 0.0377  0.2466  0.1093  628 HOH A O   
2489 O  O   . HOH J .   ? 0.6370 0.4255 0.5846 -0.2037 -0.2181 0.1534  629 HOH A O   
2490 O  O   . HOH J .   ? 0.3560 0.3353 0.2570 -0.0364 -0.0251 -0.0116 630 HOH A O   
2491 O  O   . HOH J .   ? 0.7332 1.0447 0.2782 0.5038  -0.0681 -0.0802 631 HOH A O   
2492 O  O   . HOH J .   ? 0.5588 0.3682 0.2846 0.1344  -0.1624 -0.0062 632 HOH A O   
2493 O  O   . HOH J .   ? 0.4011 0.4377 0.6341 0.1079  0.1015  -0.1102 633 HOH A O   
2494 O  O   . HOH J .   ? 0.3551 0.2718 0.5267 0.0634  0.0024  0.0372  634 HOH A O   
2495 O  O   . HOH J .   ? 0.5500 0.5041 0.3583 0.2117  0.1578  0.1837  635 HOH A O   
2496 O  O   . HOH J .   ? 0.5177 0.4693 0.4408 -0.0121 0.0417  0.0410  636 HOH A O   
2497 O  O   . HOH J .   ? 0.5820 0.2469 0.1395 0.0207  -0.0308 0.0185  637 HOH A O   
2498 O  O   . HOH J .   ? 0.5446 0.2014 0.6887 0.0544  -0.1282 0.0177  638 HOH A O   
2499 O  O   . HOH J .   ? 0.2420 0.2901 0.3856 0.0220  -0.0184 0.0287  639 HOH A O   
2500 O  O   . HOH J .   ? 0.3440 0.2161 0.3604 0.0711  -0.2085 -0.0515 640 HOH A O   
2501 O  O   . HOH J .   ? 0.3436 0.4115 0.7459 0.0934  0.0386  0.0983  641 HOH A O   
2502 O  O   . HOH J .   ? 0.6668 0.7465 0.6674 -0.1048 0.0373  0.3880  642 HOH A O   
2503 O  O   . HOH J .   ? 0.6455 0.3334 0.3292 0.0727  0.0410  0.0978  643 HOH A O   
2504 O  O   . HOH J .   ? 0.4079 0.4223 0.4153 -0.0908 0.0460  -0.0208 644 HOH A O   
2505 O  O   . HOH J .   ? 0.3630 0.4215 0.3238 -0.1547 0.0166  0.0114  645 HOH A O   
2506 O  O   . HOH J .   ? 0.1555 0.2742 0.4072 0.0520  0.0359  0.0263  646 HOH A O   
2507 O  O   . HOH J .   ? 0.2757 0.7896 0.4021 0.1272  -0.0285 0.1547  647 HOH A O   
2508 O  O   . HOH J .   ? 0.4552 0.5681 0.4491 0.0082  -0.0225 0.1061  648 HOH A O   
2509 O  O   . HOH J .   ? 0.2951 0.2180 0.3512 0.0152  -0.0908 -0.0038 649 HOH A O   
2510 O  O   . HOH J .   ? 0.3016 0.3995 0.3149 -0.0590 0.0734  -0.0870 650 HOH A O   
2511 O  O   . HOH J .   ? 0.3292 0.6118 0.5278 0.2190  0.1255  0.1641  651 HOH A O   
2512 O  O   . HOH J .   ? 0.4354 0.6033 0.9264 0.1225  0.0419  0.4025  652 HOH A O   
2513 O  O   . HOH J .   ? 0.3184 0.2480 0.7796 -0.0065 0.0860  0.0604  653 HOH A O   
2514 O  O   . HOH J .   ? 0.2789 0.2595 0.3133 -0.0828 -0.0399 -0.0146 654 HOH A O   
2515 O  O   . HOH J .   ? 0.2969 0.3399 0.3077 0.1137  -0.0467 -0.0165 655 HOH A O   
2516 O  O   . HOH J .   ? 0.3952 0.4603 0.4710 0.0812  0.0273  0.1206  656 HOH A O   
2517 O  O   . HOH J .   ? 0.3163 0.4234 0.5479 -0.0540 -0.0306 -0.0841 657 HOH A O   
2518 O  O   . HOH J .   ? 0.4318 0.6159 0.4041 -0.2682 0.1877  -0.1532 658 HOH A O   
2519 O  O   . HOH J .   ? 0.2390 0.3406 0.3131 0.0071  -0.0148 0.0667  659 HOH A O   
2520 O  O   . HOH J .   ? 0.3767 0.5175 0.3116 0.0610  0.0817  0.1052  660 HOH A O   
2521 O  O   . HOH J .   ? 0.4825 0.5173 0.3331 -0.1090 -0.1805 0.0355  661 HOH A O   
2522 O  O   . HOH J .   ? 0.5913 0.6197 0.3029 0.0384  -0.0610 0.0988  662 HOH A O   
2523 O  O   . HOH J .   ? 0.4221 0.1934 0.3672 0.0098  -0.0359 0.0104  663 HOH A O   
2524 O  O   . HOH J .   ? 0.4991 0.3515 1.0671 0.1482  -0.1360 -0.0953 664 HOH A O   
2525 O  O   . HOH J .   ? 0.4760 0.3471 0.2138 -0.0399 -0.0351 -0.0020 665 HOH A O   
2526 O  O   . HOH J .   ? 0.4914 0.6006 0.2029 -0.1005 0.1136  0.0403  666 HOH A O   
2527 O  O   . HOH J .   ? 0.2876 0.1228 0.2540 0.0151  -0.0847 -0.0041 667 HOH A O   
2528 O  O   . HOH J .   ? 0.4273 0.3648 1.3056 -0.0777 -0.0267 0.2328  668 HOH A O   
2529 O  O   . HOH J .   ? 0.3371 0.1641 0.2170 0.0076  -0.0395 -0.0044 669 HOH A O   
2530 O  O   . HOH J .   ? 0.4793 0.2828 0.2991 0.0812  -0.0392 -0.0716 670 HOH A O   
2531 O  O   . HOH J .   ? 0.3998 0.3630 0.2495 0.0850  0.0248  -0.1107 671 HOH A O   
2532 O  O   . HOH J .   ? 0.4086 0.4157 0.4241 -0.0948 -0.0265 -0.0081 672 HOH A O   
2533 O  O   . HOH J .   ? 0.3960 0.4614 0.3422 -0.0046 0.0847  -0.1771 673 HOH A O   
2534 O  O   . HOH J .   ? 0.4524 0.3292 0.3422 -0.0895 -0.0612 0.0597  674 HOH A O   
2535 O  O   . HOH J .   ? 0.2467 0.1994 0.2228 -0.0082 -0.0480 -0.0196 675 HOH A O   
2536 O  O   . HOH J .   ? 1.6497 0.1871 1.2384 -0.4280 -0.4268 0.2671  676 HOH A O   
2537 O  O   . HOH J .   ? 0.2155 0.2096 0.2469 0.0394  -0.0502 0.0138  677 HOH A O   
2538 O  O   . HOH J .   ? 0.5785 0.4090 0.2391 -0.3018 -0.0672 0.0110  678 HOH A O   
2539 O  O   . HOH J .   ? 0.2817 0.6827 0.4341 -0.0599 0.0186  0.3115  679 HOH A O   
2540 O  O   . HOH J .   ? 0.3450 0.4794 0.6662 0.0846  0.1149  0.0306  680 HOH A O   
2541 O  O   . HOH J .   ? 0.4582 0.3612 0.6394 0.1074  0.2175  0.1691  681 HOH A O   
2542 O  O   . HOH J .   ? 0.3156 0.6076 0.4643 0.0348  0.0190  -0.2874 682 HOH A O   
2543 O  O   . HOH J .   ? 0.7056 0.8086 0.6784 0.2734  0.0155  -0.0841 683 HOH A O   
2544 O  O   . HOH J .   ? 0.4824 0.5511 0.5691 0.0414  0.1494  -0.2445 684 HOH A O   
2545 O  O   . HOH J .   ? 0.5981 0.3885 0.4961 -0.2698 -0.1018 0.1282  685 HOH A O   
2546 O  O   . HOH J .   ? 0.4171 0.3849 0.5195 0.0035  0.0171  -0.0885 686 HOH A O   
2547 O  O   . HOH J .   ? 0.1706 0.3088 0.3902 -0.0416 -0.0599 0.0493  687 HOH A O   
2548 O  O   . HOH J .   ? 0.5239 0.3233 0.5952 -0.1305 0.1466  -0.2008 688 HOH A O   
2549 O  O   . HOH J .   ? 0.4735 1.0716 1.5923 -0.0794 -0.4084 0.4704  689 HOH A O   
2550 O  O   . HOH J .   ? 0.6940 0.3076 0.4843 0.0878  -0.0135 -0.0441 690 HOH A O   
2551 O  O   . HOH J .   ? 0.3343 0.1643 0.4959 -0.0241 0.1669  -0.0046 691 HOH A O   
2552 O  O   . HOH J .   ? 0.6844 0.6019 0.3730 -0.0430 0.1286  0.1694  692 HOH A O   
2553 O  O   . HOH J .   ? 0.5568 0.3116 0.4693 0.0082  -0.1597 -0.0828 693 HOH A O   
2554 O  O   . HOH J .   ? 0.1946 0.4893 0.6531 -0.0666 0.0289  -0.2222 694 HOH A O   
2555 O  O   . HOH J .   ? 0.7976 0.3598 0.5120 0.1237  0.2190  0.0219  695 HOH A O   
2556 O  O   . HOH J .   ? 0.2851 0.4722 0.4582 0.0297  0.0922  -0.0234 696 HOH A O   
2557 O  O   . HOH J .   ? 0.5008 0.2707 0.2745 -0.0074 -0.0416 -0.1569 697 HOH A O   
2558 O  O   . HOH J .   ? 0.7300 0.4941 0.5419 0.0194  -0.1930 -0.0725 698 HOH A O   
2559 O  O   . HOH J .   ? 0.2489 0.3677 0.4259 -0.1093 -0.0129 -0.1432 699 HOH A O   
2560 O  O   . HOH J .   ? 1.1554 0.7384 0.6693 0.2666  -0.5073 -0.3010 700 HOH A O   
2561 O  O   . HOH J .   ? 0.2293 0.2134 0.3302 -0.0240 0.0240  -0.0537 701 HOH A O   
2562 O  O   . HOH J .   ? 0.4699 0.4767 0.3921 -0.0571 -0.0152 0.0241  702 HOH A O   
# 
