data_6YHC
# 
_entry.id   6YHC 
# 
_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   6YHC         pdb_00006yhc 10.2210/pdb6yhc/pdb 
WWPDB D_1292106431 ?            ?                   
# 
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 2021-04-07 
2 'Structure model' 1 1 2021-06-02 
3 'Structure model' 1 2 2024-01-24 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
loop_
_pdbx_audit_revision_group.ordinal 
_pdbx_audit_revision_group.revision_ordinal 
_pdbx_audit_revision_group.data_content_type 
_pdbx_audit_revision_group.group 
1 2 'Structure model' 'Database references'    
2 3 'Structure model' 'Data collection'        
3 3 'Structure model' 'Database references'    
4 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' 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                        6YHC 
_pdbx_database_status.recvd_initial_deposition_date   2020-03-28 
_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.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Smirnov, A.'  1 0000-0001-5080-9367 
'Manakova, E.' 2 0000-0002-6027-2265 
'Grazulis, S.' 3 0000-0002-7928-5218 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   DE 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            Chemistryopen 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            ? 
_citation.journal_id_ISSN           2191-1363 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            10 
_citation.language                  ? 
_citation.page_first                567 
_citation.page_last                 580 
_citation.title                     'Switching the Inhibitor-Enzyme Recognition Profile via Chimeric Carbonic Anhydrase XII.' 
_citation.year                      2021 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1002/open.202100042 
_citation.pdbx_database_id_PubMed   33945229 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Smirnoviene, J.'   1  0000-0001-5503-4775 
primary 'Smirnov, A.'       2  ?                   
primary 'Zaksauskas, A.'    3  ?                   
primary 'Zubriene, A.'      4  0000-0001-5996-1883 
primary 'Petrauskas, V.'    5  0000-0001-7983-4128 
primary 'Mickeviciute, A.'  6  ?                   
primary 'Michailoviene, V.' 7  ?                   
primary 'Capkauskaite, E.'  8  ?                   
primary 'Manakova, E.'      9  0000-0002-6027-2265 
primary 'Grazulis, S.'      10 0000-0002-7928-5218 
primary 'Baranauskiene, L.' 11 0000-0002-9924-9177 
primary 'Chen, W.Y.'        12 ?                   
primary 'Ladbury, J.E.'     13 0000-0002-6328-7200 
primary 'Matulis, D.'       14 0000-0002-6178-6276 
# 
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'                                                           29220.879 1   4.2.1.1 
'A65S, N67K, I91T, F130A, V134S, L203N' ? ? 
2 non-polymer syn 'ZINC ION'                                                                       65.409    1   ?       ? ? ? 
3 non-polymer syn 'DIMETHYL SULFOXIDE'                                                             78.133    1   ?       ? ? ? 
4 non-polymer syn '3-(benzylamino)-2,5,6-trifluoro-4-[(2-hydroxyethyl)sulfonyl]benzenesulfonamide' 424.415   2   ?       ? ? ? 
5 water       nat water                                                                            18.015    229 ?       ? ? ? 
# 
_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       
;MSHHWGYGKHNGPEHWHKDFPIAKGERQSPVDIDTHTAKYDPSLKPLSVSYDQATSLRILNNGHSFKVEFDDSQDKAVLK
GGPLDGTYRLTQFHFHWGSLDGQGSEHTVDKKKYAAELHLVHWNTKYGDAGKASQQPDGLAVLGIFLKVGSAKPGLQKVV
DVLDSIKTKGKSADFTNFDPRGLLPESLDYWTYPGSLTTPPLNECVTWIVLKEPISVSSEQVLKFRKLNFNGEGEPEELM
VDNWRPAQPLKNRQIKASFK
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MSHHWGYGKHNGPEHWHKDFPIAKGERQSPVDIDTHTAKYDPSLKPLSVSYDQATSLRILNNGHSFKVEFDDSQDKAVLK
GGPLDGTYRLTQFHFHWGSLDGQGSEHTVDKKKYAAELHLVHWNTKYGDAGKASQQPDGLAVLGIFLKVGSAKPGLQKVV
DVLDSIKTKGKSADFTNFDPRGLLPESLDYWTYPGSLTTPPLNECVTWIVLKEPISVSSEQVLKFRKLNFNGEGEPEELM
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 '3-(benzylamino)-2,5,6-trifluoro-4-[(2-hydroxyethyl)sulfonyl]benzenesulfonamide' WWO 
5 water                                                                            HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   MET n 
1 2   SER n 
1 3   HIS n 
1 4   HIS n 
1 5   TRP n 
1 6   GLY n 
1 7   TYR n 
1 8   GLY n 
1 9   LYS n 
1 10  HIS n 
1 11  ASN n 
1 12  GLY n 
1 13  PRO n 
1 14  GLU n 
1 15  HIS n 
1 16  TRP n 
1 17  HIS n 
1 18  LYS n 
1 19  ASP n 
1 20  PHE n 
1 21  PRO n 
1 22  ILE n 
1 23  ALA n 
1 24  LYS n 
1 25  GLY n 
1 26  GLU n 
1 27  ARG n 
1 28  GLN n 
1 29  SER n 
1 30  PRO n 
1 31  VAL n 
1 32  ASP n 
1 33  ILE n 
1 34  ASP n 
1 35  THR n 
1 36  HIS n 
1 37  THR n 
1 38  ALA n 
1 39  LYS n 
1 40  TYR n 
1 41  ASP n 
1 42  PRO n 
1 43  SER n 
1 44  LEU n 
1 45  LYS n 
1 46  PRO n 
1 47  LEU n 
1 48  SER n 
1 49  VAL n 
1 50  SER n 
1 51  TYR n 
1 52  ASP n 
1 53  GLN n 
1 54  ALA n 
1 55  THR n 
1 56  SER n 
1 57  LEU n 
1 58  ARG n 
1 59  ILE n 
1 60  LEU n 
1 61  ASN n 
1 62  ASN n 
1 63  GLY n 
1 64  HIS n 
1 65  SER n 
1 66  PHE n 
1 67  LYS 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  THR 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 ALA n 
1 131 GLY n 
1 132 LYS n 
1 133 ALA n 
1 134 SER 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 ASN 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 BL21(DE3)' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     469008 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          plasmid 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       pET15b 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
ALA 'L-peptide linking' y ALANINE                                                                          ? 'C3 H7 N O2'          
89.093  
ARG 'L-peptide linking' y ARGININE                                                                         ? 'C6 H15 N4 O2 1'      
175.209 
ASN 'L-peptide linking' y ASPARAGINE                                                                       ? 'C4 H8 N2 O3'         
132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID'                                                                  ? 'C4 H7 N O4'          
133.103 
CYS 'L-peptide linking' y CYSTEINE                                                                         ? 'C3 H7 N O2 S'        
121.158 
DMS non-polymer         . 'DIMETHYL SULFOXIDE'                                                             ? 'C2 H6 O S'           
78.133  
GLN 'L-peptide linking' y GLUTAMINE                                                                        ? 'C5 H10 N2 O3'        
146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID'                                                                  ? 'C5 H9 N O4'          
147.129 
GLY 'peptide linking'   y GLYCINE                                                                          ? 'C2 H5 N O2'          
75.067  
HIS 'L-peptide linking' y HISTIDINE                                                                        ? 'C6 H10 N3 O2 1'      
156.162 
HOH non-polymer         . WATER                                                                            ? 'H2 O'                
18.015  
ILE 'L-peptide linking' y ISOLEUCINE                                                                       ? 'C6 H13 N O2'         
131.173 
LEU 'L-peptide linking' y LEUCINE                                                                          ? 'C6 H13 N O2'         
131.173 
LYS 'L-peptide linking' y LYSINE                                                                           ? 'C6 H15 N2 O2 1'      
147.195 
MET 'L-peptide linking' y METHIONINE                                                                       ? 'C5 H11 N O2 S'       
149.211 
PHE 'L-peptide linking' y PHENYLALANINE                                                                    ? 'C9 H11 N O2'         
165.189 
PRO 'L-peptide linking' y PROLINE                                                                          ? 'C5 H9 N O2'          
115.130 
SER 'L-peptide linking' y SERINE                                                                           ? 'C3 H7 N O3'          
105.093 
THR 'L-peptide linking' y THREONINE                                                                        ? 'C4 H9 N O3'          
119.119 
TRP 'L-peptide linking' y TRYPTOPHAN                                                                       ? 'C11 H12 N2 O2'       
204.225 
TYR 'L-peptide linking' y TYROSINE                                                                         ? 'C9 H11 N O3'         
181.189 
VAL 'L-peptide linking' y VALINE                                                                           ? 'C5 H11 N O2'         
117.146 
WWO non-polymer         . '3-(benzylamino)-2,5,6-trifluoro-4-[(2-hydroxyethyl)sulfonyl]benzenesulfonamide' ? 'C15 H15 F3 N2 O5 S2' 
424.415 
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   ?   ?   ?   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  SER 65  65  65  SER SER A . n 
A 1 66  PHE 66  66  66  PHE PHE A . n 
A 1 67  LYS 67  67  67  LYS LYS 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  THR 91  91  91  THR THR 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 ALA 130 131 131 ALA ALA 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 SER 134 135 135 SER SER 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 ASN 203 204 204 ASN ASN 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 4 WWO 1   303 1   WWO WWO A . 
E 4 WWO 1   304 2   WWO WWO A . 
F 5 HOH 1   401 89  HOH HOH A . 
F 5 HOH 2   402 168 HOH HOH A . 
F 5 HOH 3   403 52  HOH HOH A . 
F 5 HOH 4   404 81  HOH HOH A . 
F 5 HOH 5   405 135 HOH HOH A . 
F 5 HOH 6   406 137 HOH HOH A . 
F 5 HOH 7   407 54  HOH HOH A . 
F 5 HOH 8   408 40  HOH HOH A . 
F 5 HOH 9   409 65  HOH HOH A . 
F 5 HOH 10  410 183 HOH HOH A . 
F 5 HOH 11  411 141 HOH HOH A . 
F 5 HOH 12  412 66  HOH HOH A . 
F 5 HOH 13  413 76  HOH HOH A . 
F 5 HOH 14  414 134 HOH HOH A . 
F 5 HOH 15  415 164 HOH HOH A . 
F 5 HOH 16  416 92  HOH HOH A . 
F 5 HOH 17  417 129 HOH HOH A . 
F 5 HOH 18  418 115 HOH HOH A . 
F 5 HOH 19  419 46  HOH HOH A . 
F 5 HOH 20  420 131 HOH HOH A . 
F 5 HOH 21  421 213 HOH HOH A . 
F 5 HOH 22  422 6   HOH HOH A . 
F 5 HOH 23  423 186 HOH HOH A . 
F 5 HOH 24  424 154 HOH HOH A . 
F 5 HOH 25  425 28  HOH HOH A . 
F 5 HOH 26  426 207 HOH HOH A . 
F 5 HOH 27  427 51  HOH HOH A . 
F 5 HOH 28  428 10  HOH HOH A . 
F 5 HOH 29  429 84  HOH HOH A . 
F 5 HOH 30  430 98  HOH HOH A . 
F 5 HOH 31  431 201 HOH HOH A . 
F 5 HOH 32  432 199 HOH HOH A . 
F 5 HOH 33  433 109 HOH HOH A . 
F 5 HOH 34  434 63  HOH HOH A . 
F 5 HOH 35  435 105 HOH HOH A . 
F 5 HOH 36  436 140 HOH HOH A . 
F 5 HOH 37  437 78  HOH HOH A . 
F 5 HOH 38  438 29  HOH HOH A . 
F 5 HOH 39  439 53  HOH HOH A . 
F 5 HOH 40  440 93  HOH HOH A . 
F 5 HOH 41  441 95  HOH HOH A . 
F 5 HOH 42  442 157 HOH HOH A . 
F 5 HOH 43  443 22  HOH HOH A . 
F 5 HOH 44  444 99  HOH HOH A . 
F 5 HOH 45  445 202 HOH HOH A . 
F 5 HOH 46  446 37  HOH HOH A . 
F 5 HOH 47  447 61  HOH HOH A . 
F 5 HOH 48  448 8   HOH HOH A . 
F 5 HOH 49  449 86  HOH HOH A . 
F 5 HOH 50  450 87  HOH HOH A . 
F 5 HOH 51  451 187 HOH HOH A . 
F 5 HOH 52  452 16  HOH HOH A . 
F 5 HOH 53  453 58  HOH HOH A . 
F 5 HOH 54  454 25  HOH HOH A . 
F 5 HOH 55  455 176 HOH HOH A . 
F 5 HOH 56  456 5   HOH HOH A . 
F 5 HOH 57  457 192 HOH HOH A . 
F 5 HOH 58  458 125 HOH HOH A . 
F 5 HOH 59  459 18  HOH HOH A . 
F 5 HOH 60  460 138 HOH HOH A . 
F 5 HOH 61  461 90  HOH HOH A . 
F 5 HOH 62  462 143 HOH HOH A . 
F 5 HOH 63  463 4   HOH HOH A . 
F 5 HOH 64  464 83  HOH HOH A . 
F 5 HOH 65  465 217 HOH HOH A . 
F 5 HOH 66  466 102 HOH HOH A . 
F 5 HOH 67  467 13  HOH HOH A . 
F 5 HOH 68  468 123 HOH HOH A . 
F 5 HOH 69  469 100 HOH HOH A . 
F 5 HOH 70  470 9   HOH HOH A . 
F 5 HOH 71  471 120 HOH HOH A . 
F 5 HOH 72  472 132 HOH HOH A . 
F 5 HOH 73  473 212 HOH HOH A . 
F 5 HOH 74  474 88  HOH HOH A . 
F 5 HOH 75  475 45  HOH HOH A . 
F 5 HOH 76  476 7   HOH HOH A . 
F 5 HOH 77  477 103 HOH HOH A . 
F 5 HOH 78  478 126 HOH HOH A . 
F 5 HOH 79  479 97  HOH HOH A . 
F 5 HOH 80  480 110 HOH HOH A . 
F 5 HOH 81  481 144 HOH HOH A . 
F 5 HOH 82  482 33  HOH HOH A . 
F 5 HOH 83  483 85  HOH HOH A . 
F 5 HOH 84  484 12  HOH HOH A . 
F 5 HOH 85  485 108 HOH HOH A . 
F 5 HOH 86  486 2   HOH HOH A . 
F 5 HOH 87  487 111 HOH HOH A . 
F 5 HOH 88  488 11  HOH HOH A . 
F 5 HOH 89  489 17  HOH HOH A . 
F 5 HOH 90  490 116 HOH HOH A . 
F 5 HOH 91  491 43  HOH HOH A . 
F 5 HOH 92  492 64  HOH HOH A . 
F 5 HOH 93  493 27  HOH HOH A . 
F 5 HOH 94  494 190 HOH HOH A . 
F 5 HOH 95  495 3   HOH HOH A . 
F 5 HOH 96  496 41  HOH HOH A . 
F 5 HOH 97  497 171 HOH HOH A . 
F 5 HOH 98  498 59  HOH HOH A . 
F 5 HOH 99  499 1   HOH HOH A . 
F 5 HOH 100 500 162 HOH HOH A . 
F 5 HOH 101 501 74  HOH HOH A . 
F 5 HOH 102 502 178 HOH HOH A . 
F 5 HOH 103 503 124 HOH HOH A . 
F 5 HOH 104 504 38  HOH HOH A . 
F 5 HOH 105 505 149 HOH HOH A . 
F 5 HOH 106 506 15  HOH HOH A . 
F 5 HOH 107 507 200 HOH HOH A . 
F 5 HOH 108 508 71  HOH HOH A . 
F 5 HOH 109 509 145 HOH HOH A . 
F 5 HOH 110 510 225 HOH HOH A . 
F 5 HOH 111 511 39  HOH HOH A . 
F 5 HOH 112 512 68  HOH HOH A . 
F 5 HOH 113 513 139 HOH HOH A . 
F 5 HOH 114 514 161 HOH HOH A . 
F 5 HOH 115 515 147 HOH HOH A . 
F 5 HOH 116 516 73  HOH HOH A . 
F 5 HOH 117 517 148 HOH HOH A . 
F 5 HOH 118 518 165 HOH HOH A . 
F 5 HOH 119 519 47  HOH HOH A . 
F 5 HOH 120 520 57  HOH HOH A . 
F 5 HOH 121 521 20  HOH HOH A . 
F 5 HOH 122 522 26  HOH HOH A . 
F 5 HOH 123 523 35  HOH HOH A . 
F 5 HOH 124 524 181 HOH HOH A . 
F 5 HOH 125 525 104 HOH HOH A . 
F 5 HOH 126 526 113 HOH HOH A . 
F 5 HOH 127 527 91  HOH HOH A . 
F 5 HOH 128 528 158 HOH HOH A . 
F 5 HOH 129 529 80  HOH HOH A . 
F 5 HOH 130 530 34  HOH HOH A . 
F 5 HOH 131 531 160 HOH HOH A . 
F 5 HOH 132 532 82  HOH HOH A . 
F 5 HOH 133 533 77  HOH HOH A . 
F 5 HOH 134 534 112 HOH HOH A . 
F 5 HOH 135 535 172 HOH HOH A . 
F 5 HOH 136 536 32  HOH HOH A . 
F 5 HOH 137 537 60  HOH HOH A . 
F 5 HOH 138 538 49  HOH HOH A . 
F 5 HOH 139 539 136 HOH HOH A . 
F 5 HOH 140 540 14  HOH HOH A . 
F 5 HOH 141 541 70  HOH HOH A . 
F 5 HOH 142 542 23  HOH HOH A . 
F 5 HOH 143 543 122 HOH HOH A . 
F 5 HOH 144 544 42  HOH HOH A . 
F 5 HOH 145 545 21  HOH HOH A . 
F 5 HOH 146 546 121 HOH HOH A . 
F 5 HOH 147 547 96  HOH HOH A . 
F 5 HOH 148 548 50  HOH HOH A . 
F 5 HOH 149 549 79  HOH HOH A . 
F 5 HOH 150 550 56  HOH HOH A . 
F 5 HOH 151 551 69  HOH HOH A . 
F 5 HOH 152 552 146 HOH HOH A . 
F 5 HOH 153 553 198 HOH HOH A . 
F 5 HOH 154 554 210 HOH HOH A . 
F 5 HOH 155 555 48  HOH HOH A . 
F 5 HOH 156 556 44  HOH HOH A . 
F 5 HOH 157 557 72  HOH HOH A . 
F 5 HOH 158 558 75  HOH HOH A . 
F 5 HOH 159 559 106 HOH HOH A . 
F 5 HOH 160 560 208 HOH HOH A . 
F 5 HOH 161 561 24  HOH HOH A . 
F 5 HOH 162 562 226 HOH HOH A . 
F 5 HOH 163 563 203 HOH HOH A . 
F 5 HOH 164 564 151 HOH HOH A . 
F 5 HOH 165 565 128 HOH HOH A . 
F 5 HOH 166 566 30  HOH HOH A . 
F 5 HOH 167 567 19  HOH HOH A . 
F 5 HOH 168 568 205 HOH HOH A . 
F 5 HOH 169 569 215 HOH HOH A . 
F 5 HOH 170 570 229 HOH HOH A . 
F 5 HOH 171 571 36  HOH HOH A . 
F 5 HOH 172 572 153 HOH HOH A . 
F 5 HOH 173 573 67  HOH HOH A . 
F 5 HOH 174 574 209 HOH HOH A . 
F 5 HOH 175 575 173 HOH HOH A . 
F 5 HOH 176 576 152 HOH HOH A . 
F 5 HOH 177 577 118 HOH HOH A . 
F 5 HOH 178 578 221 HOH HOH A . 
F 5 HOH 179 579 130 HOH HOH A . 
F 5 HOH 180 580 62  HOH HOH A . 
F 5 HOH 181 581 197 HOH HOH A . 
F 5 HOH 182 582 175 HOH HOH A . 
F 5 HOH 183 583 94  HOH HOH A . 
F 5 HOH 184 584 182 HOH HOH A . 
F 5 HOH 185 585 107 HOH HOH A . 
F 5 HOH 186 586 170 HOH HOH A . 
F 5 HOH 187 587 224 HOH HOH A . 
F 5 HOH 188 588 191 HOH HOH A . 
F 5 HOH 189 589 180 HOH HOH A . 
F 5 HOH 190 590 194 HOH HOH A . 
F 5 HOH 191 591 155 HOH HOH A . 
F 5 HOH 192 592 166 HOH HOH A . 
F 5 HOH 193 593 163 HOH HOH A . 
F 5 HOH 194 594 204 HOH HOH A . 
F 5 HOH 195 595 206 HOH HOH A . 
F 5 HOH 196 596 159 HOH HOH A . 
F 5 HOH 197 597 101 HOH HOH A . 
F 5 HOH 198 598 169 HOH HOH A . 
F 5 HOH 199 599 133 HOH HOH A . 
F 5 HOH 200 600 142 HOH HOH A . 
F 5 HOH 201 601 218 HOH HOH A . 
F 5 HOH 202 602 177 HOH HOH A . 
F 5 HOH 203 603 184 HOH HOH A . 
F 5 HOH 204 604 174 HOH HOH A . 
F 5 HOH 205 605 127 HOH HOH A . 
F 5 HOH 206 606 222 HOH HOH A . 
F 5 HOH 207 607 219 HOH HOH A . 
F 5 HOH 208 608 189 HOH HOH A . 
F 5 HOH 209 609 31  HOH HOH A . 
F 5 HOH 210 610 227 HOH HOH A . 
F 5 HOH 211 611 193 HOH HOH A . 
F 5 HOH 212 612 119 HOH HOH A . 
F 5 HOH 213 613 211 HOH HOH A . 
F 5 HOH 214 614 114 HOH HOH A . 
F 5 HOH 215 615 228 HOH HOH A . 
F 5 HOH 216 616 195 HOH HOH A . 
F 5 HOH 217 617 216 HOH HOH A . 
F 5 HOH 218 618 179 HOH HOH A . 
F 5 HOH 219 619 156 HOH HOH A . 
F 5 HOH 220 620 185 HOH HOH A . 
F 5 HOH 221 621 223 HOH HOH A . 
F 5 HOH 222 622 188 HOH HOH A . 
F 5 HOH 223 623 117 HOH HOH A . 
F 5 HOH 224 624 55  HOH HOH A . 
F 5 HOH 225 625 150 HOH HOH A . 
F 5 HOH 226 626 196 HOH HOH A . 
F 5 HOH 227 627 214 HOH HOH A . 
F 5 HOH 228 628 220 HOH HOH A . 
F 5 HOH 229 629 167 HOH HOH A . 
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1  1 Y 1 A LYS 9   ? CD  ? A LYS 9   CD  
2  1 Y 1 A LYS 9   ? CE  ? A LYS 9   CE  
3  1 Y 1 A LYS 9   ? NZ  ? A LYS 9   NZ  
4  1 Y 1 A LYS 80  ? CE  ? A LYS 80  CE  
5  1 Y 1 A LYS 80  ? NZ  ? A LYS 80  NZ  
6  1 Y 1 A LYS 168 ? NZ  ? A LYS 167 NZ  
7  1 Y 1 A LYS 170 ? NZ  ? A LYS 169 NZ  
8  1 Y 1 A LYS 172 ? CE  ? A LYS 171 CE  
9  1 Y 1 A LYS 172 ? NZ  ? A LYS 171 NZ  
10 1 Y 1 A LYS 213 ? CE  ? A LYS 212 CE  
11 1 Y 1 A LYS 213 ? NZ  ? A LYS 212 NZ  
12 1 Y 1 A LEU 224 ? CD1 ? A LEU 223 CD1 
13 1 Y 1 A LYS 228 ? CE  ? A LYS 227 CE  
14 1 Y 1 A LYS 228 ? NZ  ? A LYS 227 NZ  
15 1 Y 1 A GLU 239 ? CG  ? A GLU 238 CG  
16 1 Y 1 A GLU 239 ? CD  ? A GLU 238 CD  
17 1 Y 1 A GLU 239 ? OE1 ? A GLU 238 OE1 
18 1 Y 1 A GLU 239 ? OE2 ? A GLU 238 OE2 
19 1 Y 1 A GLN 255 ? CG  ? A GLN 254 CG  
20 1 Y 1 A GLN 255 ? CD  ? A GLN 254 CD  
21 1 Y 1 A GLN 255 ? OE1 ? A GLN 254 OE1 
22 1 Y 1 A GLN 255 ? NE2 ? A GLN 254 NE2 
23 1 Y 1 A LYS 257 ? CE  ? A LYS 256 CE  
24 1 Y 1 A LYS 257 ? NZ  ? A LYS 256 NZ  
25 1 Y 1 A LYS 261 ? CG  ? A LYS 260 CG  
26 1 Y 1 A LYS 261 ? CD  ? A LYS 260 CD  
27 1 Y 1 A LYS 261 ? CE  ? A LYS 260 CE  
28 1 Y 1 A LYS 261 ? NZ  ? A LYS 260 NZ  
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? 'data scaling'    ? ? ? ? ? ? ? ? ? ? ? SCALA       ? ? ? 3.3.20   1 
? refinement        ? ? ? ? ? ? ? ? ? ? ? REFMAC      ? ? ? 5.8.0232 2 
? 'data extraction' ? ? ? ? ? ? ? ? ? ? ? PDB_EXTRACT ? ? ? 3.25     3 
? 'data reduction'  ? ? ? ? ? ? ? ? ? ? ? XDS         ? ? ? .        4 
? phasing           ? ? ? ? ? ? ? ? ? ? ? MOLREP      ? ? ? .        5 
? 'model building'  ? ? ? ? ? ? ? ? ? ? ? Coot        ? ? ? .        6 
# 
_cell.angle_alpha                  90.000 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   103.780 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.000 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     6YHC 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     41.890 
_cell.length_a_esd                 ? 
_cell.length_b                     40.963 
_cell.length_b_esd                 ? 
_cell.length_c                     71.406 
_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                         6YHC 
_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                   6YHC 
_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            2.04 
_exptl_crystal.density_method              ? 
_exptl_crystal.density_percent_sol         39.59 
_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              ? 
_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 was 0.1M sodium BICINE, pH 9, 0.2 M ammonium sulfate and 2M sodium malonate pH 7 made from 1M sodium BICINE and 3.4M sodium malonate
;
_exptl_crystal_grow.pdbx_pH_range   ? 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS PILATUS 6M-F' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2013-05-21 
_diffrn_detector.pdbx_frequency               ? 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.976300 
_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        0.976300 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   'P13 (MX1)' 
_diffrn_source.pdbx_synchrotron_site       'PETRA III, EMBL c/o DESY' 
# 
_reflns.B_iso_Wilson_estimate            ? 
_reflns.entry_id                         6YHC 
_reflns.data_reduction_details           ? 
_reflns.data_reduction_method            ? 
_reflns.d_resolution_high                1.280 
_reflns.d_resolution_low                 40.963 
_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                       59961 
_reflns.number_obs                       59961 
_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             98.700 
_reflns.R_free_details                   ? 
_reflns.Rmerge_F_all                     ? 
_reflns.Rmerge_F_obs                     ? 
_reflns.Friedel_coverage                 ? 
_reflns.number_gt                        ? 
_reflns.threshold_expression             ? 
_reflns.pdbx_redundancy                  3.300 
_reflns.pdbx_Rmerge_I_obs                ? 
_reflns.pdbx_Rmerge_I_all                ? 
_reflns.pdbx_Rsym_value                  0.046 
_reflns.pdbx_netI_over_av_sigmaI         7.200 
_reflns.pdbx_netI_over_sigmaI            9.200 
_reflns.pdbx_res_netI_over_av_sigmaI_2   ? 
_reflns.pdbx_res_netI_over_sigmaI_2      ? 
_reflns.pdbx_chi_squared                 ? 
_reflns.pdbx_scaling_rejects             ? 
_reflns.pdbx_d_res_high_opt              ? 
_reflns.pdbx_d_res_low_opt               ? 
_reflns.pdbx_d_res_opt_method            ? 
_reflns.phase_calculation_details        ? 
_reflns.pdbx_Rrim_I_all                  0.060 
_reflns.pdbx_Rpim_I_all                  0.033 
_reflns.pdbx_d_opt                       ? 
_reflns.pdbx_number_measured_all         199179 
_reflns.pdbx_diffrn_id                   1 
_reflns.pdbx_ordinal                     1 
_reflns.pdbx_CC_half                     ? 
_reflns.pdbx_CC_star                     ? 
_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_CC_star 
_reflns_shell.pdbx_R_split 
1.280 1.350  ? 2.700  28295 ? ? ? 8628 98.200 ? ? ? ? 0.266 ? ? ? ? ? ? ? ? 3.300 0.266 ? ? 3.000  0.381 0.207 ? 1  1 ? ? ? 
1.350 1.430  ? 3.800  27028 ? ? ? 8217 98.400 ? ? ? ? 0.188 ? ? ? ? ? ? ? ? 3.300 0.188 ? ? 3.800  0.268 0.145 ? 2  1 ? ? ? 
1.430 1.530  ? 5.300  25354 ? ? ? 7740 98.600 ? ? ? ? 0.128 ? ? ? ? ? ? ? ? 3.300 0.128 ? ? 5.100  0.181 0.099 ? 3  1 ? ? ? 
1.530 1.650  ? 7.000  23381 ? ? ? 7214 98.700 ? ? ? ? 0.093 ? ? ? ? ? ? ? ? 3.200 0.093 ? ? 6.700  0.128 0.070 ? 4  1 ? ? ? 
1.650 1.810  ? 8.200  22205 ? ? ? 6641 98.700 ? ? ? ? 0.075 ? ? ? ? ? ? ? ? 3.300 0.075 ? ? 8.900  0.100 0.054 ? 5  1 ? ? ? 
1.810 2.020  ? 9.900  20716 ? ? ? 6062 99.100 ? ? ? ? 0.060 ? ? ? ? ? ? ? ? 3.400 0.060 ? ? 12.400 0.078 0.042 ? 6  1 ? ? ? 
2.020 2.340  ? 11.900 18354 ? ? ? 5368 99.200 ? ? ? ? 0.051 ? ? ? ? ? ? ? ? 3.400 0.051 ? ? 15.400 0.066 0.036 ? 7  1 ? ? ? 
2.340 2.860  ? 13.500 15377 ? ? ? 4532 99.300 ? ? ? ? 0.044 ? ? ? ? ? ? ? ? 3.400 0.044 ? ? 17.200 0.059 0.031 ? 8  1 ? ? ? 
2.860 4.050  ? 15.500 11944 ? ? ? 3548 99.100 ? ? ? ? 0.037 ? ? ? ? ? ? ? ? 3.400 0.037 ? ? 20.000 0.049 0.026 ? 9  1 ? ? ? 
4.050 40.963 ? 16.200 6525  ? ? ? 2011 99.600 ? ? ? ? 0.032 ? ? ? ? ? ? ? ? 3.200 0.032 ? ? 20.300 0.042 0.023 ? 10 1 ? ? ? 
# 
_refine.aniso_B[1][1]                            -0.6600 
_refine.aniso_B[1][2]                            0.0000 
_refine.aniso_B[1][3]                            0.5700 
_refine.aniso_B[2][2]                            -1.2100 
_refine.aniso_B[2][3]                            0.0000 
_refine.aniso_B[3][3]                            1.4300 
_refine.B_iso_max                                103.040 
_refine.B_iso_mean                               21.8240 
_refine.B_iso_min                                9.670 
_refine.correlation_coeff_Fo_to_Fc               0.9800 
_refine.correlation_coeff_Fo_to_Fc_free          0.9700 
_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                                 6YHC 
_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                            1.2800 
_refine.ls_d_res_low                             40.6800 
_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                     53768 
_refine.ls_number_reflns_R_free                  6002 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    98.3200 
_refine.ls_percent_reflns_R_free                 10.0000 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1346 
_refine.ls_R_factor_R_free                       0.1721 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1304 
_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.pdbx_R_complete                          ? 
_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                      4Q09 
_refine.pdbx_stereochemistry_target_values       ? 
_refine.pdbx_R_Free_selection_details            RANDOM 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       0.0470 
_refine.pdbx_overall_ESU_R_Free                  0.0480 
_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             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         final 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       1.2800 
_refine_hist.d_res_low                        40.6800 
_refine_hist.number_atoms_solvent             229 
_refine_hist.number_atoms_total               2303 
_refine_hist.number_reflns_all                ? 
_refine_hist.number_reflns_obs                ? 
_refine_hist.number_reflns_R_free             ? 
_refine_hist.number_reflns_R_work             ? 
_refine_hist.R_factor_all                     ? 
_refine_hist.R_factor_obs                     ? 
_refine_hist.R_factor_R_free                  ? 
_refine_hist.R_factor_R_work                  ? 
_refine_hist.pdbx_number_residues_total       257 
_refine_hist.pdbx_B_iso_mean_ligand           36.03 
_refine_hist.pdbx_B_iso_mean_solvent          34.83 
_refine_hist.pdbx_number_atoms_protein        2015 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         59 
_refine_hist.pdbx_number_atoms_lipid          ? 
_refine_hist.pdbx_number_atoms_carb           ? 
_refine_hist.pdbx_pseudo_atom_details         ? 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.criterion 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.number 
_refine_ls_restr.rejects 
_refine_ls_restr.type 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' ? 0.014  0.012  2210 ? r_bond_refined_d       ? ? 
'X-RAY DIFFRACTION' ? 2.068  1.672  3024 ? r_angle_refined_deg    ? ? 
'X-RAY DIFFRACTION' ? 6.985  5.000  273  ? r_dihedral_angle_1_deg ? ? 
'X-RAY DIFFRACTION' ? 36.587 23.654 104  ? r_dihedral_angle_2_deg ? ? 
'X-RAY DIFFRACTION' ? 12.884 15.000 345  ? r_dihedral_angle_3_deg ? ? 
'X-RAY DIFFRACTION' ? 19.449 15.000 7    ? r_dihedral_angle_4_deg ? ? 
'X-RAY DIFFRACTION' ? 0.128  0.200  270  ? r_chiral_restr         ? ? 
'X-RAY DIFFRACTION' ? 0.015  0.020  1739 ? r_gen_planes_refined   ? ? 
'X-RAY DIFFRACTION' ? 5.444  3.000  2210 ? r_rigid_bond_restr     ? ? 
'X-RAY DIFFRACTION' ? 26.215 5.000  125  ? r_sphericity_free      ? ? 
'X-RAY DIFFRACTION' ? 16.288 5.000  2244 ? r_sphericity_bonded    ? ? 
# 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.d_res_high                       1.2800 
_refine_ls_shell.d_res_low                        1.3130 
_refine_ls_shell.number_reflns_all                4355 
_refine_ls_shell.number_reflns_obs                ? 
_refine_ls_shell.number_reflns_R_free             429 
_refine_ls_shell.number_reflns_R_work             3926 
_refine_ls_shell.percent_reflns_obs               97.6700 
_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                  0.2370 
_refine_ls_shell.R_factor_R_free_error            0.0000 
_refine_ls_shell.R_factor_R_work                  0.1950 
_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_R_complete                  ? 
_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                     6YHC 
_struct.title                        
;Crystal structure of chimeric carbonic anhydrase XII with 3-(benzylamino)-2,5,6-trifluoro-4-[(2-hydroxyethyl)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        6YHC 
_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 4 ? 
E N N 4 ? 
F N N 5 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    CAH2_HUMAN 
_struct_ref.pdbx_db_accession          P00918 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;MSHHWGYGKHNGPEHWHKDFPIAKGERQSPVDIDTHTAKYDPSLKPLSVSYDQATSLRILNNGHAFNVEFDDSQDKAVLK
GGPLDGTYRLIQFHFHWGSLDGQGSEHTVDKKKYAAELHLVHWNTKYGDFGKAVQQPDGLAVLGIFLKVGSAKPGLQKVV
DVLDSIKTKGKSADFTNFDPRGLLPESLDYWTYPGSLTTPPLLECVTWIVLKEPISVSSEQVLKFRKLNFNGEGEPEELM
VDNWRPAQPLKNRQIKASFK
;
_struct_ref.pdbx_align_begin           1 
# 
_struct_ref_seq.align_id                      1 
_struct_ref_seq.ref_id                        1 
_struct_ref_seq.pdbx_PDB_id_code              6YHC 
_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 
# 
loop_
_struct_ref_seq_dif.align_id 
_struct_ref_seq_dif.pdbx_pdb_id_code 
_struct_ref_seq_dif.mon_id 
_struct_ref_seq_dif.pdbx_pdb_strand_id 
_struct_ref_seq_dif.seq_num 
_struct_ref_seq_dif.pdbx_pdb_ins_code 
_struct_ref_seq_dif.pdbx_seq_db_name 
_struct_ref_seq_dif.pdbx_seq_db_accession_code 
_struct_ref_seq_dif.db_mon_id 
_struct_ref_seq_dif.pdbx_seq_db_seq_num 
_struct_ref_seq_dif.details 
_struct_ref_seq_dif.pdbx_auth_seq_num 
_struct_ref_seq_dif.pdbx_ordinal 
1 6YHC SER A 65  ? UNP P00918 ALA 65  'engineered mutation' 65  1 
1 6YHC LYS A 67  ? UNP P00918 ASN 67  'engineered mutation' 67  2 
1 6YHC THR A 91  ? UNP P00918 ILE 91  'engineered mutation' 91  3 
1 6YHC ALA A 130 ? UNP P00918 PHE 130 'engineered mutation' 131 4 
1 6YHC SER A 134 ? UNP P00918 VAL 134 'engineered mutation' 135 5 
1 6YHC ASN A 203 ? UNP P00918 LEU 203 'engineered mutation' 204 6 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_and_software_defined_assembly 
_pdbx_struct_assembly.method_details       PISA 
_pdbx_struct_assembly.oligomeric_details   monomeric 
_pdbx_struct_assembly.oligomeric_count     1 
# 
loop_
_pdbx_struct_assembly_prop.biol_id 
_pdbx_struct_assembly_prop.type 
_pdbx_struct_assembly_prop.value 
_pdbx_struct_assembly_prop.details 
1 'ABSA (A^2)' 230   ? 
1 MORE         2     ? 
1 'SSA (A^2)'  11220 ? 
# 
_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 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   none 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1 AA1 GLY A 12  ? ASP A 19  ? GLY A 12  ASP A 19  5 ? 8 
HELX_P HELX_P2 AA2 PHE A 20  ? GLY A 25  ? PHE A 20  GLY A 25  5 ? 6 
HELX_P HELX_P3 AA3 LYS A 126 ? GLY A 128 ? LYS A 127 GLY A 129 5 ? 3 
HELX_P HELX_P4 AA4 ASP A 129 ? SER A 134 ? ASP A 130 SER A 135 1 ? 6 
HELX_P HELX_P5 AA5 LYS A 153 ? GLY A 155 ? LYS A 154 GLY A 156 5 ? 3 
HELX_P HELX_P6 AA6 LEU A 156 ? LEU A 163 ? LEU A 157 LEU A 164 1 ? 8 
HELX_P HELX_P7 AA7 ASP A 164 ? LYS A 167 ? ASP A 165 LYS A 168 5 ? 4 
HELX_P HELX_P8 AA8 ASP A 179 ? LEU A 184 ? ASP A 180 LEU A 185 5 ? 6 
HELX_P HELX_P9 AA9 SER A 218 ? ARG A 226 ? SER A 219 ARG A 227 1 ? 9 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
metalc1 metalc ? ? A HIS 94  NE2 ? ? ? 1_555 B ZN  . ZN  ? ? A HIS 94  A ZN  301 1_555 ? ? ? ? ? ? ? 1.971 ? ? 
metalc2 metalc ? ? A HIS 96  NE2 ? ? ? 1_555 B ZN  . ZN  ? ? A HIS 96  A ZN  301 1_555 ? ? ? ? ? ? ? 2.032 ? ? 
metalc3 metalc ? ? A HIS 119 ND1 ? ? ? 1_555 B ZN  . ZN  ? ? A HIS 119 A ZN  301 1_555 ? ? ? ? ? ? ? 2.074 ? ? 
metalc4 metalc ? ? B ZN  .   ZN  ? ? ? 1_555 D WWO . N10 ? ? A ZN  301 A WWO 303 1_555 ? ? ? ? ? ? ? 1.920 ? ? 
# 
_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_555 103.4 ? 
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_555 111.4 ? 
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_555 100.2 ? 
4 NE2 ? A HIS 94  ? A HIS 94  ? 1_555 ZN ? B ZN . ? A ZN 301 ? 1_555 N10 ? D WWO .   ? A WWO 303 ? 1_555 116.8 ? 
5 NE2 ? A HIS 96  ? A HIS 96  ? 1_555 ZN ? B ZN . ? A ZN 301 ? 1_555 N10 ? D WWO .   ? A WWO 303 ? 1_555 116.9 ? 
6 ND1 ? A HIS 119 ? A HIS 119 ? 1_555 ZN ? B ZN . ? A ZN 301 ? 1_555 N10 ? D WWO .   ? A WWO 303 ? 1_555 107.0 ? 
# 
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 0.31 
2 PRO 200 A . ? PRO 201 A PRO 201 A ? PRO 202 A 1 9.52 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 2  ? 
AA2 ? 10 ? 
AA3 ? 6  ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2  ? parallel      
AA2 1 2  ? parallel      
AA2 2 3  ? anti-parallel 
AA2 3 4  ? anti-parallel 
AA2 4 5  ? parallel      
AA2 5 6  ? anti-parallel 
AA2 6 7  ? anti-parallel 
AA2 7 8  ? anti-parallel 
AA2 8 9  ? anti-parallel 
AA2 9 10 ? anti-parallel 
AA3 1 2  ? anti-parallel 
AA3 2 3  ? anti-parallel 
AA3 3 4  ? anti-parallel 
AA3 4 5  ? anti-parallel 
AA3 5 6  ? parallel      
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1  ASP A 32  ? ILE A 33  ? ASP A 32  ILE A 33  
AA1 2  THR A 108 ? VAL A 109 ? THR A 108 VAL A 109 
AA2 1  LYS A 39  ? TYR A 40  ? LYS A 39  TYR A 40  
AA2 2  LYS A 256 ? ALA A 257 ? LYS A 257 ALA A 258 
AA2 3  TYR A 190 ? GLY A 195 ? TYR A 191 GLY A 196 
AA2 4  VAL A 206 ? LEU A 211 ? VAL A 207 LEU A 212 
AA2 5  LEU A 140 ? VAL A 149 ? LEU A 141 VAL A 150 
AA2 6  ALA A 116 ? ASN A 124 ? ALA A 116 ASN A 124 
AA2 7  TYR A 88  ? TRP A 97  ? TYR A 88  TRP A 97  
AA2 8  PHE A 66  ? PHE A 70  ? PHE A 66  PHE A 70  
AA2 9  SER A 56  ? ASN A 61  ? SER A 56  ASN A 61  
AA2 10 SER A 172 ? ASP A 174 ? SER A 173 ASP A 175 
AA3 1  LEU A 47  ? SER A 50  ? LEU A 47  SER A 50  
AA3 2  VAL A 78  ? GLY A 81  ? VAL A 78  GLY A 81  
AA3 3  TYR A 88  ? TRP A 97  ? TYR A 88  TRP A 97  
AA3 4  ALA A 116 ? ASN A 124 ? ALA A 116 ASN A 124 
AA3 5  LEU A 140 ? VAL A 149 ? LEU A 141 VAL A 150 
AA3 6  ILE A 215 ? VAL A 217 ? ILE A 216 VAL A 218 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2  N ILE A 33  ? N ILE A 33  O THR A 108 ? O THR A 108 
AA2 1 2  N LYS A 39  ? N LYS A 39  O ALA A 257 ? O ALA A 258 
AA2 2 3  O LYS A 256 ? O LYS A 257 N THR A 192 ? N THR A 193 
AA2 3 4  N GLY A 195 ? N GLY A 196 O VAL A 206 ? O VAL A 207 
AA2 4 5  O 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 VAL A 121 ? O VAL A 121 N GLN A 92  ? N GLN A 92  
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 50  ? N SER A 50  O VAL A 78  ? O VAL A 78  
AA3 2 3  N LEU A 79  ? N LEU A 79  O TYR A 88  ? O TYR A 88  
AA3 3 4  N GLN A 92  ? N GLN A 92  O VAL A 121 ? O VAL A 121 
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 ? 3  'binding site for residue DMS A 302' 
AC3 Software A WWO 303 ? 16 'binding site for residue WWO A 303' 
AC4 Software A WWO 304 ? 10 'binding site for residue WWO A 304' 
# 
loop_
_struct_site_gen.id 
_struct_site_gen.site_id 
_struct_site_gen.pdbx_num_res 
_struct_site_gen.label_comp_id 
_struct_site_gen.label_asym_id 
_struct_site_gen.label_seq_id 
_struct_site_gen.pdbx_auth_ins_code 
_struct_site_gen.auth_comp_id 
_struct_site_gen.auth_asym_id 
_struct_site_gen.auth_seq_id 
_struct_site_gen.label_atom_id 
_struct_site_gen.label_alt_id 
_struct_site_gen.symmetry 
_struct_site_gen.details 
1  AC1 4  HIS A 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  WWO D .   ? WWO A 303 . ? 1_555 ? 
5  AC2 3  TYR A 7   ? TYR A 7   . ? 1_555 ? 
6  AC2 3  ASP A 242 ? ASP A 243 . ? 1_555 ? 
7  AC2 3  TRP A 244 ? TRP A 245 . ? 1_555 ? 
8  AC3 16 ASN A 62  ? ASN A 62  . ? 1_555 ? 
9  AC3 16 HIS A 64  ? HIS A 64  . ? 1_555 ? 
10 AC3 16 LYS A 67  ? LYS A 67  . ? 1_555 ? 
11 AC3 16 GLN A 92  ? GLN A 92  . ? 1_555 ? 
12 AC3 16 HIS A 94  ? HIS A 94  . ? 1_555 ? 
13 AC3 16 HIS A 96  ? HIS A 96  . ? 1_555 ? 
14 AC3 16 HIS A 119 ? HIS A 119 . ? 1_555 ? 
15 AC3 16 VAL A 121 ? VAL A 121 . ? 1_555 ? 
16 AC3 16 LEU A 197 ? LEU A 198 . ? 1_555 ? 
17 AC3 16 THR A 198 ? THR A 199 . ? 1_555 ? 
18 AC3 16 THR A 199 ? THR A 200 . ? 1_555 ? 
19 AC3 16 PRO A 200 ? PRO A 201 . ? 1_555 ? 
20 AC3 16 PRO A 201 ? PRO A 202 . ? 1_555 ? 
21 AC3 16 ZN  B .   ? ZN  A 301 . ? 1_555 ? 
22 AC3 16 HOH F .   ? HOH A 412 . ? 1_555 ? 
23 AC3 16 HOH F .   ? HOH A 507 . ? 1_555 ? 
24 AC4 10 HIS A 4   ? HIS A 4   . ? 1_455 ? 
25 AC4 10 HIS A 10  ? HIS A 10  . ? 1_455 ? 
26 AC4 10 ASN A 11  ? ASN A 11  . ? 1_455 ? 
27 AC4 10 PRO A 154 ? PRO A 155 . ? 1_555 ? 
28 AC4 10 GLY A 155 ? GLY A 156 . ? 1_555 ? 
29 AC4 10 PHE A 178 ? PHE A 179 . ? 1_555 ? 
30 AC4 10 ASP A 179 ? ASP A 180 . ? 1_555 ? 
31 AC4 10 ARG A 181 ? ARG A 182 . ? 1_555 ? 
32 AC4 10 GLY A 182 ? GLY A 183 . ? 1_555 ? 
33 AC4 10 HOH F .   ? HOH A 448 . ? 1_555 ? 
# 
_pdbx_validate_rmsd_bond.id                        1 
_pdbx_validate_rmsd_bond.PDB_model_num             1 
_pdbx_validate_rmsd_bond.auth_atom_id_1            CG 
_pdbx_validate_rmsd_bond.auth_asym_id_1            A 
_pdbx_validate_rmsd_bond.auth_comp_id_1            HIS 
_pdbx_validate_rmsd_bond.auth_seq_id_1             36 
_pdbx_validate_rmsd_bond.PDB_ins_code_1            ? 
_pdbx_validate_rmsd_bond.label_alt_id_1            ? 
_pdbx_validate_rmsd_bond.auth_atom_id_2            CD2 
_pdbx_validate_rmsd_bond.auth_asym_id_2            A 
_pdbx_validate_rmsd_bond.auth_comp_id_2            HIS 
_pdbx_validate_rmsd_bond.auth_seq_id_2             36 
_pdbx_validate_rmsd_bond.PDB_ins_code_2            ? 
_pdbx_validate_rmsd_bond.label_alt_id_2            ? 
_pdbx_validate_rmsd_bond.bond_value                1.411 
_pdbx_validate_rmsd_bond.bond_target_value         1.354 
_pdbx_validate_rmsd_bond.bond_deviation            0.057 
_pdbx_validate_rmsd_bond.bond_standard_deviation   0.009 
_pdbx_validate_rmsd_bond.linker_flag               N 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 ARG A 27  ? ? -143.57 56.28   
2 1 HIS A 64  ? B -145.44 -10.17  
3 1 ASN A 244 ? ? -95.41  50.53   
4 1 LYS A 252 ? ? 56.34   -135.22 
# 
_pdbx_entry_details.entry_id                 6YHC 
_pdbx_entry_details.has_ligand_of_interest   Y 
_pdbx_entry_details.compound_details         ? 
_pdbx_entry_details.source_details           ? 
_pdbx_entry_details.nonpolymer_details       ? 
_pdbx_entry_details.sequence_details         ? 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1 1 Y 1 A MET 1 ? A MET 1 
2 1 Y 1 A SER 2 ? A SER 2 
3 1 Y 1 A HIS 3 ? A HIS 3 
# 
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  
GLN N    N  N N 98  
GLN CA   C  N S 99  
GLN C    C  N N 100 
GLN O    O  N N 101 
GLN CB   C  N N 102 
GLN CG   C  N N 103 
GLN CD   C  N N 104 
GLN OE1  O  N N 105 
GLN NE2  N  N N 106 
GLN OXT  O  N N 107 
GLN H    H  N N 108 
GLN H2   H  N N 109 
GLN HA   H  N N 110 
GLN HB2  H  N N 111 
GLN HB3  H  N N 112 
GLN HG2  H  N N 113 
GLN HG3  H  N N 114 
GLN HE21 H  N N 115 
GLN HE22 H  N N 116 
GLN HXT  H  N N 117 
GLU N    N  N N 118 
GLU CA   C  N S 119 
GLU C    C  N N 120 
GLU O    O  N N 121 
GLU CB   C  N N 122 
GLU CG   C  N N 123 
GLU CD   C  N N 124 
GLU OE1  O  N N 125 
GLU OE2  O  N N 126 
GLU OXT  O  N N 127 
GLU H    H  N N 128 
GLU H2   H  N N 129 
GLU HA   H  N N 130 
GLU HB2  H  N N 131 
GLU HB3  H  N N 132 
GLU HG2  H  N N 133 
GLU HG3  H  N N 134 
GLU HE2  H  N N 135 
GLU HXT  H  N N 136 
GLY N    N  N N 137 
GLY CA   C  N N 138 
GLY C    C  N N 139 
GLY O    O  N N 140 
GLY OXT  O  N N 141 
GLY H    H  N N 142 
GLY H2   H  N N 143 
GLY HA2  H  N N 144 
GLY HA3  H  N N 145 
GLY HXT  H  N N 146 
HIS N    N  N N 147 
HIS CA   C  N S 148 
HIS C    C  N N 149 
HIS O    O  N N 150 
HIS CB   C  N N 151 
HIS CG   C  Y N 152 
HIS ND1  N  Y N 153 
HIS CD2  C  Y N 154 
HIS CE1  C  Y N 155 
HIS NE2  N  Y N 156 
HIS OXT  O  N N 157 
HIS H    H  N N 158 
HIS H2   H  N N 159 
HIS HA   H  N N 160 
HIS HB2  H  N N 161 
HIS HB3  H  N N 162 
HIS HD1  H  N N 163 
HIS HD2  H  N N 164 
HIS HE1  H  N N 165 
HIS HE2  H  N N 166 
HIS HXT  H  N N 167 
HOH O    O  N N 168 
HOH H1   H  N N 169 
HOH H2   H  N N 170 
ILE N    N  N N 171 
ILE CA   C  N S 172 
ILE C    C  N N 173 
ILE O    O  N N 174 
ILE CB   C  N S 175 
ILE CG1  C  N N 176 
ILE CG2  C  N N 177 
ILE CD1  C  N N 178 
ILE OXT  O  N N 179 
ILE H    H  N N 180 
ILE H2   H  N N 181 
ILE HA   H  N N 182 
ILE HB   H  N N 183 
ILE HG12 H  N N 184 
ILE HG13 H  N N 185 
ILE HG21 H  N N 186 
ILE HG22 H  N N 187 
ILE HG23 H  N N 188 
ILE HD11 H  N N 189 
ILE HD12 H  N N 190 
ILE HD13 H  N N 191 
ILE HXT  H  N N 192 
LEU N    N  N N 193 
LEU CA   C  N S 194 
LEU C    C  N N 195 
LEU O    O  N N 196 
LEU CB   C  N N 197 
LEU CG   C  N N 198 
LEU CD1  C  N N 199 
LEU CD2  C  N N 200 
LEU OXT  O  N N 201 
LEU H    H  N N 202 
LEU H2   H  N N 203 
LEU HA   H  N N 204 
LEU HB2  H  N N 205 
LEU HB3  H  N N 206 
LEU HG   H  N N 207 
LEU HD11 H  N N 208 
LEU HD12 H  N N 209 
LEU HD13 H  N N 210 
LEU HD21 H  N N 211 
LEU HD22 H  N N 212 
LEU HD23 H  N N 213 
LEU HXT  H  N N 214 
LYS N    N  N N 215 
LYS CA   C  N S 216 
LYS C    C  N N 217 
LYS O    O  N N 218 
LYS CB   C  N N 219 
LYS CG   C  N N 220 
LYS CD   C  N N 221 
LYS CE   C  N N 222 
LYS NZ   N  N N 223 
LYS OXT  O  N N 224 
LYS H    H  N N 225 
LYS H2   H  N N 226 
LYS HA   H  N N 227 
LYS HB2  H  N N 228 
LYS HB3  H  N N 229 
LYS HG2  H  N N 230 
LYS HG3  H  N N 231 
LYS HD2  H  N N 232 
LYS HD3  H  N N 233 
LYS HE2  H  N N 234 
LYS HE3  H  N N 235 
LYS HZ1  H  N N 236 
LYS HZ2  H  N N 237 
LYS HZ3  H  N N 238 
LYS HXT  H  N N 239 
MET N    N  N N 240 
MET CA   C  N S 241 
MET C    C  N N 242 
MET O    O  N N 243 
MET CB   C  N N 244 
MET CG   C  N N 245 
MET SD   S  N N 246 
MET CE   C  N N 247 
MET OXT  O  N N 248 
MET H    H  N N 249 
MET H2   H  N N 250 
MET HA   H  N N 251 
MET HB2  H  N N 252 
MET HB3  H  N N 253 
MET HG2  H  N N 254 
MET HG3  H  N N 255 
MET HE1  H  N N 256 
MET HE2  H  N N 257 
MET HE3  H  N N 258 
MET HXT  H  N N 259 
PHE N    N  N N 260 
PHE CA   C  N S 261 
PHE C    C  N N 262 
PHE O    O  N N 263 
PHE CB   C  N N 264 
PHE CG   C  Y N 265 
PHE CD1  C  Y N 266 
PHE CD2  C  Y N 267 
PHE CE1  C  Y N 268 
PHE CE2  C  Y N 269 
PHE CZ   C  Y N 270 
PHE OXT  O  N N 271 
PHE H    H  N N 272 
PHE H2   H  N N 273 
PHE HA   H  N N 274 
PHE HB2  H  N N 275 
PHE HB3  H  N N 276 
PHE HD1  H  N N 277 
PHE HD2  H  N N 278 
PHE HE1  H  N N 279 
PHE HE2  H  N N 280 
PHE HZ   H  N N 281 
PHE HXT  H  N N 282 
PRO N    N  N N 283 
PRO CA   C  N S 284 
PRO C    C  N N 285 
PRO O    O  N N 286 
PRO CB   C  N N 287 
PRO CG   C  N N 288 
PRO CD   C  N N 289 
PRO OXT  O  N N 290 
PRO H    H  N N 291 
PRO HA   H  N N 292 
PRO HB2  H  N N 293 
PRO HB3  H  N N 294 
PRO HG2  H  N N 295 
PRO HG3  H  N N 296 
PRO HD2  H  N N 297 
PRO HD3  H  N N 298 
PRO HXT  H  N N 299 
SER N    N  N N 300 
SER CA   C  N S 301 
SER C    C  N N 302 
SER O    O  N N 303 
SER CB   C  N N 304 
SER OG   O  N N 305 
SER OXT  O  N N 306 
SER H    H  N N 307 
SER H2   H  N N 308 
SER HA   H  N N 309 
SER HB2  H  N N 310 
SER HB3  H  N N 311 
SER HG   H  N N 312 
SER HXT  H  N N 313 
THR N    N  N N 314 
THR CA   C  N S 315 
THR C    C  N N 316 
THR O    O  N N 317 
THR CB   C  N R 318 
THR OG1  O  N N 319 
THR CG2  C  N N 320 
THR OXT  O  N N 321 
THR H    H  N N 322 
THR H2   H  N N 323 
THR HA   H  N N 324 
THR HB   H  N N 325 
THR HG1  H  N N 326 
THR HG21 H  N N 327 
THR HG22 H  N N 328 
THR HG23 H  N N 329 
THR HXT  H  N N 330 
TRP N    N  N N 331 
TRP CA   C  N S 332 
TRP C    C  N N 333 
TRP O    O  N N 334 
TRP CB   C  N N 335 
TRP CG   C  Y N 336 
TRP CD1  C  Y N 337 
TRP CD2  C  Y N 338 
TRP NE1  N  Y N 339 
TRP CE2  C  Y N 340 
TRP CE3  C  Y N 341 
TRP CZ2  C  Y N 342 
TRP CZ3  C  Y N 343 
TRP CH2  C  Y N 344 
TRP OXT  O  N N 345 
TRP H    H  N N 346 
TRP H2   H  N N 347 
TRP HA   H  N N 348 
TRP HB2  H  N N 349 
TRP HB3  H  N N 350 
TRP HD1  H  N N 351 
TRP HE1  H  N N 352 
TRP HE3  H  N N 353 
TRP HZ2  H  N N 354 
TRP HZ3  H  N N 355 
TRP HH2  H  N N 356 
TRP HXT  H  N N 357 
TYR N    N  N N 358 
TYR CA   C  N S 359 
TYR C    C  N N 360 
TYR O    O  N N 361 
TYR CB   C  N N 362 
TYR CG   C  Y N 363 
TYR CD1  C  Y N 364 
TYR CD2  C  Y N 365 
TYR CE1  C  Y N 366 
TYR CE2  C  Y N 367 
TYR CZ   C  Y N 368 
TYR OH   O  N N 369 
TYR OXT  O  N N 370 
TYR H    H  N N 371 
TYR H2   H  N N 372 
TYR HA   H  N N 373 
TYR HB2  H  N N 374 
TYR HB3  H  N N 375 
TYR HD1  H  N N 376 
TYR HD2  H  N N 377 
TYR HE1  H  N N 378 
TYR HE2  H  N N 379 
TYR HH   H  N N 380 
TYR HXT  H  N N 381 
VAL N    N  N N 382 
VAL CA   C  N S 383 
VAL C    C  N N 384 
VAL O    O  N N 385 
VAL CB   C  N N 386 
VAL CG1  C  N N 387 
VAL CG2  C  N N 388 
VAL OXT  O  N N 389 
VAL H    H  N N 390 
VAL H2   H  N N 391 
VAL HA   H  N N 392 
VAL HB   H  N N 393 
VAL HG11 H  N N 394 
VAL HG12 H  N N 395 
VAL HG13 H  N N 396 
VAL HG21 H  N N 397 
VAL HG22 H  N N 398 
VAL HG23 H  N N 399 
VAL HXT  H  N N 400 
WWO F27  F  N N 401 
WWO C5   C  Y N 402 
WWO C4   C  Y N 403 
WWO S7   S  N N 404 
WWO O9   O  N N 405 
WWO N10  N  N N 406 
WWO O8   O  N N 407 
WWO C3   C  Y N 408 
WWO F12  F  N N 409 
WWO C2   C  Y N 410 
WWO F13  F  N N 411 
WWO C6   C  Y N 412 
WWO C1   C  Y N 413 
WWO S11  S  N N 414 
WWO O22  O  N N 415 
WWO O23  O  N N 416 
WWO C21  C  N N 417 
WWO C24  C  N N 418 
WWO O25  O  N N 419 
WWO N26  N  N N 420 
WWO C14  C  N N 421 
WWO C15  C  Y N 422 
WWO C20  C  Y N 423 
WWO C19  C  Y N 424 
WWO C18  C  Y N 425 
WWO C17  C  Y N 426 
WWO C16  C  Y N 427 
WWO H1   H  N N 428 
WWO H2   H  N N 429 
WWO H3   H  N N 430 
WWO H4   H  N N 431 
WWO H5   H  N N 432 
WWO H6   H  N N 433 
WWO H7   H  N N 434 
WWO H8   H  N N 435 
WWO H9   H  N N 436 
WWO H10  H  N N 437 
WWO H11  H  N N 438 
WWO H12  H  N N 439 
WWO H13  H  N N 440 
WWO H14  H  N N 441 
WWO H15  H  N N 442 
ZN  ZN   ZN N N 443 
# 
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  
GLN N   CA   sing N N 92  
GLN N   H    sing N N 93  
GLN N   H2   sing N N 94  
GLN CA  C    sing N N 95  
GLN CA  CB   sing N N 96  
GLN CA  HA   sing N N 97  
GLN C   O    doub N N 98  
GLN C   OXT  sing N N 99  
GLN CB  CG   sing N N 100 
GLN CB  HB2  sing N N 101 
GLN CB  HB3  sing N N 102 
GLN CG  CD   sing N N 103 
GLN CG  HG2  sing N N 104 
GLN CG  HG3  sing N N 105 
GLN CD  OE1  doub N N 106 
GLN CD  NE2  sing N N 107 
GLN NE2 HE21 sing N N 108 
GLN NE2 HE22 sing N N 109 
GLN OXT HXT  sing N N 110 
GLU N   CA   sing N N 111 
GLU N   H    sing N N 112 
GLU N   H2   sing N N 113 
GLU CA  C    sing N N 114 
GLU CA  CB   sing N N 115 
GLU CA  HA   sing N N 116 
GLU C   O    doub N N 117 
GLU C   OXT  sing N N 118 
GLU CB  CG   sing N N 119 
GLU CB  HB2  sing N N 120 
GLU CB  HB3  sing N N 121 
GLU CG  CD   sing N N 122 
GLU CG  HG2  sing N N 123 
GLU CG  HG3  sing N N 124 
GLU CD  OE1  doub N N 125 
GLU CD  OE2  sing N N 126 
GLU OE2 HE2  sing N N 127 
GLU OXT HXT  sing N N 128 
GLY N   CA   sing N N 129 
GLY N   H    sing N N 130 
GLY N   H2   sing N N 131 
GLY CA  C    sing N N 132 
GLY CA  HA2  sing N N 133 
GLY CA  HA3  sing N N 134 
GLY C   O    doub N N 135 
GLY C   OXT  sing N N 136 
GLY OXT HXT  sing N N 137 
HIS N   CA   sing N N 138 
HIS N   H    sing N N 139 
HIS N   H2   sing N N 140 
HIS CA  C    sing N N 141 
HIS CA  CB   sing N N 142 
HIS CA  HA   sing N N 143 
HIS C   O    doub N N 144 
HIS C   OXT  sing N N 145 
HIS CB  CG   sing N N 146 
HIS CB  HB2  sing N N 147 
HIS CB  HB3  sing N N 148 
HIS CG  ND1  sing Y N 149 
HIS CG  CD2  doub Y N 150 
HIS ND1 CE1  doub Y N 151 
HIS ND1 HD1  sing N N 152 
HIS CD2 NE2  sing Y N 153 
HIS CD2 HD2  sing N N 154 
HIS CE1 NE2  sing Y N 155 
HIS CE1 HE1  sing N N 156 
HIS NE2 HE2  sing N N 157 
HIS OXT HXT  sing N N 158 
HOH O   H1   sing N N 159 
HOH O   H2   sing N N 160 
ILE N   CA   sing N N 161 
ILE N   H    sing N N 162 
ILE N   H2   sing N N 163 
ILE CA  C    sing N N 164 
ILE CA  CB   sing N N 165 
ILE CA  HA   sing N N 166 
ILE C   O    doub N N 167 
ILE C   OXT  sing N N 168 
ILE CB  CG1  sing N N 169 
ILE CB  CG2  sing N N 170 
ILE CB  HB   sing N N 171 
ILE CG1 CD1  sing N N 172 
ILE CG1 HG12 sing N N 173 
ILE CG1 HG13 sing N N 174 
ILE CG2 HG21 sing N N 175 
ILE CG2 HG22 sing N N 176 
ILE CG2 HG23 sing N N 177 
ILE CD1 HD11 sing N N 178 
ILE CD1 HD12 sing N N 179 
ILE CD1 HD13 sing N N 180 
ILE OXT HXT  sing N N 181 
LEU N   CA   sing N N 182 
LEU N   H    sing N N 183 
LEU N   H2   sing N N 184 
LEU CA  C    sing N N 185 
LEU CA  CB   sing N N 186 
LEU CA  HA   sing N N 187 
LEU C   O    doub N N 188 
LEU C   OXT  sing N N 189 
LEU CB  CG   sing N N 190 
LEU CB  HB2  sing N N 191 
LEU CB  HB3  sing N N 192 
LEU CG  CD1  sing N N 193 
LEU CG  CD2  sing N N 194 
LEU CG  HG   sing N N 195 
LEU CD1 HD11 sing N N 196 
LEU CD1 HD12 sing N N 197 
LEU CD1 HD13 sing N N 198 
LEU CD2 HD21 sing N N 199 
LEU CD2 HD22 sing N N 200 
LEU CD2 HD23 sing N N 201 
LEU OXT HXT  sing N N 202 
LYS N   CA   sing N N 203 
LYS N   H    sing N N 204 
LYS N   H2   sing N N 205 
LYS CA  C    sing N N 206 
LYS CA  CB   sing N N 207 
LYS CA  HA   sing N N 208 
LYS C   O    doub N N 209 
LYS C   OXT  sing N N 210 
LYS CB  CG   sing N N 211 
LYS CB  HB2  sing N N 212 
LYS CB  HB3  sing N N 213 
LYS CG  CD   sing N N 214 
LYS CG  HG2  sing N N 215 
LYS CG  HG3  sing N N 216 
LYS CD  CE   sing N N 217 
LYS CD  HD2  sing N N 218 
LYS CD  HD3  sing N N 219 
LYS CE  NZ   sing N N 220 
LYS CE  HE2  sing N N 221 
LYS CE  HE3  sing N N 222 
LYS NZ  HZ1  sing N N 223 
LYS NZ  HZ2  sing N N 224 
LYS NZ  HZ3  sing N N 225 
LYS OXT HXT  sing N N 226 
MET N   CA   sing N N 227 
MET N   H    sing N N 228 
MET N   H2   sing N N 229 
MET CA  C    sing N N 230 
MET CA  CB   sing N N 231 
MET CA  HA   sing N N 232 
MET C   O    doub N N 233 
MET C   OXT  sing N N 234 
MET CB  CG   sing N N 235 
MET CB  HB2  sing N N 236 
MET CB  HB3  sing N N 237 
MET CG  SD   sing N N 238 
MET CG  HG2  sing N N 239 
MET CG  HG3  sing N N 240 
MET SD  CE   sing N N 241 
MET CE  HE1  sing N N 242 
MET CE  HE2  sing N N 243 
MET CE  HE3  sing N N 244 
MET OXT HXT  sing N N 245 
PHE N   CA   sing N N 246 
PHE N   H    sing N N 247 
PHE N   H2   sing N N 248 
PHE CA  C    sing N N 249 
PHE CA  CB   sing N N 250 
PHE CA  HA   sing N N 251 
PHE C   O    doub N N 252 
PHE C   OXT  sing N N 253 
PHE CB  CG   sing N N 254 
PHE CB  HB2  sing N N 255 
PHE CB  HB3  sing N N 256 
PHE CG  CD1  doub Y N 257 
PHE CG  CD2  sing Y N 258 
PHE CD1 CE1  sing Y N 259 
PHE CD1 HD1  sing N N 260 
PHE CD2 CE2  doub Y N 261 
PHE CD2 HD2  sing N N 262 
PHE CE1 CZ   doub Y N 263 
PHE CE1 HE1  sing N N 264 
PHE CE2 CZ   sing Y N 265 
PHE CE2 HE2  sing N N 266 
PHE CZ  HZ   sing N N 267 
PHE OXT HXT  sing N N 268 
PRO N   CA   sing N N 269 
PRO N   CD   sing N N 270 
PRO N   H    sing N N 271 
PRO CA  C    sing N N 272 
PRO CA  CB   sing N N 273 
PRO CA  HA   sing N N 274 
PRO C   O    doub N N 275 
PRO C   OXT  sing N N 276 
PRO CB  CG   sing N N 277 
PRO CB  HB2  sing N N 278 
PRO CB  HB3  sing N N 279 
PRO CG  CD   sing N N 280 
PRO CG  HG2  sing N N 281 
PRO CG  HG3  sing N N 282 
PRO CD  HD2  sing N N 283 
PRO CD  HD3  sing N N 284 
PRO OXT HXT  sing N N 285 
SER N   CA   sing N N 286 
SER N   H    sing N N 287 
SER N   H2   sing N N 288 
SER CA  C    sing N N 289 
SER CA  CB   sing N N 290 
SER CA  HA   sing N N 291 
SER C   O    doub N N 292 
SER C   OXT  sing N N 293 
SER CB  OG   sing N N 294 
SER CB  HB2  sing N N 295 
SER CB  HB3  sing N N 296 
SER OG  HG   sing N N 297 
SER OXT HXT  sing N N 298 
THR N   CA   sing N N 299 
THR N   H    sing N N 300 
THR N   H2   sing N N 301 
THR CA  C    sing N N 302 
THR CA  CB   sing N N 303 
THR CA  HA   sing N N 304 
THR C   O    doub N N 305 
THR C   OXT  sing N N 306 
THR CB  OG1  sing N N 307 
THR CB  CG2  sing N N 308 
THR CB  HB   sing N N 309 
THR OG1 HG1  sing N N 310 
THR CG2 HG21 sing N N 311 
THR CG2 HG22 sing N N 312 
THR CG2 HG23 sing N N 313 
THR OXT HXT  sing N N 314 
TRP N   CA   sing N N 315 
TRP N   H    sing N N 316 
TRP N   H2   sing N N 317 
TRP CA  C    sing N N 318 
TRP CA  CB   sing N N 319 
TRP CA  HA   sing N N 320 
TRP C   O    doub N N 321 
TRP C   OXT  sing N N 322 
TRP CB  CG   sing N N 323 
TRP CB  HB2  sing N N 324 
TRP CB  HB3  sing N N 325 
TRP CG  CD1  doub Y N 326 
TRP CG  CD2  sing Y N 327 
TRP CD1 NE1  sing Y N 328 
TRP CD1 HD1  sing N N 329 
TRP CD2 CE2  doub Y N 330 
TRP CD2 CE3  sing Y N 331 
TRP NE1 CE2  sing Y N 332 
TRP NE1 HE1  sing N N 333 
TRP CE2 CZ2  sing Y N 334 
TRP CE3 CZ3  doub Y N 335 
TRP CE3 HE3  sing N N 336 
TRP CZ2 CH2  doub Y N 337 
TRP CZ2 HZ2  sing N N 338 
TRP CZ3 CH2  sing Y N 339 
TRP CZ3 HZ3  sing N N 340 
TRP CH2 HH2  sing N N 341 
TRP OXT HXT  sing N N 342 
TYR N   CA   sing N N 343 
TYR N   H    sing N N 344 
TYR N   H2   sing N N 345 
TYR CA  C    sing N N 346 
TYR CA  CB   sing N N 347 
TYR CA  HA   sing N N 348 
TYR C   O    doub N N 349 
TYR C   OXT  sing N N 350 
TYR CB  CG   sing N N 351 
TYR CB  HB2  sing N N 352 
TYR CB  HB3  sing N N 353 
TYR CG  CD1  doub Y N 354 
TYR CG  CD2  sing Y N 355 
TYR CD1 CE1  sing Y N 356 
TYR CD1 HD1  sing N N 357 
TYR CD2 CE2  doub Y N 358 
TYR CD2 HD2  sing N N 359 
TYR CE1 CZ   doub Y N 360 
TYR CE1 HE1  sing N N 361 
TYR CE2 CZ   sing Y N 362 
TYR CE2 HE2  sing N N 363 
TYR CZ  OH   sing N N 364 
TYR OH  HH   sing N N 365 
TYR OXT HXT  sing N N 366 
VAL N   CA   sing N N 367 
VAL N   H    sing N N 368 
VAL N   H2   sing N N 369 
VAL CA  C    sing N N 370 
VAL CA  CB   sing N N 371 
VAL CA  HA   sing N N 372 
VAL C   O    doub N N 373 
VAL C   OXT  sing N N 374 
VAL CB  CG1  sing N N 375 
VAL CB  CG2  sing N N 376 
VAL CB  HB   sing N N 377 
VAL CG1 HG11 sing N N 378 
VAL CG1 HG12 sing N N 379 
VAL CG1 HG13 sing N N 380 
VAL CG2 HG21 sing N N 381 
VAL CG2 HG22 sing N N 382 
VAL CG2 HG23 sing N N 383 
VAL OXT HXT  sing N N 384 
WWO O9  S7   doub N N 385 
WWO S7  N10  sing N N 386 
WWO S7  C4   sing N N 387 
WWO S7  O8   doub N N 388 
WWO C16 C17  doub Y N 389 
WWO C16 C15  sing Y N 390 
WWO F27 C5   sing N N 391 
WWO C17 C18  sing Y N 392 
WWO C14 C15  sing N N 393 
WWO C14 N26  sing N N 394 
WWO C4  C5   doub Y N 395 
WWO C4  C3   sing Y N 396 
WWO C5  C6   sing Y N 397 
WWO C15 C20  doub Y N 398 
WWO C3  F12  sing N N 399 
WWO C3  C2   doub Y N 400 
WWO C6  N26  sing N N 401 
WWO C6  C1   doub Y N 402 
WWO O23 S11  doub N N 403 
WWO C18 C19  doub Y N 404 
WWO C2  C1   sing Y N 405 
WWO C2  F13  sing N N 406 
WWO C1  S11  sing N N 407 
WWO O22 S11  doub N N 408 
WWO C20 C19  sing Y N 409 
WWO S11 C21  sing N N 410 
WWO C21 C24  sing N N 411 
WWO O25 C24  sing N N 412 
WWO N10 H1   sing N N 413 
WWO N10 H2   sing N N 414 
WWO C21 H3   sing N N 415 
WWO C21 H4   sing N N 416 
WWO C24 H5   sing N N 417 
WWO C24 H6   sing N N 418 
WWO O25 H7   sing N N 419 
WWO N26 H8   sing N N 420 
WWO C14 H9   sing N N 421 
WWO C14 H10  sing N N 422 
WWO C20 H11  sing N N 423 
WWO C19 H12  sing N N 424 
WWO C18 H13  sing N N 425 
WWO C17 H14  sing N N 426 
WWO C16 H15  sing N N 427 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        WWO 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   WWO 
_pdbx_entity_instance_feature.auth_asym_id   ? 
_pdbx_entity_instance_feature.auth_seq_num   ? 
_pdbx_entity_instance_feature.feature_type   'SUBJECT OF INVESTIGATION' 
_pdbx_entity_instance_feature.details        ? 
# 
_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   4Q09 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    6YHC 
_atom_sites.Cartn_transf_matrix[1][1]   ? 
_atom_sites.Cartn_transf_matrix[1][2]   ? 
_atom_sites.Cartn_transf_matrix[1][3]   ? 
_atom_sites.Cartn_transf_matrix[2][1]   ? 
_atom_sites.Cartn_transf_matrix[2][2]   ? 
_atom_sites.Cartn_transf_matrix[2][3]   ? 
_atom_sites.Cartn_transf_matrix[3][1]   ? 
_atom_sites.Cartn_transf_matrix[3][2]   ? 
_atom_sites.Cartn_transf_matrix[3][3]   ? 
_atom_sites.Cartn_transf_vector[1]      ? 
_atom_sites.Cartn_transf_vector[2]      ? 
_atom_sites.Cartn_transf_vector[3]      ? 
_atom_sites.fract_transf_matrix[1][1]   0.023872 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.005853 
_atom_sites.fract_transf_matrix[2][1]   -0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.024412 
_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]   0.014419 
_atom_sites.fract_transf_vector[1]      0.000000 
_atom_sites.fract_transf_vector[2]      0.000000 
_atom_sites.fract_transf_vector[3]      0.000000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
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 4   ? 10.967  -0.894  7.251   1.00 57.84  ? 4   HIS A N   1 
ATOM   2    C  CA  . HIS A 1 4   ? 10.174  -0.121  8.196   1.00 37.86  ? 4   HIS A CA  1 
ATOM   3    C  C   . HIS A 1 4   ? 9.508   -1.105  9.156   1.00 33.65  ? 4   HIS A C   1 
ATOM   4    O  O   . HIS A 1 4   ? 9.790   -2.299  9.065   1.00 46.26  ? 4   HIS A O   1 
ATOM   5    C  CB  . HIS A 1 4   ? 9.189   0.812   7.445   1.00 35.20  ? 4   HIS A CB  1 
ATOM   6    C  CG  . HIS A 1 4   ? 8.933   2.012   8.269   1.00 38.55  ? 4   HIS A CG  1 
ATOM   7    N  ND1 . HIS A 1 4   ? 9.749   2.349   9.356   1.00 50.14  ? 4   HIS A ND1 1 
ATOM   8    C  CD2 . HIS A 1 4   ? 7.887   2.885   8.252   1.00 55.22  ? 4   HIS A CD2 1 
ATOM   9    C  CE1 . HIS A 1 4   ? 9.262   3.429   9.941   1.00 61.12  ? 4   HIS A CE1 1 
ATOM   10   N  NE2 . HIS A 1 4   ? 8.115   3.777   9.284   1.00 65.26  ? 4   HIS A NE2 1 
ATOM   11   N  N   . TRP A 1 5   ? 8.664   -0.601  10.076  1.00 31.10  ? 5   TRP A N   1 
ATOM   12   C  CA  . TRP A 1 5   ? 8.003   -1.468  11.039  1.00 23.08  ? 5   TRP A CA  1 
ATOM   13   C  C   . TRP A 1 5   ? 6.943   -2.311  10.336  1.00 22.24  ? 5   TRP A C   1 
ATOM   14   O  O   . TRP A 1 5   ? 6.383   -1.915  9.301   1.00 25.30  ? 5   TRP A O   1 
ATOM   15   C  CB  . TRP A 1 5   ? 7.340   -0.748  12.230  1.00 21.20  ? 5   TRP A CB  1 
ATOM   16   C  CG  . TRP A 1 5   ? 6.118   0.027   11.855  1.00 19.13  ? 5   TRP A CG  1 
ATOM   17   C  CD1 . TRP A 1 5   ? 6.081   1.340   11.480  1.00 25.81  ? 5   TRP A CD1 1 
ATOM   18   C  CD2 . TRP A 1 5   ? 4.749   -0.454  11.844  1.00 18.02  ? 5   TRP A CD2 1 
ATOM   19   N  NE1 . TRP A 1 5   ? 4.783   1.723   11.274  1.00 22.90  ? 5   TRP A NE1 1 
ATOM   20   C  CE2 . TRP A 1 5   ? 3.956   0.646   11.463  1.00 19.33  ? 5   TRP A CE2 1 
ATOM   21   C  CE3 . TRP A 1 5   ? 4.116   -1.678  12.136  1.00 18.22  ? 5   TRP A CE3 1 
ATOM   22   C  CZ2 . TRP A 1 5   ? 2.580   0.561   11.349  1.00 19.30  ? 5   TRP A CZ2 1 
ATOM   23   C  CZ3 . TRP A 1 5   ? 2.740   -1.764  12.012  1.00 17.61  ? 5   TRP A CZ3 1 
ATOM   24   C  CH2 . TRP A 1 5   ? 1.986   -0.645  11.653  1.00 18.61  ? 5   TRP A CH2 1 
ATOM   25   N  N   . GLY A 1 6   ? 6.734   -3.518  10.877  1.00 19.27  ? 6   GLY A N   1 
ATOM   26   C  CA  . GLY A 1 6   ? 5.745   -4.417  10.302  1.00 20.66  ? 6   GLY A CA  1 
ATOM   27   C  C   . GLY A 1 6   ? 5.437   -5.503  11.310  1.00 17.74  ? 6   GLY A C   1 
ATOM   28   O  O   . GLY A 1 6   ? 5.393   -5.261  12.526  1.00 17.54  ? 6   GLY A O   1 
ATOM   29   N  N   . TYR A 1 7   ? 5.121   -6.690  10.810  1.00 19.77  ? 7   TYR A N   1 
ATOM   30   C  CA  . TYR A 1 7   ? 4.700   -7.777  11.647  1.00 19.16  ? 7   TYR A CA  1 
ATOM   31   C  C   . TYR A 1 7   ? 5.587   -8.999  11.503  1.00 21.27  ? 7   TYR A C   1 
ATOM   32   O  O   . TYR A 1 7   ? 5.281   -10.033 12.122  1.00 28.33  ? 7   TYR A O   1 
ATOM   33   C  CB  . TYR A 1 7   ? 3.232   -8.114  11.388  1.00 18.52  ? 7   TYR A CB  1 
ATOM   34   C  CG  . TYR A 1 7   ? 2.303   -7.037  11.876  1.00 16.41  ? 7   TYR A CG  1 
ATOM   35   C  CD1 . TYR A 1 7   ? 1.898   -7.015  13.241  1.00 15.31  ? 7   TYR A CD1 1 
ATOM   36   C  CD2 . TYR A 1 7   ? 1.830   -6.024  11.036  1.00 18.69  ? 7   TYR A CD2 1 
ATOM   37   C  CE1 . TYR A 1 7   ? 1.046   -6.025  13.705  1.00 15.36  ? 7   TYR A CE1 1 
ATOM   38   C  CE2 . TYR A 1 7   ? 0.946   -5.037  11.485  1.00 15.68  ? 7   TYR A CE2 1 
ATOM   39   C  CZ  . TYR A 1 7   ? 0.579   -5.048  12.835  1.00 14.26  ? 7   TYR A CZ  1 
ATOM   40   O  OH  . TYR A 1 7   ? -0.254  -4.081  13.249  1.00 16.58  ? 7   TYR A OH  1 
ATOM   41   N  N   . GLY A 1 8   ? 6.665   -8.852  10.719  1.00 24.09  ? 8   GLY A N   1 
ATOM   42   C  CA  . GLY A 1 8   ? 7.590   -9.949  10.471  1.00 26.38  ? 8   GLY A CA  1 
ATOM   43   C  C   . GLY A 1 8   ? 8.583   -10.181 11.626  1.00 24.39  ? 8   GLY A C   1 
ATOM   44   O  O   . GLY A 1 8   ? 8.718   -9.389  12.595  1.00 24.87  ? 8   GLY A O   1 
ATOM   45   N  N   . LYS A 1 9   ? 9.395   -11.238 11.465  1.00 27.03  ? 9   LYS A N   1 
ATOM   46   C  CA  . LYS A 1 9   ? 10.423  -11.601 12.440  1.00 28.01  ? 9   LYS A CA  1 
ATOM   47   C  C   . LYS A 1 9   ? 11.405  -10.443 12.649  1.00 23.06  ? 9   LYS A C   1 
ATOM   48   O  O   . LYS A 1 9   ? 11.881  -10.222 13.757  1.00 24.63  ? 9   LYS A O   1 
ATOM   49   C  CB  . LYS A 1 9   ? 11.185  -12.832 11.932  1.00 34.83  ? 9   LYS A CB  1 
ATOM   50   C  CG  . LYS A 1 9   ? 12.420  -13.220 12.731  1.00 38.33  ? 9   LYS A CG  1 
ATOM   51   N  N   . HIS A 1 10  ? 11.666  -9.686  11.584  1.00 23.78  ? 10  HIS A N   1 
ATOM   52   C  CA  . HIS A 1 10  ? 12.765  -8.755  11.626  1.00 26.37  ? 10  HIS A CA  1 
ATOM   53   C  C   . HIS A 1 10  ? 12.286  -7.345  11.919  1.00 22.65  ? 10  HIS A C   1 
ATOM   54   O  O   . HIS A 1 10  ? 13.124  -6.508  12.258  1.00 26.19  ? 10  HIS A O   1 
ATOM   55   C  CB  . HIS A 1 10  ? 13.579  -8.860  10.325  1.00 32.92  ? 10  HIS A CB  1 
ATOM   56   C  CG  . HIS A 1 10  ? 14.203  -10.225 10.193  1.00 41.97  ? 10  HIS A CG  1 
ATOM   57   N  ND1 . HIS A 1 10  ? 15.298  -10.584 10.979  1.00 49.13  ? 10  HIS A ND1 1 
ATOM   58   C  CD2 . HIS A 1 10  ? 13.855  -11.336 9.433   1.00 46.42  ? 10  HIS A CD2 1 
ATOM   59   C  CE1 . HIS A 1 10  ? 15.615  -11.847 10.710  1.00 46.40  ? 10  HIS A CE1 1 
ATOM   60   N  NE2 . HIS A 1 10  ? 14.746  -12.327 9.764   1.00 45.82  ? 10  HIS A NE2 1 
ATOM   61   N  N   . ASN A 1 11  ? 10.983  -7.078  11.826  1.00 22.61  ? 11  ASN A N   1 
ATOM   62   C  CA  . ASN A 1 11  ? 10.508  -5.711  12.039  1.00 19.66  ? 11  ASN A CA  1 
ATOM   63   C  C   . ASN A 1 11  ? 9.198   -5.694  12.845  1.00 17.92  ? 11  ASN A C   1 
ATOM   64   O  O   . ASN A 1 11  ? 8.507   -4.683  12.874  1.00 19.39  ? 11  ASN A O   1 
ATOM   65   C  CB  . ASN A 1 11  ? 10.362  -4.968  10.708  1.00 23.86  ? 11  ASN A CB  1 
ATOM   66   C  CG  . ASN A 1 11  ? 9.261   -5.543  9.842   1.00 25.73  ? 11  ASN A CG  1 
ATOM   67   O  OD1 . ASN A 1 11  ? 8.630   -6.534  10.191  1.00 23.16  ? 11  ASN A OD1 1 
ATOM   68   N  ND2 . ASN A 1 11  ? 9.039   -4.950  8.683   1.00 29.20  ? 11  ASN A ND2 1 
ATOM   69   N  N   . GLY A 1 12  ? 8.848   -6.826  13.455  1.00 18.52  ? 12  GLY A N   1 
ATOM   70   C  CA  . GLY A 1 12  ? 7.559   -6.980  14.118  1.00 18.16  ? 12  GLY A CA  1 
ATOM   71   C  C   . GLY A 1 12  ? 7.516   -6.422  15.536  1.00 15.82  ? 12  GLY A C   1 
ATOM   72   O  O   . GLY A 1 12  ? 8.439   -5.699  15.954  1.00 16.27  ? 12  GLY A O   1 
ATOM   73   N  N   . PRO A 1 13  ? 6.442   -6.724  16.265  1.00 15.54  ? 13  PRO A N   1 
ATOM   74   C  CA  . PRO A 1 13  ? 6.207   -6.163  17.595  1.00 15.49  ? 13  PRO A CA  1 
ATOM   75   C  C   . PRO A 1 13  ? 7.359   -6.186  18.575  1.00 15.93  ? 13  PRO A C   1 
ATOM   76   O  O   . PRO A 1 13  ? 7.482   -5.213  19.335  1.00 17.13  ? 13  PRO A O   1 
ATOM   77   C  CB  . PRO A 1 13  ? 5.030   -6.984  18.123  1.00 17.32  ? 13  PRO A CB  1 
ATOM   78   C  CG  . PRO A 1 13  ? 4.217   -7.259  16.832  1.00 16.83  ? 13  PRO A CG  1 
ATOM   79   C  CD  . PRO A 1 13  ? 5.283   -7.457  15.757  1.00 16.39  ? 13  PRO A CD  1 
ATOM   80   N  N   . GLU A 1 14  ? 8.212   -7.216  18.510  1.00 16.07  ? 14  GLU A N   1 
ATOM   81   C  CA  . GLU A 1 14  ? 9.329   -7.242  19.471  1.00 17.68  ? 14  GLU A CA  1 
ATOM   82   C  C   . GLU A 1 14  ? 10.410  -6.208  19.118  1.00 16.77  ? 14  GLU A C   1 
ATOM   83   O  O   . GLU A 1 14  ? 11.318  -6.020  19.916  1.00 18.23  ? 14  GLU A O   1 
ATOM   84   C  CB  . GLU A 1 14  ? 9.983   -8.632  19.527  1.00 23.93  ? 14  GLU A CB  1 
ATOM   85   C  CG  . GLU A 1 14  ? 8.968   -9.716  19.860  1.00 28.49  ? 14  GLU A CG  1 
ATOM   86   C  CD  . GLU A 1 14  ? 8.147   -9.502  21.130  1.00 46.35  ? 14  GLU A CD  1 
ATOM   87   O  OE1 . GLU A 1 14  ? 8.760   -9.544  22.196  1.00 51.69  ? 14  GLU A OE1 1 
ATOM   88   O  OE2 . GLU A 1 14  ? 6.884   -9.258  21.051  1.00 46.17  ? 14  GLU A OE2 1 
ATOM   89   N  N   . HIS A 1 15  ? 10.385  -5.631  17.893  1.00 16.58  ? 15  HIS A N   1 
ATOM   90   C  CA  . HIS A 1 15  ? 11.358  -4.657  17.504  1.00 15.15  ? 15  HIS A CA  1 
ATOM   91   C  C   . HIS A 1 15  ? 10.866  -3.221  17.661  1.00 14.60  ? 15  HIS A C   1 
ATOM   92   O  O   . HIS A 1 15  ? 11.684  -2.292  17.605  1.00 17.45  ? 15  HIS A O   1 
ATOM   93   C  CB  . HIS A 1 15  ? 11.704  -4.810  16.020  1.00 16.02  ? 15  HIS A CB  1 
ATOM   94   C  CG  . HIS A 1 15  ? 12.435  -6.059  15.725  1.00 18.31  ? 15  HIS A CG  1 
ATOM   95   N  ND1 . HIS A 1 15  ? 13.826  -6.082  15.736  1.00 19.28  ? 15  HIS A ND1 1 
ATOM   96   C  CD2 . HIS A 1 15  ? 11.998  -7.277  15.335  1.00 20.81  ? 15  HIS A CD2 1 
ATOM   97   C  CE1 . HIS A 1 15  ? 14.252  -7.301  15.445  1.00 23.81  ? 15  HIS A CE1 1 
ATOM   98   N  NE2 . HIS A 1 15  ? 13.144  -8.059  15.202  1.00 22.47  ? 15  HIS A NE2 1 
ATOM   99   N  N   . TRP A 1 16  ? 9.560   -3.000  17.837  1.00 14.55  ? 16  TRP A N   1 
ATOM   100  C  CA  . TRP A 1 16  ? 8.992   -1.684  17.741  1.00 14.79  ? 16  TRP A CA  1 
ATOM   101  C  C   . TRP A 1 16  ? 9.544   -0.721  18.779  1.00 14.56  ? 16  TRP A C   1 
ATOM   102  O  O   . TRP A 1 16  ? 9.649   0.461   18.498  1.00 15.57  ? 16  TRP A O   1 
ATOM   103  C  CB  . TRP A 1 16  ? 7.470   -1.759  17.882  1.00 14.01  ? 16  TRP A CB  1 
ATOM   104  C  CG  . TRP A 1 16  ? 6.813   -2.486  16.757  1.00 14.48  ? 16  TRP A CG  1 
ATOM   105  C  CD1 . TRP A 1 16  ? 7.350   -2.864  15.542  1.00 15.36  ? 16  TRP A CD1 1 
ATOM   106  C  CD2 . TRP A 1 16  ? 5.399   -2.777  16.683  1.00 13.41  ? 16  TRP A CD2 1 
ATOM   107  N  NE1 . TRP A 1 16  ? 6.365   -3.460  14.793  1.00 16.08  ? 16  TRP A NE1 1 
ATOM   108  C  CE2 . TRP A 1 16  ? 5.175   -3.428  15.448  1.00 13.77  ? 16  TRP A CE2 1 
ATOM   109  C  CE3 . TRP A 1 16  ? 4.372   -2.615  17.603  1.00 13.33  ? 16  TRP A CE3 1 
ATOM   110  C  CZ2 . TRP A 1 16  ? 3.891   -3.847  15.073  1.00 13.29  ? 16  TRP A CZ2 1 
ATOM   111  C  CZ3 . TRP A 1 16  ? 3.121   -3.081  17.276  1.00 13.89  ? 16  TRP A CZ3 1 
ATOM   112  C  CH2 . TRP A 1 16  ? 2.902   -3.627  16.013  1.00 13.66  ? 16  TRP A CH2 1 
ATOM   113  N  N   . HIS A 1 17  ? 9.945   -1.250  19.949  1.00 14.75  ? 17  HIS A N   1 
ATOM   114  C  CA  . HIS A 1 17  ? 10.397  -0.366  21.013  1.00 16.42  ? 17  HIS A CA  1 
ATOM   115  C  C   . HIS A 1 17  ? 11.643  0.411   20.625  1.00 17.43  ? 17  HIS A C   1 
ATOM   116  O  O   . HIS A 1 17  ? 11.892  1.445   21.227  1.00 17.09  ? 17  HIS A O   1 
ATOM   117  C  CB  . HIS A 1 17  ? 10.663  -1.151  22.317  1.00 16.41  ? 17  HIS A CB  1 
ATOM   118  C  CG  . HIS A 1 17  ? 11.887  -2.014  22.252  1.00 16.18  ? 17  HIS A CG  1 
ATOM   119  N  ND1 . HIS A 1 17  ? 13.098  -1.596  22.769  1.00 17.92  ? 17  HIS A ND1 1 
ATOM   120  C  CD2 . HIS A 1 17  ? 12.103  -3.191  21.628  1.00 17.27  ? 17  HIS A CD2 1 
ATOM   121  C  CE1 . HIS A 1 17  ? 14.022  -2.487  22.466  1.00 19.30  ? 17  HIS A CE1 1 
ATOM   122  N  NE2 . HIS A 1 17  ? 13.432  -3.525  21.820  1.00 19.10  ? 17  HIS A NE2 1 
ATOM   123  N  N   . LYS A 1 18  ? 12.401  -0.074  19.632  1.00 16.98  ? 18  LYS A N   1 
ATOM   124  C  CA  . LYS A 1 18  ? 13.626  0.665   19.321  1.00 18.48  ? 18  LYS A CA  1 
ATOM   125  C  C   . LYS A 1 18  ? 13.319  1.996   18.637  1.00 19.72  ? 18  LYS A C   1 
ATOM   126  O  O   . LYS A 1 18  ? 13.940  2.997   18.956  1.00 26.21  ? 18  LYS A O   1 
ATOM   127  C  CB  . LYS A 1 18  ? 14.515  -0.183  18.413  1.00 18.84  ? 18  LYS A CB  1 
ATOM   128  C  CG  . LYS A 1 18  ? 15.074  -1.427  19.095  1.00 20.81  ? 18  LYS A CG  1 
ATOM   129  C  CD  . LYS A 1 18  ? 15.816  -2.331  18.174  1.00 19.92  ? 18  LYS A CD  1 
ATOM   130  C  CE  . LYS A 1 18  ? 14.904  -3.349  17.553  1.00 21.10  ? 18  LYS A CE  1 
ATOM   131  N  NZ  . LYS A 1 18  ? 15.593  -4.073  16.453  1.00 19.72  ? 18  LYS A NZ  1 
ATOM   132  N  N   . ASP A 1 19  ? 12.304  2.038   17.773  1.00 18.36  ? 19  ASP A N   1 
ATOM   133  C  CA  . ASP A 1 19  ? 11.901  3.327   17.223  1.00 18.64  ? 19  ASP A CA  1 
ATOM   134  C  C   . ASP A 1 19  ? 10.853  4.018   18.081  1.00 18.91  ? 19  ASP A C   1 
ATOM   135  O  O   . ASP A 1 19  ? 10.730  5.242   17.991  1.00 21.66  ? 19  ASP A O   1 
ATOM   136  C  CB  . ASP A 1 19  ? 11.365  3.175   15.803  1.00 22.71  ? 19  ASP A CB  1 
ATOM   137  C  CG  . ASP A 1 19  ? 12.451  2.974   14.760  1.00 28.39  ? 19  ASP A CG  1 
ATOM   138  O  OD1 . ASP A 1 19  ? 13.514  3.660   14.838  1.00 30.71  ? 19  ASP A OD1 1 
ATOM   139  O  OD2 . ASP A 1 19  ? 12.294  2.055   13.970  1.00 50.09  ? 19  ASP A OD2 1 
ATOM   140  N  N   . PHE A 1 20  ? 10.097  3.254   18.893  1.00 15.94  ? 20  PHE A N   1 
ATOM   141  C  CA  . PHE A 1 20  ? 8.977   3.842   19.621  1.00 17.33  ? 20  PHE A CA  1 
ATOM   142  C  C   . PHE A 1 20  ? 9.094   3.338   21.057  1.00 17.49  ? 20  PHE A C   1 
ATOM   143  O  O   . PHE A 1 20  ? 8.463   2.351   21.411  1.00 16.21  ? 20  PHE A O   1 
ATOM   144  C  CB  . PHE A 1 20  ? 7.635   3.427   19.007  1.00 17.87  ? 20  PHE A CB  1 
ATOM   145  C  CG  . PHE A 1 20  ? 7.550   3.818   17.556  1.00 20.61  ? 20  PHE A CG  1 
ATOM   146  C  CD1 . PHE A 1 20  ? 7.258   5.119   17.177  1.00 24.93  ? 20  PHE A CD1 1 
ATOM   147  C  CD2 . PHE A 1 20  ? 7.922   2.901   16.584  1.00 20.82  ? 20  PHE A CD2 1 
ATOM   148  C  CE1 . PHE A 1 20  ? 7.291   5.466   15.833  1.00 25.31  ? 20  PHE A CE1 1 
ATOM   149  C  CE2 . PHE A 1 20  ? 7.933   3.232   15.238  1.00 24.15  ? 20  PHE A CE2 1 
ATOM   150  C  CZ  . PHE A 1 20  ? 7.608   4.525   14.873  1.00 24.84  ? 20  PHE A CZ  1 
ATOM   151  N  N   . PRO A 1 21  ? 9.980   3.924   21.878  1.00 18.09  ? 21  PRO A N   1 
ATOM   152  C  CA  . PRO A 1 21  ? 10.223  3.436   23.236  1.00 18.25  ? 21  PRO A CA  1 
ATOM   153  C  C   . PRO A 1 21  ? 8.990   3.325   24.123  1.00 18.49  ? 21  PRO A C   1 
ATOM   154  O  O   . PRO A 1 21  ? 9.008   2.538   25.048  1.00 18.48  ? 21  PRO A O   1 
ATOM   155  C  CB  . PRO A 1 21  ? 11.275  4.358   23.841  1.00 23.71  ? 21  PRO A CB  1 
ATOM   156  C  CG  . PRO A 1 21  ? 11.754  5.194   22.716  1.00 28.83  ? 21  PRO A CG  1 
ATOM   157  C  CD  . PRO A 1 21  ? 10.888  5.014   21.511  1.00 21.35  ? 21  PRO A CD  1 
ATOM   158  N  N   A ILE A 1 22  ? 7.911   4.051   23.788  0.50 15.53  ? 22  ILE A N   1 
ATOM   159  N  N   B ILE A 1 22  ? 7.906   4.059   23.794  0.50 16.42  ? 22  ILE A N   1 
ATOM   160  C  CA  A ILE A 1 22  ? 6.677   3.927   24.544  0.50 16.65  ? 22  ILE A CA  1 
ATOM   161  C  CA  B ILE A 1 22  ? 6.648   3.939   24.522  0.50 17.58  ? 22  ILE A CA  1 
ATOM   162  C  C   A ILE A 1 22  ? 6.097   2.512   24.429  0.50 15.47  ? 22  ILE A C   1 
ATOM   163  C  C   B ILE A 1 22  ? 6.090   2.513   24.426  0.50 15.91  ? 22  ILE A C   1 
ATOM   164  O  O   A ILE A 1 22  ? 5.208   2.172   25.206  0.50 15.92  ? 22  ILE A O   1 
ATOM   165  O  O   B ILE A 1 22  ? 5.220   2.162   25.219  0.50 16.85  ? 22  ILE A O   1 
ATOM   166  C  CB  A ILE A 1 22  ? 5.665   4.983   24.088  0.50 16.45  ? 22  ILE A CB  1 
ATOM   167  C  CB  B ILE A 1 22  ? 5.624   4.996   24.065  0.50 16.57  ? 22  ILE A CB  1 
ATOM   168  C  CG1 A ILE A 1 22  ? 4.686   5.324   25.214  0.50 17.08  ? 22  ILE A CG1 1 
ATOM   169  C  CG1 B ILE A 1 22  ? 4.530   5.236   25.113  0.50 20.76  ? 22  ILE A CG1 1 
ATOM   170  C  CG2 A ILE A 1 22  ? 4.978   4.530   22.803  0.50 16.34  ? 22  ILE A CG2 1 
ATOM   171  C  CG2 B ILE A 1 22  ? 5.066   4.679   22.681  0.50 17.67  ? 22  ILE A CG2 1 
ATOM   172  C  CD1 A ILE A 1 22  ? 3.713   6.400   24.846  0.50 17.71  ? 22  ILE A CD1 1 
ATOM   173  C  CD1 B ILE A 1 22  ? 5.015   5.977   26.336  0.50 20.64  ? 22  ILE A CD1 1 
ATOM   174  N  N   . ALA A 1 23  ? 6.630   1.703   23.500  1.00 15.01  ? 23  ALA A N   1 
ATOM   175  C  CA  . ALA A 1 23  ? 6.192   0.307   23.393  1.00 14.23  ? 23  ALA A CA  1 
ATOM   176  C  C   . ALA A 1 23  ? 6.296   -0.420  24.726  1.00 14.85  ? 23  ALA A C   1 
ATOM   177  O  O   . ALA A 1 23  ? 5.598   -1.430  24.898  1.00 16.69  ? 23  ALA A O   1 
ATOM   178  C  CB  . ALA A 1 23  ? 6.968   -0.426  22.325  1.00 14.99  ? 23  ALA A CB  1 
ATOM   179  N  N   . LYS A 1 24  ? 7.246   0.038   25.583  1.00 16.88  ? 24  LYS A N   1 
ATOM   180  C  CA  . LYS A 1 24  ? 7.424   -0.591  26.900  1.00 17.35  ? 24  LYS A CA  1 
ATOM   181  C  C   . LYS A 1 24  ? 6.797   0.269   27.992  1.00 18.54  ? 24  LYS A C   1 
ATOM   182  O  O   . LYS A 1 24  ? 7.171   0.197   29.167  1.00 21.28  ? 24  LYS A O   1 
ATOM   183  C  CB  . LYS A 1 24  ? 8.888   -0.874  27.211  1.00 20.22  ? 24  LYS A CB  1 
ATOM   184  C  CG  . LYS A 1 24  ? 9.513   -1.902  26.276  1.00 21.11  ? 24  LYS A CG  1 
ATOM   185  C  CD  . LYS A 1 24  ? 10.955  -2.057  26.683  1.00 27.06  ? 24  LYS A CD  1 
ATOM   186  C  CE  . LYS A 1 24  ? 11.616  -3.011  25.732  1.00 27.47  ? 24  LYS A CE  1 
ATOM   187  N  NZ  . LYS A 1 24  ? 11.347  -4.406  26.135  1.00 33.12  ? 24  LYS A NZ  1 
ATOM   188  N  N   . GLY A 1 25  ? 5.800   1.061   27.636  1.00 18.51  ? 25  GLY A N   1 
ATOM   189  C  CA  . GLY A 1 25  ? 5.196   2.007   28.556  1.00 21.39  ? 25  GLY A CA  1 
ATOM   190  C  C   . GLY A 1 25  ? 4.216   1.364   29.535  1.00 16.75  ? 25  GLY A C   1 
ATOM   191  O  O   . GLY A 1 25  ? 4.022   0.126   29.579  1.00 19.10  ? 25  GLY A O   1 
ATOM   192  N  N   . GLU A 1 26  ? 3.514   2.238   30.285  1.00 17.57  ? 26  GLU A N   1 
ATOM   193  C  CA  . GLU A 1 26  ? 2.701   1.808   31.391  1.00 18.26  ? 26  GLU A CA  1 
ATOM   194  C  C   . GLU A 1 26  ? 1.253   1.601   30.949  1.00 16.94  ? 26  GLU A C   1 
ATOM   195  O  O   . GLU A 1 26  ? 0.474   1.088   31.718  1.00 19.24  ? 26  GLU A O   1 
ATOM   196  C  CB  . GLU A 1 26  ? 2.710   2.890   32.480  1.00 24.95  ? 26  GLU A CB  1 
ATOM   197  C  CG  . GLU A 1 26  ? 4.120   3.195   33.016  1.00 28.08  ? 26  GLU A CG  1 
ATOM   198  C  CD  . GLU A 1 26  ? 4.858   1.965   33.560  1.00 45.03  ? 26  GLU A CD  1 
ATOM   199  O  OE1 . GLU A 1 26  ? 4.220   1.158   34.303  1.00 40.10  ? 26  GLU A OE1 1 
ATOM   200  O  OE2 . GLU A 1 26  ? 6.057   1.783   33.211  1.00 56.41  ? 26  GLU A OE2 1 
ATOM   201  N  N   . ARG A 1 27  ? 0.881   1.933   29.704  1.00 14.35  ? 27  ARG A N   1 
ATOM   202  C  CA  . ARG A 1 27  ? -0.516  1.732   29.307  1.00 13.38  ? 27  ARG A CA  1 
ATOM   203  C  C   . ARG A 1 27  ? -0.576  1.285   27.841  1.00 12.47  ? 27  ARG A C   1 
ATOM   204  O  O   . ARG A 1 27  ? -1.318  1.840   27.032  1.00 13.76  ? 27  ARG A O   1 
ATOM   205  C  CB  . ARG A 1 27  ? -1.435  2.935   29.620  1.00 16.97  ? 27  ARG A CB  1 
ATOM   206  C  CG  . ARG A 1 27  ? -1.019  4.277   29.063  1.00 20.34  ? 27  ARG A CG  1 
ATOM   207  C  CD  . ARG A 1 27  ? -2.020  5.427   29.174  1.00 22.42  ? 27  ARG A CD  1 
ATOM   208  N  NE  . ARG A 1 27  ? -3.180  5.357   28.300  1.00 18.42  ? 27  ARG A NE  1 
ATOM   209  C  CZ  . ARG A 1 27  ? -4.100  6.309   28.192  1.00 16.99  ? 27  ARG A CZ  1 
ATOM   210  N  NH1 . ARG A 1 27  ? -3.995  7.415   28.909  1.00 20.63  ? 27  ARG A NH1 1 
ATOM   211  N  NH2 . ARG A 1 27  ? -5.121  6.152   27.369  1.00 19.61  ? 27  ARG A NH2 1 
ATOM   212  N  N   . GLN A 1 28  ? 0.124   0.187   27.543  1.00 12.51  ? 28  GLN A N   1 
ATOM   213  C  CA  . GLN A 1 28  ? 0.150   -0.310  26.162  1.00 11.29  ? 28  GLN A CA  1 
ATOM   214  C  C   . GLN A 1 28  ? -1.008  -1.281  25.926  1.00 11.58  ? 28  GLN A C   1 
ATOM   215  O  O   . GLN A 1 28  ? -1.503  -1.950  26.815  1.00 13.12  ? 28  GLN A O   1 
ATOM   216  C  CB  . GLN A 1 28  ? 1.503   -0.998  25.909  1.00 12.78  ? 28  GLN A CB  1 
ATOM   217  C  CG  . GLN A 1 28  ? 2.603   0.047   25.871  1.00 13.74  ? 28  GLN A CG  1 
ATOM   218  C  CD  . GLN A 1 28  ? 2.484   0.838   24.574  1.00 12.32  ? 28  GLN A CD  1 
ATOM   219  O  OE1 . GLN A 1 28  ? 2.669   0.303   23.479  1.00 13.36  ? 28  GLN A OE1 1 
ATOM   220  N  NE2 . GLN A 1 28  ? 2.126   2.119   24.643  1.00 13.36  ? 28  GLN A NE2 1 
ATOM   221  N  N   . SER A 1 29  ? -1.393  -1.377  24.678  1.00 11.34  ? 29  SER A N   1 
ATOM   222  C  CA  . SER A 1 29  ? -2.472  -2.243  24.215  1.00 11.17  ? 29  SER A CA  1 
ATOM   223  C  C   . SER A 1 29  ? -1.946  -3.106  23.085  1.00 11.80  ? 29  SER A C   1 
ATOM   224  O  O   . SER A 1 29  ? -0.984  -2.786  22.423  1.00 12.13  ? 29  SER A O   1 
ATOM   225  C  CB  . SER A 1 29  ? -3.603  -1.376  23.671  1.00 11.56  ? 29  SER A CB  1 
ATOM   226  O  OG  . SER A 1 29  ? -4.209  -0.669  24.731  1.00 12.16  ? 29  SER A OG  1 
ATOM   227  N  N   . PRO A 1 30  ? -2.576  -4.259  22.832  1.00 10.99  ? 30  PRO A N   1 
ATOM   228  C  CA  . PRO A 1 30  ? -3.753  -4.761  23.563  1.00 11.14  ? 30  PRO A CA  1 
ATOM   229  C  C   . PRO A 1 30  ? -3.342  -5.466  24.865  1.00 10.55  ? 30  PRO A C   1 
ATOM   230  O  O   . PRO A 1 30  ? -2.155  -5.514  25.189  1.00 11.97  ? 30  PRO A O   1 
ATOM   231  C  CB  . PRO A 1 30  ? -4.285  -5.816  22.541  1.00 11.74  ? 30  PRO A CB  1 
ATOM   232  C  CG  . PRO A 1 30  ? -3.019  -6.369  21.936  1.00 11.68  ? 30  PRO A CG  1 
ATOM   233  C  CD  . PRO A 1 30  ? -2.112  -5.163  21.780  1.00 11.40  ? 30  PRO A CD  1 
ATOM   234  N  N   . VAL A 1 31  ? -4.338  -6.005  25.531  1.00 11.93  ? 31  VAL A N   1 
ATOM   235  C  CA  . VAL A 1 31  ? -4.140  -6.748  26.738  1.00 11.44  ? 31  VAL A CA  1 
ATOM   236  C  C   . VAL A 1 31  ? -5.012  -7.979  26.699  1.00 11.98  ? 31  VAL A C   1 
ATOM   237  O  O   . VAL A 1 31  ? -5.979  -8.058  25.932  1.00 12.94  ? 31  VAL A O   1 
ATOM   238  C  CB  . VAL A 1 31  ? -4.463  -5.942  28.005  1.00 13.10  ? 31  VAL A CB  1 
ATOM   239  C  CG1 . VAL A 1 31  ? -3.550  -4.725  28.094  1.00 14.01  ? 31  VAL A CG1 1 
ATOM   240  C  CG2 . VAL A 1 31  ? -5.915  -5.502  28.055  1.00 13.85  ? 31  VAL A CG2 1 
ATOM   241  N  N   . ASP A 1 32  ? -4.678  -8.941  27.579  1.00 12.56  ? 32  ASP A N   1 
ATOM   242  C  CA  . ASP A 1 32  ? -5.602  -10.019 27.865  1.00 12.22  ? 32  ASP A CA  1 
ATOM   243  C  C   . ASP A 1 32  ? -6.660  -9.510  28.829  1.00 13.13  ? 32  ASP A C   1 
ATOM   244  O  O   . ASP A 1 32  ? -6.369  -8.877  29.839  1.00 15.31  ? 32  ASP A O   1 
ATOM   245  C  CB  . ASP A 1 32  ? -4.844  -11.211 28.469  1.00 15.05  ? 32  ASP A CB  1 
ATOM   246  C  CG  . ASP A 1 32  ? -5.819  -12.350 28.774  1.00 15.70  ? 32  ASP A CG  1 
ATOM   247  O  OD1 . ASP A 1 32  ? -6.553  -12.803 27.847  1.00 15.33  ? 32  ASP A OD1 1 
ATOM   248  O  OD2 . ASP A 1 32  ? -5.883  -12.793 29.968  1.00 18.99  ? 32  ASP A OD2 1 
ATOM   249  N  N   . ILE A 1 33  ? -7.920  -9.786  28.505  1.00 12.77  ? 33  ILE A N   1 
ATOM   250  C  CA  . ILE A 1 33  ? -9.018  -9.425  29.362  1.00 13.38  ? 33  ILE A CA  1 
ATOM   251  C  C   . ILE A 1 33  ? -9.344  -10.663 30.204  1.00 13.96  ? 33  ILE A C   1 
ATOM   252  O  O   . ILE A 1 33  ? -9.899  -11.652 29.733  1.00 15.98  ? 33  ILE A O   1 
ATOM   253  C  CB  . ILE A 1 33  ? -10.208 -8.958  28.520  1.00 14.49  ? 33  ILE A CB  1 
ATOM   254  C  CG1 . ILE A 1 33  ? -9.816  -7.753  27.671  1.00 14.63  ? 33  ILE A CG1 1 
ATOM   255  C  CG2 . ILE A 1 33  ? -11.419 -8.692  29.445  1.00 16.71  ? 33  ILE A CG2 1 
ATOM   256  C  CD1 . ILE A 1 33  ? -10.873 -7.459  26.587  1.00 17.40  ? 33  ILE A CD1 1 
ATOM   257  N  N   A ASP A 1 34  ? -8.981  -10.586 31.478  0.50 15.57  ? 34  ASP A N   1 
ATOM   258  N  N   B ASP A 1 34  ? -9.025  -10.544 31.505  0.50 15.39  ? 34  ASP A N   1 
ATOM   259  C  CA  A ASP A 1 34  ? -9.249  -11.682 32.376  0.50 18.37  ? 34  ASP A CA  1 
ATOM   260  C  CA  B ASP A 1 34  ? -9.303  -11.549 32.518  0.50 16.17  ? 34  ASP A CA  1 
ATOM   261  C  C   A ASP A 1 34  ? -10.640 -11.373 32.927  0.50 17.40  ? 34  ASP A C   1 
ATOM   262  C  C   B ASP A 1 34  ? -10.738 -11.291 32.979  0.50 17.79  ? 34  ASP A C   1 
ATOM   263  O  O   A ASP A 1 34  ? -10.798 -10.435 33.698  0.50 18.73  ? 34  ASP A O   1 
ATOM   264  O  O   B ASP A 1 34  ? -11.025 -10.359 33.736  0.50 21.47  ? 34  ASP A O   1 
ATOM   265  C  CB  A ASP A 1 34  ? -8.116  -11.775 33.401  0.50 21.29  ? 34  ASP A CB  1 
ATOM   266  C  CB  B ASP A 1 34  ? -8.285  -11.517 33.672  0.50 16.74  ? 34  ASP A CB  1 
ATOM   267  C  CG  A ASP A 1 34  ? -8.302  -12.974 34.304  0.50 25.34  ? 34  ASP A CG  1 
ATOM   268  C  CG  B ASP A 1 34  ? -8.513  -12.621 34.695  0.50 19.04  ? 34  ASP A CG  1 
ATOM   269  O  OD1 A ASP A 1 34  ? -9.091  -12.845 35.278  0.50 25.86  ? 34  ASP A OD1 1 
ATOM   270  O  OD1 B ASP A 1 34  ? -9.648  -13.144 34.735  0.50 19.40  ? 34  ASP A OD1 1 
ATOM   271  O  OD2 A ASP A 1 34  ? -7.689  -14.030 34.011  0.50 32.26  ? 34  ASP A OD2 1 
ATOM   272  O  OD2 B ASP A 1 34  ? -7.532  -12.969 35.447  0.50 23.13  ? 34  ASP A OD2 1 
ATOM   273  N  N   . THR A 1 35  ? -11.652 -12.126 32.478  1.00 18.40  ? 35  THR A N   1 
ATOM   274  C  CA  . THR A 1 35  ? -13.066 -11.791 32.681  1.00 19.94  ? 35  THR A CA  1 
ATOM   275  C  C   . THR A 1 35  ? -13.477 -11.944 34.137  1.00 20.12  ? 35  THR A C   1 
ATOM   276  O  O   . THR A 1 35  ? -14.369 -11.275 34.604  1.00 20.84  ? 35  THR A O   1 
ATOM   277  C  CB  . THR A 1 35  ? -13.984 -12.705 31.876  1.00 21.12  ? 35  THR A CB  1 
ATOM   278  O  OG1 . THR A 1 35  ? -13.870 -14.067 32.308  1.00 22.56  ? 35  THR A OG1 1 
ATOM   279  C  CG2 . THR A 1 35  ? -13.676 -12.573 30.399  1.00 22.39  ? 35  THR A CG2 1 
ATOM   280  N  N   . HIS A 1 36  ? -12.747 -12.786 34.869  1.00 21.29  ? 36  HIS A N   1 
ATOM   281  C  CA  . HIS A 1 36  ? -13.006 -13.014 36.262  1.00 21.20  ? 36  HIS A CA  1 
ATOM   282  C  C   . HIS A 1 36  ? -12.477 -11.853 37.082  1.00 24.85  ? 36  HIS A C   1 
ATOM   283  O  O   . HIS A 1 36  ? -13.088 -11.580 38.094  1.00 30.41  ? 36  HIS A O   1 
ATOM   284  C  CB  . HIS A 1 36  ? -12.472 -14.401 36.661  1.00 25.28  ? 36  HIS A CB  1 
ATOM   285  C  CG  . HIS A 1 36  ? -13.265 -15.513 36.021  1.00 29.30  ? 36  HIS A CG  1 
ATOM   286  N  ND1 . HIS A 1 36  ? -14.592 -15.683 36.368  1.00 33.41  ? 36  HIS A ND1 1 
ATOM   287  C  CD2 . HIS A 1 36  ? -13.016 -16.393 34.947  1.00 33.32  ? 36  HIS A CD2 1 
ATOM   288  C  CE1 . HIS A 1 36  ? -15.122 -16.660 35.584  1.00 37.27  ? 36  HIS A CE1 1 
ATOM   289  N  NE2 . HIS A 1 36  ? -14.170 -17.097 34.744  1.00 44.34  ? 36  HIS A NE2 1 
ATOM   290  N  N   . THR A 1 37  ? -11.412 -11.168 36.666  1.00 24.31  ? 37  THR A N   1 
ATOM   291  C  CA  . THR A 1 37  ? -10.771 -10.073 37.391  1.00 23.43  ? 37  THR A CA  1 
ATOM   292  C  C   . THR A 1 37  ? -11.366 -8.709  37.010  1.00 21.31  ? 37  THR A C   1 
ATOM   293  O  O   . THR A 1 37  ? -11.249 -7.732  37.719  1.00 26.28  ? 37  THR A O   1 
ATOM   294  C  CB  . THR A 1 37  ? -9.245  -10.151 37.173  1.00 31.94  ? 37  THR A CB  1 
ATOM   295  O  OG1 . THR A 1 37  ? -8.805  -11.286 37.906  1.00 40.63  ? 37  THR A OG1 1 
ATOM   296  C  CG2 . THR A 1 37  ? -8.479  -8.989  37.775  1.00 38.58  ? 37  THR A CG2 1 
ATOM   297  N  N   . ALA A 1 38  ? -12.020 -8.600  35.850  1.00 19.26  ? 38  ALA A N   1 
ATOM   298  C  CA  . ALA A 1 38  ? -12.630 -7.337  35.422  1.00 17.53  ? 38  ALA A CA  1 
ATOM   299  C  C   . ALA A 1 38  ? -13.686 -6.989  36.467  1.00 23.43  ? 38  ALA A C   1 
ATOM   300  O  O   . ALA A 1 38  ? -14.401 -7.845  36.954  1.00 30.07  ? 38  ALA A O   1 
ATOM   301  C  CB  . ALA A 1 38  ? -13.164 -7.468  34.016  1.00 19.24  ? 38  ALA A CB  1 
ATOM   302  N  N   . LYS A 1 39  ? -13.743 -5.723  36.864  1.00 21.29  ? 39  LYS A N   1 
ATOM   303  C  CA  . LYS A 1 39  ? -14.667 -5.271  37.886  1.00 24.40  ? 39  LYS A CA  1 
ATOM   304  C  C   . LYS A 1 39  ? -15.914 -4.712  37.195  1.00 20.95  ? 39  LYS A C   1 
ATOM   305  O  O   . LYS A 1 39  ? -15.826 -3.720  36.458  1.00 18.96  ? 39  LYS A O   1 
ATOM   306  C  CB  . LYS A 1 39  ? -13.935 -4.158  38.643  1.00 29.99  ? 39  LYS A CB  1 
ATOM   307  C  CG  . LYS A 1 39  ? -14.699 -3.325  39.653  1.00 30.82  ? 39  LYS A CG  1 
ATOM   308  C  CD  . LYS A 1 39  ? -15.002 -4.041  40.959  1.00 28.78  ? 39  LYS A CD  1 
ATOM   309  C  CE  . LYS A 1 39  ? -15.714 -3.116  41.919  1.00 30.60  ? 39  LYS A CE  1 
ATOM   310  N  NZ  . LYS A 1 39  ? -16.114 -3.851  43.140  1.00 38.24  ? 39  LYS A NZ  1 
ATOM   311  N  N   . TYR A 1 40  ? -17.074 -5.251  37.539  1.00 21.34  ? 40  TYR A N   1 
ATOM   312  C  CA  . TYR A 1 40  ? -18.315 -4.631  37.107  1.00 20.88  ? 40  TYR A CA  1 
ATOM   313  C  C   . TYR A 1 40  ? -18.427 -3.256  37.740  1.00 21.81  ? 40  TYR A C   1 
ATOM   314  O  O   . TYR A 1 40  ? -18.292 -3.096  38.972  1.00 22.19  ? 40  TYR A O   1 
ATOM   315  C  CB  . TYR A 1 40  ? -19.509 -5.524  37.451  1.00 26.02  ? 40  TYR A CB  1 
ATOM   316  C  CG  . TYR A 1 40  ? -20.849 -4.854  37.371  1.00 25.47  ? 40  TYR A CG  1 
ATOM   317  C  CD1 . TYR A 1 40  ? -21.319 -4.350  36.156  1.00 23.63  ? 40  TYR A CD1 1 
ATOM   318  C  CD2 . TYR A 1 40  ? -21.664 -4.752  38.493  1.00 38.13  ? 40  TYR A CD2 1 
ATOM   319  C  CE1 . TYR A 1 40  ? -22.556 -3.753  36.060  1.00 30.00  ? 40  TYR A CE1 1 
ATOM   320  C  CE2 . TYR A 1 40  ? -22.923 -4.167  38.404  1.00 41.00  ? 40  TYR A CE2 1 
ATOM   321  C  CZ  . TYR A 1 40  ? -23.365 -3.687  37.182  1.00 36.58  ? 40  TYR A CZ  1 
ATOM   322  O  OH  . TYR A 1 40  ? -24.571 -3.089  37.050  1.00 42.19  ? 40  TYR A OH  1 
ATOM   323  N  N   . ASP A 1 41  ? -18.664 -2.253  36.926  1.00 19.66  ? 41  ASP A N   1 
ATOM   324  C  CA  . ASP A 1 41  ? -18.811 -0.895  37.397  1.00 22.45  ? 41  ASP A CA  1 
ATOM   325  C  C   . ASP A 1 41  ? -20.233 -0.423  37.146  1.00 24.75  ? 41  ASP A C   1 
ATOM   326  O  O   . ASP A 1 41  ? -20.533 -0.048  36.041  1.00 23.23  ? 41  ASP A O   1 
ATOM   327  C  CB  . ASP A 1 41  ? -17.794 0.066   36.771  1.00 26.50  ? 41  ASP A CB  1 
ATOM   328  C  CG  . ASP A 1 41  ? -17.869 1.452   37.374  1.00 33.62  ? 41  ASP A CG  1 
ATOM   329  O  OD1 . ASP A 1 41  ? -18.854 1.706   38.114  1.00 37.93  ? 41  ASP A OD1 1 
ATOM   330  O  OD2 . ASP A 1 41  ? -16.934 2.245   37.117  1.00 39.87  ? 41  ASP A OD2 1 
ATOM   331  N  N   . PRO A 1 42  ? -21.124 -0.421  38.162  1.00 31.82  ? 42  PRO A N   1 
ATOM   332  C  CA  . PRO A 1 42  ? -22.514 -0.032  37.930  1.00 32.91  ? 42  PRO A CA  1 
ATOM   333  C  C   . PRO A 1 42  ? -22.634 1.436   37.544  1.00 34.02  ? 42  PRO A C   1 
ATOM   334  O  O   . PRO A 1 42  ? -23.694 1.891   37.085  1.00 40.27  ? 42  PRO A O   1 
ATOM   335  C  CB  . PRO A 1 42  ? -23.171 -0.270  39.306  1.00 39.99  ? 42  PRO A CB  1 
ATOM   336  C  CG  . PRO A 1 42  ? -22.018 -0.146  40.315  1.00 41.63  ? 42  PRO A CG  1 
ATOM   337  C  CD  . PRO A 1 42  ? -20.831 -0.737  39.580  1.00 31.00  ? 42  PRO A CD  1 
ATOM   338  N  N   . SER A 1 43  ? -21.539 2.196   37.700  1.00 31.40  ? 43  SER A N   1 
ATOM   339  C  CA  . SER A 1 43  ? -21.670 3.605   37.326  1.00 37.72  ? 43  SER A CA  1 
ATOM   340  C  C   . SER A 1 43  ? -21.346 3.849   35.834  1.00 35.83  ? 43  SER A C   1 
ATOM   341  O  O   . SER A 1 43  ? -21.530 4.974   35.332  1.00 36.59  ? 43  SER A O   1 
ATOM   342  C  CB  . SER A 1 43  ? -20.828 4.468   38.224  1.00 50.41  ? 43  SER A CB  1 
ATOM   343  O  OG  . SER A 1 43  ? -19.465 4.355   37.846  1.00 35.74  ? 43  SER A OG  1 
ATOM   344  N  N   . LEU A 1 44  ? -20.871 2.817   35.111  1.00 29.78  ? 44  LEU A N   1 
ATOM   345  C  CA  . LEU A 1 44  ? -20.610 2.993   33.684  1.00 27.91  ? 44  LEU A CA  1 
ATOM   346  C  C   . LEU A 1 44  ? -21.939 3.153   32.967  1.00 31.57  ? 44  LEU A C   1 
ATOM   347  O  O   . LEU A 1 44  ? -22.895 2.444   33.264  1.00 37.02  ? 44  LEU A O   1 
ATOM   348  C  CB  . LEU A 1 44  ? -19.870 1.780   33.111  1.00 24.89  ? 44  LEU A CB  1 
ATOM   349  C  CG  . LEU A 1 44  ? -18.368 1.688   33.354  1.00 24.85  ? 44  LEU A CG  1 
ATOM   350  C  CD1 . LEU A 1 44  ? -17.923 0.308   32.925  1.00 22.54  ? 44  LEU A CD1 1 
ATOM   351  C  CD2 . LEU A 1 44  ? -17.635 2.770   32.583  1.00 23.58  ? 44  LEU A CD2 1 
ATOM   352  N  N   . LYS A 1 45  ? -21.944 4.001   31.948  1.00 30.72  ? 45  LYS A N   1 
ATOM   353  C  CA  . LYS A 1 45  ? -23.180 4.174   31.198  1.00 30.28  ? 45  LYS A CA  1 
ATOM   354  C  C   . LYS A 1 45  ? -23.218 3.206   30.029  1.00 26.51  ? 45  LYS A C   1 
ATOM   355  O  O   . LYS A 1 45  ? -22.185 2.607   29.628  1.00 27.32  ? 45  LYS A O   1 
ATOM   356  C  CB  . LYS A 1 45  ? -23.340 5.603   30.724  1.00 28.12  ? 45  LYS A CB  1 
ATOM   357  C  CG  . LYS A 1 45  ? -23.047 6.626   31.796  1.00 32.07  ? 45  LYS A CG  1 
ATOM   358  C  CD  . LYS A 1 45  ? -23.521 8.003   31.414  1.00 46.51  ? 45  LYS A CD  1 
ATOM   359  C  CE  . LYS A 1 45  ? -23.043 9.047   32.406  1.00 49.94  ? 45  LYS A CE  1 
ATOM   360  N  NZ  . LYS A 1 45  ? -21.592 8.891   32.682  1.00 54.57  ? 45  LYS A NZ  1 
ATOM   361  N  N   . PRO A 1 46  ? -24.439 3.023   29.440  1.00 23.83  ? 46  PRO A N   1 
ATOM   362  C  CA  . PRO A 1 46  ? -24.567 2.304   28.180  1.00 25.30  ? 46  PRO A CA  1 
ATOM   363  C  C   . PRO A 1 46  ? -23.766 3.130   27.196  1.00 21.49  ? 46  PRO A C   1 
ATOM   364  O  O   . PRO A 1 46  ? -23.680 4.354   27.262  1.00 23.04  ? 46  PRO A O   1 
ATOM   365  C  CB  . PRO A 1 46  ? -26.068 2.416   27.847  1.00 28.90  ? 46  PRO A CB  1 
ATOM   366  C  CG  . PRO A 1 46  ? -26.744 2.671   29.166  1.00 35.00  ? 46  PRO A CG  1 
ATOM   367  C  CD  . PRO A 1 46  ? -25.735 3.489   29.944  1.00 28.17  ? 46  PRO A CD  1 
ATOM   368  N  N   . LEU A 1 47  ? -23.133 2.420   26.288  1.00 25.34  ? 47  LEU A N   1 
ATOM   369  C  CA  . LEU A 1 47  ? -22.450 3.086   25.228  1.00 21.82  ? 47  LEU A CA  1 
ATOM   370  C  C   . LEU A 1 47  ? -23.508 3.624   24.270  1.00 24.51  ? 47  LEU A C   1 
ATOM   371  O  O   . LEU A 1 47  ? -24.516 2.977   24.063  1.00 28.09  ? 47  LEU A O   1 
ATOM   372  C  CB  . LEU A 1 47  ? -21.609 1.970   24.614  1.00 31.67  ? 47  LEU A CB  1 
ATOM   373  C  CG  . LEU A 1 47  ? -20.583 2.380   23.595  1.00 33.97  ? 47  LEU A CG  1 
ATOM   374  C  CD1 . LEU A 1 47  ? -19.507 3.173   24.324  1.00 34.54  ? 47  LEU A CD1 1 
ATOM   375  C  CD2 . LEU A 1 47  ? -20.026 1.122   22.959  1.00 36.56  ? 47  LEU A CD2 1 
ATOM   376  N  N   . SER A 1 48  ? -23.287 4.817   23.752  1.00 19.63  ? 48  SER A N   1 
ATOM   377  C  CA  . SER A 1 48  ? -24.157 5.374   22.724  1.00 19.17  ? 48  SER A CA  1 
ATOM   378  C  C   . SER A 1 48  ? -23.360 5.344   21.423  1.00 18.50  ? 48  SER A C   1 
ATOM   379  O  O   . SER A 1 48  ? -22.339 6.028   21.278  1.00 20.60  ? 48  SER A O   1 
ATOM   380  C  CB  . SER A 1 48  ? -24.458 6.829   23.117  1.00 22.14  ? 48  SER A CB  1 
ATOM   381  O  OG  . SER A 1 48  ? -25.110 7.526   22.074  1.00 29.04  ? 48  SER A OG  1 
ATOM   382  N  N   . VAL A 1 49  ? -23.813 4.510   20.505  1.00 20.79  ? 49  VAL A N   1 
ATOM   383  C  CA  . VAL A 1 49  ? -23.209 4.458   19.185  1.00 21.46  ? 49  VAL A CA  1 
ATOM   384  C  C   . VAL A 1 49  ? -24.209 5.080   18.216  1.00 24.57  ? 49  VAL A C   1 
ATOM   385  O  O   . VAL A 1 49  ? -25.307 4.546   18.063  1.00 29.82  ? 49  VAL A O   1 
ATOM   386  C  CB  . VAL A 1 49  ? -22.932 2.991   18.817  1.00 26.00  ? 49  VAL A CB  1 
ATOM   387  C  CG1 . VAL A 1 49  ? -22.297 2.886   17.450  1.00 32.25  ? 49  VAL A CG1 1 
ATOM   388  C  CG2 . VAL A 1 49  ? -22.094 2.299   19.875  1.00 26.72  ? 49  VAL A CG2 1 
ATOM   389  N  N   . SER A 1 50  ? -23.870 6.235   17.645  1.00 21.51  ? 50  SER A N   1 
ATOM   390  C  CA  . SER A 1 50  ? -24.793 6.977   16.799  1.00 21.59  ? 50  SER A CA  1 
ATOM   391  C  C   . SER A 1 50  ? -24.203 7.077   15.398  1.00 20.82  ? 50  SER A C   1 
ATOM   392  O  O   . SER A 1 50  ? -23.490 8.024   15.074  1.00 22.52  ? 50  SER A O   1 
ATOM   393  C  CB  . SER A 1 50  ? -25.173 8.337   17.350  1.00 29.54  ? 50  SER A CB  1 
ATOM   394  O  OG  . SER A 1 50  ? -25.698 8.226   18.668  1.00 32.65  ? 50  SER A OG  1 
ATOM   395  N  N   . TYR A 1 51  ? -24.500 6.074   14.579  1.00 22.67  ? 51  TYR A N   1 
ATOM   396  C  CA  . TYR A 1 51  ? -23.827 5.908   13.307  1.00 21.10  ? 51  TYR A CA  1 
ATOM   397  C  C   . TYR A 1 51  ? -24.785 6.159   12.120  1.00 21.69  ? 51  TYR A C   1 
ATOM   398  O  O   . TYR A 1 51  ? -24.382 6.001   10.971  1.00 23.14  ? 51  TYR A O   1 
ATOM   399  C  CB  . TYR A 1 51  ? -23.218 4.514   13.164  1.00 19.63  ? 51  TYR A CB  1 
ATOM   400  C  CG  . TYR A 1 51  ? -21.926 4.230   13.914  1.00 17.97  ? 51  TYR A CG  1 
ATOM   401  C  CD1 . TYR A 1 51  ? -21.233 5.231   14.611  1.00 16.84  ? 51  TYR A CD1 1 
ATOM   402  C  CD2 . TYR A 1 51  ? -21.395 2.946   13.890  1.00 16.91  ? 51  TYR A CD2 1 
ATOM   403  C  CE1 . TYR A 1 51  ? -20.037 4.921   15.235  1.00 17.18  ? 51  TYR A CE1 1 
ATOM   404  C  CE2 . TYR A 1 51  ? -20.210 2.628   14.527  1.00 16.17  ? 51  TYR A CE2 1 
ATOM   405  C  CZ  . TYR A 1 51  ? -19.554 3.617   15.231  1.00 15.54  ? 51  TYR A CZ  1 
ATOM   406  O  OH  . TYR A 1 51  ? -18.375 3.264   15.795  1.00 16.78  ? 51  TYR A OH  1 
ATOM   407  N  N   . ASP A 1 52  ? -26.015 6.625   12.391  1.00 24.83  ? 52  ASP A N   1 
ATOM   408  C  CA  . ASP A 1 52  ? -27.035 6.874   11.367  1.00 26.95  ? 52  ASP A CA  1 
ATOM   409  C  C   . ASP A 1 52  ? -26.583 7.723   10.159  1.00 25.49  ? 52  ASP A C   1 
ATOM   410  O  O   . ASP A 1 52  ? -26.947 7.426   9.005   1.00 29.38  ? 52  ASP A O   1 
ATOM   411  C  CB  . ASP A 1 52  ? -28.319 7.376   12.017  1.00 36.33  ? 52  ASP A CB  1 
ATOM   412  C  CG  . ASP A 1 52  ? -28.155 8.450   13.089  1.00 44.73  ? 52  ASP A CG  1 
ATOM   413  O  OD1 . ASP A 1 52  ? -27.397 8.208   14.097  1.00 52.55  ? 52  ASP A OD1 1 
ATOM   414  O  OD2 . ASP A 1 52  ? -28.822 9.513   12.951  1.00 62.08  ? 52  ASP A OD2 1 
ATOM   415  N  N   . GLN A 1 53  ? -25.795 8.768   10.379  1.00 24.65  ? 53  GLN A N   1 
ATOM   416  C  CA  . GLN A 1 53  ? -25.416 9.668   9.280   1.00 25.88  ? 53  GLN A CA  1 
ATOM   417  C  C   . GLN A 1 53  ? -23.969 9.446   8.839   1.00 19.66  ? 53  GLN A C   1 
ATOM   418  O  O   . GLN A 1 53  ? -23.333 10.313  8.250   1.00 22.82  ? 53  GLN A O   1 
ATOM   419  C  CB  . GLN A 1 53  ? -25.587 11.130  9.685   1.00 26.76  ? 53  GLN A CB  1 
ATOM   420  C  CG  . GLN A 1 53  ? -27.060 11.474  9.894   1.00 34.49  ? 53  GLN A CG  1 
ATOM   421  C  CD  . GLN A 1 53  ? -27.842 11.392  8.604   1.00 44.04  ? 53  GLN A CD  1 
ATOM   422  O  OE1 . GLN A 1 53  ? -28.870 10.714  8.520   1.00 66.72  ? 53  GLN A OE1 1 
ATOM   423  N  NE2 . GLN A 1 53  ? -27.328 12.033  7.559   1.00 44.51  ? 53  GLN A NE2 1 
ATOM   424  N  N   . ALA A 1 54  ? -23.418 8.277   9.130   1.00 20.21  ? 54  ALA A N   1 
ATOM   425  C  CA  . ALA A 1 54  ? -22.026 8.032   8.738   1.00 17.98  ? 54  ALA A CA  1 
ATOM   426  C  C   . ALA A 1 54  ? -21.822 8.208   7.231   1.00 18.32  ? 54  ALA A C   1 
ATOM   427  O  O   . ALA A 1 54  ? -22.675 7.786   6.450   1.00 22.16  ? 54  ALA A O   1 
ATOM   428  C  CB  . ALA A 1 54  ? -21.598 6.630   9.155   1.00 19.54  ? 54  ALA A CB  1 
ATOM   429  N  N   . THR A 1 55  ? -20.682 8.788   6.855   1.00 17.40  ? 55  THR A N   1 
ATOM   430  C  CA  . THR A 1 55  ? -20.304 8.966   5.457   1.00 17.67  ? 55  THR A CA  1 
ATOM   431  C  C   . THR A 1 55  ? -18.955 8.296   5.225   1.00 15.45  ? 55  THR A C   1 
ATOM   432  O  O   . THR A 1 55  ? -17.931 8.905   5.479   1.00 17.47  ? 55  THR A O   1 
ATOM   433  C  CB  . THR A 1 55  ? -20.192 10.443  5.044   1.00 21.61  ? 55  THR A CB  1 
ATOM   434  O  OG1 . THR A 1 55  ? -21.494 11.001  5.184   1.00 25.38  ? 55  THR A OG1 1 
ATOM   435  C  CG2 . THR A 1 55  ? -19.753 10.627  3.587   1.00 22.82  ? 55  THR A CG2 1 
ATOM   436  N  N   . SER A 1 56  ? -18.977 7.075   4.725   1.00 16.04  ? 56  SER A N   1 
ATOM   437  C  CA  . SER A 1 56  ? -17.735 6.434   4.364   1.00 15.85  ? 56  SER A CA  1 
ATOM   438  C  C   . SER A 1 56  ? -17.215 7.086   3.091   1.00 15.23  ? 56  SER A C   1 
ATOM   439  O  O   . SER A 1 56  ? -18.007 7.541   2.242   1.00 17.23  ? 56  SER A O   1 
ATOM   440  C  CB  . SER A 1 56  ? -17.894 4.962   4.190   1.00 15.49  ? 56  SER A CB  1 
ATOM   441  O  OG  . SER A 1 56  ? -18.760 4.629   3.085   1.00 17.43  ? 56  SER A OG  1 
ATOM   442  N  N   . LEU A 1 57  ? -15.894 7.159   2.911   1.00 15.62  ? 57  LEU A N   1 
ATOM   443  C  CA  . LEU A 1 57  ? -15.317 7.789   1.747   1.00 16.77  ? 57  LEU A CA  1 
ATOM   444  C  C   . LEU A 1 57  ? -14.536 6.804   0.920   1.00 17.22  ? 57  LEU A C   1 
ATOM   445  O  O   . LEU A 1 57  ? -14.683 6.786   -0.310  1.00 19.75  ? 57  LEU A O   1 
ATOM   446  C  CB  . LEU A 1 57  ? -14.406 8.932   2.207   1.00 18.53  ? 57  LEU A CB  1 
ATOM   447  C  CG  . LEU A 1 57  ? -15.119 10.069  2.918   1.00 21.48  ? 57  LEU A CG  1 
ATOM   448  C  CD1 . LEU A 1 57  ? -14.092 11.030  3.475   1.00 24.13  ? 57  LEU A CD1 1 
ATOM   449  C  CD2 . LEU A 1 57  ? -16.138 10.794  2.001   1.00 28.15  ? 57  LEU A CD2 1 
ATOM   450  N  N   . ARG A 1 58  ? -13.551 6.128   1.481   1.00 17.55  ? 58  ARG A N   1 
ATOM   451  C  CA  . ARG A 1 58  ? -12.514 5.454   0.704   1.00 18.81  ? 58  ARG A CA  1 
ATOM   452  C  C   . ARG A 1 58  ? -12.084 4.233   1.527   1.00 15.29  ? 58  ARG A C   1 
ATOM   453  O  O   . ARG A 1 58  ? -12.215 4.222   2.770   1.00 17.70  ? 58  ARG A O   1 
ATOM   454  C  CB  . ARG A 1 58  ? -11.294 6.369   0.440   1.00 21.31  ? 58  ARG A CB  1 
ATOM   455  C  CG  . ARG A 1 58  ? -11.526 7.519   -0.551  1.00 30.18  ? 58  ARG A CG  1 
ATOM   456  C  CD  . ARG A 1 58  ? -10.319 8.327   -1.017  1.00 38.70  ? 58  ARG A CD  1 
ATOM   457  N  NE  . ARG A 1 58  ? -9.556  7.509   -1.953  1.00 52.25  ? 58  ARG A NE  1 
ATOM   458  C  CZ  . ARG A 1 58  ? -9.940  7.231   -3.197  1.00 45.34  ? 58  ARG A CZ  1 
ATOM   459  N  NH1 . ARG A 1 58  ? -9.185  6.461   -3.962  1.00 38.12  ? 58  ARG A NH1 1 
ATOM   460  N  NH2 . ARG A 1 58  ? -11.076 7.719   -3.677  1.00 57.52  ? 58  ARG A NH2 1 
ATOM   461  N  N   . ILE A 1 59  ? -11.520 3.241   0.855   1.00 17.25  ? 59  ILE A N   1 
ATOM   462  C  CA  . ILE A 1 59  ? -10.915 2.092   1.485   1.00 16.15  ? 59  ILE A CA  1 
ATOM   463  C  C   . ILE A 1 59  ? -9.481  2.003   0.984   1.00 16.68  ? 59  ILE A C   1 
ATOM   464  O  O   . ILE A 1 59  ? -9.236  2.209   -0.197  1.00 17.74  ? 59  ILE A O   1 
ATOM   465  C  CB  . ILE A 1 59  ? -11.746 0.822   1.245   1.00 17.20  ? 59  ILE A CB  1 
ATOM   466  C  CG1 . ILE A 1 59  ? -11.232 -0.345  2.128   1.00 16.75  ? 59  ILE A CG1 1 
ATOM   467  C  CG2 . ILE A 1 59  ? -11.790 0.451   -0.250  1.00 17.82  ? 59  ILE A CG2 1 
ATOM   468  C  CD1 . ILE A 1 59  ? -12.184 -1.542  2.119   1.00 19.68  ? 59  ILE A CD1 1 
ATOM   469  N  N   . LEU A 1 60  ? -8.512  1.673   1.832   1.00 17.22  ? 60  LEU A N   1 
ATOM   470  C  CA  . LEU A 1 60  ? -7.120  1.808   1.482   1.00 17.25  ? 60  LEU A CA  1 
ATOM   471  C  C   . LEU A 1 60  ? -6.367  0.624   2.082   1.00 15.01  ? 60  LEU A C   1 
ATOM   472  O  O   . LEU A 1 60  ? -6.643  0.275   3.238   1.00 18.73  ? 60  LEU A O   1 
ATOM   473  C  CB  . LEU A 1 60  ? -6.591  3.135   2.090   1.00 29.09  ? 60  LEU A CB  1 
ATOM   474  C  CG  . LEU A 1 60  ? -5.078  3.270   2.213   1.00 32.38  ? 60  LEU A CG  1 
ATOM   475  C  CD1 . LEU A 1 60  ? -4.514  3.504   0.785   1.00 37.43  ? 60  LEU A CD1 1 
ATOM   476  C  CD2 . LEU A 1 60  ? -4.736  4.418   3.136   1.00 32.60  ? 60  LEU A CD2 1 
ATOM   477  N  N   . ASN A 1 61  ? -5.407  0.091   1.347   1.00 15.72  ? 61  ASN A N   1 
ATOM   478  C  CA  . ASN A 1 61  ? -4.421  -0.864  1.884   1.00 15.36  ? 61  ASN A CA  1 
ATOM   479  C  C   . ASN A 1 61  ? -3.183  -0.053  2.211   1.00 18.18  ? 61  ASN A C   1 
ATOM   480  O  O   . ASN A 1 61  ? -2.566  0.509   1.328   1.00 18.42  ? 61  ASN A O   1 
ATOM   481  C  CB  . ASN A 1 61  ? -4.093  -1.918  0.817   1.00 17.75  ? 61  ASN A CB  1 
ATOM   482  C  CG  . ASN A 1 61  ? -3.029  -2.907  1.226   1.00 16.01  ? 61  ASN A CG  1 
ATOM   483  O  OD1 . ASN A 1 61  ? -2.196  -2.598  2.101   1.00 18.33  ? 61  ASN A OD1 1 
ATOM   484  N  ND2 . ASN A 1 61  ? -3.064  -4.103  0.649   1.00 16.16  ? 61  ASN A ND2 1 
ATOM   485  N  N   . ASN A 1 62  ? -2.877  0.035   3.487   1.00 17.34  ? 62  ASN A N   1 
ATOM   486  C  CA  . ASN A 1 62  ? -1.759  0.883   3.915   1.00 19.10  ? 62  ASN A CA  1 
ATOM   487  C  C   . ASN A 1 62  ? -0.499  0.070   4.206   1.00 19.33  ? 62  ASN A C   1 
ATOM   488  O  O   . ASN A 1 62  ? 0.484   0.593   4.785   1.00 25.28  ? 62  ASN A O   1 
ATOM   489  C  CB  . ASN A 1 62  ? -2.123  1.724   5.136   1.00 21.24  ? 62  ASN A CB  1 
ATOM   490  C  CG  . ASN A 1 62  ? -2.430  0.906   6.380   1.00 20.27  ? 62  ASN A CG  1 
ATOM   491  O  OD1 . ASN A 1 62  ? -2.251  -0.306  6.397   1.00 19.42  ? 62  ASN A OD1 1 
ATOM   492  N  ND2 . ASN A 1 62  ? -2.902  1.560   7.411   1.00 27.11  ? 62  ASN A ND2 1 
ATOM   493  N  N   . GLY A 1 63  ? -0.497  -1.192  3.799   1.00 18.27  ? 63  GLY A N   1 
ATOM   494  C  CA  . GLY A 1 63  ? 0.687   -2.011  3.971   1.00 20.05  ? 63  GLY A CA  1 
ATOM   495  C  C   . GLY A 1 63  ? 0.720   -2.784  5.274   1.00 17.08  ? 63  GLY A C   1 
ATOM   496  O  O   . GLY A 1 63  ? 1.615   -3.618  5.448   1.00 21.16  ? 63  GLY A O   1 
ATOM   497  N  N   A HIS A 1 64  ? -0.175  -2.403  6.190   0.50 17.97  ? 64  HIS A N   1 
ATOM   498  N  N   B HIS A 1 64  ? -0.276  -2.578  6.140   0.50 17.79  ? 64  HIS A N   1 
ATOM   499  C  CA  A HIS A 1 64  ? -0.293  -3.044  7.491   0.50 17.02  ? 64  HIS A CA  1 
ATOM   500  C  CA  B HIS A 1 64  ? -0.296  -3.303  7.411   0.50 18.23  ? 64  HIS A CA  1 
ATOM   501  C  C   A HIS A 1 64  ? -1.637  -3.747  7.627   0.50 15.14  ? 64  HIS A C   1 
ATOM   502  C  C   B HIS A 1 64  ? -1.720  -3.643  7.861   0.50 15.73  ? 64  HIS A C   1 
ATOM   503  O  O   A HIS A 1 64  ? -1.661  -4.900  8.038   0.50 17.44  ? 64  HIS A O   1 
ATOM   504  O  O   B HIS A 1 64  ? -1.931  -4.410  8.799   0.50 14.98  ? 64  HIS A O   1 
ATOM   505  C  CB  A HIS A 1 64  ? -0.044  -2.051  8.620   0.50 19.96  ? 64  HIS A CB  1 
ATOM   506  C  CB  B HIS A 1 64  ? 0.536   -2.572  8.472   0.50 19.70  ? 64  HIS A CB  1 
ATOM   507  C  CG  A HIS A 1 64  ? 1.196   -1.248  8.406   0.50 17.30  ? 64  HIS A CG  1 
ATOM   508  C  CG  B HIS A 1 64  ? -0.099  -1.305  8.938   0.50 21.57  ? 64  HIS A CG  1 
ATOM   509  N  ND1 A HIS A 1 64  ? 2.487   -1.781  8.528   0.50 22.54  ? 64  HIS A ND1 1 
ATOM   510  N  ND1 B HIS A 1 64  ? 0.276   -0.033  8.487   0.50 22.94  ? 64  HIS A ND1 1 
ATOM   511  C  CD2 A HIS A 1 64  ? 1.358   0.050   8.072   0.50 21.65  ? 64  HIS A CD2 1 
ATOM   512  C  CD2 B HIS A 1 64  ? -1.033  -1.107  9.878   0.50 19.07  ? 64  HIS A CD2 1 
ATOM   513  C  CE1 A HIS A 1 64  ? 3.387   -0.839  8.307   0.50 24.06  ? 64  HIS A CE1 1 
ATOM   514  C  CE1 B HIS A 1 64  ? -0.427  0.883   9.138   0.50 21.00  ? 64  HIS A CE1 1 
ATOM   515  N  NE2 A HIS A 1 64  ? 2.704   0.306   8.021   0.50 23.62  ? 64  HIS A NE2 1 
ATOM   516  N  NE2 B HIS A 1 64  ? -1.242  0.248   9.973   0.50 24.36  ? 64  HIS A NE2 1 
ATOM   517  N  N   . SER A 1 65  ? -2.697  -3.063  7.170   1.00 16.47  ? 65  SER A N   1 
ATOM   518  C  CA  . SER A 1 65  ? -4.082  -3.393  7.353   1.00 16.04  ? 65  SER A CA  1 
ATOM   519  C  C   . SER A 1 65  ? -4.796  -2.801  6.139   1.00 15.93  ? 65  SER A C   1 
ATOM   520  O  O   . SER A 1 65  ? -4.182  -2.274  5.217   1.00 16.36  ? 65  SER A O   1 
ATOM   521  C  CB  . SER A 1 65  ? -4.622  -2.789  8.679   1.00 20.05  ? 65  SER A CB  1 
ATOM   522  O  OG  . SER A 1 65  ? -5.925  -3.274  8.890   1.00 24.65  ? 65  SER A OG  1 
ATOM   523  N  N   . PHE A 1 66  ? -6.114  -2.922  6.116   1.00 15.11  ? 66  PHE A N   1 
ATOM   524  C  CA  . PHE A 1 66  ? -6.893  -2.030  5.292   1.00 15.57  ? 66  PHE A CA  1 
ATOM   525  C  C   . PHE A 1 66  ? -7.794  -1.210  6.189   1.00 15.48  ? 66  PHE A C   1 
ATOM   526  O  O   . PHE A 1 66  ? -8.229  -1.640  7.272   1.00 16.18  ? 66  PHE A O   1 
ATOM   527  C  CB  . PHE A 1 66  ? -7.664  -2.803  4.218   1.00 16.80  ? 66  PHE A CB  1 
ATOM   528  C  CG  . PHE A 1 66  ? -8.799  -3.657  4.741   1.00 15.51  ? 66  PHE A CG  1 
ATOM   529  C  CD1 . PHE A 1 66  ? -10.066 -3.099  4.914   1.00 15.99  ? 66  PHE A CD1 1 
ATOM   530  C  CD2 . PHE A 1 66  ? -8.599  -4.993  5.088   1.00 18.34  ? 66  PHE A CD2 1 
ATOM   531  C  CE1 . PHE A 1 66  ? -11.117 -3.866  5.372   1.00 17.15  ? 66  PHE A CE1 1 
ATOM   532  C  CE2 . PHE A 1 66  ? -9.657  -5.753  5.562   1.00 17.69  ? 66  PHE A CE2 1 
ATOM   533  C  CZ  . PHE A 1 66  ? -10.924 -5.209  5.701   1.00 16.50  ? 66  PHE A CZ  1 
ATOM   534  N  N   . LYS A 1 67  ? -8.117  0.009   5.709   1.00 17.32  ? 67  LYS A N   1 
ATOM   535  C  CA  . LYS A 1 67  ? -8.936  0.896   6.504   1.00 16.60  ? 67  LYS A CA  1 
ATOM   536  C  C   . LYS A 1 67  ? -9.995  1.550   5.654   1.00 14.76  ? 67  LYS A C   1 
ATOM   537  O  O   . LYS A 1 67  ? -9.756  1.825   4.466   1.00 17.01  ? 67  LYS A O   1 
ATOM   538  C  CB  . LYS A 1 67  ? -8.136  1.995   7.205   1.00 22.27  ? 67  LYS A CB  1 
ATOM   539  C  CG  . LYS A 1 67  ? -7.446  3.024   6.342   1.00 24.78  ? 67  LYS A CG  1 
ATOM   540  C  CD  . LYS A 1 67  ? -6.976  4.210   7.252   1.00 28.31  ? 67  LYS A CD  1 
ATOM   541  C  CE  . LYS A 1 67  ? -5.640  3.967   7.900   1.00 36.90  ? 67  LYS A CE  1 
ATOM   542  N  NZ  . LYS A 1 67  ? -4.938  5.259   8.137   1.00 40.02  ? 67  LYS A NZ  1 
ATOM   543  N  N   . VAL A 1 68  ? -11.152 1.716   6.240   1.00 15.03  ? 68  VAL A N   1 
ATOM   544  C  CA  . VAL A 1 68  ? -12.206 2.501   5.639   1.00 14.86  ? 68  VAL A CA  1 
ATOM   545  C  C   . VAL A 1 68  ? -12.213 3.848   6.346   1.00 14.91  ? 68  VAL A C   1 
ATOM   546  O  O   . VAL A 1 68  ? -12.398 3.860   7.573   1.00 15.94  ? 68  VAL A O   1 
ATOM   547  C  CB  . VAL A 1 68  ? -13.538 1.769   5.721   1.00 15.07  ? 68  VAL A CB  1 
ATOM   548  C  CG1 . VAL A 1 68  ? -14.694 2.656   5.271   1.00 17.00  ? 68  VAL A CG1 1 
ATOM   549  C  CG2 . VAL A 1 68  ? -13.544 0.446   4.939   1.00 17.50  ? 68  VAL A CG2 1 
ATOM   550  N  N   . GLU A 1 69  ? -12.096 4.931   5.587   1.00 16.33  ? 69  GLU A N   1 
ATOM   551  C  CA  . GLU A 1 69  ? -12.081 6.253   6.172   1.00 15.50  ? 69  GLU A CA  1 
ATOM   552  C  C   . GLU A 1 69  ? -13.424 6.916   5.974   1.00 16.73  ? 69  GLU A C   1 
ATOM   553  O  O   . GLU A 1 69  ? -14.087 6.685   4.948   1.00 19.59  ? 69  GLU A O   1 
ATOM   554  C  CB  . GLU A 1 69  ? -10.965 7.112   5.575   1.00 21.31  ? 69  GLU A CB  1 
ATOM   555  C  CG  . GLU A 1 69  ? -9.589  6.499   5.805   1.00 29.81  ? 69  GLU A CG  1 
ATOM   556  C  CD  . GLU A 1 69  ? -8.418  7.482   5.825   1.00 36.70  ? 69  GLU A CD  1 
ATOM   557  O  OE1 . GLU A 1 69  ? -7.722  7.536   4.789   1.00 51.58  ? 69  GLU A OE1 1 
ATOM   558  O  OE2 . GLU A 1 69  ? -8.188  8.174   6.882   1.00 52.69  ? 69  GLU A OE2 1 
ATOM   559  N  N   . PHE A 1 70  ? -13.769 7.738   6.954   1.00 16.06  ? 70  PHE A N   1 
ATOM   560  C  CA  . PHE A 1 70  ? -15.045 8.431   7.043   1.00 15.19  ? 70  PHE A CA  1 
ATOM   561  C  C   . PHE A 1 70  ? -14.872 9.935   7.004   1.00 15.61  ? 70  PHE A C   1 
ATOM   562  O  O   . PHE A 1 70  ? -13.829 10.466  7.366   1.00 18.90  ? 70  PHE A O   1 
ATOM   563  C  CB  . PHE A 1 70  ? -15.804 8.067   8.317   1.00 14.97  ? 70  PHE A CB  1 
ATOM   564  C  CG  . PHE A 1 70  ? -16.347 6.670   8.271   1.00 14.87  ? 70  PHE A CG  1 
ATOM   565  C  CD1 . PHE A 1 70  ? -15.522 5.589   8.514   1.00 16.48  ? 70  PHE A CD1 1 
ATOM   566  C  CD2 . PHE A 1 70  ? -17.666 6.416   7.954   1.00 15.69  ? 70  PHE A CD2 1 
ATOM   567  C  CE1 . PHE A 1 70  ? -15.992 4.299   8.413   1.00 17.82  ? 70  PHE A CE1 1 
ATOM   568  C  CE2 . PHE A 1 70  ? -18.155 5.121   7.861   1.00 16.10  ? 70  PHE A CE2 1 
ATOM   569  C  CZ  . PHE A 1 70  ? -17.305 4.062   8.124   1.00 17.03  ? 70  PHE A CZ  1 
ATOM   570  N  N   . ASP A 1 71  ? -15.912 10.654  6.547   1.00 17.16  ? 71  ASP A N   1 
ATOM   571  C  CA  . ASP A 1 71  ? -15.959 12.086  6.724   1.00 16.95  ? 71  ASP A CA  1 
ATOM   572  C  C   . ASP A 1 71  ? -16.176 12.372  8.207   1.00 17.76  ? 71  ASP A C   1 
ATOM   573  O  O   . ASP A 1 71  ? -17.215 12.125  8.761   1.00 21.87  ? 71  ASP A O   1 
ATOM   574  C  CB  . ASP A 1 71  ? -17.092 12.652  5.850   1.00 20.97  ? 71  ASP A CB  1 
ATOM   575  C  CG  . ASP A 1 71  ? -17.330 14.137  6.083   1.00 23.24  ? 71  ASP A CG  1 
ATOM   576  O  OD1 . ASP A 1 71  ? -16.465 14.782  6.697   1.00 23.66  ? 71  ASP A OD1 1 
ATOM   577  O  OD2 . ASP A 1 71  ? -18.425 14.631  5.755   1.00 26.52  ? 71  ASP A OD2 1 
ATOM   578  N  N   . ASP A 1 72  ? -15.190 12.980  8.830   1.00 18.13  ? 72  ASP A N   1 
ATOM   579  C  CA  . ASP A 1 72  ? -15.301 13.296  10.253  1.00 17.92  ? 72  ASP A CA  1 
ATOM   580  C  C   . ASP A 1 72  ? -15.207 14.814  10.427  1.00 20.67  ? 72  ASP A C   1 
ATOM   581  O  O   . ASP A 1 72  ? -14.748 15.289  11.444  1.00 23.78  ? 72  ASP A O   1 
ATOM   582  C  CB  . ASP A 1 72  ? -14.199 12.620  11.058  1.00 18.44  ? 72  ASP A CB  1 
ATOM   583  C  CG  . ASP A 1 72  ? -12.795 12.929  10.615  1.00 19.96  ? 72  ASP A CG  1 
ATOM   584  O  OD1 . ASP A 1 72  ? -12.642 13.645  9.582   1.00 23.71  ? 72  ASP A OD1 1 
ATOM   585  O  OD2 . ASP A 1 72  ? -11.827 12.436  11.274  1.00 22.22  ? 72  ASP A OD2 1 
ATOM   586  N  N   . SER A 1 73  ? -15.681 15.565  9.428   1.00 21.64  ? 73  SER A N   1 
ATOM   587  C  CA  . SER A 1 73  ? -15.634 17.029  9.472   1.00 22.80  ? 73  SER A CA  1 
ATOM   588  C  C   . SER A 1 73  ? -16.891 17.592  10.146  1.00 25.07  ? 73  SER A C   1 
ATOM   589  O  O   . SER A 1 73  ? -17.018 18.798  10.288  1.00 26.98  ? 73  SER A O   1 
ATOM   590  C  CB  . SER A 1 73  ? -15.404 17.580  8.090   1.00 24.73  ? 73  SER A CB  1 
ATOM   591  O  OG  . SER A 1 73  ? -16.584 17.427  7.304   1.00 26.17  ? 73  SER A OG  1 
ATOM   592  N  N   . GLN A 1 74  ? -17.860 16.739  10.501  1.00 25.17  ? 74  GLN A N   1 
ATOM   593  C  CA  . GLN A 1 74  ? -19.018 17.124  11.299  1.00 26.08  ? 74  GLN A CA  1 
ATOM   594  C  C   . GLN A 1 74  ? -19.359 15.962  12.217  1.00 24.60  ? 74  GLN A C   1 
ATOM   595  O  O   . GLN A 1 74  ? -18.854 14.876  11.942  1.00 24.15  ? 74  GLN A O   1 
ATOM   596  C  CB  . GLN A 1 74  ? -20.263 17.325  10.416  1.00 30.43  ? 74  GLN A CB  1 
ATOM   597  C  CG  . GLN A 1 74  ? -20.168 18.357  9.324   1.00 33.96  ? 74  GLN A CG  1 
ATOM   598  C  CD  . GLN A 1 74  ? -21.514 18.444  8.649   1.00 38.28  ? 74  GLN A CD  1 
ATOM   599  O  OE1 . GLN A 1 74  ? -22.479 18.936  9.237   1.00 48.93  ? 74  GLN A OE1 1 
ATOM   600  N  NE2 . GLN A 1 74  ? -21.604 17.934  7.422   1.00 33.81  ? 74  GLN A NE2 1 
ATOM   601  N  N   . ASP A 1 75  ? -20.310 16.141  13.166  1.00 27.86  ? 75  ASP A N   1 
ATOM   602  C  CA  . ASP A 1 75  ? -20.711 15.066  14.076  1.00 30.28  ? 75  ASP A CA  1 
ATOM   603  C  C   . ASP A 1 75  ? -21.711 14.129  13.400  1.00 30.80  ? 75  ASP A C   1 
ATOM   604  O  O   . ASP A 1 75  ? -22.908 14.221  13.634  1.00 53.05  ? 75  ASP A O   1 
ATOM   605  C  CB  . ASP A 1 75  ? -21.295 15.577  15.398  1.00 36.00  ? 75  ASP A CB  1 
ATOM   606  C  CG  . ASP A 1 75  ? -20.292 16.253  16.326  1.00 38.89  ? 75  ASP A CG  1 
ATOM   607  O  OD1 . ASP A 1 75  ? -19.062 16.080  16.098  1.00 42.46  ? 75  ASP A OD1 1 
ATOM   608  O  OD2 . ASP A 1 75  ? -20.746 16.923  17.288  1.00 47.17  ? 75  ASP A OD2 1 
ATOM   609  N  N   . LYS A 1 76  ? -21.220 13.272  12.530  1.00 23.78  ? 76  LYS A N   1 
ATOM   610  C  CA  . LYS A 1 76  ? -22.050 12.373  11.736  1.00 24.61  ? 76  LYS A CA  1 
ATOM   611  C  C   . LYS A 1 76  ? -22.140 10.965  12.325  1.00 28.95  ? 76  LYS A C   1 
ATOM   612  O  O   . LYS A 1 76  ? -23.174 10.311  12.303  1.00 39.98  ? 76  LYS A O   1 
ATOM   613  C  CB  . LYS A 1 76  ? -21.411 12.266  10.351  1.00 27.15  ? 76  LYS A CB  1 
ATOM   614  C  CG  . LYS A 1 76  ? -21.755 13.400  9.412   1.00 28.96  ? 76  LYS A CG  1 
ATOM   615  C  CD  . LYS A 1 76  ? -21.037 13.175  8.102   1.00 28.75  ? 76  LYS A CD  1 
ATOM   616  C  CE  . LYS A 1 76  ? -21.457 14.223  7.097   1.00 30.23  ? 76  LYS A CE  1 
ATOM   617  N  NZ  . LYS A 1 76  ? -21.139 13.831  5.711   1.00 31.57  ? 76  LYS A NZ  1 
ATOM   618  N  N   . ALA A 1 77  ? -21.020 10.444  12.742  1.00 25.24  ? 77  ALA A N   1 
ATOM   619  C  CA  . ALA A 1 77  ? -20.943 9.084   13.276  1.00 21.21  ? 77  ALA A CA  1 
ATOM   620  C  C   . ALA A 1 77  ? -20.175 9.213   14.583  1.00 20.50  ? 77  ALA A C   1 
ATOM   621  O  O   . ALA A 1 77  ? -18.967 9.432   14.551  1.00 24.19  ? 77  ALA A O   1 
ATOM   622  C  CB  . ALA A 1 77  ? -20.222 8.202   12.284  1.00 23.86  ? 77  ALA A CB  1 
ATOM   623  N  N   . VAL A 1 78  ? -20.865 9.148   15.716  1.00 18.89  ? 78  VAL A N   1 
ATOM   624  C  CA  . VAL A 1 78  ? -20.210 9.489   16.983  1.00 19.73  ? 78  VAL A CA  1 
ATOM   625  C  C   . VAL A 1 78  ? -20.476 8.437   18.049  1.00 18.55  ? 78  VAL A C   1 
ATOM   626  O  O   . VAL A 1 78  ? -21.491 7.744   18.067  1.00 21.31  ? 78  VAL A O   1 
ATOM   627  C  CB  . VAL A 1 78  ? -20.606 10.883  17.474  1.00 24.41  ? 78  VAL A CB  1 
ATOM   628  C  CG1 . VAL A 1 78  ? -20.331 11.997  16.476  1.00 29.27  ? 78  VAL A CG1 1 
ATOM   629  C  CG2 . VAL A 1 78  ? -22.017 10.910  17.971  1.00 30.07  ? 78  VAL A CG2 1 
ATOM   630  N  N   . LEU A 1 79  ? -19.479 8.311   18.920  1.00 17.64  ? 79  LEU A N   1 
ATOM   631  C  CA  . LEU A 1 79  ? -19.531 7.480   20.095  1.00 17.87  ? 79  LEU A CA  1 
ATOM   632  C  C   . LEU A 1 79  ? -19.552 8.419   21.297  1.00 18.63  ? 79  LEU A C   1 
ATOM   633  O  O   . LEU A 1 79  ? -18.711 9.337   21.400  1.00 21.01  ? 79  LEU A O   1 
ATOM   634  C  CB  . LEU A 1 79  ? -18.270 6.616   20.060  1.00 20.93  ? 79  LEU A CB  1 
ATOM   635  C  CG  . LEU A 1 79  ? -18.134 5.518   21.086  1.00 20.05  ? 79  LEU A CG  1 
ATOM   636  C  CD1 . LEU A 1 79  ? -19.177 4.460   20.847  1.00 25.48  ? 79  LEU A CD1 1 
ATOM   637  C  CD2 . LEU A 1 79  ? -16.787 4.870   20.897  1.00 19.78  ? 79  LEU A CD2 1 
ATOM   638  N  N   . LYS A 1 80  ? -20.453 8.146   22.235  1.00 20.58  ? 80  LYS A N   1 
ATOM   639  C  CA  . LYS A 1 80  ? -20.413 8.794   23.540  1.00 22.81  ? 80  LYS A CA  1 
ATOM   640  C  C   . LYS A 1 80  ? -20.919 7.856   24.634  1.00 21.58  ? 80  LYS A C   1 
ATOM   641  O  O   . LYS A 1 80  ? -21.221 6.698   24.378  1.00 20.85  ? 80  LYS A O   1 
ATOM   642  C  CB  . LYS A 1 80  ? -21.168 10.124  23.530  1.00 27.74  ? 80  LYS A CB  1 
ATOM   643  C  CG  . LYS A 1 80  ? -22.610 10.016  23.109  1.00 33.10  ? 80  LYS A CG  1 
ATOM   644  C  CD  . LYS A 1 80  ? -23.239 11.399  22.961  1.00 40.12  ? 80  LYS A CD  1 
ATOM   645  N  N   . GLY A 1 81  ? -20.988 8.378   25.867  1.00 22.97  ? 81  GLY A N   1 
ATOM   646  C  CA  . GLY A 1 81  ? -21.443 7.610   27.008  1.00 23.36  ? 81  GLY A CA  1 
ATOM   647  C  C   . GLY A 1 81  ? -20.424 6.518   27.312  1.00 22.25  ? 81  GLY A C   1 
ATOM   648  O  O   . GLY A 1 81  ? -19.244 6.707   27.024  1.00 21.56  ? 81  GLY A O   1 
ATOM   649  N  N   . GLY A 1 82  ? -20.881 5.401   27.861  1.00 26.44  ? 82  GLY A N   1 
ATOM   650  C  CA  . GLY A 1 82  ? -19.955 4.395   28.344  1.00 30.88  ? 82  GLY A CA  1 
ATOM   651  C  C   . GLY A 1 82  ? -19.008 5.043   29.343  1.00 27.49  ? 82  GLY A C   1 
ATOM   652  O  O   . GLY A 1 82  ? -19.415 5.811   30.211  1.00 32.45  ? 82  GLY A O   1 
ATOM   653  N  N   . PRO A 1 83  ? -17.691 4.818   29.208  1.00 24.24  ? 83  PRO A N   1 
ATOM   654  C  CA  . PRO A 1 83  ? -16.733 5.459   30.086  1.00 22.36  ? 83  PRO A CA  1 
ATOM   655  C  C   . PRO A 1 83  ? -16.331 6.857   29.630  1.00 22.23  ? 83  PRO A C   1 
ATOM   656  O  O   . PRO A 1 83  ? -15.437 7.449   30.237  1.00 28.74  ? 83  PRO A O   1 
ATOM   657  C  CB  . PRO A 1 83  ? -15.519 4.533   29.915  1.00 22.45  ? 83  PRO A CB  1 
ATOM   658  C  CG  . PRO A 1 83  ? -15.586 4.101   28.453  1.00 21.08  ? 83  PRO A CG  1 
ATOM   659  C  CD  . PRO A 1 83  ? -17.071 3.928   28.204  1.00 22.94  ? 83  PRO A CD  1 
ATOM   660  N  N   . LEU A 1 84  ? -16.894 7.321   28.498  1.00 20.77  ? 84  LEU A N   1 
ATOM   661  C  CA  . LEU A 1 84  ? -16.361 8.503   27.842  1.00 17.84  ? 84  LEU A CA  1 
ATOM   662  C  C   . LEU A 1 84  ? -17.022 9.759   28.378  1.00 20.44  ? 84  LEU A C   1 
ATOM   663  O  O   . LEU A 1 84  ? -18.206 9.748   28.741  1.00 26.09  ? 84  LEU A O   1 
ATOM   664  C  CB  . LEU A 1 84  ? -16.639 8.441   26.337  1.00 19.07  ? 84  LEU A CB  1 
ATOM   665  C  CG  . LEU A 1 84  ? -16.071 7.207   25.626  1.00 17.37  ? 84  LEU A CG  1 
ATOM   666  C  CD1 . LEU A 1 84  ? -16.559 7.117   24.185  1.00 19.81  ? 84  LEU A CD1 1 
ATOM   667  C  CD2 . LEU A 1 84  ? -14.534 7.143   25.699  1.00 17.82  ? 84  LEU A CD2 1 
ATOM   668  N  N   . ASP A 1 85  ? -16.211 10.815  28.453  1.00 23.43  ? 85  ASP A N   1 
ATOM   669  C  CA  . ASP A 1 85  ? -16.728 12.136  28.724  1.00 26.20  ? 85  ASP A CA  1 
ATOM   670  C  C   . ASP A 1 85  ? -16.671 12.849  27.380  1.00 28.90  ? 85  ASP A C   1 
ATOM   671  O  O   . ASP A 1 85  ? -15.661 12.773  26.680  1.00 37.44  ? 85  ASP A O   1 
ATOM   672  C  CB  . ASP A 1 85  ? -15.819 12.802  29.766  1.00 32.20  ? 85  ASP A CB  1 
ATOM   673  C  CG  . ASP A 1 85  ? -15.911 12.285  31.209  1.00 44.78  ? 85  ASP A CG  1 
ATOM   674  O  OD1 . ASP A 1 85  ? -16.959 11.701  31.601  1.00 48.29  ? 85  ASP A OD1 1 
ATOM   675  O  OD2 . ASP A 1 85  ? -14.923 12.493  31.965  1.00 47.05  ? 85  ASP A OD2 1 
ATOM   676  N  N   . GLY A 1 86  ? -17.745 13.519  27.005  1.00 35.00  ? 86  GLY A N   1 
ATOM   677  C  CA  . GLY A 1 86  ? -17.727 14.155  25.698  1.00 32.15  ? 86  GLY A CA  1 
ATOM   678  C  C   . GLY A 1 86  ? -18.016 13.226  24.504  1.00 27.40  ? 86  GLY A C   1 
ATOM   679  O  O   . GLY A 1 86  ? -18.496 12.084  24.635  1.00 32.23  ? 86  GLY A O   1 
ATOM   680  N  N   . THR A 1 87  ? -17.763 13.749  23.291  1.00 23.48  ? 87  THR A N   1 
ATOM   681  C  CA  . THR A 1 87  ? -18.239 13.183  22.025  1.00 23.03  ? 87  THR A CA  1 
ATOM   682  C  C   . THR A 1 87  ? -17.029 12.806  21.176  1.00 18.47  ? 87  THR A C   1 
ATOM   683  O  O   . THR A 1 87  ? -16.062 13.552  21.083  1.00 21.15  ? 87  THR A O   1 
ATOM   684  C  CB  . THR A 1 87  ? -19.038 14.243  21.249  1.00 29.73  ? 87  THR A CB  1 
ATOM   685  O  OG1 . THR A 1 87  ? -20.222 14.518  21.992  1.00 39.00  ? 87  THR A OG1 1 
ATOM   686  C  CG2 . THR A 1 87  ? -19.429 13.752  19.859  1.00 29.80  ? 87  THR A CG2 1 
ATOM   687  N  N   . TYR A 1 88  ? -17.050 11.604  20.618  1.00 18.61  ? 88  TYR A N   1 
ATOM   688  C  CA  . TYR A 1 88  ? -15.946 11.090  19.828  1.00 17.57  ? 88  TYR A CA  1 
ATOM   689  C  C   . TYR A 1 88  ? -16.435 10.754  18.424  1.00 18.75  ? 88  TYR A C   1 
ATOM   690  O  O   . TYR A 1 88  ? -17.395 10.012  18.231  1.00 23.15  ? 88  TYR A O   1 
ATOM   691  C  CB  . TYR A 1 88  ? -15.377 9.856   20.508  1.00 16.99  ? 88  TYR A CB  1 
ATOM   692  C  CG  . TYR A 1 88  ? -14.583 10.100  21.763  1.00 15.24  ? 88  TYR A CG  1 
ATOM   693  C  CD1 . TYR A 1 88  ? -15.180 10.490  22.940  1.00 16.15  ? 88  TYR A CD1 1 
ATOM   694  C  CD2 . TYR A 1 88  ? -13.214 9.841   21.783  1.00 15.20  ? 88  TYR A CD2 1 
ATOM   695  C  CE1 . TYR A 1 88  ? -14.447 10.697  24.094  1.00 16.13  ? 88  TYR A CE1 1 
ATOM   696  C  CE2 . TYR A 1 88  ? -12.456 9.978   22.940  1.00 14.21  ? 88  TYR A CE2 1 
ATOM   697  C  CZ  . TYR A 1 88  ? -13.085 10.397  24.088  1.00 16.23  ? 88  TYR A CZ  1 
ATOM   698  O  OH  . TYR A 1 88  ? -12.335 10.528  25.212  1.00 17.09  ? 88  TYR A OH  1 
ATOM   699  N  N   . ARG A 1 89  ? -15.755 11.279  17.425  1.00 16.45  ? 89  ARG A N   1 
ATOM   700  C  CA  . ARG A 1 89  ? -16.185 11.129  16.028  1.00 17.15  ? 89  ARG A CA  1 
ATOM   701  C  C   . ARG A 1 89  ? -15.436 9.999   15.354  1.00 14.68  ? 89  ARG A C   1 
ATOM   702  O  O   . ARG A 1 89  ? -14.226 9.890   15.516  1.00 13.48  ? 89  ARG A O   1 
ATOM   703  C  CB  . ARG A 1 89  ? -15.799 12.414  15.258  1.00 22.11  ? 89  ARG A CB  1 
ATOM   704  C  CG  . ARG A 1 89  ? -16.746 13.586  15.355  1.00 27.56  ? 89  ARG A CG  1 
ATOM   705  C  CD  . ARG A 1 89  ? -16.393 14.539  14.215  1.00 26.53  ? 89  ARG A CD  1 
ATOM   706  N  NE  . ARG A 1 89  ? -17.056 15.765  14.618  1.00 28.75  ? 89  ARG A NE  1 
ATOM   707  C  CZ  . ARG A 1 89  ? -16.675 16.989  14.245  1.00 36.64  ? 89  ARG A CZ  1 
ATOM   708  N  NH1 . ARG A 1 89  ? -15.619 17.169  13.451  1.00 28.83  ? 89  ARG A NH1 1 
ATOM   709  N  NH2 . ARG A 1 89  ? -17.334 18.027  14.721  1.00 42.80  ? 89  ARG A NH2 1 
ATOM   710  N  N   . LEU A 1 90  ? -16.206 9.148   14.638  1.00 15.33  ? 90  LEU A N   1 
ATOM   711  C  CA  . LEU A 1 90  ? -15.597 8.052   13.921  1.00 15.07  ? 90  LEU A CA  1 
ATOM   712  C  C   . LEU A 1 90  ? -14.752 8.585   12.761  1.00 13.93  ? 90  LEU A C   1 
ATOM   713  O  O   . LEU A 1 90  ? -15.241 9.359   11.930  1.00 18.08  ? 90  LEU A O   1 
ATOM   714  C  CB  . LEU A 1 90  ? -16.700 7.169   13.357  1.00 15.40  ? 90  LEU A CB  1 
ATOM   715  C  CG  . LEU A 1 90  ? -16.242 6.016   12.445  1.00 15.62  ? 90  LEU A CG  1 
ATOM   716  C  CD1 . LEU A 1 90  ? -15.461 4.951   13.259  1.00 15.65  ? 90  LEU A CD1 1 
ATOM   717  C  CD2 . LEU A 1 90  ? -17.471 5.359   11.833  1.00 17.67  ? 90  LEU A CD2 1 
ATOM   718  N  N   . THR A 1 91  ? -13.478 8.171   12.689  1.00 13.90  ? 91  THR A N   1 
ATOM   719  C  CA  . THR A 1 91  ? -12.646 8.557   11.585  1.00 13.74  ? 91  THR A CA  1 
ATOM   720  C  C   . THR A 1 91  ? -12.337 7.403   10.654  1.00 14.01  ? 91  THR A C   1 
ATOM   721  O  O   . THR A 1 91  ? -12.229 7.605   9.434   1.00 14.12  ? 91  THR A O   1 
ATOM   722  C  CB  . THR A 1 91  ? -11.393 9.280   12.108  1.00 17.13  ? 91  THR A CB  1 
ATOM   723  O  OG1 . THR A 1 91  ? -10.613 9.675   10.978  1.00 22.03  ? 91  THR A OG1 1 
ATOM   724  C  CG2 . THR A 1 91  ? -10.525 8.403   12.983  1.00 17.25  ? 91  THR A CG2 1 
ATOM   725  N  N   . GLN A 1 92  ? -12.197 6.179   11.188  1.00 13.29  ? 92  GLN A N   1 
ATOM   726  C  CA  . GLN A 1 92  ? -11.845 5.069   10.291  1.00 13.38  ? 92  GLN A CA  1 
ATOM   727  C  C   . GLN A 1 92  ? -12.147 3.780   11.035  1.00 11.51  ? 92  GLN A C   1 
ATOM   728  O  O   . GLN A 1 92  ? -12.251 3.783   12.277  1.00 12.99  ? 92  GLN A O   1 
ATOM   729  C  CB  . GLN A 1 92  ? -10.373 5.099   9.851   1.00 15.21  ? 92  GLN A CB  1 
ATOM   730  C  CG  . GLN A 1 92  ? -9.374  5.082   10.996  1.00 16.20  ? 92  GLN A CG  1 
ATOM   731  C  CD  . GLN A 1 92  ? -8.633  3.786   11.126  1.00 15.30  ? 92  GLN A CD  1 
ATOM   732  O  OE1 . GLN A 1 92  ? -9.245  2.741   11.229  1.00 17.21  ? 92  GLN A OE1 1 
ATOM   733  N  NE2 . GLN A 1 92  ? -7.326  3.844   11.171  1.00 22.76  ? 92  GLN A NE2 1 
ATOM   734  N  N   . PHE A 1 93  ? -12.309 2.677   10.298  1.00 12.50  ? 93  PHE A N   1 
ATOM   735  C  CA  . PHE A 1 93  ? -12.191 1.395   10.934  1.00 12.71  ? 93  PHE A CA  1 
ATOM   736  C  C   . PHE A 1 93  ? -11.186 0.548   10.172  1.00 11.45  ? 93  PHE A C   1 
ATOM   737  O  O   . PHE A 1 93  ? -10.946 0.769   8.956   1.00 12.39  ? 93  PHE A O   1 
ATOM   738  C  CB  . PHE A 1 93  ? -13.532 0.684   11.087  1.00 13.11  ? 93  PHE A CB  1 
ATOM   739  C  CG  . PHE A 1 93  ? -14.231 0.252   9.814   1.00 12.83  ? 93  PHE A CG  1 
ATOM   740  C  CD1 . PHE A 1 93  ? -13.847 -0.889  9.136   1.00 14.74  ? 93  PHE A CD1 1 
ATOM   741  C  CD2 . PHE A 1 93  ? -15.391 0.918   9.422   1.00 14.11  ? 93  PHE A CD2 1 
ATOM   742  C  CE1 . PHE A 1 93  ? -14.507 -1.293  7.968   1.00 13.93  ? 93  PHE A CE1 1 
ATOM   743  C  CE2 . PHE A 1 93  ? -16.062 0.502   8.261   1.00 14.89  ? 93  PHE A CE2 1 
ATOM   744  C  CZ  . PHE A 1 93  ? -15.628 -0.597  7.555   1.00 14.71  ? 93  PHE A CZ  1 
ATOM   745  N  N   . HIS A 1 94  ? -10.649 -0.478  10.809  1.00 11.51  ? 94  HIS A N   1 
ATOM   746  C  CA  . HIS A 1 94  ? -9.726  -1.403  10.193  1.00 12.16  ? 94  HIS A CA  1 
ATOM   747  C  C   . HIS A 1 94  ? -9.854  -2.701  10.980  1.00 9.67   ? 94  HIS A C   1 
ATOM   748  O  O   . HIS A 1 94  ? -10.509 -2.768  12.005  1.00 11.59  ? 94  HIS A O   1 
ATOM   749  C  CB  . HIS A 1 94  ? -8.286  -0.885  10.210  1.00 11.69  ? 94  HIS A CB  1 
ATOM   750  C  CG  . HIS A 1 94  ? -7.850  -0.648  11.597  1.00 11.92  ? 94  HIS A CG  1 
ATOM   751  N  ND1 . HIS A 1 94  ? -8.054  0.545   12.263  1.00 12.54  ? 94  HIS A ND1 1 
ATOM   752  C  CD2 . HIS A 1 94  ? -7.191  -1.437  12.465  1.00 12.35  ? 94  HIS A CD2 1 
ATOM   753  C  CE1 . HIS A 1 94  ? -7.623  0.419   13.535  1.00 12.26  ? 94  HIS A CE1 1 
ATOM   754  N  NE2 . HIS A 1 94  ? -7.093  -0.854  13.704  1.00 11.03  ? 94  HIS A NE2 1 
ATOM   755  N  N   . PHE A 1 95  ? -9.108  -3.712  10.535  1.00 11.34  ? 95  PHE A N   1 
ATOM   756  C  CA  . PHE A 1 95  ? -9.152  -5.016  11.169  1.00 11.71  ? 95  PHE A CA  1 
ATOM   757  C  C   . PHE A 1 95  ? -7.736  -5.507  11.380  1.00 12.31  ? 95  PHE A C   1 
ATOM   758  O  O   . PHE A 1 95  ? -6.779  -5.061  10.755  1.00 12.42  ? 95  PHE A O   1 
ATOM   759  C  CB  . PHE A 1 95  ? -9.837  -6.072  10.252  1.00 12.95  ? 95  PHE A CB  1 
ATOM   760  C  CG  . PHE A 1 95  ? -11.284 -5.785  9.983   1.00 12.63  ? 95  PHE A CG  1 
ATOM   761  C  CD1 . PHE A 1 95  ? -11.628 -4.876  8.969   1.00 13.75  ? 95  PHE A CD1 1 
ATOM   762  C  CD2 . PHE A 1 95  ? -12.288 -6.484  10.619  1.00 13.57  ? 95  PHE A CD2 1 
ATOM   763  C  CE1 . PHE A 1 95  ? -12.972 -4.674  8.650   1.00 14.54  ? 95  PHE A CE1 1 
ATOM   764  C  CE2 . PHE A 1 95  ? -13.615 -6.279  10.308  1.00 14.04  ? 95  PHE A CE2 1 
ATOM   765  C  CZ  . PHE A 1 95  ? -13.961 -5.368  9.312   1.00 15.61  ? 95  PHE A CZ  1 
ATOM   766  N  N   . HIS A 1 96  ? -7.638  -6.486  12.265  1.00 11.68  ? 96  HIS A N   1 
ATOM   767  C  CA  . HIS A 1 96  ? -6.424  -7.284  12.450  1.00 11.59  ? 96  HIS A CA  1 
ATOM   768  C  C   . HIS A 1 96  ? -6.898  -8.724  12.299  1.00 11.77  ? 96  HIS A C   1 
ATOM   769  O  O   . HIS A 1 96  ? -7.964  -9.060  12.819  1.00 11.63  ? 96  HIS A O   1 
ATOM   770  C  CB  . HIS A 1 96  ? -5.807  -7.087  13.839  1.00 12.05  ? 96  HIS A CB  1 
ATOM   771  C  CG  . HIS A 1 96  ? -5.505  -5.649  14.112  1.00 11.66  ? 96  HIS A CG  1 
ATOM   772  N  ND1 . HIS A 1 96  ? -4.264  -5.061  13.900  1.00 12.78  ? 96  HIS A ND1 1 
ATOM   773  C  CD2 . HIS A 1 96  ? -6.312  -4.644  14.550  1.00 11.09  ? 96  HIS A CD2 1 
ATOM   774  C  CE1 . HIS A 1 96  ? -4.333  -3.780  14.261  1.00 12.08  ? 96  HIS A CE1 1 
ATOM   775  N  NE2 . HIS A 1 96  ? -5.606  -3.477  14.589  1.00 11.53  ? 96  HIS A NE2 1 
ATOM   776  N  N   . TRP A 1 97  ? -6.043  -9.596  11.713  1.00 11.70  ? 97  TRP A N   1 
ATOM   777  C  CA  . TRP A 1 97  ? -6.522  -10.956 11.509  1.00 11.37  ? 97  TRP A CA  1 
ATOM   778  C  C   . TRP A 1 97  ? -5.331  -11.898 11.407  1.00 11.16  ? 97  TRP A C   1 
ATOM   779  O  O   . TRP A 1 97  ? -4.155  -11.471 11.349  1.00 12.86  ? 97  TRP A O   1 
ATOM   780  C  CB  . TRP A 1 97  ? -7.423  -11.124 10.284  1.00 12.51  ? 97  TRP A CB  1 
ATOM   781  C  CG  . TRP A 1 97  ? -6.754  -10.781 8.997   1.00 11.43  ? 97  TRP A CG  1 
ATOM   782  C  CD1 . TRP A 1 97  ? -5.981  -11.587 8.188   1.00 13.20  ? 97  TRP A CD1 1 
ATOM   783  C  CD2 . TRP A 1 97  ? -6.656  -9.459  8.425   1.00 12.21  ? 97  TRP A CD2 1 
ATOM   784  N  NE1 . TRP A 1 97  ? -5.539  -10.896 7.074   1.00 13.61  ? 97  TRP A NE1 1 
ATOM   785  C  CE2 . TRP A 1 97  ? -5.908  -9.588  7.238   1.00 12.53  ? 97  TRP A CE2 1 
ATOM   786  C  CE3 . TRP A 1 97  ? -7.113  -8.190  8.799   1.00 11.99  ? 97  TRP A CE3 1 
ATOM   787  C  CZ2 . TRP A 1 97  ? -5.654  -8.492  6.412   1.00 14.29  ? 97  TRP A CZ2 1 
ATOM   788  C  CZ3 . TRP A 1 97  ? -6.878  -7.106  7.974   1.00 13.56  ? 97  TRP A CZ3 1 
ATOM   789  C  CH2 . TRP A 1 97  ? -6.168  -7.248  6.791   1.00 13.26  ? 97  TRP A CH2 1 
ATOM   790  N  N   . GLY A 1 98  ? -5.624  -13.204 11.416  1.00 12.04  ? 98  GLY A N   1 
ATOM   791  C  CA  . GLY A 1 98  ? -4.602  -14.239 11.527  1.00 13.55  ? 98  GLY A CA  1 
ATOM   792  C  C   . GLY A 1 98  ? -4.378  -14.963 10.192  1.00 13.60  ? 98  GLY A C   1 
ATOM   793  O  O   . GLY A 1 98  ? -5.107  -14.801 9.214   1.00 14.73  ? 98  GLY A O   1 
ATOM   794  N  N   . SER A 1 99  ? -3.376  -15.856 10.217  1.00 14.71  ? 99  SER A N   1 
ATOM   795  C  CA  . SER A 1 99  ? -3.153  -16.779 9.116   1.00 16.49  ? 99  SER A CA  1 
ATOM   796  C  C   . SER A 1 99  ? -4.038  -18.016 9.268   1.00 15.20  ? 99  SER A C   1 
ATOM   797  O  O   . SER A 1 99  ? -4.179  -18.760 8.301   1.00 22.52  ? 99  SER A O   1 
ATOM   798  C  CB  . SER A 1 99  ? -1.698  -17.150 9.094   1.00 19.33  ? 99  SER A CB  1 
ATOM   799  O  OG  . SER A 1 99  ? -1.271  -17.605 10.384  1.00 18.09  ? 99  SER A OG  1 
ATOM   800  N  N   . LEU A 1 100 ? -4.652  -18.224 10.451  1.00 16.87  ? 100 LEU A N   1 
ATOM   801  C  CA  . LEU A 1 100 ? -5.468  -19.369 10.848  1.00 19.86  ? 100 LEU A CA  1 
ATOM   802  C  C   . LEU A 1 100 ? -6.605  -18.831 11.697  1.00 17.33  ? 100 LEU A C   1 
ATOM   803  O  O   . LEU A 1 100 ? -6.411  -17.808 12.336  1.00 18.59  ? 100 LEU A O   1 
ATOM   804  C  CB  . LEU A 1 100 ? -4.622  -20.317 11.728  1.00 26.90  ? 100 LEU A CB  1 
ATOM   805  C  CG  . LEU A 1 100 ? -3.328  -20.792 11.104  1.00 26.81  ? 100 LEU A CG  1 
ATOM   806  C  CD1 . LEU A 1 100 ? -2.442  -21.542 12.096  1.00 34.19  ? 100 LEU A CD1 1 
ATOM   807  C  CD2 . LEU A 1 100 ? -3.713  -21.750 9.996   1.00 34.29  ? 100 LEU A CD2 1 
ATOM   808  N  N   . ASP A 1 101 ? -7.724  -19.543 11.774  1.00 18.59  ? 101 ASP A N   1 
ATOM   809  C  CA  . ASP A 1 101 ? -8.879  -19.024 12.472  1.00 18.12  ? 101 ASP A CA  1 
ATOM   810  C  C   . ASP A 1 101 ? -8.650  -18.959 13.989  1.00 19.13  ? 101 ASP A C   1 
ATOM   811  O  O   . ASP A 1 101 ? -9.359  -18.236 14.681  1.00 21.64  ? 101 ASP A O   1 
ATOM   812  C  CB  . ASP A 1 101 ? -10.097 -19.897 12.206  1.00 20.19  ? 101 ASP A CB  1 
ATOM   813  C  CG  . ASP A 1 101 ? -10.617 -19.908 10.773  1.00 24.21  ? 101 ASP A CG  1 
ATOM   814  O  OD1 . ASP A 1 101 ? -10.171 -19.108 9.925   1.00 23.99  ? 101 ASP A OD1 1 
ATOM   815  O  OD2 . ASP A 1 101 ? -11.518 -20.756 10.516  1.00 27.98  ? 101 ASP A OD2 1 
ATOM   816  N  N   . GLY A 1 102 ? -7.649  -19.695 14.505  1.00 19.37  ? 102 GLY A N   1 
ATOM   817  C  CA  . GLY A 1 102 ? -7.370  -19.637 15.934  1.00 20.89  ? 102 GLY A CA  1 
ATOM   818  C  C   . GLY A 1 102 ? -6.437  -18.532 16.408  1.00 17.18  ? 102 GLY A C   1 
ATOM   819  O  O   . GLY A 1 102 ? -6.076  -18.479 17.581  1.00 19.63  ? 102 GLY A O   1 
ATOM   820  N  N   . GLN A 1 103 ? -6.194  -17.528 15.572  1.00 15.91  ? 103 GLN A N   1 
ATOM   821  C  CA  . GLN A 1 103 ? -5.427  -16.373 15.973  1.00 14.15  ? 103 GLN A CA  1 
ATOM   822  C  C   . GLN A 1 103 ? -5.838  -15.211 15.091  1.00 13.76  ? 103 GLN A C   1 
ATOM   823  O  O   . GLN A 1 103 ? -6.354  -15.424 13.994  1.00 14.83  ? 103 GLN A O   1 
ATOM   824  C  CB  . GLN A 1 103 ? -3.931  -16.647 16.008  1.00 14.52  ? 103 GLN A CB  1 
ATOM   825  C  CG  . GLN A 1 103 ? -3.360  -16.876 14.598  1.00 15.39  ? 103 GLN A CG  1 
ATOM   826  C  CD  . GLN A 1 103 ? -2.004  -17.538 14.666  1.00 21.61  ? 103 GLN A CD  1 
ATOM   827  O  OE1 . GLN A 1 103 ? -1.810  -18.507 15.395  1.00 34.45  ? 103 GLN A OE1 1 
ATOM   828  N  NE2 . GLN A 1 103 ? -1.061  -17.063 13.886  1.00 18.12  ? 103 GLN A NE2 1 
ATOM   829  N  N   . GLY A 1 104 ? -5.501  -13.995 15.502  1.00 12.71  ? 104 GLY A N   1 
ATOM   830  C  CA  . GLY A 1 104 ? -5.790  -12.823 14.697  1.00 12.51  ? 104 GLY A CA  1 
ATOM   831  C  C   . GLY A 1 104 ? -6.250  -11.642 15.529  1.00 10.94  ? 104 GLY A C   1 
ATOM   832  O  O   . GLY A 1 104 ? -5.950  -10.490 15.152  1.00 13.75  ? 104 GLY A O   1 
ATOM   833  N  N   . SER A 1 105 ? -6.910  -11.890 16.664  1.00 11.20  ? 105 SER A N   1 
ATOM   834  C  CA  . SER A 1 105 ? -7.328  -10.762 17.482  1.00 12.41  ? 105 SER A CA  1 
ATOM   835  C  C   . SER A 1 105 ? -6.118  -10.214 18.242  1.00 11.05  ? 105 SER A C   1 
ATOM   836  O  O   . SER A 1 105 ? -5.081  -10.888 18.435  1.00 12.84  ? 105 SER A O   1 
ATOM   837  C  CB  . SER A 1 105 ? -8.463  -11.099 18.405  1.00 12.06  ? 105 SER A CB  1 
ATOM   838  O  OG  . SER A 1 105 ? -8.077  -12.082 19.385  1.00 12.74  ? 105 SER A OG  1 
ATOM   839  N  N   . GLU A 1 106 ? -6.270  -8.961  18.609  1.00 12.07  ? 106 GLU A N   1 
ATOM   840  C  CA  . GLU A 1 106 ? -5.227  -8.288  19.421  1.00 10.72  ? 106 GLU A CA  1 
ATOM   841  C  C   . GLU A 1 106 ? -5.572  -8.456  20.901  1.00 10.59  ? 106 GLU A C   1 
ATOM   842  O  O   . GLU A 1 106 ? -4.770  -9.031  21.655  1.00 11.96  ? 106 GLU A O   1 
ATOM   843  C  CB  . GLU A 1 106 ? -5.195  -6.805  19.019  1.00 11.45  ? 106 GLU A CB  1 
ATOM   844  C  CG  . GLU A 1 106 ? -4.789  -6.681  17.549  1.00 13.20  ? 106 GLU A CG  1 
ATOM   845  C  CD  . GLU A 1 106 ? -4.039  -5.410  17.278  1.00 12.97  ? 106 GLU A CD  1 
ATOM   846  O  OE1 . GLU A 1 106 ? -4.646  -4.317  17.525  1.00 13.30  ? 106 GLU A OE1 1 
ATOM   847  O  OE2 . GLU A 1 106 ? -2.877  -5.457  16.848  1.00 14.23  ? 106 GLU A OE2 1 
ATOM   848  N  N   . HIS A 1 107 ? -6.757  -8.039  21.315  1.00 10.96  ? 107 HIS A N   1 
ATOM   849  C  CA  . HIS A 1 107 ? -7.192  -8.392  22.648  1.00 10.30  ? 107 HIS A CA  1 
ATOM   850  C  C   . HIS A 1 107 ? -7.458  -9.884  22.663  1.00 11.44  ? 107 HIS A C   1 
ATOM   851  O  O   . HIS A 1 107 ? -7.779  -10.511 21.652  1.00 12.63  ? 107 HIS A O   1 
ATOM   852  C  CB  . HIS A 1 107 ? -8.442  -7.608  23.063  1.00 11.20  ? 107 HIS A CB  1 
ATOM   853  C  CG  . HIS A 1 107 ? -8.115  -6.183  23.206  1.00 11.08  ? 107 HIS A CG  1 
ATOM   854  N  ND1 . HIS A 1 107 ? -8.193  -5.281  22.155  1.00 11.69  ? 107 HIS A ND1 1 
ATOM   855  C  CD2 . HIS A 1 107 ? -7.633  -5.479  24.263  1.00 12.95  ? 107 HIS A CD2 1 
ATOM   856  C  CE1 . HIS A 1 107 ? -7.742  -4.083  22.541  1.00 12.00  ? 107 HIS A CE1 1 
ATOM   857  N  NE2 . HIS A 1 107 ? -7.435  -4.163  23.866  1.00 11.77  ? 107 HIS A NE2 1 
ATOM   858  N  N   . THR A 1 108 ? -7.357  -10.434 23.871  1.00 12.16  ? 108 THR A N   1 
ATOM   859  C  CA  . THR A 1 108 ? -7.734  -11.816 24.133  1.00 11.50  ? 108 THR A CA  1 
ATOM   860  C  C   . THR A 1 108 ? -8.674  -11.820 25.335  1.00 11.43  ? 108 THR A C   1 
ATOM   861  O  O   . THR A 1 108 ? -8.731  -10.866 26.093  1.00 13.19  ? 108 THR A O   1 
ATOM   862  C  CB  . THR A 1 108 ? -6.542  -12.755 24.353  1.00 13.04  ? 108 THR A CB  1 
ATOM   863  O  OG1 . THR A 1 108 ? -5.682  -12.238 25.364  1.00 13.80  ? 108 THR A OG1 1 
ATOM   864  C  CG2 . THR A 1 108 ? -5.682  -12.784 23.129  1.00 14.39  ? 108 THR A CG2 1 
ATOM   865  N  N   . VAL A 1 109 ? -9.473  -12.877 25.446  1.00 12.80  ? 109 VAL A N   1 
ATOM   866  C  CA  . VAL A 1 109 ? -10.424 -12.961 26.542  1.00 13.33  ? 109 VAL A CA  1 
ATOM   867  C  C   . VAL A 1 109 ? -10.109 -14.264 27.250  1.00 14.92  ? 109 VAL A C   1 
ATOM   868  O  O   . VAL A 1 109 ? -10.320 -15.347 26.715  1.00 15.19  ? 109 VAL A O   1 
ATOM   869  C  CB  . VAL A 1 109 ? -11.875 -12.966 25.976  1.00 14.30  ? 109 VAL A CB  1 
ATOM   870  C  CG1 . VAL A 1 109 ? -12.861 -13.053 27.109  1.00 17.59  ? 109 VAL A CG1 1 
ATOM   871  C  CG2 . VAL A 1 109 ? -12.130 -11.693 25.171  1.00 16.26  ? 109 VAL A CG2 1 
ATOM   872  N  N   . ASP A 1 110 ? -9.650  -14.153 28.489  1.00 14.53  ? 110 ASP A N   1 
ATOM   873  C  CA  . ASP A 1 110 ? -9.185  -15.333 29.232  1.00 17.37  ? 110 ASP A CA  1 
ATOM   874  C  C   . ASP A 1 110 ? -8.236  -16.157 28.365  1.00 16.19  ? 110 ASP A C   1 
ATOM   875  O  O   . ASP A 1 110 ? -8.301  -17.400 28.319  1.00 17.62  ? 110 ASP A O   1 
ATOM   876  C  CB  . ASP A 1 110 ? -10.374 -16.149 29.722  1.00 18.94  ? 110 ASP A CB  1 
ATOM   877  C  CG  . ASP A 1 110 ? -11.256 -15.394 30.720  1.00 18.07  ? 110 ASP A CG  1 
ATOM   878  O  OD1 . ASP A 1 110 ? -10.708 -14.542 31.398  1.00 21.88  ? 110 ASP A OD1 1 
ATOM   879  O  OD2 . ASP A 1 110 ? -12.471 -15.686 30.811  1.00 27.08  ? 110 ASP A OD2 1 
ATOM   880  N  N   . LYS A 1 111 ? -7.338  -15.455 27.680  1.00 15.30  ? 111 LYS A N   1 
ATOM   881  C  CA  . LYS A 1 111 ? -6.303  -15.981 26.792  1.00 15.76  ? 111 LYS A CA  1 
ATOM   882  C  C   . LYS A 1 111 ? -6.846  -16.533 25.478  1.00 15.80  ? 111 LYS A C   1 
ATOM   883  O  O   . LYS A 1 111 ? -6.059  -16.800 24.582  1.00 16.51  ? 111 LYS A O   1 
ATOM   884  C  CB  . LYS A 1 111 ? -5.410  -17.057 27.420  1.00 18.11  ? 111 LYS A CB  1 
ATOM   885  C  CG  . LYS A 1 111 ? -4.800  -16.658 28.749  1.00 23.24  ? 111 LYS A CG  1 
ATOM   886  C  CD  . LYS A 1 111 ? -3.778  -15.590 28.559  1.00 28.94  ? 111 LYS A CD  1 
ATOM   887  C  CE  . LYS A 1 111 ? -3.164  -15.203 29.889  1.00 33.51  ? 111 LYS A CE  1 
ATOM   888  N  NZ  . LYS A 1 111 ? -1.713  -14.996 29.714  1.00 35.50  ? 111 LYS A NZ  1 
ATOM   889  N  N   . LYS A 1 112 ? -8.160  -16.476 25.267  1.00 14.34  ? 112 LYS A N   1 
ATOM   890  C  CA  . LYS A 1 112 ? -8.699  -16.907 23.979  1.00 15.90  ? 112 LYS A CA  1 
ATOM   891  C  C   . LYS A 1 112 ? -8.415  -15.853 22.901  1.00 14.47  ? 112 LYS A C   1 
ATOM   892  O  O   . LYS A 1 112 ? -8.700  -14.679 23.107  1.00 14.61  ? 112 LYS A O   1 
ATOM   893  C  CB  . LYS A 1 112 ? -10.233 -17.032 24.030  1.00 18.09  ? 112 LYS A CB  1 
ATOM   894  C  CG  . LYS A 1 112 ? -10.936 -17.401 22.719  1.00 22.33  ? 112 LYS A CG  1 
ATOM   895  C  CD  . LYS A 1 112 ? -12.479 -17.462 22.818  1.00 23.69  ? 112 LYS A CD  1 
ATOM   896  C  CE  . LYS A 1 112 ? -13.079 -17.694 21.450  1.00 29.03  ? 112 LYS A CE  1 
ATOM   897  N  NZ  . LYS A 1 112 ? -12.563 -18.891 20.759  1.00 33.49  ? 112 LYS A NZ  1 
ATOM   898  N  N   A LYS A 1 113 ? -7.877  -16.292 21.755  0.50 14.06  ? 113 LYS A N   1 
ATOM   899  N  N   B LYS A 1 113 ? -7.912  -16.308 21.749  0.50 14.33  ? 113 LYS A N   1 
ATOM   900  C  CA  A LYS A 1 113 ? -7.715  -15.477 20.565  0.50 14.92  ? 113 LYS A CA  1 
ATOM   901  C  CA  B LYS A 1 113 ? -7.733  -15.494 20.564  0.50 14.97  ? 113 LYS A CA  1 
ATOM   902  C  C   A LYS A 1 113 ? -8.876  -15.725 19.627  0.50 12.95  ? 113 LYS A C   1 
ATOM   903  C  C   B LYS A 1 113 ? -8.870  -15.737 19.597  0.50 13.32  ? 113 LYS A C   1 
ATOM   904  O  O   A LYS A 1 113 ? -9.280  -16.862 19.435  0.50 17.59  ? 113 LYS A O   1 
ATOM   905  O  O   B LYS A 1 113 ? -9.244  -16.876 19.354  0.50 19.12  ? 113 LYS A O   1 
ATOM   906  C  CB  A LYS A 1 113 ? -6.426  -15.857 19.832  0.50 15.57  ? 113 LYS A CB  1 
ATOM   907  C  CB  B LYS A 1 113 ? -6.411  -15.852 19.888  0.50 16.15  ? 113 LYS A CB  1 
ATOM   908  C  CG  A LYS A 1 113 ? -5.155  -15.597 20.634  0.50 16.50  ? 113 LYS A CG  1 
ATOM   909  C  CG  B LYS A 1 113 ? -5.201  -15.414 20.699  0.50 16.56  ? 113 LYS A CG  1 
ATOM   910  C  CD  A LYS A 1 113 ? -3.920  -16.267 20.012  0.50 16.90  ? 113 LYS A CD  1 
ATOM   911  C  CD  B LYS A 1 113 ? -3.903  -16.036 20.164  0.50 16.88  ? 113 LYS A CD  1 
ATOM   912  C  CE  A LYS A 1 113 ? -2.619  -15.817 20.647  0.50 17.16  ? 113 LYS A CE  1 
ATOM   913  C  CE  B LYS A 1 113 ? -2.673  -15.315 20.682  0.50 20.18  ? 113 LYS A CE  1 
ATOM   914  N  NZ  A LYS A 1 113 ? -2.341  -16.453 21.961  0.50 19.53  ? 113 LYS A NZ  1 
ATOM   915  N  NZ  B LYS A 1 113 ? -1.458  -16.173 20.672  0.50 21.85  ? 113 LYS A NZ  1 
ATOM   916  N  N   . TYR A 1 114 ? -9.410  -14.643 19.064  1.00 13.33  ? 114 TYR A N   1 
ATOM   917  C  CA  . TYR A 1 114 ? -10.405 -14.734 18.010  1.00 12.75  ? 114 TYR A CA  1 
ATOM   918  C  C   . TYR A 1 114 ? -9.718  -14.683 16.661  1.00 12.10  ? 114 TYR A C   1 
ATOM   919  O  O   . TYR A 1 114 ? -8.536  -14.373 16.524  1.00 13.05  ? 114 TYR A O   1 
ATOM   920  C  CB  . TYR A 1 114 ? -11.447 -13.643 18.165  1.00 12.99  ? 114 TYR A CB  1 
ATOM   921  C  CG  . TYR A 1 114 ? -12.351 -13.860 19.333  1.00 13.07  ? 114 TYR A CG  1 
ATOM   922  C  CD1 . TYR A 1 114 ? -12.001 -13.421 20.599  1.00 15.26  ? 114 TYR A CD1 1 
ATOM   923  C  CD2 . TYR A 1 114 ? -13.567 -14.506 19.186  1.00 14.95  ? 114 TYR A CD2 1 
ATOM   924  C  CE1 . TYR A 1 114 ? -12.833 -13.618 21.688  1.00 18.98  ? 114 TYR A CE1 1 
ATOM   925  C  CE2 . TYR A 1 114 ? -14.412 -14.712 20.264  1.00 17.93  ? 114 TYR A CE2 1 
ATOM   926  C  CZ  . TYR A 1 114 ? -14.043 -14.266 21.521  1.00 18.55  ? 114 TYR A CZ  1 
ATOM   927  O  OH  . TYR A 1 114 ? -14.870 -14.465 22.589  1.00 27.30  ? 114 TYR A OH  1 
ATOM   928  N  N   . ALA A 1 115 ? -10.488 -14.996 15.600  1.00 12.74  ? 115 ALA A N   1 
ATOM   929  C  CA  . ALA A 1 115 ? -9.969  -15.021 14.234  1.00 11.95  ? 115 ALA A CA  1 
ATOM   930  C  C   . ALA A 1 115 ? -9.553  -13.614 13.783  1.00 12.13  ? 115 ALA A C   1 
ATOM   931  O  O   . ALA A 1 115 ? -8.711  -13.488 12.857  1.00 13.24  ? 115 ALA A O   1 
ATOM   932  C  CB  . ALA A 1 115 ? -10.978 -15.639 13.308  1.00 14.75  ? 115 ALA A CB  1 
ATOM   933  N  N   . ALA A 1 116 ? -10.223 -12.572 14.278  1.00 11.98  ? 116 ALA A N   1 
ATOM   934  C  CA  . ALA A 1 116 ? -9.890  -11.230 13.809  1.00 11.75  ? 116 ALA A CA  1 
ATOM   935  C  C   . ALA A 1 116 ? -10.516 -10.288 14.823  1.00 11.10  ? 116 ALA A C   1 
ATOM   936  O  O   . ALA A 1 116 ? -11.219 -10.674 15.741  1.00 11.31  ? 116 ALA A O   1 
ATOM   937  C  CB  . ALA A 1 116 ? -10.457 -10.920 12.380  1.00 13.29  ? 116 ALA A CB  1 
ATOM   938  N  N   . GLU A 1 117 ? -10.143 -9.005  14.703  1.00 11.63  ? 117 GLU A N   1 
ATOM   939  C  CA  . GLU A 1 117 ? -10.691 -7.960  15.544  1.00 11.40  ? 117 GLU A CA  1 
ATOM   940  C  C   . GLU A 1 117 ? -10.894 -6.735  14.662  1.00 11.12  ? 117 GLU A C   1 
ATOM   941  O  O   . GLU A 1 117 ? -9.972  -6.344  13.929  1.00 13.08  ? 117 GLU A O   1 
ATOM   942  C  CB  . GLU A 1 117 ? -9.720  -7.674  16.686  1.00 12.16  ? 117 GLU A CB  1 
ATOM   943  C  CG  . GLU A 1 117 ? -10.273 -6.800  17.830  1.00 12.55  ? 117 GLU A CG  1 
ATOM   944  C  CD  . GLU A 1 117 ? -9.375  -6.748  19.063  1.00 12.40  ? 117 GLU A CD  1 
ATOM   945  O  OE1 . GLU A 1 117 ? -8.675  -7.738  19.342  1.00 13.38  ? 117 GLU A OE1 1 
ATOM   946  O  OE2 . GLU A 1 117 ? -9.381  -5.686  19.709  1.00 14.33  ? 117 GLU A OE2 1 
ATOM   947  N  N   . LEU A 1 118 ? -12.063 -6.146  14.808  1.00 10.67  ? 118 LEU A N   1 
ATOM   948  C  CA  . LEU A 1 118 ? -12.447 -4.908  14.130  1.00 11.37  ? 118 LEU A CA  1 
ATOM   949  C  C   . LEU A 1 118 ? -12.276 -3.760  15.119  1.00 10.13  ? 118 LEU A C   1 
ATOM   950  O  O   . LEU A 1 118 ? -12.687 -3.852  16.295  1.00 10.58  ? 118 LEU A O   1 
ATOM   951  C  CB  . LEU A 1 118 ? -13.936 -5.020  13.783  1.00 11.90  ? 118 LEU A CB  1 
ATOM   952  C  CG  . LEU A 1 118 ? -14.683 -3.707  13.464  1.00 12.08  ? 118 LEU A CG  1 
ATOM   953  C  CD1 . LEU A 1 118 ? -14.101 -3.069  12.205  1.00 12.54  ? 118 LEU A CD1 1 
ATOM   954  C  CD2 . LEU A 1 118 ? -16.159 -4.055  13.238  1.00 13.64  ? 118 LEU A CD2 1 
ATOM   955  N  N   . HIS A 1 119 ? -11.635 -2.692  14.672  1.00 10.29  ? 119 HIS A N   1 
ATOM   956  C  CA  . HIS A 1 119 ? -11.391 -1.496  15.482  1.00 10.67  ? 119 HIS A CA  1 
ATOM   957  C  C   . HIS A 1 119 ? -12.027 -0.285  14.797  1.00 9.85   ? 119 HIS A C   1 
ATOM   958  O  O   . HIS A 1 119 ? -11.616 0.019   13.645  1.00 11.24  ? 119 HIS A O   1 
ATOM   959  C  CB  . HIS A 1 119 ? -9.884  -1.260  15.568  1.00 11.22  ? 119 HIS A CB  1 
ATOM   960  C  CG  . HIS A 1 119 ? -9.277  -2.288  16.472  1.00 10.90  ? 119 HIS A CG  1 
ATOM   961  N  ND1 . HIS A 1 119 ? -7.933  -2.516  16.480  1.00 11.36  ? 119 HIS A ND1 1 
ATOM   962  C  CD2 . HIS A 1 119 ? -9.823  -3.049  17.464  1.00 11.61  ? 119 HIS A CD2 1 
ATOM   963  C  CE1 . HIS A 1 119 ? -7.633  -3.435  17.363  1.00 10.82  ? 119 HIS A CE1 1 
ATOM   964  N  NE2 . HIS A 1 119 ? -8.787  -3.789  17.994  1.00 11.99  ? 119 HIS A NE2 1 
ATOM   965  N  N   . LEU A 1 120 ? -12.986 0.310   15.457  1.00 10.41  ? 120 LEU A N   1 
ATOM   966  C  CA  . LEU A 1 120 ? -13.596 1.545   14.996  1.00 11.49  ? 120 LEU A CA  1 
ATOM   967  C  C   . LEU A 1 120 ? -12.970 2.698   15.774  1.00 10.16  ? 120 LEU A C   1 
ATOM   968  O  O   . LEU A 1 120 ? -13.085 2.717   17.004  1.00 10.79  ? 120 LEU A O   1 
ATOM   969  C  CB  . LEU A 1 120 ? -15.095 1.464   15.200  1.00 12.30  ? 120 LEU A CB  1 
ATOM   970  C  CG  . LEU A 1 120 ? -15.774 0.424   14.305  1.00 13.23  ? 120 LEU A CG  1 
ATOM   971  C  CD1 . LEU A 1 120 ? -16.547 -0.559  15.172  1.00 18.09  ? 120 LEU A CD1 1 
ATOM   972  C  CD2 . LEU A 1 120 ? -16.665 1.123   13.285  1.00 16.31  ? 120 LEU A CD2 1 
ATOM   973  N  N   . VAL A 1 121 ? -12.213 3.541   15.101  1.00 11.33  ? 121 VAL A N   1 
ATOM   974  C  CA  . VAL A 1 121 ? -11.367 4.534   15.742  1.00 11.01  ? 121 VAL A CA  1 
ATOM   975  C  C   . VAL A 1 121 ? -12.067 5.885   15.760  1.00 11.40  ? 121 VAL A C   1 
ATOM   976  O  O   . VAL A 1 121 ? -12.496 6.347   14.697  1.00 13.16  ? 121 VAL A O   1 
ATOM   977  C  CB  . VAL A 1 121 ? -10.032 4.673   14.973  1.00 12.26  ? 121 VAL A CB  1 
ATOM   978  C  CG1 . VAL A 1 121 ? -9.130  5.715   15.666  1.00 13.17  ? 121 VAL A CG1 1 
ATOM   979  C  CG2 . VAL A 1 121 ? -9.322  3.334   14.828  1.00 13.17  ? 121 VAL A CG2 1 
ATOM   980  N  N   . HIS A 1 122 ? -12.221 6.466   16.963  1.00 11.68  ? 122 HIS A N   1 
ATOM   981  C  CA  . HIS A 1 122 ? -12.925 7.722   17.099  1.00 12.21  ? 122 HIS A CA  1 
ATOM   982  C  C   . HIS A 1 122 ? -12.031 8.707   17.859  1.00 12.15  ? 122 HIS A C   1 
ATOM   983  O  O   . HIS A 1 122 ? -11.215 8.312   18.687  1.00 12.89  ? 122 HIS A O   1 
ATOM   984  C  CB  . HIS A 1 122 ? -14.174 7.564   18.008  1.00 13.21  ? 122 HIS A CB  1 
ATOM   985  C  CG  . HIS A 1 122 ? -15.070 6.438   17.597  1.00 12.91  ? 122 HIS A CG  1 
ATOM   986  N  ND1 . HIS A 1 122 ? -14.754 5.118   17.789  1.00 13.73  ? 122 HIS A ND1 1 
ATOM   987  C  CD2 . HIS A 1 122 ? -16.278 6.407   16.988  1.00 14.05  ? 122 HIS A CD2 1 
ATOM   988  C  CE1 . HIS A 1 122 ? -15.731 4.346   17.340  1.00 14.65  ? 122 HIS A CE1 1 
ATOM   989  N  NE2 . HIS A 1 122 ? -16.684 5.117   16.855  1.00 13.84  ? 122 HIS A NE2 1 
ATOM   990  N  N   . TRP A 1 123 ? -12.209 10.006  17.620  1.00 12.45  ? 123 TRP A N   1 
ATOM   991  C  CA  . TRP A 1 123 ? -11.402 11.023  18.304  1.00 12.67  ? 123 TRP A CA  1 
ATOM   992  C  C   . TRP A 1 123 ? -12.305 11.990  19.028  1.00 12.77  ? 123 TRP A C   1 
ATOM   993  O  O   . TRP A 1 123 ? -13.396 12.354  18.592  1.00 15.13  ? 123 TRP A O   1 
ATOM   994  C  CB  . TRP A 1 123 ? -10.433 11.731  17.346  1.00 15.20  ? 123 TRP A CB  1 
ATOM   995  C  CG  . TRP A 1 123 ? -11.097 12.355  16.147  1.00 16.00  ? 123 TRP A CG  1 
ATOM   996  C  CD1 . TRP A 1 123 ? -11.368 11.724  14.968  1.00 18.75  ? 123 TRP A CD1 1 
ATOM   997  C  CD2 . TRP A 1 123 ? -11.562 13.694  16.009  1.00 16.40  ? 123 TRP A CD2 1 
ATOM   998  N  NE1 . TRP A 1 123 ? -11.986 12.572  14.104  1.00 19.11  ? 123 TRP A NE1 1 
ATOM   999  C  CE2 . TRP A 1 123 ? -12.061 13.812  14.691  1.00 17.21  ? 123 TRP A CE2 1 
ATOM   1000 C  CE3 . TRP A 1 123 ? -11.527 14.853  16.784  1.00 17.43  ? 123 TRP A CE3 1 
ATOM   1001 C  CZ2 . TRP A 1 123 ? -12.631 14.980  14.198  1.00 19.69  ? 123 TRP A CZ2 1 
ATOM   1002 C  CZ3 . TRP A 1 123 ? -12.065 16.012  16.301  1.00 19.86  ? 123 TRP A CZ3 1 
ATOM   1003 C  CH2 . TRP A 1 123 ? -12.539 16.101  14.985  1.00 20.37  ? 123 TRP A CH2 1 
ATOM   1004 N  N   . ASN A 1 124 ? -11.770 12.463  20.166  1.00 13.05  ? 124 ASN A N   1 
ATOM   1005 C  CA  . ASN A 1 124 ? -12.484 13.378  21.042  1.00 14.91  ? 124 ASN A CA  1 
ATOM   1006 C  C   . ASN A 1 124 ? -12.584 14.734  20.367  1.00 14.67  ? 124 ASN A C   1 
ATOM   1007 O  O   . ASN A 1 124 ? -11.571 15.381  20.133  1.00 15.05  ? 124 ASN A O   1 
ATOM   1008 C  CB  . ASN A 1 124 ? -11.660 13.476  22.328  1.00 16.39  ? 124 ASN A CB  1 
ATOM   1009 C  CG  . ASN A 1 124 ? -12.437 14.105  23.449  1.00 17.63  ? 124 ASN A CG  1 
ATOM   1010 O  OD1 . ASN A 1 124 ? -13.270 15.004  23.208  1.00 19.63  ? 124 ASN A OD1 1 
ATOM   1011 N  ND2 . ASN A 1 124 ? -12.172 13.629  24.666  1.00 20.06  ? 124 ASN A ND2 1 
ATOM   1012 N  N   . THR A 1 125 ? -13.824 15.202  20.164  1.00 17.24  ? 125 THR A N   1 
ATOM   1013 C  CA  . THR A 1 125 ? -14.005 16.459  19.427  1.00 17.31  ? 125 THR A CA  1 
ATOM   1014 C  C   . THR A 1 125 ? -13.420 17.660  20.160  1.00 17.84  ? 125 THR A C   1 
ATOM   1015 O  O   . THR A 1 125 ? -13.258 18.715  19.537  1.00 20.66  ? 125 THR A O   1 
ATOM   1016 C  CB  . THR A 1 125 ? -15.473 16.691  19.056  1.00 22.45  ? 125 THR A CB  1 
ATOM   1017 O  OG1 . THR A 1 125 ? -16.225 16.721  20.274  1.00 26.30  ? 125 THR A OG1 1 
ATOM   1018 C  CG2 . THR A 1 125 ? -15.963 15.571  18.157  1.00 24.20  ? 125 THR A CG2 1 
ATOM   1019 N  N   . LYS A 1 126 ? -13.231 17.519  21.550  1.00 18.08  ? 127 LYS A N   1 
ATOM   1020 C  CA  . LYS A 1 126 ? -12.646 18.717  22.231  1.00 20.91  ? 127 LYS A CA  1 
ATOM   1021 C  C   . LYS A 1 126 ? -11.243 19.016  21.695  1.00 17.81  ? 127 LYS A C   1 
ATOM   1022 O  O   . LYS A 1 126 ? -10.746 20.099  21.973  1.00 22.55  ? 127 LYS A O   1 
ATOM   1023 C  CB  . LYS A 1 126 ? -12.689 18.486  23.739  1.00 24.55  ? 127 LYS A CB  1 
ATOM   1024 C  CG  . LYS A 1 126 ? -11.636 17.588  24.344  1.00 23.22  ? 127 LYS A CG  1 
ATOM   1025 C  CD  . LYS A 1 126 ? -12.034 17.281  25.756  1.00 31.80  ? 127 LYS A CD  1 
ATOM   1026 C  CE  . LYS A 1 126 ? -11.070 16.455  26.563  1.00 40.94  ? 127 LYS A CE  1 
ATOM   1027 N  NZ  . LYS A 1 126 ? -10.504 17.265  27.671  1.00 49.62  ? 127 LYS A NZ  1 
ATOM   1028 N  N   . TYR A 1 127 ? -10.597 18.097  20.969  1.00 15.24  ? 128 TYR A N   1 
ATOM   1029 C  CA  . TYR A 1 127 ? -9.250  18.330  20.463  1.00 14.84  ? 128 TYR A CA  1 
ATOM   1030 C  C   . TYR A 1 127 ? -9.244  18.696  18.982  1.00 15.82  ? 128 TYR A C   1 
ATOM   1031 O  O   . TYR A 1 127 ? -8.171  18.884  18.419  1.00 18.15  ? 128 TYR A O   1 
ATOM   1032 C  CB  . TYR A 1 127 ? -8.297  17.158  20.705  1.00 15.24  ? 128 TYR A CB  1 
ATOM   1033 C  CG  . TYR A 1 127 ? -8.234  16.868  22.177  1.00 14.99  ? 128 TYR A CG  1 
ATOM   1034 C  CD1 . TYR A 1 127 ? -7.765  17.849  23.060  1.00 18.80  ? 128 TYR A CD1 1 
ATOM   1035 C  CD2 . TYR A 1 127 ? -8.530  15.609  22.687  1.00 16.27  ? 128 TYR A CD2 1 
ATOM   1036 C  CE1 . TYR A 1 127 ? -7.701  17.617  24.421  1.00 18.08  ? 128 TYR A CE1 1 
ATOM   1037 C  CE2 . TYR A 1 127 ? -8.454  15.366  24.056  1.00 16.67  ? 128 TYR A CE2 1 
ATOM   1038 C  CZ  . TYR A 1 127 ? -8.041  16.387  24.904  1.00 17.82  ? 128 TYR A CZ  1 
ATOM   1039 O  OH  . TYR A 1 127 ? -7.928  16.159  26.231  1.00 20.86  ? 128 TYR A OH  1 
ATOM   1040 N  N   . GLY A 1 128 ? -10.431 18.794  18.359  1.00 16.46  ? 129 GLY A N   1 
ATOM   1041 C  CA  . GLY A 1 128 ? -10.510 19.486  17.080  1.00 17.84  ? 129 GLY A CA  1 
ATOM   1042 C  C   . GLY A 1 128 ? -10.133 18.633  15.873  1.00 17.47  ? 129 GLY A C   1 
ATOM   1043 O  O   . GLY A 1 128 ? -10.744 18.778  14.824  1.00 19.54  ? 129 GLY A O   1 
ATOM   1044 N  N   . ASP A 1 129 ? -9.106  17.774  15.961  1.00 18.01  ? 130 ASP A N   1 
ATOM   1045 C  CA  . ASP A 1 129 ? -8.754  16.905  14.850  1.00 18.60  ? 130 ASP A CA  1 
ATOM   1046 C  C   . ASP A 1 129 ? -8.124  15.643  15.446  1.00 18.73  ? 130 ASP A C   1 
ATOM   1047 O  O   . ASP A 1 129 ? -7.655  15.656  16.587  1.00 18.24  ? 130 ASP A O   1 
ATOM   1048 C  CB  . ASP A 1 129 ? -7.825  17.595  13.828  1.00 22.61  ? 130 ASP A CB  1 
ATOM   1049 C  CG  . ASP A 1 129 ? -6.414  17.903  14.310  1.00 25.79  ? 130 ASP A CG  1 
ATOM   1050 O  OD1 . ASP A 1 129 ? -5.575  16.975  14.385  1.00 27.37  ? 130 ASP A OD1 1 
ATOM   1051 O  OD2 . ASP A 1 129 ? -6.103  19.112  14.562  1.00 28.89  ? 130 ASP A OD2 1 
ATOM   1052 N  N   . ALA A 1 130 ? -8.070  14.588  14.649  1.00 20.23  ? 131 ALA A N   1 
ATOM   1053 C  CA  . ALA A 1 130 ? -7.642  13.302  15.143  1.00 17.63  ? 131 ALA A CA  1 
ATOM   1054 C  C   . ALA A 1 130 ? -6.168  13.335  15.481  1.00 17.86  ? 131 ALA A C   1 
ATOM   1055 O  O   . ALA A 1 130 ? -5.747  12.611  16.392  1.00 17.74  ? 131 ALA A O   1 
ATOM   1056 C  CB  . ALA A 1 130 ? -7.943  12.242  14.122  1.00 20.54  ? 131 ALA A CB  1 
ATOM   1057 N  N   . GLY A 1 131 ? -5.376  14.087  14.701  1.00 20.81  ? 132 GLY A N   1 
ATOM   1058 C  CA  . GLY A 1 131 ? -3.937  14.142  14.961  1.00 21.27  ? 132 GLY A CA  1 
ATOM   1059 C  C   . GLY A 1 131 ? -3.666  14.735  16.336  1.00 18.60  ? 132 GLY A C   1 
ATOM   1060 O  O   . GLY A 1 131 ? -2.903  14.206  17.137  1.00 22.01  ? 132 GLY A O   1 
ATOM   1061 N  N   A LYS A 1 132 ? -4.306  15.868  16.629  0.50 19.59  ? 133 LYS A N   1 
ATOM   1062 N  N   B LYS A 1 132 ? -4.314  15.875  16.600  0.50 19.93  ? 133 LYS A N   1 
ATOM   1063 C  CA  A LYS A 1 132 ? -4.067  16.465  17.935  0.50 17.70  ? 133 LYS A CA  1 
ATOM   1064 C  CA  B LYS A 1 132 ? -4.178  16.529  17.894  0.50 19.15  ? 133 LYS A CA  1 
ATOM   1065 C  C   A LYS A 1 132 ? -4.637  15.575  19.040  0.50 15.12  ? 133 LYS A C   1 
ATOM   1066 C  C   B LYS A 1 132 ? -4.641  15.594  19.006  0.50 15.82  ? 133 LYS A C   1 
ATOM   1067 O  O   A LYS A 1 132 ? -4.084  15.483  20.133  0.50 17.35  ? 133 LYS A O   1 
ATOM   1068 O  O   B LYS A 1 132 ? -4.031  15.515  20.068  0.50 18.36  ? 133 LYS A O   1 
ATOM   1069 C  CB  A LYS A 1 132 ? -4.629  17.884  18.028  0.50 15.84  ? 133 LYS A CB  1 
ATOM   1070 C  CB  B LYS A 1 132 ? -5.062  17.772  17.979  0.50 22.30  ? 133 LYS A CB  1 
ATOM   1071 C  CG  A LYS A 1 132 ? -4.660  18.490  19.432  0.50 20.98  ? 133 LYS A CG  1 
ATOM   1072 C  CG  B LYS A 1 132 ? -4.359  19.102  17.784  0.50 27.88  ? 133 LYS A CG  1 
ATOM   1073 C  CD  A LYS A 1 132 ? -3.611  19.577  19.723  0.50 32.31  ? 133 LYS A CD  1 
ATOM   1074 C  CD  B LYS A 1 132 ? -3.368  19.032  16.691  0.50 30.75  ? 133 LYS A CD  1 
ATOM   1075 C  CE  A LYS A 1 132 ? -3.938  20.352  20.986  0.50 41.00  ? 133 LYS A CE  1 
ATOM   1076 C  CE  B LYS A 1 132 ? -3.636  20.200  15.774  0.50 22.41  ? 133 LYS A CE  1 
ATOM   1077 N  NZ  A LYS A 1 132 ? -2.936  21.452  21.295  0.50 50.53  ? 133 LYS A NZ  1 
ATOM   1078 N  NZ  B LYS A 1 132 ? -2.894  20.089  14.507  0.50 33.13  ? 133 LYS A NZ  1 
ATOM   1079 N  N   . ALA A 1 133 ? -5.776  14.923  18.753  1.00 14.15  ? 134 ALA A N   1 
ATOM   1080 C  CA  . ALA A 1 133 ? -6.371  14.048  19.748  1.00 13.75  ? 134 ALA A CA  1 
ATOM   1081 C  C   . ALA A 1 133 ? -5.381  12.931  20.090  1.00 14.03  ? 134 ALA A C   1 
ATOM   1082 O  O   . ALA A 1 133 ? -5.305  12.511  21.265  1.00 14.92  ? 134 ALA A O   1 
ATOM   1083 C  CB  . ALA A 1 133 ? -7.673  13.467  19.214  1.00 14.77  ? 134 ALA A CB  1 
ATOM   1084 N  N   . SER A 1 134 ? -4.622  12.466  19.113  1.00 15.23  ? 135 SER A N   1 
ATOM   1085 C  CA  . SER A 1 134 ? -3.748  11.313  19.386  1.00 16.14  ? 135 SER A CA  1 
ATOM   1086 C  C   . SER A 1 134 ? -2.596  11.688  20.329  1.00 15.65  ? 135 SER A C   1 
ATOM   1087 O  O   . SER A 1 134 ? -1.811  10.812  20.723  1.00 18.01  ? 135 SER A O   1 
ATOM   1088 C  CB  . SER A 1 134 ? -3.198  10.770  18.087  1.00 18.44  ? 135 SER A CB  1 
ATOM   1089 O  OG  . SER A 1 134 ? -2.196  11.603  17.479  1.00 22.00  ? 135 SER A OG  1 
ATOM   1090 N  N   . GLN A 1 135 ? -2.430  12.996  20.635  1.00 16.60  ? 136 GLN A N   1 
ATOM   1091 C  CA  . GLN A 1 135 ? -1.374  13.438  21.536  1.00 17.40  ? 136 GLN A CA  1 
ATOM   1092 C  C   . GLN A 1 135 ? -1.913  13.635  22.946  1.00 17.75  ? 136 GLN A C   1 
ATOM   1093 O  O   . GLN A 1 135 ? -1.195  14.148  23.793  1.00 22.71  ? 136 GLN A O   1 
ATOM   1094 C  CB  . GLN A 1 135 ? -0.779  14.781  21.057  1.00 22.71  ? 136 GLN A CB  1 
ATOM   1095 C  CG  . GLN A 1 135 ? -0.295  14.756  19.627  1.00 27.40  ? 136 GLN A CG  1 
ATOM   1096 C  CD  . GLN A 1 135 ? 0.634   13.617  19.312  1.00 36.79  ? 136 GLN A CD  1 
ATOM   1097 O  OE1 . GLN A 1 135 ? 1.598   13.353  20.036  1.00 56.39  ? 136 GLN A OE1 1 
ATOM   1098 N  NE2 . GLN A 1 135 ? 0.349   12.944  18.210  1.00 48.39  ? 136 GLN A NE2 1 
ATOM   1099 N  N   . GLN A 1 136 ? -3.164  13.236  23.207  1.00 14.89  ? 137 GLN A N   1 
ATOM   1100 C  CA  . GLN A 1 136 ? -3.773  13.482  24.484  1.00 14.59  ? 137 GLN A CA  1 
ATOM   1101 C  C   . GLN A 1 136 ? -4.097  12.165  25.138  1.00 15.67  ? 137 GLN A C   1 
ATOM   1102 O  O   . GLN A 1 136 ? -4.526  11.212  24.451  1.00 15.07  ? 137 GLN A O   1 
ATOM   1103 C  CB  . GLN A 1 136 ? -5.064  14.281  24.315  1.00 16.37  ? 137 GLN A CB  1 
ATOM   1104 C  CG  . GLN A 1 136 ? -4.911  15.517  23.440  1.00 19.23  ? 137 GLN A CG  1 
ATOM   1105 C  CD  . GLN A 1 136 ? -3.883  16.454  23.985  1.00 23.91  ? 137 GLN A CD  1 
ATOM   1106 O  OE1 . GLN A 1 136 ? -3.698  16.558  25.199  1.00 24.15  ? 137 GLN A OE1 1 
ATOM   1107 N  NE2 . GLN A 1 136 ? -3.214  17.146  23.077  1.00 31.66  ? 137 GLN A NE2 1 
ATOM   1108 N  N   . PRO A 1 137 ? -4.102  12.110  26.492  1.00 15.46  ? 138 PRO A N   1 
ATOM   1109 C  CA  . PRO A 1 137 ? -4.333  10.821  27.129  1.00 16.59  ? 138 PRO A CA  1 
ATOM   1110 C  C   . PRO A 1 137 ? -5.756  10.299  26.947  1.00 16.63  ? 138 PRO A C   1 
ATOM   1111 O  O   . PRO A 1 137 ? -5.954  9.107   27.110  1.00 21.61  ? 138 PRO A O   1 
ATOM   1112 C  CB  . PRO A 1 137 ? -3.999  11.090  28.601  1.00 20.57  ? 138 PRO A CB  1 
ATOM   1113 C  CG  . PRO A 1 137 ? -4.048  12.616  28.732  1.00 28.21  ? 138 PRO A CG  1 
ATOM   1114 C  CD  . PRO A 1 137 ? -3.657  13.199  27.399  1.00 19.81  ? 138 PRO A CD  1 
ATOM   1115 N  N   . ASP A 1 138 ? -6.719  11.203  26.686  1.00 15.55  ? 139 ASP A N   1 
ATOM   1116 C  CA  . ASP A 1 138 ? -8.130  10.867  26.458  1.00 17.18  ? 139 ASP A CA  1 
ATOM   1117 C  C   . ASP A 1 138 ? -8.521  11.270  25.023  1.00 15.74  ? 139 ASP A C   1 
ATOM   1118 O  O   . ASP A 1 138 ? -9.650  11.716  24.784  1.00 17.17  ? 139 ASP A O   1 
ATOM   1119 C  CB  . ASP A 1 138 ? -9.040  11.584  27.477  1.00 20.01  ? 139 ASP A CB  1 
ATOM   1120 C  CG  . ASP A 1 138 ? -8.953  13.090  27.422  1.00 24.14  ? 139 ASP A CG  1 
ATOM   1121 O  OD1 . ASP A 1 138 ? -7.912  13.626  26.896  1.00 21.67  ? 139 ASP A OD1 1 
ATOM   1122 O  OD2 . ASP A 1 138 ? -9.825  13.722  28.098  1.00 26.75  ? 139 ASP A OD2 1 
ATOM   1123 N  N   . GLY A 1 139 ? -7.600  11.176  24.092  1.00 13.15  ? 140 GLY A N   1 
ATOM   1124 C  CA  . GLY A 1 139 ? -7.842  11.677  22.751  1.00 13.58  ? 140 GLY A CA  1 
ATOM   1125 C  C   . GLY A 1 139 ? -8.702  10.765  21.876  1.00 11.07  ? 140 GLY A C   1 
ATOM   1126 O  O   . GLY A 1 139 ? -9.419  11.270  21.031  1.00 13.27  ? 140 GLY A O   1 
ATOM   1127 N  N   . LEU A 1 140 ? -8.477  9.461   21.998  1.00 11.75  ? 141 LEU A N   1 
ATOM   1128 C  CA  . LEU A 1 140 ? -9.118  8.526   21.095  1.00 11.49  ? 141 LEU A CA  1 
ATOM   1129 C  C   . LEU A 1 140 ? -9.944  7.538   21.857  1.00 11.82  ? 141 LEU A C   1 
ATOM   1130 O  O   . LEU A 1 140 ? -9.656  7.262   23.021  1.00 12.09  ? 141 LEU A O   1 
ATOM   1131 C  CB  . LEU A 1 140 ? -8.108  7.755   20.245  1.00 12.98  ? 141 LEU A CB  1 
ATOM   1132 C  CG  . LEU A 1 140 ? -7.158  8.563   19.372  1.00 17.14  ? 141 LEU A CG  1 
ATOM   1133 C  CD1 . LEU A 1 140 ? -6.330  7.592   18.518  1.00 17.54  ? 141 LEU A CD1 1 
ATOM   1134 C  CD2 . LEU A 1 140 ? -7.869  9.561   18.496  1.00 18.88  ? 141 LEU A CD2 1 
ATOM   1135 N  N   . ALA A 1 141 ? -10.988 7.009   21.253  1.00 11.61  ? 142 ALA A N   1 
ATOM   1136 C  CA  . ALA A 1 141 ? -11.748 5.880   21.764  1.00 12.57  ? 142 ALA A CA  1 
ATOM   1137 C  C   . ALA A 1 141 ? -11.851 4.884   20.659  1.00 10.54  ? 142 ALA A C   1 
ATOM   1138 O  O   . ALA A 1 141 ? -12.270 5.219   19.548  1.00 12.71  ? 142 ALA A O   1 
ATOM   1139 C  CB  . ALA A 1 141 ? -13.113 6.335   22.236  1.00 14.19  ? 142 ALA A CB  1 
ATOM   1140 N  N   . VAL A 1 142 ? -11.366 3.667   20.890  1.00 10.91  ? 143 VAL A N   1 
ATOM   1141 C  CA  . VAL A 1 142 ? -11.416 2.619   19.882  1.00 11.48  ? 143 VAL A CA  1 
ATOM   1142 C  C   . VAL A 1 142 ? -12.377 1.568   20.359  1.00 11.04  ? 143 VAL A C   1 
ATOM   1143 O  O   . VAL A 1 142 ? -12.266 1.085   21.495  1.00 11.65  ? 143 VAL A O   1 
ATOM   1144 C  CB  . VAL A 1 142 ? -10.054 2.020   19.554  1.00 11.01  ? 143 VAL A CB  1 
ATOM   1145 C  CG1 . VAL A 1 142 ? -10.229 1.009   18.410  1.00 12.48  ? 143 VAL A CG1 1 
ATOM   1146 C  CG2 . VAL A 1 142 ? -9.122  3.134   19.126  1.00 12.46  ? 143 VAL A CG2 1 
ATOM   1147 N  N   . LEU A 1 143 ? -13.434 1.341   19.578  1.00 11.46  ? 144 LEU A N   1 
ATOM   1148 C  CA  . LEU A 1 143 ? -14.411 0.306   19.850  1.00 11.28  ? 144 LEU A CA  1 
ATOM   1149 C  C   . LEU A 1 143 ? -13.921 -0.957  19.165  1.00 9.92   ? 144 LEU A C   1 
ATOM   1150 O  O   . LEU A 1 143 ? -13.720 -0.984  17.947  1.00 11.63  ? 144 LEU A O   1 
ATOM   1151 C  CB  . LEU A 1 143 ? -15.744 0.797   19.267  1.00 12.90  ? 144 LEU A CB  1 
ATOM   1152 C  CG  . LEU A 1 143 ? -16.909 -0.170  19.402  1.00 13.89  ? 144 LEU A CG  1 
ATOM   1153 C  CD1 . LEU A 1 143 ? -17.180 -0.454  20.845  1.00 16.39  ? 144 LEU A CD1 1 
ATOM   1154 C  CD2 . LEU A 1 143 ? -18.154 0.386   18.722  1.00 16.26  ? 144 LEU A CD2 1 
ATOM   1155 N  N   . GLY A 1 144 ? -13.649 -2.011  19.940  1.00 12.13  ? 145 GLY A N   1 
ATOM   1156 C  CA  . GLY A 1 144 ? -13.123 -3.260  19.432  1.00 10.72  ? 145 GLY A CA  1 
ATOM   1157 C  C   . GLY A 1 144 ? -14.193 -4.329  19.438  1.00 10.34  ? 145 GLY A C   1 
ATOM   1158 O  O   . GLY A 1 144 ? -14.874 -4.465  20.422  1.00 11.65  ? 145 GLY A O   1 
ATOM   1159 N  N   . ILE A 1 145 ? -14.232 -5.064  18.342  1.00 11.22  ? 146 ILE A N   1 
ATOM   1160 C  CA  . ILE A 1 145 ? -15.222 -6.105  18.168  1.00 11.22  ? 146 ILE A CA  1 
ATOM   1161 C  C   . ILE A 1 145 ? -14.480 -7.340  17.692  1.00 11.13  ? 146 ILE A C   1 
ATOM   1162 O  O   . ILE A 1 145 ? -13.792 -7.315  16.678  1.00 11.46  ? 146 ILE A O   1 
ATOM   1163 C  CB  . ILE A 1 145 ? -16.315 -5.652  17.182  1.00 12.44  ? 146 ILE A CB  1 
ATOM   1164 C  CG1 . ILE A 1 145 ? -17.000 -4.377  17.687  1.00 14.45  ? 146 ILE A CG1 1 
ATOM   1165 C  CG2 . ILE A 1 145 ? -17.313 -6.766  16.943  1.00 15.63  ? 146 ILE A CG2 1 
ATOM   1166 C  CD1 . ILE A 1 145 ? -17.994 -3.740  16.770  1.00 14.58  ? 146 ILE A CD1 1 
ATOM   1167 N  N   . PHE A 1 146 ? -14.725 -8.465  18.368  1.00 11.37  ? 147 PHE A N   1 
ATOM   1168 C  CA  . PHE A 1 146 ? -14.077 -9.707  17.962  1.00 11.35  ? 147 PHE A CA  1 
ATOM   1169 C  C   . PHE A 1 146 ? -14.865 -10.350 16.831  1.00 11.91  ? 147 PHE A C   1 
ATOM   1170 O  O   . PHE A 1 146 ? -16.092 -10.238 16.761  1.00 12.93  ? 147 PHE A O   1 
ATOM   1171 C  CB  . PHE A 1 146 ? -14.122 -10.690 19.152  1.00 11.59  ? 147 PHE A CB  1 
ATOM   1172 C  CG  . PHE A 1 146 ? -13.276 -10.187 20.289  1.00 10.98  ? 147 PHE A CG  1 
ATOM   1173 C  CD1 . PHE A 1 146 ? -11.890 -10.082 20.107  1.00 12.41  ? 147 PHE A CD1 1 
ATOM   1174 C  CD2 . PHE A 1 146 ? -13.808 -9.948  21.553  1.00 11.82  ? 147 PHE A CD2 1 
ATOM   1175 C  CE1 . PHE A 1 146 ? -11.089 -9.646  21.160  1.00 11.67  ? 147 PHE A CE1 1 
ATOM   1176 C  CE2 . PHE A 1 146 ? -12.992 -9.537  22.602  1.00 13.00  ? 147 PHE A CE2 1 
ATOM   1177 C  CZ  . PHE A 1 146 ? -11.635 -9.425  22.411  1.00 12.14  ? 147 PHE A CZ  1 
ATOM   1178 N  N   . LEU A 1 147 ? -14.133 -11.020 15.962  1.00 11.65  ? 148 LEU A N   1 
ATOM   1179 C  CA  . LEU A 1 147 ? -14.739 -11.828 14.896  1.00 11.24  ? 148 LEU A CA  1 
ATOM   1180 C  C   . LEU A 1 147 ? -14.411 -13.290 15.149  1.00 11.52  ? 148 LEU A C   1 
ATOM   1181 O  O   . LEU A 1 147 ? -13.246 -13.660 15.308  1.00 13.15  ? 148 LEU A O   1 
ATOM   1182 C  CB  . LEU A 1 147 ? -14.149 -11.448 13.522  1.00 12.25  ? 148 LEU A CB  1 
ATOM   1183 C  CG  . LEU A 1 147 ? -14.721 -10.191 12.863  1.00 12.30  ? 148 LEU A CG  1 
ATOM   1184 C  CD1 . LEU A 1 147 ? -14.503 -8.916  13.703  1.00 14.68  ? 148 LEU A CD1 1 
ATOM   1185 C  CD2 . LEU A 1 147 ? -14.117 -9.971  11.469  1.00 13.56  ? 148 LEU A CD2 1 
ATOM   1186 N  N   . LYS A 1 148 ? -15.475 -14.137 15.117  1.00 13.48  ? 149 LYS A N   1 
ATOM   1187 C  CA  . LYS A 1 148 ? -15.293 -15.564 15.107  1.00 13.26  ? 149 LYS A CA  1 
ATOM   1188 C  C   . LYS A 1 148 ? -15.808 -16.086 13.776  1.00 13.64  ? 149 LYS A C   1 
ATOM   1189 O  O   . LYS A 1 148 ? -16.645 -15.469 13.158  1.00 15.56  ? 149 LYS A O   1 
ATOM   1190 C  CB  . LYS A 1 148 ? -16.044 -16.222 16.256  1.00 17.03  ? 149 LYS A CB  1 
ATOM   1191 C  CG  . LYS A 1 148 ? -17.554 -16.013 16.248  1.00 18.76  ? 149 LYS A CG  1 
ATOM   1192 C  CD  . LYS A 1 148 ? -18.180 -16.777 17.442  1.00 26.04  ? 149 LYS A CD  1 
ATOM   1193 C  CE  . LYS A 1 148 ? -19.691 -16.815 17.318  1.00 34.16  ? 149 LYS A CE  1 
ATOM   1194 N  NZ  . LYS A 1 148 ? -20.278 -17.525 18.483  1.00 47.83  ? 149 LYS A NZ  1 
ATOM   1195 N  N   . VAL A 1 149 ? -15.305 -17.241 13.411  1.00 15.21  ? 150 VAL A N   1 
ATOM   1196 C  CA  . VAL A 1 149 ? -15.686 -17.816 12.141  1.00 15.33  ? 150 VAL A CA  1 
ATOM   1197 C  C   . VAL A 1 149 ? -16.889 -18.734 12.354  1.00 17.13  ? 150 VAL A C   1 
ATOM   1198 O  O   . VAL A 1 149 ? -16.853 -19.688 13.153  1.00 18.40  ? 150 VAL A O   1 
ATOM   1199 C  CB  . VAL A 1 149 ? -14.501 -18.555 11.487  1.00 16.79  ? 150 VAL A CB  1 
ATOM   1200 C  CG1 . VAL A 1 149 ? -14.939 -19.310 10.233  1.00 18.16  ? 150 VAL A CG1 1 
ATOM   1201 C  CG2 . VAL A 1 149 ? -13.422 -17.543 11.141  1.00 20.73  ? 150 VAL A CG2 1 
ATOM   1202 N  N   . GLY A 1 150 ? -17.950 -18.493 11.592  1.00 15.40  ? 151 GLY A N   1 
ATOM   1203 C  CA  . GLY A 1 150 ? -19.159 -19.316 11.632  1.00 17.03  ? 151 GLY A CA  1 
ATOM   1204 C  C   . GLY A 1 150 ? -20.056 -18.870 10.500  1.00 16.68  ? 151 GLY A C   1 
ATOM   1205 O  O   . GLY A 1 150 ? -19.658 -18.961 9.339   1.00 16.68  ? 151 GLY A O   1 
ATOM   1206 N  N   A SER A 1 151 ? -21.237 -18.345 10.825  0.50 17.41  ? 152 SER A N   1 
ATOM   1207 N  N   B SER A 1 151 ? -21.221 -18.297 10.849  0.50 18.02  ? 152 SER A N   1 
ATOM   1208 C  CA  A SER A 1 151 ? -22.048 -17.826 9.731   0.50 17.46  ? 152 SER A CA  1 
ATOM   1209 C  CA  B SER A 1 151 ? -22.160 -17.733 9.876   0.50 18.29  ? 152 SER A CA  1 
ATOM   1210 C  C   A SER A 1 151 ? -21.448 -16.531 9.176   0.50 17.21  ? 152 SER A C   1 
ATOM   1211 C  C   B SER A 1 151 ? -21.633 -16.427 9.271   0.50 16.36  ? 152 SER A C   1 
ATOM   1212 O  O   A SER A 1 151 ? -20.629 -15.858 9.816   0.50 15.61  ? 152 SER A O   1 
ATOM   1213 O  O   B SER A 1 151 ? -20.993 -15.643 9.979   0.50 16.34  ? 152 SER A O   1 
ATOM   1214 C  CB  A SER A 1 151 ? -23.470 -17.632 10.145  0.50 21.82  ? 152 SER A CB  1 
ATOM   1215 C  CB  B SER A 1 151 ? -23.468 -17.456 10.531  0.50 20.26  ? 152 SER A CB  1 
ATOM   1216 O  OG  A SER A 1 151 ? -23.515 -16.926 11.365  0.50 26.68  ? 152 SER A OG  1 
ATOM   1217 O  OG  B SER A 1 151 ? -24.085 -18.652 10.956  0.50 23.71  ? 152 SER A OG  1 
ATOM   1218 N  N   . ALA A 1 152 ? -21.865 -16.173 7.960   1.00 16.68  ? 153 ALA A N   1 
ATOM   1219 C  CA  . ALA A 1 152 ? -21.460 -14.916 7.345   1.00 16.53  ? 153 ALA A CA  1 
ATOM   1220 C  C   . ALA A 1 152 ? -22.080 -13.707 8.035   1.00 15.72  ? 153 ALA A C   1 
ATOM   1221 O  O   . ALA A 1 152 ? -23.184 -13.761 8.565   1.00 16.97  ? 153 ALA A O   1 
ATOM   1222 C  CB  . ALA A 1 152 ? -21.819 -14.906 5.870   1.00 18.07  ? 153 ALA A CB  1 
ATOM   1223 N  N   . LYS A 1 153 ? -21.372 -12.584 7.954   1.00 15.38  ? 154 LYS A N   1 
ATOM   1224 C  CA  . LYS A 1 153 ? -21.916 -11.319 8.431   1.00 14.97  ? 154 LYS A CA  1 
ATOM   1225 C  C   . LYS A 1 153 ? -22.309 -10.532 7.178   1.00 14.68  ? 154 LYS A C   1 
ATOM   1226 O  O   . LYS A 1 153 ? -21.467 -10.084 6.406   1.00 13.93  ? 154 LYS A O   1 
ATOM   1227 C  CB  . LYS A 1 153 ? -20.806 -10.560 9.171   1.00 14.34  ? 154 LYS A CB  1 
ATOM   1228 C  CG  . LYS A 1 153 ? -21.339 -9.303  9.891   1.00 15.60  ? 154 LYS A CG  1 
ATOM   1229 C  CD  . LYS A 1 153 ? -22.242 -9.628  11.065  1.00 17.83  ? 154 LYS A CD  1 
ATOM   1230 C  CE  . LYS A 1 153 ? -22.395 -8.441  12.020  1.00 20.84  ? 154 LYS A CE  1 
ATOM   1231 N  NZ  . LYS A 1 153 ? -23.357 -8.780  13.095  1.00 26.97  ? 154 LYS A NZ  1 
ATOM   1232 N  N   . PRO A 1 154 ? -23.616 -10.373 6.897   1.00 15.49  ? 155 PRO A N   1 
ATOM   1233 C  CA  . PRO A 1 154 ? -23.981 -9.711  5.629   1.00 16.82  ? 155 PRO A CA  1 
ATOM   1234 C  C   . PRO A 1 154 ? -23.397 -8.315  5.487   1.00 14.64  ? 155 PRO A C   1 
ATOM   1235 O  O   . PRO A 1 154 ? -22.964 -7.916  4.409   1.00 16.57  ? 155 PRO A O   1 
ATOM   1236 C  CB  . PRO A 1 154 ? -25.508 -9.725  5.661   1.00 19.20  ? 155 PRO A CB  1 
ATOM   1237 C  CG  . PRO A 1 154 ? -25.861 -10.890 6.584   1.00 24.11  ? 155 PRO A CG  1 
ATOM   1238 C  CD  . PRO A 1 154 ? -24.763 -10.947 7.647   1.00 16.94  ? 155 PRO A CD  1 
ATOM   1239 N  N   . GLY A 1 155 ? -23.341 -7.601  6.606   1.00 15.74  ? 156 GLY A N   1 
ATOM   1240 C  CA  . GLY A 1 155 ? -22.858 -6.231  6.583   1.00 17.27  ? 156 GLY A CA  1 
ATOM   1241 C  C   . GLY A 1 155 ? -21.369 -6.097  6.327   1.00 16.11  ? 156 GLY A C   1 
ATOM   1242 O  O   . GLY A 1 155 ? -20.915 -4.980  6.127   1.00 19.16  ? 156 GLY A O   1 
ATOM   1243 N  N   . LEU A 1 156 ? -20.631 -7.203  6.362   1.00 14.71  ? 157 LEU A N   1 
ATOM   1244 C  CA  . LEU A 1 156 ? -19.222 -7.197  6.019   1.00 15.67  ? 157 LEU A CA  1 
ATOM   1245 C  C   . LEU A 1 156 ? -18.999 -7.421  4.521   1.00 13.63  ? 157 LEU A C   1 
ATOM   1246 O  O   . LEU A 1 156 ? -17.917 -7.170  4.016   1.00 15.41  ? 157 LEU A O   1 
ATOM   1247 C  CB  . LEU A 1 156 ? -18.501 -8.254  6.844   1.00 15.39  ? 157 LEU A CB  1 
ATOM   1248 C  CG  . LEU A 1 156 ? -16.994 -8.374  6.658   1.00 15.56  ? 157 LEU A CG  1 
ATOM   1249 C  CD1 . LEU A 1 156 ? -16.226 -7.078  7.012   1.00 16.55  ? 157 LEU A CD1 1 
ATOM   1250 C  CD2 . LEU A 1 156 ? -16.507 -9.518  7.538   1.00 17.31  ? 157 LEU A CD2 1 
ATOM   1251 N  N   . GLN A 1 157 ? -20.011 -7.969  3.796   1.00 14.29  ? 158 GLN A N   1 
ATOM   1252 C  CA  . GLN A 1 157 ? -19.716 -8.445  2.457   1.00 14.70  ? 158 GLN A CA  1 
ATOM   1253 C  C   . GLN A 1 157 ? -19.285 -7.333  1.515   1.00 14.91  ? 158 GLN A C   1 
ATOM   1254 O  O   . GLN A 1 157 ? -18.457 -7.553  0.664   1.00 15.45  ? 158 GLN A O   1 
ATOM   1255 C  CB  . GLN A 1 157 ? -20.909 -9.226  1.901   1.00 17.25  ? 158 GLN A CB  1 
ATOM   1256 C  CG  . GLN A 1 157 ? -20.559 -10.008 0.644   1.00 17.49  ? 158 GLN A CG  1 
ATOM   1257 C  CD  . GLN A 1 157 ? -19.479 -11.032 0.859   1.00 17.43  ? 158 GLN A CD  1 
ATOM   1258 O  OE1 . GLN A 1 157 ? -19.317 -11.577 1.965   1.00 18.11  ? 158 GLN A OE1 1 
ATOM   1259 N  NE2 . GLN A 1 157 ? -18.716 -11.303 -0.190  1.00 20.02  ? 158 GLN A NE2 1 
ATOM   1260 N  N   . LYS A 1 158 ? -19.845 -6.130  1.637   1.00 15.17  ? 159 LYS A N   1 
ATOM   1261 C  CA  . LYS A 1 158 ? -19.424 -5.056  0.752   1.00 16.04  ? 159 LYS A CA  1 
ATOM   1262 C  C   . LYS A 1 158 ? -17.926 -4.775  0.910   1.00 16.24  ? 159 LYS A C   1 
ATOM   1263 O  O   . LYS A 1 158 ? -17.254 -4.413  -0.034  1.00 16.68  ? 159 LYS A O   1 
ATOM   1264 C  CB  . LYS A 1 158 ? -20.267 -3.798  0.995   1.00 20.54  ? 159 LYS A CB  1 
ATOM   1265 C  CG  . LYS A 1 158 ? -20.005 -2.600  0.101   1.00 28.37  ? 159 LYS A CG  1 
ATOM   1266 C  CD  . LYS A 1 158 ? -21.006 -1.418  0.369   1.00 31.75  ? 159 LYS A CD  1 
ATOM   1267 C  CE  . LYS A 1 158 ? -20.635 -0.084  -0.256  1.00 43.51  ? 159 LYS A CE  1 
ATOM   1268 N  NZ  . LYS A 1 158 ? -20.862 -0.119  -1.728  1.00 49.80  ? 159 LYS A NZ  1 
ATOM   1269 N  N   . VAL A 1 159 ? -17.398 -4.923  2.122   1.00 15.67  ? 160 VAL A N   1 
ATOM   1270 C  CA  . VAL A 1 159 ? -15.977 -4.729  2.352   1.00 14.56  ? 160 VAL A CA  1 
ATOM   1271 C  C   . VAL A 1 159 ? -15.216 -5.844  1.654   1.00 16.55  ? 160 VAL A C   1 
ATOM   1272 O  O   . VAL A 1 159 ? -14.274 -5.577  0.930   1.00 16.88  ? 160 VAL A O   1 
ATOM   1273 C  CB  . VAL A 1 159 ? -15.675 -4.742  3.858   1.00 15.94  ? 160 VAL A CB  1 
ATOM   1274 C  CG1 . VAL A 1 159 ? -14.162 -4.803  4.102   1.00 18.38  ? 160 VAL A CG1 1 
ATOM   1275 C  CG2 . VAL A 1 159 ? -16.260 -3.490  4.464   1.00 20.21  ? 160 VAL A CG2 1 
ATOM   1276 N  N   . VAL A 1 160 ? -15.591 -7.090  1.937   1.00 14.78  ? 161 VAL A N   1 
ATOM   1277 C  CA  . VAL A 1 160 ? -14.876 -8.245  1.394   1.00 18.19  ? 161 VAL A CA  1 
ATOM   1278 C  C   . VAL A 1 160 ? -14.820 -8.164  -0.133  1.00 16.07  ? 161 VAL A C   1 
ATOM   1279 O  O   . VAL A 1 160 ? -13.789 -8.453  -0.737  1.00 17.32  ? 161 VAL A O   1 
ATOM   1280 C  CB  . VAL A 1 160 ? -15.502 -9.582  1.919   1.00 22.82  ? 161 VAL A CB  1 
ATOM   1281 C  CG1 . VAL A 1 160 ? -15.285 -10.834 1.035   1.00 25.36  ? 161 VAL A CG1 1 
ATOM   1282 C  CG2 . VAL A 1 160 ? -15.089 -9.717  3.377   1.00 27.56  ? 161 VAL A CG2 1 
ATOM   1283 N  N   . ASP A 1 161 ? -15.927 -7.752  -0.743  1.00 15.71  ? 162 ASP A N   1 
ATOM   1284 C  CA  . ASP A 1 161 ? -15.966 -7.795  -2.200  1.00 17.27  ? 162 ASP A CA  1 
ATOM   1285 C  C   . ASP A 1 161 ? -15.106 -6.736  -2.880  1.00 18.77  ? 162 ASP A C   1 
ATOM   1286 O  O   . ASP A 1 161 ? -14.857 -6.888  -4.081  1.00 22.70  ? 162 ASP A O   1 
ATOM   1287 C  CB  . ASP A 1 161 ? -17.412 -7.623  -2.598  1.00 19.90  ? 162 ASP A CB  1 
ATOM   1288 C  CG  . ASP A 1 161 ? -18.099 -8.975  -2.596  1.00 24.17  ? 162 ASP A CG  1 
ATOM   1289 O  OD1 . ASP A 1 161 ? -17.391 -10.024 -2.700  1.00 28.57  ? 162 ASP A OD1 1 
ATOM   1290 O  OD2 . ASP A 1 161 ? -19.328 -8.981  -2.465  1.00 28.62  ? 162 ASP A OD2 1 
ATOM   1291 N  N   . VAL A 1 162 ? -14.660 -5.690  -2.186  1.00 17.35  ? 163 VAL A N   1 
ATOM   1292 C  CA  . VAL A 1 162 ? -13.827 -4.689  -2.816  1.00 20.03  ? 163 VAL A CA  1 
ATOM   1293 C  C   . VAL A 1 162 ? -12.347 -4.984  -2.574  1.00 18.55  ? 163 VAL A C   1 
ATOM   1294 O  O   . VAL A 1 162 ? -11.488 -4.286  -3.121  1.00 19.45  ? 163 VAL A O   1 
ATOM   1295 C  CB  . VAL A 1 162 ? -14.213 -3.278  -2.292  1.00 22.56  ? 163 VAL A CB  1 
ATOM   1296 C  CG1 . VAL A 1 162 ? -13.650 -2.928  -0.916  1.00 23.87  ? 163 VAL A CG1 1 
ATOM   1297 C  CG2 . VAL A 1 162 ? -13.885 -2.139  -3.220  1.00 31.37  ? 163 VAL A CG2 1 
ATOM   1298 N  N   . LEU A 1 163 ? -11.994 -5.952  -1.697  1.00 16.62  ? 164 LEU A N   1 
ATOM   1299 C  CA  . LEU A 1 163 ? -10.591 -6.109  -1.339  1.00 16.61  ? 164 LEU A CA  1 
ATOM   1300 C  C   . LEU A 1 163 ? -9.684  -6.463  -2.522  1.00 15.95  ? 164 LEU A C   1 
ATOM   1301 O  O   . LEU A 1 163 ? -8.501  -6.077  -2.508  1.00 18.72  ? 164 LEU A O   1 
ATOM   1302 C  CB  . LEU A 1 163 ? -10.480 -7.128  -0.221  1.00 16.34  ? 164 LEU A CB  1 
ATOM   1303 C  CG  . LEU A 1 163 ? -11.138 -6.740  1.111   1.00 15.53  ? 164 LEU A CG  1 
ATOM   1304 C  CD1 . LEU A 1 163 ? -10.825 -7.843  2.125   1.00 18.79  ? 164 LEU A CD1 1 
ATOM   1305 C  CD2 . LEU A 1 163 ? -10.557 -5.422  1.600   1.00 16.52  ? 164 LEU A CD2 1 
ATOM   1306 N  N   . ASP A 1 164 ? -10.170 -7.212  -3.529  1.00 19.48  ? 165 ASP A N   1 
ATOM   1307 C  CA  . ASP A 1 164 ? -9.395  -7.530  -4.733  1.00 22.38  ? 165 ASP A CA  1 
ATOM   1308 C  C   . ASP A 1 164 ? -8.914  -6.254  -5.441  1.00 24.34  ? 165 ASP A C   1 
ATOM   1309 O  O   . ASP A 1 164 ? -7.913  -6.292  -6.142  1.00 30.51  ? 165 ASP A O   1 
ATOM   1310 C  CB  . ASP A 1 164 ? -10.128 -8.430  -5.745  1.00 28.87  ? 165 ASP A CB  1 
ATOM   1311 C  CG  . ASP A 1 164 ? -11.159 -7.592  -6.486  1.00 39.63  ? 165 ASP A CG  1 
ATOM   1312 O  OD1 . ASP A 1 164 ? -12.093 -7.085  -5.792  1.00 39.06  ? 165 ASP A OD1 1 
ATOM   1313 O  OD2 . ASP A 1 164 ? -10.978 -7.353  -7.720  1.00 52.34  ? 165 ASP A OD2 1 
ATOM   1314 N  N   . SER A 1 165 ? -9.598  -5.126  -5.243  1.00 19.18  ? 166 SER A N   1 
ATOM   1315 C  CA  . SER A 1 165 ? -9.184  -3.888  -5.897  1.00 22.01  ? 166 SER A CA  1 
ATOM   1316 C  C   . SER A 1 165 ? -8.115  -3.101  -5.119  1.00 20.57  ? 166 SER A C   1 
ATOM   1317 O  O   . SER A 1 165 ? -7.588  -2.102  -5.612  1.00 22.94  ? 166 SER A O   1 
ATOM   1318 C  CB  . SER A 1 165 ? -10.367 -3.054  -6.168  1.00 26.78  ? 166 SER A CB  1 
ATOM   1319 O  OG  . SER A 1 165 ? -10.828 -2.424  -4.995  1.00 25.68  ? 166 SER A OG  1 
ATOM   1320 N  N   . ILE A 1 166 ? -7.849  -3.516  -3.867  1.00 17.38  ? 167 ILE A N   1 
ATOM   1321 C  CA  . ILE A 1 166 ? -6.807  -2.879  -3.049  1.00 18.29  ? 167 ILE A CA  1 
ATOM   1322 C  C   . ILE A 1 166 ? -5.826  -3.931  -2.532  1.00 17.78  ? 167 ILE A C   1 
ATOM   1323 O  O   . ILE A 1 166 ? -5.408  -3.968  -1.362  1.00 18.72  ? 167 ILE A O   1 
ATOM   1324 C  CB  . ILE A 1 166 ? -7.408  -2.048  -1.903  1.00 18.95  ? 167 ILE A CB  1 
ATOM   1325 C  CG1 . ILE A 1 166 ? -8.291  -2.874  -0.960  1.00 17.85  ? 167 ILE A CG1 1 
ATOM   1326 C  CG2 . ILE A 1 166 ? -8.150  -0.852  -2.489  1.00 20.16  ? 167 ILE A CG2 1 
ATOM   1327 C  CD1 . ILE A 1 166 ? -8.398  -2.255  0.419   1.00 18.06  ? 167 ILE A CD1 1 
ATOM   1328 N  N   . LYS A 1 167 ? -5.392  -4.804  -3.427  1.00 17.55  ? 168 LYS A N   1 
ATOM   1329 C  CA  . LYS A 1 167 ? -4.643  -5.983  -3.011  1.00 18.37  ? 168 LYS A CA  1 
ATOM   1330 C  C   . LYS A 1 167 ? -3.307  -5.614  -2.383  1.00 19.72  ? 168 LYS A C   1 
ATOM   1331 O  O   . LYS A 1 167 ? -2.899  -6.286  -1.452  1.00 20.15  ? 168 LYS A O   1 
ATOM   1332 C  CB  . LYS A 1 167 ? -4.443  -6.940  -4.193  1.00 21.54  ? 168 LYS A CB  1 
ATOM   1333 C  CG  . LYS A 1 167 ? -3.620  -8.186  -3.809  1.00 23.40  ? 168 LYS A CG  1 
ATOM   1334 C  CD  . LYS A 1 167 ? -3.391  -9.075  -5.018  1.00 29.84  ? 168 LYS A CD  1 
ATOM   1335 C  CE  . LYS A 1 167 ? -2.605  -10.329 -4.678  1.00 49.57  ? 168 LYS A CE  1 
ATOM   1336 N  N   . THR A 1 168 ? -2.649  -4.565  -2.893  1.00 20.36  ? 169 THR A N   1 
ATOM   1337 C  CA  . THR A 1 168 ? -1.286  -4.293  -2.478  1.00 21.68  ? 169 THR A CA  1 
ATOM   1338 C  C   . THR A 1 168 ? -1.198  -2.923  -1.801  1.00 20.04  ? 169 THR A C   1 
ATOM   1339 O  O   . THR A 1 168 ? -2.076  -2.073  -1.923  1.00 20.51  ? 169 THR A O   1 
ATOM   1340 C  CB  . THR A 1 168 ? -0.351  -4.405  -3.697  1.00 23.97  ? 169 THR A CB  1 
ATOM   1341 O  OG1 . THR A 1 168 ? -0.866  -3.596  -4.776  1.00 28.69  ? 169 THR A OG1 1 
ATOM   1342 C  CG2 . THR A 1 168 ? -0.126  -5.847  -4.126  1.00 28.36  ? 169 THR A CG2 1 
ATOM   1343 N  N   . LYS A 1 169 ? -0.111  -2.748  -1.061  1.00 20.96  ? 170 LYS A N   1 
ATOM   1344 C  CA  . LYS A 1 169 ? 0.180   -1.528  -0.329  1.00 18.86  ? 170 LYS A CA  1 
ATOM   1345 C  C   . LYS A 1 169 ? 0.079   -0.306  -1.227  1.00 21.76  ? 170 LYS A C   1 
ATOM   1346 O  O   . LYS A 1 169 ? 0.653   -0.273  -2.324  1.00 24.98  ? 170 LYS A O   1 
ATOM   1347 C  CB  . LYS A 1 169 ? 1.582   -1.634  0.275   1.00 21.52  ? 170 LYS A CB  1 
ATOM   1348 C  CG  . LYS A 1 169 ? 2.080   -0.400  1.017   1.00 23.48  ? 170 LYS A CG  1 
ATOM   1349 C  CD  . LYS A 1 169 ? 3.544   -0.600  1.496   1.00 29.79  ? 170 LYS A CD  1 
ATOM   1350 C  CE  . LYS A 1 169 ? 4.021   0.559   2.348   1.00 39.25  ? 170 LYS A CE  1 
ATOM   1351 N  N   . GLY A 1 170 ? -0.688  0.680   -0.764  1.00 20.79  ? 171 GLY A N   1 
ATOM   1352 C  CA  . GLY A 1 170 ? -0.845  1.976   -1.417  1.00 23.04  ? 171 GLY A CA  1 
ATOM   1353 C  C   . GLY A 1 170 ? -2.070  2.057   -2.330  1.00 23.15  ? 171 GLY A C   1 
ATOM   1354 O  O   . GLY A 1 170 ? -2.368  3.144   -2.859  1.00 30.49  ? 171 GLY A O   1 
ATOM   1355 N  N   . LYS A 1 171 ? -2.751  0.925   -2.553  1.00 20.01  ? 172 LYS A N   1 
ATOM   1356 C  CA  . LYS A 1 171 ? -3.969  0.970   -3.365  1.00 20.71  ? 172 LYS A CA  1 
ATOM   1357 C  C   . LYS A 1 171 ? -5.141  1.470   -2.533  1.00 20.20  ? 172 LYS A C   1 
ATOM   1358 O  O   . LYS A 1 171 ? -5.311  1.097   -1.375  1.00 20.91  ? 172 LYS A O   1 
ATOM   1359 C  CB  . LYS A 1 171 ? -4.287  -0.386  -4.012  1.00 22.32  ? 172 LYS A CB  1 
ATOM   1360 C  CG  . LYS A 1 171 ? -3.258  -0.809  -5.051  1.00 25.19  ? 172 LYS A CG  1 
ATOM   1361 C  CD  . LYS A 1 171 ? -3.568  -1.984  -5.930  1.00 32.29  ? 172 LYS A CD  1 
ATOM   1362 N  N   . SER A 1 172 ? -5.995  2.286   -3.135  1.00 20.27  ? 173 SER A N   1 
ATOM   1363 C  CA  . SER A 1 172 ? -7.205  2.769   -2.524  1.00 22.16  ? 173 SER A CA  1 
ATOM   1364 C  C   . SER A 1 172 ? -8.348  2.725   -3.536  1.00 19.78  ? 173 SER A C   1 
ATOM   1365 O  O   . SER A 1 172 ? -8.146  2.701   -4.772  1.00 23.42  ? 173 SER A O   1 
ATOM   1366 C  CB  . SER A 1 172 ? -7.001  4.162   -1.992  1.00 25.86  ? 173 SER A CB  1 
ATOM   1367 O  OG  . SER A 1 172 ? -6.666  5.029   -3.044  1.00 29.65  ? 173 SER A OG  1 
ATOM   1368 N  N   . ALA A 1 173 ? -9.556  2.731   -3.020  1.00 20.34  ? 174 ALA A N   1 
ATOM   1369 C  CA  . ALA A 1 173 ? -10.751 2.767   -3.867  1.00 21.92  ? 174 ALA A CA  1 
ATOM   1370 C  C   . ALA A 1 173 ? -11.809 3.627   -3.203  1.00 19.94  ? 174 ALA A C   1 
ATOM   1371 O  O   . ALA A 1 173 ? -11.920 3.709   -1.967  1.00 23.04  ? 174 ALA A O   1 
ATOM   1372 C  CB  . ALA A 1 173 ? -11.245 1.372   -4.131  1.00 23.21  ? 174 ALA A CB  1 
ATOM   1373 N  N   . ASP A 1 174 ? -12.663 4.275   -4.028  1.00 26.53  ? 175 ASP A N   1 
ATOM   1374 C  CA  . ASP A 1 174 ? -13.824 4.922   -3.468  1.00 29.50  ? 175 ASP A CA  1 
ATOM   1375 C  C   . ASP A 1 174 ? -14.668 3.863   -2.761  1.00 21.67  ? 175 ASP A C   1 
ATOM   1376 O  O   . ASP A 1 174 ? -14.683 2.686   -3.115  1.00 25.41  ? 175 ASP A O   1 
ATOM   1377 C  CB  . ASP A 1 174 ? -14.617 5.606   -4.594  1.00 40.25  ? 175 ASP A CB  1 
ATOM   1378 C  CG  . ASP A 1 174 ? -13.696 6.373   -5.553  1.00 56.78  ? 175 ASP A CG  1 
ATOM   1379 O  OD1 . ASP A 1 174 ? -13.152 7.454   -5.151  1.00 57.69  ? 175 ASP A OD1 1 
ATOM   1380 O  OD2 . ASP A 1 174 ? -13.478 5.867   -6.683  1.00 79.52  ? 175 ASP A OD2 1 
ATOM   1381 N  N   . PHE A 1 175 ? -15.233 4.247   -1.588  1.00 19.53  ? 176 PHE A N   1 
ATOM   1382 C  CA  . PHE A 1 175 ? -15.998 3.291   -0.807  1.00 19.05  ? 176 PHE A CA  1 
ATOM   1383 C  C   . PHE A 1 175 ? -17.081 4.042   -0.061  1.00 17.88  ? 176 PHE A C   1 
ATOM   1384 O  O   . PHE A 1 175 ? -17.018 4.245   1.132   1.00 22.04  ? 176 PHE A O   1 
ATOM   1385 C  CB  . PHE A 1 175 ? -15.097 2.529   0.169   1.00 19.50  ? 176 PHE A CB  1 
ATOM   1386 C  CG  . PHE A 1 175 ? -15.716 1.261   0.702   1.00 17.07  ? 176 PHE A CG  1 
ATOM   1387 C  CD1 . PHE A 1 175 ? -15.991 0.182   -0.117  1.00 19.29  ? 176 PHE A CD1 1 
ATOM   1388 C  CD2 . PHE A 1 175 ? -16.031 1.128   2.053   1.00 18.99  ? 176 PHE A CD2 1 
ATOM   1389 C  CE1 . PHE A 1 175 ? -16.551 -0.987  0.383   1.00 19.21  ? 176 PHE A CE1 1 
ATOM   1390 C  CE2 . PHE A 1 175 ? -16.586 -0.051  2.563   1.00 20.74  ? 176 PHE A CE2 1 
ATOM   1391 C  CZ  . PHE A 1 175 ? -16.853 -1.108  1.732   1.00 19.85  ? 176 PHE A CZ  1 
ATOM   1392 N  N   . THR A 1 176 ? -18.065 4.533   -0.793  1.00 18.22  ? 177 THR A N   1 
ATOM   1393 C  CA  . THR A 1 176 ? -19.131 5.336   -0.243  1.00 18.63  ? 177 THR A CA  1 
ATOM   1394 C  C   . THR A 1 176 ? -20.344 4.493   0.140   1.00 15.87  ? 177 THR A C   1 
ATOM   1395 O  O   . THR A 1 176 ? -20.511 3.333   -0.283  1.00 17.15  ? 177 THR A O   1 
ATOM   1396 C  CB  . THR A 1 176 ? -19.605 6.396   -1.266  1.00 19.07  ? 177 THR A CB  1 
ATOM   1397 O  OG1 . THR A 1 176 ? -19.958 5.766   -2.508  1.00 21.16  ? 177 THR A OG1 1 
ATOM   1398 C  CG2 . THR A 1 176 ? -18.541 7.472   -1.385  1.00 25.42  ? 177 THR A CG2 1 
ATOM   1399 N  N   . ASN A 1 177 ? -21.158 5.077   1.020   1.00 15.84  ? 178 ASN A N   1 
ATOM   1400 C  CA  . ASN A 1 177 ? -22.447 4.530   1.407   1.00 16.80  ? 178 ASN A CA  1 
ATOM   1401 C  C   . ASN A 1 177 ? -22.295 3.200   2.147   1.00 18.74  ? 178 ASN A C   1 
ATOM   1402 O  O   . ASN A 1 177 ? -23.162 2.339   2.027   1.00 23.24  ? 178 ASN A O   1 
ATOM   1403 C  CB  . ASN A 1 177 ? -23.383 4.369   0.206   1.00 18.19  ? 178 ASN A CB  1 
ATOM   1404 C  CG  . ASN A 1 177 ? -23.703 5.738   -0.359  1.00 17.40  ? 178 ASN A CG  1 
ATOM   1405 O  OD1 . ASN A 1 177 ? -24.397 6.508   0.274   1.00 20.51  ? 178 ASN A OD1 1 
ATOM   1406 N  ND2 . ASN A 1 177 ? -23.147 6.031   -1.528  1.00 19.45  ? 178 ASN A ND2 1 
ATOM   1407 N  N   . PHE A 1 178 ? -21.174 2.982   2.828   1.00 16.01  ? 179 PHE A N   1 
ATOM   1408 C  CA  . PHE A 1 178 ? -21.039 1.805   3.668   1.00 15.80  ? 179 PHE A CA  1 
ATOM   1409 C  C   . PHE A 1 178 ? -21.526 2.144   5.071   1.00 15.68  ? 179 PHE A C   1 
ATOM   1410 O  O   . PHE A 1 178 ? -21.101 3.150   5.660   1.00 17.89  ? 179 PHE A O   1 
ATOM   1411 C  CB  . PHE A 1 178 ? -19.583 1.376   3.725   1.00 16.20  ? 179 PHE A CB  1 
ATOM   1412 C  CG  . PHE A 1 178 ? -19.433 0.168   4.614   1.00 15.48  ? 179 PHE A CG  1 
ATOM   1413 C  CD1 . PHE A 1 178 ? -19.812 -1.068  4.130   1.00 16.74  ? 179 PHE A CD1 1 
ATOM   1414 C  CD2 . PHE A 1 178 ? -19.075 0.253   5.967   1.00 15.45  ? 179 PHE A CD2 1 
ATOM   1415 C  CE1 . PHE A 1 178 ? -19.748 -2.211  4.902   1.00 18.11  ? 179 PHE A CE1 1 
ATOM   1416 C  CE2 . PHE A 1 178 ? -19.072 -0.894  6.760   1.00 15.70  ? 179 PHE A CE2 1 
ATOM   1417 C  CZ  . PHE A 1 178 ? -19.390 -2.112  6.233   1.00 15.95  ? 179 PHE A CZ  1 
ATOM   1418 N  N   . ASP A 1 179 ? -22.418 1.310   5.599   1.00 15.79  ? 180 ASP A N   1 
ATOM   1419 C  CA  . ASP A 1 179 ? -23.036 1.572   6.887   1.00 15.32  ? 180 ASP A CA  1 
ATOM   1420 C  C   . ASP A 1 179 ? -22.361 0.733   7.975   1.00 15.13  ? 180 ASP A C   1 
ATOM   1421 O  O   . ASP A 1 179 ? -22.524 -0.486  8.026   1.00 15.10  ? 180 ASP A O   1 
ATOM   1422 C  CB  . ASP A 1 179 ? -24.522 1.202   6.840   1.00 18.04  ? 180 ASP A CB  1 
ATOM   1423 C  CG  . ASP A 1 179 ? -25.299 1.579   8.073   1.00 21.16  ? 180 ASP A CG  1 
ATOM   1424 O  OD1 . ASP A 1 179 ? -24.682 1.862   9.130   1.00 18.83  ? 180 ASP A OD1 1 
ATOM   1425 O  OD2 . ASP A 1 179 ? -26.517 1.593   7.983   1.00 27.59  ? 180 ASP A OD2 1 
ATOM   1426 N  N   . PRO A 1 180 ? -21.555 1.345   8.883   1.00 14.42  ? 181 PRO A N   1 
ATOM   1427 C  CA  . PRO A 1 180 ? -20.838 0.518   9.872   1.00 15.05  ? 181 PRO A CA  1 
ATOM   1428 C  C   . PRO A 1 180 ? -21.735 -0.107  10.931  1.00 14.63  ? 181 PRO A C   1 
ATOM   1429 O  O   . PRO A 1 180 ? -21.274 -1.016  11.650  1.00 15.93  ? 181 PRO A O   1 
ATOM   1430 C  CB  . PRO A 1 180 ? -19.817 1.521   10.433  1.00 17.42  ? 181 PRO A CB  1 
ATOM   1431 C  CG  . PRO A 1 180 ? -20.507 2.866   10.259  1.00 17.77  ? 181 PRO A CG  1 
ATOM   1432 C  CD  . PRO A 1 180 ? -21.206 2.782   8.907   1.00 16.81  ? 181 PRO A CD  1 
ATOM   1433 N  N   . ARG A 1 181 ? -23.027 0.279   10.974  1.00 14.98  ? 182 ARG A N   1 
ATOM   1434 C  CA  . ARG A 1 181 ? -23.929 -0.397  11.903  1.00 15.89  ? 182 ARG A CA  1 
ATOM   1435 C  C   . ARG A 1 181 ? -24.003 -1.878  11.544  1.00 15.50  ? 182 ARG A C   1 
ATOM   1436 O  O   . ARG A 1 181 ? -24.393 -2.676  12.390  1.00 17.63  ? 182 ARG A O   1 
ATOM   1437 C  CB  . ARG A 1 181 ? -25.332 0.224   11.846  1.00 16.06  ? 182 ARG A CB  1 
ATOM   1438 C  CG  . ARG A 1 181 ? -25.303 1.653   12.338  1.00 19.31  ? 182 ARG A CG  1 
ATOM   1439 C  CD  . ARG A 1 181 ? -26.655 2.295   12.331  1.00 22.37  ? 182 ARG A CD  1 
ATOM   1440 N  NE  . ARG A 1 181 ? -27.020 2.560   10.923  1.00 21.10  ? 182 ARG A NE  1 
ATOM   1441 C  CZ  . ARG A 1 181 ? -28.041 3.326   10.550  1.00 23.15  ? 182 ARG A CZ  1 
ATOM   1442 N  NH1 . ARG A 1 181 ? -28.796 3.893   11.482  1.00 27.16  ? 182 ARG A NH1 1 
ATOM   1443 N  NH2 . ARG A 1 181 ? -28.338 3.405   9.263   1.00 28.84  ? 182 ARG A NH2 1 
ATOM   1444 N  N   . GLY A 1 182 ? -23.756 -2.209  10.258  1.00 15.36  ? 183 GLY A N   1 
ATOM   1445 C  CA  . GLY A 1 182 ? -23.890 -3.623  9.886   1.00 16.29  ? 183 GLY A CA  1 
ATOM   1446 C  C   . GLY A 1 182 ? -22.718 -4.483  10.372  1.00 16.64  ? 183 GLY A C   1 
ATOM   1447 O  O   . GLY A 1 182 ? -22.715 -5.673  10.108  1.00 18.30  ? 183 GLY A O   1 
ATOM   1448 N  N   . LEU A 1 183 ? -21.747 -3.908  11.124  1.00 15.44  ? 184 LEU A N   1 
ATOM   1449 C  CA  . LEU A 1 183 ? -20.647 -4.663  11.663  1.00 14.67  ? 184 LEU A CA  1 
ATOM   1450 C  C   . LEU A 1 183 ? -20.797 -4.895  13.179  1.00 13.29  ? 184 LEU A C   1 
ATOM   1451 O  O   . LEU A 1 183 ? -19.894 -5.508  13.759  1.00 16.01  ? 184 LEU A O   1 
ATOM   1452 C  CB  . LEU A 1 183 ? -19.350 -3.891  11.425  1.00 15.44  ? 184 LEU A CB  1 
ATOM   1453 C  CG  . LEU A 1 183 ? -18.975 -3.770  9.946   1.00 15.76  ? 184 LEU A CG  1 
ATOM   1454 C  CD1 . LEU A 1 183 ? -17.774 -2.879  9.767   1.00 19.83  ? 184 LEU A CD1 1 
ATOM   1455 C  CD2 . LEU A 1 183 ? -18.864 -5.104  9.225   1.00 19.69  ? 184 LEU A CD2 1 
ATOM   1456 N  N   . LEU A 1 184 ? -21.882 -4.445  13.793  1.00 14.16  ? 185 LEU A N   1 
ATOM   1457 C  CA  . LEU A 1 184 ? -21.982 -4.498  15.256  1.00 14.13  ? 185 LEU A CA  1 
ATOM   1458 C  C   . LEU A 1 184 ? -22.746 -5.738  15.675  1.00 15.64  ? 185 LEU A C   1 
ATOM   1459 O  O   . LEU A 1 184 ? -23.693 -6.161  15.035  1.00 20.46  ? 185 LEU A O   1 
ATOM   1460 C  CB  . LEU A 1 184 ? -22.758 -3.255  15.762  1.00 16.01  ? 185 LEU A CB  1 
ATOM   1461 C  CG  . LEU A 1 184 ? -22.188 -1.911  15.306  1.00 19.56  ? 185 LEU A CG  1 
ATOM   1462 C  CD1 . LEU A 1 184 ? -22.980 -0.756  15.869  1.00 21.23  ? 185 LEU A CD1 1 
ATOM   1463 C  CD2 . LEU A 1 184 ? -20.764 -1.840  15.725  1.00 20.86  ? 185 LEU A CD2 1 
ATOM   1464 N  N   . PRO A 1 185 ? -22.416 -6.310  16.865  1.00 14.89  ? 186 PRO A N   1 
ATOM   1465 C  CA  . PRO A 1 185 ? -23.206 -7.418  17.428  1.00 15.55  ? 186 PRO A CA  1 
ATOM   1466 C  C   . PRO A 1 185 ? -24.481 -6.843  18.048  1.00 14.35  ? 186 PRO A C   1 
ATOM   1467 O  O   . PRO A 1 185 ? -24.650 -5.633  18.091  1.00 16.84  ? 186 PRO A O   1 
ATOM   1468 C  CB  . PRO A 1 185 ? -22.241 -8.001  18.470  1.00 15.78  ? 186 PRO A CB  1 
ATOM   1469 C  CG  . PRO A 1 185 ? -21.481 -6.773  18.933  1.00 14.37  ? 186 PRO A CG  1 
ATOM   1470 C  CD  . PRO A 1 185 ? -21.273 -5.904  17.691  1.00 13.90  ? 186 PRO A CD  1 
ATOM   1471 N  N   . GLU A 1 186 ? -25.370 -7.719  18.546  1.00 16.73  ? 187 GLU A N   1 
ATOM   1472 C  CA  . GLU A 1 186 ? -26.617 -7.248  19.136  1.00 17.35  ? 187 GLU A CA  1 
ATOM   1473 C  C   . GLU A 1 186 ? -26.313 -6.479  20.418  1.00 16.94  ? 187 GLU A C   1 
ATOM   1474 O  O   . GLU A 1 186 ? -26.885 -5.405  20.615  1.00 20.01  ? 187 GLU A O   1 
ATOM   1475 C  CB  . GLU A 1 186 ? -27.490 -8.433  19.546  1.00 21.81  ? 187 GLU A CB  1 
ATOM   1476 C  CG  . GLU A 1 186 ? -28.100 -9.187  18.399  1.00 23.73  ? 187 GLU A CG  1 
ATOM   1477 C  CD  . GLU A 1 186 ? -28.868 -10.424 18.900  1.00 25.33  ? 187 GLU A CD  1 
ATOM   1478 O  OE1 . GLU A 1 186 ? -28.899 -10.701 20.160  1.00 27.20  ? 187 GLU A OE1 1 
ATOM   1479 O  OE2 . GLU A 1 186 ? -29.390 -11.165 18.062  1.00 31.46  ? 187 GLU A OE2 1 
ATOM   1480 N  N   . SER A 1 187 ? -25.433 -7.014  21.277  1.00 16.70  ? 188 SER A N   1 
ATOM   1481 C  CA  . SER A 1 187 ? -25.238 -6.418  22.601  1.00 17.31  ? 188 SER A CA  1 
ATOM   1482 C  C   . SER A 1 187 ? -24.109 -5.386  22.555  1.00 16.24  ? 188 SER A C   1 
ATOM   1483 O  O   . SER A 1 187 ? -23.100 -5.610  21.888  1.00 17.95  ? 188 SER A O   1 
ATOM   1484 C  CB  . SER A 1 187 ? -24.838 -7.489  23.605  1.00 18.59  ? 188 SER A CB  1 
ATOM   1485 O  OG  . SER A 1 187 ? -24.613 -6.931  24.893  1.00 18.16  ? 188 SER A OG  1 
ATOM   1486 N  N   . LEU A 1 188 ? -24.257 -4.305  23.309  1.00 16.52  ? 189 LEU A N   1 
ATOM   1487 C  CA  . LEU A 1 188 ? -23.186 -3.338  23.513  1.00 16.96  ? 189 LEU A CA  1 
ATOM   1488 C  C   . LEU A 1 188 ? -22.616 -3.476  24.926  1.00 16.11  ? 189 LEU A C   1 
ATOM   1489 O  O   . LEU A 1 188 ? -21.922 -2.591  25.365  1.00 18.13  ? 189 LEU A O   1 
ATOM   1490 C  CB  . LEU A 1 188 ? -23.698 -1.912  23.262  1.00 18.59  ? 189 LEU A CB  1 
ATOM   1491 C  CG  . LEU A 1 188 ? -24.073 -1.525  21.831  1.00 21.43  ? 189 LEU A CG  1 
ATOM   1492 C  CD1 . LEU A 1 188 ? -24.614 -0.110  21.770  1.00 22.36  ? 189 LEU A CD1 1 
ATOM   1493 C  CD2 . LEU A 1 188 ? -22.937 -1.734  20.835  1.00 25.05  ? 189 LEU A CD2 1 
ATOM   1494 N  N   . ASP A 1 189 ? -22.713 -4.656  25.538  1.00 16.40  ? 190 ASP A N   1 
ATOM   1495 C  CA  . ASP A 1 189 ? -21.987 -4.894  26.792  1.00 17.57  ? 190 ASP A CA  1 
ATOM   1496 C  C   . ASP A 1 189 ? -20.482 -4.899  26.501  1.00 14.96  ? 190 ASP A C   1 
ATOM   1497 O  O   . ASP A 1 189 ? -20.035 -5.351  25.444  1.00 14.85  ? 190 ASP A O   1 
ATOM   1498 C  CB  . ASP A 1 189 ? -22.307 -6.266  27.351  1.00 20.72  ? 190 ASP A CB  1 
ATOM   1499 C  CG  . ASP A 1 189 ? -23.688 -6.352  27.991  1.00 24.14  ? 190 ASP A CG  1 
ATOM   1500 O  OD1 . ASP A 1 189 ? -24.295 -5.303  28.207  1.00 32.81  ? 190 ASP A OD1 1 
ATOM   1501 O  OD2 . ASP A 1 189 ? -24.089 -7.449  28.307  1.00 32.01  ? 190 ASP A OD2 1 
ATOM   1502 N  N   . TYR A 1 190 ? -19.675 -4.255  27.360  1.00 14.17  ? 191 TYR A N   1 
ATOM   1503 C  CA  . TYR A 1 190 ? -18.271 -4.055  27.008  1.00 13.89  ? 191 TYR A CA  1 
ATOM   1504 C  C   . TYR A 1 190 ? -17.370 -4.114  28.231  1.00 12.63  ? 191 TYR A C   1 
ATOM   1505 O  O   . TYR A 1 190 ? -17.805 -3.979  29.379  1.00 13.82  ? 191 TYR A O   1 
ATOM   1506 C  CB  . TYR A 1 190 ? -18.113 -2.669  26.348  1.00 14.59  ? 191 TYR A CB  1 
ATOM   1507 C  CG  . TYR A 1 190 ? -18.500 -1.500  27.224  1.00 13.60  ? 191 TYR A CG  1 
ATOM   1508 C  CD1 . TYR A 1 190 ? -17.565 -0.883  28.061  1.00 15.00  ? 191 TYR A CD1 1 
ATOM   1509 C  CD2 . TYR A 1 190 ? -19.777 -0.958  27.186  1.00 14.89  ? 191 TYR A CD2 1 
ATOM   1510 C  CE1 . TYR A 1 190 ? -17.941 0.160   28.907  1.00 15.43  ? 191 TYR A CE1 1 
ATOM   1511 C  CE2 . TYR A 1 190 ? -20.158 0.108   27.972  1.00 15.75  ? 191 TYR A CE2 1 
ATOM   1512 C  CZ  . TYR A 1 190 ? -19.224 0.668   28.838  1.00 15.25  ? 191 TYR A CZ  1 
ATOM   1513 O  OH  . TYR A 1 190 ? -19.565 1.676   29.698  1.00 18.35  ? 191 TYR A OH  1 
ATOM   1514 N  N   . TRP A 1 191 ? -16.079 -4.254  27.942  1.00 12.22  ? 192 TRP A N   1 
ATOM   1515 C  CA  . TRP A 1 191 ? -15.006 -3.989  28.864  1.00 12.68  ? 192 TRP A CA  1 
ATOM   1516 C  C   . TRP A 1 191 ? -14.318 -2.692  28.463  1.00 11.35  ? 192 TRP A C   1 
ATOM   1517 O  O   . TRP A 1 191 ? -14.245 -2.385  27.263  1.00 13.42  ? 192 TRP A O   1 
ATOM   1518 C  CB  . TRP A 1 191 ? -13.995 -5.127  28.869  1.00 13.34  ? 192 TRP A CB  1 
ATOM   1519 C  CG  . TRP A 1 191 ? -14.512 -6.464  29.285  1.00 12.11  ? 192 TRP A CG  1 
ATOM   1520 C  CD1 . TRP A 1 191 ? -14.762 -6.887  30.574  1.00 13.93  ? 192 TRP A CD1 1 
ATOM   1521 C  CD2 . TRP A 1 191 ? -14.804 -7.579  28.437  1.00 13.16  ? 192 TRP A CD2 1 
ATOM   1522 N  NE1 . TRP A 1 191 ? -15.169 -8.209  30.559  1.00 16.24  ? 192 TRP A NE1 1 
ATOM   1523 C  CE2 . TRP A 1 191 ? -15.207 -8.657  29.254  1.00 14.68  ? 192 TRP A CE2 1 
ATOM   1524 C  CE3 . TRP A 1 191 ? -14.709 -7.773  27.043  1.00 13.94  ? 192 TRP A CE3 1 
ATOM   1525 C  CZ2 . TRP A 1 191 ? -15.569 -9.919  28.755  1.00 14.83  ? 192 TRP A CZ2 1 
ATOM   1526 C  CZ3 . TRP A 1 191 ? -15.003 -9.036  26.555  1.00 16.14  ? 192 TRP A CZ3 1 
ATOM   1527 C  CH2 . TRP A 1 191 ? -15.428 -10.060 27.390  1.00 16.01  ? 192 TRP A CH2 1 
ATOM   1528 N  N   . THR A 1 192 ? -13.735 -1.986  29.415  1.00 12.19  ? 193 THR A N   1 
ATOM   1529 C  CA  . THR A 1 192 ? -13.014 -0.776  29.078  1.00 12.04  ? 193 THR A CA  1 
ATOM   1530 C  C   . THR A 1 192 ? -11.742 -0.649  29.903  1.00 12.05  ? 193 THR A C   1 
ATOM   1531 O  O   . THR A 1 192 ? -11.741 -1.028  31.088  1.00 13.12  ? 193 THR A O   1 
ATOM   1532 C  CB  . THR A 1 192 ? -13.927 0.451   29.173  1.00 12.11  ? 193 THR A CB  1 
ATOM   1533 O  OG1 . THR A 1 192 ? -13.223 1.634   28.744  1.00 13.63  ? 193 THR A OG1 1 
ATOM   1534 C  CG2 . THR A 1 192 ? -14.474 0.658   30.570  1.00 13.57  ? 193 THR A CG2 1 
ATOM   1535 N  N   . TYR A 1 193 ? -10.713 -0.055  29.351  1.00 11.51  ? 194 TYR A N   1 
ATOM   1536 C  CA  . TYR A 1 193 ? -9.504  0.212   30.097  1.00 12.03  ? 194 TYR A CA  1 
ATOM   1537 C  C   . TYR A 1 193 ? -8.743  1.283   29.327  1.00 10.42  ? 194 TYR A C   1 
ATOM   1538 O  O   . TYR A 1 193 ? -8.916  1.446   28.101  1.00 11.93  ? 194 TYR A O   1 
ATOM   1539 C  CB  . TYR A 1 193 ? -8.669  -1.074  30.299  1.00 12.70  ? 194 TYR A CB  1 
ATOM   1540 C  CG  . TYR A 1 193 ? -8.004  -1.523  29.019  1.00 11.55  ? 194 TYR A CG  1 
ATOM   1541 C  CD1 . TYR A 1 193 ? -8.670  -2.307  28.055  1.00 11.34  ? 194 TYR A CD1 1 
ATOM   1542 C  CD2 . TYR A 1 193 ? -6.651  -1.195  28.769  1.00 12.45  ? 194 TYR A CD2 1 
ATOM   1543 C  CE1 . TYR A 1 193 ? -8.065  -2.645  26.852  1.00 10.65  ? 194 TYR A CE1 1 
ATOM   1544 C  CE2 . TYR A 1 193 ? -6.024  -1.521  27.569  1.00 12.23  ? 194 TYR A CE2 1 
ATOM   1545 C  CZ  . TYR A 1 193 ? -6.747  -2.292  26.660  1.00 9.96   ? 194 TYR A CZ  1 
ATOM   1546 O  OH  . TYR A 1 193 ? -6.115  -2.541  25.491  1.00 11.32  ? 194 TYR A OH  1 
ATOM   1547 N  N   . PRO A 1 194 ? -7.784  1.992   29.968  1.00 12.25  ? 195 PRO A N   1 
ATOM   1548 C  CA  . PRO A 1 194 ? -6.968  2.985   29.287  1.00 12.47  ? 195 PRO A CA  1 
ATOM   1549 C  C   . PRO A 1 194 ? -5.767  2.334   28.659  1.00 10.96  ? 195 PRO A C   1 
ATOM   1550 O  O   . PRO A 1 194 ? -5.051  1.524   29.317  1.00 12.99  ? 195 PRO A O   1 
ATOM   1551 C  CB  . PRO A 1 194 ? -6.510  3.910   30.431  1.00 14.13  ? 195 PRO A CB  1 
ATOM   1552 C  CG  . PRO A 1 194 ? -6.514  3.037   31.650  1.00 15.58  ? 195 PRO A CG  1 
ATOM   1553 C  CD  . PRO A 1 194 ? -7.631  2.024   31.431  1.00 14.12  ? 195 PRO A CD  1 
ATOM   1554 N  N   . GLY A 1 195 ? -5.528  2.622   27.367  1.00 11.43  ? 196 GLY A N   1 
ATOM   1555 C  CA  . GLY A 1 195 ? -4.449  1.975   26.661  1.00 12.78  ? 196 GLY A CA  1 
ATOM   1556 C  C   . GLY A 1 195 ? -3.848  2.835   25.579  1.00 11.26  ? 196 GLY A C   1 
ATOM   1557 O  O   . GLY A 1 195 ? -3.749  4.056   25.692  1.00 11.47  ? 196 GLY A O   1 
ATOM   1558 N  N   . SER A 1 196 ? -3.442  2.168   24.498  1.00 11.68  ? 197 SER A N   1 
ATOM   1559 C  CA  . SER A 1 196 ? -2.629  2.798   23.460  1.00 12.10  ? 197 SER A CA  1 
ATOM   1560 C  C   . SER A 1 196 ? -3.092  2.386   22.074  1.00 11.43  ? 197 SER A C   1 
ATOM   1561 O  O   . SER A 1 196 ? -3.852  1.457   21.912  1.00 11.42  ? 197 SER A O   1 
ATOM   1562 C  CB  . SER A 1 196 ? -1.178  2.420   23.609  1.00 13.07  ? 197 SER A CB  1 
ATOM   1563 O  OG  . SER A 1 196 ? -0.924  1.068   23.242  1.00 11.95  ? 197 SER A OG  1 
ATOM   1564 N  N   . LEU A 1 197 ? -2.537  3.063   21.088  1.00 11.11  ? 198 LEU A N   1 
ATOM   1565 C  CA  . LEU A 1 197 ? -2.547  2.517   19.741  1.00 11.41  ? 198 LEU A CA  1 
ATOM   1566 C  C   . LEU A 1 197 ? -1.860  1.179   19.795  1.00 11.33  ? 198 LEU A C   1 
ATOM   1567 O  O   . LEU A 1 197 ? -0.833  1.023   20.449  1.00 13.24  ? 198 LEU A O   1 
ATOM   1568 C  CB  . LEU A 1 197 ? -1.802  3.461   18.805  1.00 13.34  ? 198 LEU A CB  1 
ATOM   1569 C  CG  . LEU A 1 197 ? -2.361  4.875   18.716  1.00 14.01  ? 198 LEU A CG  1 
ATOM   1570 C  CD1 . LEU A 1 197 ? -1.468  5.644   17.743  1.00 16.75  ? 198 LEU A CD1 1 
ATOM   1571 C  CD2 . LEU A 1 197 ? -3.825  4.896   18.270  1.00 17.49  ? 198 LEU A CD2 1 
ATOM   1572 N  N   . THR A 1 198 ? -2.288  0.227   18.938  1.00 11.70  ? 199 THR A N   1 
ATOM   1573 C  CA  . THR A 1 198 ? -1.627  -1.067  18.901  1.00 11.57  ? 199 THR A CA  1 
ATOM   1574 C  C   . THR A 1 198 ? -0.633  -1.152  17.739  1.00 11.46  ? 199 THR A C   1 
ATOM   1575 O  O   . THR A 1 198 ? 0.024   -2.177  17.584  1.00 13.04  ? 199 THR A O   1 
ATOM   1576 C  CB  . THR A 1 198 ? -2.618  -2.216  18.804  1.00 11.39  ? 199 THR A CB  1 
ATOM   1577 O  OG1 . THR A 1 198 ? -3.167  -2.176  17.497  1.00 11.79  ? 199 THR A OG1 1 
ATOM   1578 C  CG2 . THR A 1 198 ? -3.612  -2.199  19.935  1.00 12.92  ? 199 THR A CG2 1 
ATOM   1579 N  N   . THR A 1 199 ? -0.433  -0.034  17.025  1.00 12.51  ? 200 THR A N   1 
ATOM   1580 C  CA  . THR A 1 199 ? 0.568   0.056   16.002  1.00 12.63  ? 200 THR A CA  1 
ATOM   1581 C  C   . THR A 1 199 ? 1.425   1.264   16.315  1.00 13.27  ? 200 THR A C   1 
ATOM   1582 O  O   . THR A 1 199 ? 0.931   2.212   16.893  1.00 13.79  ? 200 THR A O   1 
ATOM   1583 C  CB  . THR A 1 199 ? -0.031  0.235   14.589  1.00 14.39  ? 200 THR A CB  1 
ATOM   1584 O  OG1 . THR A 1 199 ? -0.930  1.336   14.638  1.00 19.43  ? 200 THR A OG1 1 
ATOM   1585 C  CG2 . THR A 1 199 ? -0.756  -1.006  14.151  1.00 15.02  ? 200 THR A CG2 1 
ATOM   1586 N  N   . PRO A 1 200 ? 2.673   1.309   15.806  1.00 13.91  ? 201 PRO A N   1 
ATOM   1587 C  CA  . PRO A 1 200 ? 3.445   2.537   15.885  1.00 15.43  ? 201 PRO A CA  1 
ATOM   1588 C  C   . PRO A 1 200 ? 2.559   3.675   15.393  1.00 14.87  ? 201 PRO A C   1 
ATOM   1589 O  O   . PRO A 1 200 ? 1.876   3.525   14.361  1.00 16.52  ? 201 PRO A O   1 
ATOM   1590 C  CB  . PRO A 1 200 ? 4.575   2.217   14.916  1.00 15.75  ? 201 PRO A CB  1 
ATOM   1591 C  CG  . PRO A 1 200 ? 4.847   0.735   15.155  1.00 15.85  ? 201 PRO A CG  1 
ATOM   1592 C  CD  . PRO A 1 200 ? 3.416   0.184   15.225  1.00 14.95  ? 201 PRO A CD  1 
ATOM   1593 N  N   . PRO A 1 201 ? 2.610   4.855   16.035  1.00 15.33  ? 202 PRO A N   1 
ATOM   1594 C  CA  . PRO A 1 201 ? 3.617   5.201   17.071  1.00 15.08  ? 202 PRO A CA  1 
ATOM   1595 C  C   . PRO A 1 201 ? 3.258   4.804   18.509  1.00 15.11  ? 202 PRO A C   1 
ATOM   1596 O  O   . PRO A 1 201 ? 3.966   5.189   19.432  1.00 16.04  ? 202 PRO A O   1 
ATOM   1597 C  CB  . PRO A 1 201 ? 3.674   6.732   16.969  1.00 18.57  ? 202 PRO A CB  1 
ATOM   1598 C  CG  . PRO A 1 201 ? 2.271   7.118   16.463  1.00 20.06  ? 202 PRO A CG  1 
ATOM   1599 C  CD  . PRO A 1 201 ? 1.796   5.997   15.574  1.00 17.54  ? 202 PRO A CD  1 
ATOM   1600 N  N   . LEU A 1 202 ? 2.231   3.979   18.702  1.00 13.40  ? 203 LEU A N   1 
ATOM   1601 C  CA  . LEU A 1 202 ? 1.949   3.378   19.999  1.00 12.77  ? 203 LEU A CA  1 
ATOM   1602 C  C   . LEU A 1 202 ? 1.571   4.395   21.053  1.00 12.90  ? 203 LEU A C   1 
ATOM   1603 O  O   . LEU A 1 202 ? 1.596   4.092   22.255  1.00 13.74  ? 203 LEU A O   1 
ATOM   1604 C  CB  . LEU A 1 202 ? 3.099   2.479   20.484  1.00 12.97  ? 203 LEU A CB  1 
ATOM   1605 C  CG  . LEU A 1 202 ? 3.450   1.326   19.536  1.00 13.63  ? 203 LEU A CG  1 
ATOM   1606 C  CD1 . LEU A 1 202 ? 4.742   0.691   19.995  1.00 16.74  ? 203 LEU A CD1 1 
ATOM   1607 C  CD2 . LEU A 1 202 ? 2.331   0.302   19.480  1.00 15.52  ? 203 LEU A CD2 1 
ATOM   1608 N  N   . ASN A 1 203 ? 1.049   5.540   20.641  1.00 14.26  ? 204 ASN A N   1 
ATOM   1609 C  CA  . ASN A 1 203 ? 0.694   6.604   21.561  1.00 14.22  ? 204 ASN A CA  1 
ATOM   1610 C  C   . ASN A 1 203 ? -0.299  6.113   22.601  1.00 13.50  ? 204 ASN A C   1 
ATOM   1611 O  O   . ASN A 1 203 ? -1.266  5.393   22.300  1.00 13.44  ? 204 ASN A O   1 
ATOM   1612 C  CB  . ASN A 1 203 ? 0.027   7.770   20.823  1.00 15.80  ? 204 ASN A CB  1 
ATOM   1613 C  CG  . ASN A 1 203 ? 0.934   8.492   19.854  1.00 19.79  ? 204 ASN A CG  1 
ATOM   1614 O  OD1 . ASN A 1 203 ? 2.025   8.079   19.513  1.00 22.83  ? 204 ASN A OD1 1 
ATOM   1615 N  ND2 . ASN A 1 203 ? 0.462   9.639   19.424  1.00 23.80  ? 204 ASN A ND2 1 
ATOM   1616 N  N   . GLU A 1 204 ? -0.135  6.590   23.826  1.00 13.29  ? 205 GLU A N   1 
ATOM   1617 C  CA  . GLU A 1 204 ? -0.956  6.216   24.950  1.00 12.95  ? 205 GLU A CA  1 
ATOM   1618 C  C   . GLU A 1 204 ? -2.139  7.167   25.058  1.00 14.33  ? 205 GLU A C   1 
ATOM   1619 O  O   . GLU A 1 204 ? -2.257  7.934   26.011  1.00 17.20  ? 205 GLU A O   1 
ATOM   1620 C  CB  . GLU A 1 204 ? -0.111  6.111   26.209  1.00 15.00  ? 205 GLU A CB  1 
ATOM   1621 C  CG  . GLU A 1 204 ? 0.772   4.879   26.102  1.00 17.48  ? 205 GLU A CG  1 
ATOM   1622 C  CD  . GLU A 1 204 ? 1.663   4.571   27.289  1.00 16.49  ? 205 GLU A CD  1 
ATOM   1623 O  OE1 . GLU A 1 204 ? 1.944   5.531   28.077  1.00 20.99  ? 205 GLU A OE1 1 
ATOM   1624 O  OE2 . GLU A 1 204 ? 2.047   3.377   27.450  1.00 16.09  ? 205 GLU A OE2 1 
ATOM   1625 N  N   . CYS A 1 205 ? -3.040  7.097   24.091  1.00 12.69  ? 206 CYS A N   1 
ATOM   1626 C  CA  . CYS A 1 205 ? -4.069  8.094   23.904  1.00 13.09  ? 206 CYS A CA  1 
ATOM   1627 C  C   . CYS A 1 205 ? -5.442  7.463   23.777  1.00 12.42  ? 206 CYS A C   1 
ATOM   1628 O  O   . CYS A 1 205 ? -6.386  8.171   23.448  1.00 14.60  ? 206 CYS A O   1 
ATOM   1629 C  CB  . CYS A 1 205 ? -3.769  8.895   22.636  1.00 14.92  ? 206 CYS A CB  1 
ATOM   1630 S  SG  . CYS A 1 205 ? -3.737  7.907   21.118  1.00 15.23  ? 206 CYS A SG  1 
ATOM   1631 N  N   . VAL A 1 206 ? -5.588  6.156   24.059  1.00 11.99  ? 207 VAL A N   1 
ATOM   1632 C  CA  . VAL A 1 206 ? -6.808  5.431   23.725  1.00 11.55  ? 207 VAL A CA  1 
ATOM   1633 C  C   . VAL A 1 206 ? -7.569  5.031   24.971  1.00 11.01  ? 207 VAL A C   1 
ATOM   1634 O  O   . VAL A 1 206 ? -7.041  4.344   25.829  1.00 13.50  ? 207 VAL A O   1 
ATOM   1635 C  CB  . VAL A 1 206 ? -6.530  4.189   22.874  1.00 12.30  ? 207 VAL A CB  1 
ATOM   1636 C  CG1 . VAL A 1 206 ? -7.880  3.497   22.531  1.00 12.70  ? 207 VAL A CG1 1 
ATOM   1637 C  CG2 . VAL A 1 206 ? -5.784  4.564   21.615  1.00 13.52  ? 207 VAL A CG2 1 
ATOM   1638 N  N   . THR A 1 207 ? -8.878  5.311   24.994  1.00 11.63  ? 208 THR A N   1 
ATOM   1639 C  CA  . THR A 1 207 ? -9.824  4.631   25.866  1.00 11.98  ? 208 THR A CA  1 
ATOM   1640 C  C   . THR A 1 207 ? -10.384 3.470   25.046  1.00 11.37  ? 208 THR A C   1 
ATOM   1641 O  O   . THR A 1 207 ? -11.017 3.643   24.018  1.00 12.23  ? 208 THR A O   1 
ATOM   1642 C  CB  . THR A 1 207 ? -11.018 5.482   26.314  1.00 12.98  ? 208 THR A CB  1 
ATOM   1643 O  OG1 . THR A 1 207 ? -10.451 6.594   27.026  1.00 14.47  ? 208 THR A OG1 1 
ATOM   1644 C  CG2 . THR A 1 207 ? -11.986 4.743   27.201  1.00 14.85  ? 208 THR A CG2 1 
ATOM   1645 N  N   . TRP A 1 208 ? -9.996  2.237   25.448  1.00 11.01  ? 209 TRP A N   1 
ATOM   1646 C  CA  . TRP A 1 208 ? -10.453 1.036   24.748  1.00 10.69  ? 209 TRP A CA  1 
ATOM   1647 C  C   . TRP A 1 208 ? -11.800 0.616   25.266  1.00 10.64  ? 209 TRP A C   1 
ATOM   1648 O  O   . TRP A 1 208 ? -12.060 0.592   26.482  1.00 11.51  ? 209 TRP A O   1 
ATOM   1649 C  CB  . TRP A 1 208 ? -9.464  -0.119  24.956  1.00 10.87  ? 209 TRP A CB  1 
ATOM   1650 C  CG  . TRP A 1 208 ? -8.348  -0.012  23.983  1.00 10.39  ? 209 TRP A CG  1 
ATOM   1651 C  CD1 . TRP A 1 208 ? -7.101  0.575   24.158  1.00 10.57  ? 209 TRP A CD1 1 
ATOM   1652 C  CD2 . TRP A 1 208 ? -8.376  -0.400  22.618  1.00 10.59  ? 209 TRP A CD2 1 
ATOM   1653 N  NE1 . TRP A 1 208 ? -6.382  0.587   23.025  1.00 11.46  ? 209 TRP A NE1 1 
ATOM   1654 C  CE2 . TRP A 1 208 ? -7.137  -0.055  22.063  1.00 11.23  ? 209 TRP A CE2 1 
ATOM   1655 C  CE3 . TRP A 1 208 ? -9.355  -1.082  21.852  1.00 10.15  ? 209 TRP A CE3 1 
ATOM   1656 C  CZ2 . TRP A 1 208 ? -6.866  -0.311  20.715  1.00 11.94  ? 209 TRP A CZ2 1 
ATOM   1657 C  CZ3 . TRP A 1 208 ? -9.080  -1.325  20.530  1.00 11.43  ? 209 TRP A CZ3 1 
ATOM   1658 C  CH2 . TRP A 1 208 ? -7.855  -0.982  19.972  1.00 12.39  ? 209 TRP A CH2 1 
ATOM   1659 N  N   . ILE A 1 209 ? -12.715 0.321   24.324  1.00 11.19  ? 210 ILE A N   1 
ATOM   1660 C  CA  . ILE A 1 209 ? -14.034 -0.204  24.641  1.00 11.45  ? 210 ILE A CA  1 
ATOM   1661 C  C   . ILE A 1 209 ? -14.200 -1.475  23.831  1.00 10.47  ? 210 ILE A C   1 
ATOM   1662 O  O   . ILE A 1 209 ? -14.239 -1.386  22.582  1.00 12.05  ? 210 ILE A O   1 
ATOM   1663 C  CB  . ILE A 1 209 ? -15.117 0.823   24.272  1.00 12.74  ? 210 ILE A CB  1 
ATOM   1664 C  CG1 . ILE A 1 209 ? -14.873 2.112   25.067  1.00 15.76  ? 210 ILE A CG1 1 
ATOM   1665 C  CG2 . ILE A 1 209 ? -16.492 0.235   24.541  1.00 14.46  ? 210 ILE A CG2 1 
ATOM   1666 C  CD1 . ILE A 1 209 ? -15.685 3.292   24.620  1.00 17.18  ? 210 ILE A CD1 1 
ATOM   1667 N  N   . VAL A 1 210 ? -14.092 -2.643  24.456  1.00 11.05  ? 211 VAL A N   1 
ATOM   1668 C  CA  . VAL A 1 210 ? -14.078 -3.932  23.760  1.00 11.36  ? 211 VAL A CA  1 
ATOM   1669 C  C   . VAL A 1 210 ? -15.393 -4.636  24.011  1.00 10.84  ? 211 VAL A C   1 
ATOM   1670 O  O   . VAL A 1 210 ? -15.753 -4.859  25.174  1.00 11.97  ? 211 VAL A O   1 
ATOM   1671 C  CB  . VAL A 1 210 ? -12.890 -4.777  24.197  1.00 10.90  ? 211 VAL A CB  1 
ATOM   1672 C  CG1 . VAL A 1 210 ? -12.929 -6.162  23.527  1.00 12.72  ? 211 VAL A CG1 1 
ATOM   1673 C  CG2 . VAL A 1 210 ? -11.575 -4.050  23.922  1.00 13.55  ? 211 VAL A CG2 1 
ATOM   1674 N  N   . LEU A 1 211 ? -16.160 -4.893  22.965  1.00 12.59  ? 212 LEU A N   1 
ATOM   1675 C  CA  . LEU A 1 211 ? -17.462 -5.517  23.155  1.00 12.95  ? 212 LEU A CA  1 
ATOM   1676 C  C   . LEU A 1 211 ? -17.311 -6.988  23.534  1.00 13.28  ? 212 LEU A C   1 
ATOM   1677 O  O   . LEU A 1 211 ? -16.430 -7.691  23.050  1.00 13.14  ? 212 LEU A O   1 
ATOM   1678 C  CB  . LEU A 1 211 ? -18.293 -5.375  21.865  1.00 13.11  ? 212 LEU A CB  1 
ATOM   1679 C  CG  . LEU A 1 211 ? -18.617 -3.943  21.468  1.00 13.60  ? 212 LEU A CG  1 
ATOM   1680 C  CD1 . LEU A 1 211 ? -19.645 -3.989  20.326  1.00 16.22  ? 212 LEU A CD1 1 
ATOM   1681 C  CD2 . LEU A 1 211 ? -19.169 -3.134  22.634  1.00 14.83  ? 212 LEU A CD2 1 
ATOM   1682 N  N   . LYS A 1 212 ? -18.164 -7.412  24.470  1.00 13.39  ? 213 LYS A N   1 
ATOM   1683 C  CA  . LYS A 1 212 ? -18.111 -8.809  24.895  1.00 14.71  ? 213 LYS A CA  1 
ATOM   1684 C  C   . LYS A 1 212 ? -18.590 -9.774  23.816  1.00 13.59  ? 213 LYS A C   1 
ATOM   1685 O  O   . LYS A 1 212 ? -18.091 -10.874 23.717  1.00 16.39  ? 213 LYS A O   1 
ATOM   1686 C  CB  . LYS A 1 212 ? -18.994 -8.953  26.146  1.00 18.87  ? 213 LYS A CB  1 
ATOM   1687 C  CG  . LYS A 1 212 ? -19.306 -10.370 26.632  1.00 29.55  ? 213 LYS A CG  1 
ATOM   1688 C  CD  . LYS A 1 212 ? -20.383 -10.445 27.742  1.00 44.88  ? 213 LYS A CD  1 
ATOM   1689 N  N   . GLU A 1 213 ? -19.593 -9.370  23.052  1.00 13.26  ? 214 GLU A N   1 
ATOM   1690 C  CA  . GLU A 1 213 ? -20.192 -10.298 22.089  1.00 13.49  ? 214 GLU A CA  1 
ATOM   1691 C  C   . GLU A 1 213 ? -19.458 -10.197 20.768  1.00 12.65  ? 214 GLU A C   1 
ATOM   1692 O  O   . GLU A 1 213 ? -19.382 -9.113  20.144  1.00 13.78  ? 214 GLU A O   1 
ATOM   1693 C  CB  . GLU A 1 213 ? -21.629 -9.888  21.793  1.00 15.87  ? 214 GLU A CB  1 
ATOM   1694 C  CG  . GLU A 1 213 ? -22.410 -10.893 20.956  1.00 19.91  ? 214 GLU A CG  1 
ATOM   1695 C  CD  . GLU A 1 213 ? -23.833 -10.458 20.604  1.00 27.39  ? 214 GLU A CD  1 
ATOM   1696 O  OE1 . GLU A 1 213 ? -24.415 -9.668  21.373  1.00 21.43  ? 214 GLU A OE1 1 
ATOM   1697 O  OE2 . GLU A 1 213 ? -24.348 -10.913 19.564  1.00 45.89  ? 214 GLU A OE2 1 
ATOM   1698 N  N   A PRO A 1 214 ? -18.920 -11.318 20.252  0.50 11.77  ? 215 PRO A N   1 
ATOM   1699 N  N   B PRO A 1 214 ? -18.798 -11.276 20.299  0.50 11.93  ? 215 PRO A N   1 
ATOM   1700 C  CA  A PRO A 1 214 ? -18.256 -11.269 18.965  0.50 12.05  ? 215 PRO A CA  1 
ATOM   1701 C  CA  B PRO A 1 214 ? -18.217 -11.275 18.964  0.50 12.74  ? 215 PRO A CA  1 
ATOM   1702 C  C   A PRO A 1 214 ? -19.313 -11.144 17.874  0.50 12.90  ? 215 PRO A C   1 
ATOM   1703 C  C   B PRO A 1 214 ? -19.254 -11.319 17.846  0.50 14.19  ? 215 PRO A C   1 
ATOM   1704 O  O   A PRO A 1 214 ? -20.506 -11.374 18.125  0.50 14.94  ? 215 PRO A O   1 
ATOM   1705 O  O   B PRO A 1 214 ? -20.376 -11.817 18.047  0.50 14.22  ? 215 PRO A O   1 
ATOM   1706 C  CB  A PRO A 1 214 ? -17.565 -12.636 18.854  0.50 13.89  ? 215 PRO A CB  1 
ATOM   1707 C  CB  B PRO A 1 214 ? -17.448 -12.599 18.872  0.50 15.16  ? 215 PRO A CB  1 
ATOM   1708 C  CG  A PRO A 1 214 ? -18.415 -13.562 19.696  0.50 14.08  ? 215 PRO A CG  1 
ATOM   1709 C  CG  B PRO A 1 214 ? -17.357 -13.074 20.298  0.50 17.17  ? 215 PRO A CG  1 
ATOM   1710 C  CD  A PRO A 1 214 ? -19.036 -12.697 20.779  0.50 13.63  ? 215 PRO A CD  1 
ATOM   1711 C  CD  B PRO A 1 214 ? -18.588 -12.559 21.002  0.50 14.53  ? 215 PRO A CD  1 
ATOM   1712 N  N   . ILE A 1 215 ? -18.851 -10.852 16.654  1.00 13.16  ? 216 ILE A N   1 
ATOM   1713 C  CA  . ILE A 1 215 ? -19.668 -11.061 15.456  1.00 13.28  ? 216 ILE A CA  1 
ATOM   1714 C  C   . ILE A 1 215 ? -19.157 -12.331 14.809  1.00 13.67  ? 216 ILE A C   1 
ATOM   1715 O  O   . ILE A 1 215 ? -18.000 -12.698 14.939  1.00 14.84  ? 216 ILE A O   1 
ATOM   1716 C  CB  . ILE A 1 215 ? -19.670 -9.856  14.498  1.00 14.91  ? 216 ILE A CB  1 
ATOM   1717 C  CG1 . ILE A 1 215 ? -18.266 -9.510  13.977  1.00 13.91  ? 216 ILE A CG1 1 
ATOM   1718 C  CG2 . ILE A 1 215 ? -20.356 -8.646  15.157  1.00 15.68  ? 216 ILE A CG2 1 
ATOM   1719 C  CD1 . ILE A 1 215 ? -18.249 -8.544  12.810  1.00 16.15  ? 216 ILE A CD1 1 
ATOM   1720 N  N   . SER A 1 216 ? -20.073 -12.985 14.111  1.00 15.01  ? 217 SER A N   1 
ATOM   1721 C  CA  A SER A 1 216 ? -19.692 -14.137 13.302  0.50 15.66  ? 217 SER A CA  1 
ATOM   1722 C  CA  B SER A 1 216 ? -19.765 -14.142 13.297  0.50 15.85  ? 217 SER A CA  1 
ATOM   1723 C  C   . SER A 1 216 ? -19.488 -13.694 11.864  1.00 13.80  ? 217 SER A C   1 
ATOM   1724 O  O   . SER A 1 216 ? -20.314 -12.948 11.304  1.00 15.49  ? 217 SER A O   1 
ATOM   1725 C  CB  A SER A 1 216 ? -20.711 -15.252 13.303  0.50 17.20  ? 217 SER A CB  1 
ATOM   1726 C  CB  B SER A 1 216 ? -20.941 -15.065 13.315  0.50 18.41  ? 217 SER A CB  1 
ATOM   1727 O  OG  A SER A 1 216 ? -20.851 -15.822 14.581  0.50 18.47  ? 217 SER A OG  1 
ATOM   1728 O  OG  B SER A 1 216 ? -20.548 -16.291 12.766  0.50 21.14  ? 217 SER A OG  1 
ATOM   1729 N  N   . VAL A 1 217 ? -18.384 -14.169 11.266  1.00 13.19  ? 218 VAL A N   1 
ATOM   1730 C  CA  . VAL A 1 217 ? -18.111 -13.974 9.842   1.00 12.85  ? 218 VAL A CA  1 
ATOM   1731 C  C   . VAL A 1 217 ? -17.895 -15.351 9.282   1.00 13.68  ? 218 VAL A C   1 
ATOM   1732 O  O   . VAL A 1 217 ? -17.492 -16.292 9.960   1.00 14.55  ? 218 VAL A O   1 
ATOM   1733 C  CB  . VAL A 1 217 ? -16.925 -13.039 9.630   1.00 15.57  ? 218 VAL A CB  1 
ATOM   1734 C  CG1 . VAL A 1 217 ? -17.192 -11.688 10.327  1.00 15.80  ? 218 VAL A CG1 1 
ATOM   1735 C  CG2 . VAL A 1 217 ? -15.634 -13.662 10.150  1.00 16.43  ? 218 VAL A CG2 1 
ATOM   1736 N  N   . SER A 1 218 ? -18.022 -15.477 7.965   1.00 13.59  ? 219 SER A N   1 
ATOM   1737 C  CA  . SER A 1 218 ? -17.815 -16.794 7.378   1.00 15.02  ? 219 SER A CA  1 
ATOM   1738 C  C   . SER A 1 218 ? -16.341 -17.048 7.095   1.00 14.38  ? 219 SER A C   1 
ATOM   1739 O  O   . SER A 1 218 ? -15.536 -16.123 6.949   1.00 14.95  ? 219 SER A O   1 
ATOM   1740 C  CB  . SER A 1 218 ? -18.647 -16.998 6.145   1.00 15.97  ? 219 SER A CB  1 
ATOM   1741 O  OG  . SER A 1 218 ? -18.185 -16.116 5.136   1.00 16.78  ? 219 SER A OG  1 
ATOM   1742 N  N   A SER A 1 219 ? -16.017 -18.334 6.949   0.50 15.82  ? 220 SER A N   1 
ATOM   1743 N  N   B SER A 1 219 ? -15.988 -18.317 6.874   0.50 16.23  ? 220 SER A N   1 
ATOM   1744 C  CA  A SER A 1 219 ? -14.676 -18.679 6.538   0.50 16.22  ? 220 SER A CA  1 
ATOM   1745 C  CA  B SER A 1 219 ? -14.629 -18.662 6.499   0.50 16.73  ? 220 SER A CA  1 
ATOM   1746 C  C   A SER A 1 219 ? -14.344 -17.958 5.237   0.50 16.71  ? 220 SER A C   1 
ATOM   1747 C  C   B SER A 1 219 ? -14.290 -18.052 5.141   0.50 17.10  ? 220 SER A C   1 
ATOM   1748 O  O   A SER A 1 219 ? -13.264 -17.381 5.156   0.50 19.67  ? 220 SER A O   1 
ATOM   1749 O  O   B SER A 1 219 ? -13.160 -17.653 4.887   0.50 16.73  ? 220 SER A O   1 
ATOM   1750 C  CB  A SER A 1 219 ? -14.491 -20.168 6.455   0.50 17.98  ? 220 SER A CB  1 
ATOM   1751 C  CB  B SER A 1 219 ? -14.473 -20.158 6.498   0.50 20.28  ? 220 SER A CB  1 
ATOM   1752 O  OG  A SER A 1 219 ? -15.470 -20.737 5.595   0.50 16.78  ? 220 SER A OG  1 
ATOM   1753 O  OG  B SER A 1 219 ? -13.123 -20.542 6.330   0.50 26.93  ? 220 SER A OG  1 
ATOM   1754 N  N   . GLU A 1 220 ? -15.289 -17.908 4.263   1.00 16.05  ? 221 GLU A N   1 
ATOM   1755 C  CA  . GLU A 1 220 ? -14.981 -17.275 2.990   1.00 17.74  ? 221 GLU A CA  1 
ATOM   1756 C  C   . GLU A 1 220 ? -14.679 -15.776 3.175   1.00 15.47  ? 221 GLU A C   1 
ATOM   1757 O  O   . GLU A 1 220 ? -13.846 -15.244 2.420   1.00 18.02  ? 221 GLU A O   1 
ATOM   1758 C  CB  . GLU A 1 220 ? -16.149 -17.420 2.002   1.00 18.50  ? 221 GLU A CB  1 
ATOM   1759 C  CG  . GLU A 1 220 ? -16.425 -18.856 1.600   1.00 25.17  ? 221 GLU A CG  1 
ATOM   1760 C  CD  . GLU A 1 220 ? -17.350 -19.673 2.496   1.00 29.97  ? 221 GLU A CD  1 
ATOM   1761 O  OE1 . GLU A 1 220 ? -17.697 -19.240 3.581   1.00 25.10  ? 221 GLU A OE1 1 
ATOM   1762 O  OE2 . GLU A 1 220 ? -17.746 -20.770 2.077   1.00 44.14  ? 221 GLU A OE2 1 
ATOM   1763 N  N   . GLN A 1 221 ? -15.399 -15.120 4.109   1.00 15.60  ? 222 GLN A N   1 
ATOM   1764 C  CA  . GLN A 1 221 ? -15.123 -13.711 4.333   1.00 14.83  ? 222 GLN A CA  1 
ATOM   1765 C  C   . GLN A 1 221 ? -13.679 -13.509 4.823   1.00 16.49  ? 222 GLN A C   1 
ATOM   1766 O  O   . GLN A 1 221 ? -12.959 -12.640 4.368   1.00 15.99  ? 222 GLN A O   1 
ATOM   1767 C  CB  . GLN A 1 221 ? -16.158 -13.174 5.307   1.00 14.87  ? 222 GLN A CB  1 
ATOM   1768 C  CG  . GLN A 1 221 ? -17.493 -12.983 4.585   1.00 14.38  ? 222 GLN A CG  1 
ATOM   1769 C  CD  . GLN A 1 221 ? -18.608 -12.499 5.459   1.00 13.15  ? 222 GLN A CD  1 
ATOM   1770 O  OE1 . GLN A 1 221 ? -18.711 -12.849 6.651   1.00 14.05  ? 222 GLN A OE1 1 
ATOM   1771 N  NE2 . GLN A 1 221 ? -19.410 -11.589 4.906   1.00 14.80  ? 222 GLN A NE2 1 
ATOM   1772 N  N   . VAL A 1 222 ? -13.278 -14.293 5.835   1.00 16.13  ? 223 VAL A N   1 
ATOM   1773 C  CA  . VAL A 1 222 ? -11.963 -14.081 6.420   1.00 16.88  ? 223 VAL A CA  1 
ATOM   1774 C  C   . VAL A 1 222 ? -10.878 -14.532 5.415   1.00 17.37  ? 223 VAL A C   1 
ATOM   1775 O  O   . VAL A 1 222 ? -9.805  -13.934 5.335   1.00 17.13  ? 223 VAL A O   1 
ATOM   1776 C  CB  . VAL A 1 222 ? -11.849 -14.671 7.848   1.00 23.38  ? 223 VAL A CB  1 
ATOM   1777 C  CG1 . VAL A 1 222 ? -11.798 -16.175 7.785   1.00 29.46  ? 223 VAL A CG1 1 
ATOM   1778 C  CG2 . VAL A 1 222 ? -10.556 -14.144 8.464   1.00 23.79  ? 223 VAL A CG2 1 
ATOM   1779 N  N   . LEU A 1 223 ? -11.183 -15.552 4.568   1.00 18.26  ? 224 LEU A N   1 
ATOM   1780 C  CA  . LEU A 1 223 ? -10.239 -15.960 3.534   1.00 20.83  ? 224 LEU A CA  1 
ATOM   1781 C  C   . LEU A 1 223 ? -9.894  -14.796 2.615   1.00 18.36  ? 224 LEU A C   1 
ATOM   1782 O  O   . LEU A 1 223 ? -8.743  -14.670 2.189   1.00 19.50  ? 224 LEU A O   1 
ATOM   1783 C  CB  . LEU A 1 223 ? -10.739 -17.186 2.745   1.00 24.81  ? 224 LEU A CB  1 
ATOM   1784 C  CG  . LEU A 1 223 ? -10.567 -18.489 3.535   1.00 27.31  ? 224 LEU A CG  1 
ATOM   1785 C  CD2 . LEU A 1 223 ? -9.079  -18.870 3.678   1.00 34.40  ? 224 LEU A CD2 1 
ATOM   1786 N  N   . LYS A 1 224 ? -10.882 -13.954 2.346   1.00 17.12  ? 225 LYS A N   1 
ATOM   1787 C  CA  . LYS A 1 224 ? -10.627 -12.813 1.483   1.00 18.69  ? 225 LYS A CA  1 
ATOM   1788 C  C   . LYS A 1 224 ? -9.678  -11.781 2.133   1.00 16.27  ? 225 LYS A C   1 
ATOM   1789 O  O   . LYS A 1 224 ? -8.838  -11.191 1.473   1.00 17.37  ? 225 LYS A O   1 
ATOM   1790 C  CB  . LYS A 1 224 ? -11.970 -12.263 0.991   1.00 21.55  ? 225 LYS A CB  1 
ATOM   1791 C  CG  . LYS A 1 224 ? -12.656 -13.243 0.032   1.00 27.27  ? 225 LYS A CG  1 
ATOM   1792 C  CD  . LYS A 1 224 ? -13.928 -12.737 -0.652  1.00 35.80  ? 225 LYS A CD  1 
ATOM   1793 C  CE  . LYS A 1 224 ? -14.148 -13.174 -2.086  1.00 45.04  ? 225 LYS A CE  1 
ATOM   1794 N  NZ  . LYS A 1 224 ? -15.262 -14.156 -2.148  1.00 44.06  ? 225 LYS A NZ  1 
ATOM   1795 N  N   . PHE A 1 225 ? -9.779  -11.592 3.460   1.00 14.78  ? 226 PHE A N   1 
ATOM   1796 C  CA  . PHE A 1 225 ? -8.798  -10.742 4.148   1.00 13.41  ? 226 PHE A CA  1 
ATOM   1797 C  C   . PHE A 1 225 ? -7.389  -11.278 3.907   1.00 14.31  ? 226 PHE A C   1 
ATOM   1798 O  O   . PHE A 1 225 ? -6.438  -10.504 3.698   1.00 16.24  ? 226 PHE A O   1 
ATOM   1799 C  CB  . PHE A 1 225 ? -9.006  -10.787 5.666   1.00 15.34  ? 226 PHE A CB  1 
ATOM   1800 C  CG  . PHE A 1 225 ? -10.168 -10.018 6.226   1.00 16.08  ? 226 PHE A CG  1 
ATOM   1801 C  CD1 . PHE A 1 225 ? -11.149 -9.506  5.393   1.00 18.85  ? 226 PHE A CD1 1 
ATOM   1802 C  CD2 . PHE A 1 225 ? -10.285 -9.803  7.590   1.00 18.01  ? 226 PHE A CD2 1 
ATOM   1803 C  CE1 . PHE A 1 225 ? -12.222 -8.796  5.910   1.00 18.83  ? 226 PHE A CE1 1 
ATOM   1804 C  CE2 . PHE A 1 225 ? -11.358 -9.093  8.107   1.00 20.75  ? 226 PHE A CE2 1 
ATOM   1805 C  CZ  . PHE A 1 225 ? -12.323 -8.591  7.266   1.00 18.09  ? 226 PHE A CZ  1 
ATOM   1806 N  N   . ARG A 1 226 ? -7.237  -12.607 3.949   1.00 15.47  ? 227 ARG A N   1 
ATOM   1807 C  CA  . ARG A 1 226 ? -5.902  -13.201 3.879   1.00 16.37  ? 227 ARG A CA  1 
ATOM   1808 C  C   . ARG A 1 226 ? -5.319  -13.221 2.464   1.00 16.16  ? 227 ARG A C   1 
ATOM   1809 O  O   . ARG A 1 226 ? -4.175  -13.663 2.299   1.00 19.33  ? 227 ARG A O   1 
ATOM   1810 C  CB  . ARG A 1 226 ? -6.004  -14.657 4.386   1.00 15.90  ? 227 ARG A CB  1 
ATOM   1811 C  CG  . ARG A 1 226 ? -6.402  -14.777 5.854   1.00 15.23  ? 227 ARG A CG  1 
ATOM   1812 C  CD  . ARG A 1 226 ? -6.313  -16.196 6.315   1.00 17.82  ? 227 ARG A CD  1 
ATOM   1813 N  NE  . ARG A 1 226 ? -6.893  -16.355 7.653   1.00 16.44  ? 227 ARG A NE  1 
ATOM   1814 C  CZ  . ARG A 1 226 ? -7.809  -17.235 8.002   1.00 16.81  ? 227 ARG A CZ  1 
ATOM   1815 N  NH1 . ARG A 1 226 ? -8.214  -18.189 7.152   1.00 23.53  ? 227 ARG A NH1 1 
ATOM   1816 N  NH2 . ARG A 1 226 ? -8.290  -17.176 9.226   1.00 19.30  ? 227 ARG A NH2 1 
ATOM   1817 N  N   . LYS A 1 227 ? -6.053  -12.695 1.467   1.00 17.36  ? 228 LYS A N   1 
ATOM   1818 C  CA  . LYS A 1 227 ? -5.538  -12.622 0.137   1.00 18.13  ? 228 LYS A CA  1 
ATOM   1819 C  C   . LYS A 1 227 ? -4.876  -11.270 -0.086  1.00 17.52  ? 228 LYS A C   1 
ATOM   1820 O  O   . LYS A 1 227 ? -4.243  -11.099 -1.117  1.00 19.61  ? 228 LYS A O   1 
ATOM   1821 C  CB  . LYS A 1 227 ? -6.687  -12.844 -0.877  1.00 20.94  ? 228 LYS A CB  1 
ATOM   1822 C  CG  . LYS A 1 227 ? -7.121  -14.292 -1.048  1.00 27.62  ? 228 LYS A CG  1 
ATOM   1823 C  CD  . LYS A 1 227 ? -8.135  -14.497 -2.177  1.00 44.03  ? 228 LYS A CD  1 
ATOM   1824 N  N   . LEU A 1 228 ? -5.048  -10.310 0.829   1.00 16.38  ? 229 LEU A N   1 
ATOM   1825 C  CA  . LEU A 1 228 ? -4.365  -9.046  0.755   1.00 16.77  ? 229 LEU A CA  1 
ATOM   1826 C  C   . LEU A 1 228 ? -2.867  -9.257  0.895   1.00 17.70  ? 229 LEU A C   1 
ATOM   1827 O  O   . LEU A 1 228 ? -2.408  -10.305 1.321   1.00 18.10  ? 229 LEU A O   1 
ATOM   1828 C  CB  . LEU A 1 228 ? -4.865  -8.126  1.850   1.00 16.99  ? 229 LEU A CB  1 
ATOM   1829 C  CG  . LEU A 1 228 ? -6.307  -7.658  1.635   1.00 16.44  ? 229 LEU A CG  1 
ATOM   1830 C  CD1 . LEU A 1 228 ? -6.762  -7.013  2.936   1.00 16.25  ? 229 LEU A CD1 1 
ATOM   1831 C  CD2 . LEU A 1 228 ? -6.407  -6.696  0.437   1.00 20.09  ? 229 LEU A CD2 1 
ATOM   1832 N  N   . ASN A 1 229 ? -2.098  -8.274  0.414   1.00 18.59  ? 230 ASN A N   1 
ATOM   1833 C  CA  . ASN A 1 229 ? -0.643  -8.316  0.443   1.00 18.44  ? 230 ASN A CA  1 
ATOM   1834 C  C   . ASN A 1 229 ? -0.096  -7.166  1.286   1.00 19.72  ? 230 ASN A C   1 
ATOM   1835 O  O   . ASN A 1 229 ? -0.587  -6.042  1.235   1.00 18.56  ? 230 ASN A O   1 
ATOM   1836 C  CB  . ASN A 1 229 ? -0.088  -8.120  -0.965  1.00 19.90  ? 230 ASN A CB  1 
ATOM   1837 C  CG  . ASN A 1 229 ? -0.115  -9.338  -1.874  1.00 25.09  ? 230 ASN A CG  1 
ATOM   1838 O  OD1 . ASN A 1 229 ? 0.438   -9.260  -2.981  1.00 35.22  ? 230 ASN A OD1 1 
ATOM   1839 N  ND2 . ASN A 1 229 ? -0.799  -10.404 -1.483  1.00 29.07  ? 230 ASN A ND2 1 
ATOM   1840 N  N   . PHE A 1 230 ? 0.977   -7.471  2.054   1.00 18.48  ? 231 PHE A N   1 
ATOM   1841 C  CA  . PHE A 1 230 ? 1.663   -6.405  2.748   1.00 17.89  ? 231 PHE A CA  1 
ATOM   1842 C  C   . PHE A 1 230 ? 2.500   -5.550  1.804   1.00 20.38  ? 231 PHE A C   1 
ATOM   1843 O  O   . PHE A 1 230 ? 2.697   -4.355  2.041   1.00 23.00  ? 231 PHE A O   1 
ATOM   1844 C  CB  . PHE A 1 230 ? 2.663   -6.999  3.746   1.00 19.41  ? 231 PHE A CB  1 
ATOM   1845 C  CG  . PHE A 1 230 ? 2.082   -7.570  5.023   1.00 18.44  ? 231 PHE A CG  1 
ATOM   1846 C  CD1 . PHE A 1 230 ? 1.355   -6.768  5.906   1.00 19.19  ? 231 PHE A CD1 1 
ATOM   1847 C  CD2 . PHE A 1 230 ? 2.454   -8.865  5.444   1.00 20.26  ? 231 PHE A CD2 1 
ATOM   1848 C  CE1 . PHE A 1 230 ? 0.953   -7.268  7.140   1.00 18.93  ? 231 PHE A CE1 1 
ATOM   1849 C  CE2 . PHE A 1 230 ? 2.029   -9.360  6.664   1.00 20.48  ? 231 PHE A CE2 1 
ATOM   1850 C  CZ  . PHE A 1 230 ? 1.274   -8.559  7.512   1.00 19.36  ? 231 PHE A CZ  1 
ATOM   1851 N  N   . ASN A 1 231 ? 3.015   -6.173  0.733   1.00 21.75  ? 232 ASN A N   1 
ATOM   1852 C  CA  . ASN A 1 231 ? 3.960   -5.603  -0.222  1.00 24.48  ? 232 ASN A CA  1 
ATOM   1853 C  C   . ASN A 1 231 ? 3.208   -4.726  -1.215  1.00 25.93  ? 232 ASN A C   1 
ATOM   1854 O  O   . ASN A 1 231 ? 1.993   -4.862  -1.409  1.00 23.05  ? 232 ASN A O   1 
ATOM   1855 C  CB  . ASN A 1 231 ? 4.700   -6.730  -0.966  1.00 27.28  ? 232 ASN A CB  1 
ATOM   1856 C  CG  . ASN A 1 231 ? 3.707   -7.692  -1.602  1.00 24.79  ? 232 ASN A CG  1 
ATOM   1857 O  OD1 . ASN A 1 231 ? 3.130   -8.557  -0.923  1.00 25.41  ? 232 ASN A OD1 1 
ATOM   1858 N  ND2 . ASN A 1 231 ? 3.460   -7.507  -2.899  1.00 31.10  ? 232 ASN A ND2 1 
ATOM   1859 N  N   . GLY A 1 232 ? 3.947   -3.800  -1.837  1.00 26.01  ? 233 GLY A N   1 
ATOM   1860 C  CA  . GLY A 1 232 ? 3.406   -3.041  -2.964  1.00 28.53  ? 233 GLY A CA  1 
ATOM   1861 C  C   . GLY A 1 232 ? 3.415   -3.859  -4.254  1.00 29.31  ? 233 GLY A C   1 
ATOM   1862 O  O   . GLY A 1 232 ? 4.106   -4.882  -4.310  1.00 32.67  ? 233 GLY A O   1 
ATOM   1863 N  N   . GLU A 1 233 ? 2.635   -3.378  -5.259  1.00 35.39  ? 234 GLU A N   1 
ATOM   1864 C  CA  . GLU A 1 233 ? 2.495   -4.025  -6.564  1.00 41.98  ? 234 GLU A CA  1 
ATOM   1865 C  C   . GLU A 1 233 ? 3.901   -4.090  -7.167  1.00 42.89  ? 234 GLU A C   1 
ATOM   1866 O  O   . GLU A 1 233 ? 4.659   -3.127  -7.028  1.00 42.94  ? 234 GLU A O   1 
ATOM   1867 C  CB  . GLU A 1 233 ? 1.540   -3.193  -7.462  1.00 63.73  ? 234 GLU A CB  1 
ATOM   1868 C  CG  . GLU A 1 233 ? 1.265   -3.807  -8.895  1.00 74.37  ? 234 GLU A CG  1 
ATOM   1869 C  CD  . GLU A 1 233 ? 0.317   -2.931  -9.734  1.00 73.41  ? 234 GLU A CD  1 
ATOM   1870 O  OE1 . GLU A 1 233 ? 0.048   -1.787  -9.317  1.00 67.60  ? 234 GLU A OE1 1 
ATOM   1871 O  OE2 . GLU A 1 233 ? -0.139  -3.404  -10.794 1.00 68.19  ? 234 GLU A OE2 1 
ATOM   1872 N  N   . GLY A 1 234 ? 4.270   -5.283  -7.661  1.00 41.68  ? 235 GLY A N   1 
ATOM   1873 C  CA  . GLY A 1 234 ? 5.563   -5.512  -8.314  1.00 57.04  ? 235 GLY A CA  1 
ATOM   1874 C  C   . GLY A 1 234 ? 6.781   -5.578  -7.374  1.00 50.67  ? 235 GLY A C   1 
ATOM   1875 O  O   . GLY A 1 234 ? 7.910   -5.346  -7.783  1.00 53.07  ? 235 GLY A O   1 
ATOM   1876 N  N   . GLU A 1 235 ? 6.547   -5.830  -6.050  1.00 54.22  ? 236 GLU A N   1 
ATOM   1877 C  CA  . GLU A 1 235 ? 7.557   -6.304  -5.094  1.00 50.82  ? 236 GLU A CA  1 
ATOM   1878 C  C   . GLU A 1 235 ? 7.240   -7.765  -4.720  1.00 59.75  ? 236 GLU A C   1 
ATOM   1879 O  O   . GLU A 1 235 ? 6.144   -8.233  -4.916  1.00 64.43  ? 236 GLU A O   1 
ATOM   1880 C  CB  . GLU A 1 235 ? 7.503   -5.490  -3.775  1.00 47.78  ? 236 GLU A CB  1 
ATOM   1881 C  CG  . GLU A 1 235 ? 7.402   -3.974  -3.948  1.00 40.77  ? 236 GLU A CG  1 
ATOM   1882 C  CD  . GLU A 1 235 ? 7.286   -3.103  -2.682  1.00 52.06  ? 236 GLU A CD  1 
ATOM   1883 O  OE1 . GLU A 1 235 ? 6.858   -3.616  -1.577  1.00 52.61  ? 236 GLU A OE1 1 
ATOM   1884 O  OE2 . GLU A 1 235 ? 7.589   -1.890  -2.803  1.00 68.13  ? 236 GLU A OE2 1 
ATOM   1885 N  N   . PRO A 1 236 ? 8.158   -8.535  -3.993  1.00 53.86  ? 237 PRO A N   1 
ATOM   1886 C  CA  . PRO A 1 236 ? 7.873   -9.950  -3.615  1.00 46.52  ? 237 PRO A CA  1 
ATOM   1887 C  C   . PRO A 1 236 ? 6.640   -10.114 -2.729  1.00 31.17  ? 237 PRO A C   1 
ATOM   1888 O  O   . PRO A 1 236 ? 6.442   -9.313  -1.816  1.00 34.36  ? 237 PRO A O   1 
ATOM   1889 C  CB  . PRO A 1 236 ? 9.114   -10.400 -2.833  1.00 54.44  ? 237 PRO A CB  1 
ATOM   1890 C  CG  . PRO A 1 236 ? 10.217  -9.491  -3.347  1.00 49.60  ? 237 PRO A CG  1 
ATOM   1891 C  CD  . PRO A 1 236 ? 9.545   -8.144  -3.656  1.00 52.68  ? 237 PRO A CD  1 
ATOM   1892 N  N   . GLU A 1 237 ? 5.783   -11.110 -3.054  1.00 33.80  ? 238 GLU A N   1 
ATOM   1893 C  CA  . GLU A 1 237 ? 4.465   -11.272 -2.438  1.00 31.06  ? 238 GLU A CA  1 
ATOM   1894 C  C   . GLU A 1 237 ? 4.596   -11.810 -1.016  1.00 25.62  ? 238 GLU A C   1 
ATOM   1895 O  O   . GLU A 1 237 ? 5.178   -12.873 -0.805  1.00 31.13  ? 238 GLU A O   1 
ATOM   1896 C  CB  . GLU A 1 237 ? 3.586   -12.293 -3.191  1.00 34.15  ? 238 GLU A CB  1 
ATOM   1897 C  CG  . GLU A 1 237 ? 3.602   -12.134 -4.691  1.00 52.09  ? 238 GLU A CG  1 
ATOM   1898 C  CD  . GLU A 1 237 ? 3.691   -13.479 -5.393  1.00 62.65  ? 238 GLU A CD  1 
ATOM   1899 O  OE1 . GLU A 1 237 ? 4.812   -13.823 -5.878  1.00 52.52  ? 238 GLU A OE1 1 
ATOM   1900 O  OE2 . GLU A 1 237 ? 2.655   -14.191 -5.429  1.00 63.48  ? 238 GLU A OE2 1 
ATOM   1901 N  N   . GLU A 1 238 ? 3.997   -11.094 -0.064  1.00 26.17  ? 239 GLU A N   1 
ATOM   1902 C  CA  . GLU A 1 238 ? 3.904   -11.468 1.340   1.00 23.92  ? 239 GLU A CA  1 
ATOM   1903 C  C   . GLU A 1 238 ? 2.442   -11.278 1.723   1.00 20.77  ? 239 GLU A C   1 
ATOM   1904 O  O   . GLU A 1 238 ? 1.958   -10.152 1.760   1.00 22.79  ? 239 GLU A O   1 
ATOM   1905 C  CB  . GLU A 1 238 ? 4.809   -10.604 2.226   1.00 29.59  ? 239 GLU A CB  1 
ATOM   1906 N  N   . LEU A 1 239 ? 1.709   -12.371 1.942   1.00 20.03  ? 240 LEU A N   1 
ATOM   1907 C  CA  . LEU A 1 239 ? 0.310   -12.215 2.316   1.00 18.42  ? 240 LEU A CA  1 
ATOM   1908 C  C   . LEU A 1 239 ? 0.147   -11.432 3.617   1.00 17.01  ? 240 LEU A C   1 
ATOM   1909 O  O   . LEU A 1 239 ? 0.910   -11.614 4.586   1.00 18.70  ? 240 LEU A O   1 
ATOM   1910 C  CB  . LEU A 1 239 ? -0.303  -13.592 2.539   1.00 20.22  ? 240 LEU A CB  1 
ATOM   1911 C  CG  . LEU A 1 239 ? -0.432  -14.456 1.294   1.00 22.23  ? 240 LEU A CG  1 
ATOM   1912 C  CD1 . LEU A 1 239 ? -1.122  -15.747 1.709   1.00 29.66  ? 240 LEU A CD1 1 
ATOM   1913 C  CD2 . LEU A 1 239 ? -1.233  -13.700 0.221   1.00 28.01  ? 240 LEU A CD2 1 
ATOM   1914 N  N   . MET A 1 240 ? -0.869  -10.552 3.613   1.00 15.68  ? 241 MET A N   1 
ATOM   1915 C  CA  . MET A 1 240 ? -1.177  -9.771  4.798   1.00 16.30  ? 241 MET A CA  1 
ATOM   1916 C  C   . MET A 1 240 ? -2.010  -10.638 5.749   1.00 16.13  ? 241 MET A C   1 
ATOM   1917 O  O   . MET A 1 240 ? -3.218  -10.813 5.594   1.00 15.60  ? 241 MET A O   1 
ATOM   1918 C  CB  . MET A 1 240 ? -1.998  -8.544  4.386   1.00 18.06  ? 241 MET A CB  1 
ATOM   1919 C  CG  . MET A 1 240 ? -2.283  -7.584  5.585   1.00 16.43  ? 241 MET A CG  1 
ATOM   1920 S  SD  . MET A 1 240 ? -3.262  -6.179  5.076   1.00 17.89  ? 241 MET A SD  1 
ATOM   1921 C  CE  . MET A 1 240 ? -1.994  -5.188  4.283   1.00 19.32  ? 241 MET A CE  1 
ATOM   1922 N  N   . VAL A 1 241 ? -1.269  -11.297 6.663   1.00 15.30  ? 242 VAL A N   1 
ATOM   1923 C  CA  . VAL A 1 241 ? -1.871  -12.131 7.694   1.00 14.64  ? 242 VAL A CA  1 
ATOM   1924 C  C   . VAL A 1 241 ? -1.050  -11.926 8.950   1.00 13.33  ? 242 VAL A C   1 
ATOM   1925 O  O   . VAL A 1 241 ? 0.097   -11.488 8.877   1.00 14.69  ? 242 VAL A O   1 
ATOM   1926 C  CB  . VAL A 1 241 ? -1.856  -13.636 7.331   1.00 14.90  ? 242 VAL A CB  1 
ATOM   1927 C  CG1 . VAL A 1 241 ? -2.763  -13.957 6.124   1.00 17.93  ? 242 VAL A CG1 1 
ATOM   1928 C  CG2 . VAL A 1 241 ? -0.444  -14.156 7.093   1.00 16.86  ? 242 VAL A CG2 1 
ATOM   1929 N  N   . ASP A 1 242 ? -1.690  -12.176 10.083  1.00 12.87  ? 243 ASP A N   1 
ATOM   1930 C  CA  . ASP A 1 242 ? -1.013  -12.056 11.373  1.00 13.36  ? 243 ASP A CA  1 
ATOM   1931 C  C   . ASP A 1 242 ? -0.527  -10.624 11.622  1.00 12.52  ? 243 ASP A C   1 
ATOM   1932 O  O   . ASP A 1 242 ? 0.579   -10.394 12.124  1.00 14.46  ? 243 ASP A O   1 
ATOM   1933 C  CB  . ASP A 1 242 ? 0.066   -13.127 11.620  1.00 14.43  ? 243 ASP A CB  1 
ATOM   1934 C  CG  . ASP A 1 242 ? -0.556  -14.500 11.665  1.00 15.06  ? 243 ASP A CG  1 
ATOM   1935 O  OD1 . ASP A 1 242 ? -1.560  -14.666 12.340  1.00 15.16  ? 243 ASP A OD1 1 
ATOM   1936 O  OD2 . ASP A 1 242 ? 0.063   -15.429 11.106  1.00 17.32  ? 243 ASP A OD2 1 
ATOM   1937 N  N   . ASN A 1 243 ? -1.398  -9.671  11.322  1.00 12.01  ? 244 ASN A N   1 
ATOM   1938 C  CA  . ASN A 1 243 ? -1.122  -8.248  11.537  1.00 11.32  ? 244 ASN A CA  1 
ATOM   1939 C  C   . ASN A 1 243 ? -1.698  -7.797  12.880  1.00 12.38  ? 244 ASN A C   1 
ATOM   1940 O  O   . ASN A 1 243 ? -2.361  -6.777  12.946  1.00 13.43  ? 244 ASN A O   1 
ATOM   1941 C  CB  . ASN A 1 243 ? -1.608  -7.432  10.345  1.00 13.77  ? 244 ASN A CB  1 
ATOM   1942 C  CG  . ASN A 1 243 ? -3.087  -7.594  10.090  1.00 13.69  ? 244 ASN A CG  1 
ATOM   1943 O  OD1 . ASN A 1 243 ? -3.751  -8.453  10.655  1.00 14.04  ? 244 ASN A OD1 1 
ATOM   1944 N  ND2 . ASN A 1 243 ? -3.655  -6.692  9.290   1.00 16.74  ? 244 ASN A ND2 1 
ATOM   1945 N  N   . TRP A 1 244 ? -1.386  -8.535  13.928  1.00 12.01  ? 245 TRP A N   1 
ATOM   1946 C  CA  . TRP A 1 244 ? -1.844  -8.287  15.285  1.00 10.99  ? 245 TRP A CA  1 
ATOM   1947 C  C   . TRP A 1 244 ? -0.624  -8.179  16.177  1.00 11.76  ? 245 TRP A C   1 
ATOM   1948 O  O   . TRP A 1 244 ? 0.327   -8.931  16.061  1.00 13.16  ? 245 TRP A O   1 
ATOM   1949 C  CB  . TRP A 1 244 ? -2.829  -9.376  15.753  1.00 11.39  ? 245 TRP A CB  1 
ATOM   1950 C  CG  . TRP A 1 244 ? -2.359  -10.776 15.597  1.00 12.08  ? 245 TRP A CG  1 
ATOM   1951 C  CD1 . TRP A 1 244 ? -2.464  -11.523 14.451  1.00 13.00  ? 245 TRP A CD1 1 
ATOM   1952 C  CD2 . TRP A 1 244 ? -1.749  -11.627 16.564  1.00 12.64  ? 245 TRP A CD2 1 
ATOM   1953 N  NE1 . TRP A 1 244 ? -1.959  -12.783 14.609  1.00 12.90  ? 245 TRP A NE1 1 
ATOM   1954 C  CE2 . TRP A 1 244 ? -1.552  -12.887 15.933  1.00 12.42  ? 245 TRP A CE2 1 
ATOM   1955 C  CE3 . TRP A 1 244 ? -1.436  -11.488 17.935  1.00 13.89  ? 245 TRP A CE3 1 
ATOM   1956 C  CZ2 . TRP A 1 244 ? -0.946  -13.969 16.612  1.00 14.19  ? 245 TRP A CZ2 1 
ATOM   1957 C  CZ3 . TRP A 1 244 ? -0.880  -12.555 18.611  1.00 15.01  ? 245 TRP A CZ3 1 
ATOM   1958 C  CH2 . TRP A 1 244 ? -0.666  -13.776 17.944  1.00 15.03  ? 245 TRP A CH2 1 
ATOM   1959 N  N   . ARG A 1 245 ? -0.753  -7.236  17.126  1.00 12.55  ? 246 ARG A N   1 
ATOM   1960 C  CA  . ARG A 1 245 ? 0.225   -7.151  18.208  1.00 12.74  ? 246 ARG A CA  1 
ATOM   1961 C  C   . ARG A 1 245 ? -0.247  -8.059  19.332  1.00 12.06  ? 246 ARG A C   1 
ATOM   1962 O  O   . ARG A 1 245 ? -1.426  -8.074  19.681  1.00 13.62  ? 246 ARG A O   1 
ATOM   1963 C  CB  . ARG A 1 245 ? 0.264   -5.697  18.703  1.00 11.55  ? 246 ARG A CB  1 
ATOM   1964 C  CG  . ARG A 1 245 ? 1.413   -5.462  19.704  1.00 12.93  ? 246 ARG A CG  1 
ATOM   1965 C  CD  . ARG A 1 245 ? 1.273   -4.111  20.365  1.00 12.85  ? 246 ARG A CD  1 
ATOM   1966 N  NE  . ARG A 1 245 ? 2.543   -3.771  21.042  1.00 12.66  ? 246 ARG A NE  1 
ATOM   1967 C  CZ  . ARG A 1 245 ? 2.705   -2.743  21.868  1.00 12.91  ? 246 ARG A CZ  1 
ATOM   1968 N  NH1 . ARG A 1 245 ? 1.688   -1.941  22.132  1.00 14.77  ? 246 ARG A NH1 1 
ATOM   1969 N  NH2 . ARG A 1 245 ? 3.882   -2.521  22.426  1.00 14.94  ? 246 ARG A NH2 1 
ATOM   1970 N  N   . PRO A 1 246 ? 0.647   -8.860  19.934  1.00 13.61  ? 247 PRO A N   1 
ATOM   1971 C  CA  . PRO A 1 246 ? 0.238   -9.663  21.080  1.00 14.47  ? 247 PRO A CA  1 
ATOM   1972 C  C   . PRO A 1 246 ? -0.126  -8.831  22.307  1.00 12.81  ? 247 PRO A C   1 
ATOM   1973 O  O   . PRO A 1 246 ? 0.218   -7.644  22.447  1.00 13.29  ? 247 PRO A O   1 
ATOM   1974 C  CB  . PRO A 1 246 ? 1.471   -10.510 21.385  1.00 17.18  ? 247 PRO A CB  1 
ATOM   1975 C  CG  . PRO A 1 246 ? 2.325   -10.411 20.175  1.00 22.69  ? 247 PRO A CG  1 
ATOM   1976 C  CD  . PRO A 1 246 ? 2.043   -9.056  19.574  1.00 15.61  ? 247 PRO A CD  1 
ATOM   1977 N  N   . ALA A 1 247 ? -0.747  -9.497  23.281  1.00 13.74  ? 248 ALA A N   1 
ATOM   1978 C  CA  . ALA A 1 247 ? -1.125  -8.900  24.547  1.00 13.54  ? 248 ALA A CA  1 
ATOM   1979 C  C   . ALA A 1 247 ? 0.133   -8.362  25.252  1.00 13.22  ? 248 ALA A C   1 
ATOM   1980 O  O   . ALA A 1 247 ? 1.187   -9.008  25.312  1.00 15.83  ? 248 ALA A O   1 
ATOM   1981 C  CB  . ALA A 1 247 ? -1.851  -9.901  25.445  1.00 18.13  ? 248 ALA A CB  1 
ATOM   1982 N  N   . GLN A 1 248 ? -0.012  -7.170  25.825  1.00 13.64  ? 249 GLN A N   1 
ATOM   1983 C  CA  . GLN A 1 248 ? 1.047   -6.449  26.529  1.00 13.31  ? 249 GLN A CA  1 
ATOM   1984 C  C   . GLN A 1 248 ? 0.699   -6.476  28.013  1.00 13.94  ? 249 GLN A C   1 
ATOM   1985 O  O   . GLN A 1 248 ? -0.439  -6.668  28.463  1.00 15.01  ? 249 GLN A O   1 
ATOM   1986 C  CB  . GLN A 1 248 ? 1.052   -5.008  26.040  1.00 13.47  ? 249 GLN A CB  1 
ATOM   1987 C  CG  . GLN A 1 248 ? 1.379   -4.931  24.536  1.00 14.10  ? 249 GLN A CG  1 
ATOM   1988 C  CD  . GLN A 1 248 ? 2.684   -5.630  24.211  1.00 15.19  ? 249 GLN A CD  1 
ATOM   1989 O  OE1 . GLN A 1 248 ? 3.742   -5.287  24.762  1.00 19.18  ? 249 GLN A OE1 1 
ATOM   1990 N  NE2 . GLN A 1 248 ? 2.694   -6.559  23.251  1.00 15.88  ? 249 GLN A NE2 1 
ATOM   1991 N  N   . PRO A 1 249 ? 1.717   -6.173  28.858  1.00 16.22  ? 250 PRO A N   1 
ATOM   1992 C  CA  . PRO A 1 249 ? 1.511   -6.205  30.294  1.00 17.03  ? 250 PRO A CA  1 
ATOM   1993 C  C   . PRO A 1 249 ? 0.428   -5.219  30.748  1.00 14.48  ? 250 PRO A C   1 
ATOM   1994 O  O   . PRO A 1 249 ? 0.469   -4.043  30.425  1.00 16.54  ? 250 PRO A O   1 
ATOM   1995 C  CB  . PRO A 1 249 ? 2.899   -5.787  30.813  1.00 21.46  ? 250 PRO A CB  1 
ATOM   1996 C  CG  . PRO A 1 249 ? 3.841   -6.335  29.782  1.00 24.58  ? 250 PRO A CG  1 
ATOM   1997 C  CD  . PRO A 1 249 ? 3.128   -5.947  28.506  1.00 20.85  ? 250 PRO A CD  1 
ATOM   1998 N  N   . LEU A 1 250 ? -0.459  -5.682  31.626  1.00 16.25  ? 251 LEU A N   1 
ATOM   1999 C  CA  . LEU A 1 250 ? -1.536  -4.854  32.150  1.00 15.52  ? 251 LEU A CA  1 
ATOM   2000 C  C   . LEU A 1 250 ? -0.987  -3.786  33.089  1.00 15.11  ? 251 LEU A C   1 
ATOM   2001 O  O   . LEU A 1 250 ? -1.502  -2.677  33.168  1.00 16.42  ? 251 LEU A O   1 
ATOM   2002 C  CB  . LEU A 1 250 ? -2.571  -5.751  32.832  1.00 20.28  ? 251 LEU A CB  1 
ATOM   2003 C  CG  . LEU A 1 250 ? -3.851  -5.048  33.283  1.00 19.53  ? 251 LEU A CG  1 
ATOM   2004 C  CD1 . LEU A 1 250 ? -4.581  -4.440  32.089  1.00 19.26  ? 251 LEU A CD1 1 
ATOM   2005 C  CD2 . LEU A 1 250 ? -4.745  -6.019  34.062  1.00 23.86  ? 251 LEU A CD2 1 
ATOM   2006 N  N   . LYS A 1 251 ? 0.118   -4.092  33.798  1.00 16.82  ? 252 LYS A N   1 
ATOM   2007 C  CA  . LYS A 1 251 ? 0.731   -3.089  34.681  1.00 18.50  ? 252 LYS A CA  1 
ATOM   2008 C  C   . LYS A 1 251 ? -0.279  -2.564  35.709  1.00 18.84  ? 252 LYS A C   1 
ATOM   2009 O  O   . LYS A 1 251 ? -1.053  -3.339  36.246  1.00 23.10  ? 252 LYS A O   1 
ATOM   2010 C  CB  . LYS A 1 251 ? 1.536   -2.022  33.936  1.00 20.91  ? 252 LYS A CB  1 
ATOM   2011 C  CG  . LYS A 1 251 ? 2.651   -2.671  33.135  1.00 24.56  ? 252 LYS A CG  1 
ATOM   2012 C  CD  . LYS A 1 251 ? 3.626   -1.771  32.513  1.00 28.62  ? 252 LYS A CD  1 
ATOM   2013 C  CE  . LYS A 1 251 ? 4.841   -2.519  32.009  1.00 31.29  ? 252 LYS A CE  1 
ATOM   2014 N  NZ  . LYS A 1 251 ? 5.709   -1.592  31.238  1.00 31.41  ? 252 LYS A NZ  1 
ATOM   2015 N  N   . ASN A 1 252 ? -0.311  -1.241  35.908  1.00 17.30  ? 253 ASN A N   1 
ATOM   2016 C  CA  . ASN A 1 252 ? -1.168  -0.775  36.978  1.00 25.93  ? 253 ASN A CA  1 
ATOM   2017 C  C   . ASN A 1 252 ? -2.495  -0.366  36.348  1.00 31.98  ? 253 ASN A C   1 
ATOM   2018 O  O   . ASN A 1 252 ? -2.751  0.869   36.315  1.00 35.28  ? 253 ASN A O   1 
ATOM   2019 C  CB  . ASN A 1 252 ? -0.479  0.376   37.721  1.00 32.86  ? 253 ASN A CB  1 
ATOM   2020 C  CG  . ASN A 1 252 ? -1.257  1.023   38.855  1.00 39.22  ? 253 ASN A CG  1 
ATOM   2021 O  OD1 . ASN A 1 252 ? -1.877  0.342   39.670  1.00 55.79  ? 253 ASN A OD1 1 
ATOM   2022 N  ND2 . ASN A 1 252 ? -1.224  2.352   38.923  1.00 39.68  ? 253 ASN A ND2 1 
ATOM   2023 N  N   . ARG A 1 253 ? -3.217  -1.346  35.701  1.00 18.94  ? 254 ARG A N   1 
ATOM   2024 C  CA  . ARG A 1 253 ? -4.531  -1.002  35.184  1.00 15.76  ? 254 ARG A CA  1 
ATOM   2025 C  C   . ARG A 1 253 ? -5.582  -1.986  35.659  1.00 17.32  ? 254 ARG A C   1 
ATOM   2026 O  O   . ARG A 1 253 ? -5.325  -3.166  35.851  1.00 24.23  ? 254 ARG A O   1 
ATOM   2027 C  CB  . ARG A 1 253 ? -4.460  -0.934  33.657  1.00 14.54  ? 254 ARG A CB  1 
ATOM   2028 C  CG  . ARG A 1 253 ? -3.569  0.219   33.187  1.00 13.71  ? 254 ARG A CG  1 
ATOM   2029 C  CD  . ARG A 1 253 ? -3.453  0.180   31.701  1.00 14.75  ? 254 ARG A CD  1 
ATOM   2030 N  NE  . ARG A 1 253 ? -2.656  -0.942  31.210  1.00 13.61  ? 254 ARG A NE  1 
ATOM   2031 C  CZ  . ARG A 1 253 ? -2.400  -1.188  29.927  1.00 12.01  ? 254 ARG A CZ  1 
ATOM   2032 N  NH1 . ARG A 1 253 ? -3.012  -0.504  28.966  1.00 13.06  ? 254 ARG A NH1 1 
ATOM   2033 N  NH2 . ARG A 1 253 ? -1.592  -2.198  29.640  1.00 12.46  ? 254 ARG A NH2 1 
ATOM   2034 N  N   . GLN A 1 254 ? -6.802  -1.473  35.764  1.00 18.22  ? 255 GLN A N   1 
ATOM   2035 C  CA  . GLN A 1 254 ? -7.987  -2.258  36.017  1.00 19.62  ? 255 GLN A CA  1 
ATOM   2036 C  C   . GLN A 1 254 ? -8.827  -2.184  34.742  1.00 19.23  ? 255 GLN A C   1 
ATOM   2037 O  O   . GLN A 1 254 ? -9.000  -1.143  34.110  1.00 23.24  ? 255 GLN A O   1 
ATOM   2038 C  CB  . GLN A 1 254 ? -8.885  -1.669  37.120  1.00 24.92  ? 255 GLN A CB  1 
ATOM   2039 N  N   . ILE A 1 255 ? -9.358  -3.331  34.377  1.00 15.15  ? 256 ILE A N   1 
ATOM   2040 C  CA  . ILE A 1 255 ? -10.326 -3.439  33.303  1.00 14.22  ? 256 ILE A CA  1 
ATOM   2041 C  C   . ILE A 1 255 ? -11.686 -3.427  33.979  1.00 16.31  ? 256 ILE A C   1 
ATOM   2042 O  O   . ILE A 1 255 ? -11.900 -4.162  34.956  1.00 17.31  ? 256 ILE A O   1 
ATOM   2043 C  CB  . ILE A 1 255 ? -10.111 -4.722  32.488  1.00 15.02  ? 256 ILE A CB  1 
ATOM   2044 C  CG1 . ILE A 1 255 ? -8.683  -4.733  31.925  1.00 17.43  ? 256 ILE A CG1 1 
ATOM   2045 C  CG2 . ILE A 1 255 ? -11.171 -4.755  31.393  1.00 16.83  ? 256 ILE A CG2 1 
ATOM   2046 C  CD1 . ILE A 1 255 ? -8.425  -5.942  31.074  1.00 18.87  ? 256 ILE A CD1 1 
ATOM   2047 N  N   . LYS A 1 256 ? -12.562 -2.548  33.503  1.00 14.03  ? 257 LYS A N   1 
ATOM   2048 C  CA  . LYS A 1 256 ? -13.918 -2.443  34.032  1.00 14.65  ? 257 LYS A CA  1 
ATOM   2049 C  C   . LYS A 1 256 ? -14.892 -3.111  33.068  1.00 13.88  ? 257 LYS A C   1 
ATOM   2050 O  O   . LYS A 1 256 ? -14.722 -3.038  31.857  1.00 15.95  ? 257 LYS A O   1 
ATOM   2051 C  CB  . LYS A 1 256 ? -14.274 -0.968  34.248  1.00 17.62  ? 257 LYS A CB  1 
ATOM   2052 C  CG  . LYS A 1 256 ? -13.370 -0.296  35.305  1.00 25.97  ? 257 LYS A CG  1 
ATOM   2053 C  CD  . LYS A 1 256 ? -13.896 1.064   35.668  1.00 37.23  ? 257 LYS A CD  1 
ATOM   2054 N  N   . ALA A 1 257 ? -15.944 -3.716  33.600  1.00 15.42  ? 258 ALA A N   1 
ATOM   2055 C  CA  . ALA A 1 257 ? -17.018 -4.325  32.824  1.00 16.94  ? 258 ALA A CA  1 
ATOM   2056 C  C   . ALA A 1 257 ? -18.268 -3.484  32.980  1.00 15.77  ? 258 ALA A C   1 
ATOM   2057 O  O   . ALA A 1 257 ? -18.593 -3.059  34.090  1.00 16.34  ? 258 ALA A O   1 
ATOM   2058 C  CB  . ALA A 1 257 ? -17.188 -5.757  33.268  1.00 18.38  ? 258 ALA A CB  1 
ATOM   2059 N  N   . SER A 1 258 ? -19.072 -3.388  31.909  1.00 15.43  ? 259 SER A N   1 
ATOM   2060 C  CA  . SER A 1 258 ? -20.328 -2.656  31.932  1.00 16.04  ? 259 SER A CA  1 
ATOM   2061 C  C   . SER A 1 258 ? -21.471 -3.579  32.392  1.00 16.78  ? 259 SER A C   1 
ATOM   2062 O  O   . SER A 1 258 ? -22.600 -3.099  32.475  1.00 22.74  ? 259 SER A O   1 
ATOM   2063 C  CB  . SER A 1 258 ? -20.599 -2.073  30.558  1.00 18.43  ? 259 SER A CB  1 
ATOM   2064 O  OG  . SER A 1 258 ? -21.068 -3.087  29.664  1.00 17.40  ? 259 SER A OG  1 
ATOM   2065 N  N   . PHE A 1 259 ? -21.173 -4.880  32.645  1.00 17.49  ? 260 PHE A N   1 
ATOM   2066 C  CA  . PHE A 1 259 ? -22.188 -5.930  32.788  1.00 21.44  ? 260 PHE A CA  1 
ATOM   2067 C  C   . PHE A 1 259 ? -21.756 -6.880  33.907  1.00 31.10  ? 260 PHE A C   1 
ATOM   2068 O  O   . PHE A 1 259 ? -20.548 -6.966  34.215  1.00 24.37  ? 260 PHE A O   1 
ATOM   2069 C  CB  . PHE A 1 259 ? -22.420 -6.662  31.456  1.00 22.21  ? 260 PHE A CB  1 
ATOM   2070 C  CG  . PHE A 1 259 ? -21.152 -7.348  31.010  1.00 21.26  ? 260 PHE A CG  1 
ATOM   2071 C  CD1 . PHE A 1 259 ? -20.173 -6.649  30.304  1.00 17.94  ? 260 PHE A CD1 1 
ATOM   2072 C  CD2 . PHE A 1 259 ? -20.907 -8.683  31.353  1.00 23.22  ? 260 PHE A CD2 1 
ATOM   2073 C  CE1 . PHE A 1 259 ? -18.959 -7.277  29.982  1.00 20.57  ? 260 PHE A CE1 1 
ATOM   2074 C  CE2 . PHE A 1 259 ? -19.709 -9.308  31.043  1.00 24.80  ? 260 PHE A CE2 1 
ATOM   2075 C  CZ  . PHE A 1 259 ? -18.744 -8.603  30.327  1.00 25.13  ? 260 PHE A CZ  1 
ATOM   2076 N  N   . LYS A 1 260 ? -22.789 -7.529  34.492  1.00 45.34  ? 261 LYS A N   1 
ATOM   2077 C  CA  . LYS A 1 260 ? -22.782 -8.797  35.220  1.00 60.24  ? 261 LYS A CA  1 
ATOM   2078 C  C   . LYS A 1 260 ? -21.560 -8.908  36.141  1.00 80.97  ? 261 LYS A C   1 
ATOM   2079 O  O   . LYS A 1 260 ? -21.667 -8.608  37.345  1.00 103.04 ? 261 LYS A O   1 
ATOM   2080 C  CB  . LYS A 1 260 ? -22.916 -9.998  34.257  1.00 72.46  ? 261 LYS A CB  1 
ATOM   2081 O  OXT . LYS A 1 260 ? -20.468 -9.311  35.704  1.00 94.24  ? 261 LYS A OXT 1 
HETATM 2082 ZN ZN  . ZN  B 2 .   ? -6.397  -1.752  15.315  1.00 11.57  ? 301 ZN  A ZN  1 
HETATM 2083 S  S   . DMS C 3 .   ? 1.640   -11.649 14.927  1.00 31.03  ? 302 DMS A S   1 
HETATM 2084 O  O   . DMS C 3 .   ? 2.121   -13.071 14.479  1.00 41.56  ? 302 DMS A O   1 
HETATM 2085 C  C1  . DMS C 3 .   ? 2.000   -11.476 16.638  1.00 27.07  ? 302 DMS A C1  1 
HETATM 2086 C  C2  . DMS C 3 .   ? 2.896   -10.544 14.337  1.00 39.25  ? 302 DMS A C2  1 
HETATM 2087 F  F27 . WWO D 4 .   ? -5.850  3.608   15.976  1.00 18.82  ? 303 WWO A F27 1 
HETATM 2088 C  C5  . WWO D 4 .   ? -5.125  2.942   15.032  1.00 18.04  ? 303 WWO A C5  1 
HETATM 2089 C  C4  . WWO D 4 .   ? -4.894  1.536   15.178  1.00 15.01  ? 303 WWO A C4  1 
HETATM 2090 S  S7  . WWO D 4 .   ? -5.538  0.811   16.669  1.00 13.34  ? 303 WWO A S7  1 
HETATM 2091 O  O9  . WWO D 4 .   ? -6.910  1.155   16.582  1.00 13.65  ? 303 WWO A O9  1 
HETATM 2092 N  N10 . WWO D 4 .   ? -5.281  -0.705  16.474  1.00 13.13  ? 303 WWO A N10 1 
HETATM 2093 O  O8  . WWO D 4 .   ? -4.752  1.302   17.759  1.00 14.45  ? 303 WWO A O8  1 
HETATM 2094 C  C3  . WWO D 4 .   ? -4.179  0.917   14.205  1.00 15.22  ? 303 WWO A C3  1 
HETATM 2095 F  F12 . WWO D 4 .   ? -3.923  -0.426  14.240  1.00 18.58  ? 303 WWO A F12 1 
HETATM 2096 C  C2  . WWO D 4 .   ? -3.735  1.536   13.107  1.00 20.13  ? 303 WWO A C2  1 
HETATM 2097 F  F13 . WWO D 4 .   ? -3.057  0.884   12.164  1.00 24.70  ? 303 WWO A F13 1 
HETATM 2098 C  C6  . WWO D 4 .   ? -4.679  3.611   13.916  1.00 21.23  ? 303 WWO A C6  1 
HETATM 2099 C  C1  . WWO D 4 .   ? -3.966  2.912   12.925  1.00 19.77  ? 303 WWO A C1  1 
HETATM 2100 S  S11 . WWO D 4 .   ? -3.276  3.689   11.460  1.00 25.82  ? 303 WWO A S11 1 
HETATM 2101 O  O22 . WWO D 4 .   ? -3.880  5.055   11.244  1.00 35.19  ? 303 WWO A O22 1 
HETATM 2102 O  O23 . WWO D 4 .   ? -3.497  2.741   10.375  1.00 28.89  ? 303 WWO A O23 1 
HETATM 2103 C  C21 . WWO D 4 .   ? -1.475  3.727   11.605  1.00 34.30  ? 303 WWO A C21 1 
HETATM 2104 C  C24 . WWO D 4 .   ? -1.035  4.705   12.684  1.00 48.24  ? 303 WWO A C24 1 
HETATM 2105 O  O25 . WWO D 4 .   ? -0.882  4.065   13.934  1.00 39.32  ? 303 WWO A O25 1 
HETATM 2106 N  N26 . WWO D 4 .   ? -4.943  5.015   13.773  1.00 23.82  ? 303 WWO A N26 1 
HETATM 2107 C  C14 . WWO D 4 .   ? -5.034  5.909   14.941  1.00 25.42  ? 303 WWO A C14 1 
HETATM 2108 C  C15 . WWO D 4 .   ? -5.071  7.316   14.529  1.00 26.85  ? 303 WWO A C15 1 
HETATM 2109 C  C20 . WWO D 4 .   ? -4.073  8.171   15.067  1.00 25.36  ? 303 WWO A C20 1 
HETATM 2110 C  C19 . WWO D 4 .   ? -4.036  9.534   14.675  1.00 29.65  ? 303 WWO A C19 1 
HETATM 2111 C  C18 . WWO D 4 .   ? -4.991  10.021  13.778  1.00 29.30  ? 303 WWO A C18 1 
HETATM 2112 C  C17 . WWO D 4 .   ? -5.987  9.209   13.248  1.00 31.47  ? 303 WWO A C17 1 
HETATM 2113 C  C16 . WWO D 4 .   ? -6.042  7.834   13.603  1.00 32.45  ? 303 WWO A C16 1 
HETATM 2114 F  F27 . WWO E 4 .   ? -25.242 -1.892  7.143   1.00 37.70  ? 304 WWO A F27 1 
HETATM 2115 C  C5  . WWO E 4 .   ? -25.668 -3.057  6.610   1.00 39.75  ? 304 WWO A C5  1 
HETATM 2116 C  C4  . WWO E 4 .   ? -25.122 -3.425  5.377   1.00 37.98  ? 304 WWO A C4  1 
HETATM 2117 S  S7  . WWO E 4 .   ? -23.702 -2.438  4.843   1.00 42.99  ? 304 WWO A S7  1 
HETATM 2118 O  O9  . WWO E 4 .   ? -23.688 -0.935  4.253   1.00 31.92  ? 304 WWO A O9  1 
HETATM 2119 N  N10 . WWO E 4 .   ? -22.732 -2.741  6.463   1.00 28.15  ? 304 WWO A N10 1 
HETATM 2120 O  O8  . WWO E 4 .   ? -22.961 -3.292  3.789   1.00 34.83  ? 304 WWO A O8  1 
HETATM 2121 C  C3  . WWO E 4 .   ? -25.472 -4.633  4.803   1.00 35.47  ? 304 WWO A C3  1 
HETATM 2122 F  F12 . WWO E 4 .   ? -24.943 -5.069  3.610   1.00 41.77  ? 304 WWO A F12 1 
HETATM 2123 C  C2  . WWO E 4 .   ? -26.457 -5.383  5.428   1.00 35.30  ? 304 WWO A C2  1 
HETATM 2124 F  F13 . WWO E 4 .   ? -26.831 -6.502  4.825   1.00 36.16  ? 304 WWO A F13 1 
HETATM 2125 C  C6  . WWO E 4 .   ? -26.670 -3.790  7.264   1.00 43.07  ? 304 WWO A C6  1 
HETATM 2126 C  C1  . WWO E 4 .   ? -27.076 -4.978  6.620   1.00 45.77  ? 304 WWO A C1  1 
HETATM 2127 S  S11 . WWO E 4 .   ? -28.290 -6.081  7.317   1.00 44.03  ? 304 WWO A S11 1 
HETATM 2128 O  O22 . WWO E 4 .   ? -28.695 -5.559  8.731   1.00 73.99  ? 304 WWO A O22 1 
HETATM 2129 O  O23 . WWO E 4 .   ? -27.419 -7.314  7.596   1.00 55.42  ? 304 WWO A O23 1 
HETATM 2130 C  C21 . WWO E 4 .   ? -29.862 -6.617  6.509   1.00 54.46  ? 304 WWO A C21 1 
HETATM 2131 C  C24 . WWO E 4 .   ? -30.415 -5.589  5.522   1.00 69.89  ? 304 WWO A C24 1 
HETATM 2132 O  O25 . WWO E 4 .   ? -30.532 -4.312  6.096   1.00 80.64  ? 304 WWO A O25 1 
HETATM 2133 N  N26 . WWO E 4 .   ? -27.276 -3.374  8.497   1.00 50.67  ? 304 WWO A N26 1 
HETATM 2134 C  C14 . WWO E 4 .   ? -27.205 -2.044  9.094   1.00 37.38  ? 304 WWO A C14 1 
HETATM 2135 C  C15 . WWO E 4 .   ? -28.011 -1.983  10.349  1.00 50.01  ? 304 WWO A C15 1 
HETATM 2136 C  C20 . WWO E 4 .   ? -28.967 -0.897  10.467  1.00 58.55  ? 304 WWO A C20 1 
HETATM 2137 C  C19 . WWO E 4 .   ? -29.769 -0.821  11.628  1.00 67.77  ? 304 WWO A C19 1 
HETATM 2138 C  C18 . WWO E 4 .   ? -29.618 -1.818  12.668  1.00 70.80  ? 304 WWO A C18 1 
HETATM 2139 C  C17 . WWO E 4 .   ? -28.638 -2.891  12.564  1.00 57.69  ? 304 WWO A C17 1 
HETATM 2140 C  C16 . WWO E 4 .   ? -27.843 -2.983  11.388  1.00 51.08  ? 304 WWO A C16 1 
HETATM 2141 O  O   . HOH F 5 .   ? -15.079 19.296  13.187  1.00 36.46  ? 401 HOH A O   1 
HETATM 2142 O  O   . HOH F 5 .   ? -25.336 -10.555 17.605  1.00 33.01  ? 402 HOH A O   1 
HETATM 2143 O  O   . HOH F 5 .   ? -17.659 19.064  6.113   1.00 19.78  ? 403 HOH A O   1 
HETATM 2144 O  O   . HOH F 5 .   ? -25.150 9.590   13.217  1.00 38.82  ? 404 HOH A O   1 
HETATM 2145 O  O   . HOH F 5 .   ? -15.177 -10.038 37.680  1.00 37.31  ? 405 HOH A O   1 
HETATM 2146 O  O   . HOH F 5 .   ? -10.557 13.177  8.375   1.00 36.19  ? 406 HOH A O   1 
HETATM 2147 O  O   . HOH F 5 .   ? -23.772 8.685   20.137  1.00 27.89  ? 407 HOH A O   1 
HETATM 2148 O  O   . HOH F 5 .   ? -13.091 -22.298 11.698  1.00 34.83  ? 408 HOH A O   1 
HETATM 2149 O  O   . HOH F 5 .   ? -10.169 -18.233 17.065  1.00 25.28  ? 409 HOH A O   1 
HETATM 2150 O  O   . HOH F 5 .   ? -20.066 8.634   30.032  1.00 36.31  ? 410 HOH A O   1 
HETATM 2151 O  O   . HOH F 5 .   ? -10.924 -15.195 33.998  1.00 38.63  ? 411 HOH A O   1 
HETATM 2152 O  O   . HOH F 5 .   ? -5.438  1.152   10.034  1.00 39.10  ? 412 HOH A O   1 
HETATM 2153 O  O   . HOH F 5 .   ? -19.172 -20.548 5.192   1.00 31.39  ? 413 HOH A O   1 
HETATM 2154 O  O   . HOH F 5 .   ? -12.444 13.053  31.785  1.00 50.38  ? 414 HOH A O   1 
HETATM 2155 O  O   . HOH F 5 .   ? -11.908 12.601  29.064  1.00 41.34  ? 415 HOH A O   1 
HETATM 2156 O  O   . HOH F 5 .   ? -12.422 3.542   -6.859  1.00 40.70  ? 416 HOH A O   1 
HETATM 2157 O  O   . HOH F 5 .   ? 1.421   11.002  16.928  1.00 53.74  ? 417 HOH A O   1 
HETATM 2158 O  O   . HOH F 5 .   ? -18.184 -8.955  34.580  1.00 34.84  ? 418 HOH A O   1 
HETATM 2159 O  O   . HOH F 5 .   ? -13.807 -8.996  -5.114  1.00 26.93  ? 419 HOH A O   1 
HETATM 2160 O  O   . HOH F 5 .   ? 2.323   8.068   27.795  1.00 40.69  ? 420 HOH A O   1 
HETATM 2161 O  O   . HOH F 5 .   ? -18.490 -20.327 15.046  1.00 51.45  ? 421 HOH A O   1 
HETATM 2162 O  O   . HOH F 5 .   ? -0.979  -4.098  15.729  1.00 14.78  ? 422 HOH A O   1 
HETATM 2163 O  O   . HOH F 5 .   ? -21.505 -14.057 18.679  1.00 42.73  ? 423 HOH A O   1 
HETATM 2164 O  O   . HOH F 5 .   ? -13.820 -5.266  -6.474  1.00 43.79  ? 424 HOH A O   1 
HETATM 2165 O  O   . HOH F 5 .   ? -25.265 -5.403  13.098  1.00 34.28  ? 425 HOH A O   1 
HETATM 2166 O  O   . HOH F 5 .   ? -18.730 17.688  18.756  1.00 41.14  ? 426 HOH A O   1 
HETATM 2167 O  O   . HOH F 5 .   ? -6.397  -20.262 19.461  1.00 22.56  ? 427 HOH A O   1 
HETATM 2168 O  O   . HOH F 5 .   ? 0.593   -1.428  -4.775  1.00 31.55  ? 428 HOH A O   1 
HETATM 2169 O  O   . HOH F 5 .   ? -8.140  -15.311 36.447  1.00 34.37  ? 429 HOH A O   1 
HETATM 2170 O  O   . HOH F 5 .   ? -13.627 14.361  27.128  1.00 37.70  ? 430 HOH A O   1 
HETATM 2171 O  O   . HOH F 5 .   ? -8.168  8.127   9.510   1.00 38.89  ? 431 HOH A O   1 
HETATM 2172 O  O   . HOH F 5 .   ? -23.655 -2.905  29.233  1.00 44.45  ? 432 HOH A O   1 
HETATM 2173 O  O   . HOH F 5 .   ? -3.427  5.527   -2.521  1.00 41.26  ? 433 HOH A O   1 
HETATM 2174 O  O   . HOH F 5 .   ? -5.763  -4.782  -6.362  1.00 31.38  ? 434 HOH A O   1 
HETATM 2175 O  O   . HOH F 5 .   ? 11.777  -6.866  22.372  1.00 32.95  ? 435 HOH A O   1 
HETATM 2176 O  O   . HOH F 5 .   ? -8.678  6.012   28.894  1.00 37.20  ? 436 HOH A O   1 
HETATM 2177 O  O   . HOH F 5 .   ? -21.823 -18.390 13.736  1.00 30.98  ? 437 HOH A O   1 
HETATM 2178 O  O   . HOH F 5 .   ? -4.397  -11.897 31.963  1.00 26.02  ? 438 HOH A O   1 
HETATM 2179 O  O   . HOH F 5 .   ? 4.634   -3.394  26.386  1.00 26.25  ? 439 HOH A O   1 
HETATM 2180 O  O   . HOH F 5 .   ? 4.284   -3.351  3.917   1.00 52.96  ? 440 HOH A O   1 
HETATM 2181 O  O   . HOH F 5 .   ? -6.669  -14.825 31.485  1.00 30.56  ? 441 HOH A O   1 
HETATM 2182 O  O   . HOH F 5 .   ? 10.685  -10.703 16.078  1.00 26.62  ? 442 HOH A O   1 
HETATM 2183 O  O   . HOH F 5 .   ? -10.168 8.685   25.411  1.00 18.39  ? 443 HOH A O   1 
HETATM 2184 O  O   . HOH F 5 .   ? -16.338 -14.862 32.896  1.00 45.79  ? 444 HOH A O   1 
HETATM 2185 O  O   . HOH F 5 .   ? 14.061  6.189   15.456  1.00 51.98  ? 445 HOH A O   1 
HETATM 2186 O  O   . HOH F 5 .   ? -19.806 -16.691 3.100   1.00 30.86  ? 446 HOH A O   1 
HETATM 2187 O  O   . HOH F 5 .   ? 15.700  3.279   20.938  1.00 38.09  ? 447 HOH A O   1 
HETATM 2188 O  O   . HOH F 5 .   ? -22.350 -5.766  2.953   1.00 25.62  ? 448 HOH A O   1 
HETATM 2189 O  O   . HOH F 5 .   ? -19.801 10.917  26.659  1.00 27.52  ? 449 HOH A O   1 
HETATM 2190 O  O   . HOH F 5 .   ? -15.740 15.994  23.504  1.00 29.38  ? 450 HOH A O   1 
HETATM 2191 O  O   . HOH F 5 .   ? -21.325 19.540  17.306  1.00 49.35  ? 451 HOH A O   1 
HETATM 2192 O  O   . HOH F 5 .   ? 3.921   5.031   29.819  1.00 25.35  ? 452 HOH A O   1 
HETATM 2193 O  O   . HOH F 5 .   ? 0.191   1.037   34.386  1.00 33.57  ? 453 HOH A O   1 
HETATM 2194 O  O   . HOH F 5 .   ? -7.691  -15.472 11.365  1.00 16.24  ? 454 HOH A O   1 
HETATM 2195 O  O   . HOH F 5 .   ? -19.330 17.159  5.881   1.00 33.41  ? 455 HOH A O   1 
HETATM 2196 O  O   . HOH F 5 .   ? -3.219  -11.074 20.846  1.00 16.12  ? 456 HOH A O   1 
HETATM 2197 O  O   . HOH F 5 .   ? -10.278 1.201   33.780  1.00 49.00  ? 457 HOH A O   1 
HETATM 2198 O  O   . HOH F 5 .   ? -23.025 -11.213 17.181  1.00 32.64  ? 458 HOH A O   1 
HETATM 2199 O  O   . HOH F 5 .   ? 8.862   -3.665  21.057  1.00 18.75  ? 459 HOH A O   1 
HETATM 2200 O  O   . HOH F 5 .   ? 2.790   -13.435 5.258   1.00 30.60  ? 460 HOH A O   1 
HETATM 2201 O  O   . HOH F 5 .   ? -25.519 -15.058 8.141   1.00 42.07  ? 461 HOH A O   1 
HETATM 2202 O  O   . HOH F 5 .   ? 15.686  -6.883  11.476  1.00 36.46  ? 462 HOH A O   1 
HETATM 2203 O  O   . HOH F 5 .   ? -4.262  -13.435 17.996  1.00 14.31  ? 463 HOH A O   1 
HETATM 2204 O  O   . HOH F 5 .   ? -0.725  9.264   27.815  1.00 33.18  ? 464 HOH A O   1 
HETATM 2205 O  O   . HOH F 5 .   ? 0.245   -19.753 11.063  1.00 38.54  ? 465 HOH A O   1 
HETATM 2206 O  O   . HOH F 5 .   ? 5.508   7.218   20.371  1.00 24.23  ? 466 HOH A O   1 
HETATM 2207 O  O   . HOH F 5 .   ? -17.632 10.493  11.310  1.00 21.70  ? 467 HOH A O   1 
HETATM 2208 O  O   . HOH F 5 .   ? -18.800 -12.259 -3.344  1.00 29.60  ? 468 HOH A O   1 
HETATM 2209 O  O   . HOH F 5 .   ? -19.368 -4.171  41.227  1.00 38.49  ? 469 HOH A O   1 
HETATM 2210 O  O   . HOH F 5 .   ? -2.210  -8.652  29.040  1.00 16.37  ? 470 HOH A O   1 
HETATM 2211 O  O   . HOH F 5 .   ? -10.852 -19.215 7.029   1.00 44.73  ? 471 HOH A O   1 
HETATM 2212 O  O   . HOH F 5 .   ? -20.635 -6.603  -2.210  1.00 56.48  ? 472 HOH A O   1 
HETATM 2213 O  O   . HOH F 5 .   ? 2.029   12.358  22.544  1.00 48.77  ? 473 HOH A O   1 
HETATM 2214 O  O   . HOH F 5 .   ? 2.211   -15.706 9.436   1.00 26.55  ? 474 HOH A O   1 
HETATM 2215 O  O   . HOH F 5 .   ? -13.457 10.521  27.707  1.00 24.95  ? 475 HOH A O   1 
HETATM 2216 O  O   . HOH F 5 .   ? -3.506  -15.830 24.387  1.00 19.01  ? 476 HOH A O   1 
HETATM 2217 O  O   . HOH F 5 .   ? 1.649   -11.688 24.987  1.00 28.05  ? 477 HOH A O   1 
HETATM 2218 O  O   . HOH F 5 .   ? -6.393  -5.304  37.190  1.00 29.29  ? 478 HOH A O   1 
HETATM 2219 O  O   . HOH F 5 .   ? 4.705   -2.541  28.872  1.00 34.06  ? 479 HOH A O   1 
HETATM 2220 O  O   . HOH F 5 .   ? -5.454  17.159  27.218  1.00 36.04  ? 480 HOH A O   1 
HETATM 2221 O  O   . HOH F 5 .   ? -24.548 4.699   8.559   1.00 40.24  ? 481 HOH A O   1 
HETATM 2222 O  O   . HOH F 5 .   ? -2.178  -3.268  11.466  1.00 22.99  ? 482 HOH A O   1 
HETATM 2223 O  O   . HOH F 5 .   ? 11.939  -0.131  15.925  1.00 30.57  ? 483 HOH A O   1 
HETATM 2224 O  O   . HOH F 5 .   ? -20.712 7.745   1.794   1.00 19.09  ? 484 HOH A O   1 
HETATM 2225 O  O   . HOH F 5 .   ? -8.107  0.479   -6.405  1.00 34.27  ? 485 HOH A O   1 
HETATM 2226 O  O   . HOH F 5 .   ? -21.190 -6.967  23.538  1.00 16.99  ? 486 HOH A O   1 
HETATM 2227 O  O   . HOH F 5 .   ? -3.491  -13.076 -2.880  1.00 32.74  ? 487 HOH A O   1 
HETATM 2228 O  O   . HOH F 5 .   ? -3.101  -13.190 25.142  1.00 16.61  ? 488 HOH A O   1 
HETATM 2229 O  O   . HOH F 5 .   ? -18.922 9.956   8.843   1.00 19.38  ? 489 HOH A O   1 
HETATM 2230 O  O   . HOH F 5 .   ? -4.456  -16.077 0.981   1.00 37.13  ? 490 HOH A O   1 
HETATM 2231 O  O   . HOH F 5 .   ? -13.279 19.888  14.824  1.00 32.19  ? 491 HOH A O   1 
HETATM 2232 O  O   . HOH F 5 .   ? -23.072 -13.250 11.347  1.00 26.95  ? 492 HOH A O   1 
HETATM 2233 O  O   . HOH F 5 .   ? -11.210 10.285  8.271   1.00 27.38  ? 493 HOH A O   1 
HETATM 2234 O  O   . HOH F 5 .   ? -19.922 13.865  28.695  1.00 42.29  ? 494 HOH A O   1 
HETATM 2235 O  O   . HOH F 5 .   ? -21.487 5.709   4.649   1.00 19.15  ? 495 HOH A O   1 
HETATM 2236 O  O   . HOH F 5 .   ? -15.746 -12.226 24.355  1.00 21.76  ? 496 HOH A O   1 
HETATM 2237 O  O   . HOH F 5 .   ? -14.376 -18.459 18.693  1.00 30.03  ? 497 HOH A O   1 
HETATM 2238 O  O   . HOH F 5 .   ? -25.532 6.413   26.942  1.00 31.60  ? 498 HOH A O   1 
HETATM 2239 O  O   . HOH F 5 .   ? -16.702 -8.293  20.341  1.00 13.67  ? 499 HOH A O   1 
HETATM 2240 O  O   . HOH F 5 .   ? -2.337  4.417   7.579   1.00 43.37  ? 500 HOH A O   1 
HETATM 2241 O  O   . HOH F 5 .   ? -3.918  -8.478  31.113  1.00 28.17  ? 501 HOH A O   1 
HETATM 2242 O  O   . HOH F 5 .   ? 9.454   7.662   18.571  1.00 48.32  ? 502 HOH A O   1 
HETATM 2243 O  O   . HOH F 5 .   ? -18.243 -3.976  -2.619  1.00 33.64  ? 503 HOH A O   1 
HETATM 2244 O  O   . HOH F 5 .   ? -12.762 -16.716 26.569  1.00 23.69  ? 504 HOH A O   1 
HETATM 2245 O  O   . HOH F 5 .   ? -20.822 18.848  13.697  1.00 47.15  ? 505 HOH A O   1 
HETATM 2246 O  O   . HOH F 5 .   ? 5.223   -4.798  20.947  1.00 17.49  ? 506 HOH A O   1 
HETATM 2247 O  O   . HOH F 5 .   ? -6.158  6.546   10.314  1.00 30.42  ? 507 HOH A O   1 
HETATM 2248 O  O   . HOH F 5 .   ? -12.546 -9.077  -3.178  1.00 27.66  ? 508 HOH A O   1 
HETATM 2249 O  O   . HOH F 5 .   ? -17.106 -16.102 22.113  1.00 36.06  ? 509 HOH A O   1 
HETATM 2250 O  O   . HOH F 5 .   ? -7.608  -19.005 30.522  1.00 36.85  ? 510 HOH A O   1 
HETATM 2251 O  O   . HOH F 5 .   ? 13.622  0.543   24.520  1.00 25.39  ? 511 HOH A O   1 
HETATM 2252 O  O   . HOH F 5 .   ? -7.075  -8.628  32.552  1.00 23.02  ? 512 HOH A O   1 
HETATM 2253 O  O   . HOH F 5 .   ? -24.387 11.917  6.185   1.00 34.95  ? 513 HOH A O   1 
HETATM 2254 O  O   . HOH F 5 .   ? -14.641 20.184  17.561  1.00 31.84  ? 514 HOH A O   1 
HETATM 2255 O  O   . HOH F 5 .   ? -25.496 7.889   6.343   1.00 35.11  ? 515 HOH A O   1 
HETATM 2256 O  O   . HOH F 5 .   ? 5.465   -7.157  22.300  1.00 38.21  ? 516 HOH A O   1 
HETATM 2257 O  O   . HOH F 5 .   ? 13.354  -5.665  24.593  1.00 32.14  ? 517 HOH A O   1 
HETATM 2258 O  O   . HOH F 5 .   ? -22.787 -0.193  34.278  1.00 38.99  ? 518 HOH A O   1 
HETATM 2259 O  O   . HOH F 5 .   ? 11.509  1.627   26.005  1.00 28.14  ? 519 HOH A O   1 
HETATM 2260 O  O   . HOH F 5 .   ? -2.902  4.009   40.486  1.00 34.04  ? 520 HOH A O   1 
HETATM 2261 O  O   . HOH F 5 .   ? -24.589 -7.618  9.152   1.00 20.20  ? 521 HOH A O   1 
HETATM 2262 O  O   . HOH F 5 .   ? -16.090 -9.752  32.940  1.00 21.18  ? 522 HOH A O   1 
HETATM 2263 O  O   . HOH F 5 .   ? -17.754 4.375   -3.644  1.00 50.52  ? 523 HOH A O   1 
HETATM 2264 O  O   . HOH F 5 .   ? 3.723   10.129  18.509  1.00 37.42  ? 524 HOH A O   1 
HETATM 2265 O  O   . HOH F 5 .   ? -13.738 -21.104 3.367   1.00 50.30  ? 525 HOH A O   1 
HETATM 2266 O  O   . HOH F 5 .   ? -25.848 -7.088  30.516  1.00 42.64  ? 526 HOH A O   1 
HETATM 2267 O  O   . HOH F 5 .   ? -16.639 -13.952 37.329  1.00 34.15  ? 527 HOH A O   1 
HETATM 2268 O  O   . HOH F 5 .   ? 1.665   -6.423  34.337  1.00 35.45  ? 528 HOH A O   1 
HETATM 2269 O  O   . HOH F 5 .   ? -13.118 -18.498 14.737  1.00 28.75  ? 529 HOH A O   1 
HETATM 2270 O  O   . HOH F 5 .   ? -11.585 2.933   30.683  1.00 24.52  ? 530 HOH A O   1 
HETATM 2271 O  O   . HOH F 5 .   ? 3.181   -4.439  7.689   1.00 28.56  ? 531 HOH A O   1 
HETATM 2272 O  O   . HOH F 5 .   ? -23.592 -0.588  26.528  1.00 24.51  ? 532 HOH A O   1 
HETATM 2273 O  O   . HOH F 5 .   ? -26.131 -2.107  14.587  1.00 31.12  ? 533 HOH A O   1 
HETATM 2274 O  O   . HOH F 5 .   ? -6.980  -16.810 1.476   1.00 31.56  ? 534 HOH A O   1 
HETATM 2275 O  O   . HOH F 5 .   ? -16.822 -7.264  39.563  1.00 43.86  ? 535 HOH A O   1 
HETATM 2276 O  O   . HOH F 5 .   ? -26.375 -3.736  25.162  1.00 25.01  ? 536 HOH A O   1 
HETATM 2277 O  O   . HOH F 5 .   ? -25.930 3.489   15.466  1.00 30.16  ? 537 HOH A O   1 
HETATM 2278 O  O   . HOH F 5 .   ? 2.893   -11.503 9.551   1.00 30.77  ? 538 HOH A O   1 
HETATM 2279 O  O   . HOH F 5 .   ? -18.619 12.139  13.021  1.00 32.21  ? 539 HOH A O   1 
HETATM 2280 O  O   . HOH F 5 .   ? 1.615   -1.506  29.349  1.00 18.98  ? 540 HOH A O   1 
HETATM 2281 O  O   . HOH F 5 .   ? 1.850   8.691   23.992  1.00 29.11  ? 541 HOH A O   1 
HETATM 2282 O  O   . HOH F 5 .   ? -17.705 20.516  8.057   1.00 18.62  ? 542 HOH A O   1 
HETATM 2283 O  O   . HOH F 5 .   ? -23.644 -18.060 6.663   1.00 37.09  ? 543 HOH A O   1 
HETATM 2284 O  O   . HOH F 5 .   ? 8.331   -9.248  16.435  1.00 26.91  ? 544 HOH A O   1 
HETATM 2285 O  O   . HOH F 5 .   ? -0.654  -12.672 -3.300  1.00 33.70  ? 545 HOH A O   1 
HETATM 2286 O  O   . HOH F 5 .   ? -12.365 -18.409 31.837  1.00 42.82  ? 546 HOH A O   1 
HETATM 2287 O  O   . HOH F 5 .   ? 4.570   -6.907  7.955   1.00 27.44  ? 547 HOH A O   1 
HETATM 2288 O  O   . HOH F 5 .   ? -7.969  -22.136 10.445  1.00 29.77  ? 548 HOH A O   1 
HETATM 2289 O  O   . HOH F 5 .   ? -0.320  -8.475  32.487  1.00 30.70  ? 549 HOH A O   1 
HETATM 2290 O  O   . HOH F 5 .   ? -9.268  -7.960  34.029  1.00 29.48  ? 550 HOH A O   1 
HETATM 2291 O  O   . HOH F 5 .   ? -8.717  -5.802  35.819  1.00 25.55  ? 551 HOH A O   1 
HETATM 2292 O  O   . HOH F 5 .   ? -4.858  -13.249 34.277  1.00 47.06  ? 552 HOH A O   1 
HETATM 2293 O  O   . HOH F 5 .   ? 4.172   4.553   10.768  1.00 53.78  ? 553 HOH A O   1 
HETATM 2294 O  O   . HOH F 5 .   ? -0.895  -17.682 18.074  1.00 41.85  ? 554 HOH A O   1 
HETATM 2295 O  O   . HOH F 5 .   ? 0.091   -14.179 22.200  1.00 29.94  ? 555 HOH A O   1 
HETATM 2296 O  O   . HOH F 5 .   ? -0.262  10.554  23.229  1.00 29.80  ? 556 HOH A O   1 
HETATM 2297 O  O   . HOH F 5 .   ? -9.658  14.767  12.157  1.00 37.40  ? 557 HOH A O   1 
HETATM 2298 O  O   . HOH F 5 .   ? -9.067  -10.184 -1.303  1.00 35.71  ? 558 HOH A O   1 
HETATM 2299 O  O   . HOH F 5 .   ? -12.375 8.039   28.763  1.00 32.87  ? 559 HOH A O   1 
HETATM 2300 O  O   . HOH F 5 .   ? -9.052  13.076  10.393  1.00 43.82  ? 560 HOH A O   1 
HETATM 2301 O  O   . HOH F 5 .   ? -1.787  -12.259 22.821  1.00 15.43  ? 561 HOH A O   1 
HETATM 2302 O  O   . HOH F 5 .   ? -8.119  -19.808 26.553  1.00 36.27  ? 562 HOH A O   1 
HETATM 2303 O  O   . HOH F 5 .   ? 14.173  5.974   19.176  1.00 46.83  ? 563 HOH A O   1 
HETATM 2304 O  O   . HOH F 5 .   ? -6.131  -19.739 23.962  1.00 42.96  ? 564 HOH A O   1 
HETATM 2305 O  O   . HOH F 5 .   ? 15.056  -10.282 14.536  1.00 34.59  ? 565 HOH A O   1 
HETATM 2306 O  O   . HOH F 5 .   ? -22.739 -11.545 14.118  1.00 25.62  ? 566 HOH A O   1 
HETATM 2307 O  O   . HOH F 5 .   ? -7.859  -19.325 21.667  1.00 26.77  ? 567 HOH A O   1 
HETATM 2308 O  O   . HOH F 5 .   ? -13.234 -0.937  -6.057  1.00 40.25  ? 568 HOH A O   1 
HETATM 2309 O  O   . HOH F 5 .   ? 6.718   -10.740 14.694  1.00 42.48  ? 569 HOH A O   1 
HETATM 2310 O  O   . HOH F 5 .   ? 1.989   2.341   35.979  1.00 36.70  ? 570 HOH A O   1 
HETATM 2311 O  O   . HOH F 5 .   ? 7.797   6.258   21.706  1.00 21.74  ? 571 HOH A O   1 
HETATM 2312 O  O   . HOH F 5 .   ? 8.549   3.393   27.923  1.00 36.46  ? 572 HOH A O   1 
HETATM 2313 O  O   . HOH F 5 .   ? 10.644  -9.161  8.748   1.00 45.67  ? 573 HOH A O   1 
HETATM 2314 O  O   . HOH F 5 .   ? -5.793  14.708  11.730  1.00 48.30  ? 574 HOH A O   1 
HETATM 2315 O  O   . HOH F 5 .   ? -21.071 -19.487 6.650   1.00 33.87  ? 575 HOH A O   1 
HETATM 2316 O  O   . HOH F 5 .   ? -6.863  1.536   34.985  1.00 33.45  ? 576 HOH A O   1 
HETATM 2317 O  O   . HOH F 5 .   ? -4.832  3.223   -5.868  1.00 34.14  ? 577 HOH A O   1 
HETATM 2318 O  O   . HOH F 5 .   ? -2.408  -14.667 32.736  1.00 45.32  ? 578 HOH A O   1 
HETATM 2319 O  O   . HOH F 5 .   ? 14.759  0.323   15.036  1.00 35.11  ? 579 HOH A O   1 
HETATM 2320 O  O   . HOH F 5 .   ? -1.267  -13.062 27.184  1.00 30.47  ? 580 HOH A O   1 
HETATM 2321 O  O   . HOH F 5 .   ? 9.407   2.287   30.156  1.00 55.17  ? 581 HOH A O   1 
HETATM 2322 O  O   . HOH F 5 .   ? -7.223  -9.037  -2.258  1.00 36.44  ? 582 HOH A O   1 
HETATM 2323 O  O   . HOH F 5 .   ? -12.530 -17.190 16.832  1.00 25.01  ? 583 HOH A O   1 
HETATM 2324 O  O   . HOH F 5 .   ? -24.976 11.240  19.751  1.00 41.13  ? 584 HOH A O   1 
HETATM 2325 O  O   . HOH F 5 .   ? -1.022  11.332  25.635  1.00 37.02  ? 585 HOH A O   1 
HETATM 2326 O  O   . HOH F 5 .   ? 14.372  2.470   23.138  1.00 44.54  ? 586 HOH A O   1 
HETATM 2327 O  O   . HOH F 5 .   ? -4.035  8.192   10.228  1.00 46.53  ? 587 HOH A O   1 
HETATM 2328 O  O   . HOH F 5 .   ? -10.641 -23.567 12.103  1.00 34.49  ? 588 HOH A O   1 
HETATM 2329 O  O   . HOH F 5 .   ? 0.610   -2.718  39.124  1.00 43.36  ? 589 HOH A O   1 
HETATM 2330 O  O   . HOH F 5 .   ? -22.355 -9.458  25.344  1.00 42.57  ? 590 HOH A O   1 
HETATM 2331 O  O   . HOH F 5 .   ? 0.299   0.494   -6.780  1.00 47.47  ? 591 HOH A O   1 
HETATM 2332 O  O   . HOH F 5 .   ? -17.439 19.830  17.634  1.00 35.94  ? 592 HOH A O   1 
HETATM 2333 O  O   . HOH F 5 .   ? 8.993   -4.533  23.612  1.00 33.86  ? 593 HOH A O   1 
HETATM 2334 O  O   . HOH F 5 .   ? -8.141  -17.392 34.704  1.00 39.28  ? 594 HOH A O   1 
HETATM 2335 O  O   . HOH F 5 .   ? -17.086 18.008  3.895   1.00 40.30  ? 595 HOH A O   1 
HETATM 2336 O  O   . HOH F 5 .   ? -1.821  -11.867 31.336  1.00 39.62  ? 596 HOH A O   1 
HETATM 2337 O  O   . HOH F 5 .   ? -16.430 19.705  22.253  1.00 53.27  ? 597 HOH A O   1 
HETATM 2338 O  O   . HOH F 5 .   ? 4.193   8.807   22.337  1.00 32.62  ? 598 HOH A O   1 
HETATM 2339 O  O   . HOH F 5 .   ? -1.668  -17.399 25.440  1.00 38.08  ? 599 HOH A O   1 
HETATM 2340 O  O   . HOH F 5 .   ? -24.578 8.965   26.524  1.00 50.07  ? 600 HOH A O   1 
HETATM 2341 O  O   . HOH F 5 .   ? 3.122   -13.515 8.100   1.00 38.03  ? 601 HOH A O   1 
HETATM 2342 O  O   . HOH F 5 .   ? -26.378 9.911   4.573   1.00 45.10  ? 602 HOH A O   1 
HETATM 2343 O  O   . HOH F 5 .   ? -2.268  -17.543 5.232   1.00 43.74  ? 603 HOH A O   1 
HETATM 2344 O  O   . HOH F 5 .   ? 6.792   -5.416  27.247  1.00 37.39  ? 604 HOH A O   1 
HETATM 2345 O  O   . HOH F 5 .   ? 8.489   7.959   23.724  1.00 40.82  ? 605 HOH A O   1 
HETATM 2346 O  O   . HOH F 5 .   ? -0.612  8.017   14.314  1.00 49.70  ? 606 HOH A O   1 
HETATM 2347 O  O   . HOH F 5 .   ? -14.333 -2.970  -6.878  1.00 44.11  ? 607 HOH A O   1 
HETATM 2348 O  O   . HOH F 5 .   ? -4.570  -9.590  33.368  1.00 36.47  ? 608 HOH A O   1 
HETATM 2349 O  O   . HOH F 5 .   ? -0.881  -11.116 28.968  1.00 23.68  ? 609 HOH A O   1 
HETATM 2350 O  O   . HOH F 5 .   ? -16.509 -17.904 20.431  1.00 41.12  ? 610 HOH A O   1 
HETATM 2351 O  O   . HOH F 5 .   ? -23.702 -6.655  0.278   1.00 49.98  ? 611 HOH A O   1 
HETATM 2352 O  O   . HOH F 5 .   ? -16.545 -13.933 26.319  1.00 33.16  ? 612 HOH A O   1 
HETATM 2353 O  O   . HOH F 5 .   ? 4.381   -11.717 23.352  1.00 47.72  ? 613 HOH A O   1 
HETATM 2354 O  O   . HOH F 5 .   ? -19.768 -15.746 22.254  1.00 52.81  ? 614 HOH A O   1 
HETATM 2355 O  O   . HOH F 5 .   ? -6.958  -10.451 -4.347  1.00 40.72  ? 615 HOH A O   1 
HETATM 2356 O  O   . HOH F 5 .   ? -11.080 -11.346 -2.966  1.00 44.97  ? 616 HOH A O   1 
HETATM 2357 O  O   . HOH F 5 .   ? -16.021 -14.804 28.557  1.00 48.50  ? 617 HOH A O   1 
HETATM 2358 O  O   . HOH F 5 .   ? -17.605 -12.047 31.482  1.00 35.08  ? 618 HOH A O   1 
HETATM 2359 O  O   . HOH F 5 .   ? 2.420   -14.193 20.819  1.00 39.32  ? 619 HOH A O   1 
HETATM 2360 O  O   . HOH F 5 .   ? -1.821  3.012   -7.192  1.00 40.13  ? 620 HOH A O   1 
HETATM 2361 O  O   . HOH F 5 .   ? 6.539   5.435   29.126  1.00 46.10  ? 621 HOH A O   1 
HETATM 2362 O  O   . HOH F 5 .   ? 12.528  4.280   27.412  1.00 46.58  ? 622 HOH A O   1 
HETATM 2363 O  O   . HOH F 5 .   ? -26.393 -1.160  26.016  1.00 27.54  ? 623 HOH A O   1 
HETATM 2364 O  O   . HOH F 5 .   ? -12.641 -19.386 26.233  1.00 35.14  ? 624 HOH A O   1 
HETATM 2365 O  O   . HOH F 5 .   ? 7.011   8.658   18.613  1.00 41.71  ? 625 HOH A O   1 
HETATM 2366 O  O   . HOH F 5 .   ? 9.153   -12.976 16.409  1.00 39.06  ? 626 HOH A O   1 
HETATM 2367 O  O   . HOH F 5 .   ? -3.440  -15.657 -1.975  1.00 39.54  ? 627 HOH A O   1 
HETATM 2368 O  O   . HOH F 5 .   ? -2.426  -9.258  34.381  1.00 47.14  ? 628 HOH A O   1 
HETATM 2369 O  O   . HOH F 5 .   ? 14.363  5.041   25.137  1.00 43.44  ? 629 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 4   ? 0.6598 0.9420 0.5959 0.0120  0.2203  0.0545  4   HIS A N   
2    C  CA  . HIS A 4   ? 0.4428 0.5437 0.4521 0.0113  0.0480  0.2098  4   HIS A CA  
3    C  C   . HIS A 4   ? 0.4438 0.5683 0.2665 0.0435  0.0971  0.0954  4   HIS A C   
4    O  O   . HIS A 4   ? 0.7776 0.4857 0.4944 -0.0493 -0.0534 0.0937  4   HIS A O   
5    C  CB  . HIS A 4   ? 0.3551 0.6529 0.3292 -0.0108 0.0593  0.2371  4   HIS A CB  
6    C  CG  . HIS A 4   ? 0.4266 0.4287 0.6093 0.1254  -0.0522 0.2266  4   HIS A CG  
7    N  ND1 . HIS A 4   ? 0.4607 0.8111 0.6332 -0.0431 0.0669  0.0253  4   HIS A ND1 
8    C  CD2 . HIS A 4   ? 0.5498 0.5951 0.9531 0.2507  0.1527  0.1788  4   HIS A CD2 
9    C  CE1 . HIS A 4   ? 0.7150 0.7071 0.9003 -0.0789 0.0528  0.0306  4   HIS A CE1 
10   N  NE2 . HIS A 4   ? 0.8210 0.7359 0.9226 -0.0333 0.2051  0.2066  4   HIS A NE2 
11   N  N   . TRP A 5   ? 0.4080 0.4963 0.2770 -0.0697 0.1078  -0.0223 5   TRP A N   
12   C  CA  . TRP A 5   ? 0.2619 0.3468 0.2682 0.0035  0.0344  -0.0057 5   TRP A CA  
13   C  C   . TRP A 5   ? 0.2376 0.3286 0.2788 -0.0155 0.0214  0.0230  5   TRP A C   
14   O  O   . TRP A 5   ? 0.3122 0.4023 0.2467 -0.0121 -0.0003 0.0129  5   TRP A O   
15   C  CB  . TRP A 5   ? 0.2282 0.3046 0.2726 -0.0100 -0.0034 -0.0273 5   TRP A CB  
16   C  CG  . TRP A 5   ? 0.2414 0.3019 0.1835 -0.0143 0.0328  0.0431  5   TRP A CG  
17   C  CD1 . TRP A 5   ? 0.3612 0.3231 0.2962 -0.0486 0.0105  0.0807  5   TRP A CD1 
18   C  CD2 . TRP A 5   ? 0.2161 0.2790 0.1893 0.0027  -0.0095 -0.0150 5   TRP A CD2 
19   N  NE1 . TRP A 5   ? 0.3642 0.2957 0.2101 -0.0111 0.0054  0.0483  5   TRP A NE1 
20   C  CE2 . TRP A 5   ? 0.2561 0.2873 0.1911 0.0111  -0.0086 0.0032  5   TRP A CE2 
21   C  CE3 . TRP A 5   ? 0.2327 0.3308 0.1289 -0.0465 -0.0003 -0.0370 5   TRP A CE3 
22   C  CZ2 . TRP A 5   ? 0.2517 0.2985 0.1831 0.0300  -0.0522 0.0285  5   TRP A CZ2 
23   C  CZ3 . TRP A 5   ? 0.2453 0.2852 0.1385 0.0074  -0.0116 -0.0362 5   TRP A CZ3 
24   C  CH2 . TRP A 5   ? 0.2746 0.2811 0.1514 0.0152  -0.0271 -0.0525 5   TRP A CH2 
25   N  N   . GLY A 6   ? 0.2347 0.2674 0.2300 -0.0060 0.0286  -0.0080 6   GLY A N   
26   C  CA  . GLY A 6   ? 0.2137 0.3151 0.2559 -0.0168 0.0243  0.0006  6   GLY A CA  
27   C  C   . GLY A 6   ? 0.1958 0.3210 0.1570 0.0243  0.0127  -0.0197 6   GLY A C   
28   O  O   . GLY A 6   ? 0.1834 0.3197 0.1634 -0.0044 -0.0160 -0.0337 6   GLY A O   
29   N  N   . TYR A 7   ? 0.2148 0.3222 0.2142 0.0050  -0.0068 -0.0452 7   TYR A N   
30   C  CA  . TYR A 7   ? 0.1970 0.2899 0.2412 -0.0192 -0.0019 -0.0542 7   TYR A CA  
31   C  C   . TYR A 7   ? 0.2058 0.2816 0.3206 -0.0130 -0.0423 -0.0330 7   TYR A C   
32   O  O   . TYR A 7   ? 0.2698 0.3001 0.5065 -0.0251 0.0331  -0.0229 7   TYR A O   
33   C  CB  . TYR A 7   ? 0.2029 0.2781 0.2227 -0.0199 -0.0008 -0.0722 7   TYR A CB  
34   C  CG  . TYR A 7   ? 0.1964 0.2319 0.1953 -0.0187 -0.0029 -0.0477 7   TYR A CG  
35   C  CD1 . TYR A 7   ? 0.1692 0.2302 0.1823 -0.0210 -0.0236 -0.0324 7   TYR A CD1 
36   C  CD2 . TYR A 7   ? 0.2171 0.2722 0.2208 -0.0416 -0.0431 -0.0468 7   TYR A CD2 
37   C  CE1 . TYR A 7   ? 0.1913 0.1929 0.1992 -0.0117 -0.0724 -0.0317 7   TYR A CE1 
38   C  CE2 . TYR A 7   ? 0.2172 0.2509 0.1277 -0.0489 -0.0164 -0.0107 7   TYR A CE2 
39   C  CZ  . TYR A 7   ? 0.2061 0.2022 0.1336 -0.0505 -0.0295 -0.0312 7   TYR A CZ  
40   O  OH  . TYR A 7   ? 0.2563 0.2026 0.1708 0.0013  -0.0348 -0.0031 7   TYR A OH  
41   N  N   . GLY A 8   ? 0.2438 0.3692 0.3022 0.0521  -0.0160 -0.0657 8   GLY A N   
42   C  CA  . GLY A 8   ? 0.3078 0.3841 0.3103 0.0876  0.0053  -0.0465 8   GLY A CA  
43   C  C   . GLY A 8   ? 0.3157 0.3321 0.2789 0.0302  -0.0055 -0.0156 8   GLY A C   
44   O  O   . GLY A 8   ? 0.2619 0.4050 0.2782 -0.0240 0.0239  -0.0758 8   GLY A O   
45   N  N   . LYS A 9   ? 0.3046 0.3111 0.4112 0.0086  -0.0253 -0.0439 9   LYS A N   
46   C  CA  . LYS A 9   ? 0.3307 0.2924 0.4410 -0.0193 -0.0768 -0.0156 9   LYS A CA  
47   C  C   . LYS A 9   ? 0.2716 0.2969 0.3078 -0.0062 -0.0212 0.0163  9   LYS A C   
48   O  O   . LYS A 9   ? 0.2806 0.3484 0.3069 -0.0109 0.0043  -0.0199 9   LYS A O   
49   C  CB  . LYS A 9   ? 0.4501 0.2614 0.6120 0.0206  -0.0810 -0.0030 9   LYS A CB  
50   C  CG  . LYS A 9   ? 0.4855 0.3806 0.5900 0.0307  -0.0904 0.0004  9   LYS A CG  
51   N  N   . HIS A 10  ? 0.2890 0.2891 0.3254 0.0522  0.0367  0.0336  10  HIS A N   
52   C  CA  . HIS A 10  ? 0.3255 0.3132 0.3632 0.0355  0.1238  0.0438  10  HIS A CA  
53   C  C   . HIS A 10  ? 0.2520 0.3162 0.2925 0.0455  0.0807  0.0522  10  HIS A C   
54   O  O   . HIS A 10  ? 0.2488 0.3273 0.4190 0.0433  0.0288  0.0681  10  HIS A O   
55   C  CB  . HIS A 10  ? 0.4348 0.3189 0.4972 0.0385  0.2841  0.0514  10  HIS A CB  
56   C  CG  . HIS A 10  ? 0.5567 0.3435 0.6945 0.0899  0.3335  0.1435  10  HIS A CG  
57   N  ND1 . HIS A 10  ? 0.6584 0.4390 0.7694 0.0652  0.3481  0.1199  10  HIS A ND1 
58   C  CD2 . HIS A 10  ? 0.5881 0.5089 0.6668 0.0629  0.2539  0.1222  10  HIS A CD2 
59   C  CE1 . HIS A 10  ? 0.6049 0.3452 0.8127 0.0632  0.3602  0.1221  10  HIS A CE1 
60   N  NE2 . HIS A 10  ? 0.4247 0.5627 0.7536 0.1151  0.3265  0.0478  10  HIS A NE2 
61   N  N   . ASN A 11  ? 0.2390 0.2992 0.3209 0.0476  0.0566  0.0308  11  ASN A N   
62   C  CA  . ASN A 11  ? 0.2749 0.2785 0.1936 0.0154  0.0631  -0.0049 11  ASN A CA  
63   C  C   . ASN A 11  ? 0.1935 0.2846 0.2026 0.0134  -0.0017 0.0195  11  ASN A C   
64   O  O   . ASN A 11  ? 0.2266 0.2961 0.2137 0.0387  0.0136  0.0004  11  ASN A O   
65   C  CB  . ASN A 11  ? 0.2847 0.3705 0.2514 0.0501  0.0619  0.0485  11  ASN A CB  
66   C  CG  . ASN A 11  ? 0.2762 0.4424 0.2590 0.0218  0.0642  0.0412  11  ASN A CG  
67   O  OD1 . ASN A 11  ? 0.2975 0.3987 0.1835 0.0097  0.0046  -0.0238 11  ASN A OD1 
68   N  ND2 . ASN A 11  ? 0.3991 0.4568 0.2535 0.0725  0.0502  0.0524  11  ASN A ND2 
69   N  N   . GLY A 12  ? 0.1916 0.3157 0.1963 -0.0089 0.0020  0.0029  12  GLY A N   
70   C  CA  . GLY A 12  ? 0.2029 0.2990 0.1879 0.0055  0.0144  -0.0110 12  GLY A CA  
71   C  C   . GLY A 12  ? 0.1724 0.2477 0.1810 0.0006  -0.0109 0.0210  12  GLY A C   
72   O  O   . GLY A 12  ? 0.1608 0.2550 0.2022 -0.0142 -0.0184 0.0153  12  GLY A O   
73   N  N   . PRO A 13  ? 0.1694 0.2417 0.1794 -0.0140 -0.0044 -0.0074 13  PRO A N   
74   C  CA  . PRO A 13  ? 0.1842 0.2110 0.1932 -0.0004 -0.0307 -0.0259 13  PRO A CA  
75   C  C   . PRO A 13  ? 0.1992 0.2101 0.1958 -0.0049 -0.0392 0.0276  13  PRO A C   
76   O  O   . PRO A 13  ? 0.1864 0.2485 0.2158 0.0039  -0.0296 -0.0259 13  PRO A O   
77   C  CB  . PRO A 13  ? 0.2015 0.2275 0.2290 -0.0439 -0.0462 -0.0192 13  PRO A CB  
78   C  CG  . PRO A 13  ? 0.2168 0.2576 0.1652 -0.0313 0.0067  -0.0241 13  PRO A CG  
79   C  CD  . PRO A 13  ? 0.1940 0.2514 0.1771 -0.0356 0.0020  -0.0188 13  PRO A CD  
80   N  N   . GLU A 14  ? 0.1997 0.2172 0.1936 -0.0026 -0.0266 0.0190  14  GLU A N   
81   C  CA  . GLU A 14  ? 0.1983 0.2245 0.2488 0.0013  -0.0484 0.0337  14  GLU A CA  
82   C  C   . GLU A 14  ? 0.1691 0.2300 0.2381 0.0042  -0.0330 0.0198  14  GLU A C   
83   O  O   . GLU A 14  ? 0.1914 0.2649 0.2363 0.0155  -0.0548 0.0293  14  GLU A O   
84   C  CB  . GLU A 14  ? 0.2655 0.2398 0.4039 0.0059  -0.1066 0.0883  14  GLU A CB  
85   C  CG  . GLU A 14  ? 0.2992 0.2949 0.4882 -0.0412 -0.0961 0.0692  14  GLU A CG  
86   C  CD  . GLU A 14  ? 0.5739 0.7116 0.4755 0.0146  -0.0660 0.0440  14  GLU A CD  
87   O  OE1 . GLU A 14  ? 0.6335 0.8469 0.4837 0.1615  -0.1046 0.1211  14  GLU A OE1 
88   O  OE2 . GLU A 14  ? 0.6412 0.5376 0.5755 0.1596  0.0656  0.0845  14  GLU A OE2 
89   N  N   . HIS A 15  ? 0.2021 0.2232 0.2046 -0.0048 -0.0192 0.0168  15  HIS A N   
90   C  CA  . HIS A 15  ? 0.1663 0.2200 0.1892 0.0187  -0.0266 0.0219  15  HIS A CA  
91   C  C   . HIS A 15  ? 0.1699 0.2326 0.1522 0.0308  -0.0359 0.0273  15  HIS A C   
92   O  O   . HIS A 15  ? 0.1615 0.2622 0.2392 -0.0087 -0.0351 0.0065  15  HIS A O   
93   C  CB  . HIS A 15  ? 0.1792 0.2338 0.1953 0.0290  -0.0436 0.0158  15  HIS A CB  
94   C  CG  . HIS A 15  ? 0.1855 0.2606 0.2496 0.0463  -0.0188 0.0106  15  HIS A CG  
95   N  ND1 . HIS A 15  ? 0.1891 0.2725 0.2710 0.0179  -0.0499 -0.0027 15  HIS A ND1 
96   C  CD2 . HIS A 15  ? 0.3049 0.2538 0.2320 0.0793  -0.0279 0.0173  15  HIS A CD2 
97   C  CE1 . HIS A 15  ? 0.2304 0.3323 0.3421 0.0926  -0.0605 -0.0128 15  HIS A CE1 
98   N  NE2 . HIS A 15  ? 0.2574 0.2813 0.3149 0.0526  -0.0055 -0.0137 15  HIS A NE2 
99   N  N   . TRP A 16  ? 0.1526 0.2180 0.1820 0.0076  -0.0365 -0.0041 16  TRP A N   
100  C  CA  . TRP A 16  ? 0.1397 0.1961 0.2259 -0.0013 -0.0365 -0.0344 16  TRP A CA  
101  C  C   . TRP A 16  ? 0.1566 0.2106 0.1857 -0.0135 -0.0357 -0.0052 16  TRP A C   
102  O  O   . TRP A 16  ? 0.1681 0.1924 0.2312 -0.0046 -0.0635 -0.0002 16  TRP A O   
103  C  CB  . TRP A 16  ? 0.1363 0.2345 0.1616 0.0061  -0.0342 -0.0022 16  TRP A CB  
104  C  CG  . TRP A 16  ? 0.1606 0.2374 0.1521 -0.0025 -0.0273 0.0110  16  TRP A CG  
105  C  CD1 . TRP A 16  ? 0.1518 0.2642 0.1676 -0.0142 -0.0098 0.0019  16  TRP A CD1 
106  C  CD2 . TRP A 16  ? 0.1530 0.2086 0.1479 0.0047  -0.0418 -0.0044 16  TRP A CD2 
107  N  NE1 . TRP A 16  ? 0.1512 0.2482 0.2116 -0.0122 -0.0362 -0.0175 16  TRP A NE1 
108  C  CE2 . TRP A 16  ? 0.1555 0.2203 0.1475 0.0077  -0.0421 -0.0029 16  TRP A CE2 
109  C  CE3 . TRP A 16  ? 0.1597 0.1828 0.1638 -0.0095 -0.0284 0.0114  16  TRP A CE3 
110  C  CZ2 . TRP A 16  ? 0.1454 0.2168 0.1426 -0.0023 -0.0220 0.0161  16  TRP A CZ2 
111  C  CZ3 . TRP A 16  ? 0.1726 0.2183 0.1367 -0.0065 -0.0357 -0.0084 16  TRP A CZ3 
112  C  CH2 . TRP A 16  ? 0.1878 0.2112 0.1198 -0.0006 -0.0048 -0.0081 16  TRP A CH2 
113  N  N   . HIS A 17  ? 0.1580 0.2221 0.1802 -0.0092 -0.0512 -0.0010 17  HIS A N   
114  C  CA  . HIS A 17  ? 0.1906 0.2366 0.1967 -0.0319 -0.0750 0.0159  17  HIS A CA  
115  C  C   . HIS A 17  ? 0.1885 0.2144 0.2595 -0.0051 -0.0329 0.0150  17  HIS A C   
116  O  O   . HIS A 17  ? 0.1769 0.2390 0.2336 -0.0138 -0.0424 0.0030  17  HIS A O   
117  C  CB  . HIS A 17  ? 0.1656 0.2724 0.1853 0.0204  -0.0537 0.0243  17  HIS A CB  
118  C  CG  . HIS A 17  ? 0.1733 0.2280 0.2136 0.0015  -0.0491 0.0203  17  HIS A CG  
119  N  ND1 . HIS A 17  ? 0.1927 0.3102 0.1778 0.0070  -0.0562 0.0292  17  HIS A ND1 
120  C  CD2 . HIS A 17  ? 0.2068 0.2561 0.1932 0.0549  -0.0458 0.0384  17  HIS A CD2 
121  C  CE1 . HIS A 17  ? 0.1967 0.2788 0.2579 0.0193  -0.0313 0.0500  17  HIS A CE1 
122  N  NE2 . HIS A 17  ? 0.1960 0.2966 0.2331 0.0260  -0.0488 0.0637  17  HIS A NE2 
123  N  N   . LYS A 18  ? 0.1497 0.2795 0.2161 -0.0119 -0.0524 0.0113  18  LYS A N   
124  C  CA  . LYS A 18  ? 0.1530 0.2678 0.2814 -0.0165 -0.0273 0.0018  18  LYS A CA  
125  C  C   . LYS A 18  ? 0.1789 0.2940 0.2763 -0.0679 -0.0717 0.0439  18  LYS A C   
126  O  O   . LYS A 18  ? 0.2319 0.2813 0.4826 -0.0697 -0.1354 0.0898  18  LYS A O   
127  C  CB  . LYS A 18  ? 0.1322 0.2887 0.2949 -0.0004 -0.0530 0.0192  18  LYS A CB  
128  C  CG  . LYS A 18  ? 0.1856 0.3042 0.3007 0.0511  -0.0346 0.0102  18  LYS A CG  
129  C  CD  . LYS A 18  ? 0.1875 0.3066 0.2626 0.0518  -0.0556 0.0186  18  LYS A CD  
130  C  CE  . LYS A 18  ? 0.2081 0.2714 0.3222 0.0333  -0.0255 0.0070  18  LYS A CE  
131  N  NZ  . LYS A 18  ? 0.1795 0.3142 0.2556 0.0476  -0.0465 0.0560  18  LYS A NZ  
132  N  N   . ASP A 19  ? 0.1663 0.2782 0.2529 0.0039  -0.0450 0.0417  19  ASP A N   
133  C  CA  . ASP A 19  ? 0.2040 0.2712 0.2328 -0.0401 -0.0287 0.0161  19  ASP A CA  
134  C  C   . ASP A 19  ? 0.1706 0.2514 0.2965 -0.0160 -0.0201 0.0445  19  ASP A C   
135  O  O   . ASP A 19  ? 0.2198 0.2398 0.3634 -0.0439 -0.0253 0.0522  19  ASP A O   
136  C  CB  . ASP A 19  ? 0.2366 0.4076 0.2186 -0.0122 -0.0452 0.0121  19  ASP A CB  
137  C  CG  . ASP A 19  ? 0.3061 0.4795 0.2931 -0.0871 0.0133  -0.0700 19  ASP A CG  
138  O  OD1 . ASP A 19  ? 0.2544 0.5299 0.3825 -0.0494 -0.0130 0.0286  19  ASP A OD1 
139  O  OD2 . ASP A 19  ? 0.4711 0.8198 0.6122 -0.1254 0.0008  -0.3815 19  ASP A OD2 
140  N  N   . PHE A 20  ? 0.1473 0.2175 0.2409 -0.0268 -0.0310 0.0221  20  PHE A N   
141  C  CA  . PHE A 20  ? 0.1723 0.2676 0.2184 -0.0309 -0.0337 -0.0171 20  PHE A CA  
142  C  C   . PHE A 20  ? 0.1661 0.2385 0.2597 -0.0239 -0.0605 0.0217  20  PHE A C   
143  O  O   . PHE A 20  ? 0.1825 0.2284 0.2046 0.0024  -0.0435 0.0227  20  PHE A O   
144  C  CB  . PHE A 20  ? 0.1547 0.2976 0.2268 -0.0365 -0.0388 0.0258  20  PHE A CB  
145  C  CG  . PHE A 20  ? 0.1638 0.3601 0.2593 -0.0186 -0.0258 0.0771  20  PHE A CG  
146  C  CD1 . PHE A 20  ? 0.1820 0.4100 0.3551 -0.0641 -0.0555 0.1316  20  PHE A CD1 
147  C  CD2 . PHE A 20  ? 0.1835 0.3874 0.2202 -0.0377 -0.0525 0.0893  20  PHE A CD2 
148  C  CE1 . PHE A 20  ? 0.2175 0.4292 0.3151 -0.0300 -0.0561 0.1030  20  PHE A CE1 
149  C  CE2 . PHE A 20  ? 0.1917 0.5011 0.2245 -0.0661 -0.0641 0.1086  20  PHE A CE2 
150  C  CZ  . PHE A 20  ? 0.1877 0.5019 0.2542 -0.0151 -0.0506 0.1214  20  PHE A CZ  
151  N  N   . PRO A 21  ? 0.1734 0.2434 0.2703 -0.0099 -0.0508 -0.0069 21  PRO A N   
152  C  CA  . PRO A 21  ? 0.1738 0.2809 0.2385 -0.0337 -0.0752 0.0080  21  PRO A CA  
153  C  C   . PRO A 21  ? 0.1752 0.2466 0.2806 -0.0228 -0.0761 -0.0072 21  PRO A C   
154  O  O   . PRO A 21  ? 0.1803 0.2530 0.2689 -0.0279 -0.0708 -0.0089 21  PRO A O   
155  C  CB  . PRO A 21  ? 0.1659 0.3917 0.3432 -0.0979 -0.0596 0.0005  21  PRO A CB  
156  C  CG  . PRO A 21  ? 0.3514 0.4022 0.3416 -0.1585 -0.1100 0.0200  21  PRO A CG  
157  C  CD  . PRO A 21  ? 0.1823 0.2954 0.3335 -0.0625 -0.0650 0.0552  21  PRO A CD  
158  N  N   A ILE A 22  ? 0.1638 0.2176 0.2088 -0.0167 -0.0558 -0.0455 22  ILE A N   
159  N  N   B ILE A 22  ? 0.1670 0.2249 0.2319 -0.0154 -0.0643 -0.0469 22  ILE A N   
160  C  CA  A ILE A 22  ? 0.1764 0.2208 0.2354 -0.0057 -0.0574 -0.0036 22  ILE A CA  
161  C  CA  B ILE A 22  ? 0.1913 0.2383 0.2385 -0.0211 -0.0638 -0.0164 22  ILE A CA  
162  C  C   A ILE A 22  ? 0.1708 0.2286 0.1882 -0.0050 -0.0416 -0.0223 22  ILE A C   
163  C  C   B ILE A 22  ? 0.1814 0.2337 0.1893 -0.0055 -0.0483 -0.0300 22  ILE A C   
164  O  O   A ILE A 22  ? 0.1853 0.2197 0.1997 0.0109  -0.0296 -0.0011 22  ILE A O   
165  O  O   B ILE A 22  ? 0.1965 0.2240 0.2196 0.0091  -0.0330 -0.0032 22  ILE A O   
166  C  CB  A ILE A 22  ? 0.2054 0.2046 0.2148 0.0080  -0.0697 -0.0160 22  ILE A CB  
167  C  CB  B ILE A 22  ? 0.2344 0.2326 0.1626 0.0044  -0.0693 -0.0339 22  ILE A CB  
168  C  CG1 A ILE A 22  ? 0.2452 0.1435 0.2602 -0.0148 -0.0342 -0.0209 22  ILE A CG1 
169  C  CG1 B ILE A 22  ? 0.2942 0.2859 0.2087 -0.0035 -0.0197 -0.0622 22  ILE A CG1 
170  C  CG2 A ILE A 22  ? 0.2019 0.2100 0.2088 -0.0061 -0.0751 0.0033  22  ILE A CG2 
171  C  CG2 B ILE A 22  ? 0.2280 0.2455 0.1979 -0.0652 -0.1007 -0.0438 22  ILE A CG2 
172  C  CD1 A ILE A 22  ? 0.2249 0.2229 0.2252 0.0252  -0.0286 -0.0103 22  ILE A CD1 
173  C  CD1 B ILE A 22  ? 0.2347 0.3264 0.2231 -0.0348 -0.0242 -0.0604 22  ILE A CD1 
174  N  N   . ALA A 23  ? 0.1917 0.2056 0.1730 -0.0122 -0.0521 -0.0165 23  ALA A N   
175  C  CA  . ALA A 23  ? 0.1625 0.2154 0.1626 -0.0211 -0.0293 -0.0078 23  ALA A CA  
176  C  C   . ALA A 23  ? 0.1582 0.2347 0.1713 -0.0115 -0.0326 0.0087  23  ALA A C   
177  O  O   . ALA A 23  ? 0.2144 0.2259 0.1936 -0.0062 -0.0187 0.0047  23  ALA A O   
178  C  CB  . ALA A 23  ? 0.1576 0.2419 0.1699 -0.0031 -0.0329 -0.0075 23  ALA A CB  
179  N  N   . LYS A 24  ? 0.1947 0.2745 0.1720 0.0095  -0.0509 -0.0104 24  LYS A N   
180  C  CA  . LYS A 24  ? 0.1929 0.3080 0.1582 0.0181  -0.0462 -0.0035 24  LYS A CA  
181  C  C   . LYS A 24  ? 0.2000 0.3225 0.1819 0.0104  -0.0442 -0.0366 24  LYS A C   
182  O  O   . LYS A 24  ? 0.2488 0.3637 0.1961 -0.0163 -0.0604 0.0033  24  LYS A O   
183  C  CB  . LYS A 24  ? 0.2165 0.3291 0.2226 0.0556  -0.0410 -0.0229 24  LYS A CB  
184  C  CG  . LYS A 24  ? 0.2333 0.3975 0.1713 0.0868  -0.0070 -0.0064 24  LYS A CG  
185  C  CD  . LYS A 24  ? 0.2280 0.3883 0.4117 0.0665  -0.0183 0.0018  24  LYS A CD  
186  C  CE  . LYS A 24  ? 0.2527 0.4614 0.3297 0.1238  -0.0091 0.0541  24  LYS A CE  
187  N  NZ  . LYS A 24  ? 0.4674 0.4146 0.3764 0.0446  -0.0617 -0.0172 24  LYS A NZ  
188  N  N   . GLY A 25  ? 0.1913 0.2990 0.2130 0.0168  -0.0078 -0.0140 25  GLY A N   
189  C  CA  . GLY A 25  ? 0.2122 0.3355 0.2652 -0.0296 0.0097  -0.0767 25  GLY A CA  
190  C  C   . GLY A 25  ? 0.2033 0.2939 0.1390 0.0080  -0.0469 -0.0381 25  GLY A C   
191  O  O   . GLY A 25  ? 0.2406 0.2995 0.1857 0.0103  -0.0624 0.0065  25  GLY A O   
192  N  N   . GLU A 26  ? 0.1738 0.3480 0.1455 0.0092  -0.0619 -0.0673 26  GLU A N   
193  C  CA  . GLU A 26  ? 0.1970 0.3465 0.1503 0.0337  -0.0401 -0.0381 26  GLU A CA  
194  C  C   . GLU A 26  ? 0.2024 0.2920 0.1494 0.0237  -0.0639 -0.0070 26  GLU A C   
195  O  O   . GLU A 26  ? 0.2500 0.3344 0.1467 0.0156  -0.0743 -0.0243 26  GLU A O   
196  C  CB  . GLU A 26  ? 0.2663 0.4726 0.2088 -0.0475 -0.0490 -0.1460 26  GLU A CB  
197  C  CG  . GLU A 26  ? 0.2933 0.4949 0.2787 -0.0575 -0.0860 -0.0951 26  GLU A CG  
198  C  CD  . GLU A 26  ? 0.6091 0.6794 0.4225 0.0534  -0.1175 0.0683  26  GLU A CD  
199  O  OE1 . GLU A 26  ? 0.4127 0.5691 0.5420 -0.0125 -0.2578 0.0044  26  GLU A OE1 
200  O  OE2 . GLU A 26  ? 0.5436 0.8612 0.7385 0.2701  -0.2679 -0.0773 26  GLU A OE2 
201  N  N   . ARG A 27  ? 0.2021 0.2079 0.1351 -0.0032 -0.0634 -0.0222 27  ARG A N   
202  C  CA  . ARG A 27  ? 0.1920 0.1958 0.1206 -0.0010 -0.0480 -0.0273 27  ARG A CA  
203  C  C   . ARG A 27  ? 0.1767 0.1814 0.1157 -0.0002 -0.0538 -0.0181 27  ARG A C   
204  O  O   . ARG A 27  ? 0.1936 0.1893 0.1399 0.0200  -0.0674 -0.0096 27  ARG A O   
205  C  CB  . ARG A 27  ? 0.2520 0.2326 0.1600 0.0168  -0.0450 -0.0617 27  ARG A CB  
206  C  CG  . ARG A 27  ? 0.2450 0.3230 0.2046 -0.0120 -0.0301 0.0011  27  ARG A CG  
207  C  CD  . ARG A 27  ? 0.2710 0.3792 0.2015 0.0373  -0.0578 -0.0231 27  ARG A CD  
208  N  NE  . ARG A 27  ? 0.2809 0.2685 0.1503 0.0182  -0.0297 0.0175  27  ARG A NE  
209  C  CZ  . ARG A 27  ? 0.2999 0.2256 0.1199 0.0583  -0.0351 0.0012  27  ARG A CZ  
210  N  NH1 . ARG A 27  ? 0.2632 0.3307 0.1899 0.0359  -0.0334 -0.1411 27  ARG A NH1 
211  N  NH2 . ARG A 27  ? 0.2990 0.2949 0.1511 -0.0168 -0.0287 -0.0330 27  ARG A NH2 
212  N  N   . GLN A 28  ? 0.1839 0.1954 0.0960 0.0223  -0.0366 -0.0164 28  GLN A N   
213  C  CA  . GLN A 28  ? 0.1676 0.1701 0.0913 0.0013  -0.0268 -0.0243 28  GLN A CA  
214  C  C   . GLN A 28  ? 0.1674 0.1662 0.1060 -0.0040 -0.0536 0.0049  28  GLN A C   
215  O  O   . GLN A 28  ? 0.1787 0.1904 0.1292 -0.0124 -0.0394 -0.0128 28  GLN A O   
216  C  CB  . GLN A 28  ? 0.1580 0.1870 0.1404 0.0018  -0.0326 -0.0281 28  GLN A CB  
217  C  CG  . GLN A 28  ? 0.1734 0.2037 0.1448 -0.0220 -0.0507 -0.0150 28  GLN A CG  
218  C  CD  . GLN A 28  ? 0.1569 0.1742 0.1368 -0.0111 -0.0642 -0.0308 28  GLN A CD  
219  O  OE1 . GLN A 28  ? 0.1834 0.1866 0.1376 -0.0175 -0.0532 -0.0225 28  GLN A OE1 
220  N  NE2 . GLN A 28  ? 0.1548 0.1825 0.1701 -0.0065 -0.0541 -0.0125 28  GLN A NE2 
221  N  N   . SER A 29  ? 0.1746 0.1533 0.1029 0.0000  -0.0424 -0.0200 29  SER A N   
222  C  CA  . SER A 29  ? 0.1631 0.1486 0.1126 -0.0029 -0.0386 -0.0176 29  SER A CA  
223  C  C   . SER A 29  ? 0.1609 0.1509 0.1363 0.0177  -0.0141 0.0105  29  SER A C   
224  O  O   . SER A 29  ? 0.1667 0.1832 0.1110 -0.0071 -0.0341 -0.0109 29  SER A O   
225  C  CB  . SER A 29  ? 0.1753 0.1579 0.1058 0.0146  -0.0151 -0.0002 29  SER A CB  
226  O  OG  . SER A 29  ? 0.1791 0.1806 0.1023 0.0049  -0.0391 -0.0187 29  SER A OG  
227  N  N   . PRO A 30  ? 0.1774 0.1552 0.0847 0.0076  -0.0162 -0.0003 30  PRO A N   
228  C  CA  . PRO A 30  ? 0.1856 0.1577 0.0798 -0.0105 -0.0276 0.0013  30  PRO A CA  
229  C  C   . PRO A 30  ? 0.1692 0.1566 0.0751 0.0075  -0.0117 0.0027  30  PRO A C   
230  O  O   . PRO A 30  ? 0.1588 0.1767 0.1191 -0.0025 -0.0363 -0.0073 30  PRO A O   
231  C  CB  . PRO A 30  ? 0.1687 0.1794 0.0981 0.0159  -0.0512 -0.0092 30  PRO A CB  
232  C  CG  . PRO A 30  ? 0.1584 0.1785 0.1069 -0.0179 -0.0394 -0.0030 30  PRO A CG  
233  C  CD  . PRO A 30  ? 0.1625 0.1781 0.0926 0.0023  -0.0172 -0.0212 30  PRO A CD  
234  N  N   . VAL A 31  ? 0.1848 0.1759 0.0925 0.0025  -0.0159 0.0435  31  VAL A N   
235  C  CA  . VAL A 31  ? 0.1925 0.1723 0.0699 -0.0188 -0.0226 0.0296  31  VAL A CA  
236  C  C   . VAL A 31  ? 0.1789 0.1620 0.1143 -0.0027 -0.0178 0.0174  31  VAL A C   
237  O  O   . VAL A 31  ? 0.1771 0.1817 0.1328 0.0048  -0.0348 0.0179  31  VAL A O   
238  C  CB  . VAL A 31  ? 0.1776 0.2001 0.1198 0.0012  -0.0186 -0.0086 31  VAL A CB  
239  C  CG1 . VAL A 31  ? 0.2082 0.1917 0.1324 -0.0144 -0.0199 -0.0161 31  VAL A CG1 
240  C  CG2 . VAL A 31  ? 0.1954 0.2011 0.1297 0.0209  -0.0210 0.0066  31  VAL A CG2 
241  N  N   . ASP A 32  ? 0.1981 0.1674 0.1118 0.0023  -0.0370 0.0168  32  ASP A N   
242  C  CA  . ASP A 32  ? 0.1947 0.1491 0.1206 0.0075  -0.0240 0.0160  32  ASP A CA  
243  C  C   . ASP A 32  ? 0.1961 0.1879 0.1148 0.0053  -0.0303 0.0003  32  ASP A C   
244  O  O   . ASP A 32  ? 0.2231 0.2372 0.1214 -0.0042 -0.0271 -0.0256 32  ASP A O   
245  C  CB  . ASP A 32  ? 0.2323 0.1834 0.1562 0.0309  -0.0268 0.0341  32  ASP A CB  
246  C  CG  . ASP A 32  ? 0.2537 0.2017 0.1412 0.0027  -0.0109 0.0212  32  ASP A CG  
247  O  OD1 . ASP A 32  ? 0.2582 0.1798 0.1444 0.0118  -0.0285 0.0165  32  ASP A OD1 
248  O  OD2 . ASP A 32  ? 0.3411 0.2356 0.1450 -0.0124 -0.0064 0.0167  32  ASP A OD2 
249  N  N   . ILE A 33  ? 0.1972 0.1927 0.0952 -0.0087 -0.0027 0.0075  33  ILE A N   
250  C  CA  . ILE A 33  ? 0.2017 0.1778 0.1286 0.0153  -0.0057 0.0256  33  ILE A CA  
251  C  C   . ILE A 33  ? 0.2455 0.1799 0.1049 0.0105  0.0077  0.0184  33  ILE A C   
252  O  O   . ILE A 33  ? 0.2688 0.1904 0.1478 0.0058  -0.0036 0.0080  33  ILE A O   
253  C  CB  . ILE A 33  ? 0.2119 0.1875 0.1512 0.0176  -0.0020 0.0225  33  ILE A CB  
254  C  CG1 . ILE A 33  ? 0.1877 0.2056 0.1626 0.0005  -0.0322 0.0428  33  ILE A CG1 
255  C  CG2 . ILE A 33  ? 0.2428 0.2513 0.1407 0.0136  0.0126  0.0058  33  ILE A CG2 
256  C  CD1 . ILE A 33  ? 0.2025 0.2470 0.2116 0.0366  -0.0497 0.0515  33  ILE A CD1 
257  N  N   A ASP A 34  ? 0.2801 0.2080 0.1035 0.0329  -0.0072 0.0287  34  ASP A N   
258  N  N   B ASP A 34  ? 0.2582 0.2297 0.0969 0.0419  0.0004  0.0236  34  ASP A N   
259  C  CA  A ASP A 34  ? 0.2907 0.2277 0.1796 0.0011  0.0138  0.0542  34  ASP A CA  
260  C  CA  B ASP A 34  ? 0.2090 0.2543 0.1509 0.0266  -0.0454 0.0672  34  ASP A CA  
261  C  C   A ASP A 34  ? 0.3104 0.2173 0.1333 0.0187  0.0212  0.0670  34  ASP A C   
262  C  C   B ASP A 34  ? 0.2456 0.2552 0.1749 0.0449  -0.0025 0.0972  34  ASP A C   
263  O  O   A ASP A 34  ? 0.2863 0.3401 0.0850 0.0277  0.0510  -0.0261 34  ASP A O   
264  O  O   B ASP A 34  ? 0.3213 0.2348 0.2597 0.0996  -0.0122 0.0497  34  ASP A O   
265  C  CB  A ASP A 34  ? 0.3766 0.1995 0.2330 0.0526  -0.0395 0.0291  34  ASP A CB  
266  C  CB  B ASP A 34  ? 0.2998 0.2352 0.1011 0.0558  -0.0589 0.0485  34  ASP A CB  
267  C  CG  A ASP A 34  ? 0.4496 0.3073 0.2058 -0.0023 0.0596  0.0498  34  ASP A CG  
268  C  CG  B ASP A 34  ? 0.2294 0.2793 0.2148 0.0657  -0.0232 0.1116  34  ASP A CG  
269  O  OD1 A ASP A 34  ? 0.3820 0.3170 0.2834 0.0053  0.0561  -0.0757 34  ASP A OD1 
270  O  OD1 B ASP A 34  ? 0.2929 0.2594 0.1849 0.0114  -0.0452 0.1244  34  ASP A OD1 
271  O  OD2 A ASP A 34  ? 0.5008 0.3708 0.3540 0.1416  0.1199  0.1971  34  ASP A OD2 
272  O  OD2 B ASP A 34  ? 0.2913 0.4118 0.1759 0.0486  -0.0697 0.1030  34  ASP A OD2 
273  N  N   . THR A 35  ? 0.2728 0.2667 0.1595 0.0357  0.0121  0.0800  35  THR A N   
274  C  CA  . THR A 35  ? 0.2777 0.3089 0.1708 0.0670  0.0379  0.0478  35  THR A CA  
275  C  C   . THR A 35  ? 0.3028 0.2860 0.1756 0.0751  0.0453  0.0798  35  THR A C   
276  O  O   . THR A 35  ? 0.3373 0.3007 0.1537 0.0723  0.0159  0.0337  35  THR A O   
277  C  CB  . THR A 35  ? 0.3134 0.2864 0.2025 0.0493  0.0176  0.0650  35  THR A CB  
278  O  OG1 . THR A 35  ? 0.3243 0.2875 0.2452 0.0332  0.0384  0.0715  35  THR A OG1 
279  C  CG2 . THR A 35  ? 0.3136 0.3338 0.2035 0.0669  0.0217  0.0511  35  THR A CG2 
280  N  N   . HIS A 36  ? 0.3679 0.2789 0.1623 0.0864  0.0839  0.0914  36  HIS A N   
281  C  CA  . HIS A 36  ? 0.3776 0.2748 0.1530 0.0813  0.0763  0.0779  36  HIS A CA  
282  C  C   . HIS A 36  ? 0.4649 0.3362 0.1430 0.0741  0.0509  -0.0015 36  HIS A C   
283  O  O   . HIS A 36  ? 0.5878 0.4064 0.1612 0.0240  0.1109  -0.0273 36  HIS A O   
284  C  CB  . HIS A 36  ? 0.4900 0.2750 0.1954 0.0606  0.0168  0.1228  36  HIS A CB  
285  C  CG  . HIS A 36  ? 0.5471 0.2861 0.2799 0.0626  -0.0306 0.0709  36  HIS A CG  
286  N  ND1 . HIS A 36  ? 0.5927 0.3777 0.2990 -0.1099 -0.1491 0.1171  36  HIS A ND1 
287  C  CD2 . HIS A 36  ? 0.7712 0.2694 0.2252 0.0958  -0.1497 0.0475  36  HIS A CD2 
288  C  CE1 . HIS A 36  ? 0.8131 0.3881 0.2150 -0.0059 -0.2166 0.0386  36  HIS A CE1 
289  N  NE2 . HIS A 36  ? 0.9129 0.3529 0.4187 0.0483  -0.0644 -0.0551 36  HIS A NE2 
290  N  N   . THR A 37  ? 0.4119 0.3089 0.2026 0.0964  0.0290  0.0564  37  THR A N   
291  C  CA  . THR A 37  ? 0.4209 0.3074 0.1618 0.1048  0.0226  0.0650  37  THR A CA  
292  C  C   . THR A 37  ? 0.3540 0.3039 0.1518 0.0855  -0.0154 0.0539  37  THR A C   
293  O  O   . THR A 37  ? 0.4711 0.3465 0.1809 0.0774  -0.0591 0.0413  37  THR A O   
294  C  CB  . THR A 37  ? 0.3756 0.3698 0.4682 0.1395  -0.1495 0.0392  37  THR A CB  
295  O  OG1 . THR A 37  ? 0.5319 0.4476 0.5642 0.1615  0.0043  0.1270  37  THR A OG1 
296  C  CG2 . THR A 37  ? 0.4970 0.5540 0.4148 -0.0053 -0.1418 0.0734  37  THR A CG2 
297  N  N   . ALA A 38  ? 0.3447 0.2678 0.1194 0.1056  0.0214  0.0543  38  ALA A N   
298  C  CA  . ALA A 38  ? 0.3240 0.2385 0.1033 0.0751  0.0223  0.0496  38  ALA A CA  
299  C  C   . ALA A 38  ? 0.3876 0.2698 0.2328 0.0686  0.1021  0.0532  38  ALA A C   
300  O  O   . ALA A 38  ? 0.4243 0.2870 0.4312 0.0425  0.1530  0.0617  38  ALA A O   
301  C  CB  . ALA A 38  ? 0.3283 0.2570 0.1458 0.0627  -0.0343 0.0469  38  ALA A CB  
302  N  N   . LYS A 39  ? 0.3227 0.3121 0.1741 0.1026  -0.0359 0.0044  39  LYS A N   
303  C  CA  . LYS A 39  ? 0.3740 0.3626 0.1906 0.1586  -0.0361 -0.0089 39  LYS A CA  
304  C  C   . LYS A 39  ? 0.3001 0.3385 0.1575 0.0754  0.0006  0.0348  39  LYS A C   
305  O  O   . LYS A 39  ? 0.2679 0.3166 0.1360 0.0430  -0.0250 0.0286  39  LYS A O   
306  C  CB  . LYS A 39  ? 0.3847 0.5084 0.2464 0.1630  -0.1028 -0.0672 39  LYS A CB  
307  C  CG  . LYS A 39  ? 0.3533 0.6311 0.1864 0.0529  -0.0281 -0.0467 39  LYS A CG  
308  C  CD  . LYS A 39  ? 0.2837 0.6061 0.2036 0.1188  0.0089  0.0075  39  LYS A CD  
309  C  CE  . LYS A 39  ? 0.2903 0.6089 0.2634 0.0842  0.0009  -0.0144 39  LYS A CE  
310  N  NZ  . LYS A 39  ? 0.3121 0.7343 0.4065 0.0972  -0.0198 0.1877  39  LYS A NZ  
311  N  N   . TYR A 40  ? 0.3209 0.3476 0.1424 0.0701  -0.0037 0.0430  40  TYR A N   
312  C  CA  . TYR A 40  ? 0.2999 0.3775 0.1160 0.0251  0.0162  0.0304  40  TYR A CA  
313  C  C   . TYR A 40  ? 0.3131 0.3737 0.1419 0.0511  -0.0076 -0.0089 40  TYR A C   
314  O  O   . TYR A 40  ? 0.3096 0.4092 0.1242 0.0737  0.0078  -0.0043 40  TYR A O   
315  C  CB  . TYR A 40  ? 0.3347 0.4663 0.1877 -0.0114 0.0558  0.0604  40  TYR A CB  
316  C  CG  . TYR A 40  ? 0.3104 0.4894 0.1680 -0.0368 0.0447  0.0322  40  TYR A CG  
317  C  CD1 . TYR A 40  ? 0.3125 0.3810 0.2043 0.0144  -0.0071 -0.0053 40  TYR A CD1 
318  C  CD2 . TYR A 40  ? 0.5211 0.7228 0.2046 0.0025  0.1890  0.0475  40  TYR A CD2 
319  C  CE1 . TYR A 40  ? 0.2640 0.6805 0.1954 0.0512  -0.0502 0.0022  40  TYR A CE1 
320  C  CE2 . TYR A 40  ? 0.4974 0.7329 0.3276 0.0306  0.1230  0.0054  40  TYR A CE2 
321  C  CZ  . TYR A 40  ? 0.2720 0.7617 0.3561 0.0597  0.0671  -0.0634 40  TYR A CZ  
322  O  OH  . TYR A 40  ? 0.3040 0.9432 0.3558 0.1249  -0.0143 0.0043  40  TYR A OH  
323  N  N   . ASP A 41  ? 0.2654 0.3228 0.1588 0.0417  0.0011  -0.0174 41  ASP A N   
324  C  CA  . ASP A 41  ? 0.3088 0.3540 0.1900 0.0399  -0.0183 -0.0436 41  ASP A CA  
325  C  C   . ASP A 41  ? 0.3759 0.4115 0.1529 0.1470  -0.0332 -0.0109 41  ASP A C   
326  O  O   . ASP A 41  ? 0.3114 0.3855 0.1857 0.0762  -0.0250 0.0035  41  ASP A O   
327  C  CB  . ASP A 41  ? 0.4261 0.3785 0.2022 -0.0250 -0.0370 -0.0493 41  ASP A CB  
328  C  CG  . ASP A 41  ? 0.4912 0.3849 0.4011 -0.0043 -0.1817 -0.1057 41  ASP A CG  
329  O  OD1 . ASP A 41  ? 0.6074 0.4524 0.3811 0.0334  -0.1489 -0.1548 41  ASP A OD1 
330  O  OD2 . ASP A 41  ? 0.5259 0.4687 0.5204 -0.0695 -0.2228 0.0231  41  ASP A OD2 
331  N  N   . PRO A 42  ? 0.4071 0.5877 0.2142 0.1615  0.0190  -0.0097 42  PRO A N   
332  C  CA  . PRO A 42  ? 0.4347 0.5316 0.2842 0.1923  0.0685  0.1238  42  PRO A CA  
333  C  C   . PRO A 42  ? 0.4772 0.4737 0.3418 0.1682  0.0747  0.0637  42  PRO A C   
334  O  O   . PRO A 42  ? 0.4812 0.6990 0.3495 0.2392  0.0343  0.0064  42  PRO A O   
335  C  CB  . PRO A 42  ? 0.5130 0.7197 0.2868 0.1993  0.0897  0.1383  42  PRO A CB  
336  C  CG  . PRO A 42  ? 0.4510 0.8405 0.2904 0.2521  0.1120  0.0578  42  PRO A CG  
337  C  CD  . PRO A 42  ? 0.4379 0.5320 0.2081 0.1753  0.1036  0.0818  42  PRO A CD  
338  N  N   . SER A 43  ? 0.5232 0.4640 0.2057 0.1489  0.0944  -0.0032 43  SER A N   
339  C  CA  . SER A 43  ? 0.7564 0.4079 0.2687 0.1894  0.0016  -0.0716 43  SER A CA  
340  C  C   . SER A 43  ? 0.6783 0.3775 0.3055 0.2118  -0.0153 0.0030  43  SER A C   
341  O  O   . SER A 43  ? 0.5401 0.3325 0.5177 0.1322  -0.1452 -0.0161 43  SER A O   
342  C  CB  . SER A 43  ? 0.7052 0.7085 0.5018 0.0619  -0.0345 -0.1181 43  SER A CB  
343  O  OG  . SER A 43  ? 0.6362 0.4521 0.2697 0.0386  -0.1287 -0.0812 43  SER A OG  
344  N  N   . LEU A 44  ? 0.5252 0.4029 0.2033 0.1460  -0.0996 -0.0258 44  LEU A N   
345  C  CA  . LEU A 44  ? 0.4064 0.4293 0.2248 0.0990  -0.1282 -0.0032 44  LEU A CA  
346  C  C   . LEU A 44  ? 0.2566 0.5644 0.3787 0.0323  -0.0291 0.1720  44  LEU A C   
347  O  O   . LEU A 44  ? 0.3515 0.7052 0.3498 -0.0788 -0.0058 0.1434  44  LEU A O   
348  C  CB  . LEU A 44  ? 0.2931 0.4230 0.2295 -0.0033 -0.0572 -0.0158 44  LEU A CB  
349  C  CG  . LEU A 44  ? 0.2943 0.4209 0.2287 0.0560  -0.0151 0.0592  44  LEU A CG  
350  C  CD1 . LEU A 44  ? 0.2757 0.3720 0.2087 -0.0105 -0.0433 0.0304  44  LEU A CD1 
351  C  CD2 . LEU A 44  ? 0.3208 0.3550 0.2203 0.0154  -0.0544 0.0223  44  LEU A CD2 
352  N  N   . LYS A 45  ? 0.3455 0.4493 0.3726 0.0424  -0.0942 0.1342  45  LYS A N   
353  C  CA  . LYS A 45  ? 0.3644 0.4330 0.3531 0.0768  -0.1042 -0.0329 45  LYS A CA  
354  C  C   . LYS A 45  ? 0.2970 0.4629 0.2474 0.0669  -0.0609 0.0240  45  LYS A C   
355  O  O   . LYS A 45  ? 0.2554 0.4845 0.2982 -0.0052 -0.0164 -0.0747 45  LYS A O   
356  C  CB  . LYS A 45  ? 0.3847 0.4018 0.2818 0.1292  -0.0262 -0.1064 45  LYS A CB  
357  C  CG  . LYS A 45  ? 0.3093 0.5448 0.3646 0.0673  -0.0348 -0.1958 45  LYS A CG  
358  C  CD  . LYS A 45  ? 0.5453 0.5356 0.6864 -0.0611 -0.1375 -0.1024 45  LYS A CD  
359  C  CE  . LYS A 45  ? 0.6281 0.6585 0.6107 -0.0616 -0.0697 -0.1758 45  LYS A CE  
360  N  NZ  . LYS A 45  ? 0.5506 0.8001 0.7227 -0.0077 0.1694  -0.2539 45  LYS A NZ  
361  N  N   . PRO A 46  ? 0.2665 0.4028 0.2363 -0.0021 -0.0402 0.0019  46  PRO A N   
362  C  CA  . PRO A 46  ? 0.2480 0.4860 0.2273 -0.0547 -0.0122 0.0083  46  PRO A CA  
363  C  C   . PRO A 46  ? 0.2029 0.3152 0.2984 0.0136  -0.0006 0.0260  46  PRO A C   
364  O  O   . PRO A 46  ? 0.2330 0.3431 0.2992 -0.0109 -0.0465 0.0174  46  PRO A O   
365  C  CB  . PRO A 46  ? 0.2424 0.5501 0.3055 -0.0625 -0.0547 -0.0310 46  PRO A CB  
366  C  CG  . PRO A 46  ? 0.2428 0.6759 0.4113 0.0418  -0.0318 -0.1222 46  PRO A CG  
367  C  CD  . PRO A 46  ? 0.3383 0.4505 0.2814 0.1020  -0.0719 -0.0872 46  PRO A CD  
368  N  N   . LEU A 47  ? 0.2421 0.4013 0.3194 0.0380  -0.0215 0.0310  47  LEU A N   
369  C  CA  . LEU A 47  ? 0.2219 0.3058 0.3013 0.0006  -0.0412 0.0290  47  LEU A CA  
370  C  C   . LEU A 47  ? 0.2897 0.2606 0.3809 -0.0400 -0.1451 0.0111  47  LEU A C   
371  O  O   . LEU A 47  ? 0.2500 0.3343 0.4831 -0.0556 -0.1176 0.0898  47  LEU A O   
372  C  CB  . LEU A 47  ? 0.2957 0.3537 0.5539 0.0555  -0.0356 0.0329  47  LEU A CB  
373  C  CG  . LEU A 47  ? 0.2184 0.4994 0.5729 -0.0131 -0.0555 -0.1759 47  LEU A CG  
374  C  CD1 . LEU A 47  ? 0.2615 0.3544 0.6966 -0.0496 -0.0957 -0.1152 47  LEU A CD1 
375  C  CD2 . LEU A 47  ? 0.2372 0.4061 0.7458 0.0312  -0.1376 -0.1504 47  LEU A CD2 
376  N  N   . SER A 48  ? 0.1929 0.2708 0.2820 -0.0021 -0.0793 0.0150  48  SER A N   
377  C  CA  . SER A 48  ? 0.1720 0.3008 0.2554 0.0155  -0.0425 0.0008  48  SER A CA  
378  C  C   . SER A 48  ? 0.1825 0.2802 0.2403 -0.0080 -0.0485 -0.0068 48  SER A C   
379  O  O   . SER A 48  ? 0.2154 0.2657 0.3015 -0.0440 -0.0244 -0.0274 48  SER A O   
380  C  CB  . SER A 48  ? 0.2264 0.2953 0.3195 0.0431  -0.0439 0.0139  48  SER A CB  
381  O  OG  . SER A 48  ? 0.3071 0.3724 0.4240 0.0745  -0.0573 0.0575  48  SER A OG  
382  N  N   . VAL A 49  ? 0.2420 0.3395 0.2083 -0.0344 -0.0286 -0.0219 49  VAL A N   
383  C  CA  . VAL A 49  ? 0.2680 0.3052 0.2421 -0.0678 0.0268  -0.0350 49  VAL A CA  
384  C  C   . VAL A 49  ? 0.2688 0.3840 0.2806 -0.0921 0.0000  -0.0270 49  VAL A C   
385  O  O   . VAL A 49  ? 0.3649 0.4891 0.2789 -0.2137 -0.0192 -0.0699 49  VAL A O   
386  C  CB  . VAL A 49  ? 0.4129 0.2975 0.2776 -0.0627 0.0462  -0.0271 49  VAL A CB  
387  C  CG1 . VAL A 49  ? 0.4688 0.4220 0.3347 -0.1443 0.1162  -0.0477 49  VAL A CG1 
388  C  CG2 . VAL A 49  ? 0.3281 0.3019 0.3852 -0.0609 0.0095  -0.0157 49  VAL A CG2 
389  N  N   . SER A 50  ? 0.2390 0.3207 0.2576 -0.0139 -0.0337 -0.0144 50  SER A N   
390  C  CA  . SER A 50  ? 0.1839 0.2838 0.3528 -0.0230 -0.0431 -0.0144 50  SER A CA  
391  C  C   . SER A 50  ? 0.1839 0.3347 0.2726 -0.0234 -0.0959 -0.0312 50  SER A C   
392  O  O   . SER A 50  ? 0.2259 0.3044 0.3252 -0.0103 -0.0877 -0.0179 50  SER A O   
393  C  CB  . SER A 50  ? 0.3239 0.3285 0.4700 0.0326  0.0802  -0.0348 50  SER A CB  
394  O  OG  . SER A 50  ? 0.3160 0.4661 0.4582 -0.0547 -0.0184 -0.0762 50  SER A OG  
395  N  N   . TYR A 51  ? 0.2352 0.3159 0.3102 -0.0336 -0.0619 -0.0469 51  TYR A N   
396  C  CA  . TYR A 51  ? 0.2363 0.2728 0.2925 -0.0005 -0.0675 0.0413  51  TYR A CA  
397  C  C   . TYR A 51  ? 0.2675 0.2662 0.2906 0.0133  -0.0781 0.0165  51  TYR A C   
398  O  O   . TYR A 51  ? 0.2733 0.3219 0.2841 0.0036  -0.0877 -0.0037 51  TYR A O   
399  C  CB  . TYR A 51  ? 0.2269 0.2681 0.2507 -0.0108 -0.0988 0.0048  51  TYR A CB  
400  C  CG  . TYR A 51  ? 0.2083 0.2428 0.2316 -0.0161 -0.0769 -0.0192 51  TYR A CG  
401  C  CD1 . TYR A 51  ? 0.1940 0.2259 0.2198 -0.0187 -0.0383 -0.0249 51  TYR A CD1 
402  C  CD2 . TYR A 51  ? 0.2093 0.2294 0.2039 -0.0053 -0.0429 0.0126  51  TYR A CD2 
403  C  CE1 . TYR A 51  ? 0.2245 0.2287 0.1993 -0.0052 -0.0574 0.0057  51  TYR A CE1 
404  C  CE2 . TYR A 51  ? 0.2227 0.2134 0.1781 -0.0358 -0.0436 0.0006  51  TYR A CE2 
405  C  CZ  . TYR A 51  ? 0.1888 0.2148 0.1870 -0.0207 -0.0524 -0.0188 51  TYR A CZ  
406  O  OH  . TYR A 51  ? 0.1947 0.2221 0.2205 -0.0111 -0.0637 -0.0013 51  TYR A OH  
407  N  N   . ASP A 52  ? 0.2462 0.3151 0.3820 0.0120  -0.0996 0.0247  52  ASP A N   
408  C  CA  . ASP A 52  ? 0.2591 0.3842 0.3804 0.0266  -0.0945 0.1135  52  ASP A CA  
409  C  C   . ASP A 52  ? 0.2734 0.3670 0.3282 -0.0142 -0.0993 0.0357  52  ASP A C   
410  O  O   . ASP A 52  ? 0.3283 0.4290 0.3590 0.0105  -0.1423 0.0440  52  ASP A O   
411  C  CB  . ASP A 52  ? 0.2482 0.6306 0.5015 0.1095  -0.1213 0.0622  52  ASP A CB  
412  C  CG  . ASP A 52  ? 0.3193 0.6996 0.6805 0.0278  0.0432  -0.0199 52  ASP A CG  
413  O  OD1 . ASP A 52  ? 0.3317 0.7972 0.8677 -0.0040 0.0008  0.0223  52  ASP A OD1 
414  O  OD2 . ASP A 52  ? 0.4398 0.7476 1.1713 0.0315  0.0524  0.2279  52  ASP A OD2 
415  N  N   . GLN A 53  ? 0.2473 0.3160 0.3732 0.0228  -0.0386 0.0302  53  GLN A N   
416  C  CA  . GLN A 53  ? 0.2588 0.3023 0.4221 0.0214  -0.0572 0.0776  53  GLN A CA  
417  C  C   . GLN A 53  ? 0.2920 0.2814 0.1737 0.0122  -0.0433 0.0133  53  GLN A C   
418  O  O   . GLN A 53  ? 0.2839 0.2541 0.3290 0.0099  -0.0894 0.0572  53  GLN A O   
419  C  CB  . GLN A 53  ? 0.3473 0.3429 0.3264 0.0854  -0.0340 0.0323  53  GLN A CB  
420  C  CG  . GLN A 53  ? 0.3269 0.3602 0.6233 0.0705  -0.0609 0.0449  53  GLN A CG  
421  C  CD  . GLN A 53  ? 0.3735 0.5054 0.7943 0.0403  -0.1676 0.0776  53  GLN A CD  
422  O  OE1 . GLN A 53  ? 0.5240 0.6309 1.3803 -0.1109 0.1445  0.1997  53  GLN A OE1 
423  N  NE2 . GLN A 53  ? 0.3982 0.4785 0.8146 0.0295  -0.1974 0.1143  53  GLN A NE2 
424  N  N   . ALA A 54  ? 0.2395 0.2565 0.2720 0.0016  -0.0848 0.0268  54  ALA A N   
425  C  CA  . ALA A 54  ? 0.2623 0.2106 0.2103 -0.0031 -0.0526 -0.0017 54  ALA A CA  
426  C  C   . ALA A 54  ? 0.2755 0.2050 0.2153 -0.0245 -0.0606 -0.0483 54  ALA A C   
427  O  O   . ALA A 54  ? 0.2658 0.2800 0.2961 -0.0216 -0.1145 -0.0675 54  ALA A O   
428  C  CB  . ALA A 54  ? 0.2444 0.2067 0.2913 0.0179  -0.0454 0.0109  54  ALA A CB  
429  N  N   . THR A 55  ? 0.2476 0.1812 0.2323 -0.0061 -0.0758 0.0160  55  THR A N   
430  C  CA  . THR A 55  ? 0.2700 0.1910 0.2101 0.0085  -0.0838 0.0399  55  THR A CA  
431  C  C   . THR A 55  ? 0.2645 0.1649 0.1576 -0.0166 -0.0969 0.0529  55  THR A C   
432  O  O   . THR A 55  ? 0.2807 0.1825 0.2004 -0.0238 -0.1153 0.0212  55  THR A O   
433  C  CB  . THR A 55  ? 0.3441 0.2004 0.2764 0.0354  -0.1057 0.0595  55  THR A CB  
434  O  OG1 . THR A 55  ? 0.3319 0.2330 0.3994 0.0189  -0.1141 0.0499  55  THR A OG1 
435  C  CG2 . THR A 55  ? 0.3695 0.2595 0.2381 0.0553  -0.1179 0.0525  55  THR A CG2 
436  N  N   . SER A 56  ? 0.2801 0.1698 0.1595 -0.0040 -0.0789 0.0377  56  SER A N   
437  C  CA  . SER A 56  ? 0.2689 0.1782 0.1552 -0.0247 -0.0569 0.0211  56  SER A CA  
438  C  C   . SER A 56  ? 0.2521 0.1964 0.1303 0.0096  -0.0803 0.0342  56  SER A C   
439  O  O   . SER A 56  ? 0.2811 0.1943 0.1792 -0.0060 -0.1294 0.0449  56  SER A O   
440  C  CB  . SER A 56  ? 0.3116 0.1641 0.1128 -0.0076 -0.1003 0.0084  56  SER A CB  
441  O  OG  . SER A 56  ? 0.3110 0.1932 0.1577 -0.0211 -0.1368 0.0229  56  SER A OG  
442  N  N   . LEU A 57  ? 0.2442 0.2183 0.1310 -0.0027 -0.0572 0.0279  57  LEU A N   
443  C  CA  . LEU A 57  ? 0.2502 0.2394 0.1476 -0.0055 -0.0375 0.0237  57  LEU A CA  
444  C  C   . LEU A 57  ? 0.3163 0.2281 0.1100 0.0222  -0.0537 0.0256  57  LEU A C   
445  O  O   . LEU A 57  ? 0.3970 0.2428 0.1105 0.0155  -0.0867 0.0223  57  LEU A O   
446  C  CB  . LEU A 57  ? 0.2663 0.2140 0.2238 -0.0082 -0.0540 0.0275  57  LEU A CB  
447  C  CG  . LEU A 57  ? 0.2967 0.2136 0.3058 -0.0144 -0.0528 -0.0196 57  LEU A CG  
448  C  CD1 . LEU A 57  ? 0.3552 0.2437 0.3177 -0.0718 -0.0333 -0.0527 57  LEU A CD1 
449  C  CD2 . LEU A 57  ? 0.3898 0.2676 0.4120 0.0831  -0.0161 0.0904  57  LEU A CD2 
450  N  N   . ARG A 58  ? 0.3084 0.2142 0.1440 0.0255  -0.0713 0.0215  58  ARG A N   
451  C  CA  . ARG A 58  ? 0.2811 0.2582 0.1755 0.0339  -0.0560 0.0641  58  ARG A CA  
452  C  C   . ARG A 58  ? 0.2410 0.2306 0.1093 0.0217  -0.0542 0.0340  58  ARG A C   
453  O  O   . ARG A 58  ? 0.3425 0.2341 0.0961 0.0289  -0.0767 0.0165  58  ARG A O   
454  C  CB  . ARG A 58  ? 0.2951 0.2699 0.2446 0.0088  0.0046  0.0859  58  ARG A CB  
455  C  CG  . ARG A 58  ? 0.4544 0.2951 0.3971 0.0391  0.0374  0.1376  58  ARG A CG  
456  C  CD  . ARG A 58  ? 0.6275 0.3957 0.4473 -0.0638 0.0570  0.1656  58  ARG A CD  
457  N  NE  . ARG A 58  ? 0.8851 0.6468 0.4535 -0.0966 0.2322  0.1066  58  ARG A NE  
458  C  CZ  . ARG A 58  ? 0.6686 0.4891 0.5649 -0.0146 0.1948  0.0073  58  ARG A CZ  
459  N  NH1 . ARG A 58  ? 0.7742 0.3532 0.3209 0.0510  0.1483  0.0917  58  ARG A NH1 
460  N  NH2 . ARG A 58  ? 0.9287 0.7720 0.4847 0.2091  0.0784  0.1446  58  ARG A NH2 
461  N  N   . ILE A 59  ? 0.3141 0.2322 0.1092 0.0343  -0.0609 0.0147  59  ILE A N   
462  C  CA  . ILE A 59  ? 0.3022 0.2272 0.0842 0.0039  -0.0493 0.0305  59  ILE A CA  
463  C  C   . ILE A 59  ? 0.3044 0.2207 0.1088 -0.0089 -0.0579 0.0242  59  ILE A C   
464  O  O   . ILE A 59  ? 0.2834 0.2890 0.1014 0.0111  -0.0557 0.0425  59  ILE A O   
465  C  CB  . ILE A 59  ? 0.3368 0.2161 0.1005 -0.0161 -0.0726 0.0391  59  ILE A CB  
466  C  CG1 . ILE A 59  ? 0.2957 0.2225 0.1181 0.0009  -0.0606 0.0385  59  ILE A CG1 
467  C  CG2 . ILE A 59  ? 0.3412 0.2397 0.0963 0.0230  -0.0804 0.0350  59  ILE A CG2 
468  C  CD1 . ILE A 59  ? 0.3699 0.2298 0.1478 -0.0219 -0.0745 0.0195  59  ILE A CD1 
469  N  N   . LEU A 60  ? 0.2945 0.2572 0.1026 0.0177  -0.0659 0.0061  60  LEU A N   
470  C  CA  . LEU A 60  ? 0.2912 0.2144 0.1498 0.0055  -0.0442 0.0247  60  LEU A CA  
471  C  C   . LEU A 60  ? 0.2319 0.2148 0.1236 -0.0256 -0.0542 0.0264  60  LEU A C   
472  O  O   . LEU A 60  ? 0.3023 0.2870 0.1224 -0.0100 -0.0245 0.0538  60  LEU A O   
473  C  CB  . LEU A 60  ? 0.4239 0.1929 0.4884 -0.0800 -0.0790 0.0863  60  LEU A CB  
474  C  CG  . LEU A 60  ? 0.4991 0.2578 0.4733 -0.0920 -0.0501 -0.0472 60  LEU A CG  
475  C  CD1 . LEU A 60  ? 0.8212 0.3093 0.2916 0.0041  -0.1102 -0.0038 60  LEU A CD1 
476  C  CD2 . LEU A 60  ? 0.5011 0.3764 0.3610 -0.1096 -0.1491 -0.0277 60  LEU A CD2 
477  N  N   . ASN A 61  ? 0.2567 0.2239 0.1166 -0.0157 -0.0405 0.0359  61  ASN A N   
478  C  CA  . ASN A 61  ? 0.2446 0.2007 0.1381 -0.0278 -0.0424 0.0237  61  ASN A CA  
479  C  C   . ASN A 61  ? 0.2974 0.2433 0.1500 -0.0560 -0.0531 0.0118  61  ASN A C   
480  O  O   . ASN A 61  ? 0.2725 0.2793 0.1480 -0.0692 -0.0596 0.0249  61  ASN A O   
481  C  CB  . ASN A 61  ? 0.2807 0.2438 0.1498 0.0070  -0.0146 0.0147  61  ASN A CB  
482  C  CG  . ASN A 61  ? 0.2629 0.2040 0.1412 -0.0304 -0.0218 0.0141  61  ASN A CG  
483  O  OD1 . ASN A 61  ? 0.2724 0.2676 0.1565 -0.0531 -0.0450 0.0209  61  ASN A OD1 
484  N  ND2 . ASN A 61  ? 0.2716 0.2214 0.1211 -0.0195 -0.0239 -0.0042 61  ASN A ND2 
485  N  N   . ASN A 62  ? 0.2796 0.2306 0.1486 -0.0564 -0.0838 0.0166  62  ASN A N   
486  C  CA  . ASN A 62  ? 0.3000 0.2590 0.1669 -0.0673 -0.0892 0.0152  62  ASN A CA  
487  C  C   . ASN A 62  ? 0.2741 0.3067 0.1534 -0.0815 -0.0291 0.0435  62  ASN A C   
488  O  O   . ASN A 62  ? 0.3239 0.3728 0.2636 -0.1165 -0.0831 0.0072  62  ASN A O   
489  C  CB  . ASN A 62  ? 0.4043 0.2679 0.1349 -0.0846 -0.0946 0.0050  62  ASN A CB  
490  C  CG  . ASN A 62  ? 0.3659 0.2992 0.1049 -0.0324 -0.0872 -0.0067 62  ASN A CG  
491  O  OD1 . ASN A 62  ? 0.3222 0.2570 0.1584 -0.0346 -0.0414 -0.0226 62  ASN A OD1 
492  N  ND2 . ASN A 62  ? 0.4983 0.3300 0.2015 -0.0063 -0.0023 -0.0237 62  ASN A ND2 
493  N  N   . GLY A 63  ? 0.2726 0.2787 0.1430 -0.0331 -0.0381 0.0321  63  GLY A N   
494  C  CA  . GLY A 63  ? 0.2591 0.2974 0.2054 -0.0392 -0.0567 0.0412  63  GLY A CA  
495  C  C   . GLY A 63  ? 0.1899 0.2725 0.1864 -0.0387 -0.0563 0.0220  63  GLY A C   
496  O  O   . GLY A 63  ? 0.2715 0.3411 0.1913 0.0297  -0.0350 0.0127  63  GLY A O   
497  N  N   A HIS A 64  ? 0.2265 0.2658 0.1903 -0.0793 -0.0151 0.0529  64  HIS A N   
498  N  N   B HIS A 64  ? 0.2255 0.3199 0.1304 -0.0348 -0.0763 0.0280  64  HIS A N   
499  C  CA  A HIS A 64  ? 0.2658 0.2529 0.1278 -0.0236 -0.0617 -0.0005 64  HIS A CA  
500  C  CA  B HIS A 64  ? 0.2431 0.2777 0.1720 -0.0670 -0.0726 0.0479  64  HIS A CA  
501  C  C   A HIS A 64  ? 0.2424 0.2326 0.1004 -0.0077 -0.0553 0.0042  64  HIS A C   
502  C  C   B HIS A 64  ? 0.2287 0.2238 0.1453 -0.0328 -0.0536 0.0289  64  HIS A C   
503  O  O   A HIS A 64  ? 0.2578 0.2460 0.1590 0.0157  -0.0215 0.0350  64  HIS A O   
504  O  O   B HIS A 64  ? 0.2464 0.2189 0.1036 -0.0139 -0.0467 0.0033  64  HIS A O   
505  C  CB  A HIS A 64  ? 0.2746 0.3113 0.1724 -0.0854 -0.0181 -0.0571 64  HIS A CB  
506  C  CB  B HIS A 64  ? 0.2201 0.3553 0.1730 -0.0316 -0.0631 -0.0124 64  HIS A CB  
507  C  CG  A HIS A 64  ? 0.2727 0.2894 0.0954 -0.0629 0.0171  -0.0582 64  HIS A CG  
508  C  CG  B HIS A 64  ? 0.2521 0.3828 0.1846 -0.0098 -0.0603 -0.0210 64  HIS A CG  
509  N  ND1 A HIS A 64  ? 0.3438 0.3021 0.2104 0.0022  0.0333  -0.0417 64  HIS A ND1 
510  N  ND1 B HIS A 64  ? 0.3006 0.3898 0.1813 -0.0215 -0.0745 -0.0464 64  HIS A ND1 
511  C  CD2 A HIS A 64  ? 0.3054 0.3129 0.2042 -0.0139 -0.0225 0.0511  64  HIS A CD2 
512  C  CD2 B HIS A 64  ? 0.1857 0.3838 0.1550 -0.0280 -0.0873 -0.0186 64  HIS A CD2 
513  C  CE1 A HIS A 64  ? 0.3486 0.3436 0.2219 -0.0179 0.0292  -0.0220 64  HIS A CE1 
514  C  CE1 B HIS A 64  ? 0.3243 0.3876 0.0859 -0.0673 -0.0100 -0.0691 64  HIS A CE1 
515  N  NE2 A HIS A 64  ? 0.2964 0.3443 0.2568 0.0032  0.0930  -0.0290 64  HIS A NE2 
516  N  NE2 B HIS A 64  ? 0.3206 0.3907 0.2142 -0.0221 -0.0151 0.0142  64  HIS A NE2 
517  N  N   . SER A 65  ? 0.2201 0.2349 0.1706 -0.0043 -0.0399 0.0203  65  SER A N   
518  C  CA  . SER A 65  ? 0.2265 0.2600 0.1227 -0.0184 -0.0414 0.0304  65  SER A CA  
519  C  C   . SER A 65  ? 0.2507 0.2301 0.1243 0.0184  -0.0141 0.0263  65  SER A C   
520  O  O   . SER A 65  ? 0.2324 0.2653 0.1239 -0.0107 -0.0255 0.0234  65  SER A O   
521  C  CB  . SER A 65  ? 0.2468 0.4187 0.0961 -0.0313 -0.0206 0.0321  65  SER A CB  
522  O  OG  . SER A 65  ? 0.3227 0.4270 0.1868 -0.0262 -0.0514 0.1044  65  SER A OG  
523  N  N   . PHE A 66  ? 0.2166 0.2008 0.1568 0.0176  -0.0562 0.0242  66  PHE A N   
524  C  CA  . PHE A 66  ? 0.2117 0.2759 0.1040 0.0352  -0.0559 0.0201  66  PHE A CA  
525  C  C   . PHE A 66  ? 0.2392 0.2126 0.1361 -0.0013 -0.0258 -0.0004 66  PHE A C   
526  O  O   . PHE A 66  ? 0.2552 0.2421 0.1173 0.0163  -0.0314 0.0055  66  PHE A O   
527  C  CB  . PHE A 66  ? 0.2745 0.2525 0.1114 0.0164  -0.0458 -0.0082 66  PHE A CB  
528  C  CG  . PHE A 66  ? 0.2540 0.2409 0.0944 0.0269  -0.0517 -0.0243 66  PHE A CG  
529  C  CD1 . PHE A 66  ? 0.2263 0.2703 0.1107 0.0108  -0.0666 -0.0133 66  PHE A CD1 
530  C  CD2 . PHE A 66  ? 0.2634 0.2556 0.1778 0.0377  -0.0629 -0.0139 66  PHE A CD2 
531  C  CE1 . PHE A 66  ? 0.2525 0.2373 0.1616 -0.0150 -0.0774 -0.0083 66  PHE A CE1 
532  C  CE2 . PHE A 66  ? 0.2752 0.2453 0.1514 0.0062  -0.0802 -0.0499 66  PHE A CE2 
533  C  CZ  . PHE A 66  ? 0.2640 0.2356 0.1274 0.0026  -0.0583 -0.0188 66  PHE A CZ  
534  N  N   . LYS A 67  ? 0.2647 0.2269 0.1663 0.0391  -0.0745 0.0152  67  LYS A N   
535  C  CA  . LYS A 67  ? 0.2773 0.2254 0.1279 0.0405  -0.0946 0.0211  67  LYS A CA  
536  C  C   . LYS A 67  ? 0.2602 0.2239 0.0767 0.0269  -0.0717 0.0241  67  LYS A C   
537  O  O   . LYS A 67  ? 0.2953 0.2846 0.0665 0.0550  -0.0585 0.0350  67  LYS A O   
538  C  CB  . LYS A 67  ? 0.3370 0.2657 0.2433 -0.0430 -0.1544 0.0577  67  LYS A CB  
539  C  CG  . LYS A 67  ? 0.3486 0.3092 0.2839 -0.0625 -0.1240 0.0025  67  LYS A CG  
540  C  CD  . LYS A 67  ? 0.4417 0.3269 0.3070 -0.1482 -0.1054 -0.0114 67  LYS A CD  
541  C  CE  . LYS A 67  ? 0.4628 0.4005 0.5387 -0.1037 -0.1065 0.0474  67  LYS A CE  
542  N  NZ  . LYS A 67  ? 0.5515 0.4525 0.5163 -0.2026 -0.0493 -0.0137 67  LYS A NZ  
543  N  N   . VAL A 68  ? 0.2508 0.1800 0.1403 0.0158  -0.0572 0.0337  68  VAL A N   
544  C  CA  . VAL A 68  ? 0.2570 0.1649 0.1426 0.0348  -0.0547 0.0248  68  VAL A CA  
545  C  C   . VAL A 68  ? 0.2697 0.1735 0.1232 0.0138  -0.0502 0.0337  68  VAL A C   
546  O  O   . VAL A 68  ? 0.3005 0.2037 0.1015 0.0054  -0.0697 0.0272  68  VAL A O   
547  C  CB  . VAL A 68  ? 0.2651 0.1807 0.1267 0.0181  -0.0362 0.0143  68  VAL A CB  
548  C  CG1 . VAL A 68  ? 0.2987 0.2215 0.1257 0.0420  -0.0743 0.0175  68  VAL A CG1 
549  C  CG2 . VAL A 68  ? 0.3067 0.2178 0.1403 -0.0016 -0.0789 -0.0309 68  VAL A CG2 
550  N  N   . GLU A 69  ? 0.2883 0.1843 0.1478 -0.0047 -0.0878 0.0414  69  GLU A N   
551  C  CA  . GLU A 69  ? 0.2779 0.1737 0.1375 0.0164  -0.0682 0.0278  69  GLU A CA  
552  C  C   . GLU A 69  ? 0.2740 0.1570 0.2047 0.0102  -0.1092 0.0097  69  GLU A C   
553  O  O   . GLU A 69  ? 0.3337 0.2011 0.2096 0.0375  -0.1474 0.0121  69  GLU A O   
554  C  CB  . GLU A 69  ? 0.3412 0.2679 0.2004 0.0055  0.0067  0.0586  69  GLU A CB  
555  C  CG  . GLU A 69  ? 0.3212 0.3648 0.4467 -0.0145 -0.0472 0.0125  69  GLU A CG  
556  C  CD  . GLU A 69  ? 0.5598 0.4986 0.3359 -0.1946 0.0179  0.0057  69  GLU A CD  
557  O  OE1 . GLU A 69  ? 0.7127 0.7925 0.4545 -0.0938 0.1852  0.0388  69  GLU A OE1 
558  O  OE2 . GLU A 69  ? 0.7736 0.7488 0.4794 -0.0903 -0.1405 -0.1480 69  GLU A OE2 
559  N  N   . PHE A 70  ? 0.2462 0.1891 0.1748 0.0150  -0.0754 0.0265  70  PHE A N   
560  C  CA  . PHE A 70  ? 0.2654 0.1606 0.1512 0.0110  -0.0806 0.0120  70  PHE A CA  
561  C  C   . PHE A 70  ? 0.2438 0.1643 0.1850 -0.0353 -0.0629 0.0225  70  PHE A C   
562  O  O   . PHE A 70  ? 0.2773 0.1846 0.2560 -0.0425 -0.1020 0.0323  70  PHE A O   
563  C  CB  . PHE A 70  ? 0.2622 0.1782 0.1282 -0.0124 -0.0857 0.0115  70  PHE A CB  
564  C  CG  . PHE A 70  ? 0.2534 0.1661 0.1455 0.0027  -0.0832 0.0125  70  PHE A CG  
565  C  CD1 . PHE A 70  ? 0.2746 0.1631 0.1882 0.0184  -0.0686 0.0237  70  PHE A CD1 
566  C  CD2 . PHE A 70  ? 0.2615 0.1868 0.1476 -0.0199 -0.0899 0.0285  70  PHE A CD2 
567  C  CE1 . PHE A 70  ? 0.2931 0.1981 0.1857 -0.0297 -0.0053 0.0407  70  PHE A CE1 
568  C  CE2 . PHE A 70  ? 0.2904 0.1688 0.1526 -0.0018 -0.0651 0.0264  70  PHE A CE2 
569  C  CZ  . PHE A 70  ? 0.3017 0.1710 0.1745 -0.0159 -0.0370 0.0170  70  PHE A CZ  
570  N  N   . ASP A 71  ? 0.2938 0.1615 0.1967 -0.0079 -0.1074 0.0328  71  ASP A N   
571  C  CA  . ASP A 71  ? 0.2596 0.1620 0.2223 -0.0108 -0.0995 0.0334  71  ASP A CA  
572  C  C   . ASP A 71  ? 0.2649 0.1562 0.2535 -0.0247 -0.0656 0.0143  71  ASP A C   
573  O  O   . ASP A 71  ? 0.2957 0.2302 0.3050 -0.0456 -0.0520 -0.0232 71  ASP A O   
574  C  CB  . ASP A 71  ? 0.3269 0.1875 0.2822 0.0300  -0.1406 0.0244  71  ASP A CB  
575  C  CG  . ASP A 71  ? 0.3483 0.1875 0.3472 0.0141  -0.1795 0.0308  71  ASP A CG  
576  O  OD1 . ASP A 71  ? 0.3596 0.1972 0.3422 -0.0109 -0.1710 0.0469  71  ASP A OD1 
577  O  OD2 . ASP A 71  ? 0.3239 0.2319 0.4517 0.0212  -0.1817 0.0435  71  ASP A OD2 
578  N  N   . ASP A 72  ? 0.3171 0.1498 0.2218 -0.0361 -0.0998 0.0375  72  ASP A N   
579  C  CA  . ASP A 72  ? 0.3185 0.1533 0.2090 -0.0225 -0.0929 0.0348  72  ASP A CA  
580  C  C   . ASP A 72  ? 0.3278 0.1602 0.2975 -0.0309 -0.1327 0.0370  72  ASP A C   
581  O  O   . ASP A 72  ? 0.4065 0.1738 0.3229 -0.0080 -0.1840 0.0162  72  ASP A O   
582  C  CB  . ASP A 72  ? 0.3345 0.1458 0.2204 0.0061  -0.0948 0.0417  72  ASP A CB  
583  C  CG  . ASP A 72  ? 0.3615 0.1907 0.2060 -0.0188 -0.1042 0.0383  72  ASP A CG  
584  O  OD1 . ASP A 72  ? 0.3616 0.2920 0.2471 -0.0364 -0.1254 0.1119  72  ASP A OD1 
585  O  OD2 . ASP A 72  ? 0.3687 0.2816 0.1939 0.0228  -0.1100 0.0489  72  ASP A OD2 
586  N  N   . SER A 73  ? 0.3491 0.1627 0.3104 -0.0342 -0.1398 0.0571  73  SER A N   
587  C  CA  . SER A 73  ? 0.3960 0.1759 0.2944 -0.0359 -0.1526 0.0217  73  SER A CA  
588  C  C   . SER A 73  ? 0.3803 0.1504 0.4218 -0.0248 -0.1552 -0.0121 73  SER A C   
589  O  O   . SER A 73  ? 0.4808 0.1494 0.3949 -0.0147 -0.1797 -0.0066 73  SER A O   
590  C  CB  . SER A 73  ? 0.4028 0.2046 0.3323 -0.0275 -0.1011 0.0080  73  SER A CB  
591  O  OG  . SER A 73  ? 0.4293 0.1789 0.3861 0.0075  -0.1522 0.0389  73  SER A OG  
592  N  N   . GLN A 74  ? 0.3235 0.1871 0.4456 -0.0229 -0.1026 -0.0206 74  GLN A N   
593  C  CA  . GLN A 74  ? 0.4373 0.2269 0.3268 0.0502  -0.1029 0.0070  74  GLN A CA  
594  C  C   . GLN A 74  ? 0.3861 0.2471 0.3016 -0.0243 -0.1597 -0.0379 74  GLN A C   
595  O  O   . GLN A 74  ? 0.3857 0.2184 0.3133 -0.0257 -0.1144 -0.0178 74  GLN A O   
596  C  CB  . GLN A 74  ? 0.4628 0.3420 0.3515 0.1490  -0.1132 0.0794  74  GLN A CB  
597  C  CG  . GLN A 74  ? 0.3823 0.3920 0.5160 0.0559  -0.1171 0.1310  74  GLN A CG  
598  C  CD  . GLN A 74  ? 0.4524 0.5280 0.4740 0.1209  -0.1985 0.0597  74  GLN A CD  
599  O  OE1 . GLN A 74  ? 0.5160 0.7379 0.6054 0.0490  -0.0179 0.2210  74  GLN A OE1 
600  N  NE2 . GLN A 74  ? 0.4539 0.3956 0.4351 0.0354  -0.1311 0.0946  74  GLN A NE2 
601  N  N   . ASP A 75  ? 0.4046 0.3227 0.3312 -0.0259 -0.1659 -0.0407 75  ASP A N   
602  C  CA  . ASP A 75  ? 0.4084 0.3669 0.3752 -0.0675 -0.1031 -0.0273 75  ASP A CA  
603  C  C   . ASP A 75  ? 0.3420 0.3280 0.5004 0.1045  -0.2214 -0.1103 75  ASP A C   
604  O  O   . ASP A 75  ? 0.3920 0.9060 0.7177 -0.0165 -0.0996 -0.2567 75  ASP A O   
605  C  CB  . ASP A 75  ? 0.5565 0.3407 0.4703 0.1274  -0.1531 -0.1373 75  ASP A CB  
606  C  CG  . ASP A 75  ? 0.5313 0.4571 0.4894 0.0919  -0.1467 -0.1385 75  ASP A CG  
607  O  OD1 . ASP A 75  ? 0.5277 0.6781 0.4072 0.1421  -0.1886 -0.2226 75  ASP A OD1 
608  O  OD2 . ASP A 75  ? 0.7210 0.6248 0.4463 0.1272  0.0659  -0.0597 75  ASP A OD2 
609  N  N   . LYS A 76  ? 0.3283 0.2696 0.3055 0.0599  -0.1368 0.0381  76  LYS A N   
610  C  CA  . LYS A 76  ? 0.3273 0.2435 0.3640 -0.0192 -0.1093 0.0529  76  LYS A CA  
611  C  C   . LYS A 76  ? 0.3731 0.3474 0.3796 0.1041  0.0046  0.1584  76  LYS A C   
612  O  O   . LYS A 76  ? 0.3355 0.5168 0.6669 0.0666  0.0219  0.2027  76  LYS A O   
613  C  CB  . LYS A 76  ? 0.4449 0.2628 0.3237 -0.0431 -0.1492 0.0442  76  LYS A CB  
614  C  CG  . LYS A 76  ? 0.4237 0.2813 0.3953 0.0394  -0.1283 0.0599  76  LYS A CG  
615  C  CD  . LYS A 76  ? 0.4381 0.2568 0.3972 -0.0453 -0.0850 0.0263  76  LYS A CD  
616  C  CE  . LYS A 76  ? 0.4652 0.3431 0.3404 0.0659  -0.1478 -0.0066 76  LYS A CE  
617  N  NZ  . LYS A 76  ? 0.5234 0.3328 0.3434 0.0446  -0.1124 0.0019  76  LYS A NZ  
618  N  N   . ALA A 77  ? 0.3578 0.2908 0.3104 0.0684  -0.1068 0.0969  77  ALA A N   
619  C  CA  . ALA A 77  ? 0.3032 0.2345 0.2681 -0.0026 -0.1070 0.0186  77  ALA A CA  
620  C  C   . ALA A 77  ? 0.2397 0.2290 0.3101 0.0263  -0.1097 0.0214  77  ALA A C   
621  O  O   . ALA A 77  ? 0.2442 0.3225 0.3525 0.0117  -0.1144 -0.0672 77  ALA A O   
622  C  CB  . ALA A 77  ? 0.3171 0.3028 0.2864 0.0245  -0.1144 0.0170  77  ALA A CB  
623  N  N   . VAL A 78  ? 0.2335 0.2214 0.2628 0.0015  -0.1023 0.0079  78  VAL A N   
624  C  CA  . VAL A 78  ? 0.2546 0.2324 0.2626 -0.0179 -0.1150 0.0276  78  VAL A CA  
625  C  C   . VAL A 78  ? 0.1974 0.2247 0.2828 -0.0052 -0.0740 0.0075  78  VAL A C   
626  O  O   . VAL A 78  ? 0.2378 0.2435 0.3283 -0.0353 -0.1244 0.0268  78  VAL A O   
627  C  CB  . VAL A 78  ? 0.3333 0.2591 0.3350 -0.0042 -0.0850 -0.0233 78  VAL A CB  
628  C  CG1 . VAL A 78  ? 0.4259 0.1907 0.4954 0.0078  -0.0857 0.0428  78  VAL A CG1 
629  C  CG2 . VAL A 78  ? 0.3024 0.3792 0.4608 0.0381  -0.0543 -0.1187 78  VAL A CG2 
630  N  N   . LEU A 79  ? 0.1972 0.1965 0.2764 -0.0052 -0.0684 0.0065  79  LEU A N   
631  C  CA  . LEU A 79  ? 0.2392 0.1899 0.2496 -0.0041 -0.0735 -0.0131 79  LEU A CA  
632  C  C   . LEU A 79  ? 0.2265 0.2117 0.2696 -0.0027 -0.0540 -0.0215 79  LEU A C   
633  O  O   . LEU A 79  ? 0.2715 0.2438 0.2828 -0.0695 -0.0345 -0.0307 79  LEU A O   
634  C  CB  . LEU A 79  ? 0.2202 0.2283 0.3467 -0.0108 -0.0950 0.0228  79  LEU A CB  
635  C  CG  . LEU A 79  ? 0.2362 0.2517 0.2739 0.0125  -0.0602 0.0033  79  LEU A CG  
636  C  CD1 . LEU A 79  ? 0.2324 0.2252 0.5105 -0.0017 0.0041  0.0237  79  LEU A CD1 
637  C  CD2 . LEU A 79  ? 0.2252 0.2816 0.2449 0.0272  -0.0247 0.0263  79  LEU A CD2 
638  N  N   . LYS A 80  ? 0.2605 0.2509 0.2703 -0.0183 -0.0425 -0.0065 80  LYS A N   
639  C  CA  . LYS A 80  ? 0.3200 0.2757 0.2710 -0.0108 -0.0127 -0.0291 80  LYS A CA  
640  C  C   . LYS A 80  ? 0.2566 0.2509 0.3122 0.0051  -0.0075 -0.0283 80  LYS A C   
641  O  O   . LYS A 80  ? 0.2405 0.2610 0.2908 -0.0436 -0.0653 -0.0168 80  LYS A O   
642  C  CB  . LYS A 80  ? 0.3613 0.3322 0.3605 0.0441  -0.0122 -0.0176 80  LYS A CB  
643  C  CG  . LYS A 80  ? 0.3935 0.3979 0.4660 0.0829  -0.0967 -0.1430 80  LYS A CG  
644  C  CD  . LYS A 80  ? 0.4142 0.3903 0.7197 0.0929  -0.1411 -0.1470 80  LYS A CD  
645  N  N   . GLY A 81  ? 0.3086 0.2829 0.2813 0.0000  0.0262  -0.0200 81  GLY A N   
646  C  CA  . GLY A 81  ? 0.2446 0.3022 0.3405 0.0236  0.0290  0.0265  81  GLY A CA  
647  C  C   . GLY A 81  ? 0.2997 0.2550 0.2906 0.0296  0.0719  0.0315  81  GLY A C   
648  O  O   . GLY A 81  ? 0.2494 0.2943 0.2755 -0.0214 0.0168  -0.0395 81  GLY A O   
649  N  N   . GLY A 82  ? 0.3298 0.2409 0.4338 0.0048  0.0537  0.0522  82  GLY A N   
650  C  CA  . GLY A 82  ? 0.3488 0.2144 0.6099 0.0446  0.0763  0.0200  82  GLY A CA  
651  C  C   . GLY A 82  ? 0.3015 0.2845 0.4584 0.1020  0.0967  0.0752  82  GLY A C   
652  O  O   . GLY A 82  ? 0.3785 0.4556 0.3987 0.1747  0.1265  0.0903  82  GLY A O   
653  N  N   . PRO A 83  ? 0.2605 0.2482 0.4122 0.0361  0.0500  0.0296  83  PRO A N   
654  C  CA  . PRO A 83  ? 0.3137 0.2511 0.2846 0.0576  0.0312  0.0142  83  PRO A CA  
655  C  C   . PRO A 83  ? 0.3256 0.2764 0.2427 0.0433  0.0046  0.0220  83  PRO A C   
656  O  O   . PRO A 83  ? 0.3568 0.4160 0.3193 0.0710  -0.0998 0.0000  83  PRO A O   
657  C  CB  . PRO A 83  ? 0.2888 0.3483 0.2160 0.0932  -0.0013 0.0502  83  PRO A CB  
658  C  CG  . PRO A 83  ? 0.2441 0.3208 0.2360 0.0690  -0.0070 0.0197  83  PRO A CG  
659  C  CD  . PRO A 83  ? 0.2196 0.2425 0.4094 0.0565  0.0248  -0.0136 83  PRO A CD  
660  N  N   . LEU A 84  ? 0.3199 0.2266 0.2425 0.0449  0.0035  -0.0251 84  LEU A N   
661  C  CA  . LEU A 84  ? 0.2772 0.1997 0.2011 0.0208  -0.0148 -0.0403 84  LEU A CA  
662  C  C   . LEU A 84  ? 0.2718 0.2462 0.2586 0.0430  -0.0190 -0.0647 84  LEU A C   
663  O  O   . LEU A 84  ? 0.3057 0.2851 0.4005 0.0155  0.0462  -0.1164 84  LEU A O   
664  C  CB  . LEU A 84  ? 0.3092 0.2141 0.2013 0.0381  0.0038  -0.0364 84  LEU A CB  
665  C  CG  . LEU A 84  ? 0.2324 0.1899 0.2374 0.0466  -0.0265 -0.0228 84  LEU A CG  
666  C  CD1 . LEU A 84  ? 0.2663 0.2628 0.2234 0.0241  -0.0483 -0.0230 84  LEU A CD1 
667  C  CD2 . LEU A 84  ? 0.2169 0.2333 0.2268 0.0102  -0.0188 -0.0164 84  LEU A CD2 
668  N  N   . ASP A 85  ? 0.3290 0.2369 0.3245 0.0085  -0.0077 -0.0847 85  ASP A N   
669  C  CA  . ASP A 85  ? 0.3859 0.2320 0.3774 -0.0076 0.0050  -0.0902 85  ASP A CA  
670  C  C   . ASP A 85  ? 0.3698 0.1871 0.5411 0.0000  0.0399  -0.0182 85  ASP A C   
671  O  O   . ASP A 85  ? 0.3824 0.4208 0.6194 0.0025  0.0735  -0.0091 85  ASP A O   
672  C  CB  . ASP A 85  ? 0.5540 0.2643 0.4050 0.0699  -0.1497 -0.1284 85  ASP A CB  
673  C  CG  . ASP A 85  ? 0.6362 0.5045 0.5606 -0.0356 0.0313  -0.0098 85  ASP A CG  
674  O  OD1 . ASP A 85  ? 0.6352 0.8536 0.3459 -0.0335 0.1337  0.0049  85  ASP A OD1 
675  O  OD2 . ASP A 85  ? 0.6211 0.5188 0.6476 -0.1203 0.0487  -0.1472 85  ASP A OD2 
676  N  N   . GLY A 86  ? 0.3550 0.3911 0.5838 0.0750  0.1231  0.0604  86  GLY A N   
677  C  CA  . GLY A 86  ? 0.4962 0.3212 0.4043 -0.1293 0.0217  -0.0661 86  GLY A CA  
678  C  C   . GLY A 86  ? 0.3979 0.2819 0.3612 -0.0876 -0.1211 0.0088  86  GLY A C   
679  O  O   . GLY A 86  ? 0.4287 0.3158 0.4800 -0.1124 -0.0820 0.0753  86  GLY A O   
680  N  N   . THR A 87  ? 0.3159 0.2584 0.3177 0.0474  -0.0280 -0.0337 87  THR A N   
681  C  CA  . THR A 87  ? 0.2474 0.2782 0.3493 0.0424  -0.0275 -0.0518 87  THR A CA  
682  C  C   . THR A 87  ? 0.2175 0.1782 0.3061 0.0190  -0.0375 -0.0332 87  THR A C   
683  O  O   . THR A 87  ? 0.2551 0.1710 0.3774 -0.0088 -0.0157 -0.0342 87  THR A O   
684  C  CB  . THR A 87  ? 0.2680 0.5635 0.2980 0.1782  -0.0893 -0.0343 87  THR A CB  
685  O  OG1 . THR A 87  ? 0.3458 0.5358 0.6003 0.1280  0.0024  -0.1659 87  THR A OG1 
686  C  CG2 . THR A 87  ? 0.2782 0.4436 0.4101 0.0737  -0.1500 -0.0803 87  THR A CG2 
687  N  N   . TYR A 88  ? 0.2043 0.1807 0.3221 0.0144  -0.0537 -0.0297 88  TYR A N   
688  C  CA  . TYR A 88  ? 0.1967 0.1716 0.2992 0.0312  -0.0671 -0.0335 88  TYR A CA  
689  C  C   . TYR A 88  ? 0.1903 0.1961 0.3260 0.0089  -0.0933 -0.0085 88  TYR A C   
690  O  O   . TYR A 88  ? 0.2518 0.2646 0.3630 -0.0790 -0.1350 0.0791  88  TYR A O   
691  C  CB  . TYR A 88  ? 0.2115 0.1766 0.2576 0.0117  -0.0706 -0.0207 88  TYR A CB  
692  C  CG  . TYR A 88  ? 0.2065 0.1411 0.2313 0.0100  -0.0358 -0.0232 88  TYR A CG  
693  C  CD1 . TYR A 88  ? 0.2335 0.1742 0.2057 0.0302  -0.0572 -0.0313 88  TYR A CD1 
694  C  CD2 . TYR A 88  ? 0.2153 0.1638 0.1983 0.0201  -0.0506 -0.0081 88  TYR A CD2 
695  C  CE1 . TYR A 88  ? 0.2330 0.1868 0.1928 0.0260  -0.0365 -0.0267 88  TYR A CE1 
696  C  CE2 . TYR A 88  ? 0.1849 0.1652 0.1898 0.0093  -0.0386 -0.0002 88  TYR A CE2 
697  C  CZ  . TYR A 88  ? 0.2232 0.1713 0.2221 -0.0033 -0.0408 -0.0441 88  TYR A CZ  
698  O  OH  . TYR A 88  ? 0.2299 0.2148 0.2044 -0.0006 -0.0364 -0.0334 88  TYR A OH  
699  N  N   . ARG A 89  ? 0.1904 0.1652 0.2696 0.0228  -0.0751 -0.0493 89  ARG A N   
700  C  CA  . ARG A 89  ? 0.2363 0.1388 0.2766 0.0286  -0.1337 -0.0168 89  ARG A CA  
701  C  C   . ARG A 89  ? 0.2040 0.1383 0.2152 0.0064  -0.0996 0.0218  89  ARG A C   
702  O  O   . ARG A 89  ? 0.2051 0.1637 0.1433 0.0150  -0.0732 0.0000  89  ARG A O   
703  C  CB  . ARG A 89  ? 0.3027 0.1282 0.4090 0.0100  -0.1635 0.0155  89  ARG A CB  
704  C  CG  . ARG A 89  ? 0.3989 0.2710 0.3770 0.1095  -0.1242 0.0379  89  ARG A CG  
705  C  CD  . ARG A 89  ? 0.4046 0.2524 0.3512 0.0863  -0.1416 0.0701  89  ARG A CD  
706  N  NE  . ARG A 89  ? 0.3784 0.4440 0.2699 0.1166  -0.1527 -0.0834 89  ARG A NE  
707  C  CZ  . ARG A 89  ? 0.4532 0.4087 0.5302 0.1493  -0.1857 -0.0529 89  ARG A CZ  
708  N  NH1 . ARG A 89  ? 0.5132 0.2532 0.3291 0.1146  -0.1891 -0.0651 89  ARG A NH1 
709  N  NH2 . ARG A 89  ? 0.5006 0.4837 0.6420 0.1902  -0.2548 -0.1648 89  ARG A NH2 
710  N  N   . LEU A 90  ? 0.2168 0.1573 0.2081 -0.0054 -0.1115 0.0118  90  LEU A N   
711  C  CA  . LEU A 90  ? 0.1988 0.1568 0.2169 -0.0095 -0.0812 0.0245  90  LEU A CA  
712  C  C   . LEU A 90  ? 0.2128 0.1573 0.1590 -0.0015 -0.0915 0.0130  90  LEU A C   
713  O  O   . LEU A 90  ? 0.2406 0.2125 0.2338 0.0013  -0.1154 0.0566  90  LEU A O   
714  C  CB  . LEU A 90  ? 0.1999 0.1726 0.2125 -0.0077 -0.0869 -0.0044 90  LEU A CB  
715  C  CG  . LEU A 90  ? 0.2499 0.1699 0.1735 -0.0075 -0.1030 0.0034  90  LEU A CG  
716  C  CD1 . LEU A 90  ? 0.2462 0.1947 0.1537 0.0086  -0.0853 0.0151  90  LEU A CD1 
717  C  CD2 . LEU A 90  ? 0.2546 0.1968 0.2198 -0.0221 -0.1045 -0.0077 90  LEU A CD2 
718  N  N   . THR A 91  ? 0.2122 0.1527 0.1631 -0.0076 -0.0565 0.0118  91  THR A N   
719  C  CA  . THR A 91  ? 0.2064 0.1558 0.1598 0.0072  -0.0578 0.0141  91  THR A CA  
720  C  C   . THR A 91  ? 0.2624 0.1425 0.1273 -0.0083 -0.0886 0.0132  91  THR A C   
721  O  O   . THR A 91  ? 0.2417 0.1681 0.1266 -0.0017 -0.0859 0.0289  91  THR A O   
722  C  CB  . THR A 91  ? 0.2750 0.1990 0.1766 -0.0571 -0.0948 0.0493  91  THR A CB  
723  O  OG1 . THR A 91  ? 0.3297 0.3073 0.2001 -0.1238 -0.1147 0.0701  91  THR A OG1 
724  C  CG2 . THR A 91  ? 0.2782 0.1752 0.2018 -0.0203 -0.1156 -0.0017 91  THR A CG2 
725  N  N   . GLN A 92  ? 0.2313 0.1379 0.1354 0.0046  -0.0829 0.0106  92  GLN A N   
726  C  CA  . GLN A 92  ? 0.2371 0.1401 0.1309 0.0048  -0.0708 0.0321  92  GLN A CA  
727  C  C   . GLN A 92  ? 0.2033 0.1401 0.0938 0.0057  -0.0478 0.0242  92  GLN A C   
728  O  O   . GLN A 92  ? 0.2541 0.1465 0.0927 -0.0031 -0.0458 0.0307  92  GLN A O   
729  C  CB  . GLN A 92  ? 0.2293 0.2039 0.1447 0.0029  -0.0782 0.0216  92  GLN A CB  
730  C  CG  . GLN A 92  ? 0.2676 0.2057 0.1421 -0.0091 -0.0910 0.0275  92  GLN A CG  
731  C  CD  . GLN A 92  ? 0.2478 0.2190 0.1146 -0.0243 -0.0837 0.0584  92  GLN A CD  
732  O  OE1 . GLN A 92  ? 0.2528 0.2230 0.1782 -0.0269 -0.0508 0.0447  92  GLN A OE1 
733  N  NE2 . GLN A 92  ? 0.2449 0.3204 0.2994 -0.0183 -0.0620 0.0969  92  GLN A NE2 
734  N  N   . PHE A 93  ? 0.2051 0.1297 0.1397 -0.0062 -0.0766 0.0089  93  PHE A N   
735  C  CA  . PHE A 93  ? 0.2058 0.1363 0.1408 -0.0075 -0.0452 0.0266  93  PHE A CA  
736  C  C   . PHE A 93  ? 0.1922 0.1534 0.0893 -0.0189 -0.0762 0.0253  93  PHE A C   
737  O  O   . PHE A 93  ? 0.2306 0.1509 0.0893 -0.0002 -0.0692 0.0085  93  PHE A O   
738  C  CB  . PHE A 93  ? 0.2175 0.1799 0.1008 -0.0216 -0.0828 0.0370  93  PHE A CB  
739  C  CG  . PHE A 93  ? 0.2219 0.1541 0.1112 -0.0025 -0.0829 0.0247  93  PHE A CG  
740  C  CD1 . PHE A 93  ? 0.2538 0.1712 0.1350 0.0043  -0.0832 -0.0092 93  PHE A CD1 
741  C  CD2 . PHE A 93  ? 0.2252 0.1785 0.1324 0.0190  -0.0949 0.0397  93  PHE A CD2 
742  C  CE1 . PHE A 93  ? 0.2264 0.1687 0.1342 -0.0078 -0.0877 0.0114  93  PHE A CE1 
743  C  CE2 . PHE A 93  ? 0.2415 0.1810 0.1432 -0.0057 -0.0891 0.0244  93  PHE A CE2 
744  C  CZ  . PHE A 93  ? 0.2226 0.1627 0.1735 -0.0004 -0.0652 0.0334  93  PHE A CZ  
745  N  N   . HIS A 94  ? 0.1900 0.1390 0.1084 0.0066  -0.0630 0.0081  94  HIS A N   
746  C  CA  . HIS A 94  ? 0.2115 0.1590 0.0914 -0.0083 -0.0502 0.0236  94  HIS A CA  
747  C  C   . HIS A 94  ? 0.1530 0.1512 0.0632 -0.0036 -0.0520 0.0164  94  HIS A C   
748  O  O   . HIS A 94  ? 0.1979 0.1541 0.0880 0.0154  -0.0237 0.0167  94  HIS A O   
749  C  CB  . HIS A 94  ? 0.1992 0.1910 0.0538 -0.0133 -0.0578 0.0217  94  HIS A CB  
750  C  CG  . HIS A 94  ? 0.2119 0.1752 0.0658 -0.0270 -0.0819 0.0266  94  HIS A CG  
751  N  ND1 . HIS A 94  ? 0.2063 0.1713 0.0987 -0.0326 -0.0612 0.0008  94  HIS A ND1 
752  C  CD2 . HIS A 94  ? 0.2329 0.2101 0.0263 -0.0090 -0.0622 0.0268  94  HIS A CD2 
753  C  CE1 . HIS A 94  ? 0.2264 0.1421 0.0972 -0.0103 -0.0521 0.0140  94  HIS A CE1 
754  N  NE2 . HIS A 94  ? 0.1949 0.1846 0.0392 -0.0100 -0.0507 0.0077  94  HIS A NE2 
755  N  N   . PHE A 95  ? 0.1726 0.1572 0.1012 0.0067  -0.0538 -0.0136 95  PHE A N   
756  C  CA  . PHE A 95  ? 0.1799 0.1336 0.1313 -0.0081 -0.0564 -0.0048 95  PHE A CA  
757  C  C   . PHE A 95  ? 0.1814 0.1708 0.1155 -0.0166 -0.0457 0.0000  95  PHE A C   
758  O  O   . PHE A 95  ? 0.1924 0.1748 0.1048 -0.0012 -0.0342 0.0151  95  PHE A O   
759  C  CB  . PHE A 95  ? 0.1745 0.1745 0.1429 -0.0117 -0.0555 -0.0314 95  PHE A CB  
760  C  CG  . PHE A 95  ? 0.1889 0.1947 0.0961 -0.0038 -0.0619 -0.0156 95  PHE A CG  
761  C  CD1 . PHE A 95  ? 0.2293 0.1813 0.1120 -0.0168 -0.0789 -0.0114 95  PHE A CD1 
762  C  CD2 . PHE A 95  ? 0.1920 0.2262 0.0974 -0.0205 -0.0408 -0.0325 95  PHE A CD2 
763  C  CE1 . PHE A 95  ? 0.2257 0.1864 0.1404 -0.0008 -0.0813 -0.0121 95  PHE A CE1 
764  C  CE2 . PHE A 95  ? 0.2004 0.1770 0.1558 -0.0063 -0.0555 -0.0373 95  PHE A CE2 
765  C  CZ  . PHE A 95  ? 0.2453 0.1787 0.1688 -0.0187 -0.0743 -0.0355 95  PHE A CZ  
766  N  N   . HIS A 96  ? 0.1821 0.1649 0.0967 -0.0058 -0.0414 0.0005  96  HIS A N   
767  C  CA  . HIS A 96  ? 0.1986 0.1584 0.0832 0.0114  -0.0373 -0.0044 96  HIS A CA  
768  C  C   . HIS A 96  ? 0.1744 0.1708 0.1020 -0.0027 -0.0281 0.0093  96  HIS A C   
769  O  O   . HIS A 96  ? 0.1752 0.1809 0.0857 0.0018  -0.0259 -0.0074 96  HIS A O   
770  C  CB  . HIS A 96  ? 0.2143 0.1584 0.0850 -0.0149 -0.0408 -0.0009 96  HIS A CB  
771  C  CG  . HIS A 96  ? 0.1841 0.1494 0.1094 0.0059  -0.0450 -0.0059 96  HIS A CG  
772  N  ND1 . HIS A 96  ? 0.1733 0.1625 0.1498 -0.0034 -0.0534 -0.0089 96  HIS A ND1 
773  C  CD2 . HIS A 96  ? 0.1864 0.1394 0.0954 0.0134  -0.0297 0.0037  96  HIS A CD2 
774  C  CE1 . HIS A 96  ? 0.2075 0.1681 0.0832 0.0034  -0.0229 -0.0024 96  HIS A CE1 
775  N  NE2 . HIS A 96  ? 0.2011 0.1067 0.1303 0.0200  -0.0433 0.0011  96  HIS A NE2 
776  N  N   . TRP A 97  ? 0.1999 0.1555 0.0890 -0.0011 -0.0299 -0.0052 97  TRP A N   
777  C  CA  . TRP A 97  ? 0.1953 0.1512 0.0853 0.0042  -0.0449 -0.0136 97  TRP A CA  
778  C  C   . TRP A 97  ? 0.1954 0.1687 0.0599 0.0059  -0.0222 -0.0216 97  TRP A C   
779  O  O   . TRP A 97  ? 0.1911 0.1722 0.1254 0.0050  -0.0165 -0.0069 97  TRP A O   
780  C  CB  . TRP A 97  ? 0.2178 0.1993 0.0582 0.0032  -0.0344 -0.0356 97  TRP A CB  
781  C  CG  . TRP A 97  ? 0.2015 0.1666 0.0660 0.0032  -0.0334 -0.0184 97  TRP A CG  
782  C  CD1 . TRP A 97  ? 0.1904 0.2182 0.0929 -0.0052 -0.0278 -0.0390 97  TRP A CD1 
783  C  CD2 . TRP A 97  ? 0.2208 0.1594 0.0839 -0.0121 -0.0291 -0.0274 97  TRP A CD2 
784  N  NE1 . TRP A 97  ? 0.2061 0.1907 0.1203 0.0084  -0.0521 0.0076  97  TRP A NE1 
785  C  CE2 . TRP A 97  ? 0.2018 0.1835 0.0908 0.0082  -0.0294 0.0031  97  TRP A CE2 
786  C  CE3 . TRP A 97  ? 0.1916 0.1573 0.1067 -0.0040 -0.0491 -0.0075 97  TRP A CE3 
787  C  CZ2 . TRP A 97  ? 0.2263 0.1947 0.1220 -0.0137 -0.0540 0.0133  97  TRP A CZ2 
788  C  CZ3 . TRP A 97  ? 0.2071 0.2164 0.0918 -0.0260 -0.0361 0.0083  97  TRP A CZ3 
789  C  CH2 . TRP A 97  ? 0.2106 0.2029 0.0902 -0.0008 -0.0335 0.0173  97  TRP A CH2 
790  N  N   . GLY A 98  ? 0.2367 0.1526 0.0680 0.0108  -0.0414 -0.0201 98  GLY A N   
791  C  CA  . GLY A 98  ? 0.2215 0.1764 0.1170 0.0444  -0.0288 -0.0035 98  GLY A CA  
792  C  C   . GLY A 98  ? 0.2269 0.1598 0.1299 0.0168  -0.0447 -0.0273 98  GLY A C   
793  O  O   . GLY A 98  ? 0.2282 0.1958 0.1356 -0.0024 -0.0356 -0.0295 98  GLY A O   
794  N  N   . SER A 99  ? 0.2388 0.1776 0.1426 0.0322  -0.0157 -0.0335 99  SER A N   
795  C  CA  . SER A 99  ? 0.2771 0.1981 0.1512 0.0155  0.0166  -0.0577 99  SER A CA  
796  C  C   . SER A 99  ? 0.2570 0.1706 0.1496 0.0384  -0.0505 -0.0115 99  SER A C   
797  O  O   . SER A 99  ? 0.3676 0.2694 0.2187 0.0091  -0.0724 -0.0854 99  SER A O   
798  C  CB  . SER A 99  ? 0.2990 0.3073 0.1282 0.0376  -0.0196 -0.0643 99  SER A CB  
799  O  OG  . SER A 99  ? 0.2769 0.2110 0.1996 0.0331  -0.0342 -0.0377 99  SER A OG  
800  N  N   . LEU A 100 ? 0.2308 0.1861 0.2241 -0.0039 -0.0168 -0.0297 100 LEU A N   
801  C  CA  . LEU A 100 ? 0.2496 0.1667 0.3383 0.0081  0.0212  -0.0255 100 LEU A CA  
802  C  C   . LEU A 100 ? 0.2365 0.2187 0.2033 0.0080  -0.0138 -0.0083 100 LEU A C   
803  O  O   . LEU A 100 ? 0.2990 0.2000 0.2074 0.0109  -0.0099 -0.0292 100 LEU A O   
804  C  CB  . LEU A 100 ? 0.3531 0.2200 0.4489 0.0753  0.0125  0.0148  100 LEU A CB  
805  C  CG  . LEU A 100 ? 0.4144 0.2830 0.3211 0.1023  -0.0163 -0.0263 100 LEU A CG  
806  C  CD1 . LEU A 100 ? 0.4127 0.4235 0.4628 0.1579  -0.0772 -0.0383 100 LEU A CD1 
807  C  CD2 . LEU A 100 ? 0.5699 0.4211 0.3118 0.0397  0.0898  -0.1473 100 LEU A CD2 
808  N  N   . ASP A 101 ? 0.2489 0.2078 0.2498 -0.0134 -0.0076 -0.0297 101 ASP A N   
809  C  CA  . ASP A 101 ? 0.2374 0.2022 0.2486 -0.0026 -0.0020 0.0144  101 ASP A CA  
810  C  C   . ASP A 101 ? 0.3067 0.1672 0.2530 0.0134  -0.0234 0.0275  101 ASP A C   
811  O  O   . ASP A 101 ? 0.3173 0.1943 0.3107 0.0131  -0.0212 0.0310  101 ASP A O   
812  C  CB  . ASP A 101 ? 0.2451 0.2159 0.3063 -0.0143 -0.0417 0.0374  101 ASP A CB  
813  C  CG  . ASP A 101 ? 0.2997 0.2676 0.3525 -0.0304 -0.0809 0.0391  101 ASP A CG  
814  O  OD1 . ASP A 101 ? 0.3450 0.2551 0.3116 -0.0386 -0.0231 0.0132  101 ASP A OD1 
815  O  OD2 . ASP A 101 ? 0.3250 0.2961 0.4419 -0.0794 -0.0760 0.0348  101 ASP A OD2 
816  N  N   . GLY A 102 ? 0.2960 0.1591 0.2806 -0.0254 -0.0598 0.0238  102 GLY A N   
817  C  CA  . GLY A 102 ? 0.3057 0.1949 0.2930 -0.0221 -0.0895 0.0469  102 GLY A CA  
818  C  C   . GLY A 102 ? 0.2842 0.1734 0.1950 -0.0081 -0.0324 0.0261  102 GLY A C   
819  O  O   . GLY A 102 ? 0.3139 0.2370 0.1949 -0.0211 -0.0252 0.0315  102 GLY A O   
820  N  N   . GLN A 103 ? 0.2455 0.1580 0.2008 -0.0096 -0.0138 0.0170  103 GLN A N   
821  C  CA  . GLN A 103 ? 0.2341 0.1511 0.1523 0.0084  -0.0108 0.0047  103 GLN A CA  
822  C  C   . GLN A 103 ? 0.2531 0.1464 0.1232 -0.0068 -0.0238 0.0072  103 GLN A C   
823  O  O   . GLN A 103 ? 0.2442 0.1870 0.1322 -0.0076 -0.0254 -0.0116 103 GLN A O   
824  C  CB  . GLN A 103 ? 0.2322 0.1935 0.1261 0.0193  -0.0142 -0.0201 103 GLN A CB  
825  C  CG  . GLN A 103 ? 0.2518 0.2011 0.1315 0.0245  0.0119  0.0227  103 GLN A CG  
826  C  CD  . GLN A 103 ? 0.3222 0.2648 0.2341 0.1105  0.0583  0.0574  103 GLN A CD  
827  O  OE1 . GLN A 103 ? 0.4371 0.4153 0.4564 0.1936  0.1470  0.2244  103 GLN A OE1 
828  N  NE2 . GLN A 103 ? 0.2530 0.2667 0.1688 0.0592  0.0011  0.0322  103 GLN A NE2 
829  N  N   . GLY A 104 ? 0.1881 0.1527 0.1421 0.0078  -0.0353 0.0035  104 GLY A N   
830  C  CA  . GLY A 104 ? 0.1906 0.1652 0.1196 0.0097  -0.0480 -0.0158 104 GLY A CA  
831  C  C   . GLY A 104 ? 0.1508 0.1735 0.0914 -0.0111 -0.0203 -0.0136 104 GLY A C   
832  O  O   . GLY A 104 ? 0.2106 0.1749 0.1370 -0.0195 -0.0387 0.0052  104 GLY A O   
833  N  N   . SER A 105 ? 0.1658 0.1694 0.0900 0.0102  -0.0148 0.0001  105 SER A N   
834  C  CA  . SER A 105 ? 0.1756 0.1623 0.1335 -0.0055 -0.0257 -0.0281 105 SER A CA  
835  C  C   . SER A 105 ? 0.1662 0.1674 0.0861 0.0006  -0.0096 -0.0032 105 SER A C   
836  O  O   . SER A 105 ? 0.1831 0.1615 0.1430 0.0089  -0.0375 -0.0136 105 SER A O   
837  C  CB  . SER A 105 ? 0.1676 0.1591 0.1315 0.0236  -0.0318 0.0008  105 SER A CB  
838  O  OG  . SER A 105 ? 0.2019 0.1388 0.1435 0.0026  -0.0153 0.0038  105 SER A OG  
839  N  N   . GLU A 106 ? 0.1976 0.1460 0.1148 -0.0170 -0.0208 -0.0125 106 GLU A N   
840  C  CA  . GLU A 106 ? 0.1615 0.1483 0.0974 -0.0089 -0.0105 -0.0121 106 GLU A CA  
841  C  C   . GLU A 106 ? 0.1623 0.1443 0.0959 -0.0018 -0.0286 0.0066  106 GLU A C   
842  O  O   . GLU A 106 ? 0.1796 0.1676 0.1069 0.0065  -0.0403 0.0097  106 GLU A O   
843  C  CB  . GLU A 106 ? 0.2103 0.1458 0.0787 -0.0212 -0.0261 -0.0160 106 GLU A CB  
844  C  CG  . GLU A 106 ? 0.2282 0.1778 0.0954 -0.0067 -0.0003 -0.0144 106 GLU A CG  
845  C  CD  . GLU A 106 ? 0.1832 0.1898 0.1198 0.0175  -0.0335 0.0053  106 GLU A CD  
846  O  OE1 . GLU A 106 ? 0.1627 0.1868 0.1558 0.0151  -0.0384 -0.0177 106 GLU A OE1 
847  O  OE2 . GLU A 106 ? 0.1871 0.1807 0.1726 0.0179  -0.0284 -0.0089 106 GLU A OE2 
848  N  N   . HIS A 107 ? 0.1738 0.1561 0.0863 -0.0118 -0.0252 -0.0010 107 HIS A N   
849  C  CA  . HIS A 107 ? 0.1697 0.1487 0.0729 0.0106  -0.0201 -0.0075 107 HIS A CA  
850  C  C   . HIS A 107 ? 0.1899 0.1512 0.0933 0.0017  -0.0244 0.0018  107 HIS A C   
851  O  O   . HIS A 107 ? 0.2008 0.1576 0.1213 0.0137  -0.0510 -0.0023 107 HIS A O   
852  C  CB  . HIS A 107 ? 0.1706 0.1504 0.1047 0.0126  -0.0326 -0.0072 107 HIS A CB  
853  C  CG  . HIS A 107 ? 0.1789 0.1406 0.1015 0.0111  -0.0188 0.0002  107 HIS A CG  
854  N  ND1 . HIS A 107 ? 0.1870 0.1386 0.1186 0.0044  -0.0565 0.0128  107 HIS A ND1 
855  C  CD2 . HIS A 107 ? 0.2177 0.1540 0.1203 0.0175  -0.0241 -0.0412 107 HIS A CD2 
856  C  CE1 . HIS A 107 ? 0.2100 0.1511 0.0950 -0.0057 -0.0343 0.0089  107 HIS A CE1 
857  N  NE2 . HIS A 107 ? 0.1904 0.1541 0.1024 0.0255  -0.0474 -0.0155 107 HIS A NE2 
858  N  N   . THR A 108 ? 0.2037 0.1440 0.1144 -0.0095 -0.0207 0.0214  108 THR A N   
859  C  CA  . THR A 108 ? 0.2040 0.1376 0.0950 -0.0010 -0.0076 0.0011  108 THR A CA  
860  C  C   . THR A 108 ? 0.2082 0.1429 0.0832 0.0108  -0.0267 0.0344  108 THR A C   
861  O  O   . THR A 108 ? 0.2155 0.1816 0.1038 0.0117  -0.0333 0.0035  108 THR A O   
862  C  CB  . THR A 108 ? 0.2268 0.1863 0.0821 0.0247  -0.0452 0.0062  108 THR A CB  
863  O  OG1 . THR A 108 ? 0.2223 0.1787 0.1232 0.0012  -0.0479 0.0043  108 THR A OG1 
864  C  CG2 . THR A 108 ? 0.2245 0.2155 0.1066 0.0243  -0.0174 0.0107  108 THR A CG2 
865  N  N   . VAL A 109 ? 0.2082 0.1694 0.1085 -0.0071 -0.0130 0.0484  109 VAL A N   
866  C  CA  . VAL A 109 ? 0.2044 0.1798 0.1221 0.0022  -0.0116 0.0314  109 VAL A CA  
867  C  C   . VAL A 109 ? 0.2706 0.1784 0.1179 -0.0174 -0.0115 0.0313  109 VAL A C   
868  O  O   . VAL A 109 ? 0.2381 0.1735 0.1652 0.0020  -0.0283 0.0260  109 VAL A O   
869  C  CB  . VAL A 109 ? 0.2061 0.1972 0.1401 0.0288  -0.0131 0.0276  109 VAL A CB  
870  C  CG1 . VAL A 109 ? 0.2101 0.2413 0.2166 0.0011  0.0110  0.0460  109 VAL A CG1 
871  C  CG2 . VAL A 109 ? 0.2653 0.1916 0.1609 0.0263  -0.0363 0.0312  109 VAL A CG2 
872  N  N   . ASP A 110 ? 0.2527 0.1916 0.1078 0.0229  -0.0100 0.0277  110 ASP A N   
873  C  CA  . ASP A 110 ? 0.2590 0.2313 0.1697 0.0500  -0.0076 0.0514  110 ASP A CA  
874  C  C   . ASP A 110 ? 0.3138 0.1879 0.1134 0.0137  0.0071  0.0249  110 ASP A C   
875  O  O   . ASP A 110 ? 0.3166 0.1850 0.1676 0.0093  -0.0034 0.0369  110 ASP A O   
876  C  CB  . ASP A 110 ? 0.3105 0.2351 0.1741 0.0245  0.0668  0.0582  110 ASP A CB  
877  C  CG  . ASP A 110 ? 0.3445 0.1934 0.1487 0.0357  0.0428  0.0564  110 ASP A CG  
878  O  OD1 . ASP A 110 ? 0.3846 0.2182 0.2284 0.0164  0.0270  0.0526  110 ASP A OD1 
879  O  OD2 . ASP A 110 ? 0.3578 0.3767 0.2946 0.0154  0.0567  0.1111  110 ASP A OD2 
880  N  N   . LYS A 111 ? 0.2603 0.2035 0.1173 -0.0019 -0.0075 0.0164  111 LYS A N   
881  C  CA  . LYS A 111 ? 0.2529 0.2004 0.1454 0.0400  -0.0249 0.0345  111 LYS A CA  
882  C  C   . LYS A 111 ? 0.2521 0.2044 0.1437 0.0004  0.0084  0.0131  111 LYS A C   
883  O  O   . LYS A 111 ? 0.2370 0.2104 0.1800 0.0132  -0.0034 0.0168  111 LYS A O   
884  C  CB  . LYS A 111 ? 0.2882 0.2468 0.1532 0.0803  -0.0354 0.0431  111 LYS A CB  
885  C  CG  . LYS A 111 ? 0.3471 0.3682 0.1676 0.0700  -0.0735 0.0397  111 LYS A CG  
886  C  CD  . LYS A 111 ? 0.2934 0.4442 0.3621 0.0297  -0.1130 -0.0851 111 LYS A CD  
887  C  CE  . LYS A 111 ? 0.3357 0.5883 0.3494 0.0194  -0.1123 -0.0996 111 LYS A CE  
888  N  NZ  . LYS A 111 ? 0.3600 0.5359 0.4529 -0.0488 0.0543  0.0282  111 LYS A NZ  
889  N  N   . LYS A 112 ? 0.2543 0.1641 0.1266 0.0105  -0.0401 0.0272  112 LYS A N   
890  C  CA  . LYS A 112 ? 0.2594 0.2387 0.1060 0.0038  -0.0324 0.0290  112 LYS A CA  
891  C  C   . LYS A 112 ? 0.2342 0.1952 0.1202 0.0208  -0.0254 0.0165  112 LYS A C   
892  O  O   . LYS A 112 ? 0.2569 0.1674 0.1307 0.0134  -0.0127 0.0011  112 LYS A O   
893  C  CB  . LYS A 112 ? 0.2676 0.2178 0.2021 -0.0539 -0.0361 0.0023  112 LYS A CB  
894  C  CG  . LYS A 112 ? 0.2771 0.3258 0.2455 -0.0637 -0.0533 -0.0766 112 LYS A CG  
895  C  CD  . LYS A 112 ? 0.2866 0.3281 0.2852 -0.0243 -0.0489 0.0142  112 LYS A CD  
896  C  CE  . LYS A 112 ? 0.4589 0.3632 0.2810 0.0291  -0.1063 0.0248  112 LYS A CE  
897  N  NZ  . LYS A 112 ? 0.5024 0.3869 0.3832 0.0558  -0.1680 0.0825  112 LYS A NZ  
898  N  N   A LYS A 113 ? 0.2311 0.2019 0.1011 0.0307  -0.0373 0.0299  113 LYS A N   
899  N  N   B LYS A 113 ? 0.2349 0.2072 0.1024 0.0312  -0.0348 0.0276  113 LYS A N   
900  C  CA  A LYS A 113 ? 0.2525 0.2390 0.0754 0.0242  -0.0611 0.0276  113 LYS A CA  
901  C  CA  B LYS A 113 ? 0.2527 0.2379 0.0780 0.0252  -0.0575 0.0239  113 LYS A CA  
902  C  C   A LYS A 113 ? 0.2130 0.1491 0.1300 0.0061  -0.0431 0.0102  113 LYS A C   
903  C  C   B LYS A 113 ? 0.2254 0.1613 0.1193 0.0146  -0.0478 0.0121  113 LYS A C   
904  O  O   A LYS A 113 ? 0.3190 0.1392 0.2100 -0.0006 -0.0719 0.0044  113 LYS A O   
905  O  O   B LYS A 113 ? 0.3443 0.1462 0.2360 0.0103  -0.0923 0.0158  113 LYS A O   
906  C  CB  A LYS A 113 ? 0.2345 0.2046 0.1523 0.0060  -0.0428 -0.0230 113 LYS A CB  
907  C  CB  B LYS A 113 ? 0.2533 0.2432 0.1171 0.0000  -0.0203 -0.0222 113 LYS A CB  
908  C  CG  A LYS A 113 ? 0.2396 0.2270 0.1604 0.0013  -0.0610 0.0000  113 LYS A CG  
909  C  CG  B LYS A 113 ? 0.2092 0.2939 0.1261 0.0064  -0.0027 -0.0355 113 LYS A CG  
910  C  CD  A LYS A 113 ? 0.2333 0.2044 0.2046 0.0050  -0.0591 0.0060  113 LYS A CD  
911  C  CD  B LYS A 113 ? 0.2032 0.2724 0.1658 0.0070  -0.0040 -0.0222 113 LYS A CD  
912  C  CE  A LYS A 113 ? 0.2428 0.1613 0.2478 0.0022  -0.0663 0.0359  113 LYS A CE  
913  C  CE  B LYS A 113 ? 0.2244 0.3574 0.1846 0.0116  -0.0545 -0.0350 113 LYS A CE  
914  N  NZ  A LYS A 113 ? 0.2719 0.2464 0.2237 0.0239  -0.0758 0.0282  113 LYS A NZ  
915  N  NZ  B LYS A 113 ? 0.2570 0.2697 0.3036 0.0062  -0.0174 -0.0139 113 LYS A NZ  
916  N  N   . TYR A 114 ? 0.1963 0.1494 0.1606 0.0126  -0.0480 0.0107  114 TYR A N   
917  C  CA  . TYR A 114 ? 0.1742 0.1534 0.1566 -0.0044 -0.0353 0.0113  114 TYR A CA  
918  C  C   . TYR A 114 ? 0.1778 0.1243 0.1575 -0.0152 -0.0301 -0.0145 114 TYR A C   
919  O  O   . TYR A 114 ? 0.1954 0.1580 0.1421 -0.0168 -0.0491 -0.0044 114 TYR A O   
920  C  CB  . TYR A 114 ? 0.1850 0.1365 0.1717 0.0021  -0.0117 0.0099  114 TYR A CB  
921  C  CG  . TYR A 114 ? 0.2169 0.1540 0.1257 -0.0012 -0.0165 0.0186  114 TYR A CG  
922  C  CD1 . TYR A 114 ? 0.2592 0.1749 0.1458 0.0504  -0.0355 -0.0043 114 TYR A CD1 
923  C  CD2 . TYR A 114 ? 0.2054 0.1669 0.1958 -0.0106 -0.0107 0.0244  114 TYR A CD2 
924  C  CE1 . TYR A 114 ? 0.2707 0.2609 0.1896 0.0511  -0.0146 0.0006  114 TYR A CE1 
925  C  CE2 . TYR A 114 ? 0.2838 0.2340 0.1634 -0.0065 0.0055  0.0401  114 TYR A CE2 
926  C  CZ  . TYR A 114 ? 0.2734 0.3043 0.1270 0.0326  0.0153  0.0452  114 TYR A CZ  
927  O  OH  . TYR A 114 ? 0.3628 0.4437 0.2309 0.0631  0.0796  0.0917  114 TYR A OH  
928  N  N   . ALA A 115 ? 0.1885 0.1559 0.1394 -0.0040 -0.0303 -0.0199 115 ALA A N   
929  C  CA  . ALA A 115 ? 0.2046 0.1243 0.1249 -0.0142 -0.0293 -0.0256 115 ALA A CA  
930  C  C   . ALA A 115 ? 0.1922 0.1256 0.1429 0.0104  -0.0281 0.0038  115 ALA A C   
931  O  O   . ALA A 115 ? 0.2090 0.1501 0.1437 0.0006  -0.0311 -0.0069 115 ALA A O   
932  C  CB  . ALA A 115 ? 0.2266 0.1665 0.1674 -0.0265 -0.0741 -0.0198 115 ALA A CB  
933  N  N   . ALA A 116 ? 0.2032 0.1191 0.1329 0.0228  -0.0606 -0.0125 116 ALA A N   
934  C  CA  . ALA A 116 ? 0.2177 0.1306 0.0979 0.0114  -0.0343 -0.0082 116 ALA A CA  
935  C  C   . ALA A 116 ? 0.1554 0.1652 0.1012 0.0061  -0.0193 -0.0029 116 ALA A C   
936  O  O   . ALA A 116 ? 0.1785 0.1512 0.0999 -0.0062 -0.0245 -0.0034 116 ALA A O   
937  C  CB  . ALA A 116 ? 0.2169 0.1841 0.1037 0.0094  -0.0552 -0.0117 116 ALA A CB  
938  N  N   . GLU A 117 ? 0.2001 0.1381 0.1037 0.0022  -0.0275 -0.0034 117 GLU A N   
939  C  CA  . GLU A 117 ? 0.2051 0.1207 0.1072 0.0148  -0.0509 -0.0041 117 GLU A CA  
940  C  C   . GLU A 117 ? 0.1889 0.1367 0.0969 0.0239  -0.0290 -0.0027 117 GLU A C   
941  O  O   . GLU A 117 ? 0.1972 0.1720 0.1275 0.0271  -0.0049 0.0354  117 GLU A O   
942  C  CB  . GLU A 117 ? 0.2026 0.1763 0.0829 0.0154  -0.0491 -0.0049 117 GLU A CB  
943  C  CG  . GLU A 117 ? 0.2019 0.1823 0.0924 -0.0094 -0.0367 -0.0143 117 GLU A CG  
944  C  CD  . GLU A 117 ? 0.2245 0.1523 0.0944 0.0251  -0.0326 0.0036  117 GLU A CD  
945  O  OE1 . GLU A 117 ? 0.2056 0.1788 0.1241 0.0190  -0.0436 0.0108  117 GLU A OE1 
946  O  OE2 . GLU A 117 ? 0.2560 0.1787 0.1097 0.0076  -0.0587 -0.0054 117 GLU A OE2 
947  N  N   . LEU A 118 ? 0.1722 0.1365 0.0965 0.0062  -0.0534 -0.0021 118 LEU A N   
948  C  CA  . LEU A 118 ? 0.1839 0.1176 0.1306 0.0147  -0.0614 -0.0111 118 LEU A CA  
949  C  C   . LEU A 118 ? 0.1676 0.1381 0.0791 0.0144  -0.0365 0.0000  118 LEU A C   
950  O  O   . LEU A 118 ? 0.1798 0.1432 0.0789 0.0044  -0.0344 0.0114  118 LEU A O   
951  C  CB  . LEU A 118 ? 0.1807 0.1490 0.1223 0.0049  -0.0394 0.0039  118 LEU A CB  
952  C  CG  . LEU A 118 ? 0.1643 0.1625 0.1321 0.0166  -0.0425 0.0188  118 LEU A CG  
953  C  CD1 . LEU A 118 ? 0.1943 0.1798 0.1022 -0.0113 -0.0732 -0.0006 118 LEU A CD1 
954  C  CD2 . LEU A 118 ? 0.1724 0.2185 0.1273 -0.0069 -0.0444 0.0050  118 LEU A CD2 
955  N  N   . HIS A 119 ? 0.1688 0.1325 0.0895 -0.0031 -0.0465 0.0089  119 HIS A N   
956  C  CA  . HIS A 119 ? 0.1573 0.1184 0.1297 0.0017  -0.0561 -0.0012 119 HIS A CA  
957  C  C   . HIS A 119 ? 0.1527 0.1284 0.0933 -0.0037 -0.0458 -0.0039 119 HIS A C   
958  O  O   . HIS A 119 ? 0.1825 0.1505 0.0938 0.0035  -0.0343 0.0027  119 HIS A O   
959  C  CB  . HIS A 119 ? 0.1544 0.1509 0.1207 0.0181  -0.0601 0.0063  119 HIS A CB  
960  C  CG  . HIS A 119 ? 0.1764 0.1724 0.0652 0.0116  -0.0597 0.0001  119 HIS A CG  
961  N  ND1 . HIS A 119 ? 0.1569 0.1561 0.1186 -0.0218 -0.0410 0.0207  119 HIS A ND1 
962  C  CD2 . HIS A 119 ? 0.1726 0.1789 0.0898 0.0137  -0.0413 0.0159  119 HIS A CD2 
963  C  CE1 . HIS A 119 ? 0.1842 0.1339 0.0930 0.0000  -0.0539 -0.0130 119 HIS A CE1 
964  N  NE2 . HIS A 119 ? 0.1773 0.1763 0.1017 0.0189  -0.0467 0.0044  119 HIS A NE2 
965  N  N   . LEU A 120 ? 0.1679 0.1332 0.0945 0.0111  -0.0544 -0.0013 120 LEU A N   
966  C  CA  . LEU A 120 ? 0.1582 0.1094 0.1690 0.0017  -0.0616 -0.0048 120 LEU A CA  
967  C  C   . LEU A 120 ? 0.1634 0.1196 0.1030 0.0120  -0.0447 -0.0115 120 LEU A C   
968  O  O   . LEU A 120 ? 0.1756 0.1403 0.0938 -0.0008 -0.0513 -0.0010 120 LEU A O   
969  C  CB  . LEU A 120 ? 0.1626 0.1590 0.1458 0.0082  -0.0761 -0.0107 120 LEU A CB  
970  C  CG  . LEU A 120 ? 0.1781 0.1870 0.1375 -0.0325 -0.0847 0.0082  120 LEU A CG  
971  C  CD1 . LEU A 120 ? 0.2939 0.1895 0.2039 -0.0692 -0.0343 0.0053  120 LEU A CD1 
972  C  CD2 . LEU A 120 ? 0.2227 0.2180 0.1788 0.0043  -0.1171 -0.0013 120 LEU A CD2 
973  N  N   . VAL A 121 ? 0.1667 0.1302 0.1335 -0.0122 -0.0537 -0.0015 121 VAL A N   
974  C  CA  . VAL A 121 ? 0.1967 0.1082 0.1133 -0.0081 -0.0452 0.0039  121 VAL A CA  
975  C  C   . VAL A 121 ? 0.1886 0.1268 0.1178 0.0113  -0.0466 0.0190  121 VAL A C   
976  O  O   . VAL A 121 ? 0.2333 0.1421 0.1248 -0.0002 -0.0805 0.0203  121 VAL A O   
977  C  CB  . VAL A 121 ? 0.1934 0.1372 0.1353 -0.0133 -0.0489 0.0105  121 VAL A CB  
978  C  CG1 . VAL A 121 ? 0.1830 0.1712 0.1461 -0.0320 -0.0438 -0.0115 121 VAL A CG1 
979  C  CG2 . VAL A 121 ? 0.2226 0.1478 0.1300 0.0160  -0.0252 0.0195  121 VAL A CG2 
980  N  N   . HIS A 122 ? 0.1791 0.1320 0.1327 0.0154  -0.0543 -0.0199 122 HIS A N   
981  C  CA  . HIS A 122 ? 0.2033 0.1130 0.1473 -0.0092 -0.0598 -0.0064 122 HIS A CA  
982  C  C   . HIS A 122 ? 0.1950 0.1264 0.1403 0.0049  -0.0649 -0.0195 122 HIS A C   
983  O  O   . HIS A 122 ? 0.1952 0.1430 0.1516 -0.0025 -0.0776 0.0074  122 HIS A O   
984  C  CB  . HIS A 122 ? 0.2126 0.1432 0.1462 0.0068  -0.0300 -0.0005 122 HIS A CB  
985  C  CG  . HIS A 122 ? 0.1946 0.1404 0.1557 0.0035  -0.0541 0.0108  122 HIS A CG  
986  N  ND1 . HIS A 122 ? 0.1927 0.1465 0.1823 0.0173  -0.0753 0.0049  122 HIS A ND1 
987  C  CD2 . HIS A 122 ? 0.1895 0.1687 0.1756 0.0035  -0.0438 -0.0054 122 HIS A CD2 
988  C  CE1 . HIS A 122 ? 0.1920 0.1672 0.1974 0.0192  -0.0725 -0.0300 122 HIS A CE1 
989  N  NE2 . HIS A 122 ? 0.1904 0.1688 0.1665 -0.0077 -0.0644 -0.0034 122 HIS A NE2 
990  N  N   . TRP A 123 ? 0.2141 0.1238 0.1351 -0.0008 -0.0644 -0.0115 123 TRP A N   
991  C  CA  . TRP A 123 ? 0.2119 0.1198 0.1498 -0.0030 -0.0682 -0.0204 123 TRP A CA  
992  C  C   . TRP A 123 ? 0.2010 0.1270 0.1570 0.0117  -0.0736 0.0012  123 TRP A C   
993  O  O   . TRP A 123 ? 0.2123 0.1453 0.2173 0.0157  -0.1042 0.0013  123 TRP A O   
994  C  CB  . TRP A 123 ? 0.2394 0.1769 0.1612 -0.0204 -0.0798 0.0129  123 TRP A CB  
995  C  CG  . TRP A 123 ? 0.2731 0.1670 0.1679 -0.0248 -0.0859 0.0091  123 TRP A CG  
996  C  CD1 . TRP A 123 ? 0.3389 0.1820 0.1914 -0.0027 -0.1385 -0.0058 123 TRP A CD1 
997  C  CD2 . TRP A 123 ? 0.3094 0.1544 0.1594 -0.0392 -0.1026 0.0181  123 TRP A CD2 
998  N  NE1 . TRP A 123 ? 0.3686 0.1557 0.2019 -0.0523 -0.1401 0.0107  123 TRP A NE1 
999  C  CE2 . TRP A 123 ? 0.3464 0.1448 0.1626 -0.0464 -0.1055 0.0323  123 TRP A CE2 
1000 C  CE3 . TRP A 123 ? 0.3216 0.1480 0.1925 -0.0340 -0.0977 0.0055  123 TRP A CE3 
1001 C  CZ2 . TRP A 123 ? 0.3713 0.1756 0.2008 -0.0215 -0.1284 0.0249  123 TRP A CZ2 
1002 C  CZ3 . TRP A 123 ? 0.3968 0.1568 0.2008 -0.0476 -0.0878 0.0417  123 TRP A CZ3 
1003 C  CH2 . TRP A 123 ? 0.4144 0.1536 0.2057 -0.0275 -0.1151 0.0212  123 TRP A CH2 
1004 N  N   . ASN A 124 ? 0.1828 0.1465 0.1665 0.0096  -0.0680 -0.0318 124 ASN A N   
1005 C  CA  . ASN A 124 ? 0.2399 0.1318 0.1946 0.0150  -0.0625 -0.0348 124 ASN A CA  
1006 C  C   . ASN A 124 ? 0.2313 0.1412 0.1848 0.0161  -0.0405 -0.0367 124 ASN A C   
1007 O  O   . ASN A 124 ? 0.2219 0.1483 0.2015 0.0073  -0.0659 -0.0212 124 ASN A O   
1008 C  CB  . ASN A 124 ? 0.2459 0.1809 0.1958 0.0098  -0.0604 -0.0478 124 ASN A CB  
1009 C  CG  . ASN A 124 ? 0.2744 0.1726 0.2227 -0.0365 -0.0054 -0.0168 124 ASN A CG  
1010 O  OD1 . ASN A 124 ? 0.3179 0.1992 0.2286 0.0267  0.0239  -0.0420 124 ASN A OD1 
1011 N  ND2 . ASN A 124 ? 0.3749 0.1925 0.1943 0.0130  -0.0178 -0.0326 124 ASN A ND2 
1012 N  N   . THR A 125 ? 0.2262 0.1361 0.2928 0.0196  -0.0538 -0.0296 125 THR A N   
1013 C  CA  . THR A 125 ? 0.2291 0.1350 0.2937 -0.0023 -0.0714 -0.0038 125 THR A CA  
1014 C  C   . THR A 125 ? 0.2354 0.1410 0.3015 0.0166  -0.0190 -0.0264 125 THR A C   
1015 O  O   . THR A 125 ? 0.2818 0.1486 0.3546 0.0104  -0.0677 -0.0099 125 THR A O   
1016 C  CB  . THR A 125 ? 0.2499 0.2119 0.3912 0.0200  -0.1158 -0.0260 125 THR A CB  
1017 O  OG1 . THR A 125 ? 0.2453 0.2319 0.5219 0.0469  -0.0351 -0.0357 125 THR A OG1 
1018 C  CG2 . THR A 125 ? 0.2681 0.2017 0.4496 -0.0037 -0.1606 -0.0032 125 THR A CG2 
1019 N  N   . LYS A 126 ? 0.2622 0.1868 0.2377 -0.0098 -0.0106 -0.0572 127 LYS A N   
1020 C  CA  . LYS A 126 ? 0.3177 0.2306 0.2460 -0.0302 0.0383  -0.1017 127 LYS A CA  
1021 C  C   . LYS A 126 ? 0.2662 0.1530 0.2575 -0.0027 -0.0194 -0.0344 127 LYS A C   
1022 O  O   . LYS A 126 ? 0.3165 0.1728 0.3674 -0.0447 0.0174  -0.0934 127 LYS A O   
1023 C  CB  . LYS A 126 ? 0.4036 0.2710 0.2579 -0.0395 -0.0027 -0.1027 127 LYS A CB  
1024 C  CG  . LYS A 126 ? 0.3484 0.2819 0.2520 -0.0482 0.0416  -0.0732 127 LYS A CG  
1025 C  CD  . LYS A 126 ? 0.4749 0.4956 0.2374 -0.1298 0.0587  -0.0934 127 LYS A CD  
1026 C  CE  . LYS A 126 ? 0.4149 0.5898 0.5510 -0.0476 -0.0573 -0.1205 127 LYS A CE  
1027 N  NZ  . LYS A 126 ? 0.5483 0.6700 0.6670 -0.0974 -0.0562 -0.2766 127 LYS A NZ  
1028 N  N   . TYR A 127 ? 0.2282 0.1534 0.1974 0.0160  -0.0370 -0.0218 128 TYR A N   
1029 C  CA  . TYR A 127 ? 0.2361 0.1469 0.1807 0.0152  -0.0581 -0.0096 128 TYR A CA  
1030 C  C   . TYR A 127 ? 0.2611 0.1645 0.1753 0.0012  -0.0606 -0.0369 128 TYR A C   
1031 O  O   . TYR A 127 ? 0.2699 0.2075 0.2122 0.0042  -0.0447 -0.0074 128 TYR A O   
1032 C  CB  . TYR A 127 ? 0.2473 0.1523 0.1794 0.0219  -0.0504 -0.0163 128 TYR A CB  
1033 C  CG  . TYR A 127 ? 0.2254 0.1690 0.1751 -0.0016 -0.0514 -0.0210 128 TYR A CG  
1034 C  CD1 . TYR A 127 ? 0.3656 0.1785 0.1701 0.0265  -0.1048 -0.0373 128 TYR A CD1 
1035 C  CD2 . TYR A 127 ? 0.2906 0.1694 0.1583 0.0129  -0.0067 -0.0236 128 TYR A CD2 
1036 C  CE1 . TYR A 127 ? 0.3174 0.1952 0.1744 0.0391  -0.0814 -0.0367 128 TYR A CE1 
1037 C  CE2 . TYR A 127 ? 0.2635 0.2187 0.1509 0.0001  -0.0347 -0.0504 128 TYR A CE2 
1038 C  CZ  . TYR A 127 ? 0.3353 0.2139 0.1277 0.0089  -0.0307 -0.0525 128 TYR A CZ  
1039 O  OH  . TYR A 127 ? 0.3911 0.2518 0.1494 0.0374  -0.0579 -0.0353 128 TYR A OH  
1040 N  N   . GLY A 128 ? 0.2621 0.1588 0.2043 0.0208  -0.0664 -0.0012 129 GLY A N   
1041 C  CA  . GLY A 128 ? 0.3010 0.1692 0.2075 0.0027  -0.0427 0.0219  129 GLY A CA  
1042 C  C   . GLY A 128 ? 0.2814 0.1835 0.1990 0.0137  -0.0767 0.0144  129 GLY A C   
1043 O  O   . GLY A 128 ? 0.3344 0.1989 0.2093 -0.0052 -0.0903 0.0407  129 GLY A O   
1044 N  N   . ASP A 129 ? 0.3175 0.1922 0.1744 0.0350  -0.0279 0.0037  130 ASP A N   
1045 C  CA  . ASP A 129 ? 0.3600 0.1945 0.1523 0.0445  -0.0439 0.0021  130 ASP A CA  
1046 C  C   . ASP A 129 ? 0.3436 0.2051 0.1629 0.0456  -0.0771 -0.0100 130 ASP A C   
1047 O  O   . ASP A 129 ? 0.3398 0.2172 0.1358 0.0359  -0.0624 0.0027  130 ASP A O   
1048 C  CB  . ASP A 129 ? 0.4307 0.1972 0.2312 0.0332  -0.0167 0.0362  130 ASP A CB  
1049 C  CG  . ASP A 129 ? 0.3871 0.2743 0.3184 0.0859  0.0700  -0.0217 130 ASP A CG  
1050 O  OD1 . ASP A 129 ? 0.4559 0.3202 0.2639 0.1004  -0.0032 0.0853  130 ASP A OD1 
1051 O  OD2 . ASP A 129 ? 0.3829 0.3366 0.3780 0.0736  -0.0746 0.0233  130 ASP A OD2 
1052 N  N   . ALA A 130 ? 0.4258 0.2013 0.1414 0.0491  -0.0346 -0.0016 131 ALA A N   
1053 C  CA  . ALA A 130 ? 0.3089 0.1963 0.1648 0.0400  -0.0241 -0.0044 131 ALA A CA  
1054 C  C   . ALA A 130 ? 0.2818 0.2148 0.1819 0.0287  -0.0109 0.0218  131 ALA A C   
1055 O  O   . ALA A 130 ? 0.3406 0.1794 0.1541 0.0073  -0.0319 0.0127  131 ALA A O   
1056 C  CB  . ALA A 130 ? 0.3795 0.2101 0.1909 0.0122  -0.0414 -0.0190 131 ALA A CB  
1057 N  N   . GLY A 131 ? 0.3563 0.2742 0.1601 0.0196  0.0304  0.0222  132 GLY A N   
1058 C  CA  . GLY A 131 ? 0.3712 0.2604 0.1766 0.0345  0.0501  0.0274  132 GLY A CA  
1059 C  C   . GLY A 131 ? 0.2775 0.2335 0.1958 0.0198  0.0287  0.0370  132 GLY A C   
1060 O  O   . GLY A 131 ? 0.2933 0.2654 0.2776 0.0368  -0.0011 0.0626  132 GLY A O   
1061 N  N   A LYS A 132 ? 0.3094 0.1911 0.2438 0.0021  0.0251  0.0366  133 LYS A N   
1062 N  N   B LYS A 132 ? 0.3186 0.1846 0.2538 -0.0018 0.0369  0.0422  133 LYS A N   
1063 C  CA  A LYS A 132 ? 0.2642 0.1830 0.2255 0.0051  -0.0062 0.0435  133 LYS A CA  
1064 C  CA  B LYS A 132 ? 0.2720 0.2227 0.2330 -0.0183 -0.0214 0.0454  133 LYS A CA  
1065 C  C   A LYS A 132 ? 0.2360 0.1645 0.1740 -0.0228 -0.0388 0.0181  133 LYS A C   
1066 C  C   B LYS A 132 ? 0.2421 0.1681 0.1907 -0.0287 -0.0372 0.0080  133 LYS A C   
1067 O  O   A LYS A 132 ? 0.2557 0.2006 0.2029 -0.0266 -0.0749 -0.0074 133 LYS A O   
1068 O  O   B LYS A 132 ? 0.2654 0.1997 0.2323 -0.0207 -0.0773 0.0077  133 LYS A O   
1069 C  CB  A LYS A 132 ? 0.2046 0.1541 0.2433 -0.0269 -0.0176 0.0643  133 LYS A CB  
1070 C  CB  B LYS A 132 ? 0.2687 0.2272 0.3515 -0.0178 -0.0515 -0.0024 133 LYS A CB  
1071 C  CG  A LYS A 132 ? 0.3013 0.2317 0.2643 -0.0278 -0.0846 0.0160  133 LYS A CG  
1072 C  CG  B LYS A 132 ? 0.4546 0.2369 0.3679 -0.0273 0.0336  0.0791  133 LYS A CG  
1073 C  CD  A LYS A 132 ? 0.3340 0.4358 0.4578 -0.1051 -0.2394 -0.0264 133 LYS A CD  
1074 C  CD  B LYS A 132 ? 0.6170 0.3574 0.1939 -0.0040 0.0066  0.0996  133 LYS A CD  
1075 C  CE  A LYS A 132 ? 0.6193 0.4112 0.5274 0.0167  -0.1931 -0.0296 133 LYS A CE  
1076 C  CE  B LYS A 132 ? 0.4219 0.2902 0.1394 -0.0122 -0.0575 0.0261  133 LYS A CE  
1077 N  NZ  A LYS A 132 ? 0.5314 0.4828 0.9057 -0.0087 -0.0537 0.1026  133 LYS A NZ  
1078 N  NZ  B LYS A 132 ? 0.5338 0.4359 0.2889 0.0411  0.0882  0.0001  133 LYS A NZ  
1079 N  N   . ALA A 133 ? 0.2245 0.1564 0.1568 -0.0168 -0.0129 -0.0109 134 ALA A N   
1080 C  CA  . ALA A 133 ? 0.1924 0.1767 0.1534 -0.0081 -0.0162 0.0018  134 ALA A CA  
1081 C  C   . ALA A 133 ? 0.2076 0.1694 0.1557 -0.0116 -0.0199 0.0063  134 ALA A C   
1082 O  O   . ALA A 133 ? 0.2216 0.2072 0.1382 -0.0174 -0.0419 0.0027  134 ALA A O   
1083 C  CB  . ALA A 133 ? 0.2090 0.1958 0.1564 -0.0283 -0.0480 0.0006  134 ALA A CB  
1084 N  N   . SER A 134 ? 0.2171 0.1595 0.2021 0.0177  -0.0114 -0.0086 135 SER A N   
1085 C  CA  . SER A 134 ? 0.2294 0.2198 0.1640 0.0396  -0.0018 0.0088  135 SER A CA  
1086 C  C   . SER A 134 ? 0.2033 0.2087 0.1827 0.0087  0.0046  0.0215  135 SER A C   
1087 O  O   . SER A 134 ? 0.2304 0.2420 0.2118 0.0434  0.0019  0.0392  135 SER A O   
1088 C  CB  . SER A 134 ? 0.3294 0.2333 0.1378 0.0413  0.0358  0.0116  135 SER A CB  
1089 O  OG  . SER A 134 ? 0.3415 0.3218 0.1724 0.0576  0.0436  0.0385  135 SER A OG  
1090 N  N   . GLN A 135 ? 0.2453 0.2115 0.1738 -0.0201 -0.0333 0.0158  136 GLN A N   
1091 C  CA  . GLN A 135 ? 0.2165 0.2351 0.2094 -0.0218 -0.0351 0.0025  136 GLN A CA  
1092 C  C   . GLN A 135 ? 0.2277 0.2197 0.2270 -0.0065 -0.0297 -0.0295 136 GLN A C   
1093 O  O   . GLN A 135 ? 0.2758 0.3222 0.2649 -0.0635 -0.0930 -0.0089 136 GLN A O   
1094 C  CB  . GLN A 135 ? 0.2986 0.3006 0.2635 -0.0798 -0.0719 0.0480  136 GLN A CB  
1095 C  CG  . GLN A 135 ? 0.3642 0.3543 0.3226 -0.0508 -0.0043 0.1136  136 GLN A CG  
1096 C  CD  . GLN A 135 ? 0.4678 0.5923 0.3377 0.0970  -0.0092 0.1280  136 GLN A CD  
1097 O  OE1 . GLN A 135 ? 0.3682 1.0658 0.7087 0.1927  -0.0941 0.0387  136 GLN A OE1 
1098 N  NE2 . GLN A 135 ? 0.6282 0.7192 0.4912 0.1126  -0.0195 -0.0152 136 GLN A NE2 
1099 N  N   . GLN A 136 ? 0.2238 0.2151 0.1267 -0.0037 -0.0373 -0.0084 137 GLN A N   
1100 C  CA  . GLN A 136 ? 0.2492 0.2057 0.0994 -0.0042 -0.0596 -0.0419 137 GLN A CA  
1101 C  C   . GLN A 136 ? 0.2376 0.2148 0.1429 0.0161  -0.0493 -0.0178 137 GLN A C   
1102 O  O   . GLN A 136 ? 0.2453 0.1970 0.1302 0.0006  -0.0314 -0.0032 137 GLN A O   
1103 C  CB  . GLN A 136 ? 0.2495 0.1982 0.1742 0.0086  -0.0761 -0.0212 137 GLN A CB  
1104 C  CG  . GLN A 136 ? 0.2944 0.2464 0.1897 0.0225  -0.0373 0.0164  137 GLN A CG  
1105 C  CD  . GLN A 136 ? 0.3098 0.2721 0.3265 -0.0145 -0.0504 0.0487  137 GLN A CD  
1106 O  OE1 . GLN A 136 ? 0.4058 0.2182 0.2935 -0.0175 -0.0542 -0.0495 137 GLN A OE1 
1107 N  NE2 . GLN A 136 ? 0.3720 0.4276 0.4034 0.0288  0.0710  0.0762  137 GLN A NE2 
1108 N  N   . PRO A 137 ? 0.2276 0.2237 0.1361 0.0119  -0.0546 -0.0200 138 PRO A N   
1109 C  CA  . PRO A 137 ? 0.2822 0.2500 0.0979 0.0296  -0.0575 -0.0144 138 PRO A CA  
1110 C  C   . PRO A 137 ? 0.2753 0.2533 0.1032 0.0242  -0.0025 0.0103  138 PRO A C   
1111 O  O   . PRO A 137 ? 0.3130 0.2658 0.2421 0.0268  -0.0366 0.0512  138 PRO A O   
1112 C  CB  . PRO A 137 ? 0.3379 0.3680 0.0754 0.0598  -0.0533 -0.0055 138 PRO A CB  
1113 C  CG  . PRO A 137 ? 0.4974 0.3838 0.1904 -0.0916 -0.0800 -0.0071 138 PRO A CG  
1114 C  CD  . PRO A 137 ? 0.2657 0.3283 0.1588 -0.0550 -0.0826 -0.0630 138 PRO A CD  
1115 N  N   . ASP A 138 ? 0.2312 0.2536 0.1058 0.0168  -0.0408 -0.0233 139 ASP A N   
1116 C  CA  . ASP A 138 ? 0.2489 0.2929 0.1108 -0.0059 -0.0151 -0.0203 139 ASP A CA  
1117 C  C   . ASP A 138 ? 0.2392 0.2215 0.1371 0.0043  -0.0195 -0.0157 139 ASP A C   
1118 O  O   . ASP A 138 ? 0.2183 0.2509 0.1832 0.0121  -0.0354 -0.0177 139 ASP A O   
1119 C  CB  . ASP A 138 ? 0.3208 0.3394 0.1001 0.0214  -0.0086 -0.0392 139 ASP A CB  
1120 C  CG  . ASP A 138 ? 0.3439 0.3838 0.1893 0.0478  -0.0232 -0.0920 139 ASP A CG  
1121 O  OD1 . ASP A 138 ? 0.3401 0.2742 0.2090 0.0771  -0.0458 -0.0498 139 ASP A OD1 
1122 O  OD2 . ASP A 138 ? 0.3635 0.3974 0.2556 0.0768  0.0013  -0.1151 139 ASP A OD2 
1123 N  N   . GLY A 139 ? 0.2196 0.1866 0.0936 -0.0161 -0.0517 -0.0270 140 GLY A N   
1124 C  CA  . GLY A 139 ? 0.2415 0.1881 0.0863 -0.0211 -0.0714 -0.0221 140 GLY A CA  
1125 C  C   . GLY A 139 ? 0.1911 0.1428 0.0866 -0.0074 -0.0517 -0.0048 140 GLY A C   
1126 O  O   . GLY A 139 ? 0.2150 0.1529 0.1364 0.0236  -0.0699 -0.0043 140 GLY A O   
1127 N  N   . LEU A 140 ? 0.1970 0.1321 0.1172 -0.0001 -0.0336 -0.0106 141 LEU A N   
1128 C  CA  . LEU A 140 ? 0.1673 0.1461 0.1231 0.0046  -0.0392 -0.0164 141 LEU A CA  
1129 C  C   . LEU A 140 ? 0.1884 0.1532 0.1075 -0.0138 -0.0457 -0.0274 141 LEU A C   
1130 O  O   . LEU A 140 ? 0.2019 0.1555 0.1017 -0.0047 -0.0466 -0.0019 141 LEU A O   
1131 C  CB  . LEU A 140 ? 0.1879 0.1936 0.1117 0.0126  -0.0173 -0.0127 141 LEU A CB  
1132 C  CG  . LEU A 140 ? 0.2203 0.2367 0.1943 0.0590  0.0403  0.0440  141 LEU A CG  
1133 C  CD1 . LEU A 140 ? 0.2432 0.2151 0.2081 0.0297  0.0436  0.0027  141 LEU A CD1 
1134 C  CD2 . LEU A 140 ? 0.3466 0.1622 0.2087 0.0325  -0.0163 0.0308  141 LEU A CD2 
1135 N  N   . ALA A 141 ? 0.1673 0.1267 0.1469 -0.0091 -0.0479 -0.0300 142 ALA A N   
1136 C  CA  . ALA A 141 ? 0.1900 0.1469 0.1407 -0.0212 -0.0483 -0.0364 142 ALA A CA  
1137 C  C   . ALA A 141 ? 0.1767 0.1313 0.0924 0.0010  -0.0542 -0.0046 142 ALA A C   
1138 O  O   . ALA A 141 ? 0.2251 0.1436 0.1142 0.0088  -0.0693 0.0139  142 ALA A O   
1139 C  CB  . ALA A 141 ? 0.1903 0.1631 0.1857 -0.0027 -0.0261 -0.0204 142 ALA A CB  
1140 N  N   . VAL A 142 ? 0.1709 0.1333 0.1103 0.0076  -0.0447 -0.0146 143 VAL A N   
1141 C  CA  . VAL A 142 ? 0.1943 0.1224 0.1194 0.0094  -0.0568 -0.0184 143 VAL A CA  
1142 C  C   . VAL A 142 ? 0.1853 0.1363 0.0979 -0.0047 -0.0458 0.0047  143 VAL A C   
1143 O  O   . VAL A 142 ? 0.1888 0.1605 0.0935 0.0020  -0.0466 0.0108  143 VAL A O   
1144 C  CB  . VAL A 142 ? 0.1825 0.1444 0.0916 0.0129  -0.0306 -0.0092 143 VAL A CB  
1145 C  CG1 . VAL A 142 ? 0.2072 0.1622 0.1048 0.0322  -0.0561 -0.0260 143 VAL A CG1 
1146 C  CG2 . VAL A 142 ? 0.1698 0.1922 0.1112 -0.0063 -0.0383 0.0200  143 VAL A CG2 
1147 N  N   . LEU A 143 ? 0.1715 0.1306 0.1333 -0.0157 -0.0553 -0.0079 144 LEU A N   
1148 C  CA  . LEU A 143 ? 0.1809 0.1282 0.1196 0.0034  -0.0494 -0.0055 144 LEU A CA  
1149 C  C   . LEU A 143 ? 0.1676 0.1346 0.0746 -0.0286 -0.0264 -0.0193 144 LEU A C   
1150 O  O   . LEU A 143 ? 0.2053 0.1523 0.0841 -0.0100 -0.0223 -0.0065 144 LEU A O   
1151 C  CB  . LEU A 143 ? 0.1630 0.1771 0.1498 -0.0021 -0.0357 0.0111  144 LEU A CB  
1152 C  CG  . LEU A 143 ? 0.1634 0.2249 0.1396 0.0011  -0.0234 0.0081  144 LEU A CG  
1153 C  CD1 . LEU A 143 ? 0.2247 0.2516 0.1465 -0.0125 -0.0116 0.0137  144 LEU A CD1 
1154 C  CD2 . LEU A 143 ? 0.1685 0.2552 0.1942 0.0006  -0.0633 0.0111  144 LEU A CD2 
1155 N  N   . GLY A 144 ? 0.1849 0.1275 0.1483 -0.0013 -0.0502 -0.0057 145 GLY A N   
1156 C  CA  . GLY A 144 ? 0.1764 0.1311 0.0997 -0.0172 -0.0350 -0.0044 145 GLY A CA  
1157 C  C   . GLY A 144 ? 0.1491 0.1655 0.0780 -0.0016 -0.0268 -0.0054 145 GLY A C   
1158 O  O   . GLY A 144 ? 0.1863 0.1529 0.1033 -0.0201 -0.0139 -0.0006 145 GLY A O   
1159 N  N   . ILE A 145 ? 0.1904 0.1419 0.0938 -0.0066 -0.0611 -0.0027 146 ILE A N   
1160 C  CA  . ILE A 145 ? 0.1512 0.1386 0.1365 0.0006  -0.0542 0.0023  146 ILE A CA  
1161 C  C   . ILE A 145 ? 0.1703 0.1421 0.1103 -0.0098 -0.0332 -0.0198 146 ILE A C   
1162 O  O   . ILE A 145 ? 0.1846 0.1475 0.1031 0.0035  -0.0306 0.0018  146 ILE A O   
1163 C  CB  . ILE A 145 ? 0.1963 0.1588 0.1173 0.0091  -0.0646 0.0006  146 ILE A CB  
1164 C  CG1 . ILE A 145 ? 0.2171 0.1735 0.1584 0.0345  -0.0551 0.0091  146 ILE A CG1 
1165 C  CG2 . ILE A 145 ? 0.1985 0.1879 0.2074 0.0046  -0.1105 -0.0203 146 ILE A CG2 
1166 C  CD1 . ILE A 145 ? 0.1863 0.2103 0.1575 0.0158  -0.0619 0.0243  146 ILE A CD1 
1167 N  N   . PHE A 146 ? 0.1803 0.1448 0.1069 -0.0034 -0.0480 -0.0033 147 PHE A N   
1168 C  CA  . PHE A 146 ? 0.1943 0.1442 0.0926 0.0133  -0.0561 0.0088  147 PHE A CA  
1169 C  C   . PHE A 146 ? 0.1796 0.1516 0.1214 -0.0089 -0.0406 -0.0130 147 PHE A C   
1170 O  O   . PHE A 146 ? 0.1868 0.1773 0.1268 -0.0015 -0.0331 -0.0127 147 PHE A O   
1171 C  CB  . PHE A 146 ? 0.1670 0.1838 0.0895 -0.0050 -0.0581 0.0228  147 PHE A CB  
1172 C  CG  . PHE A 146 ? 0.1784 0.1476 0.0913 0.0095  -0.0513 0.0220  147 PHE A CG  
1173 C  CD1 . PHE A 146 ? 0.1745 0.1667 0.1304 0.0130  -0.0603 -0.0190 147 PHE A CD1 
1174 C  CD2 . PHE A 146 ? 0.1886 0.1443 0.1161 -0.0071 -0.0326 0.0225  147 PHE A CD2 
1175 C  CE1 . PHE A 146 ? 0.1983 0.1515 0.0936 -0.0076 -0.0471 -0.0060 147 PHE A CE1 
1176 C  CE2 . PHE A 146 ? 0.1954 0.1746 0.1238 -0.0055 -0.0399 0.0108  147 PHE A CE2 
1177 C  CZ  . PHE A 146 ? 0.1879 0.1767 0.0965 -0.0111 -0.0330 0.0225  147 PHE A CZ  
1178 N  N   . LEU A 147 ? 0.1910 0.1591 0.0924 0.0040  -0.0480 -0.0120 148 LEU A N   
1179 C  CA  . LEU A 147 ? 0.1942 0.1399 0.0929 0.0098  -0.0440 -0.0217 148 LEU A CA  
1180 C  C   . LEU A 147 ? 0.2007 0.1537 0.0832 0.0055  -0.0271 -0.0279 148 LEU A C   
1181 O  O   . LEU A 147 ? 0.2013 0.1656 0.1328 0.0076  -0.0220 -0.0060 148 LEU A O   
1182 C  CB  . LEU A 147 ? 0.1924 0.1582 0.1146 0.0119  -0.0340 -0.0149 148 LEU A CB  
1183 C  CG  . LEU A 147 ? 0.2180 0.1480 0.1011 0.0035  -0.0519 -0.0105 148 LEU A CG  
1184 C  CD1 . LEU A 147 ? 0.2705 0.1516 0.1354 -0.0227 -0.0586 -0.0225 148 LEU A CD1 
1185 C  CD2 . LEU A 147 ? 0.2318 0.1850 0.0986 -0.0035 -0.0486 0.0135  148 LEU A CD2 
1186 N  N   . LYS A 148 ? 0.2442 0.1443 0.1236 -0.0302 -0.0433 -0.0149 149 LYS A N   
1187 C  CA  . LYS A 148 ? 0.2169 0.1532 0.1338 0.0033  -0.0629 -0.0062 149 LYS A CA  
1188 C  C   . LYS A 148 ? 0.2001 0.1580 0.1601 -0.0133 -0.0842 0.0013  149 LYS A C   
1189 O  O   . LYS A 148 ? 0.2401 0.1879 0.1631 0.0287  -0.0895 -0.0069 149 LYS A O   
1190 C  CB  . LYS A 148 ? 0.2816 0.2329 0.1324 -0.0210 -0.0433 0.0098  149 LYS A CB  
1191 C  CG  . LYS A 148 ? 0.2875 0.2361 0.1892 -0.0179 -0.0322 0.0265  149 LYS A CG  
1192 C  CD  . LYS A 148 ? 0.3911 0.3596 0.2387 -0.0268 -0.0158 0.0864  149 LYS A CD  
1193 C  CE  . LYS A 148 ? 0.4007 0.6842 0.2130 -0.1386 0.0584  0.0021  149 LYS A CE  
1194 N  NZ  . LYS A 148 ? 0.6271 0.7202 0.4699 -0.1650 0.0344  0.2474  149 LYS A NZ  
1195 N  N   . VAL A 149 ? 0.2807 0.1417 0.1555 -0.0012 -0.0765 -0.0126 150 VAL A N   
1196 C  CA  . VAL A 149 ? 0.2633 0.1694 0.1497 -0.0008 -0.0669 -0.0238 150 VAL A CA  
1197 C  C   . VAL A 149 ? 0.2478 0.1794 0.2236 -0.0008 -0.0879 -0.0005 150 VAL A C   
1198 O  O   . VAL A 149 ? 0.2935 0.2057 0.2001 -0.0142 -0.0771 0.0119  150 VAL A O   
1199 C  CB  . VAL A 149 ? 0.2837 0.1895 0.1648 0.0006  -0.0530 -0.0468 150 VAL A CB  
1200 C  CG1 . VAL A 149 ? 0.2960 0.2342 0.1597 0.0240  -0.0882 -0.0480 150 VAL A CG1 
1201 C  CG2 . VAL A 149 ? 0.2910 0.2266 0.2699 -0.0245 -0.0518 -0.0358 150 VAL A CG2 
1202 N  N   . GLY A 150 ? 0.2355 0.1641 0.1855 -0.0139 -0.0836 -0.0245 151 GLY A N   
1203 C  CA  . GLY A 150 ? 0.2775 0.1964 0.1730 -0.0458 -0.0898 0.0214  151 GLY A CA  
1204 C  C   . GLY A 150 ? 0.2750 0.1859 0.1730 -0.0350 -0.0818 0.0052  151 GLY A C   
1205 O  O   . GLY A 150 ? 0.2584 0.1777 0.1976 -0.0331 -0.0600 -0.0200 151 GLY A O   
1206 N  N   A SER A 151 ? 0.2981 0.1843 0.1791 -0.0268 -0.0917 0.0024  152 SER A N   
1207 N  N   B SER A 151 ? 0.3034 0.1921 0.1889 -0.0342 -0.0762 -0.0086 152 SER A N   
1208 C  CA  A SER A 151 ? 0.2600 0.2050 0.1985 0.0114  -0.0767 0.0054  152 SER A CA  
1209 C  CA  B SER A 151 ? 0.2512 0.1954 0.2482 -0.0192 -0.0608 0.0126  152 SER A CA  
1210 C  C   A SER A 151 ? 0.3394 0.1296 0.1850 0.0239  -0.1177 -0.0190 152 SER A C   
1211 C  C   B SER A 151 ? 0.2773 0.2230 0.1212 -0.0731 -0.0139 -0.0313 152 SER A C   
1212 O  O   A SER A 151 ? 0.2859 0.1706 0.1365 0.0258  -0.0978 -0.0184 152 SER A O   
1213 O  O   B SER A 151 ? 0.2162 0.2363 0.1681 -0.0134 -0.1004 -0.0277 152 SER A O   
1214 C  CB  A SER A 151 ? 0.2699 0.2705 0.2886 -0.0340 0.0047  -0.0335 152 SER A CB  
1215 C  CB  B SER A 151 ? 0.3031 0.2053 0.2615 -0.0545 0.0122  -0.0800 152 SER A CB  
1216 O  OG  A SER A 151 ? 0.2748 0.4528 0.2863 0.0144  -0.0648 -0.0712 152 SER A OG  
1217 O  OG  B SER A 151 ? 0.2703 0.3018 0.3288 -0.0388 -0.0450 0.0981  152 SER A OG  
1218 N  N   . ALA A 152 ? 0.2786 0.1949 0.1602 -0.0105 -0.0866 -0.0081 153 ALA A N   
1219 C  CA  . ALA A 152 ? 0.2913 0.1868 0.1497 0.0037  -0.0787 -0.0183 153 ALA A CA  
1220 C  C   . ALA A 152 ? 0.2178 0.2040 0.1753 -0.0155 -0.0706 -0.0203 153 ALA A C   
1221 O  O   . ALA A 152 ? 0.2570 0.1950 0.1927 -0.0271 -0.0303 -0.0066 153 ALA A O   
1222 C  CB  . ALA A 152 ? 0.3027 0.2428 0.1410 0.0087  -0.0981 -0.0425 153 ALA A CB  
1223 N  N   . LYS A 153 ? 0.2649 0.1425 0.1769 -0.0119 -0.1209 -0.0048 154 LYS A N   
1224 C  CA  . LYS A 153 ? 0.2394 0.1564 0.1730 -0.0233 -0.0829 0.0079  154 LYS A CA  
1225 C  C   . LYS A 153 ? 0.2042 0.1681 0.1852 0.0035  -0.0337 0.0139  154 LYS A C   
1226 O  O   . LYS A 153 ? 0.1949 0.1843 0.1498 -0.0095 -0.0685 0.0106  154 LYS A O   
1227 C  CB  . LYS A 153 ? 0.2026 0.1771 0.1652 0.0048  -0.0866 -0.0183 154 LYS A CB  
1228 C  CG  . LYS A 153 ? 0.2558 0.1737 0.1633 -0.0098 -0.0673 -0.0148 154 LYS A CG  
1229 C  CD  . LYS A 153 ? 0.3080 0.1753 0.1940 0.0115  -0.0267 -0.0031 154 LYS A CD  
1230 C  CE  . LYS A 153 ? 0.3943 0.2252 0.1720 0.0291  -0.0666 -0.0248 154 LYS A CE  
1231 N  NZ  . LYS A 153 ? 0.4702 0.3486 0.2058 0.0009  -0.0111 -0.0048 154 LYS A NZ  
1232 N  N   . PRO A 154 ? 0.2063 0.2101 0.1722 -0.0026 -0.0578 0.0229  155 PRO A N   
1233 C  CA  . PRO A 154 ? 0.2046 0.2412 0.1931 -0.0388 -0.0839 0.0431  155 PRO A CA  
1234 C  C   . PRO A 154 ? 0.1705 0.2068 0.1791 0.0098  -0.0562 0.0097  155 PRO A C   
1235 O  O   . PRO A 154 ? 0.2269 0.2261 0.1766 -0.0135 -0.0805 0.0305  155 PRO A O   
1236 C  CB  . PRO A 154 ? 0.1965 0.2787 0.2544 -0.0111 -0.1068 0.0508  155 PRO A CB  
1237 C  CG  . PRO A 154 ? 0.2625 0.3464 0.3072 -0.0131 -0.1078 0.1112  155 PRO A CG  
1238 C  CD  . PRO A 154 ? 0.2237 0.2341 0.1860 0.0152  -0.0334 0.0390  155 PRO A CD  
1239 N  N   . GLY A 155 ? 0.2112 0.1947 0.1922 0.0038  -0.0802 -0.0030 156 GLY A N   
1240 C  CA  . GLY A 155 ? 0.2202 0.1932 0.2425 -0.0079 -0.0752 0.0207  156 GLY A CA  
1241 C  C   . GLY A 155 ? 0.2324 0.1676 0.2119 -0.0048 -0.0526 0.0061  156 GLY A C   
1242 O  O   . GLY A 155 ? 0.2673 0.1605 0.3001 -0.0069 -0.0805 0.0104  156 GLY A O   
1243 N  N   . LEU A 156 ? 0.2262 0.1814 0.1512 -0.0017 -0.0757 0.0136  157 LEU A N   
1244 C  CA  . LEU A 156 ? 0.2300 0.1942 0.1712 -0.0057 -0.0949 0.0052  157 LEU A CA  
1245 C  C   . LEU A 156 ? 0.2097 0.1487 0.1595 -0.0201 -0.0917 0.0250  157 LEU A C   
1246 O  O   . LEU A 156 ? 0.2337 0.1879 0.1638 -0.0308 -0.0681 0.0012  157 LEU A O   
1247 C  CB  . LEU A 156 ? 0.2353 0.1789 0.1706 -0.0034 -0.0748 0.0163  157 LEU A CB  
1248 C  CG  . LEU A 156 ? 0.2178 0.2075 0.1659 -0.0247 -0.0607 0.0151  157 LEU A CG  
1249 C  CD1 . LEU A 156 ? 0.2248 0.2266 0.1773 -0.0443 -0.0834 -0.0118 157 LEU A CD1 
1250 C  CD2 . LEU A 156 ? 0.2462 0.2136 0.1978 0.0093  -0.0798 0.0192  157 LEU A CD2 
1251 N  N   . GLN A 157 ? 0.2137 0.1814 0.1476 -0.0111 -0.0829 -0.0171 158 GLN A N   
1252 C  CA  . GLN A 157 ? 0.2162 0.1938 0.1486 -0.0324 -0.0523 -0.0140 158 GLN A CA  
1253 C  C   . GLN A 157 ? 0.2226 0.1963 0.1475 0.0066  -0.0692 -0.0006 158 GLN A C   
1254 O  O   . GLN A 157 ? 0.2274 0.1996 0.1602 -0.0103 -0.0784 -0.0210 158 GLN A O   
1255 C  CB  . GLN A 157 ? 0.2533 0.2265 0.1755 -0.0416 -0.0941 -0.0161 158 GLN A CB  
1256 C  CG  . GLN A 157 ? 0.2794 0.2175 0.1676 -0.0211 -0.0714 -0.0122 158 GLN A CG  
1257 C  CD  . GLN A 157 ? 0.3204 0.1827 0.1591 -0.0326 -0.0841 0.0065  158 GLN A CD  
1258 O  OE1 . GLN A 157 ? 0.3357 0.2058 0.1465 -0.0128 -0.0611 0.0098  158 GLN A OE1 
1259 N  NE2 . GLN A 157 ? 0.3370 0.2306 0.1931 -0.0223 -0.0818 -0.0395 158 GLN A NE2 
1260 N  N   . LYS A 158 ? 0.2363 0.1868 0.1530 -0.0094 -0.0836 0.0111  159 LYS A N   
1261 C  CA  . LYS A 158 ? 0.2417 0.2201 0.1476 -0.0144 -0.0739 0.0313  159 LYS A CA  
1262 C  C   . LYS A 158 ? 0.2722 0.1852 0.1595 -0.0206 -0.0615 -0.0060 159 LYS A C   
1263 O  O   . LYS A 158 ? 0.2554 0.2248 0.1537 -0.0387 -0.0623 0.0031  159 LYS A O   
1264 C  CB  . LYS A 158 ? 0.3362 0.2076 0.2366 0.0074  -0.1416 0.0208  159 LYS A CB  
1265 C  CG  . LYS A 158 ? 0.4209 0.2717 0.3854 0.0364  -0.0964 0.1111  159 LYS A CG  
1266 C  CD  . LYS A 158 ? 0.6238 0.2742 0.3082 0.0999  -0.1016 0.0510  159 LYS A CD  
1267 C  CE  . LYS A 158 ? 0.7888 0.4910 0.3732 -0.0543 -0.1082 0.2101  159 LYS A CE  
1268 N  NZ  . LYS A 158 ? 0.7840 0.7050 0.4032 -0.1252 -0.2407 0.1715  159 LYS A NZ  
1269 N  N   . VAL A 159 ? 0.2315 0.1907 0.1731 -0.0075 -0.0845 0.0042  160 VAL A N   
1270 C  CA  . VAL A 159 ? 0.2306 0.2071 0.1155 -0.0296 -0.0598 0.0168  160 VAL A CA  
1271 C  C   . VAL A 159 ? 0.2259 0.2115 0.1911 -0.0154 -0.0815 -0.0021 160 VAL A C   
1272 O  O   . VAL A 159 ? 0.2643 0.1956 0.1816 -0.0162 -0.0719 0.0155  160 VAL A O   
1273 C  CB  . VAL A 159 ? 0.2570 0.2459 0.1026 -0.0004 -0.0525 0.0084  160 VAL A CB  
1274 C  CG1 . VAL A 159 ? 0.2504 0.2889 0.1591 -0.0252 -0.0899 0.0162  160 VAL A CG1 
1275 C  CG2 . VAL A 159 ? 0.3619 0.2441 0.1620 0.0381  -0.1063 -0.0325 160 VAL A CG2 
1276 N  N   . VAL A 160 ? 0.2427 0.1807 0.1382 -0.0273 -0.0719 -0.0042 161 VAL A N   
1277 C  CA  . VAL A 160 ? 0.3030 0.2134 0.1746 0.0302  -0.0623 0.0146  161 VAL A CA  
1278 C  C   . VAL A 160 ? 0.2370 0.1821 0.1914 -0.0256 -0.0557 0.0054  161 VAL A C   
1279 O  O   . VAL A 160 ? 0.2676 0.2198 0.1703 -0.0251 -0.0403 0.0052  161 VAL A O   
1280 C  CB  . VAL A 160 ? 0.5480 0.1624 0.1566 0.0903  0.0266  0.0306  161 VAL A CB  
1281 C  CG1 . VAL A 160 ? 0.4381 0.2467 0.2786 0.0232  -0.0616 -0.0633 161 VAL A CG1 
1282 C  CG2 . VAL A 160 ? 0.5900 0.2912 0.1658 0.0818  0.0298  0.0569  161 VAL A CG2 
1283 N  N   . ASP A 161 ? 0.2530 0.2162 0.1275 -0.0150 -0.0738 -0.0165 162 ASP A N   
1284 C  CA  . ASP A 161 ? 0.2943 0.2282 0.1338 -0.0348 -0.0773 -0.0179 162 ASP A CA  
1285 C  C   . ASP A 161 ? 0.3086 0.2517 0.1529 -0.0445 -0.0518 -0.0120 162 ASP A C   
1286 O  O   . ASP A 161 ? 0.3562 0.3652 0.1410 -0.0712 -0.0414 -0.0049 162 ASP A O   
1287 C  CB  . ASP A 161 ? 0.2646 0.3556 0.1357 -0.0625 -0.0563 -0.0122 162 ASP A CB  
1288 C  CG  . ASP A 161 ? 0.3168 0.3650 0.2363 -0.0706 -0.0575 -0.0638 162 ASP A CG  
1289 O  OD1 . ASP A 161 ? 0.3832 0.4319 0.2703 -0.0252 -0.0089 0.0022  162 ASP A OD1 
1290 O  OD2 . ASP A 161 ? 0.3070 0.5136 0.2669 -0.0298 -0.0647 -0.0081 162 ASP A OD2 
1291 N  N   . VAL A 162 ? 0.2742 0.2257 0.1591 -0.0439 -0.0795 0.0119  163 VAL A N   
1292 C  CA  . VAL A 162 ? 0.3247 0.2548 0.1814 -0.0462 -0.0533 0.0222  163 VAL A CA  
1293 C  C   . VAL A 162 ? 0.3049 0.2839 0.1161 -0.0513 -0.0683 0.0302  163 VAL A C   
1294 O  O   . VAL A 162 ? 0.3398 0.2778 0.1214 -0.0519 -0.0590 0.0216  163 VAL A O   
1295 C  CB  . VAL A 162 ? 0.2890 0.2423 0.3260 0.0070  -0.0666 0.0411  163 VAL A CB  
1296 C  CG1 . VAL A 162 ? 0.3767 0.2348 0.2955 -0.0607 -0.0602 0.0284  163 VAL A CG1 
1297 C  CG2 . VAL A 162 ? 0.4445 0.3713 0.3760 -0.0002 0.0126  0.0971  163 VAL A CG2 
1298 N  N   . LEU A 163 ? 0.2570 0.2551 0.1193 -0.0354 -0.0562 -0.0057 164 LEU A N   
1299 C  CA  . LEU A 163 ? 0.2561 0.2746 0.1003 -0.0443 -0.0204 0.0077  164 LEU A CA  
1300 C  C   . LEU A 163 ? 0.2676 0.2478 0.0906 -0.0223 -0.0342 -0.0080 164 LEU A C   
1301 O  O   . LEU A 163 ? 0.2629 0.2931 0.1552 -0.0408 -0.0245 0.0173  164 LEU A O   
1302 C  CB  . LEU A 163 ? 0.2781 0.2198 0.1227 -0.0320 -0.0107 0.0063  164 LEU A CB  
1303 C  CG  . LEU A 163 ? 0.2873 0.2082 0.0947 -0.0143 -0.0201 0.0142  164 LEU A CG  
1304 C  CD1 . LEU A 163 ? 0.2870 0.2191 0.2076 0.0187  -0.0554 0.0572  164 LEU A CD1 
1305 C  CD2 . LEU A 163 ? 0.2849 0.2427 0.1001 -0.0247 -0.0311 -0.0312 164 LEU A CD2 
1306 N  N   . ASP A 164 ? 0.3560 0.2841 0.0999 -0.0367 -0.0514 -0.0233 165 ASP A N   
1307 C  CA  . ASP A 164 ? 0.3982 0.3064 0.1457 -0.0533 -0.0016 -0.0153 165 ASP A CA  
1308 C  C   . ASP A 164 ? 0.4445 0.3124 0.1677 -0.0161 -0.0211 0.0137  165 ASP A C   
1309 O  O   . ASP A 164 ? 0.5304 0.4022 0.2266 -0.0335 0.0933  0.0206  165 ASP A O   
1310 C  CB  . ASP A 164 ? 0.5114 0.3981 0.1875 -0.0873 -0.0027 -0.1227 165 ASP A CB  
1311 C  CG  . ASP A 164 ? 0.5378 0.6034 0.3646 -0.0922 -0.0326 -0.0585 165 ASP A CG  
1312 O  OD1 . ASP A 164 ? 0.4657 0.7403 0.2780 -0.1504 -0.0544 -0.0791 165 ASP A OD1 
1313 O  OD2 . ASP A 164 ? 0.7569 0.9197 0.3120 -0.2198 0.1335  -0.2291 165 ASP A OD2 
1314 N  N   . SER A 165 ? 0.3182 0.3008 0.1097 -0.0418 -0.0603 0.0238  166 SER A N   
1315 C  CA  . SER A 165 ? 0.3638 0.3179 0.1544 -0.0842 -0.0674 0.0495  166 SER A CA  
1316 C  C   . SER A 165 ? 0.3706 0.3086 0.1022 -0.0776 -0.0339 0.0275  166 SER A C   
1317 O  O   . SER A 165 ? 0.3392 0.3494 0.1831 -0.0714 -0.0407 0.0716  166 SER A O   
1318 C  CB  . SER A 165 ? 0.4334 0.3616 0.2223 -0.0010 0.0250  0.0855  166 SER A CB  
1319 O  OG  . SER A 165 ? 0.4096 0.3098 0.2561 -0.0506 -0.0741 0.0342  166 SER A OG  
1320 N  N   . ILE A 166 ? 0.2933 0.2679 0.0990 -0.0513 -0.0498 0.0081  167 ILE A N   
1321 C  CA  . ILE A 166 ? 0.2755 0.2982 0.1213 -0.0650 -0.0409 0.0044  167 ILE A CA  
1322 C  C   . ILE A 166 ? 0.3172 0.2310 0.1275 -0.0236 -0.0465 -0.0199 167 ILE A C   
1323 O  O   . ILE A 166 ? 0.3003 0.2939 0.1171 -0.0489 -0.0190 0.0182  167 ILE A O   
1324 C  CB  . ILE A 166 ? 0.2930 0.2711 0.1558 -0.0516 -0.0434 0.0111  167 ILE A CB  
1325 C  CG1 . ILE A 166 ? 0.2723 0.2980 0.1080 -0.0540 -0.0290 -0.0061 167 ILE A CG1 
1326 C  CG2 . ILE A 166 ? 0.2834 0.2363 0.2460 -0.0446 -0.0488 0.0009  167 ILE A CG2 
1327 C  CD1 . ILE A 166 ? 0.2421 0.2890 0.1552 -0.0474 -0.0051 -0.0468 167 ILE A CD1 
1328 N  N   . LYS A 167 ? 0.2685 0.2651 0.1333 -0.0067 -0.0255 -0.0062 168 LYS A N   
1329 C  CA  . LYS A 167 ? 0.2767 0.2586 0.1627 -0.0288 0.0022  -0.0322 168 LYS A CA  
1330 C  C   . LYS A 167 ? 0.3236 0.2940 0.1315 -0.0499 -0.0363 0.0174  168 LYS A C   
1331 O  O   . LYS A 167 ? 0.3115 0.3130 0.1411 -0.0152 -0.0188 0.0234  168 LYS A O   
1332 C  CB  . LYS A 167 ? 0.3823 0.2799 0.1562 -0.0200 0.0205  -0.0320 168 LYS A CB  
1333 C  CG  . LYS A 167 ? 0.4099 0.3176 0.1616 -0.0178 -0.0296 -0.0151 168 LYS A CG  
1334 C  CD  . LYS A 167 ? 0.5328 0.4051 0.1956 -0.0381 -0.0820 -0.1035 168 LYS A CD  
1335 C  CE  . LYS A 167 ? 0.7709 0.5465 0.5660 0.0797  -0.1415 0.0378  168 LYS A CE  
1336 N  N   . THR A 168 ? 0.3312 0.3220 0.1205 -0.0651 -0.0161 0.0397  169 THR A N   
1337 C  CA  . THR A 168 ? 0.3543 0.3221 0.1473 -0.1226 0.0330  0.0299  169 THR A CA  
1338 C  C   . THR A 168 ? 0.2646 0.3121 0.1846 -0.0961 0.0046  0.0522  169 THR A C   
1339 O  O   . THR A 168 ? 0.3389 0.2978 0.1424 -0.0629 -0.0379 0.0380  169 THR A O   
1340 C  CB  . THR A 168 ? 0.3931 0.3598 0.1577 -0.0995 0.0672  0.0165  169 THR A CB  
1341 O  OG1 . THR A 168 ? 0.4808 0.4618 0.1473 -0.1167 0.0187  0.0430  169 THR A OG1 
1342 C  CG2 . THR A 168 ? 0.5165 0.4172 0.1439 -0.0602 0.0406  -0.0140 169 THR A CG2 
1343 N  N   . LYS A 169 ? 0.2745 0.3459 0.1759 -0.0939 -0.0084 0.0141  170 LYS A N   
1344 C  CA  . LYS A 169 ? 0.2731 0.2832 0.1602 -0.0688 -0.0350 0.0432  170 LYS A CA  
1345 C  C   . LYS A 169 ? 0.2990 0.3441 0.1835 -0.0927 -0.0321 0.0585  170 LYS A C   
1346 O  O   . LYS A 169 ? 0.3504 0.4307 0.1679 -0.1365 -0.0383 0.0664  170 LYS A O   
1347 C  CB  . LYS A 169 ? 0.2724 0.3546 0.1906 -0.0631 -0.0363 0.0065  170 LYS A CB  
1348 C  CG  . LYS A 169 ? 0.2870 0.3650 0.2403 -0.0981 -0.0461 0.0133  170 LYS A CG  
1349 C  CD  . LYS A 169 ? 0.3211 0.4453 0.3656 -0.1140 -0.1288 0.0081  170 LYS A CD  
1350 C  CE  . LYS A 169 ? 0.5567 0.5973 0.3373 -0.1028 -0.0192 -0.1459 170 LYS A CE  
1351 N  N   . GLY A 170 ? 0.3464 0.2958 0.1475 -0.0743 -0.0577 0.0486  171 GLY A N   
1352 C  CA  . GLY A 170 ? 0.3637 0.2831 0.2286 -0.0702 -0.0730 0.0610  171 GLY A CA  
1353 C  C   . GLY A 170 ? 0.3713 0.2858 0.2223 -0.0994 -0.0575 0.0620  171 GLY A C   
1354 O  O   . GLY A 170 ? 0.4860 0.3107 0.3615 -0.1432 -0.1424 0.1163  171 GLY A O   
1355 N  N   . LYS A 171 ? 0.3138 0.2809 0.1654 -0.0895 -0.0312 0.0706  172 LYS A N   
1356 C  CA  . LYS A 171 ? 0.3519 0.2957 0.1390 -0.0746 -0.0421 0.0565  172 LYS A CA  
1357 C  C   . LYS A 171 ? 0.3481 0.2752 0.1443 -0.0599 -0.0346 0.0598  172 LYS A C   
1358 O  O   . LYS A 171 ? 0.3535 0.3151 0.1260 -0.0713 -0.0452 0.0502  172 LYS A O   
1359 C  CB  . LYS A 171 ? 0.3224 0.3107 0.2148 -0.0666 -0.0511 0.0048  172 LYS A CB  
1360 C  CG  . LYS A 171 ? 0.3274 0.3480 0.2815 -0.0643 -0.0195 0.0033  172 LYS A CG  
1361 C  CD  . LYS A 171 ? 0.4518 0.3237 0.4513 -0.0575 0.1131  -0.0723 172 LYS A CD  
1362 N  N   . SER A 172 ? 0.3516 0.2597 0.1586 -0.0614 -0.0659 0.0471  173 SER A N   
1363 C  CA  . SER A 172 ? 0.3680 0.3116 0.1622 -0.0520 -0.0674 0.0207  173 SER A CA  
1364 C  C   . SER A 172 ? 0.3702 0.2812 0.0999 -0.0359 -0.0236 0.0502  173 SER A C   
1365 O  O   . SER A 172 ? 0.4312 0.3629 0.0956 -0.0089 -0.0122 0.0460  173 SER A O   
1366 C  CB  . SER A 172 ? 0.5430 0.2614 0.1781 -0.0622 -0.0498 0.0793  173 SER A CB  
1367 O  OG  . SER A 172 ? 0.4847 0.3563 0.2854 -0.0078 0.0705  0.1229  173 SER A OG  
1368 N  N   . ALA A 173 ? 0.3405 0.2849 0.1475 0.0346  -0.0723 0.0359  174 ALA A N   
1369 C  CA  . ALA A 173 ? 0.3407 0.3662 0.1260 0.0297  -0.0581 0.0495  174 ALA A CA  
1370 C  C   . ALA A 173 ? 0.2752 0.3481 0.1343 0.0366  -0.0199 0.0048  174 ALA A C   
1371 O  O   . ALA A 173 ? 0.4196 0.3784 0.0773 0.0555  -0.0279 0.0252  174 ALA A O   
1372 C  CB  . ALA A 173 ? 0.3788 0.3512 0.1516 0.0203  -0.0656 0.0107  174 ALA A CB  
1373 N  N   . ASP A 174 ? 0.4063 0.3684 0.2333 0.0631  -0.1326 0.0916  175 ASP A N   
1374 C  CA  . ASP A 174 ? 0.3167 0.5062 0.2980 0.0146  -0.1225 0.0765  175 ASP A CA  
1375 C  C   . ASP A 174 ? 0.3253 0.3213 0.1766 0.0706  -0.1246 -0.0273 175 ASP A C   
1376 O  O   . ASP A 174 ? 0.4013 0.3397 0.2244 0.0539  -0.1187 -0.0384 175 ASP A O   
1377 C  CB  . ASP A 174 ? 0.5115 0.7215 0.2963 0.1943  -0.1042 0.1280  175 ASP A CB  
1378 C  CG  . ASP A 174 ? 0.7683 0.7869 0.6022 0.0124  0.0616  0.0504  175 ASP A CG  
1379 O  OD1 . ASP A 174 ? 0.6254 0.5888 0.9776 0.1326  0.1773  -0.0342 175 ASP A OD1 
1380 O  OD2 . ASP A 174 ? 1.4989 1.0159 0.5066 0.2233  -0.3673 -0.2297 175 ASP A OD2 
1381 N  N   . PHE A 175 ? 0.3248 0.2643 0.1527 -0.0068 -0.0760 0.0199  176 PHE A N   
1382 C  CA  . PHE A 175 ? 0.3213 0.2088 0.1936 0.0097  -0.1243 0.0178  176 PHE A CA  
1383 C  C   . PHE A 175 ? 0.3092 0.1727 0.1976 0.0131  -0.1027 0.0326  176 PHE A C   
1384 O  O   . PHE A 175 ? 0.3757 0.2611 0.2007 0.0491  -0.1393 -0.0380 176 PHE A O   
1385 C  CB  . PHE A 175 ? 0.3248 0.1731 0.2428 0.0089  -0.1377 0.0307  176 PHE A CB  
1386 C  CG  . PHE A 175 ? 0.2711 0.1864 0.1909 0.0150  -0.0806 -0.0005 176 PHE A CG  
1387 C  CD1 . PHE A 175 ? 0.3242 0.2153 0.1932 -0.0031 -0.0682 -0.0069 176 PHE A CD1 
1388 C  CD2 . PHE A 175 ? 0.3016 0.2306 0.1895 0.0346  -0.0939 0.0309  176 PHE A CD2 
1389 C  CE1 . PHE A 175 ? 0.3572 0.1914 0.1813 -0.0003 -0.0766 0.0006  176 PHE A CE1 
1390 C  CE2 . PHE A 175 ? 0.3713 0.1985 0.2182 0.0104  -0.1119 0.0023  176 PHE A CE2 
1391 C  CZ  . PHE A 175 ? 0.3716 0.2204 0.1623 0.0625  -0.1289 0.0046  176 PHE A CZ  
1392 N  N   . THR A 176 ? 0.2626 0.2240 0.2057 -0.0092 -0.1204 0.0307  177 THR A N   
1393 C  CA  . THR A 176 ? 0.2865 0.2464 0.1751 -0.0082 -0.0879 0.0651  177 THR A CA  
1394 C  C   . THR A 176 ? 0.2797 0.2162 0.1072 -0.0208 -0.0863 0.0329  177 THR A C   
1395 O  O   . THR A 176 ? 0.3190 0.2238 0.1090 -0.0032 -0.0922 0.0367  177 THR A O   
1396 C  CB  . THR A 176 ? 0.3233 0.2414 0.1597 -0.0010 -0.1130 0.0541  177 THR A CB  
1397 O  OG1 . THR A 176 ? 0.3698 0.2947 0.1396 0.0313  -0.0952 0.0486  177 THR A OG1 
1398 C  CG2 . THR A 176 ? 0.3355 0.2940 0.3365 -0.0002 -0.1132 0.1412  177 THR A CG2 
1399 N  N   . ASN A 177 ? 0.2606 0.2076 0.1338 -0.0172 -0.0961 0.0242  178 ASN A N   
1400 C  CA  . ASN A 177 ? 0.2489 0.2193 0.1703 -0.0048 -0.1020 0.0387  178 ASN A CA  
1401 C  C   . ASN A 177 ? 0.3239 0.2177 0.1703 -0.0326 -0.1461 0.0543  178 ASN A C   
1402 O  O   . ASN A 177 ? 0.3547 0.2355 0.2930 -0.0737 -0.1639 0.1077  178 ASN A O   
1403 C  CB  . ASN A 177 ? 0.2719 0.2112 0.2079 -0.0239 -0.1346 0.0542  178 ASN A CB  
1404 C  CG  . ASN A 177 ? 0.2417 0.2092 0.2101 0.0155  -0.0879 0.0262  178 ASN A CG  
1405 O  OD1 . ASN A 177 ? 0.2852 0.2568 0.2374 0.0242  -0.0395 0.0491  178 ASN A OD1 
1406 N  ND2 . ASN A 177 ? 0.3280 0.2715 0.1396 0.0060  -0.1046 0.0307  178 ASN A ND2 
1407 N  N   . PHE A 178 ? 0.2909 0.2168 0.1006 -0.0195 -0.1030 0.0533  179 PHE A N   
1408 C  CA  . PHE A 178 ? 0.2893 0.2151 0.0960 0.0049  -0.0805 0.0477  179 PHE A CA  
1409 C  C   . PHE A 178 ? 0.2867 0.1879 0.1212 0.0087  -0.0837 0.0204  179 PHE A C   
1410 O  O   . PHE A 178 ? 0.3359 0.2064 0.1375 -0.0351 -0.0811 0.0146  179 PHE A O   
1411 C  CB  . PHE A 178 ? 0.2728 0.1828 0.1598 0.0127  -0.0776 0.0323  179 PHE A CB  
1412 C  CG  . PHE A 178 ? 0.2596 0.1934 0.1351 -0.0381 -0.0959 0.0484  179 PHE A CG  
1413 C  CD1 . PHE A 178 ? 0.3079 0.1769 0.1511 -0.0211 -0.0631 0.0186  179 PHE A CD1 
1414 C  CD2 . PHE A 178 ? 0.2380 0.2139 0.1351 -0.0200 -0.0806 0.0412  179 PHE A CD2 
1415 C  CE1 . PHE A 178 ? 0.3193 0.2133 0.1555 -0.0100 -0.0798 0.0350  179 PHE A CE1 
1416 C  CE2 . PHE A 178 ? 0.2503 0.2062 0.1400 0.0029  -0.0623 0.0460  179 PHE A CE2 
1417 C  CZ  . PHE A 178 ? 0.2410 0.2162 0.1489 -0.0093 -0.0651 0.0248  179 PHE A CZ  
1418 N  N   . ASP A 179 ? 0.2543 0.2100 0.1354 0.0001  -0.0772 0.0289  180 ASP A N   
1419 C  CA  . ASP A 179 ? 0.2287 0.2069 0.1465 0.0088  -0.0658 0.0328  180 ASP A CA  
1420 C  C   . ASP A 179 ? 0.2639 0.1796 0.1313 0.0132  -0.0678 0.0143  180 ASP A C   
1421 O  O   . ASP A 179 ? 0.2318 0.1867 0.1554 -0.0070 -0.0616 0.0016  180 ASP A O   
1422 C  CB  . ASP A 179 ? 0.2137 0.2366 0.2349 -0.0146 -0.0936 0.0439  180 ASP A CB  
1423 C  CG  . ASP A 179 ? 0.2542 0.2723 0.2776 0.0288  -0.0794 0.0065  180 ASP A CG  
1424 O  OD1 . ASP A 179 ? 0.2782 0.2232 0.2139 0.0293  -0.0238 0.0192  180 ASP A OD1 
1425 O  OD2 . ASP A 179 ? 0.2658 0.4634 0.3192 0.0220  -0.0673 -0.0575 180 ASP A OD2 
1426 N  N   . PRO A 180 ? 0.2395 0.1656 0.1426 0.0147  -0.0728 0.0137  181 PRO A N   
1427 C  CA  . PRO A 180 ? 0.2100 0.1972 0.1645 -0.0251 -0.0765 0.0469  181 PRO A CA  
1428 C  C   . PRO A 180 ? 0.2165 0.1927 0.1467 0.0078  -0.0351 -0.0019 181 PRO A C   
1429 O  O   . PRO A 180 ? 0.2445 0.1996 0.1612 0.0157  -0.0631 0.0279  181 PRO A O   
1430 C  CB  . PRO A 180 ? 0.2431 0.2010 0.2178 -0.0254 -0.0819 0.0164  181 PRO A CB  
1431 C  CG  . PRO A 180 ? 0.2915 0.2142 0.1692 0.0047  -0.0812 -0.0093 181 PRO A CG  
1432 C  CD  . PRO A 180 ? 0.2732 0.2015 0.1640 -0.0209 -0.0917 0.0164  181 PRO A CD  
1433 N  N   . ARG A 181 ? 0.2068 0.2202 0.1422 0.0113  -0.0480 0.0137  182 ARG A N   
1434 C  CA  . ARG A 181 ? 0.2141 0.2122 0.1773 0.0100  -0.0307 0.0070  182 ARG A CA  
1435 C  C   . ARG A 181 ? 0.2114 0.2231 0.1546 -0.0052 -0.0776 0.0173  182 ARG A C   
1436 O  O   . ARG A 181 ? 0.2403 0.2231 0.2062 -0.0004 -0.0622 0.0377  182 ARG A O   
1437 C  CB  . ARG A 181 ? 0.2266 0.2064 0.1771 0.0176  -0.0531 -0.0022 182 ARG A CB  
1438 C  CG  . ARG A 181 ? 0.3291 0.2160 0.1886 0.0337  -0.0288 -0.0173 182 ARG A CG  
1439 C  CD  . ARG A 181 ? 0.3188 0.2322 0.2989 0.0540  -0.0087 0.0311  182 ARG A CD  
1440 N  NE  . ARG A 181 ? 0.2820 0.1903 0.3295 0.0335  -0.0212 0.0630  182 ARG A NE  
1441 C  CZ  . ARG A 181 ? 0.2643 0.2509 0.3644 0.0403  -0.0201 0.0380  182 ARG A CZ  
1442 N  NH1 . ARG A 181 ? 0.2985 0.3222 0.4111 0.0333  0.0280  0.0324  182 ARG A NH1 
1443 N  NH2 . ARG A 181 ? 0.3183 0.3881 0.3893 0.0603  -0.0455 0.1229  182 ARG A NH2 
1444 N  N   . GLY A 182 ? 0.2448 0.1925 0.1462 0.0006  -0.0832 0.0131  183 GLY A N   
1445 C  CA  . GLY A 182 ? 0.2631 0.1816 0.1741 -0.0154 -0.1111 0.0381  183 GLY A CA  
1446 C  C   . GLY A 182 ? 0.2283 0.2103 0.1936 -0.0036 -0.0644 0.0173  183 GLY A C   
1447 O  O   . GLY A 182 ? 0.2963 0.2216 0.1774 0.0215  -0.0835 0.0152  183 GLY A O   
1448 N  N   . LEU A 183 ? 0.2223 0.2001 0.1640 0.0086  -0.0640 0.0136  184 LEU A N   
1449 C  CA  . LEU A 183 ? 0.2276 0.1967 0.1331 0.0261  -0.0383 0.0249  184 LEU A CA  
1450 C  C   . LEU A 183 ? 0.2187 0.1676 0.1182 0.0105  -0.0488 0.0124  184 LEU A C   
1451 O  O   . LEU A 183 ? 0.2421 0.1992 0.1669 0.0314  -0.0537 0.0497  184 LEU A O   
1452 C  CB  . LEU A 183 ? 0.2058 0.2280 0.1526 0.0052  -0.0618 0.0798  184 LEU A CB  
1453 C  CG  . LEU A 183 ? 0.2341 0.2287 0.1360 0.0447  -0.0615 0.0500  184 LEU A CG  
1454 C  CD1 . LEU A 183 ? 0.2663 0.3269 0.1602 -0.0048 -0.0741 0.0774  184 LEU A CD1 
1455 C  CD2 . LEU A 183 ? 0.3185 0.2712 0.1584 0.0862  -0.0053 0.0051  184 LEU A CD2 
1456 N  N   . LEU A 184 ? 0.2143 0.2039 0.1200 -0.0027 -0.0535 0.0143  185 LEU A N   
1457 C  CA  . LEU A 184 ? 0.2144 0.1909 0.1315 -0.0040 -0.0614 0.0311  185 LEU A CA  
1458 C  C   . LEU A 184 ? 0.2144 0.2019 0.1777 -0.0277 -0.0822 0.0482  185 LEU A C   
1459 O  O   . LEU A 184 ? 0.2831 0.2617 0.2327 -0.0695 -0.1487 0.0651  185 LEU A O   
1460 C  CB  . LEU A 184 ? 0.1953 0.2067 0.2062 -0.0116 -0.0497 -0.0011 185 LEU A CB  
1461 C  CG  . LEU A 184 ? 0.2345 0.2572 0.2514 -0.0241 -0.0544 -0.0159 185 LEU A CG  
1462 C  CD1 . LEU A 184 ? 0.3172 0.2186 0.2708 -0.0121 -0.0133 -0.0138 185 LEU A CD1 
1463 C  CD2 . LEU A 184 ? 0.2196 0.2530 0.3201 -0.0163 -0.0826 0.0354  185 LEU A CD2 
1464 N  N   . PRO A 185 ? 0.1907 0.2240 0.1509 -0.0107 -0.0685 0.0352  186 PRO A N   
1465 C  CA  . PRO A 185 ? 0.1893 0.1971 0.2044 -0.0117 -0.0525 0.0451  186 PRO A CA  
1466 C  C   . PRO A 185 ? 0.1746 0.1831 0.1877 -0.0168 -0.0690 0.0262  186 PRO A C   
1467 O  O   . PRO A 185 ? 0.1961 0.1859 0.2577 -0.0040 -0.0713 0.0343  186 PRO A O   
1468 C  CB  . PRO A 185 ? 0.1931 0.2281 0.1785 0.0078  -0.0446 0.0306  186 PRO A CB  
1469 C  CG  . PRO A 185 ? 0.1972 0.2157 0.1331 0.0160  -0.0413 0.0134  186 PRO A CG  
1470 C  CD  . PRO A 185 ? 0.1971 0.1990 0.1318 0.0022  -0.0726 0.0201  186 PRO A CD  
1471 N  N   . GLU A 186 ? 0.2083 0.2158 0.2114 -0.0278 -0.0578 0.0425  187 GLU A N   
1472 C  CA  . GLU A 186 ? 0.2135 0.2252 0.2205 -0.0064 -0.0468 0.0135  187 GLU A CA  
1473 C  C   . GLU A 186 ? 0.1825 0.2500 0.2111 0.0055  -0.0615 0.0217  187 GLU A C   
1474 O  O   . GLU A 186 ? 0.2130 0.2690 0.2782 0.0399  -0.0716 -0.0027 187 GLU A O   
1475 C  CB  . GLU A 186 ? 0.2623 0.2675 0.2987 -0.0529 -0.0687 0.0292  187 GLU A CB  
1476 C  CG  . GLU A 186 ? 0.3208 0.2548 0.3262 -0.0513 -0.0928 0.0410  187 GLU A CG  
1477 C  CD  . GLU A 186 ? 0.2864 0.2682 0.4077 -0.0409 -0.0824 0.0713  187 GLU A CD  
1478 O  OE1 . GLU A 186 ? 0.3332 0.3323 0.3680 -0.0757 -0.0908 0.0619  187 GLU A OE1 
1479 O  OE2 . GLU A 186 ? 0.3247 0.3104 0.5601 -0.0027 -0.1386 -0.0352 187 GLU A OE2 
1480 N  N   . SER A 187 ? 0.1702 0.2584 0.2058 -0.0100 -0.0747 0.0209  188 SER A N   
1481 C  CA  . SER A 187 ? 0.2118 0.2416 0.2044 -0.0102 -0.0591 0.0130  188 SER A CA  
1482 C  C   . SER A 187 ? 0.2148 0.2164 0.1857 -0.0012 -0.0363 0.0096  188 SER A C   
1483 O  O   . SER A 187 ? 0.2043 0.2908 0.1870 -0.0312 -0.0288 -0.0143 188 SER A O   
1484 C  CB  . SER A 187 ? 0.2442 0.3023 0.1598 0.0139  -0.0612 0.0311  188 SER A CB  
1485 O  OG  . SER A 187 ? 0.2432 0.2622 0.1846 -0.0146 -0.0662 0.0240  188 SER A OG  
1486 N  N   . LEU A 188 ? 0.1676 0.2165 0.2435 0.0019  -0.0337 -0.0275 189 LEU A N   
1487 C  CA  . LEU A 188 ? 0.2096 0.2205 0.2141 -0.0203 -0.0644 -0.0186 189 LEU A CA  
1488 C  C   . LEU A 188 ? 0.1825 0.2316 0.1979 -0.0139 -0.0285 -0.0181 189 LEU A C   
1489 O  O   . LEU A 188 ? 0.2046 0.2866 0.1978 -0.0458 -0.0355 -0.0296 189 LEU A O   
1490 C  CB  . LEU A 188 ? 0.2291 0.2011 0.2761 -0.0362 -0.0748 -0.0102 189 LEU A CB  
1491 C  CG  . LEU A 188 ? 0.2797 0.2417 0.2929 -0.0210 -0.0776 -0.0233 189 LEU A CG  
1492 C  CD1 . LEU A 188 ? 0.2507 0.2601 0.3387 0.0133  -0.1092 0.0234  189 LEU A CD1 
1493 C  CD2 . LEU A 188 ? 0.2258 0.3864 0.3395 0.0245  -0.0743 0.0139  189 LEU A CD2 
1494 N  N   . ASP A 189 ? 0.1749 0.2503 0.1979 0.0108  -0.0295 -0.0061 190 ASP A N   
1495 C  CA  . ASP A 189 ? 0.1787 0.2978 0.1911 -0.0244 -0.0385 -0.0348 190 ASP A CA  
1496 C  C   . ASP A 189 ? 0.1649 0.2223 0.1810 -0.0265 -0.0161 -0.0283 190 ASP A C   
1497 O  O   . ASP A 189 ? 0.1848 0.2219 0.1573 0.0080  -0.0288 -0.0110 190 ASP A O   
1498 C  CB  . ASP A 189 ? 0.2715 0.3310 0.1848 -0.0433 0.0262  -0.0157 190 ASP A CB  
1499 C  CG  . ASP A 189 ? 0.2521 0.4385 0.2265 -0.0875 -0.0159 -0.0464 190 ASP A CG  
1500 O  OD1 . ASP A 189 ? 0.2643 0.5805 0.4019 -0.0773 0.0996  -0.1310 190 ASP A OD1 
1501 O  OD2 . ASP A 189 ? 0.3104 0.5938 0.3121 -0.1586 -0.0068 0.0778  190 ASP A OD2 
1502 N  N   . TYR A 190 ? 0.1591 0.2147 0.1645 -0.0198 -0.0269 0.0003  191 TYR A N   
1503 C  CA  . TYR A 190 ? 0.1685 0.2258 0.1336 -0.0226 -0.0372 0.0263  191 TYR A CA  
1504 C  C   . TYR A 190 ? 0.1868 0.1929 0.1001 0.0143  -0.0078 -0.0044 191 TYR A C   
1505 O  O   . TYR A 190 ? 0.1774 0.2417 0.1058 -0.0013 0.0034  -0.0206 191 TYR A O   
1506 C  CB  . TYR A 190 ? 0.2294 0.1917 0.1333 -0.0036 -0.0164 0.0022  191 TYR A CB  
1507 C  CG  . TYR A 190 ? 0.1795 0.2079 0.1293 -0.0047 -0.0367 0.0111  191 TYR A CG  
1508 C  CD1 . TYR A 190 ? 0.2073 0.2085 0.1543 -0.0187 -0.0418 -0.0005 191 TYR A CD1 
1509 C  CD2 . TYR A 190 ? 0.2028 0.2231 0.1397 0.0287  -0.0223 0.0158  191 TYR A CD2 
1510 C  CE1 . TYR A 190 ? 0.1882 0.2205 0.1774 0.0012  -0.0391 -0.0071 191 TYR A CE1 
1511 C  CE2 . TYR A 190 ? 0.2132 0.2427 0.1426 -0.0100 -0.0214 -0.0097 191 TYR A CE2 
1512 C  CZ  . TYR A 190 ? 0.2157 0.2258 0.1381 0.0164  -0.0356 -0.0002 191 TYR A CZ  
1513 O  OH  . TYR A 190 ? 0.2823 0.2259 0.1891 0.0341  -0.0287 -0.0255 191 TYR A OH  
1514 N  N   . TRP A 191 ? 0.1738 0.1986 0.0918 0.0027  -0.0339 -0.0128 192 TRP A N   
1515 C  CA  . TRP A 191 ? 0.1799 0.1889 0.1128 -0.0044 -0.0555 0.0030  192 TRP A CA  
1516 C  C   . TRP A 191 ? 0.1803 0.1874 0.0634 -0.0039 -0.0260 -0.0044 192 TRP A C   
1517 O  O   . TRP A 191 ? 0.2215 0.2195 0.0688 -0.0171 -0.0215 -0.0048 192 TRP A O   
1518 C  CB  . TRP A 191 ? 0.1967 0.1807 0.1296 0.0019  -0.0258 -0.0066 192 TRP A CB  
1519 C  CG  . TRP A 191 ? 0.1733 0.1857 0.1008 0.0114  -0.0279 0.0104  192 TRP A CG  
1520 C  CD1 . TRP A 191 ? 0.1989 0.2044 0.1260 0.0162  -0.0137 0.0299  192 TRP A CD1 
1521 C  CD2 . TRP A 191 ? 0.1913 0.1787 0.1300 0.0139  -0.0517 0.0083  192 TRP A CD2 
1522 N  NE1 . TRP A 191 ? 0.2406 0.1990 0.1773 0.0166  -0.0129 0.0323  192 TRP A NE1 
1523 C  CE2 . TRP A 191 ? 0.1816 0.1782 0.1976 0.0340  -0.0491 0.0282  192 TRP A CE2 
1524 C  CE3 . TRP A 191 ? 0.1680 0.2126 0.1491 0.0113  -0.0416 -0.0323 192 TRP A CE3 
1525 C  CZ2 . TRP A 191 ? 0.1871 0.1891 0.1870 0.0089  -0.0137 0.0490  192 TRP A CZ2 
1526 C  CZ3 . TRP A 191 ? 0.2011 0.2061 0.2061 -0.0251 -0.0444 -0.0122 192 TRP A CZ3 
1527 C  CH2 . TRP A 191 ? 0.1899 0.2284 0.1900 0.0136  -0.0345 0.0226  192 TRP A CH2 
1528 N  N   . THR A 192 ? 0.1952 0.1766 0.0913 -0.0009 -0.0458 0.0004  193 THR A N   
1529 C  CA  . THR A 192 ? 0.1609 0.1867 0.1098 -0.0044 -0.0378 0.0050  193 THR A CA  
1530 C  C   . THR A 192 ? 0.1773 0.2015 0.0789 -0.0146 -0.0266 -0.0042 193 THR A C   
1531 O  O   . THR A 192 ? 0.1995 0.2234 0.0754 0.0091  -0.0245 0.0022  193 THR A O   
1532 C  CB  . THR A 192 ? 0.1806 0.1958 0.0838 0.0175  -0.0139 0.0001  193 THR A CB  
1533 O  OG1 . THR A 192 ? 0.2176 0.1796 0.1203 0.0070  -0.0279 -0.0089 193 THR A OG1 
1534 C  CG2 . THR A 192 ? 0.2083 0.2313 0.0759 0.0070  -0.0234 -0.0234 193 THR A CG2 
1535 N  N   . TYR A 193 ? 0.1588 0.1771 0.1012 -0.0030 -0.0368 -0.0053 194 TYR A N   
1536 C  CA  . TYR A 193 ? 0.1501 0.2053 0.1015 0.0040  -0.0348 0.0017  194 TYR A CA  
1537 C  C   . TYR A 193 ? 0.1633 0.1722 0.0604 0.0004  -0.0262 -0.0254 194 TYR A C   
1538 O  O   . TYR A 193 ? 0.1945 0.1891 0.0696 -0.0011 -0.0343 -0.0095 194 TYR A O   
1539 C  CB  . TYR A 193 ? 0.1827 0.1992 0.1006 0.0234  -0.0271 -0.0094 194 TYR A CB  
1540 C  CG  . TYR A 193 ? 0.1665 0.1799 0.0925 0.0183  -0.0491 -0.0004 194 TYR A CG  
1541 C  CD1 . TYR A 193 ? 0.1805 0.1615 0.0888 0.0058  -0.0413 0.0165  194 TYR A CD1 
1542 C  CD2 . TYR A 193 ? 0.1731 0.1837 0.1160 0.0109  -0.0456 0.0064  194 TYR A CD2 
1543 C  CE1 . TYR A 193 ? 0.1376 0.1611 0.1058 0.0050  -0.0139 0.0179  194 TYR A CE1 
1544 C  CE2 . TYR A 193 ? 0.1663 0.1759 0.1224 0.0070  -0.0469 -0.0102 194 TYR A CE2 
1545 C  CZ  . TYR A 193 ? 0.1468 0.1399 0.0918 -0.0060 -0.0176 0.0082  194 TYR A CZ  
1546 O  OH  . TYR A 193 ? 0.1667 0.1627 0.1006 -0.0009 -0.0177 0.0021  194 TYR A OH  
1547 N  N   . PRO A 194 ? 0.1789 0.2022 0.0841 -0.0039 -0.0441 -0.0209 195 PRO A N   
1548 C  CA  . PRO A 194 ? 0.1697 0.2004 0.1038 -0.0025 -0.0316 -0.0452 195 PRO A CA  
1549 C  C   . PRO A 194 ? 0.1691 0.1619 0.0856 0.0084  -0.0447 -0.0359 195 PRO A C   
1550 O  O   . PRO A 194 ? 0.1932 0.1849 0.1155 0.0168  -0.0615 -0.0154 195 PRO A O   
1551 C  CB  . PRO A 194 ? 0.2409 0.2240 0.0721 -0.0044 -0.0286 -0.0465 195 PRO A CB  
1552 C  CG  . PRO A 194 ? 0.2342 0.2769 0.0805 -0.0518 -0.0303 -0.0409 195 PRO A CG  
1553 C  CD  . PRO A 194 ? 0.2148 0.2466 0.0751 -0.0290 -0.0529 -0.0199 195 PRO A CD  
1554 N  N   . GLY A 195 ? 0.1648 0.1787 0.0907 -0.0290 -0.0181 -0.0315 196 GLY A N   
1555 C  CA  . GLY A 195 ? 0.1726 0.2069 0.1058 0.0048  -0.0234 0.0221  196 GLY A CA  
1556 C  C   . GLY A 195 ? 0.1692 0.1541 0.1045 -0.0069 -0.0348 -0.0021 196 GLY A C   
1557 O  O   . GLY A 195 ? 0.1794 0.1439 0.1126 -0.0050 -0.0467 -0.0044 196 GLY A O   
1558 N  N   . SER A 196 ? 0.1777 0.1683 0.0976 0.0037  -0.0501 -0.0099 197 SER A N   
1559 C  CA  . SER A 196 ? 0.1625 0.1877 0.1097 0.0285  -0.0357 -0.0054 197 SER A CA  
1560 C  C   . SER A 196 ? 0.1472 0.1593 0.1277 -0.0010 -0.0511 0.0023  197 SER A C   
1561 O  O   . SER A 196 ? 0.1608 0.1595 0.1136 -0.0168 -0.0351 0.0046  197 SER A O   
1562 C  CB  . SER A 196 ? 0.1629 0.1791 0.1544 0.0258  -0.0650 -0.0161 197 SER A CB  
1563 O  OG  . SER A 196 ? 0.1523 0.1652 0.1364 0.0051  -0.0516 0.0041  197 SER A OG  
1564 N  N   . LEU A 197 ? 0.1472 0.1644 0.1103 0.0057  -0.0333 -0.0159 198 LEU A N   
1565 C  CA  . LEU A 197 ? 0.1709 0.1667 0.0960 0.0064  -0.0247 -0.0082 198 LEU A CA  
1566 C  C   . LEU A 197 ? 0.1360 0.1665 0.1279 0.0036  -0.0214 -0.0117 198 LEU A C   
1567 O  O   . LEU A 197 ? 0.1623 0.2094 0.1313 -0.0013 -0.0506 0.0066  198 LEU A O   
1568 C  CB  . LEU A 197 ? 0.2083 0.1805 0.1181 -0.0031 -0.0287 0.0013  198 LEU A CB  
1569 C  CG  . LEU A 197 ? 0.2072 0.1753 0.1498 -0.0042 -0.0266 0.0236  198 LEU A CG  
1570 C  CD1 . LEU A 197 ? 0.2475 0.2216 0.1674 -0.0298 -0.0013 0.0450  198 LEU A CD1 
1571 C  CD2 . LEU A 197 ? 0.1949 0.2556 0.2141 -0.0070 -0.0468 0.0290  198 LEU A CD2 
1572 N  N   . THR A 198 ? 0.1864 0.1430 0.1148 -0.0091 -0.0341 -0.0088 199 THR A N   
1573 C  CA  . THR A 198 ? 0.1789 0.1575 0.1032 -0.0004 -0.0346 0.0044  199 THR A CA  
1574 C  C   . THR A 198 ? 0.1509 0.1681 0.1162 -0.0183 -0.0359 0.0050  199 THR A C   
1575 O  O   . THR A 198 ? 0.1627 0.1771 0.1552 -0.0073 -0.0373 -0.0040 199 THR A O   
1576 C  CB  . THR A 198 ? 0.2119 0.1421 0.0787 -0.0044 -0.0390 0.0058  199 THR A CB  
1577 O  OG1 . THR A 198 ? 0.1814 0.1753 0.0909 -0.0003 -0.0494 0.0152  199 THR A OG1 
1578 C  CG2 . THR A 198 ? 0.1939 0.1940 0.1029 0.0024  -0.0094 -0.0004 199 THR A CG2 
1579 N  N   . THR A 199 ? 0.1692 0.1921 0.1141 -0.0232 -0.0247 0.0160  200 THR A N   
1580 C  CA  . THR A 199 ? 0.2142 0.1670 0.0987 -0.0212 -0.0095 -0.0031 200 THR A CA  
1581 C  C   . THR A 199 ? 0.1713 0.1925 0.1401 -0.0100 -0.0243 0.0044  200 THR A C   
1582 O  O   . THR A 199 ? 0.1861 0.1875 0.1503 -0.0146 -0.0320 -0.0106 200 THR A O   
1583 C  CB  . THR A 199 ? 0.2213 0.2107 0.1146 0.0034  -0.0370 -0.0179 200 THR A CB  
1584 O  OG1 . THR A 199 ? 0.3106 0.2196 0.2079 0.0365  -0.1152 -0.0297 200 THR A OG1 
1585 C  CG2 . THR A 199 ? 0.2162 0.2223 0.1320 -0.0316 -0.0226 -0.0126 200 THR A CG2 
1586 N  N   . PRO A 200 ? 0.1573 0.2309 0.1403 -0.0212 -0.0218 -0.0106 201 PRO A N   
1587 C  CA  . PRO A 200 ? 0.1773 0.2205 0.1884 -0.0299 -0.0143 0.0229  201 PRO A CA  
1588 C  C   . PRO A 200 ? 0.1927 0.2203 0.1518 -0.0372 -0.0457 0.0005  201 PRO A C   
1589 O  O   . PRO A 200 ? 0.2237 0.2428 0.1609 -0.0104 -0.0613 -0.0069 201 PRO A O   
1590 C  CB  . PRO A 200 ? 0.1870 0.2326 0.1787 -0.0279 -0.0208 0.0094  201 PRO A CB  
1591 C  CG  . PRO A 200 ? 0.1669 0.2360 0.1993 -0.0079 -0.0267 -0.0194 201 PRO A CG  
1592 C  CD  . PRO A 200 ? 0.1709 0.2560 0.1412 -0.0133 -0.0080 -0.0247 201 PRO A CD  
1593 N  N   . PRO A 201 ? 0.1676 0.2099 0.2047 -0.0336 -0.0409 -0.0029 202 PRO A N   
1594 C  CA  . PRO A 201 ? 0.1867 0.2126 0.1735 -0.0511 -0.0212 0.0070  202 PRO A CA  
1595 C  C   . PRO A 201 ? 0.1773 0.2142 0.1825 -0.0175 -0.0337 0.0284  202 PRO A C   
1596 O  O   . PRO A 201 ? 0.1928 0.2101 0.2064 -0.0117 -0.0391 -0.0025 202 PRO A O   
1597 C  CB  . PRO A 201 ? 0.2315 0.2004 0.2734 -0.0348 -0.0394 0.0252  202 PRO A CB  
1598 C  CG  . PRO A 201 ? 0.2858 0.2096 0.2666 -0.0075 -0.0919 0.0334  202 PRO A CG  
1599 C  CD  . PRO A 201 ? 0.2711 0.1849 0.2103 -0.0161 -0.0421 0.0576  202 PRO A CD  
1600 N  N   . LEU A 202 ? 0.1820 0.1727 0.1546 -0.0167 -0.0068 0.0024  203 LEU A N   
1601 C  CA  . LEU A 202 ? 0.1598 0.2040 0.1212 0.0231  -0.0346 0.0038  203 LEU A CA  
1602 C  C   . LEU A 202 ? 0.1626 0.1673 0.1602 -0.0111 -0.0488 -0.0147 203 LEU A C   
1603 O  O   . LEU A 202 ? 0.1814 0.1843 0.1564 0.0036  -0.0423 -0.0097 203 LEU A O   
1604 C  CB  . LEU A 202 ? 0.1541 0.1764 0.1622 0.0159  -0.0646 -0.0210 203 LEU A CB  
1605 C  CG  . LEU A 202 ? 0.1562 0.1782 0.1832 0.0166  -0.0344 -0.0242 203 LEU A CG  
1606 C  CD1 . LEU A 202 ? 0.1637 0.2193 0.2530 0.0345  -0.0485 -0.0130 203 LEU A CD1 
1607 C  CD2 . LEU A 202 ? 0.1934 0.1911 0.2049 -0.0153 -0.0176 -0.0319 203 LEU A CD2 
1608 N  N   . ASN A 203 ? 0.1763 0.1720 0.1936 0.0121  -0.0197 -0.0242 204 ASN A N   
1609 C  CA  . ASN A 203 ? 0.1756 0.1720 0.1925 0.0106  -0.0237 -0.0159 204 ASN A CA  
1610 C  C   . ASN A 203 ? 0.1855 0.1773 0.1503 0.0115  -0.0289 -0.0332 204 ASN A C   
1611 O  O   . ASN A 203 ? 0.1875 0.1667 0.1566 -0.0069 -0.0574 -0.0032 204 ASN A O   
1612 C  CB  . ASN A 203 ? 0.1945 0.1922 0.2137 0.0250  -0.0312 0.0139  204 ASN A CB  
1613 C  CG  . ASN A 203 ? 0.2512 0.2155 0.2851 0.0326  0.0225  0.0091  204 ASN A CG  
1614 O  OD1 . ASN A 203 ? 0.2635 0.2311 0.3730 0.0140  0.0394  0.0367  204 ASN A OD1 
1615 N  ND2 . ASN A 203 ? 0.3534 0.2124 0.3384 0.0560  0.0599  0.0350  204 ASN A ND2 
1616 N  N   . GLU A 204 ? 0.1996 0.1681 0.1371 -0.0110 -0.0434 -0.0154 205 GLU A N   
1617 C  CA  . GLU A 204 ? 0.1902 0.1752 0.1268 0.0016  -0.0634 -0.0217 205 GLU A CA  
1618 C  C   . GLU A 204 ? 0.1958 0.1821 0.1663 0.0212  -0.0770 -0.0178 205 GLU A C   
1619 O  O   . GLU A 204 ? 0.2359 0.2448 0.1728 0.0340  -0.0724 -0.0482 205 GLU A O   
1620 C  CB  . GLU A 204 ? 0.2076 0.1938 0.1685 0.0044  -0.0998 -0.0332 205 GLU A CB  
1621 C  CG  . GLU A 204 ? 0.2315 0.2187 0.2140 0.0297  -0.0977 -0.0017 205 GLU A CG  
1622 C  CD  . GLU A 204 ? 0.2283 0.2237 0.1746 0.0109  -0.0744 -0.0200 205 GLU A CD  
1623 O  OE1 . GLU A 204 ? 0.2692 0.2692 0.2591 -0.0066 -0.1260 -0.0553 205 GLU A OE1 
1624 O  OE2 . GLU A 204 ? 0.2264 0.2201 0.1648 -0.0074 -0.0639 -0.0268 205 GLU A OE2 
1625 N  N   . CYS A 205 ? 0.1673 0.1527 0.1620 -0.0078 -0.0730 -0.0034 206 CYS A N   
1626 C  CA  . CYS A 205 ? 0.1828 0.1861 0.1282 0.0024  -0.0506 0.0034  206 CYS A CA  
1627 C  C   . CYS A 205 ? 0.1767 0.1641 0.1311 0.0089  -0.0460 -0.0141 206 CYS A C   
1628 O  O   . CYS A 205 ? 0.1967 0.1516 0.2064 0.0111  -0.0838 0.0067  206 CYS A O   
1629 C  CB  . CYS A 205 ? 0.2266 0.2374 0.1029 0.0048  -0.0532 0.0044  206 CYS A CB  
1630 S  SG  . CYS A 205 ? 0.2317 0.1934 0.1534 0.0031  -0.0586 -0.0063 206 CYS A SG  
1631 N  N   . VAL A 206 ? 0.1824 0.1500 0.1231 -0.0100 -0.0532 -0.0061 207 VAL A N   
1632 C  CA  . VAL A 206 ? 0.1582 0.1496 0.1309 0.0067  -0.0477 -0.0029 207 VAL A CA  
1633 C  C   . VAL A 206 ? 0.1667 0.1342 0.1171 0.0010  -0.0436 -0.0038 207 VAL A C   
1634 O  O   . VAL A 206 ? 0.1953 0.1846 0.1329 0.0021  -0.0488 0.0247  207 VAL A O   
1635 C  CB  . VAL A 206 ? 0.1717 0.1662 0.1295 0.0029  -0.0184 -0.0172 207 VAL A CB  
1636 C  CG1 . VAL A 206 ? 0.1809 0.1602 0.1414 -0.0027 -0.0822 -0.0278 207 VAL A CG1 
1637 C  CG2 . VAL A 206 ? 0.1868 0.1870 0.1396 0.0108  -0.0185 0.0003  207 VAL A CG2 
1638 N  N   . THR A 207 ? 0.1487 0.1713 0.1218 -0.0143 -0.0305 -0.0317 208 THR A N   
1639 C  CA  . THR A 207 ? 0.1620 0.1814 0.1116 -0.0040 -0.0337 -0.0359 208 THR A CA  
1640 C  C   . THR A 207 ? 0.1813 0.1539 0.0969 -0.0071 -0.0524 -0.0137 208 THR A C   
1641 O  O   . THR A 207 ? 0.2033 0.1465 0.1146 -0.0040 -0.0721 -0.0023 208 THR A O   
1642 C  CB  . THR A 207 ? 0.1827 0.1649 0.1453 0.0069  -0.0300 -0.0195 208 THR A CB  
1643 O  OG1 . THR A 207 ? 0.2208 0.1670 0.1619 0.0005  -0.0257 -0.0403 208 THR A OG1 
1644 C  CG2 . THR A 207 ? 0.1942 0.1947 0.1753 0.0018  -0.0115 0.0108  208 THR A CG2 
1645 N  N   . TRP A 208 ? 0.1601 0.1354 0.1227 -0.0005 -0.0316 -0.0099 209 TRP A N   
1646 C  CA  . TRP A 208 ? 0.1699 0.1368 0.0992 -0.0055 -0.0295 0.0054  209 TRP A CA  
1647 C  C   . TRP A 208 ? 0.1478 0.1597 0.0967 0.0103  -0.0260 -0.0124 209 TRP A C   
1648 O  O   . TRP A 208 ? 0.1692 0.1684 0.0996 -0.0026 -0.0128 -0.0089 209 TRP A O   
1649 C  CB  . TRP A 208 ? 0.1706 0.1460 0.0961 0.0132  -0.0330 0.0043  209 TRP A CB  
1650 C  CG  . TRP A 208 ? 0.1485 0.1469 0.0990 0.0110  -0.0441 0.0019  209 TRP A CG  
1651 C  CD1 . TRP A 208 ? 0.1399 0.1451 0.1164 0.0030  -0.0173 0.0294  209 TRP A CD1 
1652 C  CD2 . TRP A 208 ? 0.1698 0.1199 0.1127 0.0113  -0.0425 -0.0035 209 TRP A CD2 
1653 N  NE1 . TRP A 208 ? 0.1451 0.1733 0.1171 -0.0085 -0.0328 -0.0010 209 TRP A NE1 
1654 C  CE2 . TRP A 208 ? 0.1584 0.1429 0.1254 0.0104  -0.0573 0.0129  209 TRP A CE2 
1655 C  CE3 . TRP A 208 ? 0.1717 0.1356 0.0782 0.0114  -0.0414 -0.0065 209 TRP A CE3 
1656 C  CZ2 . TRP A 208 ? 0.1764 0.1555 0.1218 0.0313  -0.0420 0.0183  209 TRP A CZ2 
1657 C  CZ3 . TRP A 208 ? 0.1967 0.1525 0.0848 0.0201  -0.0140 -0.0071 209 TRP A CZ3 
1658 C  CH2 . TRP A 208 ? 0.1904 0.1618 0.1186 0.0190  -0.0128 -0.0085 209 TRP A CH2 
1659 N  N   . ILE A 209 ? 0.1690 0.1468 0.1094 -0.0044 -0.0583 0.0032  210 ILE A N   
1660 C  CA  . ILE A 209 ? 0.1634 0.1412 0.1306 0.0000  -0.0500 -0.0254 210 ILE A CA  
1661 C  C   . ILE A 209 ? 0.1627 0.1406 0.0944 0.0047  -0.0324 -0.0190 210 ILE A C   
1662 O  O   . ILE A 209 ? 0.2083 0.1615 0.0881 0.0022  -0.0320 -0.0042 210 ILE A O   
1663 C  CB  . ILE A 209 ? 0.1609 0.1612 0.1616 0.0128  -0.0269 -0.0027 210 ILE A CB  
1664 C  CG1 . ILE A 209 ? 0.2008 0.1453 0.2526 0.0364  -0.0464 -0.0318 210 ILE A CG1 
1665 C  CG2 . ILE A 209 ? 0.1699 0.2078 0.1717 -0.0116 -0.0497 0.0145  210 ILE A CG2 
1666 C  CD1 . ILE A 209 ? 0.2233 0.1746 0.2547 0.0462  -0.0635 -0.0160 210 ILE A CD1 
1667 N  N   . VAL A 210 ? 0.1692 0.1383 0.1123 0.0046  -0.0353 -0.0051 211 VAL A N   
1668 C  CA  . VAL A 210 ? 0.1697 0.1458 0.1159 -0.0020 -0.0227 0.0003  211 VAL A CA  
1669 C  C   . VAL A 210 ? 0.1730 0.1526 0.0863 -0.0047 -0.0222 0.0053  211 VAL A C   
1670 O  O   . VAL A 210 ? 0.1947 0.1661 0.0938 -0.0148 -0.0160 0.0013  211 VAL A O   
1671 C  CB  . VAL A 210 ? 0.1641 0.1572 0.0929 0.0092  -0.0227 0.0018  211 VAL A CB  
1672 C  CG1 . VAL A 210 ? 0.2026 0.1446 0.1361 -0.0048 -0.0249 -0.0212 211 VAL A CG1 
1673 C  CG2 . VAL A 210 ? 0.1727 0.1780 0.1640 -0.0146 -0.0397 0.0077  211 VAL A CG2 
1674 N  N   . LEU A 211 ? 0.1744 0.1665 0.1374 -0.0074 -0.0593 -0.0068 212 LEU A N   
1675 C  CA  . LEU A 211 ? 0.2069 0.1897 0.0952 -0.0225 -0.0381 -0.0073 212 LEU A CA  
1676 C  C   . LEU A 211 ? 0.1751 0.1963 0.1331 0.0027  -0.0358 -0.0026 212 LEU A C   
1677 O  O   . LEU A 211 ? 0.1817 0.2064 0.1111 -0.0157 -0.0442 -0.0058 212 LEU A O   
1678 C  CB  . LEU A 211 ? 0.1952 0.1841 0.1189 0.0121  -0.0494 -0.0025 212 LEU A CB  
1679 C  CG  . LEU A 211 ? 0.1828 0.2042 0.1299 0.0069  -0.0516 0.0037  212 LEU A CG  
1680 C  CD1 . LEU A 211 ? 0.2150 0.2667 0.1343 0.0039  -0.0710 -0.0055 212 LEU A CD1 
1681 C  CD2 . LEU A 211 ? 0.1932 0.2126 0.1575 0.0048  -0.0238 -0.0034 212 LEU A CD2 
1682 N  N   . LYS A 212 ? 0.1868 0.1989 0.1229 -0.0156 -0.0243 0.0138  213 LYS A N   
1683 C  CA  . LYS A 212 ? 0.2407 0.1928 0.1253 -0.0234 -0.0402 0.0030  213 LYS A CA  
1684 C  C   . LYS A 212 ? 0.2058 0.1706 0.1399 -0.0100 -0.0359 0.0122  213 LYS A C   
1685 O  O   . LYS A 212 ? 0.2347 0.1899 0.1982 -0.0102 -0.0574 0.0152  213 LYS A O   
1686 C  CB  . LYS A 212 ? 0.3741 0.2639 0.0789 -0.0780 -0.0175 -0.0219 213 LYS A CB  
1687 C  CG  . LYS A 212 ? 0.5762 0.3116 0.2347 -0.1518 -0.0767 -0.0006 213 LYS A CG  
1688 C  CD  . LYS A 212 ? 0.7932 0.6308 0.2811 -0.3154 0.1302  -0.0693 213 LYS A CD  
1689 N  N   . GLU A 213 ? 0.1878 0.2029 0.1130 -0.0190 -0.0403 0.0012  214 GLU A N   
1690 C  CA  . GLU A 213 ? 0.1939 0.1857 0.1328 -0.0161 -0.0392 0.0019  214 GLU A CA  
1691 C  C   . GLU A 213 ? 0.1679 0.1719 0.1408 0.0001  -0.0511 0.0040  214 GLU A C   
1692 O  O   . GLU A 213 ? 0.1882 0.1741 0.1609 0.0110  -0.0344 0.0167  214 GLU A O   
1693 C  CB  . GLU A 213 ? 0.1814 0.2409 0.1806 -0.0217 -0.0165 -0.0117 214 GLU A CB  
1694 C  CG  . GLU A 213 ? 0.2606 0.2299 0.2661 -0.0436 -0.0612 -0.0302 214 GLU A CG  
1695 C  CD  . GLU A 213 ? 0.2315 0.3155 0.4937 -0.0697 0.0142  -0.0804 214 GLU A CD  
1696 O  OE1 . GLU A 213 ? 0.2040 0.2927 0.3177 -0.0132 -0.0372 -0.0003 214 GLU A OE1 
1697 O  OE2 . GLU A 213 ? 0.3933 0.8170 0.5335 -0.1565 -0.1619 -0.0933 214 GLU A OE2 
1698 N  N   A PRO A 214 ? 0.1812 0.1541 0.1118 0.0093  -0.0495 0.0140  215 PRO A N   
1699 N  N   B PRO A 214 ? 0.1753 0.1594 0.1185 -0.0094 -0.0406 -0.0034 215 PRO A N   
1700 C  CA  A PRO A 214 ? 0.1852 0.1537 0.1186 0.0114  -0.0309 -0.0100 215 PRO A CA  
1701 C  CA  B PRO A 214 ? 0.2008 0.1771 0.1058 0.0060  -0.0399 -0.0050 215 PRO A CA  
1702 C  C   A PRO A 214 ? 0.1899 0.1724 0.1279 -0.0055 -0.0361 -0.0103 215 PRO A C   
1703 C  C   B PRO A 214 ? 0.2076 0.2161 0.1155 -0.0187 -0.0447 -0.0091 215 PRO A C   
1704 O  O   A PRO A 214 ? 0.1828 0.2099 0.1748 0.0000  -0.0535 -0.0283 215 PRO A O   
1705 O  O   B PRO A 214 ? 0.2390 0.1796 0.1218 -0.0297 -0.0273 0.0186  215 PRO A O   
1706 C  CB  A PRO A 214 ? 0.2094 0.1318 0.1863 -0.0092 -0.0553 -0.0143 215 PRO A CB  
1707 C  CB  B PRO A 214 ? 0.2358 0.1789 0.1613 0.0085  -0.0458 0.0011  215 PRO A CB  
1708 C  CG  A PRO A 214 ? 0.2301 0.1710 0.1339 0.0154  -0.0409 0.0019  215 PRO A CG  
1709 C  CG  B PRO A 214 ? 0.2249 0.2516 0.1759 0.0006  -0.0460 0.0367  215 PRO A CG  
1710 C  CD  A PRO A 214 ? 0.2468 0.1335 0.1376 0.0128  -0.0388 -0.0004 215 PRO A CD  
1711 C  CD  B PRO A 214 ? 0.1990 0.1458 0.2071 -0.0113 -0.0646 0.0068  215 PRO A CD  
1712 N  N   . ILE A 215 ? 0.2085 0.1778 0.1137 -0.0020 -0.0561 -0.0015 216 ILE A N   
1713 C  CA  . ILE A 215 ? 0.2264 0.1796 0.0983 0.0006  -0.0602 -0.0053 216 ILE A CA  
1714 C  C   . ILE A 215 ? 0.2021 0.1896 0.1278 0.0016  -0.0384 0.0006  216 ILE A C   
1715 O  O   . ILE A 215 ? 0.2010 0.1752 0.1875 0.0049  -0.0507 -0.0314 216 ILE A O   
1716 C  CB  . ILE A 215 ? 0.2331 0.1647 0.1685 -0.0044 -0.0310 0.0060  216 ILE A CB  
1717 C  CG1 . ILE A 215 ? 0.2166 0.1954 0.1164 -0.0059 -0.0541 0.0137  216 ILE A CG1 
1718 C  CG2 . ILE A 215 ? 0.2148 0.1656 0.2151 0.0083  -0.0624 -0.0293 216 ILE A CG2 
1719 C  CD1 . ILE A 215 ? 0.2481 0.2085 0.1572 0.0070  -0.0417 0.0387  216 ILE A CD1 
1720 N  N   . SER A 216 ? 0.2198 0.1904 0.1601 -0.0245 -0.0568 0.0032  217 SER A N   
1721 C  CA  A SER A 216 ? 0.2632 0.1738 0.1580 -0.0229 -0.0803 -0.0051 217 SER A CA  
1722 C  CA  B SER A 216 ? 0.2394 0.2178 0.1449 0.0055  -0.0744 -0.0096 217 SER A CA  
1723 C  C   . SER A 216 ? 0.2283 0.1478 0.1483 -0.0134 -0.0653 -0.0151 217 SER A C   
1724 O  O   . SER A 216 ? 0.2320 0.2008 0.1554 0.0130  -0.0687 -0.0009 217 SER A O   
1725 C  CB  A SER A 216 ? 0.3327 0.1458 0.1749 -0.0423 -0.0482 -0.0187 217 SER A CB  
1726 C  CB  B SER A 216 ? 0.3586 0.1976 0.1433 -0.0594 0.0162  -0.0134 217 SER A CB  
1727 O  OG  A SER A 216 ? 0.2621 0.2689 0.1709 -0.0367 -0.0674 0.0092  217 SER A OG  
1728 O  OG  B SER A 216 ? 0.3741 0.2352 0.1936 0.0000  -0.0294 -0.0312 217 SER A OG  
1729 N  N   . VAL A 217 ? 0.2255 0.1485 0.1271 -0.0121 -0.0513 -0.0196 218 VAL A N   
1730 C  CA  . VAL A 217 ? 0.2148 0.1419 0.1317 -0.0071 -0.0665 0.0015  218 VAL A CA  
1731 C  C   . VAL A 217 ? 0.2410 0.1406 0.1381 -0.0054 -0.0675 -0.0079 218 VAL A C   
1732 O  O   . VAL A 217 ? 0.2446 0.1597 0.1482 0.0142  -0.0721 -0.0130 218 VAL A O   
1733 C  CB  . VAL A 217 ? 0.2046 0.1461 0.2409 -0.0182 -0.0823 -0.0020 218 VAL A CB  
1734 C  CG1 . VAL A 217 ? 0.2502 0.1717 0.1782 -0.0078 -0.0794 -0.0143 218 VAL A CG1 
1735 C  CG2 . VAL A 217 ? 0.2087 0.1842 0.2313 -0.0005 -0.0759 -0.0074 218 VAL A CG2 
1736 N  N   . SER A 218 ? 0.2329 0.1555 0.1278 -0.0135 -0.0570 -0.0126 219 SER A N   
1737 C  CA  . SER A 218 ? 0.2355 0.1544 0.1807 -0.0086 -0.0672 -0.0342 219 SER A CA  
1738 C  C   . SER A 218 ? 0.2373 0.1435 0.1654 0.0022  -0.0570 0.0075  219 SER A C   
1739 O  O   . SER A 218 ? 0.2678 0.1498 0.1503 -0.0114 -0.0668 0.0139  219 SER A O   
1740 C  CB  . SER A 218 ? 0.2460 0.2255 0.1351 -0.0351 -0.0516 -0.0124 219 SER A CB  
1741 O  OG  . SER A 218 ? 0.2369 0.2119 0.1888 -0.0321 -0.0670 -0.0062 219 SER A OG  
1742 N  N   A SER A 219 ? 0.2696 0.1663 0.1649 0.0292  -0.0653 -0.0119 220 SER A N   
1743 N  N   B SER A 219 ? 0.2716 0.1575 0.1875 0.0116  -0.0649 -0.0195 220 SER A N   
1744 C  CA  A SER A 219 ? 0.2457 0.1662 0.2044 0.0032  -0.0668 -0.0129 220 SER A CA  
1745 C  CA  B SER A 219 ? 0.2566 0.1634 0.2154 -0.0121 -0.0526 -0.0067 220 SER A CA  
1746 C  C   A SER A 219 ? 0.2434 0.1647 0.2266 0.0223  -0.0714 0.0041  220 SER A C   
1747 C  C   B SER A 219 ? 0.2216 0.1791 0.2489 0.0276  -0.0616 0.0362  220 SER A C   
1748 O  O   A SER A 219 ? 0.2788 0.2086 0.2597 -0.0099 -0.0010 0.0001  220 SER A O   
1749 O  O   B SER A 219 ? 0.2337 0.1644 0.2374 0.0027  -0.0574 -0.0324 220 SER A O   
1750 C  CB  A SER A 219 ? 0.2366 0.1771 0.2696 0.0280  -0.0595 -0.0065 220 SER A CB  
1751 C  CB  B SER A 219 ? 0.3152 0.1702 0.2852 -0.0089 -0.0322 0.0023  220 SER A CB  
1752 O  OG  A SER A 219 ? 0.2660 0.1439 0.2274 -0.0055 -0.0332 -0.0048 220 SER A OG  
1753 O  OG  B SER A 219 ? 0.3501 0.2424 0.4307 0.0108  0.0059  -0.0059 220 SER A OG  
1754 N  N   . GLU A 220 ? 0.2463 0.1595 0.2040 0.0110  -0.0523 0.0038  221 GLU A N   
1755 C  CA  . GLU A 220 ? 0.2980 0.1816 0.1946 -0.0146 -0.0616 0.0102  221 GLU A CA  
1756 C  C   . GLU A 220 ? 0.2727 0.1922 0.1229 -0.0162 -0.0447 -0.0065 221 GLU A C   
1757 O  O   . GLU A 220 ? 0.2737 0.2214 0.1895 -0.0038 -0.0115 0.0029  221 GLU A O   
1758 C  CB  . GLU A 220 ? 0.2898 0.2441 0.1690 -0.0310 -0.0622 -0.0497 221 GLU A CB  
1759 C  CG  . GLU A 220 ? 0.3753 0.2523 0.3286 -0.0485 -0.0842 -0.0627 221 GLU A CG  
1760 C  CD  . GLU A 220 ? 0.4603 0.3283 0.3502 -0.1208 -0.0040 -0.1262 221 GLU A CD  
1761 O  OE1 . GLU A 220 ? 0.3307 0.2810 0.3421 -0.0832 -0.0200 -0.0853 221 GLU A OE1 
1762 O  OE2 . GLU A 220 ? 0.8627 0.3635 0.4510 -0.2646 0.0025  -0.1483 221 GLU A OE2 
1763 N  N   . GLN A 221 ? 0.2746 0.1659 0.1523 -0.0085 -0.0588 -0.0111 222 GLN A N   
1764 C  CA  . GLN A 221 ? 0.2407 0.1529 0.1698 -0.0083 -0.0467 0.0184  222 GLN A CA  
1765 C  C   . GLN A 221 ? 0.2587 0.1633 0.2044 -0.0119 -0.0853 0.0124  222 GLN A C   
1766 O  O   . GLN A 221 ? 0.2481 0.1972 0.1622 -0.0104 -0.0511 0.0073  222 GLN A O   
1767 C  CB  . GLN A 221 ? 0.2108 0.1900 0.1643 -0.0128 -0.0679 -0.0035 222 GLN A CB  
1768 C  CG  . GLN A 221 ? 0.2140 0.1889 0.1435 -0.0249 -0.0765 -0.0133 222 GLN A CG  
1769 C  CD  . GLN A 221 ? 0.2164 0.1408 0.1425 -0.0297 -0.0723 0.0018  222 GLN A CD  
1770 O  OE1 . GLN A 221 ? 0.2319 0.1645 0.1375 -0.0069 -0.0731 -0.0005 222 GLN A OE1 
1771 N  NE2 . GLN A 221 ? 0.2496 0.1616 0.1509 0.0051  -0.0871 -0.0068 222 GLN A NE2 
1772 N  N   . VAL A 222 ? 0.2317 0.1861 0.1949 -0.0026 -0.0671 0.0282  223 VAL A N   
1773 C  CA  . VAL A 222 ? 0.2268 0.2166 0.1979 -0.0021 -0.0606 0.0162  223 VAL A CA  
1774 C  C   . VAL A 222 ? 0.2259 0.2305 0.2037 -0.0115 -0.0525 0.0355  223 VAL A C   
1775 O  O   . VAL A 222 ? 0.2310 0.2421 0.1777 -0.0187 -0.0469 0.0233  223 VAL A O   
1776 C  CB  . VAL A 222 ? 0.2891 0.3240 0.2753 -0.0252 -0.1656 0.1022  223 VAL A CB  
1777 C  CG1 . VAL A 222 ? 0.4322 0.3551 0.3321 -0.0187 -0.0324 0.0817  223 VAL A CG1 
1778 C  CG2 . VAL A 222 ? 0.3128 0.3531 0.2379 -0.0644 -0.1280 0.0631  223 VAL A CG2 
1779 N  N   . LEU A 223 ? 0.2646 0.2212 0.2080 0.0043  -0.0284 0.0097  224 LEU A N   
1780 C  CA  . LEU A 223 ? 0.2736 0.2374 0.2803 -0.0190 0.0027  0.0006  224 LEU A CA  
1781 C  C   . LEU A 223 ? 0.2322 0.2582 0.2071 -0.0200 -0.0660 -0.0055 224 LEU A C   
1782 O  O   . LEU A 223 ? 0.2236 0.2741 0.2434 -0.0041 -0.0370 -0.0168 224 LEU A O   
1783 C  CB  . LEU A 223 ? 0.3471 0.2329 0.3626 -0.0038 -0.0367 -0.0386 224 LEU A CB  
1784 C  CG  . LEU A 223 ? 0.4056 0.3181 0.3140 0.0223  0.0946  -0.0055 224 LEU A CG  
1785 C  CD2 . LEU A 223 ? 0.4373 0.3010 0.5686 0.0838  0.0653  -0.0829 224 LEU A CD2 
1786 N  N   . LYS A 224 ? 0.2446 0.2448 0.1609 -0.0076 -0.0591 -0.0027 225 LYS A N   
1787 C  CA  . LYS A 224 ? 0.2338 0.2852 0.1910 -0.0291 -0.0451 0.0328  225 LYS A CA  
1788 C  C   . LYS A 224 ? 0.2528 0.2551 0.1101 -0.0015 -0.0116 0.0207  225 LYS A C   
1789 O  O   . LYS A 224 ? 0.2653 0.2802 0.1143 0.0013  -0.0417 0.0093  225 LYS A O   
1790 C  CB  . LYS A 224 ? 0.2532 0.3590 0.2065 0.0134  -0.0624 0.0021  225 LYS A CB  
1791 C  CG  . LYS A 224 ? 0.3078 0.4330 0.2952 -0.0700 -0.1156 0.0419  225 LYS A CG  
1792 C  CD  . LYS A 224 ? 0.3371 0.6091 0.4139 -0.0648 -0.1850 -0.0516 225 LYS A CD  
1793 C  CE  . LYS A 224 ? 0.5524 0.6898 0.4690 -0.0731 -0.1667 -0.1208 225 LYS A CE  
1794 N  NZ  . LYS A 224 ? 0.8009 0.3730 0.5003 -0.1386 0.1851  -0.1254 225 LYS A NZ  
1795 N  N   . PHE A 225 ? 0.2488 0.1967 0.1159 0.0022  -0.0124 0.0119  226 PHE A N   
1796 C  CA  . PHE A 225 ? 0.2259 0.1746 0.1089 -0.0002 -0.0017 -0.0141 226 PHE A CA  
1797 C  C   . PHE A 225 ? 0.2440 0.2305 0.0690 0.0037  -0.0176 -0.0129 226 PHE A C   
1798 O  O   . PHE A 225 ? 0.2374 0.2352 0.1442 -0.0058 -0.0190 0.0044  226 PHE A O   
1799 C  CB  . PHE A 225 ? 0.2341 0.2373 0.1115 -0.0070 -0.0044 -0.0118 226 PHE A CB  
1800 C  CG  . PHE A 225 ? 0.2413 0.2324 0.1372 0.0086  -0.0113 -0.0023 226 PHE A CG  
1801 C  CD1 . PHE A 225 ? 0.2552 0.2858 0.1752 0.0245  -0.0060 0.0284  226 PHE A CD1 
1802 C  CD2 . PHE A 225 ? 0.2559 0.2940 0.1342 0.0059  -0.0022 -0.0465 226 PHE A CD2 
1803 C  CE1 . PHE A 225 ? 0.2523 0.3055 0.1573 0.0346  -0.0211 0.0168  226 PHE A CE1 
1804 C  CE2 . PHE A 225 ? 0.2298 0.3285 0.2302 0.0292  -0.0251 -0.0514 226 PHE A CE2 
1805 C  CZ  . PHE A 225 ? 0.2416 0.2547 0.1911 0.0055  -0.0392 -0.0731 226 PHE A CZ  
1806 N  N   . ARG A 226 ? 0.2460 0.2182 0.1236 0.0216  -0.0128 -0.0049 227 ARG A N   
1807 C  CA  . ARG A 226 ? 0.2288 0.2500 0.1429 0.0111  0.0027  0.0362  227 ARG A CA  
1808 C  C   . ARG A 226 ? 0.2347 0.2164 0.1627 0.0017  0.0108  0.0354  227 ARG A C   
1809 O  O   . ARG A 226 ? 0.2528 0.3183 0.1633 0.0328  0.0111  -0.0009 227 ARG A O   
1810 C  CB  . ARG A 226 ? 0.2759 0.2026 0.1257 0.0321  -0.0215 0.0128  227 ARG A CB  
1811 C  CG  . ARG A 226 ? 0.2557 0.1873 0.1358 0.0053  -0.0054 0.0003  227 ARG A CG  
1812 C  CD  . ARG A 226 ? 0.3479 0.1902 0.1390 0.0479  0.0001  -0.0017 227 ARG A CD  
1813 N  NE  . ARG A 226 ? 0.2836 0.2193 0.1216 -0.0105 -0.0412 0.0053  227 ARG A NE  
1814 C  CZ  . ARG A 226 ? 0.2790 0.1981 0.1615 -0.0190 -0.0458 -0.0179 227 ARG A CZ  
1815 N  NH1 . ARG A 226 ? 0.3112 0.2961 0.2867 -0.0648 -0.0483 -0.1201 227 ARG A NH1 
1816 N  NH2 . ARG A 226 ? 0.3161 0.2051 0.2122 -0.0406 0.0000  -0.0416 227 ARG A NH2 
1817 N  N   . LYS A 227 ? 0.2827 0.2629 0.1139 0.0110  0.0016  -0.0154 228 LYS A N   
1818 C  CA  . LYS A 227 ? 0.2638 0.3040 0.1211 -0.0234 0.0079  -0.0574 228 LYS A CA  
1819 C  C   . LYS A 227 ? 0.2710 0.3181 0.0765 -0.0077 -0.0131 -0.0446 228 LYS A C   
1820 O  O   . LYS A 227 ? 0.3101 0.3236 0.1115 -0.0155 0.0188  -0.0388 228 LYS A O   
1821 C  CB  . LYS A 227 ? 0.3052 0.3626 0.1279 -0.0086 -0.0307 -0.0248 228 LYS A CB  
1822 C  CG  . LYS A 227 ? 0.3609 0.4142 0.2742 -0.0875 -0.0258 -0.0186 228 LYS A CG  
1823 C  CD  . LYS A 227 ? 0.5405 0.6715 0.4610 -0.0449 -0.1788 -0.1606 228 LYS A CD  
1824 N  N   . LEU A 228 ? 0.2642 0.2697 0.0886 -0.0357 -0.0097 -0.0273 229 LEU A N   
1825 C  CA  . LEU A 228 ? 0.2731 0.2678 0.0961 0.0034  -0.0215 0.0084  229 LEU A CA  
1826 C  C   . LEU A 228 ? 0.2788 0.2661 0.1277 0.0352  0.0227  -0.0200 229 LEU A C   
1827 O  O   . LEU A 228 ? 0.2887 0.2588 0.1404 -0.0012 -0.0283 -0.0159 229 LEU A O   
1828 C  CB  . LEU A 228 ? 0.2470 0.2556 0.1430 0.0170  -0.0044 -0.0111 229 LEU A CB  
1829 C  CG  . LEU A 228 ? 0.2262 0.3044 0.0939 -0.0023 -0.0174 0.0093  229 LEU A CG  
1830 C  CD1 . LEU A 228 ? 0.2094 0.3116 0.0963 0.0110  -0.0167 -0.0026 229 LEU A CD1 
1831 C  CD2 . LEU A 228 ? 0.3134 0.3316 0.1182 -0.0004 -0.0064 0.0376  229 LEU A CD2 
1832 N  N   . ASN A 229 ? 0.2576 0.3169 0.1320 -0.0086 -0.0136 0.0407  230 ASN A N   
1833 C  CA  . ASN A 229 ? 0.2526 0.3410 0.1071 -0.0345 -0.0216 -0.0080 230 ASN A CA  
1834 C  C   . ASN A 229 ? 0.2852 0.3149 0.1491 -0.0099 0.0042  -0.0065 230 ASN A C   
1835 O  O   . ASN A 229 ? 0.2898 0.2948 0.1206 0.0054  0.0002  -0.0064 230 ASN A O   
1836 C  CB  . ASN A 229 ? 0.3030 0.3385 0.1145 0.0029  0.0092  -0.0029 230 ASN A CB  
1837 C  CG  . ASN A 229 ? 0.3903 0.3831 0.1800 -0.0381 -0.0176 -0.0507 230 ASN A CG  
1838 O  OD1 . ASN A 229 ? 0.5548 0.5657 0.2176 0.0212  0.0650  -0.0795 230 ASN A OD1 
1839 N  ND2 . ASN A 229 ? 0.4862 0.4084 0.2098 -0.0526 0.0488  -0.1068 230 ASN A ND2 
1840 N  N   . PHE A 230 ? 0.2353 0.3375 0.1293 -0.0642 0.0060  -0.0038 231 PHE A N   
1841 C  CA  . PHE A 230 ? 0.2478 0.2976 0.1342 -0.0392 -0.0143 0.0015  231 PHE A CA  
1842 C  C   . PHE A 230 ? 0.2385 0.3941 0.1418 -0.0450 -0.0025 -0.0062 231 PHE A C   
1843 O  O   . PHE A 230 ? 0.3651 0.3617 0.1469 -0.1105 0.0072  0.0075  231 PHE A O   
1844 C  CB  . PHE A 230 ? 0.2555 0.3446 0.1372 0.0000  -0.0277 -0.0067 231 PHE A CB  
1845 C  CG  . PHE A 230 ? 0.2509 0.3188 0.1309 -0.0165 -0.0181 -0.0358 231 PHE A CG  
1846 C  CD1 . PHE A 230 ? 0.3040 0.2900 0.1350 -0.0178 -0.0073 -0.0528 231 PHE A CD1 
1847 C  CD2 . PHE A 230 ? 0.2596 0.3206 0.1893 -0.0194 0.0279  -0.0375 231 PHE A CD2 
1848 C  CE1 . PHE A 230 ? 0.3137 0.2768 0.1286 -0.0610 -0.0463 -0.0341 231 PHE A CE1 
1849 C  CE2 . PHE A 230 ? 0.2886 0.3441 0.1454 -0.0220 0.0063  -0.0292 231 PHE A CE2 
1850 C  CZ  . PHE A 230 ? 0.2349 0.2983 0.2024 -0.0091 -0.0361 -0.0494 231 PHE A CZ  
1851 N  N   . ASN A 231 ? 0.2915 0.4158 0.1191 -0.0619 0.0204  -0.0296 232 ASN A N   
1852 C  CA  . ASN A 231 ? 0.3749 0.3760 0.1791 -0.0806 0.0425  0.0155  232 ASN A CA  
1853 C  C   . ASN A 231 ? 0.3556 0.3554 0.2744 -0.0763 0.0453  -0.0020 232 ASN A C   
1854 O  O   . ASN A 231 ? 0.3799 0.3628 0.1331 -0.0508 0.0239  -0.0025 232 ASN A O   
1855 C  CB  . ASN A 231 ? 0.2964 0.5028 0.2374 -0.0618 0.0450  -0.0666 232 ASN A CB  
1856 C  CG  . ASN A 231 ? 0.2731 0.5233 0.1455 -0.0686 -0.0150 0.0196  232 ASN A CG  
1857 O  OD1 . ASN A 231 ? 0.3448 0.4036 0.2169 -0.0642 0.0310  -0.0766 232 ASN A OD1 
1858 N  ND2 . ASN A 231 ? 0.4589 0.5740 0.1489 0.0497  -0.0280 0.0377  232 ASN A ND2 
1859 N  N   . GLY A 232 ? 0.3520 0.4826 0.1537 -0.1297 0.0337  0.0297  233 GLY A N   
1860 C  CA  . GLY A 232 ? 0.5068 0.4103 0.1670 -0.1427 -0.0295 -0.0250 233 GLY A CA  
1861 C  C   . GLY A 232 ? 0.5092 0.4402 0.1641 -0.1086 0.0822  -0.0237 233 GLY A C   
1862 O  O   . GLY A 232 ? 0.5407 0.4837 0.2166 -0.1574 0.0580  -0.0641 233 GLY A O   
1863 N  N   . GLU A 233 ? 0.5570 0.5978 0.1899 -0.1812 0.0095  -0.0142 234 GLU A N   
1864 C  CA  . GLU A 233 ? 0.6118 0.6761 0.3070 -0.0577 0.1091  -0.1878 234 GLU A CA  
1865 C  C   . GLU A 233 ? 0.5565 0.7170 0.3560 -0.0759 -0.0206 -0.0008 234 GLU A C   
1866 O  O   . GLU A 233 ? 0.7130 0.5871 0.3315 -0.1371 0.1287  -0.0184 234 GLU A O   
1867 C  CB  . GLU A 233 ? 0.6529 1.0688 0.6998 -0.1443 0.1675  0.3432  234 GLU A CB  
1868 C  CG  . GLU A 233 ? 1.0089 1.3275 0.4895 0.0002  0.1337  0.0234  234 GLU A CG  
1869 C  CD  . GLU A 233 ? 0.3781 1.6014 0.8097 -0.1567 0.1314  0.0791  234 GLU A CD  
1870 O  OE1 . GLU A 233 ? 0.4062 1.6398 0.5225 -0.0247 0.3077  0.1583  234 GLU A OE1 
1871 O  OE2 . GLU A 233 ? 0.6460 0.6484 1.2965 -0.2512 -0.0258 -0.0148 234 GLU A OE2 
1872 N  N   . GLY A 234 ? 0.5662 0.7428 0.2748 -0.0563 0.0718  0.0344  235 GLY A N   
1873 C  CA  . GLY A 234 ? 0.4546 0.8550 0.8574 -0.0091 0.0803  0.0604  235 GLY A CA  
1874 C  C   . GLY A 234 ? 0.6003 0.8127 0.5124 -0.0171 -0.0922 -0.1547 235 GLY A C   
1875 O  O   . GLY A 234 ? 0.8144 0.9214 0.2805 0.0863  0.0744  -0.0055 235 GLY A O   
1876 N  N   . GLU A 235 ? 0.7123 0.8638 0.4839 -0.1801 0.1698  -0.1990 236 GLU A N   
1877 C  CA  . GLU A 235 ? 0.7054 0.7310 0.4944 -0.1150 0.1611  -0.1904 236 GLU A CA  
1878 C  C   . GLU A 235 ? 0.8768 0.8054 0.5881 -0.0116 0.0609  -0.0746 236 GLU A C   
1879 O  O   . GLU A 235 ? 0.7869 1.0354 0.6257 -0.0266 0.2103  -0.0721 236 GLU A O   
1880 C  CB  . GLU A 235 ? 0.5139 0.7789 0.5225 -0.1989 0.0756  -0.2213 236 GLU A CB  
1881 C  CG  . GLU A 235 ? 0.4420 0.7900 0.3171 -0.2074 0.0650  -0.1206 236 GLU A CG  
1882 C  CD  . GLU A 235 ? 0.7660 0.8610 0.3512 -0.3468 -0.0187 -0.1715 236 GLU A CD  
1883 O  OE1 . GLU A 235 ? 0.6979 0.7426 0.5586 -0.2963 0.1384  -0.0253 236 GLU A OE1 
1884 O  OE2 . GLU A 235 ? 0.8822 0.8999 0.8065 -0.2791 0.0604  0.1456  236 GLU A OE2 
1885 N  N   . PRO A 236 ? 0.7156 0.7287 0.6021 -0.1620 0.0593  -0.0875 237 PRO A N   
1886 C  CA  . PRO A 236 ? 0.4764 0.7589 0.5324 -0.2081 0.2102  -0.1349 237 PRO A CA  
1887 C  C   . PRO A 236 ? 0.3231 0.5108 0.3503 -0.0626 0.0623  -0.1617 237 PRO A C   
1888 O  O   . PRO A 236 ? 0.4542 0.5529 0.2984 -0.0652 0.0941  -0.1746 237 PRO A O   
1889 C  CB  . PRO A 236 ? 0.5501 0.8763 0.6419 -0.1482 0.1122  -0.1961 237 PRO A CB  
1890 C  CG  . PRO A 236 ? 0.3825 0.8616 0.6405 -0.0369 0.0648  -0.0632 237 PRO A CG  
1891 C  CD  . PRO A 236 ? 0.6835 0.6351 0.6829 -0.1321 0.1435  -0.1518 237 PRO A CD  
1892 N  N   . GLU A 237 ? 0.4062 0.5945 0.2836 -0.1582 0.0727  -0.1754 238 GLU A N   
1893 C  CA  . GLU A 237 ? 0.3803 0.5439 0.2558 -0.1245 0.0396  -0.0978 238 GLU A CA  
1894 C  C   . GLU A 237 ? 0.2534 0.4714 0.2488 -0.0175 0.0384  -0.1316 238 GLU A C   
1895 O  O   . GLU A 237 ? 0.4726 0.4334 0.2767 0.0129  0.0732  -0.1301 238 GLU A O   
1896 C  CB  . GLU A 237 ? 0.6427 0.3455 0.3094 0.0010  -0.1935 -0.0682 238 GLU A CB  
1897 C  CG  . GLU A 237 ? 0.7937 0.8223 0.3633 -0.0816 -0.0392 -0.1133 238 GLU A CG  
1898 C  CD  . GLU A 237 ? 0.6848 0.7981 0.8975 -0.1608 0.0066  -0.2196 238 GLU A CD  
1899 O  OE1 . GLU A 237 ? 0.7928 0.7704 0.4323 -0.1693 0.2084  -0.0445 238 GLU A OE1 
1900 O  OE2 . GLU A 237 ? 0.4981 0.9022 1.0117 -0.0972 -0.2344 0.0000  238 GLU A OE2 
1901 N  N   . GLU A 238 ? 0.3768 0.4084 0.2089 -0.0872 0.1386  -0.1024 239 GLU A N   
1902 C  CA  . GLU A 238 ? 0.3169 0.3558 0.2362 -0.0727 0.0850  -0.0399 239 GLU A CA  
1903 C  C   . GLU A 238 ? 0.2878 0.3270 0.1742 -0.0391 0.0286  -0.0709 239 GLU A C   
1904 O  O   . GLU A 238 ? 0.3292 0.3224 0.2143 -0.0223 0.0457  -0.0591 239 GLU A O   
1905 C  CB  . GLU A 238 ? 0.2757 0.3863 0.4624 -0.0704 0.0543  -0.1080 239 GLU A CB  
1906 N  N   . LEU A 239 ? 0.2816 0.3239 0.1557 -0.0044 0.0251  -0.0539 240 LEU A N   
1907 C  CA  . LEU A 239 ? 0.2674 0.2713 0.1612 0.0240  0.0250  -0.0401 240 LEU A CA  
1908 C  C   . LEU A 239 ? 0.2166 0.2734 0.1562 0.0173  -0.0054 -0.0366 240 LEU A C   
1909 O  O   . LEU A 239 ? 0.2362 0.3301 0.1443 0.0314  0.0087  0.0095  240 LEU A O   
1910 C  CB  . LEU A 239 ? 0.3148 0.2745 0.1789 0.0217  0.0057  -0.0490 240 LEU A CB  
1911 C  CG  . LEU A 239 ? 0.2663 0.3382 0.2399 0.0302  -0.0118 -0.0972 240 LEU A CG  
1912 C  CD1 . LEU A 239 ? 0.3744 0.3030 0.4496 0.0438  0.0030  -0.0517 240 LEU A CD1 
1913 C  CD2 . LEU A 239 ? 0.3933 0.4101 0.2610 0.1128  -0.0693 -0.1013 240 LEU A CD2 
1914 N  N   . MET A 240 ? 0.2236 0.2749 0.0972 0.0296  0.0214  0.0008  241 MET A N   
1915 C  CA  . MET A 240 ? 0.2506 0.2638 0.1051 0.0406  0.0303  -0.0066 241 MET A CA  
1916 C  C   . MET A 240 ? 0.2128 0.2524 0.1476 0.0105  -0.0163 -0.0212 241 MET A C   
1917 O  O   . MET A 240 ? 0.2294 0.2749 0.0884 -0.0003 -0.0170 -0.0053 241 MET A O   
1918 C  CB  . MET A 240 ? 0.2631 0.2935 0.1296 0.0541  0.0398  -0.0190 241 MET A CB  
1919 C  CG  . MET A 240 ? 0.2743 0.2215 0.1282 0.0174  -0.0057 -0.0139 241 MET A CG  
1920 S  SD  . MET A 240 ? 0.2684 0.2462 0.1649 -0.0024 0.0076  0.0135  241 MET A SD  
1921 C  CE  . MET A 240 ? 0.2823 0.3061 0.1455 0.0156  0.0347  0.0482  241 MET A CE  
1922 N  N   . VAL A 241 ? 0.2499 0.2237 0.1078 0.0212  -0.0009 0.0069  242 VAL A N   
1923 C  CA  . VAL A 241 ? 0.2464 0.2134 0.0963 0.0050  -0.0230 -0.0160 242 VAL A CA  
1924 C  C   . VAL A 241 ? 0.2198 0.1918 0.0949 0.0174  -0.0110 -0.0179 242 VAL A C   
1925 O  O   . VAL A 241 ? 0.2185 0.2258 0.1137 0.0031  -0.0055 -0.0047 242 VAL A O   
1926 C  CB  . VAL A 241 ? 0.2342 0.2116 0.1203 0.0033  -0.0100 -0.0339 242 VAL A CB  
1927 C  CG1 . VAL A 241 ? 0.2800 0.2555 0.1458 -0.0127 -0.0460 -0.0333 242 VAL A CG1 
1928 C  CG2 . VAL A 241 ? 0.2403 0.2481 0.1522 0.0380  -0.0117 -0.0295 242 VAL A CG2 
1929 N  N   . ASP A 242 ? 0.2304 0.1841 0.0746 0.0153  -0.0154 -0.0203 243 ASP A N   
1930 C  CA  . ASP A 242 ? 0.2247 0.1687 0.1142 0.0236  -0.0455 -0.0247 243 ASP A CA  
1931 C  C   . ASP A 242 ? 0.1897 0.1812 0.1047 0.0051  0.0015  -0.0179 243 ASP A C   
1932 O  O   . ASP A 242 ? 0.2022 0.1910 0.1562 0.0061  -0.0524 -0.0111 243 ASP A O   
1933 C  CB  . ASP A 242 ? 0.1976 0.1846 0.1658 0.0322  -0.0408 -0.0226 243 ASP A CB  
1934 C  CG  . ASP A 242 ? 0.2135 0.1821 0.1764 0.0445  -0.0035 0.0030  243 ASP A CG  
1935 O  OD1 . ASP A 242 ? 0.2255 0.1910 0.1595 0.0318  -0.0068 -0.0308 243 ASP A OD1 
1936 O  OD2 . ASP A 242 ? 0.2499 0.2101 0.1979 0.0396  0.0078  -0.0421 243 ASP A OD2 
1937 N  N   . ASN A 243 ? 0.2115 0.1588 0.0861 0.0144  0.0047  -0.0100 244 ASN A N   
1938 C  CA  . ASN A 243 ? 0.1803 0.1604 0.0893 -0.0194 -0.0267 -0.0061 244 ASN A CA  
1939 C  C   . ASN A 243 ? 0.1993 0.1580 0.1130 -0.0258 -0.0255 -0.0113 244 ASN A C   
1940 O  O   . ASN A 243 ? 0.2168 0.1728 0.1206 0.0212  -0.0272 -0.0054 244 ASN A O   
1941 C  CB  . ASN A 243 ? 0.2035 0.2223 0.0972 -0.0125 -0.0390 0.0148  244 ASN A CB  
1942 C  CG  . ASN A 243 ? 0.1902 0.2502 0.0796 -0.0207 -0.0352 0.0301  244 ASN A CG  
1943 O  OD1 . ASN A 243 ? 0.2008 0.2015 0.1309 0.0042  -0.0289 0.0111  244 ASN A OD1 
1944 N  ND2 . ASN A 243 ? 0.2302 0.2459 0.1597 -0.0201 -0.0763 0.0555  244 ASN A ND2 
1945 N  N   . TRP A 244 ? 0.1741 0.1800 0.1021 -0.0193 -0.0179 -0.0004 245 TRP A N   
1946 C  CA  . TRP A 244 ? 0.1583 0.1724 0.0866 0.0053  -0.0245 0.0013  245 TRP A CA  
1947 C  C   . TRP A 244 ? 0.1674 0.1688 0.1103 0.0127  -0.0325 -0.0108 245 TRP A C   
1948 O  O   . TRP A 244 ? 0.1746 0.1875 0.1379 0.0190  -0.0432 -0.0194 245 TRP A O   
1949 C  CB  . TRP A 244 ? 0.2046 0.1472 0.0810 0.0058  -0.0077 0.0054  245 TRP A CB  
1950 C  CG  . TRP A 244 ? 0.1925 0.1584 0.1078 0.0230  -0.0069 0.0117  245 TRP A CG  
1951 C  CD1 . TRP A 244 ? 0.2021 0.1652 0.1264 0.0275  -0.0326 -0.0205 245 TRP A CD1 
1952 C  CD2 . TRP A 244 ? 0.2081 0.1555 0.1164 0.0018  -0.0303 0.0064  245 TRP A CD2 
1953 N  NE1 . TRP A 244 ? 0.2195 0.1656 0.1049 0.0049  -0.0189 -0.0022 245 TRP A NE1 
1954 C  CE2 . TRP A 244 ? 0.2114 0.1430 0.1173 0.0081  -0.0280 0.0117  245 TRP A CE2 
1955 C  CE3 . TRP A 244 ? 0.2222 0.1841 0.1214 0.0189  -0.0421 0.0009  245 TRP A CE3 
1956 C  CZ2 . TRP A 244 ? 0.2351 0.1813 0.1227 0.0264  -0.0398 0.0147  245 TRP A CZ2 
1957 C  CZ3 . TRP A 244 ? 0.2292 0.1841 0.1572 0.0265  -0.0223 0.0210  245 TRP A CZ3 
1958 C  CH2 . TRP A 244 ? 0.2603 0.1834 0.1273 0.0414  -0.0390 0.0196  245 TRP A CH2 
1959 N  N   . ARG A 245 ? 0.1832 0.1884 0.1053 0.0212  -0.0401 -0.0170 246 ARG A N   
1960 C  CA  . ARG A 245 ? 0.1824 0.1777 0.1238 -0.0234 -0.0476 0.0005  246 ARG A CA  
1961 C  C   . ARG A 245 ? 0.1914 0.1767 0.0898 0.0190  -0.0295 -0.0210 246 ARG A C   
1962 O  O   . ARG A 245 ? 0.2054 0.1943 0.1177 -0.0122 -0.0273 -0.0139 246 ARG A O   
1963 C  CB  . ARG A 245 ? 0.1634 0.1706 0.1048 -0.0024 -0.0245 -0.0002 246 ARG A CB  
1964 C  CG  . ARG A 245 ? 0.1724 0.1821 0.1365 0.0042  -0.0501 -0.0049 246 ARG A CG  
1965 C  CD  . ARG A 245 ? 0.1659 0.1875 0.1347 -0.0133 -0.0427 -0.0094 246 ARG A CD  
1966 N  NE  . ARG A 245 ? 0.1688 0.1770 0.1351 -0.0006 -0.0346 -0.0228 246 ARG A NE  
1967 C  CZ  . ARG A 245 ? 0.1742 0.2148 0.1015 -0.0259 -0.0175 -0.0271 246 ARG A CZ  
1968 N  NH1 . ARG A 245 ? 0.1835 0.2196 0.1580 -0.0133 0.0091  -0.0177 246 ARG A NH1 
1969 N  NH2 . ARG A 245 ? 0.1767 0.2360 0.1550 -0.0293 -0.0407 -0.0151 246 ARG A NH2 
1970 N  N   . PRO A 246 ? 0.2111 0.1835 0.1224 0.0168  -0.0401 -0.0039 247 PRO A N   
1971 C  CA  . PRO A 246 ? 0.2288 0.2191 0.1018 0.0455  -0.0110 0.0108  247 PRO A CA  
1972 C  C   . PRO A 246 ? 0.1903 0.2186 0.0778 0.0139  -0.0425 0.0173  247 PRO A C   
1973 O  O   . PRO A 246 ? 0.2026 0.1745 0.1279 -0.0047 -0.0354 0.0062  247 PRO A O   
1974 C  CB  . PRO A 246 ? 0.2355 0.2462 0.1710 0.0648  -0.0320 0.0553  247 PRO A CB  
1975 C  CG  . PRO A 246 ? 0.2569 0.3350 0.2701 0.1069  0.0046  0.1314  247 PRO A CG  
1976 C  CD  . PRO A 246 ? 0.2047 0.2262 0.1620 0.0486  -0.0310 0.0167  247 PRO A CD  
1977 N  N   . ALA A 247 ? 0.2189 0.2004 0.1026 0.0211  -0.0035 0.0234  248 ALA A N   
1978 C  CA  . ALA A 247 ? 0.2074 0.2309 0.0762 -0.0055 -0.0262 -0.0041 248 ALA A CA  
1979 C  C   . ALA A 247 ? 0.2064 0.1982 0.0976 0.0361  -0.0491 0.0201  248 ALA A C   
1980 O  O   . ALA A 247 ? 0.2309 0.2237 0.1469 0.0576  -0.0447 0.0135  248 ALA A O   
1981 C  CB  . ALA A 247 ? 0.2995 0.2457 0.1437 0.0058  0.0363  0.0288  248 ALA A CB  
1982 N  N   . GLN A 248 ? 0.1881 0.1843 0.1458 -0.0004 -0.0407 0.0109  249 GLN A N   
1983 C  CA  . GLN A 248 ? 0.1785 0.2069 0.1202 0.0071  -0.0364 0.0067  249 GLN A CA  
1984 C  C   . GLN A 248 ? 0.2104 0.1868 0.1324 0.0174  -0.0337 -0.0087 249 GLN A C   
1985 O  O   . GLN A 248 ? 0.2323 0.2241 0.1137 0.0239  -0.0234 0.0098  249 GLN A O   
1986 C  CB  . GLN A 248 ? 0.2056 0.1857 0.1205 -0.0060 -0.0568 -0.0124 249 GLN A CB  
1987 C  CG  . GLN A 248 ? 0.2202 0.2055 0.1099 -0.0111 -0.0303 -0.0148 249 GLN A CG  
1988 C  CD  . GLN A 248 ? 0.1921 0.2660 0.1191 -0.0190 -0.0126 -0.0024 249 GLN A CD  
1989 O  OE1 . GLN A 248 ? 0.2126 0.3076 0.2085 -0.0428 -0.0346 -0.0406 249 GLN A OE1 
1990 N  NE2 . GLN A 248 ? 0.2234 0.2489 0.1307 0.0332  -0.0276 -0.0151 249 GLN A NE2 
1991 N  N   . PRO A 249 ? 0.2319 0.2678 0.1166 0.0363  -0.0579 0.0070  250 PRO A N   
1992 C  CA  . PRO A 249 ? 0.2137 0.3139 0.1191 0.0750  -0.0308 0.0063  250 PRO A CA  
1993 C  C   . PRO A 249 ? 0.2148 0.2270 0.1080 0.0389  -0.0630 -0.0184 250 PRO A C   
1994 O  O   . PRO A 249 ? 0.2298 0.2577 0.1408 0.0226  -0.0553 0.0375  250 PRO A O   
1995 C  CB  . PRO A 249 ? 0.2008 0.4170 0.1976 0.1023  -0.0561 0.0217  250 PRO A CB  
1996 C  CG  . PRO A 249 ? 0.2682 0.5242 0.1414 0.0663  -0.0666 -0.0267 250 PRO A CG  
1997 C  CD  . PRO A 249 ? 0.2011 0.3727 0.2182 0.0425  -0.0939 -0.0209 250 PRO A CD  
1998 N  N   . LEU A 250 ? 0.2432 0.2426 0.1317 0.0445  -0.0325 0.0179  251 LEU A N   
1999 C  CA  . LEU A 250 ? 0.2179 0.2533 0.1182 0.0248  -0.0452 0.0075  251 LEU A CA  
2000 C  C   . LEU A 250 ? 0.2155 0.2554 0.1031 0.0336  -0.0410 -0.0055 251 LEU A C   
2001 O  O   . LEU A 250 ? 0.2264 0.2435 0.1537 0.0337  -0.0562 0.0027  251 LEU A O   
2002 C  CB  . LEU A 250 ? 0.3357 0.2527 0.1821 0.0223  0.0363  0.0301  251 LEU A CB  
2003 C  CG  . LEU A 250 ? 0.2990 0.3292 0.1137 -0.0164 -0.0143 -0.0120 251 LEU A CG  
2004 C  CD1 . LEU A 250 ? 0.2996 0.3192 0.1130 -0.0398 -0.0188 -0.0061 251 LEU A CD1 
2005 C  CD2 . LEU A 250 ? 0.3486 0.3297 0.2282 -0.0694 0.0018  -0.0164 251 LEU A CD2 
2006 N  N   . LYS A 251 ? 0.2452 0.2883 0.1057 0.0372  -0.0677 0.0041  252 LYS A N   
2007 C  CA  . LYS A 251 ? 0.2728 0.3024 0.1278 0.0472  -0.0734 -0.0308 252 LYS A CA  
2008 C  C   . LYS A 251 ? 0.2751 0.2755 0.1652 0.0522  -0.0598 -0.0190 252 LYS A C   
2009 O  O   . LYS A 251 ? 0.3161 0.4113 0.1503 0.0100  -0.0148 -0.0008 252 LYS A O   
2010 C  CB  . LYS A 251 ? 0.2547 0.3360 0.2037 0.0127  -0.0305 -0.0433 252 LYS A CB  
2011 C  CG  . LYS A 251 ? 0.3042 0.3763 0.2524 0.0322  0.0290  -0.0211 252 LYS A CG  
2012 C  CD  . LYS A 251 ? 0.2798 0.4664 0.3414 -0.0489 -0.0076 -0.0921 252 LYS A CD  
2013 C  CE  . LYS A 251 ? 0.2319 0.5417 0.4151 -0.0150 0.0121  -0.0412 252 LYS A CE  
2014 N  NZ  . LYS A 251 ? 0.2693 0.4855 0.4385 0.0064  0.0077  -0.0275 252 LYS A NZ  
2015 N  N   . ASN A 252 ? 0.2377 0.2956 0.1242 0.0403  -0.0583 -0.0182 253 ASN A N   
2016 C  CA  . ASN A 252 ? 0.3162 0.4543 0.2148 0.0771  -0.0424 -0.0917 253 ASN A CA  
2017 C  C   . ASN A 252 ? 0.3314 0.4887 0.3950 0.0983  -0.1632 -0.1559 253 ASN A C   
2018 O  O   . ASN A 252 ? 0.4372 0.4718 0.4314 0.1043  0.0159  0.0036  253 ASN A O   
2019 C  CB  . ASN A 252 ? 0.4018 0.5390 0.3077 0.0322  -0.1050 -0.1948 253 ASN A CB  
2020 C  CG  . ASN A 252 ? 0.6139 0.4663 0.4099 0.0203  0.0840  -0.1155 253 ASN A CG  
2021 O  OD1 . ASN A 252 ? 0.8121 0.6487 0.6589 -0.0609 0.1706  0.0804  253 ASN A OD1 
2022 N  ND2 . ASN A 252 ? 0.4876 0.4703 0.5495 -0.0375 -0.0735 -0.1007 253 ASN A ND2 
2023 N  N   . ARG A 253 ? 0.2438 0.3684 0.1073 0.0243  -0.0299 0.0268  254 ARG A N   
2024 C  CA  . ARG A 253 ? 0.2017 0.2872 0.1099 0.0318  0.0032  -0.0129 254 ARG A CA  
2025 C  C   . ARG A 253 ? 0.2786 0.2561 0.1232 -0.0062 0.0053  -0.0226 254 ARG A C   
2026 O  O   . ARG A 253 ? 0.3556 0.2830 0.2818 0.0384  0.0592  0.0497  254 ARG A O   
2027 C  CB  . ARG A 253 ? 0.2262 0.2295 0.0967 0.0024  -0.0130 -0.0156 254 ARG A CB  
2028 C  CG  . ARG A 253 ? 0.2605 0.2040 0.0564 0.0026  -0.0402 0.0037  254 ARG A CG  
2029 C  CD  . ARG A 253 ? 0.2577 0.2434 0.0593 0.0398  -0.0245 -0.0134 254 ARG A CD  
2030 N  NE  . ARG A 253 ? 0.2119 0.2001 0.1049 0.0201  -0.0111 -0.0126 254 ARG A NE  
2031 C  CZ  . ARG A 253 ? 0.1810 0.1931 0.0821 0.0119  -0.0238 0.0026  254 ARG A CZ  
2032 N  NH1 . ARG A 253 ? 0.1861 0.1925 0.1173 -0.0047 -0.0687 0.0143  254 ARG A NH1 
2033 N  NH2 . ARG A 253 ? 0.1906 0.1673 0.1154 0.0133  -0.0442 -0.0115 254 ARG A NH2 
2034 N  N   . GLN A 254 ? 0.2414 0.2901 0.1606 -0.0075 -0.0463 -0.0519 255 GLN A N   
2035 C  CA  . GLN A 254 ? 0.2279 0.3693 0.1483 -0.0269 -0.0440 -0.0502 255 GLN A CA  
2036 C  C   . GLN A 254 ? 0.2586 0.2782 0.1938 -0.0428 -0.0813 -0.0018 255 GLN A C   
2037 O  O   . GLN A 254 ? 0.3724 0.2585 0.2523 -0.0222 -0.0870 -0.0380 255 GLN A O   
2038 C  CB  . GLN A 254 ? 0.3868 0.4616 0.0986 0.0125  -0.0316 -0.0631 255 GLN A CB  
2039 N  N   . ILE A 255 ? 0.2489 0.2414 0.0853 0.0034  -0.0463 0.0155  256 ILE A N   
2040 C  CA  . ILE A 255 ? 0.2172 0.2442 0.0789 0.0440  -0.0425 -0.0050 256 ILE A CA  
2041 C  C   . ILE A 255 ? 0.2402 0.2122 0.1674 0.0336  0.0013  0.0030  256 ILE A C   
2042 O  O   . ILE A 255 ? 0.2272 0.2518 0.1785 0.0207  -0.0165 0.0469  256 ILE A O   
2043 C  CB  . ILE A 255 ? 0.2313 0.2306 0.1087 0.0347  -0.0471 -0.0214 256 ILE A CB  
2044 C  CG1 . ILE A 255 ? 0.2172 0.2664 0.1785 0.0739  -0.0289 -0.0265 256 ILE A CG1 
2045 C  CG2 . ILE A 255 ? 0.2613 0.2511 0.1271 -0.0079 -0.0561 -0.0242 256 ILE A CG2 
2046 C  CD1 . ILE A 255 ? 0.2773 0.2956 0.1440 -0.0038 0.0145  -0.0523 256 ILE A CD1 
2047 N  N   . LYS A 256 ? 0.2098 0.2155 0.1078 0.0152  -0.0330 -0.0050 257 LYS A N   
2048 C  CA  . LYS A 256 ? 0.2129 0.2397 0.1040 0.0234  -0.0381 -0.0055 257 LYS A CA  
2049 C  C   . LYS A 256 ? 0.1965 0.2566 0.0744 0.0070  -0.0385 0.0182  257 LYS A C   
2050 O  O   . LYS A 256 ? 0.2572 0.2713 0.0774 -0.0413 -0.0179 -0.0009 257 LYS A O   
2051 C  CB  . LYS A 256 ? 0.2223 0.2539 0.1931 0.0297  -0.0386 -0.0341 257 LYS A CB  
2052 C  CG  . LYS A 256 ? 0.3878 0.3202 0.2788 -0.0500 -0.0290 -0.1163 257 LYS A CG  
2053 C  CD  . LYS A 256 ? 0.5285 0.3807 0.5053 -0.0242 0.0217  -0.1806 257 LYS A CD  
2054 N  N   . ALA A 257 ? 0.2135 0.2680 0.1044 0.0167  -0.0046 0.0203  258 ALA A N   
2055 C  CA  . ALA A 257 ? 0.2183 0.2640 0.1612 0.0017  -0.0122 0.0026  258 ALA A CA  
2056 C  C   . ALA A 257 ? 0.2457 0.2760 0.0773 0.0178  0.0000  -0.0044 258 ALA A C   
2057 O  O   . ALA A 257 ? 0.2383 0.2970 0.0857 0.0256  -0.0006 -0.0127 258 ALA A O   
2058 C  CB  . ALA A 257 ? 0.2226 0.2637 0.2119 -0.0111 0.0093  0.0368  258 ALA A CB  
2059 N  N   . SER A 258 ? 0.2245 0.2470 0.1146 0.0176  -0.0128 0.0030  259 SER A N   
2060 C  CA  . SER A 258 ? 0.2121 0.2801 0.1172 0.0025  -0.0023 -0.0012 259 SER A CA  
2061 C  C   . SER A 258 ? 0.2274 0.2895 0.1207 -0.0027 -0.0108 -0.0120 259 SER A C   
2062 O  O   . SER A 258 ? 0.2304 0.3855 0.2482 0.0373  0.0018  0.0100  259 SER A O   
2063 C  CB  . SER A 258 ? 0.2852 0.3017 0.1133 0.0185  -0.0189 0.0066  259 SER A CB  
2064 O  OG  . SER A 258 ? 0.2223 0.3182 0.1207 0.0201  -0.0113 0.0041  259 SER A OG  
2065 N  N   . PHE A 259 ? 0.2360 0.2813 0.1472 -0.0294 -0.0272 -0.0033 260 PHE A N   
2066 C  CA  . PHE A 259 ? 0.2416 0.3170 0.2560 -0.0436 -0.0148 -0.0087 260 PHE A CA  
2067 C  C   . PHE A 259 ? 0.4053 0.5815 0.1949 0.0430  -0.0591 0.0152  260 PHE A C   
2068 O  O   . PHE A 259 ? 0.3961 0.3098 0.2198 -0.0556 -0.0243 0.0548  260 PHE A O   
2069 C  CB  . PHE A 259 ? 0.2114 0.3412 0.2913 -0.0517 -0.0294 -0.0516 260 PHE A CB  
2070 C  CG  . PHE A 259 ? 0.2159 0.2866 0.3051 -0.0179 -0.0438 0.0043  260 PHE A CG  
2071 C  CD1 . PHE A 259 ? 0.2007 0.2736 0.2075 -0.0222 -0.0500 -0.0255 260 PHE A CD1 
2072 C  CD2 . PHE A 259 ? 0.3000 0.2525 0.3299 -0.0523 0.0004  -0.0302 260 PHE A CD2 
2073 C  CE1 . PHE A 259 ? 0.2534 0.3009 0.2272 0.0324  -0.0357 -0.0163 260 PHE A CE1 
2074 C  CE2 . PHE A 259 ? 0.3176 0.2665 0.3583 0.0035  -0.0043 0.0104  260 PHE A CE2 
2075 C  CZ  . PHE A 259 ? 0.2691 0.3063 0.3793 0.0067  -0.0106 -0.0008 260 PHE A CZ  
2076 N  N   . LYS A 260 ? 0.5480 0.6479 0.5268 -0.1908 0.0650  -0.1262 261 LYS A N   
2077 C  CA  . LYS A 260 ? 0.8919 0.8477 0.5492 0.1552  -0.0041 0.0432  261 LYS A CA  
2078 C  C   . LYS A 260 ? 1.2077 1.1492 0.7195 0.2357  -0.2367 0.1624  261 LYS A C   
2079 O  O   . LYS A 260 ? 1.8020 1.2574 0.8555 -0.1521 0.4991  0.0596  261 LYS A O   
2080 C  CB  . LYS A 260 ? 0.7763 0.7785 1.1985 0.2326  0.1062  0.2199  261 LYS A CB  
2081 O  OXT . LYS A 260 ? 1.4686 1.4529 0.6590 0.3517  0.0306  0.1157  261 LYS A OXT 
2082 ZN ZN  . ZN  B .   ? 0.1773 0.1591 0.1031 0.0027  -0.0548 -0.0021 301 ZN  A ZN  
2083 S  S   . DMS C .   ? 0.3925 0.4715 0.3149 -0.0339 -0.0186 -0.0738 302 DMS A S   
2084 O  O   . DMS C .   ? 0.6154 0.5869 0.3767 0.0775  0.0577  -0.2024 302 DMS A O   
2085 C  C1  . DMS C .   ? 0.3405 0.4158 0.2723 0.1471  -0.0571 -0.0785 302 DMS A C1  
2086 C  C2  . DMS C .   ? 0.6326 0.3130 0.5459 -0.0321 0.0457  0.1099  302 DMS A C2  
2087 F  F27 . WWO D .   ? 0.2894 0.2010 0.2248 -0.0151 -0.0908 -0.0095 303 WWO A F27 
2088 C  C5  . WWO D .   ? 0.2331 0.2492 0.2029 -0.0103 -0.0618 0.0034  303 WWO A C5  
2089 C  C4  . WWO D .   ? 0.1687 0.2356 0.1659 -0.0135 -0.0649 -0.0461 303 WWO A C4  
2090 S  S7  . WWO D .   ? 0.1970 0.1738 0.1361 0.0057  -0.0775 -0.0055 303 WWO A S7  
2091 O  O9  . WWO D .   ? 0.1904 0.1751 0.1532 0.0234  -0.0849 -0.0042 303 WWO A O9  
2092 N  N10 . WWO D .   ? 0.1893 0.1544 0.1548 -0.0307 -0.0540 -0.0136 303 WWO A N10 
2093 O  O8  . WWO D .   ? 0.2331 0.1752 0.1408 0.0252  -0.1094 -0.0207 303 WWO A O8  
2094 C  C3  . WWO D .   ? 0.1663 0.2558 0.1562 -0.0075 -0.0073 0.0271  303 WWO A C3  
2095 F  F12 . WWO D .   ? 0.2329 0.2552 0.2176 0.0309  -0.0189 0.0103  303 WWO A F12 
2096 C  C2  . WWO D .   ? 0.2466 0.3233 0.1950 -0.0281 -0.0085 0.0585  303 WWO A C2  
2097 F  F13 . WWO D .   ? 0.3158 0.4065 0.2159 0.0170  -0.0129 0.0309  303 WWO A F13 
2098 C  C6  . WWO D .   ? 0.3084 0.2670 0.2312 -0.0536 -0.0749 0.0258  303 WWO A C6  
2099 C  C1  . WWO D .   ? 0.2946 0.2829 0.1737 -0.0104 -0.0859 0.0611  303 WWO A C1  
2100 S  S11 . WWO D .   ? 0.3514 0.4014 0.2280 -0.0561 -0.0599 0.0803  303 WWO A S11 
2101 O  O22 . WWO D .   ? 0.5384 0.4710 0.3278 0.0537  -0.0362 0.1780  303 WWO A O22 
2102 O  O23 . WWO D .   ? 0.4581 0.4539 0.1856 -0.0782 -0.0344 -0.0089 303 WWO A O23 
2103 C  C21 . WWO D .   ? 0.3450 0.5777 0.3806 -0.0904 -0.0414 0.1244  303 WWO A C21 
2104 C  C24 . WWO D .   ? 0.5727 0.6657 0.5946 -0.2468 -0.2992 0.1727  303 WWO A C24 
2105 O  O25 . WWO D .   ? 0.3964 0.5429 0.5547 -0.1592 -0.1408 0.1050  303 WWO A O25 
2106 N  N26 . WWO D .   ? 0.4266 0.2366 0.2417 -0.0634 -0.0775 0.0023  303 WWO A N26 
2107 C  C14 . WWO D .   ? 0.4651 0.2809 0.2197 0.0002  -0.0586 0.0257  303 WWO A C14 
2108 C  C15 . WWO D .   ? 0.5173 0.2999 0.2028 -0.0904 -0.0005 0.0758  303 WWO A C15 
2109 C  C20 . WWO D .   ? 0.4386 0.3328 0.1920 -0.0549 -0.0272 0.0464  303 WWO A C20 
2110 C  C19 . WWO D .   ? 0.5678 0.2837 0.2750 0.0184  -0.0326 -0.0154 303 WWO A C19 
2111 C  C18 . WWO D .   ? 0.4901 0.2654 0.3578 0.0364  -0.0302 -0.0086 303 WWO A C18 
2112 C  C17 . WWO D .   ? 0.5975 0.3312 0.2669 -0.0369 -0.0130 0.0226  303 WWO A C17 
2113 C  C16 . WWO D .   ? 0.4979 0.3495 0.3855 -0.0406 -0.0541 0.0533  303 WWO A C16 
2114 F  F27 . WWO E .   ? 0.4998 0.3529 0.5797 -0.0178 -0.0243 -0.0678 304 WWO A F27 
2115 C  C5  . WWO E .   ? 0.4925 0.3414 0.6766 -0.0122 0.0128  -0.0943 304 WWO A C5  
2116 C  C4  . WWO E .   ? 0.4865 0.3878 0.5687 -0.0458 -0.0993 -0.0322 304 WWO A C4  
2117 S  S7  . WWO E .   ? 0.5028 0.4323 0.6983 -0.0197 -0.0337 -0.0456 304 WWO A S7  
2118 O  O9  . WWO E .   ? 0.4100 0.2697 0.5330 0.0026  -0.2211 -0.0927 304 WWO A O9  
2119 N  N10 . WWO E .   ? 0.2788 0.3146 0.4762 -0.0157 -0.1248 -0.1410 304 WWO A N10 
2120 O  O8  . WWO E .   ? 0.4837 0.3098 0.5299 0.0781  -0.1289 0.0299  304 WWO A O8  
2121 C  C3  . WWO E .   ? 0.4536 0.4714 0.4228 -0.0732 -0.0747 -0.0398 304 WWO A C3  
2122 F  F12 . WWO E .   ? 0.6350 0.5105 0.4415 -0.1125 0.0212  -0.0446 304 WWO A F12 
2123 C  C2  . WWO E .   ? 0.3842 0.4596 0.4970 -0.0624 -0.0855 -0.0463 304 WWO A C2  
2124 F  F13 . WWO E .   ? 0.4960 0.4615 0.4164 -0.0053 -0.0957 -0.0713 304 WWO A F13 
2125 C  C6  . WWO E .   ? 0.3189 0.5033 0.8143 -0.0036 -0.0158 -0.1337 304 WWO A C6  
2126 C  C1  . WWO E .   ? 0.4377 0.6285 0.6727 -0.1624 0.0713  -0.1489 304 WWO A C1  
2127 S  S11 . WWO E .   ? 0.5822 0.4628 0.6278 -0.0491 0.0010  0.0630  304 WWO A S11 
2128 O  O22 . WWO E .   ? 0.9759 0.9871 0.8482 0.0546  0.3614  -0.0348 304 WWO A O22 
2129 O  O23 . WWO E .   ? 0.6954 0.7493 0.6609 0.2550  0.2387  0.2401  304 WWO A O23 
2130 C  C21 . WWO E .   ? 0.7218 0.8378 0.5098 0.0409  -0.2865 -0.1425 304 WWO A C21 
2131 C  C24 . WWO E .   ? 0.9342 0.8240 0.8972 0.3960  -0.1551 -0.0686 304 WWO A C24 
2132 O  O25 . WWO E .   ? 1.0378 0.6983 1.3278 0.3066  -0.2622 0.0355  304 WWO A O25 
2133 N  N26 . WWO E .   ? 0.4623 0.6451 0.8178 -0.0703 -0.0679 -0.3066 304 WWO A N26 
2134 C  C14 . WWO E .   ? 0.2535 0.4094 0.7571 0.0355  -0.1100 -0.0996 304 WWO A C14 
2135 C  C15 . WWO E .   ? 0.4374 0.7384 0.7244 -0.1053 -0.0290 -0.2683 304 WWO A C15 
2136 C  C20 . WWO E .   ? 0.7235 0.4772 1.0240 -0.1053 0.0429  -0.1974 304 WWO A C20 
2137 C  C19 . WWO E .   ? 1.0115 0.6714 0.8922 0.1217  0.0433  -0.4077 304 WWO A C19 
2138 C  C18 . WWO E .   ? 1.0238 0.9579 0.7083 0.1653  0.0255  -0.3982 304 WWO A C18 
2139 C  C17 . WWO E .   ? 0.2934 1.0069 0.8916 -0.1133 0.0370  -0.5105 304 WWO A C17 
2140 C  C16 . WWO E .   ? 0.2099 0.8873 0.8437 0.0372  -0.0611 -0.1066 304 WWO A C16 
2141 O  O   . HOH F .   ? 0.4664 0.3319 0.5872 -0.0141 -0.2037 0.1009  401 HOH A O   
2142 O  O   . HOH F .   ? 0.4111 0.3434 0.4997 -0.0305 -0.0348 -0.0473 402 HOH A O   
2143 O  O   . HOH F .   ? 0.3349 0.1652 0.2513 -0.0321 -0.0982 -0.0001 403 HOH A O   
2144 O  O   . HOH F .   ? 0.4247 0.4328 0.6175 -0.0727 -0.1978 0.1450  404 HOH A O   
2145 O  O   . HOH F .   ? 0.4997 0.3513 0.5667 -0.0395 -0.1813 0.1310  405 HOH A O   
2146 O  O   . HOH F .   ? 0.3274 0.6245 0.4233 0.0486  0.0345  0.1797  406 HOH A O   
2147 O  O   . HOH F .   ? 0.3577 0.3388 0.3633 0.0114  -0.0153 0.0051  407 HOH A O   
2148 O  O   . HOH F .   ? 0.4589 0.3032 0.5613 -0.0844 0.1129  -0.0779 408 HOH A O   
2149 O  O   . HOH F .   ? 0.3913 0.2153 0.3538 -0.0435 -0.0304 0.0194  409 HOH A O   
2150 O  O   . HOH F .   ? 0.4343 0.5136 0.4318 0.0392  0.1184  -0.0495 410 HOH A O   
2151 O  O   . HOH F .   ? 0.4091 0.5844 0.4744 0.0820  -0.1041 -0.1051 411 HOH A O   
2152 O  O   . HOH F .   ? 0.6297 0.5582 0.2976 -0.1408 -0.0749 0.0221  412 HOH A O   
2153 O  O   . HOH F .   ? 0.4846 0.2885 0.4197 -0.0567 -0.0324 -0.0756 413 HOH A O   
2154 O  O   . HOH F .   ? 0.9017 0.5102 0.5025 -0.2210 0.2559  -0.1468 414 HOH A O   
2155 O  O   . HOH F .   ? 0.4237 0.5983 0.5486 -0.1336 0.1030  -0.2667 415 HOH A O   
2156 O  O   . HOH F .   ? 0.5311 0.7762 0.2390 0.1963  -0.0564 -0.0378 416 HOH A O   
2157 O  O   . HOH F .   ? 0.9593 0.5118 0.5709 0.0052  0.4320  -0.0250 417 HOH A O   
2158 O  O   . HOH F .   ? 0.5405 0.3171 0.4663 0.0988  0.1410  0.1042  418 HOH A O   
2159 O  O   . HOH F .   ? 0.4472 0.3639 0.2121 -0.0591 -0.0080 -0.0659 419 HOH A O   
2160 O  O   . HOH F .   ? 0.7095 0.3009 0.5356 -0.0518 -0.1873 -0.0902 420 HOH A O   
2161 O  O   . HOH F .   ? 0.6101 0.7932 0.5516 0.0942  0.0662  0.0678  421 HOH A O   
2162 O  O   . HOH F .   ? 0.2191 0.2128 0.1297 0.0108  -0.0223 -0.0079 422 HOH A O   
2163 O  O   . HOH F .   ? 0.4459 0.4363 0.7415 -0.1612 -0.0217 0.0346  423 HOH A O   
2164 O  O   . HOH F .   ? 0.5963 0.7492 0.3185 -0.0514 0.0558  0.0577  424 HOH A O   
2165 O  O   . HOH F .   ? 0.4080 0.6184 0.2758 0.0904  -0.0551 0.1565  425 HOH A O   
2166 O  O   . HOH F .   ? 0.5411 0.4898 0.5320 -0.1386 -0.0833 0.0034  426 HOH A O   
2167 O  O   . HOH F .   ? 0.3148 0.2717 0.2707 0.0064  -0.0387 0.0030  427 HOH A O   
2168 O  O   . HOH F .   ? 0.5397 0.4546 0.2043 -0.1453 0.0153  0.0735  428 HOH A O   
2169 O  O   . HOH F .   ? 0.4557 0.4265 0.4237 -0.0372 -0.1082 0.1615  429 HOH A O   
2170 O  O   . HOH F .   ? 0.5923 0.4649 0.3753 -0.1292 0.2088  -0.1736 430 HOH A O   
2171 O  O   . HOH F .   ? 0.5942 0.3591 0.5245 -0.0904 -0.0177 0.1190  431 HOH A O   
2172 O  O   . HOH F .   ? 0.3628 0.9317 0.3944 -0.0439 -0.0771 -0.2219 432 HOH A O   
2173 O  O   . HOH F .   ? 0.4177 0.3428 0.8071 -0.0133 0.0840  0.1744  433 HOH A O   
2174 O  O   . HOH F .   ? 0.4923 0.5371 0.1629 -0.0281 -0.0334 0.0111  434 HOH A O   
2175 O  O   . HOH F .   ? 0.5473 0.4559 0.2486 0.0111  -0.0390 0.0648  435 HOH A O   
2176 O  O   . HOH F .   ? 0.4983 0.4417 0.4733 0.2064  -0.2656 -0.1886 436 HOH A O   
2177 O  O   . HOH F .   ? 0.5404 0.3811 0.2556 -0.0165 0.0120  -0.0186 437 HOH A O   
2178 O  O   . HOH F .   ? 0.3835 0.3739 0.2310 0.0193  -0.0780 -0.0141 438 HOH A O   
2179 O  O   . HOH F .   ? 0.3971 0.3066 0.2937 -0.0859 -0.0653 0.0063  439 HOH A O   
2180 O  O   . HOH F .   ? 0.6290 0.6370 0.7463 -0.0299 -0.2425 0.1054  440 HOH A O   
2181 O  O   . HOH F .   ? 0.6474 0.3053 0.2083 -0.1045 0.0585  0.0204  441 HOH A O   
2182 O  O   . HOH F .   ? 0.3261 0.3253 0.3602 -0.0142 -0.0133 -0.0218 442 HOH A O   
2183 O  O   . HOH F .   ? 0.3088 0.1805 0.2096 -0.0082 -0.0212 -0.0186 443 HOH A O   
2184 O  O   . HOH F .   ? 0.3658 0.6961 0.6781 0.0464  0.0743  0.2857  444 HOH A O   
2185 O  O   . HOH F .   ? 0.6903 0.4481 0.8365 0.0179  -0.2369 0.1886  445 HOH A O   
2186 O  O   . HOH F .   ? 0.3692 0.5852 0.2180 -0.1350 -0.1242 0.0091  446 HOH A O   
2187 O  O   . HOH F .   ? 0.4780 0.6650 0.3041 -0.3424 -0.1011 0.0651  447 HOH A O   
2188 O  O   . HOH F .   ? 0.3678 0.3013 0.3044 0.0706  0.0285  0.0880  448 HOH A O   
2189 O  O   . HOH F .   ? 0.3316 0.2861 0.4278 0.0195  -0.0013 -0.0534 449 HOH A O   
2190 O  O   . HOH F .   ? 0.3532 0.2378 0.5253 -0.0463 0.1157  -0.0977 450 HOH A O   
2191 O  O   . HOH F .   ? 0.5192 0.8441 0.5117 0.1837  0.0190  0.2796  451 HOH A O   
2192 O  O   . HOH F .   ? 0.3045 0.2712 0.3875 0.0173  -0.1861 -0.0759 452 HOH A O   
2193 O  O   . HOH F .   ? 0.7268 0.3905 0.1582 -0.0565 -0.0510 -0.0181 453 HOH A O   
2194 O  O   . HOH F .   ? 0.2420 0.2111 0.1638 -0.0238 -0.0304 -0.0477 454 HOH A O   
2195 O  O   . HOH F .   ? 0.5263 0.2696 0.4733 -0.0084 -0.0849 0.0612  455 HOH A O   
2196 O  O   . HOH F .   ? 0.2435 0.2405 0.1282 0.0611  -0.0196 -0.0008 456 HOH A O   
2197 O  O   . HOH F .   ? 0.6205 0.4205 0.8208 0.1039  0.2935  0.1168  457 HOH A O   
2198 O  O   . HOH F .   ? 0.3968 0.5210 0.3222 -0.0847 -0.0902 -0.0118 458 HOH A O   
2199 O  O   . HOH F .   ? 0.2065 0.2655 0.2403 -0.0170 -0.0362 0.0097  459 HOH A O   
2200 O  O   . HOH F .   ? 0.4062 0.4771 0.2791 0.1517  -0.0182 0.0653  460 HOH A O   
2201 O  O   . HOH F .   ? 0.3680 0.5288 0.7016 -0.1506 -0.1806 0.1333  461 HOH A O   
2202 O  O   . HOH F .   ? 0.3628 0.5492 0.4732 -0.0619 0.0011  0.0197  462 HOH A O   
2203 O  O   . HOH F .   ? 0.2194 0.1889 0.1351 0.0129  -0.0540 -0.0097 463 HOH A O   
2204 O  O   . HOH F .   ? 0.4634 0.3849 0.4122 0.0368  -0.1374 -0.1976 464 HOH A O   
2205 O  O   . HOH F .   ? 0.5228 0.4766 0.4651 0.1856  -0.2364 -0.1056 465 HOH A O   
2206 O  O   . HOH F .   ? 0.2746 0.2690 0.3768 -0.0564 -0.1106 0.0427  466 HOH A O   
2207 O  O   . HOH F .   ? 0.3193 0.2731 0.2320 0.0162  -0.1300 0.0260  467 HOH A O   
2208 O  O   . HOH F .   ? 0.4205 0.4517 0.2526 -0.0410 -0.1332 0.0104  468 HOH A O   
2209 O  O   . HOH F .   ? 0.6032 0.6182 0.2412 0.0249  0.0320  0.0892  469 HOH A O   
2210 O  O   . HOH F .   ? 0.2081 0.2486 0.1652 0.0153  -0.0702 0.0255  470 HOH A O   
2211 O  O   . HOH F .   ? 0.4413 0.5131 0.7452 -0.0465 -0.0461 -0.2499 471 HOH A O   
2212 O  O   . HOH F .   ? 0.5634 0.7205 0.8621 0.2429  -0.0339 -0.1502 472 HOH A O   
2213 O  O   . HOH F .   ? 0.4245 0.5493 0.8790 -0.1045 -0.0669 0.0834  473 HOH A O   
2214 O  O   . HOH F .   ? 0.2992 0.4049 0.3044 0.0436  0.0077  -0.0517 474 HOH A O   
2215 O  O   . HOH F .   ? 0.3107 0.3773 0.2597 0.0266  0.0329  -0.0751 475 HOH A O   
2216 O  O   . HOH F .   ? 0.2623 0.2434 0.2165 0.0127  -0.0373 0.0319  476 HOH A O   
2217 O  O   . HOH F .   ? 0.4506 0.2751 0.3400 0.0894  -0.0875 0.0085  477 HOH A O   
2218 O  O   . HOH F .   ? 0.3875 0.4343 0.2909 0.0391  0.0284  0.0329  478 HOH A O   
2219 O  O   . HOH F .   ? 0.5376 0.3750 0.3813 -0.1832 0.0937  -0.1254 479 HOH A O   
2220 O  O   . HOH F .   ? 0.3944 0.6521 0.3226 0.0203  -0.0256 -0.0483 480 HOH A O   
2221 O  O   . HOH F .   ? 0.6199 0.2578 0.6514 0.0002  -0.1424 -0.0627 481 HOH A O   
2222 O  O   . HOH F .   ? 0.2755 0.4090 0.1891 0.0025  -0.0297 -0.0502 482 HOH A O   
2223 O  O   . HOH F .   ? 0.3746 0.4011 0.3859 0.0542  0.0022  0.0754  483 HOH A O   
2224 O  O   . HOH F .   ? 0.2945 0.2107 0.2202 0.0158  -0.1116 0.0197  484 HOH A O   
2225 O  O   . HOH F .   ? 0.6282 0.4606 0.2134 -0.0011 -0.0347 0.0540  485 HOH A O   
2226 O  O   . HOH F .   ? 0.1904 0.2521 0.2029 0.0071  -0.0403 -0.0347 486 HOH A O   
2227 O  O   . HOH F .   ? 0.4731 0.4680 0.3028 0.0063  0.0234  -0.1184 487 HOH A O   
2228 O  O   . HOH F .   ? 0.2351 0.2122 0.1837 0.0176  -0.0396 0.0414  488 HOH A O   
2229 O  O   . HOH F .   ? 0.2794 0.2412 0.2157 -0.0078 -0.1107 0.0353  489 HOH A O   
2230 O  O   . HOH F .   ? 0.3550 0.4704 0.5851 0.0232  -0.0134 -0.1476 490 HOH A O   
2231 O  O   . HOH F .   ? 0.3538 0.2342 0.6348 0.0124  -0.2252 0.0205  491 HOH A O   
2232 O  O   . HOH F .   ? 0.3692 0.4445 0.2104 -0.0595 -0.0930 0.0418  492 HOH A O   
2233 O  O   . HOH F .   ? 0.3497 0.4040 0.2868 -0.0237 -0.0690 0.1377  493 HOH A O   
2234 O  O   . HOH F .   ? 0.4229 0.5079 0.6761 0.0770  0.1039  -0.0183 494 HOH A O   
2235 O  O   . HOH F .   ? 0.2865 0.2173 0.2236 -0.0423 -0.1118 0.0100  495 HOH A O   
2236 O  O   . HOH F .   ? 0.2929 0.2922 0.2417 0.0447  -0.0615 0.0100  496 HOH A O   
2237 O  O   . HOH F .   ? 0.4129 0.4535 0.2746 -0.0182 -0.0791 0.1026  497 HOH A O   
2238 O  O   . HOH F .   ? 0.3472 0.3977 0.4559 0.0904  -0.0839 -0.0517 498 HOH A O   
2239 O  O   . HOH F .   ? 0.2078 0.2000 0.1117 -0.0113 -0.0108 -0.0157 499 HOH A O   
2240 O  O   . HOH F .   ? 0.7263 0.3039 0.6176 -0.0930 0.1664  -0.0359 500 HOH A O   
2241 O  O   . HOH F .   ? 0.3008 0.5450 0.2245 0.0535  -0.0210 -0.0870 501 HOH A O   
2242 O  O   . HOH F .   ? 0.4087 0.3426 1.0844 0.0095  -0.1592 -0.0434 502 HOH A O   
2243 O  O   . HOH F .   ? 0.5723 0.4753 0.2306 0.0850  -0.1321 0.0219  503 HOH A O   
2244 O  O   . HOH F .   ? 0.3425 0.2728 0.2849 -0.0263 0.0359  -0.0117 504 HOH A O   
2245 O  O   . HOH F .   ? 0.6852 0.4675 0.6386 0.1645  0.0154  -0.1317 505 HOH A O   
2246 O  O   . HOH F .   ? 0.1827 0.2818 0.2001 0.0156  -0.0480 -0.0170 506 HOH A O   
2247 O  O   . HOH F .   ? 0.3726 0.3783 0.4048 -0.1247 -0.0693 0.0930  507 HOH A O   
2248 O  O   . HOH F .   ? 0.4208 0.3624 0.2678 -0.0653 -0.0083 -0.0775 508 HOH A O   
2249 O  O   . HOH F .   ? 0.4240 0.4737 0.4723 -0.0408 0.0203  0.1808  509 HOH A O   
2250 O  O   . HOH F .   ? 0.6310 0.4625 0.3068 0.0562  -0.0098 0.1650  510 HOH A O   
2251 O  O   . HOH F .   ? 0.2410 0.4165 0.3069 -0.0259 -0.0610 -0.0390 511 HOH A O   
2252 O  O   . HOH F .   ? 0.3754 0.3139 0.1855 -0.0335 0.0012  -0.0158 512 HOH A O   
2253 O  O   . HOH F .   ? 0.5791 0.4337 0.3151 -0.0026 -0.0334 0.1351  513 HOH A O   
2254 O  O   . HOH F .   ? 0.4027 0.5067 0.3004 -0.0572 -0.0657 -0.0084 514 HOH A O   
2255 O  O   . HOH F .   ? 0.3789 0.5039 0.4510 -0.0687 -0.1076 0.0881  515 HOH A O   
2256 O  O   . HOH F .   ? 0.5152 0.5450 0.3914 0.1797  0.0802  0.1411  516 HOH A O   
2257 O  O   . HOH F .   ? 0.3893 0.4014 0.4301 0.0082  0.0994  0.0641  517 HOH A O   
2258 O  O   . HOH F .   ? 0.3181 0.8396 0.3238 0.0298  -0.0996 0.0659  518 HOH A O   
2259 O  O   . HOH F .   ? 0.2524 0.4625 0.3543 0.0479  -0.0674 0.0498  519 HOH A O   
2260 O  O   . HOH F .   ? 0.4351 0.5294 0.3288 0.1726  0.0966  0.0619  520 HOH A O   
2261 O  O   . HOH F .   ? 0.2861 0.2723 0.2090 0.0244  -0.0597 0.0023  521 HOH A O   
2262 O  O   . HOH F .   ? 0.3252 0.2688 0.2107 0.0212  0.0189  0.0796  522 HOH A O   
2263 O  O   . HOH F .   ? 0.7342 1.0159 0.1694 0.1500  -0.1715 0.0081  523 HOH A O   
2264 O  O   . HOH F .   ? 0.5075 0.3981 0.5160 -0.0739 0.0692  -0.0651 524 HOH A O   
2265 O  O   . HOH F .   ? 0.7795 0.7503 0.3813 0.1937  0.1291  -0.0653 525 HOH A O   
2266 O  O   . HOH F .   ? 0.3764 0.8787 0.3649 -0.0710 0.0594  0.0512  526 HOH A O   
2267 O  O   . HOH F .   ? 0.4989 0.5058 0.2928 -0.0514 0.0425  0.0761  527 HOH A O   
2268 O  O   . HOH F .   ? 0.6712 0.4506 0.2250 0.2943  -0.0818 -0.0186 528 HOH A O   
2269 O  O   . HOH F .   ? 0.4056 0.3907 0.2960 0.1338  -0.1137 0.0330  529 HOH A O   
2270 O  O   . HOH F .   ? 0.3616 0.3107 0.2592 -0.0209 -0.0828 -0.0738 530 HOH A O   
2271 O  O   . HOH F .   ? 0.4225 0.3771 0.2852 -0.0158 -0.1232 -0.0022 531 HOH A O   
2272 O  O   . HOH F .   ? 0.2671 0.3362 0.3281 0.0368  -0.0203 -0.0540 532 HOH A O   
2273 O  O   . HOH F .   ? 0.4393 0.4568 0.2863 0.1538  0.0447  0.1449  533 HOH A O   
2274 O  O   . HOH F .   ? 0.4010 0.3776 0.4204 0.0933  -0.0740 -0.0602 534 HOH A O   
2275 O  O   . HOH F .   ? 0.5343 0.6957 0.4364 0.0980  0.0685  0.2572  535 HOH A O   
2276 O  O   . HOH F .   ? 0.2592 0.4127 0.2782 0.0727  -0.0036 0.0383  536 HOH A O   
2277 O  O   . HOH F .   ? 0.2744 0.5318 0.3396 -0.0346 -0.0718 -0.1261 537 HOH A O   
2278 O  O   . HOH F .   ? 0.2824 0.5394 0.3474 0.0551  -0.0072 0.0181  538 HOH A O   
2279 O  O   . HOH F .   ? 0.4603 0.2921 0.4713 0.0656  -0.2234 -0.0465 539 HOH A O   
2280 O  O   . HOH F .   ? 0.2165 0.3127 0.1918 -0.0069 -0.0851 0.0604  540 HOH A O   
2281 O  O   . HOH F .   ? 0.3371 0.2983 0.4708 -0.1318 0.0262  -0.1439 541 HOH A O   
2282 O  O   . HOH F .   ? 0.2898 0.1701 0.2476 -0.0129 -0.0498 -0.0092 542 HOH A O   
2283 O  O   . HOH F .   ? 0.5722 0.5183 0.3186 -0.1720 -0.1273 -0.0165 543 HOH A O   
2284 O  O   . HOH F .   ? 0.3738 0.3217 0.3269 0.1043  -0.0685 -0.0736 544 HOH A O   
2285 O  O   . HOH F .   ? 0.5318 0.4788 0.2700 -0.0320 0.0701  -0.1087 545 HOH A O   
2286 O  O   . HOH F .   ? 0.4040 0.4495 0.7736 -0.0631 -0.0785 0.2676  546 HOH A O   
2287 O  O   . HOH F .   ? 0.3933 0.4115 0.2377 0.0060  -0.0250 -0.0760 547 HOH A O   
2288 O  O   . HOH F .   ? 0.5074 0.3267 0.2972 -0.0281 -0.0677 -0.1071 548 HOH A O   
2289 O  O   . HOH F .   ? 0.5250 0.2723 0.3693 0.0528  -0.0152 0.0747  549 HOH A O   
2290 O  O   . HOH F .   ? 0.4960 0.2949 0.3291 0.0717  0.0912  0.0308  550 HOH A O   
2291 O  O   . HOH F .   ? 0.3827 0.3383 0.2496 0.0996  -0.0442 0.0557  551 HOH A O   
2292 O  O   . HOH F .   ? 0.4855 0.7905 0.5118 0.0795  -0.0106 0.3405  552 HOH A O   
2293 O  O   . HOH F .   ? 0.7403 0.4529 0.8501 0.0373  -0.3926 0.0139  553 HOH A O   
2294 O  O   . HOH F .   ? 0.7647 0.5045 0.3208 0.2036  -0.1210 0.0151  554 HOH A O   
2295 O  O   . HOH F .   ? 0.3298 0.3328 0.4750 0.1100  -0.0484 0.0825  555 HOH A O   
2296 O  O   . HOH F .   ? 0.4618 0.2958 0.3745 -0.0234 -0.1531 -0.0094 556 HOH A O   
2297 O  O   . HOH F .   ? 0.7675 0.4244 0.2291 0.2244  -0.0930 -0.0249 557 HOH A O   
2298 O  O   . HOH F .   ? 0.6358 0.3963 0.3248 0.1632  -0.0439 0.0433  558 HOH A O   
2299 O  O   . HOH F .   ? 0.3016 0.4050 0.5424 0.0084  -0.0054 -0.0785 559 HOH A O   
2300 O  O   . HOH F .   ? 0.5790 0.8190 0.2670 0.1483  -0.0234 -0.0604 560 HOH A O   
2301 O  O   . HOH F .   ? 0.2264 0.1911 0.1688 0.0010  -0.0458 -0.0042 561 HOH A O   
2302 O  O   . HOH F .   ? 0.6368 0.3313 0.4099 -0.0009 -0.0810 0.0824  562 HOH A O   
2303 O  O   . HOH F .   ? 0.3512 0.4020 1.0260 -0.0231 0.0993  0.1154  563 HOH A O   
2304 O  O   . HOH F .   ? 0.7680 0.3659 0.4984 0.1388  -0.3100 -0.1052 564 HOH A O   
2305 O  O   . HOH F .   ? 0.3400 0.3999 0.5744 0.0677  -0.1081 -0.1245 565 HOH A O   
2306 O  O   . HOH F .   ? 0.2933 0.3573 0.3229 0.0453  -0.1236 0.0234  566 HOH A O   
2307 O  O   . HOH F .   ? 0.5107 0.1938 0.3125 0.0695  -0.0066 -0.0121 567 HOH A O   
2308 O  O   . HOH F .   ? 0.7263 0.3605 0.4424 -0.0505 0.1283  -0.0930 568 HOH A O   
2309 O  O   . HOH F .   ? 0.3842 0.4953 0.7345 -0.0748 -0.1070 0.0945  569 HOH A O   
2310 O  O   . HOH F .   ? 0.5764 0.5497 0.2683 -0.0144 0.0256  -0.0436 570 HOH A O   
2311 O  O   . HOH F .   ? 0.2555 0.2745 0.2958 -0.0052 -0.0476 -0.0024 571 HOH A O   
2312 O  O   . HOH F .   ? 0.4243 0.6222 0.3389 -0.0149 -0.0345 -0.0015 572 HOH A O   
2313 O  O   . HOH F .   ? 0.4822 0.7033 0.5498 0.1032  0.0585  -0.0930 573 HOH A O   
2314 O  O   . HOH F .   ? 0.9355 0.7058 0.1938 0.0501  0.0205  0.1822  574 HOH A O   
2315 O  O   . HOH F .   ? 0.4895 0.3963 0.4011 0.0015  -0.0450 -0.0094 575 HOH A O   
2316 O  O   . HOH F .   ? 0.6240 0.3513 0.2957 0.0316  0.0840  0.0599  576 HOH A O   
2317 O  O   . HOH F .   ? 0.4167 0.6204 0.2601 -0.0462 0.0229  0.1962  577 HOH A O   
2318 O  O   . HOH F .   ? 0.7591 0.6272 0.3355 0.0035  -0.1634 0.0751  578 HOH A O   
2319 O  O   . HOH F .   ? 0.5605 0.5289 0.2446 0.2265  0.0862  0.1131  579 HOH A O   
2320 O  O   . HOH F .   ? 0.4370 0.3186 0.4022 0.0333  -0.2408 0.0103  580 HOH A O   
2321 O  O   . HOH F .   ? 0.4852 1.0001 0.6109 0.1061  -0.1003 -0.0472 581 HOH A O   
2322 O  O   . HOH F .   ? 0.4209 0.5870 0.3763 0.0388  -0.1016 -0.0848 582 HOH A O   
2323 O  O   . HOH F .   ? 0.3560 0.2900 0.3043 -0.0649 -0.1439 0.0021  583 HOH A O   
2324 O  O   . HOH F .   ? 0.5197 0.4365 0.6067 0.0646  0.0791  0.0152  584 HOH A O   
2325 O  O   . HOH F .   ? 0.4060 0.6115 0.3890 0.1745  0.0087  0.0247  585 HOH A O   
2326 O  O   . HOH F .   ? 0.4937 0.5855 0.6131 0.2689  0.1814  0.2675  586 HOH A O   
2327 O  O   . HOH F .   ? 0.5092 0.5165 0.7421 -0.1356 0.0352  -0.0757 587 HOH A O   
2328 O  O   . HOH F .   ? 0.5979 0.3208 0.3919 -0.0343 -0.1808 0.0592  588 HOH A O   
2329 O  O   . HOH F .   ? 0.5719 0.6734 0.4022 0.1576  -0.1209 -0.0491 589 HOH A O   
2330 O  O   . HOH F .   ? 0.4150 0.5580 0.6446 -0.1089 -0.0359 0.0844  590 HOH A O   
2331 O  O   . HOH F .   ? 0.8097 0.5725 0.4213 -0.2244 0.1191  0.0917  591 HOH A O   
2332 O  O   . HOH F .   ? 0.5447 0.4491 0.3718 0.0505  -0.0161 0.0585  592 HOH A O   
2333 O  O   . HOH F .   ? 0.5581 0.5104 0.2180 -0.0747 -0.0306 -0.0067 593 HOH A O   
2334 O  O   . HOH F .   ? 0.5381 0.5979 0.3564 -0.0368 0.0609  0.1720  594 HOH A O   
2335 O  O   . HOH F .   ? 0.4584 0.4948 0.5781 -0.0062 -0.1083 -0.1135 595 HOH A O   
2336 O  O   . HOH F .   ? 0.4057 0.6398 0.4597 0.0806  -0.0691 0.0061  596 HOH A O   
2337 O  O   . HOH F .   ? 0.5736 0.6090 0.8416 0.1912  0.1341  0.0201  597 HOH A O   
2338 O  O   . HOH F .   ? 0.3397 0.3260 0.5738 -0.0369 0.0309  -0.1038 598 HOH A O   
2339 O  O   . HOH F .   ? 0.4177 0.4448 0.5845 0.1251  -0.1130 0.0335  599 HOH A O   
2340 O  O   . HOH F .   ? 0.3960 0.7215 0.7850 0.1433  0.0593  0.1729  600 HOH A O   
2341 O  O   . HOH F .   ? 0.3961 0.6722 0.3766 -0.1002 -0.0636 -0.0036 601 HOH A O   
2342 O  O   . HOH F .   ? 0.5699 0.5826 0.5612 0.1292  -0.0526 0.2643  602 HOH A O   
2343 O  O   . HOH F .   ? 0.6091 0.4395 0.6135 0.1406  -0.1630 -0.1612 603 HOH A O   
2344 O  O   . HOH F .   ? 0.4501 0.6170 0.3537 -0.0333 -0.0333 0.0666  604 HOH A O   
2345 O  O   . HOH F .   ? 0.4299 0.5001 0.6208 -0.0595 -0.2228 -0.0489 605 HOH A O   
2346 O  O   . HOH F .   ? 0.4383 0.7729 0.6772 0.1603  -0.0157 0.2537  606 HOH A O   
2347 O  O   . HOH F .   ? 0.6607 0.5316 0.4837 -0.0655 -0.1680 -0.1411 607 HOH A O   
2348 O  O   . HOH F .   ? 0.4571 0.3617 0.5669 0.0004  -0.1599 -0.0336 608 HOH A O   
2349 O  O   . HOH F .   ? 0.3541 0.2912 0.2543 0.0507  -0.0653 0.0266  609 HOH A O   
2350 O  O   . HOH F .   ? 0.4766 0.5223 0.5635 -0.0272 0.0043  0.0392  610 HOH A O   
2351 O  O   . HOH F .   ? 0.5742 0.9053 0.4194 -0.0384 -0.1359 -0.0361 611 HOH A O   
2352 O  O   . HOH F .   ? 0.4189 0.4300 0.4110 -0.0134 0.0502  0.1575  612 HOH A O   
2353 O  O   . HOH F .   ? 0.4989 0.6746 0.6397 0.2806  -0.0897 0.0087  613 HOH A O   
2354 O  O   . HOH F .   ? 0.4840 0.5247 0.9979 -0.0308 0.1076  0.2870  614 HOH A O   
2355 O  O   . HOH F .   ? 0.6009 0.4769 0.4693 0.0201  -0.0189 -0.0031 615 HOH A O   
2356 O  O   . HOH F .   ? 0.6918 0.4822 0.5346 0.0220  -0.0866 0.1802  616 HOH A O   
2357 O  O   . HOH F .   ? 0.6940 0.6146 0.5343 0.0223  0.0236  -0.1989 617 HOH A O   
2358 O  O   . HOH F .   ? 0.3388 0.4509 0.5431 -0.0189 -0.0697 0.0286  618 HOH A O   
2359 O  O   . HOH F .   ? 0.5626 0.3698 0.5614 0.0482  0.1150  0.0386  619 HOH A O   
2360 O  O   . HOH F .   ? 0.4739 0.5773 0.4737 0.0195  -0.1080 0.1776  620 HOH A O   
2361 O  O   . HOH F .   ? 0.4266 0.4703 0.8547 -0.1063 -0.2662 -0.0089 621 HOH A O   
2362 O  O   . HOH F .   ? 0.4230 0.9025 0.4444 -0.0232 -0.1140 -0.0176 622 HOH A O   
2363 O  O   . HOH F .   ? 0.3797 0.3908 0.2758 0.0153  -0.0758 -0.0606 623 HOH A O   
2364 O  O   . HOH F .   ? 0.4431 0.2945 0.5973 -0.0586 0.1068  -0.0006 624 HOH A O   
2365 O  O   . HOH F .   ? 0.6319 0.4816 0.4711 -0.2418 -0.0132 0.0935  625 HOH A O   
2366 O  O   . HOH F .   ? 0.5035 0.4762 0.5043 -0.1301 0.0469  -0.0165 626 HOH A O   
2367 O  O   . HOH F .   ? 0.4117 0.5306 0.5600 -0.0522 0.0037  -0.2390 627 HOH A O   
2368 O  O   . HOH F .   ? 0.5963 0.5150 0.6797 0.0084  0.1597  0.2105  628 HOH A O   
2369 O  O   . HOH F .   ? 0.3849 0.6430 0.6225 -0.0523 -0.1222 0.1502  629 HOH A O   
# 
