data_8VAU
# 
_entry.id   8VAU 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.399 
_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   8VAU         pdb_00008vau 10.2210/pdb8vau/pdb 
WWPDB D_1000279585 ?            ?                   
# 
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 2024-11-06 
2 'Structure model' 1 1 2024-12-11 
# 
_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             ? 
# 
_pdbx_audit_revision_group.ordinal             1 
_pdbx_audit_revision_group.revision_ordinal    2 
_pdbx_audit_revision_group.data_content_type   'Structure model' 
_pdbx_audit_revision_group.group               'Database references' 
# 
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 
# 
loop_
_pdbx_audit_revision_item.ordinal 
_pdbx_audit_revision_item.revision_ordinal 
_pdbx_audit_revision_item.data_content_type 
_pdbx_audit_revision_item.item 
1 2 'Structure model' '_citation.journal_volume'          
2 2 'Structure model' '_citation.page_first'              
3 2 'Structure model' '_citation.page_last'               
4 2 'Structure model' '_citation.pdbx_database_id_PubMed' 
5 2 'Structure model' '_citation.title'                   
6 2 'Structure model' '_citation_author.identifier_ORCID' 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        8VAU 
_pdbx_database_status.recvd_initial_deposition_date   2023-12-11 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_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 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              yongz@usc.edu 
_pdbx_contact_author.name_first         Yong 
_pdbx_contact_author.name_last          Zhang 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-3132-8557 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Kao, G.'         1  ?                   
'Zhang, X.N.'     2  ?                   
'Nasertorabi, F.' 3  0000-0001-8563-2899 
'Katz, B.B.'      4  ?                   
'Li, Z.'          5  ?                   
'Dai, Z.'         6  ?                   
'Zhang, Z.'       7  ?                   
'Zhang, L.'       8  ?                   
'Louie, S.G.'     9  ?                   
'Cherezov, V.'    10 ?                   
'Zhang, Y.'       11 0000-0002-3132-8557 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   US 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'Jacs Au' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            ? 
_citation.journal_id_ISSN           2691-3704 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            4 
_citation.language                  ? 
_citation.page_first                4345 
_citation.page_last                 4360 
_citation.title                     'Nicotinamide Riboside and CD38: Covalent Inhibition and Live-Cell Labeling.' 
_citation.year                      2024 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1021/jacsau.4c00695 
_citation.pdbx_database_id_PubMed   39610739 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Kao, G.'         1  ? 
primary 'Zhang, X.N.'     2  ? 
primary 'Nasertorabi, F.' 3  ? 
primary 'Katz, B.B.'      4  ? 
primary 'Li, Z.'          5  ? 
primary 'Dai, Z.'         6  ? 
primary 'Zhang, Z.'       7  ? 
primary 'Zhang, L.'       8  ? 
primary 'Louie, S.G.'     9  ? 
primary 'Cherezov, V.'    10 ? 
primary 'Zhang, Y.'       11 ? 
# 
loop_
_entity.id 
_entity.type 
_entity.src_method 
_entity.pdbx_description 
_entity.formula_weight 
_entity.pdbx_number_of_molecules 
_entity.pdbx_ec 
_entity.pdbx_mutation 
_entity.pdbx_fragment 
_entity.details 
1 polymer     man 'ADP-ribosyl cyclase/cyclic ADP-ribose hydrolase 1' 29763.738 2   3.2.2.6,2.4.99.20 'N100D, N164A, N209D, N219D' 
? ? 
2 non-polymer nat 'Nicotinamide riboside'                             255.247   2   ?                 ?                            
? ? 
3 non-polymer syn alpha-D-ribofuranose                                150.130   2   ?                 ?                            
? ? 
4 water       nat water                                               18.015    300 ?                 ?                            
? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        
;2'-phospho-ADP-ribosyl cyclase,2'-phospho-ADP-ribosyl cyclase/2'-phospho-cyclic-ADP-ribose transferase,2'-phospho-cyclic-ADP-ribose transferase,ADP-ribosyl cyclase 1,ADPRC 1,Cyclic ADP-ribose hydrolase 1,cADPr hydrolase 1,T10
;
# 
_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       
;SRWRQQWSGPGTTKRFPETVLARCVKYTEIHPEMRHVDCQSVWDAFKGAFISKHPCDITEEDYQPLMKLGTQTVPCNKIL
LWSRIKDLAHQFTQVQRDMFTLEDTLLGYLADDLTWCGEFATSKINYQSCPDWRKDCSNNPVSVFWKTVSRRFAEAACDV
VHVMLDGSRSKIFDKDSTFGSVEVHNLQPEKVQTLEAWVIHGGREDSRDLCQDPTIKELESIISKRNIQFSCKNIYRPDK
FLQCVKNPEDSSCTSEI
;
_entity_poly.pdbx_seq_one_letter_code_can   
;SRWRQQWSGPGTTKRFPETVLARCVKYTEIHPEMRHVDCQSVWDAFKGAFISKHPCDITEEDYQPLMKLGTQTVPCNKIL
LWSRIKDLAHQFTQVQRDMFTLEDTLLGYLADDLTWCGEFATSKINYQSCPDWRKDCSNNPVSVFWKTVSRRFAEAACDV
VHVMLDGSRSKIFDKDSTFGSVEVHNLQPEKVQTLEAWVIHGGREDSRDLCQDPTIKELESIISKRNIQFSCKNIYRPDK
FLQCVKNPEDSSCTSEI
;
_entity_poly.pdbx_strand_id                 A,B 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 'Nicotinamide riboside' NNR 
3 alpha-D-ribofuranose    RIB 
4 water                   HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   SER n 
1 2   ARG n 
1 3   TRP n 
1 4   ARG n 
1 5   GLN n 
1 6   GLN n 
1 7   TRP n 
1 8   SER n 
1 9   GLY n 
1 10  PRO n 
1 11  GLY n 
1 12  THR n 
1 13  THR n 
1 14  LYS n 
1 15  ARG n 
1 16  PHE n 
1 17  PRO n 
1 18  GLU n 
1 19  THR n 
1 20  VAL n 
1 21  LEU n 
1 22  ALA n 
1 23  ARG n 
1 24  CYS n 
1 25  VAL n 
1 26  LYS n 
1 27  TYR n 
1 28  THR n 
1 29  GLU n 
1 30  ILE n 
1 31  HIS n 
1 32  PRO n 
1 33  GLU n 
1 34  MET n 
1 35  ARG n 
1 36  HIS n 
1 37  VAL n 
1 38  ASP n 
1 39  CYS n 
1 40  GLN n 
1 41  SER n 
1 42  VAL n 
1 43  TRP n 
1 44  ASP n 
1 45  ALA n 
1 46  PHE n 
1 47  LYS n 
1 48  GLY n 
1 49  ALA n 
1 50  PHE n 
1 51  ILE n 
1 52  SER n 
1 53  LYS n 
1 54  HIS n 
1 55  PRO n 
1 56  CYS n 
1 57  ASP n 
1 58  ILE n 
1 59  THR n 
1 60  GLU n 
1 61  GLU n 
1 62  ASP n 
1 63  TYR n 
1 64  GLN n 
1 65  PRO n 
1 66  LEU n 
1 67  MET n 
1 68  LYS n 
1 69  LEU n 
1 70  GLY n 
1 71  THR n 
1 72  GLN n 
1 73  THR n 
1 74  VAL n 
1 75  PRO n 
1 76  CYS n 
1 77  ASN n 
1 78  LYS n 
1 79  ILE n 
1 80  LEU n 
1 81  LEU n 
1 82  TRP n 
1 83  SER n 
1 84  ARG n 
1 85  ILE n 
1 86  LYS n 
1 87  ASP n 
1 88  LEU n 
1 89  ALA n 
1 90  HIS n 
1 91  GLN n 
1 92  PHE n 
1 93  THR n 
1 94  GLN n 
1 95  VAL n 
1 96  GLN n 
1 97  ARG n 
1 98  ASP n 
1 99  MET n 
1 100 PHE n 
1 101 THR n 
1 102 LEU n 
1 103 GLU n 
1 104 ASP n 
1 105 THR n 
1 106 LEU n 
1 107 LEU n 
1 108 GLY n 
1 109 TYR n 
1 110 LEU n 
1 111 ALA n 
1 112 ASP n 
1 113 ASP n 
1 114 LEU n 
1 115 THR n 
1 116 TRP n 
1 117 CYS n 
1 118 GLY n 
1 119 GLU n 
1 120 PHE n 
1 121 ALA n 
1 122 THR n 
1 123 SER n 
1 124 LYS n 
1 125 ILE n 
1 126 ASN n 
1 127 TYR n 
1 128 GLN n 
1 129 SER n 
1 130 CYS n 
1 131 PRO n 
1 132 ASP n 
1 133 TRP n 
1 134 ARG n 
1 135 LYS n 
1 136 ASP n 
1 137 CYS n 
1 138 SER n 
1 139 ASN n 
1 140 ASN n 
1 141 PRO n 
1 142 VAL n 
1 143 SER n 
1 144 VAL n 
1 145 PHE n 
1 146 TRP n 
1 147 LYS n 
1 148 THR n 
1 149 VAL n 
1 150 SER n 
1 151 ARG n 
1 152 ARG n 
1 153 PHE n 
1 154 ALA n 
1 155 GLU n 
1 156 ALA n 
1 157 ALA n 
1 158 CYS n 
1 159 ASP n 
1 160 VAL n 
1 161 VAL n 
1 162 HIS n 
1 163 VAL n 
1 164 MET n 
1 165 LEU n 
1 166 ASP n 
1 167 GLY n 
1 168 SER n 
1 169 ARG n 
1 170 SER n 
1 171 LYS n 
1 172 ILE n 
1 173 PHE n 
1 174 ASP n 
1 175 LYS n 
1 176 ASP n 
1 177 SER n 
1 178 THR n 
1 179 PHE n 
1 180 GLY n 
1 181 SER n 
1 182 VAL n 
1 183 GLU n 
1 184 VAL n 
1 185 HIS n 
1 186 ASN n 
1 187 LEU n 
1 188 GLN n 
1 189 PRO n 
1 190 GLU n 
1 191 LYS n 
1 192 VAL n 
1 193 GLN n 
1 194 THR n 
1 195 LEU n 
1 196 GLU n 
1 197 ALA n 
1 198 TRP n 
1 199 VAL n 
1 200 ILE n 
1 201 HIS n 
1 202 GLY n 
1 203 GLY n 
1 204 ARG n 
1 205 GLU n 
1 206 ASP n 
1 207 SER n 
1 208 ARG n 
1 209 ASP n 
1 210 LEU n 
1 211 CYS n 
1 212 GLN n 
1 213 ASP n 
1 214 PRO n 
1 215 THR n 
1 216 ILE n 
1 217 LYS n 
1 218 GLU n 
1 219 LEU n 
1 220 GLU n 
1 221 SER n 
1 222 ILE n 
1 223 ILE n 
1 224 SER n 
1 225 LYS n 
1 226 ARG n 
1 227 ASN n 
1 228 ILE n 
1 229 GLN n 
1 230 PHE n 
1 231 SER n 
1 232 CYS n 
1 233 LYS n 
1 234 ASN n 
1 235 ILE n 
1 236 TYR n 
1 237 ARG n 
1 238 PRO n 
1 239 ASP n 
1 240 LYS n 
1 241 PHE n 
1 242 LEU n 
1 243 GLN n 
1 244 CYS n 
1 245 VAL n 
1 246 LYS n 
1 247 ASN n 
1 248 PRO n 
1 249 GLU n 
1 250 ASP n 
1 251 SER n 
1 252 SER n 
1 253 CYS n 
1 254 THR n 
1 255 SER n 
1 256 GLU n 
1 257 ILE 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                   257 
_entity_src_gen.gene_src_common_name               human 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 CD38 
_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      'Homo sapiens' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     9606 
_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            HEK293 
_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                       pFuse 
_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 
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 
NNR non-polymer                   . 'Nicotinamide riboside' '3-(aminocarbonyl)-1-beta-D-ribofuranosylpyridinium' 'C11 H15 N2 O5 1' 
255.247 
PHE 'L-peptide linking'           y PHENYLALANINE           ?                                                    'C9 H11 N O2'     
165.189 
PRO 'L-peptide linking'           y PROLINE                 ?                                                    'C5 H9 N O2'      
115.130 
RIB 'D-saccharide, alpha linking' . alpha-D-ribofuranose    'alpha-D-ribose; D-ribose; ribose'                   'C5 H10 O5'       
150.130 
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 
# 
loop_
_pdbx_chem_comp_identifier.comp_id 
_pdbx_chem_comp_identifier.type 
_pdbx_chem_comp_identifier.program 
_pdbx_chem_comp_identifier.program_version 
_pdbx_chem_comp_identifier.identifier 
RIB 'CONDENSED IUPAC CARBOHYDRATE SYMBOL' GMML     1.0 DRibfa           
RIB 'COMMON NAME'                         GMML     1.0 a-D-ribofuranose 
RIB 'IUPAC CARBOHYDRATE SYMBOL'           PDB-CARE 1.0 a-D-Ribf         
RIB 'SNFG CARBOHYDRATE SYMBOL'            GMML     1.0 Rib              
# 
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   SER 1   44  44  SER SER A . n 
A 1 2   ARG 2   45  45  ARG ARG A . n 
A 1 3   TRP 3   46  46  TRP TRP A . n 
A 1 4   ARG 4   47  47  ARG ARG A . n 
A 1 5   GLN 5   48  48  GLN GLN A . n 
A 1 6   GLN 6   49  49  GLN GLN A . n 
A 1 7   TRP 7   50  50  TRP TRP A . n 
A 1 8   SER 8   51  51  SER SER A . n 
A 1 9   GLY 9   52  52  GLY GLY A . n 
A 1 10  PRO 10  53  53  PRO PRO A . n 
A 1 11  GLY 11  54  54  GLY GLY A . n 
A 1 12  THR 12  55  55  THR THR A . n 
A 1 13  THR 13  56  56  THR THR A . n 
A 1 14  LYS 14  57  57  LYS LYS A . n 
A 1 15  ARG 15  58  58  ARG ARG A . n 
A 1 16  PHE 16  59  59  PHE PHE A . n 
A 1 17  PRO 17  60  60  PRO PRO A . n 
A 1 18  GLU 18  61  61  GLU GLU A . n 
A 1 19  THR 19  62  62  THR THR A . n 
A 1 20  VAL 20  63  63  VAL VAL A . n 
A 1 21  LEU 21  64  64  LEU LEU A . n 
A 1 22  ALA 22  65  65  ALA ALA A . n 
A 1 23  ARG 23  66  66  ARG ARG A . n 
A 1 24  CYS 24  67  67  CYS CYS A . n 
A 1 25  VAL 25  68  68  VAL VAL A . n 
A 1 26  LYS 26  69  69  LYS LYS A . n 
A 1 27  TYR 27  70  70  TYR TYR A . n 
A 1 28  THR 28  71  71  THR THR A . n 
A 1 29  GLU 29  72  72  GLU GLU A . n 
A 1 30  ILE 30  73  73  ILE ILE A . n 
A 1 31  HIS 31  74  74  HIS HIS A . n 
A 1 32  PRO 32  75  75  PRO PRO A . n 
A 1 33  GLU 33  76  76  GLU GLU A . n 
A 1 34  MET 34  77  77  MET MET A . n 
A 1 35  ARG 35  78  78  ARG ARG A . n 
A 1 36  HIS 36  79  79  HIS HIS A . n 
A 1 37  VAL 37  80  80  VAL VAL A . n 
A 1 38  ASP 38  81  81  ASP ASP A . n 
A 1 39  CYS 39  82  82  CYS CYS A . n 
A 1 40  GLN 40  83  83  GLN GLN A . n 
A 1 41  SER 41  84  84  SER SER A . n 
A 1 42  VAL 42  85  85  VAL VAL A . n 
A 1 43  TRP 43  86  86  TRP TRP A . n 
A 1 44  ASP 44  87  87  ASP ASP A . n 
A 1 45  ALA 45  88  88  ALA ALA A . n 
A 1 46  PHE 46  89  89  PHE PHE A . n 
A 1 47  LYS 47  90  90  LYS LYS A . n 
A 1 48  GLY 48  91  91  GLY GLY A . n 
A 1 49  ALA 49  92  92  ALA ALA A . n 
A 1 50  PHE 50  93  93  PHE PHE A . n 
A 1 51  ILE 51  94  94  ILE ILE A . n 
A 1 52  SER 52  95  95  SER SER A . n 
A 1 53  LYS 53  96  96  LYS LYS A . n 
A 1 54  HIS 54  97  97  HIS HIS A . n 
A 1 55  PRO 55  98  98  PRO PRO A . n 
A 1 56  CYS 56  99  99  CYS CYS A . n 
A 1 57  ASP 57  100 100 ASP ASP A . n 
A 1 58  ILE 58  101 101 ILE ILE A . n 
A 1 59  THR 59  102 102 THR THR A . n 
A 1 60  GLU 60  103 103 GLU GLU A . n 
A 1 61  GLU 61  104 104 GLU GLU A . n 
A 1 62  ASP 62  105 105 ASP ASP A . n 
A 1 63  TYR 63  106 106 TYR TYR A . n 
A 1 64  GLN 64  107 107 GLN GLN A . n 
A 1 65  PRO 65  108 108 PRO PRO A . n 
A 1 66  LEU 66  109 109 LEU LEU A . n 
A 1 67  MET 67  110 110 MET MET A . n 
A 1 68  LYS 68  111 111 LYS LYS A . n 
A 1 69  LEU 69  112 112 LEU LEU A . n 
A 1 70  GLY 70  113 113 GLY GLY A . n 
A 1 71  THR 71  114 114 THR THR A . n 
A 1 72  GLN 72  115 115 GLN GLN A . n 
A 1 73  THR 73  116 116 THR THR A . n 
A 1 74  VAL 74  117 117 VAL VAL A . n 
A 1 75  PRO 75  118 118 PRO PRO A . n 
A 1 76  CYS 76  119 119 CYS CYS A . n 
A 1 77  ASN 77  120 120 ASN ASN A . n 
A 1 78  LYS 78  121 121 LYS LYS A . n 
A 1 79  ILE 79  122 122 ILE ILE A . n 
A 1 80  LEU 80  123 123 LEU LEU A . n 
A 1 81  LEU 81  124 124 LEU LEU A . n 
A 1 82  TRP 82  125 125 TRP TRP A . n 
A 1 83  SER 83  126 126 SER SER A . n 
A 1 84  ARG 84  127 127 ARG ARG A . n 
A 1 85  ILE 85  128 128 ILE ILE A . n 
A 1 86  LYS 86  129 129 LYS LYS A . n 
A 1 87  ASP 87  130 130 ASP ASP A . n 
A 1 88  LEU 88  131 131 LEU LEU A . n 
A 1 89  ALA 89  132 132 ALA ALA A . n 
A 1 90  HIS 90  133 133 HIS HIS A . n 
A 1 91  GLN 91  134 134 GLN GLN A . n 
A 1 92  PHE 92  135 135 PHE PHE A . n 
A 1 93  THR 93  136 136 THR THR A . n 
A 1 94  GLN 94  137 137 GLN GLN A . n 
A 1 95  VAL 95  138 138 VAL VAL A . n 
A 1 96  GLN 96  139 139 GLN GLN A . n 
A 1 97  ARG 97  140 140 ARG ARG A . n 
A 1 98  ASP 98  141 141 ASP ASP A . n 
A 1 99  MET 99  142 142 MET MET A . n 
A 1 100 PHE 100 143 143 PHE PHE A . n 
A 1 101 THR 101 144 144 THR THR A . n 
A 1 102 LEU 102 145 145 LEU LEU A . n 
A 1 103 GLU 103 146 146 GLU GLU A . n 
A 1 104 ASP 104 147 147 ASP ASP A . n 
A 1 105 THR 105 148 148 THR THR A . n 
A 1 106 LEU 106 149 149 LEU LEU A . n 
A 1 107 LEU 107 150 150 LEU LEU A . n 
A 1 108 GLY 108 151 151 GLY GLY A . n 
A 1 109 TYR 109 152 152 TYR TYR A . n 
A 1 110 LEU 110 153 153 LEU LEU A . n 
A 1 111 ALA 111 154 154 ALA ALA A . n 
A 1 112 ASP 112 155 155 ASP ASP A . n 
A 1 113 ASP 113 156 156 ASP ASP A . n 
A 1 114 LEU 114 157 157 LEU LEU A . n 
A 1 115 THR 115 158 158 THR THR A . n 
A 1 116 TRP 116 159 159 TRP TRP A . n 
A 1 117 CYS 117 160 160 CYS CYS A . n 
A 1 118 GLY 118 161 161 GLY GLY A . n 
A 1 119 GLU 119 162 162 GLU GLU A . n 
A 1 120 PHE 120 163 163 PHE PHE A . n 
A 1 121 ALA 121 164 164 ALA ALA A . n 
A 1 122 THR 122 165 165 THR THR A . n 
A 1 123 SER 123 166 166 SER SER A . n 
A 1 124 LYS 124 167 167 LYS LYS A . n 
A 1 125 ILE 125 168 168 ILE ILE A . n 
A 1 126 ASN 126 169 169 ASN ASN A . n 
A 1 127 TYR 127 170 170 TYR TYR A . n 
A 1 128 GLN 128 171 171 GLN GLN A . n 
A 1 129 SER 129 172 172 SER SER A . n 
A 1 130 CYS 130 173 173 CYS CYS A . n 
A 1 131 PRO 131 174 174 PRO PRO A . n 
A 1 132 ASP 132 175 175 ASP ASP A . n 
A 1 133 TRP 133 176 176 TRP TRP A . n 
A 1 134 ARG 134 177 177 ARG ARG A . n 
A 1 135 LYS 135 178 178 LYS LYS A . n 
A 1 136 ASP 136 179 179 ASP ASP A . n 
A 1 137 CYS 137 180 180 CYS CYS A . n 
A 1 138 SER 138 181 181 SER SER A . n 
A 1 139 ASN 139 182 182 ASN ASN A . n 
A 1 140 ASN 140 183 183 ASN ASN A . n 
A 1 141 PRO 141 184 184 PRO PRO A . n 
A 1 142 VAL 142 185 185 VAL VAL A . n 
A 1 143 SER 143 186 186 SER SER A . n 
A 1 144 VAL 144 187 187 VAL VAL A . n 
A 1 145 PHE 145 188 188 PHE PHE A . n 
A 1 146 TRP 146 189 189 TRP TRP A . n 
A 1 147 LYS 147 190 190 LYS LYS A . n 
A 1 148 THR 148 191 191 THR THR A . n 
A 1 149 VAL 149 192 192 VAL VAL A . n 
A 1 150 SER 150 193 193 SER SER A . n 
A 1 151 ARG 151 194 194 ARG ARG A . n 
A 1 152 ARG 152 195 195 ARG ARG A . n 
A 1 153 PHE 153 196 196 PHE PHE A . n 
A 1 154 ALA 154 197 197 ALA ALA A . n 
A 1 155 GLU 155 198 198 GLU GLU A . n 
A 1 156 ALA 156 199 199 ALA ALA A . n 
A 1 157 ALA 157 200 200 ALA ALA A . n 
A 1 158 CYS 158 201 201 CYS CYS A . n 
A 1 159 ASP 159 202 202 ASP ASP A . n 
A 1 160 VAL 160 203 203 VAL VAL A . n 
A 1 161 VAL 161 204 204 VAL VAL A . n 
A 1 162 HIS 162 205 205 HIS HIS A . n 
A 1 163 VAL 163 206 206 VAL VAL A . n 
A 1 164 MET 164 207 207 MET MET A . n 
A 1 165 LEU 165 208 208 LEU LEU A . n 
A 1 166 ASP 166 209 209 ASP ASP A . n 
A 1 167 GLY 167 210 210 GLY GLY A . n 
A 1 168 SER 168 211 211 SER SER A . n 
A 1 169 ARG 169 212 212 ARG ARG A . n 
A 1 170 SER 170 213 213 SER SER A . n 
A 1 171 LYS 171 214 214 LYS LYS A . n 
A 1 172 ILE 172 215 215 ILE ILE A . n 
A 1 173 PHE 173 216 216 PHE PHE A . n 
A 1 174 ASP 174 217 217 ASP ASP A . n 
A 1 175 LYS 175 218 218 LYS LYS A . n 
A 1 176 ASP 176 219 219 ASP ASP A . n 
A 1 177 SER 177 220 220 SER SER A . n 
A 1 178 THR 178 221 221 THR THR A . n 
A 1 179 PHE 179 222 222 PHE PHE A . n 
A 1 180 GLY 180 223 223 GLY GLY A . n 
A 1 181 SER 181 224 224 SER SER A . n 
A 1 182 VAL 182 225 225 VAL VAL A . n 
A 1 183 GLU 183 226 226 GLU GLU A . n 
A 1 184 VAL 184 227 227 VAL VAL A . n 
A 1 185 HIS 185 228 228 HIS HIS A . n 
A 1 186 ASN 186 229 229 ASN ASN A . n 
A 1 187 LEU 187 230 230 LEU LEU A . n 
A 1 188 GLN 188 231 231 GLN GLN A . n 
A 1 189 PRO 189 232 232 PRO PRO A . n 
A 1 190 GLU 190 233 233 GLU GLU A . n 
A 1 191 LYS 191 234 234 LYS LYS A . n 
A 1 192 VAL 192 235 235 VAL VAL A . n 
A 1 193 GLN 193 236 236 GLN GLN A . n 
A 1 194 THR 194 237 237 THR THR A . n 
A 1 195 LEU 195 238 238 LEU LEU A . n 
A 1 196 GLU 196 239 239 GLU GLU A . n 
A 1 197 ALA 197 240 240 ALA ALA A . n 
A 1 198 TRP 198 241 241 TRP TRP A . n 
A 1 199 VAL 199 242 242 VAL VAL A . n 
A 1 200 ILE 200 243 243 ILE ILE A . n 
A 1 201 HIS 201 244 244 HIS HIS A . n 
A 1 202 GLY 202 245 245 GLY GLY A . n 
A 1 203 GLY 203 246 246 GLY GLY A . n 
A 1 204 ARG 204 247 247 ARG ARG A . n 
A 1 205 GLU 205 248 248 GLU GLU A . n 
A 1 206 ASP 206 249 249 ASP ASP A . n 
A 1 207 SER 207 250 250 SER SER A . n 
A 1 208 ARG 208 251 251 ARG ARG A . n 
A 1 209 ASP 209 252 252 ASP ASP A . n 
A 1 210 LEU 210 253 253 LEU LEU A . n 
A 1 211 CYS 211 254 254 CYS CYS A . n 
A 1 212 GLN 212 255 255 GLN GLN A . n 
A 1 213 ASP 213 256 256 ASP ASP A . n 
A 1 214 PRO 214 257 257 PRO PRO A . n 
A 1 215 THR 215 258 258 THR THR A . n 
A 1 216 ILE 216 259 259 ILE ILE A . n 
A 1 217 LYS 217 260 260 LYS LYS A . n 
A 1 218 GLU 218 261 261 GLU GLU A . n 
A 1 219 LEU 219 262 262 LEU LEU A . n 
A 1 220 GLU 220 263 263 GLU GLU A . n 
A 1 221 SER 221 264 264 SER SER A . n 
A 1 222 ILE 222 265 265 ILE ILE A . n 
A 1 223 ILE 223 266 266 ILE ILE A . n 
A 1 224 SER 224 267 267 SER SER A . n 
A 1 225 LYS 225 268 268 LYS LYS A . n 
A 1 226 ARG 226 269 269 ARG ARG A . n 
A 1 227 ASN 227 270 270 ASN ASN A . n 
A 1 228 ILE 228 271 271 ILE ILE A . n 
A 1 229 GLN 229 272 272 GLN GLN A . n 
A 1 230 PHE 230 273 273 PHE PHE A . n 
A 1 231 SER 231 274 274 SER SER A . n 
A 1 232 CYS 232 275 275 CYS CYS A . n 
A 1 233 LYS 233 276 276 LYS LYS A . n 
A 1 234 ASN 234 277 277 ASN ASN A . n 
A 1 235 ILE 235 278 278 ILE ILE A . n 
A 1 236 TYR 236 279 279 TYR TYR A . n 
A 1 237 ARG 237 280 280 ARG ARG A . n 
A 1 238 PRO 238 281 281 PRO PRO A . n 
A 1 239 ASP 239 282 282 ASP ASP A . n 
A 1 240 LYS 240 283 283 LYS LYS A . n 
A 1 241 PHE 241 284 284 PHE PHE A . n 
A 1 242 LEU 242 285 285 LEU LEU A . n 
A 1 243 GLN 243 286 286 GLN GLN A . n 
A 1 244 CYS 244 287 287 CYS CYS A . n 
A 1 245 VAL 245 288 288 VAL VAL A . n 
A 1 246 LYS 246 289 289 LYS LYS A . n 
A 1 247 ASN 247 290 290 ASN ASN A . n 
A 1 248 PRO 248 291 291 PRO PRO A . n 
A 1 249 GLU 249 292 292 GLU GLU A . n 
A 1 250 ASP 250 293 ?   ?   ?   A . n 
A 1 251 SER 251 294 ?   ?   ?   A . n 
A 1 252 SER 252 295 ?   ?   ?   A . n 
A 1 253 CYS 253 296 ?   ?   ?   A . n 
A 1 254 THR 254 297 ?   ?   ?   A . n 
A 1 255 SER 255 298 ?   ?   ?   A . n 
A 1 256 GLU 256 299 ?   ?   ?   A . n 
A 1 257 ILE 257 300 ?   ?   ?   A . n 
B 1 1   SER 1   44  44  SER SER B . n 
B 1 2   ARG 2   45  45  ARG ARG B . n 
B 1 3   TRP 3   46  46  TRP TRP B . n 
B 1 4   ARG 4   47  47  ARG ARG B . n 
B 1 5   GLN 5   48  48  GLN GLN B . n 
B 1 6   GLN 6   49  49  GLN GLN B . n 
B 1 7   TRP 7   50  50  TRP TRP B . n 
B 1 8   SER 8   51  51  SER SER B . n 
B 1 9   GLY 9   52  52  GLY GLY B . n 
B 1 10  PRO 10  53  53  PRO PRO B . n 
B 1 11  GLY 11  54  54  GLY GLY B . n 
B 1 12  THR 12  55  55  THR THR B . n 
B 1 13  THR 13  56  56  THR THR B . n 
B 1 14  LYS 14  57  57  LYS LYS B . n 
B 1 15  ARG 15  58  58  ARG ARG B . n 
B 1 16  PHE 16  59  59  PHE PHE B . n 
B 1 17  PRO 17  60  60  PRO PRO B . n 
B 1 18  GLU 18  61  61  GLU GLU B . n 
B 1 19  THR 19  62  62  THR THR B . n 
B 1 20  VAL 20  63  63  VAL VAL B . n 
B 1 21  LEU 21  64  64  LEU LEU B . n 
B 1 22  ALA 22  65  65  ALA ALA B . n 
B 1 23  ARG 23  66  66  ARG ARG B . n 
B 1 24  CYS 24  67  67  CYS CYS B . n 
B 1 25  VAL 25  68  68  VAL VAL B . n 
B 1 26  LYS 26  69  69  LYS LYS B . n 
B 1 27  TYR 27  70  70  TYR TYR B . n 
B 1 28  THR 28  71  71  THR THR B . n 
B 1 29  GLU 29  72  72  GLU GLU B . n 
B 1 30  ILE 30  73  73  ILE ILE B . n 
B 1 31  HIS 31  74  74  HIS HIS B . n 
B 1 32  PRO 32  75  75  PRO PRO B . n 
B 1 33  GLU 33  76  76  GLU GLU B . n 
B 1 34  MET 34  77  77  MET MET B . n 
B 1 35  ARG 35  78  78  ARG ARG B . n 
B 1 36  HIS 36  79  79  HIS HIS B . n 
B 1 37  VAL 37  80  80  VAL VAL B . n 
B 1 38  ASP 38  81  81  ASP ASP B . n 
B 1 39  CYS 39  82  82  CYS CYS B . n 
B 1 40  GLN 40  83  83  GLN GLN B . n 
B 1 41  SER 41  84  84  SER SER B . n 
B 1 42  VAL 42  85  85  VAL VAL B . n 
B 1 43  TRP 43  86  86  TRP TRP B . n 
B 1 44  ASP 44  87  87  ASP ASP B . n 
B 1 45  ALA 45  88  88  ALA ALA B . n 
B 1 46  PHE 46  89  89  PHE PHE B . n 
B 1 47  LYS 47  90  90  LYS LYS B . n 
B 1 48  GLY 48  91  91  GLY GLY B . n 
B 1 49  ALA 49  92  92  ALA ALA B . n 
B 1 50  PHE 50  93  93  PHE PHE B . n 
B 1 51  ILE 51  94  94  ILE ILE B . n 
B 1 52  SER 52  95  95  SER SER B . n 
B 1 53  LYS 53  96  96  LYS LYS B . n 
B 1 54  HIS 54  97  97  HIS HIS B . n 
B 1 55  PRO 55  98  98  PRO PRO B . n 
B 1 56  CYS 56  99  99  CYS CYS B . n 
B 1 57  ASP 57  100 100 ASP ASP B . n 
B 1 58  ILE 58  101 101 ILE ILE B . n 
B 1 59  THR 59  102 102 THR THR B . n 
B 1 60  GLU 60  103 103 GLU GLU B . n 
B 1 61  GLU 61  104 104 GLU GLU B . n 
B 1 62  ASP 62  105 105 ASP ASP B . n 
B 1 63  TYR 63  106 106 TYR TYR B . n 
B 1 64  GLN 64  107 107 GLN GLN B . n 
B 1 65  PRO 65  108 108 PRO PRO B . n 
B 1 66  LEU 66  109 109 LEU LEU B . n 
B 1 67  MET 67  110 110 MET MET B . n 
B 1 68  LYS 68  111 111 LYS LYS B . n 
B 1 69  LEU 69  112 112 LEU LEU B . n 
B 1 70  GLY 70  113 113 GLY GLY B . n 
B 1 71  THR 71  114 114 THR THR B . n 
B 1 72  GLN 72  115 115 GLN GLN B . n 
B 1 73  THR 73  116 116 THR THR B . n 
B 1 74  VAL 74  117 117 VAL VAL B . n 
B 1 75  PRO 75  118 118 PRO PRO B . n 
B 1 76  CYS 76  119 119 CYS CYS B . n 
B 1 77  ASN 77  120 120 ASN ASN B . n 
B 1 78  LYS 78  121 121 LYS LYS B . n 
B 1 79  ILE 79  122 122 ILE ILE B . n 
B 1 80  LEU 80  123 123 LEU LEU B . n 
B 1 81  LEU 81  124 124 LEU LEU B . n 
B 1 82  TRP 82  125 125 TRP TRP B . n 
B 1 83  SER 83  126 126 SER SER B . n 
B 1 84  ARG 84  127 127 ARG ARG B . n 
B 1 85  ILE 85  128 128 ILE ILE B . n 
B 1 86  LYS 86  129 129 LYS LYS B . n 
B 1 87  ASP 87  130 130 ASP ASP B . n 
B 1 88  LEU 88  131 131 LEU LEU B . n 
B 1 89  ALA 89  132 132 ALA ALA B . n 
B 1 90  HIS 90  133 133 HIS HIS B . n 
B 1 91  GLN 91  134 134 GLN GLN B . n 
B 1 92  PHE 92  135 135 PHE PHE B . n 
B 1 93  THR 93  136 136 THR THR B . n 
B 1 94  GLN 94  137 137 GLN GLN B . n 
B 1 95  VAL 95  138 138 VAL VAL B . n 
B 1 96  GLN 96  139 139 GLN GLN B . n 
B 1 97  ARG 97  140 140 ARG ARG B . n 
B 1 98  ASP 98  141 141 ASP ASP B . n 
B 1 99  MET 99  142 142 MET MET B . n 
B 1 100 PHE 100 143 143 PHE PHE B . n 
B 1 101 THR 101 144 144 THR THR B . n 
B 1 102 LEU 102 145 145 LEU LEU B . n 
B 1 103 GLU 103 146 146 GLU GLU B . n 
B 1 104 ASP 104 147 147 ASP ASP B . n 
B 1 105 THR 105 148 148 THR THR B . n 
B 1 106 LEU 106 149 149 LEU LEU B . n 
B 1 107 LEU 107 150 150 LEU LEU B . n 
B 1 108 GLY 108 151 151 GLY GLY B . n 
B 1 109 TYR 109 152 152 TYR TYR B . n 
B 1 110 LEU 110 153 153 LEU LEU B . n 
B 1 111 ALA 111 154 154 ALA ALA B . n 
B 1 112 ASP 112 155 155 ASP ASP B . n 
B 1 113 ASP 113 156 156 ASP ASP B . n 
B 1 114 LEU 114 157 157 LEU LEU B . n 
B 1 115 THR 115 158 158 THR THR B . n 
B 1 116 TRP 116 159 159 TRP TRP B . n 
B 1 117 CYS 117 160 160 CYS CYS B . n 
B 1 118 GLY 118 161 161 GLY GLY B . n 
B 1 119 GLU 119 162 162 GLU GLU B . n 
B 1 120 PHE 120 163 163 PHE PHE B . n 
B 1 121 ALA 121 164 164 ALA ALA B . n 
B 1 122 THR 122 165 165 THR THR B . n 
B 1 123 SER 123 166 166 SER SER B . n 
B 1 124 LYS 124 167 167 LYS LYS B . n 
B 1 125 ILE 125 168 168 ILE ILE B . n 
B 1 126 ASN 126 169 169 ASN ASN B . n 
B 1 127 TYR 127 170 170 TYR TYR B . n 
B 1 128 GLN 128 171 171 GLN GLN B . n 
B 1 129 SER 129 172 172 SER SER B . n 
B 1 130 CYS 130 173 173 CYS CYS B . n 
B 1 131 PRO 131 174 174 PRO PRO B . n 
B 1 132 ASP 132 175 175 ASP ASP B . n 
B 1 133 TRP 133 176 176 TRP TRP B . n 
B 1 134 ARG 134 177 177 ARG ARG B . n 
B 1 135 LYS 135 178 178 LYS LYS B . n 
B 1 136 ASP 136 179 179 ASP ASP B . n 
B 1 137 CYS 137 180 180 CYS CYS B . n 
B 1 138 SER 138 181 181 SER SER B . n 
B 1 139 ASN 139 182 182 ASN ASN B . n 
B 1 140 ASN 140 183 183 ASN ASN B . n 
B 1 141 PRO 141 184 184 PRO PRO B . n 
B 1 142 VAL 142 185 185 VAL VAL B . n 
B 1 143 SER 143 186 186 SER SER B . n 
B 1 144 VAL 144 187 187 VAL VAL B . n 
B 1 145 PHE 145 188 188 PHE PHE B . n 
B 1 146 TRP 146 189 189 TRP TRP B . n 
B 1 147 LYS 147 190 190 LYS LYS B . n 
B 1 148 THR 148 191 191 THR THR B . n 
B 1 149 VAL 149 192 192 VAL VAL B . n 
B 1 150 SER 150 193 193 SER SER B . n 
B 1 151 ARG 151 194 194 ARG ARG B . n 
B 1 152 ARG 152 195 195 ARG ARG B . n 
B 1 153 PHE 153 196 196 PHE PHE B . n 
B 1 154 ALA 154 197 197 ALA ALA B . n 
B 1 155 GLU 155 198 198 GLU GLU B . n 
B 1 156 ALA 156 199 199 ALA ALA B . n 
B 1 157 ALA 157 200 200 ALA ALA B . n 
B 1 158 CYS 158 201 201 CYS CYS B . n 
B 1 159 ASP 159 202 202 ASP ASP B . n 
B 1 160 VAL 160 203 203 VAL VAL B . n 
B 1 161 VAL 161 204 204 VAL VAL B . n 
B 1 162 HIS 162 205 205 HIS HIS B . n 
B 1 163 VAL 163 206 206 VAL VAL B . n 
B 1 164 MET 164 207 207 MET MET B . n 
B 1 165 LEU 165 208 208 LEU LEU B . n 
B 1 166 ASP 166 209 209 ASP ASP B . n 
B 1 167 GLY 167 210 210 GLY GLY B . n 
B 1 168 SER 168 211 211 SER SER B . n 
B 1 169 ARG 169 212 212 ARG ARG B . n 
B 1 170 SER 170 213 213 SER SER B . n 
B 1 171 LYS 171 214 214 LYS LYS B . n 
B 1 172 ILE 172 215 215 ILE ILE B . n 
B 1 173 PHE 173 216 216 PHE PHE B . n 
B 1 174 ASP 174 217 217 ASP ASP B . n 
B 1 175 LYS 175 218 218 LYS LYS B . n 
B 1 176 ASP 176 219 219 ASP ASP B . n 
B 1 177 SER 177 220 220 SER SER B . n 
B 1 178 THR 178 221 221 THR THR B . n 
B 1 179 PHE 179 222 222 PHE PHE B . n 
B 1 180 GLY 180 223 223 GLY GLY B . n 
B 1 181 SER 181 224 224 SER SER B . n 
B 1 182 VAL 182 225 225 VAL VAL B . n 
B 1 183 GLU 183 226 226 GLU GLU B . n 
B 1 184 VAL 184 227 227 VAL VAL B . n 
B 1 185 HIS 185 228 228 HIS HIS B . n 
B 1 186 ASN 186 229 229 ASN ASN B . n 
B 1 187 LEU 187 230 230 LEU LEU B . n 
B 1 188 GLN 188 231 231 GLN GLN B . n 
B 1 189 PRO 189 232 232 PRO PRO B . n 
B 1 190 GLU 190 233 233 GLU GLU B . n 
B 1 191 LYS 191 234 234 LYS LYS B . n 
B 1 192 VAL 192 235 235 VAL VAL B . n 
B 1 193 GLN 193 236 236 GLN GLN B . n 
B 1 194 THR 194 237 237 THR THR B . n 
B 1 195 LEU 195 238 238 LEU LEU B . n 
B 1 196 GLU 196 239 239 GLU GLU B . n 
B 1 197 ALA 197 240 240 ALA ALA B . n 
B 1 198 TRP 198 241 241 TRP TRP B . n 
B 1 199 VAL 199 242 242 VAL VAL B . n 
B 1 200 ILE 200 243 243 ILE ILE B . n 
B 1 201 HIS 201 244 244 HIS HIS B . n 
B 1 202 GLY 202 245 245 GLY GLY B . n 
B 1 203 GLY 203 246 246 GLY GLY B . n 
B 1 204 ARG 204 247 247 ARG ARG B . n 
B 1 205 GLU 205 248 248 GLU GLU B . n 
B 1 206 ASP 206 249 249 ASP ASP B . n 
B 1 207 SER 207 250 250 SER SER B . n 
B 1 208 ARG 208 251 251 ARG ARG B . n 
B 1 209 ASP 209 252 252 ASP ASP B . n 
B 1 210 LEU 210 253 253 LEU LEU B . n 
B 1 211 CYS 211 254 254 CYS CYS B . n 
B 1 212 GLN 212 255 255 GLN GLN B . n 
B 1 213 ASP 213 256 256 ASP ASP B . n 
B 1 214 PRO 214 257 257 PRO PRO B . n 
B 1 215 THR 215 258 258 THR THR B . n 
B 1 216 ILE 216 259 259 ILE ILE B . n 
B 1 217 LYS 217 260 260 LYS LYS B . n 
B 1 218 GLU 218 261 261 GLU GLU B . n 
B 1 219 LEU 219 262 262 LEU LEU B . n 
B 1 220 GLU 220 263 263 GLU GLU B . n 
B 1 221 SER 221 264 264 SER SER B . n 
B 1 222 ILE 222 265 265 ILE ILE B . n 
B 1 223 ILE 223 266 266 ILE ILE B . n 
B 1 224 SER 224 267 267 SER SER B . n 
B 1 225 LYS 225 268 268 LYS LYS B . n 
B 1 226 ARG 226 269 269 ARG ARG B . n 
B 1 227 ASN 227 270 270 ASN ASN B . n 
B 1 228 ILE 228 271 271 ILE ILE B . n 
B 1 229 GLN 229 272 272 GLN GLN B . n 
B 1 230 PHE 230 273 273 PHE PHE B . n 
B 1 231 SER 231 274 274 SER SER B . n 
B 1 232 CYS 232 275 275 CYS CYS B . n 
B 1 233 LYS 233 276 276 LYS LYS B . n 
B 1 234 ASN 234 277 277 ASN ASN B . n 
B 1 235 ILE 235 278 278 ILE ILE B . n 
B 1 236 TYR 236 279 279 TYR TYR B . n 
B 1 237 ARG 237 280 280 ARG ARG B . n 
B 1 238 PRO 238 281 281 PRO PRO B . n 
B 1 239 ASP 239 282 282 ASP ASP B . n 
B 1 240 LYS 240 283 283 LYS LYS B . n 
B 1 241 PHE 241 284 284 PHE PHE B . n 
B 1 242 LEU 242 285 285 LEU LEU B . n 
B 1 243 GLN 243 286 286 GLN GLN B . n 
B 1 244 CYS 244 287 287 CYS CYS B . n 
B 1 245 VAL 245 288 288 VAL VAL B . n 
B 1 246 LYS 246 289 289 LYS LYS B . n 
B 1 247 ASN 247 290 290 ASN ASN B . n 
B 1 248 PRO 248 291 291 PRO PRO B . n 
B 1 249 GLU 249 292 292 GLU GLU B . n 
B 1 250 ASP 250 293 293 ASP ASP B . n 
B 1 251 SER 251 294 ?   ?   ?   B . n 
B 1 252 SER 252 295 ?   ?   ?   B . n 
B 1 253 CYS 253 296 ?   ?   ?   B . n 
B 1 254 THR 254 297 ?   ?   ?   B . n 
B 1 255 SER 255 298 ?   ?   ?   B . n 
B 1 256 GLU 256 299 ?   ?   ?   B . n 
B 1 257 ILE 257 300 ?   ?   ?   B . n 
# 
loop_
_pdbx_entity_instance_feature.ordinal 
_pdbx_entity_instance_feature.comp_id 
_pdbx_entity_instance_feature.asym_id 
_pdbx_entity_instance_feature.seq_num 
_pdbx_entity_instance_feature.auth_comp_id 
_pdbx_entity_instance_feature.auth_asym_id 
_pdbx_entity_instance_feature.auth_seq_num 
_pdbx_entity_instance_feature.feature_type 
_pdbx_entity_instance_feature.details 
1 NNR ? ? NNR ? ? 'SUBJECT OF INVESTIGATION' ? 
2 RIB ? ? RIB ? ? 'SUBJECT OF INVESTIGATION' ? 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
C 2 NNR 1   401 301 NNR NNR A . 
D 3 RIB 1   402 302 RIB RIB A . 
E 2 NNR 1   401 301 NNR NNR B . 
F 3 RIB 1   402 302 RIB RIB B . 
G 4 HOH 1   501 259 HOH HOH A . 
G 4 HOH 2   502 129 HOH HOH A . 
G 4 HOH 3   503 126 HOH HOH A . 
G 4 HOH 4   504 143 HOH HOH A . 
G 4 HOH 5   505 104 HOH HOH A . 
G 4 HOH 6   506 136 HOH HOH A . 
G 4 HOH 7   507 139 HOH HOH A . 
G 4 HOH 8   508 98  HOH HOH A . 
G 4 HOH 9   509 294 HOH HOH A . 
G 4 HOH 10  510 89  HOH HOH A . 
G 4 HOH 11  511 298 HOH HOH A . 
G 4 HOH 12  512 147 HOH HOH A . 
G 4 HOH 13  513 113 HOH HOH A . 
G 4 HOH 14  514 103 HOH HOH A . 
G 4 HOH 15  515 130 HOH HOH A . 
G 4 HOH 16  516 261 HOH HOH A . 
G 4 HOH 17  517 297 HOH HOH A . 
G 4 HOH 18  518 141 HOH HOH A . 
G 4 HOH 19  519 148 HOH HOH A . 
G 4 HOH 20  520 78  HOH HOH A . 
G 4 HOH 21  521 100 HOH HOH A . 
G 4 HOH 22  522 300 HOH HOH A . 
G 4 HOH 23  523 134 HOH HOH A . 
G 4 HOH 24  524 108 HOH HOH A . 
G 4 HOH 25  525 105 HOH HOH A . 
G 4 HOH 26  526 94  HOH HOH A . 
G 4 HOH 27  527 125 HOH HOH A . 
G 4 HOH 28  528 144 HOH HOH A . 
G 4 HOH 29  529 95  HOH HOH A . 
G 4 HOH 30  530 117 HOH HOH A . 
G 4 HOH 31  531 264 HOH HOH A . 
G 4 HOH 32  532 28  HOH HOH A . 
G 4 HOH 33  533 54  HOH HOH A . 
G 4 HOH 34  534 18  HOH HOH A . 
G 4 HOH 35  535 87  HOH HOH A . 
G 4 HOH 36  536 12  HOH HOH A . 
G 4 HOH 37  537 237 HOH HOH A . 
G 4 HOH 38  538 251 HOH HOH A . 
G 4 HOH 39  539 114 HOH HOH A . 
G 4 HOH 40  540 238 HOH HOH A . 
G 4 HOH 41  541 85  HOH HOH A . 
G 4 HOH 42  542 1   HOH HOH A . 
G 4 HOH 43  543 57  HOH HOH A . 
G 4 HOH 44  544 296 HOH HOH A . 
G 4 HOH 45  545 4   HOH HOH A . 
G 4 HOH 46  546 140 HOH HOH A . 
G 4 HOH 47  547 249 HOH HOH A . 
G 4 HOH 48  548 295 HOH HOH A . 
G 4 HOH 49  549 32  HOH HOH A . 
G 4 HOH 50  550 8   HOH HOH A . 
G 4 HOH 51  551 122 HOH HOH A . 
G 4 HOH 52  552 51  HOH HOH A . 
G 4 HOH 53  553 123 HOH HOH A . 
G 4 HOH 54  554 121 HOH HOH A . 
G 4 HOH 55  555 252 HOH HOH A . 
G 4 HOH 56  556 39  HOH HOH A . 
G 4 HOH 57  557 133 HOH HOH A . 
G 4 HOH 58  558 88  HOH HOH A . 
G 4 HOH 59  559 284 HOH HOH A . 
G 4 HOH 60  560 132 HOH HOH A . 
G 4 HOH 61  561 219 HOH HOH A . 
G 4 HOH 62  562 16  HOH HOH A . 
G 4 HOH 63  563 11  HOH HOH A . 
G 4 HOH 64  564 79  HOH HOH A . 
G 4 HOH 65  565 52  HOH HOH A . 
G 4 HOH 66  566 43  HOH HOH A . 
G 4 HOH 67  567 239 HOH HOH A . 
G 4 HOH 68  568 120 HOH HOH A . 
G 4 HOH 69  569 102 HOH HOH A . 
G 4 HOH 70  570 145 HOH HOH A . 
G 4 HOH 71  571 77  HOH HOH A . 
G 4 HOH 72  572 116 HOH HOH A . 
G 4 HOH 73  573 241 HOH HOH A . 
G 4 HOH 74  574 15  HOH HOH A . 
G 4 HOH 75  575 119 HOH HOH A . 
G 4 HOH 76  576 146 HOH HOH A . 
G 4 HOH 77  577 86  HOH HOH A . 
G 4 HOH 78  578 256 HOH HOH A . 
G 4 HOH 79  579 2   HOH HOH A . 
G 4 HOH 80  580 112 HOH HOH A . 
G 4 HOH 81  581 6   HOH HOH A . 
G 4 HOH 82  582 131 HOH HOH A . 
G 4 HOH 83  583 260 HOH HOH A . 
G 4 HOH 84  584 258 HOH HOH A . 
G 4 HOH 85  585 101 HOH HOH A . 
G 4 HOH 86  586 214 HOH HOH A . 
G 4 HOH 87  587 254 HOH HOH A . 
G 4 HOH 88  588 64  HOH HOH A . 
G 4 HOH 89  589 46  HOH HOH A . 
G 4 HOH 90  590 10  HOH HOH A . 
G 4 HOH 91  591 217 HOH HOH A . 
G 4 HOH 92  592 240 HOH HOH A . 
G 4 HOH 93  593 257 HOH HOH A . 
G 4 HOH 94  594 37  HOH HOH A . 
G 4 HOH 95  595 250 HOH HOH A . 
G 4 HOH 96  596 232 HOH HOH A . 
G 4 HOH 97  597 110 HOH HOH A . 
G 4 HOH 98  598 127 HOH HOH A . 
G 4 HOH 99  599 27  HOH HOH A . 
G 4 HOH 100 600 228 HOH HOH A . 
G 4 HOH 101 601 248 HOH HOH A . 
G 4 HOH 102 602 225 HOH HOH A . 
G 4 HOH 103 603 230 HOH HOH A . 
G 4 HOH 104 604 35  HOH HOH A . 
G 4 HOH 105 605 243 HOH HOH A . 
G 4 HOH 106 606 138 HOH HOH A . 
G 4 HOH 107 607 115 HOH HOH A . 
G 4 HOH 108 608 246 HOH HOH A . 
G 4 HOH 109 609 96  HOH HOH A . 
G 4 HOH 110 610 31  HOH HOH A . 
G 4 HOH 111 611 38  HOH HOH A . 
G 4 HOH 112 612 244 HOH HOH A . 
G 4 HOH 113 613 71  HOH HOH A . 
G 4 HOH 114 614 213 HOH HOH A . 
G 4 HOH 115 615 142 HOH HOH A . 
G 4 HOH 116 616 90  HOH HOH A . 
G 4 HOH 117 617 247 HOH HOH A . 
G 4 HOH 118 618 231 HOH HOH A . 
G 4 HOH 119 619 128 HOH HOH A . 
G 4 HOH 120 620 58  HOH HOH A . 
G 4 HOH 121 621 14  HOH HOH A . 
G 4 HOH 122 622 135 HOH HOH A . 
G 4 HOH 123 623 124 HOH HOH A . 
G 4 HOH 124 624 60  HOH HOH A . 
G 4 HOH 125 625 137 HOH HOH A . 
G 4 HOH 126 626 242 HOH HOH A . 
G 4 HOH 127 627 106 HOH HOH A . 
G 4 HOH 128 628 70  HOH HOH A . 
G 4 HOH 129 629 109 HOH HOH A . 
G 4 HOH 130 630 273 HOH HOH A . 
G 4 HOH 131 631 111 HOH HOH A . 
G 4 HOH 132 632 118 HOH HOH A . 
G 4 HOH 133 633 292 HOH HOH A . 
G 4 HOH 134 634 41  HOH HOH A . 
G 4 HOH 135 635 262 HOH HOH A . 
G 4 HOH 136 636 42  HOH HOH A . 
G 4 HOH 137 637 19  HOH HOH A . 
G 4 HOH 138 638 286 HOH HOH A . 
G 4 HOH 139 639 20  HOH HOH A . 
G 4 HOH 140 640 107 HOH HOH A . 
G 4 HOH 141 641 33  HOH HOH A . 
G 4 HOH 142 642 220 HOH HOH A . 
G 4 HOH 143 643 50  HOH HOH A . 
G 4 HOH 144 644 255 HOH HOH A . 
G 4 HOH 145 645 73  HOH HOH A . 
G 4 HOH 146 646 40  HOH HOH A . 
G 4 HOH 147 647 68  HOH HOH A . 
G 4 HOH 148 648 185 HOH HOH A . 
G 4 HOH 149 649 293 HOH HOH A . 
G 4 HOH 150 650 218 HOH HOH A . 
G 4 HOH 151 651 47  HOH HOH A . 
G 4 HOH 152 652 226 HOH HOH A . 
G 4 HOH 153 653 17  HOH HOH A . 
G 4 HOH 154 654 285 HOH HOH A . 
G 4 HOH 155 655 279 HOH HOH A . 
G 4 HOH 156 656 223 HOH HOH A . 
G 4 HOH 157 657 265 HOH HOH A . 
G 4 HOH 158 658 253 HOH HOH A . 
G 4 HOH 159 659 280 HOH HOH A . 
G 4 HOH 160 660 76  HOH HOH A . 
G 4 HOH 161 661 299 HOH HOH A . 
G 4 HOH 162 662 275 HOH HOH A . 
G 4 HOH 163 663 224 HOH HOH A . 
G 4 HOH 164 664 266 HOH HOH A . 
G 4 HOH 165 665 66  HOH HOH A . 
G 4 HOH 166 666 288 HOH HOH A . 
H 4 HOH 1   501 169 HOH HOH B . 
H 4 HOH 2   502 99  HOH HOH B . 
H 4 HOH 3   503 154 HOH HOH B . 
H 4 HOH 4   504 149 HOH HOH B . 
H 4 HOH 5   505 170 HOH HOH B . 
H 4 HOH 6   506 156 HOH HOH B . 
H 4 HOH 7   507 49  HOH HOH B . 
H 4 HOH 8   508 63  HOH HOH B . 
H 4 HOH 9   509 157 HOH HOH B . 
H 4 HOH 10  510 189 HOH HOH B . 
H 4 HOH 11  511 205 HOH HOH B . 
H 4 HOH 12  512 69  HOH HOH B . 
H 4 HOH 13  513 61  HOH HOH B . 
H 4 HOH 14  514 187 HOH HOH B . 
H 4 HOH 15  515 180 HOH HOH B . 
H 4 HOH 16  516 245 HOH HOH B . 
H 4 HOH 17  517 97  HOH HOH B . 
H 4 HOH 18  518 5   HOH HOH B . 
H 4 HOH 19  519 29  HOH HOH B . 
H 4 HOH 20  520 56  HOH HOH B . 
H 4 HOH 21  521 171 HOH HOH B . 
H 4 HOH 22  522 25  HOH HOH B . 
H 4 HOH 23  523 202 HOH HOH B . 
H 4 HOH 24  524 23  HOH HOH B . 
H 4 HOH 25  525 84  HOH HOH B . 
H 4 HOH 26  526 81  HOH HOH B . 
H 4 HOH 27  527 150 HOH HOH B . 
H 4 HOH 28  528 161 HOH HOH B . 
H 4 HOH 29  529 191 HOH HOH B . 
H 4 HOH 30  530 209 HOH HOH B . 
H 4 HOH 31  531 75  HOH HOH B . 
H 4 HOH 32  532 291 HOH HOH B . 
H 4 HOH 33  533 193 HOH HOH B . 
H 4 HOH 34  534 163 HOH HOH B . 
H 4 HOH 35  535 177 HOH HOH B . 
H 4 HOH 36  536 44  HOH HOH B . 
H 4 HOH 37  537 201 HOH HOH B . 
H 4 HOH 38  538 269 HOH HOH B . 
H 4 HOH 39  539 74  HOH HOH B . 
H 4 HOH 40  540 211 HOH HOH B . 
H 4 HOH 41  541 215 HOH HOH B . 
H 4 HOH 42  542 210 HOH HOH B . 
H 4 HOH 43  543 186 HOH HOH B . 
H 4 HOH 44  544 178 HOH HOH B . 
H 4 HOH 45  545 173 HOH HOH B . 
H 4 HOH 46  546 176 HOH HOH B . 
H 4 HOH 47  547 162 HOH HOH B . 
H 4 HOH 48  548 164 HOH HOH B . 
H 4 HOH 49  549 9   HOH HOH B . 
H 4 HOH 50  550 7   HOH HOH B . 
H 4 HOH 51  551 158 HOH HOH B . 
H 4 HOH 52  552 289 HOH HOH B . 
H 4 HOH 53  553 3   HOH HOH B . 
H 4 HOH 54  554 13  HOH HOH B . 
H 4 HOH 55  555 30  HOH HOH B . 
H 4 HOH 56  556 93  HOH HOH B . 
H 4 HOH 57  557 207 HOH HOH B . 
H 4 HOH 58  558 192 HOH HOH B . 
H 4 HOH 59  559 216 HOH HOH B . 
H 4 HOH 60  560 151 HOH HOH B . 
H 4 HOH 61  561 234 HOH HOH B . 
H 4 HOH 62  562 166 HOH HOH B . 
H 4 HOH 63  563 91  HOH HOH B . 
H 4 HOH 64  564 160 HOH HOH B . 
H 4 HOH 65  565 200 HOH HOH B . 
H 4 HOH 66  566 198 HOH HOH B . 
H 4 HOH 67  567 53  HOH HOH B . 
H 4 HOH 68  568 222 HOH HOH B . 
H 4 HOH 69  569 45  HOH HOH B . 
H 4 HOH 70  570 168 HOH HOH B . 
H 4 HOH 71  571 194 HOH HOH B . 
H 4 HOH 72  572 153 HOH HOH B . 
H 4 HOH 73  573 204 HOH HOH B . 
H 4 HOH 74  574 82  HOH HOH B . 
H 4 HOH 75  575 175 HOH HOH B . 
H 4 HOH 76  576 67  HOH HOH B . 
H 4 HOH 77  577 227 HOH HOH B . 
H 4 HOH 78  578 263 HOH HOH B . 
H 4 HOH 79  579 212 HOH HOH B . 
H 4 HOH 80  580 270 HOH HOH B . 
H 4 HOH 81  581 59  HOH HOH B . 
H 4 HOH 82  582 72  HOH HOH B . 
H 4 HOH 83  583 172 HOH HOH B . 
H 4 HOH 84  584 34  HOH HOH B . 
H 4 HOH 85  585 165 HOH HOH B . 
H 4 HOH 86  586 24  HOH HOH B . 
H 4 HOH 87  587 221 HOH HOH B . 
H 4 HOH 88  588 271 HOH HOH B . 
H 4 HOH 89  589 174 HOH HOH B . 
H 4 HOH 90  590 83  HOH HOH B . 
H 4 HOH 91  591 182 HOH HOH B . 
H 4 HOH 92  592 159 HOH HOH B . 
H 4 HOH 93  593 22  HOH HOH B . 
H 4 HOH 94  594 48  HOH HOH B . 
H 4 HOH 95  595 181 HOH HOH B . 
H 4 HOH 96  596 80  HOH HOH B . 
H 4 HOH 97  597 203 HOH HOH B . 
H 4 HOH 98  598 206 HOH HOH B . 
H 4 HOH 99  599 155 HOH HOH B . 
H 4 HOH 100 600 197 HOH HOH B . 
H 4 HOH 101 601 188 HOH HOH B . 
H 4 HOH 102 602 281 HOH HOH B . 
H 4 HOH 103 603 282 HOH HOH B . 
H 4 HOH 104 604 233 HOH HOH B . 
H 4 HOH 105 605 199 HOH HOH B . 
H 4 HOH 106 606 152 HOH HOH B . 
H 4 HOH 107 607 65  HOH HOH B . 
H 4 HOH 108 608 92  HOH HOH B . 
H 4 HOH 109 609 184 HOH HOH B . 
H 4 HOH 110 610 26  HOH HOH B . 
H 4 HOH 111 611 195 HOH HOH B . 
H 4 HOH 112 612 229 HOH HOH B . 
H 4 HOH 113 613 267 HOH HOH B . 
H 4 HOH 114 614 208 HOH HOH B . 
H 4 HOH 115 615 196 HOH HOH B . 
H 4 HOH 116 616 36  HOH HOH B . 
H 4 HOH 117 617 55  HOH HOH B . 
H 4 HOH 118 618 190 HOH HOH B . 
H 4 HOH 119 619 21  HOH HOH B . 
H 4 HOH 120 620 268 HOH HOH B . 
H 4 HOH 121 621 272 HOH HOH B . 
H 4 HOH 122 622 236 HOH HOH B . 
H 4 HOH 123 623 235 HOH HOH B . 
H 4 HOH 124 624 183 HOH HOH B . 
H 4 HOH 125 625 278 HOH HOH B . 
H 4 HOH 126 626 283 HOH HOH B . 
H 4 HOH 127 627 276 HOH HOH B . 
H 4 HOH 128 628 277 HOH HOH B . 
H 4 HOH 129 629 167 HOH HOH B . 
H 4 HOH 130 630 62  HOH HOH B . 
H 4 HOH 131 631 274 HOH HOH B . 
H 4 HOH 132 632 179 HOH HOH B . 
H 4 HOH 133 633 290 HOH HOH B . 
H 4 HOH 134 634 287 HOH HOH B . 
# 
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 GLU 292 ? CG  ? A GLU 249 CG  
2  1 Y 1 A GLU 292 ? CD  ? A GLU 249 CD  
3  1 Y 1 A GLU 292 ? OE1 ? A GLU 249 OE1 
4  1 Y 1 A GLU 292 ? OE2 ? A GLU 249 OE2 
5  1 Y 1 B ARG 280 ? CG  ? B ARG 237 CG  
6  1 Y 1 B ARG 280 ? CD  ? B ARG 237 CD  
7  1 Y 1 B ARG 280 ? NE  ? B ARG 237 NE  
8  1 Y 1 B ARG 280 ? CZ  ? B ARG 237 CZ  
9  1 Y 1 B ARG 280 ? NH1 ? B ARG 237 NH1 
10 1 Y 1 B ARG 280 ? NH2 ? B ARG 237 NH2 
11 1 Y 1 B LYS 283 ? CG  ? B LYS 240 CG  
12 1 Y 1 B LYS 283 ? CD  ? B LYS 240 CD  
13 1 Y 1 B LYS 283 ? CE  ? B LYS 240 CE  
14 1 Y 1 B LYS 283 ? NZ  ? B LYS 240 NZ  
15 1 Y 1 B ASN 290 ? CG  ? B ASN 247 CG  
16 1 Y 1 B ASN 290 ? OD1 ? B ASN 247 OD1 
17 1 Y 1 B ASN 290 ? ND2 ? B ASN 247 ND2 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement       ? ? ? ? ? ? ? ? ? ? ? PHENIX ? ? ? '(1.20.1_4487: ???)' 1 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? SCALA  ? ? ? 'v. 3.3.22'          2 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? XDS    ? ? ? .                    3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHASER ? ? ? 'v. 2.8.3'           4 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   97.26 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     8VAU 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     57.627 
_cell.length_a_esd                 ? 
_cell.length_b                     51.351 
_cell.length_b_esd                 ? 
_cell.length_c                     100.501 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        4 
_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             ? 
_cell.pdbx_esd_method              ? 
# 
_symmetry.entry_id                         8VAU 
_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                   8VAU 
_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             2.38 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          48.33 
_exptl_crystal.description                  'Large two dimentional, thin platelets' 
_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.pdbx_mosaic_method           ? 
_exptl_crystal.pdbx_mosaic_block_size       ? 
_exptl_crystal.pdbx_mosaic_block_size_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, HANGING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              7.0 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    '100mM HEPES pH 7.0, 14-16% PEG 3350' 
_exptl_crystal_grow.pdbx_pH_range   '6.8 - 7.3' 
_exptl_crystal_grow.temp            295 
# 
_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                      'Flat side-deflecting, Rh-coated Si mirror.' 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS EIGER X 16M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2022-07-06 
_diffrn_detector.pdbx_frequency               ? 
_diffrn_detector.id                           ? 
_diffrn_detector.number_of_axes               ? 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    
'Liquid nitrogen-cooled double-crystal Si(111) monochromator with a 0.01% energy bandpass' 
_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   0.979460 
_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                        'SSRL BEAMLINE BL12-1' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.979460 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   BL12-1 
_diffrn_source.pdbx_synchrotron_site       SSRL 
# 
_reflns.B_iso_Wilson_estimate                          29.5 
_reflns.entry_id                                       8VAU 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              2.1 
_reflns.d_resolution_low                               34.71 
_reflns.details                                        ? 
_reflns.limit_h_max                                    ? 
_reflns.limit_h_min                                    ? 
_reflns.limit_k_max                                    ? 
_reflns.limit_k_min                                    ? 
_reflns.limit_l_max                                    ? 
_reflns.limit_l_min                                    ? 
_reflns.number_all                                     ? 
_reflns.number_obs                                     33411 
_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                           97.6 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                4.4 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          9.1 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               ? 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                ? 
_reflns.pdbx_Rpim_I_all                                0.053 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.996 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.102 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
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_obs 
_reflns_shell.Rmerge_F_all 
_reflns_shell.Rmerge_F_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_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 
_reflns_shell.percent_possible_all 
_reflns_shell.Rmerge_I_all 
_reflns_shell.Rmerge_I_obs 
_reflns_shell.pdbx_Rsym_value 
_reflns_shell.pdbx_percent_possible_ellipsoidal 
_reflns_shell.pdbx_percent_possible_spherical 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous 
_reflns_shell.pdbx_percent_possible_spherical_anomalous 
_reflns_shell.pdbx_redundancy_anomalous 
_reflns_shell.pdbx_CC_half_anomalous 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous 
_reflns_shell.pdbx_percent_possible_anomalous 
2.100 2.210 ? 2.5 ? ? ? ? 4965 ? ? ? ? ? ? ? ? ? ? ? 4.4 ? ? ? ? 0.355 ? 1 1 0.848 ? ? 99.2 ? 0.687 ? ? ? ? ? ? ? ? ? 
2.21  2.35  ? 3.3 ? ? ? ? 4642 ? ? ? ? ? ? ? ? ? ? ? ?   ? ? ? ? 0.252 ? 2 1 0.903 ? ? ?    ? 0.486 ? ? ? ? ? ? ? ? ? 
2.35  2.51  ? ?   ? ? ? ? 4295 ? ? ? ? ? ? ? ? ? ? ? 4.2 ? ? ? ? 0.182 ? 3 1 0.947 ? ? ?    ? ?     ? ? ? ? ? ? ? ? ? 
2.51  2.71  ? ?   ? ? ? ? 4048 ? ? ? ? ? ? ? ? ? ? ? 4.5 ? ? ? ? 0.119 ? 4 1 0.976 ? ? ?    ? ?     ? ? ? ? ? ? ? ? ? 
2.71  2.97  ? ?   ? ? ? ? 3740 ? ? ? ? ? ? ? ? ? ? ? 4.5 ? ? ? ? 0.085 ? 5 1 0.985 ? ? ?    ? ?     ? ? ? ? ? ? ? ? ? 
# 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               ? 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.details                                  ? 
_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                                 8VAU 
_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                            2.10 
_refine.ls_d_res_low                             34.71 
_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                     33368 
_refine.ls_number_reflns_R_free                  1710 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    97.07 
_refine.ls_percent_reflns_R_free                 5.12 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1900 
_refine.ls_R_factor_R_free                       0.2193 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1885 
_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                    'FLAT BULK SOLVENT MODEL' 
_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                          1.34 
_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               'FREE R-VALUE' 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       ML 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             1.10 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.90 
_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                 25.95 
_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                            0.26 
_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                         LAST 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       2.10 
_refine_hist.d_res_low                        34.71 
_refine_hist.number_atoms_solvent             300 
_refine_hist.number_atoms_total               4403 
_refine_hist.number_reflns_all                ? 
_refine_hist.number_reflns_obs                ? 
_refine_hist.number_reflns_R_free             ? 
_refine_hist.number_reflns_R_work             ? 
_refine_hist.R_factor_all                     ? 
_refine_hist.R_factor_obs                     ? 
_refine_hist.R_factor_R_free                  ? 
_refine_hist.R_factor_R_work                  ? 
_refine_hist.pdbx_number_residues_total       ? 
_refine_hist.pdbx_B_iso_mean_ligand           ? 
_refine_hist.pdbx_B_iso_mean_solvent          ? 
_refine_hist.pdbx_number_atoms_protein        4049 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         54 
_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' ? 0.002  ? 4275 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 0.532  ? 5821 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 12.860 ? 1586 ? f_dihedral_angle_d ? ? 
'X-RAY DIFFRACTION' ? 0.041  ? 639  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.004  ? 745  ? f_plane_restr      ? ? 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.percent_reflns_obs 
_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_error 
_refine_ls_shell.R_factor_R_work 
_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 
_refine_ls_shell.pdbx_phase_error 
_refine_ls_shell.pdbx_fsc_work 
_refine_ls_shell.pdbx_fsc_free 
_refine_ls_shell.R_factor_R_free 
'X-RAY DIFFRACTION' 2.10 2.16  . . 147 2624 98.00 . . . . 0.2880 . . . . . . . . . . . 0.3438 
'X-RAY DIFFRACTION' 2.16 2.23  . . 162 2669 99.00 . . . . 0.2619 . . . . . . . . . . . 0.2756 
'X-RAY DIFFRACTION' 2.23 2.31  . . 139 2676 99.00 . . . . 0.2477 . . . . . . . . . . . 0.2822 
'X-RAY DIFFRACTION' 2.31 2.40  . . 140 2638 98.00 . . . . 0.2332 . . . . . . . . . . . 0.3048 
'X-RAY DIFFRACTION' 2.40 2.51  . . 133 2608 96.00 . . . . 0.2254 . . . . . . . . . . . 0.2677 
'X-RAY DIFFRACTION' 2.51 2.65  . . 140 2616 98.00 . . . . 0.2130 . . . . . . . . . . . 0.2737 
'X-RAY DIFFRACTION' 2.65 2.81  . . 156 2677 98.00 . . . . 0.2059 . . . . . . . . . . . 0.2421 
'X-RAY DIFFRACTION' 2.81 3.03  . . 158 2655 98.00 . . . . 0.1997 . . . . . . . . . . . 0.2102 
'X-RAY DIFFRACTION' 3.03 3.33  . . 143 2646 98.00 . . . . 0.1819 . . . . . . . . . . . 0.1991 
'X-RAY DIFFRACTION' 3.33 3.81  . . 120 2564 94.00 . . . . 0.1582 . . . . . . . . . . . 0.1909 
'X-RAY DIFFRACTION' 3.81 4.80  . . 148 2653 96.00 . . . . 0.1425 . . . . . . . . . . . 0.1664 
'X-RAY DIFFRACTION' 4.80 34.71 . . 124 2632 93.00 . . . . 0.1807 . . . . . . . . . . . 0.2060 
# 
_struct.entry_id                     8VAU 
_struct.title                        'Nicotinamide Riboside and CD38: Covalent Inhibition and Live-Cell Labeling' 
_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        8VAU 
_struct_keywords.text            'Nicotinamide Riboside, CD38, Nucleoside, Inhibitor, HYDROLASE, HYDROLASE-INHIBITOR complex' 
_struct_keywords.pdbx_keywords   HYDROLASE/INHIBITOR 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 1 ? 
C N N 2 ? 
D N N 3 ? 
E N N 2 ? 
F N N 3 ? 
G N N 4 ? 
H N N 4 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    CD38_HUMAN 
_struct_ref.pdbx_db_accession          P28907 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;RWRQQWSGPGTTKRFPETVLARCVKYTEIHPEMRHVDCQSVWDAFKGAFISKHPCNITEEDYQPLMKLGTQTVPCNKILL
WSRIKDLAHQFTQVQRDMFTLEDTLLGYLADDLTWCGEFNTSKINYQSCPDWRKDCSNNPVSVFWKTVSRRFAEAACDVV
HVMLNGSRSKIFDKNSTFGSVEVHNLQPEKVQTLEAWVIHGGREDSRDLCQDPTIKELESIISKRNIQFSCKNIYRPDKF
LQCVKNPEDSSCTSEI
;
_struct_ref.pdbx_align_begin           45 
# 
loop_
_struct_ref_seq.align_id 
_struct_ref_seq.ref_id 
_struct_ref_seq.pdbx_PDB_id_code 
_struct_ref_seq.pdbx_strand_id 
_struct_ref_seq.seq_align_beg 
_struct_ref_seq.pdbx_seq_align_beg_ins_code 
_struct_ref_seq.seq_align_end 
_struct_ref_seq.pdbx_seq_align_end_ins_code 
_struct_ref_seq.pdbx_db_accession 
_struct_ref_seq.db_align_beg 
_struct_ref_seq.pdbx_db_align_beg_ins_code 
_struct_ref_seq.db_align_end 
_struct_ref_seq.pdbx_db_align_end_ins_code 
_struct_ref_seq.pdbx_auth_seq_align_beg 
_struct_ref_seq.pdbx_auth_seq_align_end 
1 1 8VAU A 2 ? 257 ? P28907 45 ? 300 ? 45 300 
2 1 8VAU B 2 ? 257 ? P28907 45 ? 300 ? 45 300 
# 
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 8VAU SER A 1   ? UNP P28907 ?   ?   'expression tag'      44  1  
1 8VAU ASP A 57  ? UNP P28907 ASN 100 'engineered mutation' 100 2  
1 8VAU ALA A 121 ? UNP P28907 ASN 164 'engineered mutation' 164 3  
1 8VAU ASP A 166 ? UNP P28907 ASN 209 'engineered mutation' 209 4  
1 8VAU ASP A 176 ? UNP P28907 ASN 219 'engineered mutation' 219 5  
2 8VAU SER B 1   ? UNP P28907 ?   ?   'expression tag'      44  6  
2 8VAU ASP B 57  ? UNP P28907 ASN 100 'engineered mutation' 100 7  
2 8VAU ALA B 121 ? UNP P28907 ASN 164 'engineered mutation' 164 8  
2 8VAU ASP B 166 ? UNP P28907 ASN 209 'engineered mutation' 209 9  
2 8VAU ASP B 176 ? UNP P28907 ASN 219 'engineered mutation' 219 10 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_defined_assembly 
_pdbx_struct_assembly.method_details       ? 
_pdbx_struct_assembly.oligomeric_details   dimeric 
_pdbx_struct_assembly.oligomeric_count     2 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F,G,H 
# 
_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 ARG A 15  ? HIS A 31  ? ARG A 58  HIS A 74  1 ? 17 
HELX_P HELX_P2  AA2 PRO A 32  ? ARG A 35  ? PRO A 75  ARG A 78  5 ? 4  
HELX_P HELX_P3  AA3 ASP A 38  ? ILE A 51  ? ASP A 81  ILE A 94  1 ? 14 
HELX_P HELX_P4  AA4 THR A 59  ? ASP A 62  ? THR A 102 ASP A 105 5 ? 4  
HELX_P HELX_P5  AA5 TYR A 63  ? GLY A 70  ? TYR A 106 GLY A 113 1 ? 8  
HELX_P HELX_P6  AA6 ILE A 85  ? GLN A 96  ? ILE A 128 GLN A 139 1 ? 12 
HELX_P HELX_P7  AA7 THR A 101 ? ASP A 104 ? THR A 144 ASP A 147 5 ? 4  
HELX_P HELX_P8  AA8 THR A 105 ? ASP A 112 ? THR A 148 ASP A 155 1 ? 8  
HELX_P HELX_P9  AA9 ASN A 140 ? ALA A 157 ? ASN A 183 ALA A 200 1 ? 18 
HELX_P HELX_P10 AB1 SER A 177 ? VAL A 182 ? SER A 220 VAL A 225 1 ? 6  
HELX_P HELX_P11 AB2 ASP A 209 ? GLN A 212 ? ASP A 252 GLN A 255 5 ? 4  
HELX_P HELX_P12 AB3 ASP A 213 ? ARG A 226 ? ASP A 256 ARG A 269 1 ? 14 
HELX_P HELX_P13 AB4 ARG A 237 ? ASN A 247 ? ARG A 280 ASN A 290 1 ? 11 
HELX_P HELX_P14 AB5 ARG B 15  ? HIS B 31  ? ARG B 58  HIS B 74  1 ? 17 
HELX_P HELX_P15 AB6 PRO B 32  ? ARG B 35  ? PRO B 75  ARG B 78  5 ? 4  
HELX_P HELX_P16 AB7 ASP B 38  ? ILE B 51  ? ASP B 81  ILE B 94  1 ? 14 
HELX_P HELX_P17 AB8 THR B 59  ? ASP B 62  ? THR B 102 ASP B 105 5 ? 4  
HELX_P HELX_P18 AB9 TYR B 63  ? GLY B 70  ? TYR B 106 GLY B 113 1 ? 8  
HELX_P HELX_P19 AC1 ILE B 85  ? GLN B 96  ? ILE B 128 GLN B 139 1 ? 12 
HELX_P HELX_P20 AC2 THR B 101 ? ASP B 104 ? THR B 144 ASP B 147 5 ? 4  
HELX_P HELX_P21 AC3 THR B 105 ? ASP B 112 ? THR B 148 ASP B 155 1 ? 8  
HELX_P HELX_P22 AC4 ASN B 140 ? ALA B 157 ? ASN B 183 ALA B 200 1 ? 18 
HELX_P HELX_P23 AC5 SER B 177 ? VAL B 182 ? SER B 220 VAL B 225 1 ? 6  
HELX_P HELX_P24 AC6 ASP B 209 ? GLN B 212 ? ASP B 252 GLN B 255 5 ? 4  
HELX_P HELX_P25 AC7 ASP B 213 ? ARG B 226 ? ASP B 256 ARG B 269 1 ? 14 
HELX_P HELX_P26 AC8 ARG B 237 ? ASN B 247 ? ARG B 280 ASN B 290 1 ? 11 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
disulf1  disulf ?   ? A CYS 24  SG  ? ? ? 1_555 A CYS 39  SG ? ? A CYS 67  A CYS 82  1_555 ? ? ? ? ? ? ? 2.041 ? ? 
disulf2  disulf ?   ? A CYS 56  SG  ? ? ? 1_555 A CYS 137 SG ? ? A CYS 99  A CYS 180 1_555 ? ? ? ? ? ? ? 2.037 ? ? 
disulf3  disulf ?   ? A CYS 76  SG  ? ? ? 1_555 A CYS 158 SG ? ? A CYS 119 A CYS 201 1_555 ? ? ? ? ? ? ? 2.039 ? ? 
disulf4  disulf ?   ? A CYS 117 SG  ? ? ? 1_555 A CYS 130 SG ? ? A CYS 160 A CYS 173 1_555 ? ? ? ? ? ? ? 2.040 ? ? 
disulf5  disulf ?   ? A CYS 211 SG  ? ? ? 1_555 A CYS 232 SG ? ? A CYS 254 A CYS 275 1_555 ? ? ? ? ? ? ? 2.042 ? ? 
disulf6  disulf ?   ? B CYS 24  SG  ? ? ? 1_555 B CYS 39  SG ? ? B CYS 67  B CYS 82  1_555 ? ? ? ? ? ? ? 2.040 ? ? 
disulf7  disulf ?   ? B CYS 56  SG  ? ? ? 1_555 B CYS 137 SG ? ? B CYS 99  B CYS 180 1_555 ? ? ? ? ? ? ? 2.038 ? ? 
disulf8  disulf ?   ? B CYS 76  SG  ? ? ? 1_555 B CYS 158 SG ? ? B CYS 119 B CYS 201 1_555 ? ? ? ? ? ? ? 2.040 ? ? 
disulf9  disulf ?   ? B CYS 117 SG  ? ? ? 1_555 B CYS 130 SG ? ? B CYS 160 B CYS 173 1_555 ? ? ? ? ? ? ? 2.036 ? ? 
disulf10 disulf ?   ? B CYS 211 SG  ? ? ? 1_555 B CYS 232 SG ? ? B CYS 254 B CYS 275 1_555 ? ? ? ? ? ? ? 2.032 ? ? 
covale1  covale one ? A GLU 183 OE2 ? ? ? 1_555 D RIB .   C1 ? ? A GLU 226 A RIB 402 1_555 ? ? ? ? ? ? ? 1.374 ? ? 
covale2  covale one ? B GLU 183 OE2 ? ? ? 1_555 F RIB .   C1 ? ? B GLU 226 B RIB 402 1_555 ? ? ? ? ? ? ? 1.375 ? ? 
# 
loop_
_struct_conn_type.id 
_struct_conn_type.criteria 
_struct_conn_type.reference 
disulf ? ? 
covale ? ? 
# 
loop_
_pdbx_modification_feature.ordinal 
_pdbx_modification_feature.label_comp_id 
_pdbx_modification_feature.label_asym_id 
_pdbx_modification_feature.label_seq_id 
_pdbx_modification_feature.label_alt_id 
_pdbx_modification_feature.modified_residue_label_comp_id 
_pdbx_modification_feature.modified_residue_label_asym_id 
_pdbx_modification_feature.modified_residue_label_seq_id 
_pdbx_modification_feature.modified_residue_label_alt_id 
_pdbx_modification_feature.auth_comp_id 
_pdbx_modification_feature.auth_asym_id 
_pdbx_modification_feature.auth_seq_id 
_pdbx_modification_feature.PDB_ins_code 
_pdbx_modification_feature.symmetry 
_pdbx_modification_feature.modified_residue_auth_comp_id 
_pdbx_modification_feature.modified_residue_auth_asym_id 
_pdbx_modification_feature.modified_residue_auth_seq_id 
_pdbx_modification_feature.modified_residue_PDB_ins_code 
_pdbx_modification_feature.modified_residue_symmetry 
_pdbx_modification_feature.comp_id_linking_atom 
_pdbx_modification_feature.modified_residue_id_linking_atom 
_pdbx_modification_feature.modified_residue_id 
_pdbx_modification_feature.ref_pcm_id 
_pdbx_modification_feature.ref_comp_id 
_pdbx_modification_feature.type 
_pdbx_modification_feature.category 
1  RIB D .   ? GLU A 183 ? RIB A 402 ? 1_555 GLU A 226 ? 1_555 C1 OE2 GLU 2 RIB None Carbohydrate       
2  RIB F .   ? GLU B 183 ? RIB B 402 ? 1_555 GLU B 226 ? 1_555 C1 OE2 GLU 2 RIB None Carbohydrate       
3  CYS A 24  ? CYS A 39  ? CYS A 67  ? 1_555 CYS A 82  ? 1_555 SG SG  .   . .   None 'Disulfide bridge' 
4  CYS A 56  ? CYS A 137 ? CYS A 99  ? 1_555 CYS A 180 ? 1_555 SG SG  .   . .   None 'Disulfide bridge' 
5  CYS A 76  ? CYS A 158 ? CYS A 119 ? 1_555 CYS A 201 ? 1_555 SG SG  .   . .   None 'Disulfide bridge' 
6  CYS A 117 ? CYS A 130 ? CYS A 160 ? 1_555 CYS A 173 ? 1_555 SG SG  .   . .   None 'Disulfide bridge' 
7  CYS A 211 ? CYS A 232 ? CYS A 254 ? 1_555 CYS A 275 ? 1_555 SG SG  .   . .   None 'Disulfide bridge' 
8  CYS B 24  ? CYS B 39  ? CYS B 67  ? 1_555 CYS B 82  ? 1_555 SG SG  .   . .   None 'Disulfide bridge' 
9  CYS B 56  ? CYS B 137 ? CYS B 99  ? 1_555 CYS B 180 ? 1_555 SG SG  .   . .   None 'Disulfide bridge' 
10 CYS B 76  ? CYS B 158 ? CYS B 119 ? 1_555 CYS B 201 ? 1_555 SG SG  .   . .   None 'Disulfide bridge' 
11 CYS B 117 ? CYS B 130 ? CYS B 160 ? 1_555 CYS B 173 ? 1_555 SG SG  .   . .   None 'Disulfide bridge' 
12 CYS B 211 ? CYS B 232 ? CYS B 254 ? 1_555 CYS B 275 ? 1_555 SG SG  .   . .   None 'Disulfide bridge' 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 2 ? 
AA2 ? 4 ? 
AA3 ? 2 ? 
AA4 ? 4 ? 
# 
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 ? anti-parallel 
AA2 1 2 ? parallel      
AA2 2 3 ? parallel      
AA2 3 4 ? parallel      
AA3 1 2 ? anti-parallel 
AA4 1 2 ? parallel      
AA4 2 3 ? parallel      
AA4 3 4 ? 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 GLY A 9   ? PRO A 10  ? GLY A 52  PRO A 53  
AA1 2 SER A 129 ? CYS A 130 ? SER A 172 CYS A 173 
AA2 1 LEU A 80  ? SER A 83  ? LEU A 123 SER A 126 
AA2 2 ASP A 159 ? ASP A 166 ? ASP A 202 ASP A 209 
AA2 3 VAL A 192 ? ILE A 200 ? VAL A 235 ILE A 243 
AA2 4 GLN A 229 ? ILE A 235 ? GLN A 272 ILE A 278 
AA3 1 GLY B 9   ? PRO B 10  ? GLY B 52  PRO B 53  
AA3 2 SER B 129 ? CYS B 130 ? SER B 172 CYS B 173 
AA4 1 LEU B 80  ? SER B 83  ? LEU B 123 SER B 126 
AA4 2 ASP B 159 ? ASP B 166 ? ASP B 202 ASP B 209 
AA4 3 VAL B 192 ? ILE B 200 ? VAL B 235 ILE B 243 
AA4 4 GLN B 229 ? ILE B 235 ? GLN B 272 ILE B 278 
# 
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 GLY A 9   ? N GLY A 52  O CYS A 130 ? O CYS A 173 
AA2 1 2 N LEU A 81  ? N LEU A 124 O HIS A 162 ? O HIS A 205 
AA2 2 3 N VAL A 163 ? N VAL A 206 O TRP A 198 ? O TRP A 241 
AA2 3 4 N ALA A 197 ? N ALA A 240 O SER A 231 ? O SER A 274 
AA3 1 2 N GLY B 9   ? N GLY B 52  O CYS B 130 ? O CYS B 173 
AA4 1 2 N LEU B 81  ? N LEU B 124 O HIS B 162 ? O HIS B 205 
AA4 2 3 N LEU B 165 ? N LEU B 208 O ILE B 200 ? O ILE B 243 
AA4 3 4 N ALA B 197 ? N ALA B 240 O SER B 231 ? O SER B 274 
# 
_pdbx_entry_details.entry_id                   8VAU 
_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           ? 
_pdbx_entry_details.has_protein_modification   Y 
# 
loop_
_pdbx_validate_close_contact.id 
_pdbx_validate_close_contact.PDB_model_num 
_pdbx_validate_close_contact.auth_atom_id_1 
_pdbx_validate_close_contact.auth_asym_id_1 
_pdbx_validate_close_contact.auth_comp_id_1 
_pdbx_validate_close_contact.auth_seq_id_1 
_pdbx_validate_close_contact.PDB_ins_code_1 
_pdbx_validate_close_contact.label_alt_id_1 
_pdbx_validate_close_contact.auth_atom_id_2 
_pdbx_validate_close_contact.auth_asym_id_2 
_pdbx_validate_close_contact.auth_comp_id_2 
_pdbx_validate_close_contact.auth_seq_id_2 
_pdbx_validate_close_contact.PDB_ins_code_2 
_pdbx_validate_close_contact.label_alt_id_2 
_pdbx_validate_close_contact.dist 
1 1 OE1 A GLU 162 ? ? O  A HOH 501 ? ? 2.12 
2 1 O   A SER 213 ? ? O  A HOH 502 ? ? 2.19 
3 1 OD1 B ASP 81  ? ? O  B HOH 501 ? ? 2.19 
4 1 OE2 A GLU 226 ? ? O4 A RIB 402 ? ? 2.19 
# 
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 127 ? ? 70.95   -26.67  
2  1 ILE A 128 ? ? -106.79 78.28   
3  1 ASN A 182 ? ? -94.37  56.24   
4  1 ASP A 202 ? ? 63.36   -116.17 
5  1 VAL A 225 ? ? -124.73 -60.72  
6  1 PRO A 291 ? ? -82.49  44.74   
7  1 ARG B 127 ? ? 70.47   -25.52  
8  1 ILE B 128 ? ? -100.56 73.80   
9  1 CYS B 180 ? ? -173.41 146.59  
10 1 ASN B 182 ? ? -96.41  57.30   
11 1 ASP B 202 ? ? 60.80   -109.38 
12 1 VAL B 225 ? ? -128.21 -56.69  
13 1 ARG B 247 ? ? 69.38   75.77   
# 
loop_
_pdbx_refine_tls.pdbx_refine_id 
_pdbx_refine_tls.id 
_pdbx_refine_tls.details 
_pdbx_refine_tls.method 
_pdbx_refine_tls.origin_x 
_pdbx_refine_tls.origin_y 
_pdbx_refine_tls.origin_z 
_pdbx_refine_tls.T[1][1] 
_pdbx_refine_tls.T[2][2] 
_pdbx_refine_tls.T[3][3] 
_pdbx_refine_tls.T[1][2] 
_pdbx_refine_tls.T[1][3] 
_pdbx_refine_tls.T[2][3] 
_pdbx_refine_tls.L[1][1] 
_pdbx_refine_tls.L[2][2] 
_pdbx_refine_tls.L[3][3] 
_pdbx_refine_tls.L[1][2] 
_pdbx_refine_tls.L[1][3] 
_pdbx_refine_tls.L[2][3] 
_pdbx_refine_tls.S[1][1] 
_pdbx_refine_tls.S[2][2] 
_pdbx_refine_tls.S[3][3] 
_pdbx_refine_tls.S[1][2] 
_pdbx_refine_tls.S[1][3] 
_pdbx_refine_tls.S[2][3] 
_pdbx_refine_tls.S[2][1] 
_pdbx_refine_tls.S[3][1] 
_pdbx_refine_tls.S[3][2] 
'X-RAY DIFFRACTION' 1 ? refined -13.516 -0.802  -6.427  0.2289 0.2425 0.2458 -0.0004 -0.0208 -0.0079 0.5439 0.8590 0.2710 -0.1702 
0.1118 -0.1782 0.0267  -0.0081 0.0000  -0.0218 -0.0146 -0.0209 0.0156  -0.0143 0.0044 
'X-RAY DIFFRACTION' 2 ? refined -9.196  -21.728 -39.748 0.2585 0.2638 0.2397 0.0212  0.0354  -0.0021 0.2626 1.2756 0.6842 0.0002  
0.0021 -0.4143 -0.0127 -0.0426 -0.0000 -0.0098 0.0223  -0.1463 -0.0429 0.0583  0.0391 
# 
loop_
_pdbx_refine_tls_group.pdbx_refine_id 
_pdbx_refine_tls_group.id 
_pdbx_refine_tls_group.refine_tls_id 
_pdbx_refine_tls_group.beg_auth_asym_id 
_pdbx_refine_tls_group.beg_auth_seq_id 
_pdbx_refine_tls_group.end_auth_asym_id 
_pdbx_refine_tls_group.end_auth_seq_id 
_pdbx_refine_tls_group.selection_details 
_pdbx_refine_tls_group.beg_label_asym_id 
_pdbx_refine_tls_group.beg_label_seq_id 
_pdbx_refine_tls_group.end_label_asym_id 
_pdbx_refine_tls_group.end_label_seq_id 
_pdbx_refine_tls_group.selection 
'X-RAY DIFFRACTION' 1 1 A 44  A 292 '( CHAIN A AND  ( RESID 44:292 OR RESID 401:402 )  )' ? ? ? ? ? 
'X-RAY DIFFRACTION' 2 1 A 401 A 402 '( CHAIN A AND  ( RESID 44:292 OR RESID 401:402 )  )' ? ? ? ? ? 
'X-RAY DIFFRACTION' 3 2 B 44  B 293 '( CHAIN B AND  ( RESID 44:293 OR RESID 401:402 )  )' ? ? ? ? ? 
'X-RAY DIFFRACTION' 4 2 B 401 B 402 '( CHAIN B AND  ( RESID 44:293 OR RESID 401:402 )  )' ? ? ? ? ? 
# 
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 ASP 293 ? A ASP 250 
2  1 Y 1 A SER 294 ? A SER 251 
3  1 Y 1 A SER 295 ? A SER 252 
4  1 Y 1 A CYS 296 ? A CYS 253 
5  1 Y 1 A THR 297 ? A THR 254 
6  1 Y 1 A SER 298 ? A SER 255 
7  1 Y 1 A GLU 299 ? A GLU 256 
8  1 Y 1 A ILE 300 ? A ILE 257 
9  1 Y 1 B SER 294 ? B SER 251 
10 1 Y 1 B SER 295 ? B SER 252 
11 1 Y 1 B CYS 296 ? B CYS 253 
12 1 Y 1 B THR 297 ? B THR 254 
13 1 Y 1 B SER 298 ? B SER 255 
14 1 Y 1 B GLU 299 ? B GLU 256 
15 1 Y 1 B ILE 300 ? B ILE 257 
# 
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  
GLN N    N N N 88  
GLN CA   C N S 89  
GLN C    C N N 90  
GLN O    O N N 91  
GLN CB   C N N 92  
GLN CG   C N N 93  
GLN CD   C N N 94  
GLN OE1  O N N 95  
GLN NE2  N N N 96  
GLN OXT  O N N 97  
GLN H    H N N 98  
GLN H2   H N N 99  
GLN HA   H N N 100 
GLN HB2  H N N 101 
GLN HB3  H N N 102 
GLN HG2  H N N 103 
GLN HG3  H N N 104 
GLN HE21 H N N 105 
GLN HE22 H N N 106 
GLN HXT  H N N 107 
GLU N    N N N 108 
GLU CA   C N S 109 
GLU C    C N N 110 
GLU O    O N N 111 
GLU CB   C N N 112 
GLU CG   C N N 113 
GLU CD   C N N 114 
GLU OE1  O N N 115 
GLU OE2  O N N 116 
GLU OXT  O N N 117 
GLU H    H N N 118 
GLU H2   H N N 119 
GLU HA   H N N 120 
GLU HB2  H N N 121 
GLU HB3  H N N 122 
GLU HG2  H N N 123 
GLU HG3  H N N 124 
GLU HE2  H N N 125 
GLU HXT  H N N 126 
GLY N    N N N 127 
GLY CA   C N N 128 
GLY C    C N N 129 
GLY O    O N N 130 
GLY OXT  O N N 131 
GLY H    H N N 132 
GLY H2   H N N 133 
GLY HA2  H N N 134 
GLY HA3  H N N 135 
GLY HXT  H N N 136 
HIS N    N N N 137 
HIS CA   C N S 138 
HIS C    C N N 139 
HIS O    O N N 140 
HIS CB   C N N 141 
HIS CG   C Y N 142 
HIS ND1  N Y N 143 
HIS CD2  C Y N 144 
HIS CE1  C Y N 145 
HIS NE2  N Y N 146 
HIS OXT  O N N 147 
HIS H    H N N 148 
HIS H2   H N N 149 
HIS HA   H N N 150 
HIS HB2  H N N 151 
HIS HB3  H N N 152 
HIS HD1  H N N 153 
HIS HD2  H N N 154 
HIS HE1  H N N 155 
HIS HE2  H N N 156 
HIS HXT  H N N 157 
HOH O    O N N 158 
HOH H1   H N N 159 
HOH H2   H N N 160 
ILE N    N N N 161 
ILE CA   C N S 162 
ILE C    C N N 163 
ILE O    O N N 164 
ILE CB   C N S 165 
ILE CG1  C N N 166 
ILE CG2  C N N 167 
ILE CD1  C N N 168 
ILE OXT  O N N 169 
ILE H    H N N 170 
ILE H2   H N N 171 
ILE HA   H N N 172 
ILE HB   H N N 173 
ILE HG12 H N N 174 
ILE HG13 H N N 175 
ILE HG21 H N N 176 
ILE HG22 H N N 177 
ILE HG23 H N N 178 
ILE HD11 H N N 179 
ILE HD12 H N N 180 
ILE HD13 H N N 181 
ILE HXT  H N N 182 
LEU N    N N N 183 
LEU CA   C N S 184 
LEU C    C N N 185 
LEU O    O N N 186 
LEU CB   C N N 187 
LEU CG   C N N 188 
LEU CD1  C N N 189 
LEU CD2  C N N 190 
LEU OXT  O N N 191 
LEU H    H N N 192 
LEU H2   H N N 193 
LEU HA   H N N 194 
LEU HB2  H N N 195 
LEU HB3  H N N 196 
LEU HG   H N N 197 
LEU HD11 H N N 198 
LEU HD12 H N N 199 
LEU HD13 H N N 200 
LEU HD21 H N N 201 
LEU HD22 H N N 202 
LEU HD23 H N N 203 
LEU HXT  H N N 204 
LYS N    N N N 205 
LYS CA   C N S 206 
LYS C    C N N 207 
LYS O    O N N 208 
LYS CB   C N N 209 
LYS CG   C N N 210 
LYS CD   C N N 211 
LYS CE   C N N 212 
LYS NZ   N N N 213 
LYS OXT  O N N 214 
LYS H    H N N 215 
LYS H2   H N N 216 
LYS HA   H N N 217 
LYS HB2  H N N 218 
LYS HB3  H N N 219 
LYS HG2  H N N 220 
LYS HG3  H N N 221 
LYS HD2  H N N 222 
LYS HD3  H N N 223 
LYS HE2  H N N 224 
LYS HE3  H N N 225 
LYS HZ1  H N N 226 
LYS HZ2  H N N 227 
LYS HZ3  H N N 228 
LYS HXT  H N N 229 
MET N    N N N 230 
MET CA   C N S 231 
MET C    C N N 232 
MET O    O N N 233 
MET CB   C N N 234 
MET CG   C N N 235 
MET SD   S N N 236 
MET CE   C N N 237 
MET OXT  O N N 238 
MET H    H N N 239 
MET H2   H N N 240 
MET HA   H N N 241 
MET HB2  H N N 242 
MET HB3  H N N 243 
MET HG2  H N N 244 
MET HG3  H N N 245 
MET HE1  H N N 246 
MET HE2  H N N 247 
MET HE3  H N N 248 
MET HXT  H N N 249 
NNR O2R  O N N 250 
NNR C2R  C N R 251 
NNR C3R  C N S 252 
NNR O3R  O N N 253 
NNR C4R  C N R 254 
NNR C5R  C N N 255 
NNR O5R  O N N 256 
NNR O4R  O N N 257 
NNR C1R  C N R 258 
NNR N1   N Y N 259 
NNR C2   C Y N 260 
NNR C6   C Y N 261 
NNR C5   C Y N 262 
NNR C4   C Y N 263 
NNR C3   C Y N 264 
NNR C7   C N N 265 
NNR O7   O N N 266 
NNR N7   N N N 267 
NNR HO2R H N N 268 
NNR H2R  H N N 269 
NNR H3R  H N N 270 
NNR HO3R H N N 271 
NNR H4R  H N N 272 
NNR H5R1 H N N 273 
NNR H5R2 H N N 274 
NNR HO5R H N N 275 
NNR H1R  H N N 276 
NNR H2   H N N 277 
NNR H6   H N N 278 
NNR H5   H N N 279 
NNR H4   H N N 280 
NNR HN71 H N N 281 
NNR HN72 H N N 282 
PHE N    N N N 283 
PHE CA   C N S 284 
PHE C    C N N 285 
PHE O    O N N 286 
PHE CB   C N N 287 
PHE CG   C Y N 288 
PHE CD1  C Y N 289 
PHE CD2  C Y N 290 
PHE CE1  C Y N 291 
PHE CE2  C Y N 292 
PHE CZ   C Y N 293 
PHE OXT  O N N 294 
PHE H    H N N 295 
PHE H2   H N N 296 
PHE HA   H N N 297 
PHE HB2  H N N 298 
PHE HB3  H N N 299 
PHE HD1  H N N 300 
PHE HD2  H N N 301 
PHE HE1  H N N 302 
PHE HE2  H N N 303 
PHE HZ   H N N 304 
PHE HXT  H N N 305 
PRO N    N N N 306 
PRO CA   C N S 307 
PRO C    C N N 308 
PRO O    O N N 309 
PRO CB   C N N 310 
PRO CG   C N N 311 
PRO CD   C N N 312 
PRO OXT  O N N 313 
PRO H    H N N 314 
PRO HA   H N N 315 
PRO HB2  H N N 316 
PRO HB3  H N N 317 
PRO HG2  H N N 318 
PRO HG3  H N N 319 
PRO HD2  H N N 320 
PRO HD3  H N N 321 
PRO HXT  H N N 322 
RIB O5   O N N 323 
RIB C5   C N N 324 
RIB C4   C N R 325 
RIB O4   O N N 326 
RIB C3   C N S 327 
RIB O3   O N N 328 
RIB C2   C N R 329 
RIB O2   O N N 330 
RIB C1   C N S 331 
RIB O1   O N N 332 
RIB HO5  H N N 333 
RIB H51  H N N 334 
RIB H52  H N N 335 
RIB H4   H N N 336 
RIB H3   H N N 337 
RIB HO3  H N N 338 
RIB H2   H N N 339 
RIB HO2  H N N 340 
RIB H1   H N N 341 
RIB HO1  H N N 342 
SER N    N N N 343 
SER CA   C N S 344 
SER C    C N N 345 
SER O    O N N 346 
SER CB   C N N 347 
SER OG   O N N 348 
SER OXT  O N N 349 
SER H    H N N 350 
SER H2   H N N 351 
SER HA   H N N 352 
SER HB2  H N N 353 
SER HB3  H N N 354 
SER HG   H N N 355 
SER HXT  H N N 356 
THR N    N N N 357 
THR CA   C N S 358 
THR C    C N N 359 
THR O    O N N 360 
THR CB   C N R 361 
THR OG1  O N N 362 
THR CG2  C N N 363 
THR OXT  O N N 364 
THR H    H N N 365 
THR H2   H N N 366 
THR HA   H N N 367 
THR HB   H N N 368 
THR HG1  H N N 369 
THR HG21 H N N 370 
THR HG22 H N N 371 
THR HG23 H N N 372 
THR HXT  H N N 373 
TRP N    N N N 374 
TRP CA   C N S 375 
TRP C    C N N 376 
TRP O    O N N 377 
TRP CB   C N N 378 
TRP CG   C Y N 379 
TRP CD1  C Y N 380 
TRP CD2  C Y N 381 
TRP NE1  N Y N 382 
TRP CE2  C Y N 383 
TRP CE3  C Y N 384 
TRP CZ2  C Y N 385 
TRP CZ3  C Y N 386 
TRP CH2  C Y N 387 
TRP OXT  O N N 388 
TRP H    H N N 389 
TRP H2   H N N 390 
TRP HA   H N N 391 
TRP HB2  H N N 392 
TRP HB3  H N N 393 
TRP HD1  H N N 394 
TRP HE1  H N N 395 
TRP HE3  H N N 396 
TRP HZ2  H N N 397 
TRP HZ3  H N N 398 
TRP HH2  H N N 399 
TRP HXT  H N N 400 
TYR N    N N N 401 
TYR CA   C N S 402 
TYR C    C N N 403 
TYR O    O N N 404 
TYR CB   C N N 405 
TYR CG   C Y N 406 
TYR CD1  C Y N 407 
TYR CD2  C Y N 408 
TYR CE1  C Y N 409 
TYR CE2  C Y N 410 
TYR CZ   C Y N 411 
TYR OH   O N N 412 
TYR OXT  O N N 413 
TYR H    H N N 414 
TYR H2   H N N 415 
TYR HA   H N N 416 
TYR HB2  H N N 417 
TYR HB3  H N N 418 
TYR HD1  H N N 419 
TYR HD2  H N N 420 
TYR HE1  H N N 421 
TYR HE2  H N N 422 
TYR HH   H N N 423 
TYR HXT  H N N 424 
VAL N    N N N 425 
VAL CA   C N S 426 
VAL C    C N N 427 
VAL O    O N N 428 
VAL CB   C N N 429 
VAL CG1  C N N 430 
VAL CG2  C N N 431 
VAL OXT  O N N 432 
VAL H    H N N 433 
VAL H2   H N N 434 
VAL HA   H N N 435 
VAL HB   H N N 436 
VAL HG11 H N N 437 
VAL HG12 H N N 438 
VAL HG13 H N N 439 
VAL HG21 H N N 440 
VAL HG22 H N N 441 
VAL HG23 H N N 442 
VAL HXT  H 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  
GLN N   CA   sing N N 83  
GLN N   H    sing N N 84  
GLN N   H2   sing N N 85  
GLN CA  C    sing N N 86  
GLN CA  CB   sing N N 87  
GLN CA  HA   sing N N 88  
GLN C   O    doub N N 89  
GLN C   OXT  sing N N 90  
GLN CB  CG   sing N N 91  
GLN CB  HB2  sing N N 92  
GLN CB  HB3  sing N N 93  
GLN CG  CD   sing N N 94  
GLN CG  HG2  sing N N 95  
GLN CG  HG3  sing N N 96  
GLN CD  OE1  doub N N 97  
GLN CD  NE2  sing N N 98  
GLN NE2 HE21 sing N N 99  
GLN NE2 HE22 sing N N 100 
GLN OXT HXT  sing N N 101 
GLU N   CA   sing N N 102 
GLU N   H    sing N N 103 
GLU N   H2   sing N N 104 
GLU CA  C    sing N N 105 
GLU CA  CB   sing N N 106 
GLU CA  HA   sing N N 107 
GLU C   O    doub N N 108 
GLU C   OXT  sing N N 109 
GLU CB  CG   sing N N 110 
GLU CB  HB2  sing N N 111 
GLU CB  HB3  sing N N 112 
GLU CG  CD   sing N N 113 
GLU CG  HG2  sing N N 114 
GLU CG  HG3  sing N N 115 
GLU CD  OE1  doub N N 116 
GLU CD  OE2  sing N N 117 
GLU OE2 HE2  sing N N 118 
GLU OXT HXT  sing N N 119 
GLY N   CA   sing N N 120 
GLY N   H    sing N N 121 
GLY N   H2   sing N N 122 
GLY CA  C    sing N N 123 
GLY CA  HA2  sing N N 124 
GLY CA  HA3  sing N N 125 
GLY C   O    doub N N 126 
GLY C   OXT  sing N N 127 
GLY OXT HXT  sing N N 128 
HIS N   CA   sing N N 129 
HIS N   H    sing N N 130 
HIS N   H2   sing N N 131 
HIS CA  C    sing N N 132 
HIS CA  CB   sing N N 133 
HIS CA  HA   sing N N 134 
HIS C   O    doub N N 135 
HIS C   OXT  sing N N 136 
HIS CB  CG   sing N N 137 
HIS CB  HB2  sing N N 138 
HIS CB  HB3  sing N N 139 
HIS CG  ND1  sing Y N 140 
HIS CG  CD2  doub Y N 141 
HIS ND1 CE1  doub Y N 142 
HIS ND1 HD1  sing N N 143 
HIS CD2 NE2  sing Y N 144 
HIS CD2 HD2  sing N N 145 
HIS CE1 NE2  sing Y N 146 
HIS CE1 HE1  sing N N 147 
HIS NE2 HE2  sing N N 148 
HIS OXT HXT  sing N N 149 
HOH O   H1   sing N N 150 
HOH O   H2   sing N N 151 
ILE N   CA   sing N N 152 
ILE N   H    sing N N 153 
ILE N   H2   sing N N 154 
ILE CA  C    sing N N 155 
ILE CA  CB   sing N N 156 
ILE CA  HA   sing N N 157 
ILE C   O    doub N N 158 
ILE C   OXT  sing N N 159 
ILE CB  CG1  sing N N 160 
ILE CB  CG2  sing N N 161 
ILE CB  HB   sing N N 162 
ILE CG1 CD1  sing N N 163 
ILE CG1 HG12 sing N N 164 
ILE CG1 HG13 sing N N 165 
ILE CG2 HG21 sing N N 166 
ILE CG2 HG22 sing N N 167 
ILE CG2 HG23 sing N N 168 
ILE CD1 HD11 sing N N 169 
ILE CD1 HD12 sing N N 170 
ILE CD1 HD13 sing N N 171 
ILE OXT HXT  sing N N 172 
LEU N   CA   sing N N 173 
LEU N   H    sing N N 174 
LEU N   H2   sing N N 175 
LEU CA  C    sing N N 176 
LEU CA  CB   sing N N 177 
LEU CA  HA   sing N N 178 
LEU C   O    doub N N 179 
LEU C   OXT  sing N N 180 
LEU CB  CG   sing N N 181 
LEU CB  HB2  sing N N 182 
LEU CB  HB3  sing N N 183 
LEU CG  CD1  sing N N 184 
LEU CG  CD2  sing N N 185 
LEU CG  HG   sing N N 186 
LEU CD1 HD11 sing N N 187 
LEU CD1 HD12 sing N N 188 
LEU CD1 HD13 sing N N 189 
LEU CD2 HD21 sing N N 190 
LEU CD2 HD22 sing N N 191 
LEU CD2 HD23 sing N N 192 
LEU OXT HXT  sing N N 193 
LYS N   CA   sing N N 194 
LYS N   H    sing N N 195 
LYS N   H2   sing N N 196 
LYS CA  C    sing N N 197 
LYS CA  CB   sing N N 198 
LYS CA  HA   sing N N 199 
LYS C   O    doub N N 200 
LYS C   OXT  sing N N 201 
LYS CB  CG   sing N N 202 
LYS CB  HB2  sing N N 203 
LYS CB  HB3  sing N N 204 
LYS CG  CD   sing N N 205 
LYS CG  HG2  sing N N 206 
LYS CG  HG3  sing N N 207 
LYS CD  CE   sing N N 208 
LYS CD  HD2  sing N N 209 
LYS CD  HD3  sing N N 210 
LYS CE  NZ   sing N N 211 
LYS CE  HE2  sing N N 212 
LYS CE  HE3  sing N N 213 
LYS NZ  HZ1  sing N N 214 
LYS NZ  HZ2  sing N N 215 
LYS NZ  HZ3  sing N N 216 
LYS OXT HXT  sing N N 217 
MET N   CA   sing N N 218 
MET N   H    sing N N 219 
MET N   H2   sing N N 220 
MET CA  C    sing N N 221 
MET CA  CB   sing N N 222 
MET CA  HA   sing N N 223 
MET C   O    doub N N 224 
MET C   OXT  sing N N 225 
MET CB  CG   sing N N 226 
MET CB  HB2  sing N N 227 
MET CB  HB3  sing N N 228 
MET CG  SD   sing N N 229 
MET CG  HG2  sing N N 230 
MET CG  HG3  sing N N 231 
MET SD  CE   sing N N 232 
MET CE  HE1  sing N N 233 
MET CE  HE2  sing N N 234 
MET CE  HE3  sing N N 235 
MET OXT HXT  sing N N 236 
NNR C5  C6   doub Y N 237 
NNR C5  C4   sing Y N 238 
NNR C6  N1   sing Y N 239 
NNR C4  C3   doub Y N 240 
NNR O2R C2R  sing N N 241 
NNR N1  C1R  sing N N 242 
NNR N1  C2   doub Y N 243 
NNR C3  C2   sing Y N 244 
NNR C3  C7   sing N N 245 
NNR C1R C2R  sing N N 246 
NNR C1R O4R  sing N N 247 
NNR C2R C3R  sing N N 248 
NNR C7  O7   doub N N 249 
NNR C7  N7   sing N N 250 
NNR O3R C3R  sing N N 251 
NNR O4R C4R  sing N N 252 
NNR C3R C4R  sing N N 253 
NNR C4R C5R  sing N N 254 
NNR C5R O5R  sing N N 255 
NNR O2R HO2R sing N N 256 
NNR C2R H2R  sing N N 257 
NNR C3R H3R  sing N N 258 
NNR O3R HO3R sing N N 259 
NNR C4R H4R  sing N N 260 
NNR C5R H5R1 sing N N 261 
NNR C5R H5R2 sing N N 262 
NNR O5R HO5R sing N N 263 
NNR C1R H1R  sing N N 264 
NNR C2  H2   sing N N 265 
NNR C6  H6   sing N N 266 
NNR C5  H5   sing N N 267 
NNR C4  H4   sing N N 268 
NNR N7  HN71 sing N N 269 
NNR N7  HN72 sing N N 270 
PHE N   CA   sing N N 271 
PHE N   H    sing N N 272 
PHE N   H2   sing N N 273 
PHE CA  C    sing N N 274 
PHE CA  CB   sing N N 275 
PHE CA  HA   sing N N 276 
PHE C   O    doub N N 277 
PHE C   OXT  sing N N 278 
PHE CB  CG   sing N N 279 
PHE CB  HB2  sing N N 280 
PHE CB  HB3  sing N N 281 
PHE CG  CD1  doub Y N 282 
PHE CG  CD2  sing Y N 283 
PHE CD1 CE1  sing Y N 284 
PHE CD1 HD1  sing N N 285 
PHE CD2 CE2  doub Y N 286 
PHE CD2 HD2  sing N N 287 
PHE CE1 CZ   doub Y N 288 
PHE CE1 HE1  sing N N 289 
PHE CE2 CZ   sing Y N 290 
PHE CE2 HE2  sing N N 291 
PHE CZ  HZ   sing N N 292 
PHE OXT HXT  sing N N 293 
PRO N   CA   sing N N 294 
PRO N   CD   sing N N 295 
PRO N   H    sing N N 296 
PRO CA  C    sing N N 297 
PRO CA  CB   sing N N 298 
PRO CA  HA   sing N N 299 
PRO C   O    doub N N 300 
PRO C   OXT  sing N N 301 
PRO CB  CG   sing N N 302 
PRO CB  HB2  sing N N 303 
PRO CB  HB3  sing N N 304 
PRO CG  CD   sing N N 305 
PRO CG  HG2  sing N N 306 
PRO CG  HG3  sing N N 307 
PRO CD  HD2  sing N N 308 
PRO CD  HD3  sing N N 309 
PRO OXT HXT  sing N N 310 
RIB O5  C5   sing N N 311 
RIB O5  HO5  sing N N 312 
RIB C5  C4   sing N N 313 
RIB C5  H51  sing N N 314 
RIB C5  H52  sing N N 315 
RIB C4  O4   sing N N 316 
RIB C4  C3   sing N N 317 
RIB C4  H4   sing N N 318 
RIB O4  C1   sing N N 319 
RIB C3  O3   sing N N 320 
RIB C3  C2   sing N N 321 
RIB C3  H3   sing N N 322 
RIB O3  HO3  sing N N 323 
RIB C2  O2   sing N N 324 
RIB C2  C1   sing N N 325 
RIB C2  H2   sing N N 326 
RIB O2  HO2  sing N N 327 
RIB C1  O1   sing N N 328 
RIB C1  H1   sing N N 329 
RIB O1  HO1  sing N N 330 
SER N   CA   sing N N 331 
SER N   H    sing N N 332 
SER N   H2   sing N N 333 
SER CA  C    sing N N 334 
SER CA  CB   sing N N 335 
SER CA  HA   sing N N 336 
SER C   O    doub N N 337 
SER C   OXT  sing N N 338 
SER CB  OG   sing N N 339 
SER CB  HB2  sing N N 340 
SER CB  HB3  sing N N 341 
SER OG  HG   sing N N 342 
SER OXT HXT  sing N N 343 
THR N   CA   sing N N 344 
THR N   H    sing N N 345 
THR N   H2   sing N N 346 
THR CA  C    sing N N 347 
THR CA  CB   sing N N 348 
THR CA  HA   sing N N 349 
THR C   O    doub N N 350 
THR C   OXT  sing N N 351 
THR CB  OG1  sing N N 352 
THR CB  CG2  sing N N 353 
THR CB  HB   sing N N 354 
THR OG1 HG1  sing N N 355 
THR CG2 HG21 sing N N 356 
THR CG2 HG22 sing N N 357 
THR CG2 HG23 sing N N 358 
THR OXT HXT  sing N N 359 
TRP N   CA   sing N N 360 
TRP N   H    sing N N 361 
TRP N   H2   sing N N 362 
TRP CA  C    sing N N 363 
TRP CA  CB   sing N N 364 
TRP CA  HA   sing N N 365 
TRP C   O    doub N N 366 
TRP C   OXT  sing N N 367 
TRP CB  CG   sing N N 368 
TRP CB  HB2  sing N N 369 
TRP CB  HB3  sing N N 370 
TRP CG  CD1  doub Y N 371 
TRP CG  CD2  sing Y N 372 
TRP CD1 NE1  sing Y N 373 
TRP CD1 HD1  sing N N 374 
TRP CD2 CE2  doub Y N 375 
TRP CD2 CE3  sing Y N 376 
TRP NE1 CE2  sing Y N 377 
TRP NE1 HE1  sing N N 378 
TRP CE2 CZ2  sing Y N 379 
TRP CE3 CZ3  doub Y N 380 
TRP CE3 HE3  sing N N 381 
TRP CZ2 CH2  doub Y N 382 
TRP CZ2 HZ2  sing N N 383 
TRP CZ3 CH2  sing Y N 384 
TRP CZ3 HZ3  sing N N 385 
TRP CH2 HH2  sing N N 386 
TRP OXT HXT  sing N N 387 
TYR N   CA   sing N N 388 
TYR N   H    sing N N 389 
TYR N   H2   sing N N 390 
TYR CA  C    sing N N 391 
TYR CA  CB   sing N N 392 
TYR CA  HA   sing N N 393 
TYR C   O    doub N N 394 
TYR C   OXT  sing N N 395 
TYR CB  CG   sing N N 396 
TYR CB  HB2  sing N N 397 
TYR CB  HB3  sing N N 398 
TYR CG  CD1  doub Y N 399 
TYR CG  CD2  sing Y N 400 
TYR CD1 CE1  sing Y N 401 
TYR CD1 HD1  sing N N 402 
TYR CD2 CE2  doub Y N 403 
TYR CD2 HD2  sing N N 404 
TYR CE1 CZ   doub Y N 405 
TYR CE1 HE1  sing N N 406 
TYR CE2 CZ   sing Y N 407 
TYR CE2 HE2  sing N N 408 
TYR CZ  OH   sing N N 409 
TYR OH  HH   sing N N 410 
TYR OXT HXT  sing N N 411 
VAL N   CA   sing N N 412 
VAL N   H    sing N N 413 
VAL N   H2   sing N N 414 
VAL CA  C    sing N N 415 
VAL CA  CB   sing N N 416 
VAL CA  HA   sing N N 417 
VAL C   O    doub N N 418 
VAL C   OXT  sing N N 419 
VAL CB  CG1  sing N N 420 
VAL CB  CG2  sing N N 421 
VAL CB  HB   sing N N 422 
VAL CG1 HG11 sing N N 423 
VAL CG1 HG12 sing N N 424 
VAL CG1 HG13 sing N N 425 
VAL CG2 HG21 sing N N 426 
VAL CG2 HG22 sing N N 427 
VAL CG2 HG23 sing N N 428 
VAL OXT HXT  sing N N 429 
# 
loop_
_pdbx_audit_support.funding_organization 
_pdbx_audit_support.country 
_pdbx_audit_support.grant_number 
_pdbx_audit_support.ordinal 
'National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)'              'United States' 
R35GM137901 1 
'National Institutes of Health/National Institute of Biomedical Imaging and Bioengineering (NIH/NIBIB)' 'United States' 
R01EB031830 2 
'National Institutes of Health/National Cancer Institute (NIH/NCI)'                                     'United States' 
R01CA276240 3 
'Other private'                                                                                         ?               ? 4 
# 
_pdbx_initial_refinement_model.accession_code   6EDR 
_pdbx_initial_refinement_model.details          ? 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.source_name      PDB 
_pdbx_initial_refinement_model.type             'experimental model' 
# 
_atom_sites.entry_id                    8VAU 
_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.Cartn_transform_axes        ? 
_atom_sites.fract_transf_matrix[1][1]   0.017353 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.002211 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.019474 
_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]   0.010031 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
C 
N 
O 
S 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N N   . SER A 1 1   ? -30.659 25.550  -5.622  1.00 54.70  ? 44  SER A N   1 
ATOM   2    C CA  . SER A 1 1   ? -32.063 25.335  -5.295  1.00 54.46  ? 44  SER A CA  1 
ATOM   3    C C   . SER A 1 1   ? -32.374 25.829  -3.891  1.00 48.63  ? 44  SER A C   1 
ATOM   4    O O   . SER A 1 1   ? -31.540 25.728  -2.991  1.00 49.37  ? 44  SER A O   1 
ATOM   5    C CB  . SER A 1 1   ? -32.423 23.853  -5.415  1.00 53.45  ? 44  SER A CB  1 
ATOM   6    O OG  . SER A 1 1   ? -33.715 23.594  -4.890  1.00 47.46  ? 44  SER A OG  1 
ATOM   7    N N   . ARG A 1 2   ? -33.584 26.353  -3.702  1.00 44.65  ? 45  ARG A N   1 
ATOM   8    C CA  . ARG A 1 2   ? -34.000 26.837  -2.393  1.00 44.23  ? 45  ARG A CA  1 
ATOM   9    C C   . ARG A 1 2   ? -34.427 25.712  -1.459  1.00 42.99  ? 45  ARG A C   1 
ATOM   10   O O   . ARG A 1 2   ? -34.760 25.988  -0.302  1.00 41.28  ? 45  ARG A O   1 
ATOM   11   C CB  . ARG A 1 2   ? -35.136 27.855  -2.534  1.00 44.20  ? 45  ARG A CB  1 
ATOM   12   C CG  . ARG A 1 2   ? -36.408 27.328  -3.185  1.00 44.86  ? 45  ARG A CG  1 
ATOM   13   C CD  . ARG A 1 2   ? -37.593 28.231  -2.855  1.00 48.58  ? 45  ARG A CD  1 
ATOM   14   N NE  . ARG A 1 2   ? -38.755 27.957  -3.691  1.00 50.40  ? 45  ARG A NE  1 
ATOM   15   C CZ  . ARG A 1 2   ? -39.964 28.462  -3.485  1.00 53.95  ? 45  ARG A CZ  1 
ATOM   16   N NH1 . ARG A 1 2   ? -40.214 29.263  -2.461  1.00 54.49  ? 45  ARG A NH1 1 
ATOM   17   N NH2 . ARG A 1 2   ? -40.949 28.155  -4.325  1.00 52.57  ? 45  ARG A NH2 1 
ATOM   18   N N   . TRP A 1 3   ? -34.434 24.464  -1.930  1.00 39.91  ? 46  TRP A N   1 
ATOM   19   C CA  . TRP A 1 3   ? -34.720 23.320  -1.080  1.00 40.41  ? 46  TRP A CA  1 
ATOM   20   C C   . TRP A 1 3   ? -33.485 22.500  -0.729  1.00 40.21  ? 46  TRP A C   1 
ATOM   21   O O   . TRP A 1 3   ? -33.594 21.564  0.071   1.00 39.53  ? 46  TRP A O   1 
ATOM   22   C CB  . TRP A 1 3   ? -35.739 22.384  -1.750  1.00 39.32  ? 46  TRP A CB  1 
ATOM   23   C CG  . TRP A 1 3   ? -36.785 23.059  -2.582  1.00 39.31  ? 46  TRP A CG  1 
ATOM   24   C CD1 . TRP A 1 3   ? -36.881 23.041  -3.944  1.00 36.37  ? 46  TRP A CD1 1 
ATOM   25   C CD2 . TRP A 1 3   ? -37.894 23.836  -2.112  1.00 35.46  ? 46  TRP A CD2 1 
ATOM   26   N NE1 . TRP A 1 3   ? -37.977 23.758  -4.350  1.00 37.75  ? 46  TRP A NE1 1 
ATOM   27   C CE2 . TRP A 1 3   ? -38.616 24.259  -3.246  1.00 36.87  ? 46  TRP A CE2 1 
ATOM   28   C CE3 . TRP A 1 3   ? -38.344 24.217  -0.844  1.00 35.20  ? 46  TRP A CE3 1 
ATOM   29   C CZ2 . TRP A 1 3   ? -39.762 25.044  -3.152  1.00 39.23  ? 46  TRP A CZ2 1 
ATOM   30   C CZ3 . TRP A 1 3   ? -39.484 24.997  -0.752  1.00 37.23  ? 46  TRP A CZ3 1 
ATOM   31   C CH2 . TRP A 1 3   ? -40.180 25.403  -1.899  1.00 39.59  ? 46  TRP A CH2 1 
ATOM   32   N N   . ARG A 1 4   ? -32.323 22.814  -1.300  1.00 40.78  ? 47  ARG A N   1 
ATOM   33   C CA  . ARG A 1 4   ? -31.162 21.943  -1.167  1.00 42.77  ? 47  ARG A CA  1 
ATOM   34   C C   . ARG A 1 4   ? -30.615 22.003  0.253   1.00 43.77  ? 47  ARG A C   1 
ATOM   35   O O   . ARG A 1 4   ? -30.283 23.082  0.755   1.00 40.56  ? 47  ARG A O   1 
ATOM   36   C CB  . ARG A 1 4   ? -30.082 22.338  -2.170  1.00 42.90  ? 47  ARG A CB  1 
ATOM   37   C CG  . ARG A 1 4   ? -29.050 21.242  -2.403  1.00 41.30  ? 47  ARG A CG  1 
ATOM   38   C CD  . ARG A 1 4   ? -28.130 21.563  -3.567  1.00 41.68  ? 47  ARG A CD  1 
ATOM   39   N NE  . ARG A 1 4   ? -27.099 22.528  -3.209  1.00 38.64  ? 47  ARG A NE  1 
ATOM   40   C CZ  . ARG A 1 4   ? -26.165 22.966  -4.042  1.00 40.71  ? 47  ARG A CZ  1 
ATOM   41   N NH1 . ARG A 1 4   ? -26.110 22.553  -5.298  1.00 37.51  ? 47  ARG A NH1 1 
ATOM   42   N NH2 . ARG A 1 4   ? -25.263 23.838  -3.604  1.00 43.00  ? 47  ARG A NH2 1 
ATOM   43   N N   . GLN A 1 5   ? -30.510 20.843  0.894   1.00 40.08  ? 48  GLN A N   1 
ATOM   44   C CA  . GLN A 1 5   ? -29.981 20.751  2.245   1.00 43.96  ? 48  GLN A CA  1 
ATOM   45   C C   . GLN A 1 5   ? -28.465 20.572  2.217   1.00 40.61  ? 48  GLN A C   1 
ATOM   46   O O   . GLN A 1 5   ? -27.872 20.207  1.199   1.00 36.62  ? 48  GLN A O   1 
ATOM   47   C CB  . GLN A 1 5   ? -30.633 19.591  3.004   1.00 44.25  ? 48  GLN A CB  1 
ATOM   48   C CG  . GLN A 1 5   ? -30.369 18.215  2.410   1.00 40.62  ? 48  GLN A CG  1 
ATOM   49   C CD  . GLN A 1 5   ? -31.451 17.209  2.768   1.00 43.23  ? 48  GLN A CD  1 
ATOM   50   O OE1 . GLN A 1 5   ? -32.458 17.083  2.064   1.00 38.65  ? 48  GLN A OE1 1 
ATOM   51   N NE2 . GLN A 1 5   ? -31.249 16.490  3.866   1.00 34.50  ? 48  GLN A NE2 1 
ATOM   52   N N   . GLN A 1 6   ? -27.843 20.849  3.358   1.00 42.35  ? 49  GLN A N   1 
ATOM   53   C CA  . GLN A 1 6   ? -26.409 20.656  3.514   1.00 39.46  ? 49  GLN A CA  1 
ATOM   54   C C   . GLN A 1 6   ? -26.114 19.202  3.859   1.00 35.49  ? 49  GLN A C   1 
ATOM   55   O O   . GLN A 1 6   ? -26.820 18.585  4.661   1.00 34.41  ? 49  GLN A O   1 
ATOM   56   C CB  . GLN A 1 6   ? -25.866 21.581  4.606   1.00 45.05  ? 49  GLN A CB  1 
ATOM   57   C CG  . GLN A 1 6   ? -24.380 21.423  4.908   1.00 46.81  ? 49  GLN A CG  1 
ATOM   58   C CD  . GLN A 1 6   ? -23.493 21.922  3.785   1.00 49.59  ? 49  GLN A CD  1 
ATOM   59   O OE1 . GLN A 1 6   ? -23.941 22.654  2.903   1.00 57.53  ? 49  GLN A OE1 1 
ATOM   60   N NE2 . GLN A 1 6   ? -22.224 21.528  3.814   1.00 48.17  ? 49  GLN A NE2 1 
ATOM   61   N N   . TRP A 1 7   ? -25.075 18.654  3.235   1.00 33.44  ? 50  TRP A N   1 
ATOM   62   C CA  . TRP A 1 7   ? -24.568 17.328  3.550   1.00 33.17  ? 50  TRP A CA  1 
ATOM   63   C C   . TRP A 1 7   ? -23.236 17.456  4.279   1.00 33.67  ? 50  TRP A C   1 
ATOM   64   O O   . TRP A 1 7   ? -22.586 18.504  4.247   1.00 31.21  ? 50  TRP A O   1 
ATOM   65   C CB  . TRP A 1 7   ? -24.386 16.481  2.285   1.00 29.27  ? 50  TRP A CB  1 
ATOM   66   C CG  . TRP A 1 7   ? -25.608 16.390  1.421   1.00 29.88  ? 50  TRP A CG  1 
ATOM   67   C CD1 . TRP A 1 7   ? -25.779 16.944  0.184   1.00 28.48  ? 50  TRP A CD1 1 
ATOM   68   C CD2 . TRP A 1 7   ? -26.830 15.706  1.725   1.00 29.68  ? 50  TRP A CD2 1 
ATOM   69   N NE1 . TRP A 1 7   ? -27.029 16.643  -0.301  1.00 29.37  ? 50  TRP A NE1 1 
ATOM   70   C CE2 . TRP A 1 7   ? -27.695 15.886  0.626   1.00 28.92  ? 50  TRP A CE2 1 
ATOM   71   C CE3 . TRP A 1 7   ? -27.277 14.957  2.818   1.00 31.20  ? 50  TRP A CE3 1 
ATOM   72   C CZ2 . TRP A 1 7   ? -28.977 15.346  0.589   1.00 29.43  ? 50  TRP A CZ2 1 
ATOM   73   C CZ3 . TRP A 1 7   ? -28.552 14.421  2.779   1.00 30.62  ? 50  TRP A CZ3 1 
ATOM   74   C CH2 . TRP A 1 7   ? -29.387 14.619  1.673   1.00 31.80  ? 50  TRP A CH2 1 
ATOM   75   N N   . SER A 1 8   ? -22.830 16.369  4.934   1.00 30.47  ? 51  SER A N   1 
ATOM   76   C CA  . SER A 1 8   ? -21.593 16.357  5.702   1.00 35.74  ? 51  SER A CA  1 
ATOM   77   C C   . SER A 1 8   ? -20.376 15.950  4.883   1.00 35.04  ? 51  SER A C   1 
ATOM   78   O O   . SER A 1 8   ? -19.246 16.164  5.336   1.00 36.88  ? 51  SER A O   1 
ATOM   79   C CB  . SER A 1 8   ? -21.723 15.407  6.897   1.00 36.78  ? 51  SER A CB  1 
ATOM   80   O OG  . SER A 1 8   ? -22.825 15.761  7.713   1.00 40.57  ? 51  SER A OG  1 
ATOM   81   N N   . GLY A 1 9   ? -20.571 15.369  3.703   1.00 31.21  ? 52  GLY A N   1 
ATOM   82   C CA  . GLY A 1 9   ? -19.468 14.918  2.891   1.00 29.32  ? 52  GLY A CA  1 
ATOM   83   C C   . GLY A 1 9   ? -19.021 15.970  1.897   1.00 30.51  ? 52  GLY A C   1 
ATOM   84   O O   . GLY A 1 9   ? -19.743 16.928  1.606   1.00 30.10  ? 52  GLY A O   1 
ATOM   85   N N   . PRO A 1 10  ? -17.819 15.805  1.343   1.00 32.72  ? 53  PRO A N   1 
ATOM   86   C CA  . PRO A 1 10  ? -17.332 16.772  0.352   1.00 32.18  ? 53  PRO A CA  1 
ATOM   87   C C   . PRO A 1 10  ? -18.236 16.816  -0.870  1.00 28.30  ? 53  PRO A C   1 
ATOM   88   O O   . PRO A 1 10  ? -18.922 15.847  -1.199  1.00 26.71  ? 53  PRO A O   1 
ATOM   89   C CB  . PRO A 1 10  ? -15.935 16.246  -0.009  1.00 34.37  ? 53  PRO A CB  1 
ATOM   90   C CG  . PRO A 1 10  ? -15.561 15.312  1.097   1.00 36.08  ? 53  PRO A CG  1 
ATOM   91   C CD  . PRO A 1 10  ? -16.843 14.731  1.599   1.00 31.13  ? 53  PRO A CD  1 
ATOM   92   N N   . GLY A 1 11  ? -18.238 17.963  -1.539  1.00 28.49  ? 54  GLY A N   1 
ATOM   93   C CA  . GLY A 1 11  ? -19.024 18.119  -2.743  1.00 30.75  ? 54  GLY A CA  1 
ATOM   94   C C   . GLY A 1 11  ? -18.411 17.391  -3.923  1.00 27.72  ? 54  GLY A C   1 
ATOM   95   O O   . GLY A 1 11  ? -17.309 16.843  -3.860  1.00 25.07  ? 54  GLY A O   1 
ATOM   96   N N   . THR A 1 12  ? -19.156 17.393  -5.028  1.00 27.26  ? 55  THR A N   1 
ATOM   97   C CA  . THR A 1 12  ? -18.691 16.747  -6.248  1.00 24.43  ? 55  THR A CA  1 
ATOM   98   C C   . THR A 1 12  ? -17.328 17.297  -6.646  1.00 27.27  ? 55  THR A C   1 
ATOM   99   O O   . THR A 1 12  ? -17.071 18.500  -6.542  1.00 25.86  ? 55  THR A O   1 
ATOM   100  C CB  . THR A 1 12  ? -19.692 16.971  -7.385  1.00 25.02  ? 55  THR A CB  1 
ATOM   101  O OG1 . THR A 1 12  ? -20.940 16.339  -7.070  1.00 23.81  ? 55  THR A OG1 1 
ATOM   102  C CG2 . THR A 1 12  ? -19.150 16.415  -8.693  1.00 24.53  ? 55  THR A CG2 1 
ATOM   103  N N   . THR A 1 13  ? -16.448 16.406  -7.095  1.00 24.16  ? 56  THR A N   1 
ATOM   104  C CA  . THR A 1 13  ? -15.128 16.826  -7.543  1.00 26.74  ? 56  THR A CA  1 
ATOM   105  C C   . THR A 1 13  ? -15.256 17.895  -8.621  1.00 27.33  ? 56  THR A C   1 
ATOM   106  O O   . THR A 1 13  ? -16.065 17.769  -9.544  1.00 23.63  ? 56  THR A O   1 
ATOM   107  C CB  . THR A 1 13  ? -14.345 15.631  -8.084  1.00 23.96  ? 56  THR A CB  1 
ATOM   108  O OG1 . THR A 1 13  ? -14.412 14.548  -7.150  1.00 26.77  ? 56  THR A OG1 1 
ATOM   109  C CG2 . THR A 1 13  ? -12.886 16.013  -8.321  1.00 28.75  ? 56  THR A CG2 1 
ATOM   110  N N   . LYS A 1 14  ? -14.454 18.950  -8.500  1.00 26.70  ? 57  LYS A N   1 
ATOM   111  C CA  . LYS A 1 14  ? -14.478 20.020  -9.486  1.00 28.54  ? 57  LYS A CA  1 
ATOM   112  C C   . LYS A 1 14  ? -14.172 19.468  -10.871 1.00 27.85  ? 57  LYS A C   1 
ATOM   113  O O   . LYS A 1 14  ? -13.305 18.606  -11.036 1.00 27.53  ? 57  LYS A O   1 
ATOM   114  C CB  . LYS A 1 14  ? -13.470 21.110  -9.110  1.00 33.65  ? 57  LYS A CB  1 
ATOM   115  C CG  . LYS A 1 14  ? -14.079 22.291  -8.355  1.00 46.35  ? 57  LYS A CG  1 
ATOM   116  C CD  . LYS A 1 14  ? -14.807 21.851  -7.085  1.00 49.56  ? 57  LYS A CD  1 
ATOM   117  C CE  . LYS A 1 14  ? -15.861 22.868  -6.660  1.00 49.44  ? 57  LYS A CE  1 
ATOM   118  N NZ  . LYS A 1 14  ? -15.285 24.052  -5.963  1.00 55.75  ? 57  LYS A NZ  1 
ATOM   119  N N   . ARG A 1 15  ? -14.905 19.961  -11.869 1.00 26.77  ? 58  ARG A N   1 
ATOM   120  C CA  . ARG A 1 15  ? -14.722 19.546  -13.259 1.00 29.40  ? 58  ARG A CA  1 
ATOM   121  C C   . ARG A 1 15  ? -15.056 18.068  -13.453 1.00 26.42  ? 58  ARG A C   1 
ATOM   122  O O   . ARG A 1 15  ? -14.479 17.399  -14.313 1.00 27.73  ? 58  ARG A O   1 
ATOM   123  C CB  . ARG A 1 15  ? -13.292 19.834  -13.732 1.00 29.51  ? 58  ARG A CB  1 
ATOM   124  C CG  . ARG A 1 15  ? -12.900 21.307  -13.685 1.00 37.21  ? 58  ARG A CG  1 
ATOM   125  C CD  . ARG A 1 15  ? -13.039 21.961  -15.048 1.00 36.10  ? 58  ARG A CD  1 
ATOM   126  N NE  . ARG A 1 15  ? -12.126 21.373  -16.022 1.00 36.97  ? 58  ARG A NE  1 
ATOM   127  C CZ  . ARG A 1 15  ? -12.140 21.639  -17.321 1.00 37.09  ? 58  ARG A CZ  1 
ATOM   128  N NH1 . ARG A 1 15  ? -13.001 22.498  -17.843 1.00 33.92  ? 58  ARG A NH1 1 
ATOM   129  N NH2 . ARG A 1 15  ? -11.270 21.024  -18.118 1.00 33.80  ? 58  ARG A NH2 1 
ATOM   130  N N   . PHE A 1 16  ? -15.996 17.553  -12.659 1.00 25.43  ? 59  PHE A N   1 
ATOM   131  C CA  . PHE A 1 16  ? -16.349 16.138  -12.746 1.00 26.98  ? 59  PHE A CA  1 
ATOM   132  C C   . PHE A 1 16  ? -16.801 15.740  -14.146 1.00 27.39  ? 59  PHE A C   1 
ATOM   133  O O   . PHE A 1 16  ? -16.291 14.735  -14.670 1.00 27.55  ? 59  PHE A O   1 
ATOM   134  C CB  . PHE A 1 16  ? -17.413 15.814  -11.689 1.00 24.19  ? 59  PHE A CB  1 
ATOM   135  C CG  . PHE A 1 16  ? -17.894 14.384  -11.718 1.00 25.46  ? 59  PHE A CG  1 
ATOM   136  C CD1 . PHE A 1 16  ? -17.094 13.356  -11.241 1.00 21.09  ? 59  PHE A CD1 1 
ATOM   137  C CD2 . PHE A 1 16  ? -19.151 14.073  -12.207 1.00 23.01  ? 59  PHE A CD2 1 
ATOM   138  C CE1 . PHE A 1 16  ? -17.537 12.046  -11.263 1.00 25.39  ? 59  PHE A CE1 1 
ATOM   139  C CE2 . PHE A 1 16  ? -19.600 12.762  -12.232 1.00 26.19  ? 59  PHE A CE2 1 
ATOM   140  C CZ  . PHE A 1 16  ? -18.792 11.749  -11.759 1.00 25.12  ? 59  PHE A CZ  1 
ATOM   141  N N   . PRO A 1 17  ? -17.713 16.460  -14.808 1.00 28.28  ? 60  PRO A N   1 
ATOM   142  C CA  . PRO A 1 17  ? -18.090 16.046  -16.174 1.00 28.10  ? 60  PRO A CA  1 
ATOM   143  C C   . PRO A 1 17  ? -16.907 15.992  -17.124 1.00 25.44  ? 60  PRO A C   1 
ATOM   144  O O   . PRO A 1 17  ? -16.717 14.993  -17.828 1.00 26.07  ? 60  PRO A O   1 
ATOM   145  C CB  . PRO A 1 17  ? -19.115 17.113  -16.592 1.00 28.35  ? 60  PRO A CB  1 
ATOM   146  C CG  . PRO A 1 17  ? -19.620 17.691  -15.316 1.00 30.73  ? 60  PRO A CG  1 
ATOM   147  C CD  . PRO A 1 17  ? -18.455 17.655  -14.371 1.00 31.80  ? 60  PRO A CD  1 
ATOM   148  N N   . GLU A 1 18  ? -16.091 17.047  -17.152 1.00 24.37  ? 61  GLU A N   1 
ATOM   149  C CA  . GLU A 1 18  ? -14.950 17.074  -18.058 1.00 26.40  ? 61  GLU A CA  1 
ATOM   150  C C   . GLU A 1 18  ? -13.929 16.000  -17.706 1.00 26.66  ? 61  GLU A C   1 
ATOM   151  O O   . GLU A 1 18  ? -13.262 15.463  -18.597 1.00 26.25  ? 61  GLU A O   1 
ATOM   152  C CB  . GLU A 1 18  ? -14.297 18.457  -18.038 1.00 30.83  ? 61  GLU A CB  1 
ATOM   153  C CG  . GLU A 1 18  ? -15.179 19.576  -18.589 1.00 33.84  ? 61  GLU A CG  1 
ATOM   154  C CD  . GLU A 1 18  ? -16.210 20.077  -17.588 1.00 39.00  ? 61  GLU A CD  1 
ATOM   155  O OE1 . GLU A 1 18  ? -16.106 19.729  -16.394 1.00 35.03  ? 61  GLU A OE1 1 
ATOM   156  O OE2 . GLU A 1 18  ? -17.125 20.825  -17.996 1.00 49.60  ? 61  GLU A OE2 1 
ATOM   157  N N   . THR A 1 19  ? -13.791 15.676  -16.418 1.00 25.21  ? 62  THR A N   1 
ATOM   158  C CA  . THR A 1 19  ? -12.834 14.653  -16.010 1.00 23.10  ? 62  THR A CA  1 
ATOM   159  C C   . THR A 1 19  ? -13.275 13.268  -16.468 1.00 25.55  ? 62  THR A C   1 
ATOM   160  O O   . THR A 1 19  ? -12.459 12.483  -16.963 1.00 24.99  ? 62  THR A O   1 
ATOM   161  C CB  . THR A 1 19  ? -12.656 14.687  -14.493 1.00 27.36  ? 62  THR A CB  1 
ATOM   162  O OG1 . THR A 1 19  ? -12.242 16.000  -14.091 1.00 30.04  ? 62  THR A OG1 1 
ATOM   163  C CG2 . THR A 1 19  ? -11.614 13.669  -14.050 1.00 28.54  ? 62  THR A CG2 1 
ATOM   164  N N   . VAL A 1 20  ? -14.562 12.949  -16.314 1.00 24.39  ? 63  VAL A N   1 
ATOM   165  C CA  . VAL A 1 20  ? -15.055 11.648  -16.754 1.00 24.44  ? 63  VAL A CA  1 
ATOM   166  C C   . VAL A 1 20  ? -14.933 11.518  -18.266 1.00 27.69  ? 63  VAL A C   1 
ATOM   167  O O   . VAL A 1 20  ? -14.510 10.475  -18.780 1.00 22.81  ? 63  VAL A O   1 
ATOM   168  C CB  . VAL A 1 20  ? -16.504 11.437  -16.276 1.00 24.48  ? 63  VAL A CB  1 
ATOM   169  C CG1 . VAL A 1 20  ? -17.117 10.214  -16.958 1.00 24.27  ? 63  VAL A CG1 1 
ATOM   170  C CG2 . VAL A 1 20  ? -16.538 11.284  -14.757 1.00 23.78  ? 63  VAL A CG2 1 
ATOM   171  N N   . LEU A 1 21  ? -15.289 12.572  -19.005 1.00 25.80  ? 64  LEU A N   1 
ATOM   172  C CA  . LEU A 1 21  ? -15.186 12.520  -20.460 1.00 27.44  ? 64  LEU A CA  1 
ATOM   173  C C   . LEU A 1 21  ? -13.744 12.292  -20.899 1.00 25.72  ? 64  LEU A C   1 
ATOM   174  O O   . LEU A 1 21  ? -13.467 11.421  -21.732 1.00 22.82  ? 64  LEU A O   1 
ATOM   175  C CB  . LEU A 1 21  ? -15.739 13.810  -21.068 1.00 28.42  ? 64  LEU A CB  1 
ATOM   176  C CG  . LEU A 1 21  ? -17.260 13.970  -21.050 1.00 29.45  ? 64  LEU A CG  1 
ATOM   177  C CD1 . LEU A 1 21  ? -17.647 15.405  -21.369 1.00 33.79  ? 64  LEU A CD1 1 
ATOM   178  C CD2 . LEU A 1 21  ? -17.909 13.017  -22.038 1.00 30.78  ? 64  LEU A CD2 1 
ATOM   179  N N   . ALA A 1 22  ? -12.807 13.058  -20.331 1.00 22.12  ? 65  ALA A N   1 
ATOM   180  C CA  . ALA A 1 22  ? -11.402 12.911  -20.700 1.00 24.92  ? 65  ALA A CA  1 
ATOM   181  C C   . ALA A 1 22  ? -10.878 11.522  -20.353 1.00 25.51  ? 65  ALA A C   1 
ATOM   182  O O   . ALA A 1 22  ? -10.075 10.949  -21.100 1.00 24.78  ? 65  ALA A O   1 
ATOM   183  C CB  . ALA A 1 22  ? -10.559 13.981  -20.007 1.00 25.98  ? 65  ALA A CB  1 
ATOM   184  N N   . ARG A 1 23  ? -11.291 10.978  -19.206 1.00 23.76  ? 66  ARG A N   1 
ATOM   185  C CA  . ARG A 1 23  ? -10.870 9.630   -18.839 1.00 25.80  ? 66  ARG A CA  1 
ATOM   186  C C   . ARG A 1 23  ? -11.407 8.594   -19.820 1.00 25.49  ? 66  ARG A C   1 
ATOM   187  O O   . ARG A 1 23  ? -10.683 7.677   -20.221 1.00 26.32  ? 66  ARG A O   1 
ATOM   188  C CB  . ARG A 1 23  ? -11.325 9.307   -17.416 1.00 23.90  ? 66  ARG A CB  1 
ATOM   189  C CG  . ARG A 1 23  ? -10.521 10.023  -16.341 1.00 26.30  ? 66  ARG A CG  1 
ATOM   190  C CD  . ARG A 1 23  ? -11.002 9.662   -14.948 1.00 25.34  ? 66  ARG A CD  1 
ATOM   191  N NE  . ARG A 1 23  ? -10.204 10.308  -13.914 1.00 22.74  ? 66  ARG A NE  1 
ATOM   192  C CZ  . ARG A 1 23  ? -10.256 10.002  -12.624 1.00 27.22  ? 66  ARG A CZ  1 
ATOM   193  N NH1 . ARG A 1 23  ? -11.050 9.045   -12.172 1.00 22.46  ? 66  ARG A NH1 1 
ATOM   194  N NH2 . ARG A 1 23  ? -9.491  10.673  -11.767 1.00 30.59  ? 66  ARG A NH2 1 
ATOM   195  N N   . CYS A 1 24  ? -12.677 8.724   -20.219 1.00 25.08  ? 67  CYS A N   1 
ATOM   196  C CA  . CYS A 1 24  ? -13.260 7.764   -21.152 1.00 26.77  ? 67  CYS A CA  1 
ATOM   197  C C   . CYS A 1 24  ? -12.516 7.769   -22.482 1.00 26.28  ? 67  CYS A C   1 
ATOM   198  O O   . CYS A 1 24  ? -12.220 6.706   -23.043 1.00 26.10  ? 67  CYS A O   1 
ATOM   199  C CB  . CYS A 1 24  ? -14.741 8.079   -21.370 1.00 27.97  ? 67  CYS A CB  1 
ATOM   200  S SG  . CYS A 1 24  ? -15.565 6.954   -22.525 1.00 26.45  ? 67  CYS A SG  1 
ATOM   201  N N   . VAL A 1 25  ? -12.214 8.958   -23.004 1.00 24.53  ? 68  VAL A N   1 
ATOM   202  C CA  . VAL A 1 25  ? -11.463 9.060   -24.252 1.00 25.33  ? 68  VAL A CA  1 
ATOM   203  C C   . VAL A 1 25  ? -10.073 8.463   -24.087 1.00 27.92  ? 68  VAL A C   1 
ATOM   204  O O   . VAL A 1 25  ? -9.576  7.754   -24.971 1.00 27.98  ? 68  VAL A O   1 
ATOM   205  C CB  . VAL A 1 25  ? -11.391 10.529  -24.709 1.00 29.03  ? 68  VAL A CB  1 
ATOM   206  C CG1 . VAL A 1 25  ? -10.342 10.698  -25.801 1.00 28.45  ? 68  VAL A CG1 1 
ATOM   207  C CG2 . VAL A 1 25  ? -12.754 11.006  -25.187 1.00 27.89  ? 68  VAL A CG2 1 
ATOM   208  N N   . LYS A 1 26  ? -9.409  8.760   -22.967 1.00 28.86  ? 69  LYS A N   1 
ATOM   209  C CA  . LYS A 1 26  ? -8.067  8.232   -22.751 1.00 26.40  ? 69  LYS A CA  1 
ATOM   210  C C   . LYS A 1 26  ? -8.088  6.713   -22.642 1.00 24.81  ? 69  LYS A C   1 
ATOM   211  O O   . LYS A 1 26  ? -7.215  6.032   -23.192 1.00 24.02  ? 69  LYS A O   1 
ATOM   212  C CB  . LYS A 1 26  ? -7.450  8.853   -21.496 1.00 27.83  ? 69  LYS A CB  1 
ATOM   213  C CG  . LYS A 1 26  ? -6.024  8.395   -21.200 1.00 33.74  ? 69  LYS A CG  1 
ATOM   214  C CD  . LYS A 1 26  ? -5.044  8.848   -22.276 1.00 43.34  ? 69  LYS A CD  1 
ATOM   215  C CE  . LYS A 1 26  ? -3.662  8.254   -22.045 1.00 53.80  ? 69  LYS A CE  1 
ATOM   216  N NZ  . LYS A 1 26  ? -2.624  8.878   -22.913 1.00 65.19  ? 69  LYS A NZ  1 
ATOM   217  N N   . TYR A 1 27  ? -9.079  6.161   -21.938 1.00 24.97  ? 70  TYR A N   1 
ATOM   218  C CA  . TYR A 1 27  ? -9.127  4.716   -21.745 1.00 26.21  ? 70  TYR A CA  1 
ATOM   219  C C   . TYR A 1 27  ? -9.290  3.992   -23.076 1.00 29.06  ? 70  TYR A C   1 
ATOM   220  O O   . TYR A 1 27  ? -8.593  3.008   -23.349 1.00 27.34  ? 70  TYR A O   1 
ATOM   221  C CB  . TYR A 1 27  ? -10.258 4.342   -20.786 1.00 25.65  ? 70  TYR A CB  1 
ATOM   222  C CG  . TYR A 1 27  ? -10.235 2.886   -20.363 1.00 27.17  ? 70  TYR A CG  1 
ATOM   223  C CD1 . TYR A 1 27  ? -10.867 1.911   -21.124 1.00 28.51  ? 70  TYR A CD1 1 
ATOM   224  C CD2 . TYR A 1 27  ? -9.572  2.486   -19.208 1.00 27.94  ? 70  TYR A CD2 1 
ATOM   225  C CE1 . TYR A 1 27  ? -10.843 0.578   -20.747 1.00 28.26  ? 70  TYR A CE1 1 
ATOM   226  C CE2 . TYR A 1 27  ? -9.543  1.154   -18.822 1.00 28.98  ? 70  TYR A CE2 1 
ATOM   227  C CZ  . TYR A 1 27  ? -10.180 0.205   -19.594 1.00 28.89  ? 70  TYR A CZ  1 
ATOM   228  O OH  . TYR A 1 27  ? -10.153 -1.120  -19.216 1.00 28.29  ? 70  TYR A OH  1 
ATOM   229  N N   . THR A 1 28  ? -10.202 4.476   -23.929 1.00 27.63  ? 71  THR A N   1 
ATOM   230  C CA  . THR A 1 28  ? -10.405 3.840   -25.226 1.00 28.87  ? 71  THR A CA  1 
ATOM   231  C C   . THR A 1 28  ? -9.193  4.023   -26.128 1.00 30.96  ? 71  THR A C   1 
ATOM   232  O O   . THR A 1 28  ? -8.942  3.193   -27.009 1.00 32.91  ? 71  THR A O   1 
ATOM   233  C CB  . THR A 1 28  ? -11.662 4.398   -25.895 1.00 30.15  ? 71  THR A CB  1 
ATOM   234  O OG1 . THR A 1 28  ? -11.531 5.815   -26.060 1.00 31.23  ? 71  THR A OG1 1 
ATOM   235  C CG2 . THR A 1 28  ? -12.895 4.097   -25.047 1.00 28.61  ? 71  THR A CG2 1 
ATOM   236  N N   . GLU A 1 29  ? -8.434  5.101   -25.928 1.00 29.80  ? 72  GLU A N   1 
ATOM   237  C CA  . GLU A 1 29  ? -7.172  5.261   -26.642 1.00 34.57  ? 72  GLU A CA  1 
ATOM   238  C C   . GLU A 1 29  ? -6.172  4.189   -26.227 1.00 34.03  ? 72  GLU A C   1 
ATOM   239  O O   . GLU A 1 29  ? -5.460  3.633   -27.072 1.00 36.44  ? 72  GLU A O   1 
ATOM   240  C CB  . GLU A 1 29  ? -6.605  6.659   -26.382 1.00 38.40  ? 72  GLU A CB  1 
ATOM   241  C CG  . GLU A 1 29  ? -5.257  6.935   -27.033 1.00 45.11  ? 72  GLU A CG  1 
ATOM   242  C CD  . GLU A 1 29  ? -4.699  8.299   -26.659 1.00 56.35  ? 72  GLU A CD  1 
ATOM   243  O OE1 . GLU A 1 29  ? -5.496  9.186   -26.284 1.00 54.94  ? 72  GLU A OE1 1 
ATOM   244  O OE2 . GLU A 1 29  ? -3.465  8.484   -26.732 1.00 62.19  ? 72  GLU A OE2 1 
ATOM   245  N N   . ILE A 1 30  ? -6.108  3.886   -24.929 1.00 31.86  ? 73  ILE A N   1 
ATOM   246  C CA  . ILE A 1 30  ? -5.147  2.906   -24.435 1.00 35.82  ? 73  ILE A CA  1 
ATOM   247  C C   . ILE A 1 30  ? -5.603  1.485   -24.741 1.00 36.08  ? 73  ILE A C   1 
ATOM   248  O O   . ILE A 1 30  ? -4.770  0.598   -24.960 1.00 35.64  ? 73  ILE A O   1 
ATOM   249  C CB  . ILE A 1 30  ? -4.921  3.100   -22.924 1.00 35.80  ? 73  ILE A CB  1 
ATOM   250  C CG1 . ILE A 1 30  ? -4.286  4.464   -22.641 1.00 39.82  ? 73  ILE A CG1 1 
ATOM   251  C CG2 . ILE A 1 30  ? -4.058  1.977   -22.357 1.00 39.47  ? 73  ILE A CG2 1 
ATOM   252  C CD1 . ILE A 1 30  ? -2.940  4.677   -23.309 1.00 49.27  ? 73  ILE A CD1 1 
ATOM   253  N N   . HIS A 1 31  ? -6.914  1.241   -24.763 1.00 35.29  ? 74  HIS A N   1 
ATOM   254  C CA  . HIS A 1 31  ? -7.472  -0.094  -24.954 1.00 34.84  ? 74  HIS A CA  1 
ATOM   255  C C   . HIS A 1 31  ? -8.218  -0.145  -26.280 1.00 31.91  ? 74  HIS A C   1 
ATOM   256  O O   . HIS A 1 31  ? -9.420  0.154   -26.335 1.00 31.15  ? 74  HIS A O   1 
ATOM   257  C CB  . HIS A 1 31  ? -8.402  -0.453  -23.793 1.00 33.82  ? 74  HIS A CB  1 
ATOM   258  C CG  . HIS A 1 31  ? -7.698  -0.586  -22.480 1.00 35.62  ? 74  HIS A CG  1 
ATOM   259  N ND1 . HIS A 1 31  ? -7.220  -1.791  -22.012 1.00 41.39  ? 74  HIS A ND1 1 
ATOM   260  C CD2 . HIS A 1 31  ? -7.380  0.335   -21.540 1.00 35.71  ? 74  HIS A CD2 1 
ATOM   261  C CE1 . HIS A 1 31  ? -6.644  -1.607  -20.837 1.00 38.67  ? 74  HIS A CE1 1 
ATOM   262  N NE2 . HIS A 1 31  ? -6.727  -0.326  -20.528 1.00 37.65  ? 74  HIS A NE2 1 
ATOM   263  N N   . PRO A 1 32  ? -7.560  -0.536  -27.375 1.00 34.53  ? 75  PRO A N   1 
ATOM   264  C CA  . PRO A 1 32  ? -8.258  -0.554  -28.672 1.00 34.85  ? 75  PRO A CA  1 
ATOM   265  C C   . PRO A 1 32  ? -9.492  -1.439  -28.683 1.00 34.31  ? 75  PRO A C   1 
ATOM   266  O O   . PRO A 1 32  ? -10.421 -1.178  -29.456 1.00 31.31  ? 75  PRO A O   1 
ATOM   267  C CB  . PRO A 1 32  ? -7.183  -1.071  -29.640 1.00 36.02  ? 75  PRO A CB  1 
ATOM   268  C CG  . PRO A 1 32  ? -5.888  -0.729  -28.988 1.00 35.41  ? 75  PRO A CG  1 
ATOM   269  C CD  . PRO A 1 32  ? -6.131  -0.869  -27.512 1.00 32.96  ? 75  PRO A CD  1 
ATOM   270  N N   . GLU A 1 33  ? -9.538  -2.475  -27.842 1.00 31.56  ? 76  GLU A N   1 
ATOM   271  C CA  . GLU A 1 33  ? -10.676 -3.385  -27.841 1.00 30.33  ? 76  GLU A CA  1 
ATOM   272  C C   . GLU A 1 33  ? -11.948 -2.741  -27.299 1.00 31.15  ? 76  GLU A C   1 
ATOM   273  O O   . GLU A 1 33  ? -13.016 -3.355  -27.390 1.00 32.20  ? 76  GLU A O   1 
ATOM   274  C CB  . GLU A 1 33  ? -10.343 -4.654  -27.039 1.00 33.48  ? 76  GLU A CB  1 
ATOM   275  C CG  . GLU A 1 33  ? -10.357 -4.508  -25.521 1.00 33.36  ? 76  GLU A CG  1 
ATOM   276  C CD  . GLU A 1 33  ? -9.135  -3.795  -24.978 1.00 34.45  ? 76  GLU A CD  1 
ATOM   277  O OE1 . GLU A 1 33  ? -8.348  -3.251  -25.781 1.00 31.62  ? 76  GLU A OE1 1 
ATOM   278  O OE2 . GLU A 1 33  ? -8.963  -3.782  -23.741 1.00 36.02  ? 76  GLU A OE2 1 
ATOM   279  N N   . MET A 1 34  ? -11.863 -1.537  -26.733 1.00 30.52  ? 77  MET A N   1 
ATOM   280  C CA  . MET A 1 34  ? -13.030 -0.832  -26.217 1.00 30.73  ? 77  MET A CA  1 
ATOM   281  C C   . MET A 1 34  ? -13.394 0.391   -27.051 1.00 30.63  ? 77  MET A C   1 
ATOM   282  O O   . MET A 1 34  ? -14.196 1.216   -26.603 1.00 27.47  ? 77  MET A O   1 
ATOM   283  C CB  . MET A 1 34  ? -12.790 -0.417  -24.763 1.00 31.10  ? 77  MET A CB  1 
ATOM   284  C CG  . MET A 1 34  ? -12.616 -1.588  -23.800 1.00 32.60  ? 77  MET A CG  1 
ATOM   285  S SD  . MET A 1 34  ? -14.101 -2.600  -23.626 1.00 33.13  ? 77  MET A SD  1 
ATOM   286  C CE  . MET A 1 34  ? -15.201 -1.464  -22.788 1.00 30.12  ? 77  MET A CE  1 
ATOM   287  N N   . ARG A 1 35  ? -12.846 0.520   -28.258 1.00 30.60  ? 78  ARG A N   1 
ATOM   288  C CA  . ARG A 1 35  ? -13.059 1.713   -29.070 1.00 33.25  ? 78  ARG A CA  1 
ATOM   289  C C   . ARG A 1 35  ? -14.436 1.760   -29.716 1.00 33.45  ? 78  ARG A C   1 
ATOM   290  O O   . ARG A 1 35  ? -14.758 2.753   -30.376 1.00 36.70  ? 78  ARG A O   1 
ATOM   291  C CB  . ARG A 1 35  ? -11.965 1.817   -30.134 1.00 32.76  ? 78  ARG A CB  1 
ATOM   292  C CG  . ARG A 1 35  ? -10.615 2.159   -29.528 1.00 34.78  ? 78  ARG A CG  1 
ATOM   293  C CD  . ARG A 1 35  ? -9.543  2.415   -30.565 1.00 36.95  ? 78  ARG A CD  1 
ATOM   294  N NE  . ARG A 1 35  ? -8.287  2.795   -29.928 1.00 39.61  ? 78  ARG A NE  1 
ATOM   295  C CZ  . ARG A 1 35  ? -7.137  2.963   -30.565 1.00 45.35  ? 78  ARG A CZ  1 
ATOM   296  N NH1 . ARG A 1 35  ? -7.041  2.803   -31.875 1.00 47.93  ? 78  ARG A NH1 1 
ATOM   297  N NH2 . ARG A 1 35  ? -6.053  3.297   -29.870 1.00 44.49  ? 78  ARG A NH2 1 
ATOM   298  N N   . HIS A 1 36  ? -15.252 0.720   -29.547 1.00 34.26  ? 79  HIS A N   1 
ATOM   299  C CA  . HIS A 1 36  ? -16.659 0.802   -29.916 1.00 34.50  ? 79  HIS A CA  1 
ATOM   300  C C   . HIS A 1 36  ? -17.444 1.731   -28.998 1.00 33.06  ? 79  HIS A C   1 
ATOM   301  O O   . HIS A 1 36  ? -18.575 2.097   -29.331 1.00 30.84  ? 79  HIS A O   1 
ATOM   302  C CB  . HIS A 1 36  ? -17.283 -0.592  -29.882 1.00 31.82  ? 79  HIS A CB  1 
ATOM   303  C CG  . HIS A 1 36  ? -17.251 -1.227  -28.527 1.00 32.03  ? 79  HIS A CG  1 
ATOM   304  N ND1 . HIS A 1 36  ? -16.193 -1.994  -28.090 1.00 35.02  ? 79  HIS A ND1 1 
ATOM   305  C CD2 . HIS A 1 36  ? -18.140 -1.195  -27.506 1.00 32.56  ? 79  HIS A CD2 1 
ATOM   306  C CE1 . HIS A 1 36  ? -16.434 -2.415  -26.861 1.00 33.46  ? 79  HIS A CE1 1 
ATOM   307  N NE2 . HIS A 1 36  ? -17.609 -1.943  -26.483 1.00 31.59  ? 79  HIS A NE2 1 
ATOM   308  N N   . VAL A 1 37  ? -16.869 2.117   -27.858 1.00 33.90  ? 80  VAL A N   1 
ATOM   309  C CA  . VAL A 1 37  ? -17.593 2.915   -26.877 1.00 34.04  ? 80  VAL A CA  1 
ATOM   310  C C   . VAL A 1 37  ? -17.757 4.337   -27.388 1.00 30.77  ? 80  VAL A C   1 
ATOM   311  O O   . VAL A 1 37  ? -16.817 4.938   -27.927 1.00 31.14  ? 80  VAL A O   1 
ATOM   312  C CB  . VAL A 1 37  ? -16.853 2.891   -25.525 1.00 32.77  ? 80  VAL A CB  1 
ATOM   313  C CG1 . VAL A 1 37  ? -17.406 3.954   -24.586 1.00 35.91  ? 80  VAL A CG1 1 
ATOM   314  C CG2 . VAL A 1 37  ? -16.954 1.510   -24.890 1.00 34.04  ? 80  VAL A CG2 1 
ATOM   315  N N   . ASP A 1 38  ? -18.964 4.882   -27.236 1.00 28.25  ? 81  ASP A N   1 
ATOM   316  C CA  . ASP A 1 38  ? -19.235 6.293   -27.492 1.00 34.56  ? 81  ASP A CA  1 
ATOM   317  C C   . ASP A 1 38  ? -19.187 7.018   -26.150 1.00 30.67  ? 81  ASP A C   1 
ATOM   318  O O   . ASP A 1 38  ? -20.076 6.847   -25.310 1.00 27.03  ? 81  ASP A O   1 
ATOM   319  C CB  . ASP A 1 38  ? -20.586 6.486   -28.176 1.00 33.59  ? 81  ASP A CB  1 
ATOM   320  C CG  . ASP A 1 38  ? -20.898 7.948   -28.452 1.00 39.70  ? 81  ASP A CG  1 
ATOM   321  O OD1 . ASP A 1 38  ? -20.160 8.587   -29.233 1.00 43.42  ? 81  ASP A OD1 1 
ATOM   322  O OD2 . ASP A 1 38  ? -21.886 8.459   -27.884 1.00 39.80  ? 81  ASP A OD2 1 
ATOM   323  N N   . CYS A 1 39  ? -18.149 7.828   -25.948 1.00 30.87  ? 82  CYS A N   1 
ATOM   324  C CA  . CYS A 1 39  ? -17.938 8.410   -24.628 1.00 31.26  ? 82  CYS A CA  1 
ATOM   325  C C   . CYS A 1 39  ? -19.024 9.418   -24.271 1.00 28.38  ? 82  CYS A C   1 
ATOM   326  O O   . CYS A 1 39  ? -19.316 9.606   -23.086 1.00 27.81  ? 82  CYS A O   1 
ATOM   327  C CB  . CYS A 1 39  ? -16.548 9.037   -24.550 1.00 29.91  ? 82  CYS A CB  1 
ATOM   328  S SG  . CYS A 1 39  ? -15.229 7.792   -24.356 1.00 40.41  ? 82  CYS A SG  1 
ATOM   329  N N   . GLN A 1 40  ? -19.636 10.073  -25.261 1.00 30.73  ? 83  GLN A N   1 
ATOM   330  C CA  A GLN A 1 40  ? -20.764 10.952  -24.957 0.53 31.29  ? 83  GLN A CA  1 
ATOM   331  C CA  B GLN A 1 40  ? -20.758 10.953  -24.947 0.47 31.32  ? 83  GLN A CA  1 
ATOM   332  C C   . GLN A 1 40  ? -21.914 10.157  -24.359 1.00 30.86  ? 83  GLN A C   1 
ATOM   333  O O   . GLN A 1 40  ? -22.537 10.588  -23.377 1.00 31.86  ? 83  GLN A O   1 
ATOM   334  C CB  A GLN A 1 40  ? -21.229 11.691  -26.215 0.53 34.10  ? 83  GLN A CB  1 
ATOM   335  C CB  B GLN A 1 40  ? -21.206 11.713  -26.194 0.47 34.12  ? 83  GLN A CB  1 
ATOM   336  C CG  A GLN A 1 40  ? -22.528 12.479  -26.009 0.53 35.96  ? 83  GLN A CG  1 
ATOM   337  C CG  B GLN A 1 40  ? -22.126 12.887  -25.885 0.47 36.70  ? 83  GLN A CG  1 
ATOM   338  C CD  A GLN A 1 40  ? -22.910 13.341  -27.201 0.53 39.64  ? 83  GLN A CD  1 
ATOM   339  C CD  B GLN A 1 40  ? -21.566 13.785  -24.795 0.47 38.39  ? 83  GLN A CD  1 
ATOM   340  O OE1 A GLN A 1 40  ? -22.818 12.911  -28.351 0.53 38.73  ? 83  GLN A OE1 1 
ATOM   341  O OE1 B GLN A 1 40  ? -22.041 13.778  -23.659 0.47 36.88  ? 83  GLN A OE1 1 
ATOM   342  N NE2 A GLN A 1 40  ? -23.341 14.570  -26.928 0.53 41.76  ? 83  GLN A NE2 1 
ATOM   343  N NE2 B GLN A 1 40  ? -20.536 14.543  -25.130 0.47 37.21  ? 83  GLN A NE2 1 
ATOM   344  N N   . SER A 1 41  ? -22.209 8.990   -24.930 1.00 28.88  ? 84  SER A N   1 
ATOM   345  C CA  . SER A 1 41  ? -23.256 8.137   -24.386 1.00 29.43  ? 84  SER A CA  1 
ATOM   346  C C   . SER A 1 41  ? -22.904 7.666   -22.981 1.00 25.57  ? 84  SER A C   1 
ATOM   347  O O   . SER A 1 41  ? -23.775 7.589   -22.107 1.00 24.69  ? 84  SER A O   1 
ATOM   348  C CB  . SER A 1 41  ? -23.486 6.942   -25.310 1.00 28.63  ? 84  SER A CB  1 
ATOM   349  O OG  . SER A 1 41  ? -23.911 7.369   -26.594 1.00 33.54  ? 84  SER A OG  1 
ATOM   350  N N   . VAL A 1 42  ? -21.629 7.343   -22.745 1.00 24.28  ? 85  VAL A N   1 
ATOM   351  C CA  . VAL A 1 42  ? -21.213 6.889   -21.420 1.00 26.07  ? 85  VAL A CA  1 
ATOM   352  C C   . VAL A 1 42  ? -21.486 7.970   -20.382 1.00 25.19  ? 85  VAL A C   1 
ATOM   353  O O   . VAL A 1 42  ? -22.135 7.724   -19.359 1.00 26.63  ? 85  VAL A O   1 
ATOM   354  C CB  . VAL A 1 42  ? -19.727 6.487   -21.430 1.00 26.57  ? 85  VAL A CB  1 
ATOM   355  C CG1 . VAL A 1 42  ? -19.234 6.201   -20.007 1.00 23.80  ? 85  VAL A CG1 1 
ATOM   356  C CG2 . VAL A 1 42  ? -19.511 5.285   -22.327 1.00 27.63  ? 85  VAL A CG2 1 
ATOM   357  N N   . TRP A 1 43  ? -21.016 9.193   -20.642 1.00 23.62  ? 86  TRP A N   1 
ATOM   358  C CA  . TRP A 1 43  ? -21.242 10.277  -19.692 1.00 29.75  ? 86  TRP A CA  1 
ATOM   359  C C   . TRP A 1 43  ? -22.730 10.537  -19.507 1.00 29.26  ? 86  TRP A C   1 
ATOM   360  O O   . TRP A 1 43  ? -23.198 10.757  -18.384 1.00 27.39  ? 86  TRP A O   1 
ATOM   361  C CB  . TRP A 1 43  ? -20.540 11.554  -20.156 1.00 27.52  ? 86  TRP A CB  1 
ATOM   362  C CG  . TRP A 1 43  ? -20.978 12.755  -19.375 1.00 30.28  ? 86  TRP A CG  1 
ATOM   363  C CD1 . TRP A 1 43  ? -21.507 13.911  -19.870 1.00 32.79  ? 86  TRP A CD1 1 
ATOM   364  C CD2 . TRP A 1 43  ? -20.949 12.904  -17.951 1.00 29.98  ? 86  TRP A CD2 1 
ATOM   365  N NE1 . TRP A 1 43  ? -21.801 14.775  -18.842 1.00 31.35  ? 86  TRP A NE1 1 
ATOM   366  C CE2 . TRP A 1 43  ? -21.468 14.179  -17.654 1.00 29.74  ? 86  TRP A CE2 1 
ATOM   367  C CE3 . TRP A 1 43  ? -20.531 12.084  -16.899 1.00 27.22  ? 86  TRP A CE3 1 
ATOM   368  C CZ2 . TRP A 1 43  ? -21.579 14.653  -16.349 1.00 28.20  ? 86  TRP A CZ2 1 
ATOM   369  C CZ3 . TRP A 1 43  ? -20.641 12.558  -15.604 1.00 26.20  ? 86  TRP A CZ3 1 
ATOM   370  C CH2 . TRP A 1 43  ? -21.161 13.828  -15.341 1.00 28.01  ? 86  TRP A CH2 1 
ATOM   371  N N   . ASP A 1 44  ? -23.491 10.508  -20.602 1.00 28.27  ? 87  ASP A N   1 
ATOM   372  C CA  . ASP A 1 44  ? -24.925 10.745  -20.511 1.00 30.45  ? 87  ASP A CA  1 
ATOM   373  C C   . ASP A 1 44  ? -25.598 9.717   -19.611 1.00 28.62  ? 87  ASP A C   1 
ATOM   374  O O   . ASP A 1 44  ? -26.489 10.061  -18.825 1.00 27.26  ? 87  ASP A O   1 
ATOM   375  C CB  . ASP A 1 44  ? -25.538 10.724  -21.910 1.00 37.83  ? 87  ASP A CB  1 
ATOM   376  C CG  . ASP A 1 44  ? -26.889 11.397  -21.962 1.00 44.71  ? 87  ASP A CG  1 
ATOM   377  O OD1 . ASP A 1 44  ? -27.754 11.063  -21.124 1.00 54.74  ? 87  ASP A OD1 1 
ATOM   378  O OD2 . ASP A 1 44  ? -27.083 12.268  -22.833 1.00 54.62  ? 87  ASP A OD2 1 
ATOM   379  N N   . ALA A 1 45  ? -25.196 8.446   -19.717 1.00 25.71  ? 88  ALA A N   1 
ATOM   380  C CA  . ALA A 1 45  ? -25.753 7.421   -18.839 1.00 28.00  ? 88  ALA A CA  1 
ATOM   381  C C   . ALA A 1 45  ? -25.263 7.592   -17.404 1.00 27.05  ? 88  ALA A C   1 
ATOM   382  O O   . ALA A 1 45  ? -26.024 7.382   -16.452 1.00 24.38  ? 88  ALA A O   1 
ATOM   383  C CB  . ALA A 1 45  ? -25.395 6.032   -19.363 1.00 28.59  ? 88  ALA A CB  1 
ATOM   384  N N   . PHE A 1 46  ? -23.992 7.960   -17.229 1.00 27.63  ? 89  PHE A N   1 
ATOM   385  C CA  . PHE A 1 46  ? -23.467 8.217   -15.891 1.00 24.43  ? 89  PHE A CA  1 
ATOM   386  C C   . PHE A 1 46  ? -24.237 9.349   -15.222 1.00 25.24  ? 89  PHE A C   1 
ATOM   387  O O   . PHE A 1 46  ? -24.753 9.199   -14.109 1.00 25.17  ? 89  PHE A O   1 
ATOM   388  C CB  . PHE A 1 46  ? -21.978 8.559   -15.988 1.00 26.00  ? 89  PHE A CB  1 
ATOM   389  C CG  . PHE A 1 46  ? -21.196 8.317   -14.721 1.00 24.72  ? 89  PHE A CG  1 
ATOM   390  C CD1 . PHE A 1 46  ? -21.800 8.374   -13.474 1.00 23.65  ? 89  PHE A CD1 1 
ATOM   391  C CD2 . PHE A 1 46  ? -19.840 8.036   -14.789 1.00 24.11  ? 89  PHE A CD2 1 
ATOM   392  C CE1 . PHE A 1 46  ? -21.063 8.149   -12.319 1.00 28.67  ? 89  PHE A CE1 1 
ATOM   393  C CE2 . PHE A 1 46  ? -19.101 7.813   -13.641 1.00 30.47  ? 89  PHE A CE2 1 
ATOM   394  C CZ  . PHE A 1 46  ? -19.711 7.869   -12.405 1.00 26.16  ? 89  PHE A CZ  1 
ATOM   395  N N   . LYS A 1 47  ? -24.340 10.486  -15.908 1.00 27.44  ? 90  LYS A N   1 
ATOM   396  C CA  . LYS A 1 47  ? -25.079 11.628  -15.382 1.00 28.60  ? 90  LYS A CA  1 
ATOM   397  C C   . LYS A 1 47  ? -26.528 11.263  -15.085 1.00 27.97  ? 90  LYS A C   1 
ATOM   398  O O   . LYS A 1 47  ? -27.086 11.683  -14.064 1.00 26.44  ? 90  LYS A O   1 
ATOM   399  C CB  . LYS A 1 47  ? -24.999 12.772  -16.393 1.00 32.85  ? 90  LYS A CB  1 
ATOM   400  C CG  . LYS A 1 47  ? -25.717 14.048  -16.006 1.00 35.85  ? 90  LYS A CG  1 
ATOM   401  C CD  . LYS A 1 47  ? -25.314 15.202  -16.929 1.00 38.99  ? 90  LYS A CD  1 
ATOM   402  C CE  . LYS A 1 47  ? -25.611 14.918  -18.401 1.00 43.09  ? 90  LYS A CE  1 
ATOM   403  N NZ  . LYS A 1 47  ? -26.673 15.807  -18.949 1.00 49.70  ? 90  LYS A NZ  1 
ATOM   404  N N   . GLY A 1 48  ? -27.154 10.477  -15.962 1.00 27.43  ? 91  GLY A N   1 
ATOM   405  C CA  . GLY A 1 48  ? -28.542 10.097  -15.763 1.00 29.86  ? 91  GLY A CA  1 
ATOM   406  C C   . GLY A 1 48  ? -28.781 9.240   -14.538 1.00 27.51  ? 91  GLY A C   1 
ATOM   407  O O   . GLY A 1 48  ? -29.925 9.130   -14.082 1.00 27.37  ? 91  GLY A O   1 
ATOM   408  N N   . ALA A 1 49  ? -27.731 8.628   -13.989 1.00 26.76  ? 92  ALA A N   1 
ATOM   409  C CA  . ALA A 1 49  ? -27.907 7.773   -12.821 1.00 26.09  ? 92  ALA A CA  1 
ATOM   410  C C   . ALA A 1 49  ? -28.252 8.577   -11.572 1.00 27.81  ? 92  ALA A C   1 
ATOM   411  O O   . ALA A 1 49  ? -29.017 8.100   -10.726 1.00 26.53  ? 92  ALA A O   1 
ATOM   412  C CB  . ALA A 1 49  ? -26.644 6.945   -12.582 1.00 25.29  ? 92  ALA A CB  1 
ATOM   413  N N   . PHE A 1 50  ? -27.710 9.790   -11.437 1.00 25.41  ? 93  PHE A N   1 
ATOM   414  C CA  . PHE A 1 50  ? -27.843 10.558  -10.203 1.00 24.43  ? 93  PHE A CA  1 
ATOM   415  C C   . PHE A 1 50  ? -28.347 11.983  -10.384 1.00 27.25  ? 93  PHE A C   1 
ATOM   416  O O   . PHE A 1 50  ? -28.819 12.570  -9.403  1.00 26.35  ? 93  PHE A O   1 
ATOM   417  C CB  . PHE A 1 50  ? -26.495 10.619  -9.469  1.00 24.38  ? 93  PHE A CB  1 
ATOM   418  C CG  . PHE A 1 50  ? -25.460 11.449  -10.175 1.00 24.39  ? 93  PHE A CG  1 
ATOM   419  C CD1 . PHE A 1 50  ? -24.688 10.904  -11.186 1.00 26.37  ? 93  PHE A CD1 1 
ATOM   420  C CD2 . PHE A 1 50  ? -25.259 12.775  -9.828  1.00 25.13  ? 93  PHE A CD2 1 
ATOM   421  C CE1 . PHE A 1 50  ? -23.736 11.663  -11.839 1.00 24.68  ? 93  PHE A CE1 1 
ATOM   422  C CE2 . PHE A 1 50  ? -24.309 13.540  -10.479 1.00 25.06  ? 93  PHE A CE2 1 
ATOM   423  C CZ  . PHE A 1 50  ? -23.546 12.981  -11.485 1.00 25.14  ? 93  PHE A CZ  1 
ATOM   424  N N   . ILE A 1 51  ? -28.259 12.567  -11.580 1.00 26.80  ? 94  ILE A N   1 
ATOM   425  C CA  . ILE A 1 51  ? -28.714 13.939  -11.765 1.00 29.39  ? 94  ILE A CA  1 
ATOM   426  C C   . ILE A 1 51  ? -30.229 13.991  -11.624 1.00 25.94  ? 94  ILE A C   1 
ATOM   427  O O   . ILE A 1 51  ? -30.946 13.089  -12.077 1.00 27.60  ? 94  ILE A O   1 
ATOM   428  C CB  . ILE A 1 51  ? -28.258 14.485  -13.128 1.00 31.68  ? 94  ILE A CB  1 
ATOM   429  C CG1 . ILE A 1 51  ? -28.036 15.998  -13.054 1.00 37.25  ? 94  ILE A CG1 1 
ATOM   430  C CG2 . ILE A 1 51  ? -29.285 14.175  -14.211 1.00 33.50  ? 94  ILE A CG2 1 
ATOM   431  C CD1 . ILE A 1 51  ? -26.806 16.402  -12.260 1.00 35.27  ? 94  ILE A CD1 1 
ATOM   432  N N   . SER A 1 52  ? -30.724 15.046  -10.982 1.00 27.03  ? 95  SER A N   1 
ATOM   433  C CA  . SER A 1 52  ? -32.152 15.277  -10.795 1.00 30.27  ? 95  SER A CA  1 
ATOM   434  C C   . SER A 1 52  ? -32.792 14.271  -9.845  1.00 29.37  ? 95  SER A C   1 
ATOM   435  O O   . SER A 1 52  ? -34.022 14.162  -9.796  1.00 29.32  ? 95  SER A O   1 
ATOM   436  C CB  . SER A 1 52  ? -32.887 15.264  -12.144 1.00 33.11  ? 95  SER A CB  1 
ATOM   437  O OG  . SER A 1 52  ? -34.151 15.892  -12.044 1.00 35.11  ? 95  SER A OG  1 
ATOM   438  N N   . LYS A 1 53  ? -31.988 13.538  -9.077  1.00 26.09  ? 96  LYS A N   1 
ATOM   439  C CA  . LYS A 1 53  ? -32.483 12.559  -8.120  1.00 26.45  ? 96  LYS A CA  1 
ATOM   440  C C   . LYS A 1 53  ? -31.939 12.877  -6.735  1.00 26.61  ? 96  LYS A C   1 
ATOM   441  O O   . LYS A 1 53  ? -30.808 13.355  -6.594  1.00 25.76  ? 96  LYS A O   1 
ATOM   442  C CB  . LYS A 1 53  ? -32.084 11.134  -8.535  1.00 27.45  ? 96  LYS A CB  1 
ATOM   443  C CG  . LYS A 1 53  ? -32.735 10.676  -9.836  1.00 27.03  ? 96  LYS A CG  1 
ATOM   444  C CD  . LYS A 1 53  ? -32.107 9.401   -10.384 1.00 28.08  ? 96  LYS A CD  1 
ATOM   445  C CE  . LYS A 1 53  ? -32.768 8.993   -11.696 1.00 29.31  ? 96  LYS A CE  1 
ATOM   446  N NZ  . LYS A 1 53  ? -32.118 7.815   -12.320 1.00 28.93  ? 96  LYS A NZ  1 
ATOM   447  N N   . HIS A 1 54  ? -32.755 12.628  -5.717  1.00 25.99  ? 97  HIS A N   1 
ATOM   448  C CA  . HIS A 1 54  ? -32.315 12.834  -4.343  1.00 27.63  ? 97  HIS A CA  1 
ATOM   449  C C   . HIS A 1 54  ? -31.124 11.924  -4.056  1.00 25.55  ? 97  HIS A C   1 
ATOM   450  O O   . HIS A 1 54  ? -31.211 10.709  -4.281  1.00 24.93  ? 97  HIS A O   1 
ATOM   451  C CB  . HIS A 1 54  ? -33.462 12.544  -3.375  1.00 27.65  ? 97  HIS A CB  1 
ATOM   452  C CG  . HIS A 1 54  ? -33.164 12.905  -1.953  1.00 26.92  ? 97  HIS A CG  1 
ATOM   453  N ND1 . HIS A 1 54  ? -32.812 14.180  -1.565  1.00 31.62  ? 97  HIS A ND1 1 
ATOM   454  C CD2 . HIS A 1 54  ? -33.170 12.157  -0.824  1.00 30.82  ? 97  HIS A CD2 1 
ATOM   455  C CE1 . HIS A 1 54  ? -32.609 14.201  -0.259  1.00 29.27  ? 97  HIS A CE1 1 
ATOM   456  N NE2 . HIS A 1 54  ? -32.820 12.986  0.215   1.00 29.13  ? 97  HIS A NE2 1 
ATOM   457  N N   . PRO A 1 55  ? -30.005 12.456  -3.548  1.00 25.50  ? 98  PRO A N   1 
ATOM   458  C CA  . PRO A 1 55  ? -28.788 11.639  -3.445  1.00 26.94  ? 98  PRO A CA  1 
ATOM   459  C C   . PRO A 1 55  ? -28.770 10.703  -2.245  1.00 30.69  ? 98  PRO A C   1 
ATOM   460  O O   . PRO A 1 55  ? -27.696 10.279  -1.808  1.00 28.53  ? 98  PRO A O   1 
ATOM   461  C CB  . PRO A 1 55  ? -27.672 12.688  -3.355  1.00 24.14  ? 98  PRO A CB  1 
ATOM   462  C CG  . PRO A 1 55  ? -28.317 13.858  -2.712  1.00 25.99  ? 98  PRO A CG  1 
ATOM   463  C CD  . PRO A 1 55  ? -29.761 13.856  -3.153  1.00 27.53  ? 98  PRO A CD  1 
ATOM   464  N N   . CYS A 1 56  ? -29.939 10.406  -1.675  1.00 30.17  ? 99  CYS A N   1 
ATOM   465  C CA  . CYS A 1 56  ? -30.053 9.402   -0.623  1.00 27.19  ? 99  CYS A CA  1 
ATOM   466  C C   . CYS A 1 56  ? -30.982 8.254   -1.003  1.00 33.07  ? 99  CYS A C   1 
ATOM   467  O O   . CYS A 1 56  ? -31.255 7.388   -0.162  1.00 30.81  ? 99  CYS A O   1 
ATOM   468  C CB  . CYS A 1 56  ? -30.532 10.048  0.680   1.00 32.09  ? 99  CYS A CB  1 
ATOM   469  S SG  . CYS A 1 56  ? -29.259 11.002  1.553   1.00 29.98  ? 99  CYS A SG  1 
ATOM   470  N N   . ASP A 1 57  ? -31.471 8.215   -2.246  1.00 31.15  ? 100 ASP A N   1 
ATOM   471  C CA  . ASP A 1 57  ? -32.361 7.151   -2.698  1.00 30.26  ? 100 ASP A CA  1 
ATOM   472  C C   . ASP A 1 57  ? -31.892 6.568   -4.026  1.00 29.87  ? 100 ASP A C   1 
ATOM   473  O O   . ASP A 1 57  ? -32.698 6.061   -4.810  1.00 32.02  ? 100 ASP A O   1 
ATOM   474  C CB  . ASP A 1 57  ? -33.797 7.662   -2.804  1.00 33.08  ? 100 ASP A CB  1 
ATOM   475  C CG  . ASP A 1 57  ? -34.403 7.963   -1.446  1.00 33.73  ? 100 ASP A CG  1 
ATOM   476  O OD1 . ASP A 1 57  ? -34.413 7.057   -0.588  1.00 36.22  ? 100 ASP A OD1 1 
ATOM   477  O OD2 . ASP A 1 57  ? -34.854 9.107   -1.228  1.00 33.24  ? 100 ASP A OD2 1 
ATOM   478  N N   . ILE A 1 58  ? -30.585 6.618   -4.283  1.00 28.31  ? 101 ILE A N   1 
ATOM   479  C CA  . ILE A 1 58  ? -30.035 6.039   -5.500  1.00 26.92  ? 101 ILE A CA  1 
ATOM   480  C C   . ILE A 1 58  ? -30.058 4.519   -5.391  1.00 29.80  ? 101 ILE A C   1 
ATOM   481  O O   . ILE A 1 58  ? -29.818 3.949   -4.316  1.00 28.97  ? 101 ILE A O   1 
ATOM   482  C CB  . ILE A 1 58  ? -28.609 6.561   -5.741  1.00 27.07  ? 101 ILE A CB  1 
ATOM   483  C CG1 . ILE A 1 58  ? -28.577 8.095   -5.699  1.00 26.39  ? 101 ILE A CG1 1 
ATOM   484  C CG2 . ILE A 1 58  ? -28.070 6.053   -7.074  1.00 27.55  ? 101 ILE A CG2 1 
ATOM   485  C CD1 . ILE A 1 58  ? -29.478 8.776   -6.715  1.00 26.76  ? 101 ILE A CD1 1 
ATOM   486  N N   . THR A 1 59  ? -30.346 3.855   -6.505  1.00 27.97  ? 102 THR A N   1 
ATOM   487  C CA  . THR A 1 59  ? -30.470 2.406   -6.548  1.00 32.35  ? 102 THR A CA  1 
ATOM   488  C C   . THR A 1 59  ? -29.537 1.828   -7.604  1.00 31.63  ? 102 THR A C   1 
ATOM   489  O O   . THR A 1 59  ? -29.008 2.537   -8.465  1.00 28.15  ? 102 THR A O   1 
ATOM   490  C CB  . THR A 1 59  ? -31.910 1.974   -6.860  1.00 30.50  ? 102 THR A CB  1 
ATOM   491  O OG1 . THR A 1 59  ? -32.257 2.411   -8.179  1.00 33.13  ? 102 THR A OG1 1 
ATOM   492  C CG2 . THR A 1 59  ? -32.886 2.561   -5.853  1.00 32.09  ? 102 THR A CG2 1 
ATOM   493  N N   . GLU A 1 60  ? -29.352 0.510   -7.533  1.00 33.14  ? 103 GLU A N   1 
ATOM   494  C CA  . GLU A 1 60  ? -28.556 -0.179  -8.541  1.00 34.97  ? 103 GLU A CA  1 
ATOM   495  C C   . GLU A 1 60  ? -29.149 0.001   -9.930  1.00 32.86  ? 103 GLU A C   1 
ATOM   496  O O   . GLU A 1 60  ? -28.407 0.118   -10.912 1.00 30.57  ? 103 GLU A O   1 
ATOM   497  C CB  . GLU A 1 60  ? -28.444 -1.662  -8.180  1.00 40.13  ? 103 GLU A CB  1 
ATOM   498  C CG  . GLU A 1 60  ? -27.581 -1.918  -6.944  1.00 49.24  ? 103 GLU A CG  1 
ATOM   499  C CD  . GLU A 1 60  ? -27.884 -3.239  -6.261  1.00 57.06  ? 103 GLU A CD  1 
ATOM   500  O OE1 . GLU A 1 60  ? -28.838 -3.291  -5.455  1.00 54.85  ? 103 GLU A OE1 1 
ATOM   501  O OE2 . GLU A 1 60  ? -27.166 -4.226  -6.529  1.00 54.64  ? 103 GLU A OE2 1 
ATOM   502  N N   . GLU A 1 61  ? -30.480 0.051   -10.032 1.00 33.89  ? 104 GLU A N   1 
ATOM   503  C CA  . GLU A 1 61  ? -31.116 0.225   -11.333 1.00 37.19  ? 104 GLU A CA  1 
ATOM   504  C C   . GLU A 1 61  ? -30.772 1.574   -11.952 1.00 33.38  ? 104 GLU A C   1 
ATOM   505  O O   . GLU A 1 61  ? -30.691 1.687   -13.180 1.00 30.05  ? 104 GLU A O   1 
ATOM   506  C CB  . GLU A 1 61  ? -32.631 0.072   -11.196 1.00 44.89  ? 104 GLU A CB  1 
ATOM   507  C CG  . GLU A 1 61  ? -33.397 0.376   -12.473 1.00 54.19  ? 104 GLU A CG  1 
ATOM   508  C CD  . GLU A 1 61  ? -34.785 -0.235  -12.484 1.00 69.42  ? 104 GLU A CD  1 
ATOM   509  O OE1 . GLU A 1 61  ? -35.370 -0.404  -11.393 1.00 70.37  ? 104 GLU A OE1 1 
ATOM   510  O OE2 . GLU A 1 61  ? -35.287 -0.554  -13.583 1.00 79.38  ? 104 GLU A OE2 1 
ATOM   511  N N   . ASP A 1 62  ? -30.558 2.603   -11.128 1.00 33.12  ? 105 ASP A N   1 
ATOM   512  C CA  . ASP A 1 62  ? -30.178 3.903   -11.669 1.00 26.07  ? 105 ASP A CA  1 
ATOM   513  C C   . ASP A 1 62  ? -28.904 3.812   -12.500 1.00 24.81  ? 105 ASP A C   1 
ATOM   514  O O   . ASP A 1 62  ? -28.736 4.572   -13.459 1.00 25.40  ? 105 ASP A O   1 
ATOM   515  C CB  . ASP A 1 62  ? -29.996 4.919   -10.539 1.00 28.95  ? 105 ASP A CB  1 
ATOM   516  C CG  . ASP A 1 62  ? -31.316 5.378   -9.943  1.00 30.41  ? 105 ASP A CG  1 
ATOM   517  O OD1 . ASP A 1 62  ? -32.247 5.677   -10.719 1.00 31.48  ? 105 ASP A OD1 1 
ATOM   518  O OD2 . ASP A 1 62  ? -31.425 5.442   -8.699  1.00 28.48  ? 105 ASP A OD2 1 
ATOM   519  N N   . TYR A 1 63  ? -28.001 2.898   -12.153 1.00 27.25  ? 106 TYR A N   1 
ATOM   520  C CA  . TYR A 1 63  ? -26.741 2.752   -12.868 1.00 27.83  ? 106 TYR A CA  1 
ATOM   521  C C   . TYR A 1 63  ? -26.789 1.706   -13.975 1.00 30.49  ? 106 TYR A C   1 
ATOM   522  O O   . TYR A 1 63  ? -25.783 1.519   -14.667 1.00 26.84  ? 106 TYR A O   1 
ATOM   523  C CB  . TYR A 1 63  ? -25.619 2.402   -11.887 1.00 25.60  ? 106 TYR A CB  1 
ATOM   524  C CG  . TYR A 1 63  ? -25.130 3.584   -11.087 1.00 25.14  ? 106 TYR A CG  1 
ATOM   525  C CD1 . TYR A 1 63  ? -24.334 4.559   -11.674 1.00 24.29  ? 106 TYR A CD1 1 
ATOM   526  C CD2 . TYR A 1 63  ? -25.458 3.726   -9.743  1.00 26.52  ? 106 TYR A CD2 1 
ATOM   527  C CE1 . TYR A 1 63  ? -23.884 5.646   -10.950 1.00 24.90  ? 106 TYR A CE1 1 
ATOM   528  C CE2 . TYR A 1 63  ? -25.009 4.809   -9.010  1.00 21.95  ? 106 TYR A CE2 1 
ATOM   529  C CZ  . TYR A 1 63  ? -24.224 5.765   -9.619  1.00 22.82  ? 106 TYR A CZ  1 
ATOM   530  O OH  . TYR A 1 63  ? -23.775 6.842   -8.895  1.00 23.41  ? 106 TYR A OH  1 
ATOM   531  N N   . GLN A 1 64  ? -27.923 1.036   -14.174 1.00 28.03  ? 107 GLN A N   1 
ATOM   532  C CA  . GLN A 1 64  ? -27.971 -0.026  -15.174 1.00 35.01  ? 107 GLN A CA  1 
ATOM   533  C C   . GLN A 1 64  ? -27.643 0.463   -16.581 1.00 31.42  ? 107 GLN A C   1 
ATOM   534  O O   . GLN A 1 64  ? -26.882 -0.229  -17.280 1.00 32.15  ? 107 GLN A O   1 
ATOM   535  C CB  . GLN A 1 64  ? -29.344 -0.710  -15.139 1.00 37.56  ? 107 GLN A CB  1 
ATOM   536  C CG  . GLN A 1 64  ? -29.459 -1.900  -16.072 1.00 42.45  ? 107 GLN A CG  1 
ATOM   537  C CD  . GLN A 1 64  ? -28.402 -2.956  -15.804 1.00 46.77  ? 107 GLN A CD  1 
ATOM   538  O OE1 . GLN A 1 64  ? -28.025 -3.199  -14.656 1.00 44.45  ? 107 GLN A OE1 1 
ATOM   539  N NE2 . GLN A 1 64  ? -27.909 -3.581  -16.866 1.00 48.84  ? 107 GLN A NE2 1 
ATOM   540  N N   . PRO A 1 65  ? -28.166 1.594   -17.065 1.00 28.65  ? 108 PRO A N   1 
ATOM   541  C CA  . PRO A 1 65  ? -27.741 2.060   -18.396 1.00 29.96  ? 108 PRO A CA  1 
ATOM   542  C C   . PRO A 1 65  ? -26.238 2.248   -18.512 1.00 28.55  ? 108 PRO A C   1 
ATOM   543  O O   . PRO A 1 65  ? -25.655 1.910   -19.549 1.00 26.69  ? 108 PRO A O   1 
ATOM   544  C CB  . PRO A 1 65  ? -28.502 3.382   -18.560 1.00 29.76  ? 108 PRO A CB  1 
ATOM   545  C CG  . PRO A 1 65  ? -29.719 3.211   -17.722 1.00 30.53  ? 108 PRO A CG  1 
ATOM   546  C CD  . PRO A 1 65  ? -29.266 2.413   -16.524 1.00 31.16  ? 108 PRO A CD  1 
ATOM   547  N N   . LEU A 1 66  ? -25.586 2.771   -17.472 1.00 29.19  ? 109 LEU A N   1 
ATOM   548  C CA  . LEU A 1 66  ? -24.131 2.878   -17.508 1.00 27.67  ? 109 LEU A CA  1 
ATOM   549  C C   . LEU A 1 66  ? -23.480 1.500   -17.519 1.00 27.18  ? 109 LEU A C   1 
ATOM   550  O O   . LEU A 1 66  ? -22.523 1.266   -18.267 1.00 26.55  ? 109 LEU A O   1 
ATOM   551  C CB  . LEU A 1 66  ? -23.629 3.694   -16.318 1.00 24.65  ? 109 LEU A CB  1 
ATOM   552  C CG  . LEU A 1 66  ? -22.108 3.834   -16.221 1.00 28.32  ? 109 LEU A CG  1 
ATOM   553  C CD1 . LEU A 1 66  ? -21.566 4.630   -17.402 1.00 25.58  ? 109 LEU A CD1 1 
ATOM   554  C CD2 . LEU A 1 66  ? -21.715 4.479   -14.896 1.00 26.72  ? 109 LEU A CD2 1 
ATOM   555  N N   . MET A 1 67  ? -23.985 0.576   -16.695 1.00 28.39  ? 110 MET A N   1 
ATOM   556  C CA  . MET A 1 67  ? -23.435 -0.777  -16.669 1.00 32.30  ? 110 MET A CA  1 
ATOM   557  C C   . MET A 1 67  ? -23.457 -1.409  -18.057 1.00 32.91  ? 110 MET A C   1 
ATOM   558  O O   . MET A 1 67  ? -22.493 -2.068  -18.464 1.00 31.16  ? 110 MET A O   1 
ATOM   559  C CB  . MET A 1 67  ? -24.223 -1.654  -15.692 1.00 33.39  ? 110 MET A CB  1 
ATOM   560  C CG  . MET A 1 67  ? -24.171 -1.229  -14.232 1.00 33.31  ? 110 MET A CG  1 
ATOM   561  S SD  . MET A 1 67  ? -22.513 -1.274  -13.537 1.00 36.08  ? 110 MET A SD  1 
ATOM   562  C CE  . MET A 1 67  ? -22.170 0.480   -13.414 1.00 38.74  ? 110 MET A CE  1 
ATOM   563  N N   . LYS A 1 68  ? -24.559 -1.236  -18.791 1.00 30.85  ? 111 LYS A N   1 
ATOM   564  C CA  . LYS A 1 68  ? -24.662 -1.840  -20.117 1.00 29.13  ? 111 LYS A CA  1 
ATOM   565  C C   . LYS A 1 68  ? -23.636 -1.242  -21.072 1.00 30.15  ? 111 LYS A C   1 
ATOM   566  O O   . LYS A 1 68  ? -22.887 -1.970  -21.733 1.00 28.58  ? 111 LYS A O   1 
ATOM   567  C CB  . LYS A 1 68  ? -26.075 -1.660  -20.671 1.00 35.24  ? 111 LYS A CB  1 
ATOM   568  C CG  . LYS A 1 68  ? -27.140 -2.476  -19.955 1.00 43.89  ? 111 LYS A CG  1 
ATOM   569  C CD  . LYS A 1 68  ? -28.238 -2.901  -20.923 1.00 53.90  ? 111 LYS A CD  1 
ATOM   570  C CE  . LYS A 1 68  ? -29.391 -3.580  -20.202 1.00 57.73  ? 111 LYS A CE  1 
ATOM   571  N NZ  . LYS A 1 68  ? -30.202 -2.613  -19.411 1.00 56.91  ? 111 LYS A NZ  1 
ATOM   572  N N   . LEU A 1 69  ? -23.580 0.091   -21.150 1.00 31.20  ? 112 LEU A N   1 
ATOM   573  C CA  . LEU A 1 69  ? -22.628 0.734   -22.050 1.00 29.47  ? 112 LEU A CA  1 
ATOM   574  C C   . LEU A 1 69  ? -21.192 0.377   -21.693 1.00 31.57  ? 112 LEU A C   1 
ATOM   575  O O   . LEU A 1 69  ? -20.341 0.260   -22.582 1.00 30.44  ? 112 LEU A O   1 
ATOM   576  C CB  . LEU A 1 69  ? -22.814 2.250   -22.019 1.00 30.62  ? 112 LEU A CB  1 
ATOM   577  C CG  . LEU A 1 69  ? -24.137 2.784   -22.576 1.00 30.87  ? 112 LEU A CG  1 
ATOM   578  C CD1 . LEU A 1 69  ? -24.180 4.302   -22.492 1.00 28.89  ? 112 LEU A CD1 1 
ATOM   579  C CD2 . LEU A 1 69  ? -24.350 2.321   -24.011 1.00 30.69  ? 112 LEU A CD2 1 
ATOM   580  N N   . GLY A 1 70  ? -20.904 0.201   -20.409 1.00 28.77  ? 113 GLY A N   1 
ATOM   581  C CA  . GLY A 1 70  ? -19.580 -0.145  -19.950 1.00 30.71  ? 113 GLY A CA  1 
ATOM   582  C C   . GLY A 1 70  ? -19.279 -1.625  -19.929 1.00 33.21  ? 113 GLY A C   1 
ATOM   583  O O   . GLY A 1 70  ? -18.253 -2.020  -19.365 1.00 31.45  ? 113 GLY A O   1 
ATOM   584  N N   . THR A 1 71  ? -20.135 -2.458  -20.525 1.00 31.47  ? 114 THR A N   1 
ATOM   585  C CA  . THR A 1 71  ? -19.898 -3.896  -20.541 1.00 33.19  ? 114 THR A CA  1 
ATOM   586  C C   . THR A 1 71  ? -18.496 -4.185  -21.054 1.00 31.37  ? 114 THR A C   1 
ATOM   587  O O   . THR A 1 71  ? -18.069 -3.647  -22.080 1.00 29.81  ? 114 THR A O   1 
ATOM   588  C CB  . THR A 1 71  ? -20.932 -4.605  -21.422 1.00 37.83  ? 114 THR A CB  1 
ATOM   589  O OG1 . THR A 1 71  ? -22.250 -4.369  -20.914 1.00 38.05  ? 114 THR A OG1 1 
ATOM   590  C CG2 . THR A 1 71  ? -20.666 -6.106  -21.453 1.00 38.11  ? 114 THR A CG2 1 
ATOM   591  N N   . GLN A 1 72  ? -17.776 -5.032  -20.326 1.00 33.37  ? 115 GLN A N   1 
ATOM   592  C CA  . GLN A 1 72  ? -16.394 -5.338  -20.662 1.00 34.34  ? 115 GLN A CA  1 
ATOM   593  C C   . GLN A 1 72  ? -16.076 -6.740  -20.172 1.00 34.52  ? 115 GLN A C   1 
ATOM   594  O O   . GLN A 1 72  ? -16.373 -7.078  -19.023 1.00 37.44  ? 115 GLN A O   1 
ATOM   595  C CB  . GLN A 1 72  ? -15.444 -4.315  -20.033 1.00 26.86  ? 115 GLN A CB  1 
ATOM   596  C CG  . GLN A 1 72  ? -14.003 -4.428  -20.490 1.00 30.11  ? 115 GLN A CG  1 
ATOM   597  C CD  . GLN A 1 72  ? -13.137 -3.304  -19.946 1.00 28.57  ? 115 GLN A CD  1 
ATOM   598  O OE1 . GLN A 1 72  ? -13.592 -2.495  -19.136 1.00 25.81  ? 115 GLN A OE1 1 
ATOM   599  N NE2 . GLN A 1 72  ? -11.886 -3.247  -20.392 1.00 26.87  ? 115 GLN A NE2 1 
ATOM   600  N N   . THR A 1 73  ? -15.476 -7.548  -21.040 1.00 30.45  ? 116 THR A N   1 
ATOM   601  C CA  . THR A 1 73  ? -15.093 -8.913  -20.704 1.00 36.98  ? 116 THR A CA  1 
ATOM   602  C C   . THR A 1 73  ? -13.626 -8.911  -20.288 1.00 39.42  ? 116 THR A C   1 
ATOM   603  O O   . THR A 1 73  ? -12.736 -8.709  -21.120 1.00 41.07  ? 116 THR A O   1 
ATOM   604  C CB  . THR A 1 73  ? -15.326 -9.858  -21.880 1.00 39.24  ? 116 THR A CB  1 
ATOM   605  O OG1 . THR A 1 73  ? -16.719 -9.871  -22.217 1.00 45.75  ? 116 THR A OG1 1 
ATOM   606  C CG2 . THR A 1 73  ? -14.879 -11.269 -21.521 1.00 41.94  ? 116 THR A CG2 1 
ATOM   607  N N   . VAL A 1 74  ? -13.380 -9.124  -19.000 1.00 39.51  ? 117 VAL A N   1 
ATOM   608  C CA  . VAL A 1 74  ? -12.025 -9.289  -18.482 1.00 40.21  ? 117 VAL A CA  1 
ATOM   609  C C   . VAL A 1 74  ? -11.810 -10.783 -18.266 1.00 38.05  ? 117 VAL A C   1 
ATOM   610  O O   . VAL A 1 74  ? -12.727 -11.467 -17.790 1.00 38.63  ? 117 VAL A O   1 
ATOM   611  C CB  . VAL A 1 74  ? -11.817 -8.485  -17.188 1.00 42.81  ? 117 VAL A CB  1 
ATOM   612  C CG1 . VAL A 1 74  ? -12.773 -8.954  -16.094 1.00 40.22  ? 117 VAL A CG1 1 
ATOM   613  C CG2 . VAL A 1 74  ? -10.372 -8.585  -16.721 1.00 42.87  ? 117 VAL A CG2 1 
ATOM   614  N N   . PRO A 1 75  ? -10.641 -11.340 -18.610 1.00 37.38  ? 118 PRO A N   1 
ATOM   615  C CA  . PRO A 1 75  ? -10.421 -12.776 -18.367 1.00 39.36  ? 118 PRO A CA  1 
ATOM   616  C C   . PRO A 1 75  ? -10.745 -13.147 -16.928 1.00 37.55  ? 118 PRO A C   1 
ATOM   617  O O   . PRO A 1 75  ? -10.082 -12.678 -15.997 1.00 34.06  ? 118 PRO A O   1 
ATOM   618  C CB  . PRO A 1 75  ? -8.935  -12.967 -18.693 1.00 38.86  ? 118 PRO A CB  1 
ATOM   619  C CG  . PRO A 1 75  ? -8.603  -11.849 -19.628 1.00 41.49  ? 118 PRO A CG  1 
ATOM   620  C CD  . PRO A 1 75  ? -9.456  -10.690 -19.202 1.00 38.25  ? 118 PRO A CD  1 
ATOM   621  N N   . CYS A 1 76  ? -11.767 -13.986 -16.732 1.00 36.14  ? 119 CYS A N   1 
ATOM   622  C CA  . CYS A 1 76  ? -12.301 -14.200 -15.391 1.00 35.04  ? 119 CYS A CA  1 
ATOM   623  C C   . CYS A 1 76  ? -11.276 -14.790 -14.434 1.00 32.18  ? 119 CYS A C   1 
ATOM   624  O O   . CYS A 1 76  ? -11.438 -14.654 -13.217 1.00 31.27  ? 119 CYS A O   1 
ATOM   625  C CB  . CYS A 1 76  ? -13.534 -15.107 -15.444 1.00 35.80  ? 119 CYS A CB  1 
ATOM   626  S SG  . CYS A 1 76  ? -13.291 -16.762 -16.153 1.00 44.00  ? 119 CYS A SG  1 
ATOM   627  N N   . ASN A 1 77  ? -10.227 -15.429 -14.943 1.00 33.09  ? 120 ASN A N   1 
ATOM   628  C CA  . ASN A 1 77  ? -9.223  -16.057 -14.097 1.00 35.41  ? 120 ASN A CA  1 
ATOM   629  C C   . ASN A 1 77  ? -8.044  -15.138 -13.794 1.00 33.82  ? 120 ASN A C   1 
ATOM   630  O O   . ASN A 1 77  ? -7.037  -15.605 -13.251 1.00 33.20  ? 120 ASN A O   1 
ATOM   631  C CB  . ASN A 1 77  ? -8.718  -17.348 -14.750 1.00 35.53  ? 120 ASN A CB  1 
ATOM   632  C CG  . ASN A 1 77  ? -8.003  -17.099 -16.064 1.00 37.92  ? 120 ASN A CG  1 
ATOM   633  O OD1 . ASN A 1 77  ? -8.420  -16.263 -16.866 1.00 37.12  ? 120 ASN A OD1 1 
ATOM   634  N ND2 . ASN A 1 77  ? -6.917  -17.827 -16.290 1.00 40.79  ? 120 ASN A ND2 1 
ATOM   635  N N   . LYS A 1 78  ? -8.147  -13.848 -14.116 1.00 31.22  ? 121 LYS A N   1 
ATOM   636  C CA  . LYS A 1 78  ? -7.046  -12.901 -13.969 1.00 33.70  ? 121 LYS A CA  1 
ATOM   637  C C   . LYS A 1 78  ? -7.474  -11.681 -13.163 1.00 32.62  ? 121 LYS A C   1 
ATOM   638  O O   . LYS A 1 78  ? -7.057  -10.552 -13.440 1.00 35.33  ? 121 LYS A O   1 
ATOM   639  C CB  . LYS A 1 78  ? -6.521  -12.470 -15.336 1.00 38.80  ? 121 LYS A CB  1 
ATOM   640  C CG  . LYS A 1 78  ? -6.017  -13.609 -16.203 1.00 39.77  ? 121 LYS A CG  1 
ATOM   641  C CD  . LYS A 1 78  ? -4.850  -14.320 -15.540 1.00 43.97  ? 121 LYS A CD  1 
ATOM   642  C CE  . LYS A 1 78  ? -3.782  -14.708 -16.548 1.00 53.20  ? 121 LYS A CE  1 
ATOM   643  N NZ  . LYS A 1 78  ? -2.498  -15.046 -15.871 1.00 63.33  ? 121 LYS A NZ  1 
ATOM   644  N N   . ILE A 1 79  ? -8.298  -11.884 -12.141 1.00 26.88  ? 122 ILE A N   1 
ATOM   645  C CA  . ILE A 1 79  ? -8.903  -10.788 -11.393 1.00 28.15  ? 122 ILE A CA  1 
ATOM   646  C C   . ILE A 1 79  ? -8.205  -10.644 -10.049 1.00 29.90  ? 122 ILE A C   1 
ATOM   647  O O   . ILE A 1 79  ? -7.956  -11.639 -9.354  1.00 28.65  ? 122 ILE A O   1 
ATOM   648  C CB  . ILE A 1 79  ? -10.416 -11.009 -11.219 1.00 27.44  ? 122 ILE A CB  1 
ATOM   649  C CG1 . ILE A 1 79  ? -11.133 -10.636 -12.522 1.00 32.64  ? 122 ILE A CG1 1 
ATOM   650  C CG2 . ILE A 1 79  ? -10.946 -10.205 -10.041 1.00 25.23  ? 122 ILE A CG2 1 
ATOM   651  C CD1 . ILE A 1 79  ? -12.620 -10.904 -12.521 1.00 34.57  ? 122 ILE A CD1 1 
ATOM   652  N N   . LEU A 1 80  ? -7.888  -9.402  -9.684  1.00 27.17  ? 123 LEU A N   1 
ATOM   653  C CA  . LEU A 1 80  ? -7.222  -9.079  -8.428  1.00 27.63  ? 123 LEU A CA  1 
ATOM   654  C C   . LEU A 1 80  ? -8.094  -8.110  -7.642  1.00 26.85  ? 123 LEU A C   1 
ATOM   655  O O   . LEU A 1 80  ? -8.338  -6.984  -8.091  1.00 28.37  ? 123 LEU A O   1 
ATOM   656  C CB  . LEU A 1 80  ? -5.840  -8.470  -8.681  1.00 26.01  ? 123 LEU A CB  1 
ATOM   657  C CG  . LEU A 1 80  ? -5.118  -7.883  -7.466  1.00 24.91  ? 123 LEU A CG  1 
ATOM   658  C CD1 . LEU A 1 80  ? -4.841  -8.967  -6.427  1.00 29.96  ? 123 LEU A CD1 1 
ATOM   659  C CD2 . LEU A 1 80  ? -3.825  -7.193  -7.885  1.00 25.60  ? 123 LEU A CD2 1 
ATOM   660  N N   . LEU A 1 81  ? -8.561  -8.548  -6.480  1.00 26.64  ? 124 LEU A N   1 
ATOM   661  C CA  . LEU A 1 81  ? -9.251  -7.679  -5.539  1.00 28.26  ? 124 LEU A CA  1 
ATOM   662  C C   . LEU A 1 81  ? -8.235  -7.080  -4.568  1.00 25.98  ? 124 LEU A C   1 
ATOM   663  O O   . LEU A 1 81  ? -7.096  -7.542  -4.466  1.00 23.55  ? 124 LEU A O   1 
ATOM   664  C CB  . LEU A 1 81  ? -10.327 -8.459  -4.781  1.00 25.62  ? 124 LEU A CB  1 
ATOM   665  C CG  . LEU A 1 81  ? -11.272 -9.316  -5.632  1.00 26.27  ? 124 LEU A CG  1 
ATOM   666  C CD1 . LEU A 1 81  ? -12.119 -10.219 -4.743  1.00 26.96  ? 124 LEU A CD1 1 
ATOM   667  C CD2 . LEU A 1 81  ? -12.164 -8.451  -6.514  1.00 27.68  ? 124 LEU A CD2 1 
ATOM   668  N N   . TRP A 1 82  ? -8.650  -6.030  -3.860  1.00 26.50  ? 125 TRP A N   1 
ATOM   669  C CA  . TRP A 1 82  ? -7.789  -5.448  -2.838  1.00 27.76  ? 125 TRP A CA  1 
ATOM   670  C C   . TRP A 1 82  ? -8.634  -4.865  -1.714  1.00 27.99  ? 125 TRP A C   1 
ATOM   671  O O   . TRP A 1 82  ? -9.807  -4.525  -1.898  1.00 27.07  ? 125 TRP A O   1 
ATOM   672  C CB  . TRP A 1 82  ? -6.850  -4.372  -3.414  1.00 26.85  ? 125 TRP A CB  1 
ATOM   673  C CG  . TRP A 1 82  ? -7.539  -3.245  -4.142  1.00 28.79  ? 125 TRP A CG  1 
ATOM   674  C CD1 . TRP A 1 82  ? -7.620  -3.072  -5.493  1.00 28.62  ? 125 TRP A CD1 1 
ATOM   675  C CD2 . TRP A 1 82  ? -8.232  -2.135  -3.555  1.00 28.18  ? 125 TRP A CD2 1 
ATOM   676  N NE1 . TRP A 1 82  ? -8.327  -1.931  -5.785  1.00 28.70  ? 125 TRP A NE1 1 
ATOM   677  C CE2 . TRP A 1 82  ? -8.711  -1.336  -4.613  1.00 30.54  ? 125 TRP A CE2 1 
ATOM   678  C CE3 . TRP A 1 82  ? -8.494  -1.739  -2.238  1.00 30.75  ? 125 TRP A CE3 1 
ATOM   679  C CZ2 . TRP A 1 82  ? -9.442  -0.172  -4.396  1.00 30.50  ? 125 TRP A CZ2 1 
ATOM   680  C CZ3 . TRP A 1 82  ? -9.218  -0.579  -2.024  1.00 33.01  ? 125 TRP A CZ3 1 
ATOM   681  C CH2 . TRP A 1 82  ? -9.681  0.193   -3.098  1.00 33.27  ? 125 TRP A CH2 1 
ATOM   682  N N   . SER A 1 83  ? -8.012  -4.767  -0.538  1.00 29.24  ? 126 SER A N   1 
ATOM   683  C CA  . SER A 1 83  ? -8.602  -4.153  0.649   1.00 32.85  ? 126 SER A CA  1 
ATOM   684  C C   . SER A 1 83  ? -7.579  -3.198  1.256   1.00 31.50  ? 126 SER A C   1 
ATOM   685  O O   . SER A 1 83  ? -6.524  -3.633  1.725   1.00 31.17  ? 126 SER A O   1 
ATOM   686  C CB  . SER A 1 83  ? -9.022  -5.210  1.672   1.00 32.80  ? 126 SER A CB  1 
ATOM   687  O OG  . SER A 1 83  ? -9.429  -4.615  2.895   1.00 36.07  ? 126 SER A OG  1 
ATOM   688  N N   . ARG A 1 84  ? -7.879  -1.903  1.204   1.00 33.83  ? 127 ARG A N   1 
ATOM   689  C CA  . ARG A 1 84  ? -7.099  -0.805  1.766   1.00 38.39  ? 127 ARG A CA  1 
ATOM   690  C C   . ARG A 1 84  ? -5.798  -0.518  1.037   1.00 39.71  ? 127 ARG A C   1 
ATOM   691  O O   . ARG A 1 84  ? -5.355  0.633   0.998   1.00 49.46  ? 127 ARG A O   1 
ATOM   692  C CB  . ARG A 1 84  ? -6.692  -1.092  3.220   1.00 42.49  ? 127 ARG A CB  1 
ATOM   693  C CG  . ARG A 1 84  ? -7.808  -1.190  4.212   1.00 52.86  ? 127 ARG A CG  1 
ATOM   694  C CD  . ARG A 1 84  ? -8.025  0.145   4.878   1.00 63.53  ? 127 ARG A CD  1 
ATOM   695  N NE  . ARG A 1 84  ? -9.433  0.346   5.187   1.00 74.72  ? 127 ARG A NE  1 
ATOM   696  C CZ  . ARG A 1 84  ? -10.006 1.531   5.346   1.00 77.02  ? 127 ARG A CZ  1 
ATOM   697  N NH1 . ARG A 1 84  ? -9.317  2.655   5.233   1.00 76.62  ? 127 ARG A NH1 1 
ATOM   698  N NH2 . ARG A 1 84  ? -11.306 1.588   5.617   1.00 76.35  ? 127 ARG A NH2 1 
ATOM   699  N N   . ILE A 1 85  ? -5.224  -1.520  0.381   1.00 35.68  ? 128 ILE A N   1 
ATOM   700  C CA  . ILE A 1 85  ? -3.946  -1.304  -0.281  1.00 37.96  ? 128 ILE A CA  1 
ATOM   701  C C   . ILE A 1 85  ? -4.220  -1.258  -1.774  1.00 34.94  ? 128 ILE A C   1 
ATOM   702  O O   . ILE A 1 85  ? -3.919  -2.202  -2.512  1.00 37.59  ? 128 ILE A O   1 
ATOM   703  C CB  . ILE A 1 85  ? -2.927  -2.390  0.122   1.00 40.93  ? 128 ILE A CB  1 
ATOM   704  C CG1 . ILE A 1 85  ? -1.539  -2.054  -0.426  1.00 44.44  ? 128 ILE A CG1 1 
ATOM   705  C CG2 . ILE A 1 85  ? -3.384  -3.776  -0.313  1.00 36.92  ? 128 ILE A CG2 1 
ATOM   706  C CD1 . ILE A 1 85  ? -0.432  -2.846  0.230   1.00 42.36  ? 128 ILE A CD1 1 
ATOM   707  N N   . LYS A 1 86  ? -4.723  -0.118  -2.236  1.00 36.93  ? 129 LYS A N   1 
ATOM   708  C CA  . LYS A 1 86  ? -5.007  0.041   -3.653  1.00 35.44  ? 129 LYS A CA  1 
ATOM   709  C C   . LYS A 1 86  ? -3.745  0.398   -4.416  1.00 36.56  ? 129 LYS A C   1 
ATOM   710  O O   . LYS A 1 86  ? -3.602  0.027   -5.586  1.00 30.29  ? 129 LYS A O   1 
ATOM   711  C CB  . LYS A 1 86  ? -6.080  1.113   -3.847  1.00 37.44  ? 129 LYS A CB  1 
ATOM   712  C CG  . LYS A 1 86  ? -6.445  1.369   -5.291  1.00 44.04  ? 129 LYS A CG  1 
ATOM   713  C CD  . LYS A 1 86  ? -7.635  2.312   -5.410  1.00 46.17  ? 129 LYS A CD  1 
ATOM   714  C CE  . LYS A 1 86  ? -7.233  3.770   -5.306  1.00 43.94  ? 129 LYS A CE  1 
ATOM   715  N NZ  . LYS A 1 86  ? -8.436  4.646   -5.351  1.00 39.51  ? 129 LYS A NZ  1 
ATOM   716  N N   . ASP A 1 87  ? -2.813  1.081   -3.749  1.00 35.03  ? 130 ASP A N   1 
ATOM   717  C CA  A ASP A 1 87  ? -1.606  1.546   -4.422  0.48 36.03  ? 130 ASP A CA  1 
ATOM   718  C CA  B ASP A 1 87  ? -1.605  1.546   -4.419  0.52 36.02  ? 130 ASP A CA  1 
ATOM   719  C C   . ASP A 1 87  ? -0.784  0.377   -4.950  1.00 34.03  ? 130 ASP A C   1 
ATOM   720  O O   . ASP A 1 87  ? -0.363  0.376   -6.114  1.00 31.47  ? 130 ASP A O   1 
ATOM   721  C CB  A ASP A 1 87  ? -0.777  2.406   -3.465  0.48 38.14  ? 130 ASP A CB  1 
ATOM   722  C CB  B ASP A 1 87  ? -0.782  2.397   -3.450  0.52 38.14  ? 130 ASP A CB  1 
ATOM   723  C CG  A ASP A 1 87  ? -0.352  1.654   -2.213  0.48 39.42  ? 130 ASP A CG  1 
ATOM   724  C CG  B ASP A 1 87  ? 0.446   3.002   -4.100  0.52 39.79  ? 130 ASP A CG  1 
ATOM   725  O OD1 A ASP A 1 87  ? -0.758  0.484   -2.045  0.48 38.34  ? 130 ASP A OD1 1 
ATOM   726  O OD1 B ASP A 1 87  ? 0.628   2.819   -5.321  0.52 39.22  ? 130 ASP A OD1 1 
ATOM   727  O OD2 A ASP A 1 87  ? 0.392   2.235   -1.395  0.48 42.06  ? 130 ASP A OD2 1 
ATOM   728  O OD2 B ASP A 1 87  ? 1.232   3.660   -3.385  0.52 44.56  ? 130 ASP A OD2 1 
ATOM   729  N N   . LEU A 1 88  ? -0.551  -0.638  -4.113  1.00 32.48  ? 131 LEU A N   1 
ATOM   730  C CA  . LEU A 1 88  ? 0.280   -1.759  -4.541  1.00 33.06  ? 131 LEU A CA  1 
ATOM   731  C C   . LEU A 1 88  ? -0.439  -2.626  -5.567  1.00 29.25  ? 131 LEU A C   1 
ATOM   732  O O   . LEU A 1 88  ? 0.192   -3.153  -6.490  1.00 28.74  ? 131 LEU A O   1 
ATOM   733  C CB  . LEU A 1 88  ? 0.703   -2.601  -3.337  1.00 30.56  ? 131 LEU A CB  1 
ATOM   734  C CG  . LEU A 1 88  ? 1.611   -3.783  -3.685  1.00 34.27  ? 131 LEU A CG  1 
ATOM   735  C CD1 . LEU A 1 88  ? 2.931   -3.295  -4.266  1.00 36.37  ? 131 LEU A CD1 1 
ATOM   736  C CD2 . LEU A 1 88  ? 1.852   -4.663  -2.469  1.00 38.34  ? 131 LEU A CD2 1 
ATOM   737  N N   . ALA A 1 89  ? -1.754  -2.800  -5.417  1.00 28.34  ? 132 ALA A N   1 
ATOM   738  C CA  . ALA A 1 89  ? -2.500  -3.603  -6.380  1.00 29.04  ? 132 ALA A CA  1 
ATOM   739  C C   . ALA A 1 89  ? -2.385  -3.020  -7.782  1.00 29.85  ? 132 ALA A C   1 
ATOM   740  O O   . ALA A 1 89  ? -2.256  -3.761  -8.764  1.00 27.01  ? 132 ALA A O   1 
ATOM   741  C CB  . ALA A 1 89  ? -3.966  -3.701  -5.959  1.00 26.46  ? 132 ALA A CB  1 
ATOM   742  N N   . HIS A 1 90  ? -2.426  -1.690  -7.894  1.00 28.67  ? 133 HIS A N   1 
ATOM   743  C CA  . HIS A 1 90  ? -2.349  -1.050  -9.204  1.00 30.59  ? 133 HIS A CA  1 
ATOM   744  C C   . HIS A 1 90  ? -0.934  -1.095  -9.765  1.00 32.25  ? 133 HIS A C   1 
ATOM   745  O O   . HIS A 1 90  ? -0.748  -1.307  -10.969 1.00 28.81  ? 133 HIS A O   1 
ATOM   746  C CB  . HIS A 1 90  ? -2.850  0.389   -9.105  1.00 32.60  ? 133 HIS A CB  1 
ATOM   747  C CG  . HIS A 1 90  ? -4.320  0.491   -8.847  1.00 34.88  ? 133 HIS A CG  1 
ATOM   748  N ND1 . HIS A 1 90  ? -4.957  1.692   -8.619  1.00 39.12  ? 133 HIS A ND1 1 
ATOM   749  C CD2 . HIS A 1 90  ? -5.280  -0.462  -8.786  1.00 34.04  ? 133 HIS A CD2 1 
ATOM   750  C CE1 . HIS A 1 90  ? -6.246  1.474   -8.429  1.00 39.40  ? 133 HIS A CE1 1 
ATOM   751  N NE2 . HIS A 1 90  ? -6.468  0.175   -8.522  1.00 34.09  ? 133 HIS A NE2 1 
ATOM   752  N N   . GLN A 1 91  ? 0.077   -0.889  -8.916  1.00 30.66  ? 134 GLN A N   1 
ATOM   753  C CA  . GLN A 1 91  ? 1.452   -1.081  -9.364  1.00 32.20  ? 134 GLN A CA  1 
ATOM   754  C C   . GLN A 1 91  ? 1.651   -2.496  -9.884  1.00 31.71  ? 134 GLN A C   1 
ATOM   755  O O   . GLN A 1 91  ? 2.336   -2.710  -10.892 1.00 32.95  ? 134 GLN A O   1 
ATOM   756  C CB  . GLN A 1 91  ? 2.432   -0.803  -8.225  1.00 35.63  ? 134 GLN A CB  1 
ATOM   757  C CG  . GLN A 1 91  ? 2.465   0.633   -7.746  1.00 37.42  ? 134 GLN A CG  1 
ATOM   758  C CD  . GLN A 1 91  ? 3.354   0.808   -6.529  1.00 42.85  ? 134 GLN A CD  1 
ATOM   759  O OE1 . GLN A 1 91  ? 4.531   0.444   -6.547  1.00 42.26  ? 134 GLN A OE1 1 
ATOM   760  N NE2 . GLN A 1 91  ? 2.790   1.354   -5.458  1.00 44.72  ? 134 GLN A NE2 1 
ATOM   761  N N   . PHE A 1 92  ? 1.057   -3.478  -9.205  1.00 32.33  ? 135 PHE A N   1 
ATOM   762  C CA  . PHE A 1 92  ? 1.195   -4.866  -9.627  1.00 31.75  ? 135 PHE A CA  1 
ATOM   763  C C   . PHE A 1 92  ? 0.620   -5.075  -11.024 1.00 32.90  ? 135 PHE A C   1 
ATOM   764  O O   . PHE A 1 92  ? 1.293   -5.619  -11.907 1.00 36.98  ? 135 PHE A O   1 
ATOM   765  C CB  . PHE A 1 92  ? 0.512   -5.782  -8.610  1.00 28.97  ? 135 PHE A CB  1 
ATOM   766  C CG  . PHE A 1 92  ? 0.499   -7.229  -9.009  1.00 30.36  ? 135 PHE A CG  1 
ATOM   767  C CD1 . PHE A 1 92  ? 1.610   -8.028  -8.807  1.00 33.52  ? 135 PHE A CD1 1 
ATOM   768  C CD2 . PHE A 1 92  ? -0.628  -7.793  -9.580  1.00 31.50  ? 135 PHE A CD2 1 
ATOM   769  C CE1 . PHE A 1 92  ? 1.598   -9.361  -9.172  1.00 36.96  ? 135 PHE A CE1 1 
ATOM   770  C CE2 . PHE A 1 92  ? -0.645  -9.126  -9.947  1.00 29.45  ? 135 PHE A CE2 1 
ATOM   771  C CZ  . PHE A 1 92  ? 0.467   -9.908  -9.744  1.00 31.33  ? 135 PHE A CZ  1 
ATOM   772  N N   . THR A 1 93  ? -0.622  -4.638  -11.252 1.00 29.66  ? 136 THR A N   1 
ATOM   773  C CA  . THR A 1 93  ? -1.231  -4.839  -12.563 1.00 35.83  ? 136 THR A CA  1 
ATOM   774  C C   . THR A 1 93  ? -0.595  -3.960  -13.634 1.00 38.43  ? 136 THR A C   1 
ATOM   775  O O   . THR A 1 93  ? -0.677  -4.297  -14.819 1.00 39.95  ? 136 THR A O   1 
ATOM   776  C CB  . THR A 1 93  ? -2.740  -4.579  -12.510 1.00 32.28  ? 136 THR A CB  1 
ATOM   777  O OG1 . THR A 1 93  ? -2.991  -3.248  -12.042 1.00 29.61  ? 136 THR A OG1 1 
ATOM   778  C CG2 . THR A 1 93  ? -3.422  -5.586  -11.590 1.00 29.68  ? 136 THR A CG2 1 
ATOM   779  N N   . GLN A 1 94  ? 0.032   -2.846  -13.250 1.00 34.10  ? 137 GLN A N   1 
ATOM   780  C CA  . GLN A 1 94  ? 0.793   -2.067  -14.219 1.00 40.18  ? 137 GLN A CA  1 
ATOM   781  C C   . GLN A 1 94  ? 1.994   -2.839  -14.745 1.00 41.35  ? 137 GLN A C   1 
ATOM   782  O O   . GLN A 1 94  ? 2.477   -2.542  -15.843 1.00 44.60  ? 137 GLN A O   1 
ATOM   783  C CB  . GLN A 1 94  ? 1.255   -0.748  -13.598 1.00 38.10  ? 137 GLN A CB  1 
ATOM   784  C CG  . GLN A 1 94  ? 0.163   0.305   -13.509 1.00 39.03  ? 137 GLN A CG  1 
ATOM   785  C CD  . GLN A 1 94  ? -0.373  0.705   -14.871 1.00 46.29  ? 137 GLN A CD  1 
ATOM   786  O OE1 . GLN A 1 94  ? 0.383   1.113   -15.753 1.00 47.11  ? 137 GLN A OE1 1 
ATOM   787  N NE2 . GLN A 1 94  ? -1.683  0.578   -15.051 1.00 42.76  ? 137 GLN A NE2 1 
ATOM   788  N N   . VAL A 1 95  ? 2.483   -3.814  -13.988 1.00 39.82  ? 138 VAL A N   1 
ATOM   789  C CA  . VAL A 1 95  ? 3.566   -4.686  -14.423 1.00 43.08  ? 138 VAL A CA  1 
ATOM   790  C C   . VAL A 1 95  ? 3.029   -6.006  -14.960 1.00 45.91  ? 138 VAL A C   1 
ATOM   791  O O   . VAL A 1 95  ? 3.349   -6.408  -16.078 1.00 49.09  ? 138 VAL A O   1 
ATOM   792  C CB  . VAL A 1 95  ? 4.555   -4.915  -13.259 1.00 50.72  ? 138 VAL A CB  1 
ATOM   793  C CG1 . VAL A 1 95  ? 5.588   -5.961  -13.638 1.00 58.85  ? 138 VAL A CG1 1 
ATOM   794  C CG2 . VAL A 1 95  ? 5.225   -3.605  -12.867 1.00 51.85  ? 138 VAL A CG2 1 
ATOM   795  N N   . GLN A 1 96  ? 2.204   -6.691  -14.170 1.00 44.09  ? 139 GLN A N   1 
ATOM   796  C CA  . GLN A 1 96  ? 1.530   -7.915  -14.607 1.00 45.61  ? 139 GLN A CA  1 
ATOM   797  C C   . GLN A 1 96  ? 0.243   -7.530  -15.340 1.00 46.22  ? 139 GLN A C   1 
ATOM   798  O O   . GLN A 1 96  ? -0.873  -7.659  -14.832 1.00 44.57  ? 139 GLN A O   1 
ATOM   799  C CB  . GLN A 1 96  ? 1.253   -8.815  -13.411 1.00 42.61  ? 139 GLN A CB  1 
ATOM   800  C CG  . GLN A 1 96  ? 0.867   -10.237 -13.769 1.00 46.66  ? 139 GLN A CG  1 
ATOM   801  C CD  . GLN A 1 96  ? 2.020   -11.017 -14.368 1.00 51.54  ? 139 GLN A CD  1 
ATOM   802  O OE1 . GLN A 1 96  ? 3.133   -11.005 -13.841 1.00 51.99  ? 139 GLN A OE1 1 
ATOM   803  N NE2 . GLN A 1 96  ? 1.761   -11.697 -15.478 1.00 55.20  ? 139 GLN A NE2 1 
ATOM   804  N N   . ARG A 1 97  ? 0.423   -7.046  -16.573 1.00 47.77  ? 140 ARG A N   1 
ATOM   805  C CA  . ARG A 1 97  ? -0.668  -6.396  -17.291 1.00 51.65  ? 140 ARG A CA  1 
ATOM   806  C C   . ARG A 1 97  ? -1.760  -7.358  -17.742 1.00 49.14  ? 140 ARG A C   1 
ATOM   807  O O   . ARG A 1 97  ? -2.809  -6.894  -18.199 1.00 46.26  ? 140 ARG A O   1 
ATOM   808  C CB  . ARG A 1 97  ? -0.127  -5.638  -18.504 1.00 58.03  ? 140 ARG A CB  1 
ATOM   809  C CG  . ARG A 1 97  ? 0.655   -4.378  -18.153 1.00 56.59  ? 140 ARG A CG  1 
ATOM   810  C CD  . ARG A 1 97  ? 0.761   -3.450  -19.353 1.00 61.70  ? 140 ARG A CD  1 
ATOM   811  N NE  . ARG A 1 97  ? 1.561   -2.264  -19.070 1.00 74.45  ? 140 ARG A NE  1 
ATOM   812  C CZ  . ARG A 1 97  ? 1.075   -1.107  -18.638 1.00 74.36  ? 140 ARG A CZ  1 
ATOM   813  N NH1 . ARG A 1 97  ? -0.219  -0.939  -18.414 1.00 73.41  ? 140 ARG A NH1 1 
ATOM   814  N NH2 . ARG A 1 97  ? 1.908   -0.093  -18.427 1.00 74.82  ? 140 ARG A NH2 1 
ATOM   815  N N   . ASP A 1 98  ? -1.552  -8.669  -17.635 1.00 46.37  ? 141 ASP A N   1 
ATOM   816  C CA  . ASP A 1 98  ? -2.634  -9.609  -17.904 1.00 47.90  ? 141 ASP A CA  1 
ATOM   817  C C   . ASP A 1 98  ? -3.526  -9.824  -16.687 1.00 46.57  ? 141 ASP A C   1 
ATOM   818  O O   . ASP A 1 98  ? -4.482  -10.601 -16.769 1.00 47.94  ? 141 ASP A O   1 
ATOM   819  C CB  . ASP A 1 98  ? -2.070  -10.949 -18.388 1.00 49.66  ? 141 ASP A CB  1 
ATOM   820  C CG  . ASP A 1 98  ? -1.275  -11.666 -17.321 1.00 54.92  ? 141 ASP A CG  1 
ATOM   821  O OD1 . ASP A 1 98  ? -0.790  -10.990 -16.392 1.00 53.82  ? 141 ASP A OD1 1 
ATOM   822  O OD2 . ASP A 1 98  ? -1.133  -12.905 -17.412 1.00 55.03  ? 141 ASP A OD2 1 
ATOM   823  N N   . MET A 1 99  ? -3.231  -9.161  -15.570 1.00 42.68  ? 142 MET A N   1 
ATOM   824  C CA  . MET A 1 99  ? -4.066  -9.167  -14.378 1.00 39.32  ? 142 MET A CA  1 
ATOM   825  C C   . MET A 1 99  ? -4.792  -7.832  -14.260 1.00 36.86  ? 142 MET A C   1 
ATOM   826  O O   . MET A 1 99  ? -4.281  -6.792  -14.685 1.00 36.74  ? 142 MET A O   1 
ATOM   827  C CB  . MET A 1 99  ? -3.225  -9.420  -13.126 1.00 37.54  ? 142 MET A CB  1 
ATOM   828  C CG  . MET A 1 99  ? -2.715  -10.845 -13.015 1.00 42.11  ? 142 MET A CG  1 
ATOM   829  S SD  . MET A 1 99  ? -3.849  -11.932 -12.130 1.00 47.21  ? 142 MET A SD  1 
ATOM   830  C CE  . MET A 1 99  ? -3.375  -11.602 -10.436 1.00 34.03  ? 142 MET A CE  1 
ATOM   831  N N   . PHE A 1 100 ? -5.989  -7.865  -13.677 1.00 32.51  ? 143 PHE A N   1 
ATOM   832  C CA  . PHE A 1 100 ? -6.874  -6.709  -13.704 1.00 33.04  ? 143 PHE A CA  1 
ATOM   833  C C   . PHE A 1 100 ? -7.526  -6.478  -12.351 1.00 29.61  ? 143 PHE A C   1 
ATOM   834  O O   . PHE A 1 100 ? -8.120  -7.396  -11.777 1.00 28.08  ? 143 PHE A O   1 
ATOM   835  C CB  . PHE A 1 100 ? -7.963  -6.892  -14.770 1.00 35.76  ? 143 PHE A CB  1 
ATOM   836  C CG  . PHE A 1 100 ? -7.426  -7.176  -16.142 1.00 39.28  ? 143 PHE A CG  1 
ATOM   837  C CD1 . PHE A 1 100 ? -7.026  -8.456  -16.494 1.00 42.03  ? 143 PHE A CD1 1 
ATOM   838  C CD2 . PHE A 1 100 ? -7.322  -6.165  -17.080 1.00 41.32  ? 143 PHE A CD2 1 
ATOM   839  C CE1 . PHE A 1 100 ? -6.529  -8.719  -17.756 1.00 44.04  ? 143 PHE A CE1 1 
ATOM   840  C CE2 . PHE A 1 100 ? -6.828  -6.422  -18.345 1.00 40.56  ? 143 PHE A CE2 1 
ATOM   841  C CZ  . PHE A 1 100 ? -6.431  -7.699  -18.683 1.00 43.85  ? 143 PHE A CZ  1 
ATOM   842  N N   . THR A 1 101 ? -7.427  -5.246  -11.861 1.00 25.19  ? 144 THR A N   1 
ATOM   843  C CA  . THR A 1 101 ? -8.266  -4.772  -10.774 1.00 27.12  ? 144 THR A CA  1 
ATOM   844  C C   . THR A 1 101 ? -9.502  -4.087  -11.351 1.00 25.98  ? 144 THR A C   1 
ATOM   845  O O   . THR A 1 101 ? -9.586  -3.802  -12.548 1.00 25.13  ? 144 THR A O   1 
ATOM   846  C CB  . THR A 1 101 ? -7.510  -3.795  -9.873  1.00 27.04  ? 144 THR A CB  1 
ATOM   847  O OG1 . THR A 1 101 ? -7.236  -2.589  -10.600 1.00 26.55  ? 144 THR A OG1 1 
ATOM   848  C CG2 . THR A 1 101 ? -6.204  -4.406  -9.378  1.00 27.27  ? 144 THR A CG2 1 
ATOM   849  N N   . LEU A 1 102 ? -10.467 -3.805  -10.476 1.00 25.18  ? 145 LEU A N   1 
ATOM   850  C CA  . LEU A 1 102 ? -11.681 -3.131  -10.922 1.00 26.48  ? 145 LEU A CA  1 
ATOM   851  C C   . LEU A 1 102 ? -11.357 -1.786  -11.561 1.00 25.68  ? 145 LEU A C   1 
ATOM   852  O O   . LEU A 1 102 ? -11.974 -1.401  -12.563 1.00 23.58  ? 145 LEU A O   1 
ATOM   853  C CB  . LEU A 1 102 ? -12.642 -2.956  -9.747  1.00 27.72  ? 145 LEU A CB  1 
ATOM   854  C CG  . LEU A 1 102 ? -13.906 -2.139  -10.016 1.00 25.60  ? 145 LEU A CG  1 
ATOM   855  C CD1 . LEU A 1 102 ? -14.738 -2.766  -11.127 1.00 26.51  ? 145 LEU A CD1 1 
ATOM   856  C CD2 . LEU A 1 102 ? -14.724 -1.994  -8.739  1.00 24.72  ? 145 LEU A CD2 1 
ATOM   857  N N   . GLU A 1 103 ? -10.377 -1.067  -11.009 1.00 23.50  ? 146 GLU A N   1 
ATOM   858  C CA  . GLU A 1 103 ? -10.000 0.237   -11.540 1.00 25.31  ? 146 GLU A CA  1 
ATOM   859  C C   . GLU A 1 103 ? -9.298  0.136   -12.887 1.00 26.20  ? 146 GLU A C   1 
ATOM   860  O O   . GLU A 1 103 ? -9.070  1.168   -13.526 1.00 23.41  ? 146 GLU A O   1 
ATOM   861  C CB  . GLU A 1 103 ? -9.101  0.977   -10.545 1.00 27.86  ? 146 GLU A CB  1 
ATOM   862  C CG  . GLU A 1 103 ? -9.775  1.322   -9.218  1.00 28.30  ? 146 GLU A CG  1 
ATOM   863  C CD  . GLU A 1 103 ? -9.918  0.125   -8.291  1.00 29.54  ? 146 GLU A CD  1 
ATOM   864  O OE1 . GLU A 1 103 ? -9.159  -0.852  -8.458  1.00 29.75  ? 146 GLU A OE1 1 
ATOM   865  O OE2 . GLU A 1 103 ? -10.792 0.160   -7.398  1.00 28.56  ? 146 GLU A OE2 1 
ATOM   866  N N   . ASP A 1 104 ? -8.943  -1.071  -13.323 1.00 27.02  ? 147 ASP A N   1 
ATOM   867  C CA  . ASP A 1 104 ? -8.399  -1.282  -14.656 1.00 26.84  ? 147 ASP A CA  1 
ATOM   868  C C   . ASP A 1 104 ? -9.482  -1.506  -15.703 1.00 25.69  ? 147 ASP A C   1 
ATOM   869  O O   . ASP A 1 104 ? -9.167  -1.551  -16.897 1.00 25.68  ? 147 ASP A O   1 
ATOM   870  C CB  . ASP A 1 104 ? -7.432  -2.471  -14.643 1.00 29.05  ? 147 ASP A CB  1 
ATOM   871  C CG  . ASP A 1 104 ? -6.219  -2.223  -13.757 1.00 32.02  ? 147 ASP A CG  1 
ATOM   872  O OD1 . ASP A 1 104 ? -5.602  -1.144  -13.881 1.00 30.66  ? 147 ASP A OD1 1 
ATOM   873  O OD2 . ASP A 1 104 ? -5.889  -3.101  -12.931 1.00 29.16  ? 147 ASP A OD2 1 
ATOM   874  N N   . THR A 1 105 ? -10.739 -1.652  -15.290 1.00 25.33  ? 148 THR A N   1 
ATOM   875  C CA  . THR A 1 105 ? -11.849 -1.665  -16.228 1.00 23.59  ? 148 THR A CA  1 
ATOM   876  C C   . THR A 1 105 ? -12.280 -0.234  -16.535 1.00 22.54  ? 148 THR A C   1 
ATOM   877  O O   . THR A 1 105 ? -11.969 0.705   -15.800 1.00 23.11  ? 148 THR A O   1 
ATOM   878  C CB  . THR A 1 105 ? -13.036 -2.451  -15.668 1.00 22.50  ? 148 THR A CB  1 
ATOM   879  O OG1 . THR A 1 105 ? -13.620 -1.734  -14.575 1.00 25.22  ? 148 THR A OG1 1 
ATOM   880  C CG2 . THR A 1 105 ? -12.597 -3.826  -15.189 1.00 25.24  ? 148 THR A CG2 1 
ATOM   881  N N   . LEU A 1 106 ? -13.015 -0.072  -17.638 1.00 22.15  ? 149 LEU A N   1 
ATOM   882  C CA  . LEU A 1 106 ? -13.450 1.263   -18.035 1.00 25.90  ? 149 LEU A CA  1 
ATOM   883  C C   . LEU A 1 106 ? -14.206 1.948   -16.903 1.00 24.60  ? 149 LEU A C   1 
ATOM   884  O O   . LEU A 1 106 ? -13.861 3.063   -16.498 1.00 22.43  ? 149 LEU A O   1 
ATOM   885  C CB  . LEU A 1 106 ? -14.319 1.186   -19.295 1.00 26.07  ? 149 LEU A CB  1 
ATOM   886  C CG  . LEU A 1 106 ? -15.002 2.491   -19.724 1.00 25.86  ? 149 LEU A CG  1 
ATOM   887  C CD1 . LEU A 1 106 ? -13.979 3.580   -20.014 1.00 29.11  ? 149 LEU A CD1 1 
ATOM   888  C CD2 . LEU A 1 106 ? -15.897 2.265   -20.939 1.00 27.14  ? 149 LEU A CD2 1 
ATOM   889  N N   . LEU A 1 107 ? -15.225 1.277   -16.358 1.00 23.63  ? 150 LEU A N   1 
ATOM   890  C CA  . LEU A 1 107 ? -16.082 1.918   -15.364 1.00 26.61  ? 150 LEU A CA  1 
ATOM   891  C C   . LEU A 1 107 ? -15.309 2.269   -14.097 1.00 25.24  ? 150 LEU A C   1 
ATOM   892  O O   . LEU A 1 107 ? -15.462 3.370   -13.555 1.00 22.11  ? 150 LEU A O   1 
ATOM   893  C CB  . LEU A 1 107 ? -17.272 1.016   -15.043 1.00 26.37  ? 150 LEU A CB  1 
ATOM   894  C CG  . LEU A 1 107 ? -18.272 0.829   -16.187 1.00 28.89  ? 150 LEU A CG  1 
ATOM   895  C CD1 . LEU A 1 107 ? -19.331 -0.192  -15.807 1.00 34.30  ? 150 LEU A CD1 1 
ATOM   896  C CD2 . LEU A 1 107 ? -18.914 2.160   -16.569 1.00 31.08  ? 150 LEU A CD2 1 
ATOM   897  N N   . GLY A 1 108 ? -14.476 1.351   -13.605 1.00 22.72  ? 151 GLY A N   1 
ATOM   898  C CA  . GLY A 1 108 ? -13.654 1.675   -12.448 1.00 25.63  ? 151 GLY A CA  1 
ATOM   899  C C   . GLY A 1 108 ? -12.672 2.794   -12.738 1.00 22.93  ? 151 GLY A C   1 
ATOM   900  O O   . GLY A 1 108 ? -12.401 3.639   -11.881 1.00 22.57  ? 151 GLY A O   1 
ATOM   901  N N   . TYR A 1 109 ? -12.126 2.809   -13.954 1.00 21.94  ? 152 TYR A N   1 
ATOM   902  C CA  . TYR A 1 109 ? -11.188 3.852   -14.355 1.00 21.77  ? 152 TYR A CA  1 
ATOM   903  C C   . TYR A 1 109 ? -11.852 5.223   -14.354 1.00 25.82  ? 152 TYR A C   1 
ATOM   904  O O   . TYR A 1 109 ? -11.244 6.216   -13.933 1.00 22.88  ? 152 TYR A O   1 
ATOM   905  C CB  . TYR A 1 109 ? -10.632 3.507   -15.738 1.00 26.64  ? 152 TYR A CB  1 
ATOM   906  C CG  . TYR A 1 109 ? -9.553  4.422   -16.273 1.00 28.39  ? 152 TYR A CG  1 
ATOM   907  C CD1 . TYR A 1 109 ? -9.873  5.532   -17.047 1.00 27.62  ? 152 TYR A CD1 1 
ATOM   908  C CD2 . TYR A 1 109 ? -8.211  4.152   -16.040 1.00 28.16  ? 152 TYR A CD2 1 
ATOM   909  C CE1 . TYR A 1 109 ? -8.885  6.361   -17.552 1.00 26.70  ? 152 TYR A CE1 1 
ATOM   910  C CE2 . TYR A 1 109 ? -7.219  4.972   -16.541 1.00 32.43  ? 152 TYR A CE2 1 
ATOM   911  C CZ  . TYR A 1 109 ? -7.560  6.073   -17.298 1.00 30.26  ? 152 TYR A CZ  1 
ATOM   912  O OH  . TYR A 1 109 ? -6.570  6.887   -17.795 1.00 33.17  ? 152 TYR A OH  1 
ATOM   913  N N   . LEU A 1 110 ? -13.101 5.302   -14.822 1.00 23.78  ? 153 LEU A N   1 
ATOM   914  C CA  . LEU A 1 110 ? -13.779 6.593   -14.894 1.00 22.04  ? 153 LEU A CA  1 
ATOM   915  C C   . LEU A 1 110 ? -13.975 7.207   -13.511 1.00 21.05  ? 153 LEU A C   1 
ATOM   916  O O   . LEU A 1 110 ? -13.759 8.410   -13.324 1.00 21.14  ? 153 LEU A O   1 
ATOM   917  C CB  . LEU A 1 110 ? -15.132 6.442   -15.592 1.00 21.61  ? 153 LEU A CB  1 
ATOM   918  C CG  . LEU A 1 110 ? -15.120 6.013   -17.059 1.00 23.55  ? 153 LEU A CG  1 
ATOM   919  C CD1 . LEU A 1 110 ? -16.550 5.837   -17.566 1.00 25.50  ? 153 LEU A CD1 1 
ATOM   920  C CD2 . LEU A 1 110 ? -14.361 7.016   -17.915 1.00 24.16  ? 153 LEU A CD2 1 
ATOM   921  N N   . ALA A 1 111 ? -14.388 6.401   -12.531 1.00 20.04  ? 154 ALA A N   1 
ATOM   922  C CA  . ALA A 1 111 ? -14.807 6.915   -11.233 1.00 22.56  ? 154 ALA A CA  1 
ATOM   923  C C   . ALA A 1 111 ? -13.706 6.918   -10.182 1.00 22.88  ? 154 ALA A C   1 
ATOM   924  O O   . ALA A 1 111 ? -13.923 7.451   -9.087  1.00 23.71  ? 154 ALA A O   1 
ATOM   925  C CB  . ALA A 1 111 ? -15.989 6.097   -10.701 1.00 22.54  ? 154 ALA A CB  1 
ATOM   926  N N   . ASP A 1 112 ? -12.540 6.352   -10.481 1.00 24.94  ? 155 ASP A N   1 
ATOM   927  C CA  . ASP A 1 112 ? -11.489 6.195   -9.480  1.00 26.73  ? 155 ASP A CA  1 
ATOM   928  C C   . ASP A 1 112 ? -11.138 7.524   -8.820  1.00 25.34  ? 155 ASP A C   1 
ATOM   929  O O   . ASP A 1 112 ? -10.712 8.469   -9.488  1.00 22.69  ? 155 ASP A O   1 
ATOM   930  C CB  . ASP A 1 112 ? -10.247 5.586   -10.138 1.00 26.12  ? 155 ASP A CB  1 
ATOM   931  C CG  . ASP A 1 112 ? -9.149  5.271   -9.139  1.00 31.63  ? 155 ASP A CG  1 
ATOM   932  O OD1 . ASP A 1 112 ? -9.452  4.678   -8.083  1.00 27.18  ? 155 ASP A OD1 1 
ATOM   933  O OD2 . ASP A 1 112 ? -7.979  5.605   -9.416  1.00 37.34  ? 155 ASP A OD2 1 
ATOM   934  N N   . ASP A 1 113 ? -11.315 7.583   -7.496  1.00 24.98  ? 156 ASP A N   1 
ATOM   935  C CA  . ASP A 1 113 ? -10.904 8.719   -6.667  1.00 25.70  ? 156 ASP A CA  1 
ATOM   936  C C   . ASP A 1 113 ? -11.736 9.976   -6.933  1.00 27.27  ? 156 ASP A C   1 
ATOM   937  O O   . ASP A 1 113 ? -11.249 11.095  -6.750  1.00 25.51  ? 156 ASP A O   1 
ATOM   938  C CB  . ASP A 1 113 ? -9.410  9.033   -6.846  1.00 27.12  ? 156 ASP A CB  1 
ATOM   939  C CG  . ASP A 1 113 ? -8.507  8.027   -6.141  1.00 34.68  ? 156 ASP A CG  1 
ATOM   940  O OD1 . ASP A 1 113 ? -8.956  7.407   -5.154  1.00 29.33  ? 156 ASP A OD1 1 
ATOM   941  O OD2 . ASP A 1 113 ? -7.343  7.863   -6.568  1.00 34.39  ? 156 ASP A OD2 1 
ATOM   942  N N   . LEU A 1 114 ? -12.994 9.815   -7.342  1.00 24.73  ? 157 LEU A N   1 
ATOM   943  C CA  . LEU A 1 114 ? -13.899 10.935  -7.554  1.00 24.66  ? 157 LEU A CA  1 
ATOM   944  C C   . LEU A 1 114 ? -15.121 10.811  -6.650  1.00 25.09  ? 157 LEU A C   1 
ATOM   945  O O   . LEU A 1 114 ? -15.436 9.738   -6.130  1.00 25.52  ? 157 LEU A O   1 
ATOM   946  C CB  . LEU A 1 114 ? -14.360 11.019  -9.019  1.00 24.09  ? 157 LEU A CB  1 
ATOM   947  C CG  . LEU A 1 114 ? -13.273 11.180  -10.082 1.00 21.91  ? 157 LEU A CG  1 
ATOM   948  C CD1 . LEU A 1 114 ? -13.879 11.099  -11.477 1.00 21.59  ? 157 LEU A CD1 1 
ATOM   949  C CD2 . LEU A 1 114 ? -12.518 12.485  -9.894  1.00 24.28  ? 157 LEU A CD2 1 
ATOM   950  N N   . THR A 1 115 ? -15.808 11.935  -6.468  1.00 23.86  ? 158 THR A N   1 
ATOM   951  C CA  A THR A 1 115 ? -17.060 11.980  -5.728  0.37 24.75  ? 158 THR A CA  1 
ATOM   952  C CA  B THR A 1 115 ? -17.057 11.990  -5.721  0.63 24.83  ? 158 THR A CA  1 
ATOM   953  C C   . THR A 1 115 ? -18.060 12.818  -6.512  1.00 22.79  ? 158 THR A C   1 
ATOM   954  O O   . THR A 1 115 ? -17.687 13.762  -7.212  1.00 22.29  ? 158 THR A O   1 
ATOM   955  C CB  A THR A 1 115 ? -16.863 12.557  -4.316  0.37 26.48  ? 158 THR A CB  1 
ATOM   956  C CB  B THR A 1 115 ? -16.866 12.601  -4.324  0.63 26.18  ? 158 THR A CB  1 
ATOM   957  O OG1 A THR A 1 115 ? -18.118 12.583  -3.624  0.37 27.80  ? 158 THR A OG1 1 
ATOM   958  O OG1 B THR A 1 115 ? -16.688 14.018  -4.438  0.63 28.48  ? 158 THR A OG1 1 
ATOM   959  C CG2 A THR A 1 115 ? -16.286 13.965  -4.381  0.37 27.66  ? 158 THR A CG2 1 
ATOM   960  C CG2 B THR A 1 115 ? -15.651 11.999  -3.633  0.63 27.05  ? 158 THR A CG2 1 
ATOM   961  N N   . TRP A 1 116 ? -19.338 12.458  -6.400  1.00 22.87  ? 159 TRP A N   1 
ATOM   962  C CA  . TRP A 1 116 ? -20.361 13.148  -7.176  1.00 24.41  ? 159 TRP A CA  1 
ATOM   963  C C   . TRP A 1 116 ? -21.722 12.973  -6.520  1.00 23.86  ? 159 TRP A C   1 
ATOM   964  O O   . TRP A 1 116 ? -21.959 12.001  -5.799  1.00 22.46  ? 159 TRP A O   1 
ATOM   965  C CB  . TRP A 1 116 ? -20.409 12.626  -8.620  1.00 24.85  ? 159 TRP A CB  1 
ATOM   966  C CG  . TRP A 1 116 ? -20.793 11.175  -8.712  1.00 24.32  ? 159 TRP A CG  1 
ATOM   967  C CD1 . TRP A 1 116 ? -22.052 10.668  -8.870  1.00 25.08  ? 159 TRP A CD1 1 
ATOM   968  C CD2 . TRP A 1 116 ? -19.913 10.045  -8.646  1.00 23.80  ? 159 TRP A CD2 1 
ATOM   969  N NE1 . TRP A 1 116 ? -22.008 9.294   -8.905  1.00 21.67  ? 159 TRP A NE1 1 
ATOM   970  C CE2 . TRP A 1 116 ? -20.707 8.888   -8.772  1.00 21.06  ? 159 TRP A CE2 1 
ATOM   971  C CE3 . TRP A 1 116 ? -18.531 9.901   -8.495  1.00 23.87  ? 159 TRP A CE3 1 
ATOM   972  C CZ2 . TRP A 1 116 ? -20.165 7.605   -8.747  1.00 23.89  ? 159 TRP A CZ2 1 
ATOM   973  C CZ3 . TRP A 1 116 ? -17.995 8.625   -8.473  1.00 23.65  ? 159 TRP A CZ3 1 
ATOM   974  C CH2 . TRP A 1 116 ? -18.810 7.494   -8.598  1.00 23.55  ? 159 TRP A CH2 1 
ATOM   975  N N   . CYS A 1 117 ? -22.614 13.925  -6.789  1.00 22.85  ? 160 CYS A N   1 
ATOM   976  C CA  . CYS A 1 117 ? -24.002 13.830  -6.357  1.00 23.42  ? 160 CYS A CA  1 
ATOM   977  C C   . CYS A 1 117 ? -24.791 14.964  -6.993  1.00 26.97  ? 160 CYS A C   1 
ATOM   978  O O   . CYS A 1 117 ? -24.223 15.959  -7.454  1.00 26.46  ? 160 CYS A O   1 
ATOM   979  C CB  . CYS A 1 117 ? -24.130 13.884  -4.831  1.00 28.14  ? 160 CYS A CB  1 
ATOM   980  S SG  . CYS A 1 117 ? -23.673 15.469  -4.100  1.00 28.76  ? 160 CYS A SG  1 
ATOM   981  N N   . GLY A 1 118 ? -26.113 14.801  -7.005  1.00 26.12  ? 161 GLY A N   1 
ATOM   982  C CA  . GLY A 1 118 ? -27.005 15.810  -7.538  1.00 27.22  ? 161 GLY A CA  1 
ATOM   983  C C   . GLY A 1 118 ? -28.101 16.173  -6.557  1.00 28.77  ? 161 GLY A C   1 
ATOM   984  O O   . GLY A 1 118 ? -27.958 15.956  -5.350  1.00 26.71  ? 161 GLY A O   1 
ATOM   985  N N   . GLU A 1 119 ? -29.198 16.729  -7.066  1.00 25.59  ? 162 GLU A N   1 
ATOM   986  C CA  . GLU A 1 119 ? -30.337 17.112  -6.244  1.00 28.12  ? 162 GLU A CA  1 
ATOM   987  C C   . GLU A 1 119 ? -31.620 16.775  -6.986  1.00 30.63  ? 162 GLU A C   1 
ATOM   988  O O   . GLU A 1 119 ? -31.653 16.754  -8.218  1.00 30.86  ? 162 GLU A O   1 
ATOM   989  C CB  . GLU A 1 119 ? -30.303 18.611  -5.895  1.00 35.93  ? 162 GLU A CB  1 
ATOM   990  C CG  . GLU A 1 119 ? -31.662 19.199  -5.523  1.00 39.04  ? 162 GLU A CG  1 
ATOM   991  C CD  . GLU A 1 119 ? -31.576 20.640  -5.066  1.00 44.80  ? 162 GLU A CD  1 
ATOM   992  O OE1 . GLU A 1 119 ? -30.673 21.358  -5.542  1.00 44.22  ? 162 GLU A OE1 1 
ATOM   993  O OE2 . GLU A 1 119 ? -32.410 21.053  -4.230  1.00 46.33  ? 162 GLU A OE2 1 
ATOM   994  N N   . PHE A 1 120 ? -32.679 16.526  -6.222  1.00 28.67  ? 163 PHE A N   1 
ATOM   995  C CA  . PHE A 1 120 ? -33.966 16.172  -6.805  1.00 31.48  ? 163 PHE A CA  1 
ATOM   996  C C   . PHE A 1 120 ? -34.552 17.332  -7.601  1.00 31.08  ? 163 PHE A C   1 
ATOM   997  O O   . PHE A 1 120 ? -34.522 18.486  -7.167  1.00 31.47  ? 163 PHE A O   1 
ATOM   998  C CB  . PHE A 1 120 ? -34.940 15.757  -5.701  1.00 28.25  ? 163 PHE A CB  1 
ATOM   999  C CG  . PHE A 1 120 ? -36.301 15.378  -6.204  1.00 27.60  ? 163 PHE A CG  1 
ATOM   1000 C CD1 . PHE A 1 120 ? -36.517 14.137  -6.780  1.00 27.70  ? 163 PHE A CD1 1 
ATOM   1001 C CD2 . PHE A 1 120 ? -37.367 16.256  -6.095  1.00 30.47  ? 163 PHE A CD2 1 
ATOM   1002 C CE1 . PHE A 1 120 ? -37.770 13.780  -7.243  1.00 28.85  ? 163 PHE A CE1 1 
ATOM   1003 C CE2 . PHE A 1 120 ? -38.625 15.905  -6.557  1.00 32.22  ? 163 PHE A CE2 1 
ATOM   1004 C CZ  . PHE A 1 120 ? -38.825 14.664  -7.131  1.00 30.85  ? 163 PHE A CZ  1 
ATOM   1005 N N   . ALA A 1 121 ? -35.095 17.013  -8.776  1.00 32.68  ? 164 ALA A N   1 
ATOM   1006 C CA  . ALA A 1 121 ? -35.853 17.924  -9.628  1.00 38.93  ? 164 ALA A CA  1 
ATOM   1007 C C   . ALA A 1 121 ? -35.013 19.044  -10.230 1.00 41.13  ? 164 ALA A C   1 
ATOM   1008 O O   . ALA A 1 121 ? -35.577 19.994  -10.786 1.00 44.17  ? 164 ALA A O   1 
ATOM   1009 C CB  . ALA A 1 121 ? -37.037 18.542  -8.872  1.00 42.87  ? 164 ALA A CB  1 
ATOM   1010 N N   . THR A 1 122 ? -33.685 18.969  -10.139 1.00 35.97  ? 165 THR A N   1 
ATOM   1011 C CA  A THR A 1 122 ? -32.805 19.948  -10.756 0.22 37.62  ? 165 THR A CA  1 
ATOM   1012 C CA  B THR A 1 122 ? -32.806 19.949  -10.758 0.78 37.53  ? 165 THR A CA  1 
ATOM   1013 C C   . THR A 1 122 ? -31.743 19.228  -11.575 1.00 36.05  ? 165 THR A C   1 
ATOM   1014 O O   . THR A 1 122 ? -31.378 18.087  -11.280 1.00 35.61  ? 165 THR A O   1 
ATOM   1015 C CB  A THR A 1 122 ? -32.130 20.844  -9.711  0.22 38.61  ? 165 THR A CB  1 
ATOM   1016 C CB  B THR A 1 122 ? -32.120 20.856  -9.724  0.78 38.65  ? 165 THR A CB  1 
ATOM   1017 O OG1 A THR A 1 122 ? -31.420 21.901  -10.369 0.22 38.81  ? 165 THR A OG1 1 
ATOM   1018 O OG1 B THR A 1 122 ? -31.018 20.158  -9.129  0.78 37.98  ? 165 THR A OG1 1 
ATOM   1019 C CG2 A THR A 1 122 ? -31.160 20.037  -8.873  0.22 38.80  ? 165 THR A CG2 1 
ATOM   1020 C CG2 B THR A 1 122 ? -33.101 21.279  -8.637  0.78 39.94  ? 165 THR A CG2 1 
ATOM   1021 N N   . SER A 1 123 ? -31.247 19.908  -12.604 1.00 32.12  ? 166 SER A N   1 
ATOM   1022 C CA  . SER A 1 123 ? -30.229 19.357  -13.486 1.00 34.62  ? 166 SER A CA  1 
ATOM   1023 C C   . SER A 1 123 ? -28.812 19.695  -13.037 1.00 35.01  ? 166 SER A C   1 
ATOM   1024 O O   . SER A 1 123 ? -27.860 19.432  -13.779 1.00 35.24  ? 166 SER A O   1 
ATOM   1025 C CB  . SER A 1 123 ? -30.446 19.863  -14.914 1.00 36.46  ? 166 SER A CB  1 
ATOM   1026 O OG  . SER A 1 123 ? -30.249 21.264  -14.985 1.00 41.80  ? 166 SER A OG  1 
ATOM   1027 N N   . LYS A 1 124 ? -28.649 20.261  -11.845 1.00 32.17  ? 167 LYS A N   1 
ATOM   1028 C CA  . LYS A 1 124 ? -27.370 20.792  -11.401 1.00 34.21  ? 167 LYS A CA  1 
ATOM   1029 C C   . LYS A 1 124 ? -26.607 19.772  -10.567 1.00 33.16  ? 167 LYS A C   1 
ATOM   1030 O O   . LYS A 1 124 ? -27.181 19.099  -9.706  1.00 28.75  ? 167 LYS A O   1 
ATOM   1031 C CB  . LYS A 1 124 ? -27.576 22.069  -10.582 1.00 36.15  ? 167 LYS A CB  1 
ATOM   1032 C CG  . LYS A 1 124 ? -28.060 23.265  -11.392 1.00 43.41  ? 167 LYS A CG  1 
ATOM   1033 C CD  . LYS A 1 124 ? -26.994 23.744  -12.366 1.00 47.35  ? 167 LYS A CD  1 
ATOM   1034 C CE  . LYS A 1 124 ? -27.419 25.015  -13.080 1.00 54.54  ? 167 LYS A CE  1 
ATOM   1035 N NZ  . LYS A 1 124 ? -28.579 24.790  -13.985 1.00 56.47  ? 167 LYS A NZ  1 
ATOM   1036 N N   . ILE A 1 125 ? -25.305 19.666  -10.834 1.00 32.10  ? 168 ILE A N   1 
ATOM   1037 C CA  . ILE A 1 125 ? -24.412 18.914  -9.964  1.00 30.10  ? 168 ILE A CA  1 
ATOM   1038 C C   . ILE A 1 125 ? -24.163 19.716  -8.694  1.00 31.17  ? 168 ILE A C   1 
ATOM   1039 O O   . ILE A 1 125 ? -24.027 20.946  -8.732  1.00 28.89  ? 168 ILE A O   1 
ATOM   1040 C CB  . ILE A 1 125 ? -23.093 18.604  -10.692 1.00 30.37  ? 168 ILE A CB  1 
ATOM   1041 C CG1 . ILE A 1 125 ? -23.349 17.645  -11.858 1.00 32.21  ? 168 ILE A CG1 1 
ATOM   1042 C CG2 . ILE A 1 125 ? -22.063 18.041  -9.714  1.00 30.89  ? 168 ILE A CG2 1 
ATOM   1043 C CD1 . ILE A 1 125 ? -22.127 17.364  -12.707 1.00 34.70  ? 168 ILE A CD1 1 
ATOM   1044 N N   . ASN A 1 126 ? -24.092 19.024  -7.559  1.00 32.23  ? 169 ASN A N   1 
ATOM   1045 C CA  . ASN A 1 126 ? -23.892 19.679  -6.267  1.00 29.04  ? 169 ASN A CA  1 
ATOM   1046 C C   . ASN A 1 126 ? -22.399 19.690  -5.964  1.00 29.36  ? 169 ASN A C   1 
ATOM   1047 O O   . ASN A 1 126 ? -21.827 18.679  -5.549  1.00 25.89  ? 169 ASN A O   1 
ATOM   1048 C CB  . ASN A 1 126 ? -24.683 18.971  -5.172  1.00 25.85  ? 169 ASN A CB  1 
ATOM   1049 C CG  . ASN A 1 126 ? -24.604 19.691  -3.837  1.00 30.93  ? 169 ASN A CG  1 
ATOM   1050 O OD1 . ASN A 1 126 ? -23.663 20.443  -3.576  1.00 28.08  ? 169 ASN A OD1 1 
ATOM   1051 N ND2 . ASN A 1 126 ? -25.596 19.464  -2.985  1.00 31.38  ? 169 ASN A ND2 1 
ATOM   1052 N N   . TYR A 1 127 ? -21.765 20.842  -6.166  1.00 28.95  ? 170 TYR A N   1 
ATOM   1053 C CA  . TYR A 1 127 ? -20.344 21.002  -5.891  1.00 29.46  ? 170 TYR A CA  1 
ATOM   1054 C C   . TYR A 1 127 ? -20.061 21.449  -4.463  1.00 29.03  ? 170 TYR A C   1 
ATOM   1055 O O   . TYR A 1 127 ? -18.890 21.604  -4.102  1.00 31.01  ? 170 TYR A O   1 
ATOM   1056 C CB  . TYR A 1 127 ? -19.731 22.004  -6.874  1.00 32.80  ? 170 TYR A CB  1 
ATOM   1057 C CG  . TYR A 1 127 ? -19.627 21.470  -8.282  1.00 31.24  ? 170 TYR A CG  1 
ATOM   1058 C CD1 . TYR A 1 127 ? -18.599 20.609  -8.641  1.00 30.87  ? 170 TYR A CD1 1 
ATOM   1059 C CD2 . TYR A 1 127 ? -20.555 21.821  -9.251  1.00 29.27  ? 170 TYR A CD2 1 
ATOM   1060 C CE1 . TYR A 1 127 ? -18.498 20.112  -9.924  1.00 31.65  ? 170 TYR A CE1 1 
ATOM   1061 C CE2 . TYR A 1 127 ? -20.462 21.329  -10.539 1.00 33.47  ? 170 TYR A CE2 1 
ATOM   1062 C CZ  . TYR A 1 127 ? -19.430 20.474  -10.868 1.00 33.96  ? 170 TYR A CZ  1 
ATOM   1063 O OH  . TYR A 1 127 ? -19.325 19.977  -12.146 1.00 32.91  ? 170 TYR A OH  1 
ATOM   1064 N N   . GLN A 1 128 ? -21.092 21.650  -3.642  1.00 30.61  ? 171 GLN A N   1 
ATOM   1065 C CA  . GLN A 1 128 ? -20.890 22.161  -2.290  1.00 34.15  ? 171 GLN A CA  1 
ATOM   1066 C C   . GLN A 1 128 ? -20.766 21.055  -1.247  1.00 29.28  ? 171 GLN A C   1 
ATOM   1067 O O   . GLN A 1 128 ? -19.937 21.163  -0.338  1.00 27.75  ? 171 GLN A O   1 
ATOM   1068 C CB  . GLN A 1 128 ? -22.035 23.104  -1.912  1.00 37.61  ? 171 GLN A CB  1 
ATOM   1069 C CG  . GLN A 1 128 ? -22.053 24.389  -2.726  1.00 50.34  ? 171 GLN A CG  1 
ATOM   1070 C CD  . GLN A 1 128 ? -23.098 25.377  -2.246  1.00 60.85  ? 171 GLN A CD  1 
ATOM   1071 O OE1 . GLN A 1 128 ? -23.913 25.067  -1.375  1.00 63.62  ? 171 GLN A OE1 1 
ATOM   1072 N NE2 . GLN A 1 128 ? -23.077 26.579  -2.812  1.00 57.85  ? 171 GLN A NE2 1 
ATOM   1073 N N   . SER A 1 129 ? -21.571 20.000  -1.347  1.00 28.23  ? 172 SER A N   1 
ATOM   1074 C CA  . SER A 1 129 ? -21.480 18.880  -0.417  1.00 29.23  ? 172 SER A CA  1 
ATOM   1075 C C   . SER A 1 129 ? -22.264 17.704  -0.984  1.00 29.86  ? 172 SER A C   1 
ATOM   1076 O O   . SER A 1 129 ? -23.187 17.879  -1.786  1.00 25.81  ? 172 SER A O   1 
ATOM   1077 C CB  . SER A 1 129 ? -22.009 19.254  0.973   1.00 29.75  ? 172 SER A CB  1 
ATOM   1078 O OG  . SER A 1 129 ? -23.396 19.542  0.936   1.00 32.47  ? 172 SER A OG  1 
ATOM   1079 N N   . CYS A 1 130 ? -21.883 16.509  -0.553  1.00 25.64  ? 173 CYS A N   1 
ATOM   1080 C CA  . CYS A 1 130 ? -22.557 15.267  -0.901  1.00 27.88  ? 173 CYS A CA  1 
ATOM   1081 C C   . CYS A 1 130 ? -22.731 14.421  0.352   1.00 29.95  ? 173 CYS A C   1 
ATOM   1082 O O   . CYS A 1 130 ? -21.993 14.586  1.329   1.00 27.75  ? 173 CYS A O   1 
ATOM   1083 C CB  . CYS A 1 130 ? -21.774 14.474  -1.956  1.00 27.50  ? 173 CYS A CB  1 
ATOM   1084 S SG  . CYS A 1 130 ? -21.713 15.250  -3.580  1.00 28.05  ? 173 CYS A SG  1 
ATOM   1085 N N   . PRO A 1 131 ? -23.699 13.504  0.352   1.00 29.00  ? 174 PRO A N   1 
ATOM   1086 C CA  . PRO A 1 131 ? -23.972 12.730  1.570   1.00 27.85  ? 174 PRO A CA  1 
ATOM   1087 C C   . PRO A 1 131 ? -22.775 11.903  2.011   1.00 30.54  ? 174 PRO A C   1 
ATOM   1088 O O   . PRO A 1 131 ? -22.091 11.275  1.199   1.00 28.58  ? 174 PRO A O   1 
ATOM   1089 C CB  . PRO A 1 131 ? -25.150 11.831  1.164   1.00 29.56  ? 174 PRO A CB  1 
ATOM   1090 C CG  . PRO A 1 131 ? -25.764 12.506  -0.023  1.00 28.07  ? 174 PRO A CG  1 
ATOM   1091 C CD  . PRO A 1 131 ? -24.628 13.165  -0.740  1.00 26.40  ? 174 PRO A CD  1 
ATOM   1092 N N   . ASP A 1 132 ? -22.537 11.900  3.320   1.00 31.53  ? 175 ASP A N   1 
ATOM   1093 C CA  . ASP A 1 132 ? -21.591 10.985  3.941   1.00 34.47  ? 175 ASP A CA  1 
ATOM   1094 C C   . ASP A 1 132 ? -22.310 9.687   4.285   1.00 33.15  ? 175 ASP A C   1 
ATOM   1095 O O   . ASP A 1 132 ? -23.448 9.705   4.762   1.00 32.13  ? 175 ASP A O   1 
ATOM   1096 C CB  . ASP A 1 132 ? -20.983 11.604  5.200   1.00 33.90  ? 175 ASP A CB  1 
ATOM   1097 C CG  . ASP A 1 132 ? -20.110 10.629  5.965   1.00 37.24  ? 175 ASP A CG  1 
ATOM   1098 O OD1 . ASP A 1 132 ? -18.989 10.339  5.498   1.00 37.51  ? 175 ASP A OD1 1 
ATOM   1099 O OD2 . ASP A 1 132 ? -20.551 10.146  7.029   1.00 37.04  ? 175 ASP A OD2 1 
ATOM   1100 N N   . TRP A 1 133 ? -21.639 8.558   4.043   1.00 36.92  ? 176 TRP A N   1 
ATOM   1101 C CA  . TRP A 1 133 ? -22.315 7.272   4.189   1.00 37.61  ? 176 TRP A CA  1 
ATOM   1102 C C   . TRP A 1 133 ? -22.766 7.028   5.624   1.00 38.94  ? 176 TRP A C   1 
ATOM   1103 O O   . TRP A 1 133 ? -23.771 6.345   5.844   1.00 40.45  ? 176 TRP A O   1 
ATOM   1104 C CB  . TRP A 1 133 ? -21.413 6.132   3.711   1.00 40.63  ? 176 TRP A CB  1 
ATOM   1105 C CG  . TRP A 1 133 ? -20.179 5.904   4.533   1.00 45.46  ? 176 TRP A CG  1 
ATOM   1106 C CD1 . TRP A 1 133 ? -18.921 6.356   4.264   1.00 47.06  ? 176 TRP A CD1 1 
ATOM   1107 C CD2 . TRP A 1 133 ? -20.082 5.151   5.750   1.00 48.18  ? 176 TRP A CD2 1 
ATOM   1108 N NE1 . TRP A 1 133 ? -18.048 5.937   5.239   1.00 49.52  ? 176 TRP A NE1 1 
ATOM   1109 C CE2 . TRP A 1 133 ? -18.736 5.197   6.163   1.00 48.81  ? 176 TRP A CE2 1 
ATOM   1110 C CE3 . TRP A 1 133 ? -21.003 4.446   6.530   1.00 50.07  ? 176 TRP A CE3 1 
ATOM   1111 C CZ2 . TRP A 1 133 ? -18.288 4.567   7.322   1.00 51.66  ? 176 TRP A CZ2 1 
ATOM   1112 C CZ3 . TRP A 1 133 ? -20.557 3.821   7.682   1.00 52.90  ? 176 TRP A CZ3 1 
ATOM   1113 C CH2 . TRP A 1 133 ? -19.211 3.886   8.066   1.00 51.45  ? 176 TRP A CH2 1 
ATOM   1114 N N   . ARG A 1 134 ? -22.054 7.581   6.609   1.00 38.46  ? 177 ARG A N   1 
ATOM   1115 C CA  . ARG A 1 134 ? -22.402 7.352   8.007   1.00 44.40  ? 177 ARG A CA  1 
ATOM   1116 C C   . ARG A 1 134 ? -23.341 8.426   8.548   1.00 40.09  ? 177 ARG A C   1 
ATOM   1117 O O   . ARG A 1 134 ? -24.413 8.111   9.075   1.00 40.94  ? 177 ARG A O   1 
ATOM   1118 C CB  . ARG A 1 134 ? -21.134 7.285   8.870   1.00 50.22  ? 177 ARG A CB  1 
ATOM   1119 C CG  . ARG A 1 134 ? -21.421 6.999   10.343  1.00 55.84  ? 177 ARG A CG  1 
ATOM   1120 C CD  . ARG A 1 134 ? -20.148 6.882   11.166  1.00 67.22  ? 177 ARG A CD  1 
ATOM   1121 N NE  . ARG A 1 134 ? -19.406 8.137   11.210  1.00 79.78  ? 177 ARG A NE  1 
ATOM   1122 C CZ  . ARG A 1 134 ? -19.665 9.136   12.044  1.00 84.32  ? 177 ARG A CZ  1 
ATOM   1123 N NH1 . ARG A 1 134 ? -20.657 9.070   12.918  1.00 86.71  ? 177 ARG A NH1 1 
ATOM   1124 N NH2 . ARG A 1 134 ? -18.911 10.231  11.999  1.00 84.84  ? 177 ARG A NH2 1 
ATOM   1125 N N   . LYS A 1 135 ? -22.953 9.696   8.431   1.00 39.77  ? 178 LYS A N   1 
ATOM   1126 C CA  . LYS A 1 135 ? -23.728 10.766  9.048   1.00 36.84  ? 178 LYS A CA  1 
ATOM   1127 C C   . LYS A 1 135 ? -25.011 11.095  8.290   1.00 37.20  ? 178 LYS A C   1 
ATOM   1128 O O   . LYS A 1 135 ? -25.960 11.594  8.905   1.00 38.24  ? 178 LYS A O   1 
ATOM   1129 C CB  . LYS A 1 135 ? -22.876 12.031  9.176   1.00 37.84  ? 178 LYS A CB  1 
ATOM   1130 C CG  . LYS A 1 135 ? -21.601 11.860  9.988   1.00 47.64  ? 178 LYS A CG  1 
ATOM   1131 C CD  . LYS A 1 135 ? -20.804 13.158  10.018  1.00 51.18  ? 178 LYS A CD  1 
ATOM   1132 C CE  . LYS A 1 135 ? -19.305 12.911  10.092  1.00 57.48  ? 178 LYS A CE  1 
ATOM   1133 N NZ  . LYS A 1 135 ? -18.537 14.109  9.641   1.00 61.08  ? 178 LYS A NZ  1 
ATOM   1134 N N   . ASP A 1 136 ? -25.076 10.840  6.978   1.00 37.49  ? 179 ASP A N   1 
ATOM   1135 C CA  . ASP A 1 136 ? -26.227 11.256  6.181   1.00 35.81  ? 179 ASP A CA  1 
ATOM   1136 C C   . ASP A 1 136 ? -27.072 10.092  5.688   1.00 35.27  ? 179 ASP A C   1 
ATOM   1137 O O   . ASP A 1 136 ? -28.235 9.967   6.084   1.00 36.53  ? 179 ASP A O   1 
ATOM   1138 C CB  . ASP A 1 136 ? -25.747 12.097  4.983   1.00 33.16  ? 179 ASP A CB  1 
ATOM   1139 C CG  . ASP A 1 136 ? -25.113 13.410  5.401   1.00 33.69  ? 179 ASP A CG  1 
ATOM   1140 O OD1 . ASP A 1 136 ? -25.688 14.104  6.266   1.00 35.45  ? 179 ASP A OD1 1 
ATOM   1141 O OD2 . ASP A 1 136 ? -24.039 13.749  4.862   1.00 31.85  ? 179 ASP A OD2 1 
ATOM   1142 N N   . CYS A 1 137 ? -26.519 9.197   4.871   1.00 33.94  ? 180 CYS A N   1 
ATOM   1143 C CA  . CYS A 1 137 ? -27.325 8.138   4.272   1.00 35.81  ? 180 CYS A CA  1 
ATOM   1144 C C   . CYS A 1 137 ? -26.423 7.193   3.493   1.00 31.55  ? 180 CYS A C   1 
ATOM   1145 O O   . CYS A 1 137 ? -25.392 7.601   2.951   1.00 31.37  ? 180 CYS A O   1 
ATOM   1146 C CB  . CYS A 1 137 ? -28.415 8.709   3.353   1.00 35.31  ? 180 CYS A CB  1 
ATOM   1147 S SG  . CYS A 1 137 ? -27.795 9.637   1.933   1.00 36.62  ? 180 CYS A SG  1 
ATOM   1148 N N   . SER A 1 138 ? -26.841 5.932   3.423   1.00 34.29  ? 181 SER A N   1 
ATOM   1149 C CA  A SER A 1 138 ? -26.029 4.894   2.803   0.51 34.78  ? 181 SER A CA  1 
ATOM   1150 C CA  B SER A 1 138 ? -26.032 4.891   2.803   0.49 34.79  ? 181 SER A CA  1 
ATOM   1151 C C   . SER A 1 138 ? -26.244 4.783   1.300   1.00 32.59  ? 181 SER A C   1 
ATOM   1152 O O   . SER A 1 138 ? -25.327 4.366   0.582   1.00 30.41  ? 181 SER A O   1 
ATOM   1153 C CB  A SER A 1 138 ? -26.324 3.543   3.461   0.51 36.72  ? 181 SER A CB  1 
ATOM   1154 C CB  B SER A 1 138 ? -26.338 3.539   3.457   0.49 36.71  ? 181 SER A CB  1 
ATOM   1155 O OG  A SER A 1 138 ? -27.680 3.174   3.279   0.51 37.57  ? 181 SER A OG  1 
ATOM   1156 O OG  B SER A 1 138 ? -26.023 3.558   4.839   0.49 39.02  ? 181 SER A OG  1 
ATOM   1157 N N   . ASN A 1 139 ? -27.423 5.151   0.802   1.00 30.54  ? 182 ASN A N   1 
ATOM   1158 C CA  . ASN A 1 139 ? -27.748 4.979   -0.615  1.00 31.64  ? 182 ASN A CA  1 
ATOM   1159 C C   . ASN A 1 139 ? -27.449 6.250   -1.411  1.00 30.34  ? 182 ASN A C   1 
ATOM   1160 O O   . ASN A 1 139 ? -28.302 6.804   -2.105  1.00 29.57  ? 182 ASN A O   1 
ATOM   1161 C CB  . ASN A 1 139 ? -29.208 4.564   -0.767  1.00 29.14  ? 182 ASN A CB  1 
ATOM   1162 C CG  . ASN A 1 139 ? -29.466 3.161   -0.258  1.00 34.72  ? 182 ASN A CG  1 
ATOM   1163 O OD1 . ASN A 1 139 ? -28.601 2.292   -0.348  1.00 32.25  ? 182 ASN A OD1 1 
ATOM   1164 N ND2 . ASN A 1 139 ? -30.658 2.933   0.281   1.00 34.55  ? 182 ASN A ND2 1 
ATOM   1165 N N   . ASN A 1 140 ? -26.198 6.693   -1.319  1.00 29.24  ? 183 ASN A N   1 
ATOM   1166 C CA  . ASN A 1 140 ? -25.756 7.866   -2.056  1.00 25.70  ? 183 ASN A CA  1 
ATOM   1167 C C   . ASN A 1 140 ? -25.133 7.462   -3.385  1.00 26.66  ? 183 ASN A C   1 
ATOM   1168 O O   . ASN A 1 140 ? -24.769 6.300   -3.588  1.00 25.62  ? 183 ASN A O   1 
ATOM   1169 C CB  . ASN A 1 140 ? -24.755 8.663   -1.224  1.00 25.63  ? 183 ASN A CB  1 
ATOM   1170 C CG  . ASN A 1 140 ? -23.510 7.873   -0.894  1.00 26.30  ? 183 ASN A CG  1 
ATOM   1171 O OD1 . ASN A 1 140 ? -22.593 7.774   -1.706  1.00 26.83  ? 183 ASN A OD1 1 
ATOM   1172 N ND2 . ASN A 1 140 ? -23.465 7.314   0.309   1.00 27.73  ? 183 ASN A ND2 1 
ATOM   1173 N N   . PRO A 1 141 ? -25.003 8.407   -4.323  1.00 25.65  ? 184 PRO A N   1 
ATOM   1174 C CA  . PRO A 1 141 ? -24.542 8.028   -5.670  1.00 24.46  ? 184 PRO A CA  1 
ATOM   1175 C C   . PRO A 1 141 ? -23.207 7.305   -5.691  1.00 24.15  ? 184 PRO A C   1 
ATOM   1176 O O   . PRO A 1 141 ? -23.031 6.374   -6.489  1.00 22.20  ? 184 PRO A O   1 
ATOM   1177 C CB  . PRO A 1 141 ? -24.468 9.378   -6.401  1.00 23.28  ? 184 PRO A CB  1 
ATOM   1178 C CG  . PRO A 1 141 ? -25.463 10.237  -5.703  1.00 24.55  ? 184 PRO A CG  1 
ATOM   1179 C CD  . PRO A 1 141 ? -25.418 9.821   -4.256  1.00 24.46  ? 184 PRO A CD  1 
ATOM   1180 N N   . VAL A 1 142 ? -22.259 7.700   -4.837  1.00 25.06  ? 185 VAL A N   1 
ATOM   1181 C CA  . VAL A 1 142 ? -20.925 7.104   -4.879  1.00 22.63  ? 185 VAL A CA  1 
ATOM   1182 C C   . VAL A 1 142 ? -20.943 5.694   -4.295  1.00 23.78  ? 185 VAL A C   1 
ATOM   1183 O O   . VAL A 1 142 ? -20.453 4.743   -4.916  1.00 24.25  ? 185 VAL A O   1 
ATOM   1184 C CB  . VAL A 1 142 ? -19.916 8.002   -4.142  1.00 25.21  ? 185 VAL A CB  1 
ATOM   1185 C CG1 . VAL A 1 142 ? -18.583 7.283   -3.969  1.00 26.36  ? 185 VAL A CG1 1 
ATOM   1186 C CG2 . VAL A 1 142 ? -19.726 9.305   -4.896  1.00 26.76  ? 185 VAL A CG2 1 
ATOM   1187 N N   . SER A 1 143 ? -21.495 5.538   -3.088  1.00 23.22  ? 186 SER A N   1 
ATOM   1188 C CA  A SER A 1 143 ? -21.517 4.222   -2.455  0.68 27.88  ? 186 SER A CA  1 
ATOM   1189 C CA  B SER A 1 143 ? -21.516 4.222   -2.456  0.32 27.17  ? 186 SER A CA  1 
ATOM   1190 C C   . SER A 1 143 ? -22.317 3.227   -3.285  1.00 24.97  ? 186 SER A C   1 
ATOM   1191 O O   . SER A 1 143 ? -21.907 2.071   -3.448  1.00 27.66  ? 186 SER A O   1 
ATOM   1192 C CB  A SER A 1 143 ? -22.093 4.330   -1.042  0.68 32.24  ? 186 SER A CB  1 
ATOM   1193 C CB  B SER A 1 143 ? -22.095 4.323   -1.045  0.32 29.47  ? 186 SER A CB  1 
ATOM   1194 O OG  A SER A 1 143 ? -21.390 5.297   -0.277  0.68 28.48  ? 186 SER A OG  1 
ATOM   1195 O OG  B SER A 1 143 ? -23.483 4.602   -1.084  0.32 28.73  ? 186 SER A OG  1 
ATOM   1196 N N   . VAL A 1 144 ? -23.464 3.654   -3.815  1.00 26.17  ? 187 VAL A N   1 
ATOM   1197 C CA  . VAL A 1 144 ? -24.280 2.766   -4.638  1.00 23.59  ? 187 VAL A CA  1 
ATOM   1198 C C   . VAL A 1 144 ? -23.515 2.351   -5.887  1.00 23.51  ? 187 VAL A C   1 
ATOM   1199 O O   . VAL A 1 144 ? -23.572 1.192   -6.312  1.00 23.94  ? 187 VAL A O   1 
ATOM   1200 C CB  . VAL A 1 144 ? -25.618 3.444   -4.985  1.00 24.90  ? 187 VAL A CB  1 
ATOM   1201 C CG1 . VAL A 1 144 ? -26.390 2.619   -6.005  1.00 26.03  ? 187 VAL A CG1 1 
ATOM   1202 C CG2 . VAL A 1 144 ? -26.444 3.653   -3.721  1.00 27.84  ? 187 VAL A CG2 1 
ATOM   1203 N N   . PHE A 1 145 ? -22.783 3.287   -6.492  1.00 24.49  ? 188 PHE A N   1 
ATOM   1204 C CA  . PHE A 1 145 ? -21.997 2.955   -7.675  1.00 21.44  ? 188 PHE A CA  1 
ATOM   1205 C C   . PHE A 1 145 ? -21.019 1.820   -7.391  1.00 23.46  ? 188 PHE A C   1 
ATOM   1206 O O   . PHE A 1 145 ? -20.988 0.818   -8.111  1.00 21.93  ? 188 PHE A O   1 
ATOM   1207 C CB  . PHE A 1 145 ? -21.240 4.192   -8.163  1.00 21.84  ? 188 PHE A CB  1 
ATOM   1208 C CG  . PHE A 1 145 ? -20.219 3.895   -9.223  1.00 20.03  ? 188 PHE A CG  1 
ATOM   1209 C CD1 . PHE A 1 145 ? -20.582 3.846   -10.558 1.00 22.19  ? 188 PHE A CD1 1 
ATOM   1210 C CD2 . PHE A 1 145 ? -18.896 3.663   -8.885  1.00 22.51  ? 188 PHE A CD2 1 
ATOM   1211 C CE1 . PHE A 1 145 ? -19.645 3.570   -11.536 1.00 24.02  ? 188 PHE A CE1 1 
ATOM   1212 C CE2 . PHE A 1 145 ? -17.954 3.384   -9.859  1.00 24.76  ? 188 PHE A CE2 1 
ATOM   1213 C CZ  . PHE A 1 145 ? -18.331 3.337   -11.188 1.00 23.51  ? 188 PHE A CZ  1 
ATOM   1214 N N   . TRP A 1 146 ? -20.210 1.960   -6.340  1.00 24.68  ? 189 TRP A N   1 
ATOM   1215 C CA  . TRP A 1 146 ? -19.121 1.012   -6.127  1.00 24.20  ? 189 TRP A CA  1 
ATOM   1216 C C   . TRP A 1 146 ? -19.639 -0.350  -5.685  1.00 26.07  ? 189 TRP A C   1 
ATOM   1217 O O   . TRP A 1 146 ? -19.103 -1.383  -6.099  1.00 27.62  ? 189 TRP A O   1 
ATOM   1218 C CB  . TRP A 1 146 ? -18.123 1.576   -5.116  1.00 27.30  ? 189 TRP A CB  1 
ATOM   1219 C CG  . TRP A 1 146 ? -17.262 2.656   -5.711  1.00 26.92  ? 189 TRP A CG  1 
ATOM   1220 C CD1 . TRP A 1 146 ? -17.289 3.989   -5.412  1.00 29.73  ? 189 TRP A CD1 1 
ATOM   1221 C CD2 . TRP A 1 146 ? -16.265 2.494   -6.728  1.00 26.35  ? 189 TRP A CD2 1 
ATOM   1222 N NE1 . TRP A 1 146 ? -16.366 4.662   -6.175  1.00 27.71  ? 189 TRP A NE1 1 
ATOM   1223 C CE2 . TRP A 1 146 ? -15.722 3.768   -6.989  1.00 27.86  ? 189 TRP A CE2 1 
ATOM   1224 C CE3 . TRP A 1 146 ? -15.776 1.394   -7.440  1.00 28.44  ? 189 TRP A CE3 1 
ATOM   1225 C CZ2 . TRP A 1 146 ? -14.714 3.972   -7.928  1.00 26.36  ? 189 TRP A CZ2 1 
ATOM   1226 C CZ3 . TRP A 1 146 ? -14.775 1.598   -8.372  1.00 26.87  ? 189 TRP A CZ3 1 
ATOM   1227 C CH2 . TRP A 1 146 ? -14.255 2.878   -8.608  1.00 28.37  ? 189 TRP A CH2 1 
ATOM   1228 N N   . LYS A 1 147 ? -20.683 -0.384  -4.854  1.00 25.15  ? 190 LYS A N   1 
ATOM   1229 C CA  . LYS A 1 147 ? -21.227 -1.677  -4.453  1.00 26.33  ? 190 LYS A CA  1 
ATOM   1230 C C   . LYS A 1 147 ? -21.860 -2.395  -5.638  1.00 25.21  ? 190 LYS A C   1 
ATOM   1231 O O   . LYS A 1 147 ? -21.840 -3.630  -5.696  1.00 25.69  ? 190 LYS A O   1 
ATOM   1232 C CB  . LYS A 1 147 ? -22.233 -1.507  -3.312  1.00 30.78  ? 190 LYS A CB  1 
ATOM   1233 C CG  . LYS A 1 147 ? -23.671 -1.233  -3.731  1.00 30.49  ? 190 LYS A CG  1 
ATOM   1234 C CD  . LYS A 1 147 ? -24.546 -0.975  -2.506  1.00 33.79  ? 190 LYS A CD  1 
ATOM   1235 C CE  . LYS A 1 147 ? -25.950 -0.538  -2.893  1.00 37.47  ? 190 LYS A CE  1 
ATOM   1236 N NZ  . LYS A 1 147 ? -26.759 -0.139  -1.706  1.00 40.50  ? 190 LYS A NZ  1 
ATOM   1237 N N   . THR A 1 148 ? -22.412 -1.643  -6.592  1.00 25.59  ? 191 THR A N   1 
ATOM   1238 C CA  . THR A 1 148 ? -22.981 -2.259  -7.786  1.00 26.83  ? 191 THR A CA  1 
ATOM   1239 C C   . THR A 1 148 ? -21.887 -2.798  -8.701  1.00 28.94  ? 191 THR A C   1 
ATOM   1240 O O   . THR A 1 148 ? -21.920 -3.966  -9.107  1.00 25.68  ? 191 THR A O   1 
ATOM   1241 C CB  . THR A 1 148 ? -23.845 -1.246  -8.539  1.00 29.43  ? 191 THR A CB  1 
ATOM   1242 O OG1 . THR A 1 148 ? -24.845 -0.720  -7.660  1.00 29.76  ? 191 THR A OG1 1 
ATOM   1243 C CG2 . THR A 1 148 ? -24.518 -1.897  -9.746  1.00 29.32  ? 191 THR A CG2 1 
ATOM   1244 N N   . VAL A 1 149 ? -20.909 -1.959  -9.040  1.00 24.94  ? 192 VAL A N   1 
ATOM   1245 C CA  A VAL A 1 149 ? -19.861 -2.385  -9.960  0.64 28.52  ? 192 VAL A CA  1 
ATOM   1246 C CA  B VAL A 1 149 ? -19.857 -2.383  -9.958  0.36 28.64  ? 192 VAL A CA  1 
ATOM   1247 C C   . VAL A 1 149 ? -18.949 -3.417  -9.300  1.00 26.52  ? 192 VAL A C   1 
ATOM   1248 O O   . VAL A 1 149 ? -18.473 -4.347  -9.956  1.00 27.65  ? 192 VAL A O   1 
ATOM   1249 C CB  A VAL A 1 149 ? -19.082 -1.160  -10.477 0.64 30.77  ? 192 VAL A CB  1 
ATOM   1250 C CB  B VAL A 1 149 ? -19.062 -1.167  -10.465 0.36 29.87  ? 192 VAL A CB  1 
ATOM   1251 C CG1 A VAL A 1 149 ? -18.025 -0.718  -9.478  0.64 27.58  ? 192 VAL A CG1 1 
ATOM   1252 C CG1 B VAL A 1 149 ? -18.095 -1.579  -11.564 0.36 33.32  ? 192 VAL A CG1 1 
ATOM   1253 C CG2 A VAL A 1 149 ? -18.468 -1.454  -11.839 0.64 34.31  ? 192 VAL A CG2 1 
ATOM   1254 C CG2 B VAL A 1 149 ? -20.009 -0.094  -10.975 0.36 29.55  ? 192 VAL A CG2 1 
ATOM   1255 N N   . SER A 1 150 ? -18.684 -3.268  -7.995  1.00 25.67  ? 193 SER A N   1 
ATOM   1256 C CA  A SER A 1 150 ? -17.856 -4.251  -7.299  0.44 26.35  ? 193 SER A CA  1 
ATOM   1257 C CA  B SER A 1 150 ? -17.855 -4.252  -7.303  0.56 26.67  ? 193 SER A CA  1 
ATOM   1258 C C   . SER A 1 150 ? -18.512 -5.626  -7.305  1.00 25.88  ? 193 SER A C   1 
ATOM   1259 O O   . SER A 1 150 ? -17.848 -6.639  -7.543  1.00 24.53  ? 193 SER A O   1 
ATOM   1260 C CB  A SER A 1 150 ? -17.593 -3.798  -5.862  0.44 26.98  ? 193 SER A CB  1 
ATOM   1261 C CB  B SER A 1 150 ? -17.582 -3.800  -5.868  0.56 28.48  ? 193 SER A CB  1 
ATOM   1262 O OG  A SER A 1 150 ? -16.852 -2.590  -5.829  0.44 28.17  ? 193 SER A OG  1 
ATOM   1263 O OG  B SER A 1 150 ? -16.754 -4.731  -5.194  0.56 27.64  ? 193 SER A OG  1 
ATOM   1264 N N   . ARG A 1 151 ? -19.820 -5.680  -7.039  1.00 27.09  ? 194 ARG A N   1 
ATOM   1265 C CA  . ARG A 1 151 ? -20.521 -6.959  -7.045  1.00 25.72  ? 194 ARG A CA  1 
ATOM   1266 C C   . ARG A 1 151 ? -20.453 -7.606  -8.422  1.00 28.80  ? 194 ARG A C   1 
ATOM   1267 O O   . ARG A 1 151 ? -20.177 -8.806  -8.543  1.00 25.35  ? 194 ARG A O   1 
ATOM   1268 C CB  . ARG A 1 151 ? -21.975 -6.759  -6.615  1.00 29.12  ? 194 ARG A CB  1 
ATOM   1269 C CG  . ARG A 1 151 ? -22.827 -8.023  -6.699  1.00 33.76  ? 194 ARG A CG  1 
ATOM   1270 C CD  . ARG A 1 151 ? -24.170 -7.854  -6.001  1.00 36.46  ? 194 ARG A CD  1 
ATOM   1271 N NE  . ARG A 1 151 ? -25.115 -7.074  -6.790  1.00 45.97  ? 194 ARG A NE  1 
ATOM   1272 C CZ  . ARG A 1 151 ? -25.879 -7.575  -7.754  1.00 55.46  ? 194 ARG A CZ  1 
ATOM   1273 N NH1 . ARG A 1 151 ? -25.811 -8.852  -8.097  1.00 53.69  ? 194 ARG A NH1 1 
ATOM   1274 N NH2 . ARG A 1 151 ? -26.731 -6.775  -8.388  1.00 61.89  ? 194 ARG A NH2 1 
ATOM   1275 N N   . ARG A 1 152 ? -20.685 -6.818  -9.472  1.00 28.32  ? 195 ARG A N   1 
ATOM   1276 C CA  . ARG A 1 152 ? -20.628 -7.349  -10.829 1.00 29.29  ? 195 ARG A CA  1 
ATOM   1277 C C   . ARG A 1 152 ? -19.235 -7.868  -11.158 1.00 26.39  ? 195 ARG A C   1 
ATOM   1278 O O   . ARG A 1 152 ? -19.090 -8.908  -11.812 1.00 27.84  ? 195 ARG A O   1 
ATOM   1279 C CB  . ARG A 1 152 ? -21.050 -6.267  -11.824 1.00 28.87  ? 195 ARG A CB  1 
ATOM   1280 C CG  . ARG A 1 152 ? -22.494 -5.812  -11.667 1.00 36.01  ? 195 ARG A CG  1 
ATOM   1281 C CD  . ARG A 1 152 ? -23.459 -6.791  -12.317 1.00 46.44  ? 195 ARG A CD  1 
ATOM   1282 N NE  . ARG A 1 152 ? -23.398 -6.716  -13.773 1.00 51.22  ? 195 ARG A NE  1 
ATOM   1283 C CZ  . ARG A 1 152 ? -24.148 -5.914  -14.520 1.00 49.00  ? 195 ARG A CZ  1 
ATOM   1284 N NH1 . ARG A 1 152 ? -25.059 -5.118  -13.983 1.00 47.68  ? 195 ARG A NH1 1 
ATOM   1285 N NH2 . ARG A 1 152 ? -23.977 -5.910  -15.838 1.00 49.34  ? 195 ARG A NH2 1 
ATOM   1286 N N   . PHE A 1 153 ? -18.196 -7.155  -10.718 1.00 24.92  ? 196 PHE A N   1 
ATOM   1287 C CA  . PHE A 1 153 ? -16.827 -7.594  -10.971 1.00 24.25  ? 196 PHE A CA  1 
ATOM   1288 C C   . PHE A 1 153 ? -16.547 -8.933  -10.297 1.00 28.93  ? 196 PHE A C   1 
ATOM   1289 O O   . PHE A 1 153 ? -15.980 -9.846  -10.909 1.00 27.85  ? 196 PHE A O   1 
ATOM   1290 C CB  . PHE A 1 153 ? -15.853 -6.524  -10.476 1.00 26.61  ? 196 PHE A CB  1 
ATOM   1291 C CG  . PHE A 1 153 ? -14.452 -6.671  -11.004 1.00 24.77  ? 196 PHE A CG  1 
ATOM   1292 C CD1 . PHE A 1 153 ? -14.204 -6.635  -12.366 1.00 24.31  ? 196 PHE A CD1 1 
ATOM   1293 C CD2 . PHE A 1 153 ? -13.379 -6.812  -10.138 1.00 24.15  ? 196 PHE A CD2 1 
ATOM   1294 C CE1 . PHE A 1 153 ? -12.918 -6.754  -12.855 1.00 24.72  ? 196 PHE A CE1 1 
ATOM   1295 C CE2 . PHE A 1 153 ? -12.089 -6.929  -10.623 1.00 25.41  ? 196 PHE A CE2 1 
ATOM   1296 C CZ  . PHE A 1 153 ? -11.859 -6.899  -11.985 1.00 23.31  ? 196 PHE A CZ  1 
ATOM   1297 N N   . ALA A 1 154 ? -16.944 -9.070  -9.030  1.00 25.96  ? 197 ALA A N   1 
ATOM   1298 C CA  . ALA A 1 154 ? -16.723 -10.323 -8.316  1.00 27.36  ? 197 ALA A CA  1 
ATOM   1299 C C   . ALA A 1 154 ? -17.528 -11.463 -8.932  1.00 28.15  ? 197 ALA A C   1 
ATOM   1300 O O   . ALA A 1 154 ? -17.053 -12.603 -8.992  1.00 26.43  ? 197 ALA A O   1 
ATOM   1301 C CB  . ALA A 1 154 ? -17.078 -10.151 -6.840  1.00 25.81  ? 197 ALA A CB  1 
ATOM   1302 N N   . GLU A 1 155 ? -18.750 -11.176 -9.387  1.00 26.85  ? 198 GLU A N   1 
ATOM   1303 C CA  . GLU A 1 155 ? -19.588 -12.209 -9.983  1.00 29.57  ? 198 GLU A CA  1 
ATOM   1304 C C   . GLU A 1 155 ? -18.993 -12.776 -11.265 1.00 31.46  ? 198 GLU A C   1 
ATOM   1305 O O   . GLU A 1 155 ? -19.356 -13.888 -11.665 1.00 29.50  ? 198 GLU A O   1 
ATOM   1306 C CB  . GLU A 1 155 ? -20.981 -11.651 -10.276 1.00 28.12  ? 198 GLU A CB  1 
ATOM   1307 C CG  . GLU A 1 155 ? -21.874 -11.528 -9.056  1.00 32.30  ? 198 GLU A CG  1 
ATOM   1308 C CD  . GLU A 1 155 ? -23.179 -10.818 -9.363  1.00 35.61  ? 198 GLU A CD  1 
ATOM   1309 O OE1 . GLU A 1 155 ? -23.278 -10.193 -10.439 1.00 34.63  ? 198 GLU A OE1 1 
ATOM   1310 O OE2 . GLU A 1 155 ? -24.107 -10.886 -8.530  1.00 38.97  ? 198 GLU A OE2 1 
ATOM   1311 N N   . ALA A 1 156 ? -18.102 -12.039 -11.924 1.00 31.05  ? 199 ALA A N   1 
ATOM   1312 C CA  . ALA A 1 156 ? -17.514 -12.489 -13.176 1.00 33.16  ? 199 ALA A CA  1 
ATOM   1313 C C   . ALA A 1 156 ? -16.249 -13.318 -12.991 1.00 29.35  ? 199 ALA A C   1 
ATOM   1314 O O   . ALA A 1 156 ? -15.791 -13.935 -13.957 1.00 30.77  ? 199 ALA A O   1 
ATOM   1315 C CB  . ALA A 1 156 ? -17.198 -11.282 -14.067 1.00 31.21  ? 199 ALA A CB  1 
ATOM   1316 N N   . ALA A 1 157 ? -15.679 -13.355 -11.789 1.00 31.13  ? 200 ALA A N   1 
ATOM   1317 C CA  . ALA A 1 157 ? -14.424 -14.061 -11.576 1.00 29.84  ? 200 ALA A CA  1 
ATOM   1318 C C   . ALA A 1 157 ? -14.623 -15.574 -11.650 1.00 28.46  ? 200 ALA A C   1 
ATOM   1319 O O   . ALA A 1 157 ? -15.716 -16.100 -11.429 1.00 26.41  ? 200 ALA A O   1 
ATOM   1320 C CB  . ALA A 1 157 ? -13.821 -13.685 -10.221 1.00 29.48  ? 200 ALA A CB  1 
ATOM   1321 N N   . CYS A 1 158 ? -13.530 -16.276 -11.953 1.00 29.12  ? 201 CYS A N   1 
ATOM   1322 C CA  . CYS A 1 158 ? -13.542 -17.726 -12.074 1.00 31.55  ? 201 CYS A CA  1 
ATOM   1323 C C   . CYS A 1 158 ? -12.181 -18.266 -11.654 1.00 29.51  ? 201 CYS A C   1 
ATOM   1324 O O   . CYS A 1 158 ? -11.202 -17.525 -11.541 1.00 28.16  ? 201 CYS A O   1 
ATOM   1325 C CB  . CYS A 1 158 ? -13.859 -18.181 -13.506 1.00 28.83  ? 201 CYS A CB  1 
ATOM   1326 S SG  . CYS A 1 158 ? -12.493 -17.892 -14.655 1.00 37.59  ? 201 CYS A SG  1 
ATOM   1327 N N   . ASP A 1 159 ? -12.135 -19.579 -11.428 1.00 30.20  ? 202 ASP A N   1 
ATOM   1328 C CA  . ASP A 1 159 ? -10.900 -20.313 -11.139 1.00 32.72  ? 202 ASP A CA  1 
ATOM   1329 C C   . ASP A 1 159 ? -10.320 -19.798 -9.830  1.00 31.45  ? 202 ASP A C   1 
ATOM   1330 O O   . ASP A 1 159 ? -10.966 -19.978 -8.780  1.00 30.89  ? 202 ASP A O   1 
ATOM   1331 C CB  . ASP A 1 159 ? -9.975  -20.206 -12.354 1.00 33.95  ? 202 ASP A CB  1 
ATOM   1332 C CG  . ASP A 1 159 ? -8.777  -21.130 -12.252 1.00 39.28  ? 202 ASP A CG  1 
ATOM   1333 O OD1 . ASP A 1 159 ? -8.921  -22.222 -11.663 1.00 38.30  ? 202 ASP A OD1 1 
ATOM   1334 O OD2 . ASP A 1 159 ? -7.690  -20.761 -12.744 1.00 41.03  ? 202 ASP A OD2 1 
ATOM   1335 N N   . VAL A 1 160 ? -9.136  -19.190 -9.819  1.00 28.70  ? 203 VAL A N   1 
ATOM   1336 C CA  . VAL A 1 160 ? -8.507  -18.673 -8.610  1.00 27.93  ? 203 VAL A CA  1 
ATOM   1337 C C   . VAL A 1 160 ? -8.619  -17.155 -8.632  1.00 29.36  ? 203 VAL A C   1 
ATOM   1338 O O   . VAL A 1 160 ? -8.246  -16.513 -9.622  1.00 29.84  ? 203 VAL A O   1 
ATOM   1339 C CB  . VAL A 1 160 ? -7.037  -19.115 -8.502  1.00 31.57  ? 203 VAL A CB  1 
ATOM   1340 C CG1 . VAL A 1 160 ? -6.394  -18.545 -7.239  1.00 28.94  ? 203 VAL A CG1 1 
ATOM   1341 C CG2 . VAL A 1 160 ? -6.932  -20.638 -8.517  1.00 34.65  ? 203 VAL A CG2 1 
ATOM   1342 N N   . VAL A 1 161 ? -9.145  -16.586 -7.551  1.00 27.23  ? 204 VAL A N   1 
ATOM   1343 C CA  . VAL A 1 161 ? -9.264  -15.144 -7.385  1.00 27.72  ? 204 VAL A CA  1 
ATOM   1344 C C   . VAL A 1 161 ? -8.287  -14.714 -6.300  1.00 28.83  ? 204 VAL A C   1 
ATOM   1345 O O   . VAL A 1 161 ? -8.233  -15.329 -5.229  1.00 26.02  ? 204 VAL A O   1 
ATOM   1346 C CB  . VAL A 1 161 ? -10.700 -14.728 -7.022  1.00 29.13  ? 204 VAL A CB  1 
ATOM   1347 C CG1 . VAL A 1 161 ? -10.811 -13.208 -6.953  1.00 29.86  ? 204 VAL A CG1 1 
ATOM   1348 C CG2 . VAL A 1 161 ? -11.684 -15.300 -8.024  1.00 33.70  ? 204 VAL A CG2 1 
ATOM   1349 N N   . HIS A 1 162 ? -7.518  -13.666 -6.579  1.00 26.02  ? 205 HIS A N   1 
ATOM   1350 C CA  . HIS A 1 162 ? -6.534  -13.140 -5.644  1.00 27.13  ? 205 HIS A CA  1 
ATOM   1351 C C   . HIS A 1 162 ? -7.048  -11.850 -5.022  1.00 26.74  ? 205 HIS A C   1 
ATOM   1352 O O   . HIS A 1 162 ? -7.737  -11.061 -5.677  1.00 27.00  ? 205 HIS A O   1 
ATOM   1353 C CB  . HIS A 1 162 ? -5.196  -12.890 -6.343  1.00 26.75  ? 205 HIS A CB  1 
ATOM   1354 C CG  . HIS A 1 162 ? -4.584  -14.126 -6.924  1.00 31.74  ? 205 HIS A CG  1 
ATOM   1355 N ND1 . HIS A 1 162 ? -4.926  -14.611 -8.168  1.00 30.42  ? 205 HIS A ND1 1 
ATOM   1356 C CD2 . HIS A 1 162 ? -3.668  -14.990 -6.422  1.00 33.14  ? 205 HIS A CD2 1 
ATOM   1357 C CE1 . HIS A 1 162 ? -4.238  -15.713 -8.413  1.00 33.25  ? 205 HIS A CE1 1 
ATOM   1358 N NE2 . HIS A 1 162 ? -3.469  -15.965 -7.370  1.00 32.00  ? 205 HIS A NE2 1 
ATOM   1359 N N   . VAL A 1 163 ? -6.724  -11.651 -3.747  1.00 25.62  ? 206 VAL A N   1 
ATOM   1360 C CA  . VAL A 1 163 ? -7.041  -10.418 -3.035  1.00 25.95  ? 206 VAL A CA  1 
ATOM   1361 C C   . VAL A 1 163 ? -5.807  -9.976  -2.263  1.00 25.88  ? 206 VAL A C   1 
ATOM   1362 O O   . VAL A 1 163 ? -5.184  -10.784 -1.565  1.00 23.54  ? 206 VAL A O   1 
ATOM   1363 C CB  . VAL A 1 163 ? -8.239  -10.591 -2.081  1.00 25.47  ? 206 VAL A CB  1 
ATOM   1364 C CG1 . VAL A 1 163 ? -7.960  -11.680 -1.052  1.00 27.92  ? 206 VAL A CG1 1 
ATOM   1365 C CG2 . VAL A 1 163 ? -8.558  -9.267  -1.392  1.00 26.61  ? 206 VAL A CG2 1 
ATOM   1366 N N   . MET A 1 164 ? -5.453  -8.698  -2.393  1.00 26.41  ? 207 MET A N   1 
ATOM   1367 C CA  . MET A 1 164 ? -4.402  -8.098  -1.580  1.00 24.72  ? 207 MET A CA  1 
ATOM   1368 C C   . MET A 1 164 ? -5.017  -7.513  -0.316  1.00 25.69  ? 207 MET A C   1 
ATOM   1369 O O   . MET A 1 164 ? -5.998  -6.765  -0.385  1.00 26.30  ? 207 MET A O   1 
ATOM   1370 C CB  . MET A 1 164 ? -3.663  -7.003  -2.349  1.00 25.91  ? 207 MET A CB  1 
ATOM   1371 C CG  . MET A 1 164 ? -2.569  -7.496  -3.279  1.00 28.94  ? 207 MET A CG  1 
ATOM   1372 S SD  . MET A 1 164 ? -1.656  -6.133  -4.039  1.00 30.33  ? 207 MET A SD  1 
ATOM   1373 C CE  . MET A 1 164 ? -0.563  -7.042  -5.130  1.00 34.37  ? 207 MET A CE  1 
ATOM   1374 N N   . LEU A 1 165 ? -4.437  -7.853  0.832   1.00 24.38  ? 208 LEU A N   1 
ATOM   1375 C CA  . LEU A 1 165 ? -4.869  -7.340  2.121   1.00 27.17  ? 208 LEU A CA  1 
ATOM   1376 C C   . LEU A 1 165 ? -3.733  -6.551  2.760   1.00 30.46  ? 208 LEU A C   1 
ATOM   1377 O O   . LEU A 1 165 ? -2.553  -6.862  2.565   1.00 28.25  ? 208 LEU A O   1 
ATOM   1378 C CB  . LEU A 1 165 ? -5.302  -8.472  3.057   1.00 27.06  ? 208 LEU A CB  1 
ATOM   1379 C CG  . LEU A 1 165 ? -6.446  -9.362  2.569   1.00 26.73  ? 208 LEU A CG  1 
ATOM   1380 C CD1 . LEU A 1 165 ? -6.682  -10.507 3.542   1.00 26.95  ? 208 LEU A CD1 1 
ATOM   1381 C CD2 . LEU A 1 165 ? -7.716  -8.548  2.382   1.00 29.72  ? 208 LEU A CD2 1 
ATOM   1382 N N   . ASP A 1 166 ? -4.100  -5.530  3.530   1.00 28.39  ? 209 ASP A N   1 
ATOM   1383 C CA  . ASP A 1 166 ? -3.129  -4.632  4.155   1.00 32.99  ? 209 ASP A CA  1 
ATOM   1384 C C   . ASP A 1 166 ? -2.775  -5.186  5.529   1.00 31.02  ? 209 ASP A C   1 
ATOM   1385 O O   . ASP A 1 166 ? -3.548  -5.065  6.483   1.00 31.14  ? 209 ASP A O   1 
ATOM   1386 C CB  . ASP A 1 166 ? -3.694  -3.220  4.244   1.00 34.16  ? 209 ASP A CB  1 
ATOM   1387 C CG  . ASP A 1 166 ? -2.732  -2.245  4.892   1.00 40.54  ? 209 ASP A CG  1 
ATOM   1388 O OD1 . ASP A 1 166 ? -1.556  -2.611  5.108   1.00 37.43  ? 209 ASP A OD1 1 
ATOM   1389 O OD2 . ASP A 1 166 ? -3.157  -1.110  5.191   1.00 41.90  ? 209 ASP A OD2 1 
ATOM   1390 N N   . GLY A 1 167 ? -1.592  -5.786  5.634   1.00 29.37  ? 210 GLY A N   1 
ATOM   1391 C CA  . GLY A 1 167 ? -1.145  -6.406  6.862   1.00 32.97  ? 210 GLY A CA  1 
ATOM   1392 C C   . GLY A 1 167 ? -0.595  -5.465  7.908   1.00 36.00  ? 210 GLY A C   1 
ATOM   1393 O O   . GLY A 1 167 ? -0.233  -5.912  9.001   1.00 37.25  ? 210 GLY A O   1 
ATOM   1394 N N   . SER A 1 168 ? -0.515  -4.171  7.610   1.00 35.70  ? 211 SER A N   1 
ATOM   1395 C CA  . SER A 1 168 ? -0.029  -3.183  8.563   1.00 41.75  ? 211 SER A CA  1 
ATOM   1396 C C   . SER A 1 168 ? -1.127  -2.647  9.473   1.00 41.48  ? 211 SER A C   1 
ATOM   1397 O O   . SER A 1 168 ? -0.837  -1.832  10.353  1.00 42.52  ? 211 SER A O   1 
ATOM   1398 C CB  . SER A 1 168 ? 0.630   -2.017  7.817   1.00 37.74  ? 211 SER A CB  1 
ATOM   1399 O OG  . SER A 1 168 ? -0.324  -1.297  7.055   1.00 41.73  ? 211 SER A OG  1 
ATOM   1400 N N   . ARG A 1 169 ? -2.369  -3.086  9.289   1.00 44.94  ? 212 ARG A N   1 
ATOM   1401 C CA  . ARG A 1 169 ? -3.515  -2.573  10.024  1.00 52.55  ? 212 ARG A CA  1 
ATOM   1402 C C   . ARG A 1 169 ? -4.019  -3.601  11.029  1.00 52.40  ? 212 ARG A C   1 
ATOM   1403 O O   . ARG A 1 169 ? -3.747  -4.799  10.923  1.00 49.78  ? 212 ARG A O   1 
ATOM   1404 C CB  . ARG A 1 169 ? -4.646  -2.190  9.064   1.00 62.01  ? 212 ARG A CB  1 
ATOM   1405 C CG  . ARG A 1 169 ? -4.356  -0.944  8.248   1.00 63.10  ? 212 ARG A CG  1 
ATOM   1406 C CD  . ARG A 1 169 ? -4.744  0.318   9.006   1.00 76.45  ? 212 ARG A CD  1 
ATOM   1407 N NE  . ARG A 1 169 ? -6.169  0.608   8.887   1.00 81.95  ? 212 ARG A NE  1 
ATOM   1408 C CZ  . ARG A 1 169 ? -6.705  1.379   7.949   1.00 84.88  ? 212 ARG A CZ  1 
ATOM   1409 N NH1 . ARG A 1 169 ? -5.961  1.970   7.027   1.00 80.53  ? 212 ARG A NH1 1 
ATOM   1410 N NH2 . ARG A 1 169 ? -8.022  1.561   7.935   1.00 81.70  ? 212 ARG A NH2 1 
ATOM   1411 N N   . SER A 1 170 ? -4.782  -3.106  12.008  1.00 59.48  ? 213 SER A N   1 
ATOM   1412 C CA  . SER A 1 170 ? -5.268  -3.965  13.081  1.00 63.03  ? 213 SER A CA  1 
ATOM   1413 C C   . SER A 1 170 ? -6.271  -4.991  12.575  1.00 59.95  ? 213 SER A C   1 
ATOM   1414 O O   . SER A 1 170 ? -6.378  -6.083  13.146  1.00 62.12  ? 213 SER A O   1 
ATOM   1415 C CB  . SER A 1 170 ? -5.903  -3.118  14.183  1.00 72.26  ? 213 SER A CB  1 
ATOM   1416 O OG  . SER A 1 170 ? -6.948  -2.316  13.662  1.00 73.99  ? 213 SER A OG  1 
ATOM   1417 N N   . LYS A 1 171 ? -7.018  -4.660  11.527  1.00 54.38  ? 214 LYS A N   1 
ATOM   1418 C CA  . LYS A 1 171 ? -7.980  -5.570  10.911  1.00 48.54  ? 214 LYS A CA  1 
ATOM   1419 C C   . LYS A 1 171 ? -7.453  -5.880  9.514   1.00 41.30  ? 214 LYS A C   1 
ATOM   1420 O O   . LYS A 1 171 ? -7.819  -5.222  8.539   1.00 39.81  ? 214 LYS A O   1 
ATOM   1421 C CB  . LYS A 1 171 ? -9.384  -4.957  10.866  1.00 46.09  ? 214 LYS A CB  1 
ATOM   1422 C CG  . LYS A 1 171 ? -10.062 -4.849  12.229  1.00 50.64  ? 214 LYS A CG  1 
ATOM   1423 C CD  . LYS A 1 171 ? -11.454 -4.241  12.117  1.00 51.12  ? 214 LYS A CD  1 
ATOM   1424 C CE  . LYS A 1 171 ? -12.159 -4.179  13.467  1.00 58.38  ? 214 LYS A CE  1 
ATOM   1425 N NZ  . LYS A 1 171 ? -12.403 -5.531  14.046  1.00 64.60  ? 214 LYS A NZ  1 
ATOM   1426 N N   . ILE A 1 172 ? -6.576  -6.885  9.426   1.00 37.82  ? 215 ILE A N   1 
ATOM   1427 C CA  . ILE A 1 172 ? -6.030  -7.275  8.130   1.00 35.53  ? 215 ILE A CA  1 
ATOM   1428 C C   . ILE A 1 172 ? -7.164  -7.643  7.185   1.00 31.99  ? 215 ILE A C   1 
ATOM   1429 O O   . ILE A 1 172 ? -7.184  -7.231  6.019   1.00 32.07  ? 215 ILE A O   1 
ATOM   1430 C CB  . ILE A 1 172 ? -5.023  -8.430  8.292   1.00 33.16  ? 215 ILE A CB  1 
ATOM   1431 C CG1 . ILE A 1 172 ? -3.923  -8.035  9.282   1.00 35.56  ? 215 ILE A CG1 1 
ATOM   1432 C CG2 . ILE A 1 172 ? -4.409  -8.796  6.946   1.00 31.38  ? 215 ILE A CG2 1 
ATOM   1433 C CD1 . ILE A 1 172 ? -2.866  -9.098  9.491   1.00 35.75  ? 215 ILE A CD1 1 
ATOM   1434 N N   . PHE A 1 173 ? -8.123  -8.418  7.675   1.00 32.58  ? 216 PHE A N   1 
ATOM   1435 C CA  . PHE A 1 173 ? -9.410  -8.586  7.020   1.00 33.98  ? 216 PHE A CA  1 
ATOM   1436 C C   . PHE A 1 173 ? -10.445 -7.791  7.800   1.00 33.04  ? 216 PHE A C   1 
ATOM   1437 O O   . PHE A 1 173 ? -10.569 -7.958  9.019   1.00 33.91  ? 216 PHE A O   1 
ATOM   1438 C CB  . PHE A 1 173 ? -9.831  -10.052 6.947   1.00 30.19  ? 216 PHE A CB  1 
ATOM   1439 C CG  . PHE A 1 173 ? -11.279 -10.233 6.604   1.00 31.23  ? 216 PHE A CG  1 
ATOM   1440 C CD1 . PHE A 1 173 ? -11.742 -9.931  5.335   1.00 29.23  ? 216 PHE A CD1 1 
ATOM   1441 C CD2 . PHE A 1 173 ? -12.181 -10.681 7.554   1.00 31.80  ? 216 PHE A CD2 1 
ATOM   1442 C CE1 . PHE A 1 173 ? -13.075 -10.084 5.015   1.00 28.53  ? 216 PHE A CE1 1 
ATOM   1443 C CE2 . PHE A 1 173 ? -13.517 -10.837 7.239   1.00 34.04  ? 216 PHE A CE2 1 
ATOM   1444 C CZ  . PHE A 1 173 ? -13.965 -10.537 5.966   1.00 29.38  ? 216 PHE A CZ  1 
ATOM   1445 N N   . ASP A 1 174 ? -11.182 -6.935  7.100   1.00 31.74  ? 217 ASP A N   1 
ATOM   1446 C CA  . ASP A 1 174 ? -12.149 -6.035  7.713   1.00 33.39  ? 217 ASP A CA  1 
ATOM   1447 C C   . ASP A 1 174 ? -13.514 -6.295  7.093   1.00 31.80  ? 217 ASP A C   1 
ATOM   1448 O O   . ASP A 1 174 ? -13.708 -6.067  5.895   1.00 32.50  ? 217 ASP A O   1 
ATOM   1449 C CB  . ASP A 1 174 ? -11.726 -4.576  7.519   1.00 34.74  ? 217 ASP A CB  1 
ATOM   1450 C CG  . ASP A 1 174 ? -12.601 -3.607  8.286   1.00 35.70  ? 217 ASP A CG  1 
ATOM   1451 O OD1 . ASP A 1 174 ? -13.500 -4.061  9.024   1.00 37.42  ? 217 ASP A OD1 1 
ATOM   1452 O OD2 . ASP A 1 174 ? -12.388 -2.385  8.148   1.00 44.23  ? 217 ASP A OD2 1 
ATOM   1453 N N   . LYS A 1 175 ? -14.455 -6.776  7.910   1.00 32.51  ? 218 LYS A N   1 
ATOM   1454 C CA  . LYS A 1 175 ? -15.813 -6.988  7.420   1.00 37.44  ? 218 LYS A CA  1 
ATOM   1455 C C   . LYS A 1 175 ? -16.421 -5.695  6.897   1.00 37.82  ? 218 LYS A C   1 
ATOM   1456 O O   . LYS A 1 175 ? -17.280 -5.727  6.009   1.00 36.95  ? 218 LYS A O   1 
ATOM   1457 C CB  . LYS A 1 175 ? -16.692 -7.560  8.532   1.00 39.08  ? 218 LYS A CB  1 
ATOM   1458 C CG  . LYS A 1 175 ? -16.228 -8.901  9.068   1.00 41.32  ? 218 LYS A CG  1 
ATOM   1459 C CD  . LYS A 1 175 ? -17.225 -9.473  10.067  1.00 50.16  ? 218 LYS A CD  1 
ATOM   1460 C CE  . LYS A 1 175 ? -17.225 -8.696  11.376  1.00 58.04  ? 218 LYS A CE  1 
ATOM   1461 N NZ  . LYS A 1 175 ? -18.208 -9.248  12.350  1.00 67.73  ? 218 LYS A NZ  1 
ATOM   1462 N N   . ASP A 1 176 ? -15.990 -4.557  7.437   1.00 37.90  ? 219 ASP A N   1 
ATOM   1463 C CA  . ASP A 1 176 ? -16.541 -3.251  7.083   1.00 40.27  ? 219 ASP A CA  1 
ATOM   1464 C C   . ASP A 1 176 ? -15.760 -2.643  5.917   1.00 38.80  ? 219 ASP A C   1 
ATOM   1465 O O   . ASP A 1 176 ? -15.161 -1.572  6.012   1.00 40.78  ? 219 ASP A O   1 
ATOM   1466 C CB  . ASP A 1 176 ? -16.520 -2.333  8.300   1.00 45.96  ? 219 ASP A CB  1 
ATOM   1467 C CG  . ASP A 1 176 ? -17.369 -1.093  8.113   1.00 56.90  ? 219 ASP A CG  1 
ATOM   1468 O OD1 . ASP A 1 176 ? -18.198 -1.076  7.179   1.00 53.65  ? 219 ASP A OD1 1 
ATOM   1469 O OD2 . ASP A 1 176 ? -17.208 -0.133  8.898   1.00 65.07  ? 219 ASP A OD2 1 
ATOM   1470 N N   . SER A 1 177 ? -15.770 -3.362  4.798   1.00 31.39  ? 220 SER A N   1 
ATOM   1471 C CA  . SER A 1 177 ? -15.081 -2.914  3.599   1.00 31.46  ? 220 SER A CA  1 
ATOM   1472 C C   . SER A 1 177 ? -15.805 -3.477  2.387   1.00 32.42  ? 220 SER A C   1 
ATOM   1473 O O   . SER A 1 177 ? -16.654 -4.365  2.500   1.00 31.75  ? 220 SER A O   1 
ATOM   1474 C CB  . SER A 1 177 ? -13.609 -3.342  3.598   1.00 32.42  ? 220 SER A CB  1 
ATOM   1475 O OG  . SER A 1 177 ? -13.477 -4.742  3.423   1.00 29.94  ? 220 SER A OG  1 
ATOM   1476 N N   . THR A 1 178 ? -15.459 -2.947  1.213   1.00 30.98  ? 221 THR A N   1 
ATOM   1477 C CA  . THR A 1 178 ? -16.066 -3.448  -0.014  1.00 31.13  ? 221 THR A CA  1 
ATOM   1478 C C   . THR A 1 178 ? -15.762 -4.930  -0.197  1.00 30.68  ? 221 THR A C   1 
ATOM   1479 O O   . THR A 1 178 ? -16.649 -5.718  -0.547  1.00 24.43  ? 221 THR A O   1 
ATOM   1480 C CB  . THR A 1 178 ? -15.567 -2.646  -1.216  1.00 31.06  ? 221 THR A CB  1 
ATOM   1481 O OG1 . THR A 1 178 ? -15.498 -1.258  -0.873  1.00 36.64  ? 221 THR A OG1 1 
ATOM   1482 C CG2 . THR A 1 178 ? -16.506 -2.820  -2.401  1.00 32.60  ? 221 THR A CG2 1 
ATOM   1483 N N   . PHE A 1 179 ? -14.515 -5.333  0.054   1.00 27.05  ? 222 PHE A N   1 
ATOM   1484 C CA  . PHE A 1 179 ? -14.165 -6.744  -0.055  1.00 27.92  ? 222 PHE A CA  1 
ATOM   1485 C C   . PHE A 1 179 ? -14.953 -7.579  0.947   1.00 28.90  ? 222 PHE A C   1 
ATOM   1486 O O   . PHE A 1 179 ? -15.581 -8.580  0.582   1.00 24.73  ? 222 PHE A O   1 
ATOM   1487 C CB  . PHE A 1 179 ? -12.662 -6.932  0.155   1.00 26.11  ? 222 PHE A CB  1 
ATOM   1488 C CG  . PHE A 1 179 ? -12.238 -8.373  0.222   1.00 26.33  ? 222 PHE A CG  1 
ATOM   1489 C CD1 . PHE A 1 179 ? -12.255 -9.168  -0.914  1.00 26.74  ? 222 PHE A CD1 1 
ATOM   1490 C CD2 . PHE A 1 179 ? -11.829 -8.934  1.419   1.00 26.08  ? 222 PHE A CD2 1 
ATOM   1491 C CE1 . PHE A 1 179 ? -11.874 -10.496 -0.858  1.00 27.76  ? 222 PHE A CE1 1 
ATOM   1492 C CE2 . PHE A 1 179 ? -11.443 -10.260 1.484   1.00 29.05  ? 222 PHE A CE2 1 
ATOM   1493 C CZ  . PHE A 1 179 ? -11.466 -11.043 0.342   1.00 30.63  ? 222 PHE A CZ  1 
ATOM   1494 N N   . GLY A 1 180 ? -14.958 -7.160  2.214   1.00 27.81  ? 223 GLY A N   1 
ATOM   1495 C CA  . GLY A 1 180 ? -15.546 -7.983  3.257   1.00 25.77  ? 223 GLY A CA  1 
ATOM   1496 C C   . GLY A 1 180 ? -17.058 -8.068  3.199   1.00 26.53  ? 223 GLY A C   1 
ATOM   1497 O O   . GLY A 1 180 ? -17.640 -9.063  3.642   1.00 31.58  ? 223 GLY A O   1 
ATOM   1498 N N   . SER A 1 181 ? -17.717 -7.044  2.653   1.00 26.26  ? 224 SER A N   1 
ATOM   1499 C CA  . SER A 1 181 ? -19.171 -6.968  2.667   1.00 28.21  ? 224 SER A CA  1 
ATOM   1500 C C   . SER A 1 181 ? -19.817 -7.059  1.289   1.00 29.50  ? 224 SER A C   1 
ATOM   1501 O O   . SER A 1 181 ? -21.046 -7.173  1.215   1.00 26.90  ? 224 SER A O   1 
ATOM   1502 C CB  . SER A 1 181 ? -19.630 -5.665  3.342   1.00 30.12  ? 224 SER A CB  1 
ATOM   1503 O OG  . SER A 1 181 ? -19.466 -5.730  4.750   1.00 34.24  ? 224 SER A OG  1 
ATOM   1504 N N   . VAL A 1 182 ? -19.043 -7.003  0.204   1.00 28.34  ? 225 VAL A N   1 
ATOM   1505 C CA  . VAL A 1 182 ? -19.612 -7.140  -1.134  1.00 27.41  ? 225 VAL A CA  1 
ATOM   1506 C C   . VAL A 1 182 ? -18.923 -8.266  -1.897  1.00 25.15  ? 225 VAL A C   1 
ATOM   1507 O O   . VAL A 1 182 ? -19.565 -9.245  -2.290  1.00 27.05  ? 225 VAL A O   1 
ATOM   1508 C CB  . VAL A 1 182 ? -19.520 -5.818  -1.921  1.00 26.10  ? 225 VAL A CB  1 
ATOM   1509 C CG1 . VAL A 1 182 ? -20.110 -5.989  -3.323  1.00 27.39  ? 225 VAL A CG1 1 
ATOM   1510 C CG2 . VAL A 1 182 ? -20.233 -4.703  -1.173  1.00 27.14  ? 225 VAL A CG2 1 
ATOM   1511 N N   . GLU A 1 183 ? -17.611 -8.140  -2.105  1.00 24.97  ? 226 GLU A N   1 
ATOM   1512 C CA  . GLU A 1 183 ? -16.924 -9.016  -3.050  1.00 25.84  ? 226 GLU A CA  1 
ATOM   1513 C C   . GLU A 1 183 ? -16.898 -10.464 -2.566  1.00 25.97  ? 226 GLU A C   1 
ATOM   1514 O O   . GLU A 1 183 ? -17.232 -11.384 -3.323  1.00 25.58  ? 226 GLU A O   1 
ATOM   1515 C CB  . GLU A 1 183 ? -15.504 -8.502  -3.293  1.00 23.33  ? 226 GLU A CB  1 
ATOM   1516 C CG  . GLU A 1 183 ? -15.451 -7.081  -3.851  1.00 28.62  ? 226 GLU A CG  1 
ATOM   1517 C CD  . GLU A 1 183 ? -14.053 -6.498  -3.850  1.00 30.08  ? 226 GLU A CD  1 
ATOM   1518 O OE1 . GLU A 1 183 ? -13.132 -7.142  -3.300  1.00 28.24  ? 226 GLU A OE1 1 
ATOM   1519 O OE2 . GLU A 1 183 ? -13.878 -5.393  -4.401  1.00 30.81  ? 226 GLU A OE2 1 
ATOM   1520 N N   . VAL A 1 184 ? -16.508 -10.688 -1.307  1.00 24.19  ? 227 VAL A N   1 
ATOM   1521 C CA  . VAL A 1 184 ? -16.291 -12.055 -0.834  1.00 26.24  ? 227 VAL A CA  1 
ATOM   1522 C C   . VAL A 1 184 ? -17.580 -12.865 -0.885  1.00 25.97  ? 227 VAL A C   1 
ATOM   1523 O O   . VAL A 1 184 ? -17.547 -14.093 -1.034  1.00 26.06  ? 227 VAL A O   1 
ATOM   1524 C CB  . VAL A 1 184 ? -15.696 -12.046 0.591   1.00 25.83  ? 227 VAL A CB  1 
ATOM   1525 C CG1 . VAL A 1 184 ? -16.715 -11.529 1.600   1.00 29.41  ? 227 VAL A CG1 1 
ATOM   1526 C CG2 . VAL A 1 184 ? -15.216 -13.438 0.980   1.00 26.53  ? 227 VAL A CG2 1 
ATOM   1527 N N   . HIS A 1 185 ? -18.726 -12.204 -0.760  1.00 27.05  ? 228 HIS A N   1 
ATOM   1528 C CA  . HIS A 1 185 ? -20.013 -12.883 -0.729  1.00 29.76  ? 228 HIS A CA  1 
ATOM   1529 C C   . HIS A 1 185 ? -20.662 -13.012 -2.101  1.00 29.09  ? 228 HIS A C   1 
ATOM   1530 O O   . HIS A 1 185 ? -21.752 -13.585 -2.199  1.00 28.58  ? 228 HIS A O   1 
ATOM   1531 C CB  . HIS A 1 185 ? -20.965 -12.143 0.212   1.00 28.69  ? 228 HIS A CB  1 
ATOM   1532 C CG  . HIS A 1 185 ? -20.396 -11.911 1.574   1.00 29.61  ? 228 HIS A CG  1 
ATOM   1533 N ND1 . HIS A 1 185 ? -20.253 -12.920 2.501   1.00 30.42  ? 228 HIS A ND1 1 
ATOM   1534 C CD2 . HIS A 1 185 ? -19.928 -10.787 2.165   1.00 29.97  ? 228 HIS A CD2 1 
ATOM   1535 C CE1 . HIS A 1 185 ? -19.724 -12.428 3.606   1.00 30.58  ? 228 HIS A CE1 1 
ATOM   1536 N NE2 . HIS A 1 185 ? -19.517 -11.135 3.429   1.00 33.71  ? 228 HIS A NE2 1 
ATOM   1537 N N   . ASN A 1 186 ? -20.031 -12.499 -3.158  1.00 27.00  ? 229 ASN A N   1 
ATOM   1538 C CA  . ASN A 1 186 ? -20.597 -12.575 -4.499  1.00 28.50  ? 229 ASN A CA  1 
ATOM   1539 C C   . ASN A 1 186 ? -19.675 -13.267 -5.494  1.00 27.73  ? 229 ASN A C   1 
ATOM   1540 O O   . ASN A 1 186 ? -19.994 -13.310 -6.688  1.00 28.37  ? 229 ASN A O   1 
ATOM   1541 C CB  . ASN A 1 186 ? -20.968 -11.175 -4.992  1.00 29.58  ? 229 ASN A CB  1 
ATOM   1542 C CG  . ASN A 1 186 ? -22.197 -10.632 -4.296  1.00 30.82  ? 229 ASN A CG  1 
ATOM   1543 O OD1 . ASN A 1 186 ? -23.322 -11.022 -4.609  1.00 29.57  ? 229 ASN A OD1 1 
ATOM   1544 N ND2 . ASN A 1 186 ? -21.989 -9.738  -3.335  1.00 29.64  ? 229 ASN A ND2 1 
ATOM   1545 N N   . LEU A 1 187 ? -18.546 -13.806 -5.041  1.00 26.07  ? 230 LEU A N   1 
ATOM   1546 C CA  . LEU A 1 187 ? -17.831 -14.797 -5.832  1.00 28.70  ? 230 LEU A CA  1 
ATOM   1547 C C   . LEU A 1 187 ? -18.708 -16.035 -5.984  1.00 28.17  ? 230 LEU A C   1 
ATOM   1548 O O   . LEU A 1 187 ? -19.214 -16.573 -4.995  1.00 30.06  ? 230 LEU A O   1 
ATOM   1549 C CB  . LEU A 1 187 ? -16.509 -15.166 -5.160  1.00 28.79  ? 230 LEU A CB  1 
ATOM   1550 C CG  . LEU A 1 187 ? -15.516 -14.028 -4.919  1.00 25.28  ? 230 LEU A CG  1 
ATOM   1551 C CD1 . LEU A 1 187 ? -14.389 -14.495 -4.017  1.00 28.66  ? 230 LEU A CD1 1 
ATOM   1552 C CD2 . LEU A 1 187 ? -14.963 -13.503 -6.238  1.00 24.41  ? 230 LEU A CD2 1 
ATOM   1553 N N   . GLN A 1 188 ? -18.879 -16.492 -7.215  1.00 24.83  ? 231 GLN A N   1 
ATOM   1554 C CA  . GLN A 1 188 ? -19.804 -17.591 -7.477  1.00 31.96  ? 231 GLN A CA  1 
ATOM   1555 C C   . GLN A 1 188 ? -19.113 -18.927 -7.231  1.00 28.88  ? 231 GLN A C   1 
ATOM   1556 O O   . GLN A 1 188 ? -18.120 -19.230 -7.901  1.00 27.83  ? 231 GLN A O   1 
ATOM   1557 C CB  . GLN A 1 188 ? -20.324 -17.517 -8.907  1.00 29.63  ? 231 GLN A CB  1 
ATOM   1558 C CG  . GLN A 1 188 ? -21.149 -16.274 -9.191  1.00 30.13  ? 231 GLN A CG  1 
ATOM   1559 C CD  . GLN A 1 188 ? -21.963 -16.400 -10.462 1.00 33.33  ? 231 GLN A CD  1 
ATOM   1560 O OE1 . GLN A 1 188 ? -22.778 -17.312 -10.598 1.00 36.17  ? 231 GLN A OE1 1 
ATOM   1561 N NE2 . GLN A 1 188 ? -21.740 -15.491 -11.403 1.00 31.73  ? 231 GLN A NE2 1 
ATOM   1562 N N   . PRO A 1 189 ? -19.592 -19.746 -6.289  1.00 31.31  ? 232 PRO A N   1 
ATOM   1563 C CA  . PRO A 1 189 ? -18.932 -21.043 -6.054  1.00 33.53  ? 232 PRO A CA  1 
ATOM   1564 C C   . PRO A 1 189 ? -18.907 -21.936 -7.281  1.00 36.54  ? 232 PRO A C   1 
ATOM   1565 O O   . PRO A 1 189 ? -18.016 -22.786 -7.402  1.00 34.75  ? 232 PRO A O   1 
ATOM   1566 C CB  . PRO A 1 189 ? -19.765 -21.663 -4.922  1.00 32.50  ? 232 PRO A CB  1 
ATOM   1567 C CG  . PRO A 1 189 ? -20.439 -20.513 -4.259  1.00 34.28  ? 232 PRO A CG  1 
ATOM   1568 C CD  . PRO A 1 189 ? -20.693 -19.506 -5.339  1.00 31.55  ? 232 PRO A CD  1 
ATOM   1569 N N   . GLU A 1 190 ? -19.865 -21.778 -8.195  1.00 36.53  ? 233 GLU A N   1 
ATOM   1570 C CA  . GLU A 1 190 ? -19.870 -22.588 -9.407  1.00 47.17  ? 233 GLU A CA  1 
ATOM   1571 C C   . GLU A 1 190 ? -18.689 -22.271 -10.317 1.00 45.82  ? 233 GLU A C   1 
ATOM   1572 O O   . GLU A 1 190 ? -18.308 -23.119 -11.132 1.00 48.62  ? 233 GLU A O   1 
ATOM   1573 C CB  . GLU A 1 190 ? -21.179 -22.386 -10.177 1.00 53.19  ? 233 GLU A CB  1 
ATOM   1574 C CG  . GLU A 1 190 ? -22.420 -22.933 -9.477  1.00 61.30  ? 233 GLU A CG  1 
ATOM   1575 C CD  . GLU A 1 190 ? -22.837 -22.104 -8.273  1.00 65.43  ? 233 GLU A CD  1 
ATOM   1576 O OE1 . GLU A 1 190 ? -22.506 -20.899 -8.230  1.00 50.09  ? 233 GLU A OE1 1 
ATOM   1577 O OE2 . GLU A 1 190 ? -23.493 -22.660 -7.365  1.00 67.61  ? 233 GLU A OE2 1 
ATOM   1578 N N   . LYS A 1 191 ? -18.103 -21.080 -10.194 1.00 34.43  ? 234 LYS A N   1 
ATOM   1579 C CA  . LYS A 1 191 ? -17.031 -20.624 -11.072 1.00 32.43  ? 234 LYS A CA  1 
ATOM   1580 C C   . LYS A 1 191 ? -15.688 -20.499 -10.375 1.00 30.27  ? 234 LYS A C   1 
ATOM   1581 O O   . LYS A 1 191 ? -14.653 -20.757 -10.992 1.00 28.56  ? 234 LYS A O   1 
ATOM   1582 C CB  . LYS A 1 191 ? -17.390 -19.261 -11.677 1.00 33.14  ? 234 LYS A CB  1 
ATOM   1583 C CG  . LYS A 1 191 ? -18.756 -19.201 -12.332 1.00 37.88  ? 234 LYS A CG  1 
ATOM   1584 C CD  . LYS A 1 191 ? -19.151 -17.769 -12.659 1.00 36.72  ? 234 LYS A CD  1 
ATOM   1585 C CE  . LYS A 1 191 ? -18.193 -17.128 -13.648 1.00 38.12  ? 234 LYS A CE  1 
ATOM   1586 N NZ  . LYS A 1 191 ? -18.694 -15.808 -14.126 1.00 34.84  ? 234 LYS A NZ  1 
ATOM   1587 N N   . VAL A 1 192 ? -15.678 -20.089 -9.111  1.00 31.66  ? 235 VAL A N   1 
ATOM   1588 C CA  . VAL A 1 192 ? -14.450 -19.835 -8.368  1.00 32.10  ? 235 VAL A CA  1 
ATOM   1589 C C   . VAL A 1 192 ? -14.125 -21.066 -7.538  1.00 30.36  ? 235 VAL A C   1 
ATOM   1590 O O   . VAL A 1 192 ? -14.966 -21.542 -6.765  1.00 30.94  ? 235 VAL A O   1 
ATOM   1591 C CB  . VAL A 1 192 ? -14.588 -18.593 -7.472  1.00 30.18  ? 235 VAL A CB  1 
ATOM   1592 C CG1 . VAL A 1 192 ? -13.288 -18.326 -6.724  1.00 25.16  ? 235 VAL A CG1 1 
ATOM   1593 C CG2 . VAL A 1 192 ? -15.000 -17.383 -8.299  1.00 29.60  ? 235 VAL A CG2 1 
ATOM   1594 N N   . GLN A 1 193 ? -12.908 -21.585 -7.702  1.00 30.38  ? 236 GLN A N   1 
ATOM   1595 C CA  . GLN A 1 193 ? -12.438 -22.698 -6.888  1.00 35.43  ? 236 GLN A CA  1 
ATOM   1596 C C   . GLN A 1 193 ? -11.731 -22.233 -5.620  1.00 33.04  ? 236 GLN A C   1 
ATOM   1597 O O   . GLN A 1 193 ? -11.907 -22.840 -4.558  1.00 30.26  ? 236 GLN A O   1 
ATOM   1598 C CB  . GLN A 1 193 ? -11.488 -23.588 -7.695  1.00 37.21  ? 236 GLN A CB  1 
ATOM   1599 C CG  . GLN A 1 193 ? -12.175 -24.699 -8.474  1.00 47.62  ? 236 GLN A CG  1 
ATOM   1600 C CD  . GLN A 1 193 ? -13.042 -24.175 -9.601  1.00 52.90  ? 236 GLN A CD  1 
ATOM   1601 O OE1 . GLN A 1 193 ? -14.262 -24.340 -9.590  1.00 54.13  ? 236 GLN A OE1 1 
ATOM   1602 N NE2 . GLN A 1 193 ? -12.412 -23.546 -10.589 1.00 49.98  ? 236 GLN A NE2 1 
ATOM   1603 N N   . THR A 1 194 ? -10.933 -21.169 -5.705  1.00 30.06  ? 237 THR A N   1 
ATOM   1604 C CA  . THR A 1 194 ? -10.081 -20.767 -4.597  1.00 28.14  ? 237 THR A CA  1 
ATOM   1605 C C   . THR A 1 194 ? -9.984  -19.253 -4.515  1.00 28.91  ? 237 THR A C   1 
ATOM   1606 O O   . THR A 1 194 ? -9.919  -18.566 -5.539  1.00 26.22  ? 237 THR A O   1 
ATOM   1607 C CB  . THR A 1 194 ? -8.669  -21.357 -4.740  1.00 29.26  ? 237 THR A CB  1 
ATOM   1608 O OG1 . THR A 1 194 ? -8.754  -22.781 -4.871  1.00 35.15  ? 237 THR A OG1 1 
ATOM   1609 C CG2 . THR A 1 194 ? -7.809  -21.011 -3.524  1.00 28.48  ? 237 THR A CG2 1 
ATOM   1610 N N   . LEU A 1 195 ? -9.976  -18.746 -3.285  1.00 28.79  ? 238 LEU A N   1 
ATOM   1611 C CA  . LEU A 1 195 ? -9.646  -17.360 -2.985  1.00 25.99  ? 238 LEU A CA  1 
ATOM   1612 C C   . LEU A 1 195 ? -8.269  -17.360 -2.333  1.00 27.62  ? 238 LEU A C   1 
ATOM   1613 O O   . LEU A 1 195 ? -8.094  -17.927 -1.249  1.00 27.03  ? 238 LEU A O   1 
ATOM   1614 C CB  . LEU A 1 195 ? -10.695 -16.728 -2.068  1.00 29.25  ? 238 LEU A CB  1 
ATOM   1615 C CG  . LEU A 1 195 ? -10.357 -15.339 -1.519  1.00 27.31  ? 238 LEU A CG  1 
ATOM   1616 C CD1 . LEU A 1 195 ? -10.462 -14.289 -2.617  1.00 28.10  ? 238 LEU A CD1 1 
ATOM   1617 C CD2 . LEU A 1 195 ? -11.250 -14.985 -0.337  1.00 31.78  ? 238 LEU A CD2 1 
ATOM   1618 N N   . GLU A 1 196 ? -7.296  -16.740 -2.993  1.00 25.84  ? 239 GLU A N   1 
ATOM   1619 C CA  . GLU A 1 196 ? -5.929  -16.665 -2.493  1.00 26.86  ? 239 GLU A CA  1 
ATOM   1620 C C   . GLU A 1 196 ? -5.661  -15.253 -1.991  1.00 28.54  ? 239 GLU A C   1 
ATOM   1621 O O   . GLU A 1 196 ? -5.688  -14.295 -2.771  1.00 25.51  ? 239 GLU A O   1 
ATOM   1622 C CB  . GLU A 1 196 ? -4.926  -17.053 -3.578  1.00 30.31  ? 239 GLU A CB  1 
ATOM   1623 C CG  . GLU A 1 196 ? -3.471  -16.948 -3.139  1.00 34.57  ? 239 GLU A CG  1 
ATOM   1624 C CD  . GLU A 1 196 ? -2.518  -17.601 -4.120  1.00 40.01  ? 239 GLU A CD  1 
ATOM   1625 O OE1 . GLU A 1 196 ? -2.887  -18.643 -4.703  1.00 42.85  ? 239 GLU A OE1 1 
ATOM   1626 O OE2 . GLU A 1 196 ? -1.403  -17.072 -4.314  1.00 39.48  ? 239 GLU A OE2 1 
ATOM   1627 N N   . ALA A 1 197 ? -5.394  -15.130 -0.694  1.00 25.16  ? 240 ALA A N   1 
ATOM   1628 C CA  . ALA A 1 197 ? -5.117  -13.841 -0.078  1.00 27.15  ? 240 ALA A CA  1 
ATOM   1629 C C   . ALA A 1 197 ? -3.618  -13.578 -0.042  1.00 27.27  ? 240 ALA A C   1 
ATOM   1630 O O   . ALA A 1 197 ? -2.829  -14.460 0.319   1.00 27.51  ? 240 ALA A O   1 
ATOM   1631 C CB  . ALA A 1 197 ? -5.688  -13.785 1.337   1.00 28.24  ? 240 ALA A CB  1 
ATOM   1632 N N   . TRP A 1 198 ? -3.234  -12.366 -0.422  1.00 24.92  ? 241 TRP A N   1 
ATOM   1633 C CA  . TRP A 1 198 ? -1.855  -11.893 -0.350  1.00 27.35  ? 241 TRP A CA  1 
ATOM   1634 C C   . TRP A 1 198 ? -1.795  -10.829 0.742   1.00 27.45  ? 241 TRP A C   1 
ATOM   1635 O O   . TRP A 1 198 ? -2.247  -9.699  0.540   1.00 24.23  ? 241 TRP A O   1 
ATOM   1636 C CB  . TRP A 1 198 ? -1.397  -11.318 -1.688  1.00 29.81  ? 241 TRP A CB  1 
ATOM   1637 C CG  . TRP A 1 198 ? -1.266  -12.320 -2.795  1.00 31.53  ? 241 TRP A CG  1 
ATOM   1638 C CD1 . TRP A 1 198 ? -1.313  -13.679 -2.686  1.00 34.10  ? 241 TRP A CD1 1 
ATOM   1639 C CD2 . TRP A 1 198 ? -1.063  -12.035 -4.185  1.00 30.32  ? 241 TRP A CD2 1 
ATOM   1640 N NE1 . TRP A 1 198 ? -1.151  -14.258 -3.922  1.00 34.18  ? 241 TRP A NE1 1 
ATOM   1641 C CE2 . TRP A 1 198 ? -0.995  -13.270 -4.859  1.00 32.14  ? 241 TRP A CE2 1 
ATOM   1642 C CE3 . TRP A 1 198 ? -0.931  -10.854 -4.925  1.00 34.59  ? 241 TRP A CE3 1 
ATOM   1643 C CZ2 . TRP A 1 198 ? -0.802  -13.360 -6.237  1.00 32.70  ? 241 TRP A CZ2 1 
ATOM   1644 C CZ3 . TRP A 1 198 ? -0.741  -10.946 -6.296  1.00 32.49  ? 241 TRP A CZ3 1 
ATOM   1645 C CH2 . TRP A 1 198 ? -0.679  -12.190 -6.936  1.00 31.80  ? 241 TRP A CH2 1 
ATOM   1646 N N   . VAL A 1 199 ? -1.235  -11.186 1.895   1.00 27.88  ? 242 VAL A N   1 
ATOM   1647 C CA  . VAL A 1 199 ? -1.150  -10.266 3.024   1.00 26.56  ? 242 VAL A CA  1 
ATOM   1648 C C   . VAL A 1 199 ? 0.123   -9.444  2.863   1.00 30.44  ? 242 VAL A C   1 
ATOM   1649 O O   . VAL A 1 199 ? 1.234   -9.959  3.024   1.00 27.88  ? 242 VAL A O   1 
ATOM   1650 C CB  . VAL A 1 199 ? -1.173  -11.010 4.363   1.00 28.97  ? 242 VAL A CB  1 
ATOM   1651 C CG1 . VAL A 1 199 ? -1.090  -10.020 5.519   1.00 29.74  ? 242 VAL A CG1 1 
ATOM   1652 C CG2 . VAL A 1 199 ? -2.430  -11.853 4.470   1.00 29.73  ? 242 VAL A CG2 1 
ATOM   1653 N N   . ILE A 1 200 ? -0.041  -8.162  2.553   1.00 27.78  ? 243 ILE A N   1 
ATOM   1654 C CA  . ILE A 1 200 ? 1.089   -7.284  2.271   1.00 27.96  ? 243 ILE A CA  1 
ATOM   1655 C C   . ILE A 1 200 ? 1.655   -6.776  3.589   1.00 31.24  ? 243 ILE A C   1 
ATOM   1656 O O   . ILE A 1 200 ? 0.960   -6.103  4.359   1.00 30.49  ? 243 ILE A O   1 
ATOM   1657 C CB  . ILE A 1 200 ? 0.670   -6.119  1.365   1.00 31.29  ? 243 ILE A CB  1 
ATOM   1658 C CG1 . ILE A 1 200 ? -0.079  -6.643  0.134   1.00 30.39  ? 243 ILE A CG1 1 
ATOM   1659 C CG2 . ILE A 1 200 ? 1.888   -5.303  0.953   1.00 32.90  ? 243 ILE A CG2 1 
ATOM   1660 C CD1 . ILE A 1 200 ? 0.690   -7.681  -0.665  1.00 30.50  ? 243 ILE A CD1 1 
ATOM   1661 N N   . HIS A 1 201 ? 2.919   -7.089  3.848   1.00 32.08  ? 244 HIS A N   1 
ATOM   1662 C CA  . HIS A 1 201 ? 3.556   -6.681  5.088   1.00 35.45  ? 244 HIS A CA  1 
ATOM   1663 C C   . HIS A 1 201 ? 4.001   -5.228  5.017   1.00 37.09  ? 244 HIS A C   1 
ATOM   1664 O O   . HIS A 1 201 ? 4.283   -4.688  3.943   1.00 34.85  ? 244 HIS A O   1 
ATOM   1665 C CB  . HIS A 1 201 ? 4.752   -7.577  5.398   1.00 33.71  ? 244 HIS A CB  1 
ATOM   1666 C CG  . HIS A 1 201 ? 4.371   -8.900  5.981   1.00 34.45  ? 244 HIS A CG  1 
ATOM   1667 N ND1 . HIS A 1 201 ? 4.762   -9.297  7.242   1.00 32.70  ? 244 HIS A ND1 1 
ATOM   1668 C CD2 . HIS A 1 201 ? 3.618   -9.910  5.484   1.00 32.49  ? 244 HIS A CD2 1 
ATOM   1669 C CE1 . HIS A 1 201 ? 4.273   -10.499 7.493   1.00 33.51  ? 244 HIS A CE1 1 
ATOM   1670 N NE2 . HIS A 1 201 ? 3.576   -10.893 6.442   1.00 36.18  ? 244 HIS A NE2 1 
ATOM   1671 N N   . GLY A 1 202 ? 4.059   -4.598  6.184   1.00 43.83  ? 245 GLY A N   1 
ATOM   1672 C CA  . GLY A 1 202 ? 4.499   -3.225  6.301   1.00 49.07  ? 245 GLY A CA  1 
ATOM   1673 C C   . GLY A 1 202 ? 4.446   -2.770  7.742   1.00 56.20  ? 245 GLY A C   1 
ATOM   1674 O O   . GLY A 1 202 ? 4.702   -3.559  8.656   1.00 62.95  ? 245 GLY A O   1 
ATOM   1675 N N   . GLY A 1 203 ? 4.110   -1.504  7.960   1.00 58.92  ? 246 GLY A N   1 
ATOM   1676 C CA  . GLY A 1 203 ? 3.993   -0.982  9.305   1.00 65.29  ? 246 GLY A CA  1 
ATOM   1677 C C   . GLY A 1 203 ? 5.234   -1.201  10.144  1.00 67.78  ? 246 GLY A C   1 
ATOM   1678 O O   . GLY A 1 203 ? 6.319   -1.463  9.616   1.00 62.52  ? 246 GLY A O   1 
ATOM   1679 N N   . ARG A 1 204 ? 5.078   -1.115  11.461  1.00 71.52  ? 247 ARG A N   1 
ATOM   1680 C CA  . ARG A 1 204 ? 6.189   -1.158  12.403  1.00 71.77  ? 247 ARG A CA  1 
ATOM   1681 C C   . ARG A 1 204 ? 6.124   -2.404  13.283  1.00 68.20  ? 247 ARG A C   1 
ATOM   1682 O O   . ARG A 1 204 ? 6.355   -2.343  14.492  1.00 68.52  ? 247 ARG A O   1 
ATOM   1683 C CB  . ARG A 1 204 ? 6.202   0.105   13.261  1.00 77.08  ? 247 ARG A CB  1 
ATOM   1684 C CG  . ARG A 1 204 ? 4.876   0.383   13.955  1.00 83.07  ? 247 ARG A CG  1 
ATOM   1685 C CD  . ARG A 1 204 ? 5.054   0.604   15.445  1.00 82.31  ? 247 ARG A CD  1 
ATOM   1686 N NE  . ARG A 1 204 ? 3.795   0.450   16.165  1.00 87.42  ? 247 ARG A NE  1 
ATOM   1687 C CZ  . ARG A 1 204 ? 3.261   -0.718  16.497  1.00 91.89  ? 247 ARG A CZ  1 
ATOM   1688 N NH1 . ARG A 1 204 ? 3.844   -1.862  16.176  1.00 88.10  ? 247 ARG A NH1 1 
ATOM   1689 N NH2 . ARG A 1 204 ? 2.112   -0.740  17.166  1.00 96.86  ? 247 ARG A NH2 1 
ATOM   1690 N N   . GLU A 1 205 ? 5.808   -3.548  12.683  1.00 65.61  ? 248 GLU A N   1 
ATOM   1691 C CA  . GLU A 1 205 ? 5.697   -4.812  13.396  1.00 63.20  ? 248 GLU A CA  1 
ATOM   1692 C C   . GLU A 1 205 ? 6.793   -5.767  12.942  1.00 52.60  ? 248 GLU A C   1 
ATOM   1693 O O   . GLU A 1 205 ? 7.156   -5.794  11.762  1.00 47.72  ? 248 GLU A O   1 
ATOM   1694 C CB  . GLU A 1 205 ? 4.324   -5.451  13.170  1.00 65.04  ? 248 GLU A CB  1 
ATOM   1695 C CG  . GLU A 1 205 ? 3.197   -4.762  13.924  1.00 73.10  ? 248 GLU A CG  1 
ATOM   1696 C CD  . GLU A 1 205 ? 1.914   -5.571  13.925  1.00 79.30  ? 248 GLU A CD  1 
ATOM   1697 O OE1 . GLU A 1 205 ? 1.602   -6.201  12.892  1.00 74.29  ? 248 GLU A OE1 1 
ATOM   1698 O OE2 . GLU A 1 205 ? 1.222   -5.586  14.965  1.00 80.67  ? 248 GLU A OE2 1 
ATOM   1699 N N   . ASP A 1 206 ? 7.319   -6.543  13.889  1.00 46.69  ? 249 ASP A N   1 
ATOM   1700 C CA  . ASP A 1 206 ? 8.357   -7.518  13.580  1.00 44.52  ? 249 ASP A CA  1 
ATOM   1701 C C   . ASP A 1 206 ? 7.786   -8.652  12.734  1.00 41.43  ? 249 ASP A C   1 
ATOM   1702 O O   . ASP A 1 206 ? 6.625   -9.041  12.880  1.00 43.28  ? 249 ASP A O   1 
ATOM   1703 C CB  . ASP A 1 206 ? 8.971   -8.068  14.869  1.00 39.37  ? 249 ASP A CB  1 
ATOM   1704 C CG  . ASP A 1 206 ? 9.761   -7.019  15.631  1.00 42.69  ? 249 ASP A CG  1 
ATOM   1705 O OD1 . ASP A 1 206 ? 10.332  -6.116  14.981  1.00 41.60  ? 249 ASP A OD1 1 
ATOM   1706 O OD2 . ASP A 1 206 ? 9.809   -7.094  16.878  1.00 38.59  ? 249 ASP A OD2 1 
ATOM   1707 N N   . SER A 1 207 ? 8.621   -9.175  11.835  1.00 42.08  ? 250 SER A N   1 
ATOM   1708 C CA  . SER A 1 207 ? 8.157   -10.139 10.843  1.00 43.14  ? 250 SER A CA  1 
ATOM   1709 C C   . SER A 1 207 ? 7.563   -11.371 11.514  1.00 40.25  ? 250 SER A C   1 
ATOM   1710 O O   . SER A 1 207 ? 8.189   -11.994 12.377  1.00 41.30  ? 250 SER A O   1 
ATOM   1711 C CB  . SER A 1 207 ? 9.316   -10.541 9.928   1.00 43.53  ? 250 SER A CB  1 
ATOM   1712 O OG  . SER A 1 207 ? 8.865   -11.332 8.841   1.00 41.50  ? 250 SER A OG  1 
ATOM   1713 N N   . ARG A 1 208 ? 6.350   -11.726 11.102  1.00 37.81  ? 251 ARG A N   1 
ATOM   1714 C CA  . ARG A 1 208 ? 5.670   -12.908 11.610  1.00 36.17  ? 251 ARG A CA  1 
ATOM   1715 C C   . ARG A 1 208 ? 4.672   -13.357 10.554  1.00 35.30  ? 251 ARG A C   1 
ATOM   1716 O O   . ARG A 1 208 ? 4.325   -12.597 9.646   1.00 33.10  ? 251 ARG A O   1 
ATOM   1717 C CB  . ARG A 1 208 ? 4.976   -12.630 12.949  1.00 38.16  ? 251 ARG A CB  1 
ATOM   1718 C CG  . ARG A 1 208 ? 3.623   -11.928 12.855  1.00 41.19  ? 251 ARG A CG  1 
ATOM   1719 C CD  . ARG A 1 208 ? 3.067   -11.650 14.250  1.00 44.26  ? 251 ARG A CD  1 
ATOM   1720 N NE  . ARG A 1 208 ? 1.706   -11.122 14.241  1.00 53.75  ? 251 ARG A NE  1 
ATOM   1721 C CZ  . ARG A 1 208 ? 1.397   -9.832  14.255  1.00 59.36  ? 251 ARG A CZ  1 
ATOM   1722 N NH1 . ARG A 1 208 ? 2.332   -8.897  14.236  1.00 61.92  ? 251 ARG A NH1 1 
ATOM   1723 N NH2 . ARG A 1 208 ? 0.118   -9.471  14.292  1.00 61.15  ? 251 ARG A NH2 1 
ATOM   1724 N N   . ASP A 1 209 ? 4.215   -14.600 10.679  1.00 30.36  ? 252 ASP A N   1 
ATOM   1725 C CA  . ASP A 1 209 ? 3.247   -15.165 9.740   1.00 33.21  ? 252 ASP A CA  1 
ATOM   1726 C C   . ASP A 1 209 ? 1.878   -14.560 10.022  1.00 34.12  ? 252 ASP A C   1 
ATOM   1727 O O   . ASP A 1 209 ? 1.194   -14.946 10.972  1.00 35.32  ? 252 ASP A O   1 
ATOM   1728 C CB  . ASP A 1 209 ? 3.216   -16.685 9.861   1.00 33.65  ? 252 ASP A CB  1 
ATOM   1729 C CG  . ASP A 1 209 ? 2.237   -17.331 8.894   1.00 37.09  ? 252 ASP A CG  1 
ATOM   1730 O OD1 . ASP A 1 209 ? 1.649   -16.611 8.057   1.00 35.52  ? 252 ASP A OD1 1 
ATOM   1731 O OD2 . ASP A 1 209 ? 2.054   -18.564 8.974   1.00 39.18  ? 252 ASP A OD2 1 
ATOM   1732 N N   . LEU A 1 210 ? 1.467   -13.606 9.188   1.00 32.53  ? 253 LEU A N   1 
ATOM   1733 C CA  . LEU A 1 210 ? 0.199   -12.918 9.390   1.00 37.24  ? 253 LEU A CA  1 
ATOM   1734 C C   . LEU A 1 210 ? -0.998  -13.713 8.885   1.00 31.73  ? 253 LEU A C   1 
ATOM   1735 O O   . LEU A 1 210 ? -2.138  -13.325 9.159   1.00 34.32  ? 253 LEU A O   1 
ATOM   1736 C CB  . LEU A 1 210 ? 0.231   -11.547 8.708   1.00 32.45  ? 253 LEU A CB  1 
ATOM   1737 C CG  . LEU A 1 210 ? 1.207   -10.524 9.297   1.00 34.16  ? 253 LEU A CG  1 
ATOM   1738 C CD1 . LEU A 1 210 ? 1.162   -9.228  8.500   1.00 36.48  ? 253 LEU A CD1 1 
ATOM   1739 C CD2 . LEU A 1 210 ? 0.907   -10.258 10.768  1.00 38.08  ? 253 LEU A CD2 1 
ATOM   1740 N N   . CYS A 1 211 ? -0.778  -14.813 8.167   1.00 35.70  ? 254 CYS A N   1 
ATOM   1741 C CA  . CYS A 1 211 ? -1.895  -15.671 7.793   1.00 39.25  ? 254 CYS A CA  1 
ATOM   1742 C C   . CYS A 1 211 ? -2.499  -16.385 8.997   1.00 39.93  ? 254 CYS A C   1 
ATOM   1743 O O   . CYS A 1 211 ? -3.584  -16.964 8.872   1.00 42.02  ? 254 CYS A O   1 
ATOM   1744 C CB  . CYS A 1 211 ? -1.445  -16.685 6.741   1.00 37.25  ? 254 CYS A CB  1 
ATOM   1745 S SG  . CYS A 1 211 ? -1.041  -15.950 5.135   1.00 37.49  ? 254 CYS A SG  1 
ATOM   1746 N N   . GLN A 1 212 ? -1.834  -16.352 10.150  1.00 39.42  ? 255 GLN A N   1 
ATOM   1747 C CA  . GLN A 1 212 ? -2.389  -16.874 11.391  1.00 39.77  ? 255 GLN A CA  1 
ATOM   1748 C C   . GLN A 1 212 ? -3.177  -15.827 12.168  1.00 38.39  ? 255 GLN A C   1 
ATOM   1749 O O   . GLN A 1 212 ? -3.711  -16.141 13.237  1.00 38.88  ? 255 GLN A O   1 
ATOM   1750 C CB  . GLN A 1 212 ? -1.269  -17.431 12.276  1.00 40.48  ? 255 GLN A CB  1 
ATOM   1751 C CG  . GLN A 1 212 ? -0.451  -18.522 11.613  1.00 44.60  ? 255 GLN A CG  1 
ATOM   1752 C CD  . GLN A 1 212 ? -1.306  -19.678 11.137  1.00 45.93  ? 255 GLN A CD  1 
ATOM   1753 O OE1 . GLN A 1 212 ? -1.257  -20.062 9.968   1.00 48.56  ? 255 GLN A OE1 1 
ATOM   1754 N NE2 . GLN A 1 212 ? -2.101  -20.239 12.043  1.00 46.27  ? 255 GLN A NE2 1 
ATOM   1755 N N   . ASP A 1 213 ? -3.264  -14.601 11.658  1.00 36.10  ? 256 ASP A N   1 
ATOM   1756 C CA  . ASP A 1 213 ? -3.985  -13.548 12.354  1.00 35.08  ? 256 ASP A CA  1 
ATOM   1757 C C   . ASP A 1 213 ? -5.446  -13.956 12.543  1.00 36.29  ? 256 ASP A C   1 
ATOM   1758 O O   . ASP A 1 213 ? -6.024  -14.636 11.690  1.00 35.40  ? 256 ASP A O   1 
ATOM   1759 C CB  . ASP A 1 213 ? -3.896  -12.244 11.565  1.00 36.61  ? 256 ASP A CB  1 
ATOM   1760 C CG  . ASP A 1 213 ? -4.557  -11.083 12.278  1.00 40.00  ? 256 ASP A CG  1 
ATOM   1761 O OD1 . ASP A 1 213 ? -3.885  -10.427 13.103  1.00 43.58  ? 256 ASP A OD1 1 
ATOM   1762 O OD2 . ASP A 1 213 ? -5.751  -10.828 12.015  1.00 37.85  ? 256 ASP A OD2 1 
ATOM   1763 N N   . PRO A 1 214 ? -6.070  -13.566 13.661  1.00 36.36  ? 257 PRO A N   1 
ATOM   1764 C CA  . PRO A 1 214 ? -7.470  -13.973 13.876  1.00 36.12  ? 257 PRO A CA  1 
ATOM   1765 C C   . PRO A 1 214 ? -8.416  -13.533 12.771  1.00 34.13  ? 257 PRO A C   1 
ATOM   1766 O O   . PRO A 1 214 ? -9.343  -14.279 12.434  1.00 32.96  ? 257 PRO A O   1 
ATOM   1767 C CB  . PRO A 1 214 ? -7.820  -13.316 15.219  1.00 36.31  ? 257 PRO A CB  1 
ATOM   1768 C CG  . PRO A 1 214 ? -6.513  -13.151 15.913  1.00 36.09  ? 257 PRO A CG  1 
ATOM   1769 C CD  . PRO A 1 214 ? -5.518  -12.855 14.829  1.00 36.73  ? 257 PRO A CD  1 
ATOM   1770 N N   . THR A 1 215 ? -8.219  -12.342 12.196  1.00 32.99  ? 258 THR A N   1 
ATOM   1771 C CA  . THR A 1 215 ? -9.131  -11.885 11.151  1.00 36.01  ? 258 THR A CA  1 
ATOM   1772 C C   . THR A 1 215 ? -8.978  -12.705 9.875   1.00 33.62  ? 258 THR A C   1 
ATOM   1773 O O   . THR A 1 215 ? -9.929  -12.809 9.092   1.00 33.88  ? 258 THR A O   1 
ATOM   1774 C CB  . THR A 1 215 ? -8.914  -10.400 10.846  1.00 33.99  ? 258 THR A CB  1 
ATOM   1775 O OG1 . THR A 1 215 ? -7.609  -10.200 10.289  1.00 34.41  ? 258 THR A OG1 1 
ATOM   1776 C CG2 . THR A 1 215 ? -9.063  -9.563  12.110  1.00 35.15  ? 258 THR A CG2 1 
ATOM   1777 N N   . ILE A 1 216 ? -7.794  -13.276 9.637   1.00 31.90  ? 259 ILE A N   1 
ATOM   1778 C CA  . ILE A 1 216 ? -7.628  -14.183 8.506   1.00 28.68  ? 259 ILE A CA  1 
ATOM   1779 C C   . ILE A 1 216 ? -8.366  -15.491 8.762   1.00 34.70  ? 259 ILE A C   1 
ATOM   1780 O O   . ILE A 1 216 ? -9.014  -16.041 7.863   1.00 33.82  ? 259 ILE A O   1 
ATOM   1781 C CB  . ILE A 1 216 ? -6.134  -14.422 8.221   1.00 31.98  ? 259 ILE A CB  1 
ATOM   1782 C CG1 . ILE A 1 216 ? -5.442  -13.110 7.843   1.00 30.49  ? 259 ILE A CG1 1 
ATOM   1783 C CG2 . ILE A 1 216 ? -5.959  -15.456 7.117   1.00 32.53  ? 259 ILE A CG2 1 
ATOM   1784 C CD1 . ILE A 1 216 ? -5.990  -12.451 6.583   1.00 31.20  ? 259 ILE A CD1 1 
ATOM   1785 N N   . LYS A 1 217 ? -8.275  -16.017 9.987   1.00 33.27  ? 260 LYS A N   1 
ATOM   1786 C CA  . LYS A 1 217 ? -9.074  -17.186 10.340  1.00 36.50  ? 260 LYS A CA  1 
ATOM   1787 C C   . LYS A 1 217 ? -10.557 -16.884 10.182  1.00 33.06  ? 260 LYS A C   1 
ATOM   1788 O O   . LYS A 1 217 ? -11.331 -17.736 9.732   1.00 33.50  ? 260 LYS A O   1 
ATOM   1789 C CB  . LYS A 1 217 ? -8.765  -17.630 11.771  1.00 39.47  ? 260 LYS A CB  1 
ATOM   1790 C CG  . LYS A 1 217 ? -7.296  -17.939 12.031  1.00 44.11  ? 260 LYS A CG  1 
ATOM   1791 C CD  . LYS A 1 217 ? -6.771  -19.002 11.082  1.00 49.60  ? 260 LYS A CD  1 
ATOM   1792 C CE  . LYS A 1 217 ? -5.338  -19.379 11.412  1.00 56.04  ? 260 LYS A CE  1 
ATOM   1793 N NZ  . LYS A 1 217 ? -4.660  -20.002 10.241  1.00 64.95  ? 260 LYS A NZ  1 
ATOM   1794 N N   . GLU A 1 218 ? -10.971 -15.671 10.554  1.00 31.67  ? 261 GLU A N   1 
ATOM   1795 C CA  . GLU A 1 218 ? -12.337 -15.238 10.285  1.00 34.21  ? 261 GLU A CA  1 
ATOM   1796 C C   . GLU A 1 218 ? -12.634 -15.300 8.792   1.00 32.88  ? 261 GLU A C   1 
ATOM   1797 O O   . GLU A 1 218 ? -13.672 -15.825 8.373   1.00 29.81  ? 261 GLU A O   1 
ATOM   1798 C CB  . GLU A 1 218 ? -12.538 -13.820 10.819  1.00 37.22  ? 261 GLU A CB  1 
ATOM   1799 C CG  . GLU A 1 218 ? -13.963 -13.313 10.762  1.00 40.10  ? 261 GLU A CG  1 
ATOM   1800 C CD  . GLU A 1 218 ? -14.081 -11.883 11.256  1.00 47.24  ? 261 GLU A CD  1 
ATOM   1801 O OE1 . GLU A 1 218 ? -13.032 -11.242 11.476  1.00 47.15  ? 261 GLU A OE1 1 
ATOM   1802 O OE2 . GLU A 1 218 ? -15.219 -11.400 11.426  1.00 53.59  ? 261 GLU A OE2 1 
ATOM   1803 N N   . LEU A 1 219 ? -11.716 -14.781 7.973   1.00 30.20  ? 262 LEU A N   1 
ATOM   1804 C CA  . LEU A 1 219 ? -11.918 -14.791 6.528   1.00 30.52  ? 262 LEU A CA  1 
ATOM   1805 C C   . LEU A 1 219 ? -11.997 -16.214 5.997   1.00 29.58  ? 262 LEU A C   1 
ATOM   1806 O O   . LEU A 1 219 ? -12.832 -16.520 5.138   1.00 28.79  ? 262 LEU A O   1 
ATOM   1807 C CB  . LEU A 1 219 ? -10.788 -14.028 5.839   1.00 29.33  ? 262 LEU A CB  1 
ATOM   1808 C CG  . LEU A 1 219 ? -10.766 -14.070 4.310   1.00 29.19  ? 262 LEU A CG  1 
ATOM   1809 C CD1 . LEU A 1 219 ? -12.075 -13.559 3.732   1.00 27.77  ? 262 LEU A CD1 1 
ATOM   1810 C CD2 . LEU A 1 219 ? -9.592  -13.263 3.778   1.00 30.05  ? 262 LEU A CD2 1 
ATOM   1811 N N   . GLU A 1 220 ? -11.135 -17.099 6.499   1.00 33.44  ? 263 GLU A N   1 
ATOM   1812 C CA  . GLU A 1 220 ? -11.158 -18.485 6.051   1.00 31.87  ? 263 GLU A CA  1 
ATOM   1813 C C   . GLU A 1 220 ? -12.504 -19.132 6.353   1.00 31.48  ? 263 GLU A C   1 
ATOM   1814 O O   . GLU A 1 220 ? -13.054 -19.858 5.518   1.00 26.52  ? 263 GLU A O   1 
ATOM   1815 C CB  . GLU A 1 220 ? -10.020 -19.259 6.714   1.00 32.97  ? 263 GLU A CB  1 
ATOM   1816 C CG  . GLU A 1 220 ? -9.884  -20.702 6.255   1.00 38.13  ? 263 GLU A CG  1 
ATOM   1817 C CD  . GLU A 1 220 ? -8.681  -21.395 6.873   1.00 46.49  ? 263 GLU A CD  1 
ATOM   1818 O OE1 . GLU A 1 220 ? -8.332  -21.071 8.028   1.00 50.50  ? 263 GLU A OE1 1 
ATOM   1819 O OE2 . GLU A 1 220 ? -8.078  -22.258 6.201   1.00 50.32  ? 263 GLU A OE2 1 
ATOM   1820 N N   . SER A 1 221 ? -13.054 -18.871 7.542   1.00 31.75  ? 264 SER A N   1 
ATOM   1821 C CA  . SER A 1 221 ? -14.350 -19.440 7.898   1.00 33.52  ? 264 SER A CA  1 
ATOM   1822 C C   . SER A 1 221 ? -15.456 -18.915 6.990   1.00 30.52  ? 264 SER A C   1 
ATOM   1823 O O   . SER A 1 221 ? -16.352 -19.668 6.594   1.00 29.81  ? 264 SER A O   1 
ATOM   1824 C CB  . SER A 1 221 ? -14.675 -19.133 9.359   1.00 29.21  ? 264 SER A CB  1 
ATOM   1825 O OG  . SER A 1 221 ? -13.841 -19.869 10.236  1.00 45.90  ? 264 SER A OG  1 
ATOM   1826 N N   . ILE A 1 222 ? -15.416 -17.623 6.660   1.00 31.61  ? 265 ILE A N   1 
ATOM   1827 C CA  . ILE A 1 222 ? -16.464 -17.030 5.832   1.00 32.53  ? 265 ILE A CA  1 
ATOM   1828 C C   . ILE A 1 222 ? -16.487 -17.685 4.456   1.00 30.55  ? 265 ILE A C   1 
ATOM   1829 O O   . ILE A 1 222 ? -17.536 -18.127 3.975   1.00 32.43  ? 265 ILE A O   1 
ATOM   1830 C CB  . ILE A 1 222 ? -16.261 -15.507 5.723   1.00 30.44  ? 265 ILE A CB  1 
ATOM   1831 C CG1 . ILE A 1 222 ? -16.537 -14.834 7.069   1.00 31.65  ? 265 ILE A CG1 1 
ATOM   1832 C CG2 . ILE A 1 222 ? -17.151 -14.924 4.630   1.00 33.39  ? 265 ILE A CG2 1 
ATOM   1833 C CD1 . ILE A 1 222 ? -16.039 -13.402 7.147   1.00 34.96  ? 265 ILE A CD1 1 
ATOM   1834 N N   . ILE A 1 223 ? -15.325 -17.764 3.806   1.00 30.34  ? 266 ILE A N   1 
ATOM   1835 C CA  . ILE A 1 223 ? -15.283 -18.273 2.439   1.00 32.22  ? 266 ILE A CA  1 
ATOM   1836 C C   . ILE A 1 223 ? -15.529 -19.777 2.413   1.00 33.09  ? 266 ILE A C   1 
ATOM   1837 O O   . ILE A 1 223 ? -16.138 -20.296 1.469   1.00 31.63  ? 266 ILE A O   1 
ATOM   1838 C CB  . ILE A 1 223 ? -13.944 -17.893 1.778   1.00 32.48  ? 266 ILE A CB  1 
ATOM   1839 C CG1 . ILE A 1 223 ? -13.995 -18.143 0.269   1.00 37.36  ? 266 ILE A CG1 1 
ATOM   1840 C CG2 . ILE A 1 223 ? -12.798 -18.666 2.403   1.00 33.81  ? 266 ILE A CG2 1 
ATOM   1841 C CD1 . ILE A 1 223 ? -14.940 -17.215 -0.475  1.00 38.19  ? 266 ILE A CD1 1 
ATOM   1842 N N   . SER A 1 224 ? -15.071 -20.500 3.439   1.00 31.12  ? 267 SER A N   1 
ATOM   1843 C CA  . SER A 1 224 ? -15.317 -21.938 3.498   1.00 32.82  ? 267 SER A CA  1 
ATOM   1844 C C   . SER A 1 224 ? -16.809 -22.238 3.568   1.00 32.49  ? 267 SER A C   1 
ATOM   1845 O O   . SER A 1 224 ? -17.291 -23.178 2.927   1.00 29.32  ? 267 SER A O   1 
ATOM   1846 C CB  . SER A 1 224 ? -14.598 -22.549 4.702   1.00 32.84  ? 267 SER A CB  1 
ATOM   1847 O OG  . SER A 1 224 ? -13.194 -22.405 4.585   1.00 38.33  ? 267 SER A OG  1 
ATOM   1848 N N   . LYS A 1 225 ? -17.554 -21.454 4.351   1.00 31.01  ? 268 LYS A N   1 
ATOM   1849 C CA  . LYS A 1 225 ? -18.999 -21.647 4.426   1.00 36.97  ? 268 LYS A CA  1 
ATOM   1850 C C   . LYS A 1 225 ? -19.632 -21.555 3.042   1.00 37.81  ? 268 LYS A C   1 
ATOM   1851 O O   . LYS A 1 225 ? -20.595 -22.269 2.742   1.00 36.08  ? 268 LYS A O   1 
ATOM   1852 C CB  . LYS A 1 225 ? -19.617 -20.612 5.367   1.00 37.44  ? 268 LYS A CB  1 
ATOM   1853 C CG  . LYS A 1 225 ? -21.024 -20.953 5.837   1.00 40.74  ? 268 LYS A CG  1 
ATOM   1854 C CD  . LYS A 1 225 ? -21.753 -19.722 6.365   1.00 43.18  ? 268 LYS A CD  1 
ATOM   1855 C CE  . LYS A 1 225 ? -22.989 -20.106 7.170   1.00 39.60  ? 268 LYS A CE  1 
ATOM   1856 N NZ  . LYS A 1 225 ? -23.799 -18.924 7.577   1.00 37.38  ? 268 LYS A NZ  1 
ATOM   1857 N N   . ARG A 1 226 ? -19.097 -20.688 2.184   1.00 35.58  ? 269 ARG A N   1 
ATOM   1858 C CA  . ARG A 1 226 ? -19.586 -20.539 0.820   1.00 36.10  ? 269 ARG A CA  1 
ATOM   1859 C C   . ARG A 1 226 ? -19.055 -21.618 -0.118  1.00 35.96  ? 269 ARG A C   1 
ATOM   1860 O O   . ARG A 1 226 ? -19.226 -21.499 -1.337  1.00 33.65  ? 269 ARG A O   1 
ATOM   1861 C CB  . ARG A 1 226 ? -19.217 -19.153 0.286   1.00 34.51  ? 269 ARG A CB  1 
ATOM   1862 C CG  . ARG A 1 226 ? -19.607 -18.017 1.223   1.00 34.35  ? 269 ARG A CG  1 
ATOM   1863 C CD  . ARG A 1 226 ? -19.665 -16.670 0.508   1.00 33.46  ? 269 ARG A CD  1 
ATOM   1864 N NE  . ARG A 1 226 ? -20.625 -16.687 -0.590  1.00 33.17  ? 269 ARG A NE  1 
ATOM   1865 C CZ  . ARG A 1 226 ? -20.320 -16.553 -1.876  1.00 32.05  ? 269 ARG A CZ  1 
ATOM   1866 N NH1 . ARG A 1 226 ? -19.085 -16.296 -2.276  1.00 31.29  ? 269 ARG A NH1 1 
ATOM   1867 N NH2 . ARG A 1 226 ? -21.283 -16.678 -2.784  1.00 32.27  ? 269 ARG A NH2 1 
ATOM   1868 N N   . ASN A 1 227 ? -18.419 -22.659 0.421   1.00 34.87  ? 270 ASN A N   1 
ATOM   1869 C CA  . ASN A 1 227 ? -17.940 -23.791 -0.374  1.00 34.23  ? 270 ASN A CA  1 
ATOM   1870 C C   . ASN A 1 227 ? -16.915 -23.350 -1.415  1.00 32.88  ? 270 ASN A C   1 
ATOM   1871 O O   . ASN A 1 227 ? -16.899 -23.836 -2.547  1.00 30.88  ? 270 ASN A O   1 
ATOM   1872 C CB  . ASN A 1 227 ? -19.112 -24.520 -1.030  1.00 37.44  ? 270 ASN A CB  1 
ATOM   1873 C CG  . ASN A 1 227 ? -20.054 -25.124 -0.010  1.00 43.38  ? 270 ASN A CG  1 
ATOM   1874 O OD1 . ASN A 1 227 ? -19.630 -25.867 0.879   1.00 46.10  ? 270 ASN A OD1 1 
ATOM   1875 N ND2 . ASN A 1 227 ? -21.334 -24.791 -0.114  1.00 47.25  ? 270 ASN A ND2 1 
ATOM   1876 N N   . ILE A 1 228 ? -16.047 -22.423 -1.020  1.00 30.50  ? 271 ILE A N   1 
ATOM   1877 C CA  . ILE A 1 228 ? -14.894 -22.009 -1.808  1.00 30.42  ? 271 ILE A CA  1 
ATOM   1878 C C   . ILE A 1 228 ? -13.655 -22.208 -0.946  1.00 31.51  ? 271 ILE A C   1 
ATOM   1879 O O   . ILE A 1 228 ? -13.675 -21.932 0.259   1.00 35.10  ? 271 ILE A O   1 
ATOM   1880 C CB  . ILE A 1 228 ? -15.021 -20.545 -2.284  1.00 31.66  ? 271 ILE A CB  1 
ATOM   1881 C CG1 . ILE A 1 228 ? -16.157 -20.425 -3.306  1.00 32.48  ? 271 ILE A CG1 1 
ATOM   1882 C CG2 . ILE A 1 228 ? -13.700 -20.044 -2.871  1.00 28.34  ? 271 ILE A CG2 1 
ATOM   1883 C CD1 . ILE A 1 228 ? -16.389 -19.017 -3.823  1.00 32.03  ? 271 ILE A CD1 1 
ATOM   1884 N N   . GLN A 1 229 ? -12.587 -22.706 -1.556  1.00 27.31  ? 272 GLN A N   1 
ATOM   1885 C CA  . GLN A 1 229 ? -11.361 -22.962 -0.818  1.00 29.76  ? 272 GLN A CA  1 
ATOM   1886 C C   . GLN A 1 229 ? -10.578 -21.668 -0.606  1.00 28.07  ? 272 GLN A C   1 
ATOM   1887 O O   . GLN A 1 229 ? -10.760 -20.675 -1.315  1.00 28.77  ? 272 GLN A O   1 
ATOM   1888 C CB  . GLN A 1 229 ? -10.508 -23.995 -1.554  1.00 27.94  ? 272 GLN A CB  1 
ATOM   1889 C CG  . GLN A 1 229 ? -11.178 -25.357 -1.642  1.00 39.90  ? 272 GLN A CG  1 
ATOM   1890 C CD  . GLN A 1 229 ? -10.513 -26.283 -2.635  1.00 50.52  ? 272 GLN A CD  1 
ATOM   1891 O OE1 . GLN A 1 229 ? -9.902  -25.837 -3.606  1.00 51.57  ? 272 GLN A OE1 1 
ATOM   1892 N NE2 . GLN A 1 229 ? -10.631 -27.585 -2.398  1.00 55.00  ? 272 GLN A NE2 1 
ATOM   1893 N N   . PHE A 1 230 ? -9.699  -21.691 0.397   1.00 26.66  ? 273 PHE A N   1 
ATOM   1894 C CA  . PHE A 1 230 ? -8.946  -20.514 0.805   1.00 27.94  ? 273 PHE A CA  1 
ATOM   1895 C C   . PHE A 1 230 ? -7.458  -20.821 0.837   1.00 27.60  ? 273 PHE A C   1 
ATOM   1896 O O   . PHE A 1 230 ? -7.042  -21.892 1.286   1.00 28.41  ? 273 PHE A O   1 
ATOM   1897 C CB  . PHE A 1 230 ? -9.392  -20.019 2.185   1.00 29.46  ? 273 PHE A CB  1 
ATOM   1898 C CG  . PHE A 1 230 ? -8.658  -18.791 2.655   1.00 30.05  ? 273 PHE A CG  1 
ATOM   1899 C CD1 . PHE A 1 230 ? -8.857  -17.569 2.035   1.00 27.14  ? 273 PHE A CD1 1 
ATOM   1900 C CD2 . PHE A 1 230 ? -7.774  -18.860 3.719   1.00 28.16  ? 273 PHE A CD2 1 
ATOM   1901 C CE1 . PHE A 1 230 ? -8.184  -16.438 2.466   1.00 30.21  ? 273 PHE A CE1 1 
ATOM   1902 C CE2 . PHE A 1 230 ? -7.100  -17.732 4.156   1.00 30.83  ? 273 PHE A CE2 1 
ATOM   1903 C CZ  . PHE A 1 230 ? -7.305  -16.521 3.529   1.00 28.85  ? 273 PHE A CZ  1 
ATOM   1904 N N   . SER A 1 231 ? -6.664  -19.868 0.358   1.00 28.66  ? 274 SER A N   1 
ATOM   1905 C CA  . SER A 1 231 ? -5.212  -19.937 0.425   1.00 33.44  ? 274 SER A CA  1 
ATOM   1906 C C   . SER A 1 231 ? -4.687  -18.571 0.842   1.00 33.43  ? 274 SER A C   1 
ATOM   1907 O O   . SER A 1 231 ? -5.259  -17.538 0.483   1.00 29.75  ? 274 SER A O   1 
ATOM   1908 C CB  . SER A 1 231 ? -4.610  -20.360 -0.920  1.00 36.63  ? 274 SER A CB  1 
ATOM   1909 O OG  . SER A 1 231 ? -3.201  -20.224 -0.911  1.00 45.89  ? 274 SER A OG  1 
ATOM   1910 N N   . CYS A 1 232 ? -3.599  -18.569 1.611   1.00 30.76  ? 275 CYS A N   1 
ATOM   1911 C CA  . CYS A 1 232 ? -3.035  -17.331 2.130   1.00 34.43  ? 275 CYS A CA  1 
ATOM   1912 C C   . CYS A 1 232 ? -1.520  -17.348 2.003   1.00 35.06  ? 275 CYS A C   1 
ATOM   1913 O O   . CYS A 1 232 ? -0.872  -18.346 2.329   1.00 31.80  ? 275 CYS A O   1 
ATOM   1914 C CB  . CYS A 1 232 ? -3.419  -17.108 3.600   1.00 34.80  ? 275 CYS A CB  1 
ATOM   1915 S SG  . CYS A 1 232 ? -2.853  -15.523 4.296   1.00 36.88  ? 275 CYS A SG  1 
ATOM   1916 N N   . LYS A 1 233 ? -0.965  -16.229 1.542   1.00 32.67  ? 276 LYS A N   1 
ATOM   1917 C CA  . LYS A 1 233 ? 0.472   -16.050 1.429   1.00 35.78  ? 276 LYS A CA  1 
ATOM   1918 C C   . LYS A 1 233 ? 0.873   -14.729 2.068   1.00 35.79  ? 276 LYS A C   1 
ATOM   1919 O O   . LYS A 1 233 ? 0.120   -13.750 2.035   1.00 30.56  ? 276 LYS A O   1 
ATOM   1920 C CB  . LYS A 1 233 ? 0.957   -16.039 -0.028  1.00 38.89  ? 276 LYS A CB  1 
ATOM   1921 C CG  . LYS A 1 233 ? 0.759   -17.326 -0.813  1.00 45.39  ? 276 LYS A CG  1 
ATOM   1922 C CD  . LYS A 1 233 ? 1.722   -17.406 -2.010  1.00 60.08  ? 276 LYS A CD  1 
ATOM   1923 C CE  . LYS A 1 233 ? 1.918   -16.054 -2.706  1.00 65.63  ? 276 LYS A CE  1 
ATOM   1924 N NZ  . LYS A 1 233 ? 2.868   -16.133 -3.853  1.00 68.01  ? 276 LYS A NZ  1 
ATOM   1925 N N   . ASN A 1 234 ? 2.073   -14.710 2.639   1.00 29.47  ? 277 ASN A N   1 
ATOM   1926 C CA  . ASN A 1 234 ? 2.680   -13.482 3.129   1.00 31.80  ? 277 ASN A CA  1 
ATOM   1927 C C   . ASN A 1 234 ? 3.522   -12.864 2.020   1.00 32.26  ? 277 ASN A C   1 
ATOM   1928 O O   . ASN A 1 234 ? 4.332   -13.552 1.391   1.00 31.95  ? 277 ASN A O   1 
ATOM   1929 C CB  . ASN A 1 234 ? 3.551   -13.752 4.358   1.00 34.67  ? 277 ASN A CB  1 
ATOM   1930 C CG  . ASN A 1 234 ? 2.754   -14.275 5.540   1.00 35.75  ? 277 ASN A CG  1 
ATOM   1931 O OD1 . ASN A 1 234 ? 2.153   -13.505 6.289   1.00 34.54  ? 277 ASN A OD1 1 
ATOM   1932 N ND2 . ASN A 1 234 ? 2.755   -15.590 5.719   1.00 32.79  ? 277 ASN A ND2 1 
ATOM   1933 N N   . ILE A 1 235 ? 3.317   -11.577 1.772   1.00 31.98  ? 278 ILE A N   1 
ATOM   1934 C CA  . ILE A 1 235 ? 4.204   -10.795 0.913   1.00 32.04  ? 278 ILE A CA  1 
ATOM   1935 C C   . ILE A 1 235 ? 5.071   -9.983  1.871   1.00 31.61  ? 278 ILE A C   1 
ATOM   1936 O O   . ILE A 1 235 ? 4.710   -8.885  2.298   1.00 33.78  ? 278 ILE A O   1 
ATOM   1937 C CB  . ILE A 1 235 ? 3.433   -9.918  -0.071  1.00 31.24  ? 278 ILE A CB  1 
ATOM   1938 C CG1 . ILE A 1 235 ? 2.482   -10.766 -0.926  1.00 33.57  ? 278 ILE A CG1 1 
ATOM   1939 C CG2 . ILE A 1 235 ? 4.399   -9.155  -0.964  1.00 31.76  ? 278 ILE A CG2 1 
ATOM   1940 C CD1 . ILE A 1 235 ? 3.179   -11.709 -1.896  1.00 37.97  ? 278 ILE A CD1 1 
ATOM   1941 N N   . TYR A 1 236 ? 6.233   -10.538 2.219   1.00 34.64  ? 279 TYR A N   1 
ATOM   1942 C CA  . TYR A 1 236 ? 7.061   -9.933  3.257   1.00 35.59  ? 279 TYR A CA  1 
ATOM   1943 C C   . TYR A 1 236 ? 7.745   -8.665  2.762   1.00 38.75  ? 279 TYR A C   1 
ATOM   1944 O O   . TYR A 1 236 ? 7.873   -7.690  3.513   1.00 39.67  ? 279 TYR A O   1 
ATOM   1945 C CB  . TYR A 1 236 ? 8.108   -10.934 3.747   1.00 36.51  ? 279 TYR A CB  1 
ATOM   1946 C CG  . TYR A 1 236 ? 7.557   -12.094 4.553   1.00 34.25  ? 279 TYR A CG  1 
ATOM   1947 C CD1 . TYR A 1 236 ? 7.109   -11.911 5.856   1.00 34.01  ? 279 TYR A CD1 1 
ATOM   1948 C CD2 . TYR A 1 236 ? 7.511   -13.376 4.020   1.00 32.48  ? 279 TYR A CD2 1 
ATOM   1949 C CE1 . TYR A 1 236 ? 6.616   -12.970 6.601   1.00 32.36  ? 279 TYR A CE1 1 
ATOM   1950 C CE2 . TYR A 1 236 ? 7.019   -14.442 4.757   1.00 31.09  ? 279 TYR A CE2 1 
ATOM   1951 C CZ  . TYR A 1 236 ? 6.575   -14.232 6.047   1.00 33.38  ? 279 TYR A CZ  1 
ATOM   1952 O OH  . TYR A 1 236 ? 6.085   -15.285 6.785   1.00 35.17  ? 279 TYR A OH  1 
ATOM   1953 N N   . ARG A 1 237 ? 8.195   -8.658  1.505   1.00 37.14  ? 280 ARG A N   1 
ATOM   1954 C CA  . ARG A 1 237 ? 8.987   -7.568  0.938   1.00 39.66  ? 280 ARG A CA  1 
ATOM   1955 C C   . ARG A 1 237 ? 8.274   -7.068  -0.318  1.00 37.32  ? 280 ARG A C   1 
ATOM   1956 O O   . ARG A 1 237 ? 8.606   -7.484  -1.436  1.00 37.40  ? 280 ARG A O   1 
ATOM   1957 C CB  . ARG A 1 237 ? 10.410  -8.024  0.608   1.00 41.85  ? 280 ARG A CB  1 
ATOM   1958 C CG  . ARG A 1 237 ? 11.073  -8.905  1.669   1.00 45.80  ? 280 ARG A CG  1 
ATOM   1959 C CD  . ARG A 1 237 ? 11.495  -8.105  2.891   1.00 42.41  ? 280 ARG A CD  1 
ATOM   1960 N NE  . ARG A 1 237 ? 12.670  -7.282  2.624   1.00 42.90  ? 280 ARG A NE  1 
ATOM   1961 C CZ  . ARG A 1 237 ? 13.918  -7.609  2.940   1.00 39.54  ? 280 ARG A CZ  1 
ATOM   1962 N NH1 . ARG A 1 237 ? 14.203  -8.738  3.570   1.00 36.15  ? 280 ARG A NH1 1 
ATOM   1963 N NH2 . ARG A 1 237 ? 14.907  -6.780  2.619   1.00 40.73  ? 280 ARG A NH2 1 
ATOM   1964 N N   . PRO A 1 238 ? 7.291   -6.174  -0.167  1.00 36.69  ? 281 PRO A N   1 
ATOM   1965 C CA  . PRO A 1 238 ? 6.536   -5.732  -1.355  1.00 37.48  ? 281 PRO A CA  1 
ATOM   1966 C C   . PRO A 1 238 ? 7.409   -5.160  -2.458  1.00 39.14  ? 281 PRO A C   1 
ATOM   1967 O O   . PRO A 1 238 ? 7.163   -5.436  -3.638  1.00 37.22  ? 281 PRO A O   1 
ATOM   1968 C CB  . PRO A 1 238 ? 5.580   -4.673  -0.785  1.00 35.37  ? 281 PRO A CB  1 
ATOM   1969 C CG  . PRO A 1 238 ? 5.465   -4.995  0.664   1.00 37.86  ? 281 PRO A CG  1 
ATOM   1970 C CD  . PRO A 1 238 ? 6.794   -5.553  1.071   1.00 36.68  ? 281 PRO A CD  1 
ATOM   1971 N N   . ASP A 1 239 ? 8.431   -4.375  -2.110  1.00 38.68  ? 282 ASP A N   1 
ATOM   1972 C CA  . ASP A 1 239 ? 9.298   -3.804  -3.136  1.00 42.94  ? 282 ASP A CA  1 
ATOM   1973 C C   . ASP A 1 239 ? 10.034  -4.896  -3.902  1.00 41.81  ? 282 ASP A C   1 
ATOM   1974 O O   . ASP A 1 239 ? 10.202  -4.804  -5.124  1.00 43.22  ? 282 ASP A O   1 
ATOM   1975 C CB  . ASP A 1 239 ? 10.289  -2.826  -2.503  1.00 45.82  ? 282 ASP A CB  1 
ATOM   1976 C CG  . ASP A 1 239 ? 11.114  -3.461  -1.401  1.00 49.93  ? 282 ASP A CG  1 
ATOM   1977 O OD1 . ASP A 1 239 ? 10.606  -4.383  -0.728  1.00 49.26  ? 282 ASP A OD1 1 
ATOM   1978 O OD2 . ASP A 1 239 ? 12.273  -3.036  -1.205  1.00 53.81  ? 282 ASP A OD2 1 
ATOM   1979 N N   . LYS A 1 240 ? 10.487  -5.937  -3.201  1.00 42.17  ? 283 LYS A N   1 
ATOM   1980 C CA  . LYS A 1 240 ? 11.151  -7.047  -3.875  1.00 42.62  ? 283 LYS A CA  1 
ATOM   1981 C C   . LYS A 1 240 ? 10.160  -7.895  -4.658  1.00 41.15  ? 283 LYS A C   1 
ATOM   1982 O O   . LYS A 1 240 ? 10.502  -8.430  -5.717  1.00 43.86  ? 283 LYS A O   1 
ATOM   1983 C CB  . LYS A 1 240 ? 11.896  -7.907  -2.854  1.00 45.34  ? 283 LYS A CB  1 
ATOM   1984 C CG  . LYS A 1 240 ? 12.887  -7.131  -1.997  1.00 46.69  ? 283 LYS A CG  1 
ATOM   1985 C CD  . LYS A 1 240 ? 14.140  -6.761  -2.778  1.00 51.21  ? 283 LYS A CD  1 
ATOM   1986 C CE  . LYS A 1 240 ? 15.022  -5.804  -1.988  1.00 51.92  ? 283 LYS A CE  1 
ATOM   1987 N NZ  . LYS A 1 240 ? 16.255  -5.438  -2.739  1.00 60.62  ? 283 LYS A NZ  1 
ATOM   1988 N N   . PHE A 1 241 ? 8.931   -8.029  -4.154  1.00 39.86  ? 284 PHE A N   1 
ATOM   1989 C CA  . PHE A 1 241 ? 7.918   -8.799  -4.868  1.00 38.92  ? 284 PHE A CA  1 
ATOM   1990 C C   . PHE A 1 241 ? 7.603   -8.171  -6.219  1.00 42.01  ? 284 PHE A C   1 
ATOM   1991 O O   . PHE A 1 241 ? 7.508   -8.875  -7.230  1.00 43.63  ? 284 PHE A O   1 
ATOM   1992 C CB  . PHE A 1 241 ? 6.660   -8.908  -4.004  1.00 37.61  ? 284 PHE A CB  1 
ATOM   1993 C CG  . PHE A 1 241 ? 5.441   -9.368  -4.751  1.00 37.67  ? 284 PHE A CG  1 
ATOM   1994 C CD1 . PHE A 1 241 ? 5.276   -10.700 -5.092  1.00 39.75  ? 284 PHE A CD1 1 
ATOM   1995 C CD2 . PHE A 1 241 ? 4.448   -8.467  -5.093  1.00 38.31  ? 284 PHE A CD2 1 
ATOM   1996 C CE1 . PHE A 1 241 ? 4.147   -11.121 -5.773  1.00 41.80  ? 284 PHE A CE1 1 
ATOM   1997 C CE2 . PHE A 1 241 ? 3.317   -8.881  -5.772  1.00 37.59  ? 284 PHE A CE2 1 
ATOM   1998 C CZ  . PHE A 1 241 ? 3.166   -10.207 -6.111  1.00 38.05  ? 284 PHE A CZ  1 
ATOM   1999 N N   . LEU A 1 242 ? 7.453   -6.844  -6.260  1.00 43.34  ? 285 LEU A N   1 
ATOM   2000 C CA  . LEU A 1 242 ? 7.229   -6.165  -7.532  1.00 39.92  ? 285 LEU A CA  1 
ATOM   2001 C C   . LEU A 1 242 ? 8.413   -6.356  -8.471  1.00 46.52  ? 285 LEU A C   1 
ATOM   2002 O O   . LEU A 1 242 ? 8.235   -6.591  -9.671  1.00 48.86  ? 285 LEU A O   1 
ATOM   2003 C CB  . LEU A 1 242 ? 6.980   -4.676  -7.297  1.00 39.39  ? 285 LEU A CB  1 
ATOM   2004 C CG  . LEU A 1 242 ? 5.564   -4.254  -6.911  1.00 39.80  ? 285 LEU A CG  1 
ATOM   2005 C CD1 . LEU A 1 242 ? 5.554   -2.784  -6.521  1.00 39.19  ? 285 LEU A CD1 1 
ATOM   2006 C CD2 . LEU A 1 242 ? 4.593   -4.515  -8.053  1.00 37.04  ? 285 LEU A CD2 1 
ATOM   2007 N N   . GLN A 1 243 ? 9.632   -6.252  -7.938  1.00 46.31  ? 286 GLN A N   1 
ATOM   2008 C CA  . GLN A 1 243 ? 10.825  -6.420  -8.761  1.00 54.11  ? 286 GLN A CA  1 
ATOM   2009 C C   . GLN A 1 243 ? 10.876  -7.807  -9.389  1.00 56.96  ? 286 GLN A C   1 
ATOM   2010 O O   . GLN A 1 243 ? 11.334  -7.964  -10.526 1.00 62.79  ? 286 GLN A O   1 
ATOM   2011 C CB  . GLN A 1 243 ? 12.069  -6.154  -7.910  1.00 55.70  ? 286 GLN A CB  1 
ATOM   2012 C CG  . GLN A 1 243 ? 13.347  -6.802  -8.409  1.00 68.39  ? 286 GLN A CG  1 
ATOM   2013 C CD  . GLN A 1 243 ? 14.566  -6.341  -7.631  1.00 72.28  ? 286 GLN A CD  1 
ATOM   2014 O OE1 . GLN A 1 243 ? 14.464  -5.509  -6.729  1.00 67.65  ? 286 GLN A OE1 1 
ATOM   2015 N NE2 . GLN A 1 243 ? 15.727  -6.881  -7.977  1.00 78.95  ? 286 GLN A NE2 1 
ATOM   2016 N N   . CYS A 1 244 ? 10.406  -8.827  -8.665  1.00 55.08  ? 287 CYS A N   1 
ATOM   2017 C CA  . CYS A 1 244 ? 10.411  -10.182 -9.207  1.00 60.31  ? 287 CYS A CA  1 
ATOM   2018 C C   . CYS A 1 244 ? 9.324   -10.373 -10.258 1.00 63.84  ? 287 CYS A C   1 
ATOM   2019 O O   . CYS A 1 244 ? 9.509   -11.145 -11.205 1.00 67.34  ? 287 CYS A O   1 
ATOM   2020 C CB  . CYS A 1 244 ? 10.239  -11.198 -8.077  1.00 57.06  ? 287 CYS A CB  1 
ATOM   2021 S SG  . CYS A 1 244 ? 10.132  -12.917 -8.631  1.00 71.79  ? 287 CYS A SG  1 
ATOM   2022 N N   . VAL A 1 245 ? 8.188   -9.688  -10.108 1.00 55.14  ? 288 VAL A N   1 
ATOM   2023 C CA  . VAL A 1 245 ? 7.130   -9.791  -11.106 1.00 58.81  ? 288 VAL A CA  1 
ATOM   2024 C C   . VAL A 1 245 ? 7.552   -9.109  -12.402 1.00 62.32  ? 288 VAL A C   1 
ATOM   2025 O O   . VAL A 1 245 ? 7.157   -9.532  -13.495 1.00 60.33  ? 288 VAL A O   1 
ATOM   2026 C CB  . VAL A 1 245 ? 5.820   -9.201  -10.551 1.00 53.38  ? 288 VAL A CB  1 
ATOM   2027 C CG1 . VAL A 1 245 ? 4.734   -9.210  -11.613 1.00 55.74  ? 288 VAL A CG1 1 
ATOM   2028 C CG2 . VAL A 1 245 ? 5.363   -9.976  -9.325  1.00 45.29  ? 288 VAL A CG2 1 
ATOM   2029 N N   . LYS A 1 246 ? 8.360   -8.051  -12.303 1.00 68.82  ? 289 LYS A N   1 
ATOM   2030 C CA  . LYS A 1 246 ? 8.775   -7.302  -13.486 1.00 75.36  ? 289 LYS A CA  1 
ATOM   2031 C C   . LYS A 1 246 ? 9.810   -8.066  -14.301 1.00 84.52  ? 289 LYS A C   1 
ATOM   2032 O O   . LYS A 1 246 ? 9.740   -8.089  -15.535 1.00 88.78  ? 289 LYS A O   1 
ATOM   2033 C CB  . LYS A 1 246 ? 9.332   -5.942  -13.060 1.00 72.77  ? 289 LYS A CB  1 
ATOM   2034 C CG  . LYS A 1 246 ? 8.902   -4.778  -13.947 1.00 82.58  ? 289 LYS A CG  1 
ATOM   2035 C CD  . LYS A 1 246 ? 9.210   -3.415  -13.321 1.00 82.45  ? 289 LYS A CD  1 
ATOM   2036 C CE  . LYS A 1 246 ? 8.667   -3.299  -11.901 1.00 77.43  ? 289 LYS A CE  1 
ATOM   2037 N NZ  . LYS A 1 246 ? 8.450   -1.890  -11.474 1.00 79.28  ? 289 LYS A NZ  1 
ATOM   2038 N N   . ASN A 1 247 ? 10.779  -8.692  -13.635 1.00 90.43  ? 290 ASN A N   1 
ATOM   2039 C CA  . ASN A 1 247 ? 11.903  -9.354  -14.295 1.00 99.04  ? 290 ASN A CA  1 
ATOM   2040 C C   . ASN A 1 247 ? 12.118  -10.727 -13.679 1.00 101.02 ? 290 ASN A C   1 
ATOM   2041 O O   . ASN A 1 247 ? 13.125  -10.971 -13.000 1.00 105.58 ? 290 ASN A O   1 
ATOM   2042 C CB  . ASN A 1 247 ? 13.168  -8.501  -14.182 1.00 105.53 ? 290 ASN A CB  1 
ATOM   2043 C CG  . ASN A 1 247 ? 13.329  -7.882  -12.807 1.00 104.62 ? 290 ASN A CG  1 
ATOM   2044 O OD1 . ASN A 1 247 ? 12.954  -6.730  -12.586 1.00 98.87  ? 290 ASN A OD1 1 
ATOM   2045 N ND2 . ASN A 1 247 ? 13.880  -8.648  -11.871 1.00 110.78 ? 290 ASN A ND2 1 
ATOM   2046 N N   . PRO A 1 248 ? 11.189  -11.661 -13.891 1.00 97.53  ? 291 PRO A N   1 
ATOM   2047 C CA  . PRO A 1 248 ? 11.379  -13.021 -13.376 1.00 98.98  ? 291 PRO A CA  1 
ATOM   2048 C C   . PRO A 1 248 ? 12.252  -13.881 -14.285 1.00 100.16 ? 291 PRO A C   1 
ATOM   2049 O O   . PRO A 1 248 ? 11.948  -15.039 -14.552 1.00 97.07  ? 291 PRO A O   1 
ATOM   2050 C CB  . PRO A 1 248 ? 9.950   -13.561 -13.297 1.00 95.38  ? 291 PRO A CB  1 
ATOM   2051 C CG  . PRO A 1 248 ? 9.237   -12.860 -14.403 1.00 89.96  ? 291 PRO A CG  1 
ATOM   2052 C CD  . PRO A 1 248 ? 9.847   -11.478 -14.480 1.00 91.83  ? 291 PRO A CD  1 
ATOM   2053 N N   . GLU A 1 249 ? 13.361  -13.302 -14.754 1.00 98.56  ? 292 GLU A N   1 
ATOM   2054 C CA  . GLU A 1 249 ? 14.293  -14.023 -15.616 1.00 96.04  ? 292 GLU A CA  1 
ATOM   2055 C C   . GLU A 1 249 ? 15.507  -14.488 -14.816 1.00 95.45  ? 292 GLU A C   1 
ATOM   2056 O O   . GLU A 1 249 ? 16.510  -13.780 -14.720 1.00 89.54  ? 292 GLU A O   1 
ATOM   2057 C CB  . GLU A 1 249 ? 14.735  -13.144 -16.787 1.00 87.75  ? 292 GLU A CB  1 
ATOM   2058 N N   . SER B 1 1   ? -25.417 -48.186 -44.942 1.00 60.81  ? 44  SER B N   1 
ATOM   2059 C CA  . SER B 1 1   ? -26.739 -48.023 -45.534 1.00 58.61  ? 44  SER B CA  1 
ATOM   2060 C C   . SER B 1 1   ? -26.739 -48.453 -46.995 1.00 53.95  ? 44  SER B C   1 
ATOM   2061 O O   . SER B 1 1   ? -25.737 -48.304 -47.696 1.00 49.28  ? 44  SER B O   1 
ATOM   2062 C CB  . SER B 1 1   ? -27.203 -46.570 -45.419 1.00 57.57  ? 44  SER B CB  1 
ATOM   2063 O OG  . SER B 1 1   ? -28.372 -46.338 -46.188 1.00 56.55  ? 44  SER B OG  1 
ATOM   2064 N N   . ARG B 1 2   ? -27.874 -48.977 -47.453 1.00 49.57  ? 45  ARG B N   1 
ATOM   2065 C CA  . ARG B 1 2   ? -27.997 -49.425 -48.833 1.00 48.00  ? 45  ARG B CA  1 
ATOM   2066 C C   . ARG B 1 2   ? -28.195 -48.275 -49.810 1.00 48.95  ? 45  ARG B C   1 
ATOM   2067 O O   . ARG B 1 2   ? -28.253 -48.520 -51.020 1.00 46.52  ? 45  ARG B O   1 
ATOM   2068 C CB  . ARG B 1 2   ? -29.150 -50.424 -48.965 1.00 49.52  ? 45  ARG B CB  1 
ATOM   2069 C CG  . ARG B 1 2   ? -30.514 -49.898 -48.544 1.00 53.36  ? 45  ARG B CG  1 
ATOM   2070 C CD  . ARG B 1 2   ? -31.619 -50.778 -49.118 1.00 55.06  ? 45  ARG B CD  1 
ATOM   2071 N NE  . ARG B 1 2   ? -32.921 -50.516 -48.517 1.00 55.46  ? 45  ARG B NE  1 
ATOM   2072 C CZ  . ARG B 1 2   ? -34.066 -51.011 -48.967 1.00 56.60  ? 45  ARG B CZ  1 
ATOM   2073 N NH1 . ARG B 1 2   ? -34.112 -51.782 -50.042 1.00 59.28  ? 45  ARG B NH1 1 
ATOM   2074 N NH2 . ARG B 1 2   ? -35.194 -50.724 -48.324 1.00 61.39  ? 45  ARG B NH2 1 
ATOM   2075 N N   . TRP B 1 3   ? -28.301 -47.039 -49.322 1.00 48.52  ? 46  TRP B N   1 
ATOM   2076 C CA  . TRP B 1 3   ? -28.418 -45.871 -50.182 1.00 47.86  ? 46  TRP B CA  1 
ATOM   2077 C C   . TRP B 1 3   ? -27.141 -45.046 -50.253 1.00 46.70  ? 46  TRP B C   1 
ATOM   2078 O O   . TRP B 1 3   ? -27.089 -44.081 -51.025 1.00 42.50  ? 46  TRP B O   1 
ATOM   2079 C CB  . TRP B 1 3   ? -29.556 -44.961 -49.705 1.00 48.61  ? 46  TRP B CB  1 
ATOM   2080 C CG  . TRP B 1 3   ? -30.800 -45.672 -49.258 1.00 46.53  ? 46  TRP B CG  1 
ATOM   2081 C CD1 . TRP B 1 3   ? -31.317 -45.695 -47.996 1.00 45.69  ? 46  TRP B CD1 1 
ATOM   2082 C CD2 . TRP B 1 3   ? -31.687 -46.452 -50.069 1.00 44.36  ? 46  TRP B CD2 1 
ATOM   2083 N NE1 . TRP B 1 3   ? -32.471 -46.438 -47.970 1.00 47.60  ? 46  TRP B NE1 1 
ATOM   2084 C CE2 . TRP B 1 3   ? -32.719 -46.916 -49.229 1.00 46.20  ? 46  TRP B CE2 1 
ATOM   2085 C CE3 . TRP B 1 3   ? -31.708 -46.805 -51.421 1.00 42.79  ? 46  TRP B CE3 1 
ATOM   2086 C CZ2 . TRP B 1 3   ? -33.760 -47.713 -49.697 1.00 45.32  ? 46  TRP B CZ2 1 
ATOM   2087 C CZ3 . TRP B 1 3   ? -32.744 -47.597 -51.883 1.00 42.76  ? 46  TRP B CZ3 1 
ATOM   2088 C CH2 . TRP B 1 3   ? -33.754 -48.041 -51.024 1.00 44.98  ? 46  TRP B CH2 1 
ATOM   2089 N N   . ARG B 1 4   ? -26.116 -45.385 -49.476 1.00 44.03  ? 47  ARG B N   1 
ATOM   2090 C CA  . ARG B 1 4   ? -24.948 -44.525 -49.362 1.00 44.44  ? 47  ARG B CA  1 
ATOM   2091 C C   . ARG B 1 4   ? -24.084 -44.620 -50.612 1.00 43.15  ? 47  ARG B C   1 
ATOM   2092 O O   . ARG B 1 4   ? -23.712 -45.717 -51.040 1.00 41.27  ? 47  ARG B O   1 
ATOM   2093 C CB  . ARG B 1 4   ? -24.129 -44.895 -48.128 1.00 46.63  ? 47  ARG B CB  1 
ATOM   2094 C CG  . ARG B 1 4   ? -23.137 -43.816 -47.716 1.00 44.55  ? 47  ARG B CG  1 
ATOM   2095 C CD  . ARG B 1 4   ? -22.631 -44.019 -46.297 1.00 41.14  ? 47  ARG B CD  1 
ATOM   2096 N NE  . ARG B 1 4   ? -21.654 -45.096 -46.199 1.00 40.68  ? 47  ARG B NE  1 
ATOM   2097 C CZ  . ARG B 1 4   ? -21.046 -45.452 -45.075 1.00 44.82  ? 47  ARG B CZ  1 
ATOM   2098 N NH1 . ARG B 1 4   ? -21.297 -44.843 -43.927 1.00 39.80  ? 47  ARG B NH1 1 
ATOM   2099 N NH2 . ARG B 1 4   ? -20.161 -46.443 -45.104 1.00 47.90  ? 47  ARG B NH2 1 
ATOM   2100 N N   . GLN B 1 5   ? -23.759 -43.467 -51.187 1.00 43.10  ? 48  GLN B N   1 
ATOM   2101 C CA  . GLN B 1 5   ? -22.914 -43.392 -52.367 1.00 44.39  ? 48  GLN B CA  1 
ATOM   2102 C C   . GLN B 1 5   ? -21.456 -43.186 -51.967 1.00 45.69  ? 48  GLN B C   1 
ATOM   2103 O O   . GLN B 1 5   ? -21.140 -42.796 -50.840 1.00 43.06  ? 48  GLN B O   1 
ATOM   2104 C CB  . GLN B 1 5   ? -23.372 -42.258 -53.288 1.00 45.61  ? 48  GLN B CB  1 
ATOM   2105 C CG  . GLN B 1 5   ? -23.281 -40.866 -52.671 1.00 41.00  ? 48  GLN B CG  1 
ATOM   2106 C CD  . GLN B 1 5   ? -24.123 -39.842 -53.414 1.00 42.38  ? 48  GLN B CD  1 
ATOM   2107 O OE1 . GLN B 1 5   ? -23.652 -39.195 -54.350 1.00 39.71  ? 48  GLN B OE1 1 
ATOM   2108 N NE2 . GLN B 1 5   ? -25.378 -39.693 -53.000 1.00 37.42  ? 48  GLN B NE2 1 
ATOM   2109 N N   . GLN B 1 6   ? -20.564 -43.462 -52.914 1.00 49.43  ? 49  GLN B N   1 
ATOM   2110 C CA  . GLN B 1 6   ? -19.139 -43.262 -52.702 1.00 49.51  ? 49  GLN B CA  1 
ATOM   2111 C C   . GLN B 1 6   ? -18.765 -41.813 -52.984 1.00 47.17  ? 49  GLN B C   1 
ATOM   2112 O O   . GLN B 1 6   ? -19.201 -41.225 -53.978 1.00 44.87  ? 49  GLN B O   1 
ATOM   2113 C CB  . GLN B 1 6   ? -18.333 -44.201 -53.604 1.00 54.60  ? 49  GLN B CB  1 
ATOM   2114 C CG  . GLN B 1 6   ? -16.819 -44.014 -53.543 1.00 56.96  ? 49  GLN B CG  1 
ATOM   2115 C CD  . GLN B 1 6   ? -16.218 -44.487 -52.233 1.00 64.18  ? 49  GLN B CD  1 
ATOM   2116 O OE1 . GLN B 1 6   ? -16.856 -45.210 -51.468 1.00 69.75  ? 49  GLN B OE1 1 
ATOM   2117 N NE2 . GLN B 1 6   ? -14.981 -44.080 -51.970 1.00 64.16  ? 49  GLN B NE2 1 
ATOM   2118 N N   . TRP B 1 7   ? -17.958 -41.238 -52.099 1.00 39.61  ? 50  TRP B N   1 
ATOM   2119 C CA  . TRP B 1 7   ? -17.403 -39.909 -52.295 1.00 38.29  ? 50  TRP B CA  1 
ATOM   2120 C C   . TRP B 1 7   ? -15.945 -40.019 -52.727 1.00 38.59  ? 50  TRP B C   1 
ATOM   2121 O O   . TRP B 1 7   ? -15.322 -41.080 -52.642 1.00 37.78  ? 50  TRP B O   1 
ATOM   2122 C CB  . TRP B 1 7   ? -17.522 -39.074 -51.016 1.00 34.51  ? 50  TRP B CB  1 
ATOM   2123 C CG  . TRP B 1 7   ? -18.916 -39.005 -50.468 1.00 32.17  ? 50  TRP B CG  1 
ATOM   2124 C CD1 . TRP B 1 7   ? -19.369 -39.571 -49.313 1.00 30.77  ? 50  TRP B CD1 1 
ATOM   2125 C CD2 . TRP B 1 7   ? -20.040 -38.338 -51.055 1.00 32.63  ? 50  TRP B CD2 1 
ATOM   2126 N NE1 . TRP B 1 7   ? -20.703 -39.296 -49.141 1.00 29.70  ? 50  TRP B NE1 1 
ATOM   2127 C CE2 . TRP B 1 7   ? -21.140 -38.541 -50.198 1.00 30.00  ? 50  TRP B CE2 1 
ATOM   2128 C CE3 . TRP B 1 7   ? -20.223 -37.586 -52.220 1.00 31.73  ? 50  TRP B CE3 1 
ATOM   2129 C CZ2 . TRP B 1 7   ? -22.402 -38.019 -50.468 1.00 30.77  ? 50  TRP B CZ2 1 
ATOM   2130 C CZ3 . TRP B 1 7   ? -21.477 -37.071 -52.487 1.00 32.72  ? 50  TRP B CZ3 1 
ATOM   2131 C CH2 . TRP B 1 7   ? -22.551 -37.289 -51.615 1.00 31.59  ? 50  TRP B CH2 1 
ATOM   2132 N N   . SER B 1 8   ? -15.400 -38.898 -53.199 1.00 37.60  ? 51  SER B N   1 
ATOM   2133 C CA  . SER B 1 8   ? -14.024 -38.866 -53.673 1.00 41.65  ? 51  SER B CA  1 
ATOM   2134 C C   . SER B 1 8   ? -13.025 -38.465 -52.596 1.00 43.23  ? 51  SER B C   1 
ATOM   2135 O O   . SER B 1 8   ? -11.823 -38.693 -52.773 1.00 46.26  ? 51  SER B O   1 
ATOM   2136 C CB  . SER B 1 8   ? -13.897 -37.902 -54.858 1.00 46.28  ? 51  SER B CB  1 
ATOM   2137 O OG  . SER B 1 8   ? -14.752 -38.287 -55.920 1.00 49.54  ? 51  SER B OG  1 
ATOM   2138 N N   . GLY B 1 9   ? -13.485 -37.883 -51.491 1.00 39.53  ? 52  GLY B N   1 
ATOM   2139 C CA  . GLY B 1 9   ? -12.599 -37.447 -50.439 1.00 38.74  ? 52  GLY B CA  1 
ATOM   2140 C C   . GLY B 1 9   ? -12.398 -38.503 -49.372 1.00 36.85  ? 52  GLY B C   1 
ATOM   2141 O O   . GLY B 1 9   ? -13.147 -39.481 -49.283 1.00 37.50  ? 52  GLY B O   1 
ATOM   2142 N N   . PRO B 1 10  ? -11.376 -38.324 -48.536 1.00 37.25  ? 53  PRO B N   1 
ATOM   2143 C CA  . PRO B 1 10  ? -11.139 -39.284 -47.451 1.00 35.97  ? 53  PRO B CA  1 
ATOM   2144 C C   . PRO B 1 10  ? -12.294 -39.305 -46.461 1.00 32.97  ? 53  PRO B C   1 
ATOM   2145 O O   . PRO B 1 10  ? -13.014 -38.321 -46.287 1.00 33.45  ? 53  PRO B O   1 
ATOM   2146 C CB  . PRO B 1 10  ? -9.846  -38.776 -46.798 1.00 35.98  ? 53  PRO B CB  1 
ATOM   2147 C CG  . PRO B 1 10  ? -9.759  -37.338 -47.181 1.00 42.13  ? 53  PRO B CG  1 
ATOM   2148 C CD  . PRO B 1 10  ? -10.379 -37.239 -48.543 1.00 35.43  ? 53  PRO B CD  1 
ATOM   2149 N N   . GLY B 1 11  ? -12.469 -40.453 -45.814 1.00 33.46  ? 54  GLY B N   1 
ATOM   2150 C CA  . GLY B 1 11  ? -13.527 -40.619 -44.843 1.00 34.24  ? 54  GLY B CA  1 
ATOM   2151 C C   . GLY B 1 11  ? -13.207 -39.947 -43.520 1.00 31.42  ? 54  GLY B C   1 
ATOM   2152 O O   . GLY B 1 11  ? -12.119 -39.418 -43.295 1.00 31.24  ? 54  GLY B O   1 
ATOM   2153 N N   . THR B 1 12  ? -14.189 -39.989 -42.623 1.00 30.52  ? 55  THR B N   1 
ATOM   2154 C CA  . THR B 1 12  ? -14.048 -39.348 -41.323 1.00 27.23  ? 55  THR B CA  1 
ATOM   2155 C C   . THR B 1 12  ? -12.807 -39.861 -40.605 1.00 29.52  ? 55  THR B C   1 
ATOM   2156 O O   . THR B 1 12  ? -12.505 -41.057 -40.626 1.00 28.70  ? 55  THR B O   1 
ATOM   2157 C CB  . THR B 1 12  ? -15.287 -39.610 -40.465 1.00 28.68  ? 55  THR B CB  1 
ATOM   2158 O OG1 . THR B 1 12  ? -16.436 -39.019 -41.084 1.00 30.08  ? 55  THR B OG1 1 
ATOM   2159 C CG2 . THR B 1 12  ? -15.103 -39.035 -39.064 1.00 26.58  ? 55  THR B CG2 1 
ATOM   2160 N N   . THR B 1 13  ? -12.086 -38.943 -39.964 1.00 29.59  ? 56  THR B N   1 
ATOM   2161 C CA  . THR B 1 13  ? -10.882 -39.314 -39.236 1.00 29.89  ? 56  THR B CA  1 
ATOM   2162 C C   . THR B 1 13  ? -11.196 -40.404 -38.220 1.00 28.97  ? 56  THR B C   1 
ATOM   2163 O O   . THR B 1 13  ? -12.228 -40.371 -37.546 1.00 25.93  ? 56  THR B O   1 
ATOM   2164 C CB  . THR B 1 13  ? -10.291 -38.095 -38.522 1.00 30.45  ? 56  THR B CB  1 
ATOM   2165 O OG1 . THR B 1 13  ? -10.118 -37.021 -39.456 1.00 29.95  ? 56  THR B OG1 1 
ATOM   2166 C CG2 . THR B 1 13  ? -8.946  -38.445 -37.899 1.00 30.17  ? 56  THR B CG2 1 
ATOM   2167 N N   . LYS B 1 14  ? -10.298 -41.380 -38.120 1.00 34.08  ? 57  LYS B N   1 
ATOM   2168 C CA  . LYS B 1 14  ? -10.479 -42.462 -37.163 1.00 36.68  ? 57  LYS B CA  1 
ATOM   2169 C C   . LYS B 1 14  ? -10.599 -41.907 -35.750 1.00 31.49  ? 57  LYS B C   1 
ATOM   2170 O O   . LYS B 1 14  ? -9.900  -40.964 -35.373 1.00 31.92  ? 57  LYS B O   1 
ATOM   2171 C CB  . LYS B 1 14  ? -9.311  -43.441 -37.252 1.00 44.36  ? 57  LYS B CB  1 
ATOM   2172 C CG  . LYS B 1 14  ? -9.359  -44.295 -38.501 1.00 55.45  ? 57  LYS B CG  1 
ATOM   2173 C CD  . LYS B 1 14  ? -8.007  -44.883 -38.837 1.00 65.64  ? 57  LYS B CD  1 
ATOM   2174 C CE  . LYS B 1 14  ? -7.967  -45.321 -40.286 1.00 64.73  ? 57  LYS B CE  1 
ATOM   2175 N NZ  . LYS B 1 14  ? -9.204  -46.051 -40.685 1.00 65.39  ? 57  LYS B NZ  1 
ATOM   2176 N N   . ARG B 1 15  ? -11.513 -42.488 -34.975 1.00 27.94  ? 58  ARG B N   1 
ATOM   2177 C CA  . ARG B 1 15  ? -11.737 -42.088 -33.587 1.00 32.65  ? 58  ARG B CA  1 
ATOM   2178 C C   . ARG B 1 15  ? -12.173 -40.630 -33.481 1.00 29.89  ? 58  ARG B C   1 
ATOM   2179 O O   . ARG B 1 15  ? -11.843 -39.942 -32.511 1.00 30.14  ? 58  ARG B O   1 
ATOM   2180 C CB  . ARG B 1 15  ? -10.485 -42.320 -32.737 1.00 33.83  ? 58  ARG B CB  1 
ATOM   2181 C CG  . ARG B 1 15  ? -9.965  -43.749 -32.751 1.00 38.85  ? 58  ARG B CG  1 
ATOM   2182 C CD  . ARG B 1 15  ? -9.367  -44.112 -31.400 1.00 43.09  ? 58  ARG B CD  1 
ATOM   2183 N NE  . ARG B 1 15  ? -10.374 -44.697 -30.522 1.00 45.68  ? 58  ARG B NE  1 
ATOM   2184 C CZ  . ARG B 1 15  ? -10.432 -44.525 -29.207 1.00 40.30  ? 58  ARG B CZ  1 
ATOM   2185 N NH1 . ARG B 1 15  ? -9.569  -43.751 -28.568 1.00 39.21  ? 58  ARG B NH1 1 
ATOM   2186 N NH2 . ARG B 1 15  ? -11.390 -45.136 -28.518 1.00 38.96  ? 58  ARG B NH2 1 
ATOM   2187 N N   . PHE B 1 16  ? -12.922 -40.150 -34.475 1.00 28.59  ? 59  PHE B N   1 
ATOM   2188 C CA  . PHE B 1 16  ? -13.357 -38.755 -34.466 1.00 29.01  ? 59  PHE B CA  1 
ATOM   2189 C C   . PHE B 1 16  ? -14.149 -38.404 -33.213 1.00 28.23  ? 59  PHE B C   1 
ATOM   2190 O O   . PHE B 1 16  ? -13.806 -37.409 -32.553 1.00 26.23  ? 59  PHE B O   1 
ATOM   2191 C CB  . PHE B 1 16  ? -14.153 -38.467 -35.747 1.00 28.24  ? 59  PHE B CB  1 
ATOM   2192 C CG  . PHE B 1 16  ? -14.662 -37.055 -35.851 1.00 26.74  ? 59  PHE B CG  1 
ATOM   2193 C CD1 . PHE B 1 16  ? -13.796 -36.007 -36.121 1.00 23.40  ? 59  PHE B CD1 1 
ATOM   2194 C CD2 . PHE B 1 16  ? -16.011 -36.780 -35.695 1.00 27.15  ? 59  PHE B CD2 1 
ATOM   2195 C CE1 . PHE B 1 16  ? -14.266 -34.709 -36.223 1.00 25.14  ? 59  PHE B CE1 1 
ATOM   2196 C CE2 . PHE B 1 16  ? -16.486 -35.484 -35.798 1.00 26.41  ? 59  PHE B CE2 1 
ATOM   2197 C CZ  . PHE B 1 16  ? -15.613 -34.448 -36.060 1.00 24.84  ? 59  PHE B CZ  1 
ATOM   2198 N N   . PRO B 1 17  ? -15.176 -39.162 -32.811 1.00 28.27  ? 60  PRO B N   1 
ATOM   2199 C CA  . PRO B 1 17  ? -15.900 -38.786 -31.582 1.00 28.75  ? 60  PRO B CA  1 
ATOM   2200 C C   . PRO B 1 17  ? -15.000 -38.719 -30.362 1.00 31.46  ? 60  PRO B C   1 
ATOM   2201 O O   . PRO B 1 17  ? -15.072 -37.759 -29.583 1.00 30.42  ? 60  PRO B O   1 
ATOM   2202 C CB  . PRO B 1 17  ? -16.963 -39.888 -31.450 1.00 30.79  ? 60  PRO B CB  1 
ATOM   2203 C CG  . PRO B 1 17  ? -17.094 -40.474 -32.816 1.00 29.72  ? 60  PRO B CG  1 
ATOM   2204 C CD  . PRO B 1 17  ? -15.728 -40.384 -33.422 1.00 30.49  ? 60  PRO B CD  1 
ATOM   2205 N N   . GLU B 1 18  ? -14.137 -39.720 -30.181 1.00 29.03  ? 61  GLU B N   1 
ATOM   2206 C CA  . GLU B 1 18  ? -13.237 -39.719 -29.035 1.00 31.49  ? 61  GLU B CA  1 
ATOM   2207 C C   . GLU B 1 18  ? -12.255 -38.556 -29.112 1.00 29.05  ? 61  GLU B C   1 
ATOM   2208 O O   . GLU B 1 18  ? -11.904 -37.959 -28.087 1.00 25.85  ? 61  GLU B O   1 
ATOM   2209 C CB  . GLU B 1 18  ? -12.493 -41.054 -28.951 1.00 30.49  ? 61  GLU B CB  1 
ATOM   2210 C CG  . GLU B 1 18  ? -13.392 -42.256 -28.670 1.00 32.79  ? 61  GLU B CG  1 
ATOM   2211 C CD  . GLU B 1 18  ? -14.093 -42.791 -29.914 1.00 38.98  ? 61  GLU B CD  1 
ATOM   2212 O OE1 . GLU B 1 18  ? -13.731 -42.378 -31.036 1.00 35.91  ? 61  GLU B OE1 1 
ATOM   2213 O OE2 . GLU B 1 18  ? -15.008 -43.631 -29.769 1.00 40.74  ? 61  GLU B OE2 1 
ATOM   2214 N N   . THR B 1 19  ? -11.795 -38.225 -30.321 1.00 29.46  ? 62  THR B N   1 
ATOM   2215 C CA  . THR B 1 19  ? -10.836 -37.137 -30.477 1.00 25.37  ? 62  THR B CA  1 
ATOM   2216 C C   . THR B 1 19  ? -11.455 -35.791 -30.116 1.00 26.99  ? 62  THR B C   1 
ATOM   2217 O O   . THR B 1 19  ? -10.826 -34.979 -29.427 1.00 26.51  ? 62  THR B O   1 
ATOM   2218 C CB  . THR B 1 19  ? -10.304 -37.118 -31.910 1.00 30.02  ? 62  THR B CB  1 
ATOM   2219 O OG1 . THR B 1 19  ? -9.645  -38.359 -32.190 1.00 29.36  ? 62  THR B OG1 1 
ATOM   2220 C CG2 . THR B 1 19  ? -9.328  -35.964 -32.108 1.00 29.05  ? 62  THR B CG2 1 
ATOM   2221 N N   . VAL B 1 20  ? -12.682 -35.531 -30.573 1.00 27.98  ? 63  VAL B N   1 
ATOM   2222 C CA  . VAL B 1 20  ? -13.339 -34.265 -30.251 1.00 27.38  ? 63  VAL B CA  1 
ATOM   2223 C C   . VAL B 1 20  ? -13.577 -34.160 -28.748 1.00 28.65  ? 63  VAL B C   1 
ATOM   2224 O O   . VAL B 1 20  ? -13.316 -33.121 -28.130 1.00 24.62  ? 63  VAL B O   1 
ATOM   2225 C CB  . VAL B 1 20  ? -14.652 -34.124 -31.042 1.00 26.63  ? 63  VAL B CB  1 
ATOM   2226 C CG1 . VAL B 1 20  ? -15.446 -32.920 -30.548 1.00 26.65  ? 63  VAL B CG1 1 
ATOM   2227 C CG2 . VAL B 1 20  ? -14.366 -34.001 -32.534 1.00 24.79  ? 63  VAL B CG2 1 
ATOM   2228 N N   . LEU B 1 21  ? -14.077 -35.238 -28.138 1.00 28.57  ? 64  LEU B N   1 
ATOM   2229 C CA  . LEU B 1 21  ? -14.315 -35.229 -26.697 1.00 29.85  ? 64  LEU B CA  1 
ATOM   2230 C C   . LEU B 1 21  ? -13.021 -34.986 -25.929 1.00 25.84  ? 64  LEU B C   1 
ATOM   2231 O O   . LEU B 1 21  ? -12.973 -34.151 -25.018 1.00 24.35  ? 64  LEU B O   1 
ATOM   2232 C CB  . LEU B 1 21  ? -14.951 -36.549 -26.262 1.00 31.06  ? 64  LEU B CB  1 
ATOM   2233 C CG  . LEU B 1 21  ? -16.420 -36.748 -26.633 1.00 33.16  ? 64  LEU B CG  1 
ATOM   2234 C CD1 . LEU B 1 21  ? -16.823 -38.202 -26.460 1.00 35.03  ? 64  LEU B CD1 1 
ATOM   2235 C CD2 . LEU B 1 21  ? -17.296 -35.845 -25.781 1.00 36.44  ? 64  LEU B CD2 1 
ATOM   2236 N N   . ALA B 1 22  ? -11.956 -35.703 -26.292 1.00 25.71  ? 65  ALA B N   1 
ATOM   2237 C CA  . ALA B 1 22  ? -10.687 -35.541 -25.590 1.00 27.79  ? 65  ALA B CA  1 
ATOM   2238 C C   . ALA B 1 22  ? -10.154 -34.124 -25.746 1.00 28.71  ? 65  ALA B C   1 
ATOM   2239 O O   . ALA B 1 22  ? -9.617  -33.546 -24.793 1.00 24.10  ? 65  ALA B O   1 
ATOM   2240 C CB  . ALA B 1 22  ? -9.666  -36.555 -26.104 1.00 23.64  ? 65  ALA B CB  1 
ATOM   2241 N N   . ARG B 1 23  ? -10.280 -33.553 -26.947 1.00 27.08  ? 66  ARG B N   1 
ATOM   2242 C CA  . ARG B 1 23  ? -9.810  -32.190 -27.176 1.00 27.75  ? 66  ARG B CA  1 
ATOM   2243 C C   . ARG B 1 23  ? -10.617 -31.178 -26.372 1.00 27.27  ? 66  ARG B C   1 
ATOM   2244 O O   . ARG B 1 23  ? -10.052 -30.225 -25.823 1.00 29.63  ? 66  ARG B O   1 
ATOM   2245 C CB  . ARG B 1 23  ? -9.870  -31.862 -28.666 1.00 26.80  ? 66  ARG B CB  1 
ATOM   2246 C CG  . ARG B 1 23  ? -8.778  -32.530 -29.483 1.00 27.21  ? 66  ARG B CG  1 
ATOM   2247 C CD  . ARG B 1 23  ? -8.872  -32.136 -30.944 1.00 28.96  ? 66  ARG B CD  1 
ATOM   2248 N NE  . ARG B 1 23  ? -7.780  -32.686 -31.737 1.00 27.96  ? 66  ARG B NE  1 
ATOM   2249 C CZ  . ARG B 1 23  ? -7.536  -32.358 -32.999 1.00 28.43  ? 66  ARG B CZ  1 
ATOM   2250 N NH1 . ARG B 1 23  ? -8.283  -31.473 -33.640 1.00 26.10  ? 66  ARG B NH1 1 
ATOM   2251 N NH2 . ARG B 1 23  ? -6.516  -32.929 -33.633 1.00 27.90  ? 66  ARG B NH2 1 
ATOM   2252 N N   . CYS B 1 24  ? -11.937 -31.356 -26.299 1.00 25.72  ? 67  CYS B N   1 
ATOM   2253 C CA  . CYS B 1 24  ? -12.763 -30.436 -25.524 1.00 26.92  ? 67  CYS B CA  1 
ATOM   2254 C C   . CYS B 1 24  ? -12.364 -30.448 -24.051 1.00 29.48  ? 67  CYS B C   1 
ATOM   2255 O O   . CYS B 1 24  ? -12.214 -29.392 -23.426 1.00 27.84  ? 67  CYS B O   1 
ATOM   2256 C CB  . CYS B 1 24  ? -14.240 -30.798 -25.687 1.00 28.59  ? 67  CYS B CB  1 
ATOM   2257 S SG  . CYS B 1 24  ? -15.380 -29.694 -24.820 1.00 33.96  ? 67  CYS B SG  1 
ATOM   2258 N N   . VAL B 1 25  ? -12.186 -31.642 -23.480 1.00 27.04  ? 68  VAL B N   1 
ATOM   2259 C CA  . VAL B 1 25  ? -11.787 -31.745 -22.079 1.00 27.81  ? 68  VAL B CA  1 
ATOM   2260 C C   . VAL B 1 25  ? -10.408 -31.134 -21.873 1.00 28.61  ? 68  VAL B C   1 
ATOM   2261 O O   . VAL B 1 25  ? -10.173 -30.399 -20.906 1.00 27.32  ? 68  VAL B O   1 
ATOM   2262 C CB  . VAL B 1 25  ? -11.827 -33.215 -21.623 1.00 28.13  ? 68  VAL B CB  1 
ATOM   2263 C CG1 . VAL B 1 25  ? -11.123 -33.381 -20.275 1.00 31.30  ? 68  VAL B CG1 1 
ATOM   2264 C CG2 . VAL B 1 25  ? -13.265 -33.706 -21.547 1.00 29.07  ? 68  VAL B CG2 1 
ATOM   2265 N N   . LYS B 1 26  ? -9.472  -31.430 -22.777 1.00 28.59  ? 69  LYS B N   1 
ATOM   2266 C CA  . LYS B 1 26  ? -8.121  -30.896 -22.647 1.00 27.13  ? 69  LYS B CA  1 
ATOM   2267 C C   . LYS B 1 26  ? -8.118  -29.375 -22.737 1.00 29.79  ? 69  LYS B C   1 
ATOM   2268 O O   . LYS B 1 26  ? -7.426  -28.703 -21.964 1.00 27.93  ? 69  LYS B O   1 
ATOM   2269 C CB  . LYS B 1 26  ? -7.218  -31.503 -23.722 1.00 32.33  ? 69  LYS B CB  1 
ATOM   2270 C CG  . LYS B 1 26  ? -5.769  -31.037 -23.675 1.00 34.62  ? 69  LYS B CG  1 
ATOM   2271 C CD  . LYS B 1 26  ? -5.035  -31.570 -22.452 1.00 46.23  ? 69  LYS B CD  1 
ATOM   2272 C CE  . LYS B 1 26  ? -3.614  -31.027 -22.386 1.00 52.31  ? 69  LYS B CE  1 
ATOM   2273 N NZ  . LYS B 1 26  ? -2.772  -31.744 -21.388 1.00 61.73  ? 69  LYS B NZ  1 
ATOM   2274 N N   . TYR B 1 27  ? -8.888  -28.812 -23.675 1.00 29.19  ? 70  TYR B N   1 
ATOM   2275 C CA  . TYR B 1 27  ? -8.878  -27.365 -23.864 1.00 26.54  ? 70  TYR B CA  1 
ATOM   2276 C C   . TYR B 1 27  ? -9.425  -26.641 -22.640 1.00 29.94  ? 70  TYR B C   1 
ATOM   2277 O O   . TYR B 1 27  ? -8.817  -25.685 -22.148 1.00 29.54  ? 70  TYR B O   1 
ATOM   2278 C CB  . TYR B 1 27  ? -9.682  -26.986 -25.107 1.00 28.09  ? 70  TYR B CB  1 
ATOM   2279 C CG  . TYR B 1 27  ? -9.579  -25.517 -25.460 1.00 27.42  ? 70  TYR B CG  1 
ATOM   2280 C CD1 . TYR B 1 27  ? -10.474 -24.590 -24.938 1.00 29.95  ? 70  TYR B CD1 1 
ATOM   2281 C CD2 . TYR B 1 27  ? -8.579  -25.055 -26.308 1.00 29.04  ? 70  TYR B CD2 1 
ATOM   2282 C CE1 . TYR B 1 27  ? -10.379 -23.243 -25.254 1.00 29.81  ? 70  TYR B CE1 1 
ATOM   2283 C CE2 . TYR B 1 27  ? -8.477  -23.709 -26.631 1.00 30.31  ? 70  TYR B CE2 1 
ATOM   2284 C CZ  . TYR B 1 27  ? -9.379  -22.809 -26.101 1.00 29.49  ? 70  TYR B CZ  1 
ATOM   2285 O OH  . TYR B 1 27  ? -9.281  -21.471 -26.418 1.00 30.05  ? 70  TYR B OH  1 
ATOM   2286 N N   . THR B 1 28  ? -10.587 -27.076 -22.142 1.00 28.41  ? 71  THR B N   1 
ATOM   2287 C CA  . THR B 1 28  ? -11.166 -26.436 -20.965 1.00 30.99  ? 71  THR B CA  1 
ATOM   2288 C C   . THR B 1 28  ? -10.310 -26.659 -19.724 1.00 31.43  ? 71  THR B C   1 
ATOM   2289 O O   . THR B 1 28  ? -10.359 -25.850 -18.792 1.00 34.16  ? 71  THR B O   1 
ATOM   2290 C CB  . THR B 1 28  ? -12.590 -26.944 -20.727 1.00 29.30  ? 71  THR B CB  1 
ATOM   2291 O OG1 . THR B 1 28  ? -12.585 -28.369 -20.574 1.00 31.71  ? 71  THR B OG1 1 
ATOM   2292 C CG2 . THR B 1 28  ? -13.499 -26.563 -21.894 1.00 26.60  ? 71  THR B CG2 1 
ATOM   2293 N N   . GLU B 1 29  ? -9.530  -27.744 -19.687 1.00 32.60  ? 72  GLU B N   1 
ATOM   2294 C CA  . GLU B 1 29  ? -8.568  -27.922 -18.604 1.00 33.77  ? 72  GLU B CA  1 
ATOM   2295 C C   . GLU B 1 29  ? -7.468  -26.869 -18.672 1.00 38.76  ? 72  GLU B C   1 
ATOM   2296 O O   . GLU B 1 29  ? -7.074  -26.304 -17.645 1.00 42.66  ? 72  GLU B O   1 
ATOM   2297 C CB  . GLU B 1 29  ? -7.972  -29.328 -18.667 1.00 33.49  ? 72  GLU B CB  1 
ATOM   2298 C CG  . GLU B 1 29  ? -7.013  -29.658 -17.538 1.00 39.46  ? 72  GLU B CG  1 
ATOM   2299 C CD  . GLU B 1 29  ? -6.490  -31.082 -17.615 1.00 42.15  ? 72  GLU B CD  1 
ATOM   2300 O OE1 . GLU B 1 29  ? -6.037  -31.499 -18.702 1.00 42.14  ? 72  GLU B OE1 1 
ATOM   2301 O OE2 . GLU B 1 29  ? -6.539  -31.789 -16.586 1.00 42.57  ? 72  GLU B OE2 1 
ATOM   2302 N N   . ILE B 1 30  ? -6.966  -26.590 -19.877 1.00 36.62  ? 73  ILE B N   1 
ATOM   2303 C CA  . ILE B 1 30  ? -5.901  -25.607 -20.038 1.00 42.09  ? 73  ILE B CA  1 
ATOM   2304 C C   . ILE B 1 30  ? -6.426  -24.185 -19.892 1.00 39.57  ? 73  ILE B C   1 
ATOM   2305 O O   . ILE B 1 30  ? -5.689  -23.291 -19.461 1.00 39.18  ? 73  ILE B O   1 
ATOM   2306 C CB  . ILE B 1 30  ? -5.209  -25.789 -21.402 1.00 40.47  ? 73  ILE B CB  1 
ATOM   2307 C CG1 . ILE B 1 30  ? -4.490  -27.135 -21.461 1.00 48.46  ? 73  ILE B CG1 1 
ATOM   2308 C CG2 . ILE B 1 30  ? -4.234  -24.642 -21.653 1.00 45.13  ? 73  ILE B CG2 1 
ATOM   2309 C CD1 . ILE B 1 30  ? -4.081  -27.538 -22.860 1.00 55.31  ? 73  ILE B CD1 1 
ATOM   2310 N N   . HIS B 1 31  ? -7.687  -23.941 -20.259 1.00 37.68  ? 74  HIS B N   1 
ATOM   2311 C CA  . HIS B 1 31  ? -8.259  -22.597 -20.302 1.00 38.16  ? 74  HIS B CA  1 
ATOM   2312 C C   . HIS B 1 31  ? -9.367  -22.490 -19.262 1.00 40.07  ? 74  HIS B C   1 
ATOM   2313 O O   . HIS B 1 31  ? -10.530 -22.811 -19.548 1.00 36.52  ? 74  HIS B O   1 
ATOM   2314 C CB  . HIS B 1 31  ? -8.793  -22.287 -21.704 1.00 34.99  ? 74  HIS B CB  1 
ATOM   2315 C CG  . HIS B 1 31  ? -7.734  -22.269 -22.763 1.00 35.10  ? 74  HIS B CG  1 
ATOM   2316 N ND1 . HIS B 1 31  ? -7.070  -21.119 -23.131 1.00 40.17  ? 74  HIS B ND1 1 
ATOM   2317 C CD2 . HIS B 1 31  ? -7.219  -23.261 -23.527 1.00 34.29  ? 74  HIS B CD2 1 
ATOM   2318 C CE1 . HIS B 1 31  ? -6.194  -21.402 -24.078 1.00 37.62  ? 74  HIS B CE1 1 
ATOM   2319 N NE2 . HIS B 1 31  ? -6.263  -22.696 -24.336 1.00 34.25  ? 74  HIS B NE2 1 
ATOM   2320 N N   . PRO B 1 32  ? -9.062  -22.035 -18.042 1.00 42.64  ? 75  PRO B N   1 
ATOM   2321 C CA  . PRO B 1 32  ? -10.107 -21.970 -17.007 1.00 42.86  ? 75  PRO B CA  1 
ATOM   2322 C C   . PRO B 1 32  ? -11.277 -21.082 -17.378 1.00 39.93  ? 75  PRO B C   1 
ATOM   2323 O O   . PRO B 1 32  ? -12.386 -21.289 -16.869 1.00 39.06  ? 75  PRO B O   1 
ATOM   2324 C CB  . PRO B 1 32  ? -9.353  -21.421 -15.785 1.00 48.84  ? 75  PRO B CB  1 
ATOM   2325 C CG  . PRO B 1 32  ? -7.926  -21.772 -16.024 1.00 50.53  ? 75  PRO B CG  1 
ATOM   2326 C CD  . PRO B 1 32  ? -7.734  -21.681 -17.510 1.00 48.54  ? 75  PRO B CD  1 
ATOM   2327 N N   . GLU B 1 33  ? -11.069 -20.094 -18.247 1.00 39.76  ? 76  GLU B N   1 
ATOM   2328 C CA  . GLU B 1 33  ? -12.145 -19.171 -18.584 1.00 39.67  ? 76  GLU B CA  1 
ATOM   2329 C C   . GLU B 1 33  ? -13.250 -19.830 -19.400 1.00 38.86  ? 76  GLU B C   1 
ATOM   2330 O O   . GLU B 1 33  ? -14.292 -19.201 -19.614 1.00 38.70  ? 76  GLU B O   1 
ATOM   2331 C CB  . GLU B 1 33  ? -11.584 -17.951 -19.330 1.00 39.00  ? 76  GLU B CB  1 
ATOM   2332 C CG  . GLU B 1 33  ? -11.115 -18.196 -20.762 1.00 41.09  ? 76  GLU B CG  1 
ATOM   2333 C CD  . GLU B 1 33  ? -9.773  -18.900 -20.841 1.00 42.25  ? 76  GLU B CD  1 
ATOM   2334 O OE1 . GLU B 1 33  ? -9.303  -19.412 -19.805 1.00 40.73  ? 76  GLU B OE1 1 
ATOM   2335 O OE2 . GLU B 1 33  ? -9.185  -18.939 -21.944 1.00 45.31  ? 76  GLU B OE2 1 
ATOM   2336 N N   . MET B 1 34  ? -13.055 -21.070 -19.855 1.00 34.08  ? 77  MET B N   1 
ATOM   2337 C CA  . MET B 1 34  ? -14.040 -21.776 -20.664 1.00 34.07  ? 77  MET B CA  1 
ATOM   2338 C C   . MET B 1 34  ? -14.663 -22.966 -19.943 1.00 33.81  ? 77  MET B C   1 
ATOM   2339 O O   . MET B 1 34  ? -15.349 -23.771 -20.581 1.00 31.14  ? 77  MET B O   1 
ATOM   2340 C CB  . MET B 1 34  ? -13.400 -22.249 -21.972 1.00 35.00  ? 77  MET B CB  1 
ATOM   2341 C CG  . MET B 1 34  ? -12.979 -21.124 -22.898 1.00 36.53  ? 77  MET B CG  1 
ATOM   2342 S SD  . MET B 1 34  ? -14.380 -20.152 -23.478 1.00 37.33  ? 77  MET B SD  1 
ATOM   2343 C CE  . MET B 1 34  ? -15.196 -21.316 -24.564 1.00 33.65  ? 77  MET B CE  1 
ATOM   2344 N N   . ARG B 1 35  ? -14.456 -23.096 -18.633 1.00 33.16  ? 78  ARG B N   1 
ATOM   2345 C CA  . ARG B 1 35  ? -14.917 -24.281 -17.919 1.00 34.51  ? 78  ARG B CA  1 
ATOM   2346 C C   . ARG B 1 35  ? -16.420 -24.292 -17.678 1.00 34.62  ? 78  ARG B C   1 
ATOM   2347 O O   . ARG B 1 35  ? -16.937 -25.288 -17.164 1.00 36.45  ? 78  ARG B O   1 
ATOM   2348 C CB  . ARG B 1 35  ? -14.178 -24.415 -16.590 1.00 37.91  ? 78  ARG B CB  1 
ATOM   2349 C CG  . ARG B 1 35  ? -12.743 -24.851 -16.773 1.00 38.00  ? 78  ARG B CG  1 
ATOM   2350 C CD  . ARG B 1 35  ? -12.123 -25.309 -15.476 1.00 39.86  ? 78  ARG B CD  1 
ATOM   2351 N NE  . ARG B 1 35  ? -10.785 -25.842 -15.693 1.00 40.15  ? 78  ARG B NE  1 
ATOM   2352 C CZ  . ARG B 1 35  ? -10.003 -26.316 -14.734 1.00 44.34  ? 78  ARG B CZ  1 
ATOM   2353 N NH1 . ARG B 1 35  ? -10.392 -26.332 -13.470 1.00 46.40  ? 78  ARG B NH1 1 
ATOM   2354 N NH2 . ARG B 1 35  ? -8.802  -26.787 -15.054 1.00 48.32  ? 78  ARG B NH2 1 
ATOM   2355 N N   . HIS B 1 36  ? -17.130 -23.219 -18.029 1.00 31.72  ? 79  HIS B N   1 
ATOM   2356 C CA  . HIS B 1 36  ? -18.585 -23.290 -18.076 1.00 35.14  ? 79  HIS B CA  1 
ATOM   2357 C C   . HIS B 1 36  ? -19.070 -24.257 -19.150 1.00 34.96  ? 79  HIS B C   1 
ATOM   2358 O O   . HIS B 1 36  ? -20.238 -24.660 -19.126 1.00 36.57  ? 79  HIS B O   1 
ATOM   2359 C CB  . HIS B 1 36  ? -19.169 -21.902 -18.337 1.00 31.12  ? 79  HIS B CB  1 
ATOM   2360 C CG  . HIS B 1 36  ? -18.746 -21.310 -19.645 1.00 34.11  ? 79  HIS B CG  1 
ATOM   2361 N ND1 . HIS B 1 36  ? -17.614 -20.535 -19.781 1.00 33.13  ? 79  HIS B ND1 1 
ATOM   2362 C CD2 . HIS B 1 36  ? -19.300 -21.386 -20.878 1.00 34.84  ? 79  HIS B CD2 1 
ATOM   2363 C CE1 . HIS B 1 36  ? -17.491 -20.156 -21.040 1.00 35.41  ? 79  HIS B CE1 1 
ATOM   2364 N NE2 . HIS B 1 36  ? -18.501 -20.660 -21.727 1.00 34.64  ? 79  HIS B NE2 1 
ATOM   2365 N N   . VAL B 1 37  ? -18.197 -24.641 -20.083 1.00 34.79  ? 80  VAL B N   1 
ATOM   2366 C CA  . VAL B 1 37  ? -18.598 -25.477 -21.209 1.00 36.14  ? 80  VAL B CA  1 
ATOM   2367 C C   . VAL B 1 37  ? -18.849 -26.902 -20.735 1.00 35.77  ? 80  VAL B C   1 
ATOM   2368 O O   . VAL B 1 37  ? -18.052 -27.474 -19.980 1.00 37.29  ? 80  VAL B O   1 
ATOM   2369 C CB  . VAL B 1 37  ? -17.523 -25.443 -22.307 1.00 33.49  ? 80  VAL B CB  1 
ATOM   2370 C CG1 . VAL B 1 37  ? -17.767 -26.540 -23.333 1.00 34.06  ? 80  VAL B CG1 1 
ATOM   2371 C CG2 . VAL B 1 37  ? -17.489 -24.077 -22.980 1.00 36.24  ? 80  VAL B CG2 1 
ATOM   2372 N N   . ASP B 1 38  ? -19.965 -27.479 -21.178 1.00 34.63  ? 81  ASP B N   1 
ATOM   2373 C CA  . ASP B 1 38  ? -20.270 -28.893 -20.984 1.00 36.04  ? 81  ASP B CA  1 
ATOM   2374 C C   . ASP B 1 38  ? -19.852 -29.629 -22.252 1.00 35.29  ? 81  ASP B C   1 
ATOM   2375 O O   . ASP B 1 38  ? -20.490 -29.483 -23.299 1.00 32.22  ? 81  ASP B O   1 
ATOM   2376 C CB  . ASP B 1 38  ? -21.755 -29.093 -20.690 1.00 36.75  ? 81  ASP B CB  1 
ATOM   2377 C CG  . ASP B 1 38  ? -22.144 -30.560 -20.608 1.00 42.69  ? 81  ASP B CG  1 
ATOM   2378 O OD1 . ASP B 1 38  ? -21.243 -31.416 -20.486 1.00 44.39  ? 81  ASP B OD1 1 
ATOM   2379 O OD2 . ASP B 1 38  ? -23.356 -30.859 -20.671 1.00 45.35  ? 81  ASP B OD2 1 
ATOM   2380 N N   . CYS B 1 39  ? -18.778 -30.417 -22.161 1.00 36.24  ? 82  CYS B N   1 
ATOM   2381 C CA  . CYS B 1 39  ? -18.225 -31.037 -23.361 1.00 36.29  ? 82  CYS B CA  1 
ATOM   2382 C C   . CYS B 1 39  ? -19.184 -32.051 -23.974 1.00 34.60  ? 82  CYS B C   1 
ATOM   2383 O O   . CYS B 1 39  ? -19.191 -32.226 -25.197 1.00 31.90  ? 82  CYS B O   1 
ATOM   2384 C CB  . CYS B 1 39  ? -16.876 -31.685 -23.045 1.00 37.95  ? 82  CYS B CB  1 
ATOM   2385 S SG  . CYS B 1 39  ? -15.509 -30.485 -22.944 1.00 45.85  ? 82  CYS B SG  1 
ATOM   2386 N N   . GLN B 1 40  ? -20.001 -32.724 -23.160 1.00 36.09  ? 83  GLN B N   1 
ATOM   2387 C CA  . GLN B 1 40  ? -21.021 -33.602 -23.722 1.00 36.15  ? 83  GLN B CA  1 
ATOM   2388 C C   . GLN B 1 40  ? -21.968 -32.819 -24.621 1.00 37.23  ? 83  GLN B C   1 
ATOM   2389 O O   . GLN B 1 40  ? -22.306 -33.259 -25.727 1.00 34.36  ? 83  GLN B O   1 
ATOM   2390 C CB  . GLN B 1 40  ? -21.805 -34.296 -22.609 1.00 38.33  ? 83  GLN B CB  1 
ATOM   2391 C CG  . GLN B 1 40  ? -23.087 -34.958 -23.099 1.00 41.31  ? 83  GLN B CG  1 
ATOM   2392 C CD  . GLN B 1 40  ? -23.748 -35.832 -22.052 1.00 43.77  ? 83  GLN B CD  1 
ATOM   2393 O OE1 . GLN B 1 40  ? -23.995 -35.395 -20.929 1.00 45.00  ? 83  GLN B OE1 1 
ATOM   2394 N NE2 . GLN B 1 40  ? -24.041 -37.076 -22.419 1.00 42.94  ? 83  GLN B NE2 1 
ATOM   2395 N N   . SER B 1 41  ? -22.413 -31.651 -24.155 1.00 33.71  ? 84  SER B N   1 
ATOM   2396 C CA  . SER B 1 41  ? -23.293 -30.817 -24.965 1.00 35.09  ? 84  SER B CA  1 
ATOM   2397 C C   . SER B 1 41  ? -22.584 -30.342 -26.226 1.00 32.83  ? 84  SER B C   1 
ATOM   2398 O O   . SER B 1 41  ? -23.194 -30.262 -27.299 1.00 29.76  ? 84  SER B O   1 
ATOM   2399 C CB  . SER B 1 41  ? -23.789 -29.628 -24.142 1.00 35.49  ? 84  SER B CB  1 
ATOM   2400 O OG  . SER B 1 41  ? -24.520 -30.066 -23.008 1.00 37.41  ? 84  SER B OG  1 
ATOM   2401 N N   . VAL B 1 42  ? -21.292 -30.023 -26.117 1.00 30.93  ? 85  VAL B N   1 
ATOM   2402 C CA  . VAL B 1 42  ? -20.536 -29.572 -27.282 1.00 33.16  ? 85  VAL B CA  1 
ATOM   2403 C C   . VAL B 1 42  ? -20.488 -30.670 -28.338 1.00 30.69  ? 85  VAL B C   1 
ATOM   2404 O O   . VAL B 1 42  ? -20.765 -30.432 -29.520 1.00 28.54  ? 85  VAL B O   1 
ATOM   2405 C CB  . VAL B 1 42  ? -19.120 -29.130 -26.868 1.00 30.62  ? 85  VAL B CB  1 
ATOM   2406 C CG1 . VAL B 1 42  ? -18.273 -28.835 -28.100 1.00 30.56  ? 85  VAL B CG1 1 
ATOM   2407 C CG2 . VAL B 1 42  ? -19.191 -27.916 -25.962 1.00 33.23  ? 85  VAL B CG2 1 
ATOM   2408 N N   . TRP B 1 43  ? -20.137 -31.891 -27.929 1.00 29.42  ? 86  TRP B N   1 
ATOM   2409 C CA  . TRP B 1 43  ? -20.102 -32.993 -28.884 1.00 32.51  ? 86  TRP B CA  1 
ATOM   2410 C C   . TRP B 1 43  ? -21.484 -33.256 -29.465 1.00 33.15  ? 86  TRP B C   1 
ATOM   2411 O O   . TRP B 1 43  ? -21.632 -33.454 -30.677 1.00 31.95  ? 86  TRP B O   1 
ATOM   2412 C CB  . TRP B 1 43  ? -19.555 -34.257 -28.220 1.00 35.24  ? 86  TRP B CB  1 
ATOM   2413 C CG  . TRP B 1 43  ? -19.731 -35.474 -29.067 1.00 35.14  ? 86  TRP B CG  1 
ATOM   2414 C CD1 . TRP B 1 43  ? -20.394 -36.616 -28.733 1.00 37.60  ? 86  TRP B CD1 1 
ATOM   2415 C CD2 . TRP B 1 43  ? -19.253 -35.663 -30.404 1.00 33.00  ? 86  TRP B CD2 1 
ATOM   2416 N NE1 . TRP B 1 43  ? -20.354 -37.510 -29.776 1.00 36.52  ? 86  TRP B NE1 1 
ATOM   2417 C CE2 . TRP B 1 43  ? -19.659 -36.948 -30.814 1.00 33.97  ? 86  TRP B CE2 1 
ATOM   2418 C CE3 . TRP B 1 43  ? -18.519 -34.872 -31.292 1.00 30.68  ? 86  TRP B CE3 1 
ATOM   2419 C CZ2 . TRP B 1 43  ? -19.357 -37.460 -32.073 1.00 32.88  ? 86  TRP B CZ2 1 
ATOM   2420 C CZ3 . TRP B 1 43  ? -18.218 -35.383 -32.540 1.00 32.20  ? 86  TRP B CZ3 1 
ATOM   2421 C CH2 . TRP B 1 43  ? -18.637 -36.665 -32.919 1.00 30.62  ? 86  TRP B CH2 1 
ATOM   2422 N N   . ASP B 1 44  ? -22.512 -33.246 -28.615 1.00 32.67  ? 87  ASP B N   1 
ATOM   2423 C CA  . ASP B 1 44  ? -23.869 -33.485 -29.095 1.00 37.03  ? 87  ASP B CA  1 
ATOM   2424 C C   . ASP B 1 44  ? -24.275 -32.444 -30.132 1.00 35.10  ? 87  ASP B C   1 
ATOM   2425 O O   . ASP B 1 44  ? -24.887 -32.780 -31.152 1.00 34.61  ? 87  ASP B O   1 
ATOM   2426 C CB  . ASP B 1 44  ? -24.841 -33.484 -27.915 1.00 39.66  ? 87  ASP B CB  1 
ATOM   2427 C CG  . ASP B 1 44  ? -26.148 -34.177 -28.236 1.00 50.40  ? 87  ASP B CG  1 
ATOM   2428 O OD1 . ASP B 1 44  ? -26.146 -35.419 -28.367 1.00 56.44  ? 87  ASP B OD1 1 
ATOM   2429 O OD2 . ASP B 1 44  ? -27.179 -33.482 -28.354 1.00 54.59  ? 87  ASP B OD2 1 
ATOM   2430 N N   . ALA B 1 45  ? -23.948 -31.171 -29.888 1.00 33.04  ? 88  ALA B N   1 
ATOM   2431 C CA  . ALA B 1 45  ? -24.259 -30.128 -30.861 1.00 32.27  ? 88  ALA B CA  1 
ATOM   2432 C C   . ALA B 1 45  ? -23.400 -30.263 -32.113 1.00 30.75  ? 88  ALA B C   1 
ATOM   2433 O O   . ALA B 1 45  ? -23.872 -30.009 -33.227 1.00 30.39  ? 88  ALA B O   1 
ATOM   2434 C CB  . ALA B 1 45  ? -24.069 -28.748 -30.232 1.00 32.91  ? 88  ALA B CB  1 
ATOM   2435 N N   . PHE B 1 46  ? -22.127 -30.628 -31.946 1.00 30.86  ? 89  PHE B N   1 
ATOM   2436 C CA  . PHE B 1 46  ? -21.269 -30.887 -33.098 1.00 28.50  ? 89  PHE B CA  1 
ATOM   2437 C C   . PHE B 1 46  ? -21.829 -32.035 -33.927 1.00 33.29  ? 89  PHE B C   1 
ATOM   2438 O O   . PHE B 1 46  ? -22.009 -31.915 -35.145 1.00 27.70  ? 89  PHE B O   1 
ATOM   2439 C CB  . PHE B 1 46  ? -19.853 -31.209 -32.615 1.00 28.26  ? 89  PHE B CB  1 
ATOM   2440 C CG  . PHE B 1 46  ? -18.775 -31.006 -33.652 1.00 26.63  ? 89  PHE B CG  1 
ATOM   2441 C CD1 . PHE B 1 46  ? -19.047 -31.084 -35.009 1.00 30.03  ? 89  PHE B CD1 1 
ATOM   2442 C CD2 . PHE B 1 46  ? -17.476 -30.738 -33.254 1.00 24.43  ? 89  PHE B CD2 1 
ATOM   2443 C CE1 . PHE B 1 46  ? -18.043 -30.896 -35.943 1.00 27.35  ? 89  PHE B CE1 1 
ATOM   2444 C CE2 . PHE B 1 46  ? -16.471 -30.551 -34.183 1.00 28.59  ? 89  PHE B CE2 1 
ATOM   2445 C CZ  . PHE B 1 46  ? -16.754 -30.631 -35.528 1.00 28.33  ? 89  PHE B CZ  1 
ATOM   2446 N N   . LYS B 1 47  ? -22.136 -33.151 -33.266 1.00 32.42  ? 90  LYS B N   1 
ATOM   2447 C CA  . LYS B 1 47  ? -22.679 -34.314 -33.955 1.00 33.65  ? 90  LYS B CA  1 
ATOM   2448 C C   . LYS B 1 47  ? -23.988 -33.975 -34.655 1.00 35.35  ? 90  LYS B C   1 
ATOM   2449 O O   . LYS B 1 47  ? -24.205 -34.365 -35.808 1.00 31.59  ? 90  LYS B O   1 
ATOM   2450 C CB  . LYS B 1 47  ? -22.873 -35.447 -32.944 1.00 35.49  ? 90  LYS B CB  1 
ATOM   2451 C CG  . LYS B 1 47  ? -23.234 -36.788 -33.538 1.00 44.47  ? 90  LYS B CG  1 
ATOM   2452 C CD  . LYS B 1 47  ? -23.161 -37.905 -32.499 1.00 45.58  ? 90  LYS B CD  1 
ATOM   2453 C CE  . LYS B 1 47  ? -23.981 -37.584 -31.257 1.00 47.09  ? 90  LYS B CE  1 
ATOM   2454 N NZ  . LYS B 1 47  ? -24.485 -38.816 -30.588 1.00 58.46  ? 90  LYS B NZ  1 
ATOM   2455 N N   . GLY B 1 48  ? -24.863 -33.225 -33.984 1.00 34.26  ? 91  GLY B N   1 
ATOM   2456 C CA  . GLY B 1 48  ? -26.152 -32.878 -34.556 1.00 33.76  ? 91  GLY B CA  1 
ATOM   2457 C C   . GLY B 1 48  ? -26.075 -32.011 -35.797 1.00 32.66  ? 91  GLY B C   1 
ATOM   2458 O O   . GLY B 1 48  ? -27.086 -31.872 -36.497 1.00 28.76  ? 91  GLY B O   1 
ATOM   2459 N N   . ALA B 1 49  ? -24.911 -31.428 -36.090 1.00 32.82  ? 92  ALA B N   1 
ATOM   2460 C CA  . ALA B 1 49  ? -24.797 -30.556 -37.253 1.00 31.00  ? 92  ALA B CA  1 
ATOM   2461 C C   . ALA B 1 49  ? -24.810 -31.338 -38.563 1.00 31.30  ? 92  ALA B C   1 
ATOM   2462 O O   . ALA B 1 49  ? -25.266 -30.813 -39.585 1.00 27.54  ? 92  ALA B O   1 
ATOM   2463 C CB  . ALA B 1 49  ? -23.521 -29.718 -37.160 1.00 28.51  ? 92  ALA B CB  1 
ATOM   2464 N N   . PHE B 1 50  ? -24.311 -32.579 -38.564 1.00 28.31  ? 93  PHE B N   1 
ATOM   2465 C CA  . PHE B 1 50  ? -24.124 -33.323 -39.805 1.00 29.29  ? 93  PHE B CA  1 
ATOM   2466 C C   . PHE B 1 50  ? -24.639 -34.759 -39.791 1.00 30.56  ? 93  PHE B C   1 
ATOM   2467 O O   . PHE B 1 50  ? -24.886 -35.302 -40.874 1.00 28.63  ? 93  PHE B O   1 
ATOM   2468 C CB  . PHE B 1 50  ? -22.634 -33.348 -40.189 1.00 26.66  ? 93  PHE B CB  1 
ATOM   2469 C CG  . PHE B 1 50  ? -21.773 -34.127 -39.234 1.00 28.70  ? 93  PHE B CG  1 
ATOM   2470 C CD1 . PHE B 1 50  ? -21.318 -33.553 -38.058 1.00 30.48  ? 93  PHE B CD1 1 
ATOM   2471 C CD2 . PHE B 1 50  ? -21.413 -35.430 -39.516 1.00 28.50  ? 93  PHE B CD2 1 
ATOM   2472 C CE1 . PHE B 1 50  ? -20.525 -34.272 -37.183 1.00 29.23  ? 93  PHE B CE1 1 
ATOM   2473 C CE2 . PHE B 1 50  ? -20.622 -36.151 -38.647 1.00 28.72  ? 93  PHE B CE2 1 
ATOM   2474 C CZ  . PHE B 1 50  ? -20.178 -35.571 -37.478 1.00 31.43  ? 93  PHE B CZ  1 
ATOM   2475 N N   . ILE B 1 51  ? -24.801 -35.399 -38.630 1.00 30.15  ? 94  ILE B N   1 
ATOM   2476 C CA  A ILE B 1 51  ? -25.315 -36.763 -38.620 0.25 31.86  ? 94  ILE B CA  1 
ATOM   2477 C CA  B ILE B 1 51  ? -25.325 -36.760 -38.596 0.75 31.77  ? 94  ILE B CA  1 
ATOM   2478 C C   . ILE B 1 51  ? -26.769 -36.759 -39.075 1.00 31.36  ? 94  ILE B C   1 
ATOM   2479 O O   . ILE B 1 51  ? -27.532 -35.820 -38.807 1.00 32.73  ? 94  ILE B O   1 
ATOM   2480 C CB  A ILE B 1 51  ? -25.172 -37.416 -37.232 0.25 33.03  ? 94  ILE B CB  1 
ATOM   2481 C CB  B ILE B 1 51  ? -25.208 -37.345 -37.177 0.75 32.82  ? 94  ILE B CB  1 
ATOM   2482 C CG1 A ILE B 1 51  ? -26.012 -36.679 -36.184 0.25 32.92  ? 94  ILE B CG1 1 
ATOM   2483 C CG1 B ILE B 1 51  ? -23.762 -37.755 -36.875 0.75 34.60  ? 94  ILE B CG1 1 
ATOM   2484 C CG2 A ILE B 1 51  ? -23.705 -37.473 -36.824 0.25 33.94  ? 94  ILE B CG2 1 
ATOM   2485 C CG2 B ILE B 1 51  ? -26.138 -38.540 -37.002 0.75 33.77  ? 94  ILE B CG2 1 
ATOM   2486 C CD1 A ILE B 1 51  ? -27.463 -37.118 -36.116 0.25 33.14  ? 94  ILE B CD1 1 
ATOM   2487 C CD1 B ILE B 1 51  ? -23.256 -38.934 -37.698 0.75 32.69  ? 94  ILE B CD1 1 
ATOM   2488 N N   . SER B 1 52  ? -27.158 -37.817 -39.785 1.00 31.98  ? 95  SER B N   1 
ATOM   2489 C CA  . SER B 1 52  ? -28.504 -37.995 -40.318 1.00 35.50  ? 95  SER B CA  1 
ATOM   2490 C C   . SER B 1 52  ? -28.839 -36.985 -41.408 1.00 33.41  ? 95  SER B C   1 
ATOM   2491 O O   . SER B 1 52  ? -30.015 -36.839 -41.768 1.00 32.26  ? 95  SER B O   1 
ATOM   2492 C CB  . SER B 1 52  ? -29.558 -37.909 -39.207 1.00 37.47  ? 95  SER B CB  1 
ATOM   2493 O OG  . SER B 1 52  ? -30.799 -38.446 -39.629 1.00 47.87  ? 95  SER B OG  1 
ATOM   2494 N N   . LYS B 1 53  ? -27.840 -36.289 -41.950 1.00 29.77  ? 96  LYS B N   1 
ATOM   2495 C CA  . LYS B 1 53  ? -28.044 -35.274 -42.972 1.00 31.51  ? 96  LYS B CA  1 
ATOM   2496 C C   . LYS B 1 53  ? -27.186 -35.596 -44.186 1.00 30.15  ? 96  LYS B C   1 
ATOM   2497 O O   . LYS B 1 53  ? -26.065 -36.094 -44.051 1.00 28.75  ? 96  LYS B O   1 
ATOM   2498 C CB  . LYS B 1 53  ? -27.699 -33.875 -42.440 1.00 32.01  ? 96  LYS B CB  1 
ATOM   2499 C CG  . LYS B 1 53  ? -28.622 -33.391 -41.333 1.00 30.97  ? 96  LYS B CG  1 
ATOM   2500 C CD  . LYS B 1 53  ? -28.090 -32.130 -40.666 1.00 33.98  ? 96  LYS B CD  1 
ATOM   2501 C CE  . LYS B 1 53  ? -29.013 -31.671 -39.548 1.00 32.54  ? 96  LYS B CE  1 
ATOM   2502 N NZ  . LYS B 1 53  ? -28.451 -30.527 -38.785 1.00 33.23  ? 96  LYS B NZ  1 
ATOM   2503 N N   . HIS B 1 54  ? -27.722 -35.317 -45.368 1.00 30.94  ? 97  HIS B N   1 
ATOM   2504 C CA  . HIS B 1 54  ? -26.956 -35.510 -46.591 1.00 29.90  ? 97  HIS B CA  1 
ATOM   2505 C C   . HIS B 1 54  ? -25.727 -34.605 -46.561 1.00 29.77  ? 97  HIS B C   1 
ATOM   2506 O O   . HIS B 1 54  ? -25.862 -33.393 -46.345 1.00 26.66  ? 97  HIS B O   1 
ATOM   2507 C CB  . HIS B 1 54  ? -27.822 -35.200 -47.811 1.00 33.11  ? 97  HIS B CB  1 
ATOM   2508 C CG  . HIS B 1 54  ? -27.182 -35.563 -49.115 1.00 32.75  ? 97  HIS B CG  1 
ATOM   2509 N ND1 . HIS B 1 54  ? -26.747 -36.839 -49.402 1.00 32.66  ? 97  HIS B ND1 1 
ATOM   2510 C CD2 . HIS B 1 54  ? -26.908 -34.817 -50.211 1.00 35.48  ? 97  HIS B CD2 1 
ATOM   2511 C CE1 . HIS B 1 54  ? -26.228 -36.862 -50.617 1.00 31.62  ? 97  HIS B CE1 1 
ATOM   2512 N NE2 . HIS B 1 54  ? -26.315 -35.648 -51.130 1.00 33.97  ? 97  HIS B NE2 1 
ATOM   2513 N N   . PRO B 1 55  ? -24.517 -35.141 -46.783 1.00 30.72  ? 98  PRO B N   1 
ATOM   2514 C CA  . PRO B 1 55  ? -23.309 -34.325 -46.591 1.00 31.01  ? 98  PRO B CA  1 
ATOM   2515 C C   . PRO B 1 55  ? -22.996 -33.388 -47.748 1.00 32.17  ? 98  PRO B C   1 
ATOM   2516 O O   . PRO B 1 55  ? -21.852 -32.945 -47.888 1.00 31.16  ? 98  PRO B O   1 
ATOM   2517 C CB  . PRO B 1 55  ? -22.206 -35.376 -46.410 1.00 30.85  ? 98  PRO B CB  1 
ATOM   2518 C CG  . PRO B 1 55  ? -22.686 -36.552 -47.191 1.00 29.12  ? 98  PRO B CG  1 
ATOM   2519 C CD  . PRO B 1 55  ? -24.190 -36.550 -47.077 1.00 31.00  ? 98  PRO B CD  1 
ATOM   2520 N N   . CYS B 1 56  ? -23.979 -33.101 -48.602 1.00 31.11  ? 99  CYS B N   1 
ATOM   2521 C CA  . CYS B 1 56  ? -23.828 -32.076 -49.626 1.00 32.26  ? 99  CYS B CA  1 
ATOM   2522 C C   . CYS B 1 56  ? -24.802 -30.917 -49.457 1.00 35.41  ? 99  CYS B C   1 
ATOM   2523 O O   . CYS B 1 56  ? -24.823 -30.017 -50.307 1.00 35.34  ? 99  CYS B O   1 
ATOM   2524 C CB  . CYS B 1 56  ? -23.997 -32.683 -51.026 1.00 36.27  ? 99  CYS B CB  1 
ATOM   2525 S SG  . CYS B 1 56  ? -22.576 -33.651 -51.606 1.00 37.14  ? 99  CYS B SG  1 
ATOM   2526 N N   . ASP B 1 57  ? -25.600 -30.902 -48.387 1.00 32.04  ? 100 ASP B N   1 
ATOM   2527 C CA  . ASP B 1 57  ? -26.580 -29.846 -48.155 1.00 33.83  ? 100 ASP B CA  1 
ATOM   2528 C C   . ASP B 1 57  ? -26.409 -29.221 -46.774 1.00 31.06  ? 100 ASP B C   1 
ATOM   2529 O O   . ASP B 1 57  ? -27.363 -28.677 -46.211 1.00 31.54  ? 100 ASP B O   1 
ATOM   2530 C CB  . ASP B 1 57  ? -28.001 -30.384 -48.327 1.00 34.10  ? 100 ASP B CB  1 
ATOM   2531 C CG  . ASP B 1 57  ? -28.275 -30.863 -49.743 1.00 36.60  ? 100 ASP B CG  1 
ATOM   2532 O OD1 . ASP B 1 57  ? -28.017 -30.097 -50.695 1.00 38.39  ? 100 ASP B OD1 1 
ATOM   2533 O OD2 . ASP B 1 57  ? -28.738 -32.010 -49.905 1.00 34.66  ? 100 ASP B OD2 1 
ATOM   2534 N N   . ILE B 1 58  ? -25.200 -29.280 -46.216 1.00 28.40  ? 101 ILE B N   1 
ATOM   2535 C CA  . ILE B 1 58  ? -24.956 -28.698 -44.901 1.00 29.27  ? 101 ILE B CA  1 
ATOM   2536 C C   . ILE B 1 58  ? -24.964 -27.179 -45.003 1.00 30.13  ? 101 ILE B C   1 
ATOM   2537 O O   . ILE B 1 58  ? -24.436 -26.596 -45.961 1.00 30.04  ? 101 ILE B O   1 
ATOM   2538 C CB  . ILE B 1 58  ? -23.624 -29.204 -44.323 1.00 28.26  ? 101 ILE B CB  1 
ATOM   2539 C CG1 . ILE B 1 58  ? -23.573 -30.736 -44.351 1.00 32.23  ? 101 ILE B CG1 1 
ATOM   2540 C CG2 . ILE B 1 58  ? -23.431 -28.683 -42.903 1.00 29.15  ? 101 ILE B CG2 1 
ATOM   2541 C CD1 . ILE B 1 58  ? -24.706 -31.416 -43.606 1.00 28.62  ? 101 ILE B CD1 1 
ATOM   2542 N N   . THR B 1 59  ? -25.563 -26.527 -44.010 1.00 30.70  ? 102 THR B N   1 
ATOM   2543 C CA  . THR B 1 59  ? -25.687 -25.079 -43.977 1.00 31.87  ? 102 THR B CA  1 
ATOM   2544 C C   . THR B 1 59  ? -25.017 -24.520 -42.729 1.00 35.29  ? 102 THR B C   1 
ATOM   2545 O O   . THR B 1 59  ? -24.683 -25.244 -41.787 1.00 31.25  ? 102 THR B O   1 
ATOM   2546 C CB  . THR B 1 59  ? -27.157 -24.642 -43.997 1.00 34.39  ? 102 THR B CB  1 
ATOM   2547 O OG1 . THR B 1 59  ? -27.810 -25.126 -42.815 1.00 34.21  ? 102 THR B OG1 1 
ATOM   2548 C CG2 . THR B 1 59  ? -27.864 -25.180 -45.235 1.00 29.13  ? 102 THR B CG2 1 
ATOM   2549 N N   . GLU B 1 60  ? -24.834 -23.199 -42.734 1.00 35.41  ? 103 GLU B N   1 
ATOM   2550 C CA  . GLU B 1 60  ? -24.307 -22.525 -41.554 1.00 36.33  ? 103 GLU B CA  1 
ATOM   2551 C C   . GLU B 1 60  ? -25.252 -22.689 -40.370 1.00 31.01  ? 103 GLU B C   1 
ATOM   2552 O O   . GLU B 1 60  ? -24.806 -22.840 -39.227 1.00 29.84  ? 103 GLU B O   1 
ATOM   2553 C CB  . GLU B 1 60  ? -24.066 -21.050 -41.875 1.00 40.55  ? 103 GLU B CB  1 
ATOM   2554 C CG  . GLU B 1 60  ? -23.082 -20.843 -43.021 1.00 44.40  ? 103 GLU B CG  1 
ATOM   2555 C CD  . GLU B 1 60  ? -22.954 -19.393 -43.439 1.00 54.94  ? 103 GLU B CD  1 
ATOM   2556 O OE1 . GLU B 1 60  ? -23.893 -18.609 -43.184 1.00 59.81  ? 103 GLU B OE1 1 
ATOM   2557 O OE2 . GLU B 1 60  ? -21.908 -19.038 -44.023 1.00 52.66  ? 103 GLU B OE2 1 
ATOM   2558 N N   . GLU B 1 61  ? -26.562 -22.690 -40.627 1.00 31.02  ? 104 GLU B N   1 
ATOM   2559 C CA  . GLU B 1 61  ? -27.528 -22.863 -39.546 1.00 35.09  ? 104 GLU B CA  1 
ATOM   2560 C C   . GLU B 1 61  ? -27.400 -24.228 -38.877 1.00 35.10  ? 104 GLU B C   1 
ATOM   2561 O O   . GLU B 1 61  ? -27.728 -24.368 -37.693 1.00 32.29  ? 104 GLU B O   1 
ATOM   2562 C CB  . GLU B 1 61  ? -28.948 -22.667 -40.077 1.00 36.70  ? 104 GLU B CB  1 
ATOM   2563 C CG  . GLU B 1 61  ? -30.032 -22.987 -39.061 1.00 46.95  ? 104 GLU B CG  1 
ATOM   2564 C CD  . GLU B 1 61  ? -31.382 -22.408 -39.443 1.00 61.78  ? 104 GLU B CD  1 
ATOM   2565 O OE1 . GLU B 1 61  ? -31.673 -22.315 -40.654 1.00 60.72  ? 104 GLU B OE1 1 
ATOM   2566 O OE2 . GLU B 1 61  ? -32.149 -22.037 -38.529 1.00 69.01  ? 104 GLU B OE2 1 
ATOM   2567 N N   . ASP B 1 62  ? -26.945 -25.249 -39.611 1.00 34.38  ? 105 ASP B N   1 
ATOM   2568 C CA  . ASP B 1 62  ? -26.742 -26.554 -38.988 1.00 33.89  ? 105 ASP B CA  1 
ATOM   2569 C C   . ASP B 1 62  ? -25.742 -26.472 -37.843 1.00 31.67  ? 105 ASP B C   1 
ATOM   2570 O O   . ASP B 1 62  ? -25.852 -27.221 -36.866 1.00 30.22  ? 105 ASP B O   1 
ATOM   2571 C CB  . ASP B 1 62  ? -26.262 -27.572 -40.024 1.00 32.34  ? 105 ASP B CB  1 
ATOM   2572 C CG  . ASP B 1 62  ? -27.363 -27.998 -40.980 1.00 34.51  ? 105 ASP B CG  1 
ATOM   2573 O OD1 . ASP B 1 62  ? -28.506 -28.207 -40.523 1.00 35.67  ? 105 ASP B OD1 1 
ATOM   2574 O OD2 . ASP B 1 62  ? -27.083 -28.123 -42.190 1.00 31.79  ? 105 ASP B OD2 1 
ATOM   2575 N N   . TYR B 1 63  ? -24.767 -25.573 -37.943 1.00 30.34  ? 106 TYR B N   1 
ATOM   2576 C CA  . TYR B 1 63  ? -23.718 -25.444 -36.944 1.00 30.99  ? 106 TYR B CA  1 
ATOM   2577 C C   . TYR B 1 63  ? -24.020 -24.399 -35.877 1.00 31.80  ? 106 TYR B C   1 
ATOM   2578 O O   . TYR B 1 63  ? -23.218 -24.237 -34.952 1.00 32.36  ? 106 TYR B O   1 
ATOM   2579 C CB  . TYR B 1 63  ? -22.391 -25.099 -37.628 1.00 29.91  ? 106 TYR B CB  1 
ATOM   2580 C CG  . TYR B 1 63  ? -21.708 -26.285 -38.267 1.00 30.15  ? 106 TYR B CG  1 
ATOM   2581 C CD1 . TYR B 1 63  ? -21.101 -27.259 -37.487 1.00 29.98  ? 106 TYR B CD1 1 
ATOM   2582 C CD2 . TYR B 1 63  ? -21.665 -26.431 -39.648 1.00 28.27  ? 106 TYR B CD2 1 
ATOM   2583 C CE1 . TYR B 1 63  ? -20.475 -28.347 -38.060 1.00 26.29  ? 106 TYR B CE1 1 
ATOM   2584 C CE2 . TYR B 1 63  ? -21.039 -27.516 -40.230 1.00 27.59  ? 106 TYR B CE2 1 
ATOM   2585 C CZ  . TYR B 1 63  ? -20.446 -28.470 -39.430 1.00 25.24  ? 106 TYR B CZ  1 
ATOM   2586 O OH  . TYR B 1 63  ? -19.819 -29.551 -40.005 1.00 27.06  ? 106 TYR B OH  1 
ATOM   2587 N N   . GLN B 1 64  ? -25.147 -23.695 -35.970 1.00 31.88  ? 107 GLN B N   1 
ATOM   2588 C CA  . GLN B 1 64  ? -25.423 -22.636 -35.004 1.00 32.92  ? 107 GLN B CA  1 
ATOM   2589 C C   . GLN B 1 64  ? -25.458 -23.138 -33.565 1.00 32.94  ? 107 GLN B C   1 
ATOM   2590 O O   . GLN B 1 64  ? -24.880 -22.464 -32.694 1.00 30.85  ? 107 GLN B O   1 
ATOM   2591 C CB  . GLN B 1 64  ? -26.736 -21.932 -35.370 1.00 33.12  ? 107 GLN B CB  1 
ATOM   2592 C CG  . GLN B 1 64  ? -27.113 -20.792 -34.433 1.00 41.21  ? 107 GLN B CG  1 
ATOM   2593 C CD  . GLN B 1 64  ? -26.034 -19.724 -34.333 1.00 48.49  ? 107 GLN B CD  1 
ATOM   2594 O OE1 . GLN B 1 64  ? -25.762 -19.201 -33.250 1.00 50.15  ? 107 GLN B OE1 1 
ATOM   2595 N NE2 . GLN B 1 64  ? -25.419 -19.391 -35.463 1.00 47.42  ? 107 GLN B NE2 1 
ATOM   2596 N N   . PRO B 1 65  ? -26.097 -24.267 -33.238 1.00 29.04  ? 108 PRO B N   1 
ATOM   2597 C CA  . PRO B 1 65  ? -26.041 -24.740 -31.843 1.00 29.75  ? 108 PRO B CA  1 
ATOM   2598 C C   . PRO B 1 65  ? -24.625 -24.939 -31.333 1.00 28.50  ? 108 PRO B C   1 
ATOM   2599 O O   . PRO B 1 65  ? -24.343 -24.642 -30.166 1.00 30.50  ? 108 PRO B O   1 
ATOM   2600 C CB  . PRO B 1 65  ? -26.820 -26.061 -31.891 1.00 30.61  ? 108 PRO B CB  1 
ATOM   2601 C CG  . PRO B 1 65  ? -27.738 -25.916 -33.061 1.00 34.58  ? 108 PRO B CG  1 
ATOM   2602 C CD  . PRO B 1 65  ? -26.986 -25.097 -34.071 1.00 31.96  ? 108 PRO B CD  1 
ATOM   2603 N N   . LEU B 1 66  ? -23.723 -25.446 -32.176 1.00 26.77  ? 109 LEU B N   1 
ATOM   2604 C CA  . LEU B 1 66  ? -22.321 -25.544 -31.784 1.00 27.77  ? 109 LEU B CA  1 
ATOM   2605 C C   . LEU B 1 66  ? -21.698 -24.162 -31.627 1.00 31.29  ? 109 LEU B C   1 
ATOM   2606 O O   . LEU B 1 66  ? -20.935 -23.923 -30.682 1.00 28.22  ? 109 LEU B O   1 
ATOM   2607 C CB  . LEU B 1 66  ? -21.550 -26.371 -32.812 1.00 26.91  ? 109 LEU B CB  1 
ATOM   2608 C CG  . LEU B 1 66  ? -20.048 -26.535 -32.571 1.00 25.90  ? 109 LEU B CG  1 
ATOM   2609 C CD1 . LEU B 1 66  ? -19.777 -27.336 -31.302 1.00 26.98  ? 109 LEU B CD1 1 
ATOM   2610 C CD2 . LEU B 1 66  ? -19.390 -27.190 -33.775 1.00 25.10  ? 109 LEU B CD2 1 
ATOM   2611 N N   . MET B 1 67  ? -22.017 -23.237 -32.539 1.00 29.70  ? 110 MET B N   1 
ATOM   2612 C CA  . MET B 1 67  ? -21.478 -21.884 -32.442 1.00 29.91  ? 110 MET B CA  1 
ATOM   2613 C C   . MET B 1 67  ? -21.868 -21.235 -31.121 1.00 31.08  ? 110 MET B C   1 
ATOM   2614 O O   . MET B 1 67  ? -21.040 -20.587 -30.470 1.00 30.84  ? 110 MET B O   1 
ATOM   2615 C CB  . MET B 1 67  ? -21.978 -21.027 -33.608 1.00 36.03  ? 110 MET B CB  1 
ATOM   2616 C CG  . MET B 1 67  ? -21.527 -21.471 -34.991 1.00 38.24  ? 110 MET B CG  1 
ATOM   2617 S SD  . MET B 1 67  ? -19.738 -21.448 -35.196 1.00 39.94  ? 110 MET B SD  1 
ATOM   2618 C CE  . MET B 1 67  ? -19.391 -23.203 -35.279 1.00 35.83  ? 110 MET B CE  1 
ATOM   2619 N N   . LYS B 1 68  ? -23.130 -21.394 -30.712 1.00 30.25  ? 111 LYS B N   1 
ATOM   2620 C CA  . LYS B 1 68  ? -23.592 -20.786 -29.469 1.00 29.68  ? 111 LYS B CA  1 
ATOM   2621 C C   . LYS B 1 68  ? -22.853 -21.363 -28.267 1.00 29.74  ? 111 LYS B C   1 
ATOM   2622 O O   . LYS B 1 68  ? -22.372 -20.620 -27.405 1.00 29.94  ? 111 LYS B O   1 
ATOM   2623 C CB  . LYS B 1 68  ? -25.100 -20.988 -29.312 1.00 31.81  ? 111 LYS B CB  1 
ATOM   2624 C CG  . LYS B 1 68  ? -25.944 -20.261 -30.345 1.00 42.05  ? 111 LYS B CG  1 
ATOM   2625 C CD  . LYS B 1 68  ? -27.309 -19.899 -29.771 1.00 56.64  ? 111 LYS B CD  1 
ATOM   2626 C CE  . LYS B 1 68  ? -28.228 -19.308 -30.826 1.00 54.45  ? 111 LYS B CE  1 
ATOM   2627 N NZ  . LYS B 1 68  ? -28.783 -20.352 -31.723 1.00 47.73  ? 111 LYS B NZ  1 
ATOM   2628 N N   . LEU B 1 69  ? -22.752 -22.694 -28.193 1.00 29.82  ? 112 LEU B N   1 
ATOM   2629 C CA  . LEU B 1 69  ? -22.055 -23.315 -27.071 1.00 30.49  ? 112 LEU B CA  1 
ATOM   2630 C C   . LEU B 1 69  ? -20.579 -22.942 -27.056 1.00 30.06  ? 112 LEU B C   1 
ATOM   2631 O O   . LEU B 1 69  ? -19.982 -22.814 -25.981 1.00 30.29  ? 112 LEU B O   1 
ATOM   2632 C CB  . LEU B 1 69  ? -22.208 -24.836 -27.123 1.00 30.39  ? 112 LEU B CB  1 
ATOM   2633 C CG  . LEU B 1 69  ? -23.618 -25.393 -26.914 1.00 34.27  ? 112 LEU B CG  1 
ATOM   2634 C CD1 . LEU B 1 69  ? -23.616 -26.910 -27.049 1.00 36.45  ? 112 LEU B CD1 1 
ATOM   2635 C CD2 . LEU B 1 69  ? -24.172 -24.976 -25.558 1.00 36.46  ? 112 LEU B CD2 1 
ATOM   2636 N N   . GLY B 1 70  ? -19.976 -22.768 -28.227 1.00 26.89  ? 113 GLY B N   1 
ATOM   2637 C CA  . GLY B 1 70  ? -18.573 -22.441 -28.341 1.00 30.99  ? 113 GLY B CA  1 
ATOM   2638 C C   . GLY B 1 70  ? -18.240 -20.969 -28.241 1.00 32.46  ? 113 GLY B C   1 
ATOM   2639 O O   . GLY B 1 70  ? -17.092 -20.593 -28.504 1.00 30.07  ? 113 GLY B O   1 
ATOM   2640 N N   . THR B 1 71  ? -19.200 -20.121 -27.869 1.00 30.48  ? 114 THR B N   1 
ATOM   2641 C CA  . THR B 1 71  ? -18.939 -18.689 -27.782 1.00 33.82  ? 114 THR B CA  1 
ATOM   2642 C C   . THR B 1 71  ? -17.713 -18.433 -26.918 1.00 33.55  ? 114 THR B C   1 
ATOM   2643 O O   . THR B 1 71  ? -17.593 -18.965 -25.811 1.00 34.31  ? 114 THR B O   1 
ATOM   2644 C CB  . THR B 1 71  ? -20.150 -17.955 -27.202 1.00 34.41  ? 114 THR B CB  1 
ATOM   2645 O OG1 . THR B 1 71  ? -21.293 -18.169 -28.037 1.00 35.31  ? 114 THR B OG1 1 
ATOM   2646 C CG2 . THR B 1 71  ? -19.872 -16.459 -27.109 1.00 39.87  ? 114 THR B CG2 1 
ATOM   2647 N N   . GLN B 1 72  ? -16.798 -17.620 -27.438 1.00 31.11  ? 115 GLN B N   1 
ATOM   2648 C CA  . GLN B 1 72  ? -15.541 -17.337 -26.762 1.00 36.39  ? 115 GLN B CA  1 
ATOM   2649 C C   . GLN B 1 72  ? -15.072 -15.948 -27.162 1.00 38.73  ? 115 GLN B C   1 
ATOM   2650 O O   . GLN B 1 72  ? -14.990 -15.638 -28.354 1.00 37.02  ? 115 GLN B O   1 
ATOM   2651 C CB  . GLN B 1 72  ? -14.480 -18.383 -27.116 1.00 32.05  ? 115 GLN B CB  1 
ATOM   2652 C CG  . GLN B 1 72  ? -13.182 -18.238 -26.345 1.00 32.56  ? 115 GLN B CG  1 
ATOM   2653 C CD  . GLN B 1 72  ? -12.223 -19.382 -26.607 1.00 30.08  ? 115 GLN B CD  1 
ATOM   2654 O OE1 . GLN B 1 72  ? -12.471 -20.230 -27.464 1.00 29.52  ? 115 GLN B OE1 1 
ATOM   2655 N NE2 . GLN B 1 72  ? -11.120 -19.413 -25.867 1.00 31.84  ? 115 GLN B NE2 1 
ATOM   2656 N N   . THR B 1 73  ? -14.762 -15.122 -26.169 1.00 40.44  ? 116 THR B N   1 
ATOM   2657 C CA  . THR B 1 73  ? -14.295 -13.761 -26.397 1.00 45.29  ? 116 THR B CA  1 
ATOM   2658 C C   . THR B 1 73  ? -12.771 -13.764 -26.372 1.00 43.56  ? 116 THR B C   1 
ATOM   2659 O O   . THR B 1 73  ? -12.161 -13.987 -25.321 1.00 48.15  ? 116 THR B O   1 
ATOM   2660 C CB  . THR B 1 73  ? -14.858 -12.806 -25.347 1.00 50.34  ? 116 THR B CB  1 
ATOM   2661 O OG1 . THR B 1 73  ? -16.290 -12.818 -25.403 1.00 53.55  ? 116 THR B OG1 1 
ATOM   2662 C CG2 . THR B 1 73  ? -14.355 -11.388 -25.590 1.00 50.91  ? 116 THR B CG2 1 
ATOM   2663 N N   . VAL B 1 74  ? -12.162 -13.529 -27.529 1.00 40.37  ? 117 VAL B N   1 
ATOM   2664 C CA  . VAL B 1 74  ? -10.717 -13.340 -27.626 1.00 41.83  ? 117 VAL B CA  1 
ATOM   2665 C C   . VAL B 1 74  ? -10.473 -11.845 -27.801 1.00 43.35  ? 117 VAL B C   1 
ATOM   2666 O O   . VAL B 1 74  ? -11.287 -11.163 -28.442 1.00 42.28  ? 117 VAL B O   1 
ATOM   2667 C CB  . VAL B 1 74  ? -10.117 -14.149 -28.786 1.00 40.17  ? 117 VAL B CB  1 
ATOM   2668 C CG1 . VAL B 1 74  ? -10.497 -15.620 -28.666 1.00 42.92  ? 117 VAL B CG1 1 
ATOM   2669 C CG2 . VAL B 1 74  ? -10.570 -13.583 -30.122 1.00 39.10  ? 117 VAL B CG2 1 
ATOM   2670 N N   . PRO B 1 75  ? -9.385  -11.285 -27.255 1.00 42.15  ? 118 PRO B N   1 
ATOM   2671 C CA  . PRO B 1 75  ? -9.125  -9.850  -27.452 1.00 38.50  ? 118 PRO B CA  1 
ATOM   2672 C C   . PRO B 1 75  ? -9.103  -9.489  -28.928 1.00 37.21  ? 118 PRO B C   1 
ATOM   2673 O O   . PRO B 1 75  ? -8.226  -9.948  -29.669 1.00 34.83  ? 118 PRO B O   1 
ATOM   2674 C CB  . PRO B 1 75  ? -7.756  -9.643  -26.793 1.00 40.82  ? 118 PRO B CB  1 
ATOM   2675 C CG  . PRO B 1 75  ? -7.620  -10.778 -25.824 1.00 42.77  ? 118 PRO B CG  1 
ATOM   2676 C CD  . PRO B 1 75  ? -8.337  -11.935 -26.447 1.00 42.12  ? 118 PRO B CD  1 
ATOM   2677 N N   . CYS B 1 76  ? -10.055 -8.659  -29.365 1.00 36.86  ? 119 CYS B N   1 
ATOM   2678 C CA  . CYS B 1 76  ? -10.280 -8.483  -30.795 1.00 32.80  ? 119 CYS B CA  1 
ATOM   2679 C C   . CYS B 1 76  ? -9.091  -7.855  -31.508 1.00 31.52  ? 119 CYS B C   1 
ATOM   2680 O O   . CYS B 1 76  ? -8.979  -7.995  -32.731 1.00 29.13  ? 119 CYS B O   1 
ATOM   2681 C CB  . CYS B 1 76  ? -11.532 -7.638  -31.042 1.00 33.03  ? 119 CYS B CB  1 
ATOM   2682 S SG  . CYS B 1 76  ? -11.538 -5.966  -30.344 1.00 45.40  ? 119 CYS B SG  1 
ATOM   2683 N N   . ASN B 1 77  ? -8.199  -7.178  -30.787 1.00 30.08  ? 120 ASN B N   1 
ATOM   2684 C CA  . ASN B 1 77  ? -7.042  -6.549  -31.410 1.00 32.83  ? 120 ASN B CA  1 
ATOM   2685 C C   . ASN B 1 77  ? -5.813  -7.451  -31.414 1.00 32.13  ? 120 ASN B C   1 
ATOM   2686 O O   . ASN B 1 77  ? -4.727  -6.997  -31.788 1.00 32.41  ? 120 ASN B O   1 
ATOM   2687 C CB  . ASN B 1 77  ? -6.719  -5.219  -30.717 1.00 30.55  ? 120 ASN B CB  1 
ATOM   2688 C CG  . ASN B 1 77  ? -6.316  -5.393  -29.266 1.00 31.36  ? 120 ASN B CG  1 
ATOM   2689 O OD1 . ASN B 1 77  ? -6.904  -6.190  -28.536 1.00 33.52  ? 120 ASN B OD1 1 
ATOM   2690 N ND2 . ASN B 1 77  ? -5.309  -4.639  -28.839 1.00 32.00  ? 120 ASN B ND2 1 
ATOM   2691 N N   . LYS B 1 78  ? -5.962  -8.716  -31.029 1.00 32.75  ? 121 LYS B N   1 
ATOM   2692 C CA  . LYS B 1 78  ? -4.856  -9.659  -30.927 1.00 35.31  ? 121 LYS B CA  1 
ATOM   2693 C C   . LYS B 1 78  ? -5.115  -10.908 -31.765 1.00 34.95  ? 121 LYS B C   1 
ATOM   2694 O O   . LYS B 1 78  ? -4.793  -12.028 -31.359 1.00 35.34  ? 121 LYS B O   1 
ATOM   2695 C CB  . LYS B 1 78  ? -4.612  -10.046 -29.470 1.00 38.99  ? 121 LYS B CB  1 
ATOM   2696 C CG  . LYS B 1 78  ? -4.521  -8.869  -28.508 1.00 40.56  ? 121 LYS B CG  1 
ATOM   2697 C CD  . LYS B 1 78  ? -3.373  -7.927  -28.847 1.00 46.63  ? 121 LYS B CD  1 
ATOM   2698 C CE  . LYS B 1 78  ? -2.023  -8.615  -28.725 1.00 51.10  ? 121 LYS B CE  1 
ATOM   2699 N NZ  . LYS B 1 78  ? -0.894  -7.648  -28.822 1.00 58.64  ? 121 LYS B NZ  1 
ATOM   2700 N N   . ILE B 1 79  ? -5.691  -10.736 -32.951 1.00 29.69  ? 122 ILE B N   1 
ATOM   2701 C CA  . ILE B 1 79  ? -6.075  -11.857 -33.803 1.00 31.99  ? 122 ILE B CA  1 
ATOM   2702 C C   . ILE B 1 79  ? -5.056  -12.019 -34.921 1.00 30.59  ? 122 ILE B C   1 
ATOM   2703 O O   . ILE B 1 79  ? -4.630  -11.037 -35.543 1.00 30.17  ? 122 ILE B O   1 
ATOM   2704 C CB  . ILE B 1 79  ? -7.496  -11.665 -34.369 1.00 32.29  ? 122 ILE B CB  1 
ATOM   2705 C CG1 . ILE B 1 79  ? -8.528  -11.965 -33.277 1.00 32.54  ? 122 ILE B CG1 1 
ATOM   2706 C CG2 . ILE B 1 79  ? -7.703  -12.550 -35.597 1.00 29.54  ? 122 ILE B CG2 1 
ATOM   2707 C CD1 . ILE B 1 79  ? -9.971  -11.750 -33.707 1.00 36.30  ? 122 ILE B CD1 1 
ATOM   2708 N N   . LEU B 1 80  ? -4.655  -13.267 -35.166 1.00 30.37  ? 123 LEU B N   1 
ATOM   2709 C CA  . LEU B 1 80  ? -3.698  -13.611 -36.212 1.00 30.62  ? 123 LEU B CA  1 
ATOM   2710 C C   . LEU B 1 80  ? -4.346  -14.576 -37.195 1.00 30.70  ? 123 LEU B C   1 
ATOM   2711 O O   . LEU B 1 80  ? -4.712  -15.697 -36.821 1.00 28.76  ? 123 LEU B O   1 
ATOM   2712 C CB  . LEU B 1 80  ? -2.434  -14.233 -35.612 1.00 30.84  ? 123 LEU B CB  1 
ATOM   2713 C CG  . LEU B 1 80  ? -1.449  -14.838 -36.615 1.00 31.91  ? 123 LEU B CG  1 
ATOM   2714 C CD1 . LEU B 1 80  ? -0.926  -13.768 -37.562 1.00 33.22  ? 123 LEU B CD1 1 
ATOM   2715 C CD2 . LEU B 1 80  ? -0.301  -15.533 -35.894 1.00 32.47  ? 123 LEU B CD2 1 
ATOM   2716 N N   . LEU B 1 81  ? -4.472  -14.145 -38.445 1.00 26.80  ? 124 LEU B N   1 
ATOM   2717 C CA  . LEU B 1 81  ? -4.891  -14.994 -39.549 1.00 25.32  ? 124 LEU B CA  1 
ATOM   2718 C C   . LEU B 1 81  ? -3.663  -15.584 -40.240 1.00 26.93  ? 124 LEU B C   1 
ATOM   2719 O O   . LEU B 1 81  ? -2.538  -15.116 -40.057 1.00 28.26  ? 124 LEU B O   1 
ATOM   2720 C CB  . LEU B 1 81  ? -5.725  -14.191 -40.551 1.00 29.04  ? 124 LEU B CB  1 
ATOM   2721 C CG  . LEU B 1 81  ? -6.864  -13.347 -39.970 1.00 26.97  ? 124 LEU B CG  1 
ATOM   2722 C CD1 . LEU B 1 81  ? -7.429  -12.393 -41.017 1.00 26.63  ? 124 LEU B CD1 1 
ATOM   2723 C CD2 . LEU B 1 81  ? -7.966  -14.235 -39.414 1.00 28.26  ? 124 LEU B CD2 1 
ATOM   2724 N N   . TRP B 1 82  ? -3.887  -16.625 -41.043 1.00 28.35  ? 125 TRP B N   1 
ATOM   2725 C CA  . TRP B 1 82  ? -2.786  -17.228 -41.784 1.00 31.89  ? 125 TRP B CA  1 
ATOM   2726 C C   . TRP B 1 82  ? -3.293  -17.834 -43.083 1.00 31.03  ? 125 TRP B C   1 
ATOM   2727 O O   . TRP B 1 82  ? -4.479  -18.140 -43.231 1.00 28.25  ? 125 TRP B O   1 
ATOM   2728 C CB  . TRP B 1 82  ? -2.047  -18.296 -40.958 1.00 29.19  ? 125 TRP B CB  1 
ATOM   2729 C CG  . TRP B 1 82  ? -2.898  -19.430 -40.435 1.00 33.70  ? 125 TRP B CG  1 
ATOM   2730 C CD1 . TRP B 1 82  ? -3.347  -19.590 -39.156 1.00 31.29  ? 125 TRP B CD1 1 
ATOM   2731 C CD2 . TRP B 1 82  ? -3.376  -20.568 -41.170 1.00 32.35  ? 125 TRP B CD2 1 
ATOM   2732 N NE1 . TRP B 1 82  ? -4.083  -20.745 -39.051 1.00 30.50  ? 125 TRP B NE1 1 
ATOM   2733 C CE2 . TRP B 1 82  ? -4.113  -21.364 -40.272 1.00 30.74  ? 125 TRP B CE2 1 
ATOM   2734 C CE3 . TRP B 1 82  ? -3.255  -20.986 -42.498 1.00 34.02  ? 125 TRP B CE3 1 
ATOM   2735 C CZ2 . TRP B 1 82  ? -4.730  -22.550 -40.660 1.00 34.22  ? 125 TRP B CZ2 1 
ATOM   2736 C CZ3 . TRP B 1 82  ? -3.868  -22.166 -42.881 1.00 34.91  ? 125 TRP B CZ3 1 
ATOM   2737 C CH2 . TRP B 1 82  ? -4.596  -22.934 -41.966 1.00 34.39  ? 125 TRP B CH2 1 
ATOM   2738 N N   . SER B 1 83  ? -2.364  -18.005 -44.026 1.00 34.59  ? 126 SER B N   1 
ATOM   2739 C CA  . SER B 1 83  ? -2.644  -18.628 -45.319 1.00 36.08  ? 126 SER B CA  1 
ATOM   2740 C C   . SER B 1 83  ? -1.522  -19.610 -45.632 1.00 38.39  ? 126 SER B C   1 
ATOM   2741 O O   . SER B 1 83  ? -0.386  -19.200 -45.886 1.00 39.74  ? 126 SER B O   1 
ATOM   2742 C CB  . SER B 1 83  ? -2.773  -17.583 -46.428 1.00 37.43  ? 126 SER B CB  1 
ATOM   2743 O OG  . SER B 1 83  ? -2.890  -18.204 -47.697 1.00 43.74  ? 126 SER B OG  1 
ATOM   2744 N N   . ARG B 1 84  ? -1.842  -20.901 -45.571 1.00 44.14  ? 127 ARG B N   1 
ATOM   2745 C CA  . ARG B 1 84  ? -0.976  -22.028 -45.898 1.00 46.91  ? 127 ARG B CA  1 
ATOM   2746 C C   . ARG B 1 84  ? 0.156   -22.275 -44.912 1.00 46.99  ? 127 ARG B C   1 
ATOM   2747 O O   . ARG B 1 84  ? 0.606   -23.416 -44.764 1.00 51.31  ? 127 ARG B O   1 
ATOM   2748 C CB  . ARG B 1 84  ? -0.285  -21.830 -47.254 1.00 54.19  ? 127 ARG B CB  1 
ATOM   2749 C CG  . ARG B 1 84  ? -1.097  -22.074 -48.492 1.00 62.01  ? 127 ARG B CG  1 
ATOM   2750 C CD  . ARG B 1 84  ? -0.146  -22.243 -49.671 1.00 71.31  ? 127 ARG B CD  1 
ATOM   2751 N NE  . ARG B 1 84  ? 0.720   -21.083 -49.864 1.00 76.96  ? 127 ARG B NE  1 
ATOM   2752 C CZ  . ARG B 1 84  ? 0.398   -20.020 -50.590 1.00 74.56  ? 127 ARG B CZ  1 
ATOM   2753 N NH1 . ARG B 1 84  ? -0.774  -19.925 -51.196 1.00 66.56  ? 127 ARG B NH1 1 
ATOM   2754 N NH2 . ARG B 1 84  ? 1.275   -19.026 -50.710 1.00 71.67  ? 127 ARG B NH2 1 
ATOM   2755 N N   . ILE B 1 85  ? 0.593   -21.246 -44.193 1.00 44.58  ? 128 ILE B N   1 
ATOM   2756 C CA  . ILE B 1 85  ? 1.676   -21.445 -43.238 1.00 47.03  ? 128 ILE B CA  1 
ATOM   2757 C C   . ILE B 1 85  ? 1.046   -21.555 -41.859 1.00 44.30  ? 128 ILE B C   1 
ATOM   2758 O O   . ILE B 1 85  ? 1.187   -20.661 -41.018 1.00 46.40  ? 128 ILE B O   1 
ATOM   2759 C CB  . ILE B 1 85  ? 2.720   -20.316 -43.353 1.00 48.05  ? 128 ILE B CB  1 
ATOM   2760 C CG1 . ILE B 1 85  ? 3.975   -20.664 -42.552 1.00 53.05  ? 128 ILE B CG1 1 
ATOM   2761 C CG2 . ILE B 1 85  ? 2.144   -18.968 -42.937 1.00 45.44  ? 128 ILE B CG2 1 
ATOM   2762 C CD1 . ILE B 1 85  ? 5.129   -19.719 -42.806 1.00 60.20  ? 128 ILE B CD1 1 
ATOM   2763 N N   . LYS B 1 86  ? 0.409   -22.692 -41.593 1.00 42.43  ? 129 LYS B N   1 
ATOM   2764 C CA  . LYS B 1 86  ? -0.306  -22.852 -40.336 1.00 40.84  ? 129 LYS B CA  1 
ATOM   2765 C C   . LYS B 1 86  ? 0.648   -23.186 -39.202 1.00 45.08  ? 129 LYS B C   1 
ATOM   2766 O O   . LYS B 1 86  ? 0.430   -22.764 -38.060 1.00 42.28  ? 129 LYS B O   1 
ATOM   2767 C CB  . LYS B 1 86  ? -1.371  -23.941 -40.475 1.00 41.60  ? 129 LYS B CB  1 
ATOM   2768 C CG  . LYS B 1 86  ? -2.125  -24.218 -39.188 1.00 45.32  ? 129 LYS B CG  1 
ATOM   2769 C CD  . LYS B 1 86  ? -3.249  -25.215 -39.402 1.00 40.48  ? 129 LYS B CD  1 
ATOM   2770 C CE  . LYS B 1 86  ? -2.737  -26.639 -39.429 1.00 45.42  ? 129 LYS B CE  1 
ATOM   2771 N NZ  . LYS B 1 86  ? -3.846  -27.607 -39.640 1.00 46.02  ? 129 LYS B NZ  1 
ATOM   2772 N N   . ASP B 1 87  ? 1.707   -23.935 -39.502 1.00 44.99  ? 130 ASP B N   1 
ATOM   2773 C CA  . ASP B 1 87  ? 2.612   -24.396 -38.457 1.00 49.07  ? 130 ASP B CA  1 
ATOM   2774 C C   . ASP B 1 87  ? 3.332   -23.228 -37.793 1.00 46.96  ? 130 ASP B C   1 
ATOM   2775 O O   . ASP B 1 87  ? 3.385   -23.139 -36.562 1.00 46.19  ? 130 ASP B O   1 
ATOM   2776 C CB  . ASP B 1 87  ? 3.607   -25.394 -39.048 1.00 54.37  ? 130 ASP B CB  1 
ATOM   2777 C CG  . ASP B 1 87  ? 2.956   -26.719 -39.404 1.00 64.10  ? 130 ASP B CG  1 
ATOM   2778 O OD1 . ASP B 1 87  ? 2.063   -27.164 -38.651 1.00 63.63  ? 130 ASP B OD1 1 
ATOM   2779 O OD2 . ASP B 1 87  ? 3.330   -27.313 -40.437 1.00 65.89  ? 130 ASP B OD2 1 
ATOM   2780 N N   . LEU B 1 88  ? 3.886   -22.314 -38.592 1.00 45.49  ? 131 LEU B N   1 
ATOM   2781 C CA  . LEU B 1 88  ? 4.597   -21.180 -38.009 1.00 43.37  ? 131 LEU B CA  1 
ATOM   2782 C C   . LEU B 1 88  ? 3.644   -20.263 -37.251 1.00 43.23  ? 131 LEU B C   1 
ATOM   2783 O O   . LEU B 1 88  ? 4.009   -19.703 -36.211 1.00 45.15  ? 131 LEU B O   1 
ATOM   2784 C CB  . LEU B 1 88  ? 5.338   -20.398 -39.093 1.00 44.39  ? 131 LEU B CB  1 
ATOM   2785 C CG  . LEU B 1 88  ? 6.153   -19.204 -38.585 1.00 51.93  ? 131 LEU B CG  1 
ATOM   2786 C CD1 . LEU B 1 88  ? 7.276   -19.661 -37.664 1.00 51.76  ? 131 LEU B CD1 1 
ATOM   2787 C CD2 . LEU B 1 88  ? 6.703   -18.390 -39.747 1.00 52.36  ? 131 LEU B CD2 1 
ATOM   2788 N N   . ALA B 1 89  ? 2.422   -20.091 -37.760 1.00 42.55  ? 132 ALA B N   1 
ATOM   2789 C CA  . ALA B 1 89  ? 1.454   -19.248 -37.067 1.00 39.33  ? 132 ALA B CA  1 
ATOM   2790 C C   . ALA B 1 89  ? 1.165   -19.782 -35.670 1.00 39.89  ? 132 ALA B C   1 
ATOM   2791 O O   . ALA B 1 89  ? 1.015   -19.007 -34.719 1.00 36.91  ? 132 ALA B O   1 
ATOM   2792 C CB  . ALA B 1 89  ? 0.166   -19.150 -37.884 1.00 34.50  ? 132 ALA B CB  1 
ATOM   2793 N N   . HIS B 1 90  ? 1.076   -21.107 -35.529 1.00 38.85  ? 133 HIS B N   1 
ATOM   2794 C CA  . HIS B 1 90  ? 0.841   -21.697 -34.215 1.00 41.58  ? 133 HIS B CA  1 
ATOM   2795 C C   . HIS B 1 90  ? 2.095   -21.653 -33.350 1.00 40.04  ? 133 HIS B C   1 
ATOM   2796 O O   . HIS B 1 90  ? 2.007   -21.445 -32.135 1.00 39.46  ? 133 HIS B O   1 
ATOM   2797 C CB  . HIS B 1 90  ? 0.343   -23.131 -34.371 1.00 39.20  ? 133 HIS B CB  1 
ATOM   2798 C CG  . HIS B 1 90  ? -0.995  -23.229 -35.033 1.00 45.42  ? 133 HIS B CG  1 
ATOM   2799 N ND1 . HIS B 1 90  ? -1.580  -24.434 -35.359 1.00 48.63  ? 133 HIS B ND1 1 
ATOM   2800 C CD2 . HIS B 1 90  ? -1.864  -22.269 -35.428 1.00 41.60  ? 133 HIS B CD2 1 
ATOM   2801 C CE1 . HIS B 1 90  ? -2.752  -24.211 -35.928 1.00 42.55  ? 133 HIS B CE1 1 
ATOM   2802 N NE2 . HIS B 1 90  ? -2.948  -22.906 -35.983 1.00 41.55  ? 133 HIS B NE2 1 
ATOM   2803 N N   . GLN B 1 91  ? 3.271   -21.852 -33.952 1.00 42.66  ? 134 GLN B N   1 
ATOM   2804 C CA  . GLN B 1 91  ? 4.513   -21.673 -33.210 1.00 44.36  ? 134 GLN B CA  1 
ATOM   2805 C C   . GLN B 1 91  ? 4.627   -20.250 -32.683 1.00 44.92  ? 134 GLN B C   1 
ATOM   2806 O O   . GLN B 1 91  ? 5.101   -20.027 -31.563 1.00 45.64  ? 134 GLN B O   1 
ATOM   2807 C CB  . GLN B 1 91  ? 5.712   -22.004 -34.098 1.00 48.57  ? 134 GLN B CB  1 
ATOM   2808 C CG  . GLN B 1 91  ? 5.795   -23.458 -34.525 1.00 55.02  ? 134 GLN B CG  1 
ATOM   2809 C CD  . GLN B 1 91  ? 6.850   -23.688 -35.590 1.00 61.05  ? 134 GLN B CD  1 
ATOM   2810 O OE1 . GLN B 1 91  ? 8.009   -23.304 -35.426 1.00 63.92  ? 134 GLN B OE1 1 
ATOM   2811 N NE2 . GLN B 1 91  ? 6.451   -24.309 -36.694 1.00 62.29  ? 134 GLN B NE2 1 
ATOM   2812 N N   . PHE B 1 92  ? 4.201   -19.272 -33.482 1.00 42.62  ? 135 PHE B N   1 
ATOM   2813 C CA  . PHE B 1 92  ? 4.270   -17.883 -33.048 1.00 41.61  ? 135 PHE B CA  1 
ATOM   2814 C C   . PHE B 1 92  ? 3.402   -17.647 -31.818 1.00 42.60  ? 135 PHE B C   1 
ATOM   2815 O O   . PHE B 1 92  ? 3.856   -17.062 -30.828 1.00 44.27  ? 135 PHE B O   1 
ATOM   2816 C CB  . PHE B 1 92  ? 3.842   -16.957 -34.187 1.00 42.86  ? 135 PHE B CB  1 
ATOM   2817 C CG  . PHE B 1 92  ? 3.740   -15.518 -33.780 1.00 42.98  ? 135 PHE B CG  1 
ATOM   2818 C CD1 . PHE B 1 92  ? 4.862   -14.708 -33.775 1.00 45.92  ? 135 PHE B CD1 1 
ATOM   2819 C CD2 . PHE B 1 92  ? 2.527   -14.978 -33.389 1.00 39.75  ? 135 PHE B CD2 1 
ATOM   2820 C CE1 . PHE B 1 92  ? 4.774   -13.386 -33.395 1.00 46.43  ? 135 PHE B CE1 1 
ATOM   2821 C CE2 . PHE B 1 92  ? 2.435   -13.656 -33.006 1.00 40.53  ? 135 PHE B CE2 1 
ATOM   2822 C CZ  . PHE B 1 92  ? 3.559   -12.859 -33.009 1.00 40.86  ? 135 PHE B CZ  1 
ATOM   2823 N N   . THR B 1 93  ? 2.145   -18.099 -31.860 1.00 38.52  ? 136 THR B N   1 
ATOM   2824 C CA  . THR B 1 93  ? 1.237   -17.823 -30.751 1.00 38.66  ? 136 THR B CA  1 
ATOM   2825 C C   . THR B 1 93  ? 1.611   -18.616 -29.506 1.00 42.97  ? 136 THR B C   1 
ATOM   2826 O O   . THR B 1 93  ? 1.288   -18.198 -28.388 1.00 43.32  ? 136 THR B O   1 
ATOM   2827 C CB  . THR B 1 93  ? -0.208  -18.122 -31.155 1.00 35.60  ? 136 THR B CB  1 
ATOM   2828 O OG1 . THR B 1 93  ? -0.318  -19.479 -31.600 1.00 33.54  ? 136 THR B OG1 1 
ATOM   2829 C CG2 . THR B 1 93  ? -0.660  -17.178 -32.269 1.00 36.44  ? 136 THR B CG2 1 
ATOM   2830 N N   . GLN B 1 94  ? 2.288   -19.756 -29.671 1.00 44.33  ? 137 GLN B N   1 
ATOM   2831 C CA  . GLN B 1 94  ? 2.766   -20.494 -28.507 1.00 49.84  ? 137 GLN B CA  1 
ATOM   2832 C C   . GLN B 1 94  ? 3.804   -19.694 -27.732 1.00 51.58  ? 137 GLN B C   1 
ATOM   2833 O O   . GLN B 1 94  ? 3.958   -19.884 -26.521 1.00 54.58  ? 137 GLN B O   1 
ATOM   2834 C CB  . GLN B 1 94  ? 3.344   -21.844 -28.935 1.00 50.39  ? 137 GLN B CB  1 
ATOM   2835 C CG  . GLN B 1 94  ? 2.292   -22.883 -29.306 1.00 51.64  ? 137 GLN B CG  1 
ATOM   2836 C CD  . GLN B 1 94  ? 1.423   -23.285 -28.128 1.00 57.51  ? 137 GLN B CD  1 
ATOM   2837 O OE1 . GLN B 1 94  ? 0.199   -23.159 -28.173 1.00 57.16  ? 137 GLN B OE1 1 
ATOM   2838 N NE2 . GLN B 1 94  ? 2.053   -23.776 -27.066 1.00 61.63  ? 137 GLN B NE2 1 
ATOM   2839 N N   . VAL B 1 95  ? 4.519   -18.799 -28.406 1.00 50.09  ? 138 VAL B N   1 
ATOM   2840 C CA  . VAL B 1 95  ? 5.486   -17.915 -27.762 1.00 56.66  ? 138 VAL B CA  1 
ATOM   2841 C C   . VAL B 1 95  ? 4.865   -16.563 -27.435 1.00 55.17  ? 138 VAL B C   1 
ATOM   2842 O O   . VAL B 1 95  ? 4.917   -16.108 -26.293 1.00 55.61  ? 138 VAL B O   1 
ATOM   2843 C CB  . VAL B 1 95  ? 6.739   -17.759 -28.654 1.00 61.14  ? 138 VAL B CB  1 
ATOM   2844 C CG1 . VAL B 1 95  ? 7.743   -16.806 -28.018 1.00 73.79  ? 138 VAL B CG1 1 
ATOM   2845 C CG2 . VAL B 1 95  ? 7.381   -19.117 -28.903 1.00 64.40  ? 138 VAL B CG2 1 
ATOM   2846 N N   . GLN B 1 96  ? 4.269   -15.906 -28.432 1.00 49.37  ? 139 GLN B N   1 
ATOM   2847 C CA  . GLN B 1 96  ? 3.545   -14.652 -28.221 1.00 47.59  ? 139 GLN B CA  1 
ATOM   2848 C C   . GLN B 1 96  ? 2.144   -15.014 -27.732 1.00 47.66  ? 139 GLN B C   1 
ATOM   2849 O O   . GLN B 1 96  ? 1.166   -15.047 -28.484 1.00 45.94  ? 139 GLN B O   1 
ATOM   2850 C CB  . GLN B 1 96  ? 3.510   -13.826 -29.499 1.00 48.83  ? 139 GLN B CB  1 
ATOM   2851 C CG  . GLN B 1 96  ? 3.063   -12.389 -29.294 1.00 51.32  ? 139 GLN B CG  1 
ATOM   2852 C CD  . GLN B 1 96  ? 4.050   -11.586 -28.470 1.00 51.95  ? 139 GLN B CD  1 
ATOM   2853 O OE1 . GLN B 1 96  ? 5.250   -11.587 -28.745 1.00 53.41  ? 139 GLN B OE1 1 
ATOM   2854 N NE2 . GLN B 1 96  ? 3.550   -10.904 -27.447 1.00 51.89  ? 139 GLN B NE2 1 
ATOM   2855 N N   . ARG B 1 97  ? 2.056   -15.286 -26.428 1.00 46.06  ? 140 ARG B N   1 
ATOM   2856 C CA  . ARG B 1 97  ? 0.878   -15.926 -25.854 1.00 48.23  ? 140 ARG B CA  1 
ATOM   2857 C C   . ARG B 1 97  ? -0.322  -14.998 -25.728 1.00 42.20  ? 140 ARG B C   1 
ATOM   2858 O O   . ARG B 1 97  ? -1.396  -15.468 -25.340 1.00 43.72  ? 140 ARG B O   1 
ATOM   2859 C CB  . ARG B 1 97  ? 1.218   -16.503 -24.478 1.00 52.47  ? 140 ARG B CB  1 
ATOM   2860 C CG  . ARG B 1 97  ? 2.317   -17.550 -24.510 1.00 53.69  ? 140 ARG B CG  1 
ATOM   2861 C CD  . ARG B 1 97  ? 2.296   -18.428 -23.267 1.00 61.97  ? 140 ARG B CD  1 
ATOM   2862 N NE  . ARG B 1 97  ? 1.107   -19.272 -23.216 1.00 64.37  ? 140 ARG B NE  1 
ATOM   2863 C CZ  . ARG B 1 97  ? 0.941   -20.379 -23.928 1.00 61.81  ? 140 ARG B CZ  1 
ATOM   2864 N NH1 . ARG B 1 97  ? 1.869   -20.807 -24.769 1.00 60.21  ? 140 ARG B NH1 1 
ATOM   2865 N NH2 . ARG B 1 97  ? -0.186  -21.073 -23.796 1.00 64.95  ? 140 ARG B NH2 1 
ATOM   2866 N N   . ASP B 1 98  ? -0.178  -13.710 -26.021 1.00 46.75  ? 141 ASP B N   1 
ATOM   2867 C CA  . ASP B 1 98  ? -1.318  -12.803 -26.001 1.00 46.78  ? 141 ASP B CA  1 
ATOM   2868 C C   . ASP B 1 98  ? -1.990  -12.665 -27.363 1.00 44.63  ? 141 ASP B C   1 
ATOM   2869 O O   . ASP B 1 98  ? -2.943  -11.889 -27.489 1.00 43.41  ? 141 ASP B O   1 
ATOM   2870 C CB  . ASP B 1 98  ? -0.890  -11.421 -25.494 1.00 45.85  ? 141 ASP B CB  1 
ATOM   2871 C CG  . ASP B 1 98  ? 0.147   -10.771 -26.383 1.00 49.27  ? 141 ASP B CG  1 
ATOM   2872 O OD1 . ASP B 1 98  ? 0.908   -11.506 -27.044 1.00 52.27  ? 141 ASP B OD1 1 
ATOM   2873 O OD2 . ASP B 1 98  ? 0.204   -9.525  -26.417 1.00 54.45  ? 141 ASP B OD2 1 
ATOM   2874 N N   . MET B 1 99  ? -1.530  -13.394 -28.377 1.00 42.09  ? 142 MET B N   1 
ATOM   2875 C CA  . MET B 1 99  ? -2.139  -13.379 -29.699 1.00 41.19  ? 142 MET B CA  1 
ATOM   2876 C C   . MET B 1 99  ? -2.727  -14.747 -30.020 1.00 38.17  ? 142 MET B C   1 
ATOM   2877 O O   . MET B 1 99  ? -2.240  -15.777 -29.546 1.00 36.85  ? 142 MET B O   1 
ATOM   2878 C CB  . MET B 1 99  ? -1.124  -12.976 -30.771 1.00 39.71  ? 142 MET B CB  1 
ATOM   2879 C CG  . MET B 1 99  ? -0.794  -11.489 -30.749 1.00 46.05  ? 142 MET B CG  1 
ATOM   2880 S SD  . MET B 1 99  ? 0.162   -10.918 -32.165 1.00 57.02  ? 142 MET B SD  1 
ATOM   2881 C CE  . MET B 1 99  ? -1.023  -11.144 -33.485 1.00 37.90  ? 142 MET B CE  1 
ATOM   2882 N N   . PHE B 1 100 ? -3.784  -14.745 -30.832 1.00 37.55  ? 143 PHE B N   1 
ATOM   2883 C CA  . PHE B 1 100 ? -4.608  -15.928 -31.034 1.00 34.46  ? 143 PHE B CA  1 
ATOM   2884 C C   . PHE B 1 100 ? -4.873  -16.166 -32.512 1.00 32.19  ? 143 PHE B C   1 
ATOM   2885 O O   . PHE B 1 100 ? -5.225  -15.235 -33.246 1.00 31.24  ? 143 PHE B O   1 
ATOM   2886 C CB  . PHE B 1 100 ? -5.953  -15.787 -30.303 1.00 35.93  ? 143 PHE B CB  1 
ATOM   2887 C CG  . PHE B 1 100 ? -5.826  -15.501 -28.830 1.00 40.55  ? 143 PHE B CG  1 
ATOM   2888 C CD1 . PHE B 1 100 ? -5.504  -14.230 -28.380 1.00 41.45  ? 143 PHE B CD1 1 
ATOM   2889 C CD2 . PHE B 1 100 ? -6.048  -16.500 -27.897 1.00 40.38  ? 143 PHE B CD2 1 
ATOM   2890 C CE1 . PHE B 1 100 ? -5.390  -13.966 -27.028 1.00 45.41  ? 143 PHE B CE1 1 
ATOM   2891 C CE2 . PHE B 1 100 ? -5.939  -16.241 -26.545 1.00 42.74  ? 143 PHE B CE2 1 
ATOM   2892 C CZ  . PHE B 1 100 ? -5.610  -14.973 -26.110 1.00 47.80  ? 143 PHE B CZ  1 
ATOM   2893 N N   . THR B 1 101 ? -4.727  -17.415 -32.938 1.00 29.66  ? 144 THR B N   1 
ATOM   2894 C CA  . THR B 1 101 ? -5.272  -17.876 -34.204 1.00 29.86  ? 144 THR B CA  1 
ATOM   2895 C C   . THR B 1 101 ? -6.623  -18.536 -33.949 1.00 28.71  ? 144 THR B C   1 
ATOM   2896 O O   . THR B 1 101 ? -7.026  -18.765 -32.805 1.00 27.56  ? 144 THR B O   1 
ATOM   2897 C CB  . THR B 1 101 ? -4.325  -18.856 -34.904 1.00 30.64  ? 144 THR B CB  1 
ATOM   2898 O OG1 . THR B 1 101 ? -4.201  -20.056 -34.128 1.00 34.19  ? 144 THR B OG1 1 
ATOM   2899 C CG2 . THR B 1 101 ? -2.951  -18.231 -35.109 1.00 32.55  ? 144 THR B CG2 1 
ATOM   2900 N N   . LEU B 1 102 ? -7.332  -18.835 -35.037 1.00 26.11  ? 145 LEU B N   1 
ATOM   2901 C CA  . LEU B 1 102 ? -8.613  -19.521 -34.908 1.00 26.62  ? 145 LEU B CA  1 
ATOM   2902 C C   . LEU B 1 102 ? -8.447  -20.859 -34.198 1.00 27.43  ? 145 LEU B C   1 
ATOM   2903 O O   . LEU B 1 102 ? -9.316  -21.272 -33.421 1.00 25.37  ? 145 LEU B O   1 
ATOM   2904 C CB  . LEU B 1 102 ? -9.239  -19.715 -36.288 1.00 26.72  ? 145 LEU B CB  1 
ATOM   2905 C CG  . LEU B 1 102 ? -10.573 -20.460 -36.347 1.00 28.50  ? 145 LEU B CG  1 
ATOM   2906 C CD1 . LEU B 1 102 ? -11.620 -19.766 -35.489 1.00 26.77  ? 145 LEU B CD1 1 
ATOM   2907 C CD2 . LEU B 1 102 ? -11.048 -20.576 -37.794 1.00 26.68  ? 145 LEU B CD2 1 
ATOM   2908 N N   . GLU B 1 103 ? -7.332  -21.548 -34.448 1.00 27.67  ? 146 GLU B N   1 
ATOM   2909 C CA  . GLU B 1 103 ? -7.083  -22.839 -33.821 1.00 28.08  ? 146 GLU B CA  1 
ATOM   2910 C C   . GLU B 1 103 ? -6.743  -22.714 -32.341 1.00 29.45  ? 146 GLU B C   1 
ATOM   2911 O O   . GLU B 1 103 ? -6.681  -23.736 -31.648 1.00 23.33  ? 146 GLU B O   1 
ATOM   2912 C CB  . GLU B 1 103 ? -5.959  -23.567 -34.564 1.00 29.86  ? 146 GLU B CB  1 
ATOM   2913 C CG  . GLU B 1 103 ? -6.313  -23.958 -36.001 1.00 30.05  ? 146 GLU B CG  1 
ATOM   2914 C CD  . GLU B 1 103 ? -6.249  -22.790 -36.976 1.00 31.60  ? 146 GLU B CD  1 
ATOM   2915 O OE1 . GLU B 1 103 ? -5.492  -21.832 -36.713 1.00 30.96  ? 146 GLU B OE1 1 
ATOM   2916 O OE2 . GLU B 1 103 ? -6.957  -22.830 -38.006 1.00 29.56  ? 146 GLU B OE2 1 
ATOM   2917 N N   . ASP B 1 104 ? -6.522  -21.499 -31.843 1.00 27.41  ? 147 ASP B N   1 
ATOM   2918 C CA  . ASP B 1 104 ? -6.355  -21.269 -30.415 1.00 27.90  ? 147 ASP B CA  1 
ATOM   2919 C C   . ASP B 1 104 ? -7.681  -21.046 -29.698 1.00 29.28  ? 147 ASP B C   1 
ATOM   2920 O O   . ASP B 1 104 ? -7.693  -20.957 -28.465 1.00 28.09  ? 147 ASP B O   1 
ATOM   2921 C CB  . ASP B 1 104 ? -5.429  -20.072 -30.184 1.00 29.92  ? 147 ASP B CB  1 
ATOM   2922 C CG  . ASP B 1 104 ? -4.021  -20.321 -30.701 1.00 33.56  ? 147 ASP B CG  1 
ATOM   2923 O OD1 . ASP B 1 104 ? -3.477  -21.414 -30.433 1.00 32.76  ? 147 ASP B OD1 1 
ATOM   2924 O OD2 . ASP B 1 104 ? -3.462  -19.434 -31.382 1.00 31.25  ? 147 ASP B OD2 1 
ATOM   2925 N N   . THR B 1 105 ? -8.784  -20.945 -30.436 1.00 26.75  ? 148 THR B N   1 
ATOM   2926 C CA  . THR B 1 105 ? -10.118 -20.945 -29.856 1.00 27.37  ? 148 THR B CA  1 
ATOM   2927 C C   . THR B 1 105 ? -10.594 -22.382 -29.663 1.00 24.87  ? 148 THR B C   1 
ATOM   2928 O O   . THR B 1 105 ? -10.089 -23.316 -30.291 1.00 24.52  ? 148 THR B O   1 
ATOM   2929 C CB  . THR B 1 105 ? -11.111 -20.196 -30.749 1.00 27.15  ? 148 THR B CB  1 
ATOM   2930 O OG1 . THR B 1 105 ? -11.325 -20.935 -31.960 1.00 27.14  ? 148 THR B OG1 1 
ATOM   2931 C CG2 . THR B 1 105 ? -10.596 -18.807 -31.095 1.00 27.73  ? 148 THR B CG2 1 
ATOM   2932 N N   . LEU B 1 106 ? -11.594 -22.550 -28.797 1.00 23.54  ? 149 LEU B N   1 
ATOM   2933 C CA  . LEU B 1 106 ? -12.120 -23.887 -28.541 1.00 27.41  ? 149 LEU B CA  1 
ATOM   2934 C C   . LEU B 1 106 ? -12.593 -24.545 -29.833 1.00 27.18  ? 149 LEU B C   1 
ATOM   2935 O O   . LEU B 1 106 ? -12.202 -25.674 -30.145 1.00 27.55  ? 149 LEU B O   1 
ATOM   2936 C CB  . LEU B 1 106 ? -13.260 -23.824 -27.523 1.00 28.12  ? 149 LEU B CB  1 
ATOM   2937 C CG  . LEU B 1 106 ? -14.036 -25.129 -27.309 1.00 29.21  ? 149 LEU B CG  1 
ATOM   2938 C CD1 . LEU B 1 106 ? -13.115 -26.256 -26.849 1.00 30.01  ? 149 LEU B CD1 1 
ATOM   2939 C CD2 . LEU B 1 106 ? -15.168 -24.928 -26.312 1.00 30.60  ? 149 LEU B CD2 1 
ATOM   2940 N N   . LEU B 1 107 ? -13.426 -23.845 -30.608 1.00 25.04  ? 150 LEU B N   1 
ATOM   2941 C CA  . LEU B 1 107 ? -14.012 -24.455 -31.798 1.00 26.83  ? 150 LEU B CA  1 
ATOM   2942 C C   . LEU B 1 107 ? -12.941 -24.821 -32.819 1.00 25.83  ? 150 LEU B C   1 
ATOM   2943 O O   . LEU B 1 107 ? -12.951 -25.924 -33.377 1.00 23.85  ? 150 LEU B O   1 
ATOM   2944 C CB  . LEU B 1 107 ? -15.045 -23.512 -32.412 1.00 25.93  ? 150 LEU B CB  1 
ATOM   2945 C CG  . LEU B 1 107 ? -16.326 -23.327 -31.598 1.00 26.36  ? 150 LEU B CG  1 
ATOM   2946 C CD1 . LEU B 1 107 ? -17.200 -22.252 -32.223 1.00 33.51  ? 150 LEU B CD1 1 
ATOM   2947 C CD2 . LEU B 1 107 ? -17.087 -24.638 -31.485 1.00 27.97  ? 150 LEU B CD2 1 
ATOM   2948 N N   . GLY B 1 108 ? -12.010 -23.905 -33.084 1.00 23.88  ? 151 GLY B N   1 
ATOM   2949 C CA  . GLY B 1 108 ? -10.925 -24.229 -33.994 1.00 23.65  ? 151 GLY B CA  1 
ATOM   2950 C C   . GLY B 1 108 ? -10.055 -25.351 -33.464 1.00 27.72  ? 151 GLY B C   1 
ATOM   2951 O O   . GLY B 1 108 ? -9.572  -26.194 -34.225 1.00 26.45  ? 151 GLY B O   1 
ATOM   2952 N N   . TYR B 1 109 ? -9.859  -25.382 -32.145 1.00 26.20  ? 152 TYR B N   1 
ATOM   2953 C CA  . TYR B 1 109 ? -9.045  -26.421 -31.522 1.00 25.66  ? 152 TYR B CA  1 
ATOM   2954 C C   . TYR B 1 109 ? -9.650  -27.805 -31.734 1.00 25.98  ? 152 TYR B C   1 
ATOM   2955 O O   . TYR B 1 109 ? -8.930  -28.768 -32.022 1.00 25.07  ? 152 TYR B O   1 
ATOM   2956 C CB  . TYR B 1 109 ? -8.901  -26.105 -30.031 1.00 26.17  ? 152 TYR B CB  1 
ATOM   2957 C CG  . TYR B 1 109 ? -7.996  -27.026 -29.248 1.00 26.85  ? 152 TYR B CG  1 
ATOM   2958 C CD1 . TYR B 1 109 ? -6.636  -26.772 -29.146 1.00 31.22  ? 152 TYR B CD1 1 
ATOM   2959 C CD2 . TYR B 1 109 ? -8.507  -28.132 -28.580 1.00 29.93  ? 152 TYR B CD2 1 
ATOM   2960 C CE1 . TYR B 1 109 ? -5.805  -27.602 -28.416 1.00 34.64  ? 152 TYR B CE1 1 
ATOM   2961 C CE2 . TYR B 1 109 ? -7.683  -28.971 -27.849 1.00 29.15  ? 152 TYR B CE2 1 
ATOM   2962 C CZ  . TYR B 1 109 ? -6.333  -28.700 -27.770 1.00 31.40  ? 152 TYR B CZ  1 
ATOM   2963 O OH  . TYR B 1 109 ? -5.504  -29.527 -27.045 1.00 37.56  ? 152 TYR B OH  1 
ATOM   2964 N N   . LEU B 1 110 ? -10.974 -27.924 -31.598 1.00 26.00  ? 153 LEU B N   1 
ATOM   2965 C CA  . LEU B 1 110 ? -11.625 -29.223 -31.741 1.00 24.97  ? 153 LEU B CA  1 
ATOM   2966 C C   . LEU B 1 110 ? -11.429 -29.807 -33.136 1.00 24.75  ? 153 LEU B C   1 
ATOM   2967 O O   . LEU B 1 110 ? -11.143 -31.002 -33.283 1.00 23.91  ? 153 LEU B O   1 
ATOM   2968 C CB  . LEU B 1 110 ? -13.120 -29.096 -31.446 1.00 24.49  ? 153 LEU B CB  1 
ATOM   2969 C CG  . LEU B 1 110 ? -13.541 -28.645 -30.049 1.00 27.49  ? 153 LEU B CG  1 
ATOM   2970 C CD1 . LEU B 1 110 ? -15.058 -28.519 -29.975 1.00 27.87  ? 153 LEU B CD1 1 
ATOM   2971 C CD2 . LEU B 1 110 ? -13.030 -29.612 -28.992 1.00 30.45  ? 153 LEU B CD2 1 
ATOM   2972 N N   . ALA B 1 111 ? -11.593 -28.986 -34.172 1.00 25.67  ? 154 ALA B N   1 
ATOM   2973 C CA  . ALA B 1 111 ? -11.695 -29.471 -35.542 1.00 25.25  ? 154 ALA B CA  1 
ATOM   2974 C C   . ALA B 1 111 ? -10.374 -29.472 -36.297 1.00 26.40  ? 154 ALA B C   1 
ATOM   2975 O O   . ALA B 1 111 ? -10.325 -29.989 -37.418 1.00 25.00  ? 154 ALA B O   1 
ATOM   2976 C CB  . ALA B 1 111 ? -12.710 -28.619 -36.315 1.00 25.71  ? 154 ALA B CB  1 
ATOM   2977 N N   . ASP B 1 112 ? -9.308  -28.925 -35.717 1.00 25.75  ? 155 ASP B N   1 
ATOM   2978 C CA  . ASP B 1 112 ? -8.050  -28.773 -36.439 1.00 30.13  ? 155 ASP B CA  1 
ATOM   2979 C C   . ASP B 1 112 ? -7.577  -30.107 -37.006 1.00 33.15  ? 155 ASP B C   1 
ATOM   2980 O O   . ASP B 1 112 ? -7.443  -31.094 -36.278 1.00 29.83  ? 155 ASP B O   1 
ATOM   2981 C CB  . ASP B 1 112 ? -6.991  -28.187 -35.501 1.00 31.89  ? 155 ASP B CB  1 
ATOM   2982 C CG  . ASP B 1 112 ? -5.664  -27.948 -36.193 1.00 36.56  ? 155 ASP B CG  1 
ATOM   2983 O OD1 . ASP B 1 112 ? -5.646  -27.243 -37.223 1.00 38.01  ? 155 ASP B OD1 1 
ATOM   2984 O OD2 . ASP B 1 112 ? -4.636  -28.462 -35.704 1.00 45.02  ? 155 ASP B OD2 1 
ATOM   2985 N N   . ASP B 1 113 ? -7.333  -30.126 -38.320 1.00 34.63  ? 156 ASP B N   1 
ATOM   2986 C CA  . ASP B 1 113 ? -6.762  -31.259 -39.045 1.00 36.38  ? 156 ASP B CA  1 
ATOM   2987 C C   . ASP B 1 113 ? -7.683  -32.474 -39.111 1.00 34.99  ? 156 ASP B C   1 
ATOM   2988 O O   . ASP B 1 113 ? -7.224  -33.576 -39.431 1.00 37.78  ? 156 ASP B O   1 
ATOM   2989 C CB  . ASP B 1 113 ? -5.415  -31.687 -38.443 1.00 41.73  ? 156 ASP B CB  1 
ATOM   2990 C CG  . ASP B 1 113 ? -4.289  -30.728 -38.778 1.00 51.95  ? 156 ASP B CG  1 
ATOM   2991 O OD1 . ASP B 1 113 ? -4.327  -30.118 -39.867 1.00 56.84  ? 156 ASP B OD1 1 
ATOM   2992 O OD2 . ASP B 1 113 ? -3.360  -30.592 -37.953 1.00 54.55  ? 156 ASP B OD2 1 
ATOM   2993 N N   . LEU B 1 114 ? -8.975  -32.316 -38.838 1.00 30.05  ? 157 LEU B N   1 
ATOM   2994 C CA  . LEU B 1 114 ? -9.905  -33.436 -38.835 1.00 28.95  ? 157 LEU B CA  1 
ATOM   2995 C C   . LEU B 1 114 ? -10.866 -33.352 -40.015 1.00 29.55  ? 157 LEU B C   1 
ATOM   2996 O O   . LEU B 1 114 ? -11.119 -32.279 -40.571 1.00 29.54  ? 157 LEU B O   1 
ATOM   2997 C CB  . LEU B 1 114 ? -10.702 -33.488 -37.525 1.00 27.37  ? 157 LEU B CB  1 
ATOM   2998 C CG  . LEU B 1 114 ? -9.893  -33.678 -36.239 1.00 28.27  ? 157 LEU B CG  1 
ATOM   2999 C CD1 . LEU B 1 114 ? -10.808 -33.632 -35.023 1.00 24.60  ? 157 LEU B CD1 1 
ATOM   3000 C CD2 . LEU B 1 114 ? -9.113  -34.984 -36.269 1.00 28.06  ? 157 LEU B CD2 1 
ATOM   3001 N N   . THR B 1 115 ? -11.397 -34.515 -40.390 1.00 25.11  ? 158 THR B N   1 
ATOM   3002 C CA  . THR B 1 115 ? -12.392 -34.651 -41.444 1.00 27.61  ? 158 THR B CA  1 
ATOM   3003 C C   . THR B 1 115 ? -13.567 -35.443 -40.888 1.00 27.05  ? 158 THR B C   1 
ATOM   3004 O O   . THR B 1 115 ? -13.386 -36.338 -40.060 1.00 25.82  ? 158 THR B O   1 
ATOM   3005 C CB  . THR B 1 115 ? -11.812 -35.364 -42.680 1.00 30.94  ? 158 THR B CB  1 
ATOM   3006 O OG1 . THR B 1 115 ? -10.713 -34.606 -43.204 1.00 34.38  ? 158 THR B OG1 1 
ATOM   3007 C CG2 . THR B 1 115 ? -12.872 -35.529 -43.762 1.00 32.31  ? 158 THR B CG2 1 
ATOM   3008 N N   . TRP B 1 116 ? -14.776 -35.101 -41.333 1.00 26.78  ? 159 TRP B N   1 
ATOM   3009 C CA  . TRP B 1 116 ? -15.960 -35.793 -40.842 1.00 26.55  ? 159 TRP B CA  1 
ATOM   3010 C C   . TRP B 1 116 ? -17.114 -35.596 -41.813 1.00 28.44  ? 159 TRP B C   1 
ATOM   3011 O O   . TRP B 1 116 ? -17.200 -34.577 -42.502 1.00 25.54  ? 159 TRP B O   1 
ATOM   3012 C CB  . TRP B 1 116 ? -16.358 -35.295 -39.448 1.00 24.55  ? 159 TRP B CB  1 
ATOM   3013 C CG  . TRP B 1 116 ? -16.744 -33.839 -39.419 1.00 28.32  ? 159 TRP B CG  1 
ATOM   3014 C CD1 . TRP B 1 116 ? -18.005 -33.322 -39.520 1.00 26.04  ? 159 TRP B CD1 1 
ATOM   3015 C CD2 . TRP B 1 116 ? -15.862 -32.716 -39.286 1.00 24.93  ? 159 TRP B CD2 1 
ATOM   3016 N NE1 . TRP B 1 116 ? -17.961 -31.950 -39.458 1.00 27.24  ? 159 TRP B NE1 1 
ATOM   3017 C CE2 . TRP B 1 116 ? -16.658 -31.553 -39.314 1.00 25.80  ? 159 TRP B CE2 1 
ATOM   3018 C CE3 . TRP B 1 116 ? -14.477 -32.582 -39.148 1.00 25.68  ? 159 TRP B CE3 1 
ATOM   3019 C CZ2 . TRP B 1 116 ? -16.115 -30.272 -39.206 1.00 23.43  ? 159 TRP B CZ2 1 
ATOM   3020 C CZ3 . TRP B 1 116 ? -13.940 -31.309 -39.040 1.00 27.17  ? 159 TRP B CZ3 1 
ATOM   3021 C CH2 . TRP B 1 116 ? -14.758 -30.172 -39.070 1.00 24.58  ? 159 TRP B CH2 1 
ATOM   3022 N N   . CYS B 1 117 ? -17.998 -36.589 -41.855 1.00 27.75  ? 160 CYS B N   1 
ATOM   3023 C CA  . CYS B 1 117 ? -19.263 -36.476 -42.567 1.00 29.13  ? 160 CYS B CA  1 
ATOM   3024 C C   . CYS B 1 117 ? -20.156 -37.625 -42.122 1.00 30.21  ? 160 CYS B C   1 
ATOM   3025 O O   . CYS B 1 117 ? -19.688 -38.608 -41.542 1.00 26.97  ? 160 CYS B O   1 
ATOM   3026 C CB  . CYS B 1 117 ? -19.070 -36.489 -44.088 1.00 32.29  ? 160 CYS B CB  1 
ATOM   3027 S SG  . CYS B 1 117 ? -18.424 -38.037 -44.757 1.00 37.50  ? 160 CYS B SG  1 
ATOM   3028 N N   . GLY B 1 118 ? -21.449 -37.474 -42.394 1.00 31.19  ? 161 GLY B N   1 
ATOM   3029 C CA  . GLY B 1 118 ? -22.437 -38.482 -42.080 1.00 29.06  ? 161 GLY B CA  1 
ATOM   3030 C C   . GLY B 1 118 ? -23.230 -38.874 -43.308 1.00 32.24  ? 161 GLY B C   1 
ATOM   3031 O O   . GLY B 1 118 ? -22.758 -38.745 -44.447 1.00 28.89  ? 161 GLY B O   1 
ATOM   3032 N N   . GLU B 1 119 ? -24.449 -39.351 -43.076 1.00 32.28  ? 162 GLU B N   1 
ATOM   3033 C CA  . GLU B 1 119 ? -25.336 -39.788 -44.140 1.00 35.31  ? 162 GLU B CA  1 
ATOM   3034 C C   . GLU B 1 119 ? -26.772 -39.453 -43.765 1.00 34.86  ? 162 GLU B C   1 
ATOM   3035 O O   . GLU B 1 119 ? -27.123 -39.387 -42.585 1.00 34.52  ? 162 GLU B O   1 
ATOM   3036 C CB  . GLU B 1 119 ? -25.195 -41.292 -44.408 1.00 40.99  ? 162 GLU B CB  1 
ATOM   3037 C CG  . GLU B 1 119 ? -26.382 -41.903 -45.144 1.00 47.32  ? 162 GLU B CG  1 
ATOM   3038 C CD  . GLU B 1 119 ? -26.175 -43.361 -45.487 1.00 54.52  ? 162 GLU B CD  1 
ATOM   3039 O OE1 . GLU B 1 119 ? -25.497 -44.068 -44.711 1.00 52.99  ? 162 GLU B OE1 1 
ATOM   3040 O OE2 . GLU B 1 119 ? -26.695 -43.798 -46.535 1.00 56.03  ? 162 GLU B OE2 1 
ATOM   3041 N N   . PHE B 1 120 ? -27.600 -39.263 -44.788 1.00 33.78  ? 163 PHE B N   1 
ATOM   3042 C CA  . PHE B 1 120 ? -28.999 -38.923 -44.575 1.00 35.78  ? 163 PHE B CA  1 
ATOM   3043 C C   . PHE B 1 120 ? -29.759 -40.079 -43.935 1.00 38.74  ? 163 PHE B C   1 
ATOM   3044 O O   . PHE B 1 120 ? -29.596 -41.241 -44.315 1.00 34.12  ? 163 PHE B O   1 
ATOM   3045 C CB  . PHE B 1 120 ? -29.659 -38.550 -45.903 1.00 34.17  ? 163 PHE B CB  1 
ATOM   3046 C CG  . PHE B 1 120 ? -31.109 -38.181 -45.777 1.00 34.81  ? 163 PHE B CG  1 
ATOM   3047 C CD1 . PHE B 1 120 ? -31.479 -36.932 -45.306 1.00 35.18  ? 163 PHE B CD1 1 
ATOM   3048 C CD2 . PHE B 1 120 ? -32.102 -39.079 -46.134 1.00 36.35  ? 163 PHE B CD2 1 
ATOM   3049 C CE1 . PHE B 1 120 ? -32.812 -36.586 -45.188 1.00 36.16  ? 163 PHE B CE1 1 
ATOM   3050 C CE2 . PHE B 1 120 ? -33.438 -38.739 -46.020 1.00 34.93  ? 163 PHE B CE2 1 
ATOM   3051 C CZ  . PHE B 1 120 ? -33.793 -37.491 -45.546 1.00 37.59  ? 163 PHE B CZ  1 
ATOM   3052 N N   . ALA B 1 121 ? -30.598 -39.745 -42.955 1.00 40.78  ? 164 ALA B N   1 
ATOM   3053 C CA  . ALA B 1 121 ? -31.563 -40.643 -42.330 1.00 42.53  ? 164 ALA B CA  1 
ATOM   3054 C C   . ALA B 1 121 ? -30.922 -41.744 -41.496 1.00 43.83  ? 164 ALA B C   1 
ATOM   3055 O O   . ALA B 1 121 ? -31.629 -42.656 -41.049 1.00 48.35  ? 164 ALA B O   1 
ATOM   3056 C CB  . ALA B 1 121 ? -32.490 -41.280 -43.374 1.00 46.35  ? 164 ALA B CB  1 
ATOM   3057 N N   . THR B 1 122 ? -29.610 -41.695 -41.270 1.00 43.55  ? 165 THR B N   1 
ATOM   3058 C CA  A THR B 1 122 ? -28.929 -42.660 -40.420 0.61 46.46  ? 165 THR B CA  1 
ATOM   3059 C CA  B THR B 1 122 ? -28.924 -42.661 -40.425 0.39 46.45  ? 165 THR B CA  1 
ATOM   3060 C C   . THR B 1 122 ? -28.093 -41.918 -39.387 1.00 44.98  ? 165 THR B C   1 
ATOM   3061 O O   . THR B 1 122 ? -27.716 -40.759 -39.576 1.00 40.06  ? 165 THR B O   1 
ATOM   3062 C CB  A THR B 1 122 ? -28.031 -43.612 -41.226 0.61 47.00  ? 165 THR B CB  1 
ATOM   3063 C CB  B THR B 1 122 ? -28.018 -43.598 -41.238 0.39 47.02  ? 165 THR B CB  1 
ATOM   3064 O OG1 A THR B 1 122 ? -26.979 -42.869 -41.852 0.61 48.48  ? 165 THR B OG1 1 
ATOM   3065 O OG1 B THR B 1 122 ? -27.517 -44.637 -40.387 0.39 48.58  ? 165 THR B OG1 1 
ATOM   3066 C CG2 A THR B 1 122 ? -28.839 -44.346 -42.288 0.61 48.32  ? 165 THR B CG2 1 
ATOM   3067 C CG2 B THR B 1 122 ? -26.846 -42.835 -41.831 0.39 48.99  ? 165 THR B CG2 1 
ATOM   3068 N N   . SER B 1 123 ? -27.810 -42.606 -38.283 1.00 43.59  ? 166 SER B N   1 
ATOM   3069 C CA  . SER B 1 123 ? -27.047 -42.040 -37.181 1.00 42.88  ? 166 SER B CA  1 
ATOM   3070 C C   . SER B 1 123 ? -25.569 -42.398 -37.247 1.00 42.07  ? 166 SER B C   1 
ATOM   3071 O O   . SER B 1 123 ? -24.848 -42.187 -36.268 1.00 43.73  ? 166 SER B O   1 
ATOM   3072 C CB  . SER B 1 123 ? -27.633 -42.508 -35.847 1.00 43.96  ? 166 SER B CB  1 
ATOM   3073 O OG  . SER B 1 123 ? -27.499 -43.911 -35.700 1.00 48.71  ? 166 SER B OG  1 
ATOM   3074 N N   . LYS B 1 124 ? -25.101 -42.926 -38.373 1.00 41.08  ? 167 LYS B N   1 
ATOM   3075 C CA  . LYS B 1 124 ? -23.751 -43.458 -38.485 1.00 41.40  ? 167 LYS B CA  1 
ATOM   3076 C C   . LYS B 1 124 ? -22.812 -42.441 -39.123 1.00 38.64  ? 167 LYS B C   1 
ATOM   3077 O O   . LYS B 1 124 ? -23.161 -41.786 -40.109 1.00 37.39  ? 167 LYS B O   1 
ATOM   3078 C CB  . LYS B 1 124 ? -23.747 -44.749 -39.308 1.00 45.88  ? 167 LYS B CB  1 
ATOM   3079 C CG  . LYS B 1 124 ? -24.372 -45.946 -38.600 1.00 55.23  ? 167 LYS B CG  1 
ATOM   3080 C CD  . LYS B 1 124 ? -23.535 -46.389 -37.408 1.00 62.41  ? 167 LYS B CD  1 
ATOM   3081 C CE  . LYS B 1 124 ? -24.070 -47.673 -36.789 1.00 76.63  ? 167 LYS B CE  1 
ATOM   3082 N NZ  . LYS B 1 124 ? -25.409 -47.488 -36.161 1.00 77.97  ? 167 LYS B NZ  1 
ATOM   3083 N N   . ILE B 1 125 ? -21.619 -42.311 -38.539 1.00 35.33  ? 168 ILE B N   1 
ATOM   3084 C CA  . ILE B 1 125 ? -20.547 -41.554 -39.167 1.00 31.57  ? 168 ILE B CA  1 
ATOM   3085 C C   . ILE B 1 125 ? -20.000 -42.344 -40.347 1.00 32.46  ? 168 ILE B C   1 
ATOM   3086 O O   . ILE B 1 125 ? -19.881 -43.577 -40.292 1.00 32.26  ? 168 ILE B O   1 
ATOM   3087 C CB  . ILE B 1 125 ? -19.435 -41.246 -38.150 1.00 32.70  ? 168 ILE B CB  1 
ATOM   3088 C CG1 . ILE B 1 125 ? -19.935 -40.244 -37.109 1.00 32.36  ? 168 ILE B CG1 1 
ATOM   3089 C CG2 . ILE B 1 125 ? -18.188 -40.724 -38.865 1.00 34.07  ? 168 ILE B CG2 1 
ATOM   3090 C CD1 . ILE B 1 125 ? -18.937 -39.939 -36.013 1.00 35.27  ? 168 ILE B CD1 1 
ATOM   3091 N N   . ASN B 1 126 ? -19.656 -41.638 -41.420 1.00 28.96  ? 169 ASN B N   1 
ATOM   3092 C CA  . ASN B 1 126 ? -19.106 -42.266 -42.619 1.00 32.65  ? 169 ASN B CA  1 
ATOM   3093 C C   . ASN B 1 126 ? -17.585 -42.254 -42.518 1.00 32.32  ? 169 ASN B C   1 
ATOM   3094 O O   . ASN B 1 126 ? -16.938 -41.253 -42.833 1.00 28.73  ? 169 ASN B O   1 
ATOM   3095 C CB  . ASN B 1 126 ? -19.587 -41.544 -43.873 1.00 31.33  ? 169 ASN B CB  1 
ATOM   3096 C CG  . ASN B 1 126 ? -19.171 -42.252 -45.147 1.00 36.37  ? 169 ASN B CG  1 
ATOM   3097 O OD1 . ASN B 1 126 ? -18.189 -42.997 -45.167 1.00 34.10  ? 169 ASN B OD1 1 
ATOM   3098 N ND2 . ASN B 1 126 ? -19.918 -42.026 -46.219 1.00 32.96  ? 169 ASN B ND2 1 
ATOM   3099 N N   . TYR B 1 127 ? -17.009 -43.378 -42.096 1.00 32.11  ? 170 TYR B N   1 
ATOM   3100 C CA  . TYR B 1 127 ? -15.561 -43.529 -42.013 1.00 33.85  ? 170 TYR B CA  1 
ATOM   3101 C C   . TYR B 1 127 ? -14.940 -43.997 -43.323 1.00 35.54  ? 170 TYR B C   1 
ATOM   3102 O O   . TYR B 1 127 ? -13.721 -44.189 -43.379 1.00 37.83  ? 170 TYR B O   1 
ATOM   3103 C CB  . TYR B 1 127 ? -15.190 -44.516 -40.898 1.00 34.70  ? 170 TYR B CB  1 
ATOM   3104 C CG  . TYR B 1 127 ? -15.487 -44.007 -39.507 1.00 31.24  ? 170 TYR B CG  1 
ATOM   3105 C CD1 . TYR B 1 127 ? -14.609 -43.149 -38.858 1.00 32.37  ? 170 TYR B CD1 1 
ATOM   3106 C CD2 . TYR B 1 127 ? -16.646 -44.383 -38.843 1.00 29.48  ? 170 TYR B CD2 1 
ATOM   3107 C CE1 . TYR B 1 127 ? -14.878 -42.677 -37.585 1.00 29.47  ? 170 TYR B CE1 1 
ATOM   3108 C CE2 . TYR B 1 127 ? -16.924 -43.919 -37.573 1.00 29.76  ? 170 TYR B CE2 1 
ATOM   3109 C CZ  . TYR B 1 127 ? -16.037 -43.065 -36.949 1.00 31.32  ? 170 TYR B CZ  1 
ATOM   3110 O OH  . TYR B 1 127 ? -16.307 -42.600 -35.683 1.00 34.26  ? 170 TYR B OH  1 
ATOM   3111 N N   . GLN B 1 128 ? -15.741 -44.178 -44.373 1.00 36.40  ? 171 GLN B N   1 
ATOM   3112 C CA  . GLN B 1 128 ? -15.255 -44.711 -45.641 1.00 41.76  ? 171 GLN B CA  1 
ATOM   3113 C C   . GLN B 1 128 ? -14.879 -43.623 -46.644 1.00 37.91  ? 171 GLN B C   1 
ATOM   3114 O O   . GLN B 1 128 ? -13.822 -43.711 -47.272 1.00 40.42  ? 171 GLN B O   1 
ATOM   3115 C CB  . GLN B 1 128 ? -16.309 -45.641 -46.246 1.00 48.90  ? 171 GLN B CB  1 
ATOM   3116 C CG  . GLN B 1 128 ? -16.653 -46.818 -45.341 1.00 59.27  ? 171 GLN B CG  1 
ATOM   3117 C CD  . GLN B 1 128 ? -17.643 -47.777 -45.968 1.00 73.36  ? 171 GLN B CD  1 
ATOM   3118 O OE1 . GLN B 1 128 ? -18.161 -47.529 -47.057 1.00 78.79  ? 171 GLN B OE1 1 
ATOM   3119 N NE2 . GLN B 1 128 ? -17.915 -48.881 -45.279 1.00 76.45  ? 171 GLN B NE2 1 
ATOM   3120 N N   . SER B 1 129 ? -15.719 -42.604 -46.811 1.00 35.11  ? 172 SER B N   1 
ATOM   3121 C CA  . SER B 1 129 ? -15.392 -41.488 -47.691 1.00 35.01  ? 172 SER B CA  1 
ATOM   3122 C C   . SER B 1 129 ? -16.242 -40.293 -47.295 1.00 33.59  ? 172 SER B C   1 
ATOM   3123 O O   . SER B 1 129 ? -17.284 -40.435 -46.650 1.00 33.12  ? 172 SER B O   1 
ATOM   3124 C CB  . SER B 1 129 ? -15.616 -41.843 -49.167 1.00 37.22  ? 172 SER B CB  1 
ATOM   3125 O OG  . SER B 1 129 ? -16.988 -42.063 -49.441 1.00 38.33  ? 172 SER B OG  1 
ATOM   3126 N N   . CYS B 1 130 ? -15.782 -39.109 -47.685 1.00 32.87  ? 173 CYS B N   1 
ATOM   3127 C CA  . CYS B 1 130 ? -16.506 -37.869 -47.489 1.00 32.52  ? 173 CYS B CA  1 
ATOM   3128 C C   . CYS B 1 130 ? -16.392 -37.022 -48.743 1.00 31.57  ? 173 CYS B C   1 
ATOM   3129 O O   . CYS B 1 130 ? -15.453 -37.197 -49.536 1.00 31.13  ? 173 CYS B O   1 
ATOM   3130 C CB  . CYS B 1 130 ? -15.984 -37.085 -46.276 1.00 33.63  ? 173 CYS B CB  1 
ATOM   3131 S SG  . CYS B 1 130 ? -16.399 -37.836 -44.678 1.00 35.23  ? 173 CYS B SG  1 
ATOM   3132 N N   . PRO B 1 131 ? -17.325 -36.099 -48.966 1.00 31.06  ? 174 PRO B N   1 
ATOM   3133 C CA  . PRO B 1 131 ? -17.304 -35.307 -50.200 1.00 32.10  ? 174 PRO B CA  1 
ATOM   3134 C C   . PRO B 1 131 ? -16.054 -34.448 -50.317 1.00 32.07  ? 174 PRO B C   1 
ATOM   3135 O O   . PRO B 1 131 ? -15.626 -33.799 -49.360 1.00 36.14  ? 174 PRO B O   1 
ATOM   3136 C CB  . PRO B 1 131 ? -18.563 -34.437 -50.091 1.00 30.27  ? 174 PRO B CB  1 
ATOM   3137 C CG  . PRO B 1 131 ? -19.424 -35.111 -49.082 1.00 31.87  ? 174 PRO B CG  1 
ATOM   3138 C CD  . PRO B 1 131 ? -18.483 -35.758 -48.117 1.00 31.10  ? 174 PRO B CD  1 
ATOM   3139 N N   . ASP B 1 132 ? -15.484 -34.433 -51.516 1.00 34.97  ? 175 ASP B N   1 
ATOM   3140 C CA  . ASP B 1 132 ? -14.435 -33.488 -51.866 1.00 40.60  ? 175 ASP B CA  1 
ATOM   3141 C C   . ASP B 1 132 ? -15.076 -32.210 -52.392 1.00 41.17  ? 175 ASP B C   1 
ATOM   3142 O O   . ASP B 1 132 ? -16.011 -32.258 -53.196 1.00 41.65  ? 175 ASP B O   1 
ATOM   3143 C CB  . ASP B 1 132 ? -13.496 -34.084 -52.914 1.00 46.33  ? 175 ASP B CB  1 
ATOM   3144 C CG  . ASP B 1 132 ? -12.461 -33.090 -53.402 1.00 49.24  ? 175 ASP B CG  1 
ATOM   3145 O OD1 . ASP B 1 132 ? -11.627 -32.647 -52.585 1.00 48.47  ? 175 ASP B OD1 1 
ATOM   3146 O OD2 . ASP B 1 132 ? -12.483 -32.753 -54.605 1.00 51.41  ? 175 ASP B OD2 1 
ATOM   3147 N N   . TRP B 1 133 ? -14.574 -31.064 -51.927 1.00 38.61  ? 176 TRP B N   1 
ATOM   3148 C CA  . TRP B 1 133 ? -15.196 -29.794 -52.283 1.00 40.33  ? 176 TRP B CA  1 
ATOM   3149 C C   . TRP B 1 133 ? -15.221 -29.583 -53.790 1.00 42.78  ? 176 TRP B C   1 
ATOM   3150 O O   . TRP B 1 133 ? -16.144 -28.948 -54.313 1.00 44.96  ? 176 TRP B O   1 
ATOM   3151 C CB  . TRP B 1 133 ? -14.459 -28.635 -51.611 1.00 42.49  ? 176 TRP B CB  1 
ATOM   3152 C CG  . TRP B 1 133 ? -13.078 -28.398 -52.157 1.00 44.96  ? 176 TRP B CG  1 
ATOM   3153 C CD1 . TRP B 1 133 ? -11.905 -28.879 -51.656 1.00 45.14  ? 176 TRP B CD1 1 
ATOM   3154 C CD2 . TRP B 1 133 ? -12.731 -27.619 -53.311 1.00 48.92  ? 176 TRP B CD2 1 
ATOM   3155 N NE1 . TRP B 1 133 ? -10.849 -28.450 -52.425 1.00 44.89  ? 176 TRP B NE1 1 
ATOM   3156 C CE2 . TRP B 1 133 ? -11.330 -27.675 -53.447 1.00 49.22  ? 176 TRP B CE2 1 
ATOM   3157 C CE3 . TRP B 1 133 ? -13.470 -26.881 -54.241 1.00 50.42  ? 176 TRP B CE3 1 
ATOM   3158 C CZ2 . TRP B 1 133 ? -10.652 -27.023 -54.476 1.00 51.07  ? 176 TRP B CZ2 1 
ATOM   3159 C CZ3 . TRP B 1 133 ? -12.795 -26.234 -55.263 1.00 53.12  ? 176 TRP B CZ3 1 
ATOM   3160 C CH2 . TRP B 1 133 ? -11.400 -26.309 -55.371 1.00 53.75  ? 176 TRP B CH2 1 
ATOM   3161 N N   . ARG B 1 134 ? -14.224 -30.106 -54.501 1.00 44.64  ? 177 ARG B N   1 
ATOM   3162 C CA  . ARG B 1 134 ? -14.091 -29.879 -55.933 1.00 46.44  ? 177 ARG B CA  1 
ATOM   3163 C C   . ARG B 1 134 ? -14.803 -30.950 -56.753 1.00 47.44  ? 177 ARG B C   1 
ATOM   3164 O O   . ARG B 1 134 ? -15.606 -30.630 -57.634 1.00 46.40  ? 177 ARG B O   1 
ATOM   3165 C CB  . ARG B 1 134 ? -12.606 -29.821 -56.306 1.00 50.69  ? 177 ARG B CB  1 
ATOM   3166 C CG  . ARG B 1 134 ? -12.335 -29.537 -57.771 1.00 59.13  ? 177 ARG B CG  1 
ATOM   3167 C CD  . ARG B 1 134 ? -10.886 -29.129 -57.989 1.00 66.07  ? 177 ARG B CD  1 
ATOM   3168 N NE  . ARG B 1 134 ? -10.572 -28.966 -59.403 1.00 80.61  ? 177 ARG B NE  1 
ATOM   3169 C CZ  . ARG B 1 134 ? -10.925 -27.918 -60.135 1.00 83.81  ? 177 ARG B CZ  1 
ATOM   3170 N NH1 . ARG B 1 134 ? -11.625 -26.919 -59.620 1.00 78.65  ? 177 ARG B NH1 1 
ATOM   3171 N NH2 . ARG B 1 134 ? -10.570 -27.871 -61.416 1.00 85.20  ? 177 ARG B NH2 1 
ATOM   3172 N N   . LYS B 1 135 ? -14.523 -32.223 -56.471 1.00 45.68  ? 178 LYS B N   1 
ATOM   3173 C CA  . LYS B 1 135 ? -15.063 -33.305 -57.285 1.00 47.48  ? 178 LYS B CA  1 
ATOM   3174 C C   . LYS B 1 135 ? -16.503 -33.662 -56.930 1.00 45.01  ? 178 LYS B C   1 
ATOM   3175 O O   . LYS B 1 135 ? -17.224 -34.176 -57.791 1.00 43.07  ? 178 LYS B O   1 
ATOM   3176 C CB  . LYS B 1 135 ? -14.168 -34.544 -57.156 1.00 48.84  ? 178 LYS B CB  1 
ATOM   3177 C CG  . LYS B 1 135 ? -12.697 -34.277 -57.485 1.00 55.82  ? 178 LYS B CG  1 
ATOM   3178 C CD  . LYS B 1 135 ? -11.795 -35.462 -57.141 1.00 66.77  ? 178 LYS B CD  1 
ATOM   3179 C CE  . LYS B 1 135 ? -11.597 -36.393 -58.329 1.00 72.77  ? 178 LYS B CE  1 
ATOM   3180 N NZ  . LYS B 1 135 ? -10.602 -37.463 -58.029 1.00 81.07  ? 178 LYS B NZ  1 
ATOM   3181 N N   . ASP B 1 136 ? -16.954 -33.404 -55.696 1.00 43.37  ? 179 ASP B N   1 
ATOM   3182 C CA  . ASP B 1 136 ? -18.276 -33.849 -55.263 1.00 43.97  ? 179 ASP B CA  1 
ATOM   3183 C C   . ASP B 1 136 ? -19.241 -32.706 -54.990 1.00 41.62  ? 179 ASP B C   1 
ATOM   3184 O O   . ASP B 1 136 ? -20.248 -32.566 -55.690 1.00 38.23  ? 179 ASP B O   1 
ATOM   3185 C CB  . ASP B 1 136 ? -18.131 -34.720 -54.003 1.00 40.94  ? 179 ASP B CB  1 
ATOM   3186 C CG  . ASP B 1 136 ? -17.390 -36.015 -54.268 1.00 41.70  ? 179 ASP B CG  1 
ATOM   3187 O OD1 . ASP B 1 136 ? -17.728 -36.702 -55.256 1.00 47.37  ? 179 ASP B OD1 1 
ATOM   3188 O OD2 . ASP B 1 136 ? -16.467 -36.343 -53.493 1.00 39.52  ? 179 ASP B OD2 1 
ATOM   3189 N N   . CYS B 1 137 ? -18.945 -31.842 -54.023 1.00 42.55  ? 180 CYS B N   1 
ATOM   3190 C CA  . CYS B 1 137 ? -19.889 -30.795 -53.650 1.00 41.97  ? 180 CYS B CA  1 
ATOM   3191 C C   . CYS B 1 137 ? -19.225 -29.868 -52.645 1.00 41.51  ? 180 CYS B C   1 
ATOM   3192 O O   . CYS B 1 137 ? -18.419 -30.300 -51.814 1.00 35.51  ? 180 CYS B O   1 
ATOM   3193 C CB  . CYS B 1 137 ? -21.189 -31.376 -53.071 1.00 43.34  ? 180 CYS B CB  1 
ATOM   3194 S SG  . CYS B 1 137 ? -21.007 -32.351 -51.558 1.00 44.90  ? 180 CYS B SG  1 
ATOM   3195 N N   . SER B 1 138 ? -19.590 -28.594 -52.721 1.00 37.26  ? 181 SER B N   1 
ATOM   3196 C CA  A SER B 1 138 ? -18.949 -27.574 -51.906 0.59 37.37  ? 181 SER B CA  1 
ATOM   3197 C CA  B SER B 1 138 ? -18.952 -27.571 -51.907 0.41 37.42  ? 181 SER B CA  1 
ATOM   3198 C C   . SER B 1 138 ? -19.562 -27.436 -50.518 1.00 33.65  ? 181 SER B C   1 
ATOM   3199 O O   . SER B 1 138 ? -18.878 -26.967 -49.603 1.00 32.18  ? 181 SER B O   1 
ATOM   3200 C CB  A SER B 1 138 ? -19.008 -26.224 -52.628 0.59 40.06  ? 181 SER B CB  1 
ATOM   3201 C CB  B SER B 1 138 ? -19.020 -26.222 -52.630 0.41 40.04  ? 181 SER B CB  1 
ATOM   3202 O OG  A SER B 1 138 ? -20.347 -25.834 -52.872 0.59 39.21  ? 181 SER B OG  1 
ATOM   3203 O OG  B SER B 1 138 ? -18.344 -26.280 -53.875 0.41 40.33  ? 181 SER B OG  1 
ATOM   3204 N N   . ASN B 1 139 ? -20.816 -27.838 -50.334 1.00 34.05  ? 182 ASN B N   1 
ATOM   3205 C CA  . ASN B 1 139 ? -21.507 -27.658 -49.055 1.00 32.43  ? 182 ASN B CA  1 
ATOM   3206 C C   . ASN B 1 139 ? -21.431 -28.922 -48.199 1.00 31.45  ? 182 ASN B C   1 
ATOM   3207 O O   . ASN B 1 139 ? -22.443 -29.480 -47.769 1.00 30.78  ? 182 ASN B O   1 
ATOM   3208 C CB  . ASN B 1 139 ? -22.956 -27.243 -49.298 1.00 34.37  ? 182 ASN B CB  1 
ATOM   3209 C CG  . ASN B 1 139 ? -23.066 -25.878 -49.950 1.00 36.32  ? 182 ASN B CG  1 
ATOM   3210 O OD1 . ASN B 1 139 ? -22.253 -24.991 -49.693 1.00 35.30  ? 182 ASN B OD1 1 
ATOM   3211 N ND2 . ASN B 1 139 ? -24.071 -25.704 -50.799 1.00 37.76  ? 182 ASN B ND2 1 
ATOM   3212 N N   . ASN B 1 140 ? -20.205 -29.357 -47.928 1.00 28.89  ? 183 ASN B N   1 
ATOM   3213 C CA  . ASN B 1 140 ? -19.957 -30.528 -47.101 1.00 28.84  ? 183 ASN B CA  1 
ATOM   3214 C C   . ASN B 1 140 ? -19.679 -30.114 -45.661 1.00 28.32  ? 183 ASN B C   1 
ATOM   3215 O O   . ASN B 1 140 ? -19.361 -28.954 -45.384 1.00 25.34  ? 183 ASN B O   1 
ATOM   3216 C CB  . ASN B 1 140 ? -18.775 -31.329 -47.654 1.00 26.24  ? 183 ASN B CB  1 
ATOM   3217 C CG  . ASN B 1 140 ? -17.495 -30.523 -47.693 1.00 26.43  ? 183 ASN B CG  1 
ATOM   3218 O OD1 . ASN B 1 140 ? -16.790 -30.410 -46.692 1.00 25.86  ? 183 ASN B OD1 1 
ATOM   3219 N ND2 . ASN B 1 140 ? -17.188 -29.957 -48.852 1.00 29.89  ? 183 ASN B ND2 1 
ATOM   3220 N N   . PRO B 1 141 ? -19.806 -31.044 -44.708 1.00 28.09  ? 184 PRO B N   1 
ATOM   3221 C CA  . PRO B 1 141 ? -19.680 -30.655 -43.291 1.00 25.15  ? 184 PRO B CA  1 
ATOM   3222 C C   . PRO B 1 141 ? -18.383 -29.943 -42.950 1.00 23.97  ? 184 PRO B C   1 
ATOM   3223 O O   . PRO B 1 141 ? -18.397 -29.005 -42.143 1.00 23.32  ? 184 PRO B O   1 
ATOM   3224 C CB  . PRO B 1 141 ? -19.791 -31.999 -42.554 1.00 25.51  ? 184 PRO B CB  1 
ATOM   3225 C CG  . PRO B 1 141 ? -20.589 -32.870 -43.475 1.00 28.51  ? 184 PRO B CG  1 
ATOM   3226 C CD  . PRO B 1 141 ? -20.212 -32.453 -44.868 1.00 26.03  ? 184 PRO B CD  1 
ATOM   3227 N N   . VAL B 1 142 ? -17.258 -30.359 -43.532 1.00 24.21  ? 185 VAL B N   1 
ATOM   3228 C CA  . VAL B 1 142 ? -15.977 -29.755 -43.180 1.00 23.38  ? 185 VAL B CA  1 
ATOM   3229 C C   . VAL B 1 142 ? -15.869 -28.347 -43.757 1.00 24.56  ? 185 VAL B C   1 
ATOM   3230 O O   . VAL B 1 142 ? -15.595 -27.382 -43.032 1.00 23.39  ? 185 VAL B O   1 
ATOM   3231 C CB  . VAL B 1 142 ? -14.817 -30.650 -43.656 1.00 24.66  ? 185 VAL B CB  1 
ATOM   3232 C CG1 . VAL B 1 142 ? -13.487 -29.935 -43.475 1.00 26.43  ? 185 VAL B CG1 1 
ATOM   3233 C CG2 . VAL B 1 142 ? -14.823 -31.975 -42.902 1.00 25.19  ? 185 VAL B CG2 1 
ATOM   3234 N N   . SER B 1 143 ? -16.092 -28.203 -45.066 1.00 22.95  ? 186 SER B N   1 
ATOM   3235 C CA  A SER B 1 143 ? -15.965 -26.893 -45.697 0.80 26.54  ? 186 SER B CA  1 
ATOM   3236 C CA  B SER B 1 143 ? -15.963 -26.893 -45.695 0.20 25.37  ? 186 SER B CA  1 
ATOM   3237 C C   . SER B 1 143 ? -16.940 -25.891 -45.091 1.00 25.77  ? 186 SER B C   1 
ATOM   3238 O O   . SER B 1 143 ? -16.586 -24.730 -44.860 1.00 27.71  ? 186 SER B O   1 
ATOM   3239 C CB  A SER B 1 143 ? -16.191 -27.010 -47.206 0.80 27.69  ? 186 SER B CB  1 
ATOM   3240 C CB  B SER B 1 143 ? -16.181 -27.011 -47.203 0.20 28.68  ? 186 SER B CB  1 
ATOM   3241 O OG  A SER B 1 143 ? -15.208 -27.830 -47.814 0.80 28.37  ? 186 SER B OG  1 
ATOM   3242 O OG  B SER B 1 143 ? -17.500 -27.437 -47.498 0.20 27.67  ? 186 SER B OG  1 
ATOM   3243 N N   . VAL B 1 144 ? -18.176 -26.320 -44.830 1.00 25.74  ? 187 VAL B N   1 
ATOM   3244 C CA  . VAL B 1 144 ? -19.165 -25.408 -44.263 1.00 22.50  ? 187 VAL B CA  1 
ATOM   3245 C C   . VAL B 1 144 ? -18.776 -25.010 -42.844 1.00 23.24  ? 187 VAL B C   1 
ATOM   3246 O O   . VAL B 1 144 ? -18.998 -23.869 -42.424 1.00 26.13  ? 187 VAL B O   1 
ATOM   3247 C CB  . VAL B 1 144 ? -20.567 -26.041 -44.314 1.00 25.04  ? 187 VAL B CB  1 
ATOM   3248 C CG1 . VAL B 1 144 ? -21.561 -25.186 -43.547 1.00 28.76  ? 187 VAL B CG1 1 
ATOM   3249 C CG2 . VAL B 1 144 ? -21.020 -26.215 -45.766 1.00 26.42  ? 187 VAL B CG2 1 
ATOM   3250 N N   . PHE B 1 145 ? -18.200 -25.938 -42.078 1.00 24.37  ? 188 PHE B N   1 
ATOM   3251 C CA  . PHE B 1 145 ? -17.755 -25.599 -40.731 1.00 24.36  ? 188 PHE B CA  1 
ATOM   3252 C C   . PHE B 1 145 ? -16.724 -24.476 -40.763 1.00 23.90  ? 188 PHE B C   1 
ATOM   3253 O O   . PHE B 1 145 ? -16.859 -23.471 -40.056 1.00 23.20  ? 188 PHE B O   1 
ATOM   3254 C CB  . PHE B 1 145 ? -17.173 -26.834 -40.035 1.00 22.03  ? 188 PHE B CB  1 
ATOM   3255 C CG  . PHE B 1 145 ? -16.454 -26.518 -38.751 1.00 22.73  ? 188 PHE B CG  1 
ATOM   3256 C CD1 . PHE B 1 145 ? -17.144 -26.467 -37.551 1.00 22.98  ? 188 PHE B CD1 1 
ATOM   3257 C CD2 . PHE B 1 145 ? -15.093 -26.257 -38.747 1.00 20.94  ? 188 PHE B CD2 1 
ATOM   3258 C CE1 . PHE B 1 145 ? -16.490 -26.166 -36.371 1.00 25.46  ? 188 PHE B CE1 1 
ATOM   3259 C CE2 . PHE B 1 145 ? -14.432 -25.954 -37.568 1.00 24.05  ? 188 PHE B CE2 1 
ATOM   3260 C CZ  . PHE B 1 145 ? -15.131 -25.909 -36.379 1.00 22.81  ? 188 PHE B CZ  1 
ATOM   3261 N N   . TRP B 1 146 ? -15.682 -24.631 -41.584 1.00 23.29  ? 189 TRP B N   1 
ATOM   3262 C CA  . TRP B 1 146 ? -14.564 -23.694 -41.541 1.00 24.72  ? 189 TRP B CA  1 
ATOM   3263 C C   . TRP B 1 146 ? -14.942 -22.332 -42.108 1.00 26.50  ? 189 TRP B C   1 
ATOM   3264 O O   . TRP B 1 146 ? -14.500 -21.299 -41.593 1.00 29.27  ? 189 TRP B O   1 
ATOM   3265 C CB  . TRP B 1 146 ? -13.363 -24.282 -42.280 1.00 24.62  ? 189 TRP B CB  1 
ATOM   3266 C CG  . TRP B 1 146 ? -12.693 -25.360 -41.485 1.00 27.09  ? 189 TRP B CG  1 
ATOM   3267 C CD1 . TRP B 1 146 ? -12.674 -26.696 -41.763 1.00 27.29  ? 189 TRP B CD1 1 
ATOM   3268 C CD2 . TRP B 1 146 ? -11.963 -25.195 -40.262 1.00 26.37  ? 189 TRP B CD2 1 
ATOM   3269 N NE1 . TRP B 1 146 ? -11.970 -27.372 -40.795 1.00 27.89  ? 189 TRP B NE1 1 
ATOM   3270 C CE2 . TRP B 1 146 ? -11.523 -26.473 -39.862 1.00 30.65  ? 189 TRP B CE2 1 
ATOM   3271 C CE3 . TRP B 1 146 ? -11.636 -24.090 -39.470 1.00 29.32  ? 189 TRP B CE3 1 
ATOM   3272 C CZ2 . TRP B 1 146 ? -10.771 -26.677 -38.705 1.00 29.05  ? 189 TRP B CZ2 1 
ATOM   3273 C CZ3 . TRP B 1 146 ? -10.890 -24.294 -38.319 1.00 26.79  ? 189 TRP B CZ3 1 
ATOM   3274 C CH2 . TRP B 1 146 ? -10.466 -25.577 -37.949 1.00 28.14  ? 189 TRP B CH2 1 
ATOM   3275 N N   . LYS B 1 147 ? -15.756 -22.299 -43.163 1.00 27.11  ? 190 LYS B N   1 
ATOM   3276 C CA  . LYS B 1 147 ? -16.191 -21.006 -43.680 1.00 27.89  ? 190 LYS B CA  1 
ATOM   3277 C C   . LYS B 1 147 ? -17.065 -20.280 -42.666 1.00 28.25  ? 190 LYS B C   1 
ATOM   3278 O O   . LYS B 1 147 ? -17.073 -19.044 -42.628 1.00 24.74  ? 190 LYS B O   1 
ATOM   3279 C CB  . LYS B 1 147 ? -16.926 -21.180 -45.010 1.00 31.16  ? 190 LYS B CB  1 
ATOM   3280 C CG  . LYS B 1 147 ? -18.425 -21.410 -44.901 1.00 34.56  ? 190 LYS B CG  1 
ATOM   3281 C CD  . LYS B 1 147 ? -19.032 -21.673 -46.277 1.00 38.11  ? 190 LYS B CD  1 
ATOM   3282 C CE  . LYS B 1 147 ? -20.495 -22.066 -46.178 1.00 38.13  ? 190 LYS B CE  1 
ATOM   3283 N NZ  . LYS B 1 147 ? -21.043 -22.492 -47.494 1.00 42.34  ? 190 LYS B NZ  1 
ATOM   3284 N N   . THR B 1 148 ? -17.789 -21.026 -41.829 1.00 25.12  ? 191 THR B N   1 
ATOM   3285 C CA  . THR B 1 148 ? -18.643 -20.402 -40.825 1.00 28.54  ? 191 THR B CA  1 
ATOM   3286 C C   . THR B 1 148 ? -17.824 -19.855 -39.658 1.00 28.27  ? 191 THR B C   1 
ATOM   3287 O O   . THR B 1 148 ? -17.948 -18.678 -39.303 1.00 28.63  ? 191 THR B O   1 
ATOM   3288 C CB  . THR B 1 148 ? -19.681 -21.411 -40.326 1.00 27.47  ? 191 THR B CB  1 
ATOM   3289 O OG1 . THR B 1 148 ? -20.418 -21.929 -41.440 1.00 27.76  ? 191 THR B OG1 1 
ATOM   3290 C CG2 . THR B 1 148 ? -20.643 -20.756 -39.345 1.00 31.18  ? 191 THR B CG2 1 
ATOM   3291 N N   . VAL B 1 149 ? -16.982 -20.693 -39.047 1.00 27.27  ? 192 VAL B N   1 
ATOM   3292 C CA  . VAL B 1 149 ? -16.206 -20.238 -37.896 1.00 28.40  ? 192 VAL B CA  1 
ATOM   3293 C C   . VAL B 1 149 ? -15.185 -19.187 -38.311 1.00 27.28  ? 192 VAL B C   1 
ATOM   3294 O O   . VAL B 1 149 ? -14.897 -18.256 -37.553 1.00 26.74  ? 192 VAL B O   1 
ATOM   3295 C CB  . VAL B 1 149 ? -15.524 -21.419 -37.180 1.00 28.94  ? 192 VAL B CB  1 
ATOM   3296 C CG1 . VAL B 1 149 ? -16.563 -22.338 -36.573 1.00 30.11  ? 192 VAL B CG1 1 
ATOM   3297 C CG2 . VAL B 1 149 ? -14.609 -22.180 -38.128 1.00 28.14  ? 192 VAL B CG2 1 
ATOM   3298 N N   . SER B 1 150 ? -14.602 -19.325 -39.504 1.00 27.63  ? 193 SER B N   1 
ATOM   3299 C CA  A SER B 1 150 ? -13.629 -18.338 -39.962 0.43 27.85  ? 193 SER B CA  1 
ATOM   3300 C CA  B SER B 1 150 ? -13.627 -18.338 -39.956 0.57 27.93  ? 193 SER B CA  1 
ATOM   3301 C C   . SER B 1 150 ? -14.279 -16.973 -40.150 1.00 29.11  ? 193 SER B C   1 
ATOM   3302 O O   . SER B 1 150 ? -13.673 -15.940 -39.842 1.00 27.55  ? 193 SER B O   1 
ATOM   3303 C CB  A SER B 1 150 ? -12.975 -18.806 -41.262 0.43 28.00  ? 193 SER B CB  1 
ATOM   3304 C CB  B SER B 1 150 ? -12.960 -18.814 -41.245 0.57 28.04  ? 193 SER B CB  1 
ATOM   3305 O OG  A SER B 1 150 ? -12.181 -19.959 -41.045 0.43 29.50  ? 193 SER B OG  1 
ATOM   3306 O OG  B SER B 1 150 ? -11.904 -17.950 -41.623 0.57 31.40  ? 193 SER B OG  1 
ATOM   3307 N N   . ARG B 1 151 ? -15.515 -16.947 -40.659 1.00 28.75  ? 194 ARG B N   1 
ATOM   3308 C CA  . ARG B 1 151 ? -16.207 -15.676 -40.853 1.00 31.16  ? 194 ARG B CA  1 
ATOM   3309 C C   . ARG B 1 151 ? -16.491 -14.992 -39.521 1.00 30.20  ? 194 ARG B C   1 
ATOM   3310 O O   . ARG B 1 151 ? -16.274 -13.784 -39.373 1.00 29.11  ? 194 ARG B O   1 
ATOM   3311 C CB  . ARG B 1 151 ? -17.511 -15.887 -41.623 1.00 30.65  ? 194 ARG B CB  1 
ATOM   3312 C CG  . ARG B 1 151 ? -18.251 -14.582 -41.889 1.00 36.33  ? 194 ARG B CG  1 
ATOM   3313 C CD  . ARG B 1 151 ? -19.390 -14.739 -42.885 1.00 40.89  ? 194 ARG B CD  1 
ATOM   3314 N NE  . ARG B 1 151 ? -20.682 -14.898 -42.226 1.00 47.03  ? 194 ARG B NE  1 
ATOM   3315 C CZ  . ARG B 1 151 ? -21.303 -16.056 -42.036 1.00 53.60  ? 194 ARG B CZ  1 
ATOM   3316 N NH1 . ARG B 1 151 ? -20.785 -17.199 -42.458 1.00 50.69  ? 194 ARG B NH1 1 
ATOM   3317 N NH2 . ARG B 1 151 ? -22.476 -16.066 -41.410 1.00 60.28  ? 194 ARG B NH2 1 
ATOM   3318 N N   . ARG B 1 152 ? -16.996 -15.748 -38.542 1.00 31.21  ? 195 ARG B N   1 
ATOM   3319 C CA  . ARG B 1 152 ? -17.274 -15.168 -37.231 1.00 33.18  ? 195 ARG B CA  1 
ATOM   3320 C C   . ARG B 1 152 ? -15.992 -14.683 -36.568 1.00 27.89  ? 195 ARG B C   1 
ATOM   3321 O O   . ARG B 1 152 ? -15.979 -13.634 -35.916 1.00 28.61  ? 195 ARG B O   1 
ATOM   3322 C CB  . ARG B 1 152 ? -17.984 -16.189 -36.344 1.00 35.84  ? 195 ARG B CB  1 
ATOM   3323 C CG  . ARG B 1 152 ? -19.398 -16.519 -36.793 1.00 44.43  ? 195 ARG B CG  1 
ATOM   3324 C CD  . ARG B 1 152 ? -19.969 -17.696 -36.021 1.00 51.27  ? 195 ARG B CD  1 
ATOM   3325 N NE  . ARG B 1 152 ? -21.374 -17.498 -35.681 1.00 58.13  ? 195 ARG B NE  1 
ATOM   3326 C CZ  . ARG B 1 152 ? -21.817 -17.091 -34.497 1.00 58.11  ? 195 ARG B CZ  1 
ATOM   3327 N NH1 . ARG B 1 152 ? -20.990 -16.834 -33.496 1.00 54.52  ? 195 ARG B NH1 1 
ATOM   3328 N NH2 . ARG B 1 152 ? -23.126 -16.943 -34.312 1.00 60.55  ? 195 ARG B NH2 1 
ATOM   3329 N N   . PHE B 1 153 ? -14.906 -15.443 -36.717 1.00 26.75  ? 196 PHE B N   1 
ATOM   3330 C CA  . PHE B 1 153 ? -13.617 -15.014 -36.184 1.00 27.76  ? 196 PHE B CA  1 
ATOM   3331 C C   . PHE B 1 153 ? -13.179 -13.700 -36.820 1.00 29.47  ? 196 PHE B C   1 
ATOM   3332 O O   . PHE B 1 153 ? -12.774 -12.762 -36.124 1.00 29.05  ? 196 PHE B O   1 
ATOM   3333 C CB  . PHE B 1 153 ? -12.582 -16.117 -36.422 1.00 26.79  ? 196 PHE B CB  1 
ATOM   3334 C CG  . PHE B 1 153 ? -11.341 -15.993 -35.584 1.00 25.33  ? 196 PHE B CG  1 
ATOM   3335 C CD1 . PHE B 1 153 ? -11.413 -16.026 -34.200 1.00 26.67  ? 196 PHE B CD1 1 
ATOM   3336 C CD2 . PHE B 1 153 ? -10.097 -15.876 -36.181 1.00 23.82  ? 196 PHE B CD2 1 
ATOM   3337 C CE1 . PHE B 1 153 ? -10.269 -15.923 -33.429 1.00 26.25  ? 196 PHE B CE1 1 
ATOM   3338 C CE2 . PHE B 1 153 ? -8.950  -15.773 -35.416 1.00 27.66  ? 196 PHE B CE2 1 
ATOM   3339 C CZ  . PHE B 1 153 ? -9.036  -15.797 -34.039 1.00 26.57  ? 196 PHE B CZ  1 
ATOM   3340 N N   . ALA B 1 154 ? -13.279 -13.604 -38.148 1.00 28.60  ? 197 ALA B N   1 
ATOM   3341 C CA  . ALA B 1 154 ? -12.904 -12.368 -38.826 1.00 26.84  ? 197 ALA B CA  1 
ATOM   3342 C C   . ALA B 1 154 ? -13.825 -11.220 -38.429 1.00 28.39  ? 197 ALA B C   1 
ATOM   3343 O O   . ALA B 1 154 ? -13.378 -10.076 -38.286 1.00 26.87  ? 197 ALA B O   1 
ATOM   3344 C CB  . ALA B 1 154 ? -12.924 -12.573 -40.341 1.00 26.51  ? 197 ALA B CB  1 
ATOM   3345 N N   . GLU B 1 155 ? -15.118 -11.505 -38.256 1.00 27.52  ? 198 GLU B N   1 
ATOM   3346 C CA  . GLU B 1 155 ? -16.064 -10.460 -37.882 1.00 28.58  ? 198 GLU B CA  1 
ATOM   3347 C C   . GLU B 1 155 ? -15.754 -9.879  -36.507 1.00 32.66  ? 198 GLU B C   1 
ATOM   3348 O O   . GLU B 1 155 ? -16.113 -8.731  -36.226 1.00 27.27  ? 198 GLU B O   1 
ATOM   3349 C CB  . GLU B 1 155 ? -17.490 -11.011 -37.907 1.00 29.49  ? 198 GLU B CB  1 
ATOM   3350 C CG  . GLU B 1 155 ? -18.080 -11.133 -39.303 1.00 33.46  ? 198 GLU B CG  1 
ATOM   3351 C CD  . GLU B 1 155 ? -19.431 -11.833 -39.313 1.00 37.16  ? 198 GLU B CD  1 
ATOM   3352 O OE1 . GLU B 1 155 ? -19.814 -12.412 -38.274 1.00 39.64  ? 198 GLU B OE1 1 
ATOM   3353 O OE2 . GLU B 1 155 ? -20.112 -11.805 -40.360 1.00 38.96  ? 198 GLU B OE2 1 
ATOM   3354 N N   . ALA B 1 156 ? -15.099 -10.655 -35.640 1.00 29.30  ? 199 ALA B N   1 
ATOM   3355 C CA  . ALA B 1 156 ? -14.825 -10.208 -34.278 1.00 33.33  ? 199 ALA B CA  1 
ATOM   3356 C C   . ALA B 1 156 ? -13.567 -9.354  -34.162 1.00 28.90  ? 199 ALA B C   1 
ATOM   3357 O O   . ALA B 1 156 ? -13.384 -8.690  -33.136 1.00 31.01  ? 199 ALA B O   1 
ATOM   3358 C CB  . ALA B 1 156 ? -14.695 -11.420 -33.347 1.00 31.55  ? 199 ALA B CB  1 
ATOM   3359 N N   . ALA B 1 157 ? -12.706 -9.346  -35.175 1.00 29.23  ? 200 ALA B N   1 
ATOM   3360 C CA  . ALA B 1 157 ? -11.445 -8.629  -35.080 1.00 30.47  ? 200 ALA B CA  1 
ATOM   3361 C C   . ALA B 1 157 ? -11.676 -7.119  -35.065 1.00 29.30  ? 200 ALA B C   1 
ATOM   3362 O O   . ALA B 1 157 ? -12.697 -6.612  -35.536 1.00 27.78  ? 200 ALA B O   1 
ATOM   3363 C CB  . ALA B 1 157 ? -10.528 -9.008  -36.243 1.00 29.47  ? 200 ALA B CB  1 
ATOM   3364 N N   . CYS B 1 158 ? -10.700 -6.399  -34.511 1.00 27.01  ? 201 CYS B N   1 
ATOM   3365 C CA  . CYS B 1 158 ? -10.790 -4.952  -34.386 1.00 31.31  ? 201 CYS B CA  1 
ATOM   3366 C C   . CYS B 1 158 ? -9.394  -4.348  -34.475 1.00 31.03  ? 201 CYS B C   1 
ATOM   3367 O O   . CYS B 1 158 ? -8.383  -5.042  -34.331 1.00 30.18  ? 201 CYS B O   1 
ATOM   3368 C CB  . CYS B 1 158 ? -11.451 -4.529  -33.065 1.00 32.79  ? 201 CYS B CB  1 
ATOM   3369 S SG  . CYS B 1 158 ? -10.413 -4.829  -31.610 1.00 38.90  ? 201 CYS B SG  1 
ATOM   3370 N N   . ASP B 1 159 ? -9.357  -3.036  -34.712 1.00 31.48  ? 202 ASP B N   1 
ATOM   3371 C CA  . ASP B 1 159 ? -8.113  -2.274  -34.746 1.00 32.60  ? 202 ASP B CA  1 
ATOM   3372 C C   . ASP B 1 159 ? -7.182  -2.790  -35.842 1.00 30.67  ? 202 ASP B C   1 
ATOM   3373 O O   . ASP B 1 159 ? -7.454  -2.583  -37.029 1.00 30.20  ? 202 ASP B O   1 
ATOM   3374 C CB  . ASP B 1 159 ? -7.429  -2.312  -33.376 1.00 32.80  ? 202 ASP B CB  1 
ATOM   3375 C CG  . ASP B 1 159 ? -6.275  -1.322  -33.271 1.00 35.95  ? 202 ASP B CG  1 
ATOM   3376 O OD1 . ASP B 1 159 ? -6.308  -0.292  -33.978 1.00 32.83  ? 202 ASP B OD1 1 
ATOM   3377 O OD2 . ASP B 1 159 ? -5.332  -1.577  -32.490 1.00 37.49  ? 202 ASP B OD2 1 
ATOM   3378 N N   . VAL B 1 160 ? -6.082  -3.442  -35.469 1.00 28.59  ? 203 VAL B N   1 
ATOM   3379 C CA  . VAL B 1 160 ? -5.106  -3.967  -36.421 1.00 30.82  ? 203 VAL B CA  1 
ATOM   3380 C C   . VAL B 1 160 ? -5.207  -5.488  -36.423 1.00 30.99  ? 203 VAL B C   1 
ATOM   3381 O O   . VAL B 1 160 ? -5.079  -6.129  -35.373 1.00 30.08  ? 203 VAL B O   1 
ATOM   3382 C CB  . VAL B 1 160 ? -3.678  -3.519  -36.077 1.00 30.58  ? 203 VAL B CB  1 
ATOM   3383 C CG1 . VAL B 1 160 ? -2.687  -4.078  -37.091 1.00 32.72  ? 203 VAL B CG1 1 
ATOM   3384 C CG2 . VAL B 1 160 ? -3.590  -2.003  -36.017 1.00 34.30  ? 203 VAL B CG2 1 
ATOM   3385 N N   . VAL B 1 161 ? -5.420  -6.061  -37.605 1.00 29.22  ? 204 VAL B N   1 
ATOM   3386 C CA  . VAL B 1 161 ? -5.487  -7.505  -37.794 1.00 29.21  ? 204 VAL B CA  1 
ATOM   3387 C C   . VAL B 1 161 ? -4.265  -7.935  -38.590 1.00 30.13  ? 204 VAL B C   1 
ATOM   3388 O O   . VAL B 1 161 ? -3.896  -7.288  -39.578 1.00 33.91  ? 204 VAL B O   1 
ATOM   3389 C CB  . VAL B 1 161 ? -6.784  -7.923  -38.514 1.00 32.81  ? 204 VAL B CB  1 
ATOM   3390 C CG1 . VAL B 1 161 ? -6.881  -9.442  -38.605 1.00 30.82  ? 204 VAL B CG1 1 
ATOM   3391 C CG2 . VAL B 1 161 ? -7.993  -7.339  -37.804 1.00 36.58  ? 204 VAL B CG2 1 
ATOM   3392 N N   . HIS B 1 162 ? -3.638  -9.024  -38.162 1.00 31.09  ? 205 HIS B N   1 
ATOM   3393 C CA  . HIS B 1 162 ? -2.441  -9.541  -38.806 1.00 31.15  ? 205 HIS B CA  1 
ATOM   3394 C C   . HIS B 1 162 ? -2.752  -10.840 -39.534 1.00 29.69  ? 205 HIS B C   1 
ATOM   3395 O O   . HIS B 1 162 ? -3.577  -11.641 -39.081 1.00 29.51  ? 205 HIS B O   1 
ATOM   3396 C CB  . HIS B 1 162 ? -1.325  -9.770  -37.786 1.00 34.71  ? 205 HIS B CB  1 
ATOM   3397 C CG  . HIS B 1 162 ? -0.886  -8.523  -37.084 1.00 37.74  ? 205 HIS B CG  1 
ATOM   3398 N ND1 . HIS B 1 162 ? -1.506  -8.051  -35.947 1.00 36.37  ? 205 HIS B ND1 1 
ATOM   3399 C CD2 . HIS B 1 162 ? 0.104   -7.644  -37.365 1.00 39.05  ? 205 HIS B CD2 1 
ATOM   3400 C CE1 . HIS B 1 162 ? -0.913  -6.938  -35.554 1.00 34.93  ? 205 HIS B CE1 1 
ATOM   3401 N NE2 . HIS B 1 162 ? 0.067   -6.669  -36.398 1.00 39.87  ? 205 HIS B NE2 1 
ATOM   3402 N N   . VAL B 1 163 ? -2.099  -11.033 -40.675 1.00 29.49  ? 206 VAL B N   1 
ATOM   3403 C CA  . VAL B 1 163 ? -2.188  -12.272 -41.436 1.00 29.78  ? 206 VAL B CA  1 
ATOM   3404 C C   . VAL B 1 163 ? -0.781  -12.686 -41.841 1.00 32.20  ? 206 VAL B C   1 
ATOM   3405 O O   . VAL B 1 163 ? -0.017  -11.871 -42.369 1.00 31.66  ? 206 VAL B O   1 
ATOM   3406 C CB  . VAL B 1 163 ? -3.088  -12.132 -42.680 1.00 28.39  ? 206 VAL B CB  1 
ATOM   3407 C CG1 . VAL B 1 163 ? -2.556  -11.059 -43.621 1.00 30.54  ? 206 VAL B CG1 1 
ATOM   3408 C CG2 . VAL B 1 163 ? -3.205  -13.477 -43.399 1.00 30.50  ? 206 VAL B CG2 1 
ATOM   3409 N N   . MET B 1 164 ? -0.440  -13.944 -41.587 1.00 31.75  ? 207 MET B N   1 
ATOM   3410 C CA  . MET B 1 164 ? 0.820   -14.508 -42.050 1.00 34.63  ? 207 MET B CA  1 
ATOM   3411 C C   . MET B 1 164 ? 0.610   -15.153 -43.413 1.00 36.04  ? 207 MET B C   1 
ATOM   3412 O O   . MET B 1 164 ? -0.339  -15.921 -43.605 1.00 33.24  ? 207 MET B O   1 
ATOM   3413 C CB  . MET B 1 164 ? 1.356   -15.531 -41.051 1.00 37.70  ? 207 MET B CB  1 
ATOM   3414 C CG  . MET B 1 164 ? 2.113   -14.912 -39.885 1.00 42.68  ? 207 MET B CG  1 
ATOM   3415 S SD  . MET B 1 164 ? 2.587   -16.112 -38.620 1.00 51.80  ? 207 MET B SD  1 
ATOM   3416 C CE  . MET B 1 164 ? 3.228   -17.441 -39.626 1.00 40.69  ? 207 MET B CE  1 
ATOM   3417 N N   . LEU B 1 165 ? 1.488   -14.828 -44.357 1.00 41.07  ? 208 LEU B N   1 
ATOM   3418 C CA  . LEU B 1 165 ? 1.423   -15.349 -45.712 1.00 41.83  ? 208 LEU B CA  1 
ATOM   3419 C C   . LEU B 1 165 ? 2.703   -16.108 -46.032 1.00 44.74  ? 208 LEU B C   1 
ATOM   3420 O O   . LEU B 1 165 ? 3.788   -15.761 -45.553 1.00 44.38  ? 208 LEU B O   1 
ATOM   3421 C CB  . LEU B 1 165 ? 1.214   -14.223 -46.730 1.00 39.51  ? 208 LEU B CB  1 
ATOM   3422 C CG  . LEU B 1 165 ? -0.074  -13.410 -46.570 1.00 38.41  ? 208 LEU B CG  1 
ATOM   3423 C CD1 . LEU B 1 165 ? -0.118  -12.269 -47.573 1.00 39.32  ? 208 LEU B CD1 1 
ATOM   3424 C CD2 . LEU B 1 165 ? -1.302  -14.299 -46.720 1.00 39.81  ? 208 LEU B CD2 1 
ATOM   3425 N N   . ASP B 1 166 ? 2.564   -17.150 -46.849 1.00 41.61  ? 209 ASP B N   1 
ATOM   3426 C CA  . ASP B 1 166 ? 3.681   -18.016 -47.221 1.00 44.71  ? 209 ASP B CA  1 
ATOM   3427 C C   . ASP B 1 166 ? 4.350   -17.431 -48.458 1.00 46.32  ? 209 ASP B C   1 
ATOM   3428 O O   . ASP B 1 166 ? 3.840   -17.557 -49.574 1.00 47.01  ? 209 ASP B O   1 
ATOM   3429 C CB  . ASP B 1 166 ? 3.191   -19.438 -47.468 1.00 46.30  ? 209 ASP B CB  1 
ATOM   3430 C CG  . ASP B 1 166 ? 4.303   -20.375 -47.901 1.00 51.48  ? 209 ASP B CG  1 
ATOM   3431 O OD1 . ASP B 1 166 ? 5.487   -19.989 -47.810 1.00 49.66  ? 209 ASP B OD1 1 
ATOM   3432 O OD2 . ASP B 1 166 ? 3.989   -21.501 -48.340 1.00 56.46  ? 209 ASP B OD2 1 
ATOM   3433 N N   . GLY B 1 167 ? 5.504   -16.797 -48.260 1.00 48.65  ? 210 GLY B N   1 
ATOM   3434 C CA  . GLY B 1 167 ? 6.247   -16.185 -49.340 1.00 52.21  ? 210 GLY B CA  1 
ATOM   3435 C C   . GLY B 1 167 ? 7.092   -17.128 -50.162 1.00 55.91  ? 210 GLY B C   1 
ATOM   3436 O O   . GLY B 1 167 ? 7.750   -16.687 -51.108 1.00 57.97  ? 210 GLY B O   1 
ATOM   3437 N N   . SER B 1 168 ? 7.103   -18.418 -49.828 1.00 56.84  ? 211 SER B N   1 
ATOM   3438 C CA  . SER B 1 168 ? 7.850   -19.408 -50.589 1.00 59.12  ? 211 SER B CA  1 
ATOM   3439 C C   . SER B 1 168 ? 7.062   -19.975 -51.763 1.00 60.84  ? 211 SER B C   1 
ATOM   3440 O O   . SER B 1 168 ? 7.632   -20.721 -52.566 1.00 61.87  ? 211 SER B O   1 
ATOM   3441 C CB  . SER B 1 168 ? 8.279   -20.559 -49.675 1.00 59.22  ? 211 SER B CB  1 
ATOM   3442 O OG  . SER B 1 168 ? 7.155   -21.307 -49.245 1.00 61.49  ? 211 SER B OG  1 
ATOM   3443 N N   . ARG B 1 169 ? 5.782   -19.641 -51.883 1.00 63.28  ? 212 ARG B N   1 
ATOM   3444 C CA  . ARG B 1 169 ? 4.925   -20.162 -52.937 1.00 69.48  ? 212 ARG B CA  1 
ATOM   3445 C C   . ARG B 1 169 ? 4.736   -19.118 -54.034 1.00 69.47  ? 212 ARG B C   1 
ATOM   3446 O O   . ARG B 1 169 ? 4.985   -17.926 -53.842 1.00 66.28  ? 212 ARG B O   1 
ATOM   3447 C CB  . ARG B 1 169 ? 3.566   -20.579 -52.369 1.00 73.83  ? 212 ARG B CB  1 
ATOM   3448 C CG  . ARG B 1 169 ? 3.056   -21.911 -52.898 1.00 78.86  ? 212 ARG B CG  1 
ATOM   3449 C CD  . ARG B 1 169 ? 3.828   -23.082 -52.307 1.00 80.63  ? 212 ARG B CD  1 
ATOM   3450 N NE  . ARG B 1 169 ? 3.483   -23.316 -50.909 1.00 81.19  ? 212 ARG B NE  1 
ATOM   3451 C CZ  . ARG B 1 169 ? 4.052   -24.234 -50.139 1.00 80.98  ? 212 ARG B CZ  1 
ATOM   3452 N NH1 . ARG B 1 169 ? 5.016   -25.018 -50.594 1.00 80.41  ? 212 ARG B NH1 1 
ATOM   3453 N NH2 . ARG B 1 169 ? 3.644   -24.368 -48.880 1.00 76.79  ? 212 ARG B NH2 1 
ATOM   3454 N N   . SER B 1 170 ? 4.290   -19.591 -55.200 1.00 75.10  ? 213 SER B N   1 
ATOM   3455 C CA  . SER B 1 170 ? 4.113   -18.699 -56.341 1.00 77.47  ? 213 SER B CA  1 
ATOM   3456 C C   . SER B 1 170 ? 3.039   -17.652 -56.071 1.00 74.50  ? 213 SER B C   1 
ATOM   3457 O O   . SER B 1 170 ? 3.222   -16.470 -56.383 1.00 78.17  ? 213 SER B O   1 
ATOM   3458 C CB  . SER B 1 170 ? 3.764   -19.511 -57.588 1.00 85.31  ? 213 SER B CB  1 
ATOM   3459 O OG  . SER B 1 170 ? 2.600   -20.292 -57.377 1.00 85.27  ? 213 SER B OG  1 
ATOM   3460 N N   . LYS B 1 171 ? 1.911   -18.067 -55.496 1.00 65.19  ? 214 LYS B N   1 
ATOM   3461 C CA  . LYS B 1 171 ? 0.801   -17.167 -55.185 1.00 57.26  ? 214 LYS B CA  1 
ATOM   3462 C C   . LYS B 1 171 ? 0.861   -16.858 -53.693 1.00 52.43  ? 214 LYS B C   1 
ATOM   3463 O O   . LYS B 1 171 ? 0.199   -17.501 -52.878 1.00 52.26  ? 214 LYS B O   1 
ATOM   3464 C CB  . LYS B 1 171 ? -0.531  -17.788 -55.590 1.00 56.74  ? 214 LYS B CB  1 
ATOM   3465 C CG  . LYS B 1 171 ? -0.764  -17.799 -57.094 1.00 59.13  ? 214 LYS B CG  1 
ATOM   3466 C CD  . LYS B 1 171 ? -2.123  -18.375 -57.469 1.00 59.12  ? 214 LYS B CD  1 
ATOM   3467 C CE  . LYS B 1 171 ? -2.091  -19.894 -57.552 1.00 64.71  ? 214 LYS B CE  1 
ATOM   3468 N NZ  . LYS B 1 171 ? -3.242  -20.427 -58.335 1.00 68.17  ? 214 LYS B NZ  1 
ATOM   3469 N N   . ILE B 1 172 ? 1.664   -15.852 -53.338 1.00 51.32  ? 215 ILE B N   1 
ATOM   3470 C CA  . ILE B 1 172 ? 1.817   -15.486 -51.932 1.00 48.59  ? 215 ILE B CA  1 
ATOM   3471 C C   . ILE B 1 172 ? 0.457   -15.163 -51.328 1.00 45.84  ? 215 ILE B C   1 
ATOM   3472 O O   . ILE B 1 172 ? 0.126   -15.603 -50.220 1.00 45.93  ? 215 ILE B O   1 
ATOM   3473 C CB  . ILE B 1 172 ? 2.799   -14.309 -51.786 1.00 47.40  ? 215 ILE B CB  1 
ATOM   3474 C CG1 . ILE B 1 172 ? 4.136   -14.650 -52.453 1.00 51.77  ? 215 ILE B CG1 1 
ATOM   3475 C CG2 . ILE B 1 172 ? 3.015   -13.976 -50.317 1.00 46.85  ? 215 ILE B CG2 1 
ATOM   3476 C CD1 . ILE B 1 172 ? 5.190   -13.570 -52.320 1.00 53.41  ? 215 ILE B CD1 1 
ATOM   3477 N N   . PHE B 1 173 ? -0.351  -14.390 -52.047 1.00 42.24  ? 216 PHE B N   1 
ATOM   3478 C CA  . PHE B 1 173 ? -1.763  -14.227 -51.734 1.00 41.18  ? 216 PHE B CA  1 
ATOM   3479 C C   . PHE B 1 173 ? -2.583  -15.024 -52.738 1.00 42.25  ? 216 PHE B C   1 
ATOM   3480 O O   . PHE B 1 173 ? -2.392  -14.886 -53.952 1.00 42.08  ? 216 PHE B O   1 
ATOM   3481 C CB  . PHE B 1 173 ? -2.189  -12.761 -51.772 1.00 39.44  ? 216 PHE B CB  1 
ATOM   3482 C CG  . PHE B 1 173 ? -3.678  -12.576 -51.801 1.00 35.93  ? 216 PHE B CG  1 
ATOM   3483 C CD1 . PHE B 1 173 ? -4.445  -12.878 -50.691 1.00 35.13  ? 216 PHE B CD1 1 
ATOM   3484 C CD2 . PHE B 1 173 ? -4.313  -12.113 -52.942 1.00 39.15  ? 216 PHE B CD2 1 
ATOM   3485 C CE1 . PHE B 1 173 ? -5.817  -12.717 -50.712 1.00 35.24  ? 216 PHE B CE1 1 
ATOM   3486 C CE2 . PHE B 1 173 ? -5.687  -11.948 -52.969 1.00 37.35  ? 216 PHE B CE2 1 
ATOM   3487 C CZ  . PHE B 1 173 ? -6.438  -12.252 -51.853 1.00 34.07  ? 216 PHE B CZ  1 
ATOM   3488 N N   . ASP B 1 174 ? -3.497  -15.846 -52.231 1.00 40.63  ? 217 ASP B N   1 
ATOM   3489 C CA  . ASP B 1 174 ? -4.313  -16.723 -53.058 1.00 45.51  ? 217 ASP B CA  1 
ATOM   3490 C C   . ASP B 1 174 ? -5.780  -16.448 -52.763 1.00 42.86  ? 217 ASP B C   1 
ATOM   3491 O O   . ASP B 1 174 ? -6.248  -16.688 -51.644 1.00 39.80  ? 217 ASP B O   1 
ATOM   3492 C CB  . ASP B 1 174 ? -3.968  -18.192 -52.796 1.00 46.30  ? 217 ASP B CB  1 
ATOM   3493 C CG  . ASP B 1 174 ? -4.660  -19.134 -53.761 1.00 49.81  ? 217 ASP B CG  1 
ATOM   3494 O OD1 . ASP B 1 174 ? -5.346  -18.645 -54.682 1.00 51.52  ? 217 ASP B OD1 1 
ATOM   3495 O OD2 . ASP B 1 174 ? -4.518  -20.365 -53.601 1.00 52.79  ? 217 ASP B OD2 1 
ATOM   3496 N N   . LYS B 1 175 ? -6.504  -15.946 -53.766 1.00 40.05  ? 218 LYS B N   1 
ATOM   3497 C CA  . LYS B 1 175 ? -7.941  -15.760 -53.607 1.00 42.53  ? 218 LYS B CA  1 
ATOM   3498 C C   . LYS B 1 175 ? -8.635  -17.072 -53.270 1.00 43.74  ? 218 LYS B C   1 
ATOM   3499 O O   . LYS B 1 175 ? -9.681  -17.072 -52.612 1.00 43.69  ? 218 LYS B O   1 
ATOM   3500 C CB  . LYS B 1 175 ? -8.543  -15.169 -54.883 1.00 45.25  ? 218 LYS B CB  1 
ATOM   3501 C CG  . LYS B 1 175 ? -7.974  -13.819 -55.282 1.00 44.91  ? 218 LYS B CG  1 
ATOM   3502 C CD  . LYS B 1 175 ? -8.749  -13.209 -56.446 1.00 49.13  ? 218 LYS B CD  1 
ATOM   3503 C CE  . LYS B 1 175 ? -8.504  -13.958 -57.750 1.00 51.40  ? 218 LYS B CE  1 
ATOM   3504 N NZ  . LYS B 1 175 ? -7.086  -13.865 -58.200 1.00 52.64  ? 218 LYS B NZ  1 
ATOM   3505 N N   . ASP B 1 176 ? -8.067  -18.195 -53.705 1.00 46.54  ? 219 ASP B N   1 
ATOM   3506 C CA  . ASP B 1 176 ? -8.682  -19.508 -53.520 1.00 52.09  ? 219 ASP B CA  1 
ATOM   3507 C C   . ASP B 1 176 ? -8.250  -20.114 -52.182 1.00 49.29  ? 219 ASP B C   1 
ATOM   3508 O O   . ASP B 1 176 ? -7.656  -21.189 -52.107 1.00 51.02  ? 219 ASP B O   1 
ATOM   3509 C CB  . ASP B 1 176 ? -8.319  -20.421 -54.687 1.00 59.26  ? 219 ASP B CB  1 
ATOM   3510 C CG  . ASP B 1 176 ? -9.171  -21.673 -54.736 1.00 65.25  ? 219 ASP B CG  1 
ATOM   3511 O OD1 . ASP B 1 176 ? -10.221 -21.705 -54.062 1.00 61.02  ? 219 ASP B OD1 1 
ATOM   3512 O OD2 . ASP B 1 176 ? -8.788  -22.626 -55.448 1.00 69.27  ? 219 ASP B OD2 1 
ATOM   3513 N N   . SER B 1 177 ? -8.564  -19.391 -51.110 1.00 42.64  ? 220 SER B N   1 
ATOM   3514 C CA  . SER B 1 177 ? -8.218  -19.823 -49.765 1.00 39.56  ? 220 SER B CA  1 
ATOM   3515 C C   . SER B 1 177 ? -9.257  -19.281 -48.795 1.00 37.60  ? 220 SER B C   1 
ATOM   3516 O O   . SER B 1 177 ? -10.065 -18.414 -49.137 1.00 37.86  ? 220 SER B O   1 
ATOM   3517 C CB  . SER B 1 177 ? -6.813  -19.358 -49.366 1.00 38.81  ? 220 SER B CB  1 
ATOM   3518 O OG  . SER B 1 177 ? -6.775  -17.956 -49.159 1.00 35.48  ? 220 SER B OG  1 
ATOM   3519 N N   . THR B 1 178 ? -9.231  -19.812 -47.570 1.00 33.53  ? 221 THR B N   1 
ATOM   3520 C CA  . THR B 1 178 ? -10.132 -19.314 -46.537 1.00 35.07  ? 221 THR B CA  1 
ATOM   3521 C C   . THR B 1 178 ? -9.876  -17.837 -46.259 1.00 32.12  ? 221 THR B C   1 
ATOM   3522 O O   . THR B 1 178 ? -10.817 -17.062 -46.056 1.00 30.81  ? 221 THR B O   1 
ATOM   3523 C CB  . THR B 1 178 ? -9.969  -20.130 -45.255 1.00 32.90  ? 221 THR B CB  1 
ATOM   3524 O OG1 . THR B 1 178 ? -9.860  -21.518 -45.586 1.00 36.36  ? 221 THR B OG1 1 
ATOM   3525 C CG2 . THR B 1 178 ? -11.164 -19.927 -44.335 1.00 29.77  ? 221 THR B CG2 1 
ATOM   3526 N N   . PHE B 1 179 ? -8.606  -17.432 -46.233 1.00 29.39  ? 222 PHE B N   1 
ATOM   3527 C CA  . PHE B 1 179 ? -8.289  -16.023 -46.033 1.00 30.26  ? 222 PHE B CA  1 
ATOM   3528 C C   . PHE B 1 179 ? -8.777  -15.178 -47.204 1.00 30.33  ? 222 PHE B C   1 
ATOM   3529 O O   . PHE B 1 179 ? -9.437  -14.150 -47.009 1.00 28.55  ? 222 PHE B O   1 
ATOM   3530 C CB  . PHE B 1 179 ? -6.783  -15.848 -45.838 1.00 28.40  ? 222 PHE B CB  1 
ATOM   3531 C CG  . PHE B 1 179 ? -6.333  -14.413 -45.857 1.00 30.07  ? 222 PHE B CG  1 
ATOM   3532 C CD1 . PHE B 1 179 ? -6.625  -13.567 -44.799 1.00 25.92  ? 222 PHE B CD1 1 
ATOM   3533 C CD2 . PHE B 1 179 ? -5.618  -13.911 -46.933 1.00 27.55  ? 222 PHE B CD2 1 
ATOM   3534 C CE1 . PHE B 1 179 ? -6.213  -12.251 -44.813 1.00 29.79  ? 222 PHE B CE1 1 
ATOM   3535 C CE2 . PHE B 1 179 ? -5.203  -12.592 -46.954 1.00 32.68  ? 222 PHE B CE2 1 
ATOM   3536 C CZ  . PHE B 1 179 ? -5.498  -11.761 -45.892 1.00 32.78  ? 222 PHE B CZ  1 
ATOM   3537 N N   . GLY B 1 180 ? -8.471  -15.604 -48.432 1.00 30.81  ? 223 GLY B N   1 
ATOM   3538 C CA  . GLY B 1 180 ? -8.730  -14.779 -49.599 1.00 33.14  ? 223 GLY B CA  1 
ATOM   3539 C C   . GLY B 1 180 ? -10.186 -14.695 -50.007 1.00 32.61  ? 223 GLY B C   1 
ATOM   3540 O O   . GLY B 1 180 ? -10.576 -13.725 -50.665 1.00 35.00  ? 223 GLY B O   1 
ATOM   3541 N N   . SER B 1 181 ? -10.999 -15.683 -49.636 1.00 31.81  ? 224 SER B N   1 
ATOM   3542 C CA  . SER B 1 181 ? -12.391 -15.732 -50.053 1.00 33.62  ? 224 SER B CA  1 
ATOM   3543 C C   . SER B 1 181 ? -13.383 -15.663 -48.900 1.00 33.16  ? 224 SER B C   1 
ATOM   3544 O O   . SER B 1 181 ? -14.591 -15.618 -49.157 1.00 33.26  ? 224 SER B O   1 
ATOM   3545 C CB  . SER B 1 181 ? -12.655 -17.011 -50.867 1.00 39.42  ? 224 SER B CB  1 
ATOM   3546 O OG  . SER B 1 181 ? -12.093 -16.911 -52.165 1.00 39.23  ? 224 SER B OG  1 
ATOM   3547 N N   . VAL B 1 182 ? -12.923 -15.673 -47.648 1.00 31.21  ? 225 VAL B N   1 
ATOM   3548 C CA  . VAL B 1 182 ? -13.833 -15.550 -46.514 1.00 29.36  ? 225 VAL B CA  1 
ATOM   3549 C C   . VAL B 1 182 ? -13.380 -14.443 -45.567 1.00 31.01  ? 225 VAL B C   1 
ATOM   3550 O O   . VAL B 1 182 ? -14.136 -13.505 -45.290 1.00 29.33  ? 225 VAL B O   1 
ATOM   3551 C CB  . VAL B 1 182 ? -13.965 -16.890 -45.762 1.00 31.03  ? 225 VAL B CB  1 
ATOM   3552 C CG1 . VAL B 1 182 ? -14.922 -16.746 -44.582 1.00 28.48  ? 225 VAL B CG1 1 
ATOM   3553 C CG2 . VAL B 1 182 ? -14.444 -17.988 -46.707 1.00 32.45  ? 225 VAL B CG2 1 
ATOM   3554 N N   . GLU B 1 183 ? -12.143 -14.540 -45.071 1.00 30.24  ? 226 GLU B N   1 
ATOM   3555 C CA  . GLU B 1 183 ? -11.727 -13.706 -43.946 1.00 26.95  ? 226 GLU B CA  1 
ATOM   3556 C C   . GLU B 1 183 ? -11.578 -12.241 -44.346 1.00 28.17  ? 226 GLU B C   1 
ATOM   3557 O O   . GLU B 1 183 ? -12.044 -11.345 -43.633 1.00 26.44  ? 226 GLU B O   1 
ATOM   3558 C CB  . GLU B 1 183 ? -10.415 -14.236 -43.365 1.00 28.12  ? 226 GLU B CB  1 
ATOM   3559 C CG  . GLU B 1 183 ? -10.501 -15.663 -42.835 1.00 31.18  ? 226 GLU B CG  1 
ATOM   3560 C CD  . GLU B 1 183 ? -9.143  -16.246 -42.490 1.00 28.82  ? 226 GLU B CD  1 
ATOM   3561 O OE1 . GLU B 1 183 ? -8.120  -15.595 -42.789 1.00 30.32  ? 226 GLU B OE1 1 
ATOM   3562 O OE2 . GLU B 1 183 ? -9.097  -17.356 -41.921 1.00 30.68  ? 226 GLU B OE2 1 
ATOM   3563 N N   . VAL B 1 184 ? -10.928 -11.974 -45.483 1.00 26.84  ? 227 VAL B N   1 
ATOM   3564 C CA  A VAL B 1 184 ? -10.657 -10.595 -45.881 0.47 28.00  ? 227 VAL B CA  1 
ATOM   3565 C CA  B VAL B 1 184 ? -10.655 -10.592 -45.859 0.53 28.06  ? 227 VAL B CA  1 
ATOM   3566 C C   . VAL B 1 184 ? -11.947 -9.834  -46.143 1.00 29.02  ? 227 VAL B C   1 
ATOM   3567 O O   . VAL B 1 184 ? -12.018 -8.618  -45.929 1.00 28.30  ? 227 VAL B O   1 
ATOM   3568 C CB  A VAL B 1 184 ? -9.743  -10.554 -47.123 0.47 28.54  ? 227 VAL B CB  1 
ATOM   3569 C CB  B VAL B 1 184 ? -9.698  -10.550 -47.066 0.53 29.77  ? 227 VAL B CB  1 
ATOM   3570 C CG1 A VAL B 1 184 ? -8.399  -11.149 -46.807 0.47 28.55  ? 227 VAL B CG1 1 
ATOM   3571 C CG1 B VAL B 1 184 ? -10.395 -11.059 -48.324 0.53 29.37  ? 227 VAL B CG1 1 
ATOM   3572 C CG2 A VAL B 1 184 ? -10.396 -11.270 -48.305 0.47 29.36  ? 227 VAL B CG2 1 
ATOM   3573 C CG2 B VAL B 1 184 ? -9.161  -9.141  -47.272 0.53 29.95  ? 227 VAL B CG2 1 
ATOM   3574 N N   . HIS B 1 185 ? -12.975 -10.520 -46.630 1.00 28.52  ? 228 HIS B N   1 
ATOM   3575 C CA  . HIS B 1 185 ? -14.229 -9.873  -46.985 1.00 29.84  ? 228 HIS B CA  1 
ATOM   3576 C C   . HIS B 1 185 ? -15.181 -9.722  -45.808 1.00 29.33  ? 228 HIS B C   1 
ATOM   3577 O O   . HIS B 1 185 ? -16.267 -9.160  -45.982 1.00 30.30  ? 228 HIS B O   1 
ATOM   3578 C CB  . HIS B 1 185 ? -14.923 -10.658 -48.102 1.00 29.35  ? 228 HIS B CB  1 
ATOM   3579 C CG  . HIS B 1 185 ? -14.031 -10.961 -49.262 1.00 30.51  ? 228 HIS B CG  1 
ATOM   3580 N ND1 . HIS B 1 185 ? -13.612 -9.995  -50.150 1.00 29.62  ? 228 HIS B ND1 1 
ATOM   3581 C CD2 . HIS B 1 185 ? -13.471 -12.122 -49.676 1.00 31.53  ? 228 HIS B CD2 1 
ATOM   3582 C CE1 . HIS B 1 185 ? -12.835 -10.547 -51.063 1.00 32.87  ? 228 HIS B CE1 1 
ATOM   3583 N NE2 . HIS B 1 185 ? -12.732 -11.838 -50.798 1.00 34.20  ? 228 HIS B NE2 1 
ATOM   3584 N N   . ASN B 1 186 ? -14.809 -10.202 -44.622 1.00 29.06  ? 229 ASN B N   1 
ATOM   3585 C CA  . ASN B 1 186 ? -15.679 -10.131 -43.458 1.00 28.45  ? 229 ASN B CA  1 
ATOM   3586 C C   . ASN B 1 186 ? -15.031 -9.421  -42.278 1.00 27.04  ? 229 ASN B C   1 
ATOM   3587 O O   . ASN B 1 186 ? -15.626 -9.376  -41.194 1.00 25.70  ? 229 ASN B O   1 
ATOM   3588 C CB  . ASN B 1 186 ? -16.133 -11.540 -43.060 1.00 26.85  ? 229 ASN B CB  1 
ATOM   3589 C CG  . ASN B 1 186 ? -17.159 -12.102 -44.025 1.00 30.92  ? 229 ASN B CG  1 
ATOM   3590 O OD1 . ASN B 1 186 ? -18.342 -11.769 -43.949 1.00 27.83  ? 229 ASN B OD1 1 
ATOM   3591 N ND2 . ASN B 1 186 ? -16.711 -12.957 -44.939 1.00 29.82  ? 229 ASN B ND2 1 
ATOM   3592 N N   . LEU B 1 187 ? -13.832 -8.872  -42.453 1.00 28.14  ? 230 LEU B N   1 
ATOM   3593 C CA  . LEU B 1 187 ? -13.340 -7.860  -41.529 1.00 27.72  ? 230 LEU B CA  1 
ATOM   3594 C C   . LEU B 1 187 ? -14.250 -6.639  -41.603 1.00 28.55  ? 230 LEU B C   1 
ATOM   3595 O O   . LEU B 1 187 ? -14.528 -6.127  -42.692 1.00 25.53  ? 230 LEU B O   1 
ATOM   3596 C CB  . LEU B 1 187 ? -11.906 -7.469  -41.878 1.00 28.40  ? 230 LEU B CB  1 
ATOM   3597 C CG  . LEU B 1 187 ? -10.880 -8.600  -41.923 1.00 26.65  ? 230 LEU B CG  1 
ATOM   3598 C CD1 . LEU B 1 187 ? -9.579  -8.099  -42.534 1.00 28.63  ? 230 LEU B CD1 1 
ATOM   3599 C CD2 . LEU B 1 187 ? -10.640 -9.169  -40.539 1.00 26.85  ? 230 LEU B CD2 1 
ATOM   3600 N N   . GLN B 1 188 ? -14.707 -6.169  -40.447 1.00 27.32  ? 231 GLN B N   1 
ATOM   3601 C CA  . GLN B 1 188 ? -15.662 -5.066  -40.417 1.00 31.46  ? 231 GLN B CA  1 
ATOM   3602 C C   . GLN B 1 188 ? -14.917 -3.738  -40.481 1.00 33.12  ? 231 GLN B C   1 
ATOM   3603 O O   . GLN B 1 188 ? -14.141 -3.432  -39.572 1.00 31.51  ? 231 GLN B O   1 
ATOM   3604 C CB  . GLN B 1 188 ? -16.511 -5.127  -39.156 1.00 30.10  ? 231 GLN B CB  1 
ATOM   3605 C CG  . GLN B 1 188 ? -17.365 -6.379  -39.064 1.00 34.59  ? 231 GLN B CG  1 
ATOM   3606 C CD  . GLN B 1 188 ? -18.441 -6.281  -38.002 1.00 38.53  ? 231 GLN B CD  1 
ATOM   3607 O OE1 . GLN B 1 188 ? -19.300 -5.399  -38.053 1.00 40.93  ? 231 GLN B OE1 1 
ATOM   3608 N NE2 . GLN B 1 188 ? -18.401 -7.189  -37.032 1.00 34.18  ? 231 GLN B NE2 1 
ATOM   3609 N N   . PRO B 1 189 ? -15.124 -2.924  -41.525 1.00 33.80  ? 232 PRO B N   1 
ATOM   3610 C CA  . PRO B 1 189 ? -14.399 -1.643  -41.595 1.00 35.03  ? 232 PRO B CA  1 
ATOM   3611 C C   . PRO B 1 189 ? -14.674 -0.725  -40.420 1.00 37.04  ? 232 PRO B C   1 
ATOM   3612 O O   . PRO B 1 189 ? -13.818 0.100   -40.076 1.00 38.61  ? 232 PRO B O   1 
ATOM   3613 C CB  . PRO B 1 189 ? -14.893 -1.033  -42.915 1.00 36.92  ? 232 PRO B CB  1 
ATOM   3614 C CG  . PRO B 1 189 ? -15.368 -2.195  -43.721 1.00 34.26  ? 232 PRO B CG  1 
ATOM   3615 C CD  . PRO B 1 189 ? -15.934 -3.164  -42.732 1.00 34.34  ? 232 PRO B CD  1 
ATOM   3616 N N   . GLU B 1 190 ? -15.849 -0.831  -39.796 1.00 37.77  ? 233 GLU B N   1 
ATOM   3617 C CA  . GLU B 1 190 ? -16.143 0.000   -38.635 1.00 47.12  ? 233 GLU B CA  1 
ATOM   3618 C C   . GLU B 1 190 ? -15.241 -0.319  -37.448 1.00 44.15  ? 233 GLU B C   1 
ATOM   3619 O O   . GLU B 1 190 ? -15.055 0.541   -36.581 1.00 48.87  ? 233 GLU B O   1 
ATOM   3620 C CB  . GLU B 1 190 ? -17.609 -0.163  -38.222 1.00 51.14  ? 233 GLU B CB  1 
ATOM   3621 C CG  . GLU B 1 190 ? -18.616 0.411   -39.211 1.00 59.93  ? 233 GLU B CG  1 
ATOM   3622 C CD  . GLU B 1 190 ? -18.781 -0.444  -40.456 1.00 63.21  ? 233 GLU B CD  1 
ATOM   3623 O OE1 . GLU B 1 190 ? -18.444 -1.648  -40.406 1.00 49.54  ? 233 GLU B OE1 1 
ATOM   3624 O OE2 . GLU B 1 190 ? -19.246 0.088   -41.487 1.00 66.33  ? 233 GLU B OE2 1 
ATOM   3625 N N   . LYS B 1 191 ? -14.680 -1.527  -37.389 1.00 38.06  ? 234 LYS B N   1 
ATOM   3626 C CA  . LYS B 1 191 ? -13.863 -1.966  -36.264 1.00 36.33  ? 234 LYS B CA  1 
ATOM   3627 C C   . LYS B 1 191 ? -12.391 -2.125  -36.606 1.00 34.48  ? 234 LYS B C   1 
ATOM   3628 O O   . LYS B 1 191 ? -11.542 -1.926  -35.733 1.00 31.40  ? 234 LYS B O   1 
ATOM   3629 C CB  . LYS B 1 191 ? -14.378 -3.309  -35.727 1.00 36.87  ? 234 LYS B CB  1 
ATOM   3630 C CG  . LYS B 1 191 ? -15.864 -3.323  -35.416 1.00 41.34  ? 234 LYS B CG  1 
ATOM   3631 C CD  . LYS B 1 191 ? -16.397 -4.738  -35.276 1.00 36.31  ? 234 LYS B CD  1 
ATOM   3632 C CE  . LYS B 1 191 ? -15.763 -5.473  -34.112 1.00 36.28  ? 234 LYS B CE  1 
ATOM   3633 N NZ  . LYS B 1 191 ? -16.439 -6.775  -33.865 1.00 37.21  ? 234 LYS B NZ  1 
ATOM   3634 N N   . VAL B 1 192 ? -12.076 -2.487  -37.846 1.00 34.48  ? 235 VAL B N   1 
ATOM   3635 C CA  . VAL B 1 192 ? -10.712 -2.763  -38.276 1.00 33.99  ? 235 VAL B CA  1 
ATOM   3636 C C   . VAL B 1 192 ? -10.196 -1.560  -39.049 1.00 32.95  ? 235 VAL B C   1 
ATOM   3637 O O   . VAL B 1 192 ? -10.826 -1.118  -40.017 1.00 33.68  ? 235 VAL B O   1 
ATOM   3638 C CB  . VAL B 1 192 ? -10.650 -4.033  -39.143 1.00 27.89  ? 235 VAL B CB  1 
ATOM   3639 C CG1 . VAL B 1 192 ? -9.223  -4.299  -39.601 1.00 29.47  ? 235 VAL B CG1 1 
ATOM   3640 C CG2 . VAL B 1 192 ? -11.201 -5.224  -38.381 1.00 30.77  ? 235 VAL B CG2 1 
ATOM   3641 N N   . GLN B 1 193 ? -9.046  -1.038  -38.629 1.00 30.91  ? 236 GLN B N   1 
ATOM   3642 C CA  . GLN B 1 193 ? -8.402  0.055   -39.343 1.00 37.41  ? 236 GLN B CA  1 
ATOM   3643 C C   . GLN B 1 193 ? -7.380  -0.442  -40.356 1.00 36.68  ? 236 GLN B C   1 
ATOM   3644 O O   . GLN B 1 193 ? -7.244  0.145   -41.435 1.00 37.67  ? 236 GLN B O   1 
ATOM   3645 C CB  . GLN B 1 193 ? -7.714  1.006   -38.358 1.00 41.61  ? 236 GLN B CB  1 
ATOM   3646 C CG  . GLN B 1 193 ? -8.515  2.256   -38.031 1.00 52.73  ? 236 GLN B CG  1 
ATOM   3647 C CD  . GLN B 1 193 ? -9.760  1.956   -37.224 1.00 52.67  ? 236 GLN B CD  1 
ATOM   3648 O OE1 . GLN B 1 193 ? -9.719  1.197   -36.255 1.00 51.53  ? 236 GLN B OE1 1 
ATOM   3649 N NE2 . GLN B 1 193 ? -10.879 2.549   -37.623 1.00 45.37  ? 236 GLN B NE2 1 
ATOM   3650 N N   . THR B 1 194 ? -6.658  -1.515  -40.032 1.00 32.51  ? 237 THR B N   1 
ATOM   3651 C CA  . THR B 1 194 ? -5.536  -1.957  -40.844 1.00 33.70  ? 237 THR B CA  1 
ATOM   3652 C C   . THR B 1 194 ? -5.447  -3.473  -40.857 1.00 33.47  ? 237 THR B C   1 
ATOM   3653 O O   . THR B 1 194 ? -5.680  -4.128  -39.837 1.00 30.57  ? 237 THR B O   1 
ATOM   3654 C CB  . THR B 1 194 ? -4.213  -1.383  -40.315 1.00 32.72  ? 237 THR B CB  1 
ATOM   3655 O OG1 . THR B 1 194 ? -4.311  0.043   -40.219 1.00 39.37  ? 237 THR B OG1 1 
ATOM   3656 C CG2 . THR B 1 194 ? -3.062  -1.750  -41.237 1.00 35.25  ? 237 THR B CG2 1 
ATOM   3657 N N   . LEU B 1 195 ? -5.091  -4.016  -42.021 1.00 30.36  ? 238 LEU B N   1 
ATOM   3658 C CA  . LEU B 1 195 ? -4.735  -5.420  -42.190 1.00 31.65  ? 238 LEU B CA  1 
ATOM   3659 C C   . LEU B 1 195 ? -3.243  -5.462  -42.495 1.00 34.48  ? 238 LEU B C   1 
ATOM   3660 O O   . LEU B 1 195 ? -2.807  -4.986  -43.549 1.00 36.56  ? 238 LEU B O   1 
ATOM   3661 C CB  . LEU B 1 195 ? -5.546  -6.069  -43.310 1.00 32.09  ? 238 LEU B CB  1 
ATOM   3662 C CG  . LEU B 1 195 ? -5.132  -7.490  -43.704 1.00 29.86  ? 238 LEU B CG  1 
ATOM   3663 C CD1 . LEU B 1 195 ? -5.497  -8.487  -42.615 1.00 30.21  ? 238 LEU B CD1 1 
ATOM   3664 C CD2 . LEU B 1 195 ? -5.761  -7.888  -45.032 1.00 33.53  ? 238 LEU B CD2 1 
ATOM   3665 N N   . GLU B 1 196 ? -2.463  -6.024  -41.577 1.00 34.04  ? 239 GLU B N   1 
ATOM   3666 C CA  . GLU B 1 196 ? -1.012  -6.070  -41.707 1.00 38.21  ? 239 GLU B CA  1 
ATOM   3667 C C   . GLU B 1 196 ? -0.591  -7.480  -42.105 1.00 36.15  ? 239 GLU B C   1 
ATOM   3668 O O   . GLU B 1 196 ? -0.826  -8.438  -41.361 1.00 34.14  ? 239 GLU B O   1 
ATOM   3669 C CB  . GLU B 1 196 ? -0.337  -5.647  -40.402 1.00 39.06  ? 239 GLU B CB  1 
ATOM   3670 C CG  . GLU B 1 196 ? 1.184   -5.709  -40.440 1.00 43.74  ? 239 GLU B CG  1 
ATOM   3671 C CD  . GLU B 1 196 ? 1.831   -5.038  -39.241 1.00 49.47  ? 239 GLU B CD  1 
ATOM   3672 O OE1 . GLU B 1 196 ? 1.375   -3.943  -38.849 1.00 52.60  ? 239 GLU B OE1 1 
ATOM   3673 O OE2 . GLU B 1 196 ? 2.793   -5.606  -38.684 1.00 53.08  ? 239 GLU B OE2 1 
ATOM   3674 N N   . ALA B 1 197 ? 0.036   -7.599  -43.271 1.00 36.85  ? 240 ALA B N   1 
ATOM   3675 C CA  . ALA B 1 197 ? 0.475   -8.881  -43.799 1.00 34.22  ? 240 ALA B CA  1 
ATOM   3676 C C   . ALA B 1 197 ? 1.936   -9.119  -43.446 1.00 38.21  ? 240 ALA B C   1 
ATOM   3677 O O   . ALA B 1 197 ? 2.771   -8.217  -43.568 1.00 38.90  ? 240 ALA B O   1 
ATOM   3678 C CB  . ALA B 1 197 ? 0.290   -8.936  -45.316 1.00 36.11  ? 240 ALA B CB  1 
ATOM   3679 N N   . TRP B 1 198 ? 2.236   -10.335 -42.998 1.00 36.11  ? 241 TRP B N   1 
ATOM   3680 C CA  . TRP B 1 198 ? 3.599   -10.765 -42.697 1.00 40.41  ? 241 TRP B CA  1 
ATOM   3681 C C   . TRP B 1 198 ? 3.983   -11.816 -43.732 1.00 41.54  ? 241 TRP B C   1 
ATOM   3682 O O   . TRP B 1 198 ? 3.555   -12.971 -43.644 1.00 39.82  ? 241 TRP B O   1 
ATOM   3683 C CB  . TRP B 1 198 ? 3.706   -11.322 -41.281 1.00 43.01  ? 241 TRP B CB  1 
ATOM   3684 C CG  . TRP B 1 198 ? 3.492   -10.308 -40.201 1.00 42.13  ? 241 TRP B CG  1 
ATOM   3685 C CD1 . TRP B 1 198 ? 3.466   -8.950  -40.337 1.00 44.42  ? 241 TRP B CD1 1 
ATOM   3686 C CD2 . TRP B 1 198 ? 3.270   -10.577 -38.812 1.00 41.17  ? 241 TRP B CD2 1 
ATOM   3687 N NE1 . TRP B 1 198 ? 3.243   -8.357  -39.117 1.00 46.59  ? 241 TRP B NE1 1 
ATOM   3688 C CE2 . TRP B 1 198 ? 3.118   -9.335  -38.165 1.00 42.86  ? 241 TRP B CE2 1 
ATOM   3689 C CE3 . TRP B 1 198 ? 3.184   -11.749 -38.054 1.00 46.21  ? 241 TRP B CE3 1 
ATOM   3690 C CZ2 . TRP B 1 198 ? 2.888   -9.231  -36.795 1.00 46.78  ? 241 TRP B CZ2 1 
ATOM   3691 C CZ3 . TRP B 1 198 ? 2.954   -11.645 -36.694 1.00 48.40  ? 241 TRP B CZ3 1 
ATOM   3692 C CH2 . TRP B 1 198 ? 2.809   -10.394 -36.078 1.00 48.36  ? 241 TRP B CH2 1 
ATOM   3693 N N   . VAL B 1 199 ? 4.792   -11.415 -44.707 1.00 41.65  ? 242 VAL B N   1 
ATOM   3694 C CA  . VAL B 1 199 ? 5.207   -12.313 -45.780 1.00 42.82  ? 242 VAL B CA  1 
ATOM   3695 C C   . VAL B 1 199 ? 6.393   -13.129 -45.277 1.00 47.11  ? 242 VAL B C   1 
ATOM   3696 O O   . VAL B 1 199 ? 7.484   -12.594 -45.064 1.00 49.22  ? 242 VAL B O   1 
ATOM   3697 C CB  . VAL B 1 199 ? 5.559   -11.539 -47.055 1.00 43.32  ? 242 VAL B CB  1 
ATOM   3698 C CG1 . VAL B 1 199 ? 5.960   -12.494 -48.164 1.00 45.87  ? 242 VAL B CG1 1 
ATOM   3699 C CG2 . VAL B 1 199 ? 4.379   -10.680 -47.487 1.00 46.35  ? 242 VAL B CG2 1 
ATOM   3700 N N   . ILE B 1 200 ? 6.179   -14.426 -45.083 1.00 44.43  ? 243 ILE B N   1 
ATOM   3701 C CA  . ILE B 1 200 ? 7.206   -15.317 -44.555 1.00 47.16  ? 243 ILE B CA  1 
ATOM   3702 C C   . ILE B 1 200 ? 8.032   -15.844 -45.720 1.00 50.28  ? 243 ILE B C   1 
ATOM   3703 O O   . ILE B 1 200 ? 7.494   -16.459 -46.647 1.00 48.18  ? 243 ILE B O   1 
ATOM   3704 C CB  . ILE B 1 200 ? 6.581   -16.472 -43.757 1.00 45.59  ? 243 ILE B CB  1 
ATOM   3705 C CG1 . ILE B 1 200 ? 5.600   -15.930 -42.713 1.00 44.35  ? 243 ILE B CG1 1 
ATOM   3706 C CG2 . ILE B 1 200 ? 7.668   -17.312 -43.097 1.00 47.23  ? 243 ILE B CG2 1 
ATOM   3707 C CD1 . ILE B 1 200 ? 6.188   -14.882 -41.791 1.00 42.64  ? 243 ILE B CD1 1 
ATOM   3708 N N   . HIS B 1 201 ? 9.339   -15.610 -45.670 1.00 57.20  ? 244 HIS B N   1 
ATOM   3709 C CA  . HIS B 1 201 ? 10.220  -16.037 -46.743 1.00 62.41  ? 244 HIS B CA  1 
ATOM   3710 C C   . HIS B 1 201 ? 10.579  -17.510 -46.595 1.00 67.61  ? 244 HIS B C   1 
ATOM   3711 O O   . HIS B 1 201 ? 10.522  -18.089 -45.507 1.00 64.38  ? 244 HIS B O   1 
ATOM   3712 C CB  . HIS B 1 201 ? 11.489  -15.188 -46.766 1.00 67.56  ? 244 HIS B CB  1 
ATOM   3713 C CG  . HIS B 1 201 ? 11.287  -13.831 -47.358 1.00 66.45  ? 244 HIS B CG  1 
ATOM   3714 N ND1 . HIS B 1 201 ? 12.265  -13.176 -48.075 1.00 74.77  ? 244 HIS B ND1 1 
ATOM   3715 C CD2 . HIS B 1 201 ? 10.213  -13.008 -47.348 1.00 63.22  ? 244 HIS B CD2 1 
ATOM   3716 C CE1 . HIS B 1 201 ? 11.802  -12.007 -48.480 1.00 75.41  ? 244 HIS B CE1 1 
ATOM   3717 N NE2 . HIS B 1 201 ? 10.559  -11.880 -48.050 1.00 65.37  ? 244 HIS B NE2 1 
ATOM   3718 N N   . GLY B 1 202 ? 10.954  -18.113 -47.719 1.00 79.52  ? 245 GLY B N   1 
ATOM   3719 C CA  . GLY B 1 202 ? 11.321  -19.512 -47.751 1.00 89.75  ? 245 GLY B CA  1 
ATOM   3720 C C   . GLY B 1 202 ? 12.814  -19.744 -47.856 1.00 107.74 ? 245 GLY B C   1 
ATOM   3721 O O   . GLY B 1 202 ? 13.608  -19.174 -47.102 1.00 105.07 ? 245 GLY B O   1 
ATOM   3722 N N   . GLY B 1 203 ? 13.192  -20.596 -48.802 1.00 118.33 ? 246 GLY B N   1 
ATOM   3723 C CA  . GLY B 1 203 ? 14.566  -20.991 -49.034 1.00 125.53 ? 246 GLY B CA  1 
ATOM   3724 C C   . GLY B 1 203 ? 15.394  -20.035 -49.871 1.00 131.34 ? 246 GLY B C   1 
ATOM   3725 O O   . GLY B 1 203 ? 15.516  -20.233 -51.083 1.00 134.49 ? 246 GLY B O   1 
ATOM   3726 N N   . ARG B 1 204 ? 15.962  -18.999 -49.248 1.00 123.53 ? 247 ARG B N   1 
ATOM   3727 C CA  . ARG B 1 204 ? 16.877  -18.082 -49.930 1.00 129.09 ? 247 ARG B CA  1 
ATOM   3728 C C   . ARG B 1 204 ? 16.229  -17.181 -50.978 1.00 135.99 ? 247 ARG B C   1 
ATOM   3729 O O   . ARG B 1 204 ? 16.346  -17.418 -52.185 1.00 133.09 ? 247 ARG B O   1 
ATOM   3730 C CB  . ARG B 1 204 ? 18.018  -18.877 -50.581 1.00 129.00 ? 247 ARG B CB  1 
ATOM   3731 C CG  . ARG B 1 204 ? 19.164  -18.036 -51.164 1.00 129.26 ? 247 ARG B CG  1 
ATOM   3732 C CD  . ARG B 1 204 ? 19.323  -16.673 -50.490 1.00 133.22 ? 247 ARG B CD  1 
ATOM   3733 N NE  . ARG B 1 204 ? 19.453  -16.764 -49.040 1.00 131.03 ? 247 ARG B NE  1 
ATOM   3734 C CZ  . ARG B 1 204 ? 19.045  -15.829 -48.190 1.00 126.84 ? 247 ARG B CZ  1 
ATOM   3735 N NH1 . ARG B 1 204 ? 18.480  -14.709 -48.611 1.00 131.14 ? 247 ARG B NH1 1 
ATOM   3736 N NH2 . ARG B 1 204 ? 19.197  -16.029 -46.884 1.00 117.75 ? 247 ARG B NH2 1 
ATOM   3737 N N   . GLU B 1 205 ? 15.520  -16.154 -50.501 1.00 153.32 ? 248 GLU B N   1 
ATOM   3738 C CA  . GLU B 1 205 ? 14.759  -15.214 -51.316 1.00 154.81 ? 248 GLU B CA  1 
ATOM   3739 C C   . GLU B 1 205 ? 15.577  -14.008 -51.810 1.00 159.10 ? 248 GLU B C   1 
ATOM   3740 O O   . GLU B 1 205 ? 14.988  -12.991 -52.195 1.00 151.99 ? 248 GLU B O   1 
ATOM   3741 C CB  . GLU B 1 205 ? 13.552  -14.736 -50.502 1.00 140.07 ? 248 GLU B CB  1 
ATOM   3742 C CG  . GLU B 1 205 ? 12.503  -13.949 -51.262 1.00 128.12 ? 248 GLU B CG  1 
ATOM   3743 C CD  . GLU B 1 205 ? 12.025  -14.656 -52.512 1.00 133.19 ? 248 GLU B CD  1 
ATOM   3744 O OE1 . GLU B 1 205 ? 12.099  -15.901 -52.562 1.00 142.25 ? 248 GLU B OE1 1 
ATOM   3745 O OE2 . GLU B 1 205 ? 11.582  -13.961 -53.448 1.00 126.23 ? 248 GLU B OE2 1 
ATOM   3746 N N   . ASP B 1 206 ? 16.909  -14.096 -51.819 1.00 163.16 ? 249 ASP B N   1 
ATOM   3747 C CA  . ASP B 1 206 ? 17.776  -12.999 -52.275 1.00 164.61 ? 249 ASP B CA  1 
ATOM   3748 C C   . ASP B 1 206 ? 17.419  -11.673 -51.602 1.00 160.53 ? 249 ASP B C   1 
ATOM   3749 O O   . ASP B 1 206 ? 17.683  -10.596 -52.142 1.00 162.94 ? 249 ASP B O   1 
ATOM   3750 C CB  . ASP B 1 206 ? 17.741  -12.857 -53.805 1.00 169.13 ? 249 ASP B CB  1 
ATOM   3751 C CG  . ASP B 1 206 ? 16.517  -12.104 -54.312 1.00 165.47 ? 249 ASP B CG  1 
ATOM   3752 O OD1 . ASP B 1 206 ? 16.552  -10.855 -54.343 1.00 166.84 ? 249 ASP B OD1 1 
ATOM   3753 O OD2 . ASP B 1 206 ? 15.526  -12.761 -54.696 1.00 155.81 ? 249 ASP B OD2 1 
ATOM   3754 N N   . SER B 1 207 ? 16.834  -11.739 -50.405 1.00 140.39 ? 250 SER B N   1 
ATOM   3755 C CA  . SER B 1 207 ? 16.391  -10.543 -49.685 1.00 123.90 ? 250 SER B CA  1 
ATOM   3756 C C   . SER B 1 207 ? 15.545  -9.642  -50.584 1.00 114.53 ? 250 SER B C   1 
ATOM   3757 O O   . SER B 1 207 ? 15.616  -8.413  -50.517 1.00 106.45 ? 250 SER B O   1 
ATOM   3758 C CB  . SER B 1 207 ? 17.581  -9.771  -49.112 1.00 125.48 ? 250 SER B CB  1 
ATOM   3759 O OG  . SER B 1 207 ? 18.147  -10.451 -48.005 1.00 120.25 ? 250 SER B OG  1 
ATOM   3760 N N   . ARG B 1 208 ? 14.736  -10.264 -51.437 1.00 113.76 ? 251 ARG B N   1 
ATOM   3761 C CA  . ARG B 1 208 ? 13.842  -9.525  -52.318 1.00 98.37  ? 251 ARG B CA  1 
ATOM   3762 C C   . ARG B 1 208 ? 12.623  -9.040  -51.545 1.00 82.22  ? 251 ARG B C   1 
ATOM   3763 O O   . ARG B 1 208 ? 12.127  -9.724  -50.645 1.00 78.47  ? 251 ARG B O   1 
ATOM   3764 C CB  . ARG B 1 208 ? 13.409  -10.405 -53.492 1.00 101.98 ? 251 ARG B CB  1 
ATOM   3765 C CG  . ARG B 1 208 ? 12.447  -9.734  -54.463 1.00 90.49  ? 251 ARG B CG  1 
ATOM   3766 C CD  . ARG B 1 208 ? 12.135  -10.628 -55.659 1.00 86.86  ? 251 ARG B CD  1 
ATOM   3767 N NE  . ARG B 1 208 ? 11.638  -11.941 -55.262 1.00 94.69  ? 251 ARG B NE  1 
ATOM   3768 C CZ  . ARG B 1 208 ? 11.089  -12.818 -56.091 1.00 89.51  ? 251 ARG B CZ  1 
ATOM   3769 N NH1 . ARG B 1 208 ? 10.921  -12.545 -57.375 1.00 80.44  ? 251 ARG B NH1 1 
ATOM   3770 N NH2 . ARG B 1 208 ? 10.694  -13.998 -55.621 1.00 91.86  ? 251 ARG B NH2 1 
ATOM   3771 N N   . ASP B 1 209 ? 12.140  -7.852  -51.901 1.00 79.45  ? 252 ASP B N   1 
ATOM   3772 C CA  . ASP B 1 209 ? 10.962  -7.272  -51.258 1.00 72.59  ? 252 ASP B CA  1 
ATOM   3773 C C   . ASP B 1 209 ? 9.724   -7.943  -51.837 1.00 67.33  ? 252 ASP B C   1 
ATOM   3774 O O   . ASP B 1 209 ? 9.262   -7.591  -52.925 1.00 66.18  ? 252 ASP B O   1 
ATOM   3775 C CB  . ASP B 1 209 ? 10.919  -5.763  -51.467 1.00 70.28  ? 252 ASP B CB  1 
ATOM   3776 C CG  . ASP B 1 209 ? 9.754   -5.108  -50.749 1.00 68.38  ? 252 ASP B CG  1 
ATOM   3777 O OD1 . ASP B 1 209 ? 9.091   -5.794  -49.942 1.00 68.56  ? 252 ASP B OD1 1 
ATOM   3778 O OD2 . ASP B 1 209 ? 9.499   -3.911  -50.993 1.00 70.87  ? 252 ASP B OD2 1 
ATOM   3779 N N   . LEU B 1 210 ? 9.181   -8.918  -51.109 1.00 63.81  ? 253 LEU B N   1 
ATOM   3780 C CA  . LEU B 1 210 ? 7.992   -9.625  -51.567 1.00 60.29  ? 253 LEU B CA  1 
ATOM   3781 C C   . LEU B 1 210 ? 6.714   -8.821  -51.372 1.00 55.79  ? 253 LEU B C   1 
ATOM   3782 O O   . LEU B 1 210 ? 5.669   -9.218  -51.897 1.00 54.21  ? 253 LEU B O   1 
ATOM   3783 C CB  . LEU B 1 210 ? 7.870   -10.971 -50.848 1.00 58.41  ? 253 LEU B CB  1 
ATOM   3784 C CG  . LEU B 1 210 ? 8.956   -12.000 -51.174 1.00 65.89  ? 253 LEU B CG  1 
ATOM   3785 C CD1 . LEU B 1 210 ? 8.713   -13.300 -50.423 1.00 65.54  ? 253 LEU B CD1 1 
ATOM   3786 C CD2 . LEU B 1 210 ? 9.029   -12.258 -52.672 1.00 70.58  ? 253 LEU B CD2 1 
ATOM   3787 N N   . CYS B 1 211 ? 6.768   -7.708  -50.638 1.00 62.23  ? 254 CYS B N   1 
ATOM   3788 C CA  . CYS B 1 211 ? 5.615   -6.823  -50.539 1.00 63.43  ? 254 CYS B CA  1 
ATOM   3789 C C   . CYS B 1 211 ? 5.287   -6.145  -51.862 1.00 62.23  ? 254 CYS B C   1 
ATOM   3790 O O   . CYS B 1 211 ? 4.198   -5.578  -51.996 1.00 61.00  ? 254 CYS B O   1 
ATOM   3791 C CB  . CYS B 1 211 ? 5.856   -5.766  -49.460 1.00 63.91  ? 254 CYS B CB  1 
ATOM   3792 S SG  . CYS B 1 211 ? 5.885   -6.424  -47.772 1.00 68.34  ? 254 CYS B SG  1 
ATOM   3793 N N   . GLN B 1 212 ? 6.196   -6.188  -52.834 1.00 62.12  ? 255 GLN B N   1 
ATOM   3794 C CA  . GLN B 1 212 ? 5.937   -5.679  -54.173 1.00 62.35  ? 255 GLN B CA  1 
ATOM   3795 C C   . GLN B 1 212 ? 5.394   -6.750  -55.110 1.00 59.93  ? 255 GLN B C   1 
ATOM   3796 O O   . GLN B 1 212 ? 5.112   -6.447  -56.274 1.00 59.76  ? 255 GLN B O   1 
ATOM   3797 C CB  . GLN B 1 212 ? 7.218   -5.084  -54.767 1.00 66.08  ? 255 GLN B CB  1 
ATOM   3798 C CG  . GLN B 1 212 ? 7.816   -3.956  -53.943 1.00 69.14  ? 255 GLN B CG  1 
ATOM   3799 C CD  . GLN B 1 212 ? 6.851   -2.802  -53.747 1.00 71.15  ? 255 GLN B CD  1 
ATOM   3800 O OE1 . GLN B 1 212 ? 6.356   -2.220  -54.712 1.00 68.09  ? 255 GLN B OE1 1 
ATOM   3801 N NE2 . GLN B 1 212 ? 6.572   -2.473  -52.491 1.00 70.58  ? 255 GLN B NE2 1 
ATOM   3802 N N   . ASP B 1 213 ? 5.238   -7.980  -54.632 1.00 58.69  ? 256 ASP B N   1 
ATOM   3803 C CA  . ASP B 1 213 ? 4.762   -9.058  -55.485 1.00 56.12  ? 256 ASP B CA  1 
ATOM   3804 C C   . ASP B 1 213 ? 3.388   -8.705  -56.050 1.00 54.25  ? 256 ASP B C   1 
ATOM   3805 O O   . ASP B 1 213 ? 2.584   -8.061  -55.366 1.00 55.28  ? 256 ASP B O   1 
ATOM   3806 C CB  . ASP B 1 213 ? 4.684   -10.363 -54.691 1.00 55.75  ? 256 ASP B CB  1 
ATOM   3807 C CG  . ASP B 1 213 ? 4.282   -11.544 -55.548 1.00 55.98  ? 256 ASP B CG  1 
ATOM   3808 O OD1 . ASP B 1 213 ? 5.150   -12.080 -56.268 1.00 59.15  ? 256 ASP B OD1 1 
ATOM   3809 O OD2 . ASP B 1 213 ? 3.097   -11.935 -55.504 1.00 53.81  ? 256 ASP B OD2 1 
ATOM   3810 N N   . PRO B 1 214 ? 3.086   -9.096  -57.293 1.00 57.51  ? 257 PRO B N   1 
ATOM   3811 C CA  . PRO B 1 214 ? 1.775   -8.732  -57.859 1.00 55.56  ? 257 PRO B CA  1 
ATOM   3812 C C   . PRO B 1 214 ? 0.597   -9.210  -57.027 1.00 50.17  ? 257 PRO B C   1 
ATOM   3813 O O   . PRO B 1 214 ? -0.399  -8.486  -56.906 1.00 48.91  ? 257 PRO B O   1 
ATOM   3814 C CB  . PRO B 1 214 ? 1.797   -9.394  -59.246 1.00 60.12  ? 257 PRO B CB  1 
ATOM   3815 C CG  . PRO B 1 214 ? 3.241   -9.530  -59.580 1.00 62.47  ? 257 PRO B CG  1 
ATOM   3816 C CD  . PRO B 1 214 ? 3.935   -9.796  -58.275 1.00 60.00  ? 257 PRO B CD  1 
ATOM   3817 N N   . THR B 1 215 ? 0.674   -10.410 -56.446 1.00 48.69  ? 258 THR B N   1 
ATOM   3818 C CA  . THR B 1 215 ? -0.450  -10.905 -55.657 1.00 47.01  ? 258 THR B CA  1 
ATOM   3819 C C   . THR B 1 215 ? -0.639  -10.088 -54.384 1.00 45.94  ? 258 THR B C   1 
ATOM   3820 O O   . THR B 1 215 ? -1.769  -9.953  -53.899 1.00 43.81  ? 258 THR B O   1 
ATOM   3821 C CB  . THR B 1 215 ? -0.259  -12.386 -55.321 1.00 46.21  ? 258 THR B CB  1 
ATOM   3822 O OG1 . THR B 1 215 ? 0.920   -12.561 -54.528 1.00 45.65  ? 258 THR B OG1 1 
ATOM   3823 C CG2 . THR B 1 215 ? -0.137  -13.209 -56.597 1.00 47.13  ? 258 THR B CG2 1 
ATOM   3824 N N   . ILE B 1 216 ? 0.443   -9.539  -53.827 1.00 47.04  ? 259 ILE B N   1 
ATOM   3825 C CA  . ILE B 1 216 ? 0.305   -8.635  -52.689 1.00 46.50  ? 259 ILE B CA  1 
ATOM   3826 C C   . ILE B 1 216 ? -0.393  -7.348  -53.116 1.00 45.41  ? 259 ILE B C   1 
ATOM   3827 O O   . ILE B 1 216 ? -1.288  -6.852  -52.421 1.00 42.68  ? 259 ILE B O   1 
ATOM   3828 C CB  . ILE B 1 216 ? 1.679   -8.352  -52.057 1.00 46.96  ? 259 ILE B CB  1 
ATOM   3829 C CG1 . ILE B 1 216 ? 2.321   -9.650  -51.561 1.00 49.26  ? 259 ILE B CG1 1 
ATOM   3830 C CG2 . ILE B 1 216 ? 1.542   -7.353  -50.914 1.00 46.57  ? 259 ILE B CG2 1 
ATOM   3831 C CD1 . ILE B 1 216 ? 1.530   -10.363 -50.472 1.00 46.20  ? 259 ILE B CD1 1 
ATOM   3832 N N   . LYS B 1 217 ? 0.002   -6.784  -54.261 1.00 46.12  ? 260 LYS B N   1 
ATOM   3833 C CA  . LYS B 1 217 ? -0.703  -5.617  -54.781 1.00 46.82  ? 260 LYS B CA  1 
ATOM   3834 C C   . LYS B 1 217 ? -2.180  -5.925  -54.982 1.00 44.42  ? 260 LYS B C   1 
ATOM   3835 O O   . LYS B 1 217 ? -3.044  -5.086  -54.702 1.00 42.33  ? 260 LYS B O   1 
ATOM   3836 C CB  . LYS B 1 217 ? -0.073  -5.159  -56.096 1.00 48.39  ? 260 LYS B CB  1 
ATOM   3837 C CG  . LYS B 1 217 ? 1.400   -4.795  -55.999 1.00 56.72  ? 260 LYS B CG  1 
ATOM   3838 C CD  . LYS B 1 217 ? 1.640   -3.673  -55.001 1.00 66.39  ? 260 LYS B CD  1 
ATOM   3839 C CE  . LYS B 1 217 ? 3.085   -3.203  -55.035 1.00 71.86  ? 260 LYS B CE  1 
ATOM   3840 N NZ  . LYS B 1 217 ? 3.466   -2.465  -53.798 1.00 78.88  ? 260 LYS B NZ  1 
ATOM   3841 N N   . GLU B 1 218 ? -2.488  -7.132  -55.461 1.00 45.02  ? 261 GLU B N   1 
ATOM   3842 C CA  . GLU B 1 218 ? -3.879  -7.554  -55.574 1.00 44.81  ? 261 GLU B CA  1 
ATOM   3843 C C   . GLU B 1 218 ? -4.566  -7.526  -54.215 1.00 44.20  ? 261 GLU B C   1 
ATOM   3844 O O   . GLU B 1 218 ? -5.700  -7.048  -54.092 1.00 41.08  ? 261 GLU B O   1 
ATOM   3845 C CB  . GLU B 1 218 ? -3.942  -8.955  -56.183 1.00 46.20  ? 261 GLU B CB  1 
ATOM   3846 C CG  . GLU B 1 218 ? -5.341  -9.449  -56.500 1.00 46.56  ? 261 GLU B CG  1 
ATOM   3847 C CD  . GLU B 1 218 ? -5.348  -10.886 -56.986 1.00 54.46  ? 261 GLU B CD  1 
ATOM   3848 O OE1 . GLU B 1 218 ? -4.282  -11.537 -56.943 1.00 53.49  ? 261 GLU B OE1 1 
ATOM   3849 O OE2 . GLU B 1 218 ? -6.419  -11.366 -57.412 1.00 58.08  ? 261 GLU B OE2 1 
ATOM   3850 N N   . LEU B 1 219 ? -3.892  -8.032  -53.179 1.00 40.97  ? 262 LEU B N   1 
ATOM   3851 C CA  . LEU B 1 219 ? -4.462  -7.996  -51.836 1.00 38.92  ? 262 LEU B CA  1 
ATOM   3852 C C   . LEU B 1 219 ? -4.687  -6.561  -51.376 1.00 38.30  ? 262 LEU B C   1 
ATOM   3853 O O   . LEU B 1 219 ? -5.742  -6.236  -50.816 1.00 36.90  ? 262 LEU B O   1 
ATOM   3854 C CB  . LEU B 1 219 ? -3.541  -8.733  -50.863 1.00 34.88  ? 262 LEU B CB  1 
ATOM   3855 C CG  . LEU B 1 219 ? -3.915  -8.657  -49.382 1.00 35.70  ? 262 LEU B CG  1 
ATOM   3856 C CD1 . LEU B 1 219 ? -5.308  -9.223  -49.145 1.00 30.54  ? 262 LEU B CD1 1 
ATOM   3857 C CD2 . LEU B 1 219 ? -2.878  -9.385  -48.539 1.00 33.22  ? 262 LEU B CD2 1 
ATOM   3858 N N   . GLU B 1 220 ? -3.706  -5.687  -51.606 1.00 40.52  ? 263 GLU B N   1 
ATOM   3859 C CA  . GLU B 1 220 ? -3.849  -4.291  -51.207 1.00 42.42  ? 263 GLU B CA  1 
ATOM   3860 C C   . GLU B 1 220 ? -5.044  -3.645  -51.894 1.00 40.90  ? 263 GLU B C   1 
ATOM   3861 O O   . GLU B 1 220 ? -5.773  -2.856  -51.280 1.00 34.88  ? 263 GLU B O   1 
ATOM   3862 C CB  . GLU B 1 220 ? -2.568  -3.522  -51.533 1.00 44.81  ? 263 GLU B CB  1 
ATOM   3863 C CG  . GLU B 1 220 ? -2.599  -2.055  -51.129 1.00 51.62  ? 263 GLU B CG  1 
ATOM   3864 C CD  . GLU B 1 220 ? -1.309  -1.332  -51.467 1.00 64.01  ? 263 GLU B CD  1 
ATOM   3865 O OE1 . GLU B 1 220 ? -0.659  -1.710  -52.465 1.00 65.97  ? 263 GLU B OE1 1 
ATOM   3866 O OE2 . GLU B 1 220 ? -0.941  -0.391  -50.733 1.00 73.00  ? 263 GLU B OE2 1 
ATOM   3867 N N   . SER B 1 221 ? -5.250  -3.953  -53.176 1.00 38.66  ? 264 SER B N   1 
ATOM   3868 C CA  . SER B 1 221 ? -6.392  -3.396  -53.892 1.00 39.92  ? 264 SER B CA  1 
ATOM   3869 C C   . SER B 1 221 ? -7.707  -3.909  -53.320 1.00 37.40  ? 264 SER B C   1 
ATOM   3870 O O   . SER B 1 221 ? -8.661  -3.140  -53.154 1.00 37.61  ? 264 SER B O   1 
ATOM   3871 C CB  . SER B 1 221 ? -6.287  -3.731  -55.379 1.00 40.73  ? 264 SER B CB  1 
ATOM   3872 O OG  . SER B 1 221 ? -7.393  -3.211  -56.095 1.00 50.74  ? 264 SER B OG  1 
ATOM   3873 N N   . ILE B 1 222 ? -7.774  -5.205  -53.010 1.00 36.73  ? 265 ILE B N   1 
ATOM   3874 C CA  . ILE B 1 222 ? -9.013  -5.787  -52.502 1.00 36.06  ? 265 ILE B CA  1 
ATOM   3875 C C   . ILE B 1 222 ? -9.390  -5.147  -51.173 1.00 36.57  ? 265 ILE B C   1 
ATOM   3876 O O   . ILE B 1 222 ? -10.533 -4.720  -50.967 1.00 34.01  ? 265 ILE B O   1 
ATOM   3877 C CB  . ILE B 1 222 ? -8.868  -7.314  -52.368 1.00 34.93  ? 265 ILE B CB  1 
ATOM   3878 C CG1 . ILE B 1 222 ? -8.787  -7.964  -53.751 1.00 40.11  ? 265 ILE B CG1 1 
ATOM   3879 C CG2 . ILE B 1 222 ? -10.023 -7.892  -51.555 1.00 35.96  ? 265 ILE B CG2 1 
ATOM   3880 C CD1 . ILE B 1 222 ? -8.327  -9.409  -53.724 1.00 39.26  ? 265 ILE B CD1 1 
ATOM   3881 N N   . ILE B 1 223 ? -8.429  -5.066  -50.253 1.00 34.34  ? 266 ILE B N   1 
ATOM   3882 C CA  . ILE B 1 223 ? -8.726  -4.566  -48.915 1.00 34.50  ? 266 ILE B CA  1 
ATOM   3883 C C   . ILE B 1 223 ? -8.997  -3.065  -48.952 1.00 33.86  ? 266 ILE B C   1 
ATOM   3884 O O   . ILE B 1 223 ? -9.858  -2.559  -48.222 1.00 33.29  ? 266 ILE B O   1 
ATOM   3885 C CB  . ILE B 1 223 ? -7.580  -4.932  -47.951 1.00 36.12  ? 266 ILE B CB  1 
ATOM   3886 C CG1 . ILE B 1 223 ? -8.006  -4.709  -46.498 1.00 35.40  ? 266 ILE B CG1 1 
ATOM   3887 C CG2 . ILE B 1 223 ? -6.323  -4.142  -48.278 1.00 37.39  ? 266 ILE B CG2 1 
ATOM   3888 C CD1 . ILE B 1 223 ? -9.095  -5.662  -46.030 1.00 34.74  ? 266 ILE B CD1 1 
ATOM   3889 N N   . SER B 1 224 ? -8.277  -2.331  -49.805 1.00 35.26  ? 267 SER B N   1 
ATOM   3890 C CA  . SER B 1 224 ? -8.522  -0.896  -49.932 1.00 37.09  ? 267 SER B CA  1 
ATOM   3891 C C   . SER B 1 224 ? -9.942  -0.616  -50.414 1.00 35.23  ? 267 SER B C   1 
ATOM   3892 O O   . SER B 1 224 ? -10.584 0.335   -49.954 1.00 32.20  ? 267 SER B O   1 
ATOM   3893 C CB  . SER B 1 224 ? -7.506  -0.268  -50.888 1.00 35.49  ? 267 SER B CB  1 
ATOM   3894 O OG  . SER B 1 224 ? -6.185  -0.416  -50.402 1.00 40.47  ? 267 SER B OG  1 
ATOM   3895 N N   . LYS B 1 225 ? -10.446 -1.424  -51.351 1.00 33.46  ? 268 LYS B N   1 
ATOM   3896 C CA  . LYS B 1 225 ? -11.820 -1.244  -51.808 1.00 34.63  ? 268 LYS B CA  1 
ATOM   3897 C C   . LYS B 1 225 ? -12.802 -1.334  -50.649 1.00 35.54  ? 268 LYS B C   1 
ATOM   3898 O O   . LYS B 1 225 ? -13.842 -0.666  -50.663 1.00 38.31  ? 268 LYS B O   1 
ATOM   3899 C CB  . LYS B 1 225 ? -12.169 -2.286  -52.872 1.00 35.06  ? 268 LYS B CB  1 
ATOM   3900 C CG  . LYS B 1 225 ? -13.423 -1.957  -53.680 1.00 37.89  ? 268 LYS B CG  1 
ATOM   3901 C CD  . LYS B 1 225 ? -14.007 -3.199  -54.349 1.00 37.89  ? 268 LYS B CD  1 
ATOM   3902 C CE  . LYS B 1 225 ? -15.012 -2.832  -55.436 1.00 42.38  ? 268 LYS B CE  1 
ATOM   3903 N NZ  . LYS B 1 225 ? -15.660 -4.034  -56.039 1.00 39.92  ? 268 LYS B NZ  1 
ATOM   3904 N N   . ARG B 1 226 ? -12.492 -2.145  -49.638 1.00 34.92  ? 269 ARG B N   1 
ATOM   3905 C CA  . ARG B 1 226 ? -13.341 -2.281  -48.462 1.00 35.01  ? 269 ARG B CA  1 
ATOM   3906 C C   . ARG B 1 226 ? -13.093 -1.183  -47.432 1.00 34.51  ? 269 ARG B C   1 
ATOM   3907 O O   . ARG B 1 226 ? -13.653 -1.245  -46.333 1.00 32.69  ? 269 ARG B O   1 
ATOM   3908 C CB  . ARG B 1 226 ? -13.136 -3.660  -47.827 1.00 34.80  ? 269 ARG B CB  1 
ATOM   3909 C CG  . ARG B 1 226 ? -13.285 -4.812  -48.815 1.00 35.59  ? 269 ARG B CG  1 
ATOM   3910 C CD  . ARG B 1 226 ? -13.566 -6.147  -48.128 1.00 31.57  ? 269 ARG B CD  1 
ATOM   3911 N NE  . ARG B 1 226 ? -14.789 -6.105  -47.333 1.00 29.57  ? 269 ARG B NE  1 
ATOM   3912 C CZ  . ARG B 1 226 ? -14.843 -6.191  -46.009 1.00 31.89  ? 269 ARG B CZ  1 
ATOM   3913 N NH1 . ARG B 1 226 ? -13.759 -6.411  -45.281 1.00 30.30  ? 269 ARG B NH1 1 
ATOM   3914 N NH2 . ARG B 1 226 ? -16.016 -6.058  -45.399 1.00 29.90  ? 269 ARG B NH2 1 
ATOM   3915 N N   . ASN B 1 227 ? -12.272 -0.185  -47.768 1.00 35.59  ? 270 ASN B N   1 
ATOM   3916 C CA  . ASN B 1 227 ? -12.018 0.966   -46.900 1.00 35.87  ? 270 ASN B CA  1 
ATOM   3917 C C   . ASN B 1 227 ? -11.306 0.544   -45.618 1.00 35.91  ? 270 ASN B C   1 
ATOM   3918 O O   . ASN B 1 227 ? -11.637 1.000   -44.522 1.00 33.12  ? 270 ASN B O   1 
ATOM   3919 C CB  . ASN B 1 227 ? -13.315 1.715   -46.589 1.00 41.67  ? 270 ASN B CB  1 
ATOM   3920 C CG  . ASN B 1 227 ? -13.962 2.291   -47.835 1.00 46.03  ? 270 ASN B CG  1 
ATOM   3921 O OD1 . ASN B 1 227 ? -13.317 2.999   -48.609 1.00 44.62  ? 270 ASN B OD1 1 
ATOM   3922 N ND2 . ASN B 1 227 ? -15.235 1.974   -48.045 1.00 46.25  ? 270 ASN B ND2 1 
ATOM   3923 N N   . ILE B 1 228 ? -10.322 -0.338  -45.765 1.00 34.79  ? 271 ILE B N   1 
ATOM   3924 C CA  . ILE B 1 228 ? -9.419  -0.726  -44.691 1.00 34.41  ? 271 ILE B CA  1 
ATOM   3925 C C   . ILE B 1 228 ? -7.998  -0.522  -45.194 1.00 35.44  ? 271 ILE B C   1 
ATOM   3926 O O   . ILE B 1 228 ? -7.694  -0.814  -46.356 1.00 37.02  ? 271 ILE B O   1 
ATOM   3927 C CB  . ILE B 1 228 ? -9.646  -2.188  -44.247 1.00 35.59  ? 271 ILE B CB  1 
ATOM   3928 C CG1 . ILE B 1 228 ? -11.021 -2.330  -43.584 1.00 33.03  ? 271 ILE B CG1 1 
ATOM   3929 C CG2 . ILE B 1 228 ? -8.523  -2.647  -43.317 1.00 32.05  ? 271 ILE B CG2 1 
ATOM   3930 C CD1 . ILE B 1 228 ? -11.357 -3.742  -43.146 1.00 37.20  ? 271 ILE B CD1 1 
ATOM   3931 N N   . GLN B 1 229 ? -7.132  -0.010  -44.327 1.00 33.62  ? 272 GLN B N   1 
ATOM   3932 C CA  . GLN B 1 229 ? -5.750  0.232   -44.704 1.00 37.42  ? 272 GLN B CA  1 
ATOM   3933 C C   . GLN B 1 229 ? -4.970  -1.078  -44.756 1.00 36.55  ? 272 GLN B C   1 
ATOM   3934 O O   . GLN B 1 229 ? -5.361  -2.094  -44.174 1.00 34.28  ? 272 GLN B O   1 
ATOM   3935 C CB  . GLN B 1 229 ? -5.092  1.200   -43.724 1.00 37.51  ? 272 GLN B CB  1 
ATOM   3936 C CG  . GLN B 1 229 ? -5.717  2.580   -43.727 1.00 46.64  ? 272 GLN B CG  1 
ATOM   3937 C CD  . GLN B 1 229 ? -5.258  3.423   -42.558 1.00 56.97  ? 272 GLN B CD  1 
ATOM   3938 O OE1 . GLN B 1 229 ? -4.141  3.941   -42.547 1.00 59.71  ? 272 GLN B OE1 1 
ATOM   3939 N NE2 . GLN B 1 229 ? -6.119  3.559   -41.559 1.00 55.79  ? 272 GLN B NE2 1 
ATOM   3940 N N   . PHE B 1 230 ? -3.848  -1.043  -45.473 1.00 36.40  ? 273 PHE B N   1 
ATOM   3941 C CA  . PHE B 1 230 ? -3.011  -2.215  -45.672 1.00 40.15  ? 273 PHE B CA  1 
ATOM   3942 C C   . PHE B 1 230 ? -1.567  -1.890  -45.321 1.00 41.35  ? 273 PHE B C   1 
ATOM   3943 O O   . PHE B 1 230 ? -1.067  -0.806  -45.633 1.00 40.90  ? 273 PHE B O   1 
ATOM   3944 C CB  . PHE B 1 230 ? -3.095  -2.717  -47.119 1.00 39.98  ? 273 PHE B CB  1 
ATOM   3945 C CG  . PHE B 1 230 ? -2.273  -3.947  -47.381 1.00 42.78  ? 273 PHE B CG  1 
ATOM   3946 C CD1 . PHE B 1 230 ? -2.624  -5.162  -46.818 1.00 40.74  ? 273 PHE B CD1 1 
ATOM   3947 C CD2 . PHE B 1 230 ? -1.152  -3.888  -48.191 1.00 45.53  ? 273 PHE B CD2 1 
ATOM   3948 C CE1 . PHE B 1 230 ? -1.869  -6.297  -47.056 1.00 40.22  ? 273 PHE B CE1 1 
ATOM   3949 C CE2 . PHE B 1 230 ? -0.394  -5.020  -48.434 1.00 45.95  ? 273 PHE B CE2 1 
ATOM   3950 C CZ  . PHE B 1 230 ? -0.754  -6.225  -47.865 1.00 44.35  ? 273 PHE B CZ  1 
ATOM   3951 N N   . SER B 1 231 ? -0.908  -2.838  -44.661 1.00 43.17  ? 274 SER B N   1 
ATOM   3952 C CA  . SER B 1 231 ? 0.508   -2.744  -44.340 1.00 45.86  ? 274 SER B CA  1 
ATOM   3953 C C   . SER B 1 231 ? 1.146   -4.099  -44.603 1.00 43.92  ? 274 SER B C   1 
ATOM   3954 O O   . SER B 1 231 ? 0.517   -5.142  -44.406 1.00 42.77  ? 274 SER B O   1 
ATOM   3955 C CB  . SER B 1 231 ? 0.727   -2.321  -42.881 1.00 46.72  ? 274 SER B CB  1 
ATOM   3956 O OG  . SER B 1 231 ? 2.095   -2.405  -42.524 1.00 55.08  ? 274 SER B OG  1 
ATOM   3957 N N   . CYS B 1 232 ? 2.397   -4.078  -45.060 1.00 43.85  ? 275 CYS B N   1 
ATOM   3958 C CA  . CYS B 1 232 ? 3.102   -5.301  -45.414 1.00 48.13  ? 275 CYS B CA  1 
ATOM   3959 C C   . CYS B 1 232 ? 4.526   -5.249  -44.886 1.00 49.84  ? 275 CYS B C   1 
ATOM   3960 O O   . CYS B 1 232 ? 5.168   -4.195  -44.905 1.00 50.28  ? 275 CYS B O   1 
ATOM   3961 C CB  . CYS B 1 232 ? 3.116   -5.520  -46.933 1.00 49.52  ? 275 CYS B CB  1 
ATOM   3962 S SG  . CYS B 1 232 ? 3.971   -7.029  -47.455 1.00 56.99  ? 275 CYS B SG  1 
ATOM   3963 N N   . LYS B 1 233 ? 5.007   -6.397  -44.414 1.00 53.69  ? 276 LYS B N   1 
ATOM   3964 C CA  . LYS B 1 233 ? 6.352   -6.539  -43.881 1.00 56.35  ? 276 LYS B CA  1 
ATOM   3965 C C   . LYS B 1 233 ? 6.917   -7.881  -44.321 1.00 53.65  ? 276 LYS B C   1 
ATOM   3966 O O   . LYS B 1 233 ? 6.188   -8.874  -44.386 1.00 52.84  ? 276 LYS B O   1 
ATOM   3967 C CB  . LYS B 1 233 ? 6.360   -6.459  -42.350 1.00 55.50  ? 276 LYS B CB  1 
ATOM   3968 C CG  . LYS B 1 233 ? 5.926   -5.124  -41.775 1.00 59.53  ? 276 LYS B CG  1 
ATOM   3969 C CD  . LYS B 1 233 ? 5.493   -5.297  -40.328 1.00 66.65  ? 276 LYS B CD  1 
ATOM   3970 C CE  . LYS B 1 233 ? 5.853   -4.098  -39.472 1.00 73.36  ? 276 LYS B CE  1 
ATOM   3971 N NZ  . LYS B 1 233 ? 5.635   -4.388  -38.027 1.00 74.07  ? 276 LYS B NZ  1 
ATOM   3972 N N   . ASN B 1 234 ? 8.214   -7.908  -44.615 1.00 53.94  ? 277 ASN B N   1 
ATOM   3973 C CA  . ASN B 1 234 ? 8.899   -9.142  -44.973 1.00 55.79  ? 277 ASN B CA  1 
ATOM   3974 C C   . ASN B 1 234 ? 9.516   -9.767  -43.728 1.00 55.42  ? 277 ASN B C   1 
ATOM   3975 O O   . ASN B 1 234 ? 10.200  -9.084  -42.959 1.00 56.20  ? 277 ASN B O   1 
ATOM   3976 C CB  . ASN B 1 234 ? 9.989   -8.886  -46.015 1.00 58.05  ? 277 ASN B CB  1 
ATOM   3977 C CG  . ASN B 1 234 ? 9.435   -8.376  -47.327 1.00 62.67  ? 277 ASN B CG  1 
ATOM   3978 O OD1 . ASN B 1 234 ? 8.953   -9.151  -48.153 1.00 63.60  ? 277 ASN B OD1 1 
ATOM   3979 N ND2 . ASN B 1 234 ? 9.513   -7.067  -47.534 1.00 65.92  ? 277 ASN B ND2 1 
ATOM   3980 N N   . ILE B 1 235 ? 9.266   -11.058 -43.533 1.00 54.97  ? 278 ILE B N   1 
ATOM   3981 C CA  . ILE B 1 235 ? 9.929   -11.848 -42.501 1.00 56.34  ? 278 ILE B CA  1 
ATOM   3982 C C   . ILE B 1 235 ? 10.998  -12.667 -43.217 1.00 60.68  ? 278 ILE B C   1 
ATOM   3983 O O   . ILE B 1 235 ? 10.717  -13.736 -43.768 1.00 60.31  ? 278 ILE B O   1 
ATOM   3984 C CB  . ILE B 1 235 ? 8.946   -12.738 -41.738 1.00 55.83  ? 278 ILE B CB  1 
ATOM   3985 C CG1 . ILE B 1 235 ? 7.825   -11.899 -41.113 1.00 54.99  ? 278 ILE B CG1 1 
ATOM   3986 C CG2 . ILE B 1 235 ? 9.677   -13.531 -40.664 1.00 60.85  ? 278 ILE B CG2 1 
ATOM   3987 C CD1 . ILE B 1 235 ? 8.286   -10.950 -40.024 1.00 58.18  ? 278 ILE B CD1 1 
ATOM   3988 N N   . TYR B 1 236 ? 12.233  -12.161 -43.214 1.00 60.09  ? 279 TYR B N   1 
ATOM   3989 C CA  . TYR B 1 236 ? 13.295  -12.772 -44.007 1.00 62.88  ? 279 TYR B CA  1 
ATOM   3990 C C   . TYR B 1 236 ? 13.821  -14.053 -43.371 1.00 65.22  ? 279 TYR B C   1 
ATOM   3991 O O   . TYR B 1 236 ? 14.120  -15.021 -44.080 1.00 67.90  ? 279 TYR B O   1 
ATOM   3992 C CB  . TYR B 1 236 ? 14.434  -11.771 -44.207 1.00 62.67  ? 279 TYR B CB  1 
ATOM   3993 C CG  . TYR B 1 236 ? 14.046  -10.575 -45.047 1.00 60.59  ? 279 TYR B CG  1 
ATOM   3994 C CD1 . TYR B 1 236 ? 13.950  -10.677 -46.428 1.00 67.40  ? 279 TYR B CD1 1 
ATOM   3995 C CD2 . TYR B 1 236 ? 13.776  -9.346  -44.461 1.00 59.55  ? 279 TYR B CD2 1 
ATOM   3996 C CE1 . TYR B 1 236 ? 13.594  -9.589  -47.203 1.00 68.40  ? 279 TYR B CE1 1 
ATOM   3997 C CE2 . TYR B 1 236 ? 13.420  -8.250  -45.229 1.00 62.71  ? 279 TYR B CE2 1 
ATOM   3998 C CZ  . TYR B 1 236 ? 13.331  -8.379  -46.600 1.00 65.56  ? 279 TYR B CZ  1 
ATOM   3999 O OH  . TYR B 1 236 ? 12.977  -7.296  -47.372 1.00 66.45  ? 279 TYR B OH  1 
ATOM   4000 N N   . ARG B 1 237 ? 13.942  -14.082 -42.042 1.00 67.38  ? 280 ARG B N   1 
ATOM   4001 C CA  . ARG B 1 237 ? 14.490  -15.225 -41.312 1.00 71.58  ? 280 ARG B CA  1 
ATOM   4002 C C   . ARG B 1 237 ? 13.426  -15.749 -40.358 1.00 74.94  ? 280 ARG B C   1 
ATOM   4003 O O   . ARG B 1 237 ? 13.333  -15.295 -39.206 1.00 76.67  ? 280 ARG B O   1 
ATOM   4004 C CB  . ARG B 1 237 ? 15.758  -14.831 -40.556 1.00 70.99  ? 280 ARG B CB  1 
ATOM   4005 N N   . PRO B 1 238 ? 12.597  -16.706 -40.791 1.00 77.86  ? 281 PRO B N   1 
ATOM   4006 C CA  . PRO B 1 238 ? 11.545  -17.211 -39.892 1.00 79.95  ? 281 PRO B CA  1 
ATOM   4007 C C   . PRO B 1 238 ? 12.078  -17.778 -38.588 1.00 81.78  ? 281 PRO B C   1 
ATOM   4008 O O   . PRO B 1 238 ? 11.519  -17.498 -37.520 1.00 79.80  ? 281 PRO B O   1 
ATOM   4009 C CB  . PRO B 1 238 ? 10.855  -18.294 -40.738 1.00 77.09  ? 281 PRO B CB  1 
ATOM   4010 C CG  . PRO B 1 238 ? 11.176  -17.946 -42.153 1.00 76.87  ? 281 PRO B CG  1 
ATOM   4011 C CD  . PRO B 1 238 ? 12.541  -17.333 -42.124 1.00 75.44  ? 281 PRO B CD  1 
ATOM   4012 N N   . ASP B 1 239 ? 13.151  -18.569 -38.642 1.00 79.63  ? 282 ASP B N   1 
ATOM   4013 C CA  . ASP B 1 239 ? 13.707  -19.134 -37.417 1.00 79.80  ? 282 ASP B CA  1 
ATOM   4014 C C   . ASP B 1 239 ? 14.220  -18.037 -36.492 1.00 77.80  ? 282 ASP B C   1 
ATOM   4015 O O   . ASP B 1 239 ? 13.995  -18.082 -35.277 1.00 74.86  ? 282 ASP B O   1 
ATOM   4016 C CB  . ASP B 1 239 ? 14.823  -20.121 -37.756 1.00 85.10  ? 282 ASP B CB  1 
ATOM   4017 C CG  . ASP B 1 239 ? 15.903  -19.505 -38.624 1.00 87.92  ? 282 ASP B CG  1 
ATOM   4018 O OD1 . ASP B 1 239 ? 15.599  -18.535 -39.351 1.00 79.17  ? 282 ASP B OD1 1 
ATOM   4019 O OD2 . ASP B 1 239 ? 17.053  -19.990 -38.580 1.00 93.46  ? 282 ASP B OD2 1 
ATOM   4020 N N   . LYS B 1 240 ? 14.911  -17.040 -37.051 1.00 80.41  ? 283 LYS B N   1 
ATOM   4021 C CA  . LYS B 1 240 ? 15.367  -15.916 -36.241 1.00 82.27  ? 283 LYS B CA  1 
ATOM   4022 C C   . LYS B 1 240 ? 14.198  -15.066 -35.759 1.00 83.21  ? 283 LYS B C   1 
ATOM   4023 O O   . LYS B 1 240 ? 14.256  -14.499 -34.662 1.00 84.74  ? 283 LYS B O   1 
ATOM   4024 C CB  . LYS B 1 240 ? 16.351  -15.060 -37.038 1.00 78.70  ? 283 LYS B CB  1 
ATOM   4025 N N   . PHE B 1 241 ? 13.134  -14.966 -36.559 1.00 80.85  ? 284 PHE B N   1 
ATOM   4026 C CA  . PHE B 1 241 ? 11.964  -14.201 -36.142 1.00 79.43  ? 284 PHE B CA  1 
ATOM   4027 C C   . PHE B 1 241 ? 11.352  -14.781 -34.873 1.00 78.53  ? 284 PHE B C   1 
ATOM   4028 O O   . PHE B 1 241 ? 10.963  -14.036 -33.966 1.00 79.26  ? 284 PHE B O   1 
ATOM   4029 C CB  . PHE B 1 241 ? 10.942  -14.165 -37.281 1.00 79.14  ? 284 PHE B CB  1 
ATOM   4030 C CG  . PHE B 1 241 ? 9.537   -13.878 -36.836 1.00 77.53  ? 284 PHE B CG  1 
ATOM   4031 C CD1 . PHE B 1 241 ? 9.132   -12.583 -36.553 1.00 75.18  ? 284 PHE B CD1 1 
ATOM   4032 C CD2 . PHE B 1 241 ? 8.614   -14.905 -36.718 1.00 74.98  ? 284 PHE B CD2 1 
ATOM   4033 C CE1 . PHE B 1 241 ? 7.835   -12.322 -36.148 1.00 71.17  ? 284 PHE B CE1 1 
ATOM   4034 C CE2 . PHE B 1 241 ? 7.318   -14.650 -36.315 1.00 69.43  ? 284 PHE B CE2 1 
ATOM   4035 C CZ  . PHE B 1 241 ? 6.927   -13.357 -36.031 1.00 69.17  ? 284 PHE B CZ  1 
ATOM   4036 N N   . LEU B 1 242 ? 11.259  -16.110 -34.788 1.00 73.68  ? 285 LEU B N   1 
ATOM   4037 C CA  . LEU B 1 242 ? 10.723  -16.734 -33.582 1.00 71.34  ? 285 LEU B CA  1 
ATOM   4038 C C   . LEU B 1 242 ? 11.620  -16.479 -32.375 1.00 76.91  ? 285 LEU B C   1 
ATOM   4039 O O   . LEU B 1 242 ? 11.131  -16.149 -31.289 1.00 76.59  ? 285 LEU B O   1 
ATOM   4040 C CB  . LEU B 1 242 ? 10.545  -18.235 -33.801 1.00 67.55  ? 285 LEU B CB  1 
ATOM   4041 C CG  . LEU B 1 242 ? 9.213   -18.686 -34.399 1.00 64.16  ? 285 LEU B CG  1 
ATOM   4042 C CD1 . LEU B 1 242 ? 9.267   -20.165 -34.745 1.00 58.01  ? 285 LEU B CD1 1 
ATOM   4043 C CD2 . LEU B 1 242 ? 8.066   -18.405 -33.438 1.00 55.70  ? 285 LEU B CD2 1 
ATOM   4044 N N   . GLN B 1 243 ? 12.937  -16.627 -32.544 1.00 79.90  ? 286 GLN B N   1 
ATOM   4045 C CA  . GLN B 1 243 ? 13.843  -16.470 -31.411 1.00 85.58  ? 286 GLN B CA  1 
ATOM   4046 C C   . GLN B 1 243 ? 13.802  -15.052 -30.855 1.00 89.02  ? 286 GLN B C   1 
ATOM   4047 O O   . GLN B 1 243 ? 13.971  -14.855 -29.647 1.00 93.48  ? 286 GLN B O   1 
ATOM   4048 C CB  . GLN B 1 243 ? 15.269  -16.839 -31.823 1.00 87.29  ? 286 GLN B CB  1 
ATOM   4049 C CG  . GLN B 1 243 ? 16.212  -17.082 -30.653 1.00 97.06  ? 286 GLN B CG  1 
ATOM   4050 C CD  . GLN B 1 243 ? 15.867  -18.341 -29.876 1.00 100.05 ? 286 GLN B CD  1 
ATOM   4051 O OE1 . GLN B 1 243 ? 15.113  -18.298 -28.904 1.00 100.77 ? 286 GLN B OE1 1 
ATOM   4052 N NE2 . GLN B 1 243 ? 16.421  -19.470 -30.303 1.00 100.44 ? 286 GLN B NE2 1 
ATOM   4053 N N   . CYS B 1 244 ? 13.583  -14.055 -31.715 1.00 86.99  ? 287 CYS B N   1 
ATOM   4054 C CA  . CYS B 1 244 ? 13.462  -12.683 -31.233 1.00 93.32  ? 287 CYS B CA  1 
ATOM   4055 C C   . CYS B 1 244 ? 12.183  -12.486 -30.431 1.00 93.11  ? 287 CYS B C   1 
ATOM   4056 O O   . CYS B 1 244 ? 12.156  -11.678 -29.496 1.00 99.53  ? 287 CYS B O   1 
ATOM   4057 C CB  . CYS B 1 244 ? 13.514  -11.706 -32.406 1.00 97.15  ? 287 CYS B CB  1 
ATOM   4058 S SG  . CYS B 1 244 ? 15.141  -11.567 -33.181 1.00 119.12 ? 287 CYS B SG  1 
ATOM   4059 N N   . VAL B 1 245 ? 11.114  -13.201 -30.787 1.00 83.41  ? 288 VAL B N   1 
ATOM   4060 C CA  . VAL B 1 245 ? 9.900   -13.167 -29.979 1.00 81.46  ? 288 VAL B CA  1 
ATOM   4061 C C   . VAL B 1 245 ? 10.100  -13.953 -28.689 1.00 87.97  ? 288 VAL B C   1 
ATOM   4062 O O   . VAL B 1 245 ? 9.494   -13.632 -27.659 1.00 85.57  ? 288 VAL B O   1 
ATOM   4063 C CB  . VAL B 1 245 ? 8.704   -13.697 -30.791 1.00 73.08  ? 288 VAL B CB  1 
ATOM   4064 C CG1 . VAL B 1 245 ? 7.430   -13.656 -29.963 1.00 64.71  ? 288 VAL B CG1 1 
ATOM   4065 C CG2 . VAL B 1 245 ? 8.528   -12.885 -32.063 1.00 66.28  ? 288 VAL B CG2 1 
ATOM   4066 N N   . LYS B 1 246 ? 10.940  -14.992 -28.718 1.00 98.14  ? 289 LYS B N   1 
ATOM   4067 C CA  . LYS B 1 246 ? 11.238  -15.739 -27.500 1.00 102.72 ? 289 LYS B CA  1 
ATOM   4068 C C   . LYS B 1 246 ? 12.132  -14.934 -26.564 1.00 108.60 ? 289 LYS B C   1 
ATOM   4069 O O   . LYS B 1 246 ? 11.887  -14.871 -25.354 1.00 113.12 ? 289 LYS B O   1 
ATOM   4070 C CB  . LYS B 1 246 ? 11.911  -17.069 -27.842 1.00 102.83 ? 289 LYS B CB  1 
ATOM   4071 C CG  . LYS B 1 246 ? 11.041  -18.059 -28.590 1.00 100.65 ? 289 LYS B CG  1 
ATOM   4072 C CD  . LYS B 1 246 ? 11.840  -19.306 -28.943 1.00 102.16 ? 289 LYS B CD  1 
ATOM   4073 C CE  . LYS B 1 246 ? 11.045  -20.264 -29.811 1.00 102.61 ? 289 LYS B CE  1 
ATOM   4074 N NZ  . LYS B 1 246 ? 11.909  -21.342 -30.369 1.00 105.11 ? 289 LYS B NZ  1 
ATOM   4075 N N   . ASN B 1 247 ? 13.184  -14.322 -27.106 1.00 107.16 ? 290 ASN B N   1 
ATOM   4076 C CA  . ASN B 1 247 ? 14.178  -13.599 -26.315 1.00 111.76 ? 290 ASN B CA  1 
ATOM   4077 C C   . ASN B 1 247 ? 14.368  -12.218 -26.924 1.00 115.69 ? 290 ASN B C   1 
ATOM   4078 O O   . ASN B 1 247 ? 15.340  -11.973 -27.652 1.00 114.23 ? 290 ASN B O   1 
ATOM   4079 C CB  . ASN B 1 247 ? 15.504  -14.361 -26.255 1.00 111.34 ? 290 ASN B CB  1 
ATOM   4080 N N   . PRO B 1 248 ? 13.453  -11.284 -26.650 1.00 121.69 ? 291 PRO B N   1 
ATOM   4081 C CA  . PRO B 1 248 ? 13.636  -9.913  -27.149 1.00 124.82 ? 291 PRO B CA  1 
ATOM   4082 C C   . PRO B 1 248 ? 14.876  -9.247  -26.579 1.00 126.48 ? 291 PRO B C   1 
ATOM   4083 O O   . PRO B 1 248 ? 15.310  -8.214  -27.106 1.00 127.61 ? 291 PRO B O   1 
ATOM   4084 C CB  . PRO B 1 248 ? 12.348  -9.202  -26.711 1.00 127.50 ? 291 PRO B CB  1 
ATOM   4085 C CG  . PRO B 1 248 ? 11.871  -9.980  -25.531 1.00 126.90 ? 291 PRO B CG  1 
ATOM   4086 C CD  . PRO B 1 248 ? 12.248  -11.409 -25.807 1.00 123.11 ? 291 PRO B CD  1 
ATOM   4087 N N   . GLU B 1 249 ? 15.458  -9.823  -25.525 1.00 133.09 ? 292 GLU B N   1 
ATOM   4088 C CA  . GLU B 1 249 ? 16.681  -9.328  -24.899 1.00 130.84 ? 292 GLU B CA  1 
ATOM   4089 C C   . GLU B 1 249 ? 17.862  -9.692  -25.800 1.00 124.19 ? 292 GLU B C   1 
ATOM   4090 O O   . GLU B 1 249 ? 18.651  -10.588 -25.506 1.00 122.76 ? 292 GLU B O   1 
ATOM   4091 C CB  . GLU B 1 249 ? 16.842  -9.935  -23.512 1.00 131.39 ? 292 GLU B CB  1 
ATOM   4092 C CG  . GLU B 1 249 ? 17.049  -11.454 -23.547 1.00 131.16 ? 292 GLU B CG  1 
ATOM   4093 C CD  . GLU B 1 249 ? 16.365  -12.182 -22.413 1.00 131.31 ? 292 GLU B CD  1 
ATOM   4094 O OE1 . GLU B 1 249 ? 16.112  -11.555 -21.365 1.00 132.55 ? 292 GLU B OE1 1 
ATOM   4095 O OE2 . GLU B 1 249 ? 16.078  -13.387 -22.574 1.00 128.66 ? 292 GLU B OE2 1 
ATOM   4096 N N   . ASP B 1 250 ? 17.961  -8.967  -26.914 1.00 118.84 ? 293 ASP B N   1 
ATOM   4097 C CA  . ASP B 1 250 ? 18.981  -9.173  -27.950 1.00 106.81 ? 293 ASP B CA  1 
ATOM   4098 C C   . ASP B 1 250 ? 18.419  -8.731  -29.303 1.00 97.32  ? 293 ASP B C   1 
ATOM   4099 O O   . ASP B 1 250 ? 18.664  -7.612  -29.752 1.00 97.47  ? 293 ASP B O   1 
ATOM   4100 C CB  . ASP B 1 250 ? 19.449  -10.632 -28.032 1.00 102.82 ? 293 ASP B CB  1 
ATOM   4101 C CG  . ASP B 1 250 ? 20.698  -10.894 -27.193 1.00 104.83 ? 293 ASP B CG  1 
ATOM   4102 O OD1 . ASP B 1 250 ? 21.241  -9.934  -26.607 1.00 102.19 ? 293 ASP B OD1 1 
ATOM   4103 O OD2 . ASP B 1 250 ? 21.134  -12.061 -27.111 1.00 101.65 ? 293 ASP B OD2 1 
HETATM 4104 O O2R . NNR C 2 .   ? -15.763 4.481   -0.124  1.00 52.01  ? 401 NNR A O2R 1 
HETATM 4105 C C2R . NNR C 2 .   ? -14.842 4.408   -1.160  1.00 52.08  ? 401 NNR A C2R 1 
HETATM 4106 C C3R . NNR C 2 .   ? -14.192 5.732   -1.567  1.00 56.67  ? 401 NNR A C3R 1 
HETATM 4107 O O3R . NNR C 2 .   ? -13.916 6.473   -0.412  1.00 58.46  ? 401 NNR A O3R 1 
HETATM 4108 C C4R . NNR C 2 .   ? -15.347 6.320   -2.376  1.00 51.68  ? 401 NNR A C4R 1 
HETATM 4109 C C5R . NNR C 2 .   ? -14.945 7.453   -3.293  1.00 53.49  ? 401 NNR A C5R 1 
HETATM 4110 O O5R . NNR C 2 .   ? -13.688 7.151   -3.851  1.00 53.25  ? 401 NNR A O5R 1 
HETATM 4111 O O4R . NNR C 2 .   ? -15.856 5.192   -3.115  1.00 47.81  ? 401 NNR A O4R 1 
HETATM 4112 C C1R . NNR C 2 .   ? -15.560 4.020   -2.464  1.00 47.28  ? 401 NNR A C1R 1 
HETATM 4113 N N1  . NNR C 2 .   ? -14.714 3.146   -3.352  1.00 41.37  ? 401 NNR A N1  1 
HETATM 4114 C C2  . NNR C 2 .   ? -13.830 3.740   -4.166  1.00 40.94  ? 401 NNR A C2  1 
HETATM 4115 C C6  . NNR C 2 .   ? -14.856 1.814   -3.341  1.00 41.76  ? 401 NNR A C6  1 
HETATM 4116 C C5  . NNR C 2 .   ? -14.084 1.029   -4.168  1.00 39.29  ? 401 NNR A C5  1 
HETATM 4117 C C4  . NNR C 2 .   ? -13.163 1.622   -5.014  1.00 37.95  ? 401 NNR A C4  1 
HETATM 4118 C C3  . NNR C 2 .   ? -13.026 3.004   -5.015  1.00 39.08  ? 401 NNR A C3  1 
HETATM 4119 C C7  . NNR C 2 .   ? -12.062 3.765   -5.886  1.00 38.11  ? 401 NNR A C7  1 
HETATM 4120 O O7  . NNR C 2 .   ? -12.020 4.984   -5.818  1.00 39.29  ? 401 NNR A O7  1 
HETATM 4121 N N7  . NNR C 2 .   ? -11.287 3.034   -6.689  1.00 34.75  ? 401 NNR A N7  1 
HETATM 4122 O O5  . RIB D 3 .   ? -10.704 -5.179  -7.942  1.00 25.74  ? 402 RIB A O5  1 
HETATM 4123 C C5  . RIB D 3 .   ? -10.477 -4.198  -7.020  1.00 27.73  ? 402 RIB A C5  1 
HETATM 4124 C C4  . RIB D 3 .   ? -11.792 -4.076  -6.237  1.00 30.60  ? 402 RIB A C4  1 
HETATM 4125 O O4  . RIB D 3 .   ? -11.865 -5.052  -5.205  1.00 29.83  ? 402 RIB A O4  1 
HETATM 4126 C C3  . RIB D 3 .   ? -11.925 -2.728  -5.412  1.00 32.42  ? 402 RIB A C3  1 
HETATM 4127 O O3  . RIB D 3 .   ? -12.281 -1.757  -6.289  1.00 32.27  ? 402 RIB A O3  1 
HETATM 4128 C C2  . RIB D 3 .   ? -13.008 -3.112  -4.362  1.00 34.32  ? 402 RIB A C2  1 
HETATM 4129 O O2  . RIB D 3 .   ? -14.241 -2.854  -4.905  1.00 31.80  ? 402 RIB A O2  1 
HETATM 4130 C C1  . RIB D 3 .   ? -12.737 -4.654  -4.200  1.00 29.64  ? 402 RIB A C1  1 
HETATM 4131 O O2R . NNR E 2 .   ? -9.825  -27.254 -46.282 1.00 39.84  ? 401 NNR B O2R 1 
HETATM 4132 C C2R . NNR E 2 .   ? -9.173  -27.248 -45.056 1.00 39.99  ? 401 NNR B C2R 1 
HETATM 4133 C C3R . NNR E 2 .   ? -8.624  -28.602 -44.596 1.00 41.08  ? 401 NNR B C3R 1 
HETATM 4134 O O3R . NNR E 2 .   ? -8.151  -29.299 -45.712 1.00 43.62  ? 401 NNR B O3R 1 
HETATM 4135 C C4R . NNR E 2 .   ? -9.902  -29.208 -44.023 1.00 39.21  ? 401 NNR B C4R 1 
HETATM 4136 C C5R . NNR E 2 .   ? -9.661  -30.379 -43.095 1.00 40.97  ? 401 NNR B C5R 1 
HETATM 4137 O O5R . NNR E 2 .   ? -8.751  -29.973 -42.098 1.00 42.01  ? 401 NNR B O5R 1 
HETATM 4138 O O4R . NNR E 2 .   ? -10.516 -28.102 -43.332 1.00 38.36  ? 401 NNR B O4R 1 
HETATM 4139 C C1R . NNR E 2 .   ? -10.172 -26.917 -43.931 1.00 37.78  ? 401 NNR B C1R 1 
HETATM 4140 N N1  . NNR E 2 .   ? -9.566  -25.978 -42.922 1.00 35.93  ? 401 NNR B N1  1 
HETATM 4141 C C2  . NNR E 2 .   ? -8.823  -26.510 -41.939 1.00 35.37  ? 401 NNR B C2  1 
HETATM 4142 C C6  . NNR E 2 .   ? -9.767  -24.657 -43.006 1.00 33.08  ? 401 NNR B C6  1 
HETATM 4143 C C5  . NNR E 2 .   ? -9.203  -23.816 -42.074 1.00 34.29  ? 401 NNR B C5  1 
HETATM 4144 C C4  . NNR E 2 .   ? -8.433  -24.341 -41.051 1.00 33.08  ? 401 NNR B C4  1 
HETATM 4145 C C3  . NNR E 2 .   ? -8.234  -25.713 -40.976 1.00 33.78  ? 401 NNR B C3  1 
HETATM 4146 C C7  . NNR E 2 .   ? -7.417  -26.395 -39.911 1.00 36.82  ? 401 NNR B C7  1 
HETATM 4147 O O7  . NNR E 2 .   ? -7.077  -27.555 -40.070 1.00 36.95  ? 401 NNR B O7  1 
HETATM 4148 N N7  . NNR E 2 .   ? -7.112  -25.666 -38.835 1.00 34.47  ? 401 NNR B N7  1 
HETATM 4149 O O5  . RIB F 3 .   ? -6.812  -17.518 -37.546 1.00 26.25  ? 402 RIB B O5  1 
HETATM 4150 C C5  . RIB F 3 .   ? -6.407  -18.519 -38.389 1.00 29.27  ? 402 RIB B C5  1 
HETATM 4151 C C4  . RIB F 3 .   ? -7.531  -18.647 -39.444 1.00 29.07  ? 402 RIB B C4  1 
HETATM 4152 O O4  . RIB F 3 .   ? -7.432  -17.650 -40.445 1.00 28.63  ? 402 RIB B O4  1 
HETATM 4153 C C3  . RIB F 3 .   ? -7.459  -19.995 -40.274 1.00 31.06  ? 402 RIB B C3  1 
HETATM 4154 O O3  . RIB F 3 .   ? -8.063  -20.955 -39.525 1.00 31.42  ? 402 RIB B O3  1 
HETATM 4155 C C2  . RIB F 3 .   ? -8.195  -19.610 -41.601 1.00 32.40  ? 402 RIB B C2  1 
HETATM 4156 O O2  . RIB F 3 .   ? -9.526  -19.894 -41.465 1.00 31.83  ? 402 RIB B O2  1 
HETATM 4157 C C1  . RIB F 3 .   ? -7.941  -18.057 -41.670 1.00 30.19  ? 402 RIB B C1  1 
HETATM 4158 O O   . HOH G 4 .   ? -29.409 21.751  -7.197  1.00 39.18  ? 501 HOH A O   1 
HETATM 4159 O O   . HOH G 4 .   ? -6.256  -7.998  12.099  1.00 48.09  ? 502 HOH A O   1 
HETATM 4160 O O   . HOH G 4 .   ? -6.088  -19.735 -13.931 1.00 39.55  ? 503 HOH A O   1 
HETATM 4161 O O   . HOH G 4 .   ? -8.582  -23.562 4.352   1.00 35.81  ? 504 HOH A O   1 
HETATM 4162 O O   . HOH G 4 .   ? -25.136 15.794  7.891   1.00 37.17  ? 505 HOH A O   1 
HETATM 4163 O O   . HOH G 4 .   ? -16.502 -23.879 -9.194  1.00 44.66  ? 506 HOH A O   1 
HETATM 4164 O O   . HOH G 4 .   ? 9.866   -9.336  17.484  1.00 33.33  ? 507 HOH A O   1 
HETATM 4165 O O   . HOH G 4 .   ? -13.853 -0.071  4.693   1.00 40.37  ? 508 HOH A O   1 
HETATM 4166 O O   . HOH G 4 .   ? 5.898   -5.526  9.311   1.00 52.35  ? 509 HOH A O   1 
HETATM 4167 O O   . HOH G 4 .   ? -7.439  -16.367 -19.056 1.00 39.61  ? 510 HOH A O   1 
HETATM 4168 O O   . HOH G 4 .   ? 13.628  -3.869  -5.106  1.00 52.69  ? 511 HOH A O   1 
HETATM 4169 O O   . HOH G 4 .   ? 16.949  -7.445  -4.034  1.00 49.00  ? 512 HOH A O   1 
HETATM 4170 O O   . HOH G 4 .   ? -0.856  -13.638 -14.639 1.00 52.48  ? 513 HOH A O   1 
HETATM 4171 O O   . HOH G 4 .   ? -29.202 16.933  5.216   1.00 39.27  ? 514 HOH A O   1 
HETATM 4172 O O   . HOH G 4 .   ? -12.067 -8.396  10.984  1.00 39.95  ? 515 HOH A O   1 
HETATM 4173 O O   . HOH G 4 .   ? -23.141 -10.583 -12.915 1.00 39.73  ? 516 HOH A O   1 
HETATM 4174 O O   . HOH G 4 .   ? 13.101  -4.818  -10.963 1.00 69.30  ? 517 HOH A O   1 
HETATM 4175 O O   . HOH G 4 .   ? -10.669 -15.544 14.155  1.00 39.35  ? 518 HOH A O   1 
HETATM 4176 O O   . HOH G 4 .   ? 5.568   -11.546 -14.156 1.00 54.85  ? 519 HOH A O   1 
HETATM 4177 O O   . HOH G 4 .   ? -6.911  9.362   -17.506 1.00 34.47  ? 520 HOH A O   1 
HETATM 4178 O O   . HOH G 4 .   ? -39.176 27.273  -6.075  1.00 51.18  ? 521 HOH A O   1 
HETATM 4179 O O   . HOH G 4 .   ? -23.605 10.074  -28.763 1.00 41.48  ? 522 HOH A O   1 
HETATM 4180 O O   . HOH G 4 .   ? -24.315 -12.381 -6.489  1.00 35.01  ? 523 HOH A O   1 
HETATM 4181 O O   . HOH G 4 .   ? -18.858 -2.017  -23.847 1.00 31.37  ? 524 HOH A O   1 
HETATM 4182 O O   . HOH G 4 .   ? 11.062  -8.516  11.957  1.00 41.65  ? 525 HOH A O   1 
HETATM 4183 O O   . HOH G 4 .   ? 0.669   -3.271  4.085   1.00 35.33  ? 526 HOH A O   1 
HETATM 4184 O O   . HOH G 4 .   ? -17.559 -14.769 -16.143 1.00 41.77  ? 527 HOH A O   1 
HETATM 4185 O O   . HOH G 4 .   ? -17.095 -21.792 7.771   1.00 38.24  ? 528 HOH A O   1 
HETATM 4186 O O   . HOH G 4 .   ? -6.675  -14.021 -9.928  1.00 30.63  ? 529 HOH A O   1 
HETATM 4187 O O   . HOH G 4 .   ? -4.200  5.941   -17.944 1.00 39.82  ? 530 HOH A O   1 
HETATM 4188 O O   . HOH G 4 .   ? 9.359   -13.832 9.076   1.00 29.03  ? 531 HOH A O   1 
HETATM 4189 O O   . HOH G 4 .   ? -14.960 7.236   -6.424  1.00 25.85  ? 532 HOH A O   1 
HETATM 4190 O O   . HOH G 4 .   ? -14.367 5.694   -27.722 1.00 37.93  ? 533 HOH A O   1 
HETATM 4191 O O   . HOH G 4 .   ? -21.043 3.715   -26.264 1.00 33.78  ? 534 HOH A O   1 
HETATM 4192 O O   . HOH G 4 .   ? -34.680 4.883   -11.024 1.00 40.46  ? 535 HOH A O   1 
HETATM 4193 O O   . HOH G 4 .   ? 8.446   -13.250 14.622  1.00 29.88  ? 536 HOH A O   1 
HETATM 4194 O O   . HOH G 4 .   ? -1.355  -11.564 13.893  1.00 45.65  ? 537 HOH A O   1 
HETATM 4195 O O   . HOH G 4 .   ? -6.122  -3.830  -24.519 1.00 42.98  ? 538 HOH A O   1 
HETATM 4196 O O   . HOH G 4 .   ? 4.052   -0.718  -11.077 1.00 38.34  ? 539 HOH A O   1 
HETATM 4197 O O   . HOH G 4 .   ? -5.244  -9.220  15.025  1.00 47.39  ? 540 HOH A O   1 
HETATM 4198 O O   . HOH G 4 .   ? -31.793 11.527  -14.043 1.00 33.12  ? 541 HOH A O   1 
HETATM 4199 O O   . HOH G 4 .   ? -28.132 12.703  -6.845  1.00 23.24  ? 542 HOH A O   1 
HETATM 4200 O O   . HOH G 4 .   ? -16.621 20.366  -4.703  1.00 33.66  ? 543 HOH A O   1 
HETATM 4201 O O   . HOH G 4 .   ? -7.646  -3.103  6.939   1.00 48.02  ? 544 HOH A O   1 
HETATM 4202 O O   . HOH G 4 .   ? -29.278 17.305  -9.842  1.00 28.13  ? 545 HOH A O   1 
HETATM 4203 O O   . HOH G 4 .   ? -0.011  -20.108 7.607   1.00 43.40  ? 546 HOH A O   1 
HETATM 4204 O O   . HOH G 4 .   ? -8.839  12.481  -22.906 1.00 34.74  ? 547 HOH A O   1 
HETATM 4205 O O   . HOH G 4 .   ? -15.585 1.813   -0.022  1.00 48.39  ? 548 HOH A O   1 
HETATM 4206 O O   . HOH G 4 .   ? -23.476 -7.027  2.326   1.00 31.99  ? 549 HOH A O   1 
HETATM 4207 O O   . HOH G 4 .   ? -6.558  -4.937  4.415   1.00 29.75  ? 550 HOH A O   1 
HETATM 4208 O O   . HOH G 4 .   ? -28.779 5.226   5.133   1.00 40.29  ? 551 HOH A O   1 
HETATM 4209 O O   . HOH G 4 .   ? -27.947 17.488  -3.144  1.00 28.89  ? 552 HOH A O   1 
HETATM 4210 O O   . HOH G 4 .   ? -20.819 11.054  -1.158  1.00 30.54  ? 553 HOH A O   1 
HETATM 4211 O O   . HOH G 4 .   ? -20.856 20.978  -14.128 1.00 36.53  ? 554 HOH A O   1 
HETATM 4212 O O   . HOH G 4 .   ? -4.566  -1.310  -23.052 1.00 45.70  ? 555 HOH A O   1 
HETATM 4213 O O   . HOH G 4 .   ? 2.939   -19.847 11.189  1.00 36.61  ? 556 HOH A O   1 
HETATM 4214 O O   . HOH G 4 .   ? -35.975 20.656  -6.438  1.00 37.33  ? 557 HOH A O   1 
HETATM 4215 O O   . HOH G 4 .   ? -15.791 -23.675 -5.307  1.00 34.16  ? 558 HOH A O   1 
HETATM 4216 O O   . HOH G 4 .   ? -5.279  -11.791 -19.073 1.00 42.48  ? 559 HOH A O   1 
HETATM 4217 O O   . HOH G 4 .   ? -12.935 -0.378  -0.688  1.00 38.40  ? 560 HOH A O   1 
HETATM 4218 O O   . HOH G 4 .   ? -22.128 -17.509 9.186   1.00 36.94  ? 561 HOH A O   1 
HETATM 4219 O O   . HOH G 4 .   ? -9.756  -14.579 -11.078 1.00 22.38  ? 562 HOH A O   1 
HETATM 4220 O O   . HOH G 4 .   ? -16.038 -1.519  -17.853 1.00 26.37  ? 563 HOH A O   1 
HETATM 4221 O O   . HOH G 4 .   ? -22.583 -14.165 -6.798  1.00 31.10  ? 564 HOH A O   1 
HETATM 4222 O O   . HOH G 4 .   ? -2.192  -18.371 -7.551  1.00 41.76  ? 565 HOH A O   1 
HETATM 4223 O O   . HOH G 4 .   ? -26.914 4.736   -15.488 1.00 28.35  ? 566 HOH A O   1 
HETATM 4224 O O   . HOH G 4 .   ? -27.135 7.809   9.193   1.00 45.36  ? 567 HOH A O   1 
HETATM 4225 O O   . HOH G 4 .   ? -24.140 22.993  -10.556 1.00 37.52  ? 568 HOH A O   1 
HETATM 4226 O O   . HOH G 4 .   ? -25.552 20.786  -0.221  1.00 30.23  ? 569 HOH A O   1 
HETATM 4227 O O   . HOH G 4 .   ? -19.929 -17.115 4.877   1.00 35.22  ? 570 HOH A O   1 
HETATM 4228 O O   . HOH G 4 .   ? -25.170 1.972   -0.767  1.00 31.47  ? 571 HOH A O   1 
HETATM 4229 O O   . HOH G 4 .   ? -16.225 -2.633  -14.623 1.00 32.51  ? 572 HOH A O   1 
HETATM 4230 O O   . HOH G 4 .   ? -0.520  3.075   -7.819  1.00 37.08  ? 573 HOH A O   1 
HETATM 4231 O O   . HOH G 4 .   ? -22.391 10.596  -3.450  1.00 25.38  ? 574 HOH A O   1 
HETATM 4232 O O   . HOH G 4 .   ? -10.985 6.831   -3.268  1.00 40.21  ? 575 HOH A O   1 
HETATM 4233 O O   . HOH G 4 .   ? -24.646 -16.771 6.026   1.00 35.87  ? 576 HOH A O   1 
HETATM 4234 O O   . HOH G 4 .   ? -30.791 6.028   -14.650 1.00 31.90  ? 577 HOH A O   1 
HETATM 4235 O O   . HOH G 4 .   ? -30.391 -0.986  -5.263  1.00 36.05  ? 578 HOH A O   1 
HETATM 4236 O O   . HOH G 4 .   ? -17.633 -15.329 -9.421  1.00 23.01  ? 579 HOH A O   1 
HETATM 4237 O O   . HOH G 4 .   ? -21.116 -3.924  -16.903 1.00 37.15  ? 580 HOH A O   1 
HETATM 4238 O O   . HOH G 4 .   ? -10.968 -6.427  4.358   1.00 31.41  ? 581 HOH A O   1 
HETATM 4239 O O   . HOH G 4 .   ? -14.159 -7.023  10.677  1.00 40.97  ? 582 HOH A O   1 
HETATM 4240 O O   . HOH G 4 .   ? -30.117 24.476  -16.298 1.00 56.63  ? 583 HOH A O   1 
HETATM 4241 O O   . HOH G 4 .   ? -8.599  6.828   -13.246 1.00 36.41  ? 584 HOH A O   1 
HETATM 4242 O O   . HOH G 4 .   ? -18.567 4.382   -0.310  1.00 45.18  ? 585 HOH A O   1 
HETATM 4243 O O   . HOH G 4 .   ? -16.817 5.579   -30.666 1.00 45.02  ? 586 HOH A O   1 
HETATM 4244 O O   . HOH G 4 .   ? -20.248 -10.985 11.477  1.00 49.21  ? 587 HOH A O   1 
HETATM 4245 O O   . HOH G 4 .   ? -29.339 1.252   -2.869  1.00 31.73  ? 588 HOH A O   1 
HETATM 4246 O O   . HOH G 4 .   ? 7.112   -15.370 9.416   1.00 32.29  ? 589 HOH A O   1 
HETATM 4247 O O   . HOH G 4 .   ? -36.061 10.407  -3.428  1.00 29.75  ? 590 HOH A O   1 
HETATM 4248 O O   . HOH G 4 .   ? -17.348 -4.741  -24.592 1.00 36.60  ? 591 HOH A O   1 
HETATM 4249 O O   . HOH G 4 .   ? -18.292 10.475  -28.246 1.00 39.23  ? 592 HOH A O   1 
HETATM 4250 O O   . HOH G 4 .   ? -34.887 2.539   -9.229  1.00 38.83  ? 593 HOH A O   1 
HETATM 4251 O O   . HOH G 4 .   ? -24.185 -4.842  -4.661  1.00 34.26  ? 594 HOH A O   1 
HETATM 4252 O O   . HOH G 4 .   ? -1.961  0.656   -25.385 1.00 49.13  ? 595 HOH A O   1 
HETATM 4253 O O   . HOH G 4 .   ? -16.587 8.889   5.988   1.00 42.63  ? 596 HOH A O   1 
HETATM 4254 O O   . HOH G 4 .   ? -36.070 12.471  -10.829 1.00 42.53  ? 597 HOH A O   1 
HETATM 4255 O O   . HOH G 4 .   ? 3.107   -5.916  8.857   1.00 44.78  ? 598 HOH A O   1 
HETATM 4256 O O   . HOH G 4 .   ? -32.448 16.447  -3.263  1.00 29.06  ? 599 HOH A O   1 
HETATM 4257 O O   . HOH G 4 .   ? -37.129 26.516  1.207   1.00 32.06  ? 600 HOH A O   1 
HETATM 4258 O O   . HOH G 4 .   ? 10.250  -10.382 6.526   1.00 41.60  ? 601 HOH A O   1 
HETATM 4259 O O   . HOH G 4 .   ? -29.271 11.748  -18.798 1.00 43.62  ? 602 HOH A O   1 
HETATM 4260 O O   . HOH G 4 .   ? -20.765 1.133   -25.284 1.00 35.58  ? 603 HOH A O   1 
HETATM 4261 O O   . HOH G 4 .   ? -28.827 6.883   -16.839 1.00 31.27  ? 604 HOH A O   1 
HETATM 4262 O O   . HOH G 4 .   ? -33.064 12.192  2.967   1.00 41.11  ? 605 HOH A O   1 
HETATM 4263 O O   . HOH G 4 .   ? 6.645   -7.674  8.690   1.00 40.58  ? 606 HOH A O   1 
HETATM 4264 O O   . HOH G 4 .   ? -3.154  -0.300  -12.610 1.00 36.17  ? 607 HOH A O   1 
HETATM 4265 O O   . HOH G 4 .   ? -27.377 20.600  -7.007  1.00 36.49  ? 608 HOH A O   1 
HETATM 4266 O O   . HOH G 4 .   ? -6.912  -18.131 -11.814 1.00 36.91  ? 609 HOH A O   1 
HETATM 4267 O O   . HOH G 4 .   ? -10.788 -5.365  -22.124 1.00 32.25  ? 610 HOH A O   1 
HETATM 4268 O O   . HOH G 4 .   ? -21.023 -9.974  -13.705 1.00 34.08  ? 611 HOH A O   1 
HETATM 4269 O O   . HOH G 4 .   ? -3.895  -4.459  -16.384 1.00 43.08  ? 612 HOH A O   1 
HETATM 4270 O O   . HOH G 4 .   ? -31.834 18.587  -0.390  1.00 39.43  ? 613 HOH A O   1 
HETATM 4271 O O   . HOH G 4 .   ? -26.628 7.212   -22.567 1.00 33.24  ? 614 HOH A O   1 
HETATM 4272 O O   . HOH G 4 .   ? -10.582 -20.511 10.217  1.00 38.10  ? 615 HOH A O   1 
HETATM 4273 O O   . HOH G 4 .   ? -15.653 -9.951  -17.343 1.00 41.68  ? 616 HOH A O   1 
HETATM 4274 O O   . HOH G 4 .   ? -28.520 14.705  6.733   1.00 40.27  ? 617 HOH A O   1 
HETATM 4275 O O   . HOH G 4 .   ? -13.699 25.729  -4.138  1.00 43.05  ? 618 HOH A O   1 
HETATM 4276 O O   . HOH G 4 .   ? -7.695  -1.559  10.914  1.00 61.94  ? 619 HOH A O   1 
HETATM 4277 O O   . HOH G 4 .   ? 3.305   -17.329 3.202   1.00 34.01  ? 620 HOH A O   1 
HETATM 4278 O O   . HOH G 4 .   ? -35.140 10.895  -5.816  1.00 23.36  ? 621 HOH A O   1 
HETATM 4279 O O   . HOH G 4 .   ? -23.468 -18.161 -7.680  1.00 42.64  ? 622 HOH A O   1 
HETATM 4280 O O   . HOH G 4 .   ? -20.046 8.046   -0.220  1.00 36.11  ? 623 HOH A O   1 
HETATM 4281 O O   . HOH G 4 .   ? -18.690 12.796  -0.724  1.00 33.25  ? 624 HOH A O   1 
HETATM 4282 O O   . HOH G 4 .   ? 4.623   -8.643  10.728  1.00 43.14  ? 625 HOH A O   1 
HETATM 4283 O O   . HOH G 4 .   ? -2.888  2.407   -1.091  1.00 41.87  ? 626 HOH A O   1 
HETATM 4284 O O   . HOH G 4 .   ? -16.433 22.495  -11.492 1.00 36.57  ? 627 HOH A O   1 
HETATM 4285 O O   . HOH G 4 .   ? -34.051 19.628  2.295   1.00 39.41  ? 628 HOH A O   1 
HETATM 4286 O O   . HOH G 4 .   ? -22.856 17.561  -18.617 1.00 39.04  ? 629 HOH A O   1 
HETATM 4287 O O   . HOH G 4 .   ? 8.353   -10.836 -0.538  1.00 43.34  ? 630 HOH A O   1 
HETATM 4288 O O   . HOH G 4 .   ? -18.999 -5.842  -17.713 1.00 37.49  ? 631 HOH A O   1 
HETATM 4289 O O   . HOH G 4 .   ? -7.479  8.125   -10.962 1.00 31.36  ? 632 HOH A O   1 
HETATM 4290 O O   . HOH G 4 .   ? -3.234  3.849   -7.414  1.00 42.27  ? 633 HOH A O   1 
HETATM 4291 O O   . HOH G 4 .   ? -30.043 5.761   2.164   1.00 37.09  ? 634 HOH A O   1 
HETATM 4292 O O   . HOH G 4 .   ? 3.002   -3.404  11.148  1.00 55.25  ? 635 HOH A O   1 
HETATM 4293 O O   . HOH G 4 .   ? -19.467 9.091   2.008   1.00 35.56  ? 636 HOH A O   1 
HETATM 4294 O O   . HOH G 4 .   ? -23.442 23.457  -6.409  1.00 28.86  ? 637 HOH A O   1 
HETATM 4295 O O   . HOH G 4 .   ? -14.289 -2.622  -30.367 1.00 39.23  ? 638 HOH A O   1 
HETATM 4296 O O   . HOH G 4 .   ? -12.077 -3.401  -0.214  1.00 29.06  ? 639 HOH A O   1 
HETATM 4297 O O   . HOH G 4 .   ? -5.472  0.839   -18.010 1.00 43.24  ? 640 HOH A O   1 
HETATM 4298 O O   . HOH G 4 .   ? -22.893 -16.691 -5.381  1.00 32.50  ? 641 HOH A O   1 
HETATM 4299 O O   . HOH G 4 .   ? -13.687 -0.494  1.731   1.00 36.67  ? 642 HOH A O   1 
HETATM 4300 O O   . HOH G 4 .   ? -24.031 21.471  -12.967 1.00 34.00  ? 643 HOH A O   1 
HETATM 4301 O O   . HOH G 4 .   ? -34.467 18.392  -13.802 1.00 47.00  ? 644 HOH A O   1 
HETATM 4302 O O   . HOH G 4 .   ? -9.540  -24.264 2.078   1.00 34.40  ? 645 HOH A O   1 
HETATM 4303 O O   . HOH G 4 .   ? -27.818 1.656   -21.731 1.00 34.40  ? 646 HOH A O   1 
HETATM 4304 O O   . HOH G 4 .   ? 5.527   -16.519 12.711  1.00 35.55  ? 647 HOH A O   1 
HETATM 4305 O O   . HOH G 4 .   ? -13.468 -6.276  -28.296 1.00 44.45  ? 648 HOH A O   1 
HETATM 4306 O O   . HOH G 4 .   ? -5.037  5.473   -8.358  1.00 45.24  ? 649 HOH A O   1 
HETATM 4307 O O   . HOH G 4 .   ? -17.991 -4.301  -13.051 1.00 30.72  ? 650 HOH A O   1 
HETATM 4308 O O   . HOH G 4 .   ? -12.421 19.054  -6.089  1.00 31.34  ? 651 HOH A O   1 
HETATM 4309 O O   . HOH G 4 .   ? -13.632 -14.539 -19.263 1.00 38.70  ? 652 HOH A O   1 
HETATM 4310 O O   . HOH G 4 .   ? -10.896 -0.854  1.247   1.00 31.31  ? 653 HOH A O   1 
HETATM 4311 O O   . HOH G 4 .   ? -23.917 -14.180 -13.446 1.00 45.34  ? 654 HOH A O   1 
HETATM 4312 O O   . HOH G 4 .   ? -4.688  -19.373 6.936   1.00 49.25  ? 655 HOH A O   1 
HETATM 4313 O O   . HOH G 4 .   ? -6.965  9.892   -14.541 1.00 39.07  ? 656 HOH A O   1 
HETATM 4314 O O   . HOH G 4 .   ? -10.396 4.020   -2.722  1.00 46.58  ? 657 HOH A O   1 
HETATM 4315 O O   . HOH G 4 .   ? -24.102 4.049   -27.391 1.00 38.57  ? 658 HOH A O   1 
HETATM 4316 O O   . HOH G 4 .   ? -2.166  -7.462  12.639  1.00 50.93  ? 659 HOH A O   1 
HETATM 4317 O O   . HOH G 4 .   ? -27.116 24.428  0.239   1.00 47.09  ? 660 HOH A O   1 
HETATM 4318 O O   . HOH G 4 .   ? -29.087 9.618   9.454   1.00 45.59  ? 661 HOH A O   1 
HETATM 4319 O O   . HOH G 4 .   ? -9.484  -7.433  -21.804 1.00 46.23  ? 662 HOH A O   1 
HETATM 4320 O O   . HOH G 4 .   ? -9.062  13.697  -16.654 1.00 34.88  ? 663 HOH A O   1 
HETATM 4321 O O   . HOH G 4 .   ? -11.959 3.018   -0.973  1.00 46.55  ? 664 HOH A O   1 
HETATM 4322 O O   . HOH G 4 .   ? -30.278 17.524  -2.062  1.00 34.81  ? 665 HOH A O   1 
HETATM 4323 O O   . HOH G 4 .   ? -7.268  -8.555  -22.305 1.00 48.66  ? 666 HOH A O   1 
HETATM 4324 O O   . HOH H 4 .   ? -19.677 -32.871 -20.001 1.00 38.19  ? 501 HOH B O   1 
HETATM 4325 O O   . HOH H 4 .   ? -12.160 -43.232 -42.156 1.00 35.17  ? 502 HOH B O   1 
HETATM 4326 O O   . HOH H 4 .   ? -21.461 -39.668 -54.880 1.00 45.12  ? 503 HOH B O   1 
HETATM 4327 O O   . HOH H 4 .   ? -32.837 -49.789 -46.331 1.00 54.04  ? 504 HOH B O   1 
HETATM 4328 O O   . HOH H 4 .   ? -25.142 -32.298 -21.065 1.00 48.68  ? 505 HOH B O   1 
HETATM 4329 O O   . HOH H 4 .   ? -8.489  -37.437 -41.089 1.00 37.42  ? 506 HOH B O   1 
HETATM 4330 O O   . HOH H 4 .   ? -12.545 0.817   -37.358 1.00 44.34  ? 507 HOH B O   1 
HETATM 4331 O O   . HOH H 4 .   ? -8.414  -9.988  -57.468 1.00 51.31  ? 508 HOH B O   1 
HETATM 4332 O O   . HOH H 4 .   ? -16.534 -42.509 -28.238 1.00 37.73  ? 509 HOH B O   1 
HETATM 4333 O O   . HOH H 4 .   ? -5.553  -31.970 -27.185 1.00 34.67  ? 510 HOH B O   1 
HETATM 4334 O O   . HOH H 4 .   ? -17.886 -8.452  -41.561 1.00 35.32  ? 511 HOH B O   1 
HETATM 4335 O O   . HOH H 4 .   ? -19.611 -10.377 -42.311 1.00 35.14  ? 512 HOH B O   1 
HETATM 4336 O O   . HOH H 4 .   ? -22.326 -40.156 -46.428 1.00 32.01  ? 513 HOH B O   1 
HETATM 4337 O O   . HOH H 4 .   ? -4.251  -10.806 -25.691 1.00 44.88  ? 514 HOH B O   1 
HETATM 4338 O O   . HOH H 4 .   ? -23.617 -18.016 -36.591 1.00 58.70  ? 515 HOH B O   1 
HETATM 4339 O O   . HOH H 4 .   ? 4.677   -28.255 -42.306 1.00 57.40  ? 516 HOH B O   1 
HETATM 4340 O O   . HOH H 4 .   ? -19.069 -20.585 -24.620 1.00 34.76  ? 517 HOH B O   1 
HETATM 4341 O O   . HOH H 4 .   ? -23.645 -35.435 -43.047 1.00 28.40  ? 518 HOH B O   1 
HETATM 4342 O O   . HOH H 4 .   ? -19.146 -17.757 -44.306 1.00 36.10  ? 519 HOH B O   1 
HETATM 4343 O O   . HOH H 4 .   ? -3.544  -8.472  -34.498 1.00 33.26  ? 520 HOH B O   1 
HETATM 4344 O O   . HOH H 4 .   ? -25.702 -29.861 -27.155 1.00 35.56  ? 521 HOH B O   1 
HETATM 4345 O O   . HOH H 4 .   ? -6.891  -8.131  -34.193 1.00 25.03  ? 522 HOH B O   1 
HETATM 4346 O O   . HOH H 4 .   ? -3.297  -14.726 -56.359 1.00 47.55  ? 523 HOH B O   1 
HETATM 4347 O O   . HOH H 4 .   ? -3.986  -2.995  -30.798 1.00 34.81  ? 524 HOH B O   1 
HETATM 4348 O O   . HOH H 4 .   ? -0.986  -22.056 -30.791 1.00 38.99  ? 525 HOH B O   1 
HETATM 4349 O O   . HOH H 4 .   ? -10.601 -29.738 -40.283 1.00 26.01  ? 526 HOH B O   1 
HETATM 4350 O O   . HOH H 4 .   ? -27.125 -42.655 -53.202 1.00 40.01  ? 527 HOH B O   1 
HETATM 4351 O O   . HOH H 4 .   ? -4.573  -33.154 -20.078 1.00 44.55  ? 528 HOH B O   1 
HETATM 4352 O O   . HOH H 4 .   ? -5.898  -28.705 -42.105 1.00 46.20  ? 529 HOH B O   1 
HETATM 4353 O O   . HOH H 4 .   ? -13.619 -5.083  -57.301 1.00 40.55  ? 530 HOH B O   1 
HETATM 4354 O O   . HOH H 4 .   ? -28.737 -34.183 -37.150 1.00 33.52  ? 531 HOH B O   1 
HETATM 4355 O O   . HOH H 4 .   ? -21.795 -22.776 -51.023 1.00 44.89  ? 532 HOH B O   1 
HETATM 4356 O O   . HOH H 4 .   ? -28.961 -42.487 -46.797 1.00 45.37  ? 533 HOH B O   1 
HETATM 4357 O O   . HOH H 4 .   ? -5.152  -20.948 -20.531 1.00 46.16  ? 534 HOH B O   1 
HETATM 4358 O O   . HOH H 4 .   ? -28.101 -28.426 -36.220 1.00 35.37  ? 535 HOH B O   1 
HETATM 4359 O O   . HOH H 4 .   ? -25.344 -39.974 -40.407 1.00 34.66  ? 536 HOH B O   1 
HETATM 4360 O O   . HOH H 4 .   ? -8.666  0.891   -33.827 1.00 40.01  ? 537 HOH B O   1 
HETATM 4361 O O   . HOH H 4 .   ? 1.272   -9.206  -28.823 1.00 49.05  ? 538 HOH B O   1 
HETATM 4362 O O   . HOH H 4 .   ? -26.265 -50.195 -51.551 1.00 35.81  ? 539 HOH B O   1 
HETATM 4363 O O   . HOH H 4 .   ? -12.598 -5.741  -52.292 1.00 37.59  ? 540 HOH B O   1 
HETATM 4364 O O   . HOH H 4 .   ? -11.009 4.348   -48.324 1.00 51.39  ? 541 HOH B O   1 
HETATM 4365 O O   . HOH H 4 .   ? -14.750 1.657   -51.678 1.00 41.04  ? 542 HOH B O   1 
HETATM 4366 O O   . HOH H 4 .   ? 0.209   -17.697 -48.528 1.00 42.74  ? 543 HOH B O   1 
HETATM 4367 O O   . HOH H 4 .   ? -29.429 -26.065 -36.451 1.00 41.02  ? 544 HOH B O   1 
HETATM 4368 O O   . HOH H 4 .   ? -26.547 -29.809 -33.577 1.00 36.46  ? 545 HOH B O   1 
HETATM 4369 O O   . HOH H 4 .   ? -31.005 -27.146 -40.484 1.00 45.25  ? 546 HOH B O   1 
HETATM 4370 O O   . HOH H 4 .   ? -6.716  -19.069 -20.577 1.00 48.22  ? 547 HOH B O   1 
HETATM 4371 O O   . HOH H 4 .   ? -15.585 -27.616 -16.758 1.00 43.77  ? 548 HOH B O   1 
HETATM 4372 O O   . HOH H 4 .   ? -30.584 -33.278 -48.342 1.00 29.63  ? 549 HOH B O   1 
HETATM 4373 O O   . HOH H 4 .   ? -3.897  -16.357 -49.577 1.00 36.50  ? 550 HOH B O   1 
HETATM 4374 O O   . HOH H 4 .   ? -8.469  -35.213 -22.944 1.00 34.87  ? 551 HOH B O   1 
HETATM 4375 O O   . HOH H 4 .   ? -27.156 -34.271 -31.540 1.00 45.13  ? 552 HOH B O   1 
HETATM 4376 O O   . HOH H 4 .   ? -13.934 -7.397  -37.998 1.00 24.08  ? 553 HOH B O   1 
HETATM 4377 O O   . HOH H 4 .   ? -14.508 -21.090 -29.352 1.00 27.51  ? 554 HOH B O   1 
HETATM 4378 O O   . HOH H 4 .   ? -26.632 -24.478 -28.623 1.00 34.55  ? 555 HOH B O   1 
HETATM 4379 O O   . HOH H 4 .   ? -11.500 1.030   -41.643 1.00 34.74  ? 556 HOH B O   1 
HETATM 4380 O O   . HOH H 4 .   ? -20.634 -7.948  -35.561 1.00 44.59  ? 557 HOH B O   1 
HETATM 4381 O O   . HOH H 4 .   ? -3.704  -31.118 -35.244 1.00 43.26  ? 558 HOH B O   1 
HETATM 4382 O O   . HOH H 4 .   ? -1.477  -21.998 -26.082 1.00 52.70  ? 559 HOH B O   1 
HETATM 4383 O O   . HOH H 4 .   ? -23.043 -43.178 -42.529 1.00 42.31  ? 560 HOH B O   1 
HETATM 4384 O O   . HOH H 4 .   ? -10.936 -0.419  -33.462 1.00 44.28  ? 561 HOH B O   1 
HETATM 4385 O O   . HOH H 4 .   ? -21.706 -25.975 -22.764 1.00 38.82  ? 562 HOH B O   1 
HETATM 4386 O O   . HOH H 4 .   ? -6.423  -6.561  -25.804 1.00 39.75  ? 563 HOH B O   1 
HETATM 4387 O O   . HOH H 4 .   ? -15.350 -28.218 -19.809 1.00 40.70  ? 564 HOH B O   1 
HETATM 4388 O O   . HOH H 4 .   ? -18.138 -12.552 -34.472 1.00 38.08  ? 565 HOH B O   1 
HETATM 4389 O O   . HOH H 4 .   ? -14.088 -30.887 -47.383 1.00 36.34  ? 566 HOH B O   1 
HETATM 4390 O O   . HOH H 4 .   ? -15.075 -33.447 -46.606 1.00 33.39  ? 567 HOH B O   1 
HETATM 4391 O O   . HOH H 4 .   ? -32.276 -35.187 -41.258 1.00 41.14  ? 568 HOH B O   1 
HETATM 4392 O O   . HOH H 4 .   ? -24.419 -27.372 -34.394 1.00 31.00  ? 569 HOH B O   1 
HETATM 4393 O O   . HOH H 4 .   ? -20.965 -23.442 -23.365 1.00 37.73  ? 570 HOH B O   1 
HETATM 4394 O O   . HOH H 4 .   ? -28.424 -45.584 -37.836 1.00 46.52  ? 571 HOH B O   1 
HETATM 4395 O O   . HOH H 4 .   ? -19.372 -43.504 -48.696 1.00 41.85  ? 572 HOH B O   1 
HETATM 4396 O O   . HOH H 4 .   ? -17.050 -15.552 -50.637 1.00 34.02  ? 573 HOH B O   1 
HETATM 4397 O O   . HOH H 4 .   ? -17.041 -33.266 -45.065 1.00 26.54  ? 574 HOH B O   1 
HETATM 4398 O O   . HOH H 4 .   ? -16.791 -6.215  -54.524 1.00 37.04  ? 575 HOH B O   1 
HETATM 4399 O O   . HOH H 4 .   ? -22.938 -28.721 -52.085 1.00 38.72  ? 576 HOH B O   1 
HETATM 4400 O O   . HOH H 4 .   ? -21.332 -27.902 -54.927 1.00 38.01  ? 577 HOH B O   1 
HETATM 4401 O O   . HOH H 4 .   ? -14.618 -21.449 -15.029 1.00 45.74  ? 578 HOH B O   1 
HETATM 4402 O O   . HOH H 4 .   ? -9.290  -48.528 -42.191 1.00 46.27  ? 579 HOH B O   1 
HETATM 4403 O O   . HOH H 4 .   ? -15.514 -7.889  -31.330 1.00 36.83  ? 580 HOH B O   1 
HETATM 4404 O O   . HOH H 4 .   ? -27.070 -39.152 -47.646 1.00 28.92  ? 581 HOH B O   1 
HETATM 4405 O O   . HOH H 4 .   ? -18.935 -18.913 -31.580 1.00 35.93  ? 582 HOH B O   1 
HETATM 4406 O O   . HOH H 4 .   ? -21.285 -40.238 -30.175 1.00 36.09  ? 583 HOH B O   1 
HETATM 4407 O O   . HOH H 4 .   ? -23.488 -23.999 -46.957 1.00 34.59  ? 584 HOH B O   1 
HETATM 4408 O O   . HOH H 4 .   ? -23.046 -25.135 -19.842 1.00 44.92  ? 585 HOH B O   1 
HETATM 4409 O O   . HOH H 4 .   ? -19.354 -4.389  -40.957 1.00 41.59  ? 586 HOH B O   1 
HETATM 4410 O O   . HOH H 4 .   ? -30.390 -49.092 -52.959 1.00 37.23  ? 587 HOH B O   1 
HETATM 4411 O O   . HOH H 4 .   ? 1.990   -15.584 -58.910 1.00 54.44  ? 588 HOH B O   1 
HETATM 4412 O O   . HOH H 4 .   ? -19.176 -8.740  -45.735 1.00 34.82  ? 589 HOH B O   1 
HETATM 4413 O O   . HOH H 4 .   ? -12.349 -8.078  -27.585 1.00 38.85  ? 590 HOH B O   1 
HETATM 4414 O O   . HOH H 4 .   ? -12.733 -16.098 -23.322 1.00 41.70  ? 591 HOH B O   1 
HETATM 4415 O O   . HOH H 4 .   ? -5.960  -34.762 -30.651 1.00 31.59  ? 592 HOH B O   1 
HETATM 4416 O O   . HOH H 4 .   ? -30.181 -33.688 -45.699 1.00 29.81  ? 593 HOH B O   1 
HETATM 4417 O O   . HOH H 4 .   ? -10.465 -17.203 -23.989 1.00 37.07  ? 594 HOH B O   1 
HETATM 4418 O O   . HOH H 4 .   ? -17.775 -17.630 -23.147 1.00 37.47  ? 595 HOH B O   1 
HETATM 4419 O O   . HOH H 4 .   ? -6.974  -22.327 -45.469 1.00 40.12  ? 596 HOH B O   1 
HETATM 4420 O O   . HOH H 4 .   ? -5.474  -15.941 -56.587 1.00 46.64  ? 597 HOH B O   1 
HETATM 4421 O O   . HOH H 4 .   ? -18.058 -6.334  -43.210 1.00 34.74  ? 598 HOH B O   1 
HETATM 4422 O O   . HOH H 4 .   ? -9.118  -39.587 -43.211 1.00 42.38  ? 599 HOH B O   1 
HETATM 4423 O O   . HOH H 4 .   ? -12.729 -31.566 -49.594 1.00 35.07  ? 600 HOH B O   1 
HETATM 4424 O O   . HOH H 4 .   ? -3.052  -21.220 -27.433 1.00 43.96  ? 601 HOH B O   1 
HETATM 4425 O O   . HOH H 4 .   ? -4.165  1.207   -32.084 1.00 48.50  ? 602 HOH B O   1 
HETATM 4426 O O   . HOH H 4 .   ? -1.329  -7.006  -59.408 1.00 45.88  ? 603 HOH B O   1 
HETATM 4427 O O   . HOH H 4 .   ? -8.723  -0.497  -54.687 1.00 46.58  ? 604 HOH B O   1 
HETATM 4428 O O   . HOH H 4 .   ? -15.152 -18.476 -34.514 1.00 32.95  ? 605 HOH B O   1 
HETATM 4429 O O   . HOH H 4 .   ? -18.848 -45.890 -42.396 1.00 35.87  ? 606 HOH B O   1 
HETATM 4430 O O   . HOH H 4 .   ? -4.625  -21.804 -46.476 1.00 36.45  ? 607 HOH B O   1 
HETATM 4431 O O   . HOH H 4 .   ? -3.889  -3.613  -26.324 1.00 37.65  ? 608 HOH B O   1 
HETATM 4432 O O   . HOH H 4 .   ? -13.895 -12.594 -29.887 1.00 43.85  ? 609 HOH B O   1 
HETATM 4433 O O   . HOH H 4 .   ? -13.208 -35.379 -47.154 1.00 37.61  ? 610 HOH B O   1 
HETATM 4434 O O   . HOH H 4 .   ? -20.887 -44.301 -36.268 1.00 39.69  ? 611 HOH B O   1 
HETATM 4435 O O   . HOH H 4 .   ? -6.804  -40.975 -35.643 1.00 39.38  ? 612 HOH B O   1 
HETATM 4436 O O   . HOH H 4 .   ? -19.082 -27.773 -17.060 1.00 45.39  ? 613 HOH B O   1 
HETATM 4437 O O   . HOH H 4 .   ? -3.945  -11.737 -60.053 1.00 55.80  ? 614 HOH B O   1 
HETATM 4438 O O   . HOH H 4 .   ? -19.025 -43.344 -34.272 1.00 41.84  ? 615 HOH B O   1 
HETATM 4439 O O   . HOH H 4 .   ? -14.206 -19.737 -32.440 1.00 31.62  ? 616 HOH B O   1 
HETATM 4440 O O   . HOH H 4 .   ? -6.409  -19.532 -45.370 1.00 34.98  ? 617 HOH B O   1 
HETATM 4441 O O   . HOH H 4 .   ? -5.822  -29.363 -32.010 1.00 35.46  ? 618 HOH B O   1 
HETATM 4442 O O   . HOH H 4 .   ? -7.980  -41.723 -40.274 1.00 40.84  ? 619 HOH B O   1 
HETATM 4443 O O   . HOH H 4 .   ? -25.141 -21.607 -45.494 1.00 40.53  ? 620 HOH B O   1 
HETATM 4444 O O   . HOH H 4 .   ? 9.838   -5.141  -44.563 1.00 48.37  ? 621 HOH B O   1 
HETATM 4445 O O   . HOH H 4 .   ? -15.358 0.162   -33.408 1.00 41.86  ? 622 HOH B O   1 
HETATM 4446 O O   . HOH H 4 .   ? -13.184 1.815   -34.170 1.00 46.54  ? 623 HOH B O   1 
HETATM 4447 O O   . HOH H 4 .   ? -17.449 -16.945 -30.612 1.00 39.81  ? 624 HOH B O   1 
HETATM 4448 O O   . HOH H 4 .   ? -15.433 -16.585 -23.065 1.00 46.63  ? 625 HOH B O   1 
HETATM 4449 O O   . HOH H 4 .   ? -19.885 -17.345 -21.880 1.00 47.42  ? 626 HOH B O   1 
HETATM 4450 O O   . HOH H 4 .   ? -11.957 -14.068 -21.576 1.00 44.66  ? 627 HOH B O   1 
HETATM 4451 O O   . HOH H 4 .   ? -8.903  -15.112 -23.664 1.00 48.85  ? 628 HOH B O   1 
HETATM 4452 O O   . HOH H 4 .   ? -24.124 -26.290 -22.197 1.00 42.43  ? 629 HOH B O   1 
HETATM 4453 O O   . HOH H 4 .   ? -24.615 -39.961 -48.290 1.00 39.40  ? 630 HOH B O   1 
HETATM 4454 O O   . HOH H 4 .   ? -11.232 -8.384  -25.026 1.00 43.30  ? 631 HOH B O   1 
HETATM 4455 O O   . HOH H 4 .   ? -31.751 -26.649 -38.076 1.00 42.41  ? 632 HOH B O   1 
HETATM 4456 O O   . HOH H 4 .   ? -28.254 -29.649 -31.740 1.00 39.71  ? 633 HOH B O   1 
HETATM 4457 O O   . HOH H 4 .   ? -4.674  -8.297  -24.835 1.00 45.19  ? 634 HOH B 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   . SER A 1   ? 0.6841 0.6476 0.7468 0.0401  0.0079  -0.0167 44  SER A N   
2    C CA  . SER A 1   ? 0.6773 0.6453 0.7467 0.0437  0.0116  -0.0157 44  SER A CA  
3    C C   . SER A 1   ? 0.6059 0.5700 0.6718 0.0473  0.0167  -0.0204 44  SER A C   
4    O O   . SER A 1   ? 0.6198 0.5800 0.6759 0.0465  0.0174  -0.0243 44  SER A O   
5    C CB  . SER A 1   ? 0.6613 0.6377 0.7318 0.0422  0.0119  -0.0131 44  SER A CB  
6    O OG  . SER A 1   ? 0.5817 0.5627 0.6589 0.0455  0.0162  -0.0123 44  SER A OG  
7    N N   . ARG A 2   ? 0.5527 0.5175 0.6262 0.0517  0.0202  -0.0199 45  ARG A N   
8    C CA  . ARG A 2   ? 0.5498 0.5108 0.6199 0.0559  0.0258  -0.0243 45  ARG A CA  
9    C C   . ARG A 2   ? 0.5333 0.5000 0.6002 0.0569  0.0306  -0.0244 45  ARG A C   
10   O O   . ARG A 2   ? 0.5142 0.4778 0.5763 0.0606  0.0360  -0.0279 45  ARG A O   
11   C CB  . ARG A 2   ? 0.5464 0.5061 0.6268 0.0607  0.0283  -0.0236 45  ARG A CB  
12   C CG  . ARG A 2   ? 0.5474 0.5162 0.6409 0.0620  0.0293  -0.0182 45  ARG A CG  
13   C CD  . ARG A 2   ? 0.5918 0.5596 0.6946 0.0677  0.0339  -0.0186 45  ARG A CD  
14   N NE  . ARG A 2   ? 0.6072 0.5829 0.7249 0.0687  0.0331  -0.0130 45  ARG A NE  
15   C CZ  . ARG A 2   ? 0.6478 0.6255 0.7766 0.0736  0.0373  -0.0120 45  ARG A CZ  
16   N NH1 . ARG A 2   ? 0.6573 0.6296 0.7836 0.0784  0.0432  -0.0163 45  ARG A NH1 
17   N NH2 . ARG A 2   ? 0.6231 0.6082 0.7661 0.0739  0.0354  -0.0066 45  ARG A NH2 
18   N N   . TRP A 3   ? 0.4911 0.4653 0.5599 0.0537  0.0290  -0.0207 46  TRP A N   
19   C CA  . TRP A 3   ? 0.4967 0.4762 0.5624 0.0540  0.0331  -0.0203 46  TRP A CA  
20   C C   . TRP A 3   ? 0.4985 0.4769 0.5525 0.0501  0.0307  -0.0219 46  TRP A C   
21   O O   . TRP A 3   ? 0.4901 0.4718 0.5399 0.0502  0.0340  -0.0217 46  TRP A O   
22   C CB  . TRP A 3   ? 0.4757 0.4649 0.5535 0.0535  0.0332  -0.0147 46  TRP A CB  
23   C CG  . TRP A 3   ? 0.4703 0.4617 0.5617 0.0558  0.0325  -0.0117 46  TRP A CG  
24   C CD1 . TRP A 3   ? 0.4299 0.4235 0.5286 0.0535  0.0266  -0.0081 46  TRP A CD1 
25   C CD2 . TRP A 3   ? 0.4189 0.4101 0.5181 0.0610  0.0378  -0.0120 46  TRP A CD2 
26   N NE1 . TRP A 3   ? 0.4427 0.4378 0.5537 0.0568  0.0273  -0.0059 46  TRP A NE1 
27   C CE2 . TRP A 3   ? 0.4316 0.4255 0.5438 0.0614  0.0343  -0.0082 46  TRP A CE2 
28   C CE3 . TRP A 3   ? 0.4175 0.4065 0.5136 0.0656  0.0452  -0.0150 46  TRP A CE3 
29   C CZ2 . TRP A 3   ? 0.4575 0.4522 0.5809 0.0662  0.0379  -0.0073 46  TRP A CZ2 
30   C CZ3 . TRP A 3   ? 0.4394 0.4291 0.5462 0.0706  0.0494  -0.0143 46  TRP A CZ3 
31   C CH2 . TRP A 3   ? 0.4636 0.4563 0.5845 0.0708  0.0456  -0.0103 46  TRP A CH2 
32   N N   . ARG A 4   ? 0.5086 0.4827 0.5581 0.0467  0.0253  -0.0230 47  ARG A N   
33   C CA  . ARG A 4   ? 0.5366 0.5109 0.5774 0.0427  0.0224  -0.0237 47  ARG A CA  
34   C C   . ARG A 4   ? 0.5550 0.5242 0.5839 0.0439  0.0250  -0.0284 47  ARG A C   
35   O O   . ARG A 4   ? 0.5186 0.4800 0.5426 0.0456  0.0250  -0.0326 47  ARG A O   
36   C CB  . ARG A 4   ? 0.5395 0.5107 0.5798 0.0391  0.0165  -0.0233 47  ARG A CB  
37   C CG  . ARG A 4   ? 0.5200 0.4939 0.5553 0.0348  0.0133  -0.0224 47  ARG A CG  
38   C CD  . ARG A 4   ? 0.5249 0.4971 0.5615 0.0316  0.0082  -0.0209 47  ARG A CD  
39   N NE  . ARG A 4   ? 0.4906 0.4553 0.5221 0.0308  0.0065  -0.0244 47  ARG A NE  
40   C CZ  . ARG A 4   ? 0.5174 0.4796 0.5498 0.0281  0.0027  -0.0233 47  ARG A CZ  
41   N NH1 . ARG A 4   ? 0.4741 0.4404 0.5108 0.0262  0.0005  -0.0192 47  ARG A NH1 
42   N NH2 . ARG A 4   ? 0.5499 0.5052 0.5788 0.0273  0.0010  -0.0265 47  ARG A NH2 
43   N N   . GLN A 5   ? 0.5087 0.4817 0.5325 0.0430  0.0267  -0.0277 48  GLN A N   
44   C CA  . GLN A 5   ? 0.5636 0.5320 0.5748 0.0440  0.0288  -0.0317 48  GLN A CA  
45   C C   . GLN A 5   ? 0.5250 0.4897 0.5284 0.0399  0.0231  -0.0337 48  GLN A C   
46   O O   . GLN A 5   ? 0.4721 0.4396 0.4799 0.0362  0.0187  -0.0312 48  GLN A O   
47   C CB  . GLN A 5   ? 0.5659 0.5401 0.5755 0.0453  0.0337  -0.0295 48  GLN A CB  
48   C CG  . GLN A 5   ? 0.5163 0.4977 0.5294 0.0412  0.0310  -0.0253 48  GLN A CG  
49   C CD  . GLN A 5   ? 0.5453 0.5340 0.5634 0.0427  0.0361  -0.0215 48  GLN A CD  
50   O OE1 . GLN A 5   ? 0.4812 0.4755 0.5116 0.0433  0.0372  -0.0179 48  GLN A OE1 
51   N NE2 . GLN A 5   ? 0.4377 0.4263 0.4469 0.0432  0.0390  -0.0219 48  GLN A NE2 
52   N N   . GLN A 6   ? 0.5530 0.5112 0.5447 0.0409  0.0233  -0.0382 49  GLN A N   
53   C CA  . GLN A 6   ? 0.5200 0.4748 0.5045 0.0373  0.0179  -0.0402 49  GLN A CA  
54   C C   . GLN A 6   ? 0.4692 0.4294 0.4497 0.0352  0.0181  -0.0379 49  GLN A C   
55   O O   . GLN A 6   ? 0.4560 0.4187 0.4329 0.0376  0.0228  -0.0371 49  GLN A O   
56   C CB  . GLN A 6   ? 0.5977 0.5426 0.5712 0.0391  0.0171  -0.0463 49  GLN A CB  
57   C CG  . GLN A 6   ? 0.6237 0.5646 0.5900 0.0355  0.0111  -0.0486 49  GLN A CG  
58   C CD  . GLN A 6   ? 0.6566 0.5969 0.6308 0.0316  0.0056  -0.0475 49  GLN A CD  
59   O OE1 . GLN A 6   ? 0.7542 0.6946 0.7371 0.0321  0.0059  -0.0461 49  GLN A OE1 
60   N NE2 . GLN A 6   ? 0.6398 0.5793 0.6111 0.0279  0.0006  -0.0479 49  GLN A NE2 
61   N N   . TRP A 7   ? 0.4422 0.4043 0.4240 0.0309  0.0131  -0.0364 50  TRP A N   
62   C CA  . TRP A 7   ? 0.4387 0.4050 0.4167 0.0287  0.0121  -0.0346 50  TRP A CA  
63   C C   . TRP A 7   ? 0.4501 0.4105 0.4185 0.0270  0.0078  -0.0382 50  TRP A C   
64   O O   . TRP A 7   ? 0.4215 0.3757 0.3887 0.0265  0.0046  -0.0414 50  TRP A O   
65   C CB  . TRP A 7   ? 0.3841 0.3572 0.3710 0.0254  0.0097  -0.0302 50  TRP A CB  
66   C CG  . TRP A 7   ? 0.3867 0.3651 0.3837 0.0266  0.0124  -0.0267 50  TRP A CG  
67   C CD1 . TRP A 7   ? 0.3659 0.3452 0.3712 0.0259  0.0105  -0.0251 50  TRP A CD1 
68   C CD2 . TRP A 7   ? 0.3813 0.3649 0.3816 0.0287  0.0171  -0.0241 50  TRP A CD2 
69   N NE1 . TRP A 7   ? 0.3728 0.3572 0.3861 0.0274  0.0131  -0.0220 50  TRP A NE1 
70   C CE2 . TRP A 7   ? 0.3667 0.3542 0.3781 0.0291  0.0172  -0.0213 50  TRP A CE2 
71   C CE3 . TRP A 7   ? 0.4016 0.3869 0.3971 0.0304  0.0212  -0.0236 50  TRP A CE3 
72   C CZ2 . TRP A 7   ? 0.3688 0.3620 0.3875 0.0308  0.0209  -0.0180 50  TRP A CZ2 
73   C CZ3 . TRP A 7   ? 0.3898 0.3810 0.3927 0.0321  0.0255  -0.0201 50  TRP A CZ3 
74   C CH2 . TRP A 7   ? 0.3993 0.3945 0.4142 0.0322  0.0252  -0.0174 50  TRP A CH2 
75   N N   . SER A 8   ? 0.4110 0.3735 0.3733 0.0259  0.0075  -0.0374 51  SER A N   
76   C CA  . SER A 8   ? 0.4824 0.4398 0.4356 0.0244  0.0030  -0.0404 51  SER A CA  
77   C C   . SER A 8   ? 0.4710 0.4308 0.4296 0.0199  -0.0026 -0.0388 51  SER A C   
78   O O   . SER A 8   ? 0.4974 0.4528 0.4512 0.0182  -0.0073 -0.0414 51  SER A O   
79   C CB  . SER A 8   ? 0.4988 0.4567 0.4419 0.0257  0.0052  -0.0401 51  SER A CB  
80   O OG  . SER A 8   ? 0.5495 0.5052 0.4869 0.0302  0.0111  -0.0414 51  SER A OG  
81   N N   . GLY A 9   ? 0.4171 0.3835 0.3854 0.0181  -0.0022 -0.0348 52  GLY A N   
82   C CA  . GLY A 9   ? 0.3906 0.3595 0.3637 0.0144  -0.0065 -0.0330 52  GLY A CA  
83   C C   . GLY A 9   ? 0.4042 0.3710 0.3841 0.0130  -0.0088 -0.0334 52  GLY A C   
84   O O   . GLY A 9   ? 0.3989 0.3634 0.3815 0.0149  -0.0070 -0.0341 52  GLY A O   
85   N N   . PRO A 10  ? 0.4308 0.3983 0.4141 0.0099  -0.0127 -0.0325 53  PRO A N   
86   C CA  . PRO A 10  ? 0.4222 0.3880 0.4125 0.0084  -0.0146 -0.0320 53  PRO A CA  
87   C C   . PRO A 10  ? 0.3695 0.3392 0.3665 0.0092  -0.0118 -0.0288 53  PRO A C   
88   O O   . PRO A 10  ? 0.3472 0.3222 0.3453 0.0098  -0.0097 -0.0263 53  PRO A O   
89   C CB  . PRO A 10  ? 0.4483 0.4161 0.4415 0.0051  -0.0182 -0.0307 53  PRO A CB  
90   C CG  . PRO A 10  ? 0.4721 0.4403 0.4584 0.0049  -0.0195 -0.0319 53  PRO A CG  
91   C CD  . PRO A 10  ? 0.4104 0.3805 0.3920 0.0076  -0.0154 -0.0315 53  PRO A CD  
92   N N   . GLY A 11  ? 0.3715 0.3381 0.3731 0.0092  -0.0123 -0.0287 54  GLY A N   
93   C CA  . GLY A 11  ? 0.3971 0.3667 0.4047 0.0100  -0.0105 -0.0255 54  GLY A CA  
94   C C   . GLY A 11  ? 0.3558 0.3301 0.3674 0.0077  -0.0115 -0.0219 54  GLY A C   
95   O O   . GLY A 11  ? 0.3221 0.2974 0.3331 0.0055  -0.0135 -0.0217 54  GLY A O   
96   N N   . THR A 12  ? 0.3478 0.3246 0.3634 0.0086  -0.0103 -0.0190 55  THR A N   
97   C CA  . THR A 12  ? 0.3098 0.2904 0.3280 0.0070  -0.0110 -0.0157 55  THR A CA  
98   C C   . THR A 12  ? 0.3458 0.3243 0.3661 0.0048  -0.0127 -0.0151 55  THR A C   
99   O O   . THR A 12  ? 0.3288 0.3027 0.3511 0.0046  -0.0134 -0.0159 55  THR A O   
100  C CB  . THR A 12  ? 0.3157 0.2977 0.3372 0.0085  -0.0101 -0.0129 55  THR A CB  
101  O OG1 . THR A 12  ? 0.2995 0.2844 0.3208 0.0104  -0.0087 -0.0129 55  THR A OG1 
102  C CG2 . THR A 12  ? 0.3083 0.2930 0.3307 0.0073  -0.0109 -0.0097 55  THR A CG2 
103  N N   . THR A 13  ? 0.3053 0.2870 0.3258 0.0030  -0.0133 -0.0135 56  THR A N   
104  C CA  . THR A 13  ? 0.3371 0.3179 0.3611 0.0009  -0.0144 -0.0122 56  THR A CA  
105  C C   . THR A 13  ? 0.3440 0.3227 0.3717 0.0012  -0.0137 -0.0096 56  THR A C   
106  O O   . THR A 13  ? 0.2968 0.2770 0.3241 0.0027  -0.0125 -0.0073 56  THR A O   
107  C CB  . THR A 13  ? 0.3003 0.2856 0.3244 -0.0002 -0.0143 -0.0104 56  THR A CB  
108  O OG1 . THR A 13  ? 0.3363 0.3237 0.3569 -0.0002 -0.0150 -0.0124 56  THR A OG1 
109  C CG2 . THR A 13  ? 0.3596 0.3444 0.3883 -0.0025 -0.0152 -0.0092 56  THR A CG2 
110  N N   . LYS A 14  ? 0.3361 0.3110 0.3675 -0.0002 -0.0148 -0.0096 57  LYS A N   
111  C CA  . LYS A 14  ? 0.3587 0.3312 0.3943 -0.0002 -0.0140 -0.0066 57  LYS A CA  
112  C C   . LYS A 14  ? 0.3486 0.3249 0.3845 -0.0003 -0.0123 -0.0023 57  LYS A C   
113  O O   . LYS A 14  ? 0.3435 0.3231 0.3794 -0.0014 -0.0119 -0.0015 57  LYS A O   
114  C CB  . LYS A 14  ? 0.4232 0.3914 0.4641 -0.0022 -0.0158 -0.0071 57  LYS A CB  
115  C CG  . LYS A 14  ? 0.5859 0.5479 0.6271 -0.0012 -0.0170 -0.0101 57  LYS A CG  
116  C CD  . LYS A 14  ? 0.6289 0.5902 0.6640 0.0004  -0.0176 -0.0149 57  LYS A CD  
117  C CE  . LYS A 14  ? 0.6294 0.5855 0.6637 0.0028  -0.0172 -0.0172 57  LYS A CE  
118  N NZ  . LYS A 14  ? 0.7109 0.6599 0.7475 0.0019  -0.0198 -0.0201 57  LYS A NZ  
119  N N   . ARG A 15  ? 0.3354 0.3107 0.3712 0.0013  -0.0112 0.0006  58  ARG A N   
120  C CA  . ARG A 15  ? 0.3683 0.3461 0.4026 0.0017  -0.0095 0.0047  58  ARG A CA  
121  C C   . ARG A 15  ? 0.3308 0.3130 0.3601 0.0026  -0.0093 0.0040  58  ARG A C   
122  O O   . ARG A 15  ? 0.3472 0.3317 0.3746 0.0025  -0.0081 0.0062  58  ARG A O   
123  C CB  . ARG A 15  ? 0.3682 0.3462 0.4067 -0.0003 -0.0083 0.0076  58  ARG A CB  
124  C CG  . ARG A 15  ? 0.4652 0.4386 0.5100 -0.0015 -0.0087 0.0091  58  ARG A CG  
125  C CD  . ARG A 15  ? 0.4514 0.4236 0.4965 -0.0006 -0.0067 0.0143  58  ARG A CD  
126  N NE  . ARG A 15  ? 0.4616 0.4370 0.5060 -0.0010 -0.0040 0.0181  58  ARG A NE  
127  C CZ  . ARG A 15  ? 0.4640 0.4390 0.5062 0.0002  -0.0016 0.0230  58  ARG A CZ  
128  N NH1 . ARG A 15  ? 0.4254 0.3969 0.4666 0.0016  -0.0021 0.0251  58  ARG A NH1 
129  N NH2 . ARG A 15  ? 0.4218 0.3998 0.4627 0.0002  0.0014  0.0260  58  ARG A NH2 
130  N N   . PHE A 16  ? 0.3186 0.3017 0.3458 0.0036  -0.0104 0.0009  59  PHE A N   
131  C CA  . PHE A 16  ? 0.3383 0.3252 0.3617 0.0042  -0.0106 0.0002  59  PHE A CA  
132  C C   . PHE A 16  ? 0.3442 0.3320 0.3644 0.0056  -0.0103 0.0030  59  PHE A C   
133  O O   . PHE A 16  ? 0.3464 0.3365 0.3638 0.0055  -0.0099 0.0036  59  PHE A O   
134  C CB  . PHE A 16  ? 0.3030 0.2905 0.3256 0.0051  -0.0113 -0.0028 59  PHE A CB  
135  C CG  . PHE A 16  ? 0.3187 0.3099 0.3387 0.0056  -0.0118 -0.0033 59  PHE A CG  
136  C CD1 . PHE A 16  ? 0.2631 0.2565 0.2818 0.0044  -0.0119 -0.0045 59  PHE A CD1 
137  C CD2 . PHE A 16  ? 0.2875 0.2798 0.3070 0.0073  -0.0124 -0.0025 59  PHE A CD2 
138  C CE1 . PHE A 16  ? 0.3172 0.3136 0.3341 0.0048  -0.0124 -0.0048 59  PHE A CE1 
139  C CE2 . PHE A 16  ? 0.3273 0.3227 0.3454 0.0075  -0.0132 -0.0030 59  PHE A CE2 
140  C CZ  . PHE A 16  ? 0.3135 0.3108 0.3301 0.0063  -0.0131 -0.0041 59  PHE A CZ  
141  N N   . PRO A 17  ? 0.3562 0.3421 0.3764 0.0071  -0.0108 0.0048  60  PRO A N   
142  C CA  . PRO A 17  ? 0.3551 0.3415 0.3711 0.0086  -0.0113 0.0075  60  PRO A CA  
143  C C   . PRO A 17  ? 0.3224 0.3085 0.3358 0.0081  -0.0093 0.0102  60  PRO A C   
144  O O   . PRO A 17  ? 0.3315 0.3191 0.3400 0.0088  -0.0092 0.0106  60  PRO A O   
145  C CB  . PRO A 17  ? 0.3586 0.3423 0.3761 0.0101  -0.0123 0.0093  60  PRO A CB  
146  C CG  . PRO A 17  ? 0.3875 0.3704 0.4098 0.0099  -0.0124 0.0066  60  PRO A CG  
147  C CD  . PRO A 17  ? 0.4005 0.3835 0.4242 0.0079  -0.0112 0.0045  60  PRO A CD  
148  N N   . GLU A 18  ? 0.3082 0.2923 0.3252 0.0071  -0.0077 0.0122  61  GLU A N   
149  C CA  . GLU A 18  ? 0.3344 0.3186 0.3502 0.0067  -0.0050 0.0154  61  GLU A CA  
150  C C   . GLU A 18  ? 0.3365 0.3239 0.3524 0.0057  -0.0039 0.0139  61  GLU A C   
151  O O   . GLU A 18  ? 0.3321 0.3206 0.3446 0.0064  -0.0017 0.0159  61  GLU A O   
152  C CB  . GLU A 18  ? 0.3895 0.3710 0.4111 0.0054  -0.0037 0.0181  61  GLU A CB  
153  C CG  . GLU A 18  ? 0.4287 0.4066 0.4504 0.0067  -0.0045 0.0206  61  GLU A CG  
154  C CD  . GLU A 18  ? 0.4935 0.4698 0.5185 0.0069  -0.0070 0.0174  61  GLU A CD  
155  O OE1 . GLU A 18  ? 0.4420 0.4195 0.4693 0.0058  -0.0078 0.0134  61  GLU A OE1 
156  O OE2 . GLU A 18  ? 0.6286 0.6023 0.6537 0.0084  -0.0081 0.0190  61  GLU A OE2 
157  N N   . THR A 19  ? 0.3165 0.3054 0.3359 0.0042  -0.0052 0.0103  62  THR A N   
158  C CA  . THR A 19  ? 0.2886 0.2805 0.3087 0.0032  -0.0045 0.0089  62  THR A CA  
159  C C   . THR A 19  ? 0.3209 0.3148 0.3350 0.0048  -0.0050 0.0078  62  THR A C   
160  O O   . THR A 19  ? 0.3137 0.3094 0.3263 0.0051  -0.0033 0.0085  62  THR A O   
161  C CB  . THR A 19  ? 0.3410 0.3333 0.3654 0.0014  -0.0064 0.0056  62  THR A CB  
162  O OG1 . THR A 19  ? 0.3740 0.3636 0.4038 0.0000  -0.0066 0.0062  62  THR A OG1 
163  C CG2 . THR A 19  ? 0.3544 0.3498 0.3802 0.0004  -0.0062 0.0045  62  THR A CG2 
164  N N   . VAL A 20  ? 0.3072 0.3008 0.3186 0.0058  -0.0073 0.0061  63  VAL A N   
165  C CA  . VAL A 20  ? 0.3090 0.3040 0.3155 0.0071  -0.0084 0.0050  63  VAL A CA  
166  C C   . VAL A 20  ? 0.3526 0.3462 0.3530 0.0090  -0.0074 0.0075  63  VAL A C   
167  O O   . VAL A 20  ? 0.2919 0.2863 0.2883 0.0099  -0.0068 0.0070  63  VAL A O   
168  C CB  . VAL A 20  ? 0.3096 0.3046 0.3160 0.0077  -0.0112 0.0032  63  VAL A CB  
169  C CG1 . VAL A 20  ? 0.3082 0.3039 0.3101 0.0090  -0.0131 0.0025  63  VAL A CG1 
170  C CG2 . VAL A 20  ? 0.2988 0.2954 0.3094 0.0062  -0.0117 0.0006  63  VAL A CG2 
171  N N   . LEU A 21  ? 0.3300 0.3210 0.3291 0.0098  -0.0070 0.0102  64  LEU A N   
172  C CA  . LEU A 21  ? 0.3539 0.3429 0.3457 0.0119  -0.0059 0.0129  64  LEU A CA  
173  C C   . LEU A 21  ? 0.3320 0.3220 0.3231 0.0119  -0.0018 0.0146  64  LEU A C   
174  O O   . LEU A 21  ? 0.2976 0.2874 0.2821 0.0137  -0.0007 0.0146  64  LEU A O   
175  C CB  . LEU A 21  ? 0.3675 0.3535 0.3588 0.0126  -0.0062 0.0162  64  LEU A CB  
176  C CG  . LEU A 21  ? 0.3811 0.3659 0.3719 0.0135  -0.0103 0.0153  64  LEU A CG  
177  C CD1 . LEU A 21  ? 0.4363 0.4183 0.4292 0.0139  -0.0103 0.0185  64  LEU A CD1 
178  C CD2 . LEU A 21  ? 0.4010 0.3849 0.3836 0.0156  -0.0129 0.0149  64  LEU A CD2 
179  N N   . ALA A 22  ? 0.2837 0.2747 0.2821 0.0099  0.0006  0.0160  65  ALA A N   
180  C CA  . ALA A 22  ? 0.3180 0.3106 0.3181 0.0098  0.0048  0.0181  65  ALA A CA  
181  C C   . ALA A 22  ? 0.3248 0.3202 0.3245 0.0099  0.0049  0.0152  65  ALA A C   
182  O O   . ALA A 22  ? 0.3163 0.3125 0.3130 0.0114  0.0082  0.0165  65  ALA A O   
183  C CB  . ALA A 22  ? 0.3279 0.3212 0.3380 0.0072  0.0062  0.0198  65  ALA A CB  
184  N N   . ARG A 23  ? 0.3010 0.2979 0.3038 0.0086  0.0017  0.0115  66  ARG A N   
185  C CA  . ARG A 23  ? 0.3262 0.3254 0.3288 0.0087  0.0014  0.0090  66  ARG A CA  
186  C C   . ARG A 23  ? 0.3258 0.3236 0.3193 0.0113  0.0008  0.0080  66  ARG A C   
187  O O   . ARG A 23  ? 0.3366 0.3353 0.3280 0.0126  0.0027  0.0075  66  ARG A O   
188  C CB  . ARG A 23  ? 0.3002 0.3008 0.3070 0.0069  -0.0020 0.0057  66  ARG A CB  
189  C CG  . ARG A 23  ? 0.3275 0.3294 0.3425 0.0044  -0.0018 0.0058  66  ARG A CG  
190  C CD  . ARG A 23  ? 0.3144 0.3170 0.3314 0.0030  -0.0050 0.0026  66  ARG A CD  
191  N NE  . ARG A 23  ? 0.2792 0.2822 0.3027 0.0008  -0.0055 0.0023  66  ARG A NE  
192  C CZ  . ARG A 23  ? 0.3352 0.3387 0.3603 -0.0004 -0.0080 -0.0003 66  ARG A CZ  
193  N NH1 . ARG A 23  ? 0.2758 0.2801 0.2974 0.0002  -0.0095 -0.0023 66  ARG A NH1 
194  N NH2 . ARG A 23  ? 0.3763 0.3795 0.4066 -0.0024 -0.0090 -0.0006 66  ARG A NH2 
195  N N   . CYS A 24  ? 0.3231 0.3185 0.3116 0.0123  -0.0021 0.0075  67  CYS A N   
196  C CA  . CYS A 24  ? 0.3481 0.3414 0.3279 0.0147  -0.0038 0.0062  67  CYS A CA  
197  C C   . CYS A 24  ? 0.3449 0.3362 0.3174 0.0172  0.0000  0.0086  67  CYS A C   
198  O O   . CYS A 24  ? 0.3448 0.3353 0.3116 0.0192  0.0005  0.0070  67  CYS A O   
199  C CB  . CYS A 24  ? 0.3649 0.3560 0.3419 0.0152  -0.0080 0.0059  67  CYS A CB  
200  S SG  . CYS A 24  ? 0.3502 0.3380 0.3168 0.0179  -0.0115 0.0041  67  CYS A SG  
201  N N   . VAL A 25  ? 0.3231 0.3134 0.2955 0.0174  0.0028  0.0124  68  VAL A N   
202  C CA  . VAL A 25  ? 0.3362 0.3248 0.3016 0.0199  0.0073  0.0154  68  VAL A CA  
203  C C   . VAL A 25  ? 0.3666 0.3582 0.3360 0.0200  0.0118  0.0154  68  VAL A C   
204  O O   . VAL A 25  ? 0.3702 0.3606 0.3324 0.0228  0.0147  0.0155  68  VAL A O   
205  C CB  . VAL A 25  ? 0.3831 0.3703 0.3495 0.0196  0.0095  0.0202  68  VAL A CB  
206  C CG1 . VAL A 25  ? 0.3776 0.3641 0.3392 0.0218  0.0157  0.0241  68  VAL A CG1 
207  C CG2 . VAL A 25  ? 0.3719 0.3555 0.3323 0.0206  0.0052  0.0205  68  VAL A CG2 
208  N N   . LYS A 26  ? 0.3734 0.3687 0.3544 0.0171  0.0124  0.0155  69  LYS A N   
209  C CA  . LYS A 26  ? 0.3393 0.3379 0.3259 0.0170  0.0163  0.0158  69  LYS A CA  
210  C C   . LYS A 26  ? 0.3201 0.3191 0.3033 0.0184  0.0148  0.0119  69  LYS A C   
211  O O   . LYS A 26  ? 0.3105 0.3102 0.2919 0.0205  0.0187  0.0122  69  LYS A O   
212  C CB  . LYS A 26  ? 0.3519 0.3540 0.3515 0.0134  0.0158  0.0163  69  LYS A CB  
213  C CG  . LYS A 26  ? 0.4228 0.4287 0.4304 0.0130  0.0192  0.0171  69  LYS A CG  
214  C CD  . LYS A 26  ? 0.5441 0.5506 0.5519 0.0147  0.0258  0.0218  69  LYS A CD  
215  C CE  . LYS A 26  ? 0.6723 0.6832 0.6888 0.0147  0.0294  0.0226  69  LYS A CE  
216  N NZ  . LYS A 26  ? 0.8148 0.8272 0.8348 0.0158  0.0363  0.0280  69  LYS A NZ  
217  N N   . TYR A 27  ? 0.3226 0.3210 0.3053 0.0173  0.0095  0.0083  70  TYR A N   
218  C CA  . TYR A 27  ? 0.3388 0.3373 0.3196 0.0183  0.0076  0.0047  70  TYR A CA  
219  C C   . TYR A 27  ? 0.3802 0.3749 0.3492 0.0220  0.0086  0.0038  70  TYR A C   
220  O O   . TYR A 27  ? 0.3588 0.3537 0.3263 0.0239  0.0107  0.0024  70  TYR A O   
221  C CB  . TYR A 27  ? 0.3310 0.3296 0.3138 0.0164  0.0019  0.0017  70  TYR A CB  
222  C CG  . TYR A 27  ? 0.3500 0.3491 0.3332 0.0167  -0.0002 -0.0016 70  TYR A CG  
223  C CD1 . TYR A 27  ? 0.3709 0.3666 0.3460 0.0190  -0.0024 -0.0039 70  TYR A CD1 
224  C CD2 . TYR A 27  ? 0.3558 0.3583 0.3474 0.0148  -0.0003 -0.0023 70  TYR A CD2 
225  C CE1 . TYR A 27  ? 0.3673 0.3630 0.3435 0.0192  -0.0044 -0.0068 70  TYR A CE1 
226  C CE2 . TYR A 27  ? 0.3686 0.3714 0.3609 0.0151  -0.0022 -0.0048 70  TYR A CE2 
227  C CZ  . TYR A 27  ? 0.3711 0.3705 0.3561 0.0173  -0.0041 -0.0070 70  TYR A CZ  
228  O OH  . TYR A 27  ? 0.3632 0.3624 0.3494 0.0175  -0.0062 -0.0095 70  TYR A OH  
229  N N   . THR A 28  ? 0.3662 0.3571 0.3266 0.0234  0.0070  0.0045  71  THR A N   
230  C CA  . THR A 28  ? 0.3877 0.3739 0.3352 0.0272  0.0072  0.0035  71  THR A CA  
231  C C   . THR A 28  ? 0.4155 0.4016 0.3592 0.0299  0.0143  0.0063  71  THR A C   
232  O O   . THR A 28  ? 0.4444 0.4274 0.3786 0.0334  0.0160  0.0048  71  THR A O   
233  C CB  . THR A 28  ? 0.4079 0.3902 0.3475 0.0279  0.0032  0.0040  71  THR A CB  
234  O OG1 . THR A 28  ? 0.4206 0.4035 0.3623 0.0271  0.0058  0.0084  71  THR A OG1 
235  C CG2 . THR A 28  ? 0.3867 0.3694 0.3308 0.0256  -0.0035 0.0012  71  THR A CG2 
236  N N   . GLU A 29  ? 0.3973 0.3865 0.3483 0.0284  0.0187  0.0106  72  GLU A N   
237  C CA  . GLU A 29  ? 0.4576 0.4479 0.4080 0.0306  0.0262  0.0139  72  GLU A CA  
238  C C   . GLU A 29  ? 0.4478 0.4412 0.4040 0.0312  0.0287  0.0119  72  GLU A C   
239  O O   . GLU A 29  ? 0.4806 0.4729 0.4309 0.0348  0.0337  0.0122  72  GLU A O   
240  C CB  . GLU A 29  ? 0.5020 0.4953 0.4617 0.0282  0.0296  0.0191  72  GLU A CB  
241  C CG  . GLU A 29  ? 0.5856 0.5810 0.5476 0.0300  0.0379  0.0235  72  GLU A CG  
242  C CD  . GLU A 29  ? 0.7230 0.7215 0.6966 0.0269  0.0405  0.0286  72  GLU A CD  
243  O OE1 . GLU A 29  ? 0.7050 0.7022 0.6803 0.0246  0.0364  0.0291  72  GLU A OE1 
244  O OE2 . GLU A 29  ? 0.7930 0.7952 0.7748 0.0270  0.0464  0.0320  72  GLU A OE2 
245  N N   . ILE A 30  ? 0.4154 0.4125 0.3827 0.0279  0.0254  0.0099  73  ILE A N   
246  C CA  . ILE A 30  ? 0.4622 0.4624 0.4363 0.0283  0.0272  0.0083  73  ILE A CA  
247  C C   . ILE A 30  ? 0.4694 0.4661 0.4352 0.0309  0.0245  0.0036  73  ILE A C   
248  O O   . ILE A 30  ? 0.4634 0.4608 0.4298 0.0332  0.0277  0.0025  73  ILE A O   
249  C CB  . ILE A 30  ? 0.4558 0.4606 0.4439 0.0240  0.0241  0.0080  73  ILE A CB  
250  C CG1 . ILE A 30  ? 0.5026 0.5105 0.4999 0.0215  0.0268  0.0125  73  ILE A CG1 
251  C CG2 . ILE A 30  ? 0.4990 0.5067 0.4939 0.0243  0.0247  0.0061  73  ILE A CG2 
252  C CD1 . ILE A 30  ? 0.6201 0.6305 0.6216 0.0233  0.0342  0.0164  73  ILE A CD1 
253  N N   . HIS A 31  ? 0.4630 0.4560 0.4219 0.0305  0.0185  0.0007  74  HIS A N   
254  C CA  . HIS A 31  ? 0.4608 0.4500 0.4131 0.0323  0.0146  -0.0039 74  HIS A CA  
255  C C   . HIS A 31  ? 0.4309 0.4137 0.3678 0.0357  0.0135  -0.0049 74  HIS A C   
256  O O   . HIS A 31  ? 0.4234 0.4038 0.3564 0.0346  0.0082  -0.0057 74  HIS A O   
257  C CB  . HIS A 31  ? 0.4453 0.4357 0.4038 0.0289  0.0079  -0.0063 74  HIS A CB  
258  C CG  . HIS A 31  ? 0.4620 0.4577 0.4336 0.0260  0.0082  -0.0058 74  HIS A CG  
259  N ND1 . HIS A 31  ? 0.5335 0.5302 0.5091 0.0265  0.0076  -0.0082 74  HIS A ND1 
260  C CD2 . HIS A 31  ? 0.4585 0.4585 0.4398 0.0228  0.0087  -0.0034 74  HIS A CD2 
261  C CE1 . HIS A 31  ? 0.4937 0.4951 0.4805 0.0236  0.0076  -0.0069 74  HIS A CE1 
262  N NE2 . HIS A 31  ? 0.4791 0.4824 0.4692 0.0214  0.0081  -0.0042 74  HIS A NE2 
263  N N   . PRO A 32  ? 0.4682 0.4480 0.3958 0.0400  0.0183  -0.0051 75  PRO A N   
264  C CA  . PRO A 32  ? 0.4801 0.4530 0.3912 0.0434  0.0169  -0.0061 75  PRO A CA  
265  C C   . PRO A 32  ? 0.4767 0.4447 0.3821 0.0434  0.0086  -0.0110 75  PRO A C   
266  O O   . PRO A 32  ? 0.4439 0.4070 0.3387 0.0446  0.0047  -0.0114 75  PRO A O   
267  C CB  . PRO A 32  ? 0.4983 0.4689 0.4014 0.0484  0.0240  -0.0062 75  PRO A CB  
268  C CG  . PRO A 32  ? 0.4836 0.4613 0.4005 0.0470  0.0305  -0.0027 75  PRO A CG  
269  C CD  . PRO A 32  ? 0.4461 0.4286 0.3777 0.0421  0.0255  -0.0038 75  PRO A CD  
270  N N   . GLU A 33  ? 0.4390 0.4084 0.3519 0.0419  0.0053  -0.0143 76  GLU A N   
271  C CA  . GLU A 33  ? 0.4261 0.3911 0.3353 0.0416  -0.0026 -0.0187 76  GLU A CA  
272  C C   . GLU A 33  ? 0.4345 0.4008 0.3482 0.0380  -0.0086 -0.0177 76  GLU A C   
273  O O   . GLU A 33  ? 0.4499 0.4126 0.3609 0.0376  -0.0155 -0.0207 76  GLU A O   
274  C CB  . GLU A 33  ? 0.4629 0.4291 0.3800 0.0409  -0.0040 -0.0219 76  GLU A CB  
275  C CG  . GLU A 33  ? 0.4540 0.4269 0.3868 0.0362  -0.0053 -0.0204 76  GLU A CG  
276  C CD  . GLU A 33  ? 0.4627 0.4418 0.4043 0.0352  0.0012  -0.0167 76  GLU A CD  
277  O OE1 . GLU A 33  ? 0.4286 0.4075 0.3653 0.0377  0.0071  -0.0145 76  GLU A OE1 
278  O OE2 . GLU A 33  ? 0.4771 0.4611 0.4305 0.0319  0.0003  -0.0158 76  GLU A OE2 
279  N N   . MET A 34  ? 0.4225 0.3936 0.3435 0.0353  -0.0063 -0.0137 77  MET A N   
280  C CA  . MET A 34  ? 0.4232 0.3957 0.3488 0.0323  -0.0112 -0.0126 77  MET A CA  
281  C C   . MET A 34  ? 0.4250 0.3955 0.3435 0.0333  -0.0105 -0.0094 77  MET A C   
282  O O   . MET A 34  ? 0.3827 0.3550 0.3063 0.0309  -0.0132 -0.0077 77  MET A O   
283  C CB  . MET A 34  ? 0.4208 0.3998 0.3608 0.0284  -0.0102 -0.0109 77  MET A CB  
284  C CG  . MET A 34  ? 0.4367 0.4177 0.3843 0.0270  -0.0119 -0.0136 77  MET A CG  
285  S SD  . MET A 34  ? 0.4445 0.4225 0.3919 0.0260  -0.0202 -0.0171 77  MET A SD  
286  C CE  . MET A 34  ? 0.4027 0.3843 0.3576 0.0226  -0.0227 -0.0145 77  MET A CE  
287  N N   . ARG A 35  ? 0.4297 0.3964 0.3365 0.0370  -0.0067 -0.0085 78  ARG A N   
288  C CA  . ARG A 35  ? 0.4663 0.4311 0.3661 0.0381  -0.0053 -0.0047 78  ARG A CA  
289  C C   . ARG A 35  ? 0.4732 0.4329 0.3647 0.0388  -0.0126 -0.0059 78  ARG A C   
290  O O   . ARG A 35  ? 0.5171 0.4748 0.4027 0.0397  -0.0124 -0.0026 78  ARG A O   
291  C CB  . ARG A 35  ? 0.4642 0.4266 0.3538 0.0420  0.0019  -0.0027 78  ARG A CB  
292  C CG  . ARG A 35  ? 0.4844 0.4527 0.3846 0.0409  0.0095  0.0001  78  ARG A CG  
293  C CD  . ARG A 35  ? 0.5150 0.4819 0.4070 0.0447  0.0176  0.0031  78  ARG A CD  
294  N NE  . ARG A 35  ? 0.5424 0.5157 0.4471 0.0431  0.0243  0.0063  78  ARG A NE  
295  C CZ  . ARG A 35  ? 0.6155 0.5896 0.5181 0.0458  0.0325  0.0094  78  ARG A CZ  
296  N NH1 . ARG A 35  ? 0.6552 0.6239 0.5420 0.0506  0.0358  0.0099  78  ARG A NH1 
297  N NH2 . ARG A 35  ? 0.5977 0.5782 0.5145 0.0438  0.0375  0.0123  78  ARG A NH2 
298  N N   . HIS A 36  ? 0.4843 0.4418 0.3757 0.0385  -0.0193 -0.0102 79  HIS A N   
299  C CA  . HIS A 36  ? 0.4897 0.4437 0.3775 0.0382  -0.0273 -0.0111 79  HIS A CA  
300  C C   . HIS A 36  ? 0.4656 0.4245 0.3659 0.0345  -0.0294 -0.0085 79  HIS A C   
301  O O   . HIS A 36  ? 0.4388 0.3956 0.3374 0.0344  -0.0351 -0.0080 79  HIS A O   
302  C CB  . HIS A 36  ? 0.4571 0.4079 0.3441 0.0383  -0.0339 -0.0163 79  HIS A CB  
303  C CG  . HIS A 36  ? 0.4531 0.4092 0.3548 0.0350  -0.0342 -0.0177 79  HIS A CG  
304  N ND1 . HIS A 36  ? 0.4893 0.4471 0.3940 0.0353  -0.0298 -0.0192 79  HIS A ND1 
305  C CD2 . HIS A 36  ? 0.4543 0.4144 0.3683 0.0314  -0.0382 -0.0175 79  HIS A CD2 
306  C CE1 . HIS A 36  ? 0.4638 0.4261 0.3814 0.0320  -0.0315 -0.0199 79  HIS A CE1 
307  N NE2 . HIS A 36  ? 0.4377 0.4015 0.3609 0.0296  -0.0362 -0.0188 79  HIS A NE2 
308  N N   . VAL A 37  ? 0.4702 0.4352 0.3826 0.0318  -0.0250 -0.0069 80  VAL A N   
309  C CA  . VAL A 37  ? 0.4666 0.4360 0.3907 0.0285  -0.0268 -0.0051 80  VAL A CA  
310  C C   . VAL A 37  ? 0.4263 0.3950 0.3477 0.0290  -0.0253 -0.0009 80  VAL A C   
311  O O   . VAL A 37  ? 0.4329 0.4009 0.3495 0.0305  -0.0198 0.0018  80  VAL A O   
312  C CB  . VAL A 37  ? 0.4446 0.4198 0.3807 0.0258  -0.0228 -0.0050 80  VAL A CB  
313  C CG1 . VAL A 37  ? 0.4798 0.4588 0.4260 0.0230  -0.0231 -0.0028 80  VAL A CG1 
314  C CG2 . VAL A 37  ? 0.4590 0.4351 0.3993 0.0249  -0.0254 -0.0087 80  VAL A CG2 
315  N N   . ASP A 38  ? 0.3930 0.3618 0.3184 0.0279  -0.0301 -0.0001 81  ASP A N   
316  C CA  . ASP A 38  ? 0.4730 0.4416 0.3987 0.0279  -0.0292 0.0040  81  ASP A CA  
317  C C   . ASP A 38  ? 0.4173 0.3913 0.3568 0.0248  -0.0268 0.0052  81  ASP A C   
318  O O   . ASP A 38  ? 0.3675 0.3439 0.3155 0.0230  -0.0302 0.0037  81  ASP A O   
319  C CB  . ASP A 38  ? 0.4631 0.4284 0.3850 0.0290  -0.0362 0.0044  81  ASP A CB  
320  C CG  . ASP A 38  ? 0.5403 0.5051 0.4630 0.0292  -0.0354 0.0088  81  ASP A CG  
321  O OD1 . ASP A 38  ? 0.5909 0.5532 0.5055 0.0309  -0.0314 0.0119  81  ASP A OD1 
322  O OD2 . ASP A 38  ? 0.5378 0.5047 0.4695 0.0277  -0.0387 0.0094  81  ASP A OD2 
323  N N   . CYS A 39  ? 0.4186 0.3941 0.3603 0.0243  -0.0208 0.0077  82  CYS A N   
324  C CA  . CYS A 39  ? 0.4180 0.3979 0.3717 0.0215  -0.0187 0.0081  82  CYS A CA  
325  C C   . CYS A 39  ? 0.3795 0.3598 0.3391 0.0206  -0.0214 0.0096  82  CYS A C   
326  O O   . CYS A 39  ? 0.3681 0.3514 0.3371 0.0185  -0.0216 0.0085  82  CYS A O   
327  C CB  . CYS A 39  ? 0.4000 0.3811 0.3554 0.0210  -0.0124 0.0105  82  CYS A CB  
328  S SG  . CYS A 39  ? 0.5325 0.5156 0.4873 0.0212  -0.0087 0.0082  82  CYS A SG  
329  N N   . GLN A 40  ? 0.4123 0.3891 0.3662 0.0223  -0.0236 0.0120  83  GLN A N   
330  C CA  A GLN A 40  ? 0.4172 0.3943 0.3773 0.0218  -0.0267 0.0133  83  GLN A CA  
331  C CA  B GLN A 40  ? 0.4176 0.3947 0.3777 0.0218  -0.0266 0.0133  83  GLN A CA  
332  C C   . GLN A 40  ? 0.4093 0.3884 0.3749 0.0211  -0.0316 0.0104  83  GLN A C   
333  O O   . GLN A 40  ? 0.4178 0.3996 0.3931 0.0197  -0.0319 0.0101  83  GLN A O   
334  C CB  A GLN A 40  ? 0.4568 0.4296 0.4092 0.0241  -0.0288 0.0167  83  GLN A CB  
335  C CB  B GLN A 40  ? 0.4569 0.4298 0.4095 0.0240  -0.0286 0.0168  83  GLN A CB  
336  C CG  A GLN A 40  ? 0.4781 0.4510 0.4371 0.0240  -0.0329 0.0180  83  GLN A CG  
337  C CG  B GLN A 40  ? 0.4871 0.4602 0.4471 0.0236  -0.0305 0.0190  83  GLN A CG  
338  C CD  A GLN A 40  ? 0.5285 0.4970 0.4805 0.0262  -0.0349 0.0220  83  GLN A CD  
339  C CD  B GLN A 40  ? 0.5045 0.4800 0.4741 0.0216  -0.0260 0.0196  83  GLN A CD  
340  O OE1 A GLN A 40  ? 0.5222 0.4870 0.4623 0.0283  -0.0366 0.0226  83  GLN A OE1 
341  O OE1 B GLN A 40  ? 0.4813 0.4599 0.4601 0.0201  -0.0265 0.0175  83  GLN A OE1 
342  N NE2 A GLN A 40  ? 0.5531 0.5217 0.5120 0.0259  -0.0346 0.0247  83  GLN A NE2 
343  N NE2 B GLN A 40  ? 0.4907 0.4648 0.4581 0.0216  -0.0215 0.0226  83  GLN A NE2 
344  N N   . SER A 41  ? 0.3867 0.3642 0.3465 0.0221  -0.0352 0.0082  84  SER A N   
345  C CA  . SER A 41  ? 0.3908 0.3704 0.3569 0.0211  -0.0399 0.0057  84  SER A CA  
346  C C   . SER A 41  ? 0.3375 0.3215 0.3124 0.0189  -0.0370 0.0037  84  SER A C   
347  O O   . SER A 41  ? 0.3223 0.3094 0.3062 0.0176  -0.0386 0.0031  84  SER A O   
348  C CB  . SER A 41  ? 0.3846 0.3608 0.3423 0.0226  -0.0446 0.0034  84  SER A CB  
349  O OG  . SER A 41  ? 0.4515 0.4230 0.4001 0.0249  -0.0481 0.0052  84  SER A OG  
350  N N   . VAL A 42  ? 0.3219 0.3064 0.2942 0.0184  -0.0326 0.0028  85  VAL A N   
351  C CA  . VAL A 42  ? 0.3409 0.3293 0.3206 0.0163  -0.0301 0.0011  85  VAL A CA  
352  C C   . VAL A 42  ? 0.3261 0.3170 0.3141 0.0150  -0.0281 0.0023  85  VAL A C   
353  O O   . VAL A 42  ? 0.3410 0.3346 0.3361 0.0138  -0.0289 0.0012  85  VAL A O   
354  C CB  . VAL A 42  ? 0.3483 0.3368 0.3243 0.0163  -0.0259 0.0005  85  VAL A CB  
355  C CG1 . VAL A 42  ? 0.3095 0.3018 0.2931 0.0141  -0.0236 -0.0008 85  VAL A CG1 
356  C CG2 . VAL A 42  ? 0.3652 0.3511 0.3334 0.0179  -0.0277 -0.0013 85  VAL A CG2 
357  N N   . TRP A 43  ? 0.3069 0.2965 0.2939 0.0153  -0.0255 0.0046  86  TRP A N   
358  C CA  . TRP A 43  ? 0.3818 0.3727 0.3760 0.0143  -0.0238 0.0053  86  TRP A CA  
359  C C   . TRP A 43  ? 0.3736 0.3652 0.3729 0.0148  -0.0271 0.0056  86  TRP A C   
360  O O   . TRP A 43  ? 0.3468 0.3406 0.3531 0.0140  -0.0262 0.0046  86  TRP A O   
361  C CB  . TRP A 43  ? 0.3548 0.3434 0.3473 0.0146  -0.0210 0.0081  86  TRP A CB  
362  C CG  . TRP A 43  ? 0.3875 0.3762 0.3869 0.0140  -0.0202 0.0087  86  TRP A CG  
363  C CD1 . TRP A 43  ? 0.4197 0.4061 0.4200 0.0151  -0.0209 0.0112  86  TRP A CD1 
364  C CD2 . TRP A 43  ? 0.3808 0.3716 0.3867 0.0126  -0.0188 0.0066  86  TRP A CD2 
365  N NE1 . TRP A 43  ? 0.3990 0.3857 0.4063 0.0144  -0.0198 0.0106  86  TRP A NE1 
366  C CE2 . TRP A 43  ? 0.3769 0.3661 0.3871 0.0130  -0.0185 0.0076  86  TRP A CE2 
367  C CE3 . TRP A 43  ? 0.3444 0.3377 0.3522 0.0112  -0.0178 0.0040  86  TRP A CE3 
368  C CZ2 . TRP A 43  ? 0.3553 0.3452 0.3710 0.0122  -0.0171 0.0058  86  TRP A CZ2 
369  C CZ3 . TRP A 43  ? 0.3296 0.3237 0.3424 0.0104  -0.0166 0.0025  86  TRP A CZ3 
370  C CH2 . TRP A 43  ? 0.3519 0.3442 0.3682 0.0110  -0.0161 0.0031  86  TRP A CH2 
371  N N   . ASP A 44  ? 0.3630 0.3525 0.3588 0.0164  -0.0308 0.0068  87  ASP A N   
372  C CA  . ASP A 44  ? 0.3882 0.3787 0.3901 0.0170  -0.0344 0.0074  87  ASP A CA  
373  C C   . ASP A 44  ? 0.3616 0.3556 0.3700 0.0159  -0.0357 0.0053  87  ASP A C   
374  O O   . ASP A 44  ? 0.3407 0.3373 0.3576 0.0158  -0.0356 0.0055  87  ASP A O   
375  C CB  . ASP A 44  ? 0.4846 0.4719 0.4807 0.0187  -0.0392 0.0091  87  ASP A CB  
376  C CG  . ASP A 44  ? 0.5693 0.5572 0.5723 0.0196  -0.0425 0.0108  87  ASP A CG  
377  O OD1 . ASP A 44  ? 0.6920 0.6834 0.7043 0.0190  -0.0435 0.0098  87  ASP A OD1 
378  O OD2 . ASP A 44  ? 0.6970 0.6818 0.6966 0.0211  -0.0440 0.0134  87  ASP A OD2 
379  N N   . ALA A 45  ? 0.3258 0.3201 0.3308 0.0153  -0.0367 0.0034  88  ALA A N   
380  C CA  . ALA A 45  ? 0.3515 0.3492 0.3631 0.0141  -0.0377 0.0018  88  ALA A CA  
381  C C   . ALA A 45  ? 0.3371 0.3376 0.3532 0.0127  -0.0329 0.0010  88  ALA A C   
382  O O   . ALA A 45  ? 0.2998 0.3033 0.3233 0.0122  -0.0325 0.0009  88  ALA A O   
383  C CB  . ALA A 45  ? 0.3611 0.3575 0.3677 0.0139  -0.0402 0.0000  88  ALA A CB  
384  N N   . PHE A 46  ? 0.3462 0.3456 0.3579 0.0123  -0.0294 0.0006  89  PHE A N   
385  C CA  . PHE A 46  ? 0.3040 0.3052 0.3189 0.0111  -0.0256 -0.0003 89  PHE A CA  
386  C C   . PHE A 46  ? 0.3122 0.3140 0.3327 0.0116  -0.0242 0.0004  89  PHE A C   
387  O O   . PHE A 46  ? 0.3089 0.3131 0.3343 0.0113  -0.0229 -0.0003 89  PHE A O   
388  C CB  . PHE A 46  ? 0.3260 0.3257 0.3361 0.0106  -0.0228 -0.0005 89  PHE A CB  
389  C CG  . PHE A 46  ? 0.3087 0.3101 0.3206 0.0091  -0.0202 -0.0020 89  PHE A CG  
390  C CD1 . PHE A 46  ? 0.2930 0.2962 0.3096 0.0087  -0.0193 -0.0028 89  PHE A CD1 
391  C CD2 . PHE A 46  ? 0.3021 0.3031 0.3109 0.0084  -0.0186 -0.0024 89  PHE A CD2 
392  C CE1 . PHE A 46  ? 0.3561 0.3602 0.3729 0.0075  -0.0174 -0.0042 89  PHE A CE1 
393  C CE2 . PHE A 46  ? 0.3817 0.3840 0.3922 0.0070  -0.0170 -0.0037 89  PHE A CE2 
394  C CZ  . PHE A 46  ? 0.3255 0.3291 0.3394 0.0066  -0.0167 -0.0046 89  PHE A CZ  
395  N N   . LYS A 47  ? 0.3413 0.3407 0.3608 0.0127  -0.0244 0.0020  90  LYS A N   
396  C CA  . LYS A 47  ? 0.3542 0.3535 0.3790 0.0135  -0.0233 0.0027  90  LYS A CA  
397  C C   . LYS A 47  ? 0.3429 0.3450 0.3747 0.0143  -0.0250 0.0030  90  LYS A C   
398  O O   . LYS A 47  ? 0.3213 0.3249 0.3585 0.0147  -0.0227 0.0026  90  LYS A O   
399  C CB  . LYS A 47  ? 0.4098 0.4057 0.4324 0.0146  -0.0240 0.0049  90  LYS A CB  
400  C CG  . LYS A 47  ? 0.4463 0.4413 0.4745 0.0158  -0.0231 0.0057  90  LYS A CG  
401  C CD  . LYS A 47  ? 0.4883 0.4794 0.5137 0.0165  -0.0232 0.0081  90  LYS A CD  
402  C CE  . LYS A 47  ? 0.5423 0.5321 0.5631 0.0175  -0.0269 0.0105  90  LYS A CE  
403  N NZ  . LYS A 47  ? 0.6251 0.6135 0.6496 0.0193  -0.0293 0.0129  90  LYS A NZ  
404  N N   . GLY A 48  ? 0.3358 0.3386 0.3678 0.0146  -0.0291 0.0039  91  GLY A N   
405  C CA  . GLY A 48  ? 0.3629 0.3687 0.4032 0.0151  -0.0312 0.0046  91  GLY A CA  
406  C C   . GLY A 48  ? 0.3302 0.3397 0.3754 0.0141  -0.0290 0.0036  91  GLY A C   
407  O O   . GLY A 48  ? 0.3245 0.3371 0.3783 0.0146  -0.0291 0.0046  91  GLY A O   
408  N N   . ALA A 49  ? 0.3224 0.3317 0.3627 0.0127  -0.0268 0.0019  92  ALA A N   
409  C CA  . ALA A 49  ? 0.3116 0.3241 0.3557 0.0118  -0.0248 0.0012  92  ALA A CA  
410  C C   . ALA A 49  ? 0.3318 0.3455 0.3794 0.0126  -0.0203 0.0011  92  ALA A C   
411  O O   . ALA A 49  ? 0.3125 0.3295 0.3660 0.0128  -0.0186 0.0017  92  ALA A O   
412  C CB  . ALA A 49  ? 0.3038 0.3155 0.3415 0.0103  -0.0240 -0.0004 92  ALA A CB  
413  N N   . PHE A 50  ? 0.3035 0.3144 0.3477 0.0134  -0.0182 0.0004  93  PHE A N   
414  C CA  . PHE A 50  ? 0.2906 0.3014 0.3362 0.0143  -0.0140 -0.0006 93  PHE A CA  
415  C C   . PHE A 50  ? 0.3262 0.3349 0.3744 0.0162  -0.0132 -0.0002 93  PHE A C   
416  O O   . PHE A 50  ? 0.3139 0.3227 0.3647 0.0177  -0.0097 -0.0009 93  PHE A O   
417  C CB  . PHE A 50  ? 0.2931 0.3017 0.3316 0.0131  -0.0120 -0.0028 93  PHE A CB  
418  C CG  . PHE A 50  ? 0.2960 0.3008 0.3298 0.0127  -0.0129 -0.0032 93  PHE A CG  
419  C CD1 . PHE A 50  ? 0.3225 0.3268 0.3527 0.0115  -0.0153 -0.0027 93  PHE A CD1 
420  C CD2 . PHE A 50  ? 0.3066 0.3082 0.3399 0.0135  -0.0112 -0.0041 93  PHE A CD2 
421  C CE1 . PHE A 50  ? 0.3033 0.3045 0.3298 0.0112  -0.0155 -0.0025 93  PHE A CE1 
422  C CE2 . PHE A 50  ? 0.3078 0.3061 0.3382 0.0129  -0.0120 -0.0040 93  PHE A CE2 
423  C CZ  . PHE A 50  ? 0.3099 0.3083 0.3370 0.0117  -0.0139 -0.0029 93  PHE A CZ  
424  N N   . ILE A 51  ? 0.3215 0.3280 0.3688 0.0165  -0.0160 0.0010  94  ILE A N   
425  C CA  . ILE A 51  ? 0.3541 0.3582 0.4043 0.0183  -0.0154 0.0017  94  ILE A CA  
426  C C   . ILE A 51  ? 0.3062 0.3136 0.3658 0.0202  -0.0154 0.0032  94  ILE A C   
427  O O   . ILE A 51  ? 0.3247 0.3354 0.3886 0.0199  -0.0181 0.0048  94  ILE A O   
428  C CB  . ILE A 51  ? 0.3854 0.3864 0.4321 0.0182  -0.0185 0.0033  94  ILE A CB  
429  C CG1 . ILE A 51  ? 0.4571 0.4541 0.5041 0.0193  -0.0169 0.0033  94  ILE A CG1 
430  C CG2 . ILE A 51  ? 0.4066 0.4091 0.4572 0.0191  -0.0227 0.0058  94  ILE A CG2 
431  C CD1 . ILE A 51  ? 0.4345 0.4287 0.4767 0.0181  -0.0141 0.0010  94  ILE A CD1 
432  N N   . SER A 52  ? 0.3191 0.3254 0.3825 0.0223  -0.0124 0.0028  95  SER A N   
433  C CA  . SER A 52  ? 0.3558 0.3651 0.4292 0.0245  -0.0115 0.0044  95  SER A CA  
434  C C   . SER A 52  ? 0.3412 0.3554 0.4192 0.0245  -0.0089 0.0045  95  SER A C   
435  O O   . SER A 52  ? 0.3359 0.3540 0.4239 0.0260  -0.0085 0.0065  95  SER A O   
436  C CB  . SER A 52  ? 0.3897 0.4000 0.4682 0.0249  -0.0168 0.0074  95  SER A CB  
437  O OG  . SER A 52  ? 0.4109 0.4232 0.4998 0.0274  -0.0161 0.0091  95  SER A OG  
438  N N   . LYS A 53  ? 0.3017 0.3161 0.3734 0.0229  -0.0069 0.0027  96  LYS A N   
439  C CA  . LYS A 53  ? 0.3039 0.3224 0.3788 0.0228  -0.0039 0.0031  96  LYS A CA  
440  C C   . LYS A 53  ? 0.3087 0.3252 0.3772 0.0236  0.0013  0.0005  96  LYS A C   
441  O O   . LYS A 53  ? 0.3022 0.3142 0.3621 0.0228  0.0011  -0.0020 96  LYS A O   
442  C CB  . LYS A 53  ? 0.3164 0.3371 0.3896 0.0201  -0.0072 0.0038  96  LYS A CB  
443  C CG  . LYS A 53  ? 0.3085 0.3309 0.3876 0.0195  -0.0128 0.0061  96  LYS A CG  
444  C CD  . LYS A 53  ? 0.3232 0.3458 0.3981 0.0169  -0.0166 0.0059  96  LYS A CD  
445  C CE  . LYS A 53  ? 0.3369 0.3602 0.4165 0.0165  -0.0227 0.0076  96  LYS A CE  
446  N NZ  . LYS A 53  ? 0.3342 0.3565 0.4086 0.0145  -0.0266 0.0068  96  LYS A NZ  
447  N N   . HIS A 54  ? 0.2984 0.3179 0.3712 0.0253  0.0058  0.0012  97  HIS A N   
448  C CA  . HIS A 54  ? 0.3224 0.3397 0.3878 0.0264  0.0108  -0.0013 97  HIS A CA  
449  C C   . HIS A 54  ? 0.2993 0.3156 0.3559 0.0236  0.0093  -0.0025 97  HIS A C   
450  O O   . HIS A 54  ? 0.2894 0.3093 0.3486 0.0217  0.0076  -0.0005 97  HIS A O   
451  C CB  . HIS A 54  ? 0.3191 0.3406 0.3908 0.0288  0.0163  0.0005  97  HIS A CB  
452  C CG  . HIS A 54  ? 0.3137 0.3321 0.3768 0.0308  0.0219  -0.0021 97  HIS A CG  
453  N ND1 . HIS A 54  ? 0.3773 0.3898 0.4344 0.0329  0.0234  -0.0056 97  HIS A ND1 
454  C CD2 . HIS A 54  ? 0.3641 0.3840 0.4231 0.0312  0.0260  -0.0018 97  HIS A CD2 
455  C CE1 . HIS A 54  ? 0.3509 0.3612 0.3998 0.0346  0.0280  -0.0077 97  HIS A CE1 
456  N NE2 . HIS A 54  ? 0.3475 0.3623 0.3970 0.0336  0.0298  -0.0052 97  HIS A NE2 
457  N N   . PRO A 55  ? 0.3036 0.3148 0.3503 0.0232  0.0095  -0.0057 98  PRO A N   
458  C CA  . PRO A 55  ? 0.3246 0.3349 0.3640 0.0205  0.0072  -0.0066 98  PRO A CA  
459  C C   . PRO A 55  ? 0.3728 0.3849 0.4086 0.0204  0.0102  -0.0064 98  PRO A C   
460  O O   . PRO A 55  ? 0.3485 0.3587 0.3768 0.0188  0.0090  -0.0078 98  PRO A O   
461  C CB  . PRO A 55  ? 0.2935 0.2979 0.3256 0.0202  0.0061  -0.0098 98  PRO A CB  
462  C CG  . PRO A 55  ? 0.3178 0.3194 0.3502 0.0233  0.0096  -0.0114 98  PRO A CG  
463  C CD  . PRO A 55  ? 0.3324 0.3383 0.3751 0.0252  0.0111  -0.0086 98  PRO A CD  
464  N N   . CYS A 56  ? 0.3631 0.3788 0.4044 0.0223  0.0142  -0.0043 99  CYS A N   
465  C CA  . CYS A 56  ? 0.3254 0.3435 0.3643 0.0223  0.0174  -0.0030 99  CYS A CA  
466  C C   . CYS A 56  ? 0.3944 0.4186 0.4437 0.0213  0.0172  0.0012  99  CYS A C   
467  O O   . CYS A 56  ? 0.3648 0.3916 0.4142 0.0213  0.0203  0.0033  99  CYS A O   
468  C CB  . CYS A 56  ? 0.3894 0.4057 0.4240 0.0257  0.0235  -0.0041 99  CYS A CB  
469  S SG  . CYS A 56  ? 0.3705 0.3786 0.3899 0.0264  0.0233  -0.0094 99  CYS A SG  
470  N N   . ASP A 57  ? 0.3663 0.3928 0.4244 0.0204  0.0135  0.0027  100 ASP A N   
471  C CA  . ASP A 57  ? 0.3497 0.3815 0.4186 0.0193  0.0121  0.0064  100 ASP A CA  
472  C C   . ASP A 57  ? 0.3444 0.3759 0.4146 0.0166  0.0053  0.0064  100 ASP A C   
473  O O   . ASP A 57  ? 0.3674 0.4021 0.4472 0.0159  0.0024  0.0087  100 ASP A O   
474  C CB  . ASP A 57  ? 0.3803 0.4157 0.4609 0.0216  0.0147  0.0088  100 ASP A CB  
475  C CG  . ASP A 57  ? 0.3881 0.4248 0.4686 0.0246  0.0223  0.0095  100 ASP A CG  
476  O OD1 . ASP A 57  ? 0.4195 0.4582 0.4985 0.0241  0.0254  0.0113  100 ASP A OD1 
477  O OD2 . ASP A 57  ? 0.3822 0.4175 0.4634 0.0276  0.0255  0.0084  100 ASP A OD2 
478  N N   . ILE A 58  ? 0.3291 0.3567 0.3897 0.0152  0.0027  0.0038  101 ILE A N   
479  C CA  . ILE A 58  ? 0.3119 0.3387 0.3721 0.0130  -0.0030 0.0035  101 ILE A CA  
480  C C   . ILE A 58  ? 0.3467 0.3760 0.4096 0.0111  -0.0044 0.0053  101 ILE A C   
481  O O   . ILE A 58  ? 0.3368 0.3669 0.3971 0.0108  -0.0014 0.0058  101 ILE A O   
482  C CB  . ILE A 58  ? 0.3188 0.3410 0.3689 0.0123  -0.0044 0.0006  101 ILE A CB  
483  C CG1 . ILE A 58  ? 0.3119 0.3310 0.3596 0.0141  -0.0028 -0.0010 101 ILE A CG1 
484  C CG2 . ILE A 58  ? 0.3255 0.3467 0.3746 0.0106  -0.0095 0.0004  101 ILE A CG2 
485  C CD1 . ILE A 58  ? 0.3141 0.3338 0.3686 0.0153  -0.0046 0.0002  101 ILE A CD1 
486  N N   . THR A 59  ? 0.3215 0.3517 0.3893 0.0098  -0.0093 0.0061  102 THR A N   
487  C CA  . THR A 59  ? 0.3751 0.4072 0.4470 0.0080  -0.0115 0.0077  102 THR A CA  
488  C C   . THR A 59  ? 0.3688 0.3979 0.4353 0.0065  -0.0166 0.0058  102 THR A C   
489  O O   . THR A 59  ? 0.3274 0.3535 0.3888 0.0069  -0.0186 0.0040  102 THR A O   
490  C CB  . THR A 59  ? 0.3460 0.3821 0.4309 0.0079  -0.0129 0.0108  102 THR A CB  
491  O OG1 . THR A 59  ? 0.3789 0.4138 0.4662 0.0082  -0.0179 0.0102  102 THR A OG1 
492  C CG2 . THR A 59  ? 0.3629 0.4024 0.4540 0.0098  -0.0071 0.0130  102 THR A CG2 
493  N N   . GLU A 60  ? 0.3871 0.4168 0.4552 0.0049  -0.0184 0.0065  103 GLU A N   
494  C CA  . GLU A 60  ? 0.4128 0.4395 0.4765 0.0038  -0.0232 0.0047  103 GLU A CA  
495  C C   . GLU A 60  ? 0.3855 0.4110 0.4519 0.0041  -0.0281 0.0043  103 GLU A C   
496  O O   . GLU A 60  ? 0.3600 0.3821 0.4195 0.0043  -0.0309 0.0022  103 GLU A O   
497  C CB  . GLU A 60  ? 0.4769 0.5044 0.5435 0.0021  -0.0244 0.0057  103 GLU A CB  
498  C CG  . GLU A 60  ? 0.5940 0.6215 0.6554 0.0018  -0.0205 0.0058  103 GLU A CG  
499  C CD  . GLU A 60  ? 0.6905 0.7199 0.7575 0.0005  -0.0203 0.0083  103 GLU A CD  
500  O OE1 . GLU A 60  ? 0.6592 0.6919 0.7328 0.0006  -0.0172 0.0114  103 GLU A OE1 
501  O OE2 . GLU A 60  ? 0.6612 0.6887 0.7263 -0.0006 -0.0230 0.0075  103 GLU A OE2 
502  N N   . GLU A 61  ? 0.3943 0.4227 0.4708 0.0044  -0.0292 0.0065  104 GLU A N   
503  C CA  . GLU A 61  ? 0.4355 0.4626 0.5148 0.0047  -0.0347 0.0063  104 GLU A CA  
504  C C   . GLU A 61  ? 0.3903 0.4150 0.4629 0.0064  -0.0344 0.0050  104 GLU A C   
505  O O   . GLU A 61  ? 0.3504 0.3720 0.4191 0.0068  -0.0390 0.0040  104 GLU A O   
506  C CB  . GLU A 61  ? 0.5271 0.5584 0.6202 0.0046  -0.0359 0.0093  104 GLU A CB  
507  C CG  . GLU A 61  ? 0.6439 0.6741 0.7408 0.0052  -0.0421 0.0094  104 GLU A CG  
508  C CD  . GLU A 61  ? 0.8305 0.8646 0.9425 0.0043  -0.0452 0.0123  104 GLU A CD  
509  O OE1 . GLU A 61  ? 0.8380 0.8768 0.9591 0.0040  -0.0405 0.0151  104 GLU A OE1 
510  O OE2 . GLU A 61  ? 0.9562 0.9886 1.0712 0.0039  -0.0524 0.0120  104 GLU A OE2 
511  N N   . ASP A 62  ? 0.3874 0.4129 0.4580 0.0074  -0.0291 0.0051  105 ASP A N   
512  C CA  . ASP A 62  ? 0.3010 0.3237 0.3657 0.0088  -0.0287 0.0040  105 ASP A CA  
513  C C   . ASP A 62  ? 0.2900 0.3085 0.3441 0.0085  -0.0306 0.0019  105 ASP A C   
514  O O   . ASP A 62  ? 0.2998 0.3156 0.3497 0.0094  -0.0324 0.0016  105 ASP A O   
515  C CB  . ASP A 62  ? 0.3377 0.3610 0.4012 0.0099  -0.0227 0.0039  105 ASP A CB  
516  C CG  . ASP A 62  ? 0.3517 0.3786 0.4252 0.0112  -0.0203 0.0060  105 ASP A CG  
517  O OD1 . ASP A 62  ? 0.3628 0.3906 0.4428 0.0120  -0.0234 0.0074  105 ASP A OD1 
518  O OD2 . ASP A 62  ? 0.3263 0.3550 0.4009 0.0117  -0.0153 0.0063  105 ASP A OD2 
519  N N   . TYR A 63  ? 0.3224 0.3404 0.3724 0.0073  -0.0300 0.0007  106 TYR A N   
520  C CA  . TYR A 63  ? 0.3340 0.3485 0.3748 0.0071  -0.0310 -0.0012 106 TYR A CA  
521  C C   . TYR A 63  ? 0.3689 0.3814 0.4081 0.0069  -0.0360 -0.0019 106 TYR A C   
522  O O   . TYR A 63  ? 0.3264 0.3358 0.3577 0.0072  -0.0367 -0.0035 106 TYR A O   
523  C CB  . TYR A 63  ? 0.3070 0.3217 0.3441 0.0062  -0.0276 -0.0021 106 TYR A CB  
524  C CG  . TYR A 63  ? 0.3019 0.3165 0.3367 0.0066  -0.0234 -0.0024 106 TYR A CG  
525  C CD1 . TYR A 63  ? 0.2939 0.3059 0.3233 0.0072  -0.0229 -0.0032 106 TYR A CD1 
526  C CD2 . TYR A 63  ? 0.3178 0.3345 0.3554 0.0066  -0.0201 -0.0019 106 TYR A CD2 
527  C CE1 . TYR A 63  ? 0.3024 0.3136 0.3301 0.0074  -0.0197 -0.0036 106 TYR A CE1 
528  C CE2 . TYR A 63  ? 0.2613 0.2769 0.2959 0.0071  -0.0168 -0.0027 106 TYR A CE2 
529  C CZ  . TYR A 63  ? 0.2747 0.2875 0.3048 0.0074  -0.0170 -0.0037 106 TYR A CZ  
530  O OH  . TYR A 63  ? 0.2834 0.2947 0.3112 0.0078  -0.0144 -0.0047 106 TYR A OH  
531  N N   . GLN A 64  ? 0.3349 0.3487 0.3814 0.0065  -0.0397 -0.0010 107 GLN A N   
532  C CA  . GLN A 64  ? 0.4249 0.4359 0.4695 0.0062  -0.0452 -0.0022 107 GLN A CA  
533  C C   . GLN A 64  ? 0.3838 0.3905 0.4196 0.0077  -0.0482 -0.0034 107 GLN A C   
534  O O   . GLN A 64  ? 0.3966 0.3998 0.4250 0.0081  -0.0499 -0.0054 107 GLN A O   
535  C CB  . GLN A 64  ? 0.4527 0.4660 0.5084 0.0053  -0.0492 -0.0007 107 GLN A CB  
536  C CG  . GLN A 64  ? 0.5161 0.5261 0.5707 0.0049  -0.0556 -0.0023 107 GLN A CG  
537  C CD  . GLN A 64  ? 0.5731 0.5812 0.6229 0.0042  -0.0545 -0.0042 107 GLN A CD  
538  O OE1 . GLN A 64  ? 0.5418 0.5527 0.5944 0.0032  -0.0501 -0.0032 107 GLN A OE1 
539  N NE2 . GLN A 64  ? 0.6034 0.6065 0.6456 0.0049  -0.0585 -0.0068 107 GLN A NE2 
540  N N   . PRO A 65  ? 0.3488 0.3552 0.3846 0.0089  -0.0487 -0.0022 108 PRO A N   
541  C CA  . PRO A 65  ? 0.3702 0.3720 0.3960 0.0105  -0.0511 -0.0029 108 PRO A CA  
542  C C   . PRO A 65  ? 0.3563 0.3559 0.3724 0.0110  -0.0470 -0.0042 108 PRO A C   
543  O O   . PRO A 65  ? 0.3372 0.3327 0.3442 0.0121  -0.0488 -0.0055 108 PRO A O   
544  C CB  . PRO A 65  ? 0.3663 0.3690 0.3954 0.0115  -0.0511 -0.0008 108 PRO A CB  
545  C CG  . PRO A 65  ? 0.3703 0.3775 0.4123 0.0106  -0.0516 0.0008  108 PRO A CG  
546  C CD  . PRO A 65  ? 0.3764 0.3863 0.4214 0.0091  -0.0478 0.0001  108 PRO A CD  
547  N N   . LEU A 66  ? 0.3631 0.3651 0.3807 0.0103  -0.0415 -0.0038 109 LEU A N   
548  C CA  . LEU A 66  ? 0.3468 0.3473 0.3571 0.0105  -0.0379 -0.0047 109 LEU A CA  
549  C C   . LEU A 66  ? 0.3417 0.3414 0.3497 0.0100  -0.0387 -0.0066 109 LEU A C   
550  O O   . LEU A 66  ? 0.3372 0.3341 0.3375 0.0110  -0.0381 -0.0077 109 LEU A O   
551  C CB  . LEU A 66  ? 0.3067 0.3098 0.3201 0.0096  -0.0329 -0.0041 109 LEU A CB  
552  C CG  . LEU A 66  ? 0.3552 0.3574 0.3633 0.0094  -0.0294 -0.0047 109 LEU A CG  
553  C CD1 . LEU A 66  ? 0.3239 0.3229 0.3252 0.0108  -0.0289 -0.0039 109 LEU A CD1 
554  C CD2 . LEU A 66  ? 0.3331 0.3374 0.3448 0.0083  -0.0257 -0.0045 109 LEU A CD2 
555  N N   . MET A 67  ? 0.3540 0.3560 0.3688 0.0086  -0.0398 -0.0069 110 MET A N   
556  C CA  . MET A 67  ? 0.4042 0.4052 0.4178 0.0082  -0.0409 -0.0086 110 MET A CA  
557  C C   . MET A 67  ? 0.4157 0.4121 0.4227 0.0096  -0.0453 -0.0104 110 MET A C   
558  O O   . MET A 67  ? 0.3963 0.3902 0.3974 0.0104  -0.0447 -0.0122 110 MET A O   
559  C CB  . MET A 67  ? 0.4140 0.4179 0.4367 0.0065  -0.0420 -0.0079 110 MET A CB  
560  C CG  . MET A 67  ? 0.4099 0.4179 0.4377 0.0054  -0.0375 -0.0063 110 MET A CG  
561  S SD  . MET A 67  ? 0.4467 0.4547 0.4694 0.0051  -0.0332 -0.0072 110 MET A SD  
562  C CE  . MET A 67  ? 0.4813 0.4896 0.5012 0.0057  -0.0297 -0.0065 110 MET A CE  
563  N N   . LYS A 68  ? 0.3898 0.3848 0.3977 0.0102  -0.0499 -0.0100 111 LYS A N   
564  C CA  . LYS A 68  ? 0.3722 0.3619 0.3727 0.0117  -0.0549 -0.0120 111 LYS A CA  
565  C C   . LYS A 68  ? 0.3903 0.3764 0.3787 0.0139  -0.0524 -0.0126 111 LYS A C   
566  O O   . LYS A 68  ? 0.3743 0.3567 0.3549 0.0153  -0.0527 -0.0149 111 LYS A O   
567  C CB  . LYS A 68  ? 0.4485 0.4375 0.4529 0.0117  -0.0609 -0.0112 111 LYS A CB  
568  C CG  . LYS A 68  ? 0.5530 0.5449 0.5699 0.0097  -0.0642 -0.0106 111 LYS A CG  
569  C CD  . LYS A 68  ? 0.6803 0.6691 0.6985 0.0100  -0.0724 -0.0113 111 LYS A CD  
570  C CE  . LYS A 68  ? 0.7226 0.7151 0.7557 0.0077  -0.0755 -0.0099 111 LYS A CE  
571  N NZ  . LYS A 68  ? 0.7069 0.7053 0.7502 0.0070  -0.0726 -0.0064 111 LYS A NZ  
572  N N   . LEU A 69  ? 0.4037 0.3909 0.3907 0.0144  -0.0496 -0.0104 112 LEU A N   
573  C CA  . LEU A 69  ? 0.3864 0.3706 0.3629 0.0165  -0.0467 -0.0101 112 LEU A CA  
574  C C   . LEU A 69  ? 0.4136 0.3985 0.3876 0.0165  -0.0415 -0.0110 112 LEU A C   
575  O O   . LEU A 69  ? 0.4034 0.3850 0.3682 0.0185  -0.0398 -0.0117 112 LEU A O   
576  C CB  . LEU A 69  ? 0.4001 0.3857 0.3777 0.0166  -0.0444 -0.0072 112 LEU A CB  
577  C CG  . LEU A 69  ? 0.4031 0.3876 0.3821 0.0171  -0.0494 -0.0059 112 LEU A CG  
578  C CD1 . LEU A 69  ? 0.3773 0.3629 0.3577 0.0174  -0.0465 -0.0029 112 LEU A CD1 
579  C CD2 . LEU A 69  ? 0.4063 0.3851 0.3748 0.0193  -0.0544 -0.0071 112 LEU A CD2 
580  N N   . GLY A 70  ? 0.3740 0.3631 0.3561 0.0145  -0.0388 -0.0108 113 GLY A N   
581  C CA  . GLY A 70  ? 0.3984 0.3886 0.3799 0.0143  -0.0345 -0.0114 113 GLY A CA  
582  C C   . GLY A 70  ? 0.4306 0.4195 0.4119 0.0145  -0.0361 -0.0139 113 GLY A C   
583  O O   . GLY A 70  ? 0.4073 0.3977 0.3901 0.0141  -0.0329 -0.0142 113 GLY A O   
584  N N   . THR A 71  ? 0.4101 0.3959 0.3899 0.0150  -0.0415 -0.0156 114 THR A N   
585  C CA  . THR A 71  ? 0.4325 0.4162 0.4122 0.0153  -0.0436 -0.0181 114 THR A CA  
586  C C   . THR A 71  ? 0.4125 0.3941 0.3851 0.0174  -0.0397 -0.0195 114 THR A C   
587  O O   . THR A 71  ? 0.3967 0.3755 0.3602 0.0197  -0.0380 -0.0195 114 THR A O   
588  C CB  . THR A 71  ? 0.4937 0.4728 0.4707 0.0160  -0.0504 -0.0202 114 THR A CB  
589  O OG1 . THR A 71  ? 0.4927 0.4745 0.4785 0.0140  -0.0538 -0.0185 114 THR A OG1 
590  C CG2 . THR A 71  ? 0.4983 0.4744 0.4755 0.0163  -0.0528 -0.0231 114 THR A CG2 
591  N N   . GLN A 72  ? 0.4360 0.4192 0.4129 0.0167  -0.0380 -0.0202 115 GLN A N   
592  C CA  . GLN A 72  ? 0.4500 0.4321 0.4224 0.0187  -0.0339 -0.0212 115 GLN A CA  
593  C C   . GLN A 72  ? 0.4512 0.4327 0.4277 0.0184  -0.0352 -0.0231 115 GLN A C   
594  O O   . GLN A 72  ? 0.4841 0.4689 0.4693 0.0159  -0.0362 -0.0221 115 GLN A O   
595  C CB  . GLN A 72  ? 0.3527 0.3394 0.3283 0.0178  -0.0282 -0.0185 115 GLN A CB  
596  C CG  . GLN A 72  ? 0.3952 0.3815 0.3672 0.0200  -0.0234 -0.0187 115 GLN A CG  
597  C CD  . GLN A 72  ? 0.3730 0.3636 0.3490 0.0188  -0.0185 -0.0158 115 GLN A CD  
598  O OE1 . GLN A 72  ? 0.3353 0.3288 0.3164 0.0165  -0.0189 -0.0141 115 GLN A OE1 
599  N NE2 . GLN A 72  ? 0.3520 0.3429 0.3262 0.0207  -0.0139 -0.0153 115 GLN A NE2 
600  N N   . THR A 73  ? 0.4034 0.3803 0.3732 0.0212  -0.0351 -0.0258 116 THR A N   
601  C CA  . THR A 73  ? 0.4854 0.4609 0.4587 0.0215  -0.0364 -0.0279 116 THR A CA  
602  C C   . THR A 73  ? 0.5145 0.4930 0.4902 0.0223  -0.0306 -0.0270 116 THR A C   
603  O O   . THR A 73  ? 0.5382 0.5151 0.5073 0.0252  -0.0267 -0.0276 116 THR A O   
604  C CB  . THR A 73  ? 0.5194 0.4874 0.4843 0.0244  -0.0401 -0.0320 116 THR A CB  
605  O OG1 . THR A 73  ? 0.6029 0.5683 0.5670 0.0233  -0.0464 -0.0327 116 THR A OG1 
606  C CG2 . THR A 73  ? 0.5528 0.5189 0.5218 0.0248  -0.0413 -0.0342 116 THR A CG2 
607  N N   . VAL A 74  ? 0.5111 0.4940 0.4962 0.0197  -0.0301 -0.0252 117 VAL A N   
608  C CA  . VAL A 74  ? 0.5175 0.5034 0.5068 0.0202  -0.0259 -0.0243 117 VAL A CA  
609  C C   . VAL A 74  ? 0.4899 0.4733 0.4824 0.0209  -0.0281 -0.0264 117 VAL A C   
610  O O   . VAL A 74  ? 0.4964 0.4787 0.4926 0.0191  -0.0326 -0.0267 117 VAL A O   
611  C CB  . VAL A 74  ? 0.5460 0.5379 0.5428 0.0172  -0.0242 -0.0211 117 VAL A CB  
612  C CG1 . VAL A 74  ? 0.5106 0.5039 0.5136 0.0143  -0.0280 -0.0203 117 VAL A CG1 
613  C CG2 . VAL A 74  ? 0.5442 0.5391 0.5456 0.0176  -0.0205 -0.0200 117 VAL A CG2 
614  N N   . PRO A 75  ? 0.4821 0.4645 0.4738 0.0235  -0.0251 -0.0276 118 PRO A N   
615  C CA  . PRO A 75  ? 0.5068 0.4865 0.5023 0.0243  -0.0274 -0.0295 118 PRO A CA  
616  C C   . PRO A 75  ? 0.4794 0.4627 0.4847 0.0207  -0.0299 -0.0271 118 PRO A C   
617  O O   . PRO A 75  ? 0.4316 0.4201 0.4425 0.0192  -0.0275 -0.0243 118 PRO A O   
618  C CB  . PRO A 75  ? 0.5002 0.4806 0.4959 0.0273  -0.0222 -0.0298 118 PRO A CB  
619  C CG  . PRO A 75  ? 0.5357 0.5165 0.5240 0.0292  -0.0179 -0.0293 118 PRO A CG  
620  C CD  . PRO A 75  ? 0.4936 0.4774 0.4823 0.0260  -0.0192 -0.0269 118 PRO A CD  
621  N N   . CYS A 76  ? 0.4618 0.4422 0.4693 0.0194  -0.0349 -0.0280 119 CYS A N   
622  C CA  . CYS A 76  ? 0.4439 0.4277 0.4596 0.0159  -0.0371 -0.0251 119 CYS A CA  
623  C C   . CYS A 76  ? 0.4047 0.3910 0.4271 0.0156  -0.0356 -0.0234 119 CYS A C   
624  O O   . CYS A 76  ? 0.3900 0.3803 0.4180 0.0130  -0.0360 -0.0203 119 CYS A O   
625  C CB  . CYS A 76  ? 0.4540 0.4341 0.4720 0.0147  -0.0425 -0.0261 119 CYS A CB  
626  S SG  . CYS A 76  ? 0.5604 0.5331 0.5781 0.0173  -0.0459 -0.0301 119 CYS A SG  
627  N N   . ASN A 77  ? 0.4171 0.4013 0.4389 0.0185  -0.0340 -0.0253 120 ASN A N   
628  C CA  . ASN A 77  ? 0.4433 0.4297 0.4722 0.0186  -0.0331 -0.0237 120 ASN A CA  
629  C C   . ASN A 77  ? 0.4209 0.4125 0.4514 0.0189  -0.0286 -0.0218 120 ASN A C   
630  O O   . ASN A 77  ? 0.4105 0.4039 0.4469 0.0194  -0.0277 -0.0206 120 ASN A O   
631  C CB  . ASN A 77  ? 0.4466 0.4278 0.4757 0.0217  -0.0339 -0.0268 120 ASN A CB  
632  C CG  . ASN A 77  ? 0.4800 0.4587 0.5020 0.0258  -0.0301 -0.0299 120 ASN A CG  
633  O OD1 . ASN A 77  ? 0.4727 0.4506 0.4871 0.0264  -0.0289 -0.0309 120 ASN A OD1 
634  N ND2 . ASN A 77  ? 0.5160 0.4935 0.5404 0.0288  -0.0279 -0.0311 120 ASN A ND2 
635  N N   . LYS A 78  ? 0.3888 0.3826 0.4150 0.0184  -0.0262 -0.0212 121 LYS A N   
636  C CA  . LYS A 78  ? 0.4179 0.4163 0.4461 0.0186  -0.0221 -0.0194 121 LYS A CA  
637  C C   . LYS A 78  ? 0.4028 0.4050 0.4315 0.0155  -0.0222 -0.0169 121 LYS A C   
638  O O   . LYS A 78  ? 0.4368 0.4413 0.4641 0.0155  -0.0192 -0.0160 121 LYS A O   
639  C CB  . LYS A 78  ? 0.4851 0.4819 0.5074 0.0219  -0.0180 -0.0211 121 LYS A CB  
640  C CG  . LYS A 78  ? 0.4994 0.4918 0.5198 0.0257  -0.0171 -0.0241 121 LYS A CG  
641  C CD  . LYS A 78  ? 0.5488 0.5436 0.5782 0.0264  -0.0161 -0.0229 121 LYS A CD  
642  C CE  . LYS A 78  ? 0.6666 0.6599 0.6949 0.0310  -0.0115 -0.0247 121 LYS A CE  
643  N NZ  . LYS A 78  ? 0.7900 0.7876 0.8289 0.0315  -0.0098 -0.0226 121 LYS A NZ  
644  N N   . ILE A 79  ? 0.3292 0.3321 0.3602 0.0128  -0.0254 -0.0155 122 ILE A N   
645  C CA  . ILE A 79  ? 0.3446 0.3502 0.3749 0.0102  -0.0256 -0.0137 122 ILE A CA  
646  C C   . ILE A 79  ? 0.3638 0.3729 0.3992 0.0084  -0.0260 -0.0112 122 ILE A C   
647  O O   . ILE A 79  ? 0.3467 0.3557 0.3861 0.0082  -0.0279 -0.0103 122 ILE A O   
648  C CB  . ILE A 79  ? 0.3367 0.3405 0.3654 0.0088  -0.0284 -0.0137 122 ILE A CB  
649  C CG1 . ILE A 79  ? 0.4054 0.4064 0.4282 0.0101  -0.0283 -0.0158 122 ILE A CG1 
650  C CG2 . ILE A 79  ? 0.3073 0.3142 0.3371 0.0062  -0.0286 -0.0113 122 ILE A CG2 
651  C CD1 . ILE A 79  ? 0.4306 0.4298 0.4530 0.0089  -0.0315 -0.0159 122 ILE A CD1 
652  N N   . LEU A 80  ? 0.3286 0.3403 0.3636 0.0073  -0.0245 -0.0101 123 LEU A N   
653  C CA  . LEU A 80  ? 0.3321 0.3467 0.3709 0.0056  -0.0254 -0.0081 123 LEU A CA  
654  C C   . LEU A 80  ? 0.3232 0.3384 0.3588 0.0035  -0.0260 -0.0073 123 LEU A C   
655  O O   . LEU A 80  ? 0.3433 0.3587 0.3761 0.0034  -0.0243 -0.0078 123 LEU A O   
656  C CB  . LEU A 80  ? 0.3096 0.3266 0.3521 0.0063  -0.0233 -0.0077 123 LEU A CB  
657  C CG  . LEU A 80  ? 0.2936 0.3132 0.3397 0.0043  -0.0249 -0.0060 123 LEU A CG  
658  C CD1 . LEU A 80  ? 0.3564 0.3762 0.4058 0.0039  -0.0280 -0.0047 123 LEU A CD1 
659  C CD2 . LEU A 80  ? 0.2998 0.3219 0.3510 0.0048  -0.0228 -0.0054 123 LEU A CD2 
660  N N   . LEU A 81  ? 0.3203 0.3356 0.3561 0.0021  -0.0281 -0.0059 124 LEU A N   
661  C CA  . LEU A 81  ? 0.3418 0.3576 0.3744 0.0005  -0.0284 -0.0050 124 LEU A CA  
662  C C   . LEU A 81  ? 0.3121 0.3294 0.3457 -0.0004 -0.0294 -0.0042 124 LEU A C   
663  O O   . LEU A 81  ? 0.2796 0.2978 0.3174 -0.0001 -0.0304 -0.0037 124 LEU A O   
664  C CB  . LEU A 81  ? 0.3089 0.3239 0.3406 -0.0002 -0.0297 -0.0036 124 LEU A CB  
665  C CG  . LEU A 81  ? 0.3174 0.3307 0.3500 0.0005  -0.0300 -0.0042 124 LEU A CG  
666  C CD1 . LEU A 81  ? 0.3258 0.3388 0.3598 -0.0005 -0.0313 -0.0020 124 LEU A CD1 
667  C CD2 . LEU A 81  ? 0.3364 0.3492 0.3662 0.0007  -0.0286 -0.0056 124 LEU A CD2 
668  N N   . TRP A 82  ? 0.3199 0.3371 0.3498 -0.0015 -0.0293 -0.0041 125 TRP A N   
669  C CA  . TRP A 82  ? 0.3358 0.3535 0.3657 -0.0025 -0.0311 -0.0037 125 TRP A CA  
670  C C   . TRP A 82  ? 0.3411 0.3575 0.3649 -0.0033 -0.0315 -0.0034 125 TRP A C   
671  O O   . TRP A 82  ? 0.3307 0.3464 0.3514 -0.0031 -0.0296 -0.0038 125 TRP A O   
672  C CB  . TRP A 82  ? 0.3229 0.3415 0.3557 -0.0027 -0.0303 -0.0047 125 TRP A CB  
673  C CG  . TRP A 82  ? 0.3486 0.3665 0.3787 -0.0026 -0.0279 -0.0058 125 TRP A CG  
674  C CD1 . TRP A 82  ? 0.3461 0.3641 0.3772 -0.0015 -0.0253 -0.0064 125 TRP A CD1 
675  C CD2 . TRP A 82  ? 0.3429 0.3593 0.3684 -0.0033 -0.0278 -0.0065 125 TRP A CD2 
676  N NE1 . TRP A 82  ? 0.3484 0.3655 0.3764 -0.0017 -0.0239 -0.0070 125 TRP A NE1 
677  C CE2 . TRP A 82  ? 0.3731 0.3891 0.3981 -0.0028 -0.0253 -0.0072 125 TRP A CE2 
678  C CE3 . TRP A 82  ? 0.3774 0.3924 0.3986 -0.0041 -0.0295 -0.0066 125 TRP A CE3 
679  C CZ2 . TRP A 82  ? 0.3742 0.3888 0.3958 -0.0031 -0.0245 -0.0080 125 TRP A CZ2 
680  C CZ3 . TRP A 82  ? 0.4079 0.4212 0.4250 -0.0043 -0.0284 -0.0077 125 TRP A CZ3 
681  C CH2 . TRP A 82  ? 0.4109 0.4242 0.4289 -0.0038 -0.0260 -0.0084 125 TRP A CH2 
682  N N   . SER A 83  ? 0.3577 0.3735 0.3798 -0.0040 -0.0342 -0.0028 126 SER A N   
683  C CA  . SER A 83  ? 0.4063 0.4203 0.4214 -0.0044 -0.0347 -0.0028 126 SER A CA  
684  C C   . SER A 83  ? 0.3899 0.4029 0.4041 -0.0053 -0.0375 -0.0040 126 SER A C   
685  O O   . SER A 83  ? 0.3846 0.3981 0.4016 -0.0057 -0.0408 -0.0032 126 SER A O   
686  C CB  . SER A 83  ? 0.4071 0.4205 0.4189 -0.0043 -0.0357 -0.0005 126 SER A CB  
687  O OG  . SER A 83  ? 0.4519 0.4631 0.4556 -0.0043 -0.0361 -0.0005 126 SER A OG  
688  N N   . ARG A 84  ? 0.4208 0.4324 0.4322 -0.0055 -0.0365 -0.0059 127 ARG A N   
689  C CA  . ARG A 84  ? 0.4796 0.4893 0.4899 -0.0064 -0.0393 -0.0075 127 ARG A CA  
690  C C   . ARG A 84  ? 0.4927 0.5044 0.5119 -0.0073 -0.0407 -0.0075 127 ARG A C   
691  O O   . ARG A 84  ? 0.6160 0.6265 0.6366 -0.0081 -0.0417 -0.0089 127 ARG A O   
692  C CB  . ARG A 84  ? 0.5340 0.5416 0.5389 -0.0067 -0.0433 -0.0071 127 ARG A CB  
693  C CG  . ARG A 84  ? 0.6696 0.6746 0.6644 -0.0057 -0.0421 -0.0069 127 ARG A CG  
694  C CD  . ARG A 84  ? 0.8084 0.8095 0.7961 -0.0056 -0.0427 -0.0096 127 ARG A CD  
695  N NE  . ARG A 84  ? 0.9529 0.9526 0.9335 -0.0041 -0.0386 -0.0097 127 ARG A NE  
696  C CZ  . ARG A 84  ? 0.9845 0.9814 0.9604 -0.0034 -0.0370 -0.0122 127 ARG A CZ  
697  N NH1 . ARG A 84  ? 0.9797 0.9745 0.9570 -0.0043 -0.0395 -0.0148 127 ARG A NH1 
698  N NH2 . ARG A 84  ? 0.9779 0.9743 0.9486 -0.0019 -0.0328 -0.0118 127 ARG A NH2 
699  N N   . ILE A 85  ? 0.4384 0.4530 0.4642 -0.0069 -0.0403 -0.0060 128 ILE A N   
700  C CA  . ILE A 85  ? 0.4635 0.4804 0.4985 -0.0075 -0.0410 -0.0056 128 ILE A CA  
701  C C   . ILE A 85  ? 0.4235 0.4421 0.4619 -0.0065 -0.0363 -0.0056 128 ILE A C   
702  O O   . ILE A 85  ? 0.4550 0.4757 0.4977 -0.0054 -0.0348 -0.0046 128 ILE A O   
703  C CB  . ILE A 85  ? 0.4987 0.5175 0.5391 -0.0074 -0.0441 -0.0039 128 ILE A CB  
704  C CG1 . ILE A 85  ? 0.5386 0.5601 0.5897 -0.0080 -0.0449 -0.0033 128 ILE A CG1 
705  C CG2 . ILE A 85  ? 0.4474 0.4673 0.4881 -0.0060 -0.0420 -0.0027 128 ILE A CG2 
706  C CD1 . ILE A 85  ? 0.5097 0.5329 0.5668 -0.0083 -0.0492 -0.0017 128 ILE A CD1 
707  N N   . LYS A 86  ? 0.4498 0.4672 0.4861 -0.0067 -0.0343 -0.0067 129 LYS A N   
708  C CA  . LYS A 86  ? 0.4300 0.4484 0.4682 -0.0057 -0.0301 -0.0065 129 LYS A CA  
709  C C   . LYS A 86  ? 0.4406 0.4613 0.4873 -0.0059 -0.0292 -0.0055 129 LYS A C   
710  O O   . LYS A 86  ? 0.3598 0.3821 0.4090 -0.0046 -0.0258 -0.0048 129 LYS A O   
711  C CB  . LYS A 86  ? 0.4579 0.4740 0.4908 -0.0057 -0.0284 -0.0077 129 LYS A CB  
712  C CG  . LYS A 86  ? 0.5410 0.5576 0.5747 -0.0046 -0.0246 -0.0073 129 LYS A CG  
713  C CD  . LYS A 86  ? 0.5704 0.5847 0.5990 -0.0044 -0.0233 -0.0082 129 LYS A CD  
714  C CE  . LYS A 86  ? 0.5420 0.5549 0.5725 -0.0056 -0.0236 -0.0086 129 LYS A CE  
715  N NZ  . LYS A 86  ? 0.4883 0.4988 0.5140 -0.0051 -0.0225 -0.0095 129 LYS A NZ  
716  N N   . ASP A 87  ? 0.4196 0.4405 0.4709 -0.0076 -0.0321 -0.0053 130 ASP A N   
717  C CA  A ASP A 87  ? 0.4281 0.4515 0.4892 -0.0081 -0.0311 -0.0038 130 ASP A CA  
718  C CA  B ASP A 87  ? 0.4281 0.4515 0.4891 -0.0081 -0.0311 -0.0038 130 ASP A CA  
719  C C   . ASP A 87  ? 0.3995 0.4264 0.4670 -0.0067 -0.0297 -0.0023 130 ASP A C   
720  O O   . ASP A 87  ? 0.3649 0.3939 0.4370 -0.0055 -0.0255 -0.0010 130 ASP A O   
721  C CB  A ASP A 87  ? 0.4536 0.4763 0.5192 -0.0103 -0.0357 -0.0040 130 ASP A CB  
722  C CB  B ASP A 87  ? 0.4537 0.4763 0.5191 -0.0103 -0.0358 -0.0041 130 ASP A CB  
723  C CG  A ASP A 87  ? 0.4700 0.4925 0.5352 -0.0109 -0.0410 -0.0043 130 ASP A CG  
724  C CG  B ASP A 87  ? 0.4696 0.4952 0.5470 -0.0112 -0.0347 -0.0021 130 ASP A CG  
725  O OD1 A ASP A 87  ? 0.4575 0.4804 0.5188 -0.0096 -0.0407 -0.0041 130 ASP A OD1 
726  O OD1 B ASP A 87  ? 0.4605 0.4885 0.5414 -0.0098 -0.0297 -0.0005 130 ASP A OD1 
727  O OD2 A ASP A 87  ? 0.5026 0.5242 0.5713 -0.0127 -0.0457 -0.0046 130 ASP A OD2 
728  O OD2 B ASP A 87  ? 0.5283 0.5534 0.6112 -0.0132 -0.0391 -0.0021 130 ASP A OD2 
729  N N   . LEU A 88  ? 0.3797 0.4070 0.4474 -0.0066 -0.0330 -0.0022 131 LEU A N   
730  C CA  . LEU A 88  ? 0.3837 0.4141 0.4584 -0.0052 -0.0320 -0.0008 131 LEU A CA  
731  C C   . LEU A 88  ? 0.3370 0.3669 0.4073 -0.0027 -0.0278 -0.0012 131 LEU A C   
732  O O   . LEU A 88  ? 0.3282 0.3602 0.4038 -0.0009 -0.0246 -0.0004 131 LEU A O   
733  C CB  . LEU A 88  ? 0.3515 0.3820 0.4275 -0.0057 -0.0371 -0.0003 131 LEU A CB  
734  C CG  . LEU A 88  ? 0.3947 0.4282 0.4790 -0.0041 -0.0365 0.0012  131 LEU A CG  
735  C CD1 . LEU A 88  ? 0.4159 0.4533 0.5126 -0.0041 -0.0350 0.0029  131 LEU A CD1 
736  C CD2 . LEU A 88  ? 0.4465 0.4795 0.5308 -0.0045 -0.0419 0.0019  131 LEU A CD2 
737  N N   . ALA A 89  ? 0.3296 0.3566 0.3905 -0.0026 -0.0278 -0.0026 132 ALA A N   
738  C CA  . ALA A 89  ? 0.3402 0.3662 0.3971 -0.0005 -0.0247 -0.0033 132 ALA A CA  
739  C C   . ALA A 89  ? 0.3501 0.3765 0.4075 0.0008  -0.0201 -0.0033 132 ALA A C   
740  O O   . ALA A 89  ? 0.3140 0.3406 0.3716 0.0031  -0.0173 -0.0035 132 ALA A O   
741  C CB  . ALA A 89  ? 0.3113 0.3346 0.3596 -0.0009 -0.0257 -0.0044 132 ALA A CB  
742  N N   . HIS A 90  ? 0.3353 0.3616 0.3925 -0.0004 -0.0193 -0.0030 133 HIS A N   
743  C CA  . HIS A 90  ? 0.3596 0.3861 0.4167 0.0008  -0.0148 -0.0024 133 HIS A CA  
744  C C   . HIS A 90  ? 0.3765 0.4062 0.4427 0.0017  -0.0121 -0.0005 133 HIS A C   
745  O O   . HIS A 90  ? 0.3330 0.3630 0.3985 0.0040  -0.0076 0.0000  133 HIS A O   
746  C CB  . HIS A 90  ? 0.3863 0.4113 0.4410 -0.0008 -0.0149 -0.0024 133 HIS A CB  
747  C CG  . HIS A 90  ? 0.4191 0.4411 0.4651 -0.0009 -0.0161 -0.0040 133 HIS A CG  
748  N ND1 . HIS A 90  ? 0.4743 0.4945 0.5174 -0.0021 -0.0165 -0.0044 133 HIS A ND1 
749  C CD2 . HIS A 90  ? 0.4108 0.4314 0.4513 0.0000  -0.0169 -0.0052 133 HIS A CD2 
750  C CE1 . HIS A 90  ? 0.4808 0.4990 0.5173 -0.0017 -0.0172 -0.0057 133 HIS A CE1 
751  N NE2 . HIS A 90  ? 0.4138 0.4324 0.4489 -0.0006 -0.0176 -0.0061 133 HIS A NE2 
752  N N   . GLN A 91  ? 0.3526 0.3848 0.4275 -0.0001 -0.0147 0.0007  134 GLN A N   
753  C CA  . GLN A 91  ? 0.3674 0.4033 0.4529 0.0008  -0.0123 0.0029  134 GLN A CA  
754  C C   . GLN A 91  ? 0.3608 0.3974 0.4464 0.0038  -0.0103 0.0024  134 GLN A C   
755  O O   . GLN A 91  ? 0.3747 0.4131 0.4643 0.0061  -0.0054 0.0036  134 GLN A O   
756  C CB  . GLN A 91  ? 0.4067 0.4450 0.5019 -0.0016 -0.0170 0.0040  134 GLN A CB  
757  C CG  . GLN A 91  ? 0.4292 0.4666 0.5261 -0.0045 -0.0192 0.0043  134 GLN A CG  
758  C CD  . GLN A 91  ? 0.4948 0.5336 0.5999 -0.0069 -0.0252 0.0048  134 GLN A CD  
759  O OE1 . GLN A 91  ? 0.4822 0.5248 0.5987 -0.0067 -0.0254 0.0069  134 GLN A OE1 
760  N NE2 . GLN A 91  ? 0.5214 0.5569 0.6207 -0.0089 -0.0302 0.0030  134 GLN A NE2 
761  N N   . PHE A 92  ? 0.3709 0.4056 0.4519 0.0039  -0.0138 0.0008  135 PHE A N   
762  C CA  . PHE A 92  ? 0.3636 0.3981 0.4448 0.0066  -0.0125 0.0001  135 PHE A CA  
763  C C   . PHE A 92  ? 0.3814 0.4135 0.4553 0.0094  -0.0077 -0.0011 135 PHE A C   
764  O O   . PHE A 92  ? 0.4317 0.4648 0.5085 0.0123  -0.0037 -0.0009 135 PHE A O   
765  C CB  . PHE A 92  ? 0.3304 0.3628 0.4076 0.0058  -0.0173 -0.0011 135 PHE A CB  
766  C CG  . PHE A 92  ? 0.3485 0.3797 0.4254 0.0084  -0.0167 -0.0020 135 PHE A CG  
767  C CD1 . PHE A 92  ? 0.3847 0.4183 0.4707 0.0096  -0.0171 -0.0008 135 PHE A CD1 
768  C CD2 . PHE A 92  ? 0.3670 0.3945 0.4353 0.0097  -0.0160 -0.0040 135 PHE A CD2 
769  C CE1 . PHE A 92  ? 0.4287 0.4607 0.5147 0.0122  -0.0165 -0.0019 135 PHE A CE1 
770  C CE2 . PHE A 92  ? 0.3417 0.3673 0.4099 0.0121  -0.0158 -0.0052 135 PHE A CE2 
771  C CZ  . PHE A 92  ? 0.3619 0.3896 0.4387 0.0134  -0.0159 -0.0042 135 PHE A CZ  
772  N N   . THR A 93  ? 0.3446 0.3735 0.4089 0.0089  -0.0081 -0.0025 136 THR A N   
773  C CA  . THR A 93  ? 0.4263 0.4524 0.4827 0.0115  -0.0045 -0.0039 136 THR A CA  
774  C C   . THR A 93  ? 0.4583 0.4858 0.5160 0.0128  0.0009  -0.0022 136 THR A C   
775  O O   . THR A 93  ? 0.4801 0.5056 0.5323 0.0159  0.0047  -0.0029 136 THR A O   
776  C CB  . THR A 93  ? 0.3855 0.4082 0.4326 0.0105  -0.0068 -0.0055 136 THR A CB  
777  O OG1 . THR A 93  ? 0.3515 0.3749 0.3987 0.0080  -0.0076 -0.0044 136 THR A OG1 
778  C CG2 . THR A 93  ? 0.3536 0.3748 0.3994 0.0096  -0.0112 -0.0068 136 THR A CG2 
779  N N   . GLN A 94  ? 0.4002 0.4306 0.4646 0.0107  0.0012  0.0001  137 GLN A N   
780  C CA  . GLN A 94  ? 0.4755 0.5078 0.5433 0.0118  0.0068  0.0026  137 GLN A CA  
781  C C   . GLN A 94  ? 0.4870 0.5221 0.5619 0.0147  0.0109  0.0038  137 GLN A C   
782  O O   . GLN A 94  ? 0.5281 0.5638 0.6029 0.0170  0.0169  0.0054  137 GLN A O   
783  C CB  . GLN A 94  ? 0.4458 0.4805 0.5211 0.0086  0.0056  0.0050  137 GLN A CB  
784  C CG  . GLN A 94  ? 0.4611 0.4928 0.5291 0.0067  0.0039  0.0043  137 GLN A CG  
785  C CD  . GLN A 94  ? 0.5566 0.5859 0.6164 0.0089  0.0085  0.0049  137 GLN A CD  
786  O OE1 . GLN A 94  ? 0.5653 0.5962 0.6283 0.0103  0.0136  0.0075  137 GLN A OE1 
787  N NE2 . GLN A 94  ? 0.5167 0.5421 0.5659 0.0094  0.0066  0.0026  137 GLN A NE2 
788  N N   . VAL A 95  ? 0.4651 0.5017 0.5461 0.0147  0.0080  0.0031  138 VAL A N   
789  C CA  . VAL A 95  ? 0.5031 0.5422 0.5914 0.0177  0.0116  0.0039  138 VAL A CA  
790  C C   . VAL A 95  ? 0.5431 0.5782 0.6231 0.0211  0.0121  0.0007  138 VAL A C   
791  O O   . VAL A 95  ? 0.5846 0.6187 0.6618 0.0250  0.0176  0.0004  138 VAL A O   
792  C CB  . VAL A 95  ? 0.5939 0.6373 0.6958 0.0157  0.0078  0.0055  138 VAL A CB  
793  C CG1 . VAL A 95  ? 0.6934 0.7393 0.8032 0.0191  0.0111  0.0061  138 VAL A CG1 
794  C CG2 . VAL A 95  ? 0.6040 0.6511 0.7152 0.0127  0.0075  0.0086  138 VAL A CG2 
795  N N   . GLN A 96  ? 0.5223 0.5548 0.5982 0.0197  0.0064  -0.0015 139 GLN A N   
796  C CA  . GLN A 96  ? 0.5457 0.5735 0.6137 0.0223  0.0057  -0.0047 139 GLN A CA  
797  C C   . GLN A 96  ? 0.5593 0.5826 0.6143 0.0225  0.0059  -0.0066 139 GLN A C   
798  O O   . GLN A 96  ? 0.5411 0.5618 0.5907 0.0206  0.0013  -0.0081 139 GLN A O   
799  C CB  . GLN A 96  ? 0.5070 0.5343 0.5778 0.0205  -0.0003 -0.0055 139 GLN A CB  
800  C CG  . GLN A 96  ? 0.5610 0.5842 0.6277 0.0232  -0.0011 -0.0082 139 GLN A CG  
801  C CD  . GLN A 96  ? 0.6204 0.6446 0.6933 0.0271  0.0029  -0.0083 139 GLN A CD  
802  O OE1 . GLN A 96  ? 0.6207 0.6495 0.7050 0.0268  0.0034  -0.0059 139 GLN A OE1 
803  N NE2 . GLN A 96  ? 0.6707 0.6905 0.7362 0.0309  0.0058  -0.0111 139 GLN A NE2 
804  N N   . ARG A 97  ? 0.5808 0.6032 0.6310 0.0251  0.0113  -0.0063 140 ARG A N   
805  C CA  . ARG A 97  ? 0.6350 0.6537 0.6737 0.0251  0.0115  -0.0072 140 ARG A CA  
806  C C   . ARG A 97  ? 0.6087 0.6215 0.6371 0.0268  0.0086  -0.0110 140 ARG A C   
807  O O   . ARG A 97  ? 0.5761 0.5858 0.5957 0.0264  0.0073  -0.0119 140 ARG A O   
808  C CB  . ARG A 97  ? 0.7166 0.7357 0.7524 0.0276  0.0182  -0.0054 140 ARG A CB  
809  C CG  . ARG A 97  ? 0.6936 0.7178 0.7387 0.0252  0.0204  -0.0013 140 ARG A CG  
810  C CD  . ARG A 97  ? 0.7605 0.7839 0.8001 0.0270  0.0263  0.0009  140 ARG A CD  
811  N NE  . ARG A 97  ? 0.9169 0.9451 0.9667 0.0247  0.0286  0.0051  140 ARG A NE  
812  C CZ  . ARG A 97  ? 0.9156 0.9439 0.9659 0.0213  0.0261  0.0064  140 ARG A CZ  
813  N NH1 . ARG A 97  ? 0.9077 0.9323 0.9493 0.0198  0.0216  0.0042  140 ARG A NH1 
814  N NH2 . ARG A 97  ? 0.9166 0.9489 0.9772 0.0193  0.0282  0.0102  140 ARG A NH2 
815  N N   . ASP A 98  ? 0.5736 0.5847 0.6036 0.0286  0.0073  -0.0131 141 ASP A N   
816  C CA  . ASP A 98  ? 0.5975 0.6029 0.6195 0.0295  0.0035  -0.0166 141 ASP A CA  
817  C C   . ASP A 98  ? 0.5796 0.5854 0.6044 0.0256  -0.0028 -0.0166 141 ASP A C   
818  O O   . ASP A 98  ? 0.5999 0.6015 0.6201 0.0257  -0.0065 -0.0190 141 ASP A O   
819  C CB  . ASP A 98  ? 0.6206 0.6232 0.6428 0.0333  0.0048  -0.0191 141 ASP A CB  
820  C CG  . ASP A 98  ? 0.6822 0.6883 0.7163 0.0324  0.0032  -0.0179 141 ASP A CG  
821  O OD1 . ASP A 98  ? 0.6637 0.6751 0.7062 0.0294  0.0027  -0.0148 141 ASP A OD1 
822  O OD2 . ASP A 98  ? 0.6843 0.6874 0.7192 0.0346  0.0021  -0.0201 141 ASP A OD2 
823  N N   . MET A 99  ? 0.5263 0.5368 0.5585 0.0223  -0.0039 -0.0139 142 MET A N   
824  C CA  . MET A 99  ? 0.4831 0.4941 0.5169 0.0188  -0.0090 -0.0135 142 MET A CA  
825  C C   . MET A 99  ? 0.4528 0.4645 0.4830 0.0165  -0.0092 -0.0124 142 MET A C   
826  O O   . MET A 99  ? 0.4506 0.4642 0.4811 0.0167  -0.0058 -0.0109 142 MET A O   
827  C CB  . MET A 99  ? 0.4560 0.4708 0.4994 0.0171  -0.0106 -0.0115 142 MET A CB  
828  C CG  . MET A 99  ? 0.5130 0.5266 0.5606 0.0190  -0.0116 -0.0124 142 MET A CG  
829  S SD  . MET A 99  ? 0.5788 0.5895 0.6253 0.0172  -0.0174 -0.0132 142 MET A SD  
830  C CE  . MET A 99  ? 0.4080 0.4231 0.4618 0.0139  -0.0203 -0.0099 142 MET A CE  
831  N N   . PHE A 100 ? 0.3991 0.4095 0.4267 0.0144  -0.0130 -0.0128 143 PHE A N   
832  C CA  . PHE A 100 ? 0.4071 0.4174 0.4307 0.0128  -0.0132 -0.0123 143 PHE A CA  
833  C C   . PHE A 100 ? 0.3624 0.3742 0.3884 0.0098  -0.0164 -0.0113 143 PHE A C   
834  O O   . PHE A 100 ? 0.3432 0.3539 0.3698 0.0092  -0.0193 -0.0117 143 PHE A O   
835  C CB  . PHE A 100 ? 0.4457 0.4518 0.4613 0.0144  -0.0140 -0.0142 143 PHE A CB  
836  C CG  . PHE A 100 ? 0.4928 0.4963 0.5035 0.0178  -0.0109 -0.0156 143 PHE A CG  
837  C CD1 . PHE A 100 ? 0.5283 0.5295 0.5390 0.0202  -0.0111 -0.0175 143 PHE A CD1 
838  C CD2 . PHE A 100 ? 0.5204 0.5236 0.5262 0.0191  -0.0077 -0.0148 143 PHE A CD2 
839  C CE1 . PHE A 100 ? 0.5566 0.5550 0.5617 0.0239  -0.0079 -0.0191 143 PHE A CE1 
840  C CE2 . PHE A 100 ? 0.5136 0.5140 0.5135 0.0226  -0.0044 -0.0158 143 PHE A CE2 
841  C CZ  . PHE A 100 ? 0.5562 0.5543 0.5555 0.0252  -0.0043 -0.0181 143 PHE A CZ  
842  N N   . THR A 101 ? 0.3055 0.3193 0.3325 0.0081  -0.0158 -0.0099 144 THR A N   
843  C CA  . THR A 101 ? 0.3299 0.3442 0.3565 0.0057  -0.0181 -0.0093 144 THR A CA  
844  C C   . THR A 101 ? 0.3178 0.3303 0.3392 0.0058  -0.0180 -0.0099 144 THR A C   
845  O O   . THR A 101 ? 0.3086 0.3196 0.3266 0.0074  -0.0163 -0.0104 144 THR A O   
846  C CB  . THR A 101 ? 0.3269 0.3435 0.3572 0.0040  -0.0180 -0.0080 144 THR A CB  
847  O OG1 . THR A 101 ? 0.3207 0.3376 0.3503 0.0042  -0.0154 -0.0076 144 THR A OG1 
848  C CG2 . THR A 101 ? 0.3271 0.3458 0.3635 0.0040  -0.0185 -0.0073 144 THR A CG2 
849  N N   . LEU A 102 ? 0.3077 0.3204 0.3287 0.0042  -0.0197 -0.0095 145 LEU A N   
850  C CA  . LEU A 102 ? 0.3257 0.3371 0.3432 0.0042  -0.0198 -0.0098 145 LEU A CA  
851  C C   . LEU A 102 ? 0.3162 0.3275 0.3321 0.0045  -0.0175 -0.0093 145 LEU A C   
852  O O   . LEU A 102 ? 0.2913 0.3009 0.3036 0.0056  -0.0171 -0.0095 145 LEU A O   
853  C CB  . LEU A 102 ? 0.3409 0.3531 0.3592 0.0026  -0.0212 -0.0091 145 LEU A CB  
854  C CG  . LEU A 102 ? 0.3150 0.3265 0.3313 0.0026  -0.0211 -0.0091 145 LEU A CG  
855  C CD1 . LEU A 102 ? 0.3276 0.3372 0.3423 0.0038  -0.0225 -0.0098 145 LEU A CD1 
856  C CD2 . LEU A 102 ? 0.3031 0.3156 0.3205 0.0015  -0.0215 -0.0083 145 LEU A CD2 
857  N N   . GLU A 103 ? 0.2871 0.3000 0.3059 0.0036  -0.0164 -0.0085 146 GLU A N   
858  C CA  . GLU A 103 ? 0.3101 0.3229 0.3288 0.0036  -0.0143 -0.0076 146 GLU A CA  
859  C C   . GLU A 103 ? 0.3219 0.3342 0.3394 0.0055  -0.0116 -0.0072 146 GLU A C   
860  O O   . GLU A 103 ? 0.2870 0.2989 0.3038 0.0057  -0.0095 -0.0059 146 GLU A O   
861  C CB  . GLU A 103 ? 0.3404 0.3547 0.3636 0.0018  -0.0145 -0.0069 146 GLU A CB  
862  C CG  . GLU A 103 ? 0.3463 0.3602 0.3687 0.0003  -0.0166 -0.0075 146 GLU A CG  
863  C CD  . GLU A 103 ? 0.3616 0.3762 0.3843 -0.0001 -0.0187 -0.0079 146 GLU A CD  
864  O OE1 . GLU A 103 ? 0.3632 0.3788 0.3883 0.0004  -0.0189 -0.0077 146 GLU A OE1 
865  O OE2 . GLU A 103 ? 0.3502 0.3642 0.3708 -0.0007 -0.0198 -0.0082 146 GLU A OE2 
866  N N   . ASP A 104 ? 0.3325 0.3445 0.3495 0.0070  -0.0115 -0.0080 147 ASP A N   
867  C CA  . ASP A 104 ? 0.3316 0.3425 0.3457 0.0094  -0.0086 -0.0079 147 ASP A CA  
868  C C   . ASP A 104 ? 0.3208 0.3283 0.3272 0.0112  -0.0095 -0.0091 147 ASP A C   
869  O O   . ASP A 104 ? 0.3228 0.3285 0.3245 0.0136  -0.0071 -0.0091 147 ASP A O   
870  C CB  . ASP A 104 ? 0.3582 0.3700 0.3754 0.0107  -0.0079 -0.0085 147 ASP A CB  
871  C CG  . ASP A 104 ? 0.3919 0.4073 0.4174 0.0092  -0.0073 -0.0070 147 ASP A CG  
872  O OD1 . ASP A 104 ? 0.3732 0.3901 0.4016 0.0085  -0.0050 -0.0052 147 ASP A OD1 
873  O OD2 . ASP A 104 ? 0.3539 0.3705 0.3834 0.0086  -0.0093 -0.0074 147 ASP A OD2 
874  N N   . THR A 105 ? 0.3170 0.3234 0.3221 0.0102  -0.0128 -0.0100 148 THR A N   
875  C CA  . THR A 105 ? 0.2980 0.3013 0.2969 0.0114  -0.0144 -0.0108 148 THR A CA  
876  C C   . THR A 105 ? 0.2854 0.2885 0.2825 0.0111  -0.0135 -0.0092 148 THR A C   
877  O O   . THR A 105 ? 0.2905 0.2957 0.2918 0.0094  -0.0123 -0.0078 148 THR A O   
878  C CB  . THR A 105 ? 0.2841 0.2868 0.2842 0.0104  -0.0185 -0.0120 148 THR A CB  
879  O OG1 . THR A 105 ? 0.3164 0.3213 0.3205 0.0082  -0.0192 -0.0109 148 THR A OG1 
880  C CG2 . THR A 105 ? 0.3177 0.3206 0.3208 0.0104  -0.0196 -0.0132 148 THR A CG2 
881  N N   . LEU A 106 ? 0.2835 0.2836 0.2743 0.0127  -0.0144 -0.0094 149 LEU A N   
882  C CA  . LEU A 106 ? 0.3319 0.3313 0.3208 0.0126  -0.0136 -0.0076 149 LEU A CA  
883  C C   . LEU A 106 ? 0.3130 0.3144 0.3073 0.0103  -0.0151 -0.0071 149 LEU A C   
884  O O   . LEU A 106 ? 0.2843 0.2867 0.2813 0.0093  -0.0133 -0.0056 149 LEU A O   
885  C CB  . LEU A 106 ? 0.3379 0.3335 0.3190 0.0147  -0.0157 -0.0081 149 LEU A CB  
886  C CG  . LEU A 106 ? 0.3363 0.3309 0.3155 0.0148  -0.0159 -0.0061 149 LEU A CG  
887  C CD1 . LEU A 106 ? 0.3773 0.3725 0.3565 0.0150  -0.0113 -0.0034 149 LEU A CD1 
888  C CD2 . LEU A 106 ? 0.3565 0.3470 0.3277 0.0169  -0.0191 -0.0067 149 LEU A CD2 
889  N N   . LEU A 107 ? 0.3000 0.3017 0.2962 0.0096  -0.0184 -0.0083 150 LEU A N   
890  C CA  . LEU A 107 ? 0.3358 0.3391 0.3363 0.0081  -0.0193 -0.0078 150 LEU A CA  
891  C C   . LEU A 107 ? 0.3161 0.3217 0.3210 0.0064  -0.0174 -0.0075 150 LEU A C   
892  O O   . LEU A 107 ? 0.2758 0.2817 0.2825 0.0056  -0.0166 -0.0068 150 LEU A O   
893  C CB  . LEU A 107 ? 0.3320 0.3355 0.3346 0.0077  -0.0226 -0.0086 150 LEU A CB  
894  C CG  . LEU A 107 ? 0.3659 0.3669 0.3651 0.0091  -0.0256 -0.0089 150 LEU A CG  
895  C CD1 . LEU A 107 ? 0.4328 0.4344 0.4361 0.0084  -0.0291 -0.0096 150 LEU A CD1 
896  C CD2 . LEU A 107 ? 0.3940 0.3944 0.3925 0.0095  -0.0255 -0.0074 150 LEU A CD2 
897  N N   . GLY A 108 ? 0.2833 0.2901 0.2899 0.0059  -0.0172 -0.0082 151 GLY A N   
898  C CA  . GLY A 108 ? 0.3183 0.3269 0.3285 0.0044  -0.0162 -0.0079 151 GLY A CA  
899  C C   . GLY A 108 ? 0.2840 0.2925 0.2949 0.0042  -0.0139 -0.0068 151 GLY A C   
900  O O   . GLY A 108 ? 0.2783 0.2874 0.2919 0.0029  -0.0137 -0.0066 151 GLY A O   
901  N N   . TYR A 109 ? 0.2725 0.2802 0.2811 0.0057  -0.0121 -0.0061 152 TYR A N   
902  C CA  . TYR A 109 ? 0.2697 0.2775 0.2799 0.0055  -0.0094 -0.0044 152 TYR A CA  
903  C C   . TYR A 109 ? 0.3215 0.3279 0.3314 0.0050  -0.0094 -0.0034 152 TYR A C   
904  O O   . TYR A 109 ? 0.2830 0.2896 0.2966 0.0037  -0.0084 -0.0024 152 TYR A O   
905  C CB  . TYR A 109 ? 0.3330 0.3399 0.3394 0.0077  -0.0069 -0.0035 152 TYR A CB  
906  C CG  . TYR A 109 ? 0.3541 0.3616 0.3628 0.0078  -0.0033 -0.0010 152 TYR A CG  
907  C CD1 . TYR A 109 ? 0.3460 0.3516 0.3520 0.0084  -0.0019 0.0010  152 TYR A CD1 
908  C CD2 . TYR A 109 ? 0.3486 0.3586 0.3628 0.0075  -0.0012 -0.0002 152 TYR A CD2 
909  C CE1 . TYR A 109 ? 0.3332 0.3394 0.3419 0.0084  0.0018  0.0039  152 TYR A CE1 
910  C CE2 . TYR A 109 ? 0.4013 0.4122 0.4189 0.0074  0.0024  0.0025  152 TYR A CE2 
911  C CZ  . TYR A 109 ? 0.3754 0.3843 0.3903 0.0079  0.0040  0.0047  152 TYR A CZ  
912  O OH  . TYR A 109 ? 0.4104 0.4204 0.4296 0.0077  0.0079  0.0080  152 TYR A OH  
913  N N   . LEU A 110 ? 0.2976 0.3023 0.3037 0.0060  -0.0108 -0.0037 153 LEU A N   
914  C CA  . LEU A 110 ? 0.2759 0.2792 0.2822 0.0058  -0.0108 -0.0026 153 LEU A CA  
915  C C   . LEU A 110 ? 0.2618 0.2657 0.2722 0.0041  -0.0116 -0.0035 153 LEU A C   
916  O O   . LEU A 110 ? 0.2627 0.2654 0.2751 0.0035  -0.0108 -0.0027 153 LEU A O   
917  C CB  . LEU A 110 ? 0.2723 0.2741 0.2748 0.0072  -0.0128 -0.0027 153 LEU A CB  
918  C CG  . LEU A 110 ? 0.2995 0.2994 0.2958 0.0093  -0.0127 -0.0020 153 LEU A CG  
919  C CD1 . LEU A 110 ? 0.3256 0.3240 0.3193 0.0103  -0.0160 -0.0024 153 LEU A CD1 
920  C CD2 . LEU A 110 ? 0.3083 0.3068 0.3028 0.0099  -0.0098 0.0006  153 LEU A CD2 
921  N N   . ALA A 111 ? 0.2483 0.2535 0.2595 0.0036  -0.0131 -0.0052 154 ALA A N   
922  C CA  . ALA A 111 ? 0.2797 0.2848 0.2928 0.0026  -0.0137 -0.0062 154 ALA A CA  
923  C C   . ALA A 111 ? 0.2828 0.2885 0.2981 0.0011  -0.0139 -0.0070 154 ALA A C   
924  O O   . ALA A 111 ? 0.2934 0.2983 0.3090 0.0005  -0.0144 -0.0081 154 ALA A O   
925  C CB  . ALA A 111 ? 0.2792 0.2854 0.2919 0.0030  -0.0150 -0.0070 154 ALA A CB  
926  N N   . ASP A 112 ? 0.3079 0.3149 0.3246 0.0007  -0.0135 -0.0065 155 ASP A N   
927  C CA  . ASP A 112 ? 0.3294 0.3373 0.3489 -0.0007 -0.0144 -0.0071 155 ASP A CA  
928  C C   . ASP A 112 ? 0.3117 0.3178 0.3332 -0.0019 -0.0149 -0.0075 155 ASP A C   
929  O O   . ASP A 112 ? 0.2778 0.2829 0.3016 -0.0022 -0.0137 -0.0062 155 ASP A O   
930  C CB  . ASP A 112 ? 0.3202 0.3299 0.3424 -0.0007 -0.0134 -0.0060 155 ASP A CB  
931  C CG  . ASP A 112 ? 0.3882 0.3993 0.4143 -0.0021 -0.0149 -0.0064 155 ASP A CG  
932  O OD1 . ASP A 112 ? 0.3323 0.3435 0.3569 -0.0025 -0.0169 -0.0076 155 ASP A OD1 
933  O OD2 . ASP A 112 ? 0.4585 0.4706 0.4895 -0.0027 -0.0141 -0.0052 155 ASP A OD2 
934  N N   . ASP A 113 ? 0.3079 0.3130 0.3282 -0.0026 -0.0166 -0.0093 156 ASP A N   
935  C CA  . ASP A 113 ? 0.3175 0.3201 0.3390 -0.0038 -0.0180 -0.0104 156 ASP A CA  
936  C C   . ASP A 113 ? 0.3386 0.3383 0.3592 -0.0031 -0.0170 -0.0107 156 ASP A C   
937  O O   . ASP A 113 ? 0.3163 0.3135 0.3394 -0.0040 -0.0177 -0.0110 156 ASP A O   
938  C CB  . ASP A 113 ? 0.3334 0.3366 0.3606 -0.0053 -0.0188 -0.0094 156 ASP A CB  
939  C CG  . ASP A 113 ? 0.4278 0.4331 0.4567 -0.0062 -0.0208 -0.0097 156 ASP A CG  
940  O OD1 . ASP A 113 ? 0.3616 0.3666 0.3863 -0.0060 -0.0224 -0.0111 156 ASP A OD1 
941  O OD2 . ASP A 113 ? 0.4216 0.4289 0.4562 -0.0070 -0.0207 -0.0082 156 ASP A OD2 
942  N N   . LEU A 114 ? 0.3073 0.3072 0.3252 -0.0016 -0.0157 -0.0104 157 LEU A N   
943  C CA  . LEU A 114 ? 0.3074 0.3047 0.3249 -0.0006 -0.0148 -0.0105 157 LEU A CA  
944  C C   . LEU A 114 ? 0.3140 0.3108 0.3284 0.0006  -0.0146 -0.0121 157 LEU A C   
945  O O   . LEU A 114 ? 0.3194 0.3184 0.3319 0.0008  -0.0147 -0.0124 157 LEU A O   
946  C CB  . LEU A 114 ? 0.2998 0.2978 0.3179 0.0004  -0.0134 -0.0082 157 LEU A CB  
947  C CG  . LEU A 114 ? 0.2711 0.2697 0.2916 -0.0002 -0.0126 -0.0060 157 LEU A CG  
948  C CD1 . LEU A 114 ? 0.2676 0.2664 0.2862 0.0013  -0.0113 -0.0039 157 LEU A CD1 
949  C CD2 . LEU A 114 ? 0.3007 0.2967 0.3250 -0.0015 -0.0127 -0.0057 157 LEU A CD2 
950  N N   . THR A 115 ? 0.2995 0.2934 0.3138 0.0016  -0.0140 -0.0129 158 THR A N   
951  C CA  A THR A 115 ? 0.3116 0.3051 0.3237 0.0032  -0.0128 -0.0141 158 THR A CA  
952  C CA  B THR A 115 ? 0.3126 0.3061 0.3247 0.0032  -0.0128 -0.0141 158 THR A CA  
953  C C   . THR A 115 ? 0.2863 0.2789 0.3007 0.0047  -0.0117 -0.0131 158 THR A C   
954  O O   . THR A 115 ? 0.2800 0.2704 0.2966 0.0044  -0.0120 -0.0122 158 THR A O   
955  C CB  A THR A 115 ? 0.3358 0.3259 0.3446 0.0033  -0.0133 -0.0170 158 THR A CB  
956  C CB  B THR A 115 ? 0.3319 0.3219 0.3407 0.0034  -0.0133 -0.0170 158 THR A CB  
957  O OG1 A THR A 115 ? 0.3533 0.3431 0.3597 0.0054  -0.0113 -0.0179 158 THR A OG1 
958  O OG1 B THR A 115 ? 0.3620 0.3477 0.3724 0.0034  -0.0137 -0.0180 158 THR A OG1 
959  C CG2 A THR A 115 ? 0.3517 0.3372 0.3621 0.0028  -0.0143 -0.0181 158 THR A CG2 
960  C CG2 B THR A 115 ? 0.3435 0.3336 0.3505 0.0016  -0.0154 -0.0179 158 THR A CG2 
961  N N   . TRP A 116 ? 0.2867 0.2810 0.3014 0.0064  -0.0105 -0.0127 159 TRP A N   
962  C CA  . TRP A 116 ? 0.3052 0.2992 0.3230 0.0079  -0.0098 -0.0113 159 TRP A CA  
963  C C   . TRP A 116 ? 0.2974 0.2928 0.3163 0.0098  -0.0080 -0.0116 159 TRP A C   
964  O O   . TRP A 116 ? 0.2793 0.2772 0.2969 0.0098  -0.0073 -0.0119 159 TRP A O   
965  C CB  . TRP A 116 ? 0.3096 0.3057 0.3289 0.0076  -0.0110 -0.0087 159 TRP A CB  
966  C CG  . TRP A 116 ? 0.3016 0.3015 0.3208 0.0075  -0.0115 -0.0081 159 TRP A CG  
967  C CD1 . TRP A 116 ? 0.3096 0.3118 0.3314 0.0086  -0.0116 -0.0071 159 TRP A CD1 
968  C CD2 . TRP A 116 ? 0.2952 0.2968 0.3124 0.0060  -0.0123 -0.0083 159 TRP A CD2 
969  N NE1 . TRP A 116 ? 0.2656 0.2706 0.2871 0.0078  -0.0126 -0.0067 159 TRP A NE1 
970  C CE2 . TRP A 116 ? 0.2592 0.2636 0.2775 0.0064  -0.0129 -0.0075 159 TRP A CE2 
971  C CE3 . TRP A 116 ? 0.2969 0.2978 0.3123 0.0046  -0.0127 -0.0089 159 TRP A CE3 
972  C CZ2 . TRP A 116 ? 0.2948 0.3010 0.3120 0.0054  -0.0138 -0.0075 159 TRP A CZ2 
973  C CZ3 . TRP A 116 ? 0.2937 0.2968 0.3082 0.0037  -0.0135 -0.0088 159 TRP A CZ3 
974  C CH2 . TRP A 116 ? 0.2913 0.2969 0.3064 0.0042  -0.0140 -0.0082 159 TRP A CH2 
975  N N   . CYS A 117 ? 0.2841 0.2781 0.3061 0.0116  -0.0072 -0.0112 160 CYS A N   
976  C CA  . CYS A 117 ? 0.2896 0.2856 0.3146 0.0137  -0.0052 -0.0109 160 CYS A CA  
977  C C   . CYS A 117 ? 0.3337 0.3280 0.3632 0.0155  -0.0050 -0.0099 160 CYS A C   
978  O O   . CYS A 117 ? 0.3285 0.3192 0.3576 0.0152  -0.0060 -0.0101 160 CYS A O   
979  C CB  . CYS A 117 ? 0.3509 0.3457 0.3725 0.0148  -0.0025 -0.0133 160 CYS A CB  
980  S SG  . CYS A 117 ? 0.3621 0.3502 0.3803 0.0159  -0.0018 -0.0167 160 CYS A SG  
981  N N   . GLY A 118 ? 0.3202 0.3174 0.3548 0.0174  -0.0038 -0.0086 161 GLY A N   
982  C CA  . GLY A 118 ? 0.3328 0.3288 0.3727 0.0194  -0.0037 -0.0075 161 GLY A CA  
983  C C   . GLY A 118 ? 0.3510 0.3477 0.3944 0.0222  0.0000  -0.0083 161 GLY A C   
984  O O   . GLY A 118 ? 0.3264 0.3226 0.3658 0.0227  0.0028  -0.0104 161 GLY A O   
985  N N   . GLU A 119 ? 0.3080 0.3057 0.3586 0.0243  0.0001  -0.0065 162 GLU A N   
986  C CA  . GLU A 119 ? 0.3380 0.3368 0.3936 0.0274  0.0040  -0.0068 162 GLU A CA  
987  C C   . GLU A 119 ? 0.3648 0.3686 0.4305 0.0284  0.0029  -0.0033 162 GLU A C   
988  O O   . GLU A 119 ? 0.3667 0.3709 0.4349 0.0274  -0.0013 -0.0011 162 GLU A O   
989  C CB  . GLU A 119 ? 0.4391 0.4321 0.4939 0.0297  0.0057  -0.0091 162 GLU A CB  
990  C CG  . GLU A 119 ? 0.4755 0.4697 0.5381 0.0335  0.0091  -0.0085 162 GLU A CG  
991  C CD  . GLU A 119 ? 0.5511 0.5388 0.6123 0.0360  0.0109  -0.0114 162 GLU A CD  
992  O OE1 . GLU A 119 ? 0.5467 0.5293 0.6043 0.0345  0.0080  -0.0123 162 GLU A OE1 
993  O OE2 . GLU A 119 ? 0.5697 0.5571 0.6334 0.0395  0.0154  -0.0126 162 GLU A OE2 
994  N N   . PHE A 120 ? 0.3368 0.3442 0.4084 0.0306  0.0068  -0.0026 163 PHE A N   
995  C CA  . PHE A 120 ? 0.3667 0.3795 0.4498 0.0316  0.0057  0.0009  163 PHE A CA  
996  C C   . PHE A 120 ? 0.3602 0.3711 0.4496 0.0336  0.0039  0.0021  163 PHE A C   
997  O O   . PHE A 120 ? 0.3668 0.3736 0.4552 0.0359  0.0065  0.0002  163 PHE A O   
998  C CB  . PHE A 120 ? 0.3224 0.3395 0.4113 0.0337  0.0113  0.0016  163 PHE A CB  
999  C CG  . PHE A 120 ? 0.3075 0.3307 0.4103 0.0347  0.0104  0.0055  163 PHE A CG  
1000 C CD1 . PHE A 120 ? 0.3058 0.3336 0.4130 0.0321  0.0067  0.0081  163 PHE A CD1 
1001 C CD2 . PHE A 120 ? 0.3404 0.3647 0.4528 0.0382  0.0131  0.0066  163 PHE A CD2 
1002 C CE1 . PHE A 120 ? 0.3140 0.3473 0.4350 0.0327  0.0051  0.0117  163 PHE A CE1 
1003 C CE2 . PHE A 120 ? 0.3557 0.3861 0.4825 0.0390  0.0119  0.0105  163 PHE A CE2 
1004 C CZ  . PHE A 120 ? 0.3353 0.3702 0.4665 0.0361  0.0077  0.0131  163 PHE A CZ  
1005 N N   . ALA A 121 ? 0.3773 0.3910 0.4733 0.0328  -0.0009 0.0052  164 ALA A N   
1006 C CA  . ALA A 121 ? 0.4542 0.4671 0.5578 0.0348  -0.0035 0.0074  164 ALA A CA  
1007 C C   . ALA A 121 ? 0.4864 0.4928 0.5835 0.0346  -0.0055 0.0064  164 ALA A C   
1008 O O   . ALA A 121 ? 0.5235 0.5283 0.6264 0.0366  -0.0070 0.0080  164 ALA A O   
1009 C CB  . ALA A 121 ? 0.5000 0.5152 0.6138 0.0385  0.0012  0.0079  164 ALA A CB  
1010 N N   . THR A 122 ? 0.4259 0.4285 0.5121 0.0324  -0.0057 0.0042  165 THR A N   
1011 C CA  A THR A 122 ? 0.4506 0.4473 0.5313 0.0318  -0.0076 0.0038  165 THR A CA  
1012 C CA  B THR A 122 ? 0.4495 0.4463 0.5303 0.0318  -0.0076 0.0038  165 THR A CA  
1013 C C   . THR A 122 ? 0.4335 0.4298 0.5064 0.0286  -0.0111 0.0044  165 THR A C   
1014 O O   . THR A 122 ? 0.4282 0.4272 0.4976 0.0267  -0.0109 0.0035  165 THR A O   
1015 C CB  A THR A 122 ? 0.4664 0.4581 0.5425 0.0326  -0.0037 0.0002  165 THR A CB  
1016 C CB  B THR A 122 ? 0.4669 0.4585 0.5429 0.0326  -0.0038 0.0002  165 THR A CB  
1017 O OG1 A THR A 122 ? 0.4718 0.4578 0.5451 0.0321  -0.0058 0.0005  165 THR A OG1 
1018 O OG1 B THR A 122 ? 0.4615 0.4526 0.5289 0.0301  -0.0029 -0.0022 165 THR A OG1 
1019 C CG2 A THR A 122 ? 0.4716 0.4634 0.5393 0.0304  -0.0020 -0.0026 165 THR A CG2 
1020 C CG2 B THR A 122 ? 0.4812 0.4735 0.5628 0.0360  0.0010  -0.0013 165 THR A CG2 
1021 N N   . SER A 123 ? 0.3859 0.3784 0.4561 0.0281  -0.0140 0.0060  166 SER A N   
1022 C CA  . SER A 123 ? 0.4204 0.4120 0.4830 0.0256  -0.0167 0.0069  166 SER A CA  
1023 C C   . SER A 123 ? 0.4290 0.4168 0.4846 0.0238  -0.0147 0.0047  166 SER A C   
1024 O O   . SER A 123 ? 0.4342 0.4209 0.4841 0.0220  -0.0162 0.0057  166 SER A O   
1025 C CB  . SER A 123 ? 0.4443 0.4338 0.5070 0.0262  -0.0207 0.0105  166 SER A CB  
1026 O OG  . SER A 123 ? 0.5131 0.4979 0.5770 0.0273  -0.0198 0.0111  166 SER A OG  
1027 N N   . LYS A 124 ? 0.3934 0.3793 0.4495 0.0245  -0.0113 0.0018  167 LYS A N   
1028 C CA  . LYS A 124 ? 0.4225 0.4040 0.4734 0.0229  -0.0102 -0.0003 167 LYS A CA  
1029 C C   . LYS A 124 ? 0.4102 0.3937 0.4560 0.0210  -0.0089 -0.0029 167 LYS A C   
1030 O O   . LYS A 124 ? 0.3531 0.3396 0.3996 0.0218  -0.0071 -0.0044 167 LYS A O   
1031 C CB  . LYS A 124 ? 0.4477 0.4246 0.5012 0.0248  -0.0080 -0.0025 167 LYS A CB  
1032 C CG  . LYS A 124 ? 0.5392 0.5128 0.5976 0.0265  -0.0093 0.0000  167 LYS A CG  
1033 C CD  . LYS A 124 ? 0.5911 0.5613 0.6466 0.0244  -0.0114 0.0024  167 LYS A CD  
1034 C CE  . LYS A 124 ? 0.6819 0.6481 0.7421 0.0261  -0.0126 0.0051  167 LYS A CE  
1035 N NZ  . LYS A 124 ? 0.7041 0.6734 0.7682 0.0279  -0.0148 0.0086  167 LYS A NZ  
1036 N N   . ILE A 125 ? 0.3990 0.3809 0.4399 0.0186  -0.0098 -0.0030 168 ILE A N   
1037 C CA  . ILE A 125 ? 0.3748 0.3575 0.4112 0.0168  -0.0089 -0.0056 168 ILE A CA  
1038 C C   . ILE A 125 ? 0.3901 0.3688 0.4255 0.0174  -0.0072 -0.0091 168 ILE A C   
1039 O O   . ILE A 125 ? 0.3623 0.3362 0.3994 0.0180  -0.0073 -0.0095 168 ILE A O   
1040 C CB  . ILE A 125 ? 0.3795 0.3619 0.4124 0.0143  -0.0104 -0.0043 168 ILE A CB  
1041 C CG1 . ILE A 125 ? 0.4019 0.3879 0.4339 0.0141  -0.0120 -0.0016 168 ILE A CG1 
1042 C CG2 . ILE A 125 ? 0.3873 0.3699 0.4166 0.0124  -0.0098 -0.0070 168 ILE A CG2 
1043 C CD1 . ILE A 125 ? 0.4348 0.4205 0.4632 0.0122  -0.0127 0.0000  168 ILE A CD1 
1044 N N   . ASN A 126 ? 0.4041 0.3842 0.4362 0.0173  -0.0057 -0.0117 169 ASN A N   
1045 C CA  . ASN A 126 ? 0.3662 0.3420 0.3954 0.0182  -0.0042 -0.0156 169 ASN A CA  
1046 C C   . ASN A 126 ? 0.3725 0.3456 0.3976 0.0155  -0.0061 -0.0172 169 ASN A C   
1047 O O   . ASN A 126 ? 0.3288 0.3045 0.3503 0.0140  -0.0065 -0.0177 169 ASN A O   
1048 C CB  . ASN A 126 ? 0.3255 0.3039 0.3528 0.0200  -0.0015 -0.0171 169 ASN A CB  
1049 C CG  . ASN A 126 ? 0.3931 0.3663 0.4158 0.0216  0.0003  -0.0213 169 ASN A CG  
1050 O OD1 . ASN A 126 ? 0.3597 0.3276 0.3797 0.0206  -0.0014 -0.0236 169 ASN A OD1 
1051 N ND2 . ASN A 126 ? 0.3986 0.3732 0.4206 0.0244  0.0039  -0.0223 169 ASN A ND2 
1052 N N   . TYR A 127 ? 0.3685 0.3365 0.3950 0.0148  -0.0075 -0.0177 170 TYR A N   
1053 C CA  . TYR A 127 ? 0.3765 0.3419 0.4011 0.0121  -0.0096 -0.0191 170 TYR A CA  
1054 C C   . TYR A 127 ? 0.3742 0.3345 0.3943 0.0127  -0.0099 -0.0238 170 TYR A C   
1055 O O   . TYR A 127 ? 0.4006 0.3582 0.4194 0.0104  -0.0124 -0.0253 170 TYR A O   
1056 C CB  . TYR A 127 ? 0.4183 0.3806 0.4476 0.0108  -0.0111 -0.0167 170 TYR A CB  
1057 C CG  . TYR A 127 ? 0.3963 0.3629 0.4278 0.0099  -0.0111 -0.0120 170 TYR A CG  
1058 C CD1 . TYR A 127 ? 0.3909 0.3608 0.4212 0.0075  -0.0118 -0.0107 170 TYR A CD1 
1059 C CD2 . TYR A 127 ? 0.3702 0.3374 0.4045 0.0116  -0.0106 -0.0091 170 TYR A CD2 
1060 C CE1 . TYR A 127 ? 0.3996 0.3727 0.4304 0.0071  -0.0116 -0.0068 170 TYR A CE1 
1061 C CE2 . TYR A 127 ? 0.4223 0.3927 0.4569 0.0110  -0.0109 -0.0051 170 TYR A CE2 
1062 C CZ  . TYR A 127 ? 0.4283 0.4015 0.4607 0.0088  -0.0112 -0.0041 170 TYR A CZ  
1063 O OH  . TYR A 127 ? 0.4145 0.3902 0.4458 0.0087  -0.0113 -0.0005 170 TYR A OH  
1064 N N   . GLN A 128 ? 0.3955 0.3543 0.4132 0.0157  -0.0076 -0.0262 171 GLN A N   
1065 C CA  . GLN A 128 ? 0.4443 0.3972 0.4561 0.0169  -0.0078 -0.0312 171 GLN A CA  
1066 C C   . GLN A 128 ? 0.3843 0.3396 0.3888 0.0169  -0.0071 -0.0329 171 GLN A C   
1067 O O   . GLN A 128 ? 0.3682 0.3193 0.3670 0.0160  -0.0093 -0.0362 171 GLN A O   
1068 C CB  . GLN A 128 ? 0.4892 0.4383 0.5017 0.0207  -0.0051 -0.0331 171 GLN A CB  
1069 C CG  . GLN A 128 ? 0.6496 0.5944 0.6687 0.0208  -0.0063 -0.0321 171 GLN A CG  
1070 C CD  . GLN A 128 ? 0.7841 0.7242 0.8038 0.0249  -0.0038 -0.0346 171 GLN A CD  
1071 O OE1 . GLN A 128 ? 0.8202 0.7610 0.8359 0.0279  -0.0005 -0.0367 171 GLN A OE1 
1072 N NE2 . GLN A 128 ? 0.7459 0.6811 0.7712 0.0252  -0.0052 -0.0342 171 GLN A NE2 
1073 N N   . SER A 129 ? 0.3688 0.3303 0.3734 0.0179  -0.0044 -0.0306 172 SER A N   
1074 C CA  . SER A 129 ? 0.3828 0.3469 0.3811 0.0178  -0.0035 -0.0314 172 SER A CA  
1075 C C   . SER A 129 ? 0.3870 0.3586 0.3889 0.0179  -0.0013 -0.0275 172 SER A C   
1076 O O   . SER A 129 ? 0.3328 0.3071 0.3410 0.0191  0.0002  -0.0251 172 SER A O   
1077 C CB  . SER A 129 ? 0.3934 0.3529 0.3841 0.0210  -0.0010 -0.0353 172 SER A CB  
1078 O OG  . SER A 129 ? 0.4264 0.3872 0.4202 0.0244  0.0035  -0.0345 172 SER A OG  
1079 N N   . CYS A 130 ? 0.3336 0.3085 0.3319 0.0166  -0.0017 -0.0268 173 CYS A N   
1080 C CA  . CYS A 130 ? 0.3588 0.3404 0.3600 0.0165  0.0000  -0.0235 173 CYS A CA  
1081 C C   . CYS A 130 ? 0.3868 0.3693 0.3817 0.0174  0.0021  -0.0243 173 CYS A C   
1082 O O   . CYS A 130 ? 0.3629 0.3413 0.3502 0.0173  0.0009  -0.0271 173 CYS A O   
1083 C CB  . CYS A 130 ? 0.3517 0.3369 0.3562 0.0135  -0.0030 -0.0210 173 CYS A CB  
1084 S SG  . CYS A 130 ? 0.3564 0.3414 0.3678 0.0127  -0.0047 -0.0189 173 CYS A SG  
1085 N N   . PRO A 131 ? 0.3721 0.3599 0.3700 0.0183  0.0049  -0.0215 174 PRO A N   
1086 C CA  . PRO A 131 ? 0.3592 0.3479 0.3512 0.0195  0.0076  -0.0215 174 PRO A CA  
1087 C C   . PRO A 131 ? 0.3954 0.3836 0.3815 0.0171  0.0045  -0.0219 174 PRO A C   
1088 O O   . PRO A 131 ? 0.3685 0.3592 0.3582 0.0144  0.0014  -0.0203 174 PRO A O   
1089 C CB  . PRO A 131 ? 0.3762 0.3713 0.3757 0.0201  0.0103  -0.0176 174 PRO A CB  
1090 C CG  . PRO A 131 ? 0.3540 0.3504 0.3622 0.0204  0.0097  -0.0165 174 PRO A CG  
1091 C CD  . PRO A 131 ? 0.3344 0.3272 0.3414 0.0184  0.0055  -0.0181 174 PRO A CD  
1092 N N   . ASP A 132 ? 0.4121 0.3969 0.3889 0.0183  0.0055  -0.0240 175 ASP A N   
1093 C CA  . ASP A 132 ? 0.4514 0.4361 0.4222 0.0165  0.0030  -0.0238 175 ASP A CA  
1094 C C   . ASP A 132 ? 0.4327 0.4225 0.4044 0.0169  0.0061  -0.0202 175 ASP A C   
1095 O O   . ASP A 132 ? 0.4193 0.4103 0.3909 0.0196  0.0111  -0.0191 175 ASP A O   
1096 C CB  . ASP A 132 ? 0.4503 0.4282 0.4097 0.0177  0.0019  -0.0278 175 ASP A CB  
1097 C CG  . ASP A 132 ? 0.4948 0.4726 0.4475 0.0162  -0.0007 -0.0273 175 ASP A CG  
1098 O OD1 . ASP A 132 ? 0.4971 0.4755 0.4525 0.0133  -0.0055 -0.0271 175 ASP A OD1 
1099 O OD2 . ASP A 132 ? 0.4950 0.4722 0.4400 0.0182  0.0022  -0.0267 175 ASP A OD2 
1100 N N   . TRP A 133 ? 0.4790 0.4717 0.4521 0.0144  0.0034  -0.0181 176 TRP A N   
1101 C CA  . TRP A 133 ? 0.4850 0.4828 0.4611 0.0144  0.0058  -0.0142 176 TRP A CA  
1102 C C   . TRP A 133 ? 0.5053 0.5016 0.4728 0.0167  0.0097  -0.0137 176 TRP A C   
1103 O O   . TRP A 133 ? 0.5220 0.5221 0.4928 0.0178  0.0138  -0.0104 176 TRP A O   
1104 C CB  . TRP A 133 ? 0.5216 0.5218 0.5004 0.0114  0.0018  -0.0124 176 TRP A CB  
1105 C CG  . TRP A 133 ? 0.5865 0.5835 0.5571 0.0104  -0.0014 -0.0139 176 TRP A CG  
1106 C CD1 . TRP A 133 ? 0.6080 0.6023 0.5776 0.0087  -0.0060 -0.0163 176 TRP A CD1 
1107 C CD2 . TRP A 133 ? 0.6238 0.6200 0.5868 0.0111  -0.0006 -0.0127 176 TRP A CD2 
1108 N NE1 . TRP A 133 ? 0.6424 0.6344 0.6047 0.0082  -0.0086 -0.0168 176 TRP A NE1 
1109 C CE2 . TRP A 133 ? 0.6348 0.6276 0.5922 0.0097  -0.0054 -0.0147 176 TRP A CE2 
1110 C CE3 . TRP A 133 ? 0.6479 0.6460 0.6086 0.0127  0.0038  -0.0097 176 TRP A CE3 
1111 C CZ2 . TRP A 133 ? 0.6743 0.6653 0.6231 0.0100  -0.0065 -0.0140 176 TRP A CZ2 
1112 C CZ3 . TRP A 133 ? 0.6874 0.6835 0.6390 0.0130  0.0033  -0.0088 176 TRP A CZ3 
1113 C CH2 . TRP A 133 ? 0.6724 0.6648 0.6177 0.0117  -0.0020 -0.0110 176 TRP A CH2 
1114 N N   . ARG A 134 ? 0.5048 0.4953 0.4611 0.0176  0.0084  -0.0170 177 ARG A N   
1115 C CA  . ARG A 134 ? 0.5843 0.5725 0.5300 0.0201  0.0120  -0.0167 177 ARG A CA  
1116 C C   . ARG A 134 ? 0.5322 0.5174 0.4738 0.0240  0.0171  -0.0189 177 ARG A C   
1117 O O   . ARG A 134 ? 0.5423 0.5298 0.4836 0.0265  0.0232  -0.0163 177 ARG A O   
1118 C CB  . ARG A 134 ? 0.6636 0.6467 0.5980 0.0193  0.0073  -0.0190 177 ARG A CB  
1119 C CG  . ARG A 134 ? 0.7400 0.7201 0.6614 0.0221  0.0106  -0.0186 177 ARG A CG  
1120 C CD  . ARG A 134 ? 0.8897 0.8645 0.7999 0.0211  0.0050  -0.0208 177 ARG A CD  
1121 N NE  . ARG A 134 ? 1.0524 1.0208 0.9582 0.0211  0.0006  -0.0263 177 ARG A NE  
1122 C CZ  . ARG A 134 ? 1.1157 1.0774 1.0106 0.0243  0.0022  -0.0304 177 ARG A CZ  
1123 N NH1 . ARG A 134 ? 1.1492 1.1098 1.0358 0.0281  0.0087  -0.0295 177 ARG A NH1 
1124 N NH2 . ARG A 134 ? 1.1251 1.0807 1.0175 0.0237  -0.0027 -0.0353 177 ARG A NH2 
1125 N N   . LYS A 135 ? 0.5309 0.5106 0.4697 0.0246  0.0149  -0.0234 178 LYS A N   
1126 C CA  . LYS A 135 ? 0.4970 0.4725 0.4304 0.0287  0.0195  -0.0263 178 LYS A CA  
1127 C C   . LYS A 135 ? 0.4962 0.4762 0.4412 0.0302  0.0242  -0.0242 178 LYS A C   
1128 O O   . LYS A 135 ? 0.5107 0.4894 0.4528 0.0341  0.0301  -0.0248 178 LYS A O   
1129 C CB  . LYS A 135 ? 0.5143 0.4819 0.4417 0.0287  0.0150  -0.0320 178 LYS A CB  
1130 C CG  . LYS A 135 ? 0.6439 0.6062 0.5599 0.0273  0.0095  -0.0345 178 LYS A CG  
1131 C CD  . LYS A 135 ? 0.6926 0.6472 0.6050 0.0271  0.0046  -0.0400 178 LYS A CD  
1132 C CE  . LYS A 135 ? 0.7738 0.7262 0.6838 0.0235  -0.0032 -0.0413 178 LYS A CE  
1133 N NZ  . LYS A 135 ? 0.8201 0.7673 0.7333 0.0220  -0.0083 -0.0452 178 LYS A NZ  
1134 N N   . ASP A 136 ? 0.4939 0.4789 0.4516 0.0276  0.0219  -0.0219 179 ASP A N   
1135 C CA  . ASP A 136 ? 0.4677 0.4564 0.4366 0.0289  0.0251  -0.0202 179 ASP A CA  
1136 C C   . ASP A 136 ? 0.4547 0.4515 0.4340 0.0279  0.0273  -0.0148 179 ASP A C   
1137 O O   . ASP A 136 ? 0.4684 0.4682 0.4512 0.0306  0.0331  -0.0125 179 ASP A O   
1138 C CB  . ASP A 136 ? 0.4325 0.4198 0.4078 0.0270  0.0204  -0.0220 179 ASP A CB  
1139 C CG  . ASP A 136 ? 0.4443 0.4236 0.4120 0.0282  0.0186  -0.0272 179 ASP A CG  
1140 O OD1 . ASP A 136 ? 0.4699 0.4453 0.4317 0.0319  0.0226  -0.0295 179 ASP A OD1 
1141 O OD2 . ASP A 136 ? 0.4217 0.3986 0.3897 0.0255  0.0132  -0.0288 179 ASP A OD2 
1142 N N   . CYS A 137 ? 0.4349 0.4351 0.4195 0.0243  0.0228  -0.0127 180 CYS A N   
1143 C CA  . CYS A 137 ? 0.4526 0.4598 0.4480 0.0232  0.0239  -0.0080 180 CYS A CA  
1144 C C   . CYS A 137 ? 0.3973 0.4062 0.3952 0.0194  0.0183  -0.0070 180 CYS A C   
1145 O O   . CYS A 137 ? 0.3968 0.4028 0.3923 0.0177  0.0138  -0.0095 180 CYS A O   
1146 C CB  . CYS A 137 ? 0.4415 0.4517 0.4484 0.0243  0.0252  -0.0069 180 CYS A CB  
1147 S SG  . CYS A 137 ? 0.4577 0.4655 0.4683 0.0226  0.0194  -0.0093 180 CYS A SG  
1148 N N   . SER A 138 ? 0.4286 0.4422 0.4320 0.0182  0.0188  -0.0031 181 SER A N   
1149 C CA  A SER A 138 ? 0.4337 0.4487 0.4390 0.0150  0.0141  -0.0020 181 SER A CA  
1150 C CA  B SER A 138 ? 0.4339 0.4489 0.4392 0.0150  0.0141  -0.0020 181 SER A CA  
1151 C C   . SER A 138 ? 0.4018 0.4194 0.4169 0.0134  0.0106  -0.0014 181 SER A C   
1152 O O   . SER A 138 ? 0.3745 0.3915 0.3894 0.0112  0.0062  -0.0021 181 SER A O   
1153 C CB  A SER A 138 ? 0.4570 0.4751 0.4633 0.0144  0.0159  0.0018  181 SER A CB  
1154 C CB  B SER A 138 ? 0.4568 0.4749 0.4632 0.0144  0.0159  0.0019  181 SER A CB  
1155 O OG  A SER A 138 ? 0.4627 0.4856 0.4791 0.0152  0.0192  0.0054  181 SER A OG  
1156 O OG  B SER A 138 ? 0.4906 0.5059 0.4861 0.0159  0.0186  0.0015  181 SER A OG  
1157 N N   . ASN A 139 ? 0.3723 0.3925 0.3957 0.0146  0.0125  0.0000  182 ASN A N   
1158 C CA  . ASN A 139 ? 0.3824 0.4049 0.4148 0.0133  0.0088  0.0010  182 ASN A CA  
1159 C C   . ASN A 139 ? 0.3673 0.3868 0.3986 0.0139  0.0069  -0.0017 182 ASN A C   
1160 O O   . ASN A 139 ? 0.3549 0.3756 0.3929 0.0149  0.0069  -0.0010 182 ASN A O   
1161 C CB  . ASN A 139 ? 0.3455 0.3729 0.3889 0.0141  0.0110  0.0045  182 ASN A CB  
1162 C CG  . ASN A 139 ? 0.4140 0.4446 0.4607 0.0128  0.0119  0.0079  182 ASN A CG  
1163 O OD1 . ASN A 139 ? 0.3841 0.4138 0.4274 0.0108  0.0088  0.0077  182 ASN A OD1 
1164 N ND2 . ASN A 139 ? 0.4082 0.4426 0.4621 0.0142  0.0162  0.0112  182 ASN A ND2 
1165 N N   . ASN A 140 ? 0.3575 0.3729 0.3807 0.0131  0.0050  -0.0046 183 ASN A N   
1166 C CA  . ASN A 140 ? 0.3141 0.3262 0.3363 0.0132  0.0031  -0.0068 183 ASN A CA  
1167 C C   . ASN A 140 ? 0.3253 0.3379 0.3496 0.0111  -0.0013 -0.0064 183 ASN A C   
1168 O O   . ASN A 140 ? 0.3114 0.3258 0.3362 0.0095  -0.0032 -0.0053 183 ASN A O   
1169 C CB  . ASN A 140 ? 0.3177 0.3251 0.3311 0.0135  0.0034  -0.0100 183 ASN A CB  
1170 C CG  . ASN A 140 ? 0.3282 0.3348 0.3362 0.0114  0.0009  -0.0105 183 ASN A CG  
1171 O OD1 . ASN A 140 ? 0.3350 0.3411 0.3435 0.0096  -0.0024 -0.0109 183 ASN A OD1 
1172 N ND2 . ASN A 140 ? 0.3481 0.3545 0.3511 0.0118  0.0028  -0.0104 183 ASN A ND2 
1173 N N   . PRO A 141 ? 0.3128 0.3235 0.3383 0.0114  -0.0029 -0.0071 184 PRO A N   
1174 C CA  . PRO A 141 ? 0.2971 0.3081 0.3240 0.0099  -0.0066 -0.0064 184 PRO A CA  
1175 C C   . PRO A 141 ? 0.2950 0.3053 0.3174 0.0080  -0.0084 -0.0072 184 PRO A C   
1176 O O   . PRO A 141 ? 0.2694 0.2811 0.2931 0.0070  -0.0106 -0.0062 184 PRO A O   
1177 C CB  . PRO A 141 ? 0.2831 0.2913 0.3102 0.0107  -0.0071 -0.0070 184 PRO A CB  
1178 C CG  . PRO A 141 ? 0.2985 0.3063 0.3280 0.0129  -0.0042 -0.0073 184 PRO A CG  
1179 C CD  . PRO A 141 ? 0.2985 0.3066 0.3244 0.0133  -0.0013 -0.0083 184 PRO A CD  
1180 N N   . VAL A 142 ? 0.3090 0.3169 0.3263 0.0076  -0.0077 -0.0090 185 VAL A N   
1181 C CA  . VAL A 142 ? 0.2794 0.2868 0.2936 0.0058  -0.0096 -0.0096 185 VAL A CA  
1182 C C   . VAL A 142 ? 0.2932 0.3031 0.3073 0.0052  -0.0098 -0.0086 185 VAL A C   
1183 O O   . VAL A 142 ? 0.2984 0.3095 0.3135 0.0041  -0.0117 -0.0079 185 VAL A O   
1184 C CB  . VAL A 142 ? 0.3146 0.3186 0.3245 0.0055  -0.0097 -0.0117 185 VAL A CB  
1185 C CG1 . VAL A 142 ? 0.3298 0.3339 0.3377 0.0037  -0.0116 -0.0120 185 VAL A CG1 
1186 C CG2 . VAL A 142 ? 0.3348 0.3362 0.3459 0.0057  -0.0100 -0.0123 185 VAL A CG2 
1187 N N   . SER A 143 ? 0.2865 0.2968 0.2989 0.0059  -0.0075 -0.0084 186 SER A N   
1188 C CA  A SER A 143 ? 0.3449 0.3573 0.3571 0.0053  -0.0074 -0.0068 186 SER A CA  
1189 C CA  B SER A 143 ? 0.3359 0.3482 0.3481 0.0053  -0.0074 -0.0068 186 SER A CA  
1190 C C   . SER A 143 ? 0.3048 0.3203 0.3235 0.0049  -0.0084 -0.0046 186 SER A C   
1191 O O   . SER A 143 ? 0.3383 0.3548 0.3579 0.0037  -0.0102 -0.0038 186 SER A O   
1192 C CB  A SER A 143 ? 0.4013 0.4134 0.4101 0.0066  -0.0042 -0.0066 186 SER A CB  
1193 C CB  B SER A 143 ? 0.3662 0.3784 0.3751 0.0066  -0.0042 -0.0065 186 SER A CB  
1194 O OG  A SER A 143 ? 0.3572 0.3655 0.3593 0.0071  -0.0040 -0.0091 186 SER A OG  
1195 O OG  B SER A 143 ? 0.3546 0.3687 0.3682 0.0082  -0.0013 -0.0052 186 SER A OG  
1196 N N   . VAL A 144 ? 0.3180 0.3348 0.3416 0.0059  -0.0075 -0.0038 187 VAL A N   
1197 C CA  . VAL A 144 ? 0.2822 0.3015 0.3125 0.0055  -0.0093 -0.0019 187 VAL A CA  
1198 C C   . VAL A 144 ? 0.2819 0.3001 0.3115 0.0044  -0.0130 -0.0027 187 VAL A C   
1199 O O   . VAL A 144 ? 0.2861 0.3052 0.3183 0.0036  -0.0152 -0.0019 187 VAL A O   
1200 C CB  . VAL A 144 ? 0.2964 0.3172 0.3327 0.0069  -0.0082 -0.0008 187 VAL A CB  
1201 C CG1 . VAL A 144 ? 0.3076 0.3305 0.3510 0.0062  -0.0114 0.0009  187 VAL A CG1 
1202 C CG2 . VAL A 144 ? 0.3325 0.3550 0.3702 0.0082  -0.0037 0.0004  187 VAL A CG2 
1203 N N   . PHE A 145 ? 0.2962 0.3120 0.3222 0.0047  -0.0136 -0.0044 188 PHE A N   
1204 C CA  . PHE A 145 ? 0.2586 0.2732 0.2830 0.0041  -0.0163 -0.0050 188 PHE A CA  
1205 C C   . PHE A 145 ? 0.2846 0.2993 0.3073 0.0030  -0.0172 -0.0053 188 PHE A C   
1206 O O   . PHE A 145 ? 0.2648 0.2797 0.2887 0.0027  -0.0194 -0.0051 188 PHE A O   
1207 C CB  . PHE A 145 ? 0.2655 0.2776 0.2865 0.0045  -0.0159 -0.0061 188 PHE A CB  
1208 C CG  . PHE A 145 ? 0.2439 0.2548 0.2624 0.0041  -0.0175 -0.0066 188 PHE A CG  
1209 C CD1 . PHE A 145 ? 0.2715 0.2816 0.2899 0.0048  -0.0192 -0.0061 188 PHE A CD1 
1210 C CD2 . PHE A 145 ? 0.2762 0.2866 0.2923 0.0032  -0.0171 -0.0073 188 PHE A CD2 
1211 C CE1 . PHE A 145 ? 0.2963 0.3050 0.3113 0.0050  -0.0200 -0.0065 188 PHE A CE1 
1212 C CE2 . PHE A 145 ? 0.3056 0.3152 0.3201 0.0032  -0.0178 -0.0075 188 PHE A CE2 
1213 C CZ  . PHE A 145 ? 0.2904 0.2991 0.3039 0.0042  -0.0189 -0.0071 188 PHE A CZ  
1214 N N   . TRP A 146 ? 0.3013 0.3156 0.3209 0.0025  -0.0159 -0.0059 189 TRP A N   
1215 C CA  . TRP A 146 ? 0.2957 0.3100 0.3139 0.0016  -0.0171 -0.0061 189 TRP A CA  
1216 C C   . TRP A 146 ? 0.3179 0.3338 0.3389 0.0011  -0.0177 -0.0046 189 TRP A C   
1217 O O   . TRP A 146 ? 0.3373 0.3531 0.3591 0.0006  -0.0195 -0.0046 189 TRP A O   
1218 C CB  . TRP A 146 ? 0.3365 0.3496 0.3510 0.0012  -0.0163 -0.0070 189 TRP A CB  
1219 C CG  . TRP A 146 ? 0.3327 0.3441 0.3459 0.0011  -0.0164 -0.0083 189 TRP A CG  
1220 C CD1 . TRP A 146 ? 0.3693 0.3791 0.3811 0.0014  -0.0154 -0.0092 189 TRP A CD1 
1221 C CD2 . TRP A 146 ? 0.3254 0.3366 0.3392 0.0008  -0.0173 -0.0085 189 TRP A CD2 
1222 N NE1 . TRP A 146 ? 0.3440 0.3526 0.3560 0.0011  -0.0158 -0.0096 189 TRP A NE1 
1223 C CE2 . TRP A 146 ? 0.3453 0.3550 0.3584 0.0008  -0.0167 -0.0091 189 TRP A CE2 
1224 C CE3 . TRP A 146 ? 0.3512 0.3632 0.3660 0.0008  -0.0184 -0.0082 189 TRP A CE3 
1225 C CZ2 . TRP A 146 ? 0.3261 0.3355 0.3400 0.0006  -0.0167 -0.0089 189 TRP A CZ2 
1226 C CZ3 . TRP A 146 ? 0.3316 0.3430 0.3463 0.0010  -0.0182 -0.0084 189 TRP A CZ3 
1227 C CH2 . TRP A 146 ? 0.3510 0.3614 0.3655 0.0009  -0.0172 -0.0085 189 TRP A CH2 
1228 N N   . LYS A 147 ? 0.3052 0.3225 0.3280 0.0014  -0.0160 -0.0032 190 LYS A N   
1229 C CA  . LYS A 147 ? 0.3182 0.3372 0.3448 0.0008  -0.0164 -0.0011 190 LYS A CA  
1230 C C   . LYS A 147 ? 0.3023 0.3216 0.3341 0.0005  -0.0191 -0.0007 190 LYS A C   
1231 O O   . LYS A 147 ? 0.3074 0.3269 0.3420 -0.0002 -0.0209 0.0001  190 LYS A O   
1232 C CB  . LYS A 147 ? 0.3737 0.3943 0.4015 0.0013  -0.0132 0.0009  190 LYS A CB  
1233 C CG  . LYS A 147 ? 0.3673 0.3899 0.4014 0.0019  -0.0123 0.0022  190 LYS A CG  
1234 C CD  . LYS A 147 ? 0.4081 0.4325 0.4431 0.0029  -0.0081 0.0043  190 LYS A CD  
1235 C CE  . LYS A 147 ? 0.4515 0.4782 0.4939 0.0038  -0.0068 0.0056  190 LYS A CE  
1236 N NZ  . LYS A 147 ? 0.4892 0.5176 0.5321 0.0053  -0.0017 0.0075  190 LYS A NZ  
1237 N N   . THR A 148 ? 0.3069 0.3258 0.3398 0.0012  -0.0198 -0.0015 191 THR A N   
1238 C CA  . THR A 148 ? 0.3215 0.3400 0.3580 0.0012  -0.0231 -0.0016 191 THR A CA  
1239 C C   . THR A 148 ? 0.3503 0.3663 0.3830 0.0012  -0.0255 -0.0035 191 THR A C   
1240 O O   . THR A 148 ? 0.3086 0.3237 0.3433 0.0008  -0.0281 -0.0036 191 THR A O   
1241 C CB  . THR A 148 ? 0.3538 0.3724 0.3920 0.0021  -0.0235 -0.0017 191 THR A CB  
1242 O OG1 . THR A 148 ? 0.3558 0.3768 0.3982 0.0025  -0.0208 0.0001  191 THR A OG1 
1243 C CG2 . THR A 148 ? 0.3515 0.3692 0.3931 0.0021  -0.0279 -0.0018 191 THR A CG2 
1244 N N   . VAL A 149 ? 0.3020 0.3165 0.3293 0.0018  -0.0244 -0.0050 192 VAL A N   
1245 C CA  A VAL A 149 ? 0.3492 0.3616 0.3729 0.0022  -0.0258 -0.0066 192 VAL A CA  
1246 C CA  B VAL A 149 ? 0.3506 0.3631 0.3744 0.0022  -0.0258 -0.0066 192 VAL A CA  
1247 C C   . VAL A 149 ? 0.3236 0.3363 0.3476 0.0015  -0.0258 -0.0066 192 VAL A C   
1248 O O   . VAL A 149 ? 0.3387 0.3498 0.3622 0.0019  -0.0275 -0.0076 192 VAL A O   
1249 C CB  A VAL A 149 ? 0.3795 0.3908 0.3988 0.0029  -0.0241 -0.0074 192 VAL A CB  
1250 C CB  B VAL A 149 ? 0.3680 0.3794 0.3873 0.0029  -0.0241 -0.0074 192 VAL A CB  
1251 C CG1 A VAL A 149 ? 0.3392 0.3513 0.3573 0.0023  -0.0219 -0.0074 192 VAL A CG1 
1252 C CG1 B VAL A 149 ? 0.4136 0.4229 0.4294 0.0038  -0.0248 -0.0087 192 VAL A CG1 
1253 C CG2 A VAL A 149 ? 0.4263 0.4352 0.4419 0.0040  -0.0253 -0.0086 192 VAL A CG2 
1254 C CG2 B VAL A 149 ? 0.3641 0.3752 0.3836 0.0036  -0.0241 -0.0070 192 VAL A CG2 
1255 N N   . SER A 150 ? 0.3123 0.3265 0.3366 0.0008  -0.0240 -0.0056 193 SER A N   
1256 C CA  A SER A 150 ? 0.3208 0.3351 0.3454 0.0001  -0.0244 -0.0052 193 SER A CA  
1257 C CA  B SER A 150 ? 0.3248 0.3391 0.3494 0.0001  -0.0244 -0.0052 193 SER A CA  
1258 C C   . SER A 150 ? 0.3133 0.3277 0.3422 -0.0003 -0.0264 -0.0041 193 SER A C   
1259 O O   . SER A 150 ? 0.2964 0.3096 0.3260 -0.0003 -0.0279 -0.0046 193 SER A O   
1260 C CB  A SER A 150 ? 0.3288 0.3444 0.3520 -0.0005 -0.0225 -0.0041 193 SER A CB  
1261 C CB  B SER A 150 ? 0.3479 0.3634 0.3710 -0.0005 -0.0225 -0.0041 193 SER A CB  
1262 O OG  A SER A 150 ? 0.3452 0.3601 0.3649 -0.0002 -0.0213 -0.0053 193 SER A OG  
1263 O OG  B SER A 150 ? 0.3371 0.3526 0.3604 -0.0010 -0.0234 -0.0035 193 SER A OG  
1264 N N   . ARG A 151 ? 0.3270 0.3426 0.3597 -0.0007 -0.0263 -0.0025 194 ARG A N   
1265 C CA  . ARG A 151 ? 0.3077 0.3233 0.3460 -0.0015 -0.0285 -0.0011 194 ARG A CA  
1266 C C   . ARG A 151 ? 0.3476 0.3605 0.3863 -0.0010 -0.0320 -0.0033 194 ARG A C   
1267 O O   . ARG A 151 ? 0.3038 0.3150 0.3445 -0.0012 -0.0342 -0.0035 194 ARG A O   
1268 C CB  . ARG A 151 ? 0.3483 0.3662 0.3919 -0.0020 -0.0275 0.0012  194 ARG A CB  
1269 C CG  . ARG A 151 ? 0.4044 0.4225 0.4557 -0.0030 -0.0300 0.0031  194 ARG A CG  
1270 C CD  . ARG A 151 ? 0.4353 0.4567 0.4932 -0.0035 -0.0280 0.0063  194 ARG A CD  
1271 N NE  . ARG A 151 ? 0.5546 0.5768 0.6154 -0.0030 -0.0289 0.0057  194 ARG A NE  
1272 C CZ  . ARG A 151 ? 0.6731 0.6945 0.7397 -0.0034 -0.0331 0.0055  194 ARG A CZ  
1273 N NH1 . ARG A 151 ? 0.6502 0.6695 0.7202 -0.0044 -0.0368 0.0053  194 ARG A NH1 
1274 N NH2 . ARG A 151 ? 0.7535 0.7757 0.8224 -0.0028 -0.0341 0.0052  194 ARG A NH2 
1275 N N   . ARG A 152 ? 0.3428 0.3545 0.3787 0.0000  -0.0327 -0.0050 195 ARG A N   
1276 C CA  . ARG A 152 ? 0.3567 0.3651 0.3909 0.0010  -0.0361 -0.0073 195 ARG A CA  
1277 C C   . ARG A 152 ? 0.3223 0.3284 0.3521 0.0019  -0.0358 -0.0091 195 ARG A C   
1278 O O   . ARG A 152 ? 0.3416 0.3448 0.3715 0.0025  -0.0385 -0.0107 195 ARG A O   
1279 C CB  . ARG A 152 ? 0.3529 0.3604 0.3836 0.0020  -0.0365 -0.0083 195 ARG A CB  
1280 C CG  . ARG A 152 ? 0.4409 0.4504 0.4770 0.0014  -0.0373 -0.0065 195 ARG A CG  
1281 C CD  . ARG A 152 ? 0.5718 0.5796 0.6129 0.0010  -0.0423 -0.0068 195 ARG A CD  
1282 N NE  . ARG A 152 ? 0.6356 0.6394 0.6710 0.0025  -0.0457 -0.0094 195 ARG A NE  
1283 C CZ  . ARG A 152 ? 0.6081 0.6113 0.6426 0.0032  -0.0475 -0.0094 195 ARG A CZ  
1284 N NH1 . ARG A 152 ? 0.5882 0.5950 0.6283 0.0026  -0.0461 -0.0070 195 ARG A NH1 
1285 N NH2 . ARG A 152 ? 0.6161 0.6151 0.6436 0.0047  -0.0506 -0.0117 195 ARG A NH2 
1286 N N   . PHE A 153 ? 0.3043 0.3117 0.3309 0.0022  -0.0326 -0.0091 196 PHE A N   
1287 C CA  . PHE A 153 ? 0.2970 0.3032 0.3211 0.0031  -0.0319 -0.0104 196 PHE A CA  
1288 C C   . PHE A 153 ? 0.3550 0.3610 0.3832 0.0025  -0.0333 -0.0097 196 PHE A C   
1289 O O   . PHE A 153 ? 0.3424 0.3458 0.3701 0.0036  -0.0346 -0.0113 196 PHE A O   
1290 C CB  . PHE A 153 ? 0.3270 0.3352 0.3489 0.0031  -0.0287 -0.0099 196 PHE A CB  
1291 C CG  . PHE A 153 ? 0.3046 0.3120 0.3245 0.0043  -0.0275 -0.0111 196 PHE A CG  
1292 C CD1 . PHE A 153 ? 0.3010 0.3059 0.3169 0.0062  -0.0273 -0.0128 196 PHE A CD1 
1293 C CD2 . PHE A 153 ? 0.2955 0.3046 0.3175 0.0038  -0.0264 -0.0103 196 PHE A CD2 
1294 C CE1 . PHE A 153 ? 0.3068 0.3113 0.3213 0.0077  -0.0253 -0.0136 196 PHE A CE1 
1295 C CE2 . PHE A 153 ? 0.3116 0.3205 0.3333 0.0051  -0.0251 -0.0110 196 PHE A CE2 
1296 C CZ  . PHE A 153 ? 0.2869 0.2937 0.3052 0.0071  -0.0241 -0.0126 196 PHE A CZ  
1297 N N   . ALA A 154 ? 0.3154 0.3237 0.3471 0.0009  -0.0328 -0.0072 197 ALA A N   
1298 C CA  . ALA A 154 ? 0.3319 0.3400 0.3676 0.0002  -0.0340 -0.0059 197 ALA A CA  
1299 C C   . ALA A 154 ? 0.3415 0.3470 0.3811 0.0001  -0.0374 -0.0063 197 ALA A C   
1300 O O   . ALA A 154 ? 0.3197 0.3231 0.3615 0.0003  -0.0392 -0.0068 197 ALA A O   
1301 C CB  . ALA A 154 ? 0.3107 0.3216 0.3482 -0.0013 -0.0324 -0.0027 197 ALA A CB  
1302 N N   . GLU A 155 ? 0.3244 0.3299 0.3657 -0.0004 -0.0387 -0.0063 198 GLU A N   
1303 C CA  . GLU A 155 ? 0.3582 0.3610 0.4041 -0.0007 -0.0428 -0.0068 198 GLU A CA  
1304 C C   . GLU A 155 ? 0.3852 0.3832 0.4270 0.0011  -0.0454 -0.0107 198 GLU A C   
1305 O O   . GLU A 155 ? 0.3604 0.3550 0.4056 0.0010  -0.0492 -0.0117 198 GLU A O   
1306 C CB  . GLU A 155 ? 0.3385 0.3425 0.3874 -0.0015 -0.0440 -0.0060 198 GLU A CB  
1307 C CG  . GLU A 155 ? 0.3879 0.3961 0.4433 -0.0032 -0.0420 -0.0019 198 GLU A CG  
1308 C CD  . GLU A 155 ? 0.4280 0.4379 0.4869 -0.0036 -0.0426 -0.0010 198 GLU A CD  
1309 O OE1 . GLU A 155 ? 0.4175 0.4257 0.4725 -0.0024 -0.0443 -0.0035 198 GLU A OE1 
1310 O OE2 . GLU A 155 ? 0.4672 0.4803 0.5331 -0.0048 -0.0413 0.0024  198 GLU A OE2 
1311 N N   . ALA A 156 ? 0.3826 0.3799 0.4172 0.0030  -0.0433 -0.0128 199 ALA A N   
1312 C CA  . ALA A 156 ? 0.4127 0.4053 0.4420 0.0053  -0.0448 -0.0164 199 ALA A CA  
1313 C C   . ALA A 156 ? 0.3647 0.3561 0.3942 0.0064  -0.0437 -0.0173 199 ALA A C   
1314 O O   . ALA A 156 ? 0.3854 0.3725 0.4113 0.0086  -0.0449 -0.0204 199 ALA A O   
1315 C CB  . ALA A 156 ? 0.3906 0.3830 0.4123 0.0070  -0.0426 -0.0178 199 ALA A CB  
1316 N N   . ALA A 157 ? 0.3848 0.3797 0.4181 0.0052  -0.0415 -0.0147 200 ALA A N   
1317 C CA  . ALA A 157 ? 0.3684 0.3627 0.4026 0.0064  -0.0406 -0.0151 200 ALA A CA  
1318 C C   . ALA A 157 ? 0.3509 0.3412 0.3894 0.0065  -0.0441 -0.0159 200 ALA A C   
1319 O O   . ALA A 157 ? 0.3238 0.3132 0.3666 0.0049  -0.0471 -0.0148 200 ALA A O   
1320 C CB  . ALA A 157 ? 0.3614 0.3601 0.3984 0.0050  -0.0382 -0.0119 200 ALA A CB  
1321 N N   . CYS A 158 ? 0.3601 0.3482 0.3983 0.0086  -0.0436 -0.0176 201 CYS A N   
1322 C CA  . CYS A 158 ? 0.3909 0.3746 0.4331 0.0092  -0.0469 -0.0187 201 CYS A CA  
1323 C C   . CYS A 158 ? 0.3641 0.3484 0.4088 0.0106  -0.0451 -0.0183 201 CYS A C   
1324 O O   . CYS A 158 ? 0.3466 0.3341 0.3894 0.0115  -0.0415 -0.0178 201 CYS A O   
1325 C CB  . CYS A 158 ? 0.3602 0.3376 0.3975 0.0115  -0.0495 -0.0233 201 CYS A CB  
1326 S SG  . CYS A 158 ? 0.4746 0.4499 0.5037 0.0158  -0.0457 -0.0271 201 CYS A SG  
1327 N N   . ASP A 159 ? 0.3722 0.3532 0.4221 0.0107  -0.0479 -0.0183 202 ASP A N   
1328 C CA  . ASP A 159 ? 0.4031 0.3836 0.4565 0.0124  -0.0470 -0.0181 202 ASP A CA  
1329 C C   . ASP A 159 ? 0.3839 0.3704 0.4405 0.0107  -0.0450 -0.0138 202 ASP A C   
1330 O O   . ASP A 159 ? 0.3751 0.3633 0.4354 0.0080  -0.0464 -0.0102 202 ASP A O   
1331 C CB  . ASP A 159 ? 0.4212 0.3993 0.4693 0.0163  -0.0445 -0.0223 202 ASP A CB  
1332 C CG  . ASP A 159 ? 0.4877 0.4644 0.5402 0.0187  -0.0438 -0.0228 202 ASP A CG  
1333 O OD1 . ASP A 159 ? 0.4739 0.4485 0.5327 0.0179  -0.0469 -0.0215 202 ASP A OD1 
1334 O OD2 . ASP A 159 ? 0.5101 0.4881 0.5606 0.0214  -0.0400 -0.0241 202 ASP A OD2 
1335 N N   . VAL A 160 ? 0.3485 0.3380 0.4040 0.0121  -0.0418 -0.0138 203 VAL A N   
1336 C CA  . VAL A 160 ? 0.3361 0.3307 0.3943 0.0106  -0.0407 -0.0102 203 VAL A CA  
1337 C C   . VAL A 160 ? 0.3547 0.3530 0.4079 0.0096  -0.0381 -0.0100 203 VAL A C   
1338 O O   . VAL A 160 ? 0.3621 0.3603 0.4115 0.0114  -0.0356 -0.0125 203 VAL A O   
1339 C CB  . VAL A 160 ? 0.3805 0.3759 0.4430 0.0127  -0.0397 -0.0100 203 VAL A CB  
1340 C CG1 . VAL A 160 ? 0.3448 0.3451 0.4098 0.0109  -0.0396 -0.0063 203 VAL A CG1 
1341 C CG2 . VAL A 160 ? 0.4193 0.4104 0.4870 0.0139  -0.0424 -0.0104 203 VAL A CG2 
1342 N N   . VAL A 161 ? 0.3268 0.3280 0.3797 0.0070  -0.0384 -0.0070 204 VAL A N   
1343 C CA  . VAL A 161 ? 0.3334 0.3378 0.3821 0.0060  -0.0363 -0.0066 204 VAL A CA  
1344 C C   . VAL A 161 ? 0.3457 0.3535 0.3963 0.0052  -0.0360 -0.0043 204 VAL A C   
1345 O O   . VAL A 161 ? 0.3091 0.3172 0.3623 0.0041  -0.0379 -0.0016 204 VAL A O   
1346 C CB  . VAL A 161 ? 0.3519 0.3565 0.3983 0.0039  -0.0368 -0.0055 204 VAL A CB  
1347 C CG1 . VAL A 161 ? 0.3617 0.3691 0.4039 0.0032  -0.0345 -0.0056 204 VAL A CG1 
1348 C CG2 . VAL A 161 ? 0.4110 0.4121 0.4572 0.0045  -0.0383 -0.0075 204 VAL A CG2 
1349 N N   . HIS A 162 ? 0.3098 0.3199 0.3591 0.0056  -0.0338 -0.0051 205 HIS A N   
1350 C CA  . HIS A 162 ? 0.3221 0.3352 0.3735 0.0048  -0.0342 -0.0033 205 HIS A CA  
1351 C C   . HIS A 162 ? 0.3181 0.3328 0.3650 0.0029  -0.0336 -0.0026 205 HIS A C   
1352 O O   . HIS A 162 ? 0.3229 0.3372 0.3660 0.0029  -0.0318 -0.0040 205 HIS A O   
1353 C CB  . HIS A 162 ? 0.3156 0.3302 0.3706 0.0066  -0.0323 -0.0043 205 HIS A CB  
1354 C CG  . HIS A 162 ? 0.3778 0.3908 0.4374 0.0090  -0.0323 -0.0052 205 HIS A CG  
1355 N ND1 . HIS A 162 ? 0.3628 0.3727 0.4203 0.0111  -0.0308 -0.0079 205 HIS A ND1 
1356 C CD2 . HIS A 162 ? 0.3932 0.4068 0.4592 0.0097  -0.0340 -0.0038 205 HIS A CD2 
1357 C CE1 . HIS A 162 ? 0.3975 0.4060 0.4597 0.0132  -0.0312 -0.0084 205 HIS A CE1 
1358 N NE2 . HIS A 162 ? 0.3790 0.3899 0.4470 0.0124  -0.0330 -0.0058 205 HIS A NE2 
1359 N N   . VAL A 163 ? 0.3035 0.3195 0.3504 0.0016  -0.0355 -0.0005 206 VAL A N   
1360 C CA  . VAL A 163 ? 0.3090 0.3259 0.3512 0.0001  -0.0352 -0.0001 206 VAL A CA  
1361 C C   . VAL A 163 ? 0.3068 0.3254 0.3512 -0.0005 -0.0371 0.0007  206 VAL A C   
1362 O O   . VAL A 163 ? 0.2761 0.2948 0.3234 -0.0005 -0.0397 0.0025  206 VAL A O   
1363 C CB  . VAL A 163 ? 0.3047 0.3205 0.3425 -0.0011 -0.0358 0.0016  206 VAL A CB  
1364 C CG1 . VAL A 163 ? 0.3353 0.3507 0.3748 -0.0014 -0.0384 0.0043  206 VAL A CG1 
1365 C CG2 . VAL A 163 ? 0.3208 0.3370 0.3531 -0.0021 -0.0351 0.0014  206 VAL A CG2 
1366 N N   . MET A 164 ? 0.3135 0.3331 0.3569 -0.0010 -0.0362 -0.0004 207 MET A N   
1367 C CA  . MET A 164 ? 0.2911 0.3118 0.3363 -0.0020 -0.0387 0.0002  207 MET A CA  
1368 C C   . MET A 164 ? 0.3063 0.3255 0.3443 -0.0033 -0.0405 0.0007  207 MET A C   
1369 O O   . MET A 164 ? 0.3162 0.3343 0.3488 -0.0036 -0.0385 -0.0003 207 MET A O   
1370 C CB  . MET A 164 ? 0.3045 0.3268 0.3533 -0.0020 -0.0370 -0.0010 207 MET A CB  
1371 C CG  . MET A 164 ? 0.3394 0.3638 0.3965 -0.0006 -0.0357 -0.0009 207 MET A CG  
1372 S SD  . MET A 164 ? 0.3545 0.3813 0.4166 -0.0009 -0.0334 -0.0013 207 MET A SD  
1373 C CE  . MET A 164 ? 0.4019 0.4311 0.4730 0.0016  -0.0306 -0.0008 207 MET A CE  
1374 N N   . LEU A 165 ? 0.2901 0.3088 0.3276 -0.0039 -0.0443 0.0023  208 LEU A N   
1375 C CA  . LEU A 165 ? 0.3288 0.3454 0.3581 -0.0047 -0.0462 0.0027  208 LEU A CA  
1376 C C   . LEU A 165 ? 0.3700 0.3867 0.4005 -0.0057 -0.0502 0.0022  208 LEU A C   
1377 O O   . LEU A 165 ? 0.3388 0.3573 0.3772 -0.0057 -0.0524 0.0029  208 LEU A O   
1378 C CB  . LEU A 165 ? 0.3290 0.3444 0.3548 -0.0045 -0.0477 0.0055  208 LEU A CB  
1379 C CG  . LEU A 165 ? 0.3248 0.3400 0.3507 -0.0039 -0.0446 0.0065  208 LEU A CG  
1380 C CD1 . LEU A 165 ? 0.3287 0.3427 0.3526 -0.0038 -0.0464 0.0099  208 LEU A CD1 
1381 C CD2 . LEU A 165 ? 0.3648 0.3793 0.3852 -0.0040 -0.0411 0.0052  208 LEU A CD2 
1382 N N   . ASP A 166 ? 0.3473 0.3615 0.3700 -0.0063 -0.0511 0.0009  209 ASP A N   
1383 C CA  . ASP A 166 ? 0.4058 0.4190 0.4288 -0.0074 -0.0555 -0.0001 209 ASP A CA  
1384 C C   . ASP A 166 ? 0.3833 0.3944 0.4011 -0.0075 -0.0605 0.0015  209 ASP A C   
1385 O O   . ASP A 166 ? 0.3895 0.3974 0.3964 -0.0071 -0.0607 0.0016  209 ASP A O   
1386 C CB  . ASP A 166 ? 0.4234 0.4342 0.4404 -0.0079 -0.0542 -0.0028 209 ASP A CB  
1387 C CG  . ASP A 166 ? 0.5047 0.5137 0.5220 -0.0091 -0.0593 -0.0043 209 ASP A CG  
1388 O OD1 . ASP A 166 ? 0.4626 0.4730 0.4866 -0.0098 -0.0636 -0.0031 209 ASP A OD1 
1389 O OD2 . ASP A 166 ? 0.5249 0.5309 0.5362 -0.0095 -0.0592 -0.0067 209 ASP A OD2 
1390 N N   . GLY A 167 ? 0.3592 0.3721 0.3848 -0.0078 -0.0645 0.0031  210 GLY A N   
1391 C CA  . GLY A 167 ? 0.4067 0.4178 0.4283 -0.0077 -0.0699 0.0051  210 GLY A CA  
1392 C C   . GLY A 167 ? 0.4480 0.4559 0.4640 -0.0087 -0.0757 0.0036  210 GLY A C   
1393 O O   . GLY A 167 ? 0.4663 0.4719 0.4772 -0.0086 -0.0808 0.0052  210 GLY A O   
1394 N N   . SER A 168 ? 0.4444 0.4515 0.4607 -0.0096 -0.0754 0.0006  211 SER A N   
1395 C CA  . SER A 168 ? 0.5241 0.5272 0.5348 -0.0106 -0.0813 -0.0014 211 SER A CA  
1396 C C   . SER A 168 ? 0.5281 0.5258 0.5223 -0.0097 -0.0803 -0.0032 211 SER A C   
1397 O O   . SER A 168 ? 0.5451 0.5384 0.5322 -0.0102 -0.0852 -0.0054 211 SER A O   
1398 C CB  . SER A 168 ? 0.4698 0.4743 0.4900 -0.0121 -0.0817 -0.0037 211 SER A CB  
1399 O OG  . SER A 168 ? 0.5212 0.5254 0.5389 -0.0118 -0.0755 -0.0056 211 SER A OG  
1400 N N   . ARG A 169 ? 0.5738 0.5717 0.5621 -0.0084 -0.0741 -0.0023 212 ARG A N   
1401 C CA  . ARG A 169 ? 0.6764 0.6699 0.6503 -0.0072 -0.0716 -0.0037 212 ARG A CA  
1402 C C   . ARG A 169 ? 0.6784 0.6701 0.6426 -0.0059 -0.0716 -0.0006 212 ARG A C   
1403 O O   . ARG A 169 ? 0.6425 0.6369 0.6121 -0.0058 -0.0721 0.0028  212 ARG A O   
1404 C CB  . ARG A 169 ? 0.7952 0.7904 0.7705 -0.0067 -0.0642 -0.0048 212 ARG A CB  
1405 C CG  . ARG A 169 ? 0.8068 0.8023 0.7882 -0.0077 -0.0637 -0.0079 212 ARG A CG  
1406 C CD  . ARG A 169 ? 0.9813 0.9713 0.9521 -0.0073 -0.0648 -0.0114 212 ARG A CD  
1407 N NE  . ARG A 169 ? 1.0535 1.0426 1.0177 -0.0058 -0.0584 -0.0120 212 ARG A NE  
1408 C CZ  . ARG A 169 ? 1.0888 1.0790 1.0572 -0.0058 -0.0543 -0.0136 212 ARG A CZ  
1409 N NH1 . ARG A 169 ? 1.0298 1.0218 1.0084 -0.0073 -0.0555 -0.0145 212 ARG A NH1 
1410 N NH2 . ARG A 169 ? 1.0507 1.0402 1.0134 -0.0042 -0.0489 -0.0138 212 ARG A NH2 
1411 N N   . SER A 170 ? 0.7746 0.7615 0.7241 -0.0045 -0.0707 -0.0018 213 SER A N   
1412 C CA  . SER A 170 ? 0.8239 0.8085 0.7624 -0.0030 -0.0705 0.0015  213 SER A CA  
1413 C C   . SER A 170 ? 0.7824 0.7707 0.7246 -0.0024 -0.0638 0.0051  213 SER A C   
1414 O O   . SER A 170 ? 0.8108 0.7992 0.7503 -0.0018 -0.0641 0.0092  213 SER A O   
1415 C CB  . SER A 170 ? 0.9486 0.9270 0.8700 -0.0013 -0.0700 -0.0008 213 SER A CB  
1416 O OG  . SER A 170 ? 0.9708 0.9494 0.8912 -0.0006 -0.0636 -0.0032 213 SER A OG  
1417 N N   . LYS A 171 ? 0.7088 0.7001 0.6574 -0.0026 -0.0582 0.0038  214 LYS A N   
1418 C CA  . LYS A 171 ? 0.6320 0.6267 0.5857 -0.0022 -0.0525 0.0068  214 LYS A CA  
1419 C C   . LYS A 171 ? 0.5337 0.5329 0.5024 -0.0035 -0.0525 0.0063  214 LYS A C   
1420 O O   . LYS A 171 ? 0.5128 0.5136 0.4862 -0.0038 -0.0494 0.0040  214 LYS A O   
1421 C CB  . LYS A 171 ? 0.6029 0.5971 0.5512 -0.0011 -0.0461 0.0059  214 LYS A CB  
1422 C CG  . LYS A 171 ? 0.6668 0.6570 0.6003 0.0008  -0.0445 0.0071  214 LYS A CG  
1423 C CD  . LYS A 171 ? 0.6740 0.6643 0.6041 0.0022  -0.0375 0.0063  214 LYS A CD  
1424 C CE  . LYS A 171 ? 0.7722 0.7586 0.6874 0.0045  -0.0348 0.0079  214 LYS A CE  
1425 N NZ  . LYS A 171 ? 0.8511 0.8386 0.7649 0.0048  -0.0337 0.0137  214 LYS A NZ  
1426 N N   . ILE A 172 ? 0.4869 0.4878 0.4624 -0.0041 -0.0560 0.0086  215 ILE A N   
1427 C CA  . ILE A 172 ? 0.4522 0.4569 0.4410 -0.0048 -0.0557 0.0083  215 ILE A CA  
1428 C C   . ILE A 172 ? 0.4054 0.4122 0.3980 -0.0044 -0.0499 0.0087  215 ILE A C   
1429 O O   . ILE A 172 ? 0.4036 0.4124 0.4027 -0.0047 -0.0478 0.0065  215 ILE A O   
1430 C CB  . ILE A 172 ? 0.4197 0.4255 0.4149 -0.0049 -0.0598 0.0110  215 ILE A CB  
1431 C CG1 . ILE A 172 ? 0.4519 0.4556 0.4435 -0.0053 -0.0664 0.0107  215 ILE A CG1 
1432 C CG2 . ILE A 172 ? 0.3913 0.4009 0.3999 -0.0052 -0.0590 0.0103  215 ILE A CG2 
1433 C CD1 . ILE A 172 ? 0.4516 0.4566 0.4502 -0.0054 -0.0711 0.0136  215 ILE A CD1 
1434 N N   . PHE A 173 ? 0.4144 0.4206 0.4030 -0.0038 -0.0475 0.0116  216 PHE A N   
1435 C CA  . PHE A 173 ? 0.4309 0.4386 0.4216 -0.0036 -0.0423 0.0121  216 PHE A CA  
1436 C C   . PHE A 173 ? 0.4230 0.4287 0.4035 -0.0028 -0.0391 0.0118  216 PHE A C   
1437 O O   . PHE A 173 ? 0.4378 0.4412 0.4095 -0.0021 -0.0396 0.0139  216 PHE A O   
1438 C CB  . PHE A 173 ? 0.3811 0.3897 0.3765 -0.0036 -0.0415 0.0159  216 PHE A CB  
1439 C CG  . PHE A 173 ? 0.3935 0.4031 0.3899 -0.0034 -0.0367 0.0170  216 PHE A CG  
1440 C CD1 . PHE A 173 ? 0.3656 0.3769 0.3682 -0.0036 -0.0346 0.0146  216 PHE A CD1 
1441 C CD2 . PHE A 173 ? 0.4027 0.4115 0.3940 -0.0030 -0.0344 0.0208  216 PHE A CD2 
1442 C CE1 . PHE A 173 ? 0.3558 0.3680 0.3602 -0.0035 -0.0309 0.0157  216 PHE A CE1 
1443 C CE2 . PHE A 173 ? 0.4298 0.4400 0.4238 -0.0030 -0.0300 0.0221  216 PHE A CE2 
1444 C CZ  . PHE A 173 ? 0.3678 0.3798 0.3688 -0.0033 -0.0286 0.0195  216 PHE A CZ  
1445 N N   . ASP A 174 ? 0.4059 0.4125 0.3876 -0.0026 -0.0357 0.0094  217 ASP A N   
1446 C CA  . ASP A 174 ? 0.4302 0.4350 0.4034 -0.0016 -0.0322 0.0086  217 ASP A CA  
1447 C C   . ASP A 174 ? 0.4077 0.4150 0.3855 -0.0013 -0.0272 0.0100  217 ASP A C   
1448 O O   . ASP A 174 ? 0.4135 0.4226 0.3986 -0.0018 -0.0264 0.0082  217 ASP A O   
1449 C CB  . ASP A 174 ? 0.4488 0.4520 0.4194 -0.0016 -0.0332 0.0041  217 ASP A CB  
1450 C CG  . ASP A 174 ? 0.4650 0.4655 0.4259 -0.0001 -0.0301 0.0029  217 ASP A CG  
1451 O OD1 . ASP A 174 ? 0.4886 0.4888 0.4443 0.0011  -0.0268 0.0056  217 ASP A OD1 
1452 O OD2 . ASP A 174 ? 0.5745 0.5730 0.5331 0.0000  -0.0307 -0.0008 217 ASP A OD2 
1453 N N   . LYS A 175 ? 0.4182 0.4253 0.3919 -0.0004 -0.0240 0.0133  218 LYS A N   
1454 C CA  . LYS A 175 ? 0.4779 0.4875 0.4570 -0.0002 -0.0194 0.0150  218 LYS A CA  
1455 C C   . LYS A 175 ? 0.4828 0.4927 0.4616 0.0005  -0.0168 0.0117  218 LYS A C   
1456 O O   . LYS A 175 ? 0.4685 0.4808 0.4547 0.0003  -0.0146 0.0118  218 LYS A O   
1457 C CB  . LYS A 175 ? 0.5004 0.5098 0.4747 0.0008  -0.0157 0.0196  218 LYS A CB  
1458 C CG  . LYS A 175 ? 0.5286 0.5377 0.5037 0.0001  -0.0180 0.0238  218 LYS A CG  
1459 C CD  . LYS A 175 ? 0.6417 0.6511 0.6132 0.0010  -0.0135 0.0290  218 LYS A CD  
1460 C CE  . LYS A 175 ? 0.7475 0.7536 0.7041 0.0031  -0.0116 0.0288  218 LYS A CE  
1461 N NZ  . LYS A 175 ? 0.8715 0.8779 0.8241 0.0044  -0.0063 0.0344  218 LYS A NZ  
1462 N N   . ASP A 176 ? 0.4876 0.4945 0.4580 0.0013  -0.0174 0.0086  219 ASP A N   
1463 C CA  . ASP A 176 ? 0.5181 0.5245 0.4874 0.0022  -0.0150 0.0054  219 ASP A CA  
1464 C C   . ASP A 176 ? 0.4975 0.5041 0.4725 0.0011  -0.0180 0.0020  219 ASP A C   
1465 O O   . ASP A 176 ? 0.5248 0.5289 0.4959 0.0012  -0.0197 -0.0013 219 ASP A O   
1466 C CB  . ASP A 176 ? 0.5957 0.5979 0.5527 0.0040  -0.0141 0.0037  219 ASP A CB  
1467 C CG  . ASP A 176 ? 0.7350 0.7365 0.6906 0.0055  -0.0104 0.0011  219 ASP A CG  
1468 O OD1 . ASP A 176 ? 0.6899 0.6946 0.6541 0.0053  -0.0079 0.0017  219 ASP A OD1 
1469 O OD2 . ASP A 176 ? 0.8431 0.8403 0.7890 0.0069  -0.0104 -0.0017 219 ASP A OD2 
1470 N N   . SER A 177 ? 0.3996 0.4091 0.3839 0.0000  -0.0187 0.0029  220 SER A N   
1471 C CA  . SER A 177 ? 0.3984 0.4085 0.3882 -0.0009 -0.0208 0.0003  220 SER A CA  
1472 C C   . SER A 177 ? 0.4070 0.4198 0.4050 -0.0012 -0.0195 0.0013  220 SER A C   
1473 O O   . SER A 177 ? 0.3971 0.4114 0.3979 -0.0012 -0.0180 0.0040  220 SER A O   
1474 C CB  . SER A 177 ? 0.4105 0.4201 0.4014 -0.0019 -0.0251 -0.0001 220 SER A CB  
1475 O OG  . SER A 177 ? 0.3769 0.3881 0.3725 -0.0024 -0.0261 0.0025  220 SER A OG  
1476 N N   . THR A 178 ? 0.3874 0.4005 0.3892 -0.0015 -0.0204 -0.0009 221 THR A N   
1477 C CA  . THR A 178 ? 0.3866 0.4015 0.3949 -0.0016 -0.0199 -0.0005 221 THR A CA  
1478 C C   . THR A 178 ? 0.3793 0.3949 0.3916 -0.0022 -0.0218 0.0013  221 THR A C   
1479 O O   . THR A 178 ? 0.2983 0.3150 0.3150 -0.0023 -0.0213 0.0029  221 THR A O   
1480 C CB  . THR A 178 ? 0.3851 0.3997 0.3953 -0.0016 -0.0206 -0.0030 221 THR A CB  
1481 O OG1 . THR A 178 ? 0.4576 0.4707 0.4639 -0.0013 -0.0197 -0.0047 221 THR A OG1 
1482 C CG2 . THR A 178 ? 0.4028 0.4184 0.4174 -0.0013 -0.0199 -0.0029 221 THR A CG2 
1483 N N   . PHE A 179 ? 0.3336 0.3487 0.3455 -0.0026 -0.0242 0.0011  222 PHE A N   
1484 C CA  . PHE A 179 ? 0.3432 0.3587 0.3591 -0.0030 -0.0260 0.0028  222 PHE A CA  
1485 C C   . PHE A 179 ? 0.3557 0.3713 0.3709 -0.0031 -0.0252 0.0061  222 PHE A C   
1486 O O   . PHE A 179 ? 0.3010 0.3172 0.3213 -0.0034 -0.0252 0.0078  222 PHE A O   
1487 C CB  . PHE A 179 ? 0.3204 0.3353 0.3363 -0.0032 -0.0286 0.0022  222 PHE A CB  
1488 C CG  . PHE A 179 ? 0.3218 0.3368 0.3417 -0.0033 -0.0306 0.0041  222 PHE A CG  
1489 C CD1 . PHE A 179 ? 0.3251 0.3403 0.3506 -0.0030 -0.0310 0.0035  222 PHE A CD1 
1490 C CD2 . PHE A 179 ? 0.3196 0.3340 0.3373 -0.0036 -0.0322 0.0065  222 PHE A CD2 
1491 C CE1 . PHE A 179 ? 0.3370 0.3516 0.3664 -0.0029 -0.0329 0.0050  222 PHE A CE1 
1492 C CE2 . PHE A 179 ? 0.3559 0.3702 0.3778 -0.0036 -0.0341 0.0085  222 PHE A CE2 
1493 C CZ  . PHE A 179 ? 0.3738 0.3881 0.4020 -0.0033 -0.0344 0.0076  222 PHE A CZ  
1494 N N   . GLY A 180 ? 0.3443 0.3592 0.3531 -0.0029 -0.0243 0.0072  223 GLY A N   
1495 C CA  . GLY A 180 ? 0.3189 0.3338 0.3262 -0.0029 -0.0232 0.0110  223 GLY A CA  
1496 C C   . GLY A 180 ? 0.3272 0.3436 0.3373 -0.0027 -0.0197 0.0129  223 GLY A C   
1497 O O   . GLY A 180 ? 0.3899 0.4070 0.4028 -0.0030 -0.0189 0.0166  223 GLY A O   
1498 N N   . SER A 181 ? 0.3234 0.3405 0.3338 -0.0022 -0.0177 0.0108  224 SER A N   
1499 C CA  . SER A 181 ? 0.3464 0.3653 0.3601 -0.0018 -0.0142 0.0127  224 SER A CA  
1500 C C   . SER A 181 ? 0.3596 0.3799 0.3814 -0.0022 -0.0151 0.0116  224 SER A C   
1501 O O   . SER A 181 ? 0.3244 0.3465 0.3513 -0.0022 -0.0129 0.0136  224 SER A O   
1502 C CB  . SER A 181 ? 0.3730 0.3913 0.3800 -0.0004 -0.0108 0.0116  224 SER A CB  
1503 O OG  . SER A 181 ? 0.4283 0.4453 0.4274 0.0004  -0.0093 0.0134  224 SER A OG  
1504 N N   . VAL A 182 ? 0.3447 0.3640 0.3679 -0.0026 -0.0180 0.0087  225 VAL A N   
1505 C CA  . VAL A 182 ? 0.3307 0.3505 0.3601 -0.0028 -0.0193 0.0076  225 VAL A CA  
1506 C C   . VAL A 182 ? 0.3014 0.3200 0.3342 -0.0034 -0.0228 0.0069  225 VAL A C   
1507 O O   . VAL A 182 ? 0.3234 0.3421 0.3622 -0.0040 -0.0242 0.0083  225 VAL A O   
1508 C CB  . VAL A 182 ? 0.3151 0.3345 0.3421 -0.0020 -0.0190 0.0044  225 VAL A CB  
1509 C CG1 . VAL A 182 ? 0.3297 0.3491 0.3617 -0.0020 -0.0208 0.0034  225 VAL A CG1 
1510 C CG2 . VAL A 182 ? 0.3291 0.3492 0.3530 -0.0012 -0.0156 0.0048  225 VAL A CG2 
1511 N N   . GLU A 183 ? 0.3007 0.3180 0.3302 -0.0031 -0.0242 0.0049  226 GLU A N   
1512 C CA  . GLU A 183 ? 0.3111 0.3271 0.3436 -0.0030 -0.0269 0.0035  226 GLU A CA  
1513 C C   . GLU A 183 ? 0.3116 0.3271 0.3480 -0.0037 -0.0285 0.0060  226 GLU A C   
1514 O O   . GLU A 183 ? 0.3055 0.3198 0.3468 -0.0038 -0.0305 0.0057  226 GLU A O   
1515 C CB  . GLU A 183 ? 0.2807 0.2960 0.3098 -0.0025 -0.0274 0.0013  226 GLU A CB  
1516 C CG  . GLU A 183 ? 0.3487 0.3641 0.3746 -0.0020 -0.0260 -0.0009 226 GLU A CG  
1517 C CD  . GLU A 183 ? 0.3680 0.3833 0.3918 -0.0018 -0.0262 -0.0023 226 GLU A CD  
1518 O OE1 . GLU A 183 ? 0.3443 0.3596 0.3689 -0.0020 -0.0276 -0.0016 226 GLU A OE1 
1519 O OE2 . GLU A 183 ? 0.3778 0.3930 0.3999 -0.0014 -0.0252 -0.0039 226 GLU A OE2 
1520 N N   . VAL A 184 ? 0.2897 0.3056 0.3238 -0.0040 -0.0280 0.0084  227 VAL A N   
1521 C CA  . VAL A 184 ? 0.3148 0.3299 0.3525 -0.0045 -0.0296 0.0110  227 VAL A CA  
1522 C C   . VAL A 184 ? 0.3092 0.3246 0.3530 -0.0054 -0.0295 0.0137  227 VAL A C   
1523 O O   . VAL A 184 ? 0.3090 0.3230 0.3581 -0.0059 -0.0317 0.0150  227 VAL A O   
1524 C CB  . VAL A 184 ? 0.3112 0.3264 0.3440 -0.0046 -0.0292 0.0135  227 VAL A CB  
1525 C CG1 . VAL A 184 ? 0.3573 0.3737 0.3866 -0.0047 -0.0259 0.0162  227 VAL A CG1 
1526 C CG2 . VAL A 184 ? 0.3192 0.3332 0.3556 -0.0050 -0.0315 0.0162  227 VAL A CG2 
1527 N N   . HIS A 185 ? 0.3221 0.3392 0.3663 -0.0055 -0.0270 0.0146  228 HIS A N   
1528 C CA  . HIS A 185 ? 0.3537 0.3719 0.4053 -0.0065 -0.0266 0.0177  228 HIS A CA  
1529 C C   . HIS A 185 ? 0.3435 0.3609 0.4008 -0.0067 -0.0291 0.0153  228 HIS A C   
1530 O O   . HIS A 185 ? 0.3343 0.3525 0.3992 -0.0077 -0.0296 0.0176  228 HIS A O   
1531 C CB  . HIS A 185 ? 0.3398 0.3605 0.3897 -0.0063 -0.0223 0.0204  228 HIS A CB  
1532 C CG  . HIS A 185 ? 0.3541 0.3748 0.3963 -0.0058 -0.0199 0.0224  228 HIS A CG  
1533 N ND1 . HIS A 185 ? 0.3642 0.3845 0.4070 -0.0063 -0.0199 0.0265  228 HIS A ND1 
1534 C CD2 . HIS A 185 ? 0.3617 0.3822 0.3950 -0.0047 -0.0181 0.0208  228 HIS A CD2 
1535 C CE1 . HIS A 185 ? 0.3694 0.3892 0.4032 -0.0054 -0.0181 0.0273  228 HIS A CE1 
1536 N NE2 . HIS A 185 ? 0.4110 0.4309 0.4390 -0.0045 -0.0172 0.0237  228 HIS A NE2 
1537 N N   . ASN A 186 ? 0.3187 0.3346 0.3726 -0.0058 -0.0307 0.0109  229 ASN A N   
1538 C CA  . ASN A 186 ? 0.3370 0.3515 0.3943 -0.0057 -0.0334 0.0084  229 ASN A CA  
1539 C C   . ASN A 186 ? 0.3288 0.3397 0.3851 -0.0049 -0.0367 0.0051  229 ASN A C   
1540 O O   . ASN A 186 ? 0.3374 0.3462 0.3944 -0.0044 -0.0392 0.0024  229 ASN A O   
1541 C CB  . ASN A 186 ? 0.3515 0.3672 0.4052 -0.0049 -0.0318 0.0065  229 ASN A CB  
1542 C CG  . ASN A 186 ? 0.3650 0.3839 0.4220 -0.0053 -0.0290 0.0094  229 ASN A CG  
1543 O OD1 . ASN A 186 ? 0.3464 0.3662 0.4109 -0.0061 -0.0302 0.0109  229 ASN A OD1 
1544 N ND2 . ASN A 186 ? 0.3512 0.3718 0.4031 -0.0048 -0.0252 0.0103  229 ASN A ND2 
1545 N N   . LEU A 187 ? 0.3086 0.3186 0.3632 -0.0046 -0.0368 0.0053  230 LEU A N   
1546 C CA  . LEU A 187 ? 0.3428 0.3492 0.3986 -0.0038 -0.0397 0.0030  230 LEU A CA  
1547 C C   . LEU A 187 ? 0.3342 0.3386 0.3976 -0.0049 -0.0428 0.0044  230 LEU A C   
1548 O O   . LEU A 187 ? 0.3560 0.3618 0.4243 -0.0063 -0.0423 0.0085  230 LEU A O   
1549 C CB  . LEU A 187 ? 0.3445 0.3508 0.3985 -0.0032 -0.0392 0.0036  230 LEU A CB  
1550 C CG  . LEU A 187 ? 0.3014 0.3097 0.3493 -0.0024 -0.0368 0.0025  230 LEU A CG  
1551 C CD1 . LEU A 187 ? 0.3442 0.3527 0.3921 -0.0023 -0.0370 0.0041  230 LEU A CD1 
1552 C CD2 . LEU A 187 ? 0.2920 0.2989 0.3367 -0.0008 -0.0368 -0.0016 230 LEU A CD2 
1553 N N   . GLN A 188 ? 0.2927 0.2935 0.3572 -0.0041 -0.0461 0.0010  231 GLN A N   
1554 C CA  . GLN A 188 ? 0.3812 0.3795 0.4536 -0.0054 -0.0499 0.0019  231 GLN A CA  
1555 C C   . GLN A 188 ? 0.3421 0.3372 0.4180 -0.0052 -0.0519 0.0023  231 GLN A C   
1556 O O   . GLN A 188 ? 0.3312 0.3230 0.4032 -0.0033 -0.0529 -0.0012 231 GLN A O   
1557 C CB  . GLN A 188 ? 0.3532 0.3481 0.4244 -0.0045 -0.0535 -0.0023 231 GLN A CB  
1558 C CG  . GLN A 188 ? 0.3593 0.3571 0.4285 -0.0047 -0.0522 -0.0023 231 GLN A CG  
1559 C CD  . GLN A 188 ? 0.4007 0.3950 0.4709 -0.0044 -0.0570 -0.0053 231 GLN A CD  
1560 O OE1 . GLN A 188 ? 0.4346 0.4269 0.5126 -0.0058 -0.0611 -0.0045 231 GLN A OE1 
1561 N NE2 . GLN A 188 ? 0.3834 0.3766 0.4456 -0.0027 -0.0568 -0.0085 231 GLN A NE2 
1562 N N   . PRO A 189 ? 0.3701 0.3660 0.4534 -0.0071 -0.0523 0.0069  232 PRO A N   
1563 C CA  . PRO A 189 ? 0.3982 0.3907 0.4853 -0.0069 -0.0544 0.0076  232 PRO A CA  
1564 C C   . PRO A 189 ? 0.4377 0.4240 0.5269 -0.0059 -0.0593 0.0032  232 PRO A C   
1565 O O   . PRO A 189 ? 0.4161 0.3988 0.5056 -0.0047 -0.0607 0.0017  232 PRO A O   
1566 C CB  . PRO A 189 ? 0.3817 0.3761 0.4770 -0.0094 -0.0540 0.0138  232 PRO A CB  
1567 C CG  . PRO A 189 ? 0.4032 0.4031 0.4962 -0.0102 -0.0498 0.0166  232 PRO A CG  
1568 C CD  . PRO A 189 ? 0.3701 0.3701 0.4584 -0.0092 -0.0501 0.0120  232 PRO A CD  
1569 N N   . GLU A 190 ? 0.4376 0.4222 0.5281 -0.0063 -0.0621 0.0008  233 GLU A N   
1570 C CA  . GLU A 190 ? 0.5746 0.5523 0.6655 -0.0051 -0.0672 -0.0040 233 GLU A CA  
1571 C C   . GLU A 190 ? 0.5617 0.5367 0.6425 -0.0018 -0.0663 -0.0094 233 GLU A C   
1572 O O   . GLU A 190 ? 0.5996 0.5683 0.6794 0.0000  -0.0695 -0.0134 233 GLU A O   
1573 C CB  . GLU A 190 ? 0.6501 0.6267 0.7440 -0.0063 -0.0710 -0.0053 233 GLU A CB  
1574 C CG  . GLU A 190 ? 0.7480 0.7267 0.8546 -0.0096 -0.0727 -0.0002 233 GLU A CG  
1575 C CD  . GLU A 190 ? 0.7971 0.7834 0.9056 -0.0112 -0.0672 0.0055  233 GLU A CD  
1576 O OE1 . GLU A 190 ? 0.6044 0.5942 0.7047 -0.0099 -0.0633 0.0047  233 GLU A OE1 
1577 O OE2 . GLU A 190 ? 0.8207 0.8092 0.9388 -0.0135 -0.0666 0.0110  233 GLU A OE2 
1578 N N   . LYS A 191 ? 0.4185 0.3977 0.4919 -0.0007 -0.0617 -0.0095 234 LYS A N   
1579 C CA  . LYS A 191 ? 0.3968 0.3741 0.4612 0.0024  -0.0600 -0.0139 234 LYS A CA  
1580 C C   . LYS A 191 ? 0.3691 0.3492 0.4319 0.0035  -0.0562 -0.0126 234 LYS A C   
1581 O O   . LYS A 191 ? 0.3495 0.3269 0.4087 0.0062  -0.0555 -0.0158 234 LYS A O   
1582 C CB  . LYS A 191 ? 0.4073 0.3869 0.4648 0.0029  -0.0583 -0.0154 234 LYS A CB  
1583 C CG  . LYS A 191 ? 0.4674 0.4451 0.5267 0.0017  -0.0623 -0.0163 234 LYS A CG  
1584 C CD  . LYS A 191 ? 0.4534 0.4345 0.5073 0.0019  -0.0601 -0.0163 234 LYS A CD  
1585 C CE  . LYS A 191 ? 0.4753 0.4544 0.5185 0.0050  -0.0580 -0.0202 234 LYS A CE  
1586 N NZ  . LYS A 191 ? 0.4348 0.4161 0.4730 0.0051  -0.0567 -0.0203 234 LYS A NZ  
1587 N N   . VAL A 192 ? 0.3841 0.3694 0.4493 0.0016  -0.0536 -0.0080 235 VAL A N   
1588 C CA  . VAL A 192 ? 0.3892 0.3774 0.4529 0.0023  -0.0506 -0.0065 235 VAL A CA  
1589 C C   . VAL A 192 ? 0.3655 0.3524 0.4358 0.0017  -0.0523 -0.0037 235 VAL A C   
1590 O O   . VAL A 192 ? 0.3708 0.3583 0.4464 -0.0005 -0.0535 0.0001  235 VAL A O   
1591 C CB  . VAL A 192 ? 0.3640 0.3579 0.4250 0.0009  -0.0473 -0.0036 235 VAL A CB  
1592 C CG1 . VAL A 192 ? 0.3001 0.2964 0.3595 0.0016  -0.0451 -0.0023 235 VAL A CG1 
1593 C CG2 . VAL A 192 ? 0.3583 0.3531 0.4135 0.0014  -0.0459 -0.0061 235 VAL A CG2 
1594 N N   . GLN A 193 ? 0.3662 0.3514 0.4366 0.0039  -0.0521 -0.0052 236 GLN A N   
1595 C CA  . GLN A 193 ? 0.4286 0.4126 0.5052 0.0036  -0.0537 -0.0023 236 GLN A CA  
1596 C C   . GLN A 193 ? 0.3969 0.3857 0.4730 0.0028  -0.0516 0.0018  236 GLN A C   
1597 O O   . GLN A 193 ? 0.3601 0.3494 0.4403 0.0013  -0.0526 0.0063  236 GLN A O   
1598 C CB  . GLN A 193 ? 0.4522 0.4315 0.5301 0.0066  -0.0549 -0.0059 236 GLN A CB  
1599 C CG  . GLN A 193 ? 0.5851 0.5579 0.6664 0.0070  -0.0589 -0.0085 236 GLN A CG  
1600 C CD  . GLN A 193 ? 0.6543 0.6249 0.7305 0.0072  -0.0597 -0.0125 236 GLN A CD  
1601 O OE1 . GLN A 193 ? 0.6694 0.6390 0.7485 0.0050  -0.0624 -0.0114 236 GLN A OE1 
1602 N NE2 . GLN A 193 ? 0.6200 0.5900 0.6889 0.0100  -0.0575 -0.0167 236 GLN A NE2 
1603 N N   . THR A 194 ? 0.3596 0.3516 0.4308 0.0038  -0.0489 0.0005  237 THR A N   
1604 C CA  . THR A 194 ? 0.3343 0.3300 0.4051 0.0034  -0.0478 0.0036  237 THR A CA  
1605 C C   . THR A 194 ? 0.3447 0.3444 0.4095 0.0029  -0.0450 0.0029  237 THR A C   
1606 O O   . THR A 194 ? 0.3117 0.3113 0.3732 0.0041  -0.0434 -0.0006 237 THR A O   
1607 C CB  . THR A 194 ? 0.3476 0.3425 0.4218 0.0057  -0.0483 0.0027  237 THR A CB  
1608 O OG1 . THR A 194 ? 0.4216 0.4122 0.5017 0.0063  -0.0510 0.0029  237 THR A OG1 
1609 C CG2 . THR A 194 ? 0.3364 0.3349 0.4109 0.0050  -0.0483 0.0062  237 THR A CG2 
1610 N N   . LEU A 195 ? 0.3427 0.3454 0.4056 0.0014  -0.0446 0.0064  238 LEU A N   
1611 C CA  . LEU A 195 ? 0.3080 0.3139 0.3657 0.0010  -0.0426 0.0059  238 LEU A CA  
1612 C C   . LEU A 195 ? 0.3276 0.3351 0.3868 0.0016  -0.0435 0.0071  238 LEU A C   
1613 O O   . LEU A 195 ? 0.3197 0.3271 0.3801 0.0009  -0.0454 0.0106  238 LEU A O   
1614 C CB  . LEU A 195 ? 0.3500 0.3575 0.4038 -0.0009 -0.0416 0.0085  238 LEU A CB  
1615 C CG  . LEU A 195 ? 0.3265 0.3367 0.3746 -0.0013 -0.0400 0.0083  238 LEU A CG  
1616 C CD1 . LEU A 195 ? 0.3370 0.3478 0.3827 -0.0007 -0.0380 0.0047  238 LEU A CD1 
1617 C CD2 . LEU A 195 ? 0.3841 0.3951 0.4281 -0.0027 -0.0391 0.0114  238 LEU A CD2 
1618 N N   . GLU A 196 ? 0.3045 0.3133 0.3639 0.0029  -0.0424 0.0046  239 GLU A N   
1619 C CA  . GLU A 196 ? 0.3158 0.3266 0.3783 0.0035  -0.0434 0.0056  239 GLU A CA  
1620 C C   . GLU A 196 ? 0.3375 0.3510 0.3958 0.0023  -0.0427 0.0056  239 GLU A C   
1621 O O   . GLU A 196 ? 0.2995 0.3139 0.3558 0.0026  -0.0403 0.0031  239 GLU A O   
1622 C CB  . GLU A 196 ? 0.3577 0.3683 0.4255 0.0060  -0.0424 0.0031  239 GLU A CB  
1623 C CG  . GLU A 196 ? 0.4091 0.4223 0.4820 0.0067  -0.0435 0.0043  239 GLU A CG  
1624 C CD  . GLU A 196 ? 0.4760 0.4888 0.5554 0.0095  -0.0421 0.0024  239 GLU A CD  
1625 O OE1 . GLU A 196 ? 0.5127 0.5220 0.5933 0.0110  -0.0422 0.0012  239 GLU A OE1 
1626 O OE2 . GLU A 196 ? 0.4669 0.4828 0.5505 0.0105  -0.0410 0.0022  239 GLU A OE2 
1627 N N   . ALA A 197 ? 0.2950 0.3093 0.3517 0.0011  -0.0450 0.0083  240 ALA A N   
1628 C CA  . ALA A 197 ? 0.3210 0.3371 0.3734 0.0000  -0.0452 0.0082  240 ALA A CA  
1629 C C   . ALA A 197 ? 0.3201 0.3382 0.3779 0.0005  -0.0469 0.0080  240 ALA A C   
1630 O O   . ALA A 197 ? 0.3213 0.3395 0.3844 0.0012  -0.0495 0.0098  240 ALA A O   
1631 C CB  . ALA A 197 ? 0.3373 0.3524 0.3834 -0.0013 -0.0469 0.0110  240 ALA A CB  
1632 N N   . TRP A 198 ? 0.2899 0.3097 0.3472 0.0002  -0.0456 0.0061  241 TRP A N   
1633 C CA  . TRP A 198 ? 0.3178 0.3401 0.3811 0.0003  -0.0472 0.0062  241 TRP A CA  
1634 C C   . TRP A 198 ? 0.3209 0.3430 0.3790 -0.0016 -0.0498 0.0066  241 TRP A C   
1635 O O   . TRP A 198 ? 0.2817 0.3036 0.3354 -0.0024 -0.0480 0.0049  241 TRP A O   
1636 C CB  . TRP A 198 ? 0.3470 0.3711 0.4147 0.0013  -0.0434 0.0040  241 TRP A CB  
1637 C CG  . TRP A 198 ? 0.3673 0.3910 0.4395 0.0037  -0.0409 0.0031  241 TRP A CG  
1638 C CD1 . TRP A 198 ? 0.3996 0.4217 0.4744 0.0048  -0.0422 0.0040  241 TRP A CD1 
1639 C CD2 . TRP A 198 ? 0.3511 0.3755 0.4252 0.0054  -0.0366 0.0010  241 TRP A CD2 
1640 N NE1 . TRP A 198 ? 0.3998 0.4211 0.4777 0.0072  -0.0392 0.0022  241 TRP A NE1 
1641 C CE2 . TRP A 198 ? 0.3738 0.3966 0.4508 0.0077  -0.0356 0.0003  241 TRP A CE2 
1642 C CE3 . TRP A 198 ? 0.4051 0.4308 0.4783 0.0053  -0.0334 -0.0002 241 TRP A CE3 
1643 C CZ2 . TRP A 198 ? 0.3808 0.4031 0.4586 0.0102  -0.0315 -0.0018 241 TRP A CZ2 
1644 C CZ3 . TRP A 198 ? 0.3781 0.4038 0.4524 0.0076  -0.0292 -0.0018 241 TRP A CZ3 
1645 C CH2 . TRP A 198 ? 0.3694 0.3933 0.4455 0.0102  -0.0282 -0.0027 241 TRP A CH2 
1646 N N   . VAL A 199 ? 0.3264 0.3482 0.3846 -0.0021 -0.0544 0.0088  242 VAL A N   
1647 C CA  . VAL A 199 ? 0.3122 0.3329 0.3642 -0.0036 -0.0577 0.0089  242 VAL A CA  
1648 C C   . VAL A 199 ? 0.3580 0.3810 0.4173 -0.0042 -0.0599 0.0081  242 VAL A C   
1649 O O   . VAL A 199 ? 0.3222 0.3471 0.3899 -0.0039 -0.0630 0.0096  242 VAL A O   
1650 C CB  . VAL A 199 ? 0.3450 0.3636 0.3923 -0.0038 -0.0620 0.0118  242 VAL A CB  
1651 C CG1 . VAL A 199 ? 0.3582 0.3747 0.3971 -0.0050 -0.0656 0.0114  242 VAL A CG1 
1652 C CG2 . VAL A 199 ? 0.3571 0.3737 0.3989 -0.0034 -0.0594 0.0132  242 VAL A CG2 
1653 N N   . ILE A 200 ? 0.3251 0.3481 0.3822 -0.0051 -0.0582 0.0059  243 ILE A N   
1654 C CA  . ILE A 200 ? 0.3240 0.3493 0.3891 -0.0059 -0.0597 0.0052  243 ILE A CA  
1655 C C   . ILE A 200 ? 0.3669 0.3906 0.4295 -0.0074 -0.0662 0.0056  243 ILE A C   
1656 O O   . ILE A 200 ? 0.3621 0.3823 0.4140 -0.0082 -0.0675 0.0043  243 ILE A O   
1657 C CB  . ILE A 200 ? 0.3664 0.3919 0.4306 -0.0063 -0.0553 0.0030  243 ILE A CB  
1658 C CG1 . ILE A 200 ? 0.3549 0.3810 0.4187 -0.0047 -0.0494 0.0024  243 ILE A CG1 
1659 C CG2 . ILE A 200 ? 0.3823 0.4107 0.4569 -0.0072 -0.0562 0.0030  243 ILE A CG2 
1660 C CD1 . ILE A 200 ? 0.3523 0.3811 0.4256 -0.0030 -0.0479 0.0035  243 ILE A CD1 
1661 N N   . HIS A 201 ? 0.3736 0.3995 0.4458 -0.0077 -0.0705 0.0072  244 HIS A N   
1662 C CA  . HIS A 201 ? 0.4175 0.4416 0.4879 -0.0091 -0.0779 0.0075  244 HIS A CA  
1663 C C   . HIS A 201 ? 0.4375 0.4614 0.5105 -0.0108 -0.0795 0.0055  244 HIS A C   
1664 O O   . HIS A 201 ? 0.4053 0.4322 0.4867 -0.0110 -0.0754 0.0049  244 HIS A O   
1665 C CB  . HIS A 201 ? 0.3911 0.4177 0.4721 -0.0086 -0.0826 0.0103  244 HIS A CB  
1666 C CG  . HIS A 201 ? 0.4026 0.4277 0.4787 -0.0073 -0.0838 0.0126  244 HIS A CG  
1667 N ND1 . HIS A 201 ? 0.3824 0.4053 0.4548 -0.0077 -0.0908 0.0146  244 HIS A ND1 
1668 C CD2 . HIS A 201 ? 0.3783 0.4033 0.4526 -0.0058 -0.0791 0.0135  244 HIS A CD2 
1669 C CE1 . HIS A 201 ? 0.3943 0.4160 0.4630 -0.0063 -0.0900 0.0169  244 HIS A CE1 
1670 N NE2 . HIS A 201 ? 0.4271 0.4501 0.4975 -0.0053 -0.0830 0.0162  244 HIS A NE2 
1671 N N   . GLY A 202 ? 0.5266 0.5466 0.5919 -0.0121 -0.0855 0.0045  245 GLY A N   
1672 C CA  . GLY A 202 ? 0.5928 0.6116 0.6602 -0.0140 -0.0885 0.0023  245 GLY A CA  
1673 C C   . GLY A 202 ? 0.6888 0.7019 0.7446 -0.0148 -0.0957 0.0009  245 GLY A C   
1674 O O   . GLY A 202 ? 0.7760 0.7877 0.8280 -0.0143 -0.1007 0.0026  245 GLY A O   
1675 N N   . GLY A 203 ? 0.7265 0.7359 0.7761 -0.0159 -0.0965 -0.0022 246 GLY A N   
1676 C CA  . GLY A 203 ? 0.8137 0.8165 0.8504 -0.0163 -0.1032 -0.0043 246 GLY A CA  
1677 C C   . GLY A 203 ? 0.8436 0.8461 0.8856 -0.0174 -0.1128 -0.0032 246 GLY A C   
1678 O O   . GLY A 203 ? 0.7696 0.7773 0.8284 -0.0183 -0.1146 -0.0010 246 GLY A O   
1679 N N   . ARG A 204 ? 0.8979 0.8941 0.9256 -0.0171 -0.1190 -0.0044 247 ARG A N   
1680 C CA  . ARG A 204 ? 0.9008 0.8951 0.9309 -0.0182 -0.1296 -0.0039 247 ARG A CA  
1681 C C   . ARG A 204 ? 0.8588 0.8519 0.8805 -0.0165 -0.1326 -0.0009 247 ARG A C   
1682 O O   . ARG A 204 ? 0.8683 0.8558 0.8792 -0.0164 -0.1405 -0.0015 247 ARG A O   
1683 C CB  . ARG A 204 ? 0.9739 0.9608 0.9939 -0.0192 -0.1361 -0.0082 247 ARG A CB  
1684 C CG  . ARG A 204 ? 1.0595 1.0395 1.0571 -0.0173 -0.1328 -0.0109 247 ARG A CG  
1685 C CD  . ARG A 204 ? 1.0580 1.0298 1.0397 -0.0168 -0.1420 -0.0128 247 ARG A CD  
1686 N NE  . ARG A 204 ? 1.1316 1.0980 1.0917 -0.0142 -0.1378 -0.0138 247 ARG A NE  
1687 C CZ  . ARG A 204 ? 1.1905 1.1580 1.1431 -0.0122 -0.1344 -0.0101 247 ARG A CZ  
1688 N NH1 . ARG A 204 ? 1.1367 1.1100 1.1009 -0.0125 -0.1350 -0.0056 247 ARG A NH1 
1689 N NH2 . ARG A 204 ? 1.2614 1.2239 1.1949 -0.0099 -0.1302 -0.0109 247 ARG A NH2 
1690 N N   . GLU A 205 ? 0.8230 0.8207 0.8493 -0.0152 -0.1265 0.0025  248 GLU A N   
1691 C CA  . GLU A 205 ? 0.7948 0.7917 0.8147 -0.0136 -0.1283 0.0060  248 GLU A CA  
1692 C C   . GLU A 205 ? 0.6526 0.6556 0.6905 -0.0137 -0.1306 0.0097  248 GLU A C   
1693 O O   . GLU A 205 ? 0.5836 0.5925 0.6371 -0.0141 -0.1259 0.0101  248 GLU A O   
1694 C CB  . GLU A 205 ? 0.8217 0.8183 0.8315 -0.0118 -0.1194 0.0070  248 GLU A CB  
1695 C CG  . GLU A 205 ? 0.9325 0.9226 0.9224 -0.0109 -0.1176 0.0043  248 GLU A CG  
1696 C CD  . GLU A 205 ? 1.0142 1.0041 0.9947 -0.0091 -0.1101 0.0065  248 GLU A CD  
1697 O OE1 . GLU A 205 ? 0.9458 0.9407 0.9361 -0.0088 -0.1038 0.0081  248 GLU A OE1 
1698 O OE2 . GLU A 205 ? 1.0389 1.0235 1.0025 -0.0078 -0.1105 0.0067  248 GLU A OE2 
1699 N N   . ASP A 206 ? 0.5790 0.5804 0.6144 -0.0132 -0.1377 0.0125  249 ASP A N   
1700 C CA  . ASP A 206 ? 0.5442 0.5509 0.5964 -0.0130 -0.1404 0.0163  249 ASP A CA  
1701 C C   . ASP A 206 ? 0.5023 0.5129 0.5590 -0.0112 -0.1318 0.0187  249 ASP A C   
1702 O O   . ASP A 206 ? 0.5310 0.5388 0.5747 -0.0100 -0.1266 0.0190  249 ASP A O   
1703 C CB  . ASP A 206 ? 0.4819 0.4852 0.5288 -0.0127 -0.1506 0.0188  249 ASP A CB  
1704 C CG  . ASP A 206 ? 0.5255 0.5253 0.5711 -0.0145 -0.1608 0.0164  249 ASP A CG  
1705 O OD1 . ASP A 206 ? 0.5065 0.5092 0.5649 -0.0163 -0.1610 0.0141  249 ASP A OD1 
1706 O OD2 . ASP A 206 ? 0.4803 0.4740 0.5120 -0.0141 -0.1686 0.0168  249 ASP A OD2 
1707 N N   . SER A 207 ? 0.5021 0.5189 0.5778 -0.0110 -0.1303 0.0205  250 SER A N   
1708 C CA  . SER A 207 ? 0.5125 0.5328 0.5939 -0.0092 -0.1219 0.0220  250 SER A CA  
1709 C C   . SER A 207 ? 0.4799 0.4973 0.5519 -0.0077 -0.1223 0.0251  250 SER A C   
1710 O O   . SER A 207 ? 0.4935 0.5097 0.5661 -0.0073 -0.1294 0.0281  250 SER A O   
1711 C CB  . SER A 207 ? 0.5080 0.5349 0.6110 -0.0088 -0.1213 0.0235  250 SER A CB  
1712 O OG  . SER A 207 ? 0.4798 0.5094 0.5877 -0.0070 -0.1128 0.0239  250 SER A OG  
1713 N N   . ARG A 208 ? 0.4521 0.4683 0.5160 -0.0068 -0.1147 0.0248  251 ARG A N   
1714 C CA  . ARG A 208 ? 0.4348 0.4484 0.4910 -0.0054 -0.1138 0.0281  251 ARG A CA  
1715 C C   . ARG A 208 ? 0.4230 0.4380 0.4802 -0.0045 -0.1046 0.0273  251 ARG A C   
1716 O O   . ARG A 208 ? 0.3939 0.4106 0.4530 -0.0050 -0.0994 0.0240  251 ARG A O   
1717 C CB  . ARG A 208 ? 0.4685 0.4761 0.5053 -0.0056 -0.1170 0.0286  251 ARG A CB  
1718 C CG  . ARG A 208 ? 0.5122 0.5172 0.5357 -0.0058 -0.1105 0.0259  251 ARG A CG  
1719 C CD  . ARG A 208 ? 0.5595 0.5584 0.5637 -0.0055 -0.1137 0.0266  251 ARG A CD  
1720 N NE  . ARG A 208 ? 0.6847 0.6813 0.6764 -0.0052 -0.1070 0.0247  251 ARG A NE  
1721 C CZ  . ARG A 208 ? 0.7586 0.7532 0.7435 -0.0058 -0.1060 0.0205  251 ARG A CZ  
1722 N NH1 . ARG A 208 ? 0.7894 0.7841 0.7790 -0.0071 -0.1113 0.0175  251 ARG A NH1 
1723 N NH2 . ARG A 208 ? 0.7855 0.7782 0.7596 -0.0052 -0.0996 0.0193  251 ARG A NH2 
1724 N N   . ASP A 209 ? 0.3611 0.3751 0.4173 -0.0033 -0.1031 0.0306  252 ASP A N   
1725 C CA  . ASP A 209 ? 0.3967 0.4113 0.4540 -0.0025 -0.0954 0.0301  252 ASP A CA  
1726 C C   . ASP A 209 ? 0.4141 0.4258 0.4567 -0.0031 -0.0913 0.0287  252 ASP A C   
1727 O O   . ASP A 209 ? 0.4340 0.4423 0.4656 -0.0030 -0.0920 0.0314  252 ASP A O   
1728 C CB  . ASP A 209 ? 0.4011 0.4150 0.4626 -0.0012 -0.0959 0.0341  252 ASP A CB  
1729 C CG  . ASP A 209 ? 0.4439 0.4579 0.5073 -0.0005 -0.0889 0.0334  252 ASP A CG  
1730 O OD1 . ASP A 209 ? 0.4242 0.4393 0.4863 -0.0008 -0.0838 0.0299  252 ASP A OD1 
1731 O OD2 . ASP A 209 ? 0.4698 0.4826 0.5362 0.0005  -0.0890 0.0365  252 ASP A OD2 
1732 N N   . LEU A 210 ? 0.3935 0.4065 0.4361 -0.0037 -0.0867 0.0248  253 LEU A N   
1733 C CA  . LEU A 210 ? 0.4581 0.4687 0.4882 -0.0041 -0.0827 0.0233  253 LEU A CA  
1734 C C   . LEU A 210 ? 0.3888 0.3992 0.4178 -0.0035 -0.0768 0.0244  253 LEU A C   
1735 O O   . LEU A 210 ? 0.4255 0.4340 0.4446 -0.0037 -0.0734 0.0241  253 LEU A O   
1736 C CB  . LEU A 210 ? 0.3967 0.4086 0.4277 -0.0050 -0.0805 0.0189  253 LEU A CB  
1737 C CG  . LEU A 210 ? 0.4188 0.4300 0.4493 -0.0060 -0.0863 0.0173  253 LEU A CG  
1738 C CD1 . LEU A 210 ? 0.4470 0.4595 0.4797 -0.0069 -0.0834 0.0134  253 LEU A CD1 
1739 C CD2 . LEU A 210 ? 0.4749 0.4813 0.4905 -0.0062 -0.0906 0.0182  253 LEU A CD2 
1740 N N   . CYS A 211 ? 0.4352 0.4471 0.4743 -0.0027 -0.0757 0.0258  254 CYS A N   
1741 C CA  . CYS A 211 ? 0.4806 0.4916 0.5190 -0.0022 -0.0713 0.0271  254 CYS A CA  
1742 C C   . CYS A 211 ? 0.4930 0.5010 0.5232 -0.0022 -0.0727 0.0317  254 CYS A C   
1743 O O   . CYS A 211 ? 0.5203 0.5273 0.5488 -0.0022 -0.0690 0.0333  254 CYS A O   
1744 C CB  . CYS A 211 ? 0.4505 0.4631 0.5016 -0.0012 -0.0704 0.0271  254 CYS A CB  
1745 S SG  . CYS A 211 ? 0.4498 0.4656 0.5090 -0.0007 -0.0666 0.0221  254 CYS A SG  
1746 N N   . GLN A 212 ? 0.4888 0.4952 0.5139 -0.0023 -0.0780 0.0340  255 GLN A N   
1747 C CA  . GLN A 212 ? 0.4977 0.5008 0.5125 -0.0021 -0.0791 0.0385  255 GLN A CA  
1748 C C   . GLN A 212 ? 0.4860 0.4869 0.4859 -0.0023 -0.0773 0.0375  255 GLN A C   
1749 O O   . GLN A 212 ? 0.4966 0.4946 0.4861 -0.0019 -0.0774 0.0412  255 GLN A O   
1750 C CB  . GLN A 212 ? 0.5068 0.5088 0.5226 -0.0016 -0.0863 0.0418  255 GLN A CB  
1751 C CG  . GLN A 212 ? 0.5533 0.5572 0.5841 -0.0010 -0.0882 0.0432  255 GLN A CG  
1752 C CD  . GLN A 212 ? 0.5688 0.5722 0.6041 -0.0006 -0.0840 0.0456  255 GLN A CD  
1753 O OE1 . GLN A 212 ? 0.5980 0.6032 0.6440 -0.0002 -0.0814 0.0434  255 GLN A OE1 
1754 N NE2 . GLN A 212 ? 0.5769 0.5774 0.6039 -0.0007 -0.0834 0.0502  255 GLN A NE2 
1755 N N   . ASP A 213 ? 0.4570 0.4590 0.4556 -0.0028 -0.0755 0.0327  256 ASP A N   
1756 C CA  . ASP A 213 ? 0.4495 0.4490 0.4343 -0.0028 -0.0737 0.0312  256 ASP A CA  
1757 C C   . ASP A 213 ? 0.4670 0.4657 0.4461 -0.0023 -0.0675 0.0338  256 ASP A C   
1758 O O   . ASP A 213 ? 0.4522 0.4530 0.4398 -0.0026 -0.0638 0.0346  256 ASP A O   
1759 C CB  . ASP A 213 ? 0.4677 0.4686 0.4546 -0.0034 -0.0721 0.0257  256 ASP A CB  
1760 C CG  . ASP A 213 ? 0.5162 0.5141 0.4894 -0.0031 -0.0706 0.0235  256 ASP A CG  
1761 O OD1 . ASP A 213 ? 0.5649 0.5600 0.5309 -0.0031 -0.0757 0.0222  256 ASP A OD1 
1762 O OD2 . ASP A 213 ? 0.4901 0.4882 0.4599 -0.0028 -0.0646 0.0230  256 ASP A OD2 
1763 N N   . PRO A 214 ? 0.4738 0.4692 0.4385 -0.0016 -0.0665 0.0352  257 PRO A N   
1764 C CA  . PRO A 214 ? 0.4722 0.4675 0.4326 -0.0011 -0.0601 0.0384  257 PRO A CA  
1765 C C   . PRO A 214 ? 0.4440 0.4421 0.4107 -0.0016 -0.0542 0.0355  257 PRO A C   
1766 O O   . PRO A 214 ? 0.4271 0.4266 0.3987 -0.0017 -0.0500 0.0383  257 PRO A O   
1767 C CB  . PRO A 214 ? 0.4819 0.4730 0.4247 0.0002  -0.0598 0.0392  257 PRO A CB  
1768 C CG  . PRO A 214 ? 0.4815 0.4700 0.4197 0.0003  -0.0677 0.0385  257 PRO A CG  
1769 C CD  . PRO A 214 ? 0.4840 0.4756 0.4358 -0.0010 -0.0712 0.0345  257 PRO A CD  
1770 N N   . THR A 215 ? 0.4292 0.4281 0.3962 -0.0018 -0.0540 0.0302  258 THR A N   
1771 C CA  . THR A 215 ? 0.4649 0.4661 0.4371 -0.0021 -0.0488 0.0277  258 THR A CA  
1772 C C   . THR A 215 ? 0.4290 0.4332 0.4154 -0.0029 -0.0486 0.0275  258 THR A C   
1773 O O   . THR A 215 ? 0.4300 0.4360 0.4213 -0.0032 -0.0444 0.0272  258 THR A O   
1774 C CB  . THR A 215 ? 0.4405 0.4414 0.4096 -0.0022 -0.0489 0.0223  258 THR A CB  
1775 O OG1 . THR A 215 ? 0.4431 0.4450 0.4194 -0.0030 -0.0536 0.0198  258 THR A OG1 
1776 C CG2 . THR A 215 ? 0.4615 0.4584 0.4156 -0.0011 -0.0493 0.0217  258 THR A CG2 
1777 N N   . ILE A 216 ? 0.4046 0.4094 0.3979 -0.0032 -0.0531 0.0277  259 ILE A N   
1778 C CA  . ILE A 216 ? 0.3591 0.3658 0.3648 -0.0035 -0.0529 0.0277  259 ILE A CA  
1779 C C   . ILE A 216 ? 0.4348 0.4409 0.4429 -0.0034 -0.0515 0.0324  259 ILE A C   
1780 O O   . ILE A 216 ? 0.4208 0.4279 0.4363 -0.0037 -0.0490 0.0322  259 ILE A O   
1781 C CB  . ILE A 216 ? 0.3982 0.4058 0.4110 -0.0034 -0.0577 0.0266  259 ILE A CB  
1782 C CG1 . ILE A 216 ? 0.3791 0.3877 0.3916 -0.0036 -0.0587 0.0222  259 ILE A CG1 
1783 C CG2 . ILE A 216 ? 0.4009 0.4098 0.4255 -0.0031 -0.0572 0.0266  259 ILE A CG2 
1784 C CD1 . ILE A 216 ? 0.3863 0.3966 0.4025 -0.0038 -0.0544 0.0186  259 ILE A CD1 
1785 N N   . LYS A 217 ? 0.4194 0.4235 0.4214 -0.0032 -0.0533 0.0368  260 LYS A N   
1786 C CA  . LYS A 217 ? 0.4599 0.4632 0.4636 -0.0033 -0.0515 0.0420  260 LYS A CA  
1787 C C   . LYS A 217 ? 0.4167 0.4209 0.4186 -0.0036 -0.0456 0.0425  260 LYS A C   
1788 O O   . LYS A 217 ? 0.4196 0.4244 0.4290 -0.0041 -0.0435 0.0448  260 LYS A O   
1789 C CB  . LYS A 217 ? 0.5013 0.5020 0.4965 -0.0027 -0.0541 0.0470  260 LYS A CB  
1790 C CG  . LYS A 217 ? 0.5596 0.5594 0.5570 -0.0024 -0.0606 0.0471  260 LYS A CG  
1791 C CD  . LYS A 217 ? 0.6240 0.6250 0.6357 -0.0026 -0.0624 0.0472  260 LYS A CD  
1792 C CE  . LYS A 217 ? 0.7046 0.7051 0.7196 -0.0020 -0.0687 0.0480  260 LYS A CE  
1793 N NZ  . LYS A 217 ? 0.8122 0.8143 0.8414 -0.0018 -0.0698 0.0459  260 LYS A NZ  
1794 N N   . GLU A 218 ? 0.4023 0.4064 0.3949 -0.0031 -0.0431 0.0403  261 GLU A N   
1795 C CA  . GLU A 218 ? 0.4340 0.4395 0.4263 -0.0032 -0.0374 0.0401  261 GLU A CA  
1796 C C   . GLU A 218 ? 0.4127 0.4204 0.4162 -0.0040 -0.0366 0.0368  261 GLU A C   
1797 O O   . GLU A 218 ? 0.3714 0.3803 0.3811 -0.0045 -0.0337 0.0387  261 GLU A O   
1798 C CB  . GLU A 218 ? 0.4762 0.4809 0.4571 -0.0022 -0.0355 0.0372  261 GLU A CB  
1799 C CG  . GLU A 218 ? 0.5126 0.5187 0.4922 -0.0018 -0.0293 0.0376  261 GLU A CG  
1800 C CD  . GLU A 218 ? 0.6072 0.6119 0.5757 -0.0006 -0.0276 0.0342  261 GLU A CD  
1801 O OE1 . GLU A 218 ? 0.6086 0.6113 0.5717 -0.0004 -0.0317 0.0309  261 GLU A OE1 
1802 O OE2 . GLU A 218 ? 0.6884 0.6938 0.6541 0.0002  -0.0222 0.0347  261 GLU A OE2 
1803 N N   . LEU A 219 ? 0.3776 0.3858 0.3841 -0.0040 -0.0392 0.0321  262 LEU A N   
1804 C CA  . LEU A 219 ? 0.3781 0.3879 0.3936 -0.0044 -0.0385 0.0288  262 LEU A CA  
1805 C C   . LEU A 219 ? 0.3631 0.3725 0.3882 -0.0048 -0.0397 0.0309  262 LEU A C   
1806 O O   . LEU A 219 ? 0.3508 0.3608 0.3821 -0.0052 -0.0381 0.0303  262 LEU A O   
1807 C CB  . LEU A 219 ? 0.3626 0.3729 0.3791 -0.0041 -0.0408 0.0241  262 LEU A CB  
1808 C CG  . LEU A 219 ? 0.3577 0.3691 0.3823 -0.0041 -0.0403 0.0206  262 LEU A CG  
1809 C CD1 . LEU A 219 ? 0.3394 0.3517 0.3639 -0.0043 -0.0366 0.0195  262 LEU A CD1 
1810 C CD2 . LEU A 219 ? 0.3681 0.3803 0.3933 -0.0037 -0.0419 0.0169  262 LEU A CD2 
1811 N N   . GLU A 220 ? 0.4119 0.4200 0.4386 -0.0046 -0.0431 0.0335  263 GLU A N   
1812 C CA  . GLU A 220 ? 0.3893 0.3964 0.4253 -0.0048 -0.0446 0.0355  263 GLU A CA  
1813 C C   . GLU A 220 ? 0.3837 0.3906 0.4219 -0.0057 -0.0419 0.0397  263 GLU A C   
1814 O O   . GLU A 220 ? 0.3182 0.3246 0.3648 -0.0063 -0.0419 0.0395  263 GLU A O   
1815 C CB  . GLU A 220 ? 0.4034 0.4091 0.4403 -0.0043 -0.0487 0.0381  263 GLU A CB  
1816 C CG  . GLU A 220 ? 0.4660 0.4700 0.5129 -0.0043 -0.0507 0.0399  263 GLU A CG  
1817 C CD  . GLU A 220 ? 0.5718 0.5745 0.6202 -0.0036 -0.0549 0.0424  263 GLU A CD  
1818 O OE1 . GLU A 220 ? 0.6252 0.6277 0.6659 -0.0035 -0.0562 0.0451  263 GLU A OE1 
1819 O OE2 . GLU A 220 ? 0.6177 0.6194 0.6749 -0.0029 -0.0571 0.0414  263 GLU A OE2 
1820 N N   . SER A 221 ? 0.3896 0.3965 0.4201 -0.0058 -0.0396 0.0437  264 SER A N   
1821 C CA  . SER A 221 ? 0.4110 0.4183 0.4442 -0.0066 -0.0362 0.0484  264 SER A CA  
1822 C C   . SER A 221 ? 0.3709 0.3802 0.4085 -0.0071 -0.0331 0.0458  264 SER A C   
1823 O O   . SER A 221 ? 0.3589 0.3684 0.4052 -0.0082 -0.0323 0.0480  264 SER A O   
1824 C CB  . SER A 221 ? 0.3600 0.3671 0.3827 -0.0060 -0.0335 0.0530  264 SER A CB  
1825 O OG  . SER A 221 ? 0.5732 0.5780 0.5927 -0.0056 -0.0367 0.0568  264 SER A OG  
1826 N N   . ILE A 222 ? 0.3861 0.3967 0.4183 -0.0065 -0.0318 0.0412  265 ILE A N   
1827 C CA  . ILE A 222 ? 0.3959 0.4084 0.4318 -0.0069 -0.0291 0.0389  265 ILE A CA  
1828 C C   . ILE A 222 ? 0.3677 0.3795 0.4137 -0.0075 -0.0317 0.0362  265 ILE A C   
1829 O O   . ILE A 222 ? 0.3888 0.4012 0.4423 -0.0084 -0.0309 0.0374  265 ILE A O   
1830 C CB  . ILE A 222 ? 0.3717 0.3851 0.3998 -0.0059 -0.0277 0.0344  265 ILE A CB  
1831 C CG1 . ILE A 222 ? 0.3906 0.4039 0.4081 -0.0051 -0.0245 0.0369  265 ILE A CG1 
1832 C CG2 . ILE A 222 ? 0.4069 0.4220 0.4397 -0.0062 -0.0260 0.0314  265 ILE A CG2 
1833 C CD1 . ILE A 222 ? 0.4355 0.4485 0.4444 -0.0041 -0.0243 0.0324  265 ILE A CD1 
1834 N N   . ILE A 223 ? 0.3653 0.3758 0.4118 -0.0069 -0.0351 0.0324  266 ILE A N   
1835 C CA  . ILE A 223 ? 0.3869 0.3962 0.4410 -0.0069 -0.0373 0.0290  266 ILE A CA  
1836 C C   . ILE A 223 ? 0.3959 0.4030 0.4584 -0.0077 -0.0395 0.0322  266 ILE A C   
1837 O O   . ILE A 223 ? 0.3755 0.3814 0.4449 -0.0082 -0.0407 0.0307  266 ILE A O   
1838 C CB  . ILE A 223 ? 0.3911 0.3998 0.4432 -0.0057 -0.0393 0.0245  266 ILE A CB  
1839 C CG1 . ILE A 223 ? 0.4516 0.4589 0.5088 -0.0052 -0.0406 0.0202  266 ILE A CG1 
1840 C CG2 . ILE A 223 ? 0.4082 0.4156 0.4609 -0.0052 -0.0420 0.0264  266 ILE A CG2 
1841 C CD1 . ILE A 223 ? 0.4622 0.4708 0.5181 -0.0054 -0.0387 0.0177  266 ILE A CD1 
1842 N N   . SER A 224 ? 0.3714 0.3777 0.4334 -0.0078 -0.0403 0.0366  267 SER A N   
1843 C CA  . SER A 224 ? 0.3909 0.3948 0.4613 -0.0086 -0.0424 0.0402  267 SER A CA  
1844 C C   . SER A 224 ? 0.3845 0.3892 0.4606 -0.0102 -0.0403 0.0436  267 SER A C   
1845 O O   . SER A 224 ? 0.3419 0.3447 0.4275 -0.0111 -0.0424 0.0439  267 SER A O   
1846 C CB  . SER A 224 ? 0.3923 0.3952 0.4602 -0.0084 -0.0434 0.0450  267 SER A CB  
1847 O OG  . SER A 224 ? 0.4630 0.4652 0.5281 -0.0070 -0.0461 0.0421  267 SER A OG  
1848 N N   . LYS A 225 ? 0.3665 0.3742 0.4376 -0.0105 -0.0361 0.0463  268 LYS A N   
1849 C CA  . LYS A 225 ? 0.4392 0.4486 0.5168 -0.0119 -0.0334 0.0499  268 LYS A CA  
1850 C C   . LYS A 225 ? 0.4475 0.4567 0.5323 -0.0124 -0.0352 0.0455  268 LYS A C   
1851 O O   . LYS A 225 ? 0.4223 0.4313 0.5172 -0.0139 -0.0359 0.0478  268 LYS A O   
1852 C CB  . LYS A 225 ? 0.4466 0.4593 0.5165 -0.0114 -0.0281 0.0524  268 LYS A CB  
1853 C CG  . LYS A 225 ? 0.4855 0.5004 0.5622 -0.0126 -0.0243 0.0582  268 LYS A CG  
1854 C CD  . LYS A 225 ? 0.5174 0.5356 0.5875 -0.0116 -0.0187 0.0587  268 LYS A CD  
1855 C CE  . LYS A 225 ? 0.4693 0.4902 0.5449 -0.0123 -0.0137 0.0659  268 LYS A CE  
1856 N NZ  . LYS A 225 ? 0.4418 0.4660 0.5124 -0.0110 -0.0079 0.0661  268 LYS A NZ  
1857 N N   . ARG A 226 ? 0.4209 0.4301 0.5009 -0.0113 -0.0362 0.0392  269 ARG A N   
1858 C CA  . ARG A 226 ? 0.4262 0.4346 0.5109 -0.0115 -0.0382 0.0346  269 ARG A CA  
1859 C C   . ARG A 226 ? 0.4240 0.4281 0.5143 -0.0113 -0.0431 0.0318  269 ARG A C   
1860 O O   . ARG A 226 ? 0.3948 0.3971 0.4867 -0.0109 -0.0454 0.0271  269 ARG A O   
1861 C CB  . ARG A 226 ? 0.4083 0.4182 0.4849 -0.0101 -0.0369 0.0296  269 ARG A CB  
1862 C CG  . ARG A 226 ? 0.4074 0.4207 0.4772 -0.0098 -0.0323 0.0316  269 ARG A CG  
1863 C CD  . ARG A 226 ? 0.3973 0.4119 0.4623 -0.0089 -0.0312 0.0269  269 ARG A CD  
1864 N NE  . ARG A 226 ? 0.3914 0.4060 0.4630 -0.0094 -0.0326 0.0251  269 ARG A NE  
1865 C CZ  . ARG A 226 ? 0.3778 0.3904 0.4494 -0.0088 -0.0355 0.0202  269 ARG A CZ  
1866 N NH1 . ARG A 226 ? 0.3707 0.3817 0.4364 -0.0075 -0.0365 0.0166  269 ARG A NH1 
1867 N NH2 . ARG A 226 ? 0.3788 0.3910 0.4564 -0.0094 -0.0374 0.0190  269 ARG A NH2 
1868 N N   . ASN A 227 ? 0.4102 0.4119 0.5029 -0.0114 -0.0448 0.0346  270 ASN A N   
1869 C CA  . ASN A 227 ? 0.4015 0.3986 0.5003 -0.0110 -0.0493 0.0322  270 ASN A CA  
1870 C C   . ASN A 227 ? 0.3869 0.3822 0.4802 -0.0088 -0.0507 0.0254  270 ASN A C   
1871 O O   . ASN A 227 ? 0.3617 0.3534 0.4582 -0.0082 -0.0537 0.0212  270 ASN A O   
1872 C CB  . ASN A 227 ? 0.4395 0.4345 0.5484 -0.0127 -0.0518 0.0325  270 ASN A CB  
1873 C CG  . ASN A 227 ? 0.5118 0.5084 0.6280 -0.0149 -0.0503 0.0400  270 ASN A CG  
1874 O OD1 . ASN A 227 ? 0.5461 0.5419 0.6637 -0.0151 -0.0502 0.0445  270 ASN A OD1 
1875 N ND2 . ASN A 227 ? 0.5583 0.5575 0.6796 -0.0164 -0.0490 0.0416  270 ASN A ND2 
1876 N N   . ILE A 228 ? 0.3585 0.3564 0.4437 -0.0077 -0.0484 0.0245  271 ILE A N   
1877 C CA  . ILE A 228 ? 0.3594 0.3564 0.4402 -0.0056 -0.0490 0.0193  271 ILE A CA  
1878 C C   . ILE A 228 ? 0.3737 0.3712 0.4524 -0.0047 -0.0492 0.0213  271 ILE A C   
1879 O O   . ILE A 228 ? 0.4195 0.4193 0.4950 -0.0055 -0.0477 0.0255  271 ILE A O   
1880 C CB  . ILE A 228 ? 0.3764 0.3762 0.4504 -0.0051 -0.0465 0.0160  271 ILE A CB  
1881 C CG1 . ILE A 228 ? 0.3864 0.3851 0.4628 -0.0056 -0.0473 0.0136  271 ILE A CG1 
1882 C CG2 . ILE A 228 ? 0.3358 0.3354 0.4054 -0.0030 -0.0463 0.0119  271 ILE A CG2 
1883 C CD1 . ILE A 228 ? 0.3819 0.3829 0.4522 -0.0051 -0.0451 0.0107  271 ILE A CD1 
1884 N N   . GLN A 229 ? 0.3206 0.3158 0.4011 -0.0029 -0.0510 0.0183  272 GLN A N   
1885 C CA  . GLN A 229 ? 0.3517 0.3473 0.4318 -0.0020 -0.0518 0.0202  272 GLN A CA  
1886 C C   . GLN A 229 ? 0.3313 0.3305 0.4046 -0.0013 -0.0499 0.0186  272 GLN A C   
1887 O O   . GLN A 229 ? 0.3410 0.3416 0.4105 -0.0010 -0.0480 0.0151  272 GLN A O   
1888 C CB  . GLN A 229 ? 0.3280 0.3200 0.4137 0.0000  -0.0542 0.0177  272 GLN A CB  
1889 C CG  . GLN A 229 ? 0.4784 0.4661 0.5716 -0.0007 -0.0569 0.0195  272 GLN A CG  
1890 C CD  . GLN A 229 ? 0.6129 0.5959 0.7107 0.0016  -0.0591 0.0155  272 GLN A CD  
1891 O OE1 . GLN A 229 ? 0.6272 0.6100 0.7222 0.0038  -0.0581 0.0105  272 GLN A OE1 
1892 N NE2 . GLN A 229 ? 0.6685 0.6475 0.7736 0.0014  -0.0619 0.0179  272 GLN A NE2 
1893 N N   . PHE A 230 ? 0.3134 0.3139 0.3855 -0.0012 -0.0508 0.0214  273 PHE A N   
1894 C CA  . PHE A 230 ? 0.3305 0.3340 0.3969 -0.0009 -0.0499 0.0206  273 PHE A CA  
1895 C C   . PHE A 230 ? 0.3250 0.3288 0.3949 0.0006  -0.0520 0.0201  273 PHE A C   
1896 O O   . PHE A 230 ? 0.3343 0.3364 0.4089 0.0010  -0.0544 0.0229  273 PHE A O   
1897 C CB  . PHE A 230 ? 0.3514 0.3564 0.4115 -0.0024 -0.0492 0.0247  273 PHE A CB  
1898 C CG  . PHE A 230 ? 0.3602 0.3675 0.4140 -0.0022 -0.0490 0.0235  273 PHE A CG  
1899 C CD1 . PHE A 230 ? 0.3240 0.3329 0.3742 -0.0023 -0.0467 0.0198  273 PHE A CD1 
1900 C CD2 . PHE A 230 ? 0.3369 0.3444 0.3886 -0.0021 -0.0516 0.0261  273 PHE A CD2 
1901 C CE1 . PHE A 230 ? 0.3641 0.3746 0.4093 -0.0023 -0.0468 0.0186  273 PHE A CE1 
1902 C CE2 . PHE A 230 ? 0.3719 0.3810 0.4183 -0.0022 -0.0521 0.0248  273 PHE A CE2 
1903 C CZ  . PHE A 230 ? 0.3474 0.3580 0.3909 -0.0023 -0.0497 0.0210  273 PHE A CZ  
1904 N N   . SER A 231 ? 0.3383 0.3442 0.4067 0.0014  -0.0510 0.0169  274 SER A N   
1905 C CA  . SER A 231 ? 0.3970 0.4042 0.4695 0.0028  -0.0526 0.0167  274 SER A CA  
1906 C C   . SER A 231 ? 0.3973 0.4077 0.4652 0.0021  -0.0522 0.0160  274 SER A C   
1907 O O   . SER A 231 ? 0.3520 0.3633 0.4149 0.0014  -0.0498 0.0139  274 SER A O   
1908 C CB  . SER A 231 ? 0.4357 0.4420 0.5141 0.0051  -0.0515 0.0130  274 SER A CB  
1909 O OG  . SER A 231 ? 0.5507 0.5592 0.6338 0.0065  -0.0523 0.0127  274 SER A OG  
1910 N N   . CYS A 232 ? 0.3624 0.3741 0.4324 0.0023  -0.0551 0.0179  275 CYS A N   
1911 C CA  . CYS A 232 ? 0.4093 0.4233 0.4756 0.0014  -0.0559 0.0175  275 CYS A CA  
1912 C C   . CYS A 232 ? 0.4139 0.4301 0.4880 0.0026  -0.0580 0.0172  275 CYS A C   
1913 O O   . CYS A 232 ? 0.3708 0.3866 0.4509 0.0035  -0.0608 0.0195  275 CYS A O   
1914 C CB  . CYS A 232 ? 0.4169 0.4300 0.4753 0.0000  -0.0582 0.0208  275 CYS A CB  
1915 S SG  . CYS A 232 ? 0.4448 0.4594 0.4970 -0.0011 -0.0598 0.0195  275 CYS A SG  
1916 N N   . LYS A 233 ? 0.3826 0.4013 0.4575 0.0024  -0.0567 0.0148  276 LYS A N   
1917 C CA  . LYS A 233 ? 0.4182 0.4398 0.5016 0.0032  -0.0584 0.0148  276 LYS A CA  
1918 C C   . LYS A 233 ? 0.4188 0.4420 0.4990 0.0015  -0.0604 0.0146  276 LYS A C   
1919 O O   . LYS A 233 ? 0.3553 0.3779 0.4280 0.0003  -0.0585 0.0129  276 LYS A O   
1920 C CB  . LYS A 233 ? 0.4546 0.4779 0.5451 0.0052  -0.0542 0.0121  276 LYS A CB  
1921 C CG  . LYS A 233 ? 0.5364 0.5575 0.6307 0.0075  -0.0525 0.0114  276 LYS A CG  
1922 C CD  . LYS A 233 ? 0.7190 0.7421 0.8217 0.0101  -0.0492 0.0094  276 LYS A CD  
1923 C CE  . LYS A 233 ? 0.7889 0.8147 0.8902 0.0097  -0.0456 0.0073  276 LYS A CE  
1924 N NZ  . LYS A 233 ? 0.8156 0.8435 0.9248 0.0125  -0.0417 0.0059  276 LYS A NZ  
1925 N N   . ASN A 234 ? 0.3359 0.3610 0.4226 0.0014  -0.0646 0.0162  277 ASN A N   
1926 C CA  . ASN A 234 ? 0.3651 0.3918 0.4514 -0.0001 -0.0673 0.0157  277 ASN A CA  
1927 C C   . ASN A 234 ? 0.3665 0.3969 0.4625 0.0005  -0.0642 0.0139  277 ASN A C   
1928 O O   . ASN A 234 ? 0.3582 0.3909 0.4648 0.0023  -0.0631 0.0145  277 ASN A O   
1929 C CB  . ASN A 234 ? 0.4007 0.4274 0.4892 -0.0007 -0.0742 0.0185  277 ASN A CB  
1930 C CG  . ASN A 234 ? 0.4193 0.4421 0.4968 -0.0013 -0.0771 0.0208  277 ASN A CG  
1931 O OD1 . ASN A 234 ? 0.4085 0.4289 0.4749 -0.0026 -0.0782 0.0203  277 ASN A OD1 
1932 N ND2 . ASN A 234 ? 0.3813 0.4030 0.4617 -0.0001 -0.0781 0.0235  277 ASN A ND2 
1933 N N   . ILE A 235 ? 0.3639 0.3948 0.4565 -0.0008 -0.0625 0.0119  278 ILE A N   
1934 C CA  . ILE A 235 ? 0.3603 0.3948 0.4622 -0.0007 -0.0602 0.0109  278 ILE A CA  
1935 C C   . ILE A 235 ? 0.3534 0.3890 0.4586 -0.0027 -0.0661 0.0118  278 ILE A C   
1936 O O   . ILE A 235 ? 0.3837 0.4176 0.4821 -0.0046 -0.0675 0.0105  278 ILE A O   
1937 C CB  . ILE A 235 ? 0.3521 0.3861 0.4488 -0.0008 -0.0546 0.0084  278 ILE A CB  
1938 C CG1 . ILE A 235 ? 0.3836 0.4158 0.4759 0.0011  -0.0499 0.0073  278 ILE A CG1 
1939 C CG2 . ILE A 235 ? 0.3540 0.3919 0.4608 -0.0005 -0.0518 0.0082  278 ILE A CG2 
1940 C CD1 . ILE A 235 ? 0.4357 0.4698 0.5373 0.0038  -0.0470 0.0075  278 ILE A CD1 
1941 N N   . TYR A 236 ? 0.3874 0.4255 0.5034 -0.0022 -0.0701 0.0141  279 TYR A N   
1942 C CA  . TYR A 236 ? 0.3982 0.4367 0.5173 -0.0042 -0.0773 0.0151  279 TYR A CA  
1943 C C   . TYR A 236 ? 0.4346 0.4761 0.5618 -0.0056 -0.0765 0.0142  279 TYR A C   
1944 O O   . TYR A 236 ? 0.4478 0.4876 0.5718 -0.0079 -0.0814 0.0134  279 TYR A O   
1945 C CB  . TYR A 236 ? 0.4057 0.4463 0.5353 -0.0032 -0.0822 0.0181  279 TYR A CB  
1946 C CG  . TYR A 236 ? 0.3809 0.4180 0.5026 -0.0024 -0.0850 0.0198  279 TYR A CG  
1947 C CD1 . TYR A 236 ? 0.3832 0.4162 0.4928 -0.0038 -0.0906 0.0204  279 TYR A CD1 
1948 C CD2 . TYR A 236 ? 0.3567 0.3943 0.4830 0.0000  -0.0820 0.0210  279 TYR A CD2 
1949 C CE1 . TYR A 236 ? 0.3657 0.3955 0.4682 -0.0030 -0.0928 0.0227  279 TYR A CE1 
1950 C CE2 . TYR A 236 ? 0.3423 0.3767 0.4624 0.0006  -0.0846 0.0231  279 TYR A CE2 
1951 C CZ  . TYR A 236 ? 0.3764 0.4071 0.4848 -0.0010 -0.0898 0.0242  279 TYR A CZ  
1952 O OH  . TYR A 236 ? 0.4022 0.4297 0.5044 -0.0003 -0.0920 0.0268  279 TYR A OH  
1953 N N   . ARG A 237 ? 0.4095 0.4549 0.5469 -0.0042 -0.0705 0.0143  280 ARG A N   
1954 C CA  . ARG A 237 ? 0.4366 0.4856 0.5845 -0.0053 -0.0690 0.0144  280 ARG A CA  
1955 C C   . ARG A 237 ? 0.4085 0.4574 0.5520 -0.0044 -0.0607 0.0126  280 ARG A C   
1956 O O   . ARG A 237 ? 0.4062 0.4581 0.5568 -0.0021 -0.0546 0.0132  280 ARG A O   
1957 C CB  . ARG A 237 ? 0.4563 0.5110 0.6229 -0.0042 -0.0694 0.0171  280 ARG A CB  
1958 C CG  . ARG A 237 ? 0.5045 0.5595 0.6761 -0.0041 -0.0769 0.0193  280 ARG A CG  
1959 C CD  . ARG A 237 ? 0.4622 0.5157 0.6335 -0.0072 -0.0861 0.0196  280 ARG A CD  
1960 N NE  . ARG A 237 ? 0.4613 0.5196 0.6491 -0.0086 -0.0875 0.0209  280 ARG A NE  
1961 C CZ  . ARG A 237 ? 0.4119 0.4744 0.6159 -0.0086 -0.0924 0.0237  280 ARG A CZ  
1962 N NH1 . ARG A 237 ? 0.3685 0.4308 0.5741 -0.0072 -0.0969 0.0255  280 ARG A NH1 
1963 N NH2 . ARG A 237 ? 0.4201 0.4873 0.6400 -0.0101 -0.0930 0.0251  280 ARG A NH2 
1964 N N   . PRO A 238 ? 0.4057 0.4509 0.5373 -0.0060 -0.0602 0.0104  281 PRO A N   
1965 C CA  . PRO A 238 ? 0.4176 0.4623 0.5442 -0.0050 -0.0528 0.0089  281 PRO A CA  
1966 C C   . PRO A 238 ? 0.4330 0.4821 0.5718 -0.0045 -0.0479 0.0101  281 PRO A C   
1967 O O   . PRO A 238 ? 0.4087 0.4587 0.5469 -0.0022 -0.0410 0.0099  281 PRO A O   
1968 C CB  . PRO A 238 ? 0.3963 0.4368 0.5110 -0.0072 -0.0547 0.0068  281 PRO A CB  
1969 C CG  . PRO A 238 ? 0.4307 0.4683 0.5393 -0.0083 -0.0618 0.0068  281 PRO A CG  
1970 C CD  . PRO A 238 ? 0.4105 0.4515 0.5319 -0.0083 -0.0663 0.0092  281 PRO A CD  
1971 N N   . ASP A 239 ? 0.4227 0.4745 0.5726 -0.0065 -0.0513 0.0116  282 ASP A N   
1972 C CA  . ASP A 239 ? 0.4707 0.5272 0.6336 -0.0061 -0.0463 0.0135  282 ASP A CA  
1973 C C   . ASP A 239 ? 0.4517 0.5124 0.6245 -0.0028 -0.0417 0.0154  282 ASP A C   
1974 O O   . ASP A 239 ? 0.4676 0.5306 0.6439 -0.0008 -0.0341 0.0161  282 ASP A O   
1975 C CB  . ASP A 239 ? 0.5026 0.5612 0.6772 -0.0092 -0.0518 0.0151  282 ASP A CB  
1976 C CG  . ASP A 239 ? 0.5517 0.6116 0.7339 -0.0099 -0.0598 0.0163  282 ASP A CG  
1977 O OD1 . ASP A 239 ? 0.5471 0.6042 0.7202 -0.0090 -0.0629 0.0154  282 ASP A OD1 
1978 O OD2 . ASP A 239 ? 0.5944 0.6582 0.7921 -0.0114 -0.0631 0.0186  282 ASP A OD2 
1979 N N   . LYS A 240 ? 0.4546 0.5161 0.6316 -0.0020 -0.0462 0.0162  283 LYS A N   
1980 C CA  . LYS A 240 ? 0.4561 0.5210 0.6424 0.0014  -0.0420 0.0177  283 LYS A CA  
1981 C C   . LYS A 240 ? 0.4426 0.5041 0.6169 0.0045  -0.0364 0.0155  283 LYS A C   
1982 O O   . LYS A 240 ? 0.4747 0.5382 0.6537 0.0078  -0.0298 0.0158  283 LYS A O   
1983 C CB  . LYS A 240 ? 0.4873 0.5536 0.6818 0.0014  -0.0490 0.0194  283 LYS A CB  
1984 C CG  . LYS A 240 ? 0.4995 0.5687 0.7059 -0.0017 -0.0560 0.0215  283 LYS A CG  
1985 C CD  . LYS A 240 ? 0.5479 0.6239 0.7738 -0.0010 -0.0519 0.0245  283 LYS A CD  
1986 C CE  . LYS A 240 ? 0.5520 0.6305 0.7900 -0.0047 -0.0592 0.0263  283 LYS A CE  
1987 N NZ  . LYS A 240 ? 0.6529 0.7387 0.9118 -0.0042 -0.0550 0.0299  283 LYS A NZ  
1988 N N   . PHE A 241 ? 0.4330 0.4893 0.5921 0.0035  -0.0389 0.0132  284 PHE A N   
1989 C CA  . PHE A 241 ? 0.4259 0.4786 0.5741 0.0059  -0.0345 0.0110  284 PHE A CA  
1990 C C   . PHE A 241 ? 0.4662 0.5190 0.6111 0.0073  -0.0269 0.0100  284 PHE A C   
1991 O O   . PHE A 241 ? 0.4874 0.5396 0.6308 0.0106  -0.0215 0.0091  284 PHE A O   
1992 C CB  . PHE A 241 ? 0.4157 0.4634 0.5498 0.0042  -0.0387 0.0093  284 PHE A CB  
1993 C CG  . PHE A 241 ? 0.4216 0.4655 0.5441 0.0058  -0.0346 0.0070  284 PHE A CG  
1994 C CD1 . PHE A 241 ? 0.4486 0.4910 0.5707 0.0085  -0.0333 0.0065  284 PHE A CD1 
1995 C CD2 . PHE A 241 ? 0.4338 0.4754 0.5465 0.0047  -0.0325 0.0053  284 PHE A CD2 
1996 C CE1 . PHE A 241 ? 0.4792 0.5177 0.5913 0.0098  -0.0304 0.0042  284 PHE A CE1 
1997 C CE2 . PHE A 241 ? 0.4290 0.4672 0.5319 0.0061  -0.0294 0.0033  284 PHE A CE2 
1998 C CZ  . PHE A 241 ? 0.4356 0.4721 0.5381 0.0085  -0.0286 0.0027  284 PHE A CZ  
1999 N N   . LEU A 242 ? 0.4835 0.5365 0.6267 0.0049  -0.0266 0.0101  285 LEU A N   
2000 C CA  . LEU A 242 ? 0.4410 0.4942 0.5816 0.0062  -0.0195 0.0098  285 LEU A CA  
2001 C C   . LEU A 242 ? 0.5188 0.5767 0.6719 0.0088  -0.0137 0.0120  285 LEU A C   
2002 O O   . LEU A 242 ? 0.5501 0.6073 0.6992 0.0120  -0.0069 0.0114  285 LEU A O   
2003 C CB  . LEU A 242 ? 0.4351 0.4878 0.5737 0.0029  -0.0208 0.0100  285 LEU A CB  
2004 C CG  . LEU A 242 ? 0.4469 0.4946 0.5707 0.0014  -0.0230 0.0075  285 LEU A CG  
2005 C CD1 . LEU A 242 ? 0.4391 0.4864 0.5635 -0.0018 -0.0251 0.0078  285 LEU A CD1 
2006 C CD2 . LEU A 242 ? 0.4163 0.4613 0.5297 0.0038  -0.0175 0.0058  285 LEU A CD2 
2007 N N   . GLN A 243 ? 0.5096 0.5723 0.6778 0.0078  -0.0163 0.0148  286 GLN A N   
2008 C CA  . GLN A 243 ? 0.6019 0.6698 0.7841 0.0104  -0.0105 0.0174  286 GLN A CA  
2009 C C   . GLN A 243 ? 0.6388 0.7059 0.8196 0.0150  -0.0065 0.0163  286 GLN A C   
2010 O O   . GLN A 243 ? 0.7108 0.7798 0.8951 0.0185  0.0013  0.0171  286 GLN A O   
2011 C CB  . GLN A 243 ? 0.6145 0.6876 0.8143 0.0082  -0.0155 0.0206  286 GLN A CB  
2012 C CG  . GLN A 243 ? 0.7678 0.8467 0.9842 0.0113  -0.0113 0.0234  286 GLN A CG  
2013 C CD  . GLN A 243 ? 0.8088 0.8933 1.0441 0.0087  -0.0165 0.0269  286 GLN A CD  
2014 O OE1 . GLN A 243 ? 0.7506 0.8340 0.9856 0.0045  -0.0235 0.0269  286 GLN A OE1 
2015 N NE2 . GLN A 243 ? 0.8859 0.9761 1.1379 0.0113  -0.0132 0.0298  286 GLN A NE2 
2016 N N   . CYS A 244 ? 0.6178 0.6817 0.7933 0.0152  -0.0115 0.0145  287 CYS A N   
2017 C CA  . CYS A 244 ? 0.6849 0.7473 0.8592 0.0194  -0.0085 0.0131  287 CYS A CA  
2018 C C   . CYS A 244 ? 0.7365 0.7937 0.8954 0.0217  -0.0034 0.0099  287 CYS A C   
2019 O O   . CYS A 244 ? 0.7814 0.8376 0.9397 0.0260  0.0020  0.0087  287 CYS A O   
2020 C CB  . CYS A 244 ? 0.6446 0.7049 0.8187 0.0187  -0.0158 0.0127  287 CYS A CB  
2021 S SG  . CYS A 244 ? 0.8329 0.8899 1.0051 0.0236  -0.0132 0.0107  287 CYS A SG  
2022 N N   . VAL A 245 ? 0.6317 0.6853 0.7781 0.0191  -0.0054 0.0083  288 VAL A N   
2023 C CA  . VAL A 245 ? 0.6846 0.7333 0.8168 0.0211  -0.0014 0.0054  288 VAL A CA  
2024 C C   . VAL A 245 ? 0.7282 0.7786 0.8611 0.0234  0.0066  0.0063  288 VAL A C   
2025 O O   . VAL A 245 ? 0.7069 0.7540 0.8312 0.0269  0.0115  0.0042  288 VAL A O   
2026 C CB  . VAL A 245 ? 0.6210 0.6660 0.7414 0.0177  -0.0057 0.0038  288 VAL A CB  
2027 C CG1 . VAL A 245 ? 0.6569 0.6972 0.7638 0.0195  -0.0021 0.0011  288 VAL A CG1 
2028 C CG2 . VAL A 245 ? 0.5197 0.5627 0.6384 0.0159  -0.0127 0.0032  288 VAL A CG2 
2029 N N   . LYS A 246 ? 0.8056 0.8609 0.9484 0.0215  0.0079  0.0095  289 LYS A N   
2030 C CA  . LYS A 246 ? 0.8873 0.9446 1.0314 0.0234  0.0158  0.0112  289 LYS A CA  
2031 C C   . LYS A 246 ? 0.9997 1.0598 1.1520 0.0282  0.0225  0.0124  289 LYS A C   
2032 O O   . LYS A 246 ? 1.0564 1.1148 1.2020 0.0319  0.0298  0.0118  289 LYS A O   
2033 C CB  . LYS A 246 ? 0.8498 0.9114 1.0036 0.0196  0.0147  0.0147  289 LYS A CB  
2034 C CG  . LYS A 246 ? 0.9768 1.0372 1.1236 0.0193  0.0196  0.0156  289 LYS A CG  
2035 C CD  . LYS A 246 ? 0.9714 1.0346 1.1265 0.0148  0.0165  0.0183  289 LYS A CD  
2036 C CE  . LYS A 246 ? 0.9093 0.9705 1.0621 0.0107  0.0071  0.0164  289 LYS A CE  
2037 N NZ  . LYS A 246 ? 0.9327 0.9934 1.0861 0.0067  0.0042  0.0174  289 LYS A NZ  
2038 N N   . ASN A 247 ? 1.0685 1.1326 1.2349 0.0284  0.0201  0.0139  290 ASN A N   
2039 C CA  . ASN A 247 ? 1.1726 1.2404 1.3501 0.0330  0.0265  0.0155  290 ASN A CA  
2040 C C   . ASN A 247 ? 1.1966 1.2635 1.3783 0.0346  0.0224  0.0140  290 ASN A C   
2041 O O   . ASN A 247 ? 1.2473 1.3193 1.4451 0.0341  0.0198  0.0167  290 ASN A O   
2042 C CB  . ASN A 247 ? 1.2460 1.3216 1.4421 0.0316  0.0289  0.0206  290 ASN A CB  
2043 C CG  . ASN A 247 ? 1.2308 1.3089 1.4354 0.0259  0.0197  0.0222  290 ASN A CG  
2044 O OD1 . ASN A 247 ? 1.1591 1.2369 1.3608 0.0222  0.0176  0.0230  290 ASN A OD1 
2045 N ND2 . ASN A 247 ? 1.3048 1.3850 1.5194 0.0255  0.0139  0.0227  290 ASN A ND2 
2046 N N   . PRO A 248 ? 1.1591 1.2194 1.3273 0.0366  0.0212  0.0099  291 PRO A N   
2047 C CA  . PRO A 248 ? 1.1766 1.2354 1.3489 0.0384  0.0176  0.0086  291 PRO A CA  
2048 C C   . PRO A 248 ? 1.1890 1.2488 1.3678 0.0444  0.0248  0.0083  291 PRO A C   
2049 O O   . PRO A 248 ? 1.1533 1.2082 1.3266 0.0478  0.0249  0.0051  291 PRO A O   
2050 C CB  . PRO A 248 ? 1.1392 1.1903 1.2945 0.0378  0.0136  0.0044  291 PRO A CB  
2051 C CG  . PRO A 248 ? 1.0760 1.1240 1.2181 0.0387  0.0188  0.0027  291 PRO A CG  
2052 C CD  . PRO A 248 ? 1.0954 1.1491 1.2446 0.0365  0.0218  0.0064  291 PRO A CD  
2053 N N   . GLU A 249 ? 1.1624 1.2286 1.3538 0.0459  0.0311  0.0119  292 GLU A N   
2054 C CA  . GLU A 249 ? 1.1273 1.1954 1.3263 0.0520  0.0391  0.0122  292 GLU A CA  
2055 C C   . GLU A 249 ? 1.1106 1.1851 1.3309 0.0520  0.0365  0.0156  292 GLU A C   
2056 O O   . GLU A 249 ? 1.0279 1.1101 1.2642 0.0510  0.0388  0.0201  292 GLU A O   
2057 C CB  . GLU A 249 ? 1.0213 1.0923 1.2203 0.0544  0.0492  0.0144  292 GLU A CB  
2058 N N   . SER B 1   ? 0.9139 0.6994 0.6971 -0.0745 -0.0195 -0.0008 44  SER B N   
2059 C CA  . SER B 1   ? 0.8835 0.6718 0.6717 -0.0845 -0.0299 0.0016  44  SER B CA  
2060 C C   . SER B 1   ? 0.8407 0.6043 0.6048 -0.0883 -0.0366 -0.0011 44  SER B C   
2061 O O   . SER B 1   ? 0.7913 0.5421 0.5390 -0.0814 -0.0322 -0.0048 44  SER B O   
2062 C CB  . SER B 1   ? 0.8550 0.6680 0.6644 -0.0832 -0.0307 0.0035  44  SER B CB  
2063 O OG  . SER B 1   ? 0.8402 0.6548 0.6535 -0.0920 -0.0413 0.0059  44  SER B OG  
2064 N N   . ARG B 2   ? 0.7884 0.5450 0.5500 -0.0993 -0.0473 0.0012  45  ARG B N   
2065 C CA  . ARG B 2   ? 0.7852 0.5164 0.5221 -0.1042 -0.0553 -0.0012 45  ARG B CA  
2066 C C   . ARG B 2   ? 0.7954 0.5317 0.5327 -0.1038 -0.0601 -0.0016 45  ARG B C   
2067 O O   . ARG B 2   ? 0.7795 0.4938 0.4943 -0.1073 -0.0667 -0.0037 45  ARG B O   
2068 C CB  . ARG B 2   ? 0.8090 0.5298 0.5428 -0.1171 -0.0663 0.0017  45  ARG B CB  
2069 C CG  . ARG B 2   ? 0.8401 0.5854 0.6019 -0.1253 -0.0739 0.0076  45  ARG B CG  
2070 C CD  . ARG B 2   ? 0.8686 0.5998 0.6236 -0.1390 -0.0874 0.0103  45  ARG B CD  
2071 N NE  . ARG B 2   ? 0.8559 0.6109 0.6404 -0.1471 -0.0934 0.0170  45  ARG B NE  
2072 C CZ  . ARG B 2   ? 0.8712 0.6215 0.6581 -0.1598 -0.1066 0.0209  45  ARG B CZ  
2073 N NH1 . ARG B 2   ? 0.9238 0.6450 0.6837 -0.1665 -0.1161 0.0185  45  ARG B NH1 
2074 N NH2 . ARG B 2   ? 0.9135 0.6884 0.7307 -0.1661 -0.1101 0.0276  45  ARG B NH2 
2075 N N   . TRP B 3   ? 0.7733 0.5363 0.5341 -0.0997 -0.0570 0.0003  46  TRP B N   
2076 C CA  . TRP B 3   ? 0.7625 0.5313 0.5247 -0.0983 -0.0606 0.0000  46  TRP B CA  
2077 C C   . TRP B 3   ? 0.7479 0.5196 0.5067 -0.0865 -0.0500 -0.0034 46  TRP B C   
2078 O O   . TRP B 3   ? 0.6946 0.4687 0.4517 -0.0845 -0.0519 -0.0040 46  TRP B O   
2079 C CB  . TRP B 3   ? 0.7529 0.5494 0.5446 -0.1025 -0.0657 0.0051  46  TRP B CB  
2080 C CG  . TRP B 3   ? 0.7206 0.5223 0.5249 -0.1131 -0.0736 0.0098  46  TRP B CG  
2081 C CD1 . TRP B 3   ? 0.6952 0.5174 0.5236 -0.1140 -0.0699 0.0137  46  TRP B CD1 
2082 C CD2 . TRP B 3   ? 0.7021 0.4879 0.4956 -0.1244 -0.0866 0.0115  46  TRP B CD2 
2083 N NE1 . TRP B 3   ? 0.7175 0.5388 0.5524 -0.1252 -0.0791 0.0180  46  TRP B NE1 
2084 C CE2 . TRP B 3   ? 0.7139 0.5132 0.5282 -0.1321 -0.0900 0.0168  46  TRP B CE2 
2085 C CE3 . TRP B 3   ? 0.6993 0.4596 0.4667 -0.1291 -0.0957 0.0092  46  TRP B CE3 
2086 C CZ2 . TRP B 3   ? 0.7069 0.4964 0.5186 -0.1446 -0.1028 0.0201  46  TRP B CZ2 
2087 C CZ3 . TRP B 3   ? 0.7042 0.4534 0.4671 -0.1416 -0.1090 0.0121  46  TRP B CZ3 
2088 C CH2 . TRP B 3   ? 0.7195 0.4839 0.5054 -0.1494 -0.1126 0.0176  46  TRP B CH2 
2089 N N   . ARG B 4   ? 0.7143 0.4860 0.4724 -0.0788 -0.0393 -0.0052 47  ARG B N   
2090 C CA  . ARG B 4   ? 0.7163 0.4953 0.4768 -0.0681 -0.0294 -0.0074 47  ARG B CA  
2091 C C   . ARG B 4   ? 0.7163 0.4722 0.4509 -0.0639 -0.0271 -0.0111 47  ARG B C   
2092 O O   . ARG B 4   ? 0.7078 0.4397 0.4204 -0.0644 -0.0262 -0.0133 47  ARG B O   
2093 C CB  . ARG B 4   ? 0.7390 0.5251 0.5076 -0.0616 -0.0196 -0.0076 47  ARG B CB  
2094 C CG  . ARG B 4   ? 0.7040 0.5052 0.4836 -0.0518 -0.0109 -0.0084 47  ARG B CG  
2095 C CD  . ARG B 4   ? 0.6523 0.4656 0.4451 -0.0473 -0.0039 -0.0074 47  ARG B CD  
2096 N NE  . ARG B 4   ? 0.6571 0.4535 0.4352 -0.0429 0.0019  -0.0092 47  ARG B NE  
2097 C CZ  . ARG B 4   ? 0.7052 0.5074 0.4904 -0.0384 0.0078  -0.0085 47  ARG B CZ  
2098 N NH1 . ARG B 4   ? 0.6279 0.4513 0.4331 -0.0378 0.0091  -0.0063 47  ARG B NH1 
2099 N NH2 . ARG B 4   ? 0.7544 0.5399 0.5257 -0.0341 0.0127  -0.0098 47  ARG B NH2 
2100 N N   . GLN B 5   ? 0.7128 0.4753 0.4494 -0.0596 -0.0255 -0.0118 48  GLN B N   
2101 C CA  . GLN B 5   ? 0.7437 0.4860 0.4569 -0.0550 -0.0221 -0.0149 48  GLN B CA  
2102 C C   . GLN B 5   ? 0.7586 0.5039 0.4735 -0.0438 -0.0089 -0.0165 48  GLN B C   
2103 O O   . GLN B 5   ? 0.7114 0.4772 0.4473 -0.0398 -0.0038 -0.0151 48  GLN B O   
2104 C CB  . GLN B 5   ? 0.7578 0.5041 0.4710 -0.0568 -0.0279 -0.0143 48  GLN B CB  
2105 C CG  . GLN B 5   ? 0.6817 0.4558 0.4204 -0.0523 -0.0245 -0.0125 48  GLN B CG  
2106 C CD  . GLN B 5   ? 0.6957 0.4762 0.4385 -0.0564 -0.0330 -0.0107 48  GLN B CD  
2107 O OE1 . GLN B 5   ? 0.6684 0.4411 0.3995 -0.0531 -0.0316 -0.0120 48  GLN B OE1 
2108 N NE2 . GLN B 5   ? 0.6222 0.4172 0.3823 -0.0636 -0.0418 -0.0073 48  GLN B NE2 
2109 N N   . GLN B 6   ? 0.8207 0.5446 0.5129 -0.0389 -0.0034 -0.0191 49  GLN B N   
2110 C CA  . GLN B 6   ? 0.8206 0.5463 0.5143 -0.0281 0.0092  -0.0201 49  GLN B CA  
2111 C C   . GLN B 6   ? 0.7824 0.5230 0.4869 -0.0238 0.0121  -0.0195 49  GLN B C   
2112 O O   . GLN B 6   ? 0.7583 0.4930 0.4536 -0.0267 0.0071  -0.0198 49  GLN B O   
2113 C CB  . GLN B 6   ? 0.9047 0.6004 0.5696 -0.0241 0.0151  -0.0227 49  GLN B CB  
2114 C CG  . GLN B 6   ? 0.9340 0.6302 0.6001 -0.0126 0.0287  -0.0231 49  GLN B CG  
2115 C CD  . GLN B 6   ? 1.0156 0.7244 0.6986 -0.0081 0.0344  -0.0218 49  GLN B CD  
2116 O OE1 . GLN B 6   ? 1.0839 0.7947 0.7715 -0.0131 0.0295  -0.0211 49  GLN B OE1 
2117 N NE2 . GLN B 6   ? 1.0094 0.7265 0.7017 0.0013  0.0446  -0.0210 49  GLN B NE2 
2118 N N   . TRP B 7   ? 0.6739 0.4334 0.3978 -0.0171 0.0196  -0.0184 50  TRP B N   
2119 C CA  . TRP B 7   ? 0.6492 0.4221 0.3835 -0.0121 0.0238  -0.0178 50  TRP B CA  
2120 C C   . TRP B 7   ? 0.6595 0.4222 0.3847 -0.0030 0.0353  -0.0186 50  TRP B C   
2121 O O   . TRP B 7   ? 0.6570 0.4062 0.3720 0.0004  0.0407  -0.0194 50  TRP B O   
2122 C CB  . TRP B 7   ? 0.5826 0.3835 0.3451 -0.0114 0.0236  -0.0158 50  TRP B CB  
2123 C CG  . TRP B 7   ? 0.5454 0.3577 0.3193 -0.0193 0.0141  -0.0144 50  TRP B CG  
2124 C CD1 . TRP B 7   ? 0.5208 0.3420 0.3062 -0.0220 0.0124  -0.0132 50  TRP B CD1 
2125 C CD2 . TRP B 7   ? 0.5495 0.3654 0.3248 -0.0255 0.0053  -0.0135 50  TRP B CD2 
2126 N NE1 . TRP B 7   ? 0.5009 0.3317 0.2957 -0.0293 0.0038  -0.0115 50  TRP B NE1 
2127 C CE2 . TRP B 7   ? 0.5075 0.3356 0.2970 -0.0315 -0.0010 -0.0115 50  TRP B CE2 
2128 C CE3 . TRP B 7   ? 0.5432 0.3531 0.3093 -0.0264 0.0021  -0.0138 50  TRP B CE3 
2129 C CZ2 . TRP B 7   ? 0.5122 0.3479 0.3090 -0.0381 -0.0102 -0.0096 50  TRP B CZ2 
2130 C CZ3 . TRP B 7   ? 0.5514 0.3680 0.3236 -0.0331 -0.0078 -0.0120 50  TRP B CZ3 
2131 C CH2 . TRP B 7   ? 0.5273 0.3573 0.3155 -0.0388 -0.0138 -0.0098 50  TRP B CH2 
2132 N N   . SER B 8   ? 0.6432 0.4127 0.3728 0.0010  0.0394  -0.0181 51  SER B N   
2133 C CA  . SER B 8   ? 0.6992 0.4609 0.4224 0.0097  0.0509  -0.0181 51  SER B CA  
2134 C C   . SER B 8   ? 0.7048 0.4865 0.4514 0.0160  0.0578  -0.0161 51  SER B C   
2135 O O   . SER B 8   ? 0.7455 0.5220 0.4901 0.0234  0.0677  -0.0154 51  SER B O   
2136 C CB  . SER B 8   ? 0.7629 0.5189 0.4765 0.0107  0.0522  -0.0182 51  SER B CB  
2137 O OG  . SER B 8   ? 0.8193 0.5544 0.5088 0.0050  0.0454  -0.0200 51  SER B OG  
2138 N N   . GLY B 9   ? 0.6432 0.4471 0.4116 0.0133  0.0528  -0.0149 52  GLY B N   
2139 C CA  . GLY B 9   ? 0.6201 0.4423 0.4096 0.0184  0.0577  -0.0130 52  GLY B CA  
2140 C C   . GLY B 9   ? 0.5942 0.4173 0.3885 0.0194  0.0585  -0.0126 52  GLY B C   
2141 O O   . GLY B 9   ? 0.6092 0.4221 0.3935 0.0150  0.0541  -0.0137 52  GLY B O   
2142 N N   . PRO B 10  ? 0.5900 0.4253 0.3999 0.0250  0.0637  -0.0106 53  PRO B N   
2143 C CA  . PRO B 10  ? 0.5716 0.4084 0.3866 0.0263  0.0641  -0.0098 53  PRO B CA  
2144 C C   . PRO B 10  ? 0.5278 0.3746 0.3503 0.0197  0.0559  -0.0100 53  PRO B C   
2145 O O   . PRO B 10  ? 0.5267 0.3861 0.3582 0.0158  0.0510  -0.0101 53  PRO B O   
2146 C CB  . PRO B 10  ? 0.5613 0.4119 0.3938 0.0331  0.0697  -0.0071 53  PRO B CB  
2147 C CG  . PRO B 10  ? 0.6325 0.4945 0.4739 0.0329  0.0695  -0.0068 53  PRO B CG  
2148 C CD  . PRO B 10  ? 0.5583 0.4060 0.3818 0.0301  0.0688  -0.0088 53  PRO B CD  
2149 N N   . GLY B 11  ? 0.5373 0.3779 0.3561 0.0186  0.0549  -0.0099 54  GLY B N   
2150 C CA  . GLY B 11  ? 0.5423 0.3910 0.3676 0.0126  0.0484  -0.0096 54  GLY B CA  
2151 C C   . GLY B 11  ? 0.4937 0.3618 0.3382 0.0144  0.0483  -0.0078 54  GLY B C   
2152 O O   . GLY B 11  ? 0.4860 0.3615 0.3395 0.0201  0.0524  -0.0066 54  GLY B O   
2153 N N   . THR B 12  ? 0.4778 0.3537 0.3282 0.0093  0.0433  -0.0074 55  THR B N   
2154 C CA  . THR B 12  ? 0.4255 0.3178 0.2912 0.0104  0.0427  -0.0060 55  THR B CA  
2155 C C   . THR B 12  ? 0.4536 0.3455 0.3226 0.0163  0.0466  -0.0044 55  THR B C   
2156 O O   . THR B 12  ? 0.4502 0.3299 0.3105 0.0178  0.0486  -0.0041 55  THR B O   
2157 C CB  . THR B 12  ? 0.4415 0.3384 0.3100 0.0043  0.0382  -0.0055 55  THR B CB  
2158 O OG1 . THR B 12  ? 0.4580 0.3579 0.3270 -0.0010 0.0341  -0.0062 55  THR B OG1 
2159 C CG2 . THR B 12  ? 0.4059 0.3168 0.2871 0.0058  0.0382  -0.0041 55  THR B CG2 
2160 N N   . THR B 13  ? 0.4458 0.3507 0.3277 0.0197  0.0474  -0.0033 56  THR B N   
2161 C CA  . THR B 13  ? 0.4473 0.3537 0.3347 0.0252  0.0500  -0.0011 56  THR B CA  
2162 C C   . THR B 13  ? 0.4383 0.3403 0.3221 0.0237  0.0483  -0.0001 56  THR B C   
2163 O O   . THR B 13  ? 0.3986 0.3042 0.2826 0.0187  0.0448  -0.0005 56  THR B O   
2164 C CB  . THR B 13  ? 0.4445 0.3662 0.3464 0.0270  0.0489  0.0001  56  THR B CB  
2165 O OG1 . THR B 13  ? 0.4355 0.3615 0.3408 0.0276  0.0502  -0.0007 56  THR B OG1 
2166 C CG2 . THR B 13  ? 0.4380 0.3615 0.3468 0.0327  0.0508  0.0029  56  THR B CG2 
2167 N N   . LYS B 14  ? 0.5069 0.4006 0.3875 0.0283  0.0514  0.0014  57  LYS B N   
2168 C CA  . LYS B 14  ? 0.5429 0.4312 0.4194 0.0275  0.0500  0.0027  57  LYS B CA  
2169 C C   . LYS B 14  ? 0.4700 0.3706 0.3558 0.0262  0.0463  0.0041  57  LYS B C   
2170 O O   . LYS B 14  ? 0.4682 0.3798 0.3647 0.0289  0.0457  0.0050  57  LYS B O   
2171 C CB  . LYS B 14  ? 0.6441 0.5231 0.5181 0.0341  0.0541  0.0047  57  LYS B CB  
2172 C CG  . LYS B 14  ? 0.7950 0.6569 0.6548 0.0350  0.0581  0.0032  57  LYS B CG  
2173 C CD  . LYS B 14  ? 0.9263 0.7813 0.7864 0.0433  0.0641  0.0053  57  LYS B CD  
2174 C CE  . LYS B 14  ? 0.9248 0.7638 0.7709 0.0450  0.0692  0.0034  57  LYS B CE  
2175 N NZ  . LYS B 14  ? 0.9436 0.7683 0.7728 0.0383  0.0662  0.0005  57  LYS B NZ  
2176 N N   . ARG B 15  ? 0.4275 0.3254 0.3085 0.0218  0.0440  0.0042  58  ARG B N   
2177 C CA  . ARG B 15  ? 0.4825 0.3891 0.3688 0.0204  0.0411  0.0055  58  ARG B CA  
2178 C C   . ARG B 15  ? 0.4406 0.3600 0.3350 0.0184  0.0394  0.0042  58  ARG B C   
2179 O O   . ARG B 15  ? 0.4392 0.3666 0.3395 0.0194  0.0376  0.0051  58  ARG B O   
2180 C CB  . ARG B 15  ? 0.4956 0.4033 0.3863 0.0258  0.0408  0.0082  58  ARG B CB  
2181 C CG  . ARG B 15  ? 0.5658 0.4609 0.4494 0.0289  0.0426  0.0100  58  ARG B CG  
2182 C CD  . ARG B 15  ? 0.6186 0.5146 0.5041 0.0312  0.0402  0.0131  58  ARG B CD  
2183 N NE  . ARG B 15  ? 0.6556 0.5470 0.5331 0.0265  0.0386  0.0133  58  ARG B NE  
2184 C CZ  . ARG B 15  ? 0.5862 0.4811 0.4640 0.0256  0.0357  0.0150  58  ARG B CZ  
2185 N NH1 . ARG B 15  ? 0.5672 0.4702 0.4526 0.0287  0.0329  0.0164  58  ARG B NH1 
2186 N NH2 . ARG B 15  ? 0.5736 0.4632 0.4434 0.0213  0.0355  0.0154  58  ARG B NH2 
2187 N N   . PHE B 16  ? 0.4240 0.3445 0.3177 0.0153  0.0397  0.0022  59  PHE B N   
2188 C CA  . PHE B 16  ? 0.4230 0.3549 0.3242 0.0138  0.0383  0.0010  59  PHE B CA  
2189 C C   . PHE B 16  ? 0.4104 0.3485 0.3138 0.0109  0.0367  0.0016  59  PHE B C   
2190 O O   . PHE B 16  ? 0.3804 0.3264 0.2898 0.0125  0.0357  0.0016  59  PHE B O   
2191 C CB  . PHE B 16  ? 0.4145 0.3450 0.3135 0.0107  0.0383  -0.0008 59  PHE B CB  
2192 C CG  . PHE B 16  ? 0.3893 0.3308 0.2959 0.0093  0.0370  -0.0018 59  PHE B CG  
2193 C CD1 . PHE B 16  ? 0.3429 0.2905 0.2558 0.0128  0.0376  -0.0021 59  PHE B CD1 
2194 C CD2 . PHE B 16  ? 0.3926 0.3382 0.3006 0.0045  0.0354  -0.0020 59  PHE B CD2 
2195 C CE1 . PHE B 16  ? 0.3599 0.3163 0.2790 0.0116  0.0365  -0.0030 59  PHE B CE1 
2196 C CE2 . PHE B 16  ? 0.3777 0.3328 0.2928 0.0038  0.0345  -0.0027 59  PHE B CE2 
2197 C CZ  . PHE B 16  ? 0.3547 0.3146 0.2746 0.0074  0.0350  -0.0034 59  PHE B CZ  
2198 N N   . PRO B 17  ? 0.4137 0.3479 0.3124 0.0068  0.0366  0.0022  60  PRO B N   
2199 C CA  . PRO B 17  ? 0.4174 0.3572 0.3179 0.0047  0.0363  0.0030  60  PRO B CA  
2200 C C   . PRO B 17  ? 0.4519 0.3919 0.3517 0.0082  0.0357  0.0043  60  PRO B C   
2201 O O   . PRO B 17  ? 0.4357 0.3819 0.3383 0.0087  0.0351  0.0041  60  PRO B O   
2202 C CB  . PRO B 17  ? 0.4470 0.3807 0.3422 0.0000  0.0369  0.0042  60  PRO B CB  
2203 C CG  . PRO B 17  ? 0.4368 0.3637 0.3285 -0.0017 0.0363  0.0032  60  PRO B CG  
2204 C CD  . PRO B 17  ? 0.4479 0.3717 0.3388 0.0037  0.0369  0.0023  60  PRO B CD  
2205 N N   . GLU B 18  ? 0.4251 0.3575 0.3205 0.0108  0.0355  0.0057  61  GLU B N   
2206 C CA  . GLU B 18  ? 0.4566 0.3886 0.3513 0.0140  0.0337  0.0074  61  GLU B CA  
2207 C C   . GLU B 18  ? 0.4205 0.3602 0.3232 0.0173  0.0318  0.0069  61  GLU B C   
2208 O O   . GLU B 18  ? 0.3789 0.3213 0.2819 0.0181  0.0293  0.0076  61  GLU B O   
2209 C CB  . GLU B 18  ? 0.4487 0.3712 0.3385 0.0165  0.0338  0.0094  61  GLU B CB  
2210 C CG  . GLU B 18  ? 0.4838 0.3973 0.3648 0.0129  0.0352  0.0104  61  GLU B CG  
2211 C CD  . GLU B 18  ? 0.5645 0.4733 0.4431 0.0099  0.0369  0.0089  61  GLU B CD  
2212 O OE1 . GLU B 18  ? 0.5239 0.4344 0.4060 0.0115  0.0374  0.0073  61  GLU B OE1 
2213 O OE2 . GLU B 18  ? 0.5908 0.4935 0.4636 0.0057  0.0376  0.0096  61  GLU B OE2 
2214 N N   . THR B 19  ? 0.4232 0.3652 0.3311 0.0190  0.0328  0.0059  62  THR B N   
2215 C CA  . THR B 19  ? 0.3661 0.3154 0.2826 0.0218  0.0313  0.0059  62  THR B CA  
2216 C C   . THR B 19  ? 0.3832 0.3399 0.3025 0.0195  0.0300  0.0042  62  THR B C   
2217 O O   . THR B 19  ? 0.3747 0.3353 0.2973 0.0207  0.0272  0.0046  62  THR B O   
2218 C CB  . THR B 19  ? 0.4236 0.3729 0.3442 0.0240  0.0338  0.0054  62  THR B CB  
2219 O OG1 . THR B 19  ? 0.4190 0.3602 0.3365 0.0269  0.0356  0.0071  62  THR B OG1 
2220 C CG2 . THR B 19  ? 0.4052 0.3626 0.3359 0.0265  0.0326  0.0058  62  THR B CG2 
2221 N N   . VAL B 20  ? 0.3958 0.3539 0.3136 0.0162  0.0319  0.0024  63  VAL B N   
2222 C CA  . VAL B 20  ? 0.3851 0.3498 0.3056 0.0146  0.0315  0.0010  63  VAL B CA  
2223 C C   . VAL B 20  ? 0.4033 0.3666 0.3187 0.0141  0.0305  0.0016  63  VAL B C   
2224 O O   . VAL B 20  ? 0.3510 0.3171 0.2674 0.0149  0.0287  0.0010  63  VAL B O   
2225 C CB  . VAL B 20  ? 0.3747 0.3414 0.2957 0.0114  0.0335  -0.0003 63  VAL B CB  
2226 C CG1 . VAL B 20  ? 0.3720 0.3449 0.2957 0.0103  0.0339  -0.0013 63  VAL B CG1 
2227 C CG2 . VAL B 20  ? 0.3502 0.3172 0.2744 0.0120  0.0340  -0.0012 63  VAL B CG2 
2228 N N   . LEU B 21  ? 0.4065 0.3639 0.3151 0.0127  0.0316  0.0029  64  LEU B N   
2229 C CA  . LEU B 21  ? 0.4261 0.3804 0.3277 0.0123  0.0313  0.0038  64  LEU B CA  
2230 C C   . LEU B 21  ? 0.3764 0.3287 0.2766 0.0151  0.0269  0.0048  64  LEU B C   
2231 O O   . LEU B 21  ? 0.3589 0.3109 0.2554 0.0153  0.0252  0.0043  64  LEU B O   
2232 C CB  . LEU B 21  ? 0.4459 0.3935 0.3406 0.0103  0.0334  0.0055  64  LEU B CB  
2233 C CG  . LEU B 21  ? 0.4715 0.4211 0.3673 0.0065  0.0372  0.0054  64  LEU B CG  
2234 C CD1 . LEU B 21  ? 0.4996 0.4418 0.3897 0.0042  0.0386  0.0074  64  LEU B CD1 
2235 C CD2 . LEU B 21  ? 0.5123 0.4653 0.4071 0.0056  0.0397  0.0051  64  LEU B CD2 
2236 N N   . ALA B 22  ? 0.3745 0.3248 0.2774 0.0174  0.0249  0.0063  65  ALA B N   
2237 C CA  . ALA B 22  ? 0.4010 0.3503 0.3047 0.0200  0.0199  0.0081  65  ALA B CA  
2238 C C   . ALA B 22  ? 0.4081 0.3641 0.3188 0.0205  0.0172  0.0069  65  ALA B C   
2239 O O   . ALA B 22  ? 0.3510 0.3057 0.2590 0.0207  0.0126  0.0075  65  ALA B O   
2240 C CB  . ALA B 22  ? 0.3475 0.2949 0.2556 0.0229  0.0192  0.0105  65  ALA B CB  
2241 N N   . ARG B 23  ? 0.3828 0.3449 0.3014 0.0205  0.0195  0.0053  66  ARG B N   
2242 C CA  . ARG B 23  ? 0.3870 0.3549 0.3123 0.0207  0.0173  0.0043  66  ARG B CA  
2243 C C   . ARG B 23  ? 0.3833 0.3505 0.3024 0.0187  0.0169  0.0022  66  ARG B C   
2244 O O   . ARG B 23  ? 0.4130 0.3805 0.3323 0.0188  0.0129  0.0020  66  ARG B O   
2245 C CB  . ARG B 23  ? 0.3705 0.3438 0.3040 0.0211  0.0205  0.0032  66  ARG B CB  
2246 C CG  . ARG B 23  ? 0.3732 0.3471 0.3136 0.0240  0.0211  0.0053  66  ARG B CG  
2247 C CD  . ARG B 23  ? 0.3923 0.3697 0.3382 0.0243  0.0247  0.0041  66  ARG B CD  
2248 N NE  . ARG B 23  ? 0.3776 0.3549 0.3297 0.0277  0.0264  0.0063  66  ARG B NE  
2249 C CZ  . ARG B 23  ? 0.3814 0.3607 0.3382 0.0288  0.0298  0.0060  66  ARG B CZ  
2250 N NH1 . ARG B 23  ? 0.3512 0.3330 0.3074 0.0267  0.0309  0.0036  66  ARG B NH1 
2251 N NH2 . ARG B 23  ? 0.3733 0.3517 0.3352 0.0325  0.0323  0.0083  66  ARG B NH2 
2252 N N   . CYS B 24  ? 0.3659 0.3317 0.2796 0.0170  0.0213  0.0009  67  CYS B N   
2253 C CA  . CYS B 24  ? 0.3835 0.3481 0.2911 0.0159  0.0224  -0.0007 67  CYS B CA  
2254 C C   . CYS B 24  ? 0.4222 0.3790 0.3191 0.0162  0.0190  0.0001  67  CYS B C   
2255 O O   . CYS B 24  ? 0.4034 0.3581 0.2961 0.0161  0.0167  -0.0012 67  CYS B O   
2256 C CB  . CYS B 24  ? 0.4051 0.3703 0.3108 0.0142  0.0281  -0.0012 67  CYS B CB  
2257 S SG  . CYS B 24  ? 0.4755 0.4397 0.3752 0.0138  0.0316  -0.0028 67  CYS B SG  
2258 N N   . VAL B 25  ? 0.3950 0.3464 0.2860 0.0163  0.0184  0.0022  68  VAL B N   
2259 C CA  . VAL B 25  ? 0.4115 0.3542 0.2908 0.0164  0.0146  0.0033  68  VAL B CA  
2260 C C   . VAL B 25  ? 0.4204 0.3634 0.3031 0.0173  0.0069  0.0041  68  VAL B C   
2261 O O   . VAL B 25  ? 0.4089 0.3461 0.2829 0.0167  0.0028  0.0035  68  VAL B O   
2262 C CB  . VAL B 25  ? 0.4196 0.3564 0.2928 0.0165  0.0153  0.0058  68  VAL B CB  
2263 C CG1 . VAL B 25  ? 0.4668 0.3943 0.3284 0.0169  0.0096  0.0076  68  VAL B CG1 
2264 C CG2 . VAL B 25  ? 0.4337 0.3690 0.3020 0.0148  0.0225  0.0054  68  VAL B CG2 
2265 N N   . LYS B 26  ? 0.4137 0.3632 0.3092 0.0186  0.0047  0.0056  69  LYS B N   
2266 C CA  . LYS B 26  ? 0.3923 0.3439 0.2944 0.0192  -0.0026 0.0073  69  LYS B CA  
2267 C C   . LYS B 26  ? 0.4246 0.3786 0.3286 0.0179  -0.0044 0.0049  69  LYS B C   
2268 O O   . LYS B 26  ? 0.4034 0.3538 0.3040 0.0170  -0.0112 0.0055  69  LYS B O   
2269 C CB  . LYS B 26  ? 0.4509 0.4096 0.3677 0.0214  -0.0025 0.0097  69  LYS B CB  
2270 C CG  . LYS B 26  ? 0.4751 0.4380 0.4025 0.0222  -0.0095 0.0125  69  LYS B CG  
2271 C CD  . LYS B 26  ? 0.6260 0.5827 0.5477 0.0225  -0.0169 0.0157  69  LYS B CD  
2272 C CE  . LYS B 26  ? 0.6971 0.6591 0.6313 0.0226  -0.0250 0.0190  69  LYS B CE  
2273 N NZ  . LYS B 26  ? 0.8188 0.7761 0.7507 0.0234  -0.0326 0.0233  69  LYS B NZ  
2274 N N   . TYR B 27  ? 0.4136 0.3730 0.3224 0.0177  0.0012  0.0025  70  TYR B N   
2275 C CA  . TYR B 27  ? 0.3785 0.3401 0.2898 0.0167  -0.0001 0.0004  70  TYR B CA  
2276 C C   . TYR B 27  ? 0.4297 0.3819 0.3259 0.0156  -0.0013 -0.0016 70  TYR B C   
2277 O O   . TYR B 27  ? 0.4266 0.3754 0.3202 0.0145  -0.0070 -0.0021 70  TYR B O   
2278 C CB  . TYR B 27  ? 0.3935 0.3619 0.3120 0.0170  0.0062  -0.0016 70  TYR B CB  
2279 C CG  . TYR B 27  ? 0.3827 0.3538 0.3052 0.0163  0.0050  -0.0033 70  TYR B CG  
2280 C CD1 . TYR B 27  ? 0.4191 0.3857 0.3329 0.0157  0.0068  -0.0060 70  TYR B CD1 
2281 C CD2 . TYR B 27  ? 0.3971 0.3745 0.3320 0.0164  0.0025  -0.0021 70  TYR B CD2 
2282 C CE1 . TYR B 27  ? 0.4160 0.3838 0.3327 0.0152  0.0057  -0.0076 70  TYR B CE1 
2283 C CE2 . TYR B 27  ? 0.4114 0.3905 0.3498 0.0155  0.0012  -0.0035 70  TYR B CE2 
2284 C CZ  . TYR B 27  ? 0.4059 0.3799 0.3348 0.0149  0.0026  -0.0064 70  TYR B CZ  
2285 O OH  . TYR B 27  ? 0.4119 0.3864 0.3434 0.0141  0.0014  -0.0078 70  TYR B OH  
2286 N N   . THR B 28  ? 0.4154 0.3629 0.3012 0.0157  0.0042  -0.0027 71  THR B N   
2287 C CA  . THR B 28  ? 0.4568 0.3940 0.3267 0.0153  0.0047  -0.0044 71  THR B CA  
2288 C C   . THR B 28  ? 0.4698 0.3967 0.3279 0.0146  -0.0028 -0.0029 71  THR B C   
2289 O O   . THR B 28  ? 0.5122 0.4291 0.3567 0.0139  -0.0053 -0.0045 71  THR B O   
2290 C CB  . THR B 28  ? 0.4384 0.3736 0.3015 0.0158  0.0132  -0.0050 71  THR B CB  
2291 O OG1 . THR B 28  ? 0.4695 0.4038 0.3314 0.0157  0.0141  -0.0026 71  THR B OG1 
2292 C CG2 . THR B 28  ? 0.3971 0.3420 0.2716 0.0161  0.0195  -0.0063 71  THR B CG2 
2293 N N   . GLU B 29  ? 0.4828 0.4110 0.3448 0.0148  -0.0067 0.0002  72  GLU B N   
2294 C CA  . GLU B 29  ? 0.5035 0.4231 0.3567 0.0141  -0.0155 0.0023  72  GLU B CA  
2295 C C   . GLU B 29  ? 0.5640 0.4853 0.4236 0.0126  -0.0241 0.0025  72  GLU B C   
2296 O O   . GLU B 29  ? 0.6210 0.5318 0.4680 0.0110  -0.0311 0.0023  72  GLU B O   
2297 C CB  . GLU B 29  ? 0.4974 0.4191 0.3559 0.0152  -0.0175 0.0061  72  GLU B CB  
2298 C CG  . GLU B 29  ? 0.5788 0.4918 0.4286 0.0146  -0.0270 0.0090  72  GLU B CG  
2299 C CD  . GLU B 29  ? 0.6105 0.5254 0.4658 0.0163  -0.0282 0.0129  72  GLU B CD  
2300 O OE1 . GLU B 29  ? 0.6009 0.5266 0.4736 0.0180  -0.0265 0.0144  72  GLU B OE1 
2301 O OE2 . GLU B 29  ? 0.6239 0.5285 0.4651 0.0163  -0.0305 0.0146  72  GLU B OE2 
2302 N N   . ILE B 30  ? 0.5265 0.4600 0.4050 0.0130  -0.0238 0.0031  73  ILE B N   
2303 C CA  . ILE B 30  ? 0.5917 0.5283 0.4790 0.0113  -0.0316 0.0040  73  ILE B CA  
2304 C C   . ILE B 30  ? 0.5642 0.4957 0.4436 0.0098  -0.0309 0.0002  73  ILE B C   
2305 O O   . ILE B 30  ? 0.5613 0.4884 0.4389 0.0074  -0.0389 0.0003  73  ILE B O   
2306 C CB  . ILE B 30  ? 0.5591 0.5100 0.4687 0.0125  -0.0301 0.0062  73  ILE B CB  
2307 C CG1 . ILE B 30  ? 0.6566 0.6111 0.5738 0.0145  -0.0317 0.0104  73  ILE B CG1 
2308 C CG2 . ILE B 30  ? 0.6133 0.5682 0.5333 0.0104  -0.0368 0.0071  73  ILE B CG2 
2309 C CD1 . ILE B 30  ? 0.7330 0.6995 0.6690 0.0168  -0.0269 0.0122  73  ILE B CD1 
2310 N N   . HIS B 31  ? 0.5415 0.4732 0.4169 0.0110  -0.0217 -0.0030 74  HIS B N   
2311 C CA  . HIS B 31  ? 0.5505 0.4786 0.4207 0.0104  -0.0196 -0.0065 74  HIS B CA  
2312 C C   . HIS B 31  ? 0.5858 0.5013 0.4355 0.0112  -0.0149 -0.0090 74  HIS B C   
2313 O O   . HIS B 31  ? 0.5401 0.4582 0.3892 0.0131  -0.0057 -0.0101 74  HIS B O   
2314 C CB  . HIS B 31  ? 0.5015 0.4415 0.3863 0.0117  -0.0126 -0.0075 74  HIS B CB  
2315 C CG  . HIS B 31  ? 0.4930 0.4440 0.3965 0.0112  -0.0158 -0.0051 74  HIS B CG  
2316 N ND1 . HIS B 31  ? 0.5543 0.5073 0.4648 0.0095  -0.0201 -0.0053 74  HIS B ND1 
2317 C CD2 . HIS B 31  ? 0.4755 0.4355 0.3920 0.0123  -0.0149 -0.0023 74  HIS B CD2 
2318 C CE1 . HIS B 31  ? 0.5128 0.4763 0.4404 0.0097  -0.0212 -0.0024 74  HIS B CE1 
2319 N NE2 . HIS B 31  ? 0.4675 0.4352 0.3988 0.0117  -0.0179 -0.0007 74  HIS B NE2 
2320 N N   . PRO B 32  ? 0.6290 0.5301 0.4611 0.0098  -0.0207 -0.0098 75  PRO B N   
2321 C CA  . PRO B 32  ? 0.6435 0.5308 0.4541 0.0111  -0.0151 -0.0119 75  PRO B CA  
2322 C C   . PRO B 32  ? 0.6067 0.4943 0.4161 0.0131  -0.0058 -0.0151 75  PRO B C   
2323 O O   . PRO B 32  ? 0.6012 0.4832 0.3996 0.0152  0.0025  -0.0161 75  PRO B O   
2324 C CB  . PRO B 32  ? 0.7309 0.6016 0.5231 0.0088  -0.0249 -0.0124 75  PRO B CB  
2325 C CG  . PRO B 32  ? 0.7457 0.6231 0.5510 0.0063  -0.0359 -0.0089 75  PRO B CG  
2326 C CD  . PRO B 32  ? 0.7060 0.6018 0.5365 0.0069  -0.0330 -0.0081 75  PRO B CD  
2327 N N   . GLU B 33  ? 0.5985 0.4928 0.4194 0.0127  -0.0069 -0.0163 76  GLU B N   
2328 C CA  . GLU B 33  ? 0.5978 0.4919 0.4177 0.0149  0.0013  -0.0191 76  GLU B CA  
2329 C C   . GLU B 33  ? 0.5795 0.4858 0.4111 0.0172  0.0111  -0.0183 76  GLU B C   
2330 O O   . GLU B 33  ? 0.5774 0.4842 0.4088 0.0194  0.0186  -0.0199 76  GLU B O   
2331 C CB  . GLU B 33  ? 0.5851 0.4825 0.4142 0.0136  -0.0030 -0.0203 76  GLU B CB  
2332 C CG  . GLU B 33  ? 0.5979 0.5127 0.4505 0.0130  -0.0038 -0.0183 76  GLU B CG  
2333 C CD  . GLU B 33  ? 0.6081 0.5277 0.4693 0.0105  -0.0123 -0.0152 76  GLU B CD  
2334 O OE1 . GLU B 33  ? 0.5955 0.5065 0.4457 0.0094  -0.0175 -0.0142 76  GLU B OE1 
2335 O OE2 . GLU B 33  ? 0.6369 0.5686 0.5159 0.0100  -0.0135 -0.0135 76  GLU B OE2 
2336 N N   . MET B 34  ? 0.5125 0.4281 0.3542 0.0166  0.0110  -0.0157 77  MET B N   
2337 C CA  . MET B 34  ? 0.5051 0.4316 0.3578 0.0179  0.0189  -0.0148 77  MET B CA  
2338 C C   . MET B 34  ? 0.5057 0.4286 0.3503 0.0184  0.0234  -0.0132 77  MET B C   
2339 O O   . MET B 34  ? 0.4659 0.3975 0.3199 0.0185  0.0284  -0.0118 77  MET B O   
2340 C CB  . MET B 34  ? 0.5063 0.4460 0.3776 0.0169  0.0162  -0.0132 77  MET B CB  
2341 C CG  . MET B 34  ? 0.5204 0.4656 0.4019 0.0167  0.0138  -0.0143 77  MET B CG  
2342 S SD  . MET B 34  ? 0.5285 0.4769 0.4128 0.0187  0.0219  -0.0163 77  MET B SD  
2343 C CE  . MET B 34  ? 0.4735 0.4342 0.3708 0.0189  0.0273  -0.0143 77  MET B CE  
2344 N N   . ARG B 35  ? 0.5080 0.4174 0.3347 0.0182  0.0214  -0.0133 78  ARG B N   
2345 C CA  . ARG B 35  ? 0.5293 0.4343 0.3475 0.0184  0.0250  -0.0114 78  ARG B CA  
2346 C C   . ARG B 35  ? 0.5321 0.4366 0.3467 0.0203  0.0362  -0.0115 78  ARG B C   
2347 O O   . ARG B 35  ? 0.5580 0.4599 0.3672 0.0202  0.0405  -0.0095 78  ARG B O   
2348 C CB  . ARG B 35  ? 0.5840 0.4736 0.3829 0.0176  0.0188  -0.0111 78  ARG B CB  
2349 C CG  . ARG B 35  ? 0.5821 0.4743 0.3874 0.0156  0.0080  -0.0093 78  ARG B CG  
2350 C CD  . ARG B 35  ? 0.6165 0.4944 0.4037 0.0147  0.0017  -0.0079 78  ARG B CD  
2351 N NE  . ARG B 35  ? 0.6156 0.4980 0.4120 0.0132  -0.0084 -0.0053 78  ARG B NE  
2352 C CZ  . ARG B 35  ? 0.6757 0.5482 0.4607 0.0121  -0.0163 -0.0032 78  ARG B CZ  
2353 N NH1 . ARG B 35  ? 0.7151 0.5711 0.4767 0.0121  -0.0157 -0.0037 78  ARG B NH1 
2354 N NH2 . ARG B 35  ? 0.7199 0.5989 0.5172 0.0112  -0.0250 -0.0002 78  ARG B NH2 
2355 N N   . HIS B 36  ? 0.4934 0.4003 0.3115 0.0220  0.0412  -0.0133 79  HIS B N   
2356 C CA  . HIS B 36  ? 0.5343 0.4452 0.3556 0.0240  0.0520  -0.0125 79  HIS B CA  
2357 C C   . HIS B 36  ? 0.5209 0.4469 0.3607 0.0225  0.0542  -0.0101 79  HIS B C   
2358 O O   . HIS B 36  ? 0.5385 0.4686 0.3822 0.0231  0.0623  -0.0083 79  HIS B O   
2359 C CB  . HIS B 36  ? 0.4827 0.3938 0.3059 0.0265  0.0562  -0.0146 79  HIS B CB  
2360 C CG  . HIS B 36  ? 0.5113 0.4337 0.3512 0.0257  0.0515  -0.0155 79  HIS B CG  
2361 N ND1 . HIS B 36  ? 0.5008 0.4193 0.3386 0.0247  0.0432  -0.0175 79  HIS B ND1 
2362 C CD2 . HIS B 36  ? 0.5094 0.4463 0.3679 0.0256  0.0537  -0.0144 79  HIS B CD2 
2363 C CE1 . HIS B 36  ? 0.5204 0.4506 0.3747 0.0242  0.0414  -0.0175 79  HIS B CE1 
2364 N NE2 . HIS B 36  ? 0.5031 0.4439 0.3692 0.0248  0.0475  -0.0158 79  HIS B NE2 
2365 N N   . VAL B 37  ? 0.5124 0.4461 0.3634 0.0206  0.0473  -0.0098 80  VAL B N   
2366 C CA  . VAL B 37  ? 0.5200 0.4661 0.3869 0.0191  0.0487  -0.0080 80  VAL B CA  
2367 C C   . VAL B 37  ? 0.5174 0.4613 0.3803 0.0176  0.0507  -0.0055 80  VAL B C   
2368 O O   . VAL B 37  ? 0.5429 0.4785 0.3954 0.0172  0.0466  -0.0050 80  VAL B O   
2369 C CB  . VAL B 37  ? 0.4807 0.4334 0.3583 0.0180  0.0415  -0.0086 80  VAL B CB  
2370 C CG1 . VAL B 37  ? 0.4812 0.4426 0.3704 0.0163  0.0422  -0.0067 80  VAL B CG1 
2371 C CG2 . VAL B 37  ? 0.5121 0.4686 0.3961 0.0191  0.0407  -0.0106 80  VAL B CG2 
2372 N N   . ASP B 38  ? 0.4978 0.4488 0.3693 0.0167  0.0565  -0.0036 81  ASP B N   
2373 C CA  . ASP B 38  ? 0.5160 0.4665 0.3867 0.0146  0.0583  -0.0008 81  ASP B CA  
2374 C C   . ASP B 38  ? 0.5000 0.4581 0.3828 0.0125  0.0538  -0.0004 81  ASP B C   
2375 O O   . ASP B 38  ? 0.4539 0.4212 0.3491 0.0115  0.0552  -0.0001 81  ASP B O   
2376 C CB  . ASP B 38  ? 0.5231 0.4765 0.3966 0.0143  0.0673  0.0014  81  ASP B CB  
2377 C CG  . ASP B 38  ? 0.5981 0.5515 0.4723 0.0114  0.0691  0.0046  81  ASP B CG  
2378 O OD1 . ASP B 38  ? 0.6234 0.5715 0.4918 0.0103  0.0640  0.0048  81  ASP B OD1 
2379 O OD2 . ASP B 38  ? 0.6276 0.5865 0.5091 0.0101  0.0754  0.0071  81  ASP B OD2 
2380 N N   . CYS B 39  ? 0.5150 0.4686 0.3935 0.0120  0.0485  0.0000  82  CYS B N   
2381 C CA  . CYS B 39  ? 0.5106 0.4695 0.3987 0.0109  0.0446  0.0002  82  CYS B CA  
2382 C C   . CYS B 39  ? 0.4859 0.4486 0.3801 0.0081  0.0480  0.0021  82  CYS B C   
2383 O O   . CYS B 39  ? 0.4469 0.4151 0.3502 0.0070  0.0463  0.0018  82  CYS B O   
2384 C CB  . CYS B 39  ? 0.5354 0.4883 0.4181 0.0116  0.0389  0.0007  82  CYS B CB  
2385 S SG  . CYS B 39  ? 0.6358 0.5880 0.5183 0.0137  0.0323  -0.0011 82  CYS B SG  
2386 N N   . GLN B 40  ? 0.5077 0.4668 0.3965 0.0068  0.0525  0.0042  83  GLN B N   
2387 C CA  . GLN B 40  ? 0.5049 0.4680 0.4007 0.0034  0.0555  0.0064  83  GLN B CA  
2388 C C   . GLN B 40  ? 0.5109 0.4843 0.4193 0.0026  0.0574  0.0062  83  GLN B C   
2389 O O   . GLN B 40  ? 0.4702 0.4483 0.3871 0.0000  0.0556  0.0067  83  GLN B O   
2390 C CB  . GLN B 40  ? 0.5364 0.4946 0.4252 0.0021  0.0609  0.0092  83  GLN B CB  
2391 C CG  . GLN B 40  ? 0.5691 0.5331 0.4674 -0.0019 0.0647  0.0120  83  GLN B CG  
2392 C CD  . GLN B 40  ? 0.6042 0.5628 0.4959 -0.0037 0.0700  0.0153  83  GLN B CD  
2393 O OE1 . GLN B 40  ? 0.6239 0.5784 0.5076 -0.0016 0.0750  0.0159  83  GLN B OE1 
2394 N NE2 . GLN B 40  ? 0.5934 0.5507 0.4873 -0.0077 0.0692  0.0176  83  GLN B NE2 
2395 N N   . SER B 41  ? 0.4653 0.4412 0.3742 0.0049  0.0609  0.0054  84  SER B N   
2396 C CA  . SER B 41  ? 0.4754 0.4611 0.3968 0.0048  0.0626  0.0055  84  SER B CA  
2397 C C   . SER B 41  ? 0.4435 0.4330 0.3708 0.0051  0.0567  0.0032  84  SER B C   
2398 O O   . SER B 41  ? 0.3989 0.3954 0.3366 0.0033  0.0558  0.0039  84  SER B O   
2399 C CB  . SER B 41  ? 0.4814 0.4669 0.4003 0.0082  0.0678  0.0050  84  SER B CB  
2400 O OG  . SER B 41  ? 0.5089 0.4906 0.4221 0.0082  0.0745  0.0075  84  SER B OG  
2401 N N   . VAL B 42  ? 0.4233 0.4078 0.3441 0.0072  0.0527  0.0009  85  VAL B N   
2402 C CA  . VAL B 42  ? 0.4487 0.4363 0.3749 0.0077  0.0480  -0.0009 85  VAL B CA  
2403 C C   . VAL B 42  ? 0.4159 0.4042 0.3458 0.0050  0.0456  0.0000  85  VAL B C   
2404 O O   . VAL B 42  ? 0.3848 0.3778 0.3218 0.0039  0.0441  -0.0003 85  VAL B O   
2405 C CB  . VAL B 42  ? 0.4204 0.4028 0.3401 0.0102  0.0442  -0.0027 85  VAL B CB  
2406 C CG1 . VAL B 42  ? 0.4166 0.4022 0.3425 0.0106  0.0401  -0.0039 85  VAL B CG1 
2407 C CG2 . VAL B 42  ? 0.4558 0.4361 0.3708 0.0125  0.0457  -0.0040 85  VAL B CG2 
2408 N N   . TRP B 43  ? 0.4040 0.3862 0.3277 0.0039  0.0452  0.0011  86  TRP B N   
2409 C CA  . TRP B 43  ? 0.4433 0.4237 0.3683 0.0014  0.0432  0.0018  86  TRP B CA  
2410 C C   . TRP B 43  ? 0.4476 0.4327 0.3794 -0.0025 0.0447  0.0035  86  TRP B C   
2411 O O   . TRP B 43  ? 0.4307 0.4170 0.3662 -0.0044 0.0421  0.0032  86  TRP B O   
2412 C CB  . TRP B 43  ? 0.4834 0.4554 0.4000 0.0011  0.0429  0.0030  86  TRP B CB  
2413 C CG  . TRP B 43  ? 0.4835 0.4518 0.3997 -0.0018 0.0418  0.0039  86  TRP B CG  
2414 C CD1 . TRP B 43  ? 0.5172 0.4812 0.4303 -0.0051 0.0432  0.0060  86  TRP B CD1 
2415 C CD2 . TRP B 43  ? 0.4563 0.4233 0.3742 -0.0018 0.0392  0.0027  86  TRP B CD2 
2416 N NE1 . TRP B 43  ? 0.5054 0.4648 0.4175 -0.0074 0.0411  0.0060  86  TRP B NE1 
2417 C CE2 . TRP B 43  ? 0.4719 0.4327 0.3863 -0.0052 0.0388  0.0039  86  TRP B CE2 
2418 C CE3 . TRP B 43  ? 0.4250 0.3946 0.3461 0.0006  0.0374  0.0008  86  TRP B CE3 
2419 C CZ2 . TRP B 43  ? 0.4604 0.4162 0.3728 -0.0060 0.0368  0.0030  86  TRP B CZ2 
2420 C CZ3 . TRP B 43  ? 0.4461 0.4115 0.3659 0.0000  0.0360  0.0002  86  TRP B CZ3 
2421 C CH2 . TRP B 43  ? 0.4303 0.3883 0.3450 -0.0031 0.0357  0.0011  86  TRP B CH2 
2422 N N   . ASP B 44  ? 0.4401 0.4278 0.3736 -0.0037 0.0488  0.0055  87  ASP B N   
2423 C CA  . ASP B 44  ? 0.4902 0.4840 0.4327 -0.0076 0.0500  0.0080  87  ASP B CA  
2424 C C   . ASP B 44  ? 0.4600 0.4616 0.4121 -0.0073 0.0481  0.0072  87  ASP B C   
2425 O O   . ASP B 44  ? 0.4508 0.4552 0.4089 -0.0109 0.0452  0.0084  87  ASP B O   
2426 C CB  . ASP B 44  ? 0.5223 0.5184 0.4662 -0.0079 0.0560  0.0107  87  ASP B CB  
2427 C CG  . ASP B 44  ? 0.6535 0.6546 0.6067 -0.0130 0.0571  0.0144  87  ASP B CG  
2428 O OD1 . ASP B 44  ? 0.7331 0.7287 0.6827 -0.0168 0.0554  0.0157  87  ASP B OD1 
2429 O OD2 . ASP B 44  ? 0.6997 0.7101 0.6643 -0.0133 0.0596  0.0164  87  ASP B OD2 
2430 N N   . ALA B 45  ? 0.4326 0.4371 0.3855 -0.0033 0.0492  0.0054  88  ALA B N   
2431 C CA  . ALA B 45  ? 0.4179 0.4291 0.3791 -0.0026 0.0473  0.0048  88  ALA B CA  
2432 C C   . ALA B 45  ? 0.4005 0.4085 0.3593 -0.0030 0.0421  0.0028  88  ALA B C   
2433 O O   . ALA B 45  ? 0.3928 0.4044 0.3574 -0.0048 0.0393  0.0033  88  ALA B O   
2434 C CB  . ALA B 45  ? 0.4254 0.4386 0.3864 0.0019  0.0500  0.0033  88  ALA B CB  
2435 N N   . PHE B 46  ? 0.4070 0.4081 0.3575 -0.0013 0.0409  0.0010  89  PHE B N   
2436 C CA  . PHE B 46  ? 0.3794 0.3765 0.3271 -0.0013 0.0374  -0.0004 89  PHE B CA  
2437 C C   . PHE B 46  ? 0.4415 0.4352 0.3882 -0.0056 0.0353  0.0008  89  PHE B C   
2438 O O   . PHE B 46  ? 0.3703 0.3638 0.3183 -0.0071 0.0325  0.0005  89  PHE B O   
2439 C CB  . PHE B 46  ? 0.3808 0.3717 0.3214 0.0016  0.0371  -0.0017 89  PHE B CB  
2440 C CG  . PHE B 46  ? 0.3611 0.3497 0.3008 0.0034  0.0350  -0.0031 89  PHE B CG  
2441 C CD1 . PHE B 46  ? 0.4042 0.3919 0.3447 0.0017  0.0334  -0.0034 89  PHE B CD1 
2442 C CD2 . PHE B 46  ? 0.3345 0.3213 0.2724 0.0067  0.0347  -0.0039 89  PHE B CD2 
2443 C CE1 . PHE B 46  ? 0.3719 0.3566 0.3106 0.0038  0.0327  -0.0044 89  PHE B CE1 
2444 C CE2 . PHE B 46  ? 0.3875 0.3728 0.3259 0.0086  0.0337  -0.0046 89  PHE B CE2 
2445 C CZ  . PHE B 46  ? 0.3847 0.3687 0.3231 0.0074  0.0333  -0.0049 89  PHE B CZ  
2446 N N   . LYS B 47  ? 0.4329 0.4227 0.3762 -0.0078 0.0365  0.0023  90  LYS B N   
2447 C CA  . LYS B 47  ? 0.4508 0.4358 0.3921 -0.0125 0.0342  0.0036  90  LYS B CA  
2448 C C   . LYS B 47  ? 0.4671 0.4588 0.4173 -0.0164 0.0321  0.0054  90  LYS B C   
2449 O O   . LYS B 47  ? 0.4213 0.4091 0.3697 -0.0196 0.0280  0.0054  90  LYS B O   
2450 C CB  . LYS B 47  ? 0.4770 0.4573 0.4140 -0.0143 0.0363  0.0054  90  LYS B CB  
2451 C CG  . LYS B 47  ? 0.5949 0.5674 0.5273 -0.0192 0.0339  0.0065  90  LYS B CG  
2452 C CD  . LYS B 47  ? 0.6131 0.5793 0.5396 -0.0201 0.0362  0.0081  90  LYS B CD  
2453 C CE  . LYS B 47  ? 0.6279 0.6013 0.5602 -0.0206 0.0404  0.0105  90  LYS B CE  
2454 N NZ  . LYS B 47  ? 0.7747 0.7428 0.7036 -0.0244 0.0420  0.0133  90  LYS B NZ  
2455 N N   . GLY B 48  ? 0.4469 0.4482 0.4065 -0.0161 0.0348  0.0072  91  GLY B N   
2456 C CA  . GLY B 48  ? 0.4341 0.4435 0.4050 -0.0195 0.0329  0.0098  91  GLY B CA  
2457 C C   . GLY B 48  ? 0.4187 0.4302 0.3920 -0.0188 0.0287  0.0086  91  GLY B C   
2458 O O   . GLY B 48  ? 0.3649 0.3815 0.3464 -0.0223 0.0253  0.0109  91  GLY B O   
2459 N N   . ALA B 49  ? 0.4242 0.4318 0.3909 -0.0146 0.0288  0.0054  92  ALA B N   
2460 C CA  . ALA B 49  ? 0.4004 0.4091 0.3684 -0.0138 0.0255  0.0043  92  ALA B CA  
2461 C C   . ALA B 49  ? 0.4091 0.4097 0.3705 -0.0177 0.0202  0.0042  92  ALA B C   
2462 O O   . ALA B 49  ? 0.3601 0.3623 0.3240 -0.0191 0.0162  0.0047  92  ALA B O   
2463 C CB  . ALA B 49  ? 0.3709 0.3778 0.3344 -0.0085 0.0274  0.0014  92  ALA B CB  
2464 N N   . PHE B 50  ? 0.3778 0.3684 0.3293 -0.0193 0.0201  0.0034  93  PHE B N   
2465 C CA  . PHE B 50  ? 0.3973 0.3768 0.3387 -0.0222 0.0158  0.0026  93  PHE B CA  
2466 C C   . PHE B 50  ? 0.4177 0.3894 0.3539 -0.0276 0.0136  0.0039  93  PHE B C   
2467 O O   . PHE B 50  ? 0.3988 0.3616 0.3276 -0.0315 0.0087  0.0038  93  PHE B O   
2468 C CB  . PHE B 50  ? 0.3706 0.3412 0.3013 -0.0176 0.0181  -0.0004 93  PHE B CB  
2469 C CG  . PHE B 50  ? 0.3993 0.3656 0.3254 -0.0151 0.0220  -0.0011 93  PHE B CG  
2470 C CD1 . PHE B 50  ? 0.4178 0.3912 0.3493 -0.0112 0.0258  -0.0012 93  PHE B CD1 
2471 C CD2 . PHE B 50  ? 0.4046 0.3584 0.3198 -0.0165 0.0217  -0.0016 93  PHE B CD2 
2472 C CE1 . PHE B 50  ? 0.4048 0.3739 0.3319 -0.0091 0.0284  -0.0015 93  PHE B CE1 
2473 C CE2 . PHE B 50  ? 0.4100 0.3598 0.3214 -0.0139 0.0250  -0.0018 93  PHE B CE2 
2474 C CZ  . PHE B 50  ? 0.4396 0.3974 0.3573 -0.0103 0.0281  -0.0016 93  PHE B CZ  
2475 N N   . ILE B 51  ? 0.4111 0.3846 0.3498 -0.0282 0.0167  0.0052  94  ILE B N   
2476 C CA  A ILE B 51  ? 0.4370 0.4027 0.3710 -0.0338 0.0146  0.0068  94  ILE B CA  
2477 C CA  B ILE B 51  ? 0.4357 0.4015 0.3698 -0.0337 0.0146  0.0068  94  ILE B CA  
2478 C C   . ILE B 51  ? 0.4255 0.3971 0.3690 -0.0403 0.0094  0.0101  94  ILE B C   
2479 O O   . ILE B 51  ? 0.4338 0.4188 0.3911 -0.0400 0.0099  0.0122  94  ILE B O   
2480 C CB  A ILE B 51  ? 0.4516 0.4177 0.3858 -0.0329 0.0194  0.0078  94  ILE B CB  
2481 C CB  B ILE B 51  ? 0.4483 0.4154 0.3834 -0.0327 0.0196  0.0079  94  ILE B CB  
2482 C CG1 A ILE B 51  ? 0.4408 0.4212 0.3890 -0.0324 0.0228  0.0104  94  ILE B CG1 
2483 C CG1 B ILE B 51  ? 0.4776 0.4355 0.4015 -0.0276 0.0227  0.0052  94  ILE B CG1 
2484 C CG2 A ILE B 51  ? 0.4681 0.4281 0.3935 -0.0266 0.0232  0.0050  94  ILE B CG2 
2485 C CG2 B ILE B 51  ? 0.4615 0.4247 0.3968 -0.0395 0.0175  0.0108  94  ILE B CG2 
2486 C CD1 A ILE B 51  ? 0.4383 0.4243 0.3965 -0.0390 0.0208  0.0146  94  ILE B CD1 
2487 C CD1 B ILE B 51  ? 0.4634 0.4054 0.3735 -0.0292 0.0205  0.0039  94  ILE B CD1 
2488 N N   . SER B 52  ? 0.4394 0.4004 0.3754 -0.0464 0.0042  0.0108  95  SER B N   
2489 C CA  . SER B 52  ? 0.4798 0.4447 0.4241 -0.0539 -0.0025 0.0144  95  SER B CA  
2490 C C   . SER B 52  ? 0.4508 0.4198 0.3988 -0.0541 -0.0077 0.0144  95  SER B C   
2491 O O   . SER B 52  ? 0.4302 0.4063 0.3893 -0.0595 -0.0134 0.0181  95  SER B O   
2492 C CB  . SER B 52  ? 0.4940 0.4735 0.4560 -0.0560 0.0004  0.0189  95  SER B CB  
2493 O OG  . SER B 52  ? 0.6225 0.6040 0.5924 -0.0644 -0.0061 0.0231  95  SER B OG  
2494 N N   . LYS B 53  ? 0.4089 0.3737 0.3485 -0.0484 -0.0061 0.0108  96  LYS B N   
2495 C CA  . LYS B 53  ? 0.4294 0.3969 0.3708 -0.0479 -0.0104 0.0107  96  LYS B CA  
2496 C C   . LYS B 53  ? 0.4247 0.3747 0.3462 -0.0474 -0.0130 0.0073  96  LYS B C   
2497 O O   . LYS B 53  ? 0.4144 0.3543 0.3238 -0.0435 -0.0082 0.0043  96  LYS B O   
2498 C CB  . LYS B 53  ? 0.4281 0.4085 0.3796 -0.0410 -0.0050 0.0101  96  LYS B CB  
2499 C CG  . LYS B 53  ? 0.4032 0.4001 0.3734 -0.0409 -0.0020 0.0136  96  LYS B CG  
2500 C CD  . LYS B 53  ? 0.4364 0.4422 0.4125 -0.0336 0.0043  0.0121  96  LYS B CD  
2501 C CE  . LYS B 53  ? 0.4079 0.4280 0.4006 -0.0329 0.0084  0.0155  96  LYS B CE  
2502 N NZ  . LYS B 53  ? 0.4138 0.4397 0.4092 -0.0259 0.0147  0.0137  96  LYS B NZ  
2503 N N   . HIS B 54  ? 0.4372 0.3831 0.3552 -0.0510 -0.0204 0.0081  97  HIS B N   
2504 C CA  . HIS B 54  ? 0.4368 0.3649 0.3344 -0.0502 -0.0224 0.0050  97  HIS B CA  
2505 C C   . HIS B 54  ? 0.4355 0.3652 0.3305 -0.0418 -0.0151 0.0021  97  HIS B C   
2506 O O   . HIS B 54  ? 0.3874 0.3306 0.2948 -0.0387 -0.0138 0.0030  97  HIS B O   
2507 C CB  . HIS B 54  ? 0.4796 0.4040 0.3745 -0.0555 -0.0322 0.0068  97  HIS B CB  
2508 C CG  . HIS B 54  ? 0.4903 0.3931 0.3609 -0.0558 -0.0348 0.0038  97  HIS B CG  
2509 N ND1 . HIS B 54  ? 0.5018 0.3854 0.3537 -0.0579 -0.0347 0.0016  97  HIS B ND1 
2510 C CD2 . HIS B 54  ? 0.5302 0.4265 0.3912 -0.0540 -0.0370 0.0027  97  HIS B CD2 
2511 C CE1 . HIS B 54  ? 0.5015 0.3673 0.3327 -0.0571 -0.0363 -0.0008 97  HIS B CE1 
2512 N NE2 . HIS B 54  ? 0.5272 0.4003 0.3633 -0.0549 -0.0378 -0.0001 97  HIS B NE2 
2513 N N   . PRO B 55  ? 0.4571 0.3734 0.3367 -0.0379 -0.0102 -0.0011 98  PRO B N   
2514 C CA  . PRO B 55  ? 0.4593 0.3792 0.3398 -0.0302 -0.0029 -0.0031 98  PRO B CA  
2515 C C   . PRO B 55  ? 0.4775 0.3934 0.3515 -0.0281 -0.0040 -0.0039 98  PRO B C   
2516 O O   . PRO B 55  ? 0.4668 0.3805 0.3368 -0.0223 0.0019  -0.0057 98  PRO B O   
2517 C CB  . PRO B 55  ? 0.4657 0.3729 0.3337 -0.0271 0.0026  -0.0052 98  PRO B CB  
2518 C CG  . PRO B 55  ? 0.4546 0.3447 0.3071 -0.0328 -0.0026 -0.0055 98  PRO B CG  
2519 C CD  . PRO B 55  ? 0.4724 0.3705 0.3351 -0.0402 -0.0105 -0.0025 98  PRO B CD  
2520 N N   . CYS B 56  ? 0.4649 0.3794 0.3378 -0.0329 -0.0118 -0.0024 99  CYS B N   
2521 C CA  . CYS B 56  ? 0.4817 0.3940 0.3499 -0.0312 -0.0134 -0.0026 99  CYS B CA  
2522 C C   . CYS B 56  ? 0.5103 0.4391 0.3960 -0.0323 -0.0177 0.0003  99  CYS B C   
2523 O O   . CYS B 56  ? 0.5108 0.4383 0.3937 -0.0313 -0.0201 0.0006  99  CYS B O   
2524 C CB  . CYS B 56  ? 0.5464 0.4384 0.3934 -0.0353 -0.0193 -0.0033 99  CYS B CB  
2525 S SG  . CYS B 56  ? 0.5732 0.4425 0.3957 -0.0313 -0.0121 -0.0069 99  CYS B SG  
2526 N N   . ASP B 57  ? 0.4568 0.4005 0.3602 -0.0339 -0.0181 0.0025  100 ASP B N   
2527 C CA  . ASP B 57  ? 0.4682 0.4278 0.3894 -0.0344 -0.0212 0.0056  100 ASP B CA  
2528 C C   . ASP B 57  ? 0.4227 0.3977 0.3598 -0.0296 -0.0140 0.0058  100 ASP B C   
2529 O O   . ASP B 57  ? 0.4186 0.4074 0.3722 -0.0303 -0.0151 0.0087  100 ASP B O   
2530 C CB  . ASP B 57  ? 0.4683 0.4309 0.3966 -0.0418 -0.0298 0.0094  100 ASP B CB  
2531 C CG  . ASP B 57  ? 0.5107 0.4573 0.4226 -0.0471 -0.0387 0.0095  100 ASP B CG  
2532 O OD1 . ASP B 57  ? 0.5377 0.4790 0.4418 -0.0453 -0.0408 0.0089  100 ASP B OD1 
2533 O OD2 . ASP B 57  ? 0.4911 0.4292 0.3967 -0.0532 -0.0437 0.0102  100 ASP B OD2 
2534 N N   . ILE B 58  ? 0.3915 0.3638 0.3236 -0.0248 -0.0067 0.0028  101 ILE B N   
2535 C CA  . ILE B 58  ? 0.3945 0.3788 0.3387 -0.0205 -0.0005 0.0027  101 ILE B CA  
2536 C C   . ILE B 58  ? 0.3999 0.3926 0.3522 -0.0167 0.0004  0.0031  101 ILE B C   
2537 O O   . ILE B 58  ? 0.4032 0.3902 0.3481 -0.0151 -0.0006 0.0020  101 ILE B O   
2538 C CB  . ILE B 58  ? 0.3862 0.3647 0.3227 -0.0168 0.0058  -0.0001 101 ILE B CB  
2539 C CG1 . ILE B 58  ? 0.4433 0.4112 0.3700 -0.0202 0.0049  -0.0005 101 ILE B CG1 
2540 C CG2 . ILE B 58  ? 0.3903 0.3797 0.3376 -0.0132 0.0110  -0.0001 101 ILE B CG2 
2541 C CD1 . ILE B 58  ? 0.3929 0.3667 0.3280 -0.0248 0.0028  0.0020  101 ILE B CD1 
2542 N N   . THR B 59  ? 0.3981 0.4036 0.3647 -0.0151 0.0026  0.0046  102 THR B N   
2543 C CA  . THR B 59  ? 0.4076 0.4209 0.3825 -0.0114 0.0037  0.0051  102 THR B CA  
2544 C C   . THR B 59  ? 0.4480 0.4661 0.4267 -0.0066 0.0105  0.0034  102 THR B C   
2545 O O   . THR B 59  ? 0.3975 0.4150 0.3749 -0.0064 0.0140  0.0025  102 THR B O   
2546 C CB  . THR B 59  ? 0.4313 0.4550 0.4203 -0.0134 -0.0001 0.0091  102 THR B CB  
2547 O OG1 . THR B 59  ? 0.4231 0.4546 0.4219 -0.0142 0.0031  0.0108  102 THR B OG1 
2548 C CG2 . THR B 59  ? 0.3676 0.3862 0.3529 -0.0189 -0.0085 0.0112  102 THR B CG2 
2549 N N   . GLU B 60  ? 0.4468 0.4688 0.4296 -0.0028 0.0120  0.0031  103 GLU B N   
2550 C CA  . GLU B 60  ? 0.4562 0.4820 0.4423 0.0014  0.0175  0.0016  103 GLU B CA  
2551 C C   . GLU B 60  ? 0.3832 0.4167 0.3785 0.0014  0.0202  0.0033  103 GLU B C   
2552 O O   . GLU B 60  ? 0.3690 0.4022 0.3627 0.0032  0.0246  0.0020  103 GLU B O   
2553 C CB  . GLU B 60  ? 0.5083 0.5356 0.4967 0.0048  0.0178  0.0012  103 GLU B CB  
2554 C CG  . GLU B 60  ? 0.5627 0.5822 0.5420 0.0050  0.0162  -0.0002 103 GLU B CG  
2555 C CD  . GLU B 60  ? 0.6951 0.7158 0.6768 0.0078  0.0160  0.0000  103 GLU B CD  
2556 O OE1 . GLU B 60  ? 0.7516 0.7788 0.7421 0.0091  0.0156  0.0017  103 GLU B OE1 
2557 O OE2 . GLU B 60  ? 0.6703 0.6852 0.6454 0.0089  0.0168  -0.0013 103 GLU B OE2 
2558 N N   . GLU B 61  ? 0.3778 0.4180 0.3828 -0.0008 0.0177  0.0067  104 GLU B N   
2559 C CA  . GLU B 61  ? 0.4233 0.4715 0.4384 -0.0007 0.0213  0.0091  104 GLU B CA  
2560 C C   . GLU B 61  ? 0.4260 0.4711 0.4367 -0.0036 0.0229  0.0089  104 GLU B C   
2561 O O   . GLU B 61  ? 0.3880 0.4366 0.4024 -0.0023 0.0280  0.0097  104 GLU B O   
2562 C CB  . GLU B 61  ? 0.4363 0.4931 0.4648 -0.0028 0.0176  0.0136  104 GLU B CB  
2563 C CG  . GLU B 61  ? 0.5592 0.6249 0.5999 -0.0032 0.0217  0.0171  104 GLU B CG  
2564 C CD  . GLU B 61  ? 0.7377 0.8143 0.7953 -0.0034 0.0195  0.0221  104 GLU B CD  
2565 O OE1 . GLU B 61  ? 0.7238 0.8004 0.7830 -0.0061 0.0120  0.0237  104 GLU B OE1 
2566 O OE2 . GLU B 61  ? 0.8226 0.9076 0.8918 -0.0005 0.0254  0.0248  104 GLU B OE2 
2567 N N   . ASP B 62  ? 0.4225 0.4598 0.4242 -0.0072 0.0189  0.0079  105 ASP B N   
2568 C CA  . ASP B 62  ? 0.4194 0.4523 0.4158 -0.0097 0.0205  0.0076  105 ASP B CA  
2569 C C   . ASP B 62  ? 0.3942 0.4243 0.3847 -0.0058 0.0260  0.0050  105 ASP B C   
2570 O O   . ASP B 62  ? 0.3763 0.4060 0.3660 -0.0065 0.0291  0.0056  105 ASP B O   
2571 C CB  . ASP B 62  ? 0.4069 0.4296 0.3924 -0.0134 0.0158  0.0065  105 ASP B CB  
2572 C CG  . ASP B 62  ? 0.4327 0.4563 0.4222 -0.0189 0.0092  0.0095  105 ASP B CG  
2573 O OD1 . ASP B 62  ? 0.4407 0.4725 0.4419 -0.0216 0.0089  0.0130  105 ASP B OD1 
2574 O OD2 . ASP B 62  ? 0.4038 0.4195 0.3848 -0.0207 0.0043  0.0086  105 ASP B OD2 
2575 N N   . TYR B 63  ? 0.3795 0.4073 0.3658 -0.0019 0.0270  0.0024  106 TYR B N   
2576 C CA  . TYR B 63  ? 0.3909 0.4153 0.3714 0.0014  0.0307  0.0001  106 TYR B CA  
2577 C C   . TYR B 63  ? 0.3980 0.4271 0.3830 0.0049  0.0348  0.0001  106 TYR B C   
2578 O O   . TYR B 63  ? 0.4082 0.4337 0.3876 0.0073  0.0373  -0.0017 106 TYR B O   
2579 C CB  . TYR B 63  ? 0.3814 0.4001 0.3551 0.0032  0.0293  -0.0023 106 TYR B CB  
2580 C CG  . TYR B 63  ? 0.3897 0.4007 0.3554 0.0013  0.0276  -0.0030 106 TYR B CG  
2581 C CD1 . TYR B 63  ? 0.3907 0.3974 0.3512 0.0013  0.0293  -0.0035 106 TYR B CD1 
2582 C CD2 . TYR B 63  ? 0.3684 0.3752 0.3305 -0.0004 0.0244  -0.0030 106 TYR B CD2 
2583 C CE1 . TYR B 63  ? 0.3490 0.3478 0.3020 0.0002  0.0284  -0.0039 106 TYR B CE1 
2584 C CE2 . TYR B 63  ? 0.3658 0.3637 0.3188 -0.0016 0.0237  -0.0037 106 TYR B CE2 
2585 C CZ  . TYR B 63  ? 0.3386 0.3328 0.2877 -0.0012 0.0259  -0.0041 106 TYR B CZ  
2586 O OH  . TYR B 63  ? 0.3679 0.3525 0.3079 -0.0018 0.0257  -0.0047 106 TYR B OH  
2587 N N   . GLN B 64  ? 0.3935 0.4297 0.3880 0.0054  0.0355  0.0022  107 GLN B N   
2588 C CA  . GLN B 64  ? 0.4049 0.4438 0.4023 0.0095  0.0402  0.0020  107 GLN B CA  
2589 C C   . GLN B 64  ? 0.4072 0.4440 0.4004 0.0103  0.0452  0.0020  107 GLN B C   
2590 O O   . GLN B 64  ? 0.3841 0.4167 0.3712 0.0136  0.0480  -0.0001 107 GLN B O   
2591 C CB  . GLN B 64  ? 0.4003 0.4478 0.4102 0.0101  0.0407  0.0051  107 GLN B CB  
2592 C CG  . GLN B 64  ? 0.5012 0.5506 0.5139 0.0151  0.0464  0.0051  107 GLN B CG  
2593 C CD  . GLN B 64  ? 0.5984 0.6413 0.6028 0.0184  0.0462  0.0016  107 GLN B CD  
2594 O OE1 . GLN B 64  ? 0.6227 0.6613 0.6214 0.0215  0.0505  -0.0001 107 GLN B OE1 
2595 N NE2 . GLN B 64  ? 0.5857 0.6270 0.5889 0.0175  0.0413  0.0005  107 GLN B NE2 
2596 N N   . PRO B 65  ? 0.3565 0.3949 0.3518 0.0073  0.0464  0.0043  108 PRO B N   
2597 C CA  . PRO B 65  ? 0.3687 0.4035 0.3580 0.0082  0.0515  0.0043  108 PRO B CA  
2598 C C   . PRO B 65  ? 0.3603 0.3860 0.3367 0.0093  0.0503  0.0010  108 PRO B C   
2599 O O   . PRO B 65  ? 0.3894 0.4106 0.3588 0.0119  0.0538  0.0000  108 PRO B O   
2600 C CB  . PRO B 65  ? 0.3774 0.4148 0.3710 0.0037  0.0514  0.0074  108 PRO B CB  
2601 C CG  . PRO B 65  ? 0.4211 0.4662 0.4268 0.0011  0.0477  0.0100  108 PRO B CG  
2602 C CD  . PRO B 65  ? 0.3893 0.4325 0.3925 0.0027  0.0432  0.0074  108 PRO B CD  
2603 N N   . LEU B 66  ? 0.3406 0.3631 0.3135 0.0076  0.0455  -0.0003 109 LEU B N   
2604 C CA  . LEU B 66  ? 0.3588 0.3741 0.3222 0.0090  0.0440  -0.0028 109 LEU B CA  
2605 C C   . LEU B 66  ? 0.4042 0.4185 0.3662 0.0124  0.0437  -0.0049 109 LEU B C   
2606 O O   . LEU B 66  ? 0.3696 0.3785 0.3242 0.0141  0.0441  -0.0063 109 LEU B O   
2607 C CB  . LEU B 66  ? 0.3495 0.3619 0.3109 0.0070  0.0399  -0.0033 109 LEU B CB  
2608 C CG  . LEU B 66  ? 0.3410 0.3475 0.2955 0.0086  0.0383  -0.0050 109 LEU B CG  
2609 C CD1 . LEU B 66  ? 0.3585 0.3603 0.3062 0.0087  0.0397  -0.0046 109 LEU B CD1 
2610 C CD2 . LEU B 66  ? 0.3321 0.3360 0.2857 0.0075  0.0355  -0.0052 109 LEU B CD2 
2611 N N   . MET B 67  ? 0.3805 0.3991 0.3489 0.0130  0.0426  -0.0050 110 MET B N   
2612 C CA  . MET B 67  ? 0.3841 0.4011 0.3512 0.0159  0.0423  -0.0068 110 MET B CA  
2613 C C   . MET B 67  ? 0.4012 0.4155 0.3643 0.0186  0.0465  -0.0073 110 MET B C   
2614 O O   . MET B 67  ? 0.4025 0.4108 0.3585 0.0202  0.0458  -0.0093 110 MET B O   
2615 C CB  . MET B 67  ? 0.4575 0.4794 0.4322 0.0163  0.0409  -0.0062 110 MET B CB  
2616 C CG  . MET B 67  ? 0.4849 0.5071 0.4609 0.0141  0.0369  -0.0060 110 MET B CG  
2617 S SD  . MET B 67  ? 0.5105 0.5268 0.4802 0.0146  0.0345  -0.0080 110 MET B SD  
2618 C CE  . MET B 67  ? 0.4608 0.4742 0.4265 0.0121  0.0339  -0.0074 110 MET B CE  
2619 N N   . LYS B 68  ? 0.3879 0.4060 0.3553 0.0189  0.0510  -0.0052 111 LYS B N   
2620 C CA  . LYS B 68  ? 0.3835 0.3981 0.3462 0.0220  0.0564  -0.0055 111 LYS B CA  
2621 C C   . LYS B 68  ? 0.3914 0.3972 0.3413 0.0219  0.0569  -0.0068 111 LYS B C   
2622 O O   . LYS B 68  ? 0.3998 0.3977 0.3400 0.0242  0.0577  -0.0088 111 LYS B O   
2623 C CB  . LYS B 68  ? 0.4052 0.4267 0.3768 0.0225  0.0619  -0.0022 111 LYS B CB  
2624 C CG  . LYS B 68  ? 0.5276 0.5578 0.5124 0.0232  0.0614  -0.0004 111 LYS B CG  
2625 C CD  . LYS B 68  ? 0.7081 0.7433 0.7007 0.0260  0.0685  0.0027  111 LYS B CD  
2626 C CE  . LYS B 68  ? 0.6720 0.7171 0.6798 0.0266  0.0672  0.0054  111 LYS B CE  
2627 N NZ  . LYS B 68  ? 0.5808 0.6340 0.5988 0.0216  0.0630  0.0086  111 LYS B NZ  
2628 N N   . LEU B 69  ? 0.3927 0.3987 0.3415 0.0191  0.0560  -0.0055 112 LEU B N   
2629 C CA  . LEU B 69  ? 0.4082 0.4056 0.3448 0.0189  0.0560  -0.0063 112 LEU B CA  
2630 C C   . LEU B 69  ? 0.4068 0.3985 0.3369 0.0191  0.0502  -0.0087 112 LEU B C   
2631 O O   . LEU B 69  ? 0.4163 0.3994 0.3351 0.0201  0.0496  -0.0098 112 LEU B O   
2632 C CB  . LEU B 69  ? 0.4062 0.4048 0.3436 0.0158  0.0558  -0.0042 112 LEU B CB  
2633 C CG  . LEU B 69  ? 0.4518 0.4553 0.3951 0.0146  0.0614  -0.0011 112 LEU B CG  
2634 C CD1 . LEU B 69  ? 0.4795 0.4827 0.4227 0.0109  0.0600  0.0007  112 LEU B CD1 
2635 C CD2 . LEU B 69  ? 0.4836 0.4822 0.4196 0.0174  0.0682  -0.0007 112 LEU B CD2 
2636 N N   . GLY B 70  ? 0.3630 0.3589 0.2999 0.0182  0.0459  -0.0092 113 GLY B N   
2637 C CA  . GLY B 70  ? 0.4172 0.4094 0.3511 0.0183  0.0408  -0.0107 113 GLY B CA  
2638 C C   . GLY B 70  ? 0.4371 0.4267 0.3695 0.0200  0.0396  -0.0126 113 GLY B C   
2639 O O   . GLY B 70  ? 0.4073 0.3954 0.3399 0.0196  0.0350  -0.0133 113 GLY B O   
2640 N N   . THR B 71  ? 0.4126 0.4015 0.3439 0.0221  0.0438  -0.0130 114 THR B N   
2641 C CA  . THR B 71  ? 0.4571 0.4420 0.3859 0.0239  0.0429  -0.0149 114 THR B CA  
2642 C C   . THR B 71  ? 0.4603 0.4358 0.3786 0.0232  0.0383  -0.0165 114 THR B C   
2643 O O   . THR B 71  ? 0.4756 0.4443 0.3838 0.0231  0.0386  -0.0166 114 THR B O   
2644 C CB  . THR B 71  ? 0.4661 0.4489 0.3925 0.0269  0.0492  -0.0150 114 THR B CB  
2645 O OG1 . THR B 71  ? 0.4701 0.4629 0.4085 0.0272  0.0526  -0.0129 114 THR B OG1 
2646 C CG2 . THR B 71  ? 0.5386 0.5153 0.4608 0.0289  0.0484  -0.0172 114 THR B CG2 
2647 N N   . GLN B 72  ? 0.4287 0.4037 0.3497 0.0226  0.0336  -0.0174 115 GLN B N   
2648 C CA  . GLN B 72  ? 0.5004 0.4679 0.4143 0.0212  0.0278  -0.0183 115 GLN B CA  
2649 C C   . GLN B 72  ? 0.5303 0.4956 0.4458 0.0212  0.0250  -0.0195 115 GLN B C   
2650 O O   . GLN B 72  ? 0.5027 0.4752 0.4288 0.0209  0.0248  -0.0188 115 GLN B O   
2651 C CB  . GLN B 72  ? 0.4423 0.4140 0.3615 0.0191  0.0233  -0.0165 115 GLN B CB  
2652 C CG  . GLN B 72  ? 0.4528 0.4180 0.3665 0.0174  0.0165  -0.0165 115 GLN B CG  
2653 C CD  . GLN B 72  ? 0.4177 0.3875 0.3377 0.0162  0.0131  -0.0141 115 GLN B CD  
2654 O OE1 . GLN B 72  ? 0.4056 0.3826 0.3333 0.0165  0.0160  -0.0129 115 GLN B OE1 
2655 N NE2 . GLN B 72  ? 0.4428 0.4078 0.3592 0.0147  0.0067  -0.0133 115 GLN B NE2 
2656 N N   . THR B 73  ? 0.5596 0.5136 0.4634 0.0212  0.0227  -0.0213 116 THR B N   
2657 C CA  . THR B 73  ? 0.6227 0.5722 0.5261 0.0207  0.0195  -0.0226 116 THR B CA  
2658 C C   . THR B 73  ? 0.6002 0.5489 0.5060 0.0172  0.0112  -0.0217 116 THR B C   
2659 O O   . THR B 73  ? 0.6643 0.6048 0.5604 0.0156  0.0066  -0.0220 116 THR B O   
2660 C CB  . THR B 73  ? 0.6962 0.6322 0.5844 0.0227  0.0218  -0.0252 116 THR B CB  
2661 O OG1 . THR B 73  ? 0.7359 0.6743 0.6246 0.0265  0.0303  -0.0253 116 THR B OG1 
2662 C CG2 . THR B 73  ? 0.7058 0.6357 0.5928 0.0219  0.0181  -0.0266 116 THR B CG2 
2663 N N   . VAL B 74  ? 0.5527 0.5096 0.4716 0.0159  0.0093  -0.0203 117 VAL B N   
2664 C CA  . VAL B 74  ? 0.5692 0.5266 0.4935 0.0126  0.0020  -0.0187 117 VAL B CA  
2665 C C   . VAL B 74  ? 0.5907 0.5425 0.5139 0.0115  -0.0004 -0.0199 117 VAL B C   
2666 O O   . VAL B 74  ? 0.5763 0.5292 0.5011 0.0136  0.0043  -0.0209 117 VAL B O   
2667 C CB  . VAL B 74  ? 0.5390 0.5088 0.4785 0.0121  0.0025  -0.0158 117 VAL B CB  
2668 C CG1 . VAL B 74  ? 0.5725 0.5464 0.5119 0.0134  0.0054  -0.0149 117 VAL B CG1 
2669 C CG2 . VAL B 74  ? 0.5206 0.4965 0.4685 0.0133  0.0066  -0.0157 117 VAL B CG2 
2670 N N   . PRO B 75  ? 0.5784 0.5239 0.4992 0.0081  -0.0080 -0.0195 118 PRO B N   
2671 C CA  . PRO B 75  ? 0.5347 0.4739 0.4543 0.0065  -0.0106 -0.0205 118 PRO B CA  
2672 C C   . PRO B 75  ? 0.5101 0.4596 0.4443 0.0070  -0.0073 -0.0189 118 PRO B C   
2673 O O   . PRO B 75  ? 0.4723 0.4314 0.4198 0.0053  -0.0089 -0.0158 118 PRO B O   
2674 C CB  . PRO B 75  ? 0.5658 0.5002 0.4851 0.0018  -0.0205 -0.0190 118 PRO B CB  
2675 C CG  . PRO B 75  ? 0.5933 0.5259 0.5060 0.0018  -0.0228 -0.0186 118 PRO B CG  
2676 C CD  . PRO B 75  ? 0.5792 0.5227 0.4986 0.0053  -0.0151 -0.0178 118 PRO B CD  
2677 N N   . CYS B 76  ? 0.5074 0.4543 0.4387 0.0095  -0.0025 -0.0206 119 CYS B N   
2678 C CA  . CYS B 76  ? 0.4489 0.4051 0.3921 0.0107  0.0015  -0.0191 119 CYS B CA  
2679 C C   . CYS B 76  ? 0.4286 0.3875 0.3817 0.0072  -0.0027 -0.0167 119 CYS B C   
2680 O O   . CYS B 76  ? 0.3918 0.3594 0.3556 0.0076  0.0002  -0.0145 119 CYS B O   
2681 C CB  . CYS B 76  ? 0.4548 0.4070 0.3930 0.0142  0.0066  -0.0211 119 CYS B CB  
2682 S SG  . CYS B 76  ? 0.6208 0.5570 0.5470 0.0137  0.0040  -0.0237 119 CYS B SG  
2683 N N   . ASN B 77  ? 0.4140 0.3652 0.3638 0.0035  -0.0095 -0.0167 120 ASN B N   
2684 C CA  . ASN B 77  ? 0.4443 0.3983 0.4049 -0.0003 -0.0136 -0.0138 120 ASN B CA  
2685 C C   . ASN B 77  ? 0.4286 0.3913 0.4010 -0.0030 -0.0175 -0.0101 120 ASN B C   
2686 O O   . ASN B 77  ? 0.4275 0.3932 0.4105 -0.0066 -0.0214 -0.0069 120 ASN B O   
2687 C CB  . ASN B 77  ? 0.4228 0.3634 0.3747 -0.0035 -0.0194 -0.0154 120 ASN B CB  
2688 C CG  . ASN B 77  ? 0.4401 0.3708 0.3807 -0.0060 -0.0264 -0.0167 120 ASN B CG  
2689 O OD1 . ASN B 77  ? 0.4711 0.3998 0.4028 -0.0035 -0.0246 -0.0185 120 ASN B OD1 
2690 N ND2 . ASN B 77  ? 0.4505 0.3743 0.3910 -0.0113 -0.0349 -0.0156 120 ASN B ND2 
2691 N N   . LYS B 78  ? 0.4353 0.4023 0.4069 -0.0012 -0.0163 -0.0100 121 LYS B N   
2692 C CA  . LYS B 78  ? 0.4616 0.4362 0.4436 -0.0029 -0.0198 -0.0063 121 LYS B CA  
2693 C C   . LYS B 78  ? 0.4511 0.4362 0.4404 0.0005  -0.0131 -0.0049 121 LYS B C   
2694 O O   . LYS B 78  ? 0.4543 0.4429 0.4454 0.0012  -0.0141 -0.0036 121 LYS B O   
2695 C CB  . LYS B 78  ? 0.5141 0.4813 0.4862 -0.0045 -0.0265 -0.0072 121 LYS B CB  
2696 C CG  . LYS B 78  ? 0.5427 0.4958 0.5025 -0.0078 -0.0332 -0.0095 121 LYS B CG  
2697 C CD  . LYS B 78  ? 0.6157 0.5697 0.5863 -0.0126 -0.0394 -0.0065 121 LYS B CD  
2698 C CE  . LYS B 78  ? 0.6645 0.6273 0.6499 -0.0157 -0.0457 -0.0014 121 LYS B CE  
2699 N NZ  . LYS B 78  ? 0.7566 0.7192 0.7522 -0.0214 -0.0531 0.0019  121 LYS B NZ  
2700 N N   . ILE B 79  ? 0.3821 0.3713 0.3747 0.0027  -0.0066 -0.0051 122 ILE B N   
2701 C CA  . ILE B 79  ? 0.4074 0.4040 0.4040 0.0058  -0.0003 -0.0042 122 ILE B CA  
2702 C C   . ILE B 79  ? 0.3824 0.3868 0.3929 0.0054  0.0017  -0.0002 122 ILE B C   
2703 O O   . ILE B 79  ? 0.3751 0.3798 0.3912 0.0038  0.0017  0.0013  122 ILE B O   
2704 C CB  . ILE B 79  ? 0.4142 0.4091 0.4036 0.0086  0.0052  -0.0070 122 ILE B CB  
2705 C CG1 . ILE B 79  ? 0.4232 0.4125 0.4007 0.0100  0.0052  -0.0102 122 ILE B CG1 
2706 C CG2 . ILE B 79  ? 0.3754 0.3770 0.3700 0.0107  0.0108  -0.0055 122 ILE B CG2 
2707 C CD1 . ILE B 79  ? 0.4728 0.4613 0.4452 0.0127  0.0103  -0.0123 122 ILE B CD1 
2708 N N   . LEU B 80  ? 0.3759 0.3862 0.3919 0.0071  0.0040  0.0019  123 LEU B N   
2709 C CA  . LEU B 80  ? 0.3726 0.3898 0.4012 0.0077  0.0076  0.0060  123 LEU B CA  
2710 C C   . LEU B 80  ? 0.3741 0.3929 0.3995 0.0112  0.0148  0.0055  123 LEU B C   
2711 O O   . LEU B 80  ? 0.3512 0.3697 0.3720 0.0128  0.0156  0.0045  123 LEU B O   
2712 C CB  . LEU B 80  ? 0.3702 0.3923 0.4093 0.0067  0.0037  0.0098  123 LEU B CB  
2713 C CG  . LEU B 80  ? 0.3766 0.4063 0.4294 0.0086  0.0088  0.0146  123 LEU B CG  
2714 C CD1 . LEU B 80  ? 0.3896 0.4216 0.4509 0.0071  0.0112  0.0171  123 LEU B CD1 
2715 C CD2 . LEU B 80  ? 0.3783 0.4133 0.4421 0.0082  0.0045  0.0186  123 LEU B CD2 
2716 N N   . LEU B 81  ? 0.3242 0.3434 0.3509 0.0119  0.0196  0.0062  124 LEU B N   
2717 C CA  . LEU B 81  ? 0.3065 0.3258 0.3299 0.0147  0.0261  0.0062  124 LEU B CA  
2718 C C   . LEU B 81  ? 0.3220 0.3457 0.3557 0.0162  0.0302  0.0106  124 LEU B C   
2719 O O   . LEU B 81  ? 0.3335 0.3613 0.3789 0.0147  0.0285  0.0140  124 LEU B O   
2720 C CB  . LEU B 81  ? 0.3566 0.3725 0.3742 0.0149  0.0288  0.0048  124 LEU B CB  
2721 C CG  . LEU B 81  ? 0.3343 0.3464 0.3442 0.0140  0.0254  0.0014  124 LEU B CG  
2722 C CD1 . LEU B 81  ? 0.3319 0.3412 0.3388 0.0141  0.0276  0.0011  124 LEU B CD1 
2723 C CD2 . LEU B 81  ? 0.3537 0.3645 0.3555 0.0152  0.0252  -0.0014 124 LEU B CD2 
2724 N N   . TRP B 82  ? 0.3419 0.3641 0.3713 0.0190  0.0358  0.0107  125 TRP B N   
2725 C CA  . TRP B 82  ? 0.3831 0.4079 0.4207 0.0214  0.0414  0.0148  125 TRP B CA  
2726 C C   . TRP B 82  ? 0.3774 0.3965 0.4052 0.0240  0.0484  0.0140  125 TRP B C   
2727 O O   . TRP B 82  ? 0.3480 0.3620 0.3635 0.0239  0.0478  0.0105  125 TRP B O   
2728 C CB  . TRP B 82  ? 0.3454 0.3740 0.3897 0.0228  0.0400  0.0168  125 TRP B CB  
2729 C CG  . TRP B 82  ? 0.4073 0.4320 0.4410 0.0239  0.0389  0.0136  125 TRP B CG  
2730 C CD1 . TRP B 82  ? 0.3781 0.4025 0.4083 0.0224  0.0328  0.0115  125 TRP B CD1 
2731 C CD2 . TRP B 82  ? 0.3950 0.4145 0.4197 0.0267  0.0443  0.0126  125 TRP B CD2 
2732 N NE1 . TRP B 82  ? 0.3726 0.3930 0.3934 0.0239  0.0342  0.0094  125 TRP B NE1 
2733 C CE2 . TRP B 82  ? 0.3777 0.3951 0.3951 0.0264  0.0409  0.0100  125 TRP B CE2 
2734 C CE3 . TRP B 82  ? 0.4188 0.4341 0.4395 0.0293  0.0517  0.0136  125 TRP B CE3 
2735 C CZ2 . TRP B 82  ? 0.4270 0.4386 0.4345 0.0281  0.0440  0.0084  125 TRP B CZ2 
2736 C CZ3 . TRP B 82  ? 0.4362 0.4446 0.4455 0.0312  0.0546  0.0117  125 TRP B CZ3 
2737 C CH2 . TRP B 82  ? 0.4321 0.4391 0.4355 0.0303  0.0506  0.0092  125 TRP B CH2 
2738 N N   . SER B 83  ? 0.4204 0.4400 0.4538 0.0262  0.0551  0.0177  126 SER B N   
2739 C CA  . SER B 83  ? 0.4453 0.4574 0.4681 0.0290  0.0624  0.0175  126 SER B CA  
2740 C C   . SER B 83  ? 0.4720 0.4851 0.5015 0.0329  0.0691  0.0213  126 SER B C   
2741 O O   . SER B 83  ? 0.4829 0.5013 0.5256 0.0338  0.0728  0.0259  126 SER B O   
2742 C CB  . SER B 83  ? 0.4649 0.4734 0.4840 0.0283  0.0656  0.0182  126 SER B CB  
2743 O OG  . SER B 83  ? 0.5515 0.5513 0.5593 0.0310  0.0729  0.0184  126 SER B OG  
2744 N N   . ARG B 84  ? 0.5492 0.5574 0.5705 0.0353  0.0706  0.0198  127 ARG B N   
2745 C CA  . ARG B 84  ? 0.5839 0.5904 0.6081 0.0399  0.0775  0.0227  127 ARG B CA  
2746 C C   . ARG B 84  ? 0.5754 0.5921 0.6179 0.0410  0.0756  0.0267  127 ARG B C   
2747 O O   . ARG B 84  ? 0.6300 0.6456 0.6740 0.0446  0.0787  0.0283  127 ARG B O   
2748 C CB  . ARG B 84  ? 0.6775 0.6800 0.7014 0.0429  0.0874  0.0260  127 ARG B CB  
2749 C CG  . ARG B 84  ? 0.7879 0.7769 0.7914 0.0438  0.0920  0.0232  127 ARG B CG  
2750 C CD  . ARG B 84  ? 0.9075 0.8913 0.9108 0.0483  0.1036  0.0272  127 ARG B CD  
2751 N NE  . ARG B 84  ? 0.9711 0.9632 0.9896 0.0475  0.1060  0.0316  127 ARG B NE  
2752 C CZ  . ARG B 84  ? 0.9436 0.9327 0.9568 0.0452  0.1066  0.0313  127 ARG B CZ  
2753 N NH1 . ARG B 84  ? 0.8524 0.8308 0.8459 0.0435  0.1043  0.0270  127 ARG B NH1 
2754 N NH2 . ARG B 84  ? 0.8994 0.8962 0.9277 0.0443  0.1090  0.0358  127 ARG B NH2 
2755 N N   . ILE B 85  ? 0.5374 0.5633 0.5933 0.0377  0.0698  0.0285  128 ILE B N   
2756 C CA  . ILE B 85  ? 0.5593 0.5947 0.6330 0.0381  0.0664  0.0327  128 ILE B CA  
2757 C C   . ILE B 85  ? 0.5257 0.5620 0.5956 0.0350  0.0564  0.0294  128 ILE B C   
2758 O O   . ILE B 85  ? 0.5483 0.5897 0.6250 0.0311  0.0488  0.0296  128 ILE B O   
2759 C CB  . ILE B 85  ? 0.5631 0.6074 0.6549 0.0362  0.0664  0.0377  128 ILE B CB  
2760 C CG1 . ILE B 85  ? 0.6162 0.6708 0.7285 0.0371  0.0637  0.0434  128 ILE B CG1 
2761 C CG2 . ILE B 85  ? 0.5307 0.5756 0.6201 0.0306  0.0588  0.0349  128 ILE B CG2 
2762 C CD1 . ILE B 85  ? 0.6969 0.7608 0.8294 0.0355  0.0649  0.0496  128 ILE B CD1 
2763 N N   . LYS B 86  ? 0.5077 0.5382 0.5664 0.0368  0.0565  0.0266  129 LYS B N   
2764 C CA  . LYS B 86  ? 0.4896 0.5196 0.5424 0.0341  0.0481  0.0234  129 LYS B CA  
2765 C C   . LYS B 86  ? 0.5369 0.5735 0.6025 0.0343  0.0428  0.0270  129 LYS B C   
2766 O O   . LYS B 86  ? 0.5010 0.5391 0.5662 0.0309  0.0344  0.0256  129 LYS B O   
2767 C CB  . LYS B 86  ? 0.5076 0.5289 0.5440 0.0354  0.0501  0.0195  129 LYS B CB  
2768 C CG  . LYS B 86  ? 0.5572 0.5775 0.5872 0.0330  0.0428  0.0166  129 LYS B CG  
2769 C CD  . LYS B 86  ? 0.5038 0.5159 0.5185 0.0335  0.0449  0.0130  129 LYS B CD  
2770 C CE  . LYS B 86  ? 0.5676 0.5763 0.5819 0.0373  0.0484  0.0150  129 LYS B CE  
2771 N NZ  . LYS B 86  ? 0.5832 0.5830 0.5822 0.0371  0.0498  0.0116  129 LYS B NZ  
2772 N N   . ASP B 87  ? 0.5309 0.5709 0.6076 0.0384  0.0475  0.0318  130 ASP B N   
2773 C CA  . ASP B 87  ? 0.5763 0.6225 0.6657 0.0390  0.0421  0.0358  130 ASP B CA  
2774 C C   . ASP B 87  ? 0.5420 0.5967 0.6458 0.0348  0.0344  0.0388  130 ASP B C   
2775 O O   . ASP B 87  ? 0.5315 0.5875 0.6362 0.0320  0.0250  0.0387  130 ASP B O   
2776 C CB  . ASP B 87  ? 0.6392 0.6876 0.7390 0.0450  0.0499  0.0409  130 ASP B CB  
2777 C CG  . ASP B 87  ? 0.7710 0.8093 0.8553 0.0489  0.0555  0.0381  130 ASP B CG  
2778 O OD1 . ASP B 87  ? 0.7710 0.8040 0.8425 0.0470  0.0503  0.0340  130 ASP B OD1 
2779 O OD2 . ASP B 87  ? 0.7948 0.8296 0.8790 0.0538  0.0653  0.0399  130 ASP B OD2 
2780 N N   . LEU B 88  ? 0.5183 0.5777 0.6325 0.0340  0.0380  0.0415  131 LEU B N   
2781 C CA  . LEU B 88  ? 0.4842 0.5510 0.6125 0.0294  0.0303  0.0446  131 LEU B CA  
2782 C C   . LEU B 88  ? 0.4887 0.5501 0.6038 0.0240  0.0220  0.0391  131 LEU B C   
2783 O O   . LEU B 88  ? 0.5105 0.5742 0.6307 0.0200  0.0123  0.0401  131 LEU B O   
2784 C CB  . LEU B 88  ? 0.4910 0.5633 0.6326 0.0295  0.0368  0.0488  131 LEU B CB  
2785 C CG  . LEU B 88  ? 0.5784 0.6585 0.7363 0.0242  0.0291  0.0527  131 LEU B CG  
2786 C CD1 . LEU B 88  ? 0.5670 0.6560 0.7434 0.0241  0.0223  0.0587  131 LEU B CD1 
2787 C CD2 . LEU B 88  ? 0.5789 0.6631 0.7475 0.0241  0.0366  0.0564  131 LEU B CD2 
2788 N N   . ALA B 89  ? 0.4884 0.5421 0.5863 0.0240  0.0257  0.0334  132 ALA B N   
2789 C CA  . ALA B 89  ? 0.4536 0.5018 0.5390 0.0199  0.0191  0.0284  132 ALA B CA  
2790 C C   . ALA B 89  ? 0.4640 0.5093 0.5424 0.0188  0.0114  0.0266  132 ALA B C   
2791 O O   . ALA B 89  ? 0.4282 0.4711 0.5030 0.0149  0.0035  0.0250  132 ALA B O   
2792 C CB  . ALA B 89  ? 0.4000 0.4413 0.4697 0.0208  0.0247  0.0234  132 ALA B CB  
2793 N N   . HIS B 90  ? 0.4523 0.4964 0.5274 0.0222  0.0139  0.0268  133 HIS B N   
2794 C CA  . HIS B 90  ? 0.4903 0.5310 0.5584 0.0214  0.0071  0.0256  133 HIS B CA  
2795 C C   . HIS B 90  ? 0.4643 0.5106 0.5465 0.0200  -0.0008 0.0307  133 HIS B C   
2796 O O   . HIS B 90  ? 0.4601 0.5028 0.5364 0.0170  -0.0096 0.0297  133 HIS B O   
2797 C CB  . HIS B 90  ? 0.4643 0.5011 0.5241 0.0254  0.0122  0.0244  133 HIS B CB  
2798 C CG  . HIS B 90  ? 0.5502 0.5807 0.5951 0.0258  0.0178  0.0193  133 HIS B CG  
2799 N ND1 . HIS B 90  ? 0.5952 0.6210 0.6314 0.0286  0.0227  0.0179  133 HIS B ND1 
2800 C CD2 . HIS B 90  ? 0.5049 0.5329 0.5426 0.0236  0.0186  0.0158  133 HIS B CD2 
2801 C CE1 . HIS B 90  ? 0.5235 0.5448 0.5484 0.0277  0.0258  0.0138  133 HIS B CE1 
2802 N NE2 . HIS B 90  ? 0.5099 0.5328 0.5359 0.0250  0.0236  0.0126  133 HIS B NE2 
2803 N N   . GLN B 91  ? 0.4885 0.5433 0.5892 0.0222  0.0022  0.0366  134 GLN B N   
2804 C CA  . GLN B 91  ? 0.5020 0.5639 0.6195 0.0202  -0.0061 0.0424  134 GLN B CA  
2805 C C   . GLN B 91  ? 0.5089 0.5703 0.6274 0.0140  -0.0146 0.0418  134 GLN B C   
2806 O O   . GLN B 91  ? 0.5174 0.5784 0.6382 0.0105  -0.0254 0.0435  134 GLN B O   
2807 C CB  . GLN B 91  ? 0.5446 0.6168 0.6840 0.0238  0.0002  0.0493  134 GLN B CB  
2808 C CG  . GLN B 91  ? 0.6264 0.6982 0.7658 0.0304  0.0081  0.0508  134 GLN B CG  
2809 C CD  . GLN B 91  ? 0.6935 0.7738 0.8522 0.0348  0.0171  0.0571  134 GLN B CD  
2810 O OE1 . GLN B 91  ? 0.7193 0.8098 0.8995 0.0338  0.0136  0.0637  134 GLN B OE1 
2811 N NE2 . GLN B 91  ? 0.7133 0.7890 0.8643 0.0397  0.0288  0.0553  134 GLN B NE2 
2812 N N   . PHE B 92  ? 0.4811 0.5413 0.5969 0.0125  -0.0103 0.0393  135 PHE B N   
2813 C CA  . PHE B 92  ? 0.4692 0.5272 0.5846 0.0066  -0.0178 0.0385  135 PHE B CA  
2814 C C   . PHE B 92  ? 0.4918 0.5391 0.5876 0.0038  -0.0256 0.0331  135 PHE B C   
2815 O O   . PHE B 92  ? 0.5136 0.5584 0.6099 -0.0007 -0.0361 0.0341  135 PHE B O   
2816 C CB  . PHE B 92  ? 0.4858 0.5431 0.5997 0.0062  -0.0108 0.0365  135 PHE B CB  
2817 C CG  . PHE B 92  ? 0.4898 0.5428 0.6004 0.0006  -0.0177 0.0348  135 PHE B CG  
2818 C CD1 . PHE B 92  ? 0.5194 0.5784 0.6471 -0.0035 -0.0228 0.0400  135 PHE B CD1 
2819 C CD2 . PHE B 92  ? 0.4591 0.5015 0.5496 -0.0007 -0.0191 0.0282  135 PHE B CD2 
2820 C CE1 . PHE B 92  ? 0.5292 0.5825 0.6526 -0.0090 -0.0295 0.0383  135 PHE B CE1 
2821 C CE2 . PHE B 92  ? 0.4724 0.5091 0.5586 -0.0054 -0.0251 0.0265  135 PHE B CE2 
2822 C CZ  . PHE B 92  ? 0.4698 0.5112 0.5715 -0.0098 -0.0305 0.0313  135 PHE B CZ  
2823 N N   . THR B 93  ? 0.4484 0.4886 0.5264 0.0063  -0.0206 0.0275  136 THR B N   
2824 C CA  . THR B 93  ? 0.4601 0.4897 0.5191 0.0041  -0.0261 0.0225  136 THR B CA  
2825 C C   . THR B 93  ? 0.5167 0.5436 0.5725 0.0038  -0.0337 0.0240  136 THR B C   
2826 O O   . THR B 93  ? 0.5286 0.5464 0.5711 0.0008  -0.0409 0.0214  136 THR B O   
2827 C CB  . THR B 93  ? 0.4284 0.4526 0.4718 0.0069  -0.0182 0.0170  136 THR B CB  
2828 O OG1 . THR B 93  ? 0.4008 0.4280 0.4454 0.0112  -0.0121 0.0180  136 THR B OG1 
2829 C CG2 . THR B 93  ? 0.4385 0.4634 0.4827 0.0068  -0.0125 0.0153  136 THR B CG2 
2830 N N   . GLN B 94  ? 0.5280 0.5617 0.5947 0.0070  -0.0320 0.0283  137 GLN B N   
2831 C CA  . GLN B 94  ? 0.5990 0.6306 0.6643 0.0066  -0.0400 0.0307  137 GLN B CA  
2832 C C   . GLN B 94  ? 0.6177 0.6504 0.6919 0.0016  -0.0521 0.0344  137 GLN B C   
2833 O O   . GLN B 94  ? 0.6605 0.6868 0.7265 -0.0006 -0.0614 0.0348  137 GLN B O   
2834 C CB  . GLN B 94  ? 0.5995 0.6384 0.6766 0.0116  -0.0352 0.0350  137 GLN B CB  
2835 C CG  . GLN B 94  ? 0.6213 0.6555 0.6853 0.0159  -0.0263 0.0312  137 GLN B CG  
2836 C CD  . GLN B 94  ? 0.7058 0.7295 0.7498 0.0149  -0.0304 0.0274  137 GLN B CD  
2837 O OE1 . GLN B 94  ? 0.7087 0.7258 0.7373 0.0148  -0.0260 0.0221  137 GLN B OE1 
2838 N NE2 . GLN B 94  ? 0.7584 0.7804 0.8030 0.0142  -0.0387 0.0305  137 GLN B NE2 
2839 N N   . VAL B 95  ? 0.5911 0.6311 0.6812 -0.0007 -0.0523 0.0375  138 VAL B N   
2840 C CA  . VAL B 95  ? 0.6709 0.7118 0.7703 -0.0066 -0.0642 0.0412  138 VAL B CA  
2841 C C   . VAL B 95  ? 0.6605 0.6908 0.7450 -0.0114 -0.0681 0.0361  138 VAL B C   
2842 O O   . VAL B 95  ? 0.6731 0.6935 0.7462 -0.0157 -0.0789 0.0349  138 VAL B O   
2843 C CB  . VAL B 95  ? 0.7130 0.7689 0.8411 -0.0065 -0.0624 0.0487  138 VAL B CB  
2844 C CG1 . VAL B 95  ? 0.8689 0.9264 1.0084 -0.0135 -0.0755 0.0530  138 VAL B CG1 
2845 C CG2 . VAL B 95  ? 0.7463 0.8117 0.8888 -0.0011 -0.0583 0.0540  138 VAL B CG2 
2846 N N   . GLN B 96  ? 0.5874 0.6181 0.6704 -0.0105 -0.0595 0.0331  139 GLN B N   
2847 C CA  . GLN B 96  ? 0.5735 0.5934 0.6414 -0.0139 -0.0614 0.0280  139 GLN B CA  
2848 C C   . GLN B 96  ? 0.5861 0.5950 0.6298 -0.0111 -0.0574 0.0212  139 GLN B C   
2849 O O   . GLN B 96  ? 0.5665 0.5750 0.6039 -0.0078 -0.0477 0.0176  139 GLN B O   
2850 C CB  . GLN B 96  ? 0.5843 0.6095 0.6614 -0.0139 -0.0540 0.0282  139 GLN B CB  
2851 C CG  . GLN B 96  ? 0.6231 0.6380 0.6889 -0.0181 -0.0575 0.0244  139 GLN B CG  
2852 C CD  . GLN B 96  ? 0.6305 0.6420 0.7014 -0.0249 -0.0706 0.0275  139 GLN B CD  
2853 O OE1 . GLN B 96  ? 0.6382 0.6604 0.7309 -0.0273 -0.0743 0.0340  139 GLN B OE1 
2854 N NE2 . GLN B 96  ? 0.6415 0.6377 0.6923 -0.0281 -0.0778 0.0229  139 GLN B NE2 
2855 N N   . ARG B 97  ? 0.5736 0.5730 0.6036 -0.0127 -0.0653 0.0200  140 ARG B N   
2856 C CA  . ARG B 97  ? 0.6108 0.6012 0.6203 -0.0096 -0.0612 0.0151  140 ARG B CA  
2857 C C   . ARG B 97  ? 0.5444 0.5236 0.5354 -0.0098 -0.0577 0.0089  140 ARG B C   
2858 O O   . ARG B 97  ? 0.5710 0.5437 0.5464 -0.0070 -0.0529 0.0050  140 ARG B O   
2859 C CB  . ARG B 97  ? 0.6703 0.6532 0.6702 -0.0111 -0.0707 0.0162  140 ARG B CB  
2860 C CG  . ARG B 97  ? 0.6763 0.6699 0.6938 -0.0100 -0.0741 0.0226  140 ARG B CG  
2861 C CD  . ARG B 97  ? 0.7883 0.7737 0.7927 -0.0097 -0.0804 0.0229  140 ARG B CD  
2862 N NE  . ARG B 97  ? 0.8251 0.8060 0.8146 -0.0054 -0.0714 0.0188  140 ARG B NE  
2863 C CZ  . ARG B 97  ? 0.7873 0.7765 0.7848 -0.0007 -0.0631 0.0201  140 ARG B CZ  
2864 N NH1 . ARG B 97  ? 0.7554 0.7576 0.7749 0.0010  -0.0614 0.0251  140 ARG B NH1 
2865 N NH2 . ARG B 97  ? 0.8338 0.8175 0.8167 0.0022  -0.0560 0.0164  140 ARG B NH2 
2866 N N   . ASP B 98  ? 0.6023 0.5789 0.5950 -0.0129 -0.0597 0.0081  141 ASP B N   
2867 C CA  . ASP B 98  ? 0.6115 0.5779 0.5881 -0.0123 -0.0554 0.0025  141 ASP B CA  
2868 C C   . ASP B 98  ? 0.5793 0.5535 0.5630 -0.0089 -0.0446 0.0014  141 ASP B C   
2869 O O   . ASP B 98  ? 0.5697 0.5371 0.5428 -0.0080 -0.0405 -0.0026 141 ASP B O   
2870 C CB  . ASP B 98  ? 0.6050 0.5611 0.5761 -0.0175 -0.0639 0.0018  141 ASP B CB  
2871 C CG  . ASP B 98  ? 0.6381 0.6039 0.6300 -0.0207 -0.0663 0.0061  141 ASP B CG  
2872 O OD1 . ASP B 98  ? 0.6649 0.6449 0.6763 -0.0198 -0.0646 0.0110  141 ASP B OD1 
2873 O OD2 . ASP B 98  ? 0.7072 0.6660 0.6958 -0.0241 -0.0694 0.0049  141 ASP B OD2 
2874 N N   . MET B 99  ? 0.5370 0.5245 0.5376 -0.0069 -0.0398 0.0050  142 MET B N   
2875 C CA  . MET B 99  ? 0.5218 0.5156 0.5275 -0.0037 -0.0300 0.0042  142 MET B CA  
2876 C C   . MET B 99  ? 0.4824 0.4808 0.4869 0.0006  -0.0231 0.0038  142 MET B C   
2877 O O   . MET B 99  ? 0.4640 0.4648 0.4712 0.0013  -0.0254 0.0060  142 MET B O   
2878 C CB  . MET B 99  ? 0.4936 0.4970 0.5184 -0.0051 -0.0290 0.0087  142 MET B CB  
2879 C CG  . MET B 99  ? 0.5751 0.5738 0.6007 -0.0093 -0.0338 0.0086  142 MET B CG  
2880 S SD  . MET B 99  ? 0.7034 0.7128 0.7502 -0.0106 -0.0302 0.0136  142 MET B SD  
2881 C CE  . MET B 99  ? 0.4623 0.4735 0.5040 -0.0054 -0.0179 0.0108  142 MET B CE  
2882 N N   . PHE B 100 ? 0.4758 0.4747 0.4761 0.0034  -0.0152 0.0012  143 PHE B N   
2883 C CA  . PHE B 100 ? 0.4377 0.4382 0.4333 0.0068  -0.0093 0.0000  143 PHE B CA  
2884 C C   . PHE B 100 ? 0.4046 0.4115 0.4071 0.0091  -0.0017 0.0006  143 PHE B C   
2885 O O   . PHE B 100 ? 0.3925 0.3991 0.3956 0.0088  0.0007  -0.0004 143 PHE B O   
2886 C CB  . PHE B 100 ? 0.4645 0.4567 0.4438 0.0077  -0.0077 -0.0044 143 PHE B CB  
2887 C CG  . PHE B 100 ? 0.5299 0.5128 0.4981 0.0057  -0.0144 -0.0057 143 PHE B CG  
2888 C CD1 . PHE B 100 ? 0.5448 0.5209 0.5093 0.0029  -0.0196 -0.0066 143 PHE B CD1 
2889 C CD2 . PHE B 100 ? 0.5317 0.5111 0.4916 0.0065  -0.0153 -0.0060 143 PHE B CD2 
2890 C CE1 . PHE B 100 ? 0.6028 0.5680 0.5544 0.0009  -0.0261 -0.0080 143 PHE B CE1 
2891 C CE2 . PHE B 100 ? 0.5693 0.5383 0.5165 0.0048  -0.0214 -0.0071 143 PHE B CE2 
2892 C CZ  . PHE B 100 ? 0.6374 0.5988 0.5799 0.0020  -0.0269 -0.0082 143 PHE B CZ  
2893 N N   . THR B 101 ? 0.3698 0.3810 0.3761 0.0114  0.0019  0.0023  144 THR B N   
2894 C CA  . THR B 101 ? 0.3712 0.3851 0.3783 0.0138  0.0092  0.0020  144 THR B CA  
2895 C C   . THR B 101 ? 0.3617 0.3718 0.3572 0.0150  0.0118  -0.0012 144 THR B C   
2896 O O   . THR B 101 ? 0.3511 0.3572 0.3388 0.0145  0.0091  -0.0027 144 THR B O   
2897 C CB  . THR B 101 ? 0.3760 0.3951 0.3929 0.0158  0.0123  0.0057  144 THR B CB  
2898 O OG1 . THR B 101 ? 0.4221 0.4404 0.4366 0.0169  0.0108  0.0063  144 THR B OG1 
2899 C CG2 . THR B 101 ? 0.3938 0.4180 0.4248 0.0146  0.0100  0.0098  144 THR B CG2 
2900 N N   . LEU B 102 ? 0.3290 0.3400 0.3231 0.0164  0.0172  -0.0019 145 LEU B N   
2901 C CA  . LEU B 102 ? 0.3392 0.3478 0.3245 0.0171  0.0196  -0.0042 145 LEU B CA  
2902 C C   . LEU B 102 ? 0.3506 0.3582 0.3333 0.0178  0.0190  -0.0035 145 LEU B C   
2903 O O   . LEU B 102 ? 0.3281 0.3326 0.3031 0.0176  0.0189  -0.0051 145 LEU B O   
2904 C CB  . LEU B 102 ? 0.3403 0.3497 0.3252 0.0180  0.0242  -0.0045 145 LEU B CB  
2905 C CG  . LEU B 102 ? 0.3658 0.3735 0.3436 0.0181  0.0262  -0.0061 145 LEU B CG  
2906 C CD1 . LEU B 102 ? 0.3457 0.3522 0.3190 0.0175  0.0249  -0.0082 145 LEU B CD1 
2907 C CD2 . LEU B 102 ? 0.3431 0.3505 0.3201 0.0184  0.0293  -0.0060 145 LEU B CD2 
2908 N N   . GLU B 103 ? 0.3508 0.3605 0.3401 0.0189  0.0191  -0.0007 146 GLU B N   
2909 C CA  . GLU B 103 ? 0.3571 0.3654 0.3444 0.0199  0.0185  0.0004  146 GLU B CA  
2910 C C   . GLU B 103 ? 0.3760 0.3821 0.3607 0.0187  0.0127  0.0007  146 GLU B C   
2911 O O   . GLU B 103 ? 0.3005 0.3043 0.2816 0.0194  0.0116  0.0014  146 GLU B O   
2912 C CB  . GLU B 103 ? 0.3758 0.3869 0.3717 0.0222  0.0209  0.0038  146 GLU B CB  
2913 C CG  . GLU B 103 ? 0.3791 0.3891 0.3735 0.0237  0.0272  0.0034  146 GLU B CG  
2914 C CD  . GLU B 103 ? 0.3967 0.4089 0.3951 0.0231  0.0290  0.0033  146 GLU B CD  
2915 O OE1 . GLU B 103 ? 0.3848 0.4006 0.3910 0.0221  0.0262  0.0048  146 GLU B OE1 
2916 O OE2 . GLU B 103 ? 0.3734 0.3830 0.3666 0.0234  0.0327  0.0020  146 GLU B OE2 
2917 N N   . ASP B 104 ? 0.3502 0.3559 0.3356 0.0168  0.0086  0.0001  147 ASP B N   
2918 C CA  . ASP B 104 ? 0.3600 0.3609 0.3392 0.0153  0.0026  -0.0003 147 ASP B CA  
2919 C C   . ASP B 104 ? 0.3840 0.3787 0.3498 0.0149  0.0040  -0.0038 147 ASP B C   
2920 O O   . ASP B 104 ? 0.3740 0.3625 0.3310 0.0139  0.0000  -0.0045 147 ASP B O   
2921 C CB  . ASP B 104 ? 0.3834 0.3849 0.3684 0.0131  -0.0030 0.0008  147 ASP B CB  
2922 C CG  . ASP B 104 ? 0.4222 0.4306 0.4224 0.0134  -0.0047 0.0053  147 ASP B CG  
2923 O OD1 . ASP B 104 ? 0.4104 0.4205 0.4139 0.0149  -0.0055 0.0079  147 ASP B OD1 
2924 O OD2 . ASP B 104 ? 0.3884 0.4009 0.3980 0.0123  -0.0047 0.0066  147 ASP B OD2 
2925 N N   . THR B 105 ? 0.3522 0.3480 0.3160 0.0157  0.0094  -0.0057 148 THR B N   
2926 C CA  . THR B 105 ? 0.3648 0.3565 0.3186 0.0159  0.0121  -0.0082 148 THR B CA  
2927 C C   . THR B 105 ? 0.3346 0.3258 0.2847 0.0165  0.0147  -0.0076 148 THR B C   
2928 O O   . THR B 105 ? 0.3274 0.3215 0.2828 0.0172  0.0155  -0.0058 148 THR B O   
2929 C CB  . THR B 105 ? 0.3606 0.3548 0.3160 0.0163  0.0162  -0.0098 148 THR B CB  
2930 O OG1 . THR B 105 ? 0.3572 0.3560 0.3179 0.0169  0.0196  -0.0089 148 THR B OG1 
2931 C CG2 . THR B 105 ? 0.3666 0.3610 0.3260 0.0157  0.0140  -0.0102 148 THR B CG2 
2932 N N   . LEU B 106 ? 0.3223 0.3091 0.2631 0.0165  0.0165  -0.0089 149 LEU B N   
2933 C CA  . LEU B 106 ? 0.3729 0.3586 0.3099 0.0166  0.0190  -0.0081 149 LEU B CA  
2934 C C   . LEU B 106 ? 0.3663 0.3569 0.3093 0.0167  0.0227  -0.0076 149 LEU B C   
2935 O O   . LEU B 106 ? 0.3707 0.3612 0.3150 0.0170  0.0230  -0.0061 149 LEU B O   
2936 C CB  . LEU B 106 ? 0.3869 0.3678 0.3140 0.0166  0.0218  -0.0093 149 LEU B CB  
2937 C CG  . LEU B 106 ? 0.4020 0.3821 0.3256 0.0162  0.0253  -0.0083 149 LEU B CG  
2938 C CD1 . LEU B 106 ? 0.4140 0.3908 0.3352 0.0162  0.0222  -0.0065 149 LEU B CD1 
2939 C CD2 . LEU B 106 ? 0.4239 0.3997 0.3389 0.0164  0.0291  -0.0091 149 LEU B CD2 
2940 N N   . LEU B 107 ? 0.3371 0.3311 0.2833 0.0166  0.0252  -0.0087 150 LEU B N   
2941 C CA  . LEU B 107 ? 0.3575 0.3546 0.3073 0.0161  0.0279  -0.0083 150 LEU B CA  
2942 C C   . LEU B 107 ? 0.3428 0.3410 0.2975 0.0167  0.0271  -0.0072 150 LEU B C   
2943 O O   . LEU B 107 ? 0.3185 0.3153 0.2724 0.0166  0.0285  -0.0064 150 LEU B O   
2944 C CB  . LEU B 107 ? 0.3440 0.3444 0.2966 0.0159  0.0297  -0.0093 150 LEU B CB  
2945 C CG  . LEU B 107 ? 0.3507 0.3509 0.3001 0.0157  0.0322  -0.0097 150 LEU B CG  
2946 C CD1 . LEU B 107 ? 0.4385 0.4425 0.3924 0.0162  0.0336  -0.0102 150 LEU B CD1 
2947 C CD2 . LEU B 107 ? 0.3717 0.3718 0.3194 0.0143  0.0342  -0.0085 150 LEU B CD2 
2948 N N   . GLY B 108 ? 0.3160 0.3159 0.2755 0.0174  0.0253  -0.0070 151 GLY B N   
2949 C CA  . GLY B 108 ? 0.3108 0.3119 0.2758 0.0185  0.0256  -0.0054 151 GLY B CA  
2950 C C   . GLY B 108 ? 0.3630 0.3622 0.3280 0.0195  0.0246  -0.0035 151 GLY B C   
2951 O O   . GLY B 108 ? 0.3466 0.3451 0.3134 0.0209  0.0268  -0.0022 151 GLY B O   
2952 N N   . TYR B 109 ? 0.3454 0.3428 0.3073 0.0192  0.0214  -0.0033 152 TYR B N   
2953 C CA  . TYR B 109 ? 0.3393 0.3346 0.3010 0.0202  0.0196  -0.0012 152 TYR B CA  
2954 C C   . TYR B 109 ? 0.3463 0.3382 0.3028 0.0206  0.0228  -0.0011 152 TYR B C   
2955 O O   . TYR B 109 ? 0.3345 0.3250 0.2930 0.0223  0.0236  0.0009  152 TYR B O   
2956 C CB  . TYR B 109 ? 0.3485 0.3408 0.3051 0.0193  0.0150  -0.0012 152 TYR B CB  
2957 C CG  . TYR B 109 ? 0.3580 0.3479 0.3143 0.0203  0.0116  0.0014  152 TYR B CG  
2958 C CD1 . TYR B 109 ? 0.4095 0.4023 0.3745 0.0209  0.0072  0.0041  152 TYR B CD1 
2959 C CD2 . TYR B 109 ? 0.4015 0.3863 0.3494 0.0203  0.0125  0.0016  152 TYR B CD2 
2960 C CE1 . TYR B 109 ? 0.4530 0.4442 0.4189 0.0220  0.0035  0.0070  152 TYR B CE1 
2961 C CE2 . TYR B 109 ? 0.3928 0.3748 0.3400 0.0214  0.0090  0.0042  152 TYR B CE2 
2962 C CZ  . TYR B 109 ? 0.4170 0.4024 0.3734 0.0224  0.0043  0.0070  152 TYR B CZ  
2963 O OH  . TYR B 109 ? 0.4956 0.4787 0.4525 0.0237  0.0003  0.0102  152 TYR B OH  
2964 N N   . LEU B 110 ? 0.3493 0.3394 0.2994 0.0189  0.0248  -0.0028 153 LEU B N   
2965 C CA  . LEU B 110 ? 0.3391 0.3255 0.2841 0.0183  0.0272  -0.0026 153 LEU B CA  
2966 C C   . LEU B 110 ? 0.3360 0.3213 0.2830 0.0191  0.0298  -0.0022 153 LEU B C   
2967 O O   . LEU B 110 ? 0.3279 0.3086 0.2720 0.0200  0.0309  -0.0011 153 LEU B O   
2968 C CB  . LEU B 110 ? 0.3345 0.3208 0.2750 0.0159  0.0289  -0.0040 153 LEU B CB  
2969 C CG  . LEU B 110 ? 0.3746 0.3597 0.3103 0.0154  0.0281  -0.0044 153 LEU B CG  
2970 C CD1 . LEU B 110 ? 0.3796 0.3659 0.3134 0.0137  0.0313  -0.0051 153 LEU B CD1 
2971 C CD2 . LEU B 110 ? 0.4159 0.3955 0.3456 0.0159  0.0265  -0.0029 153 LEU B CD2 
2972 N N   . ALA B 111 ? 0.3455 0.3339 0.2960 0.0188  0.0309  -0.0032 154 ALA B N   
2973 C CA  . ALA B 111 ? 0.3416 0.3270 0.2906 0.0190  0.0335  -0.0033 154 ALA B CA  
2974 C C   . ALA B 111 ? 0.3549 0.3400 0.3084 0.0221  0.0352  -0.0018 154 ALA B C   
2975 O O   . ALA B 111 ? 0.3398 0.3202 0.2899 0.0229  0.0381  -0.0019 154 ALA B O   
2976 C CB  . ALA B 111 ? 0.3466 0.3344 0.2957 0.0170  0.0337  -0.0048 154 ALA B CB  
2977 N N   . ASP B 112 ? 0.3427 0.3321 0.3034 0.0238  0.0335  -0.0003 155 ASP B N   
2978 C CA  . ASP B 112 ? 0.3953 0.3863 0.3632 0.0266  0.0356  0.0018  155 ASP B CA  
2979 C C   . ASP B 112 ? 0.4366 0.4214 0.4014 0.0294  0.0394  0.0032  155 ASP B C   
2980 O O   . ASP B 112 ? 0.3964 0.3782 0.3588 0.0302  0.0386  0.0041  155 ASP B O   
2981 C CB  . ASP B 112 ? 0.4127 0.4093 0.3898 0.0274  0.0319  0.0039  155 ASP B CB  
2982 C CG  . ASP B 112 ? 0.4672 0.4673 0.4548 0.0302  0.0342  0.0069  155 ASP B CG  
2983 O OD1 . ASP B 112 ? 0.4844 0.4858 0.4741 0.0302  0.0371  0.0066  155 ASP B OD1 
2984 O OD2 . ASP B 112 ? 0.5714 0.5733 0.5658 0.0324  0.0331  0.0100  155 ASP B OD2 
2985 N N   . ASP B 113 ? 0.4567 0.4385 0.4205 0.0310  0.0439  0.0033  156 ASP B N   
2986 C CA  . ASP B 113 ? 0.4826 0.4570 0.4426 0.0344  0.0489  0.0046  156 ASP B CA  
2987 C C   . ASP B 113 ? 0.4725 0.4372 0.4198 0.0330  0.0492  0.0029  156 ASP B C   
2988 O O   . ASP B 113 ? 0.5120 0.4689 0.4548 0.0359  0.0527  0.0039  156 ASP B O   
2989 C CB  . ASP B 113 ? 0.5460 0.5237 0.5159 0.0384  0.0494  0.0083  156 ASP B CB  
2990 C CG  . ASP B 113 ? 0.6684 0.6539 0.6516 0.0404  0.0509  0.0111  156 ASP B CG  
2991 O OD1 . ASP B 113 ? 0.7309 0.7156 0.7131 0.0405  0.0546  0.0105  156 ASP B OD1 
2992 O OD2 . ASP B 113 ? 0.6952 0.6874 0.6899 0.0417  0.0480  0.0142  156 ASP B OD2 
2993 N N   . LEU B 114 ? 0.4119 0.3764 0.3535 0.0286  0.0459  0.0005  157 LEU B N   
2994 C CA  . LEU B 114 ? 0.4043 0.3604 0.3352 0.0263  0.0455  -0.0008 157 LEU B CA  
2995 C C   . LEU B 114 ? 0.4167 0.3671 0.3391 0.0235  0.0458  -0.0028 157 LEU B C   
2996 O O   . LEU B 114 ? 0.4142 0.3690 0.3393 0.0225  0.0453  -0.0035 157 LEU B O   
2997 C CB  . LEU B 114 ? 0.3827 0.3428 0.3142 0.0233  0.0415  -0.0012 157 LEU B CB  
2998 C CG  . LEU B 114 ? 0.3912 0.3548 0.3281 0.0254  0.0398  0.0008  157 LEU B CG  
2999 C CD1 . LEU B 114 ? 0.3446 0.3105 0.2795 0.0221  0.0366  0.0001  157 LEU B CD1 
3000 C CD2 . LEU B 114 ? 0.3920 0.3481 0.3259 0.0287  0.0421  0.0026  157 LEU B CD2 
3001 N N   . THR B 115 ? 0.3676 0.3074 0.2792 0.0220  0.0463  -0.0035 158 THR B N   
3002 C CA  . THR B 115 ? 0.4050 0.3374 0.3068 0.0184  0.0452  -0.0052 158 THR B CA  
3003 C C   . THR B 115 ? 0.4003 0.3300 0.2976 0.0136  0.0416  -0.0056 158 THR B C   
3004 O O   . THR B 115 ? 0.3858 0.3131 0.2822 0.0142  0.0420  -0.0048 158 THR B O   
3005 C CB  . THR B 115 ? 0.4556 0.3740 0.3460 0.0210  0.0494  -0.0054 158 THR B CB  
3006 O OG1 . THR B 115 ? 0.4963 0.4179 0.3920 0.0256  0.0537  -0.0044 158 THR B OG1 
3007 C CG2 . THR B 115 ? 0.4802 0.3891 0.3583 0.0166  0.0470  -0.0072 158 THR B CG2 
3008 N N   . TRP B 116 ? 0.3971 0.3277 0.2926 0.0088  0.0381  -0.0065 159 TRP B N   
3009 C CA  . TRP B 116 ? 0.3953 0.3247 0.2887 0.0037  0.0347  -0.0063 159 TRP B CA  
3010 C C   . TRP B 116 ? 0.4215 0.3483 0.3108 -0.0012 0.0308  -0.0068 159 TRP B C   
3011 O O   . TRP B 116 ? 0.3826 0.3134 0.2745 -0.0009 0.0300  -0.0072 159 TRP B O   
3012 C CB  . TRP B 116 ? 0.3623 0.3041 0.2665 0.0030  0.0338  -0.0053 159 TRP B CB  
3013 C CG  . TRP B 116 ? 0.4032 0.3564 0.3165 0.0029  0.0325  -0.0055 159 TRP B CG  
3014 C CD1 . TRP B 116 ? 0.3710 0.3299 0.2885 -0.0010 0.0297  -0.0052 159 TRP B CD1 
3015 C CD2 . TRP B 116 ? 0.3558 0.3158 0.2757 0.0068  0.0341  -0.0058 159 TRP B CD2 
3016 N NE1 . TRP B 116 ? 0.3806 0.3486 0.3059 0.0008  0.0298  -0.0055 159 TRP B NE1 
3017 C CE2 . TRP B 116 ? 0.3619 0.3303 0.2882 0.0052  0.0322  -0.0060 159 TRP B CE2 
3018 C CE3 . TRP B 116 ? 0.3648 0.3246 0.2865 0.0114  0.0366  -0.0055 159 TRP B CE3 
3019 C CZ2 . TRP B 116 ? 0.3274 0.3027 0.2603 0.0079  0.0329  -0.0063 159 TRP B CZ2 
3020 C CZ3 . TRP B 116 ? 0.3783 0.3461 0.3079 0.0135  0.0369  -0.0055 159 TRP B CZ3 
3021 C CH2 . TRP B 116 ? 0.3417 0.3164 0.2759 0.0116  0.0350  -0.0061 159 TRP B CH2 
3022 N N   . CYS B 117 ? 0.4170 0.3369 0.3003 -0.0061 0.0279  -0.0065 160 CYS B N   
3023 C CA  . CYS B 117 ? 0.4353 0.3544 0.3172 -0.0120 0.0226  -0.0062 160 CYS B CA  
3024 C C   . CYS B 117 ? 0.4513 0.3660 0.3307 -0.0174 0.0198  -0.0050 160 CYS B C   
3025 O O   . CYS B 117 ? 0.4140 0.3222 0.2887 -0.0163 0.0222  -0.0049 160 CYS B O   
3026 C CB  . CYS B 117 ? 0.4837 0.3904 0.3528 -0.0122 0.0214  -0.0075 160 CYS B CB  
3027 S SG  . CYS B 117 ? 0.5638 0.4480 0.4130 -0.0116 0.0234  -0.0088 160 CYS B SG  
3028 N N   . GLY B 118 ? 0.4610 0.3795 0.3445 -0.0234 0.0145  -0.0036 161 GLY B N   
3029 C CA  . GLY B 118 ? 0.4353 0.3506 0.3183 -0.0297 0.0111  -0.0018 161 GLY B CA  
3030 C C   . GLY B 118 ? 0.4819 0.3869 0.3562 -0.0359 0.0043  -0.0017 161 GLY B C   
3031 O O   . GLY B 118 ? 0.4470 0.3413 0.3094 -0.0346 0.0033  -0.0036 161 GLY B O   
3032 N N   . GLU B 119 ? 0.4795 0.3874 0.3596 -0.0429 -0.0005 0.0010  162 GLU B N   
3033 C CA  . GLU B 119 ? 0.5232 0.4219 0.3964 -0.0502 -0.0087 0.0018  162 GLU B CA  
3034 C C   . GLU B 119 ? 0.5066 0.4203 0.3976 -0.0563 -0.0135 0.0059  162 GLU B C   
3035 O O   . GLU B 119 ? 0.4935 0.4199 0.3982 -0.0559 -0.0098 0.0081  162 GLU B O   
3036 C CB  . GLU B 119 ? 0.6075 0.4863 0.4637 -0.0539 -0.0103 0.0009  162 GLU B CB  
3037 C CG  . GLU B 119 ? 0.6916 0.5626 0.5438 -0.0636 -0.0199 0.0029  162 GLU B CG  
3038 C CD  . GLU B 119 ? 0.7967 0.6451 0.6295 -0.0671 -0.0216 0.0015  162 GLU B CD  
3039 O OE1 . GLU B 119 ? 0.7801 0.6241 0.6092 -0.0636 -0.0154 0.0007  162 GLU B OE1 
3040 O OE2 . GLU B 119 ? 0.8249 0.6590 0.6451 -0.0734 -0.0295 0.0013  162 GLU B OE2 
3041 N N   . PHE B 120 ? 0.4940 0.4054 0.3842 -0.0618 -0.0217 0.0073  163 PHE B N   
3042 C CA  . PHE B 120 ? 0.5081 0.4343 0.4169 -0.0677 -0.0271 0.0119  163 PHE B CA  
3043 C C   . PHE B 120 ? 0.5446 0.4698 0.4577 -0.0745 -0.0289 0.0150  163 PHE B C   
3044 O O   . PHE B 120 ? 0.4971 0.4047 0.3945 -0.0785 -0.0318 0.0138  163 PHE B O   
3045 C CB  . PHE B 120 ? 0.4903 0.4123 0.3958 -0.0725 -0.0369 0.0130  163 PHE B CB  
3046 C CG  . PHE B 120 ? 0.4861 0.4241 0.4126 -0.0785 -0.0432 0.0185  163 PHE B CG  
3047 C CD1 . PHE B 120 ? 0.4775 0.4355 0.4237 -0.0744 -0.0401 0.0207  163 PHE B CD1 
3048 C CD2 . PHE B 120 ? 0.5070 0.4398 0.4342 -0.0881 -0.0521 0.0218  163 PHE B CD2 
3049 C CE1 . PHE B 120 ? 0.4779 0.4512 0.4449 -0.0791 -0.0452 0.0263  163 PHE B CE1 
3050 C CE2 . PHE B 120 ? 0.4764 0.4253 0.4254 -0.0936 -0.0579 0.0277  163 PHE B CE2 
3051 C CZ  . PHE B 120 ? 0.4963 0.4660 0.4659 -0.0888 -0.0541 0.0301  163 PHE B CZ  
3052 N N   . ALA B 121 ? 0.5573 0.5007 0.4913 -0.0756 -0.0267 0.0191  164 ALA B N   
3053 C CA  . ALA B 121 ? 0.5753 0.5220 0.5186 -0.0827 -0.0284 0.0234  164 ALA B CA  
3054 C C   . ALA B 121 ? 0.5985 0.5352 0.5317 -0.0817 -0.0226 0.0219  164 ALA B C   
3055 O O   . ALA B 121 ? 0.6546 0.5905 0.5921 -0.0882 -0.0242 0.0253  164 ALA B O   
3056 C CB  . ALA B 121 ? 0.6274 0.5657 0.5678 -0.0928 -0.0402 0.0259  164 ALA B CB  
3057 N N   . THR B 122 ? 0.6017 0.5309 0.5222 -0.0740 -0.0161 0.0174  165 THR B N   
3058 C CA  A THR B 122 ? 0.6442 0.5648 0.5560 -0.0720 -0.0105 0.0163  165 THR B CA  
3059 C CA  B THR B 122 ? 0.6443 0.5648 0.5559 -0.0720 -0.0105 0.0163  165 THR B CA  
3060 C C   . THR B 122 ? 0.6207 0.5510 0.5372 -0.0631 -0.0016 0.0148  165 THR B C   
3061 O O   . THR B 122 ? 0.5543 0.4926 0.4751 -0.0578 0.0001  0.0132  165 THR B O   
3062 C CB  A THR B 122 ? 0.6666 0.5641 0.5551 -0.0716 -0.0122 0.0125  165 THR B CB  
3063 C CB  B THR B 122 ? 0.6668 0.5644 0.5552 -0.0716 -0.0122 0.0124  165 THR B CB  
3064 O OG1 A THR B 122 ? 0.6892 0.5834 0.5695 -0.0644 -0.0098 0.0085  165 THR B OG1 
3065 O OG1 B THR B 122 ? 0.6918 0.5810 0.5731 -0.0704 -0.0074 0.0122  165 THR B OG1 
3066 C CG2 A THR B 122 ? 0.6902 0.5751 0.5707 -0.0809 -0.0218 0.0136  165 THR B CG2 
3067 C CG2 B THR B 122 ? 0.6960 0.5900 0.5755 -0.0635 -0.0091 0.0082  165 THR B CG2 
3068 N N   . SER B 123 ? 0.6042 0.5327 0.5192 -0.0618 0.0037  0.0155  166 SER B N   
3069 C CA  . SER B 123 ? 0.5918 0.5277 0.5099 -0.0543 0.0113  0.0145  166 SER B CA  
3070 C C   . SER B 123 ? 0.5907 0.5141 0.4937 -0.0481 0.0141  0.0106  166 SER B C   
3071 O O   . SER B 123 ? 0.6104 0.5372 0.5139 -0.0425 0.0195  0.0101  166 SER B O   
3072 C CB  . SER B 123 ? 0.6011 0.5427 0.5266 -0.0562 0.0155  0.0180  166 SER B CB  
3073 O OG  . SER B 123 ? 0.6696 0.5971 0.5841 -0.0597 0.0148  0.0185  166 SER B OG  
3074 N N   . LYS B 124 ? 0.5875 0.4963 0.4770 -0.0488 0.0107  0.0083  167 LYS B N   
3075 C CA  . LYS B 124 ? 0.6007 0.4963 0.4762 -0.0430 0.0139  0.0054  167 LYS B CA  
3076 C C   . LYS B 124 ? 0.5652 0.4633 0.4396 -0.0366 0.0155  0.0025  167 LYS B C   
3077 O O   . LYS B 124 ? 0.5487 0.4483 0.4238 -0.0381 0.0120  0.0018  167 LYS B O   
3078 C CB  . LYS B 124 ? 0.6694 0.5449 0.5288 -0.0471 0.0105  0.0045  167 LYS B CB  
3079 C CG  . LYS B 124 ? 0.7903 0.6601 0.6482 -0.0527 0.0098  0.0072  167 LYS B CG  
3080 C CD  . LYS B 124 ? 0.8821 0.7509 0.7383 -0.0473 0.0159  0.0075  167 LYS B CD  
3081 C CE  . LYS B 124 ? 1.0665 0.9266 0.9185 -0.0527 0.0154  0.0100  167 LYS B CE  
3082 N NZ  . LYS B 124 ? 1.0743 0.9475 0.9407 -0.0593 0.0140  0.0140  167 LYS B NZ  
3083 N N   . ILE B 125 ? 0.5237 0.4221 0.3966 -0.0294 0.0206  0.0013  168 ILE B N   
3084 C CA  . ILE B 125 ? 0.4769 0.3751 0.3475 -0.0232 0.0228  -0.0010 168 ILE B CA  
3085 C C   . ILE B 125 ? 0.4996 0.3796 0.3542 -0.0226 0.0223  -0.0029 168 ILE B C   
3086 O O   . ILE B 125 ? 0.5050 0.3714 0.3492 -0.0238 0.0226  -0.0028 168 ILE B O   
3087 C CB  . ILE B 125 ? 0.4878 0.3919 0.3629 -0.0163 0.0276  -0.0011 168 ILE B CB  
3088 C CG1 . ILE B 125 ? 0.4735 0.3940 0.3620 -0.0164 0.0282  0.0003  168 ILE B CG1 
3089 C CG2 . ILE B 125 ? 0.5069 0.4085 0.3790 -0.0100 0.0302  -0.0029 168 ILE B CG2 
3090 C CD1 . ILE B 125 ? 0.5077 0.4330 0.3994 -0.0107 0.0316  0.0004  168 ILE B CD1 
3091 N N   . ASN B 126 ? 0.4570 0.3353 0.3083 -0.0206 0.0221  -0.0047 169 ASN B N   
3092 C CA  . ASN B 126 ? 0.5155 0.3752 0.3498 -0.0193 0.0226  -0.0066 169 ASN B CA  
3093 C C   . ASN B 126 ? 0.5129 0.3699 0.3452 -0.0107 0.0294  -0.0074 169 ASN B C   
3094 O O   . ASN B 126 ? 0.4634 0.3275 0.3009 -0.0062 0.0320  -0.0080 169 ASN B O   
3095 C CB  . ASN B 126 ? 0.5007 0.3586 0.3311 -0.0220 0.0187  -0.0077 169 ASN B CB  
3096 C CG  . ASN B 126 ? 0.5788 0.4146 0.3884 -0.0215 0.0190  -0.0097 169 ASN B CG  
3097 O OD1 . ASN B 126 ? 0.5571 0.3812 0.3572 -0.0165 0.0243  -0.0106 169 ASN B OD1 
3098 N ND2 . ASN B 126 ? 0.5404 0.3697 0.3423 -0.0265 0.0132  -0.0103 169 ASN B ND2 
3099 N N   . TYR B 127 ? 0.5159 0.3626 0.3413 -0.0083 0.0324  -0.0071 170 TYR B N   
3100 C CA  . TYR B 127 ? 0.5395 0.3829 0.3637 0.0001  0.0388  -0.0071 170 TYR B CA  
3101 C C   . TYR B 127 ? 0.5725 0.3974 0.3803 0.0032  0.0421  -0.0089 170 TYR B C   
3102 O O   . TYR B 127 ? 0.6031 0.4242 0.4100 0.0106  0.0483  -0.0085 170 TYR B O   
3103 C CB  . TYR B 127 ? 0.5509 0.3917 0.3758 0.0019  0.0406  -0.0055 170 TYR B CB  
3104 C CG  . TYR B 127 ? 0.4965 0.3544 0.3362 0.0009  0.0390  -0.0037 170 TYR B CG  
3105 C CD1 . TYR B 127 ? 0.5025 0.3735 0.3541 0.0063  0.0414  -0.0028 170 TYR B CD1 
3106 C CD2 . TYR B 127 ? 0.4729 0.3331 0.3142 -0.0057 0.0353  -0.0026 170 TYR B CD2 
3107 C CE1 . TYR B 127 ? 0.4578 0.3419 0.3200 0.0053  0.0399  -0.0013 170 TYR B CE1 
3108 C CE2 . TYR B 127 ? 0.4680 0.3421 0.3208 -0.0063 0.0349  -0.0009 170 TYR B CE2 
3109 C CZ  . TYR B 127 ? 0.4809 0.3661 0.3430 -0.0007 0.0371  -0.0005 170 TYR B CZ  
3110 O OH  . TYR B 127 ? 0.5114 0.4081 0.3823 -0.0012 0.0366  0.0010  170 TYR B OH  
3111 N N   . GLN B 128 ? 0.5917 0.4048 0.3867 -0.0021 0.0382  -0.0105 171 GLN B N   
3112 C CA  . GLN B 128 ? 0.6731 0.4651 0.4486 0.0004  0.0413  -0.0124 171 GLN B CA  
3113 C C   . GLN B 128 ? 0.6238 0.4180 0.3984 0.0032  0.0434  -0.0133 171 GLN B C   
3114 O O   . GLN B 128 ? 0.6613 0.4462 0.4283 0.0100  0.0505  -0.0138 171 GLN B O   
3115 C CB  . GLN B 128 ? 0.7752 0.5492 0.5336 -0.0075 0.0352  -0.0136 171 GLN B CB  
3116 C CG  . GLN B 128 ? 0.9086 0.6776 0.6659 -0.0105 0.0336  -0.0125 171 GLN B CG  
3117 C CD  . GLN B 128 ? 1.0991 0.8489 0.8392 -0.0187 0.0272  -0.0135 171 GLN B CD  
3118 O OE1 . GLN B 128 ? 1.1745 0.9154 0.9037 -0.0228 0.0228  -0.0150 171 GLN B OE1 
3119 N NE2 . GLN B 128 ? 1.1417 0.8844 0.8787 -0.0216 0.0260  -0.0125 171 GLN B NE2 
3120 N N   . SER B 129 ? 0.5818 0.3880 0.3643 -0.0016 0.0379  -0.0133 172 SER B N   
3121 C CA  . SER B 129 ? 0.5794 0.3889 0.3621 0.0009  0.0396  -0.0139 172 SER B CA  
3122 C C   . SER B 129 ? 0.5492 0.3787 0.3484 -0.0032 0.0340  -0.0129 172 SER B C   
3123 O O   . SER B 129 ? 0.5384 0.3752 0.3447 -0.0091 0.0281  -0.0120 172 SER B O   
3124 C CB  . SER B 129 ? 0.6225 0.4097 0.3819 -0.0011 0.0384  -0.0159 172 SER B CB  
3125 O OG  . SER B 129 ? 0.6398 0.4228 0.3936 -0.0102 0.0288  -0.0162 172 SER B OG  
3126 N N   . CYS B 130 ? 0.5351 0.3731 0.3406 0.0001  0.0363  -0.0128 173 CYS B N   
3127 C CA  . CYS B 130 ? 0.5204 0.3754 0.3397 -0.0028 0.0317  -0.0120 173 CYS B CA  
3128 C C   . CYS B 130 ? 0.5125 0.3625 0.3243 -0.0020 0.0319  -0.0127 173 CYS B C   
3129 O O   . CYS B 130 ? 0.5150 0.3527 0.3150 0.0027  0.0378  -0.0135 173 CYS B O   
3130 C CB  . CYS B 130 ? 0.5212 0.3959 0.3605 0.0009  0.0346  -0.0107 173 CYS B CB  
3131 S SG  . CYS B 130 ? 0.5356 0.4184 0.3846 -0.0012 0.0330  -0.0095 173 CYS B SG  
3132 N N   . PRO B 131 ? 0.5011 0.3600 0.3192 -0.0062 0.0259  -0.0122 174 PRO B N   
3133 C CA  . PRO B 131 ? 0.5191 0.3721 0.3286 -0.0059 0.0251  -0.0126 174 PRO B CA  
3134 C C   . PRO B 131 ? 0.5152 0.3733 0.3298 0.0012  0.0330  -0.0123 174 PRO B C   
3135 O O   . PRO B 131 ? 0.5554 0.4300 0.3876 0.0040  0.0355  -0.0113 174 PRO B O   
3136 C CB  . PRO B 131 ? 0.4878 0.3537 0.3085 -0.0112 0.0171  -0.0113 174 PRO B CB  
3137 C CG  . PRO B 131 ? 0.5028 0.3756 0.3323 -0.0157 0.0129  -0.0104 174 PRO B CG  
3138 C CD  . PRO B 131 ? 0.4914 0.3656 0.3245 -0.0112 0.0196  -0.0108 174 PRO B CD  
3139 N N   . ASP B 132 ? 0.5622 0.4054 0.3610 0.0037  0.0368  -0.0130 175 ASP B N   
3140 C CA  . ASP B 132 ? 0.6307 0.4782 0.4338 0.0095  0.0438  -0.0123 175 ASP B CA  
3141 C C   . ASP B 132 ? 0.6345 0.4886 0.4410 0.0068  0.0389  -0.0117 175 ASP B C   
3142 O O   . ASP B 132 ? 0.6478 0.4925 0.4422 0.0020  0.0323  -0.0122 175 ASP B O   
3143 C CB  . ASP B 132 ? 0.7164 0.5438 0.5003 0.0140  0.0516  -0.0129 175 ASP B CB  
3144 C CG  . ASP B 132 ? 0.7505 0.5817 0.5386 0.0195  0.0592  -0.0115 175 ASP B CG  
3145 O OD1 . ASP B 132 ? 0.7297 0.5760 0.5361 0.0235  0.0637  -0.0099 175 ASP B OD1 
3146 O OD2 . ASP B 132 ? 0.7874 0.6058 0.5600 0.0195  0.0603  -0.0118 175 ASP B OD2 
3147 N N   . TRP B 133 ? 0.5914 0.4612 0.4143 0.0098  0.0417  -0.0104 176 TRP B N   
3148 C CA  . TRP B 133 ? 0.6090 0.4864 0.4371 0.0076  0.0371  -0.0096 176 TRP B CA  
3149 C C   . TRP B 133 ? 0.6518 0.5129 0.4607 0.0073  0.0371  -0.0098 176 TRP B C   
3150 O O   . TRP B 133 ? 0.6801 0.5414 0.4867 0.0035  0.0302  -0.0094 176 TRP B O   
3151 C CB  . TRP B 133 ? 0.6248 0.5186 0.4712 0.0114  0.0410  -0.0084 176 TRP B CB  
3152 C CG  . TRP B 133 ? 0.6586 0.5476 0.5020 0.0169  0.0500  -0.0075 176 TRP B CG  
3153 C CD1 . TRP B 133 ? 0.6585 0.5492 0.5076 0.0215  0.0572  -0.0068 176 TRP B CD1 
3154 C CD2 . TRP B 133 ? 0.7139 0.5959 0.5489 0.0184  0.0530  -0.0067 176 TRP B CD2 
3155 N NE1 . TRP B 133 ? 0.6578 0.5438 0.5039 0.0258  0.0649  -0.0053 176 TRP B NE1 
3156 C CE2 . TRP B 133 ? 0.7177 0.5978 0.5545 0.0240  0.0628  -0.0054 176 TRP B CE2 
3157 C CE3 . TRP B 133 ? 0.7375 0.6143 0.5638 0.0156  0.0484  -0.0066 176 TRP B CE3 
3158 C CZ2 . TRP B 133 ? 0.7456 0.6190 0.5757 0.0268  0.0688  -0.0040 176 TRP B CZ2 
3159 C CZ3 . TRP B 133 ? 0.7770 0.6461 0.5951 0.0183  0.0539  -0.0054 176 TRP B CZ3 
3160 C CH2 . TRP B 133 ? 0.7849 0.6524 0.6049 0.0238  0.0644  -0.0041 176 TRP B CH2 
3161 N N   . ARG B 134 ? 0.6849 0.5313 0.4798 0.0114  0.0450  -0.0102 177 ARG B N   
3162 C CA  . ARG B 134 ? 0.7202 0.5494 0.4949 0.0120  0.0468  -0.0103 177 ARG B CA  
3163 C C   . ARG B 134 ? 0.7482 0.5557 0.4987 0.0080  0.0419  -0.0121 177 ARG B C   
3164 O O   . ARG B 134 ? 0.7422 0.5407 0.4801 0.0038  0.0350  -0.0121 177 ARG B O   
3165 C CB  . ARG B 134 ? 0.7766 0.6006 0.5486 0.0191  0.0592  -0.0094 177 ARG B CB  
3166 C CG  . ARG B 134 ? 0.8970 0.7024 0.6474 0.0206  0.0632  -0.0091 177 ARG B CG  
3167 C CD  . ARG B 134 ? 0.9828 0.7895 0.7379 0.0276  0.0759  -0.0071 177 ARG B CD  
3168 N NE  . ARG B 134 ? 1.1812 0.9680 0.9135 0.0296  0.0813  -0.0067 177 ARG B NE  
3169 C CZ  . ARG B 134 ? 1.2239 1.0092 0.9512 0.0277  0.0784  -0.0058 177 ARG B CZ  
3170 N NH1 . ARG B 134 ? 1.1474 0.9499 0.8912 0.0240  0.0701  -0.0052 177 ARG B NH1 
3171 N NH2 . ARG B 134 ? 1.2559 1.0210 0.9602 0.0299  0.0843  -0.0054 177 ARG B NH2 
3172 N N   . LYS B 135 ? 0.7315 0.5296 0.4748 0.0089  0.0448  -0.0134 178 LYS B N   
3173 C CA  . LYS B 135 ? 0.7706 0.5450 0.4884 0.0053  0.0408  -0.0152 178 LYS B CA  
3174 C C   . LYS B 135 ? 0.7372 0.5151 0.4578 -0.0030 0.0280  -0.0155 178 LYS B C   
3175 O O   . LYS B 135 ? 0.7257 0.4853 0.4257 -0.0080 0.0212  -0.0165 178 LYS B O   
3176 C CB  . LYS B 135 ? 0.7953 0.5567 0.5035 0.0099  0.0495  -0.0163 178 LYS B CB  
3177 C CG  . LYS B 135 ? 0.8848 0.6436 0.5924 0.0186  0.0631  -0.0153 178 LYS B CG  
3178 C CD  . LYS B 135 ? 1.0277 0.7779 0.7314 0.0240  0.0719  -0.0157 178 LYS B CD  
3179 C CE  . LYS B 135 ? 1.1248 0.8438 0.7963 0.0257  0.0765  -0.0175 178 LYS B CE  
3180 N NZ  . LYS B 135 ? 1.2336 0.9443 0.9024 0.0324  0.0867  -0.0175 178 LYS B NZ  
3181 N N   . ASP B 136 ? 0.7010 0.5011 0.4459 -0.0048 0.0245  -0.0144 179 ASP B N   
3182 C CA  . ASP B 136 ? 0.7055 0.5098 0.4552 -0.0123 0.0138  -0.0141 179 ASP B CA  
3183 C C   . ASP B 136 ? 0.6637 0.4867 0.4311 -0.0158 0.0063  -0.0121 179 ASP B C   
3184 O O   . ASP B 136 ? 0.6249 0.4424 0.3852 -0.0214 -0.0030 -0.0113 179 ASP B O   
3185 C CB  . ASP B 136 ? 0.6606 0.4729 0.4219 -0.0117 0.0162  -0.0143 179 ASP B CB  
3186 C CG  . ASP B 136 ? 0.6832 0.4753 0.4261 -0.0091 0.0221  -0.0161 179 ASP B CG  
3187 O OD1 . ASP B 136 ? 0.7700 0.5401 0.4897 -0.0123 0.0186  -0.0174 179 ASP B OD1 
3188 O OD2 . ASP B 136 ? 0.6509 0.4486 0.4022 -0.0037 0.0300  -0.0160 179 ASP B OD2 
3189 N N   . CYS B 137 ? 0.6609 0.5050 0.4506 -0.0124 0.0099  -0.0110 180 CYS B N   
3190 C CA  . CYS B 137 ? 0.6419 0.5036 0.4491 -0.0151 0.0036  -0.0090 180 CYS B CA  
3191 C C   . CYS B 137 ? 0.6232 0.5036 0.4503 -0.0100 0.0098  -0.0085 180 CYS B C   
3192 O O   . CYS B 137 ? 0.5440 0.4283 0.3768 -0.0065 0.0162  -0.0092 180 CYS B O   
3193 C CB  . CYS B 137 ? 0.6545 0.5224 0.4698 -0.0217 -0.0049 -0.0078 180 CYS B CB  
3194 S SG  . CYS B 137 ? 0.6675 0.5439 0.4946 -0.0211 -0.0008 -0.0082 180 CYS B SG  
3195 N N   . SER B 138 ? 0.5624 0.4537 0.3997 -0.0097 0.0074  -0.0071 181 SER B N   
3196 C CA  A SER B 138 ? 0.5531 0.4598 0.4070 -0.0052 0.0127  -0.0067 181 SER B CA  
3197 C CA  B SER B 138 ? 0.5537 0.4604 0.4076 -0.0052 0.0127  -0.0067 181 SER B CA  
3198 C C   . SER B 138 ? 0.4939 0.4177 0.3669 -0.0062 0.0110  -0.0060 181 SER B C   
3199 O O   . SER B 138 ? 0.4681 0.4021 0.3525 -0.0025 0.0160  -0.0062 181 SER B O   
3200 C CB  A SER B 138 ? 0.5861 0.4950 0.4409 -0.0041 0.0115  -0.0056 181 SER B CB  
3201 C CB  B SER B 138 ? 0.5859 0.4948 0.4408 -0.0041 0.0115  -0.0055 181 SER B CB  
3202 O OG  A SER B 138 ? 0.5727 0.4857 0.4313 -0.0085 0.0027  -0.0040 181 SER B OG  
3203 O OG  B SER B 138 ? 0.6010 0.4937 0.4376 -0.0026 0.0145  -0.0060 181 SER B OG  
3204 N N   . ASN B 139 ? 0.4967 0.4235 0.3733 -0.0112 0.0041  -0.0049 182 ASN B N   
3205 C CA  . ASN B 139 ? 0.4650 0.4078 0.3595 -0.0121 0.0032  -0.0038 182 ASN B CA  
3206 C C   . ASN B 139 ? 0.4532 0.3945 0.3474 -0.0133 0.0050  -0.0044 182 ASN B C   
3207 O O   . ASN B 139 ? 0.4417 0.3867 0.3412 -0.0176 0.0008  -0.0031 182 ASN B O   
3208 C CB  . ASN B 139 ? 0.4849 0.4341 0.3869 -0.0164 -0.0047 -0.0012 182 ASN B CB  
3209 C CG  . ASN B 139 ? 0.5076 0.4602 0.4123 -0.0146 -0.0063 -0.0002 182 ASN B CG  
3210 O OD1 . ASN B 139 ? 0.4919 0.4488 0.4005 -0.0099 -0.0010 -0.0011 182 ASN B OD1 
3211 N ND2 . ASN B 139 ? 0.5271 0.4775 0.4300 -0.0185 -0.0142 0.0019  182 ASN B ND2 
3212 N N   . ASN B 140 ? 0.4241 0.3604 0.3132 -0.0093 0.0114  -0.0061 183 ASN B N   
3213 C CA  . ASN B 140 ? 0.4246 0.3586 0.3127 -0.0096 0.0138  -0.0066 183 ASN B CA  
3214 C C   . ASN B 140 ? 0.4084 0.3563 0.3112 -0.0068 0.0173  -0.0063 183 ASN B C   
3215 O O   . ASN B 140 ? 0.3648 0.3217 0.2761 -0.0038 0.0191  -0.0062 183 ASN B O   
3216 C CB  . ASN B 140 ? 0.4013 0.3208 0.2751 -0.0065 0.0187  -0.0082 183 ASN B CB  
3217 C CG  . ASN B 140 ? 0.4016 0.3241 0.2784 -0.0006 0.0250  -0.0086 183 ASN B CG  
3218 O OD1 . ASN B 140 ? 0.3885 0.3191 0.2748 0.0027  0.0288  -0.0084 183 ASN B OD1 
3219 N ND2 . ASN B 140 ? 0.4506 0.3661 0.3191 0.0006  0.0258  -0.0087 183 ASN B ND2 
3220 N N   . PRO B 141 ? 0.4047 0.3534 0.3094 -0.0079 0.0181  -0.0062 184 PRO B N   
3221 C CA  . PRO B 141 ? 0.3594 0.3201 0.2762 -0.0057 0.0208  -0.0057 184 PRO B CA  
3222 C C   . PRO B 141 ? 0.3424 0.3062 0.2622 -0.0003 0.0254  -0.0066 184 PRO B C   
3223 O O   . PRO B 141 ? 0.3275 0.3014 0.2571 0.0013  0.0262  -0.0063 184 PRO B O   
3224 C CB  . PRO B 141 ? 0.3664 0.3228 0.2801 -0.0075 0.0214  -0.0054 184 PRO B CB  
3225 C CG  . PRO B 141 ? 0.4107 0.3572 0.3154 -0.0126 0.0169  -0.0051 184 PRO B CG  
3226 C CD  . PRO B 141 ? 0.3852 0.3235 0.2806 -0.0117 0.0160  -0.0061 184 PRO B CD  
3227 N N   . VAL B 142 ? 0.3510 0.3060 0.2629 0.0025  0.0285  -0.0073 185 VAL B N   
3228 C CA  . VAL B 142 ? 0.3375 0.2964 0.2544 0.0073  0.0326  -0.0074 185 VAL B CA  
3229 C C   . VAL B 142 ? 0.3494 0.3132 0.2706 0.0085  0.0324  -0.0073 185 VAL B C   
3230 O O   . VAL B 142 ? 0.3285 0.3013 0.2591 0.0101  0.0329  -0.0071 185 VAL B O   
3231 C CB  . VAL B 142 ? 0.3598 0.3085 0.2686 0.0104  0.0368  -0.0075 185 VAL B CB  
3232 C CG1 . VAL B 142 ? 0.3782 0.3318 0.2942 0.0151  0.0407  -0.0067 185 VAL B CG1 
3233 C CG2 . VAL B 142 ? 0.3691 0.3135 0.2747 0.0099  0.0371  -0.0073 185 VAL B CG2 
3234 N N   . SER B 143 ? 0.3340 0.2906 0.2472 0.0075  0.0315  -0.0075 186 SER B N   
3235 C CA  A SER B 143 ? 0.3776 0.3374 0.2936 0.0086  0.0315  -0.0071 186 SER B CA  
3236 C CA  B SER B 143 ? 0.3627 0.3225 0.2787 0.0086  0.0315  -0.0071 186 SER B CA  
3237 C C   . SER B 143 ? 0.3606 0.3314 0.2869 0.0070  0.0280  -0.0068 186 SER B C   
3238 O O   . SER B 143 ? 0.3807 0.3579 0.3141 0.0090  0.0289  -0.0066 186 SER B O   
3239 C CB  A SER B 143 ? 0.4001 0.3486 0.3034 0.0073  0.0305  -0.0072 186 SER B CB  
3240 C CB  B SER B 143 ? 0.4127 0.3611 0.3160 0.0074  0.0305  -0.0072 186 SER B CB  
3241 O OG  A SER B 143 ? 0.4160 0.3531 0.3088 0.0097  0.0352  -0.0076 186 SER B OG  
3242 O OG  B SER B 143 ? 0.4021 0.3479 0.3013 0.0027  0.0247  -0.0071 186 SER B OG  
3243 N N   . VAL B 144 ? 0.3593 0.3321 0.2868 0.0035  0.0241  -0.0064 187 VAL B N   
3244 C CA  . VAL B 144 ? 0.3113 0.2945 0.2492 0.0026  0.0217  -0.0055 187 VAL B CA  
3245 C C   . VAL B 144 ? 0.3152 0.3064 0.2616 0.0050  0.0245  -0.0059 187 VAL B C   
3246 O O   . VAL B 144 ? 0.3471 0.3450 0.3007 0.0064  0.0245  -0.0058 187 VAL B O   
3247 C CB  . VAL B 144 ? 0.3428 0.3270 0.2817 -0.0018 0.0172  -0.0043 187 VAL B CB  
3248 C CG1 . VAL B 144 ? 0.3818 0.3777 0.3333 -0.0019 0.0162  -0.0029 187 VAL B CG1 
3249 C CG2 . VAL B 144 ? 0.3660 0.3418 0.2960 -0.0046 0.0128  -0.0037 187 VAL B CG2 
3250 N N   . PHE B 145 ? 0.3308 0.3199 0.2752 0.0056  0.0266  -0.0064 188 PHE B N   
3251 C CA  . PHE B 145 ? 0.3268 0.3216 0.2771 0.0077  0.0286  -0.0067 188 PHE B CA  
3252 C C   . PHE B 145 ? 0.3194 0.3161 0.2728 0.0107  0.0300  -0.0072 188 PHE B C   
3253 O O   . PHE B 145 ? 0.3069 0.3090 0.2658 0.0117  0.0299  -0.0074 188 PHE B O   
3254 C CB  . PHE B 145 ? 0.2999 0.2908 0.2465 0.0079  0.0301  -0.0068 188 PHE B CB  
3255 C CG  . PHE B 145 ? 0.3062 0.3007 0.2566 0.0102  0.0315  -0.0070 188 PHE B CG  
3256 C CD1 . PHE B 145 ? 0.3073 0.3057 0.2602 0.0096  0.0314  -0.0069 188 PHE B CD1 
3257 C CD2 . PHE B 145 ? 0.2834 0.2771 0.2349 0.0129  0.0327  -0.0071 188 PHE B CD2 
3258 C CE1 . PHE B 145 ? 0.3378 0.3376 0.2918 0.0114  0.0320  -0.0072 188 PHE B CE1 
3259 C CE2 . PHE B 145 ? 0.3209 0.3173 0.2755 0.0144  0.0325  -0.0070 188 PHE B CE2 
3260 C CZ  . PHE B 145 ? 0.3044 0.3031 0.2592 0.0136  0.0319  -0.0073 188 PHE B CZ  
3261 N N   . TRP B 146 ? 0.3144 0.3062 0.2642 0.0121  0.0316  -0.0071 189 TRP B N   
3262 C CA  . TRP B 146 ? 0.3304 0.3244 0.2845 0.0146  0.0332  -0.0069 189 TRP B CA  
3263 C C   . TRP B 146 ? 0.3512 0.3477 0.3080 0.0146  0.0321  -0.0069 189 TRP B C   
3264 O O   . TRP B 146 ? 0.3831 0.3836 0.3455 0.0157  0.0321  -0.0069 189 TRP B O   
3265 C CB  . TRP B 146 ? 0.3322 0.3205 0.2829 0.0165  0.0363  -0.0061 189 TRP B CB  
3266 C CG  . TRP B 146 ? 0.3637 0.3509 0.3145 0.0176  0.0375  -0.0058 189 TRP B CG  
3267 C CD1 . TRP B 146 ? 0.3710 0.3513 0.3148 0.0176  0.0389  -0.0057 189 TRP B CD1 
3268 C CD2 . TRP B 146 ? 0.3508 0.3428 0.3082 0.0188  0.0369  -0.0052 189 TRP B CD2 
3269 N NE1 . TRP B 146 ? 0.3773 0.3585 0.3238 0.0192  0.0395  -0.0050 189 TRP B NE1 
3270 C CE2 . TRP B 146 ? 0.4071 0.3956 0.3619 0.0198  0.0380  -0.0046 189 TRP B CE2 
3271 C CE3 . TRP B 146 ? 0.3840 0.3818 0.3482 0.0191  0.0351  -0.0052 189 TRP B CE3 
3272 C CZ2 . TRP B 146 ? 0.3843 0.3757 0.3438 0.0210  0.0370  -0.0037 189 TRP B CZ2 
3273 C CZ3 . TRP B 146 ? 0.3500 0.3499 0.3179 0.0199  0.0339  -0.0045 189 TRP B CZ3 
3274 C CH2 . TRP B 146 ? 0.3688 0.3658 0.3345 0.0209  0.0346  -0.0036 189 TRP B CH2 
3275 N N   . LYS B 147 ? 0.3613 0.3549 0.3139 0.0131  0.0307  -0.0066 190 LYS B N   
3276 C CA  . LYS B 147 ? 0.3695 0.3655 0.3248 0.0132  0.0292  -0.0063 190 LYS B CA  
3277 C C   . LYS B 147 ? 0.3694 0.3724 0.3317 0.0132  0.0277  -0.0065 190 LYS B C   
3278 O O   . LYS B 147 ? 0.3228 0.3283 0.2889 0.0144  0.0275  -0.0065 190 LYS B O   
3279 C CB  . LYS B 147 ? 0.4150 0.4056 0.3635 0.0115  0.0271  -0.0056 190 LYS B CB  
3280 C CG  . LYS B 147 ? 0.4563 0.4500 0.4067 0.0089  0.0231  -0.0051 190 LYS B CG  
3281 C CD  . LYS B 147 ? 0.5063 0.4932 0.4487 0.0066  0.0197  -0.0042 190 LYS B CD  
3282 C CE  . LYS B 147 ? 0.5041 0.4946 0.4500 0.0033  0.0150  -0.0029 190 LYS B CE  
3283 N NZ  . LYS B 147 ? 0.5633 0.5456 0.4999 0.0003  0.0104  -0.0020 190 LYS B NZ  
3284 N N   . THR B 148 ? 0.3285 0.3339 0.2919 0.0121  0.0272  -0.0067 191 THR B N   
3285 C CA  . THR B 148 ? 0.3679 0.3792 0.3373 0.0126  0.0271  -0.0067 191 THR B CA  
3286 C C   . THR B 148 ? 0.3636 0.3758 0.3346 0.0146  0.0288  -0.0078 191 THR B C   
3287 O O   . THR B 148 ? 0.3667 0.3807 0.3406 0.0160  0.0289  -0.0082 191 THR B O   
3288 C CB  . THR B 148 ? 0.3533 0.3667 0.3236 0.0105  0.0267  -0.0060 191 THR B CB  
3289 O OG1 . THR B 148 ? 0.3582 0.3699 0.3267 0.0079  0.0238  -0.0047 191 THR B OG1 
3290 C CG2 . THR B 148 ? 0.3962 0.4156 0.3729 0.0116  0.0278  -0.0055 191 THR B CG2 
3291 N N   . VAL B 149 ? 0.3526 0.3627 0.3210 0.0146  0.0296  -0.0083 192 VAL B N   
3292 C CA  . VAL B 149 ? 0.3666 0.3768 0.3357 0.0159  0.0300  -0.0091 192 VAL B CA  
3293 C C   . VAL B 149 ? 0.3519 0.3614 0.3232 0.0169  0.0294  -0.0091 192 VAL B C   
3294 O O   . VAL B 149 ? 0.3448 0.3542 0.3172 0.0176  0.0287  -0.0098 192 VAL B O   
3295 C CB  . VAL B 149 ? 0.3751 0.3832 0.3415 0.0157  0.0302  -0.0090 192 VAL B CB  
3296 C CG1 . VAL B 149 ? 0.3905 0.3989 0.3547 0.0145  0.0310  -0.0088 192 VAL B CG1 
3297 C CG2 . VAL B 149 ? 0.3661 0.3715 0.3313 0.0158  0.0308  -0.0082 192 VAL B CG2 
3298 N N   . SER B 150 ? 0.3570 0.3649 0.3281 0.0168  0.0300  -0.0082 193 SER B N   
3299 C CA  A SER B 150 ? 0.3588 0.3664 0.3329 0.0175  0.0301  -0.0077 193 SER B CA  
3300 C CA  B SER B 150 ? 0.3598 0.3674 0.3339 0.0175  0.0301  -0.0077 193 SER B CA  
3301 C C   . SER B 150 ? 0.3740 0.3824 0.3495 0.0178  0.0292  -0.0081 193 SER B C   
3302 O O   . SER B 150 ? 0.3535 0.3616 0.3316 0.0181  0.0285  -0.0082 193 SER B O   
3303 C CB  A SER B 150 ? 0.3622 0.3670 0.3347 0.0177  0.0321  -0.0063 193 SER B CB  
3304 C CB  B SER B 150 ? 0.3627 0.3676 0.3353 0.0177  0.0321  -0.0063 193 SER B CB  
3305 O OG  A SER B 150 ? 0.3817 0.3854 0.3537 0.0182  0.0335  -0.0057 193 SER B OG  
3306 O OG  B SER B 150 ? 0.4038 0.4089 0.3804 0.0183  0.0329  -0.0052 193 SER B OG  
3307 N N   . ARG B 151 ? 0.3697 0.3788 0.3440 0.0176  0.0288  -0.0080 194 ARG B N   
3308 C CA  . ARG B 151 ? 0.3992 0.4091 0.3755 0.0184  0.0281  -0.0080 194 ARG B CA  
3309 C C   . ARG B 151 ? 0.3864 0.3971 0.3641 0.0195  0.0281  -0.0093 194 ARG B C   
3310 O O   . ARG B 151 ? 0.3729 0.3819 0.3514 0.0204  0.0278  -0.0097 194 ARG B O   
3311 C CB  . ARG B 151 ? 0.3924 0.4037 0.3686 0.0179  0.0270  -0.0070 194 ARG B CB  
3312 C CG  . ARG B 151 ? 0.4629 0.4753 0.4421 0.0193  0.0262  -0.0065 194 ARG B CG  
3313 C CD  . ARG B 151 ? 0.5199 0.5337 0.4998 0.0185  0.0240  -0.0047 194 ARG B CD  
3314 N NE  . ARG B 151 ? 0.5942 0.6132 0.5794 0.0189  0.0238  -0.0040 194 ARG B NE  
3315 C CZ  . ARG B 151 ? 0.6763 0.6979 0.6623 0.0170  0.0233  -0.0034 194 ARG B CZ  
3316 N NH1 . ARG B 151 ? 0.6424 0.6606 0.6229 0.0147  0.0226  -0.0037 194 ARG B NH1 
3317 N NH2 . ARG B 151 ? 0.7569 0.7841 0.7494 0.0176  0.0238  -0.0022 194 ARG B NH2 
3318 N N   . ARG B 152 ? 0.3991 0.4111 0.3757 0.0195  0.0289  -0.0099 195 ARG B N   
3319 C CA  . ARG B 152 ? 0.4249 0.4356 0.4002 0.0208  0.0297  -0.0111 195 ARG B CA  
3320 C C   . ARG B 152 ? 0.3600 0.3667 0.3331 0.0205  0.0282  -0.0122 195 ARG B C   
3321 O O   . ARG B 152 ? 0.3709 0.3741 0.3419 0.0215  0.0279  -0.0133 195 ARG B O   
3322 C CB  . ARG B 152 ? 0.4586 0.4708 0.4324 0.0206  0.0313  -0.0112 195 ARG B CB  
3323 C CG  . ARG B 152 ? 0.5645 0.5814 0.5423 0.0206  0.0324  -0.0097 195 ARG B CG  
3324 C CD  . ARG B 152 ? 0.6509 0.6693 0.6278 0.0197  0.0341  -0.0093 195 ARG B CD  
3325 N NE  . ARG B 152 ? 0.7348 0.7573 0.7163 0.0208  0.0366  -0.0079 195 ARG B NE  
3326 C CZ  . ARG B 152 ? 0.7355 0.7568 0.7154 0.0230  0.0401  -0.0084 195 ARG B CZ  
3327 N NH1 . ARG B 152 ? 0.6948 0.7098 0.6670 0.0239  0.0407  -0.0105 195 ARG B NH1 
3328 N NH2 . ARG B 152 ? 0.7628 0.7889 0.7489 0.0244  0.0432  -0.0065 195 ARG B NH2 
3329 N N   . PHE B 153 ? 0.3453 0.3521 0.3188 0.0192  0.0271  -0.0116 196 PHE B N   
3330 C CA  . PHE B 153 ? 0.3590 0.3632 0.3326 0.0185  0.0248  -0.0117 196 PHE B CA  
3331 C C   . PHE B 153 ? 0.3802 0.3831 0.3566 0.0183  0.0239  -0.0113 196 PHE B C   
3332 O O   . PHE B 153 ? 0.3766 0.3756 0.3515 0.0179  0.0218  -0.0122 196 PHE B O   
3333 C CB  . PHE B 153 ? 0.3453 0.3513 0.3214 0.0176  0.0244  -0.0102 196 PHE B CB  
3334 C CG  . PHE B 153 ? 0.3269 0.3313 0.3043 0.0166  0.0213  -0.0097 196 PHE B CG  
3335 C CD1 . PHE B 153 ? 0.3468 0.3477 0.3188 0.0164  0.0191  -0.0110 196 PHE B CD1 
3336 C CD2 . PHE B 153 ? 0.3049 0.3112 0.2890 0.0159  0.0205  -0.0076 196 PHE B CD2 
3337 C CE1 . PHE B 153 ? 0.3418 0.3407 0.3147 0.0150  0.0149  -0.0102 196 PHE B CE1 
3338 C CE2 . PHE B 153 ? 0.3525 0.3585 0.3398 0.0147  0.0168  -0.0065 196 PHE B CE2 
3339 C CZ  . PHE B 153 ? 0.3420 0.3441 0.3235 0.0140  0.0134  -0.0078 196 PHE B CZ  
3340 N N   . ALA B 154 ? 0.3676 0.3724 0.3469 0.0184  0.0253  -0.0101 197 ALA B N   
3341 C CA  . ALA B 154 ? 0.3451 0.3482 0.3266 0.0182  0.0248  -0.0094 197 ALA B CA  
3342 C C   . ALA B 154 ? 0.3665 0.3667 0.3455 0.0196  0.0245  -0.0108 197 ALA B C   
3343 O O   . ALA B 154 ? 0.3485 0.3448 0.3275 0.0192  0.0231  -0.0110 197 ALA B O   
3344 C CB  . ALA B 154 ? 0.3400 0.3444 0.3228 0.0183  0.0266  -0.0077 197 ALA B CB  
3345 N N   . GLU B 155 ? 0.3554 0.3572 0.3329 0.0212  0.0260  -0.0114 198 GLU B N   
3346 C CA  . GLU B 155 ? 0.3702 0.3695 0.3462 0.0233  0.0268  -0.0123 198 GLU B CA  
3347 C C   . GLU B 155 ? 0.4256 0.4188 0.3964 0.0236  0.0261  -0.0143 198 GLU B C   
3348 O O   . GLU B 155 ? 0.3599 0.3480 0.3281 0.0253  0.0265  -0.0152 198 GLU B O   
3349 C CB  . GLU B 155 ? 0.3799 0.3834 0.3573 0.0250  0.0288  -0.0118 198 GLU B CB  
3350 C CG  . GLU B 155 ? 0.4275 0.4349 0.4088 0.0248  0.0283  -0.0098 198 GLU B CG  
3351 C CD  . GLU B 155 ? 0.4717 0.4842 0.4561 0.0255  0.0293  -0.0087 198 GLU B CD  
3352 O OE1 . GLU B 155 ? 0.5029 0.5166 0.4866 0.0259  0.0311  -0.0094 198 GLU B OE1 
3353 O OE2 . GLU B 155 ? 0.4925 0.5077 0.4800 0.0254  0.0280  -0.0068 198 GLU B OE2 
3354 N N   . ALA B 156 ? 0.3843 0.3766 0.3524 0.0222  0.0249  -0.0150 199 ALA B N   
3355 C CA  . ALA B 156 ? 0.4403 0.4252 0.4011 0.0222  0.0236  -0.0169 199 ALA B CA  
3356 C C   . ALA B 156 ? 0.3860 0.3658 0.3462 0.0198  0.0194  -0.0170 199 ALA B C   
3357 O O   . ALA B 156 ? 0.4181 0.3894 0.3708 0.0195  0.0174  -0.0188 199 ALA B O   
3358 C CB  . ALA B 156 ? 0.4188 0.4042 0.3760 0.0215  0.0234  -0.0173 199 ALA B CB  
3359 N N   . ALA B 157 ? 0.3863 0.3703 0.3539 0.0179  0.0180  -0.0150 200 ALA B N   
3360 C CA  . ALA B 157 ? 0.4025 0.3831 0.3720 0.0150  0.0139  -0.0143 200 ALA B CA  
3361 C C   . ALA B 157 ? 0.3915 0.3645 0.3573 0.0153  0.0132  -0.0154 200 ALA B C   
3362 O O   . ALA B 157 ? 0.3729 0.3453 0.3375 0.0181  0.0163  -0.0159 200 ALA B O   
3363 C CB  . ALA B 157 ? 0.3844 0.3718 0.3637 0.0135  0.0142  -0.0113 200 ALA B CB  
3364 N N   . CYS B 158 ? 0.3650 0.3318 0.3293 0.0123  0.0085  -0.0155 201 CYS B N   
3365 C CA  . CYS B 158 ? 0.4243 0.3817 0.3835 0.0120  0.0071  -0.0167 201 CYS B CA  
3366 C C   . CYS B 158 ? 0.4198 0.3752 0.3841 0.0073  0.0018  -0.0148 201 CYS B C   
3367 O O   . CYS B 158 ? 0.4051 0.3657 0.3758 0.0045  -0.0012 -0.0128 201 CYS B O   
3368 C CB  . CYS B 158 ? 0.4513 0.3974 0.3970 0.0137  0.0068  -0.0201 201 CYS B CB  
3369 S SG  . CYS B 158 ? 0.5337 0.4723 0.4718 0.0098  -0.0001 -0.0211 201 CYS B SG  
3370 N N   . ASP B 159 ? 0.4287 0.3767 0.3908 0.0064  0.0007  -0.0151 202 ASP B N   
3371 C CA  . ASP B 159 ? 0.4425 0.3872 0.4090 0.0014  -0.0047 -0.0132 202 ASP B CA  
3372 C C   . ASP B 159 ? 0.4090 0.3655 0.3906 -0.0006 -0.0037 -0.0088 202 ASP B C   
3373 O O   . ASP B 159 ? 0.4003 0.3607 0.3864 0.0010  0.0007  -0.0072 202 ASP B O   
3374 C CB  . ASP B 159 ? 0.4496 0.3869 0.4098 -0.0021 -0.0116 -0.0144 202 ASP B CB  
3375 C CG  . ASP B 159 ? 0.4903 0.4217 0.4538 -0.0079 -0.0183 -0.0126 202 ASP B CG  
3376 O OD1 . ASP B 159 ? 0.4515 0.3794 0.4165 -0.0084 -0.0172 -0.0119 202 ASP B OD1 
3377 O OD2 . ASP B 159 ? 0.5099 0.4401 0.4746 -0.0121 -0.0251 -0.0116 202 ASP B OD2 
3378 N N   . VAL B 160 ? 0.3786 0.3401 0.3675 -0.0038 -0.0075 -0.0066 203 VAL B N   
3379 C CA  . VAL B 160 ? 0.3982 0.3708 0.4020 -0.0053 -0.0058 -0.0020 203 VAL B CA  
3380 C C   . VAL B 160 ? 0.3966 0.3778 0.4032 -0.0027 -0.0029 -0.0017 203 VAL B C   
3381 O O   . VAL B 160 ? 0.3864 0.3668 0.3898 -0.0031 -0.0065 -0.0027 203 VAL B O   
3382 C CB  . VAL B 160 ? 0.3920 0.3648 0.4052 -0.0110 -0.0122 0.0013  203 VAL B CB  
3383 C CG1 . VAL B 160 ? 0.4095 0.3943 0.4394 -0.0117 -0.0089 0.0066  203 VAL B CG1 
3384 C CG2 . VAL B 160 ? 0.4438 0.4063 0.4530 -0.0141 -0.0157 0.0008  203 VAL B CG2 
3385 N N   . VAL B 161 ? 0.3702 0.3583 0.3817 -0.0001 0.0034  0.0000  204 VAL B N   
3386 C CA  . VAL B 161 ? 0.3669 0.3623 0.3808 0.0024  0.0067  0.0006  204 VAL B CA  
3387 C C   . VAL B 161 ? 0.3715 0.3747 0.3988 0.0013  0.0088  0.0053  204 VAL B C   
3388 O O   . VAL B 161 ? 0.4173 0.4213 0.4499 0.0006  0.0116  0.0078  204 VAL B O   
3389 C CB  . VAL B 161 ? 0.4146 0.4103 0.4217 0.0063  0.0122  -0.0015 204 VAL B CB  
3390 C CG1 . VAL B 161 ? 0.3873 0.3886 0.3953 0.0083  0.0149  -0.0011 204 VAL B CG1 
3391 C CG2 . VAL B 161 ? 0.4683 0.4570 0.4645 0.0077  0.0110  -0.0053 204 VAL B CG2 
3392 N N   . HIS B 162 ? 0.3799 0.3885 0.4128 0.0016  0.0080  0.0069  205 HIS B N   
3393 C CA  . HIS B 162 ? 0.3735 0.3899 0.4203 0.0013  0.0106  0.0118  205 HIS B CA  
3394 C C   . HIS B 162 ? 0.3542 0.3742 0.3996 0.0054  0.0173  0.0120  205 HIS B C   
3395 O O   . HIS B 162 ? 0.3555 0.3737 0.3920 0.0074  0.0172  0.0090  205 HIS B O   
3396 C CB  . HIS B 162 ? 0.4142 0.4342 0.4705 -0.0015 0.0041  0.0145  205 HIS B CB  
3397 C CG  . HIS B 162 ? 0.4536 0.4690 0.5112 -0.0064 -0.0034 0.0147  205 HIS B CG  
3398 N ND1 . HIS B 162 ? 0.4436 0.4499 0.4884 -0.0079 -0.0096 0.0106  205 HIS B ND1 
3399 C CD2 . HIS B 162 ? 0.4656 0.4831 0.5350 -0.0103 -0.0057 0.0187  205 HIS B CD2 
3400 C CE1 . HIS B 162 ? 0.4259 0.4279 0.4734 -0.0125 -0.0158 0.0116  205 HIS B CE1 
3401 N NE2 . HIS B 162 ? 0.4809 0.4901 0.5439 -0.0143 -0.0139 0.0167  205 HIS B NE2 
3402 N N   . VAL B 163 ? 0.3478 0.3718 0.4010 0.0066  0.0233  0.0157  206 VAL B N   
3403 C CA  . VAL B 163 ? 0.3514 0.3771 0.4029 0.0104  0.0299  0.0164  206 VAL B CA  
3404 C C   . VAL B 163 ? 0.3748 0.4072 0.4413 0.0110  0.0335  0.0220  206 VAL B C   
3405 O O   . VAL B 163 ? 0.3641 0.3989 0.4401 0.0094  0.0351  0.0256  206 VAL B O   
3406 C CB  . VAL B 163 ? 0.3388 0.3596 0.3802 0.0124  0.0355  0.0148  206 VAL B CB  
3407 C CG1 . VAL B 163 ? 0.3645 0.3848 0.4110 0.0112  0.0386  0.0178  206 VAL B CG1 
3408 C CG2 . VAL B 163 ? 0.3671 0.3874 0.4042 0.0160  0.0416  0.0151  206 VAL B CG2 
3409 N N   . MET B 164 ? 0.3671 0.4027 0.4364 0.0136  0.0350  0.0231  207 MET B N   
3410 C CA  . MET B 164 ? 0.3967 0.4387 0.4803 0.0155  0.0400  0.0287  207 MET B CA  
3411 C C   . MET B 164 ? 0.4180 0.4563 0.4949 0.0197  0.0501  0.0290  207 MET B C   
3412 O O   . MET B 164 ? 0.3891 0.4216 0.4521 0.0219  0.0517  0.0252  207 MET B O   
3413 C CB  . MET B 164 ? 0.4318 0.4784 0.5221 0.0165  0.0363  0.0301  207 MET B CB  
3414 C CG  . MET B 164 ? 0.4894 0.5410 0.5913 0.0123  0.0269  0.0323  207 MET B CG  
3415 S SD  . MET B 164 ? 0.6021 0.6573 0.7087 0.0133  0.0211  0.0336  207 MET B SD  
3416 C CE  . MET B 164 ? 0.4575 0.5169 0.5718 0.0196  0.0319  0.0378  207 MET B CE  
3417 N N   . LEU B 165 ? 0.4778 0.5187 0.5641 0.0206  0.0567  0.0337  208 LEU B N   
3418 C CA  . LEU B 165 ? 0.4917 0.5273 0.5705 0.0246  0.0670  0.0345  208 LEU B CA  
3419 C C   . LEU B 165 ? 0.5220 0.5631 0.6149 0.0282  0.0742  0.0404  208 LEU B C   
3420 O O   . LEU B 165 ? 0.5078 0.5584 0.6200 0.0267  0.0723  0.0454  208 LEU B O   
3421 C CB  . LEU B 165 ? 0.4653 0.4964 0.5395 0.0232  0.0704  0.0350  208 LEU B CB  
3422 C CG  . LEU B 165 ? 0.4579 0.4830 0.5185 0.0204  0.0643  0.0298  208 LEU B CG  
3423 C CD1 . LEU B 165 ? 0.4718 0.4927 0.5296 0.0191  0.0676  0.0312  208 LEU B CD1 
3424 C CD2 . LEU B 165 ? 0.4838 0.5018 0.5271 0.0225  0.0642  0.0248  208 LEU B CD2 
3425 N N   . ASP B 166 ? 0.4877 0.5225 0.5708 0.0331  0.0825  0.0400  209 ASP B N   
3426 C CA  . ASP B 166 ? 0.5221 0.5604 0.6163 0.0378  0.0910  0.0453  209 ASP B CA  
3427 C C   . ASP B 166 ? 0.5415 0.5786 0.6398 0.0393  0.1011  0.0498  209 ASP B C   
3428 O O   . ASP B 166 ? 0.5595 0.5856 0.6410 0.0416  0.1082  0.0480  209 ASP B O   
3429 C CB  . ASP B 166 ? 0.5500 0.5797 0.6296 0.0424  0.0952  0.0424  209 ASP B CB  
3430 C CG  . ASP B 166 ? 0.6118 0.6433 0.7011 0.0484  0.1051  0.0477  209 ASP B CG  
3431 O OD1 . ASP B 166 ? 0.5781 0.6200 0.6887 0.0488  0.1076  0.0541  209 ASP B OD1 
3432 O OD2 . ASP B 166 ? 0.6825 0.7045 0.7582 0.0526  0.1105  0.0458  209 ASP B OD2 
3433 N N   . GLY B 167 ? 0.5600 0.6081 0.6806 0.0379  0.1017  0.0561  210 GLY B N   
3434 C CA  . GLY B 167 ? 0.6025 0.6510 0.7302 0.0390  0.1116  0.0614  210 GLY B CA  
3435 C C   . GLY B 167 ? 0.6483 0.6957 0.7803 0.0458  0.1251  0.0663  210 GLY B C   
3436 O O   . GLY B 167 ? 0.6726 0.7199 0.8102 0.0474  0.1351  0.0712  210 GLY B O   
3437 N N   . SER B 168 ? 0.6614 0.7075 0.7908 0.0503  0.1264  0.0653  211 SER B N   
3438 C CA  . SER B 168 ? 0.6906 0.7337 0.8221 0.0577  0.1399  0.0695  211 SER B CA  
3439 C C   . SER B 168 ? 0.7282 0.7526 0.8309 0.0615  0.1484  0.0651  211 SER B C   
3440 O O   . SER B 168 ? 0.7441 0.7624 0.8442 0.0680  0.1612  0.0682  211 SER B O   
3441 C CB  . SER B 168 ? 0.6862 0.7356 0.8282 0.0610  0.1372  0.0708  211 SER B CB  
3442 O OG  . SER B 168 ? 0.7250 0.7650 0.8464 0.0607  0.1308  0.0635  211 SER B OG  
3443 N N   . ARG B 169 ? 0.7695 0.7842 0.8506 0.0578  0.1418  0.0582  212 ARG B N   
3444 C CA  . ARG B 169 ? 0.8637 0.8600 0.9164 0.0603  0.1473  0.0537  212 ARG B CA  
3445 C C   . ARG B 169 ? 0.8692 0.8582 0.9121 0.0586  0.1519  0.0543  212 ARG B C   
3446 O O   . ARG B 169 ? 0.8216 0.8194 0.8774 0.0544  0.1483  0.0566  212 ARG B O   
3447 C CB  . ARG B 169 ? 0.9264 0.9166 0.9620 0.0573  0.1365  0.0461  212 ARG B CB  
3448 C CG  . ARG B 169 ? 1.0024 0.9774 1.0165 0.0615  0.1412  0.0427  212 ARG B CG  
3449 C CD  . ARG B 169 ? 1.0196 0.9990 1.0448 0.0663  0.1446  0.0452  212 ARG B CD  
3450 N NE  . ARG B 169 ? 1.0206 1.0096 1.0546 0.0631  0.1328  0.0430  212 ARG B NE  
3451 C CZ  . ARG B 169 ? 1.0124 1.0071 1.0575 0.0661  0.1325  0.0450  212 ARG B CZ  
3452 N NH1 . ARG B 169 ? 1.0039 0.9967 1.0546 0.0728  0.1434  0.0495  212 ARG B NH1 
3453 N NH2 . ARG B 169 ? 0.9552 0.9571 1.0055 0.0627  0.1213  0.0426  212 ARG B NH2 
3454 N N   . SER B 170 ? 0.9544 0.9259 0.9730 0.0618  0.1597  0.0521  213 SER B N   
3455 C CA  . SER B 170 ? 0.9917 0.9538 0.9979 0.0608  0.1648  0.0529  213 SER B CA  
3456 C C   . SER B 170 ? 0.9559 0.9188 0.9559 0.0542  0.1527  0.0486  213 SER B C   
3457 O O   . SER B 170 ? 0.9997 0.9653 1.0051 0.0513  0.1529  0.0511  213 SER B O   
3458 C CB  . SER B 170 ? 1.1076 1.0483 1.0854 0.0654  0.1742  0.0509  213 SER B CB  
3459 O OG  . SER B 170 ? 1.1167 1.0479 1.0752 0.0641  0.1662  0.0442  213 SER B OG  
3460 N N   . LYS B 171 ? 0.8426 0.8027 0.8316 0.0518  0.1424  0.0425  214 LYS B N   
3461 C CA  . LYS B 171 ? 0.7439 0.7047 0.7272 0.0463  0.1311  0.0384  214 LYS B CA  
3462 C C   . LYS B 171 ? 0.6707 0.6474 0.6739 0.0428  0.1210  0.0379  214 LYS B C   
3463 O O   . LYS B 171 ? 0.6690 0.6472 0.6694 0.0420  0.1138  0.0339  214 LYS B O   
3464 C CB  . LYS B 171 ? 0.7502 0.6971 0.7084 0.0458  0.1266  0.0326  214 LYS B CB  
3465 C CG  . LYS B 171 ? 0.7942 0.7232 0.7294 0.0477  0.1339  0.0328  214 LYS B CG  
3466 C CD  . LYS B 171 ? 0.8065 0.7220 0.7177 0.0462  0.1276  0.0273  214 LYS B CD  
3467 C CE  . LYS B 171 ? 0.8841 0.7904 0.7843 0.0497  0.1315  0.0256  214 LYS B CE  
3468 N NZ  . LYS B 171 ? 0.9429 0.8315 0.8158 0.0484  0.1278  0.0214  214 LYS B NZ  
3469 N N   . ILE B 172 ? 0.6465 0.6344 0.6692 0.0406  0.1205  0.0420  215 ILE B N   
3470 C CA  . ILE B 172 ? 0.6016 0.6029 0.6419 0.0371  0.1108  0.0418  215 ILE B CA  
3471 C C   . ILE B 172 ? 0.5712 0.5701 0.6006 0.0334  0.0998  0.0356  215 ILE B C   
3472 O O   . ILE B 172 ? 0.5695 0.5735 0.6023 0.0324  0.0925  0.0329  215 ILE B O   
3473 C CB  . ILE B 172 ? 0.5765 0.5877 0.6369 0.0343  0.1111  0.0471  215 ILE B CB  
3474 C CG1 . ILE B 172 ? 0.6266 0.6409 0.6994 0.0382  0.1233  0.0540  215 ILE B CG1 
3475 C CG2 . ILE B 172 ? 0.5599 0.5831 0.6369 0.0304  0.1005  0.0469  215 ILE B CG2 
3476 C CD1 . ILE B 172 ? 0.6364 0.6614 0.7315 0.0351  0.1240  0.0603  215 ILE B CD1 
3477 N N   . PHE B 173 ? 0.5326 0.5236 0.5487 0.0318  0.0987  0.0336  216 PHE B N   
3478 C CA  . PHE B 173 ? 0.5247 0.5116 0.5281 0.0295  0.0902  0.0281  216 PHE B CA  
3479 C C   . PHE B 173 ? 0.5498 0.5237 0.5318 0.0317  0.0933  0.0256  216 PHE B C   
3480 O O   . PHE B 173 ? 0.5541 0.5187 0.5261 0.0333  0.1003  0.0275  216 PHE B O   
3481 C CB  . PHE B 173 ? 0.5025 0.4897 0.5065 0.0260  0.0854  0.0278  216 PHE B CB  
3482 C CG  . PHE B 173 ? 0.4649 0.4461 0.4544 0.0247  0.0788  0.0231  216 PHE B CG  
3483 C CD1 . PHE B 173 ? 0.4528 0.4384 0.4434 0.0235  0.0712  0.0193  216 PHE B CD1 
3484 C CD2 . PHE B 173 ? 0.5137 0.4851 0.4889 0.0248  0.0804  0.0229  216 PHE B CD2 
3485 C CE1 . PHE B 173 ? 0.4593 0.4408 0.4390 0.0225  0.0657  0.0157  216 PHE B CE1 
3486 C CE2 . PHE B 173 ? 0.4961 0.4631 0.4601 0.0236  0.0738  0.0193  216 PHE B CE2 
3487 C CZ  . PHE B 173 ? 0.4515 0.4243 0.4188 0.0226  0.0667  0.0158  216 PHE B CZ  
3488 N N   . ASP B 174 ? 0.5324 0.5045 0.5067 0.0315  0.0879  0.0214  217 ASP B N   
3489 C CA  . ASP B 174 ? 0.6050 0.5647 0.5593 0.0328  0.0892  0.0189  217 ASP B CA  
3490 C C   . ASP B 174 ? 0.5745 0.5330 0.5210 0.0297  0.0799  0.0148  217 ASP B C   
3491 O O   . ASP B 174 ? 0.5312 0.4969 0.4840 0.0283  0.0737  0.0126  217 ASP B O   
3492 C CB  . ASP B 174 ? 0.6161 0.5740 0.5689 0.0357  0.0926  0.0184  217 ASP B CB  
3493 C CG  . ASP B 174 ? 0.6731 0.6157 0.6038 0.0369  0.0947  0.0161  217 ASP B CG  
3494 O OD1 . ASP B 174 ? 0.7025 0.6359 0.6192 0.0356  0.0936  0.0153  217 ASP B OD1 
3495 O OD2 . ASP B 174 ? 0.7135 0.6523 0.6401 0.0391  0.0970  0.0153  217 ASP B OD2 
3496 N N   . LYS B 175 ? 0.5465 0.4959 0.4794 0.0288  0.0790  0.0143  218 LYS B N   
3497 C CA  . LYS B 175 ? 0.5806 0.5288 0.5065 0.0262  0.0704  0.0112  218 LYS B CA  
3498 C C   . LYS B 175 ? 0.5990 0.5447 0.5181 0.0260  0.0674  0.0084  218 LYS B C   
3499 O O   . LYS B 175 ? 0.5964 0.5464 0.5171 0.0239  0.0602  0.0061  218 LYS B O   
3500 C CB  . LYS B 175 ? 0.6237 0.5609 0.5347 0.0256  0.0700  0.0117  218 LYS B CB  
3501 C CG  . LYS B 175 ? 0.6173 0.5556 0.5335 0.0255  0.0727  0.0147  218 LYS B CG  
3502 C CD  . LYS B 175 ? 0.6795 0.6068 0.5803 0.0246  0.0706  0.0151  218 LYS B CD  
3503 C CE  . LYS B 175 ? 0.7200 0.6317 0.6014 0.0264  0.0768  0.0160  218 LYS B CE  
3504 N NZ  . LYS B 175 ? 0.7352 0.6450 0.6197 0.0290  0.0877  0.0195  218 LYS B NZ  
3505 N N   . ASP B 176 ? 0.6395 0.5778 0.5511 0.0284  0.0733  0.0087  219 ASP B N   
3506 C CA  . ASP B 176 ? 0.7143 0.6477 0.6172 0.0280  0.0709  0.0062  219 ASP B CA  
3507 C C   . ASP B 176 ? 0.6706 0.6146 0.5875 0.0287  0.0703  0.0058  219 ASP B C   
3508 O O   . ASP B 176 ? 0.6942 0.6349 0.6094 0.0311  0.0747  0.0060  219 ASP B O   
3509 C CB  . ASP B 176 ? 0.8163 0.7338 0.7015 0.0304  0.0776  0.0066  219 ASP B CB  
3510 C CG  . ASP B 176 ? 0.8995 0.8082 0.7714 0.0291  0.0737  0.0038  219 ASP B CG  
3511 O OD1 . ASP B 176 ? 0.8428 0.7574 0.7182 0.0258  0.0654  0.0018  219 ASP B OD1 
3512 O OD2 . ASP B 176 ? 0.9596 0.8550 0.8174 0.0313  0.0794  0.0037  219 ASP B OD2 
3513 N N   . SER B 177 ? 0.5781 0.5340 0.5081 0.0268  0.0647  0.0051  220 SER B N   
3514 C CA  . SER B 177 ? 0.5318 0.4972 0.4740 0.0270  0.0630  0.0048  220 SER B CA  
3515 C C   . SER B 177 ? 0.5029 0.4755 0.4501 0.0241  0.0553  0.0026  220 SER B C   
3516 O O   . SER B 177 ? 0.5073 0.4794 0.4518 0.0225  0.0519  0.0021  220 SER B O   
3517 C CB  . SER B 177 ? 0.5150 0.4879 0.4719 0.0287  0.0671  0.0078  220 SER B CB  
3518 O OG  . SER B 177 ? 0.4680 0.4469 0.4331 0.0270  0.0644  0.0086  220 SER B OG  
3519 N N   . THR B 178 ? 0.4470 0.4259 0.4012 0.0239  0.0529  0.0017  221 THR B N   
3520 C CA  . THR B 178 ? 0.4628 0.4481 0.4217 0.0218  0.0469  -0.0001 221 THR B CA  
3521 C C   . THR B 178 ? 0.4209 0.4115 0.3880 0.0212  0.0455  0.0007  221 THR B C   
3522 O O   . THR B 178 ? 0.4040 0.3961 0.3707 0.0199  0.0417  -0.0006 221 THR B O   
3523 C CB  . THR B 178 ? 0.4321 0.4219 0.3960 0.0219  0.0454  -0.0008 221 THR B CB  
3524 O OG1 . THR B 178 ? 0.4803 0.4642 0.4372 0.0230  0.0480  -0.0009 221 THR B OG1 
3525 C CG2 . THR B 178 ? 0.3911 0.3846 0.3554 0.0200  0.0404  -0.0029 221 THR B CG2 
3526 N N   . PHE B 179 ? 0.3829 0.3760 0.3579 0.0222  0.0484  0.0029  222 PHE B N   
3527 C CA  . PHE B 179 ? 0.3902 0.3871 0.3725 0.0211  0.0469  0.0039  222 PHE B CA  
3528 C C   . PHE B 179 ? 0.3949 0.3867 0.3708 0.0208  0.0478  0.0043  222 PHE B C   
3529 O O   . PHE B 179 ? 0.3719 0.3646 0.3483 0.0197  0.0442  0.0034  222 PHE B O   
3530 C CB  . PHE B 179 ? 0.3616 0.3626 0.3550 0.0217  0.0496  0.0070  222 PHE B CB  
3531 C CG  . PHE B 179 ? 0.3797 0.3829 0.3801 0.0201  0.0485  0.0085  222 PHE B CG  
3532 C CD1 . PHE B 179 ? 0.3248 0.3310 0.3290 0.0181  0.0429  0.0070  222 PHE B CD1 
3533 C CD2 . PHE B 179 ? 0.3480 0.3490 0.3499 0.0206  0.0535  0.0116  222 PHE B CD2 
3534 C CE1 . PHE B 179 ? 0.3719 0.3786 0.3815 0.0164  0.0415  0.0083  222 PHE B CE1 
3535 C CE2 . PHE B 179 ? 0.4103 0.4129 0.4187 0.0188  0.0524  0.0132  222 PHE B CE2 
3536 C CZ  . PHE B 179 ? 0.4093 0.4146 0.4215 0.0165  0.0461  0.0115  222 PHE B CZ  
3537 N N   . GLY B 180 ? 0.4056 0.3908 0.3742 0.0221  0.0527  0.0058  223 GLY B N   
3538 C CA  . GLY B 180 ? 0.4394 0.4186 0.4012 0.0219  0.0540  0.0068  223 GLY B CA  
3539 C C   . GLY B 180 ? 0.4374 0.4124 0.3893 0.0209  0.0494  0.0049  223 GLY B C   
3540 O O   . GLY B 180 ? 0.4698 0.4417 0.4184 0.0204  0.0482  0.0056  223 GLY B O   
3541 N N   . SER B 181 ? 0.4286 0.4035 0.3764 0.0204  0.0465  0.0028  224 SER B N   
3542 C CA  . SER B 181 ? 0.4552 0.4268 0.3952 0.0190  0.0418  0.0016  224 SER B CA  
3543 C C   . SER B 181 ? 0.4447 0.4239 0.3914 0.0180  0.0367  -0.0001 224 SER B C   
3544 O O   . SER B 181 ? 0.4473 0.4257 0.3906 0.0169  0.0325  -0.0005 224 SER B O   
3545 C CB  . SER B 181 ? 0.5360 0.4986 0.4631 0.0188  0.0427  0.0012  224 SER B CB  
3546 O OG  . SER B 181 ? 0.5404 0.4931 0.4572 0.0198  0.0470  0.0028  224 SER B OG  
3547 N N   . VAL B 182 ? 0.4146 0.4007 0.3705 0.0184  0.0369  -0.0009 225 VAL B N   
3548 C CA  . VAL B 182 ? 0.3876 0.3796 0.3485 0.0178  0.0332  -0.0024 225 VAL B CA  
3549 C C   . VAL B 182 ? 0.4042 0.4007 0.3734 0.0183  0.0328  -0.0027 225 VAL B C   
3550 O O   . VAL B 182 ? 0.3817 0.3798 0.3529 0.0184  0.0305  -0.0031 225 VAL B O   
3551 C CB  . VAL B 182 ? 0.4083 0.4019 0.3688 0.0174  0.0332  -0.0036 225 VAL B CB  
3552 C CG1 . VAL B 182 ? 0.3725 0.3718 0.3378 0.0169  0.0303  -0.0048 225 VAL B CG1 
3553 C CG2 . VAL B 182 ? 0.4315 0.4188 0.3826 0.0164  0.0330  -0.0035 225 VAL B CG2 
3554 N N   . GLU B 183 ? 0.3924 0.3904 0.3662 0.0185  0.0348  -0.0022 226 GLU B N   
3555 C CA  . GLU B 183 ? 0.3474 0.3488 0.3279 0.0182  0.0331  -0.0027 226 GLU B CA  
3556 C C   . GLU B 183 ? 0.3627 0.3625 0.3450 0.0180  0.0326  -0.0018 226 GLU B C   
3557 O O   . GLU B 183 ? 0.3403 0.3404 0.3239 0.0180  0.0302  -0.0030 226 GLU B O   
3558 C CB  . GLU B 183 ? 0.3597 0.3633 0.3455 0.0181  0.0342  -0.0017 226 GLU B CB  
3559 C CG  . GLU B 183 ? 0.3987 0.4033 0.3826 0.0185  0.0345  -0.0025 226 GLU B CG  
3560 C CD  . GLU B 183 ? 0.3662 0.3729 0.3560 0.0189  0.0359  -0.0007 226 GLU B CD  
3561 O OE1 . GLU B 183 ? 0.3826 0.3905 0.3787 0.0187  0.0371  0.0015  226 GLU B OE1 
3562 O OE2 . GLU B 183 ? 0.3898 0.3971 0.3787 0.0194  0.0358  -0.0011 226 GLU B OE2 
3563 N N   . VAL B 184 ? 0.3471 0.3441 0.3286 0.0180  0.0353  0.0003  227 VAL B N   
3564 C CA  A VAL B 184 ? 0.3619 0.3568 0.3453 0.0175  0.0352  0.0016  227 VAL B CA  
3565 C CA  B VAL B 184 ? 0.3626 0.3575 0.3461 0.0175  0.0352  0.0016  227 VAL B CA  
3566 C C   . VAL B 184 ? 0.3770 0.3696 0.3561 0.0182  0.0327  0.0006  227 VAL B C   
3567 O O   . VAL B 184 ? 0.3677 0.3589 0.3487 0.0181  0.0313  0.0007  227 VAL B O   
3568 C CB  A VAL B 184 ? 0.3701 0.3618 0.3526 0.0176  0.0397  0.0045  227 VAL B CB  
3569 C CB  B VAL B 184 ? 0.3854 0.3774 0.3684 0.0175  0.0396  0.0045  227 VAL B CB  
3570 C CG1 A VAL B 184 ? 0.3666 0.3618 0.3564 0.0174  0.0425  0.0062  227 VAL B CG1 
3571 C CG1 B VAL B 184 ? 0.3855 0.3721 0.3582 0.0185  0.0413  0.0048  227 VAL B CG1 
3572 C CG2 A VAL B 184 ? 0.3855 0.3722 0.3579 0.0186  0.0414  0.0047  227 VAL B CG2 
3573 C CG2 B VAL B 184 ? 0.3868 0.3774 0.3739 0.0165  0.0396  0.0063  227 VAL B CG2 
3574 N N   . HIS B 185 ? 0.3728 0.3647 0.3464 0.0188  0.0320  0.0001  228 HIS B N   
3575 C CA  . HIS B 185 ? 0.3906 0.3813 0.3617 0.0196  0.0293  0.0001  228 HIS B CA  
3576 C C   . HIS B 185 ? 0.3815 0.3763 0.3564 0.0204  0.0270  -0.0017 228 HIS B C   
3577 O O   . HIS B 185 ? 0.3938 0.3888 0.3687 0.0216  0.0251  -0.0014 228 HIS B O   
3578 C CB  . HIS B 185 ? 0.3879 0.3756 0.3517 0.0193  0.0286  0.0009  228 HIS B CB  
3579 C CG  . HIS B 185 ? 0.4067 0.3884 0.3642 0.0189  0.0319  0.0026  228 HIS B CG  
3580 N ND1 . HIS B 185 ? 0.3980 0.3747 0.3527 0.0191  0.0333  0.0046  228 HIS B ND1 
3581 C CD2 . HIS B 185 ? 0.4221 0.4010 0.3747 0.0186  0.0347  0.0027  228 HIS B CD2 
3582 C CE1 . HIS B 185 ? 0.4431 0.4144 0.3915 0.0190  0.0373  0.0059  228 HIS B CE1 
3583 N NE2 . HIS B 185 ? 0.4601 0.4324 0.4069 0.0189  0.0384  0.0047  228 HIS B NE2 
3584 N N   . ASN B 186 ? 0.3762 0.3740 0.3540 0.0202  0.0274  -0.0034 229 ASN B N   
3585 C CA  . ASN B 186 ? 0.3669 0.3674 0.3466 0.0212  0.0263  -0.0050 229 ASN B CA  
3586 C C   . ASN B 186 ? 0.3490 0.3481 0.3304 0.0213  0.0261  -0.0065 229 ASN B C   
3587 O O   . ASN B 186 ? 0.3320 0.3316 0.3131 0.0224  0.0259  -0.0081 229 ASN B O   
3588 C CB  . ASN B 186 ? 0.3458 0.3497 0.3248 0.0207  0.0265  -0.0057 229 ASN B CB  
3589 C CG  . ASN B 186 ? 0.3976 0.4023 0.3748 0.0204  0.0253  -0.0045 229 ASN B CG  
3590 O OD1 . ASN B 186 ? 0.3569 0.3640 0.3366 0.0214  0.0239  -0.0040 229 ASN B OD1 
3591 N ND2 . ASN B 186 ? 0.3860 0.3882 0.3588 0.0191  0.0257  -0.0037 229 ASN B ND2 
3592 N N   . LEU B 187 ? 0.3633 0.3600 0.3460 0.0199  0.0261  -0.0057 230 LEU B N   
3593 C CA  . LEU B 187 ? 0.3589 0.3522 0.3422 0.0195  0.0246  -0.0068 230 LEU B CA  
3594 C C   . LEU B 187 ? 0.3713 0.3608 0.3527 0.0214  0.0243  -0.0072 230 LEU B C   
3595 O O   . LEU B 187 ? 0.3333 0.3218 0.3148 0.0220  0.0246  -0.0055 230 LEU B O   
3596 C CB  . LEU B 187 ? 0.3667 0.3588 0.3536 0.0171  0.0244  -0.0050 230 LEU B CB  
3597 C CG  . LEU B 187 ? 0.3420 0.3381 0.3326 0.0158  0.0253  -0.0038 230 LEU B CG  
3598 C CD1 . LEU B 187 ? 0.3653 0.3611 0.3614 0.0139  0.0262  -0.0010 230 LEU B CD1 
3599 C CD2 . LEU B 187 ? 0.3441 0.3414 0.3348 0.0152  0.0231  -0.0054 230 LEU B CD2 
3600 N N   . GLN B 188 ? 0.3574 0.3440 0.3365 0.0227  0.0237  -0.0093 231 GLN B N   
3601 C CA  . GLN B 188 ? 0.4117 0.3944 0.3890 0.0255  0.0242  -0.0097 231 GLN B CA  
3602 C C   . GLN B 188 ? 0.4358 0.4110 0.4115 0.0244  0.0228  -0.0096 231 GLN B C   
3603 O O   . GLN B 188 ? 0.4177 0.3883 0.3911 0.0226  0.0211  -0.0110 231 GLN B O   
3604 C CB  . GLN B 188 ? 0.3960 0.3773 0.3702 0.0280  0.0255  -0.0118 231 GLN B CB  
3605 C CG  . GLN B 188 ? 0.4496 0.4383 0.4262 0.0289  0.0271  -0.0115 231 GLN B CG  
3606 C CD  . GLN B 188 ? 0.5005 0.4882 0.4752 0.0322  0.0298  -0.0127 231 GLN B CD  
3607 O OE1 . GLN B 188 ? 0.5313 0.5170 0.5067 0.0355  0.0314  -0.0123 231 GLN B OE1 
3608 N NE2 . GLN B 188 ? 0.4460 0.4347 0.4181 0.0316  0.0308  -0.0139 231 GLN B NE2 
3609 N N   . PRO B 189 ? 0.4448 0.4181 0.4214 0.0251  0.0229  -0.0077 232 PRO B N   
3610 C CA  . PRO B 189 ? 0.4634 0.4289 0.4385 0.0237  0.0216  -0.0074 232 PRO B CA  
3611 C C   . PRO B 189 ? 0.4935 0.4505 0.4632 0.0251  0.0209  -0.0100 232 PRO B C   
3612 O O   . PRO B 189 ? 0.5167 0.4664 0.4841 0.0226  0.0187  -0.0104 232 PRO B O   
3613 C CB  . PRO B 189 ? 0.4874 0.4522 0.4633 0.0252  0.0222  -0.0049 232 PRO B CB  
3614 C CG  . PRO B 189 ? 0.4505 0.4229 0.4284 0.0256  0.0232  -0.0035 232 PRO B CG  
3615 C CD  . PRO B 189 ? 0.4497 0.4270 0.4282 0.0267  0.0237  -0.0056 232 PRO B CD  
3616 N N   . GLU B 190 ? 0.5036 0.4607 0.4709 0.0291  0.0229  -0.0115 233 GLU B N   
3617 C CA  . GLU B 190 ? 0.6277 0.5749 0.5877 0.0312  0.0233  -0.0141 233 GLU B CA  
3618 C C   . GLU B 190 ? 0.5932 0.5361 0.5481 0.0280  0.0210  -0.0164 233 GLU B C   
3619 O O   . GLU B 190 ? 0.6596 0.5910 0.6063 0.0280  0.0198  -0.0186 233 GLU B O   
3620 C CB  . GLU B 190 ? 0.6780 0.6274 0.6378 0.0366  0.0272  -0.0146 233 GLU B CB  
3621 C CG  . GLU B 190 ? 0.7870 0.7387 0.7516 0.0403  0.0287  -0.0121 233 GLU B CG  
3622 C CD  . GLU B 190 ? 0.8223 0.7849 0.7945 0.0389  0.0276  -0.0092 233 GLU B CD  
3623 O OE1 . GLU B 190 ? 0.6462 0.6155 0.6203 0.0364  0.0271  -0.0094 233 GLU B OE1 
3624 O OE2 . GLU B 190 ? 0.8606 0.8239 0.8358 0.0405  0.0270  -0.0067 233 GLU B OE2 
3625 N N   . LYS B 191 ? 0.5122 0.4629 0.4708 0.0254  0.0200  -0.0160 234 LYS B N   
3626 C CA  . LYS B 191 ? 0.4928 0.4404 0.4472 0.0225  0.0172  -0.0176 234 LYS B CA  
3627 C C   . LYS B 191 ? 0.4667 0.4168 0.4267 0.0173  0.0133  -0.0158 234 LYS B C   
3628 O O   . LYS B 191 ? 0.4308 0.3750 0.3872 0.0141  0.0091  -0.0168 234 LYS B O   
3629 C CB  . LYS B 191 ? 0.4973 0.4517 0.4518 0.0238  0.0193  -0.0183 234 LYS B CB  
3630 C CG  . LYS B 191 ? 0.5548 0.5092 0.5066 0.0289  0.0240  -0.0192 234 LYS B CG  
3631 C CD  . LYS B 191 ? 0.4870 0.4506 0.4420 0.0296  0.0262  -0.0187 234 LYS B CD  
3632 C CE  . LYS B 191 ? 0.4895 0.4503 0.4387 0.0275  0.0245  -0.0203 234 LYS B CE  
3633 N NZ  . LYS B 191 ? 0.4982 0.4664 0.4493 0.0286  0.0273  -0.0198 234 LYS B NZ  
3634 N N   . VAL B 192 ? 0.4611 0.4194 0.4296 0.0164  0.0144  -0.0130 235 VAL B N   
3635 C CA  . VAL B 192 ? 0.4510 0.4134 0.4269 0.0122  0.0122  -0.0105 235 VAL B CA  
3636 C C   . VAL B 192 ? 0.4385 0.3965 0.4168 0.0104  0.0115  -0.0086 235 VAL B C   
3637 O O   . VAL B 192 ? 0.4478 0.4057 0.4261 0.0126  0.0142  -0.0076 235 VAL B O   
3638 C CB  . VAL B 192 ? 0.3682 0.3410 0.3505 0.0128  0.0151  -0.0085 235 VAL B CB  
3639 C CG1 . VAL B 192 ? 0.3840 0.3611 0.3747 0.0093  0.0142  -0.0054 235 VAL B CG1 
3640 C CG2 . VAL B 192 ? 0.4043 0.3808 0.3839 0.0144  0.0159  -0.0102 235 VAL B CG2 
3641 N N   . GLN B 193 ? 0.4132 0.3674 0.3937 0.0060  0.0074  -0.0077 236 GLN B N   
3642 C CA  . GLN B 193 ? 0.4956 0.4460 0.4798 0.0033  0.0065  -0.0053 236 GLN B CA  
3643 C C   . GLN B 193 ? 0.4795 0.4389 0.4752 0.0009  0.0083  -0.0009 236 GLN B C   
3644 O O   . GLN B 193 ? 0.4913 0.4502 0.4897 0.0006  0.0108  0.0016  236 GLN B O   
3645 C CB  . GLN B 193 ? 0.5533 0.4936 0.5339 -0.0008 0.0006  -0.0062 236 GLN B CB  
3646 C CG  . GLN B 193 ? 0.7022 0.6294 0.6717 0.0011  0.0002  -0.0090 236 GLN B CG  
3647 C CD  . GLN B 193 ? 0.7061 0.6296 0.6654 0.0061  0.0023  -0.0129 236 GLN B CD  
3648 O OE1 . GLN B 193 ? 0.6926 0.6168 0.6485 0.0060  0.0008  -0.0147 236 GLN B OE1 
3649 N NE2 . GLN B 193 ? 0.6164 0.5361 0.5712 0.0108  0.0061  -0.0138 236 GLN B NE2 
3650 N N   . THR B 194 ? 0.4221 0.3891 0.4242 -0.0005 0.0076  0.0002  237 THR B N   
3651 C CA  . THR B 194 ? 0.4305 0.4055 0.4444 -0.0026 0.0096  0.0046  237 THR B CA  
3652 C C   . THR B 194 ? 0.4236 0.4073 0.4409 -0.0006 0.0121  0.0050  237 THR B C   
3653 O O   . THR B 194 ? 0.3878 0.3720 0.4018 0.0000  0.0095  0.0026  237 THR B O   
3654 C CB  . THR B 194 ? 0.4156 0.3898 0.4379 -0.0081 0.0045  0.0072  237 THR B CB  
3655 O OG1 . THR B 194 ? 0.5047 0.4689 0.5223 -0.0103 0.0016  0.0066  237 THR B OG1 
3656 C CG2 . THR B 194 ? 0.4399 0.4230 0.4764 -0.0098 0.0079  0.0127  237 THR B CG2 
3657 N N   . LEU B 195 ? 0.3804 0.3698 0.4033 0.0005  0.0175  0.0081  238 LEU B N   
3658 C CA  . LEU B 195 ? 0.3927 0.3897 0.4202 0.0021  0.0205  0.0094  238 LEU B CA  
3659 C C   . LEU B 195 ? 0.4220 0.4247 0.4634 -0.0005 0.0215  0.0144  238 LEU B C   
3660 O O   . LEU B 195 ? 0.4470 0.4498 0.4925 -0.0010 0.0258  0.0177  238 LEU B O   
3661 C CB  . LEU B 195 ? 0.4002 0.3976 0.4216 0.0058  0.0263  0.0090  238 LEU B CB  
3662 C CG  . LEU B 195 ? 0.3690 0.3721 0.3936 0.0076  0.0304  0.0105  238 LEU B CG  
3663 C CD1 . LEU B 195 ? 0.3734 0.3788 0.3956 0.0085  0.0276  0.0078  238 LEU B CD1 
3664 C CD2 . LEU B 195 ? 0.4186 0.4194 0.4359 0.0104  0.0359  0.0108  238 LEU B CD2 
3665 N N   . GLU B 196 ? 0.4124 0.4197 0.4613 -0.0022 0.0177  0.0155  239 GLU B N   
3666 C CA  . GLU B 196 ? 0.4576 0.4717 0.5224 -0.0048 0.0178  0.0209  239 GLU B CA  
3667 C C   . GLU B 196 ? 0.4271 0.4487 0.4978 -0.0015 0.0232  0.0232  239 GLU B C   
3668 O O   . GLU B 196 ? 0.4021 0.4253 0.4699 0.0000  0.0211  0.0211  239 GLU B O   
3669 C CB  . GLU B 196 ? 0.4665 0.4804 0.5370 -0.0094 0.0087  0.0213  239 GLU B CB  
3670 C CG  . GLU B 196 ? 0.5166 0.5391 0.6064 -0.0126 0.0076  0.0277  239 GLU B CG  
3671 C CD  . GLU B 196 ? 0.5882 0.6085 0.6827 -0.0183 -0.0030 0.0284  239 GLU B CD  
3672 O OE1 . GLU B 196 ? 0.6343 0.6450 0.7193 -0.0210 -0.0077 0.0255  239 GLU B OE1 
3673 O OE2 . GLU B 196 ? 0.6274 0.6549 0.7344 -0.0200 -0.0070 0.0321  239 GLU B OE2 
3674 N N   . ALA B 197 ? 0.4324 0.4575 0.5104 -0.0003 0.0306  0.0274  240 ALA B N   
3675 C CA  . ALA B 197 ? 0.3957 0.4261 0.4783 0.0034  0.0372  0.0298  240 ALA B CA  
3676 C C   . ALA B 197 ? 0.4366 0.4763 0.5388 0.0018  0.0364  0.0356  240 ALA B C   
3677 O O   . ALA B 197 ? 0.4404 0.4829 0.5546 -0.0018 0.0353  0.0398  240 ALA B O   
3678 C CB  . ALA B 197 ? 0.4225 0.4497 0.4997 0.0064  0.0466  0.0312  240 ALA B CB  
3679 N N   . TRP B 198 ? 0.4072 0.4516 0.5133 0.0043  0.0366  0.0362  241 TRP B N   
3680 C CA  . TRP B 198 ? 0.4517 0.5059 0.5776 0.0038  0.0364  0.0423  241 TRP B CA  
3681 C C   . TRP B 198 ? 0.4642 0.5211 0.5932 0.0093  0.0475  0.0454  241 TRP B C   
3682 O O   . TRP B 198 ? 0.4455 0.5007 0.5666 0.0132  0.0496  0.0430  241 TRP B O   
3683 C CB  . TRP B 198 ? 0.4832 0.5399 0.6111 0.0025  0.0273  0.0411  241 TRP B CB  
3684 C CG  . TRP B 198 ? 0.4746 0.5272 0.5991 -0.0029 0.0163  0.0386  241 TRP B CG  
3685 C CD1 . TRP B 198 ? 0.5050 0.5537 0.6290 -0.0071 0.0136  0.0385  241 TRP B CD1 
3686 C CD2 . TRP B 198 ? 0.4650 0.5153 0.5840 -0.0046 0.0069  0.0358  241 TRP B CD2 
3687 N NE1 . TRP B 198 ? 0.5362 0.5796 0.6544 -0.0112 0.0031  0.0355  241 TRP B NE1 
3688 C CE2 . TRP B 198 ? 0.4900 0.5341 0.6046 -0.0098 -0.0011 0.0338  241 TRP B CE2 
3689 C CE3 . TRP B 198 ? 0.5292 0.5808 0.6456 -0.0023 0.0047  0.0347  241 TRP B CE3 
3690 C CZ2 . TRP B 198 ? 0.5442 0.5827 0.6507 -0.0125 -0.0110 0.0308  241 TRP B CZ2 
3691 C CZ3 . TRP B 198 ? 0.5609 0.6078 0.6700 -0.0051 -0.0052 0.0320  241 TRP B CZ3 
3692 C CH2 . TRP B 198 ? 0.5646 0.6046 0.6682 -0.0101 -0.0128 0.0300  241 TRP B CH2 
3693 N N   . VAL B 199 ? 0.4608 0.5211 0.6007 0.0097  0.0550  0.0508  242 VAL B N   
3694 C CA  . VAL B 199 ? 0.4748 0.5358 0.6164 0.0153  0.0670  0.0540  242 VAL B CA  
3695 C C   . VAL B 199 ? 0.5188 0.5906 0.6806 0.0170  0.0675  0.0597  242 VAL B C   
3696 O O   . VAL B 199 ? 0.5355 0.6166 0.7182 0.0141  0.0658  0.0659  242 VAL B O   
3697 C CB  . VAL B 199 ? 0.4811 0.5400 0.6247 0.0153  0.0758  0.0577  242 VAL B CB  
3698 C CG1 . VAL B 199 ? 0.5144 0.5717 0.6568 0.0216  0.0891  0.0607  242 VAL B CG1 
3699 C CG2 . VAL B 199 ? 0.5296 0.5778 0.6538 0.0135  0.0740  0.0524  242 VAL B CG2 
3700 N N   . ILE B 200 ? 0.4871 0.5577 0.6431 0.0216  0.0695  0.0580  243 ILE B N   
3701 C CA  . ILE B 200 ? 0.5127 0.5928 0.6865 0.0241  0.0697  0.0631  243 ILE B CA  
3702 C C   . ILE B 200 ? 0.5485 0.6309 0.7312 0.0297  0.0837  0.0689  243 ILE B C   
3703 O O   . ILE B 200 ? 0.5305 0.6035 0.6968 0.0344  0.0929  0.0663  243 ILE B O   
3704 C CB  . ILE B 200 ? 0.4976 0.5743 0.6604 0.0265  0.0653  0.0586  243 ILE B CB  
3705 C CG1 . ILE B 200 ? 0.4875 0.5596 0.6378 0.0215  0.0533  0.0523  243 ILE B CG1 
3706 C CG2 . ILE B 200 ? 0.5086 0.5953 0.6907 0.0287  0.0638  0.0643  243 ILE B CG2 
3707 C CD1 . ILE B 200 ? 0.4594 0.5377 0.6232 0.0153  0.0429  0.0548  243 ILE B CD1 
3708 N N   . HIS B 201 ? 0.6235 0.7179 0.8319 0.0292  0.0854  0.0771  244 HIS B N   
3709 C CA  . HIS B 201 ? 0.6848 0.7823 0.9041 0.0348  0.0998  0.0836  244 HIS B CA  
3710 C C   . HIS B 201 ? 0.7491 0.8482 0.9717 0.0417  0.1047  0.0853  244 HIS B C   
3711 O O   . HIS B 201 ? 0.7061 0.8086 0.9314 0.0412  0.0956  0.0839  244 HIS B O   
3712 C CB  . HIS B 201 ? 0.7361 0.8468 0.9840 0.0316  0.1003  0.0925  244 HIS B CB  
3713 C CG  . HIS B 201 ? 0.7245 0.8317 0.9688 0.0266  0.1009  0.0923  244 HIS B CG  
3714 N ND1 . HIS B 201 ? 0.8212 0.9355 1.0842 0.0258  0.1088  0.1002  244 HIS B ND1 
3715 C CD2 . HIS B 201 ? 0.6935 0.7908 0.9179 0.0223  0.0949  0.0854  244 HIS B CD2 
3716 C CE1 . HIS B 201 ? 0.8346 0.9426 1.0882 0.0211  0.1073  0.0980  244 HIS B CE1 
3717 N NE2 . HIS B 201 ? 0.7185 0.8163 0.9489 0.0190  0.0988  0.0891  244 HIS B NE2 
3718 N N   . GLY B 202 ? 0.9017 0.9970 1.1227 0.0485  0.1197  0.0883  245 GLY B N   
3719 C CA  . GLY B 202 ? 1.0309 1.1256 1.2537 0.0560  0.1266  0.0902  245 GLY B CA  
3720 C C   . GLY B 202 ? 1.2439 1.3525 1.4972 0.0599  0.1340  0.1007  245 GLY B C   
3721 O O   . GLY B 202 ? 1.1967 1.3200 1.4754 0.0555  0.1260  0.1064  245 GLY B O   
3722 N N   . GLY B 203 ? 1.3808 1.4841 1.6313 0.0682  0.1495  0.1035  246 GLY B N   
3723 C CA  . GLY B 203 ? 1.4588 1.5739 1.7370 0.0739  0.1595  0.1137  246 GLY B CA  
3724 C C   . GLY B 203 ? 1.5243 1.6464 1.8198 0.0731  0.1691  0.1212  246 GLY B C   
3725 O O   . GLY B 203 ? 1.5703 1.6833 1.8563 0.0789  0.1852  0.1226  246 GLY B O   
3726 N N   . ARG B 204 ? 1.4124 1.5494 1.7319 0.0657  0.1594  0.1260  247 ARG B N   
3727 C CA  . ARG B 204 ? 1.4726 1.6188 1.8135 0.0642  0.1677  0.1345  247 ARG B CA  
3728 C C   . ARG B 204 ? 1.5713 1.7047 1.8908 0.0618  0.1740  0.1306  247 ARG B C   
3729 O O   . ARG B 204 ? 1.5409 1.6653 1.8506 0.0679  0.1907  0.1323  247 ARG B O   
3730 C CB  . ARG B 204 ? 1.4625 1.6155 1.8235 0.0736  0.1848  0.1440  247 ARG B CB  
3731 C CG  . ARG B 204 ? 1.4517 1.6178 1.8418 0.0725  0.1939  0.1550  247 ARG B CG  
3732 C CD  . ARG B 204 ? 1.4926 1.6700 1.8992 0.0610  0.1790  0.1569  247 ARG B CD  
3733 N NE  . ARG B 204 ? 1.4562 1.6448 1.8776 0.0558  0.1601  0.1569  247 ARG B NE  
3734 C CZ  . ARG B 204 ? 1.4031 1.5933 1.8228 0.0457  0.1427  0.1531  247 ARG B CZ  
3735 N NH1 . ARG B 204 ? 1.4650 1.6471 1.8704 0.0397  0.1412  0.1491  247 ARG B NH1 
3736 N NH2 . ARG B 204 ? 1.2814 1.4800 1.7126 0.0418  0.1264  0.1532  247 ARG B NH2 
3737 N N   . GLU B 205 ? 1.7946 1.9258 2.1052 0.0530  0.1606  0.1253  248 GLU B N   
3738 C CA  . GLU B 205 ? 1.8247 1.9435 2.1138 0.0496  0.1631  0.1207  248 GLU B CA  
3739 C C   . GLU B 205 ? 1.8696 1.9967 2.1787 0.0452  0.1675  0.1285  248 GLU B C   
3740 O O   . GLU B 205 ? 1.7868 1.9060 2.0821 0.0402  0.1652  0.1251  248 GLU B O   
3741 C CB  . GLU B 205 ? 1.6467 1.7588 1.9165 0.0429  0.1465  0.1111  248 GLU B CB  
3742 C CG  . GLU B 205 ? 1.5093 1.6064 1.7523 0.0403  0.1475  0.1047  248 GLU B CG  
3743 C CD  . GLU B 205 ? 1.5870 1.6684 1.8054 0.0475  0.1617  0.1020  248 GLU B CD  
3744 O OE1 . GLU B 205 ? 1.7041 1.7827 1.9181 0.0541  0.1675  0.1015  248 GLU B OE1 
3745 O OE2 . GLU B 205 ? 1.5075 1.5785 1.7101 0.0464  0.1669  0.1004  248 GLU B OE2 
3746 N N   . ASP B 206 ? 1.9049 2.0478 2.2468 0.0471  0.1740  0.1393  249 ASP B N   
3747 C CA  . ASP B 206 ? 1.9126 2.0648 2.2769 0.0427  0.1787  0.1480  249 ASP B CA  
3748 C C   . ASP B 206 ? 1.8600 2.0139 2.2253 0.0316  0.1624  0.1453  249 ASP B C   
3749 O O   . ASP B 206 ? 1.8885 2.0429 2.2597 0.0270  0.1655  0.1491  249 ASP B O   
3750 C CB  . ASP B 206 ? 1.9789 2.1190 2.3281 0.0478  0.1978  0.1495  249 ASP B CB  
3751 C CG  . ASP B 206 ? 1.9497 2.0718 2.2655 0.0440  0.1946  0.1406  249 ASP B CG  
3752 O OD1 . ASP B 206 ? 1.9646 2.0887 2.2857 0.0366  0.1896  0.1422  249 ASP B OD1 
3753 O OD2 . ASP B 206 ? 1.8433 1.9491 2.1277 0.0484  0.1970  0.1323  249 ASP B OD2 
3754 N N   . SER B 207 ? 1.6068 1.7610 1.9663 0.0272  0.1451  0.1389  250 SER B N   
3755 C CA  . SER B 207 ? 1.3993 1.5523 1.7558 0.0172  0.1292  0.1352  250 SER B CA  
3756 C C   . SER B 207 ? 1.2939 1.4319 1.6257 0.0152  0.1336  0.1302  250 SER B C   
3757 O O   . SER B 207 ? 1.1898 1.3284 1.5266 0.0078  0.1277  0.1315  250 SER B O   
3758 C CB  . SER B 207 ? 1.4019 1.5720 1.7939 0.0100  0.1221  0.1448  250 SER B CB  
3759 O OG  . SER B 207 ? 1.3251 1.5075 1.7365 0.0098  0.1123  0.1478  250 SER B OG  
3760 N N   . ARG B 208 ? 1.2980 1.4218 1.6025 0.0219  0.1435  0.1245  251 ARG B N   
3761 C CA  . ARG B 208 ? 1.1168 1.2252 1.3956 0.0207  0.1472  0.1194  251 ARG B CA  
3762 C C   . ARG B 208 ? 0.9218 1.0218 1.1804 0.0156  0.1318  0.1098  251 ARG B C   
3763 O O   . ARG B 208 ? 0.8762 0.9764 1.1288 0.0163  0.1228  0.1045  251 ARG B O   
3764 C CB  . ARG B 208 ? 1.1746 1.2697 1.4305 0.0294  0.1623  0.1170  251 ARG B CB  
3765 C CG  . ARG B 208 ? 1.0443 1.1222 1.2716 0.0287  0.1658  0.1119  251 ARG B CG  
3766 C CD  . ARG B 208 ? 1.0106 1.0743 1.2153 0.0370  0.1807  0.1103  251 ARG B CD  
3767 N NE  . ARG B 208 ? 1.1149 1.1749 1.3079 0.0420  0.1788  0.1048  251 ARG B NE  
3768 C CZ  . ARG B 208 ? 1.0626 1.1077 1.2307 0.0484  0.1877  0.1010  251 ARG B CZ  
3769 N NH1 . ARG B 208 ? 0.9584 0.9896 1.1083 0.0508  0.1990  0.1016  251 ARG B NH1 
3770 N NH2 . ARG B 208 ? 1.0959 1.1385 1.2558 0.0522  0.1849  0.0965  251 ARG B NH2 
3771 N N   . ASP B 209 ? 0.8927 0.9851 1.1410 0.0107  0.1292  0.1078  252 ASP B N   
3772 C CA  . ASP B 209 ? 0.8151 0.8988 1.0443 0.0063  0.1160  0.0991  252 ASP B CA  
3773 C C   . ASP B 209 ? 0.7635 0.8327 0.9620 0.0118  0.1199  0.0912  252 ASP B C   
3774 O O   . ASP B 209 ? 0.7582 0.8163 0.9400 0.0134  0.1275  0.0901  252 ASP B O   
3775 C CB  . ASP B 209 ? 0.7869 0.8669 1.0165 -0.0004 0.1123  0.1003  252 ASP B CB  
3776 C CG  . ASP B 209 ? 0.7719 0.8430 0.9833 -0.0046 0.0990  0.0918  252 ASP B CG  
3777 O OD1 . ASP B 209 ? 0.7777 0.8476 0.9798 -0.0030 0.0917  0.0857  252 ASP B OD1 
3778 O OD2 . ASP B 209 ? 0.8071 0.8720 1.0135 -0.0091 0.0964  0.0915  252 ASP B OD2 
3779 N N   . LEU B 210 ? 0.7215 0.7904 0.9123 0.0143  0.1143  0.0859  253 LEU B N   
3780 C CA  . LEU B 210 ? 0.6906 0.7466 0.8537 0.0188  0.1167  0.0786  253 LEU B CA  
3781 C C   . LEU B 210 ? 0.6433 0.6896 0.7869 0.0151  0.1075  0.0714  253 LEU B C   
3782 O O   . LEU B 210 ? 0.6346 0.6698 0.7555 0.0181  0.1093  0.0660  253 LEU B O   
3783 C CB  . LEU B 210 ? 0.6659 0.7249 0.8285 0.0226  0.1141  0.0759  253 LEU B CB  
3784 C CG  . LEU B 210 ? 0.7535 0.8193 0.9308 0.0283  0.1248  0.0822  253 LEU B CG  
3785 C CD1 . LEU B 210 ? 0.7496 0.8166 0.9239 0.0319  0.1212  0.0789  253 LEU B CD1 
3786 C CD2 . LEU B 210 ? 0.8202 0.8761 0.9853 0.0337  0.1405  0.0842  253 LEU B CD2 
3787 N N   . CYS B 211 ? 0.7208 0.7707 0.8729 0.0088  0.0977  0.0715  254 CYS B N   
3788 C CA  . CYS B 211 ? 0.7451 0.7854 0.8797 0.0058  0.0904  0.0655  254 CYS B CA  
3789 C C   . CYS B 211 ? 0.7374 0.7676 0.8592 0.0066  0.0982  0.0664  254 CYS B C   
3790 O O   . CYS B 211 ? 0.7308 0.7516 0.8353 0.0057  0.0938  0.0613  254 CYS B O   
3791 C CB  . CYS B 211 ? 0.7458 0.7906 0.8920 -0.0010 0.0788  0.0658  254 CYS B CB  
3792 S SG  . CYS B 211 ? 0.7970 0.8491 0.9505 -0.0026 0.0667  0.0628  254 CYS B SG  
3793 N N   . GLN B 212 ? 0.7330 0.7647 0.8628 0.0085  0.1098  0.0729  255 GLN B N   
3794 C CA  . GLN B 212 ? 0.7443 0.7650 0.8598 0.0100  0.1185  0.0741  255 GLN B CA  
3795 C C   . GLN B 212 ? 0.7237 0.7343 0.8189 0.0164  0.1271  0.0716  255 GLN B C   
3796 O O   . GLN B 212 ? 0.7306 0.7299 0.8103 0.0181  0.1343  0.0723  255 GLN B O   
3797 C CB  . GLN B 212 ? 0.7836 0.8097 0.9175 0.0084  0.1274  0.0831  255 GLN B CB  
3798 C CG  . GLN B 212 ? 0.8127 0.8475 0.9667 0.0011  0.1187  0.0863  255 GLN B CG  
3799 C CD  . GLN B 212 ? 0.8458 0.8715 0.9860 -0.0032 0.1094  0.0814  255 GLN B CD  
3800 O OE1 . GLN B 212 ? 0.8158 0.8305 0.9407 -0.0025 0.1140  0.0810  255 GLN B OE1 
3801 N NE2 . GLN B 212 ? 0.8359 0.8651 0.9806 -0.0073 0.0964  0.0777  255 GLN B NE2 
3802 N N   . ASP B 213 ? 0.7078 0.7210 0.8013 0.0199  0.1262  0.0687  256 ASP B N   
3803 C CA  . ASP B 213 ? 0.6854 0.6879 0.7591 0.0257  0.1339  0.0663  256 ASP B CA  
3804 C C   . ASP B 213 ? 0.6750 0.6635 0.7227 0.0252  0.1299  0.0605  256 ASP B C   
3805 O O   . ASP B 213 ? 0.6885 0.6778 0.7340 0.0215  0.1189  0.0564  256 ASP B O   
3806 C CB  . ASP B 213 ? 0.6783 0.6857 0.7544 0.0286  0.1310  0.0634  256 ASP B CB  
3807 C CG  . ASP B 213 ? 0.6919 0.6874 0.7478 0.0344  0.1391  0.0612  256 ASP B CG  
3808 O OD1 . ASP B 213 ? 0.7315 0.7255 0.7906 0.0388  0.1514  0.0659  256 ASP B OD1 
3809 O OD2 . ASP B 213 ? 0.6735 0.6606 0.7103 0.0345  0.1332  0.0548  256 ASP B OD2 
3810 N N   . PRO B 214 ? 0.7275 0.7024 0.7551 0.0290  0.1384  0.0604  257 PRO B N   
3811 C CA  . PRO B 214 ? 0.7153 0.6770 0.7189 0.0282  0.1335  0.0555  257 PRO B CA  
3812 C C   . PRO B 214 ? 0.6492 0.6115 0.6454 0.0273  0.1222  0.0486  257 PRO B C   
3813 O O   . PRO B 214 ? 0.6371 0.5960 0.6252 0.0247  0.1139  0.0453  257 PRO B O   
3814 C CB  . PRO B 214 ? 0.7849 0.7315 0.7681 0.0328  0.1448  0.0567  257 PRO B CB  
3815 C CG  . PRO B 214 ? 0.8078 0.7596 0.8063 0.0352  0.1574  0.0637  257 PRO B CG  
3816 C CD  . PRO B 214 ? 0.7615 0.7314 0.7867 0.0340  0.1530  0.0650  257 PRO B CD  
3817 N N   . THR B 215 ? 0.6281 0.5947 0.6273 0.0296  0.1218  0.0468  258 THR B N   
3818 C CA  . THR B 215 ? 0.6089 0.5759 0.6012 0.0287  0.1117  0.0406  258 THR B CA  
3819 C C   . THR B 215 ? 0.5871 0.5649 0.5936 0.0245  0.1013  0.0391  258 THR B C   
3820 O O   . THR B 215 ? 0.5631 0.5395 0.5620 0.0230  0.0928  0.0344  258 THR B O   
3821 C CB  . THR B 215 ? 0.5985 0.5669 0.5906 0.0321  0.1142  0.0394  258 THR B CB  
3822 O OG1 . THR B 215 ? 0.5794 0.5608 0.5942 0.0324  0.1161  0.0431  258 THR B OG1 
3823 C CG2 . THR B 215 ? 0.6204 0.5752 0.5951 0.0365  0.1246  0.0403  258 THR B CG2 
3824 N N   . ILE B 216 ? 0.5907 0.5788 0.6177 0.0226  0.1019  0.0432  259 ILE B N   
3825 C CA  . ILE B 216 ? 0.5778 0.5733 0.6158 0.0182  0.0920  0.0419  259 ILE B CA  
3826 C C   . ILE B 216 ? 0.5692 0.5578 0.5984 0.0157  0.0887  0.0409  259 ILE B C   
3827 O O   . ILE B 216 ? 0.5360 0.5241 0.5614 0.0137  0.0800  0.0368  259 ILE B O   
3828 C CB  . ILE B 216 ? 0.5719 0.5789 0.6335 0.0160  0.0926  0.0471  259 ILE B CB  
3829 C CG1 . ILE B 216 ? 0.5956 0.6098 0.6665 0.0189  0.0950  0.0483  259 ILE B CG1 
3830 C CG2 . ILE B 216 ? 0.5625 0.5743 0.6325 0.0110  0.0818  0.0456  259 ILE B CG2 
3831 C CD1 . ILE B 216 ? 0.5578 0.5736 0.6239 0.0190  0.0865  0.0428  259 ILE B CD1 
3832 N N   . LYS B 217 ? 0.5814 0.5640 0.6069 0.0160  0.0960  0.0448  260 LYS B N   
3833 C CA  . LYS B 217 ? 0.5964 0.5709 0.6117 0.0141  0.0932  0.0440  260 LYS B CA  
3834 C C   . LYS B 217 ? 0.5750 0.5416 0.5713 0.0157  0.0882  0.0386  260 LYS B C   
3835 O O   . LYS B 217 ? 0.5507 0.5149 0.5428 0.0140  0.0811  0.0361  260 LYS B O   
3836 C CB  . LYS B 217 ? 0.6198 0.5874 0.6313 0.0149  0.1030  0.0492  260 LYS B CB  
3837 C CG  . LYS B 217 ? 0.7156 0.6917 0.7478 0.0131  0.1088  0.0557  260 LYS B CG  
3838 C CD  . LYS B 217 ? 0.8307 0.8139 0.8780 0.0078  0.1003  0.0562  260 LYS B CD  
3839 C CE  . LYS B 217 ? 0.8902 0.8814 0.9586 0.0051  0.1056  0.0634  260 LYS B CE  
3840 N NZ  . LYS B 217 ? 0.9708 0.9704 1.0560 -0.0003 0.0960  0.0637  260 LYS B NZ  
3841 N N   . GLU B 218 ? 0.5878 0.5498 0.5728 0.0190  0.0917  0.0370  261 GLU B N   
3842 C CA  . GLU B 218 ? 0.5926 0.5483 0.5615 0.0200  0.0860  0.0322  261 GLU B CA  
3843 C C   . GLU B 218 ? 0.5798 0.5435 0.5559 0.0184  0.0765  0.0282  261 GLU B C   
3844 O O   . GLU B 218 ? 0.5437 0.5046 0.5128 0.0177  0.0701  0.0253  261 GLU B O   
3845 C CB  . GLU B 218 ? 0.6162 0.5659 0.5733 0.0232  0.0911  0.0314  261 GLU B CB  
3846 C CG  . GLU B 218 ? 0.6292 0.5710 0.5688 0.0236  0.0855  0.0272  261 GLU B CG  
3847 C CD  . GLU B 218 ? 0.7354 0.6704 0.6633 0.0263  0.0898  0.0261  261 GLU B CD  
3848 O OE1 . GLU B 218 ? 0.7201 0.6577 0.6547 0.0283  0.0973  0.0283  261 GLU B OE1 
3849 O OE2 . GLU B 218 ? 0.7893 0.7161 0.7015 0.0263  0.0856  0.0233  261 GLU B OE2 
3850 N N   . LEU B 219 ? 0.5311 0.5044 0.5210 0.0180  0.0758  0.0281  262 LEU B N   
3851 C CA  . LEU B 219 ? 0.5012 0.4809 0.4967 0.0165  0.0674  0.0245  262 LEU B CA  
3852 C C   . LEU B 219 ? 0.4918 0.4719 0.4916 0.0138  0.0620  0.0242  262 LEU B C   
3853 O O   . LEU B 219 ? 0.4758 0.4550 0.4711 0.0135  0.0558  0.0207  262 LEU B O   
3854 C CB  . LEU B 219 ? 0.4424 0.4313 0.4515 0.0164  0.0676  0.0253  262 LEU B CB  
3855 C CG  . LEU B 219 ? 0.4488 0.4436 0.4639 0.0146  0.0594  0.0220  262 LEU B CG  
3856 C CD1 . LEU B 219 ? 0.3884 0.3802 0.3917 0.0159  0.0554  0.0174  262 LEU B CD1 
3857 C CD2 . LEU B 219 ? 0.4103 0.4134 0.4386 0.0145  0.0595  0.0237  262 LEU B CD2 
3858 N N   . GLU B 220 ? 0.5166 0.4976 0.5253 0.0118  0.0647  0.0282  263 GLU B N   
3859 C CA  . GLU B 220 ? 0.5401 0.5197 0.5520 0.0089  0.0598  0.0281  263 GLU B CA  
3860 C C   . GLU B 220 ? 0.5285 0.4993 0.5264 0.0100  0.0580  0.0264  263 GLU B C   
3861 O O   . GLU B 220 ? 0.4531 0.4225 0.4497 0.0092  0.0520  0.0239  263 GLU B O   
3862 C CB  . GLU B 220 ? 0.5660 0.5472 0.5893 0.0062  0.0637  0.0334  263 GLU B CB  
3863 C CG  . GLU B 220 ? 0.6520 0.6305 0.6786 0.0027  0.0586  0.0337  263 GLU B CG  
3864 C CD  . GLU B 220 ? 0.8042 0.7845 0.8432 -0.0006 0.0624  0.0395  263 GLU B CD  
3865 O OE1 . GLU B 220 ? 0.8286 0.8091 0.8689 0.0008  0.0708  0.0436  263 GLU B OE1 
3866 O OE2 . GLU B 220 ? 0.9151 0.8963 0.9623 -0.0046 0.0570  0.0401  263 GLU B OE2 
3867 N N   . SER B 221 ? 0.5059 0.4701 0.4928 0.0120  0.0631  0.0279  264 SER B N   
3868 C CA  . SER B 221 ? 0.5292 0.4850 0.5027 0.0131  0.0605  0.0268  264 SER B CA  
3869 C C   . SER B 221 ? 0.4986 0.4558 0.4668 0.0145  0.0543  0.0223  264 SER B C   
3870 O O   . SER B 221 ? 0.5032 0.4579 0.4681 0.0147  0.0493  0.0208  264 SER B O   
3871 C CB  . SER B 221 ? 0.5464 0.4935 0.5075 0.0147  0.0670  0.0294  264 SER B CB  
3872 O OG  . SER B 221 ? 0.6805 0.6191 0.6283 0.0155  0.0635  0.0288  264 SER B OG  
3873 N N   . ILE B 222 ? 0.4889 0.4499 0.4566 0.0156  0.0549  0.0204  265 ILE B N   
3874 C CA  . ILE B 222 ? 0.4814 0.4441 0.4448 0.0167  0.0495  0.0167  265 ILE B CA  
3875 C C   . ILE B 222 ? 0.4834 0.4514 0.4549 0.0159  0.0441  0.0143  265 ILE B C   
3876 O O   . ILE B 222 ? 0.4524 0.4192 0.4206 0.0168  0.0397  0.0125  265 ILE B O   
3877 C CB  . ILE B 222 ? 0.4666 0.4320 0.4285 0.0177  0.0516  0.0154  265 ILE B CB  
3878 C CG1 . ILE B 222 ? 0.5393 0.4961 0.4885 0.0190  0.0565  0.0171  265 ILE B CG1 
3879 C CG2 . ILE B 222 ? 0.4788 0.4479 0.4398 0.0181  0.0460  0.0118  265 ILE B CG2 
3880 C CD1 . ILE B 222 ? 0.5288 0.4864 0.4765 0.0202  0.0604  0.0166  265 ILE B CD1 
3881 N N   . ILE B 223 ? 0.4497 0.4231 0.4318 0.0143  0.0443  0.0145  266 ILE B N   
3882 C CA  . ILE B 223 ? 0.4490 0.4255 0.4365 0.0135  0.0392  0.0119  266 ILE B CA  
3883 C C   . ILE B 223 ? 0.4429 0.4142 0.4296 0.0128  0.0369  0.0124  266 ILE B C   
3884 O O   . ILE B 223 ? 0.4365 0.4067 0.4217 0.0137  0.0330  0.0098  266 ILE B O   
3885 C CB  . ILE B 223 ? 0.4641 0.4465 0.4619 0.0116  0.0391  0.0123  266 ILE B CB  
3886 C CG1 . ILE B 223 ? 0.4537 0.4378 0.4534 0.0110  0.0337  0.0090  266 ILE B CG1 
3887 C CG2 . ILE B 223 ? 0.4777 0.4597 0.4834 0.0090  0.0414  0.0162  266 ILE B CG2 
3888 C CD1 . ILE B 223 ? 0.4465 0.4325 0.4410 0.0133  0.0323  0.0058  266 ILE B CD1 
3889 N N   . SER B 224 ? 0.4617 0.4290 0.4490 0.0115  0.0398  0.0158  267 SER B N   
3890 C CA  . SER B 224 ? 0.4874 0.4485 0.4731 0.0108  0.0378  0.0165  267 SER B CA  
3891 C C   . SER B 224 ? 0.4686 0.4251 0.4450 0.0137  0.0356  0.0152  267 SER B C   
3892 O O   . SER B 224 ? 0.4316 0.3848 0.4071 0.0145  0.0323  0.0139  267 SER B O   
3893 C CB  . SER B 224 ? 0.4677 0.4252 0.4553 0.0088  0.0421  0.0209  267 SER B CB  
3894 O OG  . SER B 224 ? 0.5253 0.4880 0.5242 0.0058  0.0436  0.0229  267 SER B OG  
3895 N N   . LYS B 225 ? 0.4487 0.4046 0.4181 0.0154  0.0373  0.0158  268 LYS B N   
3896 C CA  . LYS B 225 ? 0.4670 0.4197 0.4290 0.0179  0.0341  0.0152  268 LYS B CA  
3897 C C   . LYS B 225 ? 0.4759 0.4331 0.4413 0.0195  0.0300  0.0119  268 LYS B C   
3898 O O   . LYS B 225 ? 0.5124 0.4674 0.4760 0.0216  0.0271  0.0116  268 LYS B O   
3899 C CB  . LYS B 225 ? 0.4759 0.4269 0.4294 0.0187  0.0355  0.0161  268 LYS B CB  
3900 C CG  . LYS B 225 ? 0.5162 0.4621 0.4614 0.0205  0.0317  0.0169  268 LYS B CG  
3901 C CD  . LYS B 225 ? 0.5191 0.4644 0.4563 0.0208  0.0308  0.0167  268 LYS B CD  
3902 C CE  . LYS B 225 ? 0.5814 0.5198 0.5091 0.0218  0.0268  0.0187  268 LYS B CE  
3903 N NZ  . LYS B 225 ? 0.5536 0.4903 0.4728 0.0214  0.0244  0.0184  268 LYS B NZ  
3904 N N   . ARG B 226 ? 0.4643 0.4278 0.4348 0.0189  0.0302  0.0096  269 ARG B N   
3905 C CA  . ARG B 226 ? 0.4633 0.4305 0.4364 0.0204  0.0273  0.0065  269 ARG B CA  
3906 C C   . ARG B 226 ? 0.4568 0.4213 0.4330 0.0200  0.0259  0.0052  269 ARG B C   
3907 O O   . ARG B 226 ? 0.4329 0.3990 0.4101 0.0214  0.0244  0.0026  269 ARG B O   
3908 C CB  . ARG B 226 ? 0.4577 0.4314 0.4331 0.0198  0.0280  0.0048  269 ARG B CB  
3909 C CG  . ARG B 226 ? 0.4690 0.4436 0.4398 0.0199  0.0295  0.0059  269 ARG B CG  
3910 C CD  . ARG B 226 ? 0.4157 0.3960 0.3878 0.0200  0.0292  0.0038  269 ARG B CD  
3911 N NE  . ARG B 226 ? 0.3889 0.3721 0.3625 0.0216  0.0264  0.0020  269 ARG B NE  
3912 C CZ  . ARG B 226 ? 0.4160 0.4024 0.3934 0.0219  0.0259  -0.0002 269 ARG B CZ  
3913 N NH1 . ARG B 226 ? 0.3946 0.3820 0.3747 0.0203  0.0268  -0.0010 269 ARG B NH1 
3914 N NH2 . ARG B 226 ? 0.3897 0.3781 0.3681 0.0239  0.0245  -0.0014 269 ARG B NH2 
3915 N N   . ASN B 227 ? 0.4721 0.4313 0.4489 0.0181  0.0265  0.0070  270 ASN B N   
3916 C CA  . ASN B 227 ? 0.4770 0.4310 0.4550 0.0173  0.0245  0.0059  270 ASN B CA  
3917 C C   . ASN B 227 ? 0.4752 0.4320 0.4571 0.0151  0.0232  0.0037  270 ASN B C   
3918 O O   . ASN B 227 ? 0.4416 0.3950 0.4217 0.0157  0.0209  0.0011  270 ASN B O   
3919 C CB  . ASN B 227 ? 0.5530 0.5028 0.5272 0.0210  0.0228  0.0044  270 ASN B CB  
3920 C CG  . ASN B 227 ? 0.6107 0.5568 0.5814 0.0231  0.0231  0.0071  270 ASN B CG  
3921 O OD1 . ASN B 227 ? 0.5950 0.5358 0.5643 0.0212  0.0239  0.0097  270 ASN B OD1 
3922 N ND2 . ASN B 227 ? 0.6130 0.5618 0.5825 0.0266  0.0222  0.0070  270 ASN B ND2 
3923 N N   . ILE B 228 ? 0.4576 0.4200 0.4444 0.0127  0.0246  0.0051  271 ILE B N   
3924 C CA  . ILE B 228 ? 0.4500 0.4154 0.4419 0.0100  0.0228  0.0041  271 ILE B CA  
3925 C C   . ILE B 228 ? 0.4602 0.4268 0.4594 0.0062  0.0241  0.0079  271 ILE B C   
3926 O O   . ILE B 228 ? 0.4792 0.4477 0.4796 0.0065  0.0282  0.0108  271 ILE B O   
3927 C CB  . ILE B 228 ? 0.4623 0.4349 0.4548 0.0113  0.0234  0.0026  271 ILE B CB  
3928 C CG1 . ILE B 228 ? 0.4321 0.4039 0.4189 0.0146  0.0223  -0.0007 271 ILE B CG1 
3929 C CG2 . ILE B 228 ? 0.4144 0.3904 0.4130 0.0083  0.0214  0.0027  271 ILE B CG2 
3930 C CD1 . ILE B 228 ? 0.4828 0.4609 0.4697 0.0156  0.0229  -0.0021 271 ILE B CD1 
3931 N N   . GLN B 229 ? 0.4361 0.4012 0.4401 0.0027  0.0206  0.0080  272 GLN B N   
3932 C CA  . GLN B 229 ? 0.4802 0.4476 0.4939 -0.0014 0.0213  0.0122  272 GLN B CA  
3933 C C   . GLN B 229 ? 0.4632 0.4404 0.4852 -0.0016 0.0238  0.0141  272 GLN B C   
3934 O O   . GLN B 229 ? 0.4339 0.4149 0.4538 0.0004  0.0231  0.0116  272 GLN B O   
3935 C CB  . GLN B 229 ? 0.4820 0.4444 0.4986 -0.0058 0.0155  0.0120  272 GLN B CB  
3936 C CG  . GLN B 229 ? 0.6042 0.5553 0.6127 -0.0057 0.0136  0.0105  272 GLN B CG  
3937 C CD  . GLN B 229 ? 0.7379 0.6814 0.7453 -0.0098 0.0071  0.0091  272 GLN B CD  
3938 O OE1 . GLN B 229 ? 0.7700 0.7131 0.7855 -0.0150 0.0046  0.0123  272 GLN B OE1 
3939 N NE2 . GLN B 229 ? 0.7285 0.6654 0.7257 -0.0075 0.0042  0.0044  272 GLN B NE2 
3940 N N   . PHE B 230 ? 0.4569 0.4377 0.4883 -0.0037 0.0271  0.0188  273 PHE B N   
3941 C CA  . PHE B 230 ? 0.4985 0.4881 0.5388 -0.0033 0.0307  0.0216  273 PHE B CA  
3942 C C   . PHE B 230 ? 0.5071 0.5014 0.5626 -0.0079 0.0290  0.0260  273 PHE B C   
3943 O O   . PHE B 230 ? 0.5010 0.4922 0.5609 -0.0112 0.0285  0.0288  273 PHE B O   
3944 C CB  . PHE B 230 ? 0.4973 0.4872 0.5344 -0.0003 0.0388  0.0239  273 PHE B CB  
3945 C CG  . PHE B 230 ? 0.5278 0.5251 0.5725 0.0010  0.0437  0.0266  273 PHE B CG  
3946 C CD1 . PHE B 230 ? 0.5015 0.5025 0.5439 0.0034  0.0428  0.0239  273 PHE B CD1 
3947 C CD2 . PHE B 230 ? 0.5584 0.5587 0.6128 0.0002  0.0499  0.0321  273 PHE B CD2 
3948 C CE1 . PHE B 230 ? 0.4908 0.4976 0.5398 0.0051  0.0476  0.0265  273 PHE B CE1 
3949 C CE2 . PHE B 230 ? 0.5592 0.5659 0.6209 0.0022  0.0553  0.0349  273 PHE B CE2 
3950 C CZ  . PHE B 230 ? 0.5388 0.5485 0.5976 0.0047  0.0540  0.0319  273 PHE B CZ  
3951 N N   . SER B 231 ? 0.5247 0.5267 0.5889 -0.0082 0.0276  0.0269  274 SER B N   
3952 C CA  . SER B 231 ? 0.5507 0.5595 0.6321 -0.0123 0.0257  0.0320  274 SER B CA  
3953 C C   . SER B 231 ? 0.5200 0.5382 0.6104 -0.0095 0.0309  0.0349  274 SER B C   
3954 O O   . SER B 231 ? 0.5077 0.5267 0.5906 -0.0057 0.0319  0.0316  274 SER B O   
3955 C CB  . SER B 231 ? 0.5617 0.5686 0.6449 -0.0165 0.0153  0.0301  274 SER B CB  
3956 O OG  . SER B 231 ? 0.6589 0.6738 0.7601 -0.0206 0.0124  0.0354  274 SER B OG  
3957 N N   . CYS B 232 ? 0.5113 0.5367 0.6183 -0.0112 0.0346  0.0413  275 CYS B N   
3958 C CA  . CYS B 232 ? 0.5593 0.5934 0.6762 -0.0079 0.0410  0.0449  275 CYS B CA  
3959 C C   . CYS B 232 ? 0.5701 0.6141 0.7094 -0.0117 0.0379  0.0512  275 CYS B C   
3960 O O   . CYS B 232 ? 0.5721 0.6169 0.7214 -0.0166 0.0353  0.0548  275 CYS B O   
3961 C CB  . CYS B 232 ? 0.5786 0.6109 0.6920 -0.0041 0.0527  0.0475  275 CYS B CB  
3962 S SG  . CYS B 232 ? 0.6671 0.7076 0.7905 0.0010  0.0623  0.0519  275 CYS B SG  
3963 N N   . LYS B 233 ? 0.6135 0.6653 0.7612 -0.0094 0.0379  0.0526  276 LYS B N   
3964 C CA  . LYS B 233 ? 0.6359 0.6987 0.8066 -0.0123 0.0346  0.0591  276 LYS B CA  
3965 C C   . LYS B 233 ? 0.5960 0.6668 0.7757 -0.0067 0.0430  0.0628  276 LYS B C   
3966 O O   . LYS B 233 ? 0.5914 0.6587 0.7578 -0.0017 0.0462  0.0585  276 LYS B O   
3967 C CB  . LYS B 233 ? 0.6250 0.6876 0.7962 -0.0164 0.0212  0.0567  276 LYS B CB  
3968 C CG  . LYS B 233 ? 0.6820 0.7355 0.8444 -0.0222 0.0122  0.0534  276 LYS B CG  
3969 C CD  . LYS B 233 ? 0.7769 0.8256 0.9299 -0.0240 0.0010  0.0485  276 LYS B CD  
3970 C CE  . LYS B 233 ? 0.8630 0.9064 1.0179 -0.0315 -0.0103 0.0488  276 LYS B CE  
3971 N NZ  . LYS B 233 ? 0.8764 0.9151 1.0229 -0.0332 -0.0211 0.0451  276 LYS B NZ  
3972 N N   . ASN B 234 ? 0.5885 0.6699 0.7912 -0.0075 0.0469  0.0709  277 ASN B N   
3973 C CA  . ASN B 234 ? 0.6054 0.6949 0.8194 -0.0018 0.0552  0.0754  277 ASN B CA  
3974 C C   . ASN B 234 ? 0.5931 0.6914 0.8211 -0.0031 0.0460  0.0775  277 ASN B C   
3975 O O   . ASN B 234 ? 0.5962 0.7000 0.8391 -0.0093 0.0362  0.0810  277 ASN B O   
3976 C CB  . ASN B 234 ? 0.6254 0.7222 0.8582 -0.0010 0.0660  0.0839  277 ASN B CB  
3977 C CG  . ASN B 234 ? 0.6921 0.7793 0.9099 0.0009  0.0762  0.0824  277 ASN B CG  
3978 O OD1 . ASN B 234 ? 0.7106 0.7916 0.9142 0.0071  0.0859  0.0801  277 ASN B OD1 
3979 N ND2 . ASN B 234 ? 0.7333 0.8181 0.9533 -0.0045 0.0737  0.0838  277 ASN B ND2 
3980 N N   . ILE B 235 ? 0.5893 0.6877 0.8115 0.0024  0.0484  0.0754  278 ILE B N   
3981 C CA  . ILE B 235 ? 0.5992 0.7061 0.8352 0.0026  0.0415  0.0784  278 ILE B CA  
3982 C C   . ILE B 235 ? 0.6443 0.7614 0.9001 0.0081  0.0527  0.0862  278 ILE B C   
3983 O O   . ILE B 235 ? 0.6436 0.7575 0.8906 0.0150  0.0620  0.0848  278 ILE B O   
3984 C CB  . ILE B 235 ? 0.6017 0.7014 0.8183 0.0051  0.0368  0.0712  278 ILE B CB  
3985 C CG1 . ILE B 235 ? 0.6013 0.6904 0.7978 0.0006  0.0278  0.0635  278 ILE B CG1 
3986 C CG2 . ILE B 235 ? 0.6578 0.7658 0.8884 0.0052  0.0293  0.0747  278 ILE B CG2 
3987 C CD1 . ILE B 235 ? 0.6383 0.7291 0.8432 -0.0069 0.0144  0.0649  278 ILE B CD1 
3988 N N   . TYR B 236 ? 0.6238 0.7528 0.9065 0.0049  0.0518  0.0949  279 TYR B N   
3989 C CA  . TYR B 236 ? 0.6488 0.7880 0.9525 0.0103  0.0642  0.1034  279 TYR B CA  
3990 C C   . TYR B 236 ? 0.6720 0.8189 0.9872 0.0150  0.0628  0.1065  279 TYR B C   
3991 O O   . TYR B 236 ? 0.7044 0.8528 1.0226 0.0228  0.0754  0.1092  279 TYR B O   
3992 C CB  . TYR B 236 ? 0.6333 0.7838 0.9642 0.0050  0.0638  0.1124  279 TYR B CB  
3993 C CG  . TYR B 236 ? 0.6126 0.7556 0.9339 0.0015  0.0681  0.1108  279 TYR B CG  
3994 C CD1 . TYR B 236 ? 0.7027 0.8411 1.0170 0.0069  0.0844  0.1118  279 TYR B CD1 
3995 C CD2 . TYR B 236 ? 0.6019 0.7411 0.9196 -0.0071 0.0560  0.1083  279 TYR B CD2 
3996 C CE1 . TYR B 236 ? 0.7211 0.8520 1.0258 0.0037  0.0881  0.1106  279 TYR B CE1 
3997 C CE2 . TYR B 236 ? 0.6474 0.7792 0.9562 -0.0100 0.0599  0.1070  279 TYR B CE2 
3998 C CZ  . TYR B 236 ? 0.6868 0.8148 0.9894 -0.0046 0.0758  0.1083  279 TYR B CZ  
3999 O OH  . TYR B 236 ? 0.7038 0.8239 0.9969 -0.0075 0.0795  0.1073  279 TYR B OH  
4000 N N   . ARG B 237 ? 0.6964 0.8469 1.0168 0.0106  0.0477  0.1060  280 ARG B N   
4001 C CA  . ARG B 237 ? 0.7432 0.9011 1.0755 0.0143  0.0443  0.1095  280 ARG B CA  
4002 C C   . ARG B 237 ? 0.7975 0.9447 1.1052 0.0140  0.0350  0.1007  280 ARG B C   
4003 O O   . ARG B 237 ? 0.8203 0.9666 1.1263 0.0077  0.0202  0.0989  280 ARG B O   
4004 C CB  . ARG B 237 ? 0.7201 0.8931 1.0840 0.0090  0.0340  0.1188  280 ARG B CB  
4005 N N   . PRO B 238 ? 0.8443 0.9824 1.1316 0.0206  0.0434  0.0951  281 PRO B N   
4006 C CA  . PRO B 238 ? 0.8817 1.0098 1.1460 0.0202  0.0352  0.0870  281 PRO B CA  
4007 C C   . PRO B 238 ? 0.8995 1.0335 1.1744 0.0189  0.0234  0.0899  281 PRO B C   
4008 O O   . PRO B 238 ? 0.8806 1.0086 1.1430 0.0142  0.0112  0.0851  281 PRO B O   
4009 C CB  . PRO B 238 ? 0.8541 0.9738 1.1011 0.0279  0.0478  0.0830  281 PRO B CB  
4010 C CG  . PRO B 238 ? 0.8495 0.9700 1.1013 0.0307  0.0616  0.0861  281 PRO B CG  
4011 C CD  . PRO B 238 ? 0.8163 0.9512 1.0989 0.0282  0.0605  0.0957  281 PRO B CD  
4012 N N   . ASP B 239 ? 0.8611 1.0061 1.1584 0.0234  0.0270  0.0978  282 ASP B N   
4013 C CA  . ASP B 239 ? 0.8577 1.0084 1.1659 0.0224  0.0152  0.1014  282 ASP B CA  
4014 C C   . ASP B 239 ? 0.8267 0.9825 1.1469 0.0132  -0.0003 0.1042  282 ASP B C   
4015 O O   . ASP B 239 ? 0.7936 0.9451 1.1056 0.0093  -0.0140 0.1017  282 ASP B O   
4016 C CB  . ASP B 239 ? 0.9127 1.0753 1.2455 0.0294  0.0229  0.1104  282 ASP B CB  
4017 C CG  . ASP B 239 ? 0.9350 1.1103 1.2953 0.0295  0.0306  0.1192  282 ASP B CG  
4018 O OD1 . ASP B 239 ? 0.8271 0.9991 1.1817 0.0263  0.0353  0.1170  282 ASP B OD1 
4019 O OD2 . ASP B 239 ? 0.9913 1.1801 1.3795 0.0328  0.0323  0.1288  282 ASP B OD2 
4020 N N   . LYS B 240 ? 0.8510 1.0147 1.1895 0.0094  0.0014  0.1096  283 LYS B N   
4021 C CA  . LYS B 240 ? 0.8702 1.0370 1.2186 -0.0002 -0.0136 0.1121  283 LYS B CA  
4022 C C   . LYS B 240 ? 0.8969 1.0481 1.2164 -0.0058 -0.0212 0.1022  283 LYS B C   
4023 O O   . LYS B 240 ? 0.9185 1.0662 1.2351 -0.0129 -0.0364 0.1013  283 LYS B O   
4024 C CB  . LYS B 240 ? 0.8123 0.9908 1.1872 -0.0030 -0.0088 0.1203  283 LYS B CB  
4025 N N   . PHE B 241 ? 0.8778 1.0189 1.1753 -0.0028 -0.0108 0.0949  284 PHE B N   
4026 C CA  . PHE B 241 ? 0.8736 1.0003 1.1442 -0.0071 -0.0167 0.0857  284 PHE B CA  
4027 C C   . PHE B 241 ? 0.8707 0.9891 1.1238 -0.0075 -0.0269 0.0805  284 PHE B C   
4028 O O   . PHE B 241 ? 0.8870 0.9968 1.1276 -0.0135 -0.0383 0.0766  284 PHE B O   
4029 C CB  . PHE B 241 ? 0.8787 0.9974 1.1309 -0.0027 -0.0034 0.0798  284 PHE B CB  
4030 C CG  . PHE B 241 ? 0.8731 0.9771 1.0957 -0.0041 -0.0072 0.0699  284 PHE B CG  
4031 C CD1 . PHE B 241 ? 0.8486 0.9454 1.0624 -0.0103 -0.0139 0.0665  284 PHE B CD1 
4032 C CD2 . PHE B 241 ? 0.8491 0.9464 1.0535 0.0010  -0.0035 0.0644  284 PHE B CD2 
4033 C CE1 . PHE B 241 ? 0.8109 0.8946 0.9987 -0.0109 -0.0163 0.0579  284 PHE B CE1 
4034 C CE2 . PHE B 241 ? 0.7912 0.8763 0.9706 -0.0001 -0.0063 0.0561  284 PHE B CE2 
4035 C CZ  . PHE B 241 ? 0.7927 0.8712 0.9641 -0.0057 -0.0124 0.0529  284 PHE B CZ  
4036 N N   . LEU B 242 ? 0.8097 0.9293 1.0605 -0.0011 -0.0226 0.0806  285 LEU B N   
4037 C CA  . LEU B 242 ? 0.7881 0.8999 1.0227 -0.0014 -0.0317 0.0763  285 LEU B CA  
4038 C C   . LEU B 242 ? 0.8530 0.9688 1.1003 -0.0071 -0.0475 0.0813  285 LEU B C   
4039 O O   . LEU B 242 ? 0.8582 0.9635 1.0884 -0.0116 -0.0588 0.0768  285 LEU B O   
4040 C CB  . LEU B 242 ? 0.7408 0.8534 0.9724 0.0066  -0.0235 0.0762  285 LEU B CB  
4041 C CG  . LEU B 242 ? 0.7095 0.8116 0.9166 0.0110  -0.0135 0.0682  285 LEU B CG  
4042 C CD1 . LEU B 242 ? 0.6310 0.7345 0.8388 0.0187  -0.0050 0.0696  285 LEU B CD1 
4043 C CD2 . LEU B 242 ? 0.6151 0.7044 0.7969 0.0075  -0.0213 0.0603  285 LEU B CD2 
4044 N N   . GLN B 243 ? 0.8762 1.0065 1.1532 -0.0071 -0.0487 0.0909  286 GLN B N   
4045 C CA  . GLN B 243 ? 0.9420 1.0769 1.2328 -0.0127 -0.0649 0.0966  286 GLN B CA  
4046 C C   . GLN B 243 ? 0.9899 1.1178 1.2747 -0.0224 -0.0769 0.0946  286 GLN B C   
4047 O O   . GLN B 243 ? 1.0502 1.1724 1.3295 -0.0279 -0.0923 0.0946  286 GLN B O   
4048 C CB  . GLN B 243 ? 0.9453 1.0989 1.2724 -0.0107 -0.0628 0.1082  286 GLN B CB  
4049 C CG  . GLN B 243 ? 1.0618 1.2215 1.4047 -0.0146 -0.0791 0.1151  286 GLN B CG  
4050 C CD  . GLN B 243 ? 1.1058 1.2600 1.4356 -0.0096 -0.0820 0.1129  286 GLN B CD  
4051 O OE1 . GLN B 243 ? 1.1282 1.2683 1.4325 -0.0127 -0.0912 0.1062  286 GLN B OE1 
4052 N NE2 . GLN B 243 ? 1.1015 1.2662 1.4484 -0.0018 -0.0736 0.1187  286 GLN B NE2 
4053 N N   . CYS B 244 ? 0.9646 1.0916 1.2492 -0.0245 -0.0704 0.0930  287 CYS B N   
4054 C CA  . CYS B 244 ? 1.0504 1.1686 1.3269 -0.0334 -0.0810 0.0905  287 CYS B CA  
4055 C C   . CYS B 244 ? 1.0658 1.1648 1.3072 -0.0345 -0.0858 0.0801  287 CYS B C   
4056 O O   . CYS B 244 ? 1.1538 1.2428 1.3850 -0.0416 -0.0990 0.0781  287 CYS B O   
4057 C CB  . CYS B 244 ? 1.0952 1.2165 1.3796 -0.0348 -0.0718 0.0914  287 CYS B CB  
4058 S SG  . CYS B 244 ? 1.3520 1.4948 1.6792 -0.0360 -0.0686 0.1047  287 CYS B SG  
4059 N N   . VAL B 245 ? 0.9511 1.0444 1.1738 -0.0276 -0.0750 0.0737  288 VAL B N   
4060 C CA  . VAL B 245 ? 0.9423 1.0190 1.1338 -0.0279 -0.0786 0.0647  288 VAL B CA  
4061 C C   . VAL B 245 ? 1.0278 1.1009 1.2137 -0.0284 -0.0895 0.0654  288 VAL B C   
4062 O O   . VAL B 245 ? 1.0098 1.0684 1.1732 -0.0316 -0.0980 0.0601  288 VAL B O   
4063 C CB  . VAL B 245 ? 0.8429 0.9156 1.0184 -0.0209 -0.0641 0.0584  288 VAL B CB  
4064 C CG1 . VAL B 245 ? 0.7521 0.8089 0.8975 -0.0209 -0.0669 0.0497  288 VAL B CG1 
4065 C CG2 . VAL B 245 ? 0.7543 0.8296 0.9344 -0.0206 -0.0542 0.0579  288 VAL B CG2 
4066 N N   . LYS B 246 ? 1.1461 1.2314 1.3513 -0.0249 -0.0892 0.0721  289 LYS B N   
4067 C CA  . LYS B 246 ? 1.2064 1.2887 1.4079 -0.0255 -0.1004 0.0739  289 LYS B CA  
4068 C C   . LYS B 246 ? 1.2785 1.3595 1.4881 -0.0342 -0.1180 0.0783  289 LYS B C   
4069 O O   . LYS B 246 ? 1.3463 1.4144 1.5373 -0.0379 -0.1299 0.0754  289 LYS B O   
4070 C CB  . LYS B 246 ? 1.1967 1.2925 1.4179 -0.0189 -0.0948 0.0803  289 LYS B CB  
4071 C CG  . LYS B 246 ? 1.1732 1.2676 1.3834 -0.0105 -0.0795 0.0759  289 LYS B CG  
4072 C CD  . LYS B 246 ? 1.1813 1.2881 1.4121 -0.0040 -0.0741 0.0830  289 LYS B CD  
4073 C CE  . LYS B 246 ? 1.1911 1.2958 1.4116 0.0041  -0.0585 0.0789  289 LYS B CE  
4074 N NZ  . LYS B 246 ? 1.2116 1.3282 1.4537 0.0109  -0.0512 0.0861  289 LYS B NZ  
4075 N N   . ASN B 247 ? 1.2470 1.3408 1.4841 -0.0379 -0.1198 0.0857  290 ASN B N   
4076 C CA  . ASN B 247 ? 1.3006 1.3955 1.5503 -0.0467 -0.1371 0.0915  290 ASN B CA  
4077 C C   . ASN B 247 ? 1.3477 1.4431 1.6047 -0.0528 -0.1368 0.0920  290 ASN B C   
4078 O O   . ASN B 247 ? 1.3139 1.4251 1.6011 -0.0541 -0.1343 0.1001  290 ASN B O   
4079 C CB  . ASN B 247 ? 1.2784 1.3913 1.5609 -0.0457 -0.1418 0.1027  290 ASN B CB  
4080 N N   . PRO B 248 ? 1.4386 1.5164 1.6686 -0.0564 -0.1387 0.0836  291 PRO B N   
4081 C CA  . PRO B 248 ? 1.4770 1.5533 1.7123 -0.0626 -0.1396 0.0840  291 PRO B CA  
4082 C C   . PRO B 248 ? 1.4899 1.5706 1.7452 -0.0722 -0.1562 0.0919  291 PRO B C   
4083 O O   . PRO B 248 ? 1.4989 1.5827 1.7669 -0.0777 -0.1569 0.0948  291 PRO B O   
4084 C CB  . PRO B 248 ? 1.5305 1.5847 1.7294 -0.0638 -0.1399 0.0731  291 PRO B CB  
4085 C CG  . PRO B 248 ? 1.5338 1.5767 1.7110 -0.0621 -0.1468 0.0691  291 PRO B CG  
4086 C CD  . PRO B 248 ? 1.4753 1.5335 1.6691 -0.0550 -0.1406 0.0740  291 PRO B CD  
4087 N N   . GLU B 249 ? 1.5725 1.6533 1.8310 -0.0746 -0.1700 0.0958  292 GLU B N   
4088 C CA  . GLU B 249 ? 1.5357 1.6213 1.8144 -0.0839 -0.1878 0.1042  292 GLU B CA  
4089 C C   . GLU B 249 ? 1.4283 1.5401 1.7503 -0.0821 -0.1821 0.1158  292 GLU B C   
4090 O O   . GLU B 249 ? 1.3989 1.5237 1.7415 -0.0801 -0.1867 0.1234  292 GLU B O   
4091 C CB  . GLU B 249 ? 1.5496 1.6264 1.8161 -0.0860 -0.2037 0.1045  292 GLU B CB  
4092 C CG  . GLU B 249 ? 1.5384 1.6282 1.8169 -0.0773 -0.1979 0.1084  292 GLU B CG  
4093 C CD  . GLU B 249 ? 1.5558 1.6294 1.8040 -0.0750 -0.2041 0.1025  292 GLU B CD  
4094 O OE1 . GLU B 249 ? 1.5862 1.6404 1.8098 -0.0818 -0.2180 0.0983  292 GLU B OE1 
4095 O OE2 . GLU B 249 ? 1.5204 1.5997 1.7684 -0.0664 -0.1948 0.1022  292 GLU B OE2 
4096 N N   . ASP B 250 ? 1.3537 1.4728 1.6890 -0.0827 -0.1715 0.1173  293 ASP B N   
4097 C CA  . ASP B 250 ? 1.1802 1.3230 1.5551 -0.0804 -0.1625 0.1278  293 ASP B CA  
4098 C C   . ASP B 250 ? 1.0603 1.2044 1.4328 -0.0761 -0.1435 0.1244  293 ASP B C   
4099 O O   . ASP B 250 ? 1.0600 1.2039 1.4397 -0.0823 -0.1440 0.1261  293 ASP B O   
4100 C CB  . ASP B 250 ? 1.1185 1.2767 1.5116 -0.0718 -0.1569 0.1337  293 ASP B CB  
4101 C CG  . ASP B 250 ? 1.1313 1.3008 1.5510 -0.0771 -0.1739 0.1443  293 ASP B CG  
4102 O OD1 . ASP B 250 ? 1.0971 1.2633 1.5225 -0.0879 -0.1902 0.1475  293 ASP B OD1 
4103 O OD2 . ASP B 250 ? 1.0821 1.2633 1.5169 -0.0705 -0.1717 0.1496  293 ASP B OD2 
4104 O O2R . NNR C .   ? 0.6592 0.6628 0.6541 0.0008  -0.0166 -0.0128 401 NNR A O2R 
4105 C C2R . NNR C .   ? 0.6582 0.6628 0.6578 -0.0004 -0.0183 -0.0126 401 NNR A C2R 
4106 C C3R . NNR C .   ? 0.7168 0.7191 0.7175 -0.0009 -0.0192 -0.0142 401 NNR A C3R 
4107 O O3R . NNR C .   ? 0.7422 0.7410 0.7381 -0.0008 -0.0204 -0.0163 401 NNR A O3R 
4108 C C4R . NNR C .   ? 0.6529 0.6554 0.6554 0.0003  -0.0167 -0.0139 401 NNR A C4R 
4109 C C5R . NNR C .   ? 0.6753 0.6763 0.6807 0.0000  -0.0168 -0.0143 401 NNR A C5R 
4110 O O5R . NNR C .   ? 0.6709 0.6730 0.6794 -0.0014 -0.0184 -0.0136 401 NNR A O5R 
4111 O O4R . NNR C .   ? 0.6019 0.6076 0.6072 0.0005  -0.0160 -0.0119 401 NNR A O4R 
4112 C C1R . NNR C .   ? 0.5950 0.6021 0.5992 0.0000  -0.0170 -0.0112 401 NNR A C1R 
4113 N N1  . NNR C .   ? 0.5183 0.5273 0.5261 -0.0008 -0.0184 -0.0103 401 NNR A N1  
4114 C C2  . NNR C .   ? 0.5123 0.5208 0.5223 -0.0013 -0.0189 -0.0107 401 NNR A C2  
4115 C C6  . NNR C .   ? 0.5223 0.5331 0.5312 -0.0009 -0.0188 -0.0090 401 NNR A C6  
4116 C C5  . NNR C .   ? 0.4897 0.5016 0.5016 -0.0013 -0.0199 -0.0085 401 NNR A C5  
4117 C C4  . NNR C .   ? 0.4722 0.4839 0.4859 -0.0015 -0.0200 -0.0091 401 NNR A C4  
4118 C C3  . NNR C .   ? 0.4873 0.4974 0.5003 -0.0016 -0.0195 -0.0099 401 NNR A C3  
4119 C C7  . NNR C .   ? 0.4742 0.4840 0.4899 -0.0020 -0.0191 -0.0099 401 NNR A C7  
4120 O O7  . NNR C .   ? 0.4897 0.4977 0.5054 -0.0023 -0.0188 -0.0104 401 NNR A O7  
4121 N N7  . NNR C .   ? 0.4302 0.4415 0.4485 -0.0018 -0.0190 -0.0091 401 NNR A N7  
4122 O O5  . RIB D .   ? 0.3128 0.3271 0.3381 0.0017  -0.0237 -0.0080 402 RIB A O5  
4123 C C5  . RIB D .   ? 0.3378 0.3531 0.3627 0.0005  -0.0235 -0.0074 402 RIB A C5  
4124 C C4  . RIB D .   ? 0.3751 0.3900 0.3976 -0.0003 -0.0240 -0.0069 402 RIB A C4  
4125 O O4  . RIB D .   ? 0.3649 0.3801 0.3883 -0.0009 -0.0255 -0.0056 402 RIB A O4  
4126 C C3  . RIB D .   ? 0.3990 0.4139 0.4190 -0.0012 -0.0234 -0.0069 402 RIB A C3  
4127 O O3  . RIB D .   ? 0.3976 0.4119 0.4167 -0.0007 -0.0219 -0.0077 402 RIB A O3  
4128 C C2  . RIB D .   ? 0.4236 0.4385 0.4419 -0.0015 -0.0236 -0.0059 402 RIB A C2  
4129 O O2  . RIB D .   ? 0.3918 0.4065 0.4098 -0.0011 -0.0225 -0.0059 402 RIB A O2  
4130 C C1  . RIB D .   ? 0.3634 0.3786 0.3842 -0.0016 -0.0252 -0.0047 402 RIB A C1  
4131 O O2R . NNR E .   ? 0.5459 0.4985 0.4691 0.0265  0.0561  -0.0026 401 NNR B O2R 
4132 C C2R . NNR E .   ? 0.5407 0.5026 0.4763 0.0278  0.0555  -0.0014 401 NNR B C2R 
4133 C C3R . NNR E .   ? 0.5563 0.5140 0.4903 0.0302  0.0579  -0.0007 401 NNR B C3R 
4134 O O3R . NNR E .   ? 0.5957 0.5420 0.5198 0.0330  0.0637  -0.0002 401 NNR B O3R 
4135 C C4R . NNR E .   ? 0.5353 0.4912 0.4632 0.0264  0.0527  -0.0029 401 NNR B C4R 
4136 C C5R . NNR E .   ? 0.5579 0.5125 0.4862 0.0274  0.0526  -0.0024 401 NNR B C5R 
4137 O O5R . NNR E .   ? 0.5637 0.5277 0.5047 0.0294  0.0523  -0.0006 401 NNR B O5R 
4138 O O4R . NNR E .   ? 0.5186 0.4846 0.4544 0.0238  0.0481  -0.0035 401 NNR B O4R 
4139 C C1R . NNR E .   ? 0.5087 0.4780 0.4486 0.0244  0.0492  -0.0029 401 NNR B C1R 
4140 N N1  . NNR E .   ? 0.4773 0.4574 0.4303 0.0249  0.0475  -0.0019 401 NNR B N1  
4141 C C2  . NNR E .   ? 0.4672 0.4504 0.4262 0.0265  0.0474  -0.0007 401 NNR B C2  
4142 C C6  . NNR E .   ? 0.4381 0.4232 0.3957 0.0238  0.0458  -0.0021 401 NNR B C6  
4143 C C5  . NNR E .   ? 0.4473 0.4402 0.4152 0.0238  0.0438  -0.0013 401 NNR B C5  
4144 C C4  . NNR E .   ? 0.4291 0.4251 0.4027 0.0250  0.0430  -0.0001 401 NNR B C4  
4145 C C3  . NNR E .   ? 0.4409 0.4323 0.4104 0.0265  0.0449  0.0004  401 NNR B C3  
4146 C C7  . NNR E .   ? 0.4767 0.4706 0.4519 0.0281  0.0438  0.0021  401 NNR B C7  
4147 O O7  . NNR E .   ? 0.4809 0.4700 0.4529 0.0302  0.0465  0.0030  401 NNR B O7  
4148 N N7  . NNR E .   ? 0.4424 0.4425 0.4248 0.0270  0.0395  0.0026  401 NNR B N7  
4149 O O5  . RIB F .   ? 0.3262 0.3410 0.3304 0.0169  0.0232  0.0003  402 RIB B O5  
4150 C C5  . RIB F .   ? 0.3632 0.3792 0.3696 0.0188  0.0276  0.0022  402 RIB B C5  
4151 C C4  . RIB F .   ? 0.3645 0.3772 0.3629 0.0195  0.0313  0.0003  402 RIB B C4  
4152 O O4  . RIB F .   ? 0.3584 0.3708 0.3586 0.0192  0.0332  0.0011  402 RIB B O4  
4153 C C3  . RIB F .   ? 0.3915 0.4019 0.3866 0.0216  0.0359  0.0012  402 RIB B C3  
4154 O O3  . RIB F .   ? 0.3984 0.4073 0.3882 0.0215  0.0345  -0.0003 402 RIB B O3  
4155 C C2  . RIB F .   ? 0.4118 0.4185 0.4007 0.0215  0.0388  0.0004  402 RIB B C2  
4156 O O2  . RIB F .   ? 0.4078 0.4124 0.3891 0.0206  0.0372  -0.0021 402 RIB B O2  
4157 C C1  . RIB F .   ? 0.3812 0.3903 0.3755 0.0203  0.0372  0.0009  402 RIB B C1  
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