data_9MZY
# 
_entry.id   9MZY 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.403 
_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   9MZY         pdb_00009mzy 10.2210/pdb9mzy/pdb 
WWPDB D_1000291537 ?            ?                   
# 
_pdbx_audit_revision_history.ordinal             1 
_pdbx_audit_revision_history.data_content_type   'Structure model' 
_pdbx_audit_revision_history.major_revision      1 
_pdbx_audit_revision_history.minor_revision      0 
_pdbx_audit_revision_history.revision_date       2025-05-28 
_pdbx_audit_revision_history.part_number         ? 
# 
_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_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        9MZY 
_pdbx_database_status.recvd_initial_deposition_date   2025-01-23 
_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           N 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              rachel.kubiak@merck.com 
_pdbx_contact_author.name_first         Rachel 
_pdbx_contact_author.name_last          Palte 
_pdbx_contact_author.name_mi            L. 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0001-6146-0551 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Palte, R.L.'   1 0000-0001-6146-0551 
'Lesburg, C.A.' 2 ?                   
'Maskos, K.'    3 ?                   
'Thomsen, M.'   4 ?                   
'Lammens, A.'   5 ?                   
# 
_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            'Acs Med.Chem.Lett.' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            ? 
_citation.journal_id_ISSN           1948-5875 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            16 
_citation.language                  ? 
_citation.page_first                811 
_citation.page_last                 818 
_citation.title                     'The Discovery of Bridged Benzoazepine Amides as Selective Allosteric Modulators of RIPK1.' 
_citation.year                      2025 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1021/acsmedchemlett.5c00063 
_citation.pdbx_database_id_PubMed   40365380 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Chen, J.L.'        1  0009-0008-1574-1000 
primary 'Methot, J.L.'      2  0000-0003-3374-181X 
primary 'Mitcheltree, M.J.' 3  0000-0003-3774-628X 
primary 'Musacchio, A.'     4  ?                   
primary 'Corcoran, E.B.'    5  ?                   
primary 'Feng, G.'          6  ?                   
primary 'Lammens, A.'       7  ?                   
primary 'Maskos, K.'        8  ?                   
primary 'Palte, R.L.'       9  ?                   
primary 'Rickard, M.M.'     10 ?                   
primary 'Otte, K.M.'        11 ?                   
primary 'Mansueto, M.S.'    12 ?                   
primary 'Venkat, S.'        13 ?                   
primary 'Sondey, C.'        14 ?                   
primary 'Thomsen, M.'       15 ?                   
primary 'Lesburg, C.A.'     16 0000-0001-7245-7331 
primary 'Fradera, X.'       17 ?                   
primary 'Fell, M.J.'        18 ?                   
primary 'DiMauro, E.F.'     19 0009-0009-5054-1140 
primary 'Siliphaivanh, P.'  20 ?                   
# 
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 'Receptor-interacting serine/threonine-protein kinase 1'                                              32665.777 
2  2.7.11.1 ? ? ? 
2 non-polymer syn '1-[(2S,5S)-2,3-dihydro-2,5-methano-1,4-benzoxazepin-4(5H)-yl]-3,3-difluoro-2,2-dimethylpropan-1-one' 281.298   
2  ?        ? ? ? 
3 non-polymer syn 'IODIDE ION'                                                                                          126.904   
4  ?        ? ? ? 
4 non-polymer syn GLYCINE                                                                                               75.067    
1  ?        ? ? ? 
5 non-polymer syn 'CHLORIDE ION'                                                                                        35.453    
1  ?        ? ? ? 
6 water       nat water                                                                                                 18.015    
69 ?        ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'Cell death protein RIP,Receptor-interacting protein 1,RIP-1' 
# 
_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       
;NVIKMKSSDFLESAELDSGGFGKVSLAFHRTQGLMIMKTVYKGPNCIEHNEALLEEAKMMNRLRHSRVVKLLGVIIEEGK
YSLVMEYMEKGNLMHVLKAEMSTPLSVKGRIILEIIEGMAYLHGKGVIHKDLKPENILVDNDFHIKIADLGLASFKMWSK
LNNEEHNELREVDGTAKKNGGTLYYMAPEHLNDVNAKPTEKSDVYSFAVVLWAIFANKEPYENAIAEQQLIMAIKSGNRP
DVDDITEYCPREIISLMKLCWEANPEARPTFPGIEEKFRPFYLSQLE
;
_entity_poly.pdbx_seq_one_letter_code_can   
;NVIKMKSSDFLESAELDSGGFGKVSLAFHRTQGLMIMKTVYKGPNCIEHNEALLEEAKMMNRLRHSRVVKLLGVIIEEGK
YSLVMEYMEKGNLMHVLKAEMSTPLSVKGRIILEIIEGMAYLHGKGVIHKDLKPENILVDNDFHIKIADLGLASFKMWSK
LNNEEHNELREVDGTAKKNGGTLYYMAPEHLNDVNAKPTEKSDVYSFAVVLWAIFANKEPYENAIAEQQLIMAIKSGNRP
DVDDITEYCPREIISLMKLCWEANPEARPTFPGIEEKFRPFYLSQLE
;
_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 '1-[(2S,5S)-2,3-dihydro-2,5-methano-1,4-benzoxazepin-4(5H)-yl]-3,3-difluoro-2,2-dimethylpropan-1-one' A1BU6 
3 'IODIDE ION'                                                                                          IOD   
4 GLYCINE                                                                                               GLY   
5 'CHLORIDE ION'                                                                                        CL    
6 water                                                                                                 HOH   
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   ASN n 
1 2   VAL n 
1 3   ILE n 
1 4   LYS n 
1 5   MET n 
1 6   LYS n 
1 7   SER n 
1 8   SER n 
1 9   ASP n 
1 10  PHE n 
1 11  LEU n 
1 12  GLU n 
1 13  SER n 
1 14  ALA n 
1 15  GLU n 
1 16  LEU n 
1 17  ASP n 
1 18  SER n 
1 19  GLY n 
1 20  GLY n 
1 21  PHE n 
1 22  GLY n 
1 23  LYS n 
1 24  VAL n 
1 25  SER n 
1 26  LEU n 
1 27  ALA n 
1 28  PHE n 
1 29  HIS n 
1 30  ARG n 
1 31  THR n 
1 32  GLN n 
1 33  GLY n 
1 34  LEU n 
1 35  MET n 
1 36  ILE n 
1 37  MET n 
1 38  LYS n 
1 39  THR n 
1 40  VAL n 
1 41  TYR n 
1 42  LYS n 
1 43  GLY n 
1 44  PRO n 
1 45  ASN n 
1 46  CYS n 
1 47  ILE n 
1 48  GLU n 
1 49  HIS n 
1 50  ASN n 
1 51  GLU n 
1 52  ALA n 
1 53  LEU n 
1 54  LEU n 
1 55  GLU n 
1 56  GLU n 
1 57  ALA n 
1 58  LYS n 
1 59  MET n 
1 60  MET n 
1 61  ASN n 
1 62  ARG n 
1 63  LEU n 
1 64  ARG n 
1 65  HIS n 
1 66  SER n 
1 67  ARG n 
1 68  VAL n 
1 69  VAL n 
1 70  LYS n 
1 71  LEU n 
1 72  LEU n 
1 73  GLY n 
1 74  VAL n 
1 75  ILE n 
1 76  ILE n 
1 77  GLU n 
1 78  GLU n 
1 79  GLY n 
1 80  LYS n 
1 81  TYR n 
1 82  SER n 
1 83  LEU n 
1 84  VAL n 
1 85  MET n 
1 86  GLU n 
1 87  TYR n 
1 88  MET n 
1 89  GLU n 
1 90  LYS n 
1 91  GLY n 
1 92  ASN n 
1 93  LEU n 
1 94  MET n 
1 95  HIS n 
1 96  VAL n 
1 97  LEU n 
1 98  LYS n 
1 99  ALA n 
1 100 GLU n 
1 101 MET n 
1 102 SER n 
1 103 THR n 
1 104 PRO n 
1 105 LEU n 
1 106 SER n 
1 107 VAL n 
1 108 LYS n 
1 109 GLY n 
1 110 ARG n 
1 111 ILE n 
1 112 ILE n 
1 113 LEU n 
1 114 GLU n 
1 115 ILE n 
1 116 ILE n 
1 117 GLU n 
1 118 GLY n 
1 119 MET n 
1 120 ALA n 
1 121 TYR n 
1 122 LEU n 
1 123 HIS n 
1 124 GLY n 
1 125 LYS n 
1 126 GLY n 
1 127 VAL n 
1 128 ILE n 
1 129 HIS n 
1 130 LYS n 
1 131 ASP n 
1 132 LEU n 
1 133 LYS n 
1 134 PRO n 
1 135 GLU n 
1 136 ASN n 
1 137 ILE n 
1 138 LEU n 
1 139 VAL n 
1 140 ASP n 
1 141 ASN n 
1 142 ASP n 
1 143 PHE n 
1 144 HIS n 
1 145 ILE n 
1 146 LYS n 
1 147 ILE n 
1 148 ALA n 
1 149 ASP n 
1 150 LEU n 
1 151 GLY n 
1 152 LEU n 
1 153 ALA n 
1 154 SER n 
1 155 PHE n 
1 156 LYS n 
1 157 MET n 
1 158 TRP n 
1 159 SER n 
1 160 LYS n 
1 161 LEU n 
1 162 ASN n 
1 163 ASN n 
1 164 GLU n 
1 165 GLU n 
1 166 HIS n 
1 167 ASN n 
1 168 GLU n 
1 169 LEU n 
1 170 ARG n 
1 171 GLU n 
1 172 VAL n 
1 173 ASP n 
1 174 GLY n 
1 175 THR n 
1 176 ALA n 
1 177 LYS n 
1 178 LYS n 
1 179 ASN n 
1 180 GLY n 
1 181 GLY n 
1 182 THR n 
1 183 LEU n 
1 184 TYR n 
1 185 TYR n 
1 186 MET n 
1 187 ALA n 
1 188 PRO n 
1 189 GLU n 
1 190 HIS n 
1 191 LEU n 
1 192 ASN n 
1 193 ASP n 
1 194 VAL n 
1 195 ASN n 
1 196 ALA n 
1 197 LYS n 
1 198 PRO n 
1 199 THR n 
1 200 GLU n 
1 201 LYS n 
1 202 SER n 
1 203 ASP n 
1 204 VAL n 
1 205 TYR n 
1 206 SER n 
1 207 PHE n 
1 208 ALA n 
1 209 VAL n 
1 210 VAL n 
1 211 LEU n 
1 212 TRP n 
1 213 ALA n 
1 214 ILE n 
1 215 PHE n 
1 216 ALA n 
1 217 ASN n 
1 218 LYS n 
1 219 GLU n 
1 220 PRO n 
1 221 TYR n 
1 222 GLU n 
1 223 ASN n 
1 224 ALA n 
1 225 ILE n 
1 226 ALA n 
1 227 GLU n 
1 228 GLN n 
1 229 GLN n 
1 230 LEU n 
1 231 ILE n 
1 232 MET n 
1 233 ALA n 
1 234 ILE n 
1 235 LYS n 
1 236 SER n 
1 237 GLY n 
1 238 ASN n 
1 239 ARG n 
1 240 PRO n 
1 241 ASP n 
1 242 VAL n 
1 243 ASP n 
1 244 ASP n 
1 245 ILE n 
1 246 THR n 
1 247 GLU n 
1 248 TYR n 
1 249 CYS n 
1 250 PRO n 
1 251 ARG n 
1 252 GLU n 
1 253 ILE n 
1 254 ILE n 
1 255 SER n 
1 256 LEU n 
1 257 MET n 
1 258 LYS n 
1 259 LEU n 
1 260 CYS n 
1 261 TRP n 
1 262 GLU n 
1 263 ALA n 
1 264 ASN n 
1 265 PRO n 
1 266 GLU n 
1 267 ALA n 
1 268 ARG n 
1 269 PRO n 
1 270 THR n 
1 271 PHE n 
1 272 PRO n 
1 273 GLY n 
1 274 ILE n 
1 275 GLU n 
1 276 GLU n 
1 277 LYS n 
1 278 PHE n 
1 279 ARG n 
1 280 PRO n 
1 281 PHE n 
1 282 TYR n 
1 283 LEU n 
1 284 SER n 
1 285 GLN n 
1 286 LEU n 
1 287 GLU 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                   287 
_entity_src_gen.gene_src_common_name               human 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 'RIPK1, RIP, RIP1' 
_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      'Spodoptera frugiperda' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     7108 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          ? 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       ? 
_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 
A1BU6 non-polymer         . '1-[(2S,5S)-2,3-dihydro-2,5-methano-1,4-benzoxazepin-4(5H)-yl]-3,3-difluoro-2,2-dimethylpropan-1-one' 
? 'C15 H17 F2 N O2' 281.298 
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 
CL    non-polymer         . 'CHLORIDE ION'                                                                                        
? 'Cl -1'           35.453  
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 
IOD   non-polymer         . 'IODIDE ION'                                                                                          
? 'I -1'            126.904 
LEU   'L-peptide linking' y LEUCINE                                                                                               
? 'C6 H13 N O2'     131.173 
LYS   'L-peptide linking' y LYSINE                                                                                                
? 'C6 H15 N2 O2 1'  147.195 
MET   'L-peptide linking' y METHIONINE                                                                                            
? 'C5 H11 N O2 S'   149.211 
PHE   'L-peptide linking' y PHENYLALANINE                                                                                         
? 'C9 H11 N O2'     165.189 
PRO   'L-peptide linking' y PROLINE                                                                                               
? 'C5 H9 N O2'      115.130 
SER   'L-peptide linking' y SERINE                                                                                                
? 'C3 H7 N O3'      105.093 
THR   'L-peptide linking' y THREONINE                                                                                             
? 'C4 H9 N O3'      119.119 
TRP   'L-peptide linking' y TRYPTOPHAN                                                                                            
? 'C11 H12 N2 O2'   204.225 
TYR   'L-peptide linking' y TYROSINE                                                                                              
? 'C9 H11 N O3'     181.189 
VAL   'L-peptide linking' y VALINE                                                                                                
? 'C5 H11 N O2'     117.146 
# 
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   ASN 1   8   8   ASN ASN A . n 
A 1 2   VAL 2   9   9   VAL VAL A . n 
A 1 3   ILE 3   10  10  ILE ILE A . n 
A 1 4   LYS 4   11  11  LYS LYS A . n 
A 1 5   MET 5   12  12  MET MET A . n 
A 1 6   LYS 6   13  13  LYS LYS A . n 
A 1 7   SER 7   14  14  SER SER A . n 
A 1 8   SER 8   15  15  SER SER A . n 
A 1 9   ASP 9   16  16  ASP ASP A . n 
A 1 10  PHE 10  17  17  PHE PHE A . n 
A 1 11  LEU 11  18  18  LEU LEU A . n 
A 1 12  GLU 12  19  19  GLU GLU A . n 
A 1 13  SER 13  20  ?   ?   ?   A . n 
A 1 14  ALA 14  21  ?   ?   ?   A . n 
A 1 15  GLU 15  22  ?   ?   ?   A . n 
A 1 16  LEU 16  23  ?   ?   ?   A . n 
A 1 17  ASP 17  24  ?   ?   ?   A . n 
A 1 18  SER 18  25  ?   ?   ?   A . n 
A 1 19  GLY 19  26  ?   ?   ?   A . n 
A 1 20  GLY 20  27  ?   ?   ?   A . n 
A 1 21  PHE 21  28  ?   ?   ?   A . n 
A 1 22  GLY 22  29  ?   ?   ?   A . n 
A 1 23  LYS 23  30  30  LYS LYS A . n 
A 1 24  VAL 24  31  31  VAL VAL A . n 
A 1 25  SER 25  32  32  SER SER A . n 
A 1 26  LEU 26  33  33  LEU LEU A . n 
A 1 27  ALA 27  34  34  ALA ALA A . n 
A 1 28  PHE 28  35  35  PHE PHE A . n 
A 1 29  HIS 29  36  36  HIS HIS A . n 
A 1 30  ARG 30  37  37  ARG ARG A . n 
A 1 31  THR 31  38  38  THR THR A . n 
A 1 32  GLN 32  39  39  GLN GLN A . n 
A 1 33  GLY 33  40  40  GLY GLY A . n 
A 1 34  LEU 34  41  41  LEU LEU A . n 
A 1 35  MET 35  42  42  MET MET A . n 
A 1 36  ILE 36  43  43  ILE ILE A . n 
A 1 37  MET 37  44  44  MET MET A . n 
A 1 38  LYS 38  45  45  LYS LYS A . n 
A 1 39  THR 39  46  46  THR THR A . n 
A 1 40  VAL 40  47  47  VAL VAL A . n 
A 1 41  TYR 41  48  48  TYR TYR A . n 
A 1 42  LYS 42  49  49  LYS LYS A . n 
A 1 43  GLY 43  50  50  GLY GLY A . n 
A 1 44  PRO 44  51  51  PRO PRO A . n 
A 1 45  ASN 45  52  52  ASN ASN A . n 
A 1 46  CYS 46  53  53  CYS CYS A . n 
A 1 47  ILE 47  54  54  ILE ILE A . n 
A 1 48  GLU 48  55  55  GLU GLU A . n 
A 1 49  HIS 49  56  56  HIS HIS A . n 
A 1 50  ASN 50  57  57  ASN ASN A . n 
A 1 51  GLU 51  58  58  GLU GLU A . n 
A 1 52  ALA 52  59  59  ALA ALA A . n 
A 1 53  LEU 53  60  60  LEU LEU A . n 
A 1 54  LEU 54  61  61  LEU LEU A . n 
A 1 55  GLU 55  62  62  GLU GLU A . n 
A 1 56  GLU 56  63  63  GLU GLU A . n 
A 1 57  ALA 57  64  64  ALA ALA A . n 
A 1 58  LYS 58  65  65  LYS LYS A . n 
A 1 59  MET 59  66  66  MET MET A . n 
A 1 60  MET 60  67  67  MET MET A . n 
A 1 61  ASN 61  68  68  ASN ASN A . n 
A 1 62  ARG 62  69  69  ARG ARG A . n 
A 1 63  LEU 63  70  70  LEU LEU A . n 
A 1 64  ARG 64  71  71  ARG ARG A . n 
A 1 65  HIS 65  72  72  HIS HIS A . n 
A 1 66  SER 66  73  73  SER SER A . n 
A 1 67  ARG 67  74  74  ARG ARG A . n 
A 1 68  VAL 68  75  75  VAL VAL A . n 
A 1 69  VAL 69  76  76  VAL VAL A . n 
A 1 70  LYS 70  77  77  LYS LYS A . n 
A 1 71  LEU 71  78  78  LEU LEU A . n 
A 1 72  LEU 72  79  79  LEU LEU A . n 
A 1 73  GLY 73  80  80  GLY GLY A . n 
A 1 74  VAL 74  81  81  VAL VAL A . n 
A 1 75  ILE 75  82  82  ILE ILE A . n 
A 1 76  ILE 76  83  83  ILE ILE A . n 
A 1 77  GLU 77  84  84  GLU GLU A . n 
A 1 78  GLU 78  85  85  GLU GLU A . n 
A 1 79  GLY 79  86  86  GLY GLY A . n 
A 1 80  LYS 80  87  87  LYS LYS A . n 
A 1 81  TYR 81  88  88  TYR TYR A . n 
A 1 82  SER 82  89  89  SER SER A . n 
A 1 83  LEU 83  90  90  LEU LEU A . n 
A 1 84  VAL 84  91  91  VAL VAL A . n 
A 1 85  MET 85  92  92  MET MET A . n 
A 1 86  GLU 86  93  93  GLU GLU A . n 
A 1 87  TYR 87  94  94  TYR TYR A . n 
A 1 88  MET 88  95  95  MET MET A . n 
A 1 89  GLU 89  96  96  GLU GLU A . n 
A 1 90  LYS 90  97  97  LYS LYS A . n 
A 1 91  GLY 91  98  98  GLY GLY A . n 
A 1 92  ASN 92  99  99  ASN ASN A . n 
A 1 93  LEU 93  100 100 LEU LEU A . n 
A 1 94  MET 94  101 101 MET MET A . n 
A 1 95  HIS 95  102 102 HIS HIS A . n 
A 1 96  VAL 96  103 103 VAL VAL A . n 
A 1 97  LEU 97  104 104 LEU LEU A . n 
A 1 98  LYS 98  105 105 LYS LYS A . n 
A 1 99  ALA 99  106 106 ALA ALA A . n 
A 1 100 GLU 100 107 107 GLU GLU A . n 
A 1 101 MET 101 108 108 MET MET A . n 
A 1 102 SER 102 109 109 SER SER A . n 
A 1 103 THR 103 110 110 THR THR A . n 
A 1 104 PRO 104 111 111 PRO PRO A . n 
A 1 105 LEU 105 112 112 LEU LEU A . n 
A 1 106 SER 106 113 113 SER SER A . n 
A 1 107 VAL 107 114 114 VAL VAL A . n 
A 1 108 LYS 108 115 115 LYS LYS A . n 
A 1 109 GLY 109 116 116 GLY GLY A . n 
A 1 110 ARG 110 117 117 ARG ARG A . n 
A 1 111 ILE 111 118 118 ILE ILE A . n 
A 1 112 ILE 112 119 119 ILE ILE A . n 
A 1 113 LEU 113 120 120 LEU LEU A . n 
A 1 114 GLU 114 121 121 GLU GLU A . n 
A 1 115 ILE 115 122 122 ILE ILE A . n 
A 1 116 ILE 116 123 123 ILE ILE A . n 
A 1 117 GLU 117 124 124 GLU GLU A . n 
A 1 118 GLY 118 125 125 GLY GLY A . n 
A 1 119 MET 119 126 126 MET MET A . n 
A 1 120 ALA 120 127 127 ALA ALA A . n 
A 1 121 TYR 121 128 128 TYR TYR A . n 
A 1 122 LEU 122 129 129 LEU LEU A . n 
A 1 123 HIS 123 130 130 HIS HIS A . n 
A 1 124 GLY 124 131 131 GLY GLY A . n 
A 1 125 LYS 125 132 132 LYS LYS A . n 
A 1 126 GLY 126 133 133 GLY GLY A . n 
A 1 127 VAL 127 134 134 VAL VAL A . n 
A 1 128 ILE 128 135 135 ILE ILE A . n 
A 1 129 HIS 129 136 136 HIS HIS A . n 
A 1 130 LYS 130 137 137 LYS LYS A . n 
A 1 131 ASP 131 138 138 ASP ASP A . n 
A 1 132 LEU 132 139 139 LEU LEU A . n 
A 1 133 LYS 133 140 140 LYS LYS A . n 
A 1 134 PRO 134 141 141 PRO PRO A . n 
A 1 135 GLU 135 142 142 GLU GLU A . n 
A 1 136 ASN 136 143 143 ASN ASN A . n 
A 1 137 ILE 137 144 144 ILE ILE A . n 
A 1 138 LEU 138 145 145 LEU LEU A . n 
A 1 139 VAL 139 146 146 VAL VAL A . n 
A 1 140 ASP 140 147 147 ASP ASP A . n 
A 1 141 ASN 141 148 148 ASN ASN A . n 
A 1 142 ASP 142 149 149 ASP ASP A . n 
A 1 143 PHE 143 150 150 PHE PHE A . n 
A 1 144 HIS 144 151 151 HIS HIS A . n 
A 1 145 ILE 145 152 152 ILE ILE A . n 
A 1 146 LYS 146 153 153 LYS LYS A . n 
A 1 147 ILE 147 154 154 ILE ILE A . n 
A 1 148 ALA 148 155 155 ALA ALA A . n 
A 1 149 ASP 149 156 156 ASP ASP A . n 
A 1 150 LEU 150 157 157 LEU LEU A . n 
A 1 151 GLY 151 158 158 GLY GLY A . n 
A 1 152 LEU 152 159 159 LEU LEU A . n 
A 1 153 ALA 153 160 160 ALA ALA A . n 
A 1 154 SER 154 161 161 SER SER A . n 
A 1 155 PHE 155 162 162 PHE PHE A . n 
A 1 156 LYS 156 163 163 LYS LYS A . n 
A 1 157 MET 157 164 164 MET MET A . n 
A 1 158 TRP 158 165 165 TRP TRP A . n 
A 1 159 SER 159 166 166 SER SER A . n 
A 1 160 LYS 160 167 167 LYS LYS A . n 
A 1 161 LEU 161 168 168 LEU LEU A . n 
A 1 162 ASN 162 169 169 ASN ASN A . n 
A 1 163 ASN 163 170 170 ASN ASN A . n 
A 1 164 GLU 164 171 171 GLU GLU A . n 
A 1 165 GLU 165 172 172 GLU GLU A . n 
A 1 166 HIS 166 173 173 HIS HIS A . n 
A 1 167 ASN 167 174 174 ASN ASN A . n 
A 1 168 GLU 168 175 175 GLU GLU A . n 
A 1 169 LEU 169 176 176 LEU LEU A . n 
A 1 170 ARG 170 177 ?   ?   ?   A . n 
A 1 171 GLU 171 178 ?   ?   ?   A . n 
A 1 172 VAL 172 179 ?   ?   ?   A . n 
A 1 173 ASP 173 180 ?   ?   ?   A . n 
A 1 174 GLY 174 181 ?   ?   ?   A . n 
A 1 175 THR 175 182 ?   ?   ?   A . n 
A 1 176 ALA 176 183 ?   ?   ?   A . n 
A 1 177 LYS 177 184 ?   ?   ?   A . n 
A 1 178 LYS 178 185 ?   ?   ?   A . n 
A 1 179 ASN 179 186 ?   ?   ?   A . n 
A 1 180 GLY 180 187 ?   ?   ?   A . n 
A 1 181 GLY 181 188 188 GLY GLY A . n 
A 1 182 THR 182 189 189 THR THR A . n 
A 1 183 LEU 183 190 190 LEU LEU A . n 
A 1 184 TYR 184 191 191 TYR TYR A . n 
A 1 185 TYR 185 192 192 TYR TYR A . n 
A 1 186 MET 186 193 193 MET MET A . n 
A 1 187 ALA 187 194 194 ALA ALA A . n 
A 1 188 PRO 188 195 195 PRO PRO A . n 
A 1 189 GLU 189 196 196 GLU GLU A . n 
A 1 190 HIS 190 197 197 HIS HIS A . n 
A 1 191 LEU 191 198 198 LEU LEU A . n 
A 1 192 ASN 192 199 199 ASN ASN A . n 
A 1 193 ASP 193 200 200 ASP ASP A . n 
A 1 194 VAL 194 201 201 VAL VAL A . n 
A 1 195 ASN 195 202 202 ASN ASN A . n 
A 1 196 ALA 196 203 203 ALA ALA A . n 
A 1 197 LYS 197 204 204 LYS LYS A . n 
A 1 198 PRO 198 205 205 PRO PRO A . n 
A 1 199 THR 199 206 206 THR THR A . n 
A 1 200 GLU 200 207 207 GLU GLU A . n 
A 1 201 LYS 201 208 208 LYS LYS A . n 
A 1 202 SER 202 209 209 SER SER A . n 
A 1 203 ASP 203 210 210 ASP ASP A . n 
A 1 204 VAL 204 211 211 VAL VAL A . n 
A 1 205 TYR 205 212 212 TYR TYR A . n 
A 1 206 SER 206 213 213 SER SER A . n 
A 1 207 PHE 207 214 214 PHE PHE A . n 
A 1 208 ALA 208 215 215 ALA ALA A . n 
A 1 209 VAL 209 216 216 VAL VAL A . n 
A 1 210 VAL 210 217 217 VAL VAL A . n 
A 1 211 LEU 211 218 218 LEU LEU A . n 
A 1 212 TRP 212 219 219 TRP TRP A . n 
A 1 213 ALA 213 220 220 ALA ALA A . n 
A 1 214 ILE 214 221 221 ILE ILE A . n 
A 1 215 PHE 215 222 222 PHE PHE A . n 
A 1 216 ALA 216 223 223 ALA ALA A . n 
A 1 217 ASN 217 224 224 ASN ASN A . n 
A 1 218 LYS 218 225 225 LYS LYS A . n 
A 1 219 GLU 219 226 226 GLU GLU A . n 
A 1 220 PRO 220 227 227 PRO PRO A . n 
A 1 221 TYR 221 228 228 TYR TYR A . n 
A 1 222 GLU 222 229 229 GLU GLU A . n 
A 1 223 ASN 223 230 230 ASN ASN A . n 
A 1 224 ALA 224 231 231 ALA ALA A . n 
A 1 225 ILE 225 232 232 ILE ILE A . n 
A 1 226 ALA 226 233 233 ALA ALA A . n 
A 1 227 GLU 227 234 234 GLU GLU A . n 
A 1 228 GLN 228 235 235 GLN GLN A . n 
A 1 229 GLN 229 236 236 GLN GLN A . n 
A 1 230 LEU 230 237 237 LEU LEU A . n 
A 1 231 ILE 231 238 238 ILE ILE A . n 
A 1 232 MET 232 239 239 MET MET A . n 
A 1 233 ALA 233 240 240 ALA ALA A . n 
A 1 234 ILE 234 241 241 ILE ILE A . n 
A 1 235 LYS 235 242 242 LYS LYS A . n 
A 1 236 SER 236 243 243 SER SER A . n 
A 1 237 GLY 237 244 244 GLY GLY A . n 
A 1 238 ASN 238 245 245 ASN ASN A . n 
A 1 239 ARG 239 246 246 ARG ARG A . n 
A 1 240 PRO 240 247 247 PRO PRO A . n 
A 1 241 ASP 241 248 248 ASP ASP A . n 
A 1 242 VAL 242 249 249 VAL VAL A . n 
A 1 243 ASP 243 250 250 ASP ASP A . n 
A 1 244 ASP 244 251 251 ASP ASP A . n 
A 1 245 ILE 245 252 252 ILE ILE A . n 
A 1 246 THR 246 253 253 THR THR A . n 
A 1 247 GLU 247 254 254 GLU GLU A . n 
A 1 248 TYR 248 255 255 TYR TYR A . n 
A 1 249 CYS 249 256 256 CYS CYS A . n 
A 1 250 PRO 250 257 257 PRO PRO A . n 
A 1 251 ARG 251 258 258 ARG ARG A . n 
A 1 252 GLU 252 259 259 GLU GLU A . n 
A 1 253 ILE 253 260 260 ILE ILE A . n 
A 1 254 ILE 254 261 261 ILE ILE A . n 
A 1 255 SER 255 262 262 SER SER A . n 
A 1 256 LEU 256 263 263 LEU LEU A . n 
A 1 257 MET 257 264 264 MET MET A . n 
A 1 258 LYS 258 265 265 LYS LYS A . n 
A 1 259 LEU 259 266 266 LEU LEU A . n 
A 1 260 CYS 260 267 267 CYS CYS A . n 
A 1 261 TRP 261 268 268 TRP TRP A . n 
A 1 262 GLU 262 269 269 GLU GLU A . n 
A 1 263 ALA 263 270 270 ALA ALA A . n 
A 1 264 ASN 264 271 271 ASN ASN A . n 
A 1 265 PRO 265 272 272 PRO PRO A . n 
A 1 266 GLU 266 273 273 GLU GLU A . n 
A 1 267 ALA 267 274 274 ALA ALA A . n 
A 1 268 ARG 268 275 275 ARG ARG A . n 
A 1 269 PRO 269 276 276 PRO PRO A . n 
A 1 270 THR 270 277 277 THR THR A . n 
A 1 271 PHE 271 278 278 PHE PHE A . n 
A 1 272 PRO 272 279 279 PRO PRO A . n 
A 1 273 GLY 273 280 280 GLY GLY A . n 
A 1 274 ILE 274 281 281 ILE ILE A . n 
A 1 275 GLU 275 282 282 GLU GLU A . n 
A 1 276 GLU 276 283 283 GLU GLU A . n 
A 1 277 LYS 277 284 284 LYS LYS A . n 
A 1 278 PHE 278 285 285 PHE PHE A . n 
A 1 279 ARG 279 286 286 ARG ARG A . n 
A 1 280 PRO 280 287 287 PRO PRO A . n 
A 1 281 PHE 281 288 288 PHE PHE A . n 
A 1 282 TYR 282 289 289 TYR TYR A . n 
A 1 283 LEU 283 290 290 LEU LEU A . n 
A 1 284 SER 284 291 291 SER SER A . n 
A 1 285 GLN 285 292 292 GLN GLN A . n 
A 1 286 LEU 286 293 293 LEU LEU A . n 
A 1 287 GLU 287 294 294 GLU GLU A . n 
B 1 1   ASN 1   8   8   ASN ASN B . n 
B 1 2   VAL 2   9   9   VAL VAL B . n 
B 1 3   ILE 3   10  10  ILE ILE B . n 
B 1 4   LYS 4   11  11  LYS LYS B . n 
B 1 5   MET 5   12  12  MET MET B . n 
B 1 6   LYS 6   13  13  LYS LYS B . n 
B 1 7   SER 7   14  14  SER SER B . n 
B 1 8   SER 8   15  15  SER SER B . n 
B 1 9   ASP 9   16  16  ASP ASP B . n 
B 1 10  PHE 10  17  17  PHE PHE B . n 
B 1 11  LEU 11  18  18  LEU LEU B . n 
B 1 12  GLU 12  19  19  GLU GLU B . n 
B 1 13  SER 13  20  20  SER SER B . n 
B 1 14  ALA 14  21  21  ALA ALA B . n 
B 1 15  GLU 15  22  22  GLU GLU B . n 
B 1 16  LEU 16  23  23  LEU LEU B . n 
B 1 17  ASP 17  24  24  ASP ASP B . n 
B 1 18  SER 18  25  25  SER SER B . n 
B 1 19  GLY 19  26  ?   ?   ?   B . n 
B 1 20  GLY 20  27  ?   ?   ?   B . n 
B 1 21  PHE 21  28  ?   ?   ?   B . n 
B 1 22  GLY 22  29  ?   ?   ?   B . n 
B 1 23  LYS 23  30  30  LYS LYS B . n 
B 1 24  VAL 24  31  31  VAL VAL B . n 
B 1 25  SER 25  32  32  SER SER B . n 
B 1 26  LEU 26  33  33  LEU LEU B . n 
B 1 27  ALA 27  34  34  ALA ALA B . n 
B 1 28  PHE 28  35  35  PHE PHE B . n 
B 1 29  HIS 29  36  36  HIS HIS B . n 
B 1 30  ARG 30  37  37  ARG ARG B . n 
B 1 31  THR 31  38  38  THR THR B . n 
B 1 32  GLN 32  39  39  GLN GLN B . n 
B 1 33  GLY 33  40  40  GLY GLY B . n 
B 1 34  LEU 34  41  41  LEU LEU B . n 
B 1 35  MET 35  42  42  MET MET B . n 
B 1 36  ILE 36  43  43  ILE ILE B . n 
B 1 37  MET 37  44  44  MET MET B . n 
B 1 38  LYS 38  45  45  LYS LYS B . n 
B 1 39  THR 39  46  46  THR THR B . n 
B 1 40  VAL 40  47  47  VAL VAL B . n 
B 1 41  TYR 41  48  48  TYR TYR B . n 
B 1 42  LYS 42  49  49  LYS LYS B . n 
B 1 43  GLY 43  50  50  GLY GLY B . n 
B 1 44  PRO 44  51  51  PRO PRO B . n 
B 1 45  ASN 45  52  52  ASN ASN B . n 
B 1 46  CYS 46  53  53  CYS CYS B . n 
B 1 47  ILE 47  54  54  ILE ILE B . n 
B 1 48  GLU 48  55  55  GLU GLU B . n 
B 1 49  HIS 49  56  56  HIS HIS B . n 
B 1 50  ASN 50  57  57  ASN ASN B . n 
B 1 51  GLU 51  58  58  GLU GLU B . n 
B 1 52  ALA 52  59  59  ALA ALA B . n 
B 1 53  LEU 53  60  60  LEU LEU B . n 
B 1 54  LEU 54  61  61  LEU LEU B . n 
B 1 55  GLU 55  62  62  GLU GLU B . n 
B 1 56  GLU 56  63  63  GLU GLU B . n 
B 1 57  ALA 57  64  64  ALA ALA B . n 
B 1 58  LYS 58  65  65  LYS LYS B . n 
B 1 59  MET 59  66  66  MET MET B . n 
B 1 60  MET 60  67  67  MET MET B . n 
B 1 61  ASN 61  68  68  ASN ASN B . n 
B 1 62  ARG 62  69  69  ARG ARG B . n 
B 1 63  LEU 63  70  70  LEU LEU B . n 
B 1 64  ARG 64  71  71  ARG ARG B . n 
B 1 65  HIS 65  72  72  HIS HIS B . n 
B 1 66  SER 66  73  73  SER SER B . n 
B 1 67  ARG 67  74  74  ARG ARG B . n 
B 1 68  VAL 68  75  75  VAL VAL B . n 
B 1 69  VAL 69  76  76  VAL VAL B . n 
B 1 70  LYS 70  77  77  LYS LYS B . n 
B 1 71  LEU 71  78  78  LEU LEU B . n 
B 1 72  LEU 72  79  79  LEU LEU B . n 
B 1 73  GLY 73  80  80  GLY GLY B . n 
B 1 74  VAL 74  81  81  VAL VAL B . n 
B 1 75  ILE 75  82  82  ILE ILE B . n 
B 1 76  ILE 76  83  83  ILE ILE B . n 
B 1 77  GLU 77  84  84  GLU GLU B . n 
B 1 78  GLU 78  85  85  GLU GLU B . n 
B 1 79  GLY 79  86  86  GLY GLY B . n 
B 1 80  LYS 80  87  87  LYS LYS B . n 
B 1 81  TYR 81  88  88  TYR TYR B . n 
B 1 82  SER 82  89  89  SER SER B . n 
B 1 83  LEU 83  90  90  LEU LEU B . n 
B 1 84  VAL 84  91  91  VAL VAL B . n 
B 1 85  MET 85  92  92  MET MET B . n 
B 1 86  GLU 86  93  93  GLU GLU B . n 
B 1 87  TYR 87  94  94  TYR TYR B . n 
B 1 88  MET 88  95  95  MET MET B . n 
B 1 89  GLU 89  96  96  GLU GLU B . n 
B 1 90  LYS 90  97  97  LYS LYS B . n 
B 1 91  GLY 91  98  98  GLY GLY B . n 
B 1 92  ASN 92  99  99  ASN ASN B . n 
B 1 93  LEU 93  100 100 LEU LEU B . n 
B 1 94  MET 94  101 101 MET MET B . n 
B 1 95  HIS 95  102 102 HIS HIS B . n 
B 1 96  VAL 96  103 103 VAL VAL B . n 
B 1 97  LEU 97  104 104 LEU LEU B . n 
B 1 98  LYS 98  105 105 LYS LYS B . n 
B 1 99  ALA 99  106 106 ALA ALA B . n 
B 1 100 GLU 100 107 107 GLU GLU B . n 
B 1 101 MET 101 108 108 MET MET B . n 
B 1 102 SER 102 109 109 SER SER B . n 
B 1 103 THR 103 110 110 THR THR B . n 
B 1 104 PRO 104 111 111 PRO PRO B . n 
B 1 105 LEU 105 112 112 LEU LEU B . n 
B 1 106 SER 106 113 113 SER SER B . n 
B 1 107 VAL 107 114 114 VAL VAL B . n 
B 1 108 LYS 108 115 115 LYS LYS B . n 
B 1 109 GLY 109 116 116 GLY GLY B . n 
B 1 110 ARG 110 117 117 ARG ARG B . n 
B 1 111 ILE 111 118 118 ILE ILE B . n 
B 1 112 ILE 112 119 119 ILE ILE B . n 
B 1 113 LEU 113 120 120 LEU LEU B . n 
B 1 114 GLU 114 121 121 GLU GLU B . n 
B 1 115 ILE 115 122 122 ILE ILE B . n 
B 1 116 ILE 116 123 123 ILE ILE B . n 
B 1 117 GLU 117 124 124 GLU GLU B . n 
B 1 118 GLY 118 125 125 GLY GLY B . n 
B 1 119 MET 119 126 126 MET MET B . n 
B 1 120 ALA 120 127 127 ALA ALA B . n 
B 1 121 TYR 121 128 128 TYR TYR B . n 
B 1 122 LEU 122 129 129 LEU LEU B . n 
B 1 123 HIS 123 130 130 HIS HIS B . n 
B 1 124 GLY 124 131 131 GLY GLY B . n 
B 1 125 LYS 125 132 132 LYS LYS B . n 
B 1 126 GLY 126 133 133 GLY GLY B . n 
B 1 127 VAL 127 134 134 VAL VAL B . n 
B 1 128 ILE 128 135 135 ILE ILE B . n 
B 1 129 HIS 129 136 136 HIS HIS B . n 
B 1 130 LYS 130 137 137 LYS LYS B . n 
B 1 131 ASP 131 138 138 ASP ASP B . n 
B 1 132 LEU 132 139 139 LEU LEU B . n 
B 1 133 LYS 133 140 140 LYS LYS B . n 
B 1 134 PRO 134 141 141 PRO PRO B . n 
B 1 135 GLU 135 142 142 GLU GLU B . n 
B 1 136 ASN 136 143 143 ASN ASN B . n 
B 1 137 ILE 137 144 144 ILE ILE B . n 
B 1 138 LEU 138 145 145 LEU LEU B . n 
B 1 139 VAL 139 146 146 VAL VAL B . n 
B 1 140 ASP 140 147 147 ASP ASP B . n 
B 1 141 ASN 141 148 148 ASN ASN B . n 
B 1 142 ASP 142 149 149 ASP ASP B . n 
B 1 143 PHE 143 150 150 PHE PHE B . n 
B 1 144 HIS 144 151 151 HIS HIS B . n 
B 1 145 ILE 145 152 152 ILE ILE B . n 
B 1 146 LYS 146 153 153 LYS LYS B . n 
B 1 147 ILE 147 154 154 ILE ILE B . n 
B 1 148 ALA 148 155 155 ALA ALA B . n 
B 1 149 ASP 149 156 156 ASP ASP B . n 
B 1 150 LEU 150 157 157 LEU LEU B . n 
B 1 151 GLY 151 158 158 GLY GLY B . n 
B 1 152 LEU 152 159 159 LEU LEU B . n 
B 1 153 ALA 153 160 160 ALA ALA B . n 
B 1 154 SER 154 161 161 SER SER B . n 
B 1 155 PHE 155 162 162 PHE PHE B . n 
B 1 156 LYS 156 163 163 LYS LYS B . n 
B 1 157 MET 157 164 164 MET MET B . n 
B 1 158 TRP 158 165 165 TRP TRP B . n 
B 1 159 SER 159 166 166 SER SER B . n 
B 1 160 LYS 160 167 167 LYS LYS B . n 
B 1 161 LEU 161 168 168 LEU LEU B . n 
B 1 162 ASN 162 169 169 ASN ASN B . n 
B 1 163 ASN 163 170 170 ASN ASN B . n 
B 1 164 GLU 164 171 171 GLU GLU B . n 
B 1 165 GLU 165 172 172 GLU GLU B . n 
B 1 166 HIS 166 173 173 HIS HIS B . n 
B 1 167 ASN 167 174 174 ASN ASN B . n 
B 1 168 GLU 168 175 175 GLU GLU B . n 
B 1 169 LEU 169 176 176 LEU LEU B . n 
B 1 170 ARG 170 177 177 ARG ARG B . n 
B 1 171 GLU 171 178 178 GLU GLU B . n 
B 1 172 VAL 172 179 179 VAL VAL B . n 
B 1 173 ASP 173 180 180 ASP ASP B . n 
B 1 174 GLY 174 181 ?   ?   ?   B . n 
B 1 175 THR 175 182 ?   ?   ?   B . n 
B 1 176 ALA 176 183 ?   ?   ?   B . n 
B 1 177 LYS 177 184 ?   ?   ?   B . n 
B 1 178 LYS 178 185 ?   ?   ?   B . n 
B 1 179 ASN 179 186 ?   ?   ?   B . n 
B 1 180 GLY 180 187 ?   ?   ?   B . n 
B 1 181 GLY 181 188 188 GLY GLY B . n 
B 1 182 THR 182 189 189 THR THR B . n 
B 1 183 LEU 183 190 190 LEU LEU B . n 
B 1 184 TYR 184 191 191 TYR TYR B . n 
B 1 185 TYR 185 192 192 TYR TYR B . n 
B 1 186 MET 186 193 193 MET MET B . n 
B 1 187 ALA 187 194 194 ALA ALA B . n 
B 1 188 PRO 188 195 195 PRO PRO B . n 
B 1 189 GLU 189 196 196 GLU GLU B . n 
B 1 190 HIS 190 197 197 HIS HIS B . n 
B 1 191 LEU 191 198 198 LEU LEU B . n 
B 1 192 ASN 192 199 199 ASN ASN B . n 
B 1 193 ASP 193 200 200 ASP ASP B . n 
B 1 194 VAL 194 201 201 VAL VAL B . n 
B 1 195 ASN 195 202 202 ASN ASN B . n 
B 1 196 ALA 196 203 203 ALA ALA B . n 
B 1 197 LYS 197 204 204 LYS LYS B . n 
B 1 198 PRO 198 205 205 PRO PRO B . n 
B 1 199 THR 199 206 206 THR THR B . n 
B 1 200 GLU 200 207 207 GLU GLU B . n 
B 1 201 LYS 201 208 208 LYS LYS B . n 
B 1 202 SER 202 209 209 SER SER B . n 
B 1 203 ASP 203 210 210 ASP ASP B . n 
B 1 204 VAL 204 211 211 VAL VAL B . n 
B 1 205 TYR 205 212 212 TYR TYR B . n 
B 1 206 SER 206 213 213 SER SER B . n 
B 1 207 PHE 207 214 214 PHE PHE B . n 
B 1 208 ALA 208 215 215 ALA ALA B . n 
B 1 209 VAL 209 216 216 VAL VAL B . n 
B 1 210 VAL 210 217 217 VAL VAL B . n 
B 1 211 LEU 211 218 218 LEU LEU B . n 
B 1 212 TRP 212 219 219 TRP TRP B . n 
B 1 213 ALA 213 220 220 ALA ALA B . n 
B 1 214 ILE 214 221 221 ILE ILE B . n 
B 1 215 PHE 215 222 222 PHE PHE B . n 
B 1 216 ALA 216 223 223 ALA ALA B . n 
B 1 217 ASN 217 224 224 ASN ASN B . n 
B 1 218 LYS 218 225 225 LYS LYS B . n 
B 1 219 GLU 219 226 226 GLU GLU B . n 
B 1 220 PRO 220 227 227 PRO PRO B . n 
B 1 221 TYR 221 228 228 TYR TYR B . n 
B 1 222 GLU 222 229 229 GLU GLU B . n 
B 1 223 ASN 223 230 230 ASN ASN B . n 
B 1 224 ALA 224 231 231 ALA ALA B . n 
B 1 225 ILE 225 232 232 ILE ILE B . n 
B 1 226 ALA 226 233 233 ALA ALA B . n 
B 1 227 GLU 227 234 234 GLU GLU B . n 
B 1 228 GLN 228 235 235 GLN GLN B . n 
B 1 229 GLN 229 236 236 GLN GLN B . n 
B 1 230 LEU 230 237 237 LEU LEU B . n 
B 1 231 ILE 231 238 238 ILE ILE B . n 
B 1 232 MET 232 239 239 MET MET B . n 
B 1 233 ALA 233 240 240 ALA ALA B . n 
B 1 234 ILE 234 241 241 ILE ILE B . n 
B 1 235 LYS 235 242 242 LYS LYS B . n 
B 1 236 SER 236 243 243 SER SER B . n 
B 1 237 GLY 237 244 244 GLY GLY B . n 
B 1 238 ASN 238 245 245 ASN ASN B . n 
B 1 239 ARG 239 246 246 ARG ARG B . n 
B 1 240 PRO 240 247 247 PRO PRO B . n 
B 1 241 ASP 241 248 248 ASP ASP B . n 
B 1 242 VAL 242 249 249 VAL VAL B . n 
B 1 243 ASP 243 250 250 ASP ASP B . n 
B 1 244 ASP 244 251 251 ASP ASP B . n 
B 1 245 ILE 245 252 252 ILE ILE B . n 
B 1 246 THR 246 253 253 THR THR B . n 
B 1 247 GLU 247 254 254 GLU GLU B . n 
B 1 248 TYR 248 255 255 TYR TYR B . n 
B 1 249 CYS 249 256 256 CYS CYS B . n 
B 1 250 PRO 250 257 257 PRO PRO B . n 
B 1 251 ARG 251 258 258 ARG ARG B . n 
B 1 252 GLU 252 259 259 GLU GLU B . n 
B 1 253 ILE 253 260 260 ILE ILE B . n 
B 1 254 ILE 254 261 261 ILE ILE B . n 
B 1 255 SER 255 262 262 SER SER B . n 
B 1 256 LEU 256 263 263 LEU LEU B . n 
B 1 257 MET 257 264 264 MET MET B . n 
B 1 258 LYS 258 265 265 LYS LYS B . n 
B 1 259 LEU 259 266 266 LEU LEU B . n 
B 1 260 CYS 260 267 267 CYS CYS B . n 
B 1 261 TRP 261 268 268 TRP TRP B . n 
B 1 262 GLU 262 269 269 GLU GLU B . n 
B 1 263 ALA 263 270 270 ALA ALA B . n 
B 1 264 ASN 264 271 271 ASN ASN B . n 
B 1 265 PRO 265 272 272 PRO PRO B . n 
B 1 266 GLU 266 273 273 GLU GLU B . n 
B 1 267 ALA 267 274 274 ALA ALA B . n 
B 1 268 ARG 268 275 275 ARG ARG B . n 
B 1 269 PRO 269 276 276 PRO PRO B . n 
B 1 270 THR 270 277 277 THR THR B . n 
B 1 271 PHE 271 278 278 PHE PHE B . n 
B 1 272 PRO 272 279 279 PRO PRO B . n 
B 1 273 GLY 273 280 280 GLY GLY B . n 
B 1 274 ILE 274 281 281 ILE ILE B . n 
B 1 275 GLU 275 282 282 GLU GLU B . n 
B 1 276 GLU 276 283 283 GLU GLU B . n 
B 1 277 LYS 277 284 284 LYS LYS B . n 
B 1 278 PHE 278 285 285 PHE PHE B . n 
B 1 279 ARG 279 286 286 ARG ARG B . n 
B 1 280 PRO 280 287 287 PRO PRO B . n 
B 1 281 PHE 281 288 288 PHE PHE B . n 
B 1 282 TYR 282 289 289 TYR TYR B . n 
B 1 283 LEU 283 290 290 LEU LEU B . n 
B 1 284 SER 284 291 291 SER SER B . n 
B 1 285 GLN 285 292 292 GLN GLN B . n 
B 1 286 LEU 286 293 293 LEU LEU B . n 
B 1 287 GLU 287 294 294 GLU GLU B . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        A1BU6 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1BU6 
_pdbx_entity_instance_feature.auth_asym_id   ? 
_pdbx_entity_instance_feature.auth_seq_num   ? 
_pdbx_entity_instance_feature.feature_type   'SUBJECT OF INVESTIGATION' 
_pdbx_entity_instance_feature.details        ? 
# 
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 A1BU6 1  301 1   A1BU6 INX A . 
D 3 IOD   1  302 1   IOD   IOD A . 
E 3 IOD   1  303 3   IOD   IOD A . 
F 3 IOD   1  304 4   IOD   IOD A . 
G 4 GLY   1  305 401 GLY   GLY A . 
H 2 A1BU6 1  301 2   A1BU6 INX B . 
I 5 CL    1  302 5   CL    CL  B . 
J 3 IOD   1  303 2   IOD   IOD B . 
K 6 HOH   1  401 34  HOH   HOH A . 
K 6 HOH   2  402 33  HOH   HOH A . 
K 6 HOH   3  403 44  HOH   HOH A . 
K 6 HOH   4  404 29  HOH   HOH A . 
K 6 HOH   5  405 52  HOH   HOH A . 
K 6 HOH   6  406 56  HOH   HOH A . 
K 6 HOH   7  407 20  HOH   HOH A . 
K 6 HOH   8  408 89  HOH   HOH A . 
K 6 HOH   9  409 17  HOH   HOH A . 
K 6 HOH   10 410 27  HOH   HOH A . 
K 6 HOH   11 411 35  HOH   HOH A . 
K 6 HOH   12 412 53  HOH   HOH A . 
K 6 HOH   13 413 51  HOH   HOH A . 
K 6 HOH   14 414 62  HOH   HOH A . 
K 6 HOH   15 415 64  HOH   HOH A . 
K 6 HOH   16 416 97  HOH   HOH A . 
K 6 HOH   17 417 90  HOH   HOH A . 
K 6 HOH   18 418 79  HOH   HOH A . 
K 6 HOH   19 419 42  HOH   HOH A . 
K 6 HOH   20 420 49  HOH   HOH A . 
K 6 HOH   21 421 21  HOH   HOH A . 
K 6 HOH   22 422 28  HOH   HOH A . 
K 6 HOH   23 423 14  HOH   HOH A . 
K 6 HOH   24 424 69  HOH   HOH A . 
K 6 HOH   25 425 15  HOH   HOH A . 
K 6 HOH   26 426 22  HOH   HOH A . 
K 6 HOH   27 427 70  HOH   HOH A . 
K 6 HOH   28 428 11  HOH   HOH A . 
K 6 HOH   29 429 95  HOH   HOH A . 
K 6 HOH   30 430 23  HOH   HOH A . 
K 6 HOH   31 431 73  HOH   HOH A . 
K 6 HOH   32 432 92  HOH   HOH A . 
K 6 HOH   33 433 98  HOH   HOH A . 
K 6 HOH   34 434 13  HOH   HOH A . 
K 6 HOH   35 435 67  HOH   HOH A . 
K 6 HOH   36 436 80  HOH   HOH A . 
L 6 HOH   1  401 77  HOH   HOH B . 
L 6 HOH   2  402 83  HOH   HOH B . 
L 6 HOH   3  403 37  HOH   HOH B . 
L 6 HOH   4  404 30  HOH   HOH B . 
L 6 HOH   5  405 48  HOH   HOH B . 
L 6 HOH   6  406 60  HOH   HOH B . 
L 6 HOH   7  407 1   HOH   HOH B . 
L 6 HOH   8  408 84  HOH   HOH B . 
L 6 HOH   9  409 78  HOH   HOH B . 
L 6 HOH   10 410 26  HOH   HOH B . 
L 6 HOH   11 411 24  HOH   HOH B . 
L 6 HOH   12 412 31  HOH   HOH B . 
L 6 HOH   13 413 63  HOH   HOH B . 
L 6 HOH   14 414 2   HOH   HOH B . 
L 6 HOH   15 415 54  HOH   HOH B . 
L 6 HOH   16 416 3   HOH   HOH B . 
L 6 HOH   17 417 40  HOH   HOH B . 
L 6 HOH   18 418 58  HOH   HOH B . 
L 6 HOH   19 419 76  HOH   HOH B . 
L 6 HOH   20 420 82  HOH   HOH B . 
L 6 HOH   21 421 87  HOH   HOH B . 
L 6 HOH   22 422 6   HOH   HOH B . 
L 6 HOH   23 423 75  HOH   HOH B . 
L 6 HOH   24 424 74  HOH   HOH B . 
L 6 HOH   25 425 57  HOH   HOH B . 
L 6 HOH   26 426 59  HOH   HOH B . 
L 6 HOH   27 427 9   HOH   HOH B . 
L 6 HOH   28 428 86  HOH   HOH B . 
L 6 HOH   29 429 72  HOH   HOH B . 
L 6 HOH   30 430 45  HOH   HOH B . 
L 6 HOH   31 431 4   HOH   HOH B . 
L 6 HOH   32 432 103 HOH   HOH B . 
L 6 HOH   33 433 102 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 0 A LYS 11  ? CE  ? A LYS 4   CE  
2   1 Y 0 A LYS 11  ? NZ  ? A LYS 4   NZ  
3   1 Y 0 A LYS 13  ? CE  ? A LYS 6   CE  
4   1 Y 0 A LYS 13  ? NZ  ? A LYS 6   NZ  
5   1 Y 0 A LYS 30  ? CE  ? A LYS 23  CE  
6   1 Y 0 A LYS 30  ? NZ  ? A LYS 23  NZ  
7   1 Y 0 A ARG 37  ? CZ  ? A ARG 30  CZ  
8   1 Y 0 A ARG 37  ? NH1 ? A ARG 30  NH1 
9   1 Y 0 A ARG 37  ? NH2 ? A ARG 30  NH2 
10  1 Y 0 A ILE 43  ? CD1 ? A ILE 36  CD1 
11  1 Y 0 A LYS 45  ? NZ  ? A LYS 38  NZ  
12  1 Y 0 A LYS 49  ? NZ  ? A LYS 42  NZ  
13  1 Y 0 A ASN 52  ? CG  ? A ASN 45  CG  
14  1 Y 0 A ASN 52  ? OD1 ? A ASN 45  OD1 
15  1 Y 0 A ASN 52  ? ND2 ? A ASN 45  ND2 
16  1 Y 0 A ILE 54  ? CG1 ? A ILE 47  CG1 
17  1 Y 0 A ILE 54  ? CG2 ? A ILE 47  CG2 
18  1 Y 0 A ILE 54  ? CD1 ? A ILE 47  CD1 
19  1 Y 0 A GLU 55  ? CD  ? A GLU 48  CD  
20  1 Y 0 A GLU 55  ? OE1 ? A GLU 48  OE1 
21  1 Y 0 A GLU 55  ? OE2 ? A GLU 48  OE2 
22  1 Y 0 A LEU 61  ? CD1 ? A LEU 54  CD1 
23  1 Y 0 A LEU 61  ? CD2 ? A LEU 54  CD2 
24  1 Y 0 A LYS 65  ? CE  ? A LYS 58  CE  
25  1 Y 0 A LYS 65  ? NZ  ? A LYS 58  NZ  
26  1 Y 0 A ILE 83  ? CD1 ? A ILE 76  CD1 
27  1 Y 0 A LYS 97  ? NZ  ? A LYS 90  NZ  
28  1 Y 0 A GLU 107 ? CD  ? A GLU 100 CD  
29  1 Y 0 A GLU 107 ? OE1 ? A GLU 100 OE1 
30  1 Y 0 A GLU 107 ? OE2 ? A GLU 100 OE2 
31  1 Y 0 A MET 108 ? SD  ? A MET 101 SD  
32  1 Y 0 A MET 108 ? CE  ? A MET 101 CE  
33  1 Y 0 A LYS 132 ? NZ  ? A LYS 125 NZ  
34  1 Y 0 A LYS 163 ? CD  ? A LYS 156 CD  
35  1 Y 0 A LYS 163 ? CE  ? A LYS 156 CE  
36  1 Y 0 A LYS 163 ? NZ  ? A LYS 156 NZ  
37  1 Y 0 A LYS 167 ? CD  ? A LYS 160 CD  
38  1 Y 0 A LYS 167 ? CE  ? A LYS 160 CE  
39  1 Y 0 A LYS 167 ? NZ  ? A LYS 160 NZ  
40  1 Y 0 A ASN 170 ? CG  ? A ASN 163 CG  
41  1 Y 0 A ASN 170 ? OD1 ? A ASN 163 OD1 
42  1 Y 0 A ASN 170 ? ND2 ? A ASN 163 ND2 
43  1 Y 0 A GLU 172 ? CD  ? A GLU 165 CD  
44  1 Y 0 A GLU 172 ? OE1 ? A GLU 165 OE1 
45  1 Y 0 A GLU 172 ? OE2 ? A GLU 165 OE2 
46  1 Y 0 A GLU 175 ? CD  ? A GLU 168 CD  
47  1 Y 0 A GLU 175 ? OE1 ? A GLU 168 OE1 
48  1 Y 0 A GLU 175 ? OE2 ? A GLU 168 OE2 
49  1 Y 0 A LYS 204 ? CE  ? A LYS 197 CE  
50  1 Y 0 A LYS 204 ? NZ  ? A LYS 197 NZ  
51  1 Y 0 A LYS 225 ? NZ  ? A LYS 218 NZ  
52  1 Y 0 A ASN 230 ? CG  ? A ASN 223 CG  
53  1 Y 0 A ASN 230 ? OD1 ? A ASN 223 OD1 
54  1 Y 0 A ASN 230 ? ND2 ? A ASN 223 ND2 
55  1 Y 0 A ILE 232 ? CD1 ? A ILE 225 CD1 
56  1 Y 0 A GLN 235 ? CD  ? A GLN 228 CD  
57  1 Y 0 A GLN 235 ? OE1 ? A GLN 228 OE1 
58  1 Y 0 A GLN 235 ? NE2 ? A GLN 228 NE2 
59  1 Y 0 A GLN 236 ? CD  ? A GLN 229 CD  
60  1 Y 0 A GLN 236 ? OE1 ? A GLN 229 OE1 
61  1 Y 0 A GLN 236 ? NE2 ? A GLN 229 NE2 
62  1 Y 0 A ILE 261 ? CD1 ? A ILE 254 CD1 
63  1 Y 0 A GLU 283 ? CD  ? A GLU 276 CD  
64  1 Y 0 A GLU 283 ? OE1 ? A GLU 276 OE1 
65  1 Y 0 A GLU 283 ? OE2 ? A GLU 276 OE2 
66  1 Y 0 A GLU 294 ? CD  ? A GLU 287 CD  
67  1 Y 0 A GLU 294 ? OE1 ? A GLU 287 OE1 
68  1 Y 0 A GLU 294 ? OE2 ? A GLU 287 OE2 
69  1 Y 0 B ILE 10  ? CD1 ? B ILE 3   CD1 
70  1 Y 0 B LYS 11  ? CD  ? B LYS 4   CD  
71  1 Y 0 B LYS 11  ? CE  ? B LYS 4   CE  
72  1 Y 0 B LYS 11  ? NZ  ? B LYS 4   NZ  
73  1 Y 0 B LYS 13  ? NZ  ? B LYS 6   NZ  
74  1 Y 0 B LYS 30  ? CE  ? B LYS 23  CE  
75  1 Y 0 B LYS 30  ? NZ  ? B LYS 23  NZ  
76  1 Y 0 B LYS 45  ? NZ  ? B LYS 38  NZ  
77  1 Y 0 B LYS 49  ? CE  ? B LYS 42  CE  
78  1 Y 0 B LYS 49  ? NZ  ? B LYS 42  NZ  
79  1 Y 0 B ILE 54  ? CG1 ? B ILE 47  CG1 
80  1 Y 0 B ILE 54  ? CG2 ? B ILE 47  CG2 
81  1 Y 0 B ILE 54  ? CD1 ? B ILE 47  CD1 
82  1 Y 0 B GLU 55  ? CD  ? B GLU 48  CD  
83  1 Y 0 B GLU 55  ? OE1 ? B GLU 48  OE1 
84  1 Y 0 B GLU 55  ? OE2 ? B GLU 48  OE2 
85  1 Y 0 B GLU 58  ? CD  ? B GLU 51  CD  
86  1 Y 0 B GLU 58  ? OE1 ? B GLU 51  OE1 
87  1 Y 0 B GLU 58  ? OE2 ? B GLU 51  OE2 
88  1 Y 0 B LYS 65  ? CD  ? B LYS 58  CD  
89  1 Y 0 B LYS 65  ? CE  ? B LYS 58  CE  
90  1 Y 0 B LYS 65  ? NZ  ? B LYS 58  NZ  
91  1 Y 0 B ARG 69  ? NE  ? B ARG 62  NE  
92  1 Y 0 B ARG 69  ? CZ  ? B ARG 62  CZ  
93  1 Y 0 B ARG 69  ? NH1 ? B ARG 62  NH1 
94  1 Y 0 B ARG 69  ? NH2 ? B ARG 62  NH2 
95  1 Y 0 B ARG 71  ? CZ  ? B ARG 64  CZ  
96  1 Y 0 B ARG 71  ? NH1 ? B ARG 64  NH1 
97  1 Y 0 B ARG 71  ? NH2 ? B ARG 64  NH2 
98  1 Y 0 B GLU 85  ? CD  ? B GLU 78  CD  
99  1 Y 0 B GLU 85  ? OE1 ? B GLU 78  OE1 
100 1 Y 0 B GLU 85  ? OE2 ? B GLU 78  OE2 
101 1 Y 0 B LYS 87  ? CE  ? B LYS 80  CE  
102 1 Y 0 B LYS 87  ? NZ  ? B LYS 80  NZ  
103 1 Y 0 B LYS 105 ? NZ  ? B LYS 98  NZ  
104 1 Y 0 B GLU 107 ? CD  ? B GLU 100 CD  
105 1 Y 0 B GLU 107 ? OE1 ? B GLU 100 OE1 
106 1 Y 0 B GLU 107 ? OE2 ? B GLU 100 OE2 
107 1 Y 0 B MET 108 ? SD  ? B MET 101 SD  
108 1 Y 0 B MET 108 ? CE  ? B MET 101 CE  
109 1 Y 0 B LYS 132 ? NZ  ? B LYS 125 NZ  
110 1 Y 0 B LYS 137 ? NZ  ? B LYS 130 NZ  
111 1 Y 0 B GLU 142 ? CD  ? B GLU 135 CD  
112 1 Y 0 B GLU 142 ? OE1 ? B GLU 135 OE1 
113 1 Y 0 B GLU 142 ? OE2 ? B GLU 135 OE2 
114 1 Y 0 B LYS 167 ? CD  ? B LYS 160 CD  
115 1 Y 0 B LYS 167 ? CE  ? B LYS 160 CE  
116 1 Y 0 B LYS 167 ? NZ  ? B LYS 160 NZ  
117 1 Y 0 B ASN 170 ? CG  ? B ASN 163 CG  
118 1 Y 0 B ASN 170 ? OD1 ? B ASN 163 OD1 
119 1 Y 0 B ASN 170 ? ND2 ? B ASN 163 ND2 
120 1 Y 0 B GLU 172 ? CD  ? B GLU 165 CD  
121 1 Y 0 B GLU 172 ? OE1 ? B GLU 165 OE1 
122 1 Y 0 B GLU 172 ? OE2 ? B GLU 165 OE2 
123 1 Y 0 B GLU 175 ? CD  ? B GLU 168 CD  
124 1 Y 0 B GLU 175 ? OE1 ? B GLU 168 OE1 
125 1 Y 0 B GLU 175 ? OE2 ? B GLU 168 OE2 
126 1 Y 0 B ARG 177 ? CZ  ? B ARG 170 CZ  
127 1 Y 0 B ARG 177 ? NH1 ? B ARG 170 NH1 
128 1 Y 0 B ARG 177 ? NH2 ? B ARG 170 NH2 
129 1 Y 0 B GLU 178 ? CD  ? B GLU 171 CD  
130 1 Y 0 B GLU 178 ? OE1 ? B GLU 171 OE1 
131 1 Y 0 B GLU 178 ? OE2 ? B GLU 171 OE2 
132 1 Y 0 B ASN 202 ? CG  ? B ASN 195 CG  
133 1 Y 0 B ASN 202 ? OD1 ? B ASN 195 OD1 
134 1 Y 0 B ASN 202 ? ND2 ? B ASN 195 ND2 
135 1 Y 0 B LYS 204 ? CD  ? B LYS 197 CD  
136 1 Y 0 B LYS 204 ? CE  ? B LYS 197 CE  
137 1 Y 0 B LYS 204 ? NZ  ? B LYS 197 NZ  
138 1 Y 0 B GLU 207 ? CD  ? B GLU 200 CD  
139 1 Y 0 B GLU 207 ? OE1 ? B GLU 200 OE1 
140 1 Y 0 B GLU 207 ? OE2 ? B GLU 200 OE2 
141 1 Y 0 B ASP 250 ? CG  ? B ASP 243 CG  
142 1 Y 0 B ASP 250 ? OD1 ? B ASP 243 OD1 
143 1 Y 0 B ASP 250 ? OD2 ? B ASP 243 OD2 
144 1 Y 0 B ARG 258 ? CZ  ? B ARG 251 CZ  
145 1 Y 0 B ARG 258 ? NH1 ? B ARG 251 NH1 
146 1 Y 0 B ARG 258 ? NH2 ? B ARG 251 NH2 
147 1 Y 0 B GLU 283 ? CD  ? B GLU 276 CD  
148 1 Y 0 B GLU 283 ? OE1 ? B GLU 276 OE1 
149 1 Y 0 B GLU 283 ? OE2 ? B GLU 276 OE2 
150 1 Y 0 B LYS 284 ? NZ  ? B LYS 277 NZ  
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? autoPROC ? ? ? .                 1 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? XDS      ? ? ? '(VERSION Jan 31' 2 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? autoPROC ? ? ? '(Version 1.1.7)' 3 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? Aimless  ? ? ? .                 4 
? refinement       ? ? ? ? ? ? ? ? ? ? ? REFMAC   ? ? ? 5.8.0155          5 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.00 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9MZY 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     47.307 
_cell.length_a_esd                 ? 
_cell.length_b                     95.163 
_cell.length_b_esd                 ? 
_cell.length_c                     128.121 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        8 
_cell.reciprocal_angle_alpha       ? 
_cell.reciprocal_angle_beta        ? 
_cell.reciprocal_angle_gamma       ? 
_cell.reciprocal_angle_alpha_esd   ? 
_cell.reciprocal_angle_beta_esd    ? 
_cell.reciprocal_angle_gamma_esd   ? 
_cell.reciprocal_length_a          ? 
_cell.reciprocal_length_b          ? 
_cell.reciprocal_length_c          ? 
_cell.reciprocal_length_a_esd      ? 
_cell.reciprocal_length_b_esd      ? 
_cell.reciprocal_length_c_esd      ? 
_cell.pdbx_unique_axis             ? 
_cell.pdbx_esd_method              ? 
# 
_symmetry.entry_id                         9MZY 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                19 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 21 21 21' 
_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                   9MZY 
_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             2.21 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          44.27 
_exptl_crystal.description                  ? 
_exptl_crystal.F_000                        ? 
_exptl_crystal.id                           1 
_exptl_crystal.preparation                  ? 
_exptl_crystal.size_max                     ? 
_exptl_crystal.size_mid                     ? 
_exptl_crystal.size_min                     ? 
_exptl_crystal.size_rad                     ? 
_exptl_crystal.colour_lustre                ? 
_exptl_crystal.colour_modifier              ? 
_exptl_crystal.colour_primary               ? 
_exptl_crystal.density_meas                 ? 
_exptl_crystal.density_meas_esd             ? 
_exptl_crystal.density_meas_gt              ? 
_exptl_crystal.density_meas_lt              ? 
_exptl_crystal.density_meas_temp            ? 
_exptl_crystal.density_meas_temp_esd        ? 
_exptl_crystal.density_meas_temp_gt         ? 
_exptl_crystal.density_meas_temp_lt         ? 
_exptl_crystal.pdbx_crystal_image_url       ? 
_exptl_crystal.pdbx_crystal_image_format    ? 
_exptl_crystal.pdbx_mosaicity               ? 
_exptl_crystal.pdbx_mosaicity_esd           ? 
_exptl_crystal.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, SITTING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              ? 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    '20% (w/v) PEG3350; 6 mM Gly3; 0.22 M NH4I' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            277 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS EIGER2 XE 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         2020-08-05 
_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                    ? 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   1.0001 
_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                        'DIAMOND BEAMLINE I03' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        1.0001 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   I03 
_diffrn_source.pdbx_synchrotron_site       Diamond 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       9MZY 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              2.32 
_reflns.d_resolution_low                               76.4 
_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                                     25627 
_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                           99.6 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                7.9 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          16.5 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               ? 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                ? 
_reflns.pdbx_Rpim_I_all                                ? 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.998 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              ? 
_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                        ? 
# 
_reflns_shell.d_res_high                                    2.32 
_reflns_shell.d_res_low                                     2.36 
_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                             1226 
_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                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.962 
_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               ? 
# 
_refine.aniso_B[1][1]                            1.72 
_refine.aniso_B[1][2]                            0.00 
_refine.aniso_B[1][3]                            0.00 
_refine.aniso_B[2][2]                            3.63 
_refine.aniso_B[2][3]                            -0.00 
_refine.aniso_B[3][3]                            -5.35 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               82.762 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               0.942 
_refine.correlation_coeff_Fo_to_Fc_free          0.922 
_refine.details                                  'HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS' 
_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                                 9MZY 
_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                            2.32 
_refine.ls_d_res_low                             76.40 
_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                     22093 
_refine.ls_number_reflns_R_free                  1034 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    89.90 
_refine.ls_percent_reflns_R_free                 4.5 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.24247 
_refine.ls_R_factor_R_free                       0.31468 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.23913 
_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                    MASK 
_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                          ? 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               THROUGHOUT 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       'MAXIMUM LIKELIHOOD' 
_refine.pdbx_R_Free_selection_details            RANDOM 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       0.558 
_refine.pdbx_overall_ESU_R_Free                  0.341 
_refine.pdbx_solvent_vdw_probe_radii             1.20 
_refine.pdbx_solvent_ion_probe_radii             0.80 
_refine.pdbx_solvent_shrinkage_radii             0.80 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 ? 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_diffrn_id                           1 
_refine.overall_SU_B                             27.576 
_refine.overall_SU_ML                            0.306 
_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                       2.32 
_refine_hist.d_res_low                        76.40 
_refine_hist.number_atoms_solvent             69 
_refine_hist.number_atoms_total               4478 
_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        4359 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         50 
_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' ? 0.012  0.019  4352 ? r_bond_refined_d             ? ? 
'X-RAY DIFFRACTION' ? 0.003  0.020  4204 ? r_bond_other_d               ? ? 
'X-RAY DIFFRACTION' ? 1.580  1.981  5890 ? r_angle_refined_deg          ? ? 
'X-RAY DIFFRACTION' ? 1.235  3.000  9651 ? r_angle_other_deg            ? ? 
'X-RAY DIFFRACTION' ? 6.900  5.000  538  ? r_dihedral_angle_1_deg       ? ? 
'X-RAY DIFFRACTION' ? 33.727 24.798 173  ? r_dihedral_angle_2_deg       ? ? 
'X-RAY DIFFRACTION' ? 13.788 15.051 779  ? r_dihedral_angle_3_deg       ? ? 
'X-RAY DIFFRACTION' ? 11.133 15.000 14   ? r_dihedral_angle_4_deg       ? ? 
'X-RAY DIFFRACTION' ? 0.090  0.200  664  ? r_chiral_restr               ? ? 
'X-RAY DIFFRACTION' ? 0.006  0.021  4800 ? r_gen_planes_refined         ? ? 
'X-RAY DIFFRACTION' ? 0.002  0.020  922  ? r_gen_planes_other           ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_nbd_refined                ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_nbd_other                  ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_nbtor_refined              ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_nbtor_other                ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_xyhbond_nbd_refined        ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_xyhbond_nbd_other          ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_metal_ion_refined          ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_metal_ion_other            ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_symmetry_vdw_refined       ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_symmetry_vdw_other         ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_symmetry_hbond_refined     ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_symmetry_hbond_other       ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_symmetry_metal_ion_refined ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_symmetry_metal_ion_other   ? ? 
'X-RAY DIFFRACTION' ? 5.244  6.045  2170 ? r_mcbond_it                  ? ? 
'X-RAY DIFFRACTION' ? 5.245  6.042  2169 ? r_mcbond_other               ? ? 
'X-RAY DIFFRACTION' ? 7.520  10.178 2702 ? r_mcangle_it                 ? ? 
'X-RAY DIFFRACTION' ? 7.519  10.180 2703 ? r_mcangle_other              ? ? 
'X-RAY DIFFRACTION' ? 5.175  6.313  2182 ? r_scbond_it                  ? ? 
'X-RAY DIFFRACTION' ? 5.174  6.313  2182 ? r_scbond_other               ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_scangle_it                 ? ? 
'X-RAY DIFFRACTION' ? 7.427  10.517 3189 ? r_scangle_other              ? ? 
'X-RAY DIFFRACTION' ? 9.727  53.203 4499 ? r_long_range_B_refined       ? ? 
'X-RAY DIFFRACTION' ? 9.725  53.171 4496 ? r_long_range_B_other         ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_rigid_bond_restr           ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_sphericity_free            ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_sphericity_bonded          ? ? 
# 
loop_
_refine_ls_restr_ncs.pdbx_refine_id 
_refine_ls_restr_ncs.dom_id 
_refine_ls_restr_ncs.ncs_model_details 
_refine_ls_restr_ncs.rms_dev_B_iso 
_refine_ls_restr_ncs.rms_dev_position 
_refine_ls_restr_ncs.weight_B_iso 
_refine_ls_restr_ncs.weight_position 
_refine_ls_restr_ncs.pdbx_ordinal 
_refine_ls_restr_ncs.pdbx_type 
_refine_ls_restr_ncs.pdbx_asym_id 
_refine_ls_restr_ncs.pdbx_auth_asym_id 
_refine_ls_restr_ncs.pdbx_number 
_refine_ls_restr_ncs.pdbx_rms 
_refine_ls_restr_ncs.pdbx_weight 
_refine_ls_restr_ncs.pdbx_ens_id 
'X-RAY DIFFRACTION' 1 ? ? 0.04 ? 0.05 1 'interatomic distance' ? A 5856 ? ? 1 
'X-RAY DIFFRACTION' 2 ? ? 0.04 ? 0.05 2 'interatomic distance' ? B 5856 ? ? 1 
# 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.d_res_high                       2.323 
_refine_ls_shell.d_res_low                        2.383 
_refine_ls_shell.number_reflns_all                ? 
_refine_ls_shell.number_reflns_obs                ? 
_refine_ls_shell.number_reflns_R_free             62 
_refine_ls_shell.number_reflns_R_work             1272 
_refine_ls_shell.percent_reflns_obs               71.38 
_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                  0.499 
_refine_ls_shell.redundancy_reflns_all            ? 
_refine_ls_shell.redundancy_reflns_obs            ? 
_refine_ls_shell.wR_factor_all                    ? 
_refine_ls_shell.wR_factor_obs                    ? 
_refine_ls_shell.wR_factor_R_free                 ? 
_refine_ls_shell.wR_factor_R_work                 ? 
_refine_ls_shell.pdbx_R_complete                  ? 
_refine_ls_shell.pdbx_total_number_of_bins_used   20 
_refine_ls_shell.pdbx_phase_error                 ? 
_refine_ls_shell.pdbx_fsc_work                    ? 
_refine_ls_shell.pdbx_fsc_free                    ? 
_refine_ls_shell.R_factor_R_free                  0.490 
# 
_struct_ncs_dom.id            1 
_struct_ncs_dom.details       ? 
_struct_ncs_dom.pdbx_ens_id   1 
# 
_struct_ncs_ens.id        1 
_struct_ncs_ens.details   ? 
# 
_struct.entry_id                     9MZY 
_struct.title                        'Crystal structure of human RIPK1 with Compound 22' 
_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        9MZY 
_struct_keywords.text            'Kinase, serine/threonine-protein kinase, Inhibitor, TRANSFERASE, TRANSFERASE-INHIBITOR complex' 
_struct_keywords.pdbx_keywords   TRANSFERASE/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 3 ? 
F N N 3 ? 
G N N 4 ? 
H N N 2 ? 
I N N 5 ? 
J N N 3 ? 
K N N 6 ? 
L N N 6 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    RIPK1_HUMAN 
_struct_ref.pdbx_db_accession          Q13546 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;NVIKMKSSDFLESAELDSGGFGKVSLCFHRTQGLMIMKTVYKGPNCIEHNEALLEEAKMMNRLRHSRVVKLLGVIIEEGK
YSLVMEYMEKGNLMHVLKAEMSTPLSVKGRIILEIIEGMCYLHGKGVIHKDLKPENILVDNDFHIKIADLGLASFKMWSK
LNNEEHNELREVDGTAKKNGGTLYYMAPEHLNDVNAKPTEKSDVYSFAVVLWAIFANKEPYENAICEQQLIMCIKSGNRP
DVDDITEYCPREIISLMKLCWEANPEARPTFPGIEEKFRPFYLSQLE
;
_struct_ref.pdbx_align_begin           8 
# 
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 9MZY A 1 ? 287 ? Q13546 8 ? 294 ? 8 294 
2 1 9MZY B 1 ? 287 ? Q13546 8 ? 294 ? 8 294 
# 
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 9MZY ALA A 27  ? UNP Q13546 CYS 34  conflict 34  1 
1 9MZY ALA A 120 ? UNP Q13546 CYS 127 conflict 127 2 
1 9MZY ALA A 226 ? UNP Q13546 CYS 233 conflict 233 3 
1 9MZY ALA A 233 ? UNP Q13546 CYS 240 conflict 240 4 
2 9MZY ALA B 27  ? UNP Q13546 CYS 34  conflict 34  5 
2 9MZY ALA B 120 ? UNP Q13546 CYS 127 conflict 127 6 
2 9MZY ALA B 226 ? UNP Q13546 CYS 233 conflict 233 7 
2 9MZY ALA B 233 ? UNP Q13546 CYS 240 conflict 240 8 
# 
_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,I,J,K,L 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   'gel filtration' 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 HIS A 49  ? ARG A 62  ? HIS A 56  ARG A 69  1 ? 14 
HELX_P HELX_P2  AA2 LEU A 93  ? LYS A 98  ? LEU A 100 LYS A 105 1 ? 6  
HELX_P HELX_P3  AA3 PRO A 104 ? LYS A 125 ? PRO A 111 LYS A 132 1 ? 22 
HELX_P HELX_P4  AA4 LYS A 133 ? GLU A 135 ? LYS A 140 GLU A 142 5 ? 3  
HELX_P HELX_P5  AA5 PHE A 155 ? ASN A 163 ? PHE A 162 ASN A 170 1 ? 9  
HELX_P HELX_P6  AA6 THR A 182 ? MET A 186 ? THR A 189 MET A 193 5 ? 5  
HELX_P HELX_P7  AA7 THR A 199 ? ASN A 217 ? THR A 206 ASN A 224 1 ? 19 
HELX_P HELX_P8  AA8 ALA A 226 ? SER A 236 ? ALA A 233 SER A 243 1 ? 11 
HELX_P HELX_P9  AA9 ASP A 241 ? ILE A 245 ? ASP A 248 ILE A 252 5 ? 5  
HELX_P HELX_P10 AB1 PRO A 250 ? TRP A 261 ? PRO A 257 TRP A 268 1 ? 12 
HELX_P HELX_P11 AB2 ASN A 264 ? ARG A 268 ? ASN A 271 ARG A 275 5 ? 5  
HELX_P HELX_P12 AB3 THR A 270 ? LEU A 286 ? THR A 277 LEU A 293 1 ? 17 
HELX_P HELX_P13 AB4 LYS B 6   ? SER B 8   ? LYS B 13  SER B 15  5 ? 3  
HELX_P HELX_P14 AB5 HIS B 49  ? ARG B 62  ? HIS B 56  ARG B 69  1 ? 14 
HELX_P HELX_P15 AB6 LEU B 93  ? LYS B 98  ? LEU B 100 LYS B 105 1 ? 6  
HELX_P HELX_P16 AB7 PRO B 104 ? LYS B 125 ? PRO B 111 LYS B 132 1 ? 22 
HELX_P HELX_P17 AB8 LYS B 133 ? GLU B 135 ? LYS B 140 GLU B 142 5 ? 3  
HELX_P HELX_P18 AB9 PHE B 155 ? ASN B 163 ? PHE B 162 ASN B 170 1 ? 9  
HELX_P HELX_P19 AC1 ALA B 187 ? LEU B 191 ? ALA B 194 LEU B 198 5 ? 5  
HELX_P HELX_P20 AC2 THR B 199 ? ASN B 217 ? THR B 206 ASN B 224 1 ? 19 
HELX_P HELX_P21 AC3 ALA B 226 ? SER B 236 ? ALA B 233 SER B 243 1 ? 11 
HELX_P HELX_P22 AC4 ASP B 241 ? ILE B 245 ? ASP B 248 ILE B 252 5 ? 5  
HELX_P HELX_P23 AC5 PRO B 250 ? TRP B 261 ? PRO B 257 TRP B 268 1 ? 12 
HELX_P HELX_P24 AC6 ASN B 264 ? ARG B 268 ? ASN B 271 ARG B 275 5 ? 5  
HELX_P HELX_P25 AC7 THR B 270 ? LEU B 286 ? THR B 277 LEU B 293 1 ? 17 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 5 ? 
AA2 ? 3 ? 
AA3 ? 6 ? 
AA4 ? 3 ? 
# 
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 
AA1 2 3 ? anti-parallel 
AA1 3 4 ? anti-parallel 
AA1 4 5 ? anti-parallel 
AA2 1 2 ? anti-parallel 
AA2 2 3 ? anti-parallel 
AA3 1 2 ? parallel      
AA3 2 3 ? anti-parallel 
AA3 3 4 ? anti-parallel 
AA3 4 5 ? anti-parallel 
AA3 5 6 ? anti-parallel 
AA4 1 2 ? anti-parallel 
AA4 2 3 ? anti-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 PHE A 10  ? LEU A 11  ? PHE A 17  LEU A 18  
AA1 2 VAL A 24  ? HIS A 29  ? VAL A 31  HIS A 36  
AA1 3 GLY A 33  ? LYS A 42  ? GLY A 40  LYS A 49  
AA1 4 LYS A 80  ? MET A 85  ? LYS A 87  MET A 92  
AA1 5 LEU A 71  ? GLU A 77  ? LEU A 78  GLU A 84  
AA2 1 GLY A 91  ? ASN A 92  ? GLY A 98  ASN A 99  
AA2 2 ILE A 137 ? VAL A 139 ? ILE A 144 VAL A 146 
AA2 3 ILE A 145 ? ILE A 147 ? ILE A 152 ILE A 154 
AA3 1 LYS B 4   ? MET B 5   ? LYS B 11  MET B 12  
AA3 2 LEU B 71  ? GLU B 77  ? LEU B 78  GLU B 84  
AA3 3 LYS B 80  ? MET B 85  ? LYS B 87  MET B 92  
AA3 4 GLY B 33  ? LYS B 42  ? GLY B 40  LYS B 49  
AA3 5 VAL B 24  ? HIS B 29  ? VAL B 31  HIS B 36  
AA3 6 PHE B 10  ? GLU B 15  ? PHE B 17  GLU B 22  
AA4 1 GLY B 91  ? ASN B 92  ? GLY B 98  ASN B 99  
AA4 2 ILE B 137 ? VAL B 139 ? ILE B 144 VAL B 146 
AA4 3 ILE B 145 ? ILE B 147 ? ILE B 152 ILE B 154 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 N LEU A 11  ? N LEU A 18  O PHE A 28  ? O PHE A 35  
AA1 2 3 N ALA A 27  ? N ALA A 34  O MET A 35  ? O MET A 42  
AA1 3 4 N LYS A 38  ? N LYS A 45  O LEU A 83  ? O LEU A 90  
AA1 4 5 O VAL A 84  ? O VAL A 91  N GLY A 73  ? N GLY A 80  
AA2 1 2 N GLY A 91  ? N GLY A 98  O VAL A 139 ? O VAL A 146 
AA2 2 3 N LEU A 138 ? N LEU A 145 O LYS A 146 ? O LYS A 153 
AA3 1 2 N MET B 5   ? N MET B 12  O VAL B 74  ? O VAL B 81  
AA3 2 3 N GLY B 73  ? N GLY B 80  O VAL B 84  ? O VAL B 91  
AA3 3 4 O LEU B 83  ? O LEU B 90  N LYS B 38  ? N LYS B 45  
AA3 4 5 O MET B 35  ? O MET B 42  N ALA B 27  ? N ALA B 34  
AA3 5 6 O LEU B 26  ? O LEU B 33  N ALA B 14  ? N ALA B 21  
AA4 1 2 N GLY B 91  ? N GLY B 98  O VAL B 139 ? O VAL B 146 
AA4 2 3 N LEU B 138 ? N LEU B 145 O LYS B 146 ? O LYS B 153 
# 
_pdbx_entry_details.entry_id                   9MZY 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 LYS A 137 ? ? 74.85   -2.94 
2 1 ASP A 138 ? ? -156.23 46.29 
3 1 ASP A 200 ? ? -162.63 76.40 
4 1 SER A 243 ? ? -95.95  32.01 
5 1 ILE B 54  ? ? -96.34  39.45 
6 1 LYS B 137 ? ? 76.17   -4.64 
7 1 ASP B 138 ? ? -158.74 44.86 
8 1 ASP B 200 ? ? -158.42 77.02 
# 
loop_
_pdbx_refine_tls.id 
_pdbx_refine_tls.pdbx_refine_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[1][1]_esd 
_pdbx_refine_tls.T[1][2] 
_pdbx_refine_tls.T[1][2]_esd 
_pdbx_refine_tls.T[1][3] 
_pdbx_refine_tls.T[1][3]_esd 
_pdbx_refine_tls.T[2][2] 
_pdbx_refine_tls.T[2][2]_esd 
_pdbx_refine_tls.T[2][3] 
_pdbx_refine_tls.T[2][3]_esd 
_pdbx_refine_tls.T[3][3] 
_pdbx_refine_tls.T[3][3]_esd 
_pdbx_refine_tls.L[1][1] 
_pdbx_refine_tls.L[1][1]_esd 
_pdbx_refine_tls.L[1][2] 
_pdbx_refine_tls.L[1][2]_esd 
_pdbx_refine_tls.L[1][3] 
_pdbx_refine_tls.L[1][3]_esd 
_pdbx_refine_tls.L[2][2] 
_pdbx_refine_tls.L[2][2]_esd 
_pdbx_refine_tls.L[2][3] 
_pdbx_refine_tls.L[2][3]_esd 
_pdbx_refine_tls.L[3][3] 
_pdbx_refine_tls.L[3][3]_esd 
_pdbx_refine_tls.S[1][1] 
_pdbx_refine_tls.S[1][1]_esd 
_pdbx_refine_tls.S[1][2] 
_pdbx_refine_tls.S[1][2]_esd 
_pdbx_refine_tls.S[1][3] 
_pdbx_refine_tls.S[1][3]_esd 
_pdbx_refine_tls.S[2][1] 
_pdbx_refine_tls.S[2][1]_esd 
_pdbx_refine_tls.S[2][2] 
_pdbx_refine_tls.S[2][2]_esd 
_pdbx_refine_tls.S[2][3] 
_pdbx_refine_tls.S[2][3]_esd 
_pdbx_refine_tls.S[3][1] 
_pdbx_refine_tls.S[3][1]_esd 
_pdbx_refine_tls.S[3][2] 
_pdbx_refine_tls.S[3][2]_esd 
_pdbx_refine_tls.S[3][3] 
_pdbx_refine_tls.S[3][3]_esd 
1 'X-RAY DIFFRACTION' ? refined 19.3260 -13.6140 54.7450 0.3745 ? -0.0398 ? 0.0411 ? 0.1819 ? -0.0119 ? 0.5203 ? 4.7050 ? 1.5568  
? -2.9480 ? 5.8623 ? -2.2669 ? 5.4268 ? -0.3463 ? -0.5018 ? -0.7465 ? 0.3716  ? 0.0325  ? 0.1472  ? 0.5687  ? -0.0452 ? 0.3138  ? 
2 'X-RAY DIFFRACTION' ? refined 17.9290 -4.5770  62.7960 0.4026 ? 0.0940  ? 0.0038 ? 0.3999 ? -0.0231 ? 0.3821 ? 0.2278 ? 0.5426  
? -0.9812 ? 3.2930 ? -2.2400 ? 7.1125 ? -0.0893 ? -0.1254 ? 0.0418  ? 0.4631  ? 0.0047  ? 0.2148  ? 0.1570  ? -0.1184 ? 0.0847  ? 
3 'X-RAY DIFFRACTION' ? refined 28.3950 12.6280  52.4180 0.1594 ? -0.0456 ? 0.0259 ? 0.0273 ? 0.0043  ? 0.3766 ? 3.1128 ? 0.1087  
? -0.7451 ? 3.1393 ? 0.9901  ? 3.8608 ? 0.1232  ? 0.0398  ? 0.1627  ? 0.0118  ? 0.0586  ? -0.2703 ? -0.2538 ? 0.2578  ? -0.1819 ? 
4 'X-RAY DIFFRACTION' ? refined 4.7430  22.3430  28.3230 0.4301 ? 0.1608  ? 0.0731 ? 0.6891 ? -0.0507 ? 0.5302 ? 2.6381 ? -1.4827 
? -0.1671 ? 5.7136 ? -1.6179 ? 0.7633 ? -0.0340 ? -0.1453 ? 0.3757  ? 0.2190  ? 0.2752  ? 0.3893  ? -0.1850 ? -0.3714 ? -0.2412 ? 
5 'X-RAY DIFFRACTION' ? refined -4.6240 14.5500  23.3600 0.4005 ? -0.1059 ? 0.0443 ? 0.9948 ? 0.3111  ? 0.9735 ? 0.9405 ? -0.2538 
? 0.3923  ? 4.8570 ? 2.9059  ? 2.0751 ? 0.0293  ? -0.6098 ? -0.5402 ? -0.4403 ? -0.1262 ? 0.7776  ? -0.2424 ? -0.4962 ? 0.0970  ? 
6 'X-RAY DIFFRACTION' ? refined 13.6070 -2.8630  22.1510 0.2113 ? -0.0587 ? 0.0188 ? 0.1146 ? 0.0710  ? 0.3450 ? 1.6177 ? 0.3238  
? 1.7680  ? 2.8406 ? 1.3663  ? 3.9151 ? 0.2005  ? -0.2028 ? -0.0971 ? -0.1395 ? -0.1120 ? 0.0806  ? 0.2553  ? -0.2896 ? -0.0885 ? 
# 
loop_
_pdbx_refine_tls_group.id 
_pdbx_refine_tls_group.pdbx_refine_id 
_pdbx_refine_tls_group.refine_tls_id 
_pdbx_refine_tls_group.beg_label_asym_id 
_pdbx_refine_tls_group.beg_label_seq_id 
_pdbx_refine_tls_group.beg_auth_asym_id 
_pdbx_refine_tls_group.beg_auth_seq_id 
_pdbx_refine_tls_group.beg_PDB_ins_code 
_pdbx_refine_tls_group.end_label_asym_id 
_pdbx_refine_tls_group.end_label_seq_id 
_pdbx_refine_tls_group.end_auth_asym_id 
_pdbx_refine_tls_group.end_auth_seq_id 
_pdbx_refine_tls_group.end_PDB_ins_code 
_pdbx_refine_tls_group.selection 
_pdbx_refine_tls_group.selection_details 
1 'X-RAY DIFFRACTION' 1 ? ? A 8   ? ? ? A 95  ? ? ? 
2 'X-RAY DIFFRACTION' 2 ? ? A 155 ? ? ? A 176 ? ? ? 
3 'X-RAY DIFFRACTION' 3 ? ? A 96  ? ? ? A 154 ? ? ? 
4 'X-RAY DIFFRACTION' 3 ? ? A 188 ? ? ? A 294 ? ? ? 
5 'X-RAY DIFFRACTION' 4 ? ? B 8   ? ? ? B 95  ? ? ? 
6 'X-RAY DIFFRACTION' 5 ? ? B 155 ? ? ? B 180 ? ? ? 
7 'X-RAY DIFFRACTION' 6 ? ? B 96  ? ? ? B 154 ? ? ? 
8 'X-RAY DIFFRACTION' 6 ? ? B 188 ? ? ? B 294 ? ? ? 
# 
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 SER 20  ? A SER 13  
2  1 Y 1 A ALA 21  ? A ALA 14  
3  1 Y 1 A GLU 22  ? A GLU 15  
4  1 Y 1 A LEU 23  ? A LEU 16  
5  1 Y 1 A ASP 24  ? A ASP 17  
6  1 Y 1 A SER 25  ? A SER 18  
7  1 Y 1 A GLY 26  ? A GLY 19  
8  1 Y 1 A GLY 27  ? A GLY 20  
9  1 Y 1 A PHE 28  ? A PHE 21  
10 1 Y 1 A GLY 29  ? A GLY 22  
11 1 Y 1 A ARG 177 ? A ARG 170 
12 1 Y 1 A GLU 178 ? A GLU 171 
13 1 Y 1 A VAL 179 ? A VAL 172 
14 1 Y 1 A ASP 180 ? A ASP 173 
15 1 Y 1 A GLY 181 ? A GLY 174 
16 1 Y 1 A THR 182 ? A THR 175 
17 1 Y 1 A ALA 183 ? A ALA 176 
18 1 Y 1 A LYS 184 ? A LYS 177 
19 1 Y 1 A LYS 185 ? A LYS 178 
20 1 Y 1 A ASN 186 ? A ASN 179 
21 1 Y 1 A GLY 187 ? A GLY 180 
22 1 Y 1 B GLY 26  ? B GLY 19  
23 1 Y 1 B GLY 27  ? B GLY 20  
24 1 Y 1 B PHE 28  ? B PHE 21  
25 1 Y 1 B GLY 29  ? B GLY 22  
26 1 Y 1 B GLY 181 ? B GLY 174 
27 1 Y 1 B THR 182 ? B THR 175 
28 1 Y 1 B ALA 183 ? B ALA 176 
29 1 Y 1 B LYS 184 ? B LYS 177 
30 1 Y 1 B LYS 185 ? B LYS 178 
31 1 Y 1 B ASN 186 ? B ASN 179 
32 1 Y 1 B GLY 187 ? B GLY 180 
# 
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 
A1BU6 C1   C  Y N 1   
A1BU6 C2   C  Y N 2   
A1BU6 C3   C  Y N 3   
A1BU6 C4   C  Y N 4   
A1BU6 C5   C  Y N 5   
A1BU6 C6   C  Y N 6   
A1BU6 C7   C  N S 7   
A1BU6 C11  C  N S 8   
A1BU6 C15  C  N N 9   
A1BU6 C17  C  N N 10  
A1BU6 C18  C  N N 11  
A1BU6 C19  C  N N 12  
A1BU6 N9   N  N N 13  
A1BU6 C10  C  N N 14  
A1BU6 O13  O  N N 15  
A1BU6 C14  C  N N 16  
A1BU6 O16  O  N N 17  
A1BU6 F20  F  N N 18  
A1BU6 F21  F  N N 19  
A1BU6 C22  C  N N 20  
A1BU6 H1   H  N N 21  
A1BU6 H2   H  N N 22  
A1BU6 H3   H  N N 23  
A1BU6 H4   H  N N 24  
A1BU6 H5   H  N N 25  
A1BU6 H6   H  N N 26  
A1BU6 H7   H  N N 27  
A1BU6 H8   H  N N 28  
A1BU6 H9   H  N N 29  
A1BU6 H10  H  N N 30  
A1BU6 H11  H  N N 31  
A1BU6 H12  H  N N 32  
A1BU6 H13  H  N N 33  
A1BU6 H14  H  N N 34  
A1BU6 H15  H  N N 35  
A1BU6 H16  H  N N 36  
A1BU6 H17  H  N N 37  
ALA   N    N  N N 38  
ALA   CA   C  N S 39  
ALA   C    C  N N 40  
ALA   O    O  N N 41  
ALA   CB   C  N N 42  
ALA   OXT  O  N N 43  
ALA   H    H  N N 44  
ALA   H2   H  N N 45  
ALA   HA   H  N N 46  
ALA   HB1  H  N N 47  
ALA   HB2  H  N N 48  
ALA   HB3  H  N N 49  
ALA   HXT  H  N N 50  
ARG   N    N  N N 51  
ARG   CA   C  N S 52  
ARG   C    C  N N 53  
ARG   O    O  N N 54  
ARG   CB   C  N N 55  
ARG   CG   C  N N 56  
ARG   CD   C  N N 57  
ARG   NE   N  N N 58  
ARG   CZ   C  N N 59  
ARG   NH1  N  N N 60  
ARG   NH2  N  N N 61  
ARG   OXT  O  N N 62  
ARG   H    H  N N 63  
ARG   H2   H  N N 64  
ARG   HA   H  N N 65  
ARG   HB2  H  N N 66  
ARG   HB3  H  N N 67  
ARG   HG2  H  N N 68  
ARG   HG3  H  N N 69  
ARG   HD2  H  N N 70  
ARG   HD3  H  N N 71  
ARG   HE   H  N N 72  
ARG   HH11 H  N N 73  
ARG   HH12 H  N N 74  
ARG   HH21 H  N N 75  
ARG   HH22 H  N N 76  
ARG   HXT  H  N N 77  
ASN   N    N  N N 78  
ASN   CA   C  N S 79  
ASN   C    C  N N 80  
ASN   O    O  N N 81  
ASN   CB   C  N N 82  
ASN   CG   C  N N 83  
ASN   OD1  O  N N 84  
ASN   ND2  N  N N 85  
ASN   OXT  O  N N 86  
ASN   H    H  N N 87  
ASN   H2   H  N N 88  
ASN   HA   H  N N 89  
ASN   HB2  H  N N 90  
ASN   HB3  H  N N 91  
ASN   HD21 H  N N 92  
ASN   HD22 H  N N 93  
ASN   HXT  H  N N 94  
ASP   N    N  N N 95  
ASP   CA   C  N S 96  
ASP   C    C  N N 97  
ASP   O    O  N N 98  
ASP   CB   C  N N 99  
ASP   CG   C  N N 100 
ASP   OD1  O  N N 101 
ASP   OD2  O  N N 102 
ASP   OXT  O  N N 103 
ASP   H    H  N N 104 
ASP   H2   H  N N 105 
ASP   HA   H  N N 106 
ASP   HB2  H  N N 107 
ASP   HB3  H  N N 108 
ASP   HD2  H  N N 109 
ASP   HXT  H  N N 110 
CL    CL   CL N N 111 
CYS   N    N  N N 112 
CYS   CA   C  N R 113 
CYS   C    C  N N 114 
CYS   O    O  N N 115 
CYS   CB   C  N N 116 
CYS   SG   S  N N 117 
CYS   OXT  O  N N 118 
CYS   H    H  N N 119 
CYS   H2   H  N N 120 
CYS   HA   H  N N 121 
CYS   HB2  H  N N 122 
CYS   HB3  H  N N 123 
CYS   HG   H  N N 124 
CYS   HXT  H  N N 125 
GLN   N    N  N N 126 
GLN   CA   C  N S 127 
GLN   C    C  N N 128 
GLN   O    O  N N 129 
GLN   CB   C  N N 130 
GLN   CG   C  N N 131 
GLN   CD   C  N N 132 
GLN   OE1  O  N N 133 
GLN   NE2  N  N N 134 
GLN   OXT  O  N N 135 
GLN   H    H  N N 136 
GLN   H2   H  N N 137 
GLN   HA   H  N N 138 
GLN   HB2  H  N N 139 
GLN   HB3  H  N N 140 
GLN   HG2  H  N N 141 
GLN   HG3  H  N N 142 
GLN   HE21 H  N N 143 
GLN   HE22 H  N N 144 
GLN   HXT  H  N N 145 
GLU   N    N  N N 146 
GLU   CA   C  N S 147 
GLU   C    C  N N 148 
GLU   O    O  N N 149 
GLU   CB   C  N N 150 
GLU   CG   C  N N 151 
GLU   CD   C  N N 152 
GLU   OE1  O  N N 153 
GLU   OE2  O  N N 154 
GLU   OXT  O  N N 155 
GLU   H    H  N N 156 
GLU   H2   H  N N 157 
GLU   HA   H  N N 158 
GLU   HB2  H  N N 159 
GLU   HB3  H  N N 160 
GLU   HG2  H  N N 161 
GLU   HG3  H  N N 162 
GLU   HE2  H  N N 163 
GLU   HXT  H  N N 164 
GLY   N    N  N N 165 
GLY   CA   C  N N 166 
GLY   C    C  N N 167 
GLY   O    O  N N 168 
GLY   OXT  O  N N 169 
GLY   H    H  N N 170 
GLY   H2   H  N N 171 
GLY   HA2  H  N N 172 
GLY   HA3  H  N N 173 
GLY   HXT  H  N N 174 
HIS   N    N  N N 175 
HIS   CA   C  N S 176 
HIS   C    C  N N 177 
HIS   O    O  N N 178 
HIS   CB   C  N N 179 
HIS   CG   C  Y N 180 
HIS   ND1  N  Y N 181 
HIS   CD2  C  Y N 182 
HIS   CE1  C  Y N 183 
HIS   NE2  N  Y N 184 
HIS   OXT  O  N N 185 
HIS   H    H  N N 186 
HIS   H2   H  N N 187 
HIS   HA   H  N N 188 
HIS   HB2  H  N N 189 
HIS   HB3  H  N N 190 
HIS   HD1  H  N N 191 
HIS   HD2  H  N N 192 
HIS   HE1  H  N N 193 
HIS   HE2  H  N N 194 
HIS   HXT  H  N N 195 
HOH   O    O  N N 196 
HOH   H1   H  N N 197 
HOH   H2   H  N N 198 
ILE   N    N  N N 199 
ILE   CA   C  N S 200 
ILE   C    C  N N 201 
ILE   O    O  N N 202 
ILE   CB   C  N S 203 
ILE   CG1  C  N N 204 
ILE   CG2  C  N N 205 
ILE   CD1  C  N N 206 
ILE   OXT  O  N N 207 
ILE   H    H  N N 208 
ILE   H2   H  N N 209 
ILE   HA   H  N N 210 
ILE   HB   H  N N 211 
ILE   HG12 H  N N 212 
ILE   HG13 H  N N 213 
ILE   HG21 H  N N 214 
ILE   HG22 H  N N 215 
ILE   HG23 H  N N 216 
ILE   HD11 H  N N 217 
ILE   HD12 H  N N 218 
ILE   HD13 H  N N 219 
ILE   HXT  H  N N 220 
IOD   I    I  N N 221 
LEU   N    N  N N 222 
LEU   CA   C  N S 223 
LEU   C    C  N N 224 
LEU   O    O  N N 225 
LEU   CB   C  N N 226 
LEU   CG   C  N N 227 
LEU   CD1  C  N N 228 
LEU   CD2  C  N N 229 
LEU   OXT  O  N N 230 
LEU   H    H  N N 231 
LEU   H2   H  N N 232 
LEU   HA   H  N N 233 
LEU   HB2  H  N N 234 
LEU   HB3  H  N N 235 
LEU   HG   H  N N 236 
LEU   HD11 H  N N 237 
LEU   HD12 H  N N 238 
LEU   HD13 H  N N 239 
LEU   HD21 H  N N 240 
LEU   HD22 H  N N 241 
LEU   HD23 H  N N 242 
LEU   HXT  H  N N 243 
LYS   N    N  N N 244 
LYS   CA   C  N S 245 
LYS   C    C  N N 246 
LYS   O    O  N N 247 
LYS   CB   C  N N 248 
LYS   CG   C  N N 249 
LYS   CD   C  N N 250 
LYS   CE   C  N N 251 
LYS   NZ   N  N N 252 
LYS   OXT  O  N N 253 
LYS   H    H  N N 254 
LYS   H2   H  N N 255 
LYS   HA   H  N N 256 
LYS   HB2  H  N N 257 
LYS   HB3  H  N N 258 
LYS   HG2  H  N N 259 
LYS   HG3  H  N N 260 
LYS   HD2  H  N N 261 
LYS   HD3  H  N N 262 
LYS   HE2  H  N N 263 
LYS   HE3  H  N N 264 
LYS   HZ1  H  N N 265 
LYS   HZ2  H  N N 266 
LYS   HZ3  H  N N 267 
LYS   HXT  H  N N 268 
MET   N    N  N N 269 
MET   CA   C  N S 270 
MET   C    C  N N 271 
MET   O    O  N N 272 
MET   CB   C  N N 273 
MET   CG   C  N N 274 
MET   SD   S  N N 275 
MET   CE   C  N N 276 
MET   OXT  O  N N 277 
MET   H    H  N N 278 
MET   H2   H  N N 279 
MET   HA   H  N N 280 
MET   HB2  H  N N 281 
MET   HB3  H  N N 282 
MET   HG2  H  N N 283 
MET   HG3  H  N N 284 
MET   HE1  H  N N 285 
MET   HE2  H  N N 286 
MET   HE3  H  N N 287 
MET   HXT  H  N N 288 
PHE   N    N  N N 289 
PHE   CA   C  N S 290 
PHE   C    C  N N 291 
PHE   O    O  N N 292 
PHE   CB   C  N N 293 
PHE   CG   C  Y N 294 
PHE   CD1  C  Y N 295 
PHE   CD2  C  Y N 296 
PHE   CE1  C  Y N 297 
PHE   CE2  C  Y N 298 
PHE   CZ   C  Y N 299 
PHE   OXT  O  N N 300 
PHE   H    H  N N 301 
PHE   H2   H  N N 302 
PHE   HA   H  N N 303 
PHE   HB2  H  N N 304 
PHE   HB3  H  N N 305 
PHE   HD1  H  N N 306 
PHE   HD2  H  N N 307 
PHE   HE1  H  N N 308 
PHE   HE2  H  N N 309 
PHE   HZ   H  N N 310 
PHE   HXT  H  N N 311 
PRO   N    N  N N 312 
PRO   CA   C  N S 313 
PRO   C    C  N N 314 
PRO   O    O  N N 315 
PRO   CB   C  N N 316 
PRO   CG   C  N N 317 
PRO   CD   C  N N 318 
PRO   OXT  O  N N 319 
PRO   H    H  N N 320 
PRO   HA   H  N N 321 
PRO   HB2  H  N N 322 
PRO   HB3  H  N N 323 
PRO   HG2  H  N N 324 
PRO   HG3  H  N N 325 
PRO   HD2  H  N N 326 
PRO   HD3  H  N N 327 
PRO   HXT  H  N N 328 
SER   N    N  N N 329 
SER   CA   C  N S 330 
SER   C    C  N N 331 
SER   O    O  N N 332 
SER   CB   C  N N 333 
SER   OG   O  N N 334 
SER   OXT  O  N N 335 
SER   H    H  N N 336 
SER   H2   H  N N 337 
SER   HA   H  N N 338 
SER   HB2  H  N N 339 
SER   HB3  H  N N 340 
SER   HG   H  N N 341 
SER   HXT  H  N N 342 
THR   N    N  N N 343 
THR   CA   C  N S 344 
THR   C    C  N N 345 
THR   O    O  N N 346 
THR   CB   C  N R 347 
THR   OG1  O  N N 348 
THR   CG2  C  N N 349 
THR   OXT  O  N N 350 
THR   H    H  N N 351 
THR   H2   H  N N 352 
THR   HA   H  N N 353 
THR   HB   H  N N 354 
THR   HG1  H  N N 355 
THR   HG21 H  N N 356 
THR   HG22 H  N N 357 
THR   HG23 H  N N 358 
THR   HXT  H  N N 359 
TRP   N    N  N N 360 
TRP   CA   C  N S 361 
TRP   C    C  N N 362 
TRP   O    O  N N 363 
TRP   CB   C  N N 364 
TRP   CG   C  Y N 365 
TRP   CD1  C  Y N 366 
TRP   CD2  C  Y N 367 
TRP   NE1  N  Y N 368 
TRP   CE2  C  Y N 369 
TRP   CE3  C  Y N 370 
TRP   CZ2  C  Y N 371 
TRP   CZ3  C  Y N 372 
TRP   CH2  C  Y N 373 
TRP   OXT  O  N N 374 
TRP   H    H  N N 375 
TRP   H2   H  N N 376 
TRP   HA   H  N N 377 
TRP   HB2  H  N N 378 
TRP   HB3  H  N N 379 
TRP   HD1  H  N N 380 
TRP   HE1  H  N N 381 
TRP   HE3  H  N N 382 
TRP   HZ2  H  N N 383 
TRP   HZ3  H  N N 384 
TRP   HH2  H  N N 385 
TRP   HXT  H  N N 386 
TYR   N    N  N N 387 
TYR   CA   C  N S 388 
TYR   C    C  N N 389 
TYR   O    O  N N 390 
TYR   CB   C  N N 391 
TYR   CG   C  Y N 392 
TYR   CD1  C  Y N 393 
TYR   CD2  C  Y N 394 
TYR   CE1  C  Y N 395 
TYR   CE2  C  Y N 396 
TYR   CZ   C  Y N 397 
TYR   OH   O  N N 398 
TYR   OXT  O  N N 399 
TYR   H    H  N N 400 
TYR   H2   H  N N 401 
TYR   HA   H  N N 402 
TYR   HB2  H  N N 403 
TYR   HB3  H  N N 404 
TYR   HD1  H  N N 405 
TYR   HD2  H  N N 406 
TYR   HE1  H  N N 407 
TYR   HE2  H  N N 408 
TYR   HH   H  N N 409 
TYR   HXT  H  N N 410 
VAL   N    N  N N 411 
VAL   CA   C  N S 412 
VAL   C    C  N N 413 
VAL   O    O  N N 414 
VAL   CB   C  N N 415 
VAL   CG1  C  N N 416 
VAL   CG2  C  N N 417 
VAL   OXT  O  N N 418 
VAL   H    H  N N 419 
VAL   H2   H  N N 420 
VAL   HA   H  N N 421 
VAL   HB   H  N N 422 
VAL   HG11 H  N N 423 
VAL   HG12 H  N N 424 
VAL   HG13 H  N N 425 
VAL   HG21 H  N N 426 
VAL   HG22 H  N N 427 
VAL   HG23 H  N N 428 
VAL   HXT  H  N N 429 
# 
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 
A1BU6 C14 C7   sing N N 1   
A1BU6 C14 C11  sing N N 2   
A1BU6 C7  C5   sing N N 3   
A1BU6 C7  N9   sing N N 4   
A1BU6 C11 C10  sing N N 5   
A1BU6 C11 O13  sing N N 6   
A1BU6 C6  C5   doub Y N 7   
A1BU6 C6  C1   sing Y N 8   
A1BU6 C5  C4   sing Y N 9   
A1BU6 N9  C10  sing N N 10  
A1BU6 N9  C15  sing N N 11  
A1BU6 O16 C15  doub N N 12  
A1BU6 C1  C2   doub Y N 13  
A1BU6 C4  O13  sing N N 14  
A1BU6 C4  C3   doub Y N 15  
A1BU6 C15 C17  sing N N 16  
A1BU6 C22 C17  sing N N 17  
A1BU6 C2  C3   sing Y N 18  
A1BU6 C17 C19  sing N N 19  
A1BU6 C17 C18  sing N N 20  
A1BU6 C19 F20  sing N N 21  
A1BU6 C19 F21  sing N N 22  
A1BU6 C1  H1   sing N N 23  
A1BU6 C2  H2   sing N N 24  
A1BU6 C3  H3   sing N N 25  
A1BU6 C6  H4   sing N N 26  
A1BU6 C7  H5   sing N N 27  
A1BU6 C11 H6   sing N N 28  
A1BU6 C18 H7   sing N N 29  
A1BU6 C18 H8   sing N N 30  
A1BU6 C18 H9   sing N N 31  
A1BU6 C19 H10  sing N N 32  
A1BU6 C10 H11  sing N N 33  
A1BU6 C10 H12  sing N N 34  
A1BU6 C14 H13  sing N N 35  
A1BU6 C14 H14  sing N N 36  
A1BU6 C22 H15  sing N N 37  
A1BU6 C22 H16  sing N N 38  
A1BU6 C22 H17  sing N N 39  
ALA   N   CA   sing N N 40  
ALA   N   H    sing N N 41  
ALA   N   H2   sing N N 42  
ALA   CA  C    sing N N 43  
ALA   CA  CB   sing N N 44  
ALA   CA  HA   sing N N 45  
ALA   C   O    doub N N 46  
ALA   C   OXT  sing N N 47  
ALA   CB  HB1  sing N N 48  
ALA   CB  HB2  sing N N 49  
ALA   CB  HB3  sing N N 50  
ALA   OXT HXT  sing N N 51  
ARG   N   CA   sing N N 52  
ARG   N   H    sing N N 53  
ARG   N   H2   sing N N 54  
ARG   CA  C    sing N N 55  
ARG   CA  CB   sing N N 56  
ARG   CA  HA   sing N N 57  
ARG   C   O    doub N N 58  
ARG   C   OXT  sing N N 59  
ARG   CB  CG   sing N N 60  
ARG   CB  HB2  sing N N 61  
ARG   CB  HB3  sing N N 62  
ARG   CG  CD   sing N N 63  
ARG   CG  HG2  sing N N 64  
ARG   CG  HG3  sing N N 65  
ARG   CD  NE   sing N N 66  
ARG   CD  HD2  sing N N 67  
ARG   CD  HD3  sing N N 68  
ARG   NE  CZ   sing N N 69  
ARG   NE  HE   sing N N 70  
ARG   CZ  NH1  sing N N 71  
ARG   CZ  NH2  doub N N 72  
ARG   NH1 HH11 sing N N 73  
ARG   NH1 HH12 sing N N 74  
ARG   NH2 HH21 sing N N 75  
ARG   NH2 HH22 sing N N 76  
ARG   OXT HXT  sing N N 77  
ASN   N   CA   sing N N 78  
ASN   N   H    sing N N 79  
ASN   N   H2   sing N N 80  
ASN   CA  C    sing N N 81  
ASN   CA  CB   sing N N 82  
ASN   CA  HA   sing N N 83  
ASN   C   O    doub N N 84  
ASN   C   OXT  sing N N 85  
ASN   CB  CG   sing N N 86  
ASN   CB  HB2  sing N N 87  
ASN   CB  HB3  sing N N 88  
ASN   CG  OD1  doub N N 89  
ASN   CG  ND2  sing N N 90  
ASN   ND2 HD21 sing N N 91  
ASN   ND2 HD22 sing N N 92  
ASN   OXT HXT  sing N N 93  
ASP   N   CA   sing N N 94  
ASP   N   H    sing N N 95  
ASP   N   H2   sing N N 96  
ASP   CA  C    sing N N 97  
ASP   CA  CB   sing N N 98  
ASP   CA  HA   sing N N 99  
ASP   C   O    doub N N 100 
ASP   C   OXT  sing N N 101 
ASP   CB  CG   sing N N 102 
ASP   CB  HB2  sing N N 103 
ASP   CB  HB3  sing N N 104 
ASP   CG  OD1  doub N N 105 
ASP   CG  OD2  sing N N 106 
ASP   OD2 HD2  sing N N 107 
ASP   OXT HXT  sing N N 108 
CYS   N   CA   sing N N 109 
CYS   N   H    sing N N 110 
CYS   N   H2   sing N N 111 
CYS   CA  C    sing N N 112 
CYS   CA  CB   sing N N 113 
CYS   CA  HA   sing N N 114 
CYS   C   O    doub N N 115 
CYS   C   OXT  sing N N 116 
CYS   CB  SG   sing N N 117 
CYS   CB  HB2  sing N N 118 
CYS   CB  HB3  sing N N 119 
CYS   SG  HG   sing N N 120 
CYS   OXT HXT  sing N N 121 
GLN   N   CA   sing N N 122 
GLN   N   H    sing N N 123 
GLN   N   H2   sing N N 124 
GLN   CA  C    sing N N 125 
GLN   CA  CB   sing N N 126 
GLN   CA  HA   sing N N 127 
GLN   C   O    doub N N 128 
GLN   C   OXT  sing N N 129 
GLN   CB  CG   sing N N 130 
GLN   CB  HB2  sing N N 131 
GLN   CB  HB3  sing N N 132 
GLN   CG  CD   sing N N 133 
GLN   CG  HG2  sing N N 134 
GLN   CG  HG3  sing N N 135 
GLN   CD  OE1  doub N N 136 
GLN   CD  NE2  sing N N 137 
GLN   NE2 HE21 sing N N 138 
GLN   NE2 HE22 sing N N 139 
GLN   OXT HXT  sing N N 140 
GLU   N   CA   sing N N 141 
GLU   N   H    sing N N 142 
GLU   N   H2   sing N N 143 
GLU   CA  C    sing N N 144 
GLU   CA  CB   sing N N 145 
GLU   CA  HA   sing N N 146 
GLU   C   O    doub N N 147 
GLU   C   OXT  sing N N 148 
GLU   CB  CG   sing N N 149 
GLU   CB  HB2  sing N N 150 
GLU   CB  HB3  sing N N 151 
GLU   CG  CD   sing N N 152 
GLU   CG  HG2  sing N N 153 
GLU   CG  HG3  sing N N 154 
GLU   CD  OE1  doub N N 155 
GLU   CD  OE2  sing N N 156 
GLU   OE2 HE2  sing N N 157 
GLU   OXT HXT  sing N N 158 
GLY   N   CA   sing N N 159 
GLY   N   H    sing N N 160 
GLY   N   H2   sing N N 161 
GLY   CA  C    sing N N 162 
GLY   CA  HA2  sing N N 163 
GLY   CA  HA3  sing N N 164 
GLY   C   O    doub N N 165 
GLY   C   OXT  sing N N 166 
GLY   OXT HXT  sing N N 167 
HIS   N   CA   sing N N 168 
HIS   N   H    sing N N 169 
HIS   N   H2   sing N N 170 
HIS   CA  C    sing N N 171 
HIS   CA  CB   sing N N 172 
HIS   CA  HA   sing N N 173 
HIS   C   O    doub N N 174 
HIS   C   OXT  sing N N 175 
HIS   CB  CG   sing N N 176 
HIS   CB  HB2  sing N N 177 
HIS   CB  HB3  sing N N 178 
HIS   CG  ND1  sing Y N 179 
HIS   CG  CD2  doub Y N 180 
HIS   ND1 CE1  doub Y N 181 
HIS   ND1 HD1  sing N N 182 
HIS   CD2 NE2  sing Y N 183 
HIS   CD2 HD2  sing N N 184 
HIS   CE1 NE2  sing Y N 185 
HIS   CE1 HE1  sing N N 186 
HIS   NE2 HE2  sing N N 187 
HIS   OXT HXT  sing N N 188 
HOH   O   H1   sing N N 189 
HOH   O   H2   sing N N 190 
ILE   N   CA   sing N N 191 
ILE   N   H    sing N N 192 
ILE   N   H2   sing N N 193 
ILE   CA  C    sing N N 194 
ILE   CA  CB   sing N N 195 
ILE   CA  HA   sing N N 196 
ILE   C   O    doub N N 197 
ILE   C   OXT  sing N N 198 
ILE   CB  CG1  sing N N 199 
ILE   CB  CG2  sing N N 200 
ILE   CB  HB   sing N N 201 
ILE   CG1 CD1  sing N N 202 
ILE   CG1 HG12 sing N N 203 
ILE   CG1 HG13 sing N N 204 
ILE   CG2 HG21 sing N N 205 
ILE   CG2 HG22 sing N N 206 
ILE   CG2 HG23 sing N N 207 
ILE   CD1 HD11 sing N N 208 
ILE   CD1 HD12 sing N N 209 
ILE   CD1 HD13 sing N N 210 
ILE   OXT HXT  sing N N 211 
LEU   N   CA   sing N N 212 
LEU   N   H    sing N N 213 
LEU   N   H2   sing N N 214 
LEU   CA  C    sing N N 215 
LEU   CA  CB   sing N N 216 
LEU   CA  HA   sing N N 217 
LEU   C   O    doub N N 218 
LEU   C   OXT  sing N N 219 
LEU   CB  CG   sing N N 220 
LEU   CB  HB2  sing N N 221 
LEU   CB  HB3  sing N N 222 
LEU   CG  CD1  sing N N 223 
LEU   CG  CD2  sing N N 224 
LEU   CG  HG   sing N N 225 
LEU   CD1 HD11 sing N N 226 
LEU   CD1 HD12 sing N N 227 
LEU   CD1 HD13 sing N N 228 
LEU   CD2 HD21 sing N N 229 
LEU   CD2 HD22 sing N N 230 
LEU   CD2 HD23 sing N N 231 
LEU   OXT HXT  sing N N 232 
LYS   N   CA   sing N N 233 
LYS   N   H    sing N N 234 
LYS   N   H2   sing N N 235 
LYS   CA  C    sing N N 236 
LYS   CA  CB   sing N N 237 
LYS   CA  HA   sing N N 238 
LYS   C   O    doub N N 239 
LYS   C   OXT  sing N N 240 
LYS   CB  CG   sing N N 241 
LYS   CB  HB2  sing N N 242 
LYS   CB  HB3  sing N N 243 
LYS   CG  CD   sing N N 244 
LYS   CG  HG2  sing N N 245 
LYS   CG  HG3  sing N N 246 
LYS   CD  CE   sing N N 247 
LYS   CD  HD2  sing N N 248 
LYS   CD  HD3  sing N N 249 
LYS   CE  NZ   sing N N 250 
LYS   CE  HE2  sing N N 251 
LYS   CE  HE3  sing N N 252 
LYS   NZ  HZ1  sing N N 253 
LYS   NZ  HZ2  sing N N 254 
LYS   NZ  HZ3  sing N N 255 
LYS   OXT HXT  sing N N 256 
MET   N   CA   sing N N 257 
MET   N   H    sing N N 258 
MET   N   H2   sing N N 259 
MET   CA  C    sing N N 260 
MET   CA  CB   sing N N 261 
MET   CA  HA   sing N N 262 
MET   C   O    doub N N 263 
MET   C   OXT  sing N N 264 
MET   CB  CG   sing N N 265 
MET   CB  HB2  sing N N 266 
MET   CB  HB3  sing N N 267 
MET   CG  SD   sing N N 268 
MET   CG  HG2  sing N N 269 
MET   CG  HG3  sing N N 270 
MET   SD  CE   sing N N 271 
MET   CE  HE1  sing N N 272 
MET   CE  HE2  sing N N 273 
MET   CE  HE3  sing N N 274 
MET   OXT HXT  sing N N 275 
PHE   N   CA   sing N N 276 
PHE   N   H    sing N N 277 
PHE   N   H2   sing N N 278 
PHE   CA  C    sing N N 279 
PHE   CA  CB   sing N N 280 
PHE   CA  HA   sing N N 281 
PHE   C   O    doub N N 282 
PHE   C   OXT  sing N N 283 
PHE   CB  CG   sing N N 284 
PHE   CB  HB2  sing N N 285 
PHE   CB  HB3  sing N N 286 
PHE   CG  CD1  doub Y N 287 
PHE   CG  CD2  sing Y N 288 
PHE   CD1 CE1  sing Y N 289 
PHE   CD1 HD1  sing N N 290 
PHE   CD2 CE2  doub Y N 291 
PHE   CD2 HD2  sing N N 292 
PHE   CE1 CZ   doub Y N 293 
PHE   CE1 HE1  sing N N 294 
PHE   CE2 CZ   sing Y N 295 
PHE   CE2 HE2  sing N N 296 
PHE   CZ  HZ   sing N N 297 
PHE   OXT HXT  sing N N 298 
PRO   N   CA   sing N N 299 
PRO   N   CD   sing N N 300 
PRO   N   H    sing N N 301 
PRO   CA  C    sing N N 302 
PRO   CA  CB   sing N N 303 
PRO   CA  HA   sing N N 304 
PRO   C   O    doub N N 305 
PRO   C   OXT  sing N N 306 
PRO   CB  CG   sing N N 307 
PRO   CB  HB2  sing N N 308 
PRO   CB  HB3  sing N N 309 
PRO   CG  CD   sing N N 310 
PRO   CG  HG2  sing N N 311 
PRO   CG  HG3  sing N N 312 
PRO   CD  HD2  sing N N 313 
PRO   CD  HD3  sing N N 314 
PRO   OXT HXT  sing N N 315 
SER   N   CA   sing N N 316 
SER   N   H    sing N N 317 
SER   N   H2   sing N N 318 
SER   CA  C    sing N N 319 
SER   CA  CB   sing N N 320 
SER   CA  HA   sing N N 321 
SER   C   O    doub N N 322 
SER   C   OXT  sing N N 323 
SER   CB  OG   sing N N 324 
SER   CB  HB2  sing N N 325 
SER   CB  HB3  sing N N 326 
SER   OG  HG   sing N N 327 
SER   OXT HXT  sing N N 328 
THR   N   CA   sing N N 329 
THR   N   H    sing N N 330 
THR   N   H2   sing N N 331 
THR   CA  C    sing N N 332 
THR   CA  CB   sing N N 333 
THR   CA  HA   sing N N 334 
THR   C   O    doub N N 335 
THR   C   OXT  sing N N 336 
THR   CB  OG1  sing N N 337 
THR   CB  CG2  sing N N 338 
THR   CB  HB   sing N N 339 
THR   OG1 HG1  sing N N 340 
THR   CG2 HG21 sing N N 341 
THR   CG2 HG22 sing N N 342 
THR   CG2 HG23 sing N N 343 
THR   OXT HXT  sing N N 344 
TRP   N   CA   sing N N 345 
TRP   N   H    sing N N 346 
TRP   N   H2   sing N N 347 
TRP   CA  C    sing N N 348 
TRP   CA  CB   sing N N 349 
TRP   CA  HA   sing N N 350 
TRP   C   O    doub N N 351 
TRP   C   OXT  sing N N 352 
TRP   CB  CG   sing N N 353 
TRP   CB  HB2  sing N N 354 
TRP   CB  HB3  sing N N 355 
TRP   CG  CD1  doub Y N 356 
TRP   CG  CD2  sing Y N 357 
TRP   CD1 NE1  sing Y N 358 
TRP   CD1 HD1  sing N N 359 
TRP   CD2 CE2  doub Y N 360 
TRP   CD2 CE3  sing Y N 361 
TRP   NE1 CE2  sing Y N 362 
TRP   NE1 HE1  sing N N 363 
TRP   CE2 CZ2  sing Y N 364 
TRP   CE3 CZ3  doub Y N 365 
TRP   CE3 HE3  sing N N 366 
TRP   CZ2 CH2  doub Y N 367 
TRP   CZ2 HZ2  sing N N 368 
TRP   CZ3 CH2  sing Y N 369 
TRP   CZ3 HZ3  sing N N 370 
TRP   CH2 HH2  sing N N 371 
TRP   OXT HXT  sing N N 372 
TYR   N   CA   sing N N 373 
TYR   N   H    sing N N 374 
TYR   N   H2   sing N N 375 
TYR   CA  C    sing N N 376 
TYR   CA  CB   sing N N 377 
TYR   CA  HA   sing N N 378 
TYR   C   O    doub N N 379 
TYR   C   OXT  sing N N 380 
TYR   CB  CG   sing N N 381 
TYR   CB  HB2  sing N N 382 
TYR   CB  HB3  sing N N 383 
TYR   CG  CD1  doub Y N 384 
TYR   CG  CD2  sing Y N 385 
TYR   CD1 CE1  sing Y N 386 
TYR   CD1 HD1  sing N N 387 
TYR   CD2 CE2  doub Y N 388 
TYR   CD2 HD2  sing N N 389 
TYR   CE1 CZ   doub Y N 390 
TYR   CE1 HE1  sing N N 391 
TYR   CE2 CZ   sing Y N 392 
TYR   CE2 HE2  sing N N 393 
TYR   CZ  OH   sing N N 394 
TYR   OH  HH   sing N N 395 
TYR   OXT HXT  sing N N 396 
VAL   N   CA   sing N N 397 
VAL   N   H    sing N N 398 
VAL   N   H2   sing N N 399 
VAL   CA  C    sing N N 400 
VAL   CA  CB   sing N N 401 
VAL   CA  HA   sing N N 402 
VAL   C   O    doub N N 403 
VAL   C   OXT  sing N N 404 
VAL   CB  CG1  sing N N 405 
VAL   CB  CG2  sing N N 406 
VAL   CB  HB   sing N N 407 
VAL   CG1 HG11 sing N N 408 
VAL   CG1 HG12 sing N N 409 
VAL   CG1 HG13 sing N N 410 
VAL   CG2 HG21 sing N N 411 
VAL   CG2 HG22 sing N N 412 
VAL   CG2 HG23 sing N N 413 
VAL   OXT HXT  sing N N 414 
# 
_pdbx_audit_support.funding_organization   'Not funded' 
_pdbx_audit_support.country                ? 
_pdbx_audit_support.grant_number           ? 
_pdbx_audit_support.ordinal                1 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'experimental model' 
_pdbx_initial_refinement_model.source_name      PDB 
_pdbx_initial_refinement_model.accession_code   4ith 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    9MZY 
_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]   0.021139 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000000 
_atom_sites.fract_transf_matrix[2][1]   -0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.010508 
_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]   0.007805 
_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  
CL 
F  
I  
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   . ASN   A 1 1   ? 7.916   -11.760 47.314 1.00 117.68 ?  8   ASN   A N   1 
ATOM   2    C  CA  . ASN   A 1 1   ? 8.247   -12.497 48.579 1.00 118.04 ?  8   ASN   A CA  1 
ATOM   3    C  C   . ASN   A 1 1   ? 9.746   -12.671 48.803 1.00 111.84 ?  8   ASN   A C   1 
ATOM   4    O  O   . ASN   A 1 1   ? 10.533  -12.679 47.853 1.00 103.75 ?  8   ASN   A O   1 
ATOM   5    C  CB  . ASN   A 1 1   ? 7.574   -13.882 48.628 1.00 124.31 ?  8   ASN   A CB  1 
ATOM   6    C  CG  . ASN   A 1 1   ? 6.092   -13.797 48.924 1.00 131.73 ?  8   ASN   A CG  1 
ATOM   7    O  OD1 . ASN   A 1 1   ? 5.412   -12.895 48.442 1.00 148.74 ?  8   ASN   A OD1 1 
ATOM   8    N  ND2 . ASN   A 1 1   ? 5.578   -14.735 49.722 1.00 135.66 ?  8   ASN   A ND2 1 
ATOM   9    N  N   . VAL   A 1 2   ? 10.104  -12.818 50.081 1.00 104.69 ?  9   VAL   A N   1 
ATOM   10   C  CA  . VAL   A 1 2   ? 11.472  -13.129 50.521 1.00 88.31  ?  9   VAL   A CA  1 
ATOM   11   C  C   . VAL   A 1 2   ? 11.786  -14.617 50.302 1.00 82.66  ?  9   VAL   A C   1 
ATOM   12   O  O   . VAL   A 1 2   ? 10.932  -15.460 50.554 1.00 92.05  ?  9   VAL   A O   1 
ATOM   13   C  CB  . VAL   A 1 2   ? 11.697  -12.715 52.012 1.00 86.19  ?  9   VAL   A CB  1 
ATOM   14   C  CG1 . VAL   A 1 2   ? 10.957  -13.602 53.016 1.00 85.69  ?  9   VAL   A CG1 1 
ATOM   15   C  CG2 . VAL   A 1 2   ? 13.180  -12.675 52.352 1.00 86.58  ?  9   VAL   A CG2 1 
ATOM   16   N  N   . ILE   A 1 3   ? 12.995  -14.915 49.816 1.00 75.84  ?  10  ILE   A N   1 
ATOM   17   C  CA  . ILE   A 1 3   ? 13.474  -16.283 49.620 1.00 83.67  ?  10  ILE   A CA  1 
ATOM   18   C  C   . ILE   A 1 3   ? 13.935  -16.826 50.984 1.00 82.17  ?  10  ILE   A C   1 
ATOM   19   O  O   . ILE   A 1 3   ? 14.826  -16.244 51.607 1.00 77.16  ?  10  ILE   A O   1 
ATOM   20   C  CB  . ILE   A 1 3   ? 14.623  -16.345 48.559 1.00 82.91  ?  10  ILE   A CB  1 
ATOM   21   C  CG1 . ILE   A 1 3   ? 14.086  -15.930 47.176 1.00 81.51  ?  10  ILE   A CG1 1 
ATOM   22   C  CG2 . ILE   A 1 3   ? 15.233  -17.754 48.454 1.00 90.30  ?  10  ILE   A CG2 1 
ATOM   23   C  CD1 . ILE   A 1 3   ? 15.147  -15.574 46.154 1.00 82.78  ?  10  ILE   A CD1 1 
ATOM   24   N  N   . LYS   A 1 4   ? 13.299  -17.913 51.440 1.00 83.71  ?  11  LYS   A N   1 
ATOM   25   C  CA  . LYS   A 1 4   ? 13.699  -18.610 52.671 1.00 85.65  ?  11  LYS   A CA  1 
ATOM   26   C  C   . LYS   A 1 4   ? 14.797  -19.610 52.321 1.00 78.69  ?  11  LYS   A C   1 
ATOM   27   O  O   . LYS   A 1 4   ? 14.568  -20.520 51.533 1.00 89.90  ?  11  LYS   A O   1 
ATOM   28   C  CB  . LYS   A 1 4   ? 12.508  -19.304 53.339 1.00 90.76  ?  11  LYS   A CB  1 
ATOM   29   C  CG  . LYS   A 1 4   ? 11.553  -18.329 54.019 1.00 95.85  ?  11  LYS   A CG  1 
ATOM   30   C  CD  . LYS   A 1 4   ? 10.347  -19.040 54.628 1.00 104.33 ?  11  LYS   A CD  1 
ATOM   31   C  CE  . LYS   A 1 4   ? 9.276   -18.111 55.084 0.00 103.22 ?  11  LYS   A CE  1 
ATOM   32   N  NZ  . LYS   A 1 4   ? 8.052   -18.840 55.517 0.00 107.03 ?  11  LYS   A NZ  1 
ATOM   33   N  N   . MET   A 1 5   ? 15.991  -19.389 52.879 1.00 73.18  ?  12  MET   A N   1 
ATOM   34   C  CA  . MET   A 1 5   ? 17.197  -20.178 52.621 1.00 77.98  ?  12  MET   A CA  1 
ATOM   35   C  C   . MET   A 1 5   ? 17.506  -21.069 53.821 1.00 79.31  ?  12  MET   A C   1 
ATOM   36   O  O   . MET   A 1 5   ? 17.005  -20.844 54.934 1.00 90.20  ?  12  MET   A O   1 
ATOM   37   C  CB  . MET   A 1 5   ? 18.411  -19.263 52.341 1.00 74.79  ?  12  MET   A CB  1 
ATOM   38   C  CG  . MET   A 1 5   ? 18.377  -18.517 51.010 1.00 76.95  ?  12  MET   A CG  1 
ATOM   39   S  SD  . MET   A 1 5   ? 19.810  -17.429 50.682 1.00 78.51  ?  12  MET   A SD  1 
ATOM   40   C  CE  . MET   A 1 5   ? 19.845  -17.439 48.894 1.00 69.17  ?  12  MET   A CE  1 
ATOM   41   N  N   . LYS   A 1 6   ? 18.341  -22.072 53.570 1.00 79.00  ?  13  LYS   A N   1 
ATOM   42   C  CA  . LYS   A 1 6   ? 18.766  -23.054 54.577 1.00 88.67  ?  13  LYS   A CA  1 
ATOM   43   C  C   . LYS   A 1 6   ? 20.263  -22.934 54.830 1.00 89.56  ?  13  LYS   A C   1 
ATOM   44   O  O   . LYS   A 1 6   ? 20.984  -22.456 53.965 1.00 90.46  ?  13  LYS   A O   1 
ATOM   45   C  CB  . LYS   A 1 6   ? 18.427  -24.479 54.111 1.00 95.60  ?  13  LYS   A CB  1 
ATOM   46   C  CG  . LYS   A 1 6   ? 16.947  -24.742 53.859 1.00 100.95 ?  13  LYS   A CG  1 
ATOM   47   C  CD  . LYS   A 1 6   ? 16.656  -26.232 53.646 1.00 102.96 ?  13  LYS   A CD  1 
ATOM   48   C  CE  . LYS   A 1 6   ? 15.152  -26.470 53.591 0.00 109.41 ?  13  LYS   A CE  1 
ATOM   49   N  NZ  . LYS   A 1 6   ? 14.830  -27.914 53.428 0.00 114.49 ?  13  LYS   A NZ  1 
ATOM   50   N  N   . SER   A 1 7   ? 20.729  -23.391 55.997 1.00 97.04  ?  14  SER   A N   1 
ATOM   51   C  CA  . SER   A 1 7   ? 22.184  -23.484 56.282 1.00 96.55  ?  14  SER   A CA  1 
ATOM   52   C  C   . SER   A 1 7   ? 22.903  -24.526 55.406 1.00 98.45  ?  14  SER   A C   1 
ATOM   53   O  O   . SER   A 1 7   ? 24.051  -24.303 55.003 1.00 99.38  ?  14  SER   A O   1 
ATOM   54   C  CB  . SER   A 1 7   ? 22.445  -23.775 57.765 1.00 99.59  ?  14  SER   A CB  1 
ATOM   55   O  OG  . SER   A 1 7   ? 22.074  -22.670 58.547 1.00 93.69  ?  14  SER   A OG  1 
ATOM   56   N  N   . SER   A 1 8   ? 22.227  -25.648 55.130 1.00 105.99 ?  15  SER   A N   1 
ATOM   57   C  CA  . SER   A 1 8   ? 22.703  -26.690 54.178 1.00 105.76 ?  15  SER   A CA  1 
ATOM   58   C  C   . SER   A 1 8   ? 22.889  -26.207 52.724 1.00 103.17 ?  15  SER   A C   1 
ATOM   59   O  O   . SER   A 1 8   ? 23.663  -26.807 51.969 1.00 101.19 ?  15  SER   A O   1 
ATOM   60   C  CB  . SER   A 1 8   ? 21.757  -27.892 54.169 1.00 103.07 ?  15  SER   A CB  1 
ATOM   61   O  OG  . SER   A 1 8   ? 20.498  -27.557 53.601 1.00 102.69 ?  15  SER   A OG  1 
ATOM   62   N  N   . ASP   A 1 9   ? 22.171  -25.145 52.339 1.00 95.55  ?  16  ASP   A N   1 
ATOM   63   C  CA  . ASP   A 1 9   ? 22.401  -24.473 51.049 1.00 95.33  ?  16  ASP   A CA  1 
ATOM   64   C  C   . ASP   A 1 9   ? 23.773  -23.758 50.924 1.00 89.42  ?  16  ASP   A C   1 
ATOM   65   O  O   . ASP   A 1 9   ? 24.149  -23.381 49.808 1.00 84.27  ?  16  ASP   A O   1 
ATOM   66   C  CB  . ASP   A 1 9   ? 21.295  -23.448 50.739 1.00 95.15  ?  16  ASP   A CB  1 
ATOM   67   C  CG  . ASP   A 1 9   ? 19.896  -24.058 50.617 1.00 102.67 ?  16  ASP   A CG  1 
ATOM   68   O  OD1 . ASP   A 1 9   ? 19.735  -25.300 50.508 1.00 111.63 ?  16  ASP   A OD1 1 
ATOM   69   O  OD2 . ASP   A 1 9   ? 18.935  -23.249 50.614 1.00 97.39  ?  16  ASP   A OD2 1 
ATOM   70   N  N   . PHE   A 1 10  ? 24.482  -23.539 52.043 1.00 89.93  ?  17  PHE   A N   1 
ATOM   71   C  CA  . PHE   A 1 10  ? 25.772  -22.841 52.092 1.00 96.44  ?  17  PHE   A CA  1 
ATOM   72   C  C   . PHE   A 1 10  ? 26.956  -23.637 52.631 1.00 99.71  ?  17  PHE   A C   1 
ATOM   73   O  O   . PHE   A 1 10  ? 26.774  -24.532 53.420 1.00 101.72 ?  17  PHE   A O   1 
ATOM   74   C  CB  . PHE   A 1 10  ? 25.631  -21.609 52.981 1.00 87.78  ?  17  PHE   A CB  1 
ATOM   75   C  CG  . PHE   A 1 10  ? 24.783  -20.547 52.389 1.00 83.28  ?  17  PHE   A CG  1 
ATOM   76   C  CD1 . PHE   A 1 10  ? 25.342  -19.588 51.543 1.00 83.78  ?  17  PHE   A CD1 1 
ATOM   77   C  CD2 . PHE   A 1 10  ? 23.424  -20.489 52.662 1.00 81.28  ?  17  PHE   A CD2 1 
ATOM   78   C  CE1 . PHE   A 1 10  ? 24.559  -18.583 50.991 1.00 83.61  ?  17  PHE   A CE1 1 
ATOM   79   C  CE2 . PHE   A 1 10  ? 22.625  -19.485 52.114 1.00 80.73  ?  17  PHE   A CE2 1 
ATOM   80   C  CZ  . PHE   A 1 10  ? 23.197  -18.532 51.276 1.00 78.53  ?  17  PHE   A CZ  1 
ATOM   81   N  N   . LEU   A 1 11  ? 28.156  -23.250 52.201 1.00 106.38 ?  18  LEU   A N   1 
ATOM   82   C  CA  . LEU   A 1 11  ? 29.431  -23.621 52.810 1.00 113.42 ?  18  LEU   A CA  1 
ATOM   83   C  C   . LEU   A 1 11  ? 30.034  -22.275 53.261 1.00 123.47 ?  18  LEU   A C   1 
ATOM   84   O  O   . LEU   A 1 11  ? 30.163  -21.347 52.436 1.00 123.15 ?  18  LEU   A O   1 
ATOM   85   C  CB  . LEU   A 1 11  ? 30.371  -24.302 51.793 1.00 108.26 ?  18  LEU   A CB  1 
ATOM   86   C  CG  . LEU   A 1 11  ? 29.764  -25.289 50.792 1.00 113.16 ?  18  LEU   A CG  1 
ATOM   87   C  CD1 . LEU   A 1 11  ? 30.776  -25.710 49.745 1.00 113.91 ?  18  LEU   A CD1 1 
ATOM   88   C  CD2 . LEU   A 1 11  ? 29.201  -26.482 51.546 1.00 126.92 ?  18  LEU   A CD2 1 
ATOM   89   N  N   . GLU   A 1 12  ? 30.388  -22.155 54.547 1.00 134.99 ?  19  GLU   A N   1 
ATOM   90   C  CA  . GLU   A 1 12  ? 31.093  -20.962 55.067 1.00 136.20 ?  19  GLU   A CA  1 
ATOM   91   C  C   . GLU   A 1 12  ? 32.595  -21.069 54.828 1.00 137.03 ?  19  GLU   A C   1 
ATOM   92   O  O   . GLU   A 1 12  ? 33.228  -22.017 55.284 1.00 145.00 ?  19  GLU   A O   1 
ATOM   93   C  CB  . GLU   A 1 12  ? 30.802  -20.749 56.558 1.00 141.13 ?  19  GLU   A CB  1 
ATOM   94   C  CG  . GLU   A 1 12  ? 29.357  -20.316 56.829 1.00 137.20 ?  19  GLU   A CG  1 
ATOM   95   C  CD  . GLU   A 1 12  ? 29.123  -19.685 58.204 1.00 131.99 ?  19  GLU   A CD  1 
ATOM   96   O  OE1 . GLU   A 1 12  ? 29.949  -18.862 58.662 1.00 125.25 ?  19  GLU   A OE1 1 
ATOM   97   O  OE2 . GLU   A 1 12  ? 28.075  -19.983 58.819 1.00 121.59 ?  19  GLU   A OE2 1 
ATOM   98   N  N   . LYS   A 1 23  ? 28.040  -13.613 63.227 1.00 131.20 ?  30  LYS   A N   1 
ATOM   99   C  CA  . LYS   A 1 23  ? 29.269  -13.354 62.483 1.00 123.80 ?  30  LYS   A CA  1 
ATOM   100  C  C   . LYS   A 1 23  ? 28.975  -12.986 61.025 1.00 116.03 ?  30  LYS   A C   1 
ATOM   101  O  O   . LYS   A 1 23  ? 28.226  -13.704 60.355 1.00 113.29 ?  30  LYS   A O   1 
ATOM   102  C  CB  . LYS   A 1 23  ? 30.184  -14.590 62.510 1.00 122.55 ?  30  LYS   A CB  1 
ATOM   103  C  CG  . LYS   A 1 23  ? 30.505  -15.110 63.902 1.00 127.91 ?  30  LYS   A CG  1 
ATOM   104  C  CD  . LYS   A 1 23  ? 31.764  -15.964 63.919 1.00 127.80 ?  30  LYS   A CD  1 
ATOM   105  C  CE  . LYS   A 1 23  ? 32.067  -16.459 65.342 0.00 142.11 ?  30  LYS   A CE  1 
ATOM   106  N  NZ  . LYS   A 1 23  ? 33.267  -17.339 65.394 0.00 147.05 ?  30  LYS   A NZ  1 
ATOM   107  N  N   . VAL   A 1 24  ? 29.569  -11.883 60.545 1.00 109.41 ?  31  VAL   A N   1 
ATOM   108  C  CA  . VAL   A 1 24  ? 29.591  -11.543 59.107 1.00 97.12  ?  31  VAL   A CA  1 
ATOM   109  C  C   . VAL   A 1 24  ? 30.699  -12.381 58.458 1.00 94.94  ?  31  VAL   A C   1 
ATOM   110  O  O   . VAL   A 1 24  ? 31.821  -12.404 58.965 1.00 105.60 ?  31  VAL   A O   1 
ATOM   111  C  CB  . VAL   A 1 24  ? 29.827  -10.037 58.833 1.00 89.38  ?  31  VAL   A CB  1 
ATOM   112  C  CG1 . VAL   A 1 24  ? 29.752  -9.727  57.335 1.00 79.32  ?  31  VAL   A CG1 1 
ATOM   113  C  CG2 . VAL   A 1 24  ? 28.796  -9.192  59.575 1.00 97.82  ?  31  VAL   A CG2 1 
ATOM   114  N  N   . SER   A 1 25  ? 30.372  -13.056 57.354 1.00 87.72  ?  32  SER   A N   1 
ATOM   115  C  CA  . SER   A 1 25  ? 31.307  -13.980 56.684 1.00 89.80  ?  32  SER   A CA  1 
ATOM   116  C  C   . SER   A 1 25  ? 31.006  -14.165 55.190 1.00 83.37  ?  32  SER   A C   1 
ATOM   117  O  O   . SER   A 1 25  ? 29.893  -13.886 54.738 1.00 77.51  ?  32  SER   A O   1 
ATOM   118  C  CB  . SER   A 1 25  ? 31.288  -15.348 57.402 1.00 94.19  ?  32  SER   A CB  1 
ATOM   119  O  OG  . SER   A 1 25  ? 29.982  -15.898 57.463 1.00 92.07  ?  32  SER   A OG  1 
ATOM   120  N  N   . LEU   A 1 26  ? 32.000  -14.662 54.447 1.00 82.46  ?  33  LEU   A N   1 
ATOM   121  C  CA  . LEU   A 1 26  ? 31.819  -15.089 53.051 1.00 79.16  ?  33  LEU   A CA  1 
ATOM   122  C  C   . LEU   A 1 26  ? 31.032  -16.414 52.998 1.00 81.03  ?  33  LEU   A C   1 
ATOM   123  O  O   . LEU   A 1 26  ? 31.347  -17.337 53.745 1.00 81.85  ?  33  LEU   A O   1 
ATOM   124  C  CB  . LEU   A 1 26  ? 33.175  -15.273 52.361 1.00 76.44  ?  33  LEU   A CB  1 
ATOM   125  C  CG  . LEU   A 1 26  ? 34.029  -14.006 52.230 1.00 73.60  ?  33  LEU   A CG  1 
ATOM   126  C  CD1 . LEU   A 1 26  ? 35.462  -14.359 51.874 1.00 72.50  ?  33  LEU   A CD1 1 
ATOM   127  C  CD2 . LEU   A 1 26  ? 33.442  -13.039 51.210 1.00 68.40  ?  33  LEU   A CD2 1 
ATOM   128  N  N   . ALA   A 1 27  ? 30.008  -16.461 52.143 1.00 73.55  ?  34  ALA   A N   1 
ATOM   129  C  CA  . ALA   A 1 27  ? 29.089  -17.573 52.056 1.00 73.16  ?  34  ALA   A CA  1 
ATOM   130  C  C   . ALA   A 1 27  ? 28.998  -18.036 50.609 1.00 71.11  ?  34  ALA   A C   1 
ATOM   131  O  O   . ALA   A 1 27  ? 28.652  -17.252 49.735 1.00 69.81  ?  34  ALA   A O   1 
ATOM   132  C  CB  . ALA   A 1 27  ? 27.730  -17.131 52.565 1.00 70.04  ?  34  ALA   A CB  1 
ATOM   133  N  N   . PHE   A 1 28  ? 29.297  -19.312 50.363 1.00 74.49  ?  35  PHE   A N   1 
ATOM   134  C  CA  . PHE   A 1 28  ? 29.114  -19.935 49.040 1.00 75.02  ?  35  PHE   A CA  1 
ATOM   135  C  C   . PHE   A 1 28  ? 27.769  -20.654 48.993 1.00 72.65  ?  35  PHE   A C   1 
ATOM   136  O  O   . PHE   A 1 28  ? 27.639  -21.729 49.572 1.00 76.65  ?  35  PHE   A O   1 
ATOM   137  C  CB  . PHE   A 1 28  ? 30.263  -20.919 48.716 1.00 81.31  ?  35  PHE   A CB  1 
ATOM   138  C  CG  . PHE   A 1 28  ? 31.492  -20.259 48.190 1.00 80.97  ?  35  PHE   A CG  1 
ATOM   139  C  CD1 . PHE   A 1 28  ? 31.594  -19.952 46.831 1.00 79.00  ?  35  PHE   A CD1 1 
ATOM   140  C  CD2 . PHE   A 1 28  ? 32.558  -19.937 49.042 1.00 82.15  ?  35  PHE   A CD2 1 
ATOM   141  C  CE1 . PHE   A 1 28  ? 32.729  -19.326 46.326 1.00 77.21  ?  35  PHE   A CE1 1 
ATOM   142  C  CE2 . PHE   A 1 28  ? 33.698  -19.318 48.542 1.00 83.03  ?  35  PHE   A CE2 1 
ATOM   143  C  CZ  . PHE   A 1 28  ? 33.783  -19.010 47.181 1.00 81.72  ?  35  PHE   A CZ  1 
ATOM   144  N  N   . HIS   A 1 29  ? 26.780  -20.066 48.302 1.00 70.47  ?  36  HIS   A N   1 
ATOM   145  C  CA  . HIS   A 1 29  ? 25.529  -20.780 47.989 1.00 79.12  ?  36  HIS   A CA  1 
ATOM   146  C  C   . HIS   A 1 29  ? 25.833  -21.873 46.967 1.00 84.43  ?  36  HIS   A C   1 
ATOM   147  O  O   . HIS   A 1 29  ? 26.519  -21.611 45.986 1.00 87.93  ?  36  HIS   A O   1 
ATOM   148  C  CB  . HIS   A 1 29  ? 24.429  -19.859 47.459 1.00 78.39  ?  36  HIS   A CB  1 
ATOM   149  C  CG  . HIS   A 1 29  ? 23.061  -20.480 47.497 1.00 77.26  ?  36  HIS   A CG  1 
ATOM   150  N  ND1 . HIS   A 1 29  ? 22.444  -21.010 46.382 1.00 77.17  ?  36  HIS   A ND1 1 
ATOM   151  C  CD2 . HIS   A 1 29  ? 22.210  -20.688 48.527 1.00 77.72  ?  36  HIS   A CD2 1 
ATOM   152  C  CE1 . HIS   A 1 29  ? 21.260  -21.487 46.717 1.00 75.62  ?  36  HIS   A CE1 1 
ATOM   153  N  NE2 . HIS   A 1 29  ? 21.092  -21.304 48.014 1.00 76.57  ?  36  HIS   A NE2 1 
ATOM   154  N  N   . ARG   A 1 30  ? 25.311  -23.072 47.228 1.00 92.92  ?  37  ARG   A N   1 
ATOM   155  C  CA  . ARG   A 1 30  ? 25.670  -24.303 46.504 1.00 95.18  ?  37  ARG   A CA  1 
ATOM   156  C  C   . ARG   A 1 30  ? 25.355  -24.294 45.003 1.00 94.57  ?  37  ARG   A C   1 
ATOM   157  O  O   . ARG   A 1 30  ? 26.029  -24.989 44.271 1.00 95.80  ?  37  ARG   A O   1 
ATOM   158  C  CB  . ARG   A 1 30  ? 25.021  -25.544 47.163 1.00 99.38  ?  37  ARG   A CB  1 
ATOM   159  C  CG  . ARG   A 1 30  ? 25.738  -26.065 48.402 1.00 107.35 ?  37  ARG   A CG  1 
ATOM   160  C  CD  . ARG   A 1 30  ? 25.152  -27.407 48.852 1.00 118.68 ?  37  ARG   A CD  1 
ATOM   161  N  NE  . ARG   A 1 30  ? 25.945  -28.060 49.890 1.00 120.43 ?  37  ARG   A NE  1 
ATOM   162  C  CZ  . ARG   A 1 30  ? 26.998  -28.812 49.766 0.00 128.93 ?  37  ARG   A CZ  1 
ATOM   163  N  NH1 . ARG   A 1 30  ? 27.557  -29.023 48.572 0.00 130.98 ?  37  ARG   A NH1 1 
ATOM   164  N  NH2 . ARG   A 1 30  ? 27.582  -29.352 50.834 0.00 131.91 ?  37  ARG   A NH2 1 
ATOM   165  N  N   . THR   A 1 31  ? 24.332  -23.545 44.573 1.00 92.11  ?  38  THR   A N   1 
ATOM   166  C  CA  . THR   A 1 31  ? 23.998  -23.346 43.143 1.00 94.72  ?  38  THR   A CA  1 
ATOM   167  C  C   . THR   A 1 31  ? 24.285  -21.930 42.580 1.00 86.13  ?  38  THR   A C   1 
ATOM   168  O  O   . THR   A 1 31  ? 24.507  -21.817 41.376 1.00 80.94  ?  38  THR   A O   1 
ATOM   169  C  CB  . THR   A 1 31  ? 22.521  -23.731 42.843 1.00 92.05  ?  38  THR   A CB  1 
ATOM   170  O  OG1 . THR   A 1 31  ? 21.625  -22.837 43.513 1.00 99.65  ?  38  THR   A OG1 1 
ATOM   171  C  CG2 . THR   A 1 31  ? 22.227  -25.138 43.295 1.00 100.42 ?  38  THR   A CG2 1 
ATOM   172  N  N   . GLN   A 1 32  ? 24.349  -20.895 43.434 1.00 89.20  ?  39  GLN   A N   1 
ATOM   173  C  CA  . GLN   A 1 32  ? 24.340  -19.458 43.029 1.00 88.87  ?  39  GLN   A CA  1 
ATOM   174  C  C   . GLN   A 1 32  ? 25.630  -18.657 43.324 1.00 86.02  ?  39  GLN   A C   1 
ATOM   175  O  O   . GLN   A 1 32  ? 25.677  -17.448 43.060 1.00 79.88  ?  39  GLN   A O   1 
ATOM   176  C  CB  . GLN   A 1 32  ? 23.159  -18.725 43.695 1.00 88.82  ?  39  GLN   A CB  1 
ATOM   177  C  CG  . GLN   A 1 32  ? 21.793  -19.155 43.186 1.00 97.51  ?  39  GLN   A CG  1 
ATOM   178  C  CD  . GLN   A 1 32  ? 20.638  -18.309 43.732 1.00 103.33 ?  39  GLN   A CD  1 
ATOM   179  O  OE1 . GLN   A 1 32  ? 20.806  -17.493 44.647 1.00 92.79  ?  39  GLN   A OE1 1 
ATOM   180  N  NE2 . GLN   A 1 32  ? 19.445  -18.512 43.169 1.00 111.52 ?  39  GLN   A NE2 1 
ATOM   181  N  N   . GLY   A 1 33  ? 26.658  -19.304 43.871 1.00 85.99  ?  40  GLY   A N   1 
ATOM   182  C  CA  . GLY   A 1 33  ? 27.945  -18.658 44.114 1.00 82.48  ?  40  GLY   A CA  1 
ATOM   183  C  C   . GLY   A 1 33  ? 28.035  -17.793 45.353 1.00 76.17  ?  40  GLY   A C   1 
ATOM   184  O  O   . GLY   A 1 33  ? 27.304  -18.003 46.316 1.00 78.09  ?  40  GLY   A O   1 
ATOM   185  N  N   . LEU   A 1 34  ? 28.927  -16.805 45.299 1.00 80.64  ?  41  LEU   A N   1 
ATOM   186  C  CA  . LEU   A 1 34  ? 29.412  -16.091 46.478 1.00 79.73  ?  41  LEU   A CA  1 
ATOM   187  C  C   . LEU   A 1 34  ? 28.412  -15.035 46.963 1.00 75.36  ?  41  LEU   A C   1 
ATOM   188  O  O   . LEU   A 1 34  ? 27.832  -14.315 46.157 1.00 76.01  ?  41  LEU   A O   1 
ATOM   189  C  CB  . LEU   A 1 34  ? 30.774  -15.446 46.151 1.00 89.80  ?  41  LEU   A CB  1 
ATOM   190  C  CG  . LEU   A 1 34  ? 31.620  -14.839 47.271 1.00 90.25  ?  41  LEU   A CG  1 
ATOM   191  C  CD1 . LEU   A 1 34  ? 31.967  -15.846 48.361 1.00 91.50  ?  41  LEU   A CD1 1 
ATOM   192  C  CD2 . LEU   A 1 34  ? 32.896  -14.281 46.659 1.00 98.74  ?  41  LEU   A CD2 1 
ATOM   193  N  N   . MET   A 1 35  ? 28.197  -14.997 48.278 1.00 70.73  ?  42  MET   A N   1 
ATOM   194  C  CA  . MET   A 1 35  ? 27.376  -13.999 48.976 1.00 66.06  ?  42  MET   A CA  1 
ATOM   195  C  C   . MET   A 1 35  ? 28.018  -13.668 50.318 1.00 67.19  ?  42  MET   A C   1 
ATOM   196  O  O   . MET   A 1 35  ? 28.968  -14.337 50.747 1.00 77.27  ?  42  MET   A O   1 
ATOM   197  C  CB  . MET   A 1 35  ? 25.981  -14.555 49.266 1.00 72.10  ?  42  MET   A CB  1 
ATOM   198  C  CG  . MET   A 1 35  ? 25.140  -14.857 48.044 1.00 75.81  ?  42  MET   A CG  1 
ATOM   199  S  SD  . MET   A 1 35  ? 23.814  -16.012 48.426 1.00 76.12  ?  42  MET   A SD  1 
ATOM   200  C  CE  . MET   A 1 35  ? 23.058  -16.105 46.811 1.00 75.14  ?  42  MET   A CE  1 
ATOM   201  N  N   . ILE   A 1 36  ? 27.477  -12.645 50.981 1.00 59.78  ?  43  ILE   A N   1 
ATOM   202  C  CA  . ILE   A 1 36  ? 27.808  -12.330 52.377 1.00 64.74  ?  43  ILE   A CA  1 
ATOM   203  C  C   . ILE   A 1 36  ? 26.610  -12.772 53.217 1.00 70.62  ?  43  ILE   A C   1 
ATOM   204  O  O   . ILE   A 1 36  ? 25.447  -12.644 52.774 1.00 68.35  ?  43  ILE   A O   1 
ATOM   205  C  CB  . ILE   A 1 36  ? 28.121  -10.830 52.632 1.00 63.69  ?  43  ILE   A CB  1 
ATOM   206  C  CG1 . ILE   A 1 36  ? 29.226  -10.316 51.701 1.00 67.19  ?  43  ILE   A CG1 1 
ATOM   207  C  CG2 . ILE   A 1 36  ? 28.604  -10.624 54.064 1.00 60.16  ?  43  ILE   A CG2 1 
ATOM   208  C  CD1 . ILE   A 1 36  ? 29.011  -8.851  51.493 0.00 63.18  ?  43  ILE   A CD1 1 
ATOM   209  N  N   . MET   A 1 37  ? 26.912  -13.297 54.408 1.00 74.58  ?  44  MET   A N   1 
ATOM   210  C  CA  . MET   A 1 37  ? 25.919  -13.708 55.373 1.00 83.18  ?  44  MET   A CA  1 
ATOM   211  C  C   . MET   A 1 37  ? 26.205  -12.994 56.692 1.00 81.86  ?  44  MET   A C   1 
ATOM   212  O  O   . MET   A 1 37  ? 27.198  -13.292 57.350 1.00 93.57  ?  44  MET   A O   1 
ATOM   213  C  CB  . MET   A 1 37  ? 25.981  -15.222 55.529 1.00 86.21  ?  44  MET   A CB  1 
ATOM   214  C  CG  . MET   A 1 37  ? 24.853  -15.814 56.350 1.00 91.21  ?  44  MET   A CG  1 
ATOM   215  S  SD  . MET   A 1 37  ? 24.725  -17.605 56.120 1.00 93.49  ?  44  MET   A SD  1 
ATOM   216  C  CE  . MET   A 1 37  ? 26.199  -18.174 56.959 1.00 106.40 ?  44  MET   A CE  1 
ATOM   217  N  N   . LYS   A 1 38  ? 25.360  -12.017 57.034 1.00 83.76  ?  45  LYS   A N   1 
ATOM   218  C  CA  . LYS   A 1 38  ? 25.313  -11.441 58.374 1.00 89.32  ?  45  LYS   A CA  1 
ATOM   219  C  C   . LYS   A 1 38  ? 24.400  -12.341 59.214 1.00 88.54  ?  45  LYS   A C   1 
ATOM   220  O  O   . LYS   A 1 38  ? 23.186  -12.370 59.002 1.00 74.48  ?  45  LYS   A O   1 
ATOM   221  C  CB  . LYS   A 1 38  ? 24.805  -9.987  58.369 1.00 88.04  ?  45  LYS   A CB  1 
ATOM   222  C  CG  . LYS   A 1 38  ? 24.790  -9.341  59.760 1.00 98.56  ?  45  LYS   A CG  1 
ATOM   223  C  CD  . LYS   A 1 38  ? 24.900  -7.814  59.742 1.00 102.02 ?  45  LYS   A CD  1 
ATOM   224  C  CE  . LYS   A 1 38  ? 25.034  -7.223  61.147 1.00 101.46 ?  45  LYS   A CE  1 
ATOM   225  N  NZ  . LYS   A 1 38  ? 25.576  -5.965  61.367 0.00 101.39 ?  45  LYS   A NZ  1 
ATOM   226  N  N   . THR   A 1 39  ? 25.024  -13.100 60.114 1.00 96.03  ?  46  THR   A N   1 
ATOM   227  C  CA  . THR   A 1 39  ? 24.348  -13.960 61.089 1.00 94.46  ?  46  THR   A CA  1 
ATOM   228  C  C   . THR   A 1 39  ? 24.123  -13.105 62.334 1.00 94.06  ?  46  THR   A C   1 
ATOM   229  O  O   . THR   A 1 39  ? 25.085  -12.814 63.070 1.00 92.25  ?  46  THR   A O   1 
ATOM   230  C  CB  . THR   A 1 39  ? 25.214  -15.198 61.424 1.00 88.33  ?  46  THR   A CB  1 
ATOM   231  O  OG1 . THR   A 1 39  ? 25.500  -15.914 60.219 1.00 86.23  ?  46  THR   A OG1 1 
ATOM   232  C  CG2 . THR   A 1 39  ? 24.518  -16.128 62.407 1.00 94.00  ?  46  THR   A CG2 1 
ATOM   233  N  N   . VAL   A 1 40  ? 22.863  -12.716 62.570 1.00 91.81  ?  47  VAL   A N   1 
ATOM   234  C  CA  . VAL   A 1 40  ? 22.531  -11.767 63.646 1.00 97.85  ?  47  VAL   A CA  1 
ATOM   235  C  C   . VAL   A 1 40  ? 22.459  -12.427 65.026 1.00 98.27  ?  47  VAL   A C   1 
ATOM   236  O  O   . VAL   A 1 40  ? 22.897  -11.833 66.022 1.00 104.13 ?  47  VAL   A O   1 
ATOM   237  C  CB  . VAL   A 1 40  ? 21.265  -10.924 63.334 1.00 97.76  ?  47  VAL   A CB  1 
ATOM   238  C  CG1 . VAL   A 1 40  ? 21.429  -10.194 62.004 1.00 94.38  ?  47  VAL   A CG1 1 
ATOM   239  C  CG2 . VAL   A 1 40  ? 19.986  -11.739 63.324 1.00 100.04 ?  47  VAL   A CG2 1 
ATOM   240  N  N   . TYR   A 1 41  ? 21.914  -13.647 65.064 1.00 99.30  ?  48  TYR   A N   1 
ATOM   241  C  CA  . TYR   A 1 41  ? 21.774  -14.434 66.294 1.00 104.55 ?  48  TYR   A CA  1 
ATOM   242  C  C   . TYR   A 1 41  ? 22.261  -15.876 66.074 1.00 102.67 ?  48  TYR   A C   1 
ATOM   243  O  O   . TYR   A 1 41  ? 21.965  -16.473 65.035 1.00 91.73  ?  48  TYR   A O   1 
ATOM   244  C  CB  . TYR   A 1 41  ? 20.302  -14.419 66.733 1.00 107.78 ?  48  TYR   A CB  1 
ATOM   245  C  CG  . TYR   A 1 41  ? 19.982  -15.179 68.009 1.00 116.93 ?  48  TYR   A CG  1 
ATOM   246  C  CD1 . TYR   A 1 41  ? 19.736  -16.565 67.990 1.00 117.32 ?  48  TYR   A CD1 1 
ATOM   247  C  CD2 . TYR   A 1 41  ? 19.876  -14.511 69.243 1.00 121.55 ?  48  TYR   A CD2 1 
ATOM   248  C  CE1 . TYR   A 1 41  ? 19.442  -17.262 69.153 1.00 124.41 ?  48  TYR   A CE1 1 
ATOM   249  C  CE2 . TYR   A 1 41  ? 19.567  -15.203 70.417 1.00 121.60 ?  48  TYR   A CE2 1 
ATOM   250  C  CZ  . TYR   A 1 41  ? 19.350  -16.578 70.370 1.00 126.96 ?  48  TYR   A CZ  1 
ATOM   251  O  OH  . TYR   A 1 41  ? 19.052  -17.266 71.521 1.00 128.13 ?  48  TYR   A OH  1 
ATOM   252  N  N   . LYS   A 1 42  ? 23.034  -16.390 67.038 1.00 108.01 ?  49  LYS   A N   1 
ATOM   253  C  CA  . LYS   A 1 42  ? 23.288  -17.833 67.205 1.00 114.85 ?  49  LYS   A CA  1 
ATOM   254  C  C   . LYS   A 1 42  ? 23.145  -18.168 68.698 1.00 120.75 ?  49  LYS   A C   1 
ATOM   255  O  O   . LYS   A 1 42  ? 23.776  -17.510 69.540 1.00 123.16 ?  49  LYS   A O   1 
ATOM   256  C  CB  . LYS   A 1 42  ? 24.689  -18.217 66.700 1.00 118.96 ?  49  LYS   A CB  1 
ATOM   257  C  CG  . LYS   A 1 42  ? 24.740  -18.799 65.291 1.00 117.41 ?  49  LYS   A CG  1 
ATOM   258  C  CD  . LYS   A 1 42  ? 26.174  -19.107 64.868 1.00 119.34 ?  49  LYS   A CD  1 
ATOM   259  C  CE  . LYS   A 1 42  ? 26.258  -19.672 63.457 1.00 113.96 ?  49  LYS   A CE  1 
ATOM   260  N  NZ  . LYS   A 1 42  ? 27.603  -19.603 62.874 0.00 112.42 ?  49  LYS   A NZ  1 
ATOM   261  N  N   . GLY   A 1 43  ? 22.326  -19.175 69.018 1.00 123.46 ?  50  GLY   A N   1 
ATOM   262  C  CA  . GLY   A 1 43  ? 22.051  -19.542 70.414 1.00 134.09 ?  50  GLY   A CA  1 
ATOM   263  C  C   . GLY   A 1 43  ? 20.858  -20.476 70.604 1.00 138.37 ?  50  GLY   A C   1 
ATOM   264  O  O   . GLY   A 1 43  ? 20.553  -21.260 69.711 1.00 134.41 ?  50  GLY   A O   1 
ATOM   265  N  N   . PRO   A 1 44  ? 20.209  -20.432 71.788 1.00 145.14 ?  51  PRO   A N   1 
ATOM   266  C  CA  . PRO   A 1 44  ? 18.923  -21.099 72.028 1.00 143.37 ?  51  PRO   A CA  1 
ATOM   267  C  C   . PRO   A 1 44  ? 17.738  -20.591 71.179 1.00 132.61 ?  51  PRO   A C   1 
ATOM   268  O  O   . PRO   A 1 44  ? 17.768  -19.476 70.668 1.00 117.87 ?  51  PRO   A O   1 
ATOM   269  C  CB  . PRO   A 1 44  ? 18.672  -20.809 73.516 1.00 153.53 ?  51  PRO   A CB  1 
ATOM   270  C  CG  . PRO   A 1 44  ? 20.030  -20.783 74.109 1.00 159.28 ?  51  PRO   A CG  1 
ATOM   271  C  CD  . PRO   A 1 44  ? 20.908  -20.156 73.063 1.00 154.17 ?  51  PRO   A CD  1 
ATOM   272  N  N   . ASN   A 1 45  ? 16.678  -21.402 71.106 1.00 130.76 ?  52  ASN   A N   1 
ATOM   273  C  CA  . ASN   A 1 45  ? 15.497  -21.127 70.280 1.00 125.78 ?  52  ASN   A CA  1 
ATOM   274  C  C   . ASN   A 1 45  ? 14.584  -20.041 70.878 1.00 122.86 ?  52  ASN   A C   1 
ATOM   275  O  O   . ASN   A 1 45  ? 14.018  -20.234 71.957 1.00 120.13 ?  52  ASN   A O   1 
ATOM   276  C  CB  . ASN   A 1 45  ? 14.695  -22.418 70.066 1.00 126.19 ?  52  ASN   A CB  1 
ATOM   277  C  CG  . ASN   A 1 45  ? 13.571  -22.307 69.078 0.00 126.14 ?  52  ASN   A CG  1 
ATOM   278  O  OD1 . ASN   A 1 45  ? 13.591  -21.453 68.187 0.00 122.14 ?  52  ASN   A OD1 1 
ATOM   279  N  ND2 . ASN   A 1 45  ? 12.576  -23.182 69.202 0.00 128.61 ?  52  ASN   A ND2 1 
ATOM   280  N  N   . CYS   A 1 46  ? 14.484  -18.902 70.179 1.00 122.67 ?  53  CYS   A N   1 
ATOM   281  C  CA  . CYS   A 1 46  ? 13.498  -17.836 70.461 1.00 126.84 ?  53  CYS   A CA  1 
ATOM   282  C  C   . CYS   A 1 46  ? 12.353  -17.909 69.427 1.00 129.68 ?  53  CYS   A C   1 
ATOM   283  O  O   . CYS   A 1 46  ? 12.545  -17.540 68.266 1.00 135.96 ?  53  CYS   A O   1 
ATOM   284  C  CB  . CYS   A 1 46  ? 14.188  -16.459 70.440 1.00 123.25 ?  53  CYS   A CB  1 
ATOM   285  S  SG  . CYS   A 1 46  ? 15.313  -16.194 69.045 1.00 105.61 ?  53  CYS   A SG  1 
ATOM   286  N  N   . ILE   A 1 47  ? 11.178  -18.379 69.857 1.00 142.00 ?  54  ILE   A N   1 
ATOM   287  C  CA  . ILE   A 1 47  ? 10.097  -18.803 68.945 1.00 146.17 ?  54  ILE   A CA  1 
ATOM   288  C  C   . ILE   A 1 47  ? 9.006   -17.788 68.630 1.00 140.79 ?  54  ILE   A C   1 
ATOM   289  O  O   . ILE   A 1 47  ? 8.279   -17.999 67.662 1.00 131.95 ?  54  ILE   A O   1 
ATOM   290  C  CB  . ILE   A 1 47  ? 9.350   -20.027 69.502 1.00 159.55 ?  54  ILE   A CB  1 
ATOM   291  C  CG1 . ILE   A 1 47  ? 10.324  -21.017 70.263 0.00 166.78 ?  54  ILE   A CG1 1 
ATOM   292  C  CG2 . ILE   A 1 47  ? 8.596   -20.862 68.523 0.00 163.70 ?  54  ILE   A CG2 1 
ATOM   293  C  CD1 . ILE   A 1 47  ? 9.739   -22.391 70.508 0.00 170.33 ?  54  ILE   A CD1 1 
ATOM   294  N  N   . GLU   A 1 48  ? 8.863   -16.736 69.441 1.00 137.36 ?  55  GLU   A N   1 
ATOM   295  C  CA  . GLU   A 1 48  ? 7.660   -15.877 69.417 1.00 140.97 ?  55  GLU   A CA  1 
ATOM   296  C  C   . GLU   A 1 48  ? 7.586   -14.934 68.211 1.00 130.44 ?  55  GLU   A C   1 
ATOM   297  O  O   . GLU   A 1 48  ? 6.563   -14.893 67.522 1.00 132.19 ?  55  GLU   A O   1 
ATOM   298  C  CB  . GLU   A 1 48  ? 7.545   -15.063 70.717 1.00 152.07 ?  55  GLU   A CB  1 
ATOM   299  C  CG  . GLU   A 1 48  ? 7.349   -15.907 71.969 1.00 157.04 ?  55  GLU   A CG  1 
ATOM   300  C  CD  . GLU   A 1 48  ? 7.348   -15.064 73.251 0.00 165.11 ?  55  GLU   A CD  1 
ATOM   301  O  OE1 . GLU   A 1 48  ? 6.623   -14.046 73.299 0.00 166.02 ?  55  GLU   A OE1 1 
ATOM   302  O  OE2 . GLU   A 1 48  ? 8.054   -15.432 74.214 0.00 167.67 ?  55  GLU   A OE2 1 
ATOM   303  N  N   . HIS   A 1 49  ? 8.679   -14.210 67.957 1.00 118.47 ?  56  HIS   A N   1 
ATOM   304  C  CA  . HIS   A 1 49  ? 8.728   -13.130 66.949 1.00 113.24 ?  56  HIS   A CA  1 
ATOM   305  C  C   . HIS   A 1 49  ? 9.316   -13.503 65.564 1.00 107.30 ?  56  HIS   A C   1 
ATOM   306  O  O   . HIS   A 1 49  ? 9.613   -12.615 64.758 1.00 104.81 ?  56  HIS   A O   1 
ATOM   307  C  CB  . HIS   A 1 49  ? 9.452   -11.911 67.545 1.00 117.07 ?  56  HIS   A CB  1 
ATOM   308  C  CG  . HIS   A 1 49  ? 8.723   -11.284 68.699 1.00 123.93 ?  56  HIS   A CG  1 
ATOM   309  N  ND1 . HIS   A 1 49  ? 8.929   -11.667 70.007 1.00 125.50 ?  56  HIS   A ND1 1 
ATOM   310  C  CD2 . HIS   A 1 49  ? 7.784   -10.307 68.737 1.00 123.54 ?  56  HIS   A CD2 1 
ATOM   311  C  CE1 . HIS   A 1 49  ? 8.152   -10.953 70.802 1.00 129.39 ?  56  HIS   A CE1 1 
ATOM   312  N  NE2 . HIS   A 1 49  ? 7.448   -10.120 70.057 1.00 129.15 ?  56  HIS   A NE2 1 
ATOM   313  N  N   . ASN   A 1 50  ? 9.394   -14.802 65.242 1.00 103.90 ?  57  ASN   A N   1 
ATOM   314  C  CA  . ASN   A 1 50  ? 9.722   -15.276 63.864 1.00 95.06  ?  57  ASN   A CA  1 
ATOM   315  C  C   . ASN   A 1 50  ? 8.775   -14.759 62.761 1.00 90.76  ?  57  ASN   A C   1 
ATOM   316  O  O   . ASN   A 1 50  ? 9.195   -14.568 61.623 1.00 82.23  ?  57  ASN   A O   1 
ATOM   317  C  CB  . ASN   A 1 50  ? 9.769   -16.822 63.806 1.00 95.24  ?  57  ASN   A CB  1 
ATOM   318  C  CG  . ASN   A 1 50  ? 10.931  -17.427 64.601 1.00 95.34  ?  57  ASN   A CG  1 
ATOM   319  O  OD1 . ASN   A 1 50  ? 11.661  -16.733 65.317 1.00 100.24 ?  57  ASN   A OD1 1 
ATOM   320  N  ND2 . ASN   A 1 50  ? 11.084  -18.734 64.495 1.00 97.25  ?  57  ASN   A ND2 1 
ATOM   321  N  N   . GLU   A 1 51  ? 7.504   -14.564 63.104 1.00 100.31 ?  58  GLU   A N   1 
ATOM   322  C  CA  . GLU   A 1 51  ? 6.511   -13.931 62.211 1.00 103.21 ?  58  GLU   A CA  1 
ATOM   323  C  C   . GLU   A 1 51  ? 6.825   -12.457 61.902 1.00 95.53  ?  58  GLU   A C   1 
ATOM   324  O  O   . GLU   A 1 51  ? 6.664   -12.005 60.755 1.00 94.37  ?  58  GLU   A O   1 
ATOM   325  C  CB  . GLU   A 1 51  ? 5.102   -14.061 62.805 1.00 108.21 ?  58  GLU   A CB  1 
ATOM   326  C  CG  . GLU   A 1 51  ? 4.582   -15.494 62.775 1.00 111.50 ?  58  GLU   A CG  1 
ATOM   327  C  CD  . GLU   A 1 51  ? 3.540   -15.780 63.836 1.00 120.68 ?  58  GLU   A CD  1 
ATOM   328  O  OE1 . GLU   A 1 51  ? 3.857   -15.630 65.034 1.00 126.21 ?  58  GLU   A OE1 1 
ATOM   329  O  OE2 . GLU   A 1 51  ? 2.410   -16.176 63.475 1.00 126.31 ?  58  GLU   A OE2 1 
ATOM   330  N  N   . ALA   A 1 52  ? 7.241   -11.713 62.929 1.00 89.77  ?  59  ALA   A N   1 
ATOM   331  C  CA  . ALA   A 1 52  ? 7.637   -10.302 62.779 1.00 86.99  ?  59  ALA   A CA  1 
ATOM   332  C  C   . ALA   A 1 52  ? 8.986   -10.128 62.072 1.00 85.98  ?  59  ALA   A C   1 
ATOM   333  O  O   . ALA   A 1 52  ? 9.170   -9.163  61.315 1.00 79.06  ?  59  ALA   A O   1 
ATOM   334  C  CB  . ALA   A 1 52  ? 7.663   -9.605  64.130 1.00 91.82  ?  59  ALA   A CB  1 
ATOM   335  N  N   . LEU   A 1 53  ? 9.931   -11.034 62.347 1.00 84.33  ?  60  LEU   A N   1 
ATOM   336  C  CA  . LEU   A 1 53  ? 11.213  -11.078 61.639 1.00 81.03  ?  60  LEU   A CA  1 
ATOM   337  C  C   . LEU   A 1 53  ? 11.061  -11.365 60.141 1.00 80.67  ?  60  LEU   A C   1 
ATOM   338  O  O   . LEU   A 1 53  ? 11.709  -10.712 59.324 1.00 77.55  ?  60  LEU   A O   1 
ATOM   339  C  CB  . LEU   A 1 53  ? 12.151  -12.107 62.272 1.00 80.43  ?  60  LEU   A CB  1 
ATOM   340  C  CG  . LEU   A 1 53  ? 12.700  -11.779 63.668 1.00 83.91  ?  60  LEU   A CG  1 
ATOM   341  C  CD1 . LEU   A 1 53  ? 13.289  -13.036 64.297 1.00 89.68  ?  60  LEU   A CD1 1 
ATOM   342  C  CD2 . LEU   A 1 53  ? 13.743  -10.667 63.636 1.00 78.66  ?  60  LEU   A CD2 1 
ATOM   343  N  N   . LEU   A 1 54  ? 10.212  -12.332 59.790 1.00 85.98  ?  61  LEU   A N   1 
ATOM   344  C  CA  . LEU   A 1 54  ? 9.906   -12.654 58.379 1.00 83.95  ?  61  LEU   A CA  1 
ATOM   345  C  C   . LEU   A 1 54  ? 9.150   -11.512 57.661 1.00 80.36  ?  61  LEU   A C   1 
ATOM   346  O  O   . LEU   A 1 54  ? 9.429   -11.235 56.502 1.00 71.42  ?  61  LEU   A O   1 
ATOM   347  C  CB  . LEU   A 1 54  ? 9.124   -13.973 58.273 1.00 85.60  ?  61  LEU   A CB  1 
ATOM   348  C  CG  . LEU   A 1 54  ? 8.888   -14.540 56.863 1.00 85.83  ?  61  LEU   A CG  1 
ATOM   349  C  CD1 . LEU   A 1 54  ? 9.998   -14.855 56.075 0.00 83.74  ?  61  LEU   A CD1 1 
ATOM   350  C  CD2 . LEU   A 1 54  ? 7.865   -15.751 57.013 0.00 89.38  ?  61  LEU   A CD2 1 
ATOM   351  N  N   . GLU   A 1 55  ? 8.206   -10.867 58.352 1.00 86.52  ?  62  GLU   A N   1 
ATOM   352  C  CA  . GLU   A 1 55  ? 7.475   -9.704  57.808 1.00 88.48  ?  62  GLU   A CA  1 
ATOM   353  C  C   . GLU   A 1 55  ? 8.402   -8.495  57.610 1.00 82.11  ?  62  GLU   A C   1 
ATOM   354  O  O   . GLU   A 1 55  ? 8.268   -7.772  56.626 1.00 89.87  ?  62  GLU   A O   1 
ATOM   355  C  CB  . GLU   A 1 55  ? 6.269   -9.340  58.695 1.00 96.10  ?  62  GLU   A CB  1 
ATOM   356  C  CG  . GLU   A 1 55  ? 5.260   -8.387  58.064 1.00 105.90 ?  62  GLU   A CG  1 
ATOM   357  C  CD  . GLU   A 1 55  ? 4.333   -9.090  57.099 1.00 116.01 ?  62  GLU   A CD  1 
ATOM   358  O  OE1 . GLU   A 1 55  ? 3.533   -9.907  57.585 1.00 121.97 ?  62  GLU   A OE1 1 
ATOM   359  O  OE2 . GLU   A 1 55  ? 4.401   -8.830  55.876 1.00 118.99 ?  62  GLU   A OE2 1 
ATOM   360  N  N   . GLU   A 1 56  ? 9.333   -8.300  58.537 1.00 81.98  ?  63  GLU   A N   1 
ATOM   361  C  CA  . GLU   A 1 56  ? 10.390  -7.281  58.404 1.00 74.11  ?  63  GLU   A CA  1 
ATOM   362  C  C   . GLU   A 1 56  ? 11.412  -7.645  57.308 1.00 74.29  ?  63  GLU   A C   1 
ATOM   363  O  O   . GLU   A 1 56  ? 11.931  -6.758  56.622 1.00 75.12  ?  63  GLU   A O   1 
ATOM   364  C  CB  . GLU   A 1 56  ? 11.068  -7.094  59.761 1.00 74.57  ?  63  GLU   A CB  1 
ATOM   365  C  CG  . GLU   A 1 56  ? 11.854  -5.822  59.935 1.00 75.92  ?  63  GLU   A CG  1 
ATOM   366  C  CD  . GLU   A 1 56  ? 12.095  -5.504  61.399 1.00 84.74  ?  63  GLU   A CD  1 
ATOM   367  O  OE1 . GLU   A 1 56  ? 13.220  -5.746  61.886 1.00 90.74  ?  63  GLU   A OE1 1 
ATOM   368  O  OE2 . GLU   A 1 56  ? 11.153  -5.030  62.079 1.00 82.71  ?  63  GLU   A OE2 1 
ATOM   369  N  N   . ALA   A 1 57  ? 11.705  -8.942  57.155 1.00 74.56  ?  64  ALA   A N   1 
ATOM   370  C  CA  . ALA   A 1 57  ? 12.500  -9.450  56.020 1.00 67.04  ?  64  ALA   A CA  1 
ATOM   371  C  C   . ALA   A 1 57  ? 11.818  -9.203  54.669 1.00 66.68  ?  64  ALA   A C   1 
ATOM   372  O  O   . ALA   A 1 57  ? 12.502  -8.847  53.715 1.00 72.89  ?  64  ALA   A O   1 
ATOM   373  C  CB  . ALA   A 1 57  ? 12.854  -10.929 56.180 1.00 63.45  ?  64  ALA   A CB  1 
ATOM   374  N  N   . LYS   A 1 58  ? 10.488  -9.368  54.606 1.00 67.78  ?  65  LYS   A N   1 
ATOM   375  C  CA  . LYS   A 1 58  ? 9.697   -9.048  53.398 1.00 69.05  ?  65  LYS   A CA  1 
ATOM   376  C  C   . LYS   A 1 58  ? 9.800   -7.567  53.015 1.00 72.60  ?  65  LYS   A C   1 
ATOM   377  O  O   . LYS   A 1 58  ? 9.987   -7.245  51.831 1.00 71.44  ?  65  LYS   A O   1 
ATOM   378  C  CB  . LYS   A 1 58  ? 8.219   -9.454  53.544 1.00 79.39  ?  65  LYS   A CB  1 
ATOM   379  C  CG  . LYS   A 1 58  ? 7.954   -10.951 53.399 1.00 87.34  ?  65  LYS   A CG  1 
ATOM   380  C  CD  . LYS   A 1 58  ? 6.508   -11.323 53.709 1.00 94.90  ?  65  LYS   A CD  1 
ATOM   381  C  CE  . LYS   A 1 58  ? 6.203   -12.741 53.764 0.00 93.45  ?  65  LYS   A CE  1 
ATOM   382  N  NZ  . LYS   A 1 58  ? 4.794   -13.020 54.160 0.00 97.63  ?  65  LYS   A NZ  1 
ATOM   383  N  N   . MET   A 1 59  ? 9.718   -6.694  54.024 1.00 74.65  ?  66  MET   A N   1 
ATOM   384  C  CA  . MET   A 1 59  ? 9.865   -5.245  53.840 1.00 85.41  ?  66  MET   A CA  1 
ATOM   385  C  C   . MET   A 1 59  ? 11.225  -4.835  53.263 1.00 82.05  ?  66  MET   A C   1 
ATOM   386  O  O   . MET   A 1 59  ? 11.277  -4.025  52.340 1.00 74.38  ?  66  MET   A O   1 
ATOM   387  C  CB  . MET   A 1 59  ? 9.628   -4.491  55.164 1.00 94.14  ?  66  MET   A CB  1 
ATOM   388  C  CG  . MET   A 1 59  ? 8.185   -4.478  55.642 1.00 101.63 ?  66  MET   A CG  1 
ATOM   389  S  SD  . MET   A 1 59  ? 7.122   -3.506  54.571 1.00 121.76 ?  66  MET   A SD  1 
ATOM   390  C  CE  . MET   A 1 59  ? 7.622   -1.839  55.011 1.00 122.17 ?  66  MET   A CE  1 
ATOM   391  N  N   . MET   A 1 60  ? 12.303  -5.415  53.790 1.00 79.72  ?  67  MET   A N   1 
ATOM   392  C  CA  . MET   A 1 60  ? 13.653  -5.161  53.238 1.00 76.69  ?  67  MET   A CA  1 
ATOM   393  C  C   . MET   A 1 60  ? 13.886  -5.791  51.837 1.00 76.54  ?  67  MET   A C   1 
ATOM   394  O  O   . MET   A 1 60  ? 14.723  -5.312  51.066 1.00 73.07  ?  67  MET   A O   1 
ATOM   395  C  CB  . MET   A 1 60  ? 14.752  -5.503  54.267 1.00 76.07  ?  67  MET   A CB  1 
ATOM   396  C  CG  . MET   A 1 60  ? 14.964  -6.939  54.610 1.00 76.72  ?  67  MET   A CG  1 
ATOM   397  S  SD  . MET   A 1 60  ? 16.493  -7.195  55.574 1.00 73.15  ?  67  MET   A SD  1 
ATOM   398  C  CE  . MET   A 1 60  ? 16.043  -6.599  57.181 1.00 69.52  ?  67  MET   A CE  1 
ATOM   399  N  N   . ASN   A 1 61  ? 13.121  -6.831  51.501 1.00 76.94  ?  68  ASN   A N   1 
ATOM   400  C  CA  . ASN   A 1 61  ? 13.151  -7.434  50.160 1.00 69.66  ?  68  ASN   A CA  1 
ATOM   401  C  C   . ASN   A 1 61  ? 12.503  -6.613  49.040 1.00 66.35  ?  68  ASN   A C   1 
ATOM   402  O  O   . ASN   A 1 61  ? 12.872  -6.785  47.858 1.00 66.39  ?  68  ASN   A O   1 
ATOM   403  C  CB  . ASN   A 1 61  ? 12.511  -8.825  50.189 1.00 74.06  ?  68  ASN   A CB  1 
ATOM   404  C  CG  . ASN   A 1 61  ? 12.999  -9.701  49.069 1.00 70.10  ?  68  ASN   A CG  1 
ATOM   405  O  OD1 . ASN   A 1 61  ? 12.282  -9.950  48.110 1.00 73.72  ?  68  ASN   A OD1 1 
ATOM   406  N  ND2 . ASN   A 1 61  ? 14.237  -10.160 49.178 1.00 74.22  ?  68  ASN   A ND2 1 
ATOM   407  N  N   . ARG   A 1 62  ? 11.565  -5.724  49.395 1.00 65.68  ?  69  ARG   A N   1 
ATOM   408  C  CA  . ARG   A 1 62  ? 10.933  -4.833  48.402 1.00 69.44  ?  69  ARG   A CA  1 
ATOM   409  C  C   . ARG   A 1 62  ? 11.880  -3.777  47.759 1.00 70.23  ?  69  ARG   A C   1 
ATOM   410  O  O   . ARG   A 1 62  ? 11.553  -3.216  46.708 1.00 79.56  ?  69  ARG   A O   1 
ATOM   411  C  CB  . ARG   A 1 62  ? 9.685   -4.170  49.001 1.00 75.63  ?  69  ARG   A CB  1 
ATOM   412  C  CG  . ARG   A 1 62  ? 9.935   -2.878  49.757 1.00 83.91  ?  69  ARG   A CG  1 
ATOM   413  C  CD  . ARG   A 1 62  ? 8.846   -2.577  50.779 1.00 89.29  ?  69  ARG   A CD  1 
ATOM   414  N  NE  . ARG   A 1 62  ? 9.004   -1.239  51.360 1.00 90.76  ?  69  ARG   A NE  1 
ATOM   415  C  CZ  . ARG   A 1 62  ? 8.640   -0.077  50.786 1.00 100.17 ?  69  ARG   A CZ  1 
ATOM   416  N  NH1 . ARG   A 1 62  ? 8.079   -0.023  49.569 1.00 99.60  ?  69  ARG   A NH1 1 
ATOM   417  N  NH2 . ARG   A 1 62  ? 8.847   1.069   51.444 1.00 98.10  ?  69  ARG   A NH2 1 
ATOM   418  N  N   . LEU   A 1 63  ? 13.020  -3.506  48.404 1.00 66.15  ?  70  LEU   A N   1 
ATOM   419  C  CA  . LEU   A 1 63  ? 14.024  -2.530  47.934 1.00 71.50  ?  70  LEU   A CA  1 
ATOM   420  C  C   . LEU   A 1 63  ? 15.023  -3.169  46.963 1.00 72.61  ?  70  LEU   A C   1 
ATOM   421  O  O   . LEU   A 1 63  ? 16.062  -3.724  47.379 1.00 64.63  ?  70  LEU   A O   1 
ATOM   422  C  CB  . LEU   A 1 63  ? 14.741  -1.852  49.129 1.00 65.20  ?  70  LEU   A CB  1 
ATOM   423  C  CG  . LEU   A 1 63  ? 13.792  -1.204  50.166 1.00 60.61  ?  70  LEU   A CG  1 
ATOM   424  C  CD1 . LEU   A 1 63  ? 14.577  -0.817  51.398 1.00 59.69  ?  70  LEU   A CD1 1 
ATOM   425  C  CD2 . LEU   A 1 63  ? 12.976  -0.028  49.635 1.00 62.25  ?  70  LEU   A CD2 1 
ATOM   426  N  N   . ARG   A 1 64  ? 14.682  -3.079  45.673 1.00 76.66  ?  71  ARG   A N   1 
ATOM   427  C  CA  . ARG   A 1 64  ? 15.536  -3.535  44.568 1.00 79.76  ?  71  ARG   A CA  1 
ATOM   428  C  C   . ARG   A 1 64  ? 16.074  -2.335  43.768 1.00 75.11  ?  71  ARG   A C   1 
ATOM   429  O  O   . ARG   A 1 64  ? 15.295  -1.617  43.158 1.00 67.95  ?  71  ARG   A O   1 
ATOM   430  C  CB  . ARG   A 1 64  ? 14.746  -4.481  43.661 1.00 85.55  ?  71  ARG   A CB  1 
ATOM   431  C  CG  . ARG   A 1 64  ? 14.292  -5.765  44.357 1.00 98.49  ?  71  ARG   A CG  1 
ATOM   432  C  CD  . ARG   A 1 64  ? 14.465  -7.007  43.493 1.00 117.17 ?  71  ARG   A CD  1 
ATOM   433  N  NE  . ARG   A 1 64  ? 14.188  -8.245  44.232 1.00 119.08 ?  71  ARG   A NE  1 
ATOM   434  C  CZ  . ARG   A 1 64  ? 14.981  -8.810  45.155 1.00 113.31 ?  71  ARG   A CZ  1 
ATOM   435  N  NH1 . ARG   A 1 64  ? 16.149  -8.269  45.522 1.00 106.44 ?  71  ARG   A NH1 1 
ATOM   436  N  NH2 . ARG   A 1 64  ? 14.591  -9.946  45.735 1.00 132.55 ?  71  ARG   A NH2 1 
ATOM   437  N  N   . HIS   A 1 65  ? 17.393  -2.112  43.793 1.00 70.26  ?  72  HIS   A N   1 
ATOM   438  C  CA  . HIS   A 1 65  ? 18.025  -1.026  42.994 1.00 64.43  ?  72  HIS   A CA  1 
ATOM   439  C  C   . HIS   A 1 65  ? 19.519  -1.256  42.819 1.00 57.38  ?  72  HIS   A C   1 
ATOM   440  O  O   . HIS   A 1 65  ? 20.159  -1.735  43.740 1.00 55.14  ?  72  HIS   A O   1 
ATOM   441  C  CB  . HIS   A 1 65  ? 17.792  0.331   43.663 1.00 57.03  ?  72  HIS   A CB  1 
ATOM   442  C  CG  . HIS   A 1 65  ? 17.981  1.502   42.744 1.00 62.95  ?  72  HIS   A CG  1 
ATOM   443  N  ND1 . HIS   A 1 65  ? 18.984  2.437   42.911 1.00 60.92  ?  72  HIS   A ND1 1 
ATOM   444  C  CD2 . HIS   A 1 65  ? 17.278  1.898   41.657 1.00 60.65  ?  72  HIS   A CD2 1 
ATOM   445  C  CE1 . HIS   A 1 65  ? 18.900  3.344   41.955 1.00 60.75  ?  72  HIS   A CE1 1 
ATOM   446  N  NE2 . HIS   A 1 65  ? 17.875  3.038   41.179 1.00 56.48  ?  72  HIS   A NE2 1 
ATOM   447  N  N   . SER   A 1 66  ? 20.077  -0.865  41.674 1.00 60.07  ?  73  SER   A N   1 
ATOM   448  C  CA  . SER   A 1 66  ? 21.523  -1.098  41.378 1.00 62.60  ?  73  SER   A CA  1 
ATOM   449  C  C   . SER   A 1 66  ? 22.508  -0.468  42.369 1.00 62.88  ?  73  SER   A C   1 
ATOM   450  O  O   . SER   A 1 66  ? 23.638  -0.938  42.501 1.00 59.76  ?  73  SER   A O   1 
ATOM   451  C  CB  . SER   A 1 66  ? 21.878  -0.636  39.960 1.00 67.00  ?  73  SER   A CB  1 
ATOM   452  O  OG  . SER   A 1 66  ? 21.839  0.772   39.846 1.00 75.15  ?  73  SER   A OG  1 
ATOM   453  N  N   . ARG   A 1 67  ? 22.068  0.606   43.031 1.00 55.83  ?  74  ARG   A N   1 
ATOM   454  C  CA  . ARG   A 1 67  ? 22.817  1.308   44.080 1.00 53.29  ?  74  ARG   A CA  1 
ATOM   455  C  C   . ARG   A 1 67  ? 22.368  1.019   45.508 1.00 51.34  ?  74  ARG   A C   1 
ATOM   456  O  O   . ARG   A 1 67  ? 22.721  1.778   46.424 1.00 53.94  ?  74  ARG   A O   1 
ATOM   457  C  CB  . ARG   A 1 67  ? 22.771  2.837   43.833 1.00 54.89  ?  74  ARG   A CB  1 
ATOM   458  C  CG  . ARG   A 1 67  ? 22.902  3.292   42.390 1.00 52.63  ?  74  ARG   A CG  1 
ATOM   459  C  CD  . ARG   A 1 67  ? 24.151  2.738   41.736 1.00 58.04  ?  74  ARG   A CD  1 
ATOM   460  N  NE  . ARG   A 1 67  ? 24.189  3.144   40.344 1.00 67.58  ?  74  ARG   A NE  1 
ATOM   461  C  CZ  . ARG   A 1 67  ? 24.896  2.567   39.372 1.00 70.39  ?  74  ARG   A CZ  1 
ATOM   462  N  NH1 . ARG   A 1 67  ? 25.697  1.516   39.602 1.00 61.42  ?  74  ARG   A NH1 1 
ATOM   463  N  NH2 . ARG   A 1 67  ? 24.814  3.081   38.142 1.00 78.72  ?  74  ARG   A NH2 1 
ATOM   464  N  N   . VAL   A 1 68  ? 21.620  -0.068  45.715 1.00 55.12  ?  75  VAL   A N   1 
ATOM   465  C  CA  . VAL   A 1 68  ? 21.231  -0.525  47.061 1.00 54.21  ?  75  VAL   A CA  1 
ATOM   466  C  C   . VAL   A 1 68  ? 21.608  -2.009  47.193 1.00 57.75  ?  75  VAL   A C   1 
ATOM   467  O  O   . VAL   A 1 68  ? 21.429  -2.764  46.234 1.00 60.67  ?  75  VAL   A O   1 
ATOM   468  C  CB  . VAL   A 1 68  ? 19.735  -0.297  47.337 1.00 53.50  ?  75  VAL   A CB  1 
ATOM   469  C  CG1 . VAL   A 1 68  ? 19.402  -0.627  48.787 1.00 55.32  ?  75  VAL   A CG1 1 
ATOM   470  C  CG2 . VAL   A 1 68  ? 19.344  1.159   47.096 1.00 64.83  ?  75  VAL   A CG2 1 
ATOM   471  N  N   . VAL   A 1 69  ? 22.142  -2.415  48.358 1.00 53.47  ?  76  VAL   A N   1 
ATOM   472  C  CA  . VAL   A 1 69  ? 22.449  -3.832  48.643 1.00 54.10  ?  76  VAL   A CA  1 
ATOM   473  C  C   . VAL   A 1 69  ? 21.143  -4.627  48.670 1.00 55.36  ?  76  VAL   A C   1 
ATOM   474  O  O   . VAL   A 1 69  ? 20.260  -4.302  49.450 1.00 64.26  ?  76  VAL   A O   1 
ATOM   475  C  CB  . VAL   A 1 69  ? 23.261  -3.983  49.958 1.00 54.08  ?  76  VAL   A CB  1 
ATOM   476  C  CG1 . VAL   A 1 69  ? 23.370  -5.428  50.425 1.00 50.36  ?  76  VAL   A CG1 1 
ATOM   477  C  CG2 . VAL   A 1 69  ? 24.658  -3.410  49.766 1.00 48.88  ?  76  VAL   A CG2 1 
ATOM   478  N  N   . LYS   A 1 70  ? 21.017  -5.613  47.780 1.00 60.70  ?  77  LYS   A N   1 
ATOM   479  C  CA  . LYS   A 1 70  ? 19.856  -6.521  47.760 1.00 67.83  ?  77  LYS   A CA  1 
ATOM   480  C  C   . LYS   A 1 70  ? 19.997  -7.583  48.836 1.00 60.91  ?  77  LYS   A C   1 
ATOM   481  O  O   . LYS   A 1 70  ? 21.055  -8.199  48.967 1.00 60.28  ?  77  LYS   A O   1 
ATOM   482  C  CB  . LYS   A 1 70  ? 19.666  -7.175  46.388 1.00 75.17  ?  77  LYS   A CB  1 
ATOM   483  C  CG  . LYS   A 1 70  ? 19.162  -6.173  45.361 1.00 95.06  ?  77  LYS   A CG  1 
ATOM   484  C  CD  . LYS   A 1 70  ? 19.217  -6.658  43.915 1.00 94.91  ?  77  LYS   A CD  1 
ATOM   485  C  CE  . LYS   A 1 70  ? 18.666  -5.591  42.967 1.00 87.64  ?  77  LYS   A CE  1 
ATOM   486  N  NZ  . LYS   A 1 70  ? 19.488  -5.414  41.746 1.00 87.19  ?  77  LYS   A NZ  1 
ATOM   487  N  N   . LEU   A 1 71  ? 18.918  -7.783  49.597 1.00 64.09  ?  78  LEU   A N   1 
ATOM   488  C  CA  . LEU   A 1 71  ? 18.749  -8.974  50.423 1.00 56.04  ?  78  LEU   A CA  1 
ATOM   489  C  C   . LEU   A 1 71  ? 18.394  -10.110 49.473 1.00 58.77  ?  78  LEU   A C   1 
ATOM   490  O  O   . LEU   A 1 71  ? 17.366  -10.051 48.801 1.00 62.25  ?  78  LEU   A O   1 
ATOM   491  C  CB  . LEU   A 1 71  ? 17.634  -8.777  51.461 1.00 57.84  ?  78  LEU   A CB  1 
ATOM   492  C  CG  . LEU   A 1 71  ? 17.370  -9.959  52.422 1.00 60.74  ?  78  LEU   A CG  1 
ATOM   493  C  CD1 . LEU   A 1 71  ? 18.343  -9.960  53.595 1.00 58.77  ?  78  LEU   A CD1 1 
ATOM   494  C  CD2 . LEU   A 1 71  ? 15.945  -9.977  52.929 1.00 57.54  ?  78  LEU   A CD2 1 
ATOM   495  N  N   . LEU   A 1 72  ? 19.264  -11.122 49.405 1.00 57.17  ?  79  LEU   A N   1 
ATOM   496  C  CA  . LEU   A 1 72  ? 19.084  -12.259 48.509 1.00 57.92  ?  79  LEU   A CA  1 
ATOM   497  C  C   . LEU   A 1 72  ? 18.269  -13.372 49.170 1.00 61.91  ?  79  LEU   A C   1 
ATOM   498  O  O   . LEU   A 1 72  ? 17.499  -14.056 48.494 1.00 65.74  ?  79  LEU   A O   1 
ATOM   499  C  CB  . LEU   A 1 72  ? 20.439  -12.767 48.024 1.00 63.00  ?  79  LEU   A CB  1 
ATOM   500  C  CG  . LEU   A 1 72  ? 21.192  -11.789 47.102 1.00 64.07  ?  79  LEU   A CG  1 
ATOM   501  C  CD1 . LEU   A 1 72  ? 22.648  -12.208 46.948 1.00 58.50  ?  79  LEU   A CD1 1 
ATOM   502  C  CD2 . LEU   A 1 72  ? 20.518  -11.674 45.729 1.00 63.33  ?  79  LEU   A CD2 1 
ATOM   503  N  N   . GLY   A 1 73  ? 18.447  -13.549 50.478 1.00 61.21  ?  80  GLY   A N   1 
ATOM   504  C  CA  . GLY   A 1 73  ? 17.517  -14.364 51.274 1.00 63.57  ?  80  GLY   A CA  1 
ATOM   505  C  C   . GLY   A 1 73  ? 17.742  -14.253 52.770 1.00 64.84  ?  80  GLY   A C   1 
ATOM   506  O  O   . GLY   A 1 73  ? 18.634  -13.531 53.233 1.00 62.26  ?  80  GLY   A O   1 
ATOM   507  N  N   . VAL   A 1 74  ? 16.921  -14.992 53.514 1.00 67.14  ?  81  VAL   A N   1 
ATOM   508  C  CA  . VAL   A 1 74  ? 16.979  -15.065 54.984 1.00 70.13  ?  81  VAL   A CA  1 
ATOM   509  C  C   . VAL   A 1 74  ? 16.952  -16.516 55.433 1.00 71.16  ?  81  VAL   A C   1 
ATOM   510  O  O   . VAL   A 1 74  ? 16.277  -17.333 54.830 1.00 78.67  ?  81  VAL   A O   1 
ATOM   511  C  CB  . VAL   A 1 74  ? 15.821  -14.293 55.676 1.00 68.85  ?  81  VAL   A CB  1 
ATOM   512  C  CG1 . VAL   A 1 74  ? 15.991  -12.815 55.427 1.00 70.68  ?  81  VAL   A CG1 1 
ATOM   513  C  CG2 . VAL   A 1 74  ? 14.442  -14.745 55.201 1.00 65.94  ?  81  VAL   A CG2 1 
ATOM   514  N  N   . ILE   A 1 75  ? 17.717  -16.806 56.481 1.00 71.29  ?  82  ILE   A N   1 
ATOM   515  C  CA  . ILE   A 1 75  ? 17.748  -18.079 57.169 1.00 68.46  ?  82  ILE   A CA  1 
ATOM   516  C  C   . ILE   A 1 75  ? 17.009  -17.804 58.481 1.00 76.14  ?  82  ILE   A C   1 
ATOM   517  O  O   . ILE   A 1 75  ? 17.486  -17.003 59.291 1.00 78.30  ?  82  ILE   A O   1 
ATOM   518  C  CB  . ILE   A 1 75  ? 19.206  -18.556 57.428 1.00 70.17  ?  82  ILE   A CB  1 
ATOM   519  C  CG1 . ILE   A 1 75  ? 19.950  -18.693 56.076 1.00 69.01  ?  82  ILE   A CG1 1 
ATOM   520  C  CG2 . ILE   A 1 75  ? 19.221  -19.880 58.225 1.00 75.81  ?  82  ILE   A CG2 1 
ATOM   521  C  CD1 . ILE   A 1 75  ? 21.359  -19.285 56.095 1.00 71.17  ?  82  ILE   A CD1 1 
ATOM   522  N  N   . ILE   A 1 76  ? 15.837  -18.431 58.646 1.00 78.66  ?  83  ILE   A N   1 
ATOM   523  C  CA  . ILE   A 1 76  ? 15.037  -18.371 59.878 1.00 77.73  ?  83  ILE   A CA  1 
ATOM   524  C  C   . ILE   A 1 76  ? 14.881  -19.832 60.321 1.00 84.56  ?  83  ILE   A C   1 
ATOM   525  O  O   . ILE   A 1 76  ? 13.948  -20.523 59.896 1.00 83.35  ?  83  ILE   A O   1 
ATOM   526  C  CB  . ILE   A 1 76  ? 13.668  -17.681 59.644 1.00 79.18  ?  83  ILE   A CB  1 
ATOM   527  C  CG1 . ILE   A 1 76  ? 13.853  -16.219 59.211 1.00 80.67  ?  83  ILE   A CG1 1 
ATOM   528  C  CG2 . ILE   A 1 76  ? 12.813  -17.683 60.907 1.00 83.94  ?  83  ILE   A CG2 1 
ATOM   529  C  CD1 . ILE   A 1 76  ? 12.638  -15.546 58.625 0.00 77.00  ?  83  ILE   A CD1 1 
ATOM   530  N  N   . GLU   A 1 77  ? 15.811  -20.281 61.169 1.00 83.93  ?  84  GLU   A N   1 
ATOM   531  C  CA  . GLU   A 1 77  ? 15.925  -21.669 61.619 1.00 91.68  ?  84  GLU   A CA  1 
ATOM   532  C  C   . GLU   A 1 77  ? 16.010  -21.745 63.148 1.00 97.13  ?  84  GLU   A C   1 
ATOM   533  O  O   . GLU   A 1 77  ? 16.123  -20.718 63.834 1.00 94.74  ?  84  GLU   A O   1 
ATOM   534  C  CB  . GLU   A 1 77  ? 17.171  -22.313 60.989 1.00 91.58  ?  84  GLU   A CB  1 
ATOM   535  C  CG  . GLU   A 1 77  ? 17.064  -22.517 59.486 1.00 89.29  ?  84  GLU   A CG  1 
ATOM   536  C  CD  . GLU   A 1 77  ? 18.290  -23.180 58.872 1.00 93.45  ?  84  GLU   A CD  1 
ATOM   537  O  OE1 . GLU   A 1 77  ? 19.422  -22.999 59.390 1.00 92.22  ?  84  GLU   A OE1 1 
ATOM   538  O  OE2 . GLU   A 1 77  ? 18.128  -23.874 57.841 1.00 90.53  ?  84  GLU   A OE2 1 
ATOM   539  N  N   . GLU   A 1 78  ? 15.951  -22.981 63.654 1.00 101.14 ?  85  GLU   A N   1 
ATOM   540  C  CA  . GLU   A 1 78  ? 16.053  -23.299 65.091 1.00 107.26 ?  85  GLU   A CA  1 
ATOM   541  C  C   . GLU   A 1 78  ? 17.397  -22.836 65.696 1.00 102.31 ?  85  GLU   A C   1 
ATOM   542  O  O   . GLU   A 1 78  ? 18.444  -23.439 65.450 1.00 102.60 ?  85  GLU   A O   1 
ATOM   543  C  CB  . GLU   A 1 78  ? 15.844  -24.816 65.316 1.00 113.36 ?  85  GLU   A CB  1 
ATOM   544  C  CG  . GLU   A 1 78  ? 15.587  -25.244 66.759 1.00 123.70 ?  85  GLU   A CG  1 
ATOM   545  C  CD  . GLU   A 1 78  ? 14.120  -25.201 67.158 1.00 128.05 ?  85  GLU   A CD  1 
ATOM   546  O  OE1 . GLU   A 1 78  ? 13.415  -24.227 66.803 1.00 125.18 ?  85  GLU   A OE1 1 
ATOM   547  O  OE2 . GLU   A 1 78  ? 13.674  -26.147 67.844 1.00 132.75 ?  85  GLU   A OE2 1 
ATOM   548  N  N   . GLY   A 1 79  ? 17.346  -21.738 66.452 1.00 101.35 ?  86  GLY   A N   1 
ATOM   549  C  CA  . GLY   A 1 79  ? 18.519  -21.147 67.091 1.00 101.04 ?  86  GLY   A CA  1 
ATOM   550  C  C   . GLY   A 1 79  ? 19.526  -20.400 66.220 1.00 96.88  ?  86  GLY   A C   1 
ATOM   551  O  O   . GLY   A 1 79  ? 20.663  -20.199 66.651 1.00 100.79 ?  86  GLY   A O   1 
ATOM   552  N  N   . LYS   A 1 80  ? 19.135  -19.999 65.003 1.00 90.83  ?  87  LYS   A N   1 
ATOM   553  C  CA  . LYS   A 1 80  ? 20.045  -19.303 64.061 1.00 89.80  ?  87  LYS   A CA  1 
ATOM   554  C  C   . LYS   A 1 80  ? 19.263  -18.454 63.044 1.00 88.90  ?  87  LYS   A C   1 
ATOM   555  O  O   . LYS   A 1 80  ? 18.400  -18.967 62.320 1.00 85.06  ?  87  LYS   A O   1 
ATOM   556  C  CB  . LYS   A 1 80  ? 20.964  -20.306 63.338 1.00 88.97  ?  87  LYS   A CB  1 
ATOM   557  C  CG  . LYS   A 1 80  ? 22.146  -19.694 62.581 1.00 82.57  ?  87  LYS   A CG  1 
ATOM   558  C  CD  . LYS   A 1 80  ? 22.717  -20.647 61.546 1.00 81.45  ?  87  LYS   A CD  1 
ATOM   559  C  CE  . LYS   A 1 80  ? 23.586  -19.931 60.528 1.00 80.35  ?  87  LYS   A CE  1 
ATOM   560  N  NZ  . LYS   A 1 80  ? 24.080  -20.863 59.482 1.00 82.72  ?  87  LYS   A NZ  1 
ATOM   561  N  N   . TYR   A 1 81  ? 19.609  -17.164 62.991 1.00 93.28  ?  88  TYR   A N   1 
ATOM   562  C  CA  . TYR   A 1 81  ? 18.874  -16.147 62.220 1.00 89.97  ?  88  TYR   A CA  1 
ATOM   563  C  C   . TYR   A 1 81  ? 19.880  -15.295 61.459 1.00 80.82  ?  88  TYR   A C   1 
ATOM   564  O  O   . TYR   A 1 81  ? 20.682  -14.604 62.091 1.00 84.40  ?  88  TYR   A O   1 
ATOM   565  C  CB  . TYR   A 1 81  ? 18.011  -15.291 63.166 1.00 99.07  ?  88  TYR   A CB  1 
ATOM   566  C  CG  . TYR   A 1 81  ? 17.014  -16.111 63.981 1.00 101.94 ?  88  TYR   A CG  1 
ATOM   567  C  CD1 . TYR   A 1 81  ? 17.384  -16.685 65.210 1.00 105.59 ?  88  TYR   A CD1 1 
ATOM   568  C  CD2 . TYR   A 1 81  ? 15.702  -16.336 63.518 1.00 105.40 ?  88  TYR   A CD2 1 
ATOM   569  C  CE1 . TYR   A 1 81  ? 16.487  -17.456 65.949 1.00 118.77 ?  88  TYR   A CE1 1 
ATOM   570  C  CE2 . TYR   A 1 81  ? 14.795  -17.102 64.255 1.00 111.72 ?  88  TYR   A CE2 1 
ATOM   571  C  CZ  . TYR   A 1 81  ? 15.191  -17.659 65.468 1.00 115.33 ?  88  TYR   A CZ  1 
ATOM   572  O  OH  . TYR   A 1 81  ? 14.311  -18.413 66.196 1.00 120.98 ?  88  TYR   A OH  1 
ATOM   573  N  N   . SER   A 1 82  ? 19.889  -15.409 60.120 1.00 77.09  ?  89  SER   A N   1 
ATOM   574  C  CA  . SER   A 1 82  ? 20.866  -14.716 59.258 1.00 74.12  ?  89  SER   A CA  1 
ATOM   575  C  C   . SER   A 1 82  ? 20.211  -13.981 58.102 1.00 70.57  ?  89  SER   A C   1 
ATOM   576  O  O   . SER   A 1 82  ? 19.206  -14.454 57.553 1.00 68.98  ?  89  SER   A O   1 
ATOM   577  C  CB  . SER   A 1 82  ? 21.892  -15.692 58.665 1.00 73.30  ?  89  SER   A CB  1 
ATOM   578  O  OG  . SER   A 1 82  ? 22.539  -16.441 59.665 1.00 78.91  ?  89  SER   A OG  1 
ATOM   579  N  N   . LEU   A 1 83  ? 20.791  -12.825 57.750 1.00 73.01  ?  90  LEU   A N   1 
ATOM   580  C  CA  . LEU   A 1 83  ? 20.459  -12.087 56.527 1.00 65.79  ?  90  LEU   A CA  1 
ATOM   581  C  C   . LEU   A 1 83  ? 21.558  -12.379 55.538 1.00 68.49  ?  90  LEU   A C   1 
ATOM   582  O  O   . LEU   A 1 83  ? 22.763  -12.414 55.909 1.00 62.49  ?  90  LEU   A O   1 
ATOM   583  C  CB  . LEU   A 1 83  ? 20.370  -10.581 56.786 1.00 60.49  ?  90  LEU   A CB  1 
ATOM   584  C  CG  . LEU   A 1 83  ? 19.366  -10.153 57.850 1.00 59.66  ?  90  LEU   A CG  1 
ATOM   585  C  CD1 . LEU   A 1 83  ? 19.492  -8.658  58.127 1.00 56.53  ?  90  LEU   A CD1 1 
ATOM   586  C  CD2 . LEU   A 1 83  ? 17.928  -10.522 57.478 1.00 59.56  ?  90  LEU   A CD2 1 
ATOM   587  N  N   . VAL   A 1 84  ? 21.141  -12.616 54.290 1.00 65.44  ?  91  VAL   A N   1 
ATOM   588  C  CA  . VAL   A 1 84  ? 22.046  -12.997 53.200 1.00 68.88  ?  91  VAL   A CA  1 
ATOM   589  C  C   . VAL   A 1 84  ? 21.924  -11.927 52.132 1.00 65.11  ?  91  VAL   A C   1 
ATOM   590  O  O   . VAL   A 1 84  ? 20.817  -11.666 51.636 1.00 60.21  ?  91  VAL   A O   1 
ATOM   591  C  CB  . VAL   A 1 84  ? 21.716  -14.387 52.606 1.00 72.00  ?  91  VAL   A CB  1 
ATOM   592  C  CG1 . VAL   A 1 84  ? 22.634  -14.748 51.441 1.00 76.36  ?  91  VAL   A CG1 1 
ATOM   593  C  CG2 . VAL   A 1 84  ? 21.826  -15.445 53.691 1.00 80.29  ?  91  VAL   A CG2 1 
ATOM   594  N  N   . MET   A 1 85  ? 23.072  -11.361 51.775 1.00 62.12  ?  92  MET   A N   1 
ATOM   595  C  CA  . MET   A 1 85  ? 23.135  -10.177 50.916 1.00 66.87  ?  92  MET   A CA  1 
ATOM   596  C  C   . MET   A 1 85  ? 24.249  -10.352 49.915 1.00 68.52  ?  92  MET   A C   1 
ATOM   597  O  O   . MET   A 1 85  ? 25.122  -11.233 50.065 1.00 60.92  ?  92  MET   A O   1 
ATOM   598  C  CB  . MET   A 1 85  ? 23.348  -8.888  51.741 1.00 63.80  ?  92  MET   A CB  1 
ATOM   599  C  CG  . MET   A 1 85  ? 24.230  -9.068  52.961 1.00 73.67  ?  92  MET   A CG  1 
ATOM   600  S  SD  . MET   A 1 85  ? 24.810  -7.538  53.682 1.00 88.00  ?  92  MET   A SD  1 
ATOM   601  C  CE  . MET   A 1 85  ? 26.081  -7.045  52.511 1.00 70.72  ?  92  MET   A CE  1 
ATOM   602  N  N   . GLU   A 1 86  ? 24.208  -9.492  48.901 1.00 65.82  ?  93  GLU   A N   1 
ATOM   603  C  CA  . GLU   A 1 86  ? 25.165  -9.564  47.795 1.00 60.70  ?  93  GLU   A CA  1 
ATOM   604  C  C   . GLU   A 1 86  ? 26.570  -9.194  48.218 1.00 55.56  ?  93  GLU   A C   1 
ATOM   605  O  O   . GLU   A 1 86  ? 26.771  -8.510  49.203 1.00 60.26  ?  93  GLU   A O   1 
ATOM   606  C  CB  . GLU   A 1 86  ? 24.710  -8.832  46.522 1.00 62.80  ?  93  GLU   A CB  1 
ATOM   607  C  CG  . GLU   A 1 86  ? 24.274  -7.379  46.633 1.00 73.03  ?  93  GLU   A CG  1 
ATOM   608  C  CD  . GLU   A 1 86  ? 23.601  -6.845  45.372 1.00 76.24  ?  93  GLU   A CD  1 
ATOM   609  O  OE1 . GLU   A 1 86  ? 23.679  -7.480  44.291 1.00 80.12  ?  93  GLU   A OE1 1 
ATOM   610  O  OE2 . GLU   A 1 86  ? 22.990  -5.753  45.478 1.00 61.75  ?  93  GLU   A OE2 1 
ATOM   611  N  N   . TYR   A 1 87  ? 27.540  -9.745  47.493 1.00 66.04  ?  94  TYR   A N   1 
ATOM   612  C  CA  . TYR   A 1 87  ? 28.990  -9.606  47.783 1.00 72.58  ?  94  TYR   A CA  1 
ATOM   613  C  C   . TYR   A 1 87  ? 29.537  -8.333  47.126 1.00 66.07  ?  94  TYR   A C   1 
ATOM   614  O  O   . TYR   A 1 87  ? 29.216  -8.067  45.965 1.00 64.29  ?  94  TYR   A O   1 
ATOM   615  C  CB  . TYR   A 1 87  ? 29.753  -10.838 47.246 1.00 68.70  ?  94  TYR   A CB  1 
ATOM   616  C  CG  . TYR   A 1 87  ? 31.262  -10.801 47.432 1.00 66.44  ?  94  TYR   A CG  1 
ATOM   617  C  CD1 . TYR   A 1 87  ? 31.819  -10.585 48.696 1.00 69.35  ?  94  TYR   A CD1 1 
ATOM   618  C  CD2 . TYR   A 1 87  ? 32.136  -10.957 46.344 1.00 72.23  ?  94  TYR   A CD2 1 
ATOM   619  C  CE1 . TYR   A 1 87  ? 33.204  -10.542 48.883 1.00 84.33  ?  94  TYR   A CE1 1 
ATOM   620  C  CE2 . TYR   A 1 87  ? 33.527  -10.924 46.519 1.00 82.48  ?  94  TYR   A CE2 1 
ATOM   621  C  CZ  . TYR   A 1 87  ? 34.058  -10.721 47.789 1.00 87.49  ?  94  TYR   A CZ  1 
ATOM   622  O  OH  . TYR   A 1 87  ? 35.422  -10.682 47.974 1.00 90.59  ?  94  TYR   A OH  1 
ATOM   623  N  N   . MET   A 1 88  ? 30.350  -7.566  47.868 1.00 68.59  ?  95  MET   A N   1 
ATOM   624  C  CA  . MET   A 1 88  ? 30.955  -6.325  47.376 1.00 62.69  ?  95  MET   A CA  1 
ATOM   625  C  C   . MET   A 1 88  ? 32.453  -6.377  47.657 1.00 64.10  ?  95  MET   A C   1 
ATOM   626  O  O   . MET   A 1 88  ? 32.870  -6.179  48.789 1.00 69.39  ?  95  MET   A O   1 
ATOM   627  C  CB  . MET   A 1 88  ? 30.292  -5.118  48.038 1.00 58.64  ?  95  MET   A CB  1 
ATOM   628  C  CG  . MET   A 1 88  ? 28.823  -4.972  47.671 1.00 63.25  ?  95  MET   A CG  1 
ATOM   629  S  SD  . MET   A 1 88  ? 28.523  -4.635  45.918 1.00 72.59  ?  95  MET   A SD  1 
ATOM   630  C  CE  . MET   A 1 88  ? 28.864  -2.890  45.837 1.00 70.58  ?  95  MET   A CE  1 
ATOM   631  N  N   . GLU   A 1 89  ? 33.237  -6.628  46.607 1.00 66.71  ?  96  GLU   A N   1 
ATOM   632  C  CA  . GLU   A 1 89  ? 34.635  -7.108  46.720 1.00 75.89  ?  96  GLU   A CA  1 
ATOM   633  C  C   . GLU   A 1 89  ? 35.598  -6.145  47.442 1.00 76.76  ?  96  GLU   A C   1 
ATOM   634  O  O   . GLU   A 1 89  ? 36.386  -6.576  48.283 1.00 76.14  ?  96  GLU   A O   1 
ATOM   635  C  CB  . GLU   A 1 89  ? 35.165  -7.470  45.331 1.00 73.13  ?  96  GLU   A CB  1 
ATOM   636  C  CG  . GLU   A 1 89  ? 36.530  -8.124  45.315 1.00 78.77  ?  96  GLU   A CG  1 
ATOM   637  C  CD  . GLU   A 1 89  ? 36.874  -8.797  43.997 1.00 87.07  ?  96  GLU   A CD  1 
ATOM   638  O  OE1 . GLU   A 1 89  ? 38.003  -9.319  43.903 1.00 85.36  ?  96  GLU   A OE1 1 
ATOM   639  O  OE2 . GLU   A 1 89  ? 36.045  -8.819  43.057 1.00 88.06  ?  96  GLU   A OE2 1 
ATOM   640  N  N   . LYS   A 1 90  ? 35.494  -4.852  47.143 1.00 74.97  ?  97  LYS   A N   1 
ATOM   641  C  CA  . LYS   A 1 90  ? 36.399  -3.849  47.728 1.00 75.02  ?  97  LYS   A CA  1 
ATOM   642  C  C   . LYS   A 1 90  ? 36.020  -3.352  49.132 1.00 67.92  ?  97  LYS   A C   1 
ATOM   643  O  O   . LYS   A 1 90  ? 36.748  -2.520  49.682 1.00 80.30  ?  97  LYS   A O   1 
ATOM   644  C  CB  . LYS   A 1 90  ? 36.630  -2.691  46.745 1.00 71.17  ?  97  LYS   A CB  1 
ATOM   645  C  CG  . LYS   A 1 90  ? 37.415  -3.123  45.519 1.00 79.07  ?  97  LYS   A CG  1 
ATOM   646  C  CD  . LYS   A 1 90  ? 37.868  -1.936  44.669 1.00 88.68  ?  97  LYS   A CD  1 
ATOM   647  C  CE  . LYS   A 1 90  ? 39.049  -2.298  43.767 1.00 92.20  ?  97  LYS   A CE  1 
ATOM   648  N  NZ  . LYS   A 1 90  ? 40.314  -2.302  44.383 0.00 92.42  ?  97  LYS   A NZ  1 
ATOM   649  N  N   . GLY   A 1 91  ? 34.937  -3.868  49.727 1.00 63.45  ?  98  GLY   A N   1 
ATOM   650  C  CA  . GLY   A 1 91  ? 34.549  -3.490  51.097 1.00 63.68  ?  98  GLY   A CA  1 
ATOM   651  C  C   . GLY   A 1 91  ? 33.904  -2.102  51.139 1.00 57.82  ?  98  GLY   A C   1 
ATOM   652  O  O   . GLY   A 1 91  ? 33.382  -1.648  50.129 1.00 53.63  ?  98  GLY   A O   1 
ATOM   653  N  N   . ASN   A 1 92  ? 33.946  -1.444  52.293 1.00 55.61  ?  99  ASN   A N   1 
ATOM   654  C  CA  . ASN   A 1 92  ? 33.290  -0.112  52.462 1.00 55.48  ?  99  ASN   A CA  1 
ATOM   655  C  C   . ASN   A 1 92  ? 34.076  1.032   51.805 1.00 56.67  ?  99  ASN   A C   1 
ATOM   656  O  O   . ASN   A 1 92  ? 35.249  0.875   51.406 1.00 55.99  ?  99  ASN   A O   1 
ATOM   657  C  CB  . ASN   A 1 92  ? 32.917  0.190   53.935 1.00 51.32  ?  99  ASN   A CB  1 
ATOM   658  C  CG  . ASN   A 1 92  ? 34.116  0.272   54.871 1.00 57.92  ?  99  ASN   A CG  1 
ATOM   659  O  OD1 . ASN   A 1 92  ? 35.158  0.848   54.542 1.00 59.85  ?  99  ASN   A OD1 1 
ATOM   660  N  ND2 . ASN   A 1 92  ? 33.970  -0.313  56.054 1.00 65.95  ?  99  ASN   A ND2 1 
ATOM   661  N  N   . LEU   A 1 93  ? 33.417  2.181   51.699 1.00 56.87  ?  100 LEU   A N   1 
ATOM   662  C  CA  . LEU   A 1 93  ? 33.972  3.350   51.051 1.00 58.72  ?  100 LEU   A CA  1 
ATOM   663  C  C   . LEU   A 1 93  ? 35.255  3.901   51.700 1.00 60.36  ?  100 LEU   A C   1 
ATOM   664  O  O   . LEU   A 1 93  ? 36.158  4.308   50.979 1.00 55.91  ?  100 LEU   A O   1 
ATOM   665  C  CB  . LEU   A 1 93  ? 32.927  4.451   50.982 1.00 57.81  ?  100 LEU   A CB  1 
ATOM   666  C  CG  . LEU   A 1 93  ? 33.305  5.734   50.235 1.00 51.60  ?  100 LEU   A CG  1 
ATOM   667  C  CD1 . LEU   A 1 93  ? 33.711  5.480   48.786 1.00 53.23  ?  100 LEU   A CD1 1 
ATOM   668  C  CD2 . LEU   A 1 93  ? 32.115  6.654   50.290 1.00 53.57  ?  100 LEU   A CD2 1 
ATOM   669  N  N   . MET   A 1 94  ? 35.317  3.909   53.033 1.00 65.73  ?  101 MET   A N   1 
ATOM   670  C  CA  . MET   A 1 94  ? 36.482  4.423   53.760 1.00 68.41  ?  101 MET   A CA  1 
ATOM   671  C  C   . MET   A 1 94  ? 37.718  3.565   53.561 1.00 71.66  ?  101 MET   A C   1 
ATOM   672  O  O   . MET   A 1 94  ? 38.808  4.105   53.408 1.00 71.82  ?  101 MET   A O   1 
ATOM   673  C  CB  . MET   A 1 94  ? 36.182  4.588   55.264 1.00 66.99  ?  101 MET   A CB  1 
ATOM   674  C  CG  . MET   A 1 94  ? 37.219  5.379   56.065 1.00 65.54  ?  101 MET   A CG  1 
ATOM   675  S  SD  . MET   A 1 94  ? 37.665  7.024   55.447 1.00 76.16  ?  101 MET   A SD  1 
ATOM   676  C  CE  . MET   A 1 94  ? 36.079  7.832   55.272 1.00 63.57  ?  101 MET   A CE  1 
ATOM   677  N  N   . HIS   A 1 95  ? 37.532  2.243   53.549 1.00 67.90  ?  102 HIS   A N   1 
ATOM   678  C  CA  . HIS   A 1 95  ? 38.609  1.294   53.239 1.00 68.40  ?  102 HIS   A CA  1 
ATOM   679  C  C   . HIS   A 1 95  ? 39.225  1.500   51.842 1.00 73.05  ?  102 HIS   A C   1 
ATOM   680  O  O   . HIS   A 1 95  ? 40.451  1.405   51.691 1.00 72.29  ?  102 HIS   A O   1 
ATOM   681  C  CB  . HIS   A 1 95  ? 38.127  -0.153  53.415 1.00 70.40  ?  102 HIS   A CB  1 
ATOM   682  C  CG  . HIS   A 1 95  ? 39.209  -1.172  53.295 1.00 70.41  ?  102 HIS   A CG  1 
ATOM   683  N  ND1 . HIS   A 1 95  ? 39.523  -1.790  52.103 1.00 77.36  ?  102 HIS   A ND1 1 
ATOM   684  C  CD2 . HIS   A 1 95  ? 40.046  -1.693  54.219 1.00 77.66  ?  102 HIS   A CD2 1 
ATOM   685  C  CE1 . HIS   A 1 95  ? 40.515  -2.640  52.295 1.00 71.92  ?  102 HIS   A CE1 1 
ATOM   686  N  NE2 . HIS   A 1 95  ? 40.847  -2.604  53.572 1.00 74.55  ?  102 HIS   A NE2 1 
ATOM   687  N  N   . VAL   A 1 96  ? 38.389  1.818   50.850 1.00 70.98  ?  103 VAL   A N   1 
ATOM   688  C  CA  . VAL   A 1 96  ? 38.868  2.090   49.477 1.00 73.46  ?  103 VAL   A CA  1 
ATOM   689  C  C   . VAL   A 1 96  ? 39.579  3.447   49.375 1.00 74.66  ?  103 VAL   A C   1 
ATOM   690  O  O   . VAL   A 1 96  ? 40.604  3.560   48.696 1.00 73.39  ?  103 VAL   A O   1 
ATOM   691  C  CB  . VAL   A 1 96  ? 37.727  1.962   48.443 1.00 79.86  ?  103 VAL   A CB  1 
ATOM   692  C  CG1 . VAL   A 1 96  ? 38.175  2.345   47.030 1.00 80.42  ?  103 VAL   A CG1 1 
ATOM   693  C  CG2 . VAL   A 1 96  ? 37.203  0.526   48.440 1.00 86.01  ?  103 VAL   A CG2 1 
ATOM   694  N  N   . LEU   A 1 97  ? 39.037  4.461   50.047 1.00 75.05  ?  104 LEU   A N   1 
ATOM   695  C  CA  . LEU   A 1 97  ? 39.671  5.787   50.111 1.00 77.25  ?  104 LEU   A CA  1 
ATOM   696  C  C   . LEU   A 1 97  ? 41.037  5.825   50.805 1.00 76.33  ?  104 LEU   A C   1 
ATOM   697  O  O   . LEU   A 1 97  ? 41.825  6.715   50.508 1.00 79.06  ?  104 LEU   A O   1 
ATOM   698  C  CB  . LEU   A 1 97  ? 38.730  6.807   50.765 1.00 67.16  ?  104 LEU   A CB  1 
ATOM   699  C  CG  . LEU   A 1 97  ? 37.503  7.145   49.920 1.00 64.52  ?  104 LEU   A CG  1 
ATOM   700  C  CD1 . LEU   A 1 97  ? 36.421  7.781   50.775 1.00 68.83  ?  104 LEU   A CD1 1 
ATOM   701  C  CD2 . LEU   A 1 97  ? 37.836  8.021   48.725 1.00 63.98  ?  104 LEU   A CD2 1 
ATOM   702  N  N   . LYS   A 1 98  ? 41.295  4.881   51.714 1.00 81.82  ?  105 LYS   A N   1 
ATOM   703  C  CA  . LYS   A 1 98  ? 42.586  4.758   52.415 1.00 79.98  ?  105 LYS   A CA  1 
ATOM   704  C  C   . LYS   A 1 98  ? 43.683  3.922   51.721 1.00 77.35  ?  105 LYS   A C   1 
ATOM   705  O  O   . LYS   A 1 98  ? 44.818  3.912   52.219 1.00 81.49  ?  105 LYS   A O   1 
ATOM   706  C  CB  . LYS   A 1 98  ? 42.349  4.264   53.853 1.00 79.95  ?  105 LYS   A CB  1 
ATOM   707  C  CG  . LYS   A 1 98  ? 41.691  5.323   54.720 1.00 86.82  ?  105 LYS   A CG  1 
ATOM   708  C  CD  . LYS   A 1 98  ? 41.553  4.865   56.155 1.00 92.36  ?  105 LYS   A CD  1 
ATOM   709  C  CE  . LYS   A 1 98  ? 41.172  6.020   57.058 1.00 94.65  ?  105 LYS   A CE  1 
ATOM   710  N  NZ  . LYS   A 1 98  ? 41.071  5.542   58.459 1.00 101.69 ?  105 LYS   A NZ  1 
ATOM   711  N  N   . ALA   A 1 99  ? 43.393  3.287   50.577 1.00 75.74  ?  106 ALA   A N   1 
ATOM   712  C  CA  . ALA   A 1 99  ? 44.373  2.395   49.889 1.00 81.29  ?  106 ALA   A CA  1 
ATOM   713  C  C   . ALA   A 1 99  ? 45.578  3.136   49.284 1.00 95.30  ?  106 ALA   A C   1 
ATOM   714  O  O   . ALA   A 1 99  ? 45.511  4.342   49.050 1.00 96.05  ?  106 ALA   A O   1 
ATOM   715  C  CB  . ALA   A 1 99  ? 43.692  1.564   48.813 1.00 77.09  ?  106 ALA   A CB  1 
ATOM   716  N  N   . GLU   A 1 100 ? 46.664  2.394   49.030 1.00 109.77 ?  107 GLU   A N   1 
ATOM   717  C  CA  . GLU   A 1 100 ? 47.932  2.960   48.494 1.00 119.56 ?  107 GLU   A CA  1 
ATOM   718  C  C   . GLU   A 1 100 ? 47.786  3.545   47.071 1.00 129.27 ?  107 GLU   A C   1 
ATOM   719  O  O   . GLU   A 1 100 ? 48.360  4.598   46.771 1.00 131.57 ?  107 GLU   A O   1 
ATOM   720  C  CB  . GLU   A 1 100 ? 49.081  1.928   48.535 1.00 127.02 ?  107 GLU   A CB  1 
ATOM   721  C  CG  . GLU   A 1 100 ? 49.623  1.631   49.928 1.00 123.71 ?  107 GLU   A CG  1 
ATOM   722  C  CD  . GLU   A 1 100 ? 50.642  0.487   49.923 0.00 136.12 ?  107 GLU   A CD  1 
ATOM   723  O  OE1 . GLU   A 1 100 ? 51.547  0.481   49.060 0.00 138.62 ?  107 GLU   A OE1 1 
ATOM   724  O  OE2 . GLU   A 1 100 ? 50.543  -0.399  50.800 0.00 136.94 ?  107 GLU   A OE2 1 
ATOM   725  N  N   . MET   A 1 101 ? 47.027  2.856   46.213 1.00 137.72 ?  108 MET   A N   1 
ATOM   726  C  CA  . MET   A 1 101 ? 46.620  3.377   44.903 1.00 135.15 ?  108 MET   A CA  1 
ATOM   727  C  C   . MET   A 1 101 ? 45.494  4.381   45.131 1.00 127.95 ?  108 MET   A C   1 
ATOM   728  O  O   . MET   A 1 101 ? 44.459  4.031   45.714 1.00 128.57 ?  108 MET   A O   1 
ATOM   729  C  CB  . MET   A 1 101 ? 46.129  2.250   43.987 1.00 137.49 ?  108 MET   A CB  1 
ATOM   730  C  CG  . MET   A 1 101 ? 47.167  1.171   43.704 1.00 147.55 ?  108 MET   A CG  1 
ATOM   731  S  SD  . MET   A 1 101 ? 48.751  1.640   43.073 0.00 158.15 ?  108 MET   A SD  1 
ATOM   732  C  CE  . MET   A 1 101 ? 48.300  2.514   41.575 0.00 157.29 ?  108 MET   A CE  1 
ATOM   733  N  N   . SER   A 1 102 ? 45.694  5.618   44.670 1.00 125.37 ?  109 SER   A N   1 
ATOM   734  C  CA  . SER   A 1 102 ? 44.711  6.707   44.871 1.00 119.06 ?  109 SER   A CA  1 
ATOM   735  C  C   . SER   A 1 102 ? 43.512  6.558   43.917 1.00 97.48  ?  109 SER   A C   1 
ATOM   736  O  O   . SER   A 1 102 ? 43.658  6.054   42.802 1.00 86.59  ?  109 SER   A O   1 
ATOM   737  C  CB  . SER   A 1 102 ? 45.363  8.104   44.727 1.00 124.93 ?  109 SER   A CB  1 
ATOM   738  O  OG  . SER   A 1 102 ? 45.166  8.680   43.443 1.00 125.13 ?  109 SER   A OG  1 
ATOM   739  N  N   . THR   A 1 103 ? 42.344  7.031   44.357 1.00 92.03  ?  110 THR   A N   1 
ATOM   740  C  CA  . THR   A 1 103 ? 41.137  7.098   43.523 1.00 77.27  ?  110 THR   A CA  1 
ATOM   741  C  C   . THR   A 1 103 ? 41.155  8.437   42.771 1.00 76.86  ?  110 THR   A C   1 
ATOM   742  O  O   . THR   A 1 103 ? 41.228  9.483   43.425 1.00 81.53  ?  110 THR   A O   1 
ATOM   743  C  CB  . THR   A 1 103 ? 39.871  7.000   44.387 1.00 71.05  ?  110 THR   A CB  1 
ATOM   744  O  OG1 . THR   A 1 103 ? 39.964  5.844   45.237 1.00 61.71  ?  110 THR   A OG1 1 
ATOM   745  C  CG2 . THR   A 1 103 ? 38.621  6.877   43.526 1.00 73.44  ?  110 THR   A CG2 1 
ATOM   746  N  N   . PRO   A 1 104 ? 41.079  8.422   41.416 1.00 73.86  ?  111 PRO   A N   1 
ATOM   747  C  CA  . PRO   A 1 104 ? 40.985  9.710   40.703 1.00 77.69  ?  111 PRO   A CA  1 
ATOM   748  C  C   . PRO   A 1 104 ? 39.660  10.461  40.877 1.00 74.11  ?  111 PRO   A C   1 
ATOM   749  O  O   . PRO   A 1 104 ? 38.683  9.910   41.369 1.00 71.29  ?  111 PRO   A O   1 
ATOM   750  C  CB  . PRO   A 1 104 ? 41.197  9.322   39.233 1.00 83.47  ?  111 PRO   A CB  1 
ATOM   751  C  CG  . PRO   A 1 104 ? 40.754  7.910   39.164 1.00 79.77  ?  111 PRO   A CG  1 
ATOM   752  C  CD  . PRO   A 1 104 ? 41.208  7.307   40.461 1.00 77.57  ?  111 PRO   A CD  1 
ATOM   753  N  N   . LEU   A 1 105 ? 39.681  11.729  40.475 1.00 80.92  ?  112 LEU   A N   1 
ATOM   754  C  CA  . LEU   A 1 105 ? 38.536  12.643  40.588 1.00 71.65  ?  112 LEU   A CA  1 
ATOM   755  C  C   . LEU   A 1 105 ? 37.281  12.197  39.813 1.00 70.75  ?  112 LEU   A C   1 
ATOM   756  O  O   . LEU   A 1 105 ? 36.162  12.428  40.284 1.00 76.94  ?  112 LEU   A O   1 
ATOM   757  C  CB  . LEU   A 1 105 ? 38.952  14.042  40.125 1.00 72.13  ?  112 LEU   A CB  1 
ATOM   758  C  CG  . LEU   A 1 105 ? 37.932  15.176  40.046 1.00 67.76  ?  112 LEU   A CG  1 
ATOM   759  C  CD1 . LEU   A 1 105 ? 37.305  15.426  41.395 1.00 62.02  ?  112 LEU   A CD1 1 
ATOM   760  C  CD2 . LEU   A 1 105 ? 38.637  16.418  39.536 1.00 74.38  ?  112 LEU   A CD2 1 
ATOM   761  N  N   . SER   A 1 106 ? 37.469  11.601  38.632 1.00 72.53  ?  113 SER   A N   1 
ATOM   762  C  CA  . SER   A 1 106 ? 36.347  11.114  37.810 1.00 72.10  ?  113 SER   A CA  1 
ATOM   763  C  C   . SER   A 1 106 ? 35.587  9.974   38.486 1.00 68.46  ?  113 SER   A C   1 
ATOM   764  O  O   . SER   A 1 106 ? 34.350  9.948   38.444 1.00 62.09  ?  113 SER   A O   1 
ATOM   765  C  CB  . SER   A 1 106 ? 36.831  10.650  36.445 1.00 76.99  ?  113 SER   A CB  1 
ATOM   766  O  OG  . SER   A 1 106 ? 37.387  11.733  35.746 1.00 96.90  ?  113 SER   A OG  1 
ATOM   767  N  N   . VAL   A 1 107 ? 36.338  9.061   39.117 1.00 62.28  ?  114 VAL   A N   1 
ATOM   768  C  CA  . VAL   A 1 107 ? 35.767  7.936   39.869 1.00 68.67  ?  114 VAL   A CA  1 
ATOM   769  C  C   . VAL   A 1 107 ? 35.012  8.439   41.103 1.00 62.65  ?  114 VAL   A C   1 
ATOM   770  O  O   . VAL   A 1 107 ? 33.905  7.986   41.367 1.00 49.91  ?  114 VAL   A O   1 
ATOM   771  C  CB  . VAL   A 1 107 ? 36.856  6.872   40.225 1.00 62.66  ?  114 VAL   A CB  1 
ATOM   772  C  CG1 . VAL   A 1 107 ? 36.355  5.800   41.191 1.00 56.53  ?  114 VAL   A CG1 1 
ATOM   773  C  CG2 . VAL   A 1 107 ? 37.354  6.210   38.952 1.00 62.84  ?  114 VAL   A CG2 1 
ATOM   774  N  N   . LYS   A 1 108 ? 35.627  9.366   41.837 1.00 65.19  ?  115 LYS   A N   1 
ATOM   775  C  CA  . LYS   A 1 108 ? 34.980  10.046  42.969 1.00 57.23  ?  115 LYS   A CA  1 
ATOM   776  C  C   . LYS   A 1 108 ? 33.671  10.714  42.588 1.00 55.93  ?  115 LYS   A C   1 
ATOM   777  O  O   . LYS   A 1 108 ? 32.659  10.515  43.278 1.00 64.30  ?  115 LYS   A O   1 
ATOM   778  C  CB  . LYS   A 1 108 ? 35.936  11.056  43.633 1.00 61.37  ?  115 LYS   A CB  1 
ATOM   779  C  CG  . LYS   A 1 108 ? 37.010  10.344  44.430 1.00 64.14  ?  115 LYS   A CG  1 
ATOM   780  C  CD  . LYS   A 1 108 ? 37.887  11.255  45.263 1.00 63.79  ?  115 LYS   A CD  1 
ATOM   781  C  CE  . LYS   A 1 108 ? 38.928  10.407  45.968 1.00 64.23  ?  115 LYS   A CE  1 
ATOM   782  N  NZ  . LYS   A 1 108 ? 39.716  11.144  46.978 1.00 70.32  ?  115 LYS   A NZ  1 
ATOM   783  N  N   . GLY   A 1 109 ? 33.679  11.457  41.485 1.00 53.84  ?  116 GLY   A N   1 
ATOM   784  C  CA  . GLY   A 1 109 ? 32.451  12.051  40.921 1.00 58.07  ?  116 GLY   A CA  1 
ATOM   785  C  C   . GLY   A 1 109 ? 31.340  11.050  40.634 1.00 62.54  ?  116 GLY   A C   1 
ATOM   786  O  O   . GLY   A 1 109 ? 30.174  11.297  40.953 1.00 68.70  ?  116 GLY   A O   1 
ATOM   787  N  N   . ARG   A 1 110 ? 31.723  9.919   40.053 1.00 61.10  ?  117 ARG   A N   1 
ATOM   788  C  CA  . ARG   A 1 110 ? 30.788  8.836   39.745 1.00 61.98  ?  117 ARG   A CA  1 
ATOM   789  C  C   . ARG   A 1 110 ? 30.277  8.154   41.026 1.00 61.49  ?  117 ARG   A C   1 
ATOM   790  O  O   . ARG   A 1 110 ? 29.095  7.862   41.130 1.00 46.53  ?  117 ARG   A O   1 
ATOM   791  C  CB  . ARG   A 1 110 ? 31.451  7.817   38.805 1.00 66.11  ?  117 ARG   A CB  1 
ATOM   792  C  CG  . ARG   A 1 110 ? 30.484  6.873   38.081 1.00 67.24  ?  117 ARG   A CG  1 
ATOM   793  C  CD  . ARG   A 1 110 ? 31.239  5.777   37.320 1.00 68.80  ?  117 ARG   A CD  1 
ATOM   794  N  NE  . ARG   A 1 110 ? 32.052  4.931   38.201 1.00 69.44  ?  117 ARG   A NE  1 
ATOM   795  C  CZ  . ARG   A 1 110 ? 32.976  4.045   37.809 1.00 76.11  ?  117 ARG   A CZ  1 
ATOM   796  N  NH1 . ARG   A 1 110 ? 33.216  3.819   36.513 1.00 81.94  ?  117 ARG   A NH1 1 
ATOM   797  N  NH2 . ARG   A 1 110 ? 33.651  3.337   38.731 1.00 78.01  ?  117 ARG   A NH2 1 
ATOM   798  N  N   . ILE   A 1 111 ? 31.175  7.908   41.988 1.00 56.07  ?  118 ILE   A N   1 
ATOM   799  C  CA  . ILE   A 1 111 ? 30.792  7.453   43.348 1.00 49.47  ?  118 ILE   A CA  1 
ATOM   800  C  C   . ILE   A 1 111 ? 29.706  8.360   43.980 1.00 50.28  ?  118 ILE   A C   1 
ATOM   801  O  O   . ILE   A 1 111 ? 28.751  7.860   44.550 1.00 59.58  ?  118 ILE   A O   1 
ATOM   802  C  CB  . ILE   A 1 111 ? 32.043  7.290   44.273 1.00 43.65  ?  118 ILE   A CB  1 
ATOM   803  C  CG1 . ILE   A 1 111 ? 32.844  6.064   43.856 1.00 48.26  ?  118 ILE   A CG1 1 
ATOM   804  C  CG2 . ILE   A 1 111 ? 31.702  7.184   45.771 1.00 40.51  ?  118 ILE   A CG2 1 
ATOM   805  C  CD1 . ILE   A 1 111 ? 34.272  6.046   44.344 1.00 52.83  ?  118 ILE   A CD1 1 
ATOM   806  N  N   . ILE   A 1 112 ? 29.863  9.678   43.868 1.00 60.20  ?  119 ILE   A N   1 
ATOM   807  C  CA  . ILE   A 1 112 ? 28.915  10.661  44.428 1.00 51.46  ?  119 ILE   A CA  1 
ATOM   808  C  C   . ILE   A 1 112 ? 27.553  10.573  43.736 1.00 52.44  ?  119 ILE   A C   1 
ATOM   809  O  O   . ILE   A 1 112 ? 26.535  10.572  44.417 1.00 52.80  ?  119 ILE   A O   1 
ATOM   810  C  CB  . ILE   A 1 112 ? 29.481  12.113  44.398 1.00 55.23  ?  119 ILE   A CB  1 
ATOM   811  C  CG1 . ILE   A 1 112 ? 30.655  12.226  45.374 1.00 66.29  ?  119 ILE   A CG1 1 
ATOM   812  C  CG2 . ILE   A 1 112 ? 28.427  13.149  44.782 1.00 58.57  ?  119 ILE   A CG2 1 
ATOM   813  C  CD1 . ILE   A 1 112 ? 31.613  13.374  45.110 1.00 73.76  ?  119 ILE   A CD1 1 
ATOM   814  N  N   . LEU   A 1 113 ? 27.549  10.495  42.406 1.00 58.23  ?  120 LEU   A N   1 
ATOM   815  C  CA  . LEU   A 1 113 ? 26.316  10.338  41.625 1.00 58.81  ?  120 LEU   A CA  1 
ATOM   816  C  C   . LEU   A 1 113 ? 25.564  9.030   41.917 1.00 62.46  ?  120 LEU   A C   1 
ATOM   817  O  O   . LEU   A 1 113 ? 24.336  9.031   42.000 1.00 60.29  ?  120 LEU   A O   1 
ATOM   818  C  CB  . LEU   A 1 113 ? 26.590  10.468  40.123 1.00 61.09  ?  120 LEU   A CB  1 
ATOM   819  C  CG  . LEU   A 1 113 ? 25.361  10.541  39.194 1.00 63.29  ?  120 LEU   A CG  1 
ATOM   820  C  CD1 . LEU   A 1 113 ? 24.382  11.642  39.590 1.00 68.83  ?  120 LEU   A CD1 1 
ATOM   821  C  CD2 . LEU   A 1 113 ? 25.793  10.727  37.748 1.00 62.88  ?  120 LEU   A CD2 1 
ATOM   822  N  N   . GLU   A 1 114 ? 26.302  7.936   42.097 1.00 56.29  ?  121 GLU   A N   1 
ATOM   823  C  CA  . GLU   A 1 114 ? 25.702  6.670   42.463 1.00 56.24  ?  121 GLU   A CA  1 
ATOM   824  C  C   . GLU   A 1 114 ? 25.078  6.712   43.864 1.00 62.49  ?  121 GLU   A C   1 
ATOM   825  O  O   . GLU   A 1 114 ? 23.992  6.142   44.071 1.00 61.42  ?  121 GLU   A O   1 
ATOM   826  C  CB  . GLU   A 1 114 ? 26.722  5.539   42.331 1.00 64.54  ?  121 GLU   A CB  1 
ATOM   827  C  CG  . GLU   A 1 114 ? 27.051  5.222   40.875 1.00 61.78  ?  121 GLU   A CG  1 
ATOM   828  C  CD  . GLU   A 1 114 ? 28.107  4.157   40.688 1.00 68.47  ?  121 GLU   A CD  1 
ATOM   829  O  OE1 . GLU   A 1 114 ? 28.892  3.896   41.623 1.00 86.77  ?  121 GLU   A OE1 1 
ATOM   830  O  OE2 . GLU   A 1 114 ? 28.165  3.586   39.578 1.00 70.96  ?  121 GLU   A OE2 1 
ATOM   831  N  N   . ILE   A 1 115 ? 25.755  7.387   44.802 1.00 52.37  ?  122 ILE   A N   1 
ATOM   832  C  CA  . ILE   A 1 115 ? 25.213  7.662   46.148 1.00 52.90  ?  122 ILE   A CA  1 
ATOM   833  C  C   . ILE   A 1 115 ? 23.895  8.452   46.046 1.00 55.97  ?  122 ILE   A C   1 
ATOM   834  O  O   . ILE   A 1 115 ? 22.910  8.101   46.697 1.00 67.08  ?  122 ILE   A O   1 
ATOM   835  C  CB  . ILE   A 1 115 ? 26.239  8.378   47.084 1.00 50.99  ?  122 ILE   A CB  1 
ATOM   836  C  CG1 . ILE   A 1 115 ? 27.410  7.441   47.415 1.00 57.10  ?  122 ILE   A CG1 1 
ATOM   837  C  CG2 . ILE   A 1 115 ? 25.617  8.733   48.435 1.00 47.88  ?  122 ILE   A CG2 1 
ATOM   838  C  CD1 . ILE   A 1 115 ? 28.689  8.139   47.812 1.00 47.20  ?  122 ILE   A CD1 1 
ATOM   839  N  N   . ILE   A 1 116 ? 23.870  9.465   45.190 1.00 60.45  ?  123 ILE   A N   1 
ATOM   840  C  CA  . ILE   A 1 116 ? 22.664  10.275  44.957 1.00 58.97  ?  123 ILE   A CA  1 
ATOM   841  C  C   . ILE   A 1 116 ? 21.513  9.448   44.366 1.00 54.59  ?  123 ILE   A C   1 
ATOM   842  O  O   . ILE   A 1 116 ? 20.373  9.576   44.828 1.00 62.78  ?  123 ILE   A O   1 
ATOM   843  C  CB  . ILE   A 1 116 ? 22.981  11.503  44.066 1.00 61.29  ?  123 ILE   A CB  1 
ATOM   844  C  CG1 . ILE   A 1 116 ? 23.947  12.471  44.794 1.00 63.95  ?  123 ILE   A CG1 1 
ATOM   845  C  CG2 . ILE   A 1 116 ? 21.717  12.262  43.708 1.00 68.16  ?  123 ILE   A CG2 1 
ATOM   846  C  CD1 . ILE   A 1 116 ? 24.808  13.314  43.874 1.00 67.89  ?  123 ILE   A CD1 1 
ATOM   847  N  N   . GLU   A 1 117 ? 21.814  8.642   43.343 1.00 56.27  ?  124 GLU   A N   1 
ATOM   848  C  CA  . GLU   A 1 117 ? 20.838  7.720   42.710 1.00 61.31  ?  124 GLU   A CA  1 
ATOM   849  C  C   . GLU   A 1 117 ? 20.170  6.794   43.731 1.00 58.00  ?  124 GLU   A C   1 
ATOM   850  O  O   . GLU   A 1 117 ? 18.945  6.695   43.789 1.00 76.75  ?  124 GLU   A O   1 
ATOM   851  C  CB  . GLU   A 1 117 ? 21.520  6.847   41.641 1.00 67.87  ?  124 GLU   A CB  1 
ATOM   852  C  CG  . GLU   A 1 117 ? 21.829  7.541   40.329 1.00 74.17  ?  124 GLU   A CG  1 
ATOM   853  C  CD  . GLU   A 1 117 ? 22.732  6.723   39.397 1.00 77.71  ?  124 GLU   A CD  1 
ATOM   854  O  OE1 . GLU   A 1 117 ? 22.920  5.503   39.605 1.00 80.49  ?  124 GLU   A OE1 1 
ATOM   855  O  OE2 . GLU   A 1 117 ? 23.254  7.310   38.421 1.00 78.98  ?  124 GLU   A OE2 1 
ATOM   856  N  N   . GLY   A 1 118 ? 21.000  6.153   44.543 1.00 58.80  ?  125 GLY   A N   1 
ATOM   857  C  CA  . GLY   A 1 118 ? 20.552  5.235   45.571 1.00 57.96  ?  125 GLY   A CA  1 
ATOM   858  C  C   . GLY   A 1 118 ? 19.725  5.864   46.670 1.00 58.34  ?  125 GLY   A C   1 
ATOM   859  O  O   . GLY   A 1 118 ? 18.713  5.300   47.075 1.00 53.44  ?  125 GLY   A O   1 
ATOM   860  N  N   . MET   A 1 119 ? 20.155  7.021   47.161 1.00 55.42  ?  126 MET   A N   1 
ATOM   861  C  CA  . MET   A 1 119 ? 19.388  7.747   48.192 1.00 54.88  ?  126 MET   A CA  1 
ATOM   862  C  C   . MET   A 1 119 ? 18.043  8.288   47.646 1.00 55.19  ?  126 MET   A C   1 
ATOM   863  O  O   . MET   A 1 119 ? 17.042  8.292   48.373 1.00 57.46  ?  126 MET   A O   1 
ATOM   864  C  CB  . MET   A 1 119 ? 20.230  8.874   48.802 1.00 60.25  ?  126 MET   A CB  1 
ATOM   865  C  CG  . MET   A 1 119 ? 21.447  8.389   49.608 1.00 54.74  ?  126 MET   A CG  1 
ATOM   866  S  SD  . MET   A 1 119 ? 21.083  7.231   50.945 1.00 58.74  ?  126 MET   A SD  1 
ATOM   867  C  CE  . MET   A 1 119 ? 20.116  8.315   51.984 1.00 62.16  ?  126 MET   A CE  1 
ATOM   868  N  N   . ALA   A 1 120 ? 18.027  8.704   46.379 1.00 50.70  ?  127 ALA   A N   1 
ATOM   869  C  CA  . ALA   A 1 120 ? 16.782  9.065   45.682 1.00 56.64  ?  127 ALA   A CA  1 
ATOM   870  C  C   . ALA   A 1 120 ? 15.817  7.873   45.508 1.00 59.19  ?  127 ALA   A C   1 
ATOM   871  O  O   . ALA   A 1 120 ? 14.590  8.038   45.637 1.00 52.08  ?  127 ALA   A O   1 
ATOM   872  C  CB  . ALA   A 1 120 ? 17.085  9.696   44.339 1.00 54.47  ?  127 ALA   A CB  1 
ATOM   873  N  N   . TYR   A 1 121 ? 16.370  6.691   45.224 1.00 61.66  ?  128 TYR   A N   1 
ATOM   874  C  CA  . TYR   A 1 121 ? 15.584  5.460   45.173 1.00 60.52  ?  128 TYR   A CA  1 
ATOM   875  C  C   . TYR   A 1 121 ? 14.884  5.190   46.511 1.00 64.09  ?  128 TYR   A C   1 
ATOM   876  O  O   . TYR   A 1 121 ? 13.658  5.023   46.548 1.00 68.82  ?  128 TYR   A O   1 
ATOM   877  C  CB  . TYR   A 1 121 ? 16.416  4.229   44.757 1.00 61.61  ?  128 TYR   A CB  1 
ATOM   878  C  CG  . TYR   A 1 121 ? 15.587  2.960   44.851 1.00 58.57  ?  128 TYR   A CG  1 
ATOM   879  C  CD1 . TYR   A 1 121 ? 14.591  2.688   43.911 1.00 60.58  ?  128 TYR   A CD1 1 
ATOM   880  C  CD2 . TYR   A 1 121 ? 15.710  2.097   45.954 1.00 57.98  ?  128 TYR   A CD2 1 
ATOM   881  C  CE1 . TYR   A 1 121 ? 13.790  1.552   44.020 1.00 67.38  ?  128 TYR   A CE1 1 
ATOM   882  C  CE2 . TYR   A 1 121 ? 14.909  0.961   46.074 1.00 57.38  ?  128 TYR   A CE2 1 
ATOM   883  C  CZ  . TYR   A 1 121 ? 13.955  0.690   45.103 1.00 61.32  ?  128 TYR   A CZ  1 
ATOM   884  O  OH  . TYR   A 1 121 ? 13.153  -0.418  45.196 1.00 67.60  ?  128 TYR   A OH  1 
ATOM   885  N  N   . LEU   A 1 122 ? 15.683  5.154   47.573 1.00 55.44  ?  129 LEU   A N   1 
ATOM   886  C  CA  . LEU   A 1 122 ? 15.212  4.902   48.935 1.00 56.21  ?  129 LEU   A CA  1 
ATOM   887  C  C   . LEU   A 1 122 ? 14.165  5.895   49.461 1.00 55.64  ?  129 LEU   A C   1 
ATOM   888  O  O   . LEU   A 1 122 ? 13.165  5.498   50.079 1.00 73.91  ?  129 LEU   A O   1 
ATOM   889  C  CB  . LEU   A 1 122 ? 16.408  4.839   49.900 1.00 53.37  ?  129 LEU   A CB  1 
ATOM   890  C  CG  . LEU   A 1 122 ? 17.365  3.646   49.773 1.00 56.32  ?  129 LEU   A CG  1 
ATOM   891  C  CD1 . LEU   A 1 122 ? 18.506  3.826   50.760 1.00 54.58  ?  129 LEU   A CD1 1 
ATOM   892  C  CD2 . LEU   A 1 122 ? 16.683  2.302   50.046 1.00 65.09  ?  129 LEU   A CD2 1 
ATOM   893  N  N   . HIS   A 1 123 ? 14.401  7.177   49.227 1.00 62.16  ?  130 HIS   A N   1 
ATOM   894  C  CA  . HIS   A 1 123 ? 13.427  8.242   49.563 1.00 57.17  ?  130 HIS   A CA  1 
ATOM   895  C  C   . HIS   A 1 123 ? 12.136  8.152   48.740 1.00 60.74  ?  130 HIS   A C   1 
ATOM   896  O  O   . HIS   A 1 123 ? 11.054  8.453   49.254 1.00 58.87  ?  130 HIS   A O   1 
ATOM   897  C  CB  . HIS   A 1 123 ? 14.077  9.633   49.424 1.00 52.58  ?  130 HIS   A CB  1 
ATOM   898  C  CG  . HIS   A 1 123 ? 15.071  9.932   50.502 1.00 58.24  ?  130 HIS   A CG  1 
ATOM   899  N  ND1 . HIS   A 1 123 ? 15.525  11.203  50.764 1.00 58.86  ?  130 HIS   A ND1 1 
ATOM   900  C  CD2 . HIS   A 1 123 ? 15.678  9.121   51.406 1.00 61.08  ?  130 HIS   A CD2 1 
ATOM   901  C  CE1 . HIS   A 1 123 ? 16.383  11.160  51.767 1.00 61.35  ?  130 HIS   A CE1 1 
ATOM   902  N  NE2 . HIS   A 1 123 ? 16.496  9.909   52.174 1.00 57.28  ?  130 HIS   A NE2 1 
ATOM   903  N  N   . GLY   A 1 124 ? 12.261  7.736   47.477 1.00 65.93  ?  131 GLY   A N   1 
ATOM   904  C  CA  . GLY   A 1 124 ? 11.116  7.384   46.620 1.00 65.60  ?  131 GLY   A CA  1 
ATOM   905  C  C   . GLY   A 1 124 ? 10.218  6.254   47.120 1.00 67.77  ?  131 GLY   A C   1 
ATOM   906  O  O   . GLY   A 1 124 ? 9.011   6.255   46.838 1.00 65.84  ?  131 GLY   A O   1 
ATOM   907  N  N   . LYS   A 1 125 ? 10.810  5.296   47.850 1.00 64.91  ?  132 LYS   A N   1 
ATOM   908  C  CA  . LYS   A 1 125 ? 10.077  4.212   48.533 1.00 70.51  ?  132 LYS   A CA  1 
ATOM   909  C  C   . LYS   A 1 125 ? 9.728   4.530   50.010 1.00 70.45  ?  132 LYS   A C   1 
ATOM   910  O  O   . LYS   A 1 125 ? 9.430   3.615   50.776 1.00 72.16  ?  132 LYS   A O   1 
ATOM   911  C  CB  . LYS   A 1 125 ? 10.891  2.896   48.465 1.00 67.70  ?  132 LYS   A CB  1 
ATOM   912  C  CG  . LYS   A 1 125 ? 11.368  2.445   47.086 1.00 65.69  ?  132 LYS   A CG  1 
ATOM   913  C  CD  . LYS   A 1 125 ? 10.272  2.030   46.106 1.00 71.38  ?  132 LYS   A CD  1 
ATOM   914  C  CE  . LYS   A 1 125 ? 9.645   0.654   46.354 1.00 78.87  ?  132 LYS   A CE  1 
ATOM   915  N  NZ  . LYS   A 1 125 ? 8.304   0.502   45.859 0.00 77.49  ?  132 LYS   A NZ  1 
ATOM   916  N  N   . GLY   A 1 126 ? 9.771   5.807   50.416 1.00 70.72  ?  133 GLY   A N   1 
ATOM   917  C  CA  . GLY   A 1 126 ? 9.477   6.214   51.796 1.00 64.34  ?  133 GLY   A CA  1 
ATOM   918  C  C   . GLY   A 1 126 ? 10.464  5.843   52.900 1.00 66.37  ?  133 GLY   A C   1 
ATOM   919  O  O   . GLY   A 1 126 ? 10.128  6.000   54.082 1.00 75.34  ?  133 GLY   A O   1 
ATOM   920  N  N   . VAL   A 1 127 ? 11.663  5.381   52.532 1.00 54.43  ?  134 VAL   A N   1 
ATOM   921  C  CA  . VAL   A 1 127 ? 12.678  4.955   53.495 1.00 58.63  ?  134 VAL   A CA  1 
ATOM   922  C  C   . VAL   A 1 127 ? 13.619  6.124   53.810 1.00 54.83  ?  134 VAL   A C   1 
ATOM   923  O  O   . VAL   A 1 127 ? 14.259  6.652   52.907 1.00 48.67  ?  134 VAL   A O   1 
ATOM   924  C  CB  . VAL   A 1 127 ? 13.489  3.756   52.934 1.00 59.31  ?  134 VAL   A CB  1 
ATOM   925  C  CG1 . VAL   A 1 127 ? 14.699  3.397   53.796 1.00 61.82  ?  134 VAL   A CG1 1 
ATOM   926  C  CG2 . VAL   A 1 127 ? 12.568  2.549   52.785 1.00 59.40  ?  134 VAL   A CG2 1 
ATOM   927  N  N   . ILE   A 1 128 ? 13.741  6.465   55.090 1.00 58.59  ?  135 ILE   A N   1 
ATOM   928  C  CA  . ILE   A 1 128 ? 14.833  7.312   55.588 1.00 57.81  ?  135 ILE   A CA  1 
ATOM   929  C  C   . ILE   A 1 128 ? 15.915  6.350   56.064 1.00 56.09  ?  135 ILE   A C   1 
ATOM   930  O  O   . ILE   A 1 128 ? 15.609  5.428   56.822 1.00 56.98  ?  135 ILE   A O   1 
ATOM   931  C  CB  . ILE   A 1 128 ? 14.402  8.234   56.762 1.00 60.27  ?  135 ILE   A CB  1 
ATOM   932  C  CG1 . ILE   A 1 128 ? 13.062  8.955   56.494 1.00 57.08  ?  135 ILE   A CG1 1 
ATOM   933  C  CG2 . ILE   A 1 128 ? 15.507  9.253   57.059 1.00 61.70  ?  135 ILE   A CG2 1 
ATOM   934  C  CD1 . ILE   A 1 128 ? 13.003  9.728   55.197 1.00 59.63  ?  135 ILE   A CD1 1 
ATOM   935  N  N   . HIS   A 1 129 ? 17.157  6.540   55.621 1.00 53.61  ?  136 HIS   A N   1 
ATOM   936  C  CA  . HIS   A 1 129 ? 18.279  5.662   56.041 1.00 51.85  ?  136 HIS   A CA  1 
ATOM   937  C  C   . HIS   A 1 129 ? 18.541  5.787   57.526 1.00 52.98  ?  136 HIS   A C   1 
ATOM   938  O  O   . HIS   A 1 129 ? 18.648  4.773   58.218 1.00 59.12  ?  136 HIS   A O   1 
ATOM   939  C  CB  . HIS   A 1 129 ? 19.571  5.996   55.282 1.00 52.34  ?  136 HIS   A CB  1 
ATOM   940  C  CG  . HIS   A 1 129 ? 20.584  4.896   55.275 1.00 55.44  ?  136 HIS   A CG  1 
ATOM   941  N  ND1 . HIS   A 1 129 ? 21.141  4.345   56.415 1.00 60.05  ?  136 HIS   A ND1 1 
ATOM   942  C  CD2 . HIS   A 1 129 ? 21.152  4.249   54.239 1.00 58.71  ?  136 HIS   A CD2 1 
ATOM   943  C  CE1 . HIS   A 1 129 ? 22.012  3.416   56.078 1.00 51.86  ?  136 HIS   A CE1 1 
ATOM   944  N  NE2 . HIS   A 1 129 ? 22.036  3.339   54.763 1.00 61.56  ?  136 HIS   A NE2 1 
ATOM   945  N  N   . LYS   A 1 130 ? 18.701  7.034   57.971 1.00 46.65  ?  137 LYS   A N   1 
ATOM   946  C  CA  . LYS   A 1 130 ? 18.983  7.418   59.358 1.00 50.48  ?  137 LYS   A CA  1 
ATOM   947  C  C   . LYS   A 1 130 ? 20.423  7.168   59.860 1.00 52.73  ?  137 LYS   A C   1 
ATOM   948  O  O   . LYS   A 1 130 ? 20.744  7.595   60.956 1.00 63.78  ?  137 LYS   A O   1 
ATOM   949  C  CB  . LYS   A 1 130 ? 17.959  6.837   60.342 1.00 56.81  ?  137 LYS   A CB  1 
ATOM   950  C  CG  . LYS   A 1 130 ? 16.496  7.105   59.987 1.00 57.64  ?  137 LYS   A CG  1 
ATOM   951  C  CD  . LYS   A 1 130 ? 15.575  6.135   60.717 1.00 61.70  ?  137 LYS   A CD  1 
ATOM   952  C  CE  . LYS   A 1 130 ? 15.422  4.814   59.967 1.00 65.53  ?  137 LYS   A CE  1 
ATOM   953  N  NZ  . LYS   A 1 130 ? 14.250  4.815   59.037 1.00 66.36  ?  137 LYS   A NZ  1 
ATOM   954  N  N   . ASP   A 1 131 ? 21.287  6.574   59.036 1.00 56.20  ?  138 ASP   A N   1 
ATOM   955  C  CA  . ASP   A 1 131 ? 22.682  6.236   59.401 1.00 54.32  ?  138 ASP   A CA  1 
ATOM   956  C  C   . ASP   A 1 131 ? 23.598  6.117   58.158 1.00 59.80  ?  138 ASP   A C   1 
ATOM   957  O  O   . ASP   A 1 131 ? 24.424  5.189   58.035 1.00 47.42  ?  138 ASP   A O   1 
ATOM   958  C  CB  . ASP   A 1 131 ? 22.743  4.990   60.287 1.00 55.64  ?  138 ASP   A CB  1 
ATOM   959  C  CG  . ASP   A 1 131 ? 24.072  4.847   61.061 1.00 71.37  ?  138 ASP   A CG  1 
ATOM   960  O  OD1 . ASP   A 1 131 ? 24.865  5.821   61.161 1.00 73.16  ?  138 ASP   A OD1 1 
ATOM   961  O  OD2 . ASP   A 1 131 ? 24.343  3.719   61.541 1.00 75.26  ?  138 ASP   A OD2 1 
ATOM   962  N  N   . LEU   A 1 132 ? 23.485  7.100   57.257 1.00 51.91  ?  139 LEU   A N   1 
ATOM   963  C  CA  . LEU   A 1 132 ? 24.330  7.135   56.067 1.00 57.93  ?  139 LEU   A CA  1 
ATOM   964  C  C   . LEU   A 1 132 ? 25.736  7.564   56.520 1.00 54.34  ?  139 LEU   A C   1 
ATOM   965  O  O   . LEU   A 1 132 ? 25.893  8.526   57.278 1.00 60.30  ?  139 LEU   A O   1 
ATOM   966  C  CB  . LEU   A 1 132 ? 23.738  8.052   54.993 1.00 59.79  ?  139 LEU   A CB  1 
ATOM   967  C  CG  . LEU   A 1 132 ? 24.501  8.278   53.681 1.00 62.08  ?  139 LEU   A CG  1 
ATOM   968  C  CD1 . LEU   A 1 132 ? 24.594  6.994   52.881 1.00 60.68  ?  139 LEU   A CD1 1 
ATOM   969  C  CD2 . LEU   A 1 132 ? 23.802  9.346   52.854 1.00 65.65  ?  139 LEU   A CD2 1 
ATOM   970  N  N   . LYS   A 1 133 ? 26.732  6.794   56.107 1.00 52.43  ?  140 LYS   A N   1 
ATOM   971  C  CA  . LYS   A 1 133 ? 28.139  6.992   56.482 1.00 51.33  ?  140 LYS   A CA  1 
ATOM   972  C  C   . LYS   A 1 133 ? 29.030  6.081   55.590 1.00 59.96  ?  140 LYS   A C   1 
ATOM   973  O  O   . LYS   A 1 133 ? 28.514  5.083   55.046 1.00 52.14  ?  140 LYS   A O   1 
ATOM   974  C  CB  . LYS   A 1 133 ? 28.354  6.639   57.962 1.00 61.66  ?  140 LYS   A CB  1 
ATOM   975  C  CG  . LYS   A 1 133 ? 28.068  5.181   58.335 1.00 64.76  ?  140 LYS   A CG  1 
ATOM   976  C  CD  . LYS   A 1 133 ? 27.954  4.983   59.832 1.00 66.79  ?  140 LYS   A CD  1 
ATOM   977  C  CE  . LYS   A 1 133 ? 27.436  3.596   60.150 1.00 70.55  ?  140 LYS   A CE  1 
ATOM   978  N  NZ  . LYS   A 1 133 ? 27.250  3.379   61.608 1.00 73.34  ?  140 LYS   A NZ  1 
ATOM   979  N  N   . PRO   A 1 134 ? 30.341  6.391   55.448 1.00 55.05  ?  141 PRO   A N   1 
ATOM   980  C  CA  . PRO   A 1 134 ? 31.225  5.574   54.591 1.00 54.35  ?  141 PRO   A CA  1 
ATOM   981  C  C   . PRO   A 1 134 ? 31.173  4.059   54.836 1.00 50.49  ?  141 PRO   A C   1 
ATOM   982  O  O   . PRO   A 1 134 ? 31.159  3.309   53.861 1.00 50.09  ?  141 PRO   A O   1 
ATOM   983  C  CB  . PRO   A 1 134 ? 32.634  6.144   54.872 1.00 51.91  ?  141 PRO   A CB  1 
ATOM   984  C  CG  . PRO   A 1 134 ? 32.381  7.565   55.225 1.00 54.76  ?  141 PRO   A CG  1 
ATOM   985  C  CD  . PRO   A 1 134 ? 31.066  7.556   55.995 1.00 59.67  ?  141 PRO   A CD  1 
ATOM   986  N  N   . GLU   A 1 135 ? 31.097  3.630   56.100 1.00 59.80  ?  142 GLU   A N   1 
ATOM   987  C  CA  . GLU   A 1 135 ? 30.891  2.185   56.473 1.00 63.13  ?  142 GLU   A CA  1 
ATOM   988  C  C   . GLU   A 1 135 ? 29.678  1.479   55.823 1.00 60.04  ?  142 GLU   A C   1 
ATOM   989  O  O   . GLU   A 1 135 ? 29.676  0.236   55.655 1.00 61.88  ?  142 GLU   A O   1 
ATOM   990  C  CB  . GLU   A 1 135 ? 30.766  2.031   58.004 1.00 69.15  ?  142 GLU   A CB  1 
ATOM   991  C  CG  . GLU   A 1 135 ? 32.069  1.847   58.758 1.00 77.46  ?  142 GLU   A CG  1 
ATOM   992  C  CD  . GLU   A 1 135 ? 31.870  1.949   60.274 1.00 94.08  ?  142 GLU   A CD  1 
ATOM   993  O  OE1 . GLU   A 1 135 ? 32.020  0.920   60.983 1.00 95.62  ?  142 GLU   A OE1 1 
ATOM   994  O  OE2 . GLU   A 1 135 ? 31.527  3.059   60.757 1.00 93.78  ?  142 GLU   A OE2 1 
ATOM   995  N  N   . ASN   A 1 136 ? 28.642  2.258   55.521 1.00 48.41  ?  143 ASN   A N   1 
ATOM   996  C  CA  . ASN   A 1 136 ? 27.423  1.788   54.837 1.00 50.01  ?  143 ASN   A CA  1 
ATOM   997  C  C   . ASN   A 1 136 ? 27.407  1.962   53.319 1.00 50.18  ?  143 ASN   A C   1 
ATOM   998  O  O   . ASN   A 1 136 ? 26.336  1.807   52.688 1.00 47.10  ?  143 ASN   A O   1 
ATOM   999  C  CB  . ASN   A 1 136 ? 26.176  2.476   55.486 1.00 45.08  ?  143 ASN   A CB  1 
ATOM   1000 C  CG  . ASN   A 1 136 ? 25.642  1.706   56.670 1.00 48.71  ?  143 ASN   A CG  1 
ATOM   1001 O  OD1 . ASN   A 1 136 ? 25.675  0.457   56.693 1.00 56.87  ?  143 ASN   A OD1 1 
ATOM   1002 N  ND2 . ASN   A 1 136 ? 25.143  2.423   57.664 1.00 44.83  ?  143 ASN   A ND2 1 
ATOM   1003 N  N   . ILE   A 1 137 ? 28.551  2.298   52.722 1.00 46.13  ?  144 ILE   A N   1 
ATOM   1004 C  CA  . ILE   A 1 137 ? 28.644  2.492   51.282 1.00 49.39  ?  144 ILE   A CA  1 
ATOM   1005 C  C   . ILE   A 1 137 ? 29.663  1.452   50.863 1.00 51.78  ?  144 ILE   A C   1 
ATOM   1006 O  O   . ILE   A 1 137 ? 30.842  1.599   51.163 1.00 55.07  ?  144 ILE   A O   1 
ATOM   1007 C  CB  . ILE   A 1 137 ? 29.039  3.942   50.920 1.00 59.12  ?  144 ILE   A CB  1 
ATOM   1008 C  CG1 . ILE   A 1 137 ? 27.906  4.904   51.319 1.00 64.12  ?  144 ILE   A CG1 1 
ATOM   1009 C  CG2 . ILE   A 1 137 ? 29.308  4.067   49.425 1.00 65.76  ?  144 ILE   A CG2 1 
ATOM   1010 C  CD1 . ILE   A 1 137 ? 28.250  6.396   51.285 1.00 61.85  ?  144 ILE   A CD1 1 
ATOM   1011 N  N   . LEU   A 1 138 ? 29.189  0.391   50.201 1.00 47.12  ?  145 LEU   A N   1 
ATOM   1012 C  CA  . LEU   A 1 138 ? 30.028  -0.718  49.786 1.00 51.33  ?  145 LEU   A CA  1 
ATOM   1013 C  C   . LEU   A 1 138 ? 30.413  -0.512  48.338 1.00 50.19  ?  145 LEU   A C   1 
ATOM   1014 O  O   . LEU   A 1 138 ? 29.643  0.042   47.587 1.00 47.23  ?  145 LEU   A O   1 
ATOM   1015 C  CB  . LEU   A 1 138 ? 29.261  -2.055  49.980 1.00 49.03  ?  145 LEU   A CB  1 
ATOM   1016 C  CG  . LEU   A 1 138 ? 28.570  -2.256  51.332 1.00 46.19  ?  145 LEU   A CG  1 
ATOM   1017 C  CD1 . LEU   A 1 138 ? 27.930  -3.644  51.433 1.00 56.97  ?  145 LEU   A CD1 1 
ATOM   1018 C  CD2 . LEU   A 1 138 ? 29.566  -2.079  52.455 1.00 46.30  ?  145 LEU   A CD2 1 
ATOM   1019 N  N   . VAL   A 1 139 ? 31.575  -1.039  47.963 1.00 58.84  ?  146 VAL   A N   1 
ATOM   1020 C  CA  . VAL   A 1 139 ? 32.252  -0.778  46.690 1.00 61.05  ?  146 VAL   A CA  1 
ATOM   1021 C  C   . VAL   A 1 139 ? 32.613  -2.124  46.061 1.00 59.76  ?  146 VAL   A C   1 
ATOM   1022 O  O   . VAL   A 1 139 ? 33.176  -2.972  46.746 1.00 66.15  ?  146 VAL   A O   1 
ATOM   1023 C  CB  . VAL   A 1 139 ? 33.554  0.040   46.946 1.00 58.30  ?  146 VAL   A CB  1 
ATOM   1024 C  CG1 . VAL   A 1 139 ? 34.282  0.394   45.652 1.00 54.66  ?  146 VAL   A CG1 1 
ATOM   1025 C  CG2 . VAL   A 1 139 ? 33.239  1.314   47.727 1.00 52.12  ?  146 VAL   A CG2 1 
ATOM   1026 N  N   . ASP   A 1 140 ? 32.265  -2.313  44.784 1.00 64.69  ?  147 ASP   A N   1 
ATOM   1027 C  CA  . ASP   A 1 140 ? 32.685  -3.507  43.993 1.00 62.77  ?  147 ASP   A CA  1 
ATOM   1028 C  C   . ASP   A 1 140 ? 34.047  -3.263  43.313 1.00 66.92  ?  147 ASP   A C   1 
ATOM   1029 O  O   . ASP   A 1 140 ? 34.578  -2.163  43.387 1.00 64.40  ?  147 ASP   A O   1 
ATOM   1030 C  CB  . ASP   A 1 140 ? 31.585  -4.001  43.014 1.00 63.49  ?  147 ASP   A CB  1 
ATOM   1031 C  CG  . ASP   A 1 140 ? 31.258  -3.023  41.867 1.00 70.60  ?  147 ASP   A CG  1 
ATOM   1032 O  OD1 . ASP   A 1 140 ? 32.172  -2.373  41.299 1.00 72.15  ?  147 ASP   A OD1 1 
ATOM   1033 O  OD2 . ASP   A 1 140 ? 30.045  -2.934  41.535 1.00 67.41  ?  147 ASP   A OD2 1 
ATOM   1034 N  N   . ASN   A 1 141 ? 34.588  -4.296  42.660 1.00 72.66  ?  148 ASN   A N   1 
ATOM   1035 C  CA  . ASN   A 1 141 ? 35.922  -4.276  41.997 1.00 74.98  ?  148 ASN   A CA  1 
ATOM   1036 C  C   . ASN   A 1 141 ? 36.072  -3.247  40.846 1.00 77.69  ?  148 ASN   A C   1 
ATOM   1037 O  O   . ASN   A 1 141 ? 37.195  -2.861  40.541 1.00 81.43  ?  148 ASN   A O   1 
ATOM   1038 C  CB  . ASN   A 1 141 ? 36.278  -5.707  41.485 1.00 70.77  ?  148 ASN   A CB  1 
ATOM   1039 C  CG  . ASN   A 1 141 ? 37.783  -5.982  41.403 1.00 76.67  ?  148 ASN   A CG  1 
ATOM   1040 O  OD1 . ASN   A 1 141 ? 38.291  -6.381  40.347 1.00 73.95  ?  148 ASN   A OD1 1 
ATOM   1041 N  ND2 . ASN   A 1 141 ? 38.492  -5.836  42.530 1.00 73.54  ?  148 ASN   A ND2 1 
ATOM   1042 N  N   . ASP   A 1 142 ? 34.959  -2.857  40.209 1.00 74.73  ?  149 ASP   A N   1 
ATOM   1043 C  CA  . ASP   A 1 142 ? 34.905  -1.751  39.223 1.00 78.42  ?  149 ASP   A CA  1 
ATOM   1044 C  C   . ASP   A 1 142 ? 34.662  -0.334  39.830 1.00 74.26  ?  149 ASP   A C   1 
ATOM   1045 O  O   . ASP   A 1 142 ? 34.367  0.624   39.089 1.00 73.45  ?  149 ASP   A O   1 
ATOM   1046 C  CB  . ASP   A 1 142 ? 33.788  -2.038  38.197 1.00 85.67  ?  149 ASP   A CB  1 
ATOM   1047 C  CG  . ASP   A 1 142 ? 34.062  -3.247  37.324 1.00 86.88  ?  149 ASP   A CG  1 
ATOM   1048 O  OD1 . ASP   A 1 142 ? 35.160  -3.334  36.740 1.00 90.91  ?  149 ASP   A OD1 1 
ATOM   1049 O  OD2 . ASP   A 1 142 ? 33.143  -4.089  37.183 1.00 92.97  ?  149 ASP   A OD2 1 
ATOM   1050 N  N   . PHE   A 1 143 ? 34.745  -0.208  41.161 1.00 71.01  ?  150 PHE   A N   1 
ATOM   1051 C  CA  . PHE   A 1 143 ? 34.486  1.040   41.909 1.00 68.83  ?  150 PHE   A CA  1 
ATOM   1052 C  C   . PHE   A 1 143 ? 33.034  1.547   41.885 1.00 64.75  ?  150 PHE   A C   1 
ATOM   1053 O  O   . PHE   A 1 143 ? 32.775  2.662   42.334 1.00 59.20  ?  150 PHE   A O   1 
ATOM   1054 C  CB  . PHE   A 1 143 ? 35.489  2.167   41.556 1.00 67.70  ?  150 PHE   A CB  1 
ATOM   1055 C  CG  . PHE   A 1 143 ? 36.907  1.820   41.883 1.00 75.65  ?  150 PHE   A CG  1 
ATOM   1056 C  CD1 . PHE   A 1 143 ? 37.431  2.089   43.151 1.00 75.14  ?  150 PHE   A CD1 1 
ATOM   1057 C  CD2 . PHE   A 1 143 ? 37.727  1.190   40.931 1.00 76.88  ?  150 PHE   A CD2 1 
ATOM   1058 C  CE1 . PHE   A 1 143 ? 38.752  1.754   43.458 1.00 71.32  ?  150 PHE   A CE1 1 
ATOM   1059 C  CE2 . PHE   A 1 143 ? 39.042  0.849   41.237 1.00 77.17  ?  150 PHE   A CE2 1 
ATOM   1060 C  CZ  . PHE   A 1 143 ? 39.555  1.135   42.503 1.00 79.79  ?  150 PHE   A CZ  1 
ATOM   1061 N  N   . HIS   A 1 144 ? 32.085  0.714   41.447 1.00 62.68  ?  151 HIS   A N   1 
ATOM   1062 C  CA  . HIS   A 1 144 ? 30.667  1.052   41.532 1.00 59.29  ?  151 HIS   A CA  1 
ATOM   1063 C  C   . HIS   A 1 144 ? 30.209  0.733   42.958 1.00 62.00  ?  151 HIS   A C   1 
ATOM   1064 O  O   . HIS   A 1 144 ? 30.737  -0.193  43.589 1.00 65.03  ?  151 HIS   A O   1 
ATOM   1065 C  CB  . HIS   A 1 144 ? 29.841  0.310   40.482 1.00 59.92  ?  151 HIS   A CB  1 
ATOM   1066 C  CG  . HIS   A 1 144 ? 30.260  0.600   39.072 1.00 61.38  ?  151 HIS   A CG  1 
ATOM   1067 N  ND1 . HIS   A 1 144 ? 30.050  1.816   38.461 1.00 63.02  ?  151 HIS   A ND1 1 
ATOM   1068 C  CD2 . HIS   A 1 144 ? 30.917  -0.162  38.171 1.00 67.73  ?  151 HIS   A CD2 1 
ATOM   1069 C  CE1 . HIS   A 1 144 ? 30.532  1.779   37.232 1.00 65.85  ?  151 HIS   A CE1 1 
ATOM   1070 N  NE2 . HIS   A 1 144 ? 31.072  0.591   37.035 1.00 74.29  ?  151 HIS   A NE2 1 
ATOM   1071 N  N   . ILE   A 1 145 ? 29.222  1.485   43.453 1.00 58.84  ?  152 ILE   A N   1 
ATOM   1072 C  CA  . ILE   A 1 145 ? 28.839  1.448   44.875 1.00 58.71  ?  152 ILE   A CA  1 
ATOM   1073 C  C   . ILE   A 1 145 ? 27.392  1.030   45.128 1.00 54.75  ?  152 ILE   A C   1 
ATOM   1074 O  O   . ILE   A 1 145 ? 26.542  1.144   44.244 1.00 54.34  ?  152 ILE   A O   1 
ATOM   1075 C  CB  . ILE   A 1 145 ? 29.125  2.797   45.597 1.00 55.39  ?  152 ILE   A CB  1 
ATOM   1076 C  CG1 . ILE   A 1 145 ? 28.212  3.950   45.106 1.00 57.38  ?  152 ILE   A CG1 1 
ATOM   1077 C  CG2 . ILE   A 1 145 ? 30.582  3.171   45.425 1.00 55.90  ?  152 ILE   A CG2 1 
ATOM   1078 C  CD1 . ILE   A 1 145 ? 26.992  4.215   45.962 1.00 52.53  ?  152 ILE   A CD1 1 
ATOM   1079 N  N   . LYS   A 1 146 ? 27.130  0.570   46.352 1.00 51.25  ?  153 LYS   A N   1 
ATOM   1080 C  CA  . LYS   A 1 146 ? 25.763  0.307   46.833 1.00 56.06  ?  153 LYS   A CA  1 
ATOM   1081 C  C   . LYS   A 1 146 ? 25.608  0.740   48.285 1.00 56.39  ?  153 LYS   A C   1 
ATOM   1082 O  O   . LYS   A 1 146 ? 26.474  0.422   49.111 1.00 62.80  ?  153 LYS   A O   1 
ATOM   1083 C  CB  . LYS   A 1 146 ? 25.408  -1.172  46.727 1.00 53.41  ?  153 LYS   A CB  1 
ATOM   1084 C  CG  . LYS   A 1 146 ? 25.343  -1.713  45.317 1.00 56.60  ?  153 LYS   A CG  1 
ATOM   1085 C  CD  . LYS   A 1 146 ? 24.911  -3.187  45.312 1.00 54.25  ?  153 LYS   A CD  1 
ATOM   1086 C  CE  . LYS   A 1 146 ? 25.433  -3.956  44.107 1.00 52.04  ?  153 LYS   A CE  1 
ATOM   1087 N  NZ  . LYS   A 1 146 ? 24.734  -3.617  42.847 1.00 51.04  ?  153 LYS   A NZ  1 
ATOM   1088 N  N   . ILE   A 1 147 ? 24.496  1.427   48.593 1.00 44.59  ?  154 ILE   A N   1 
ATOM   1089 C  CA  . ILE   A 1 147 ? 24.168  1.785   49.978 1.00 45.28  ?  154 ILE   A CA  1 
ATOM   1090 C  C   . ILE   A 1 147 ? 23.622  0.537   50.716 1.00 49.94  ?  154 ILE   A C   1 
ATOM   1091 O  O   . ILE   A 1 147 ? 22.787  -0.205  50.175 1.00 47.92  ?  154 ILE   A O   1 
ATOM   1092 C  CB  . ILE   A 1 147 ? 23.165  2.934   50.022 1.00 45.50  ?  154 ILE   A CB  1 
ATOM   1093 C  CG1 . ILE   A 1 147 ? 23.780  4.205   49.401 1.00 44.41  ?  154 ILE   A CG1 1 
ATOM   1094 C  CG2 . ILE   A 1 147 ? 22.719  3.237   51.441 1.00 45.07  ?  154 ILE   A CG2 1 
ATOM   1095 C  CD1 . ILE   A 1 147 ? 22.800  4.888   48.509 1.00 51.05  ?  154 ILE   A CD1 1 
ATOM   1096 N  N   . ALA   A 1 148 ? 24.127  0.362   51.941 1.00 55.96  ?  155 ALA   A N   1 
ATOM   1097 C  CA  . ALA   A 1 148 ? 23.825  -0.722  52.842 1.00 56.01  ?  155 ALA   A CA  1 
ATOM   1098 C  C   . ALA   A 1 148 ? 23.271  -0.148  54.124 1.00 59.15  ?  155 ALA   A C   1 
ATOM   1099 O  O   . ALA   A 1 148 ? 23.393  1.040   54.383 1.00 63.81  ?  155 ALA   A O   1 
ATOM   1100 C  CB  . ALA   A 1 148 ? 25.089  -1.514  53.144 1.00 60.10  ?  155 ALA   A CB  1 
ATOM   1101 N  N   . ASP   A 1 149 ? 22.637  -1.012  54.915 1.00 60.33  ?  156 ASP   A N   1 
ATOM   1102 C  CA  . ASP   A 1 149 ? 22.151  -0.673  56.257 1.00 60.69  ?  156 ASP   A CA  1 
ATOM   1103 C  C   . ASP   A 1 149 ? 22.624  -1.778  57.161 1.00 62.25  ?  156 ASP   A C   1 
ATOM   1104 O  O   . ASP   A 1 149 ? 21.823  -2.586  57.654 1.00 64.92  ?  156 ASP   A O   1 
ATOM   1105 C  CB  . ASP   A 1 149 ? 20.625  -0.506  56.283 1.00 57.79  ?  156 ASP   A CB  1 
ATOM   1106 C  CG  . ASP   A 1 149 ? 20.087  -0.130  57.650 1.00 66.76  ?  156 ASP   A CG  1 
ATOM   1107 O  OD1 . ASP   A 1 149 ? 20.830  0.464   58.450 1.00 71.65  ?  156 ASP   A OD1 1 
ATOM   1108 O  OD2 . ASP   A 1 149 ? 18.905  -0.427  57.934 1.00 76.62  ?  156 ASP   A OD2 1 
ATOM   1109 N  N   . LEU   A 1 150 ? 23.940  -1.805  57.365 1.00 62.71  ?  157 LEU   A N   1 
ATOM   1110 C  CA  . LEU   A 1 150 ? 24.590  -2.890  58.131 1.00 63.55  ?  157 LEU   A CA  1 
ATOM   1111 C  C   . LEU   A 1 150 ? 24.275  -2.894  59.627 1.00 63.45  ?  157 LEU   A C   1 
ATOM   1112 O  O   . LEU   A 1 150 ? 24.321  -3.957  60.249 1.00 81.24  ?  157 LEU   A O   1 
ATOM   1113 C  CB  . LEU   A 1 150 ? 26.116  -2.901  57.895 1.00 62.43  ?  157 LEU   A CB  1 
ATOM   1114 C  CG  . LEU   A 1 150 ? 26.527  -3.156  56.442 1.00 64.08  ?  157 LEU   A CG  1 
ATOM   1115 C  CD1 . LEU   A 1 150 ? 28.013  -2.899  56.272 1.00 65.61  ?  157 LEU   A CD1 1 
ATOM   1116 C  CD2 . LEU   A 1 150 ? 26.200  -4.573  55.988 1.00 68.65  ?  157 LEU   A CD2 1 
ATOM   1117 N  N   . GLY   A 1 151 ? 23.960  -1.721  60.186 1.00 63.65  ?  158 GLY   A N   1 
ATOM   1118 C  CA  . GLY   A 1 151 ? 23.495  -1.585  61.562 1.00 59.44  ?  158 GLY   A CA  1 
ATOM   1119 C  C   . GLY   A 1 151 ? 22.007  -1.760  61.786 1.00 58.60  ?  158 GLY   A C   1 
ATOM   1120 O  O   . GLY   A 1 151 ? 21.560  -1.609  62.920 1.00 69.10  ?  158 GLY   A O   1 
ATOM   1121 N  N   . LEU   A 1 152 ? 21.242  -2.067  60.734 1.00 64.05  ?  159 LEU   A N   1 
ATOM   1122 C  CA  . LEU   A 1 152 ? 19.801  -2.375  60.815 1.00 68.29  ?  159 LEU   A CA  1 
ATOM   1123 C  C   . LEU   A 1 152 ? 18.969  -1.244  61.453 1.00 69.36  ?  159 LEU   A C   1 
ATOM   1124 O  O   . LEU   A 1 152 ? 18.052  -1.478  62.240 1.00 68.80  ?  159 LEU   A O   1 
ATOM   1125 C  CB  . LEU   A 1 152 ? 19.582  -3.725  61.515 1.00 67.65  ?  159 LEU   A CB  1 
ATOM   1126 C  CG  . LEU   A 1 152 ? 20.274  -4.937  60.867 1.00 70.84  ?  159 LEU   A CG  1 
ATOM   1127 C  CD1 . LEU   A 1 152 ? 20.346  -6.105  61.836 1.00 71.28  ?  159 LEU   A CD1 1 
ATOM   1128 C  CD2 . LEU   A 1 152 ? 19.566  -5.338  59.583 1.00 70.17  ?  159 LEU   A CD2 1 
ATOM   1129 N  N   . ALA   A 1 153 ? 19.328  -0.011  61.103 1.00 75.20  ?  160 ALA   A N   1 
ATOM   1130 C  CA  . ALA   A 1 153 ? 18.631  1.205   61.571 1.00 73.34  ?  160 ALA   A CA  1 
ATOM   1131 C  C   . ALA   A 1 153 ? 17.158  1.294   61.140 1.00 68.87  ?  160 ALA   A C   1 
ATOM   1132 O  O   . ALA   A 1 153 ? 16.341  1.839   61.887 1.00 74.90  ?  160 ALA   A O   1 
ATOM   1133 C  CB  . ALA   A 1 153 ? 19.391  2.449   61.121 1.00 74.80  ?  160 ALA   A CB  1 
ATOM   1134 N  N   . SER   A 1 154 ? 16.837  0.758   59.956 1.00 70.69  ?  161 SER   A N   1 
ATOM   1135 C  CA  . SER   A 1 154 ? 15.448  0.686   59.446 1.00 71.50  ?  161 SER   A CA  1 
ATOM   1136 C  C   . SER   A 1 154 ? 14.630  -0.551  59.892 1.00 72.92  ?  161 SER   A C   1 
ATOM   1137 O  O   . SER   A 1 154 ? 13.442  -0.650  59.542 1.00 64.08  ?  161 SER   A O   1 
ATOM   1138 C  CB  . SER   A 1 154 ? 15.455  0.777   57.914 1.00 69.81  ?  161 SER   A CB  1 
ATOM   1139 O  OG  . SER   A 1 154 ? 15.854  2.064   57.501 1.00 67.33  ?  161 SER   A OG  1 
ATOM   1140 N  N   . PHE   A 1 155 ? 15.251  -1.464  60.654 1.00 73.83  ?  162 PHE   A N   1 
ATOM   1141 C  CA  . PHE   A 1 155 ? 14.718  -2.810  60.930 1.00 83.66  ?  162 PHE   A CA  1 
ATOM   1142 C  C   . PHE   A 1 155 ? 14.930  -3.171  62.410 1.00 85.82  ?  162 PHE   A C   1 
ATOM   1143 O  O   . PHE   A 1 155 ? 15.929  -3.807  62.770 1.00 82.83  ?  162 PHE   A O   1 
ATOM   1144 C  CB  . PHE   A 1 155 ? 15.352  -3.838  59.968 1.00 85.41  ?  162 PHE   A CB  1 
ATOM   1145 C  CG  . PHE   A 1 155 ? 15.253  -3.423  58.533 1.00 76.50  ?  162 PHE   A CG  1 
ATOM   1146 C  CD1 . PHE   A 1 155 ? 14.007  -3.392  57.910 1.00 74.62  ?  162 PHE   A CD1 1 
ATOM   1147 C  CD2 . PHE   A 1 155 ? 16.375  -2.979  57.823 1.00 65.70  ?  162 PHE   A CD2 1 
ATOM   1148 C  CE1 . PHE   A 1 155 ? 13.877  -2.957  56.593 1.00 74.38  ?  162 PHE   A CE1 1 
ATOM   1149 C  CE2 . PHE   A 1 155 ? 16.247  -2.547  56.507 1.00 65.48  ?  162 PHE   A CE2 1 
ATOM   1150 C  CZ  . PHE   A 1 155 ? 14.997  -2.532  55.890 1.00 65.69  ?  162 PHE   A CZ  1 
ATOM   1151 N  N   . LYS   A 1 156 ? 13.970  -2.758  63.247 1.00 86.84  ?  163 LYS   A N   1 
ATOM   1152 C  CA  . LYS   A 1 156 ? 14.098  -2.787  64.723 1.00 89.36  ?  163 LYS   A CA  1 
ATOM   1153 C  C   . LYS   A 1 156 ? 14.166  -4.193  65.324 1.00 90.57  ?  163 LYS   A C   1 
ATOM   1154 O  O   . LYS   A 1 156 ? 14.947  -4.433  66.247 1.00 90.93  ?  163 LYS   A O   1 
ATOM   1155 C  CB  . LYS   A 1 156 ? 12.950  -2.010  65.398 1.00 93.64  ?  163 LYS   A CB  1 
ATOM   1156 C  CG  . LYS   A 1 156 ? 12.931  -0.507  65.130 1.00 101.05 ?  163 LYS   A CG  1 
ATOM   1157 C  CD  . LYS   A 1 156 ? 11.687  0.134   65.706 0.00 104.99 ?  163 LYS   A CD  1 
ATOM   1158 C  CE  . LYS   A 1 156 ? 11.609  1.610   65.350 0.00 105.87 ?  163 LYS   A CE  1 
ATOM   1159 N  NZ  . LYS   A 1 156 ? 10.341  2.230   65.825 0.00 108.55 ?  163 LYS   A NZ  1 
ATOM   1160 N  N   . MET   A 1 157 ? 13.339  -5.104  64.801 1.00 95.14  ?  164 MET   A N   1 
ATOM   1161 C  CA  . MET   A 1 157 ? 13.256  -6.490  65.293 1.00 92.03  ?  164 MET   A CA  1 
ATOM   1162 C  C   . MET   A 1 157 ? 14.531  -7.292  65.006 1.00 86.82  ?  164 MET   A C   1 
ATOM   1163 O  O   . MET   A 1 157 ? 15.013  -8.006  65.884 1.00 90.84  ?  164 MET   A O   1 
ATOM   1164 C  CB  . MET   A 1 157 ? 12.020  -7.212  64.723 1.00 101.75 ?  164 MET   A CB  1 
ATOM   1165 C  CG  . MET   A 1 157 ? 11.393  -8.232  65.663 1.00 119.36 ?  164 MET   A CG  1 
ATOM   1166 S  SD  . MET   A 1 157 ? 10.737  -7.538  67.201 1.00 122.81 ?  164 MET   A SD  1 
ATOM   1167 C  CE  . MET   A 1 157 ? 9.393   -6.502  66.619 1.00 118.76 ?  164 MET   A CE  1 
ATOM   1168 N  N   . TRP   A 1 158 ? 15.064  -7.162  63.790 1.00 81.25  ?  165 TRP   A N   1 
ATOM   1169 C  CA  . TRP   A 1 158 ? 16.384  -7.714  63.444 1.00 72.98  ?  165 TRP   A CA  1 
ATOM   1170 C  C   . TRP   A 1 158 ? 17.561  -7.086  64.210 1.00 76.57  ?  165 TRP   A C   1 
ATOM   1171 O  O   . TRP   A 1 158 ? 18.524  -7.780  64.531 1.00 82.47  ?  165 TRP   A O   1 
ATOM   1172 C  CB  . TRP   A 1 158 ? 16.627  -7.634  61.930 1.00 75.30  ?  165 TRP   A CB  1 
ATOM   1173 C  CG  . TRP   A 1 158 ? 15.886  -8.670  61.168 1.00 75.39  ?  165 TRP   A CG  1 
ATOM   1174 C  CD1 . TRP   A 1 158 ? 14.628  -8.570  60.658 1.00 75.45  ?  165 TRP   A CD1 1 
ATOM   1175 C  CD2 . TRP   A 1 158 ? 16.348  -9.986  60.847 1.00 73.13  ?  165 TRP   A CD2 1 
ATOM   1176 N  NE1 . TRP   A 1 158 ? 14.272  -9.737  60.033 1.00 72.11  ?  165 TRP   A NE1 1 
ATOM   1177 C  CE2 . TRP   A 1 158 ? 15.307  -10.629 60.132 1.00 74.70  ?  165 TRP   A CE2 1 
ATOM   1178 C  CE3 . TRP   A 1 158 ? 17.538  -10.689 61.094 1.00 69.82  ?  165 TRP   A CE3 1 
ATOM   1179 C  CZ2 . TRP   A 1 158 ? 15.422  -11.952 59.653 1.00 70.80  ?  165 TRP   A CZ2 1 
ATOM   1180 C  CZ3 . TRP   A 1 158 ? 17.662  -12.006 60.616 1.00 70.42  ?  165 TRP   A CZ3 1 
ATOM   1181 C  CH2 . TRP   A 1 158 ? 16.604  -12.623 59.906 1.00 73.14  ?  165 TRP   A CH2 1 
ATOM   1182 N  N   . SER   A 1 159 ? 17.488  -5.790  64.504 1.00 87.24  ?  166 SER   A N   1 
ATOM   1183 C  CA  . SER   A 1 159 ? 18.543  -5.100  65.275 1.00 92.69  ?  166 SER   A CA  1 
ATOM   1184 C  C   . SER   A 1 159 ? 18.511  -5.498  66.759 1.00 93.39  ?  166 SER   A C   1 
ATOM   1185 O  O   . SER   A 1 159 ? 19.564  -5.776  67.339 1.00 92.69  ?  166 SER   A O   1 
ATOM   1186 C  CB  . SER   A 1 159 ? 18.438  -3.580  65.113 1.00 90.43  ?  166 SER   A CB  1 
ATOM   1187 O  OG  . SER   A 1 159 ? 17.325  -3.057  65.811 1.00 102.43 ?  166 SER   A OG  1 
ATOM   1188 N  N   . LYS   A 1 160 ? 17.307  -5.508  67.350 1.00 88.47  ?  167 LYS   A N   1 
ATOM   1189 C  CA  . LYS   A 1 160 ? 17.085  -5.991  68.728 1.00 94.16  ?  167 LYS   A CA  1 
ATOM   1190 C  C   . LYS   A 1 160 ? 17.399  -7.484  68.938 1.00 102.87 ?  167 LYS   A C   1 
ATOM   1191 O  O   . LYS   A 1 160 ? 17.808  -7.877  70.038 1.00 109.52 ?  167 LYS   A O   1 
ATOM   1192 C  CB  . LYS   A 1 160 ? 15.644  -5.702  69.195 1.00 105.16 ?  167 LYS   A CB  1 
ATOM   1193 C  CG  . LYS   A 1 160 ? 15.348  -4.230  69.450 1.00 111.34 ?  167 LYS   A CG  1 
ATOM   1194 C  CD  . LYS   A 1 160 ? 13.854  -3.961  69.520 0.00 113.42 ?  167 LYS   A CD  1 
ATOM   1195 C  CE  . LYS   A 1 160 ? 13.564  -2.475  69.658 0.00 114.34 ?  167 LYS   A CE  1 
ATOM   1196 N  NZ  . LYS   A 1 160 ? 12.105  -2.185  69.600 0.00 115.87 ?  167 LYS   A NZ  1 
ATOM   1197 N  N   . LEU   A 1 161 ? 17.182  -8.302  67.902 1.00 103.58 ?  168 LEU   A N   1 
ATOM   1198 C  CA  . LEU   A 1 161 ? 17.578  -9.724  67.901 1.00 100.74 ?  168 LEU   A CA  1 
ATOM   1199 C  C   . LEU   A 1 161 ? 19.089  -9.962  68.073 1.00 103.50 ?  168 LEU   A C   1 
ATOM   1200 O  O   . LEU   A 1 161 ? 19.477  -11.000 68.622 1.00 114.24 ?  168 LEU   A O   1 
ATOM   1201 C  CB  . LEU   A 1 161 ? 17.091  -10.409 66.618 1.00 105.64 ?  168 LEU   A CB  1 
ATOM   1202 C  CG  . LEU   A 1 161 ? 17.400  -11.888 66.365 1.00 105.56 ?  168 LEU   A CG  1 
ATOM   1203 C  CD1 . LEU   A 1 161 ? 16.852  -12.780 67.471 1.00 105.71 ?  168 LEU   A CD1 1 
ATOM   1204 C  CD2 . LEU   A 1 161 ? 16.829  -12.291 65.018 1.00 106.23 ?  168 LEU   A CD2 1 
ATOM   1205 N  N   . ASN   A 1 162 ? 19.921  -9.024  67.600 1.00 99.82  ?  169 ASN   A N   1 
ATOM   1206 C  CA  . ASN   A 1 162 ? 21.374  -9.070  67.818 1.00 106.61 ?  169 ASN   A CA  1 
ATOM   1207 C  C   . ASN   A 1 162 ? 21.680  -8.867  69.306 1.00 127.61 ?  169 ASN   A C   1 
ATOM   1208 O  O   . ASN   A 1 162 ? 22.271  -9.747  69.942 1.00 126.04 ?  169 ASN   A O   1 
ATOM   1209 C  CB  . ASN   A 1 162 ? 22.086  -8.012  66.941 1.00 108.91 ?  169 ASN   A CB  1 
ATOM   1210 C  CG  . ASN   A 1 162 ? 23.635  -8.102  66.924 1.00 116.58 ?  169 ASN   A CG  1 
ATOM   1211 O  OD1 . ASN   A 1 162 ? 24.250  -7.194  66.372 1.00 124.57 ?  169 ASN   A OD1 1 
ATOM   1212 N  ND2 . ASN   A 1 162 ? 24.270  -9.150  67.487 1.00 116.19 ?  169 ASN   A ND2 1 
ATOM   1213 N  N   . ASN   A 1 163 ? 21.244  -7.727  69.847 1.00 153.07 ?  170 ASN   A N   1 
ATOM   1214 C  CA  . ASN   A 1 163 ? 21.465  -7.375  71.261 1.00 147.95 ?  170 ASN   A CA  1 
ATOM   1215 C  C   . ASN   A 1 163 ? 20.502  -8.160  72.176 1.00 148.36 ?  170 ASN   A C   1 
ATOM   1216 O  O   . ASN   A 1 163 ? 19.480  -7.629  72.627 1.00 144.74 ?  170 ASN   A O   1 
ATOM   1217 C  CB  . ASN   A 1 163 ? 21.328  -5.856  71.464 1.00 138.25 ?  170 ASN   A CB  1 
ATOM   1218 C  CG  . ASN   A 1 163 ? 21.879  -5.329  72.778 0.00 154.16 ?  170 ASN   A CG  1 
ATOM   1219 O  OD1 . ASN   A 1 163 ? 22.399  -6.079  73.609 0.00 154.90 ?  170 ASN   A OD1 1 
ATOM   1220 N  ND2 . ASN   A 1 163 ? 21.757  -4.020  72.985 0.00 154.30 ?  170 ASN   A ND2 1 
ATOM   1221 N  N   . GLU   A 1 164 ? 20.847  -9.429  72.425 1.00 150.66 ?  171 GLU   A N   1 
ATOM   1222 C  CA  . GLU   A 1 164 ? 20.053  -10.353 73.266 1.00 154.77 ?  171 GLU   A CA  1 
ATOM   1223 C  C   . GLU   A 1 164 ? 20.964  -11.186 74.184 1.00 174.03 ?  171 GLU   A C   1 
ATOM   1224 O  O   . GLU   A 1 164 ? 22.095  -11.507 73.807 1.00 184.19 ?  171 GLU   A O   1 
ATOM   1225 C  CB  . GLU   A 1 164 ? 19.193  -11.276 72.391 1.00 145.86 ?  171 GLU   A CB  1 
ATOM   1226 C  CG  . GLU   A 1 164 ? 18.038  -11.946 73.137 1.00 148.57 ?  171 GLU   A CG  1 
ATOM   1227 C  CD  . GLU   A 1 164 ? 17.239  -12.922 72.288 1.00 152.96 ?  171 GLU   A CD  1 
ATOM   1228 O  OE1 . GLU   A 1 164 ? 17.005  -12.641 71.094 1.00 173.25 ?  171 GLU   A OE1 1 
ATOM   1229 O  OE2 . GLU   A 1 164 ? 16.829  -13.975 72.827 1.00 142.45 ?  171 GLU   A OE2 1 
ATOM   1230 N  N   . GLU   A 1 165 ? 20.453  -11.519 75.373 1.00 180.27 ?  172 GLU   A N   1 
ATOM   1231 C  CA  . GLU   A 1 165 ? 21.236  -12.178 76.438 1.00 172.73 ?  172 GLU   A CA  1 
ATOM   1232 C  C   . GLU   A 1 165 ? 21.647  -13.625 76.099 1.00 168.46 ?  172 GLU   A C   1 
ATOM   1233 O  O   . GLU   A 1 165 ? 22.773  -14.032 76.407 1.00 162.35 ?  172 GLU   A O   1 
ATOM   1234 C  CB  . GLU   A 1 165 ? 20.479  -12.132 77.779 1.00 166.62 ?  172 GLU   A CB  1 
ATOM   1235 C  CG  . GLU   A 1 165 ? 21.373  -12.202 79.007 1.00 156.66 ?  172 GLU   A CG  1 
ATOM   1236 C  CD  . GLU   A 1 165 ? 20.595  -11.983 80.306 0.00 171.16 ?  172 GLU   A CD  1 
ATOM   1237 O  OE1 . GLU   A 1 165 ? 19.809  -11.017 80.416 0.00 170.15 ?  172 GLU   A OE1 1 
ATOM   1238 O  OE2 . GLU   A 1 165 ? 20.790  -12.797 81.234 0.00 172.53 ?  172 GLU   A OE2 1 
ATOM   1239 N  N   . HIS   A 1 166 ? 20.739  -14.384 75.475 1.00 162.49 ?  173 HIS   A N   1 
ATOM   1240 C  CA  . HIS   A 1 166 ? 21.035  -15.758 75.006 1.00 155.79 ?  173 HIS   A CA  1 
ATOM   1241 C  C   . HIS   A 1 166 ? 22.081  -15.884 73.871 1.00 155.23 ?  173 HIS   A C   1 
ATOM   1242 O  O   . HIS   A 1 166 ? 22.672  -16.959 73.699 1.00 127.49 ?  173 HIS   A O   1 
ATOM   1243 C  CB  . HIS   A 1 166 ? 19.743  -16.464 74.565 1.00 150.23 ?  173 HIS   A CB  1 
ATOM   1244 C  CG  . HIS   A 1 166 ? 18.880  -16.932 75.694 1.00 149.14 ?  173 HIS   A CG  1 
ATOM   1245 N  ND1 . HIS   A 1 166 ? 19.355  -17.707 76.731 1.00 140.32 ?  173 HIS   A ND1 1 
ATOM   1246 C  CD2 . HIS   A 1 166 ? 17.549  -16.806 75.903 1.00 146.33 ?  173 HIS   A CD2 1 
ATOM   1247 C  CE1 . HIS   A 1 166 ? 18.365  -17.998 77.554 1.00 133.53 ?  173 HIS   A CE1 1 
ATOM   1248 N  NE2 . HIS   A 1 166 ? 17.257  -17.466 77.073 1.00 140.92 ?  173 HIS   A NE2 1 
ATOM   1249 N  N   . ASN   A 1 167 ? 22.281  -14.814 73.094 1.00 162.90 ?  174 ASN   A N   1 
ATOM   1250 C  CA  . ASN   A 1 167 ? 23.141  -14.824 71.886 1.00 159.05 ?  174 ASN   A CA  1 
ATOM   1251 C  C   . ASN   A 1 167 ? 24.631  -15.030 72.219 1.00 156.40 ?  174 ASN   A C   1 
ATOM   1252 O  O   . ASN   A 1 167 ? 25.211  -14.218 72.948 1.00 145.50 ?  174 ASN   A O   1 
ATOM   1253 C  CB  . ASN   A 1 167 ? 22.950  -13.496 71.110 1.00 159.08 ?  174 ASN   A CB  1 
ATOM   1254 C  CG  . ASN   A 1 167 ? 23.623  -13.478 69.736 1.00 157.29 ?  174 ASN   A CG  1 
ATOM   1255 O  OD1 . ASN   A 1 167 ? 23.910  -14.521 69.148 1.00 153.64 ?  174 ASN   A OD1 1 
ATOM   1256 N  ND2 . ASN   A 1 167 ? 23.885  -12.279 69.227 1.00 152.38 ?  174 ASN   A ND2 1 
ATOM   1257 N  N   . GLU   A 1 168 ? 25.224  -16.094 71.658 1.00 165.44 ?  175 GLU   A N   1 
ATOM   1258 C  CA  . GLU   A 1 168 ? 26.643  -16.446 71.919 1.00 168.18 ?  175 GLU   A CA  1 
ATOM   1259 C  C   . GLU   A 1 168 ? 27.665  -15.911 70.877 1.00 164.88 ?  175 GLU   A C   1 
ATOM   1260 O  O   . GLU   A 1 168 ? 28.805  -16.391 70.835 1.00 172.94 ?  175 GLU   A O   1 
ATOM   1261 C  CB  . GLU   A 1 168 ? 26.790  -17.970 72.153 1.00 161.30 ?  175 GLU   A CB  1 
ATOM   1262 C  CG  . GLU   A 1 168 ? 26.603  -18.877 70.943 1.00 153.64 ?  175 GLU   A CG  1 
ATOM   1263 C  CD  . GLU   A 1 168 ? 26.901  -20.342 71.277 0.00 168.85 ?  175 GLU   A CD  1 
ATOM   1264 O  OE1 . GLU   A 1 168 ? 26.346  -20.866 72.268 0.00 169.48 ?  175 GLU   A OE1 1 
ATOM   1265 O  OE2 . GLU   A 1 168 ? 27.680  -20.972 70.531 0.00 170.40 ?  175 GLU   A OE2 1 
ATOM   1266 N  N   . LEU   A 1 169 ? 27.273  -14.907 70.075 1.00 161.50 ?  176 LEU   A N   1 
ATOM   1267 C  CA  . LEU   A 1 169 ? 28.171  -14.214 69.126 1.00 158.93 ?  176 LEU   A CA  1 
ATOM   1268 C  C   . LEU   A 1 169 ? 28.880  -13.043 69.807 1.00 158.33 ?  176 LEU   A C   1 
ATOM   1269 O  O   . LEU   A 1 169 ? 29.480  -12.200 69.145 1.00 155.32 ?  176 LEU   A O   1 
ATOM   1270 C  CB  . LEU   A 1 169 ? 27.385  -13.695 67.913 1.00 149.17 ?  176 LEU   A CB  1 
ATOM   1271 C  CG  . LEU   A 1 169 ? 26.703  -14.775 67.062 1.00 141.28 ?  176 LEU   A CG  1 
ATOM   1272 C  CD1 . LEU   A 1 169 ? 25.622  -14.181 66.176 1.00 138.00 ?  176 LEU   A CD1 1 
ATOM   1273 C  CD2 . LEU   A 1 169 ? 27.719  -15.512 66.206 1.00 131.10 ?  176 LEU   A CD2 1 
ATOM   1274 N  N   . GLY   A 1 181 ? 32.965  8.197   65.967 1.00 72.06  ?  188 GLY   A N   1 
ATOM   1275 C  CA  . GLY   A 1 181 ? 32.828  7.612   64.625 1.00 77.56  ?  188 GLY   A CA  1 
ATOM   1276 C  C   . GLY   A 1 181 ? 31.398  7.338   64.170 1.00 80.34  ?  188 GLY   A C   1 
ATOM   1277 O  O   . GLY   A 1 181 ? 31.059  7.509   62.988 1.00 76.43  ?  188 GLY   A O   1 
ATOM   1278 N  N   . THR   A 1 182 ? 30.564  6.884   65.105 1.00 83.45  ?  189 THR   A N   1 
ATOM   1279 C  CA  . THR   A 1 182 ? 29.108  6.810   64.908 1.00 89.75  ?  189 THR   A CA  1 
ATOM   1280 C  C   . THR   A 1 182 ? 28.490  8.214   64.706 1.00 86.85  ?  189 THR   A C   1 
ATOM   1281 O  O   . THR   A 1 182 ? 27.738  8.422   63.749 1.00 72.82  ?  189 THR   A O   1 
ATOM   1282 C  CB  . THR   A 1 182 ? 28.407  6.047   66.067 1.00 97.51  ?  189 THR   A CB  1 
ATOM   1283 O  OG1 . THR   A 1 182 ? 28.786  6.595   67.337 1.00 93.10  ?  189 THR   A OG1 1 
ATOM   1284 C  CG2 . THR   A 1 182 ? 28.776  4.545   66.041 1.00 93.60  ?  189 THR   A CG2 1 
ATOM   1285 N  N   . LEU   A 1 183 ? 28.883  9.169   65.557 1.00 84.66  ?  190 LEU   A N   1 
ATOM   1286 C  CA  . LEU   A 1 183 ? 28.295  10.523  65.566 1.00 77.72  ?  190 LEU   A CA  1 
ATOM   1287 C  C   . LEU   A 1 183 ? 28.687  11.465  64.415 1.00 69.80  ?  190 LEU   A C   1 
ATOM   1288 O  O   . LEU   A 1 183 ? 28.045  12.513  64.277 1.00 77.87  ?  190 LEU   A O   1 
ATOM   1289 C  CB  . LEU   A 1 183 ? 28.622  11.221  66.893 1.00 78.43  ?  190 LEU   A CB  1 
ATOM   1290 C  CG  . LEU   A 1 183 ? 28.134  10.586  68.186 1.00 78.89  ?  190 LEU   A CG  1 
ATOM   1291 C  CD1 . LEU   A 1 183 ? 28.739  11.325  69.369 1.00 81.80  ?  190 LEU   A CD1 1 
ATOM   1292 C  CD2 . LEU   A 1 183 ? 26.618  10.583  68.272 1.00 73.34  ?  190 LEU   A CD2 1 
ATOM   1293 N  N   . TYR   A 1 184 ? 29.746  11.159  63.659 1.00 68.00  ?  191 TYR   A N   1 
ATOM   1294 C  CA  . TYR   A 1 184 ? 30.334  12.156  62.724 1.00 65.04  ?  191 TYR   A CA  1 
ATOM   1295 C  C   . TYR   A 1 184 ? 29.442  12.554  61.553 1.00 59.11  ?  191 TYR   A C   1 
ATOM   1296 O  O   . TYR   A 1 184 ? 29.574  13.663  61.038 1.00 62.74  ?  191 TYR   A O   1 
ATOM   1297 C  CB  . TYR   A 1 184 ? 31.684  11.688  62.145 1.00 62.14  ?  191 TYR   A CB  1 
ATOM   1298 C  CG  . TYR   A 1 184 ? 32.845  11.466  63.111 1.00 64.52  ?  191 TYR   A CG  1 
ATOM   1299 C  CD1 . TYR   A 1 184 ? 32.917  12.065  64.390 1.00 63.20  ?  191 TYR   A CD1 1 
ATOM   1300 C  CD2 . TYR   A 1 184 ? 33.935  10.685  62.704 1.00 74.85  ?  191 TYR   A CD2 1 
ATOM   1301 C  CE1 . TYR   A 1 184 ? 34.001  11.838  65.232 1.00 64.68  ?  191 TYR   A CE1 1 
ATOM   1302 C  CE2 . TYR   A 1 184 ? 35.029  10.469  63.539 1.00 68.58  ?  191 TYR   A CE2 1 
ATOM   1303 C  CZ  . TYR   A 1 184 ? 35.054  11.036  64.796 1.00 66.96  ?  191 TYR   A CZ  1 
ATOM   1304 O  OH  . TYR   A 1 184 ? 36.136  10.801  65.600 1.00 74.92  ?  191 TYR   A OH  1 
ATOM   1305 N  N   . TYR   A 1 185 ? 28.533  11.659  61.160 1.00 63.02  ?  192 TYR   A N   1 
ATOM   1306 C  CA  . TYR   A 1 185 ? 27.631  11.866  60.013 1.00 56.60  ?  192 TYR   A CA  1 
ATOM   1307 C  C   . TYR   A 1 185 ? 26.174  12.218  60.396 1.00 51.03  ?  192 TYR   A C   1 
ATOM   1308 O  O   . TYR   A 1 185 ? 25.314  12.284  59.523 1.00 44.31  ?  192 TYR   A O   1 
ATOM   1309 C  CB  . TYR   A 1 185 ? 27.733  10.641  59.091 1.00 54.72  ?  192 TYR   A CB  1 
ATOM   1310 C  CG  . TYR   A 1 185 ? 29.165  10.378  58.703 1.00 53.44  ?  192 TYR   A CG  1 
ATOM   1311 C  CD1 . TYR   A 1 185 ? 29.993  9.597   59.514 1.00 52.90  ?  192 TYR   A CD1 1 
ATOM   1312 C  CD2 . TYR   A 1 185 ? 29.734  10.986  57.575 1.00 52.90  ?  192 TYR   A CD2 1 
ATOM   1313 C  CE1 . TYR   A 1 185 ? 31.339  9.405   59.196 1.00 58.93  ?  192 TYR   A CE1 1 
ATOM   1314 C  CE2 . TYR   A 1 185 ? 31.073  10.791  57.246 1.00 52.90  ?  192 TYR   A CE2 1 
ATOM   1315 C  CZ  . TYR   A 1 185 ? 31.878  10.015  58.055 1.00 53.02  ?  192 TYR   A CZ  1 
ATOM   1316 O  OH  . TYR   A 1 185 ? 33.195  9.826   57.690 1.00 54.98  ?  192 TYR   A OH  1 
ATOM   1317 N  N   . MET   A 1 186 ? 25.935  12.528  61.667 1.00 48.91  ?  193 MET   A N   1 
ATOM   1318 C  CA  . MET   A 1 186 ? 24.589  12.675  62.202 1.00 52.54  ?  193 MET   A CA  1 
ATOM   1319 C  C   . MET   A 1 186 ? 24.214  14.145  62.226 1.00 54.90  ?  193 MET   A C   1 
ATOM   1320 O  O   . MET   A 1 186 ? 24.964  14.985  62.760 1.00 66.48  ?  193 MET   A O   1 
ATOM   1321 C  CB  . MET   A 1 186 ? 24.548  12.087  63.602 1.00 56.07  ?  193 MET   A CB  1 
ATOM   1322 C  CG  . MET   A 1 186 ? 23.155  11.927  64.161 1.00 56.66  ?  193 MET   A CG  1 
ATOM   1323 S  SD  . MET   A 1 186 ? 23.251  11.007  65.706 1.00 70.15  ?  193 MET   A SD  1 
ATOM   1324 C  CE  . MET   A 1 186 ? 23.311  9.314   65.108 1.00 62.65  ?  193 MET   A CE  1 
ATOM   1325 N  N   . ALA   A 1 187 ? 23.045  14.462  61.682 1.00 55.39  ?  194 ALA   A N   1 
ATOM   1326 C  CA  . ALA   A 1 187 ? 22.548  15.833  61.643 1.00 47.33  ?  194 ALA   A CA  1 
ATOM   1327 C  C   . ALA   A 1 187 ? 22.341  16.413  63.044 1.00 54.33  ?  194 ALA   A C   1 
ATOM   1328 O  O   . ALA   A 1 187 ? 21.939  15.681  63.932 1.00 56.70  ?  194 ALA   A O   1 
ATOM   1329 C  CB  . ALA   A 1 187 ? 21.272  15.922  60.854 1.00 52.71  ?  194 ALA   A CB  1 
ATOM   1330 N  N   . PRO   A 1 188 ? 22.663  17.723  63.258 1.00 54.18  ?  195 PRO   A N   1 
ATOM   1331 C  CA  . PRO   A 1 188 ? 22.585  18.344  64.599 1.00 51.16  ?  195 PRO   A CA  1 
ATOM   1332 C  C   . PRO   A 1 188 ? 21.226  18.278  65.297 1.00 50.03  ?  195 PRO   A C   1 
ATOM   1333 O  O   . PRO   A 1 188 ? 21.170  18.222  66.534 1.00 48.75  ?  195 PRO   A O   1 
ATOM   1334 C  CB  . PRO   A 1 188 ? 22.954  19.828  64.332 1.00 53.53  ?  195 PRO   A CB  1 
ATOM   1335 C  CG  . PRO   A 1 188 ? 22.644  20.044  62.902 1.00 54.45  ?  195 PRO   A CG  1 
ATOM   1336 C  CD  . PRO   A 1 188 ? 23.027  18.725  62.237 1.00 51.33  ?  195 PRO   A CD  1 
ATOM   1337 N  N   . GLU   A 1 189 ? 20.142  18.312  64.526 1.00 50.78  ?  196 GLU   A N   1 
ATOM   1338 C  CA  . GLU   A 1 189 ? 18.787  18.035  65.057 1.00 56.76  ?  196 GLU   A CA  1 
ATOM   1339 C  C   . GLU   A 1 189 ? 18.639  16.714  65.850 1.00 60.92  ?  196 GLU   A C   1 
ATOM   1340 O  O   . GLU   A 1 189 ? 17.785  16.638  66.727 1.00 73.63  ?  196 GLU   A O   1 
ATOM   1341 C  CB  . GLU   A 1 189 ? 17.695  18.151  63.964 1.00 57.95  ?  196 GLU   A CB  1 
ATOM   1342 C  CG  . GLU   A 1 189 ? 17.804  17.216  62.750 1.00 63.21  ?  196 GLU   A CG  1 
ATOM   1343 C  CD  . GLU   A 1 189 ? 18.455  17.853  61.524 1.00 61.07  ?  196 GLU   A CD  1 
ATOM   1344 O  OE1 . GLU   A 1 189 ? 18.036  17.560  60.366 1.00 53.80  ?  196 GLU   A OE1 1 
ATOM   1345 O  OE2 . GLU   A 1 189 ? 19.405  18.642  61.704 1.00 59.52  ?  196 GLU   A OE2 1 
ATOM   1346 N  N   . HIS   A 1 190 ? 19.462  15.704  65.547 1.00 58.87  ?  197 HIS   A N   1 
ATOM   1347 C  CA  . HIS   A 1 190 ? 19.486  14.409  66.279 1.00 61.33  ?  197 HIS   A CA  1 
ATOM   1348 C  C   . HIS   A 1 190 ? 20.538  14.288  67.389 1.00 60.98  ?  197 HIS   A C   1 
ATOM   1349 O  O   . HIS   A 1 190 ? 20.397  13.422  68.242 1.00 63.87  ?  197 HIS   A O   1 
ATOM   1350 C  CB  . HIS   A 1 190 ? 19.674  13.256  65.292 1.00 56.34  ?  197 HIS   A CB  1 
ATOM   1351 C  CG  . HIS   A 1 190 ? 18.635  13.218  64.227 1.00 57.25  ?  197 HIS   A CG  1 
ATOM   1352 N  ND1 . HIS   A 1 190 ? 17.310  12.990  64.518 1.00 62.27  ?  197 HIS   A ND1 1 
ATOM   1353 C  CD2 . HIS   A 1 190 ? 18.705  13.394  62.887 1.00 52.89  ?  197 HIS   A CD2 1 
ATOM   1354 C  CE1 . HIS   A 1 190 ? 16.602  13.026  63.407 1.00 55.32  ?  197 HIS   A CE1 1 
ATOM   1355 N  NE2 . HIS   A 1 190 ? 17.424  13.264  62.399 1.00 56.39  ?  197 HIS   A NE2 1 
ATOM   1356 N  N   . LEU   A 1 191 ? 21.577  15.133  67.376 1.00 65.92  ?  198 LEU   A N   1 
ATOM   1357 C  CA  . LEU   A 1 191 ? 22.582  15.173  68.448 1.00 66.79  ?  198 LEU   A CA  1 
ATOM   1358 C  C   . LEU   A 1 191 ? 21.954  15.766  69.711 1.00 70.15  ?  198 LEU   A C   1 
ATOM   1359 O  O   . LEU   A 1 191 ? 21.393  16.867  69.655 1.00 67.71  ?  198 LEU   A O   1 
ATOM   1360 C  CB  . LEU   A 1 191 ? 23.796  16.023  68.029 1.00 68.36  ?  198 LEU   A CB  1 
ATOM   1361 C  CG  . LEU   A 1 191 ? 24.580  15.643  66.776 1.00 70.88  ?  198 LEU   A CG  1 
ATOM   1362 C  CD1 . LEU   A 1 191 ? 25.688  16.651  66.586 1.00 70.04  ?  198 LEU   A CD1 1 
ATOM   1363 C  CD2 . LEU   A 1 191 ? 25.156  14.224  66.840 1.00 76.42  ?  198 LEU   A CD2 1 
ATOM   1364 N  N   . ASN   A 1 192 ? 22.029  15.030  70.829 1.00 71.15  ?  199 ASN   A N   1 
ATOM   1365 C  CA  . ASN   A 1 192 ? 21.327  15.388  72.087 1.00 74.81  ?  199 ASN   A CA  1 
ATOM   1366 C  C   . ASN   A 1 192 ? 19.790  15.601  71.939 1.00 71.24  ?  199 ASN   A C   1 
ATOM   1367 O  O   . ASN   A 1 192 ? 19.199  16.425  72.635 1.00 74.16  ?  199 ASN   A O   1 
ATOM   1368 C  CB  . ASN   A 1 192 ? 22.034  16.593  72.792 1.00 73.52  ?  199 ASN   A CB  1 
ATOM   1369 C  CG  . ASN   A 1 192 ? 23.431  16.244  73.325 1.00 70.96  ?  199 ASN   A CG  1 
ATOM   1370 O  OD1 . ASN   A 1 192 ? 23.922  15.128  73.159 1.00 73.95  ?  199 ASN   A OD1 1 
ATOM   1371 N  ND2 . ASN   A 1 192 ? 24.068  17.204  73.978 1.00 80.31  ?  199 ASN   A ND2 1 
ATOM   1372 N  N   . ASP   A 1 193 ? 19.164  14.807  71.066 1.00 78.33  ?  200 ASP   A N   1 
ATOM   1373 C  CA  . ASP   A 1 193 ? 17.710  14.815  70.841 1.00 78.77  ?  200 ASP   A CA  1 
ATOM   1374 C  C   . ASP   A 1 193 ? 17.326  13.510  70.122 1.00 78.12  ?  200 ASP   A C   1 
ATOM   1375 O  O   . ASP   A 1 193 ? 17.099  13.486  68.917 1.00 77.49  ?  200 ASP   A O   1 
ATOM   1376 C  CB  . ASP   A 1 193 ? 17.248  16.071  70.071 1.00 86.25  ?  200 ASP   A CB  1 
ATOM   1377 C  CG  . ASP   A 1 193 ? 15.717  16.296  70.124 1.00 89.16  ?  200 ASP   A CG  1 
ATOM   1378 O  OD1 . ASP   A 1 193 ? 14.934  15.395  70.520 1.00 94.93  ?  200 ASP   A OD1 1 
ATOM   1379 O  OD2 . ASP   A 1 193 ? 15.297  17.411  69.757 1.00 84.06  ?  200 ASP   A OD2 1 
ATOM   1380 N  N   . VAL   A 1 194 ? 17.296  12.432  70.904 1.00 73.38  ?  201 VAL   A N   1 
ATOM   1381 C  CA  . VAL   A 1 194 ? 16.934  11.095  70.424 1.00 71.50  ?  201 VAL   A CA  1 
ATOM   1382 C  C   . VAL   A 1 194 ? 15.461  10.923  70.044 1.00 64.37  ?  201 VAL   A C   1 
ATOM   1383 O  O   . VAL   A 1 194 ? 15.126  10.021  69.254 1.00 57.97  ?  201 VAL   A O   1 
ATOM   1384 C  CB  . VAL   A 1 194 ? 17.357  9.979   71.416 1.00 81.73  ?  201 VAL   A CB  1 
ATOM   1385 C  CG1 . VAL   A 1 194 ? 18.864  9.952   71.559 1.00 83.64  ?  201 VAL   A CG1 1 
ATOM   1386 C  CG2 . VAL   A 1 194 ? 16.672  10.098  72.772 1.00 88.95  ?  201 VAL   A CG2 1 
ATOM   1387 N  N   . ASN   A 1 195 ? 14.588  11.751  70.614 1.00 64.67  ?  202 ASN   A N   1 
ATOM   1388 C  CA  . ASN   A 1 195 ? 13.147  11.680  70.346 1.00 67.42  ?  202 ASN   A CA  1 
ATOM   1389 C  C   . ASN   A 1 195 ? 12.691  12.266  69.009 1.00 67.81  ?  202 ASN   A C   1 
ATOM   1390 O  O   . ASN   A 1 195 ? 11.698  11.800  68.463 1.00 73.63  ?  202 ASN   A O   1 
ATOM   1391 C  CB  . ASN   A 1 195 ? 12.360  12.276  71.512 1.00 71.19  ?  202 ASN   A CB  1 
ATOM   1392 C  CG  . ASN   A 1 195 ? 12.510  11.454  72.799 1.00 75.85  ?  202 ASN   A CG  1 
ATOM   1393 O  OD1 . ASN   A 1 195 ? 12.586  10.210  72.769 1.00 74.00  ?  202 ASN   A OD1 1 
ATOM   1394 N  ND2 . ASN   A 1 195 ? 12.538  12.139  73.937 1.00 76.36  ?  202 ASN   A ND2 1 
ATOM   1395 N  N   . ALA   A 1 196 ? 13.415  13.249  68.473 1.00 74.50  ?  203 ALA   A N   1 
ATOM   1396 C  CA  . ALA   A 1 196 ? 13.063  13.894  67.186 1.00 71.36  ?  203 ALA   A CA  1 
ATOM   1397 C  C   . ALA   A 1 196 ? 13.026  12.924  65.987 1.00 68.20  ?  203 ALA   A C   1 
ATOM   1398 O  O   . ALA   A 1 196 ? 13.936  12.104  65.816 1.00 73.36  ?  203 ALA   A O   1 
ATOM   1399 C  CB  . ALA   A 1 196 ? 14.007  15.064  66.898 1.00 62.97  ?  203 ALA   A CB  1 
ATOM   1400 N  N   . LYS   A 1 197 ? 11.976  13.052  65.169 1.00 63.91  ?  204 LYS   A N   1 
ATOM   1401 C  CA  . LYS   A 1 197 ? 11.698  12.160  64.030 1.00 65.87  ?  204 LYS   A CA  1 
ATOM   1402 C  C   . LYS   A 1 197 ? 12.688  12.487  62.896 1.00 63.93  ?  204 LYS   A C   1 
ATOM   1403 O  O   . LYS   A 1 197 ? 12.790  13.658  62.525 1.00 66.63  ?  204 LYS   A O   1 
ATOM   1404 C  CB  . LYS   A 1 197 ? 10.267  12.380  63.484 1.00 70.62  ?  204 LYS   A CB  1 
ATOM   1405 C  CG  . LYS   A 1 197 ? 9.092   12.305  64.476 1.00 85.27  ?  204 LYS   A CG  1 
ATOM   1406 C  CD  . LYS   A 1 197 ? 8.564   10.891  64.682 1.00 91.59  ?  204 LYS   A CD  1 
ATOM   1407 C  CE  . LYS   A 1 197 ? 7.552   10.899  65.831 0.00 93.64  ?  204 LYS   A CE  1 
ATOM   1408 N  NZ  . LYS   A 1 197 ? 7.074   9.523   66.139 0.00 94.83  ?  204 LYS   A NZ  1 
ATOM   1409 N  N   . PRO   A 1 198 ? 13.437  11.483  62.366 1.00 69.75  ?  205 PRO   A N   1 
ATOM   1410 C  CA  . PRO   A 1 198 ? 14.259  11.750  61.166 1.00 62.08  ?  205 PRO   A CA  1 
ATOM   1411 C  C   . PRO   A 1 198 ? 13.462  12.042  59.896 1.00 58.80  ?  205 PRO   A C   1 
ATOM   1412 O  O   . PRO   A 1 198 ? 12.327  11.606  59.763 1.00 61.00  ?  205 PRO   A O   1 
ATOM   1413 C  CB  . PRO   A 1 198 ? 15.098  10.488  61.022 1.00 62.02  ?  205 PRO   A CB  1 
ATOM   1414 C  CG  . PRO   A 1 198 ? 15.140  9.900   62.392 1.00 70.88  ?  205 PRO   A CG  1 
ATOM   1415 C  CD  . PRO   A 1 198 ? 13.784  10.177  62.957 1.00 72.66  ?  205 PRO   A CD  1 
ATOM   1416 N  N   . THR   A 1 199 ? 14.080  12.795  58.988 1.00 61.48  ?  206 THR   A N   1 
ATOM   1417 C  CA  . THR   A 1 199 ? 13.473  13.184  57.710 1.00 63.51  ?  206 THR   A CA  1 
ATOM   1418 C  C   . THR   A 1 199 ? 14.437  12.866  56.581 1.00 62.33  ?  206 THR   A C   1 
ATOM   1419 O  O   . THR   A 1 199 ? 15.570  12.438  56.819 1.00 57.96  ?  206 THR   A O   1 
ATOM   1420 C  CB  . THR   A 1 199 ? 13.139  14.699  57.699 1.00 59.47  ?  206 THR   A CB  1 
ATOM   1421 O  OG1 . THR   A 1 199 ? 14.355  15.466  57.780 1.00 63.32  ?  206 THR   A OG1 1 
ATOM   1422 C  CG2 . THR   A 1 199 ? 12.185  15.061  58.872 1.00 50.53  ?  206 THR   A CG2 1 
ATOM   1423 N  N   . GLU   A 1 200 ? 13.983  13.106  55.351 1.00 64.38  ?  207 GLU   A N   1 
ATOM   1424 C  CA  . GLU   A 1 200 ? 14.852  13.064  54.167 1.00 59.26  ?  207 GLU   A CA  1 
ATOM   1425 C  C   . GLU   A 1 200 ? 16.082  13.994  54.340 1.00 61.41  ?  207 GLU   A C   1 
ATOM   1426 O  O   . GLU   A 1 200 ? 17.198  13.641  53.937 1.00 66.96  ?  207 GLU   A O   1 
ATOM   1427 C  CB  . GLU   A 1 200 ? 14.075  13.441  52.899 1.00 68.90  ?  207 GLU   A CB  1 
ATOM   1428 C  CG  . GLU   A 1 200 ? 12.937  12.487  52.490 1.00 71.20  ?  207 GLU   A CG  1 
ATOM   1429 C  CD  . GLU   A 1 200 ? 12.122  12.968  51.281 1.00 80.82  ?  207 GLU   A CD  1 
ATOM   1430 O  OE1 . GLU   A 1 200 ? 12.183  14.165  50.896 1.00 101.39 ?  207 GLU   A OE1 1 
ATOM   1431 O  OE2 . GLU   A 1 200 ? 11.387  12.141  50.705 1.00 93.67  ?  207 GLU   A OE2 1 
ATOM   1432 N  N   . LYS   A 1 201 ? 15.883  15.135  54.998 1.00 55.75  ?  208 LYS   A N   1 
ATOM   1433 C  CA  . LYS   A 1 201 ? 16.967  16.098  55.264 1.00 62.75  ?  208 LYS   A CA  1 
ATOM   1434 C  C   . LYS   A 1 201 ? 18.029  15.632  56.253 1.00 54.46  ?  208 LYS   A C   1 
ATOM   1435 O  O   . LYS   A 1 201 ? 19.153  16.128  56.195 1.00 68.49  ?  208 LYS   A O   1 
ATOM   1436 C  CB  . LYS   A 1 201 ? 16.404  17.468  55.693 1.00 57.25  ?  208 LYS   A CB  1 
ATOM   1437 C  CG  . LYS   A 1 201 ? 15.400  18.104  54.711 1.00 62.21  ?  208 LYS   A CG  1 
ATOM   1438 C  CD  . LYS   A 1 201 ? 15.914  18.241  53.276 1.00 60.15  ?  208 LYS   A CD  1 
ATOM   1439 C  CE  . LYS   A 1 201 ? 14.912  18.920  52.353 1.00 65.10  ?  208 LYS   A CE  1 
ATOM   1440 N  NZ  . LYS   A 1 201 ? 14.713  20.367  52.624 1.00 69.97  ?  208 LYS   A NZ  1 
ATOM   1441 N  N   . SER   A 1 202 ? 17.682  14.741  57.180 1.00 54.74  ?  209 SER   A N   1 
ATOM   1442 C  CA  . SER   A 1 202 ? 18.673  14.061  58.042 1.00 55.37  ?  209 SER   A CA  1 
ATOM   1443 C  C   . SER   A 1 202 ? 19.759  13.303  57.270 1.00 57.54  ?  209 SER   A C   1 
ATOM   1444 O  O   . SER   A 1 202 ? 20.955  13.375  57.622 1.00 67.09  ?  209 SER   A O   1 
ATOM   1445 C  CB  . SER   A 1 202 ? 17.979  13.083  58.982 1.00 56.01  ?  209 SER   A CB  1 
ATOM   1446 O  OG  . SER   A 1 202 ? 16.949  13.740  59.702 1.00 63.93  ?  209 SER   A OG  1 
ATOM   1447 N  N   . ASP   A 1 203 ? 19.331  12.578  56.231 1.00 49.58  ?  210 ASP   A N   1 
ATOM   1448 C  CA  . ASP   A 1 203 ? 20.247  11.884  55.317 1.00 45.09  ?  210 ASP   A CA  1 
ATOM   1449 C  C   . ASP   A 1 203 ? 21.073  12.839  54.438 1.00 50.82  ?  210 ASP   A C   1 
ATOM   1450 O  O   . ASP   A 1 203 ? 22.209  12.517  54.122 1.00 49.48  ?  210 ASP   A O   1 
ATOM   1451 C  CB  . ASP   A 1 203 ? 19.490  10.932  54.397 1.00 43.66  ?  210 ASP   A CB  1 
ATOM   1452 C  CG  . ASP   A 1 203 ? 18.915  9.715   55.121 1.00 52.09  ?  210 ASP   A CG  1 
ATOM   1453 O  OD1 . ASP   A 1 203 ? 19.273  9.441   56.291 1.00 58.44  ?  210 ASP   A OD1 1 
ATOM   1454 O  OD2 . ASP   A 1 203 ? 18.100  9.002   54.486 1.00 45.27  ?  210 ASP   A OD2 1 
ATOM   1455 N  N   . VAL   A 1 204 ? 20.486  13.968  54.023 1.00 52.39  ?  211 VAL   A N   1 
ATOM   1456 C  CA  . VAL   A 1 204 ? 21.192  15.010  53.246 1.00 53.28  ?  211 VAL   A CA  1 
ATOM   1457 C  C   . VAL   A 1 204 ? 22.388  15.571  54.036 1.00 52.51  ?  211 VAL   A C   1 
ATOM   1458 O  O   . VAL   A 1 204 ? 23.441  15.810  53.443 1.00 72.91  ?  211 VAL   A O   1 
ATOM   1459 C  CB  . VAL   A 1 204 ? 20.232  16.156  52.766 1.00 51.31  ?  211 VAL   A CB  1 
ATOM   1460 C  CG1 . VAL   A 1 204 ? 20.984  17.276  52.045 1.00 52.89  ?  211 VAL   A CG1 1 
ATOM   1461 C  CG2 . VAL   A 1 204 ? 19.153  15.625  51.834 1.00 47.97  ?  211 VAL   A CG2 1 
ATOM   1462 N  N   . TYR   A 1 205 ? 22.245  15.768  55.350 1.00 50.66  ?  212 TYR   A N   1 
ATOM   1463 C  CA  . TYR   A 1 205 ? 23.397  16.155  56.197 1.00 50.86  ?  212 TYR   A CA  1 
ATOM   1464 C  C   . TYR   A 1 205 ? 24.500  15.052  56.171 1.00 49.29  ?  212 TYR   A C   1 
ATOM   1465 O  O   . TYR   A 1 205 ? 25.674  15.375  56.034 1.00 50.99  ?  212 TYR   A O   1 
ATOM   1466 C  CB  . TYR   A 1 205 ? 22.989  16.436  57.637 1.00 45.57  ?  212 TYR   A CB  1 
ATOM   1467 C  CG  . TYR   A 1 205 ? 24.141  16.954  58.486 1.00 50.25  ?  212 TYR   A CG  1 
ATOM   1468 C  CD1 . TYR   A 1 205 ? 25.069  16.083  59.085 1.00 55.28  ?  212 TYR   A CD1 1 
ATOM   1469 C  CD2 . TYR   A 1 205 ? 24.319  18.312  58.685 1.00 55.20  ?  212 TYR   A CD2 1 
ATOM   1470 C  CE1 . TYR   A 1 205 ? 26.132  16.563  59.840 1.00 52.14  ?  212 TYR   A CE1 1 
ATOM   1471 C  CE2 . TYR   A 1 205 ? 25.388  18.799  59.448 1.00 64.81  ?  212 TYR   A CE2 1 
ATOM   1472 C  CZ  . TYR   A 1 205 ? 26.293  17.903  60.022 1.00 56.11  ?  212 TYR   A CZ  1 
ATOM   1473 O  OH  . TYR   A 1 205 ? 27.340  18.331  60.797 1.00 64.96  ?  212 TYR   A OH  1 
ATOM   1474 N  N   . SER   A 1 206 ? 24.116  13.789  56.357 1.00 49.42  ?  213 SER   A N   1 
ATOM   1475 C  CA  . SER   A 1 206 ? 25.077  12.664  56.340 1.00 44.08  ?  213 SER   A CA  1 
ATOM   1476 C  C   . SER   A 1 206 ? 25.895  12.639  55.054 1.00 44.11  ?  213 SER   A C   1 
ATOM   1477 O  O   . SER   A 1 206 ? 27.132  12.693  55.103 1.00 38.36  ?  213 SER   A O   1 
ATOM   1478 C  CB  . SER   A 1 206 ? 24.362  11.322  56.531 1.00 50.97  ?  213 SER   A CB  1 
ATOM   1479 O  OG  . SER   A 1 206 ? 23.638  11.247  57.756 1.00 47.41  ?  213 SER   A OG  1 
ATOM   1480 N  N   . PHE   A 1 207 ? 25.181  12.648  53.925 1.00 47.64  ?  214 PHE   A N   1 
ATOM   1481 C  CA  . PHE   A 1 207 ? 25.734  12.801  52.565 1.00 54.23  ?  214 PHE   A CA  1 
ATOM   1482 C  C   . PHE   A 1 207 ? 26.751  13.953  52.448 1.00 58.16  ?  214 PHE   A C   1 
ATOM   1483 O  O   . PHE   A 1 207 ? 27.810  13.778  51.865 1.00 48.81  ?  214 PHE   A O   1 
ATOM   1484 C  CB  . PHE   A 1 207 ? 24.585  13.038  51.562 1.00 55.68  ?  214 PHE   A CB  1 
ATOM   1485 C  CG  . PHE   A 1 207 ? 25.034  13.314  50.153 1.00 52.00  ?  214 PHE   A CG  1 
ATOM   1486 C  CD1 . PHE   A 1 207 ? 25.567  12.289  49.355 1.00 62.74  ?  214 PHE   A CD1 1 
ATOM   1487 C  CD2 . PHE   A 1 207 ? 24.956  14.588  49.619 1.00 53.90  ?  214 PHE   A CD2 1 
ATOM   1488 C  CE1 . PHE   A 1 207 ? 26.004  12.548  48.051 1.00 56.46  ?  214 PHE   A CE1 1 
ATOM   1489 C  CE2 . PHE   A 1 207 ? 25.391  14.854  48.320 1.00 53.75  ?  214 PHE   A CE2 1 
ATOM   1490 C  CZ  . PHE   A 1 207 ? 25.902  13.841  47.532 1.00 48.13  ?  214 PHE   A CZ  1 
ATOM   1491 N  N   . ALA   A 1 208 ? 26.407  15.114  53.007 1.00 61.96  ?  215 ALA   A N   1 
ATOM   1492 C  CA  . ALA   A 1 208 ? 27.320  16.284  53.059 1.00 56.45  ?  215 ALA   A CA  1 
ATOM   1493 C  C   . ALA   A 1 208 ? 28.659  15.938  53.692 1.00 57.91  ?  215 ALA   A C   1 
ATOM   1494 O  O   . ALA   A 1 208 ? 29.715  16.303  53.178 1.00 55.03  ?  215 ALA   A O   1 
ATOM   1495 C  CB  . ALA   A 1 208 ? 26.695  17.430  53.824 1.00 62.06  ?  215 ALA   A CB  1 
ATOM   1496 N  N   . VAL   A 1 209 ? 28.600  15.221  54.805 1.00 55.90  ?  216 VAL   A N   1 
ATOM   1497 C  CA  . VAL   A 1 209 ? 29.815  14.797  55.511 1.00 55.92  ?  216 VAL   A CA  1 
ATOM   1498 C  C   . VAL   A 1 209 ? 30.521  13.662  54.738 1.00 58.55  ?  216 VAL   A C   1 
ATOM   1499 O  O   . VAL   A 1 209 ? 31.767  13.629  54.702 1.00 54.85  ?  216 VAL   A O   1 
ATOM   1500 C  CB  . VAL   A 1 209 ? 29.537  14.476  56.988 1.00 53.17  ?  216 VAL   A CB  1 
ATOM   1501 C  CG1 . VAL   A 1 209 ? 30.827  14.149  57.739 1.00 52.44  ?  216 VAL   A CG1 1 
ATOM   1502 C  CG2 . VAL   A 1 209 ? 28.896  15.694  57.672 1.00 53.76  ?  216 VAL   A CG2 1 
ATOM   1503 N  N   . VAL   A 1 210 ? 29.745  12.775  54.101 1.00 57.02  ?  217 VAL   A N   1 
ATOM   1504 C  CA  . VAL   A 1 210 ? 30.282  11.754  53.168 1.00 56.02  ?  217 VAL   A CA  1 
ATOM   1505 C  C   . VAL   A 1 210 ? 31.064  12.387  51.999 1.00 60.68  ?  217 VAL   A C   1 
ATOM   1506 O  O   . VAL   A 1 210 ? 32.087  11.816  51.577 1.00 62.18  ?  217 VAL   A O   1 
ATOM   1507 C  CB  . VAL   A 1 210 ? 29.177  10.773  52.638 1.00 57.47  ?  217 VAL   A CB  1 
ATOM   1508 C  CG1 . VAL   A 1 210 ? 29.690  9.829   51.552 1.00 56.10  ?  217 VAL   A CG1 1 
ATOM   1509 C  CG2 . VAL   A 1 210 ? 28.602  9.931   53.776 1.00 55.62  ?  217 VAL   A CG2 1 
ATOM   1510 N  N   . LEU   A 1 211 ? 30.602  13.538  51.494 1.00 49.88  ?  218 LEU   A N   1 
ATOM   1511 C  CA  . LEU   A 1 211 ? 31.305  14.259  50.412 1.00 56.76  ?  218 LEU   A CA  1 
ATOM   1512 C  C   . LEU   A 1 211 ? 32.680  14.688  50.858 1.00 53.11  ?  218 LEU   A C   1 
ATOM   1513 O  O   . LEU   A 1 211 ? 33.647  14.370  50.200 1.00 60.03  ?  218 LEU   A O   1 
ATOM   1514 C  CB  . LEU   A 1 211 ? 30.543  15.500  49.892 1.00 53.57  ?  218 LEU   A CB  1 
ATOM   1515 C  CG  . LEU   A 1 211 ? 29.254  15.333  49.097 1.00 58.43  ?  218 LEU   A CG  1 
ATOM   1516 C  CD1 . LEU   A 1 211 ? 28.659  16.685  48.739 1.00 68.28  ?  218 LEU   A CD1 1 
ATOM   1517 C  CD2 . LEU   A 1 211 ? 29.507  14.536  47.841 1.00 64.79  ?  218 LEU   A CD2 1 
ATOM   1518 N  N   . TRP   A 1 212 ? 32.734  15.410  51.975 1.00 55.95  ?  219 TRP   A N   1 
ATOM   1519 C  CA  . TRP   A 1 212 ? 33.993  15.807  52.640 1.00 52.41  ?  219 TRP   A CA  1 
ATOM   1520 C  C   . TRP   A 1 212 ? 34.999  14.655  52.797 1.00 50.08  ?  219 TRP   A C   1 
ATOM   1521 O  O   . TRP   A 1 212 ? 36.182  14.778  52.420 1.00 43.27  ?  219 TRP   A O   1 
ATOM   1522 C  CB  . TRP   A 1 212 ? 33.696  16.395  54.025 1.00 52.44  ?  219 TRP   A CB  1 
ATOM   1523 C  CG  . TRP   A 1 212 ? 34.882  16.953  54.672 1.00 55.22  ?  219 TRP   A CG  1 
ATOM   1524 C  CD1 . TRP   A 1 212 ? 35.331  18.228  54.570 1.00 60.37  ?  219 TRP   A CD1 1 
ATOM   1525 C  CD2 . TRP   A 1 212 ? 35.798  16.263  55.524 1.00 58.14  ?  219 TRP   A CD2 1 
ATOM   1526 N  NE1 . TRP   A 1 212 ? 36.476  18.382  55.292 1.00 58.07  ?  219 TRP   A NE1 1 
ATOM   1527 C  CE2 . TRP   A 1 212 ? 36.785  17.197  55.904 1.00 59.83  ?  219 TRP   A CE2 1 
ATOM   1528 C  CE3 . TRP   A 1 212 ? 35.882  14.944  56.008 1.00 56.27  ?  219 TRP   A CE3 1 
ATOM   1529 C  CZ2 . TRP   A 1 212 ? 37.864  16.853  56.738 1.00 67.50  ?  219 TRP   A CZ2 1 
ATOM   1530 C  CZ3 . TRP   A 1 212 ? 36.936  14.598  56.821 1.00 59.63  ?  219 TRP   A CZ3 1 
ATOM   1531 C  CH2 . TRP   A 1 212 ? 37.923  15.558  57.194 1.00 65.43  ?  219 TRP   A CH2 1 
ATOM   1532 N  N   . ALA   A 1 213 ? 34.505  13.551  53.365 1.00 47.23  ?  220 ALA   A N   1 
ATOM   1533 C  CA  . ALA   A 1 213 ? 35.275  12.327  53.553 1.00 48.99  ?  220 ALA   A CA  1 
ATOM   1534 C  C   . ALA   A 1 213 ? 35.865  11.792  52.265 1.00 52.18  ?  220 ALA   A C   1 
ATOM   1535 O  O   . ALA   A 1 213 ? 37.007  11.330  52.268 1.00 68.52  ?  220 ALA   A O   1 
ATOM   1536 C  CB  . ALA   A 1 213 ? 34.418  11.254  54.222 1.00 45.02  ?  220 ALA   A CB  1 
ATOM   1537 N  N   . ILE   A 1 214 ? 35.095  11.862  51.176 1.00 52.97  ?  221 ILE   A N   1 
ATOM   1538 C  CA  . ILE   A 1 214 ? 35.546  11.400  49.851 1.00 55.23  ?  221 ILE   A CA  1 
ATOM   1539 C  C   . ILE   A 1 214 ? 36.765  12.185  49.367 1.00 59.28  ?  221 ILE   A C   1 
ATOM   1540 O  O   . ILE   A 1 214 ? 37.664  11.582  48.795 1.00 59.26  ?  221 ILE   A O   1 
ATOM   1541 C  CB  . ILE   A 1 214 ? 34.383  11.366  48.806 1.00 57.39  ?  221 ILE   A CB  1 
ATOM   1542 C  CG1 . ILE   A 1 214 ? 33.469  10.161  49.084 1.00 57.18  ?  221 ILE   A CG1 1 
ATOM   1543 C  CG2 . ILE   A 1 214 ? 34.882  11.313  47.359 1.00 59.17  ?  221 ILE   A CG2 1 
ATOM   1544 C  CD1 . ILE   A 1 214 ? 32.062  10.328  48.557 1.00 54.25  ?  221 ILE   A CD1 1 
ATOM   1545 N  N   . PHE   A 1 215 ? 36.805  13.501  49.612 1.00 60.70  ?  222 PHE   A N   1 
ATOM   1546 C  CA  . PHE   A 1 215 ? 37.967  14.330  49.215 1.00 60.94  ?  222 PHE   A CA  1 
ATOM   1547 C  C   . PHE   A 1 215 ? 39.089  14.417  50.242 1.00 58.66  ?  222 PHE   A C   1 
ATOM   1548 O  O   . PHE   A 1 215 ? 40.216  14.730  49.867 1.00 83.27  ?  222 PHE   A O   1 
ATOM   1549 C  CB  . PHE   A 1 215 ? 37.495  15.696  48.719 1.00 64.77  ?  222 PHE   A CB  1 
ATOM   1550 C  CG  . PHE   A 1 215 ? 36.779  15.598  47.409 1.00 67.24  ?  222 PHE   A CG  1 
ATOM   1551 C  CD1 . PHE   A 1 215 ? 37.505  15.598  46.221 1.00 75.47  ?  222 PHE   A CD1 1 
ATOM   1552 C  CD2 . PHE   A 1 215 ? 35.407  15.393  47.352 1.00 63.65  ?  222 PHE   A CD2 1 
ATOM   1553 C  CE1 . PHE   A 1 215 ? 36.870  15.454  44.994 1.00 74.12  ?  222 PHE   A CE1 1 
ATOM   1554 C  CE2 . PHE   A 1 215 ? 34.760  15.237  46.129 1.00 63.28  ?  222 PHE   A CE2 1 
ATOM   1555 C  CZ  . PHE   A 1 215 ? 35.491  15.268  44.947 1.00 72.19  ?  222 PHE   A CZ  1 
ATOM   1556 N  N   . ALA   A 1 216 ? 38.792  14.115  51.505 1.00 56.87  ?  223 ALA   A N   1 
ATOM   1557 C  CA  . ALA   A 1 216 ? 39.794  14.055  52.566 1.00 57.75  ?  223 ALA   A CA  1 
ATOM   1558 C  C   . ALA   A 1 216 ? 40.529  12.720  52.691 1.00 62.46  ?  223 ALA   A C   1 
ATOM   1559 O  O   . ALA   A 1 216 ? 41.661  12.715  53.176 1.00 64.40  ?  223 ALA   A O   1 
ATOM   1560 C  CB  . ALA   A 1 216 ? 39.171  14.424  53.903 1.00 61.79  ?  223 ALA   A CB  1 
ATOM   1561 N  N   . ASN   A 1 217 ? 39.903  11.608  52.287 1.00 59.70  ?  224 ASN   A N   1 
ATOM   1562 C  CA  . ASN   A 1 217 ? 40.466  10.252  52.471 1.00 64.64  ?  224 ASN   A CA  1 
ATOM   1563 C  C   . ASN   A 1 217 ? 40.694  9.880   53.949 1.00 61.00  ?  224 ASN   A C   1 
ATOM   1564 O  O   . ASN   A 1 217 ? 41.678  9.192   54.284 1.00 58.92  ?  224 ASN   A O   1 
ATOM   1565 C  CB  . ASN   A 1 217 ? 41.774  10.053  51.643 1.00 69.39  ?  224 ASN   A CB  1 
ATOM   1566 C  CG  . ASN   A 1 217 ? 41.606  10.369  50.159 1.00 78.38  ?  224 ASN   A CG  1 
ATOM   1567 O  OD1 . ASN   A 1 217 ? 40.734  11.140  49.756 1.00 104.28 ?  224 ASN   A OD1 1 
ATOM   1568 N  ND2 . ASN   A 1 217 ? 42.459  9.775   49.334 1.00 84.45  ?  224 ASN   A ND2 1 
ATOM   1569 N  N   . LYS   A 1 218 ? 39.786  10.344  54.812 1.00 58.94  ?  225 LYS   A N   1 
ATOM   1570 C  CA  . LYS   A 1 218 ? 39.855  10.122  56.267 1.00 64.16  ?  225 LYS   A CA  1 
ATOM   1571 C  C   . LYS   A 1 218 ? 38.572  10.562  56.967 1.00 70.06  ?  225 LYS   A C   1 
ATOM   1572 O  O   . LYS   A 1 218 ? 37.738  11.297  56.395 1.00 68.87  ?  225 LYS   A O   1 
ATOM   1573 C  CB  . LYS   A 1 218 ? 41.065  10.843  56.900 1.00 71.76  ?  225 LYS   A CB  1 
ATOM   1574 C  CG  . LYS   A 1 218 ? 41.128  12.356  56.688 1.00 74.75  ?  225 LYS   A CG  1 
ATOM   1575 C  CD  . LYS   A 1 218 ? 42.497  12.907  57.086 1.00 87.70  ?  225 LYS   A CD  1 
ATOM   1576 C  CE  . LYS   A 1 218 ? 42.544  14.429  57.203 1.00 90.29  ?  225 LYS   A CE  1 
ATOM   1577 N  NZ  . LYS   A 1 218 ? 43.763  14.930  57.855 0.00 90.76  ?  225 LYS   A NZ  1 
ATOM   1578 N  N   . GLU   A 1 219 ? 38.424  10.092  58.205 1.00 72.81  ?  226 GLU   A N   1 
ATOM   1579 C  CA  . GLU   A 1 219 ? 37.294  10.473  59.051 1.00 74.38  ?  226 GLU   A CA  1 
ATOM   1580 C  C   . GLU   A 1 219 ? 37.451  11.937  59.499 1.00 70.63  ?  226 GLU   A C   1 
ATOM   1581 O  O   . GLU   A 1 219 ? 38.587  12.388  59.710 1.00 73.27  ?  226 GLU   A O   1 
ATOM   1582 C  CB  . GLU   A 1 219 ? 37.176  9.549   60.273 1.00 75.17  ?  226 GLU   A CB  1 
ATOM   1583 C  CG  . GLU   A 1 219 ? 36.811  8.105   59.942 1.00 77.77  ?  226 GLU   A CG  1 
ATOM   1584 C  CD  . GLU   A 1 219 ? 35.376  7.882   59.455 1.00 81.06  ?  226 GLU   A CD  1 
ATOM   1585 O  OE1 . GLU   A 1 219 ? 35.124  6.844   58.799 1.00 88.85  ?  226 GLU   A OE1 1 
ATOM   1586 O  OE2 . GLU   A 1 219 ? 34.488  8.714   59.724 1.00 88.02  ?  226 GLU   A OE2 1 
ATOM   1587 N  N   . PRO   A 1 220 ? 36.330  12.688  59.598 1.00 66.60  ?  227 PRO   A N   1 
ATOM   1588 C  CA  . PRO   A 1 220 ? 36.425  14.072  60.107 1.00 58.08  ?  227 PRO   A CA  1 
ATOM   1589 C  C   . PRO   A 1 220 ? 36.707  14.214  61.601 1.00 65.69  ?  227 PRO   A C   1 
ATOM   1590 O  O   . PRO   A 1 220 ? 36.641  13.240  62.360 1.00 68.02  ?  227 PRO   A O   1 
ATOM   1591 C  CB  . PRO   A 1 220 ? 35.053  14.660  59.777 1.00 54.65  ?  227 PRO   A CB  1 
ATOM   1592 C  CG  . PRO   A 1 220 ? 34.149  13.479  59.851 1.00 59.42  ?  227 PRO   A CG  1 
ATOM   1593 C  CD  . PRO   A 1 220 ? 34.941  12.371  59.192 1.00 58.67  ?  227 PRO   A CD  1 
ATOM   1594 N  N   . TYR   A 1 221 ? 37.075  15.443  61.978 1.00 72.15  ?  228 TYR   A N   1 
ATOM   1595 C  CA  . TYR   A 1 221 ? 37.235  15.883  63.368 1.00 70.05  ?  228 TYR   A CA  1 
ATOM   1596 C  C   . TYR   A 1 221 ? 38.349  15.179  64.162 1.00 71.82  ?  228 TYR   A C   1 
ATOM   1597 O  O   . TYR   A 1 221 ? 38.213  15.015  65.392 1.00 65.47  ?  228 TYR   A O   1 
ATOM   1598 C  CB  . TYR   A 1 221 ? 35.904  15.753  64.135 1.00 64.48  ?  228 TYR   A CB  1 
ATOM   1599 C  CG  . TYR   A 1 221 ? 34.697  16.373  63.498 1.00 65.85  ?  228 TYR   A CG  1 
ATOM   1600 C  CD1 . TYR   A 1 221 ? 34.586  17.763  63.362 1.00 65.72  ?  228 TYR   A CD1 1 
ATOM   1601 C  CD2 . TYR   A 1 221 ? 33.607  15.578  63.097 1.00 62.75  ?  228 TYR   A CD2 1 
ATOM   1602 C  CE1 . TYR   A 1 221 ? 33.438  18.342  62.810 1.00 67.70  ?  228 TYR   A CE1 1 
ATOM   1603 C  CE2 . TYR   A 1 221 ? 32.467  16.142  62.544 1.00 58.11  ?  228 TYR   A CE2 1 
ATOM   1604 C  CZ  . TYR   A 1 221 ? 32.376  17.512  62.399 1.00 61.88  ?  228 TYR   A CZ  1 
ATOM   1605 O  OH  . TYR   A 1 221 ? 31.238  18.046  61.850 1.00 55.82  ?  228 TYR   A OH  1 
ATOM   1606 N  N   . GLU   A 1 222 ? 39.445  14.799  63.489 1.00 83.07  ?  229 GLU   A N   1 
ATOM   1607 C  CA  . GLU   A 1 222 ? 40.565  14.083  64.143 1.00 92.43  ?  229 GLU   A CA  1 
ATOM   1608 C  C   . GLU   A 1 222 ? 41.148  14.805  65.380 1.00 104.01 ?  229 GLU   A C   1 
ATOM   1609 O  O   . GLU   A 1 222 ? 41.503  14.146  66.362 1.00 119.24 ?  229 GLU   A O   1 
ATOM   1610 C  CB  . GLU   A 1 222 ? 41.680  13.770  63.133 1.00 99.66  ?  229 GLU   A CB  1 
ATOM   1611 C  CG  . GLU   A 1 222 ? 42.468  14.984  62.641 1.00 108.21 ?  229 GLU   A CG  1 
ATOM   1612 C  CD  . GLU   A 1 222 ? 43.173  14.761  61.309 1.00 105.36 ?  229 GLU   A CD  1 
ATOM   1613 O  OE1 . GLU   A 1 222 ? 44.314  15.238  61.161 1.00 97.43  ?  229 GLU   A OE1 1 
ATOM   1614 O  OE2 . GLU   A 1 222 ? 42.589  14.121  60.406 1.00 96.65  ?  229 GLU   A OE2 1 
ATOM   1615 N  N   . ASN   A 1 223 ? 41.217  16.142  65.320 1.00 105.42 ?  230 ASN   A N   1 
ATOM   1616 C  CA  . ASN   A 1 223 ? 41.780  16.983  66.411 1.00 109.39 ?  230 ASN   A CA  1 
ATOM   1617 C  C   . ASN   A 1 223 ? 40.840  17.282  67.608 1.00 102.78 ?  230 ASN   A C   1 
ATOM   1618 O  O   . ASN   A 1 223 ? 41.287  17.891  68.583 1.00 97.27  ?  230 ASN   A O   1 
ATOM   1619 C  CB  . ASN   A 1 223 ? 42.330  18.306  65.841 1.00 99.03  ?  230 ASN   A CB  1 
ATOM   1620 C  CG  . ASN   A 1 223 ? 41.365  19.254  65.340 0.00 100.04 ?  230 ASN   A CG  1 
ATOM   1621 O  OD1 . ASN   A 1 223 ? 40.323  18.859  64.814 0.00 96.31  ?  230 ASN   A OD1 1 
ATOM   1622 N  ND2 . ASN   A 1 223 ? 41.654  20.548  65.465 0.00 101.89 ?  230 ASN   A ND2 1 
ATOM   1623 N  N   . ALA   A 1 224 ? 39.563  16.888  67.544 1.00 100.00 ?  231 ALA   A N   1 
ATOM   1624 C  CA  . ALA   A 1 224 ? 38.658  16.981  68.719 1.00 99.54  ?  231 ALA   A CA  1 
ATOM   1625 C  C   . ALA   A 1 224 ? 39.124  16.037  69.839 1.00 103.71 ?  231 ALA   A C   1 
ATOM   1626 O  O   . ALA   A 1 224 ? 39.625  14.938  69.553 1.00 97.53  ?  231 ALA   A O   1 
ATOM   1627 C  CB  . ALA   A 1 224 ? 37.218  16.680  68.327 1.00 93.08  ?  231 ALA   A CB  1 
ATOM   1628 N  N   . ILE   A 1 225 ? 38.953  16.471  71.097 1.00 110.15 ?  232 ILE   A N   1 
ATOM   1629 C  CA  . ILE   A 1 225 ? 39.459  15.756  72.297 1.00 120.36 ?  232 ILE   A CA  1 
ATOM   1630 C  C   . ILE   A 1 225 ? 38.373  15.205  73.259 1.00 115.36 ?  232 ILE   A C   1 
ATOM   1631 O  O   . ILE   A 1 225 ? 38.724  14.492  74.199 1.00 117.45 ?  232 ILE   A O   1 
ATOM   1632 C  CB  . ILE   A 1 225 ? 40.546  16.628  73.029 1.00 139.61 ?  232 ILE   A CB  1 
ATOM   1633 C  CG1 . ILE   A 1 225 ? 41.614  15.758  73.724 1.00 143.26 ?  232 ILE   A CG1 1 
ATOM   1634 C  CG2 . ILE   A 1 225 ? 39.941  17.661  73.989 1.00 138.65 ?  232 ILE   A CG2 1 
ATOM   1635 C  CD1 . ILE   A 1 225 ? 42.525  14.969  72.785 0.00 143.86 ?  232 ILE   A CD1 1 
ATOM   1636 N  N   . ALA   A 1 226 ? 37.089  15.556  73.071 1.00 112.25 ?  233 ALA   A N   1 
ATOM   1637 C  CA  . ALA   A 1 226 ? 35.964  14.976  73.857 1.00 117.79 ?  233 ALA   A CA  1 
ATOM   1638 C  C   . ALA   A 1 226 ? 34.704  14.846  73.015 1.00 126.15 ?  233 ALA   A C   1 
ATOM   1639 O  O   . ALA   A 1 226 ? 34.542  15.550  72.009 1.00 132.98 ?  233 ALA   A O   1 
ATOM   1640 C  CB  . ALA   A 1 226 ? 35.656  15.803  75.110 1.00 123.24 ?  233 ALA   A CB  1 
ATOM   1641 N  N   . GLU   A 1 227 ? 33.806  13.965  73.464 1.00 127.10 ?  234 GLU   A N   1 
ATOM   1642 C  CA  . GLU   A 1 227 ? 32.534  13.702  72.778 1.00 116.15 ?  234 GLU   A CA  1 
ATOM   1643 C  C   . GLU   A 1 227 ? 31.572  14.876  72.970 1.00 101.08 ?  234 GLU   A C   1 
ATOM   1644 O  O   . GLU   A 1 227 ? 31.045  15.412  71.991 1.00 89.56  ?  234 GLU   A O   1 
ATOM   1645 C  CB  . GLU   A 1 227 ? 31.892  12.399  73.279 1.00 129.15 ?  234 GLU   A CB  1 
ATOM   1646 C  CG  . GLU   A 1 227 ? 32.612  11.132  72.847 1.00 137.95 ?  234 GLU   A CG  1 
ATOM   1647 C  CD  . GLU   A 1 227 ? 32.203  10.664  71.461 1.00 134.77 ?  234 GLU   A CD  1 
ATOM   1648 O  OE1 . GLU   A 1 227 ? 31.486  9.642   71.367 1.00 144.67 ?  234 GLU   A OE1 1 
ATOM   1649 O  OE2 . GLU   A 1 227 ? 32.589  11.325  70.471 1.00 118.45 ?  234 GLU   A OE2 1 
ATOM   1650 N  N   . GLN   A 1 228 ? 31.343  15.238  74.234 1.00 93.52  ?  235 GLN   A N   1 
ATOM   1651 C  CA  . GLN   A 1 228 ? 30.425  16.334  74.604 1.00 98.26  ?  235 GLN   A CA  1 
ATOM   1652 C  C   . GLN   A 1 228 ? 30.874  17.714  74.079 1.00 94.93  ?  235 GLN   A C   1 
ATOM   1653 O  O   . GLN   A 1 228 ? 30.026  18.528  73.686 1.00 82.75  ?  235 GLN   A O   1 
ATOM   1654 C  CB  . GLN   A 1 228 ? 30.220  16.378  76.128 1.00 103.28 ?  235 GLN   A CB  1 
ATOM   1655 C  CG  . GLN   A 1 228 ? 29.170  17.367  76.628 1.00 108.07 ?  235 GLN   A CG  1 
ATOM   1656 C  CD  . GLN   A 1 228 ? 27.822  17.252  76.102 0.00 104.64 ?  235 GLN   A CD  1 
ATOM   1657 O  OE1 . GLN   A 1 228 ? 27.384  16.159  75.732 0.00 103.09 ?  235 GLN   A OE1 1 
ATOM   1658 N  NE2 . GLN   A 1 228 ? 27.084  18.361  76.070 0.00 104.52 ?  235 GLN   A NE2 1 
ATOM   1659 N  N   . GLN   A 1 229 ? 32.186  17.959  74.072 1.00 92.81  ?  236 GLN   A N   1 
ATOM   1660 C  CA  . GLN   A 1 229 ? 32.747  19.163  73.443 1.00 94.05  ?  236 GLN   A CA  1 
ATOM   1661 C  C   . GLN   A 1 229 ? 32.397  19.221  71.954 1.00 88.73  ?  236 GLN   A C   1 
ATOM   1662 O  O   . GLN   A 1 229 ? 31.896  20.247  71.470 1.00 97.37  ?  236 GLN   A O   1 
ATOM   1663 C  CB  . GLN   A 1 229 ? 34.262  19.221  73.624 1.00 96.71  ?  236 GLN   A CB  1 
ATOM   1664 C  CG  . GLN   A 1 229 ? 34.697  19.480  75.060 1.00 101.14 ?  236 GLN   A CG  1 
ATOM   1665 C  CD  . GLN   A 1 229 ? 36.200  19.801  75.156 0.00 106.79 ?  236 GLN   A CD  1 
ATOM   1666 O  OE1 . GLN   A 1 229 ? 37.007  19.222  74.432 0.00 106.16 ?  236 GLN   A OE1 1 
ATOM   1667 N  NE2 . GLN   A 1 229 ? 36.572  20.696  76.070 0.00 110.17 ?  236 GLN   A NE2 1 
ATOM   1668 N  N   . LEU   A 1 230 ? 32.646  18.110  71.258 1.00 80.40  ?  237 LEU   A N   1 
ATOM   1669 C  CA  . LEU   A 1 230 ? 32.402  18.002  69.809 1.00 71.62  ?  237 LEU   A CA  1 
ATOM   1670 C  C   . LEU   A 1 230 ? 30.919  18.073  69.416 1.00 72.37  ?  237 LEU   A C   1 
ATOM   1671 O  O   . LEU   A 1 230 ? 30.567  18.739  68.437 1.00 70.65  ?  237 LEU   A O   1 
ATOM   1672 C  CB  . LEU   A 1 230 ? 33.023  16.715  69.257 1.00 73.52  ?  237 LEU   A CB  1 
ATOM   1673 C  CG  . LEU   A 1 230 ? 32.891  16.367  67.759 1.00 70.33  ?  237 LEU   A CG  1 
ATOM   1674 C  CD1 . LEU   A 1 230 ? 33.371  17.507  66.873 1.00 76.12  ?  237 LEU   A CD1 1 
ATOM   1675 C  CD2 . LEU   A 1 230 ? 33.657  15.093  67.448 1.00 66.28  ?  237 LEU   A CD2 1 
ATOM   1676 N  N   . ILE   A 1 231 ? 30.068  17.366  70.159 1.00 73.36  ?  238 ILE   A N   1 
ATOM   1677 C  CA  . ILE   A 1 231 ? 28.609  17.361  69.944 1.00 72.72  ?  238 ILE   A CA  1 
ATOM   1678 C  C   . ILE   A 1 231 ? 28.064  18.776  70.004 1.00 73.89  ?  238 ILE   A C   1 
ATOM   1679 O  O   . ILE   A 1 231 ? 27.392  19.215  69.065 1.00 78.33  ?  238 ILE   A O   1 
ATOM   1680 C  CB  . ILE   A 1 231 ? 27.869  16.450  70.970 1.00 79.06  ?  238 ILE   A CB  1 
ATOM   1681 C  CG1 . ILE   A 1 231 ? 28.090  14.969  70.613 1.00 73.16  ?  238 ILE   A CG1 1 
ATOM   1682 C  CG2 . ILE   A 1 231 ? 26.356  16.722  71.022 1.00 82.06  ?  238 ILE   A CG2 1 
ATOM   1683 C  CD1 . ILE   A 1 231 ? 27.889  14.011  71.768 1.00 69.17  ?  238 ILE   A CD1 1 
ATOM   1684 N  N   . MET   A 1 232 ? 28.343  19.459  71.111 1.00 75.42  ?  239 MET   A N   1 
ATOM   1685 C  CA  . MET   A 1 232 ? 27.886  20.856  71.309 1.00 80.47  ?  239 MET   A CA  1 
ATOM   1686 C  C   . MET   A 1 232 ? 28.482  21.831  70.283 1.00 74.72  ?  239 MET   A C   1 
ATOM   1687 O  O   . MET   A 1 232 ? 27.790  22.745  69.829 1.00 80.62  ?  239 MET   A O   1 
ATOM   1688 C  CB  . MET   A 1 232 ? 28.150  21.340  72.746 1.00 85.28  ?  239 MET   A CB  1 
ATOM   1689 C  CG  . MET   A 1 232 ? 27.357  20.588  73.814 1.00 87.98  ?  239 MET   A CG  1 
ATOM   1690 S  SD  . MET   A 1 232 ? 25.590  20.953  73.805 1.00 95.68  ?  239 MET   A SD  1 
ATOM   1691 C  CE  . MET   A 1 232 ? 25.563  22.620  74.474 1.00 100.49 ?  239 MET   A CE  1 
ATOM   1692 N  N   . ALA   A 1 233 ? 29.749  21.627  69.915 1.00 72.74  ?  240 ALA   A N   1 
ATOM   1693 C  CA  . ALA   A 1 233 ? 30.402  22.362  68.820 1.00 69.83  ?  240 ALA   A CA  1 
ATOM   1694 C  C   . ALA   A 1 233 ? 29.638  22.224  67.502 1.00 71.19  ?  240 ALA   A C   1 
ATOM   1695 O  O   . ALA   A 1 233 ? 29.342  23.216  66.846 1.00 71.96  ?  240 ALA   A O   1 
ATOM   1696 C  CB  . ALA   A 1 233 ? 31.837  21.886  68.645 1.00 67.89  ?  240 ALA   A CB  1 
ATOM   1697 N  N   . ILE   A 1 234 ? 29.301  20.986  67.142 1.00 70.96  ?  241 ILE   A N   1 
ATOM   1698 C  CA  . ILE   A 1 234 ? 28.524  20.687  65.935 1.00 63.29  ?  241 ILE   A CA  1 
ATOM   1699 C  C   . ILE   A 1 234 ? 27.115  21.313  65.984 1.00 62.80  ?  241 ILE   A C   1 
ATOM   1700 O  O   . ILE   A 1 234 ? 26.668  21.889  64.998 1.00 63.58  ?  241 ILE   A O   1 
ATOM   1701 C  CB  . ILE   A 1 234 ? 28.509  19.160  65.617 1.00 62.25  ?  241 ILE   A CB  1 
ATOM   1702 C  CG1 . ILE   A 1 234 ? 29.924  18.686  65.250 1.00 59.42  ?  241 ILE   A CG1 1 
ATOM   1703 C  CG2 . ILE   A 1 234 ? 27.564  18.815  64.460 1.00 59.83  ?  241 ILE   A CG2 1 
ATOM   1704 C  CD1 . ILE   A 1 234 ? 30.175  17.214  65.487 1.00 65.12  ?  241 ILE   A CD1 1 
ATOM   1705 N  N   . LYS   A 1 235 ? 26.430  21.178  67.117 1.00 63.60  ?  242 LYS   A N   1 
ATOM   1706 C  CA  . LYS   A 1 235 ? 25.107  21.803  67.340 1.00 58.80  ?  242 LYS   A CA  1 
ATOM   1707 C  C   . LYS   A 1 235 ? 25.093  23.325  67.195 1.00 69.07  ?  242 LYS   A C   1 
ATOM   1708 O  O   . LYS   A 1 235 ? 24.082  23.888  66.770 1.00 67.30  ?  242 LYS   A O   1 
ATOM   1709 C  CB  . LYS   A 1 235 ? 24.527  21.400  68.700 1.00 57.98  ?  242 LYS   A CB  1 
ATOM   1710 C  CG  . LYS   A 1 235 ? 24.004  19.968  68.723 1.00 61.13  ?  242 LYS   A CG  1 
ATOM   1711 C  CD  . LYS   A 1 235 ? 23.257  19.645  70.012 1.00 60.82  ?  242 LYS   A CD  1 
ATOM   1712 C  CE  . LYS   A 1 235 ? 21.828  20.193  70.044 1.00 69.03  ?  242 LYS   A CE  1 
ATOM   1713 N  NZ  . LYS   A 1 235 ? 20.863  19.623  69.055 1.00 66.86  ?  242 LYS   A NZ  1 
ATOM   1714 N  N   . SER   A 1 236 ? 26.211  23.967  67.554 1.00 72.78  ?  243 SER   A N   1 
ATOM   1715 C  CA  . SER   A 1 236 ? 26.426  25.403  67.387 1.00 74.38  ?  243 SER   A CA  1 
ATOM   1716 C  C   . SER   A 1 236 ? 27.196  25.767  66.092 1.00 77.16  ?  243 SER   A C   1 
ATOM   1717 O  O   . SER   A 1 236 ? 27.986  26.719  66.079 1.00 74.76  ?  243 SER   A O   1 
ATOM   1718 C  CB  . SER   A 1 236 ? 27.190  25.928  68.617 1.00 77.68  ?  243 SER   A CB  1 
ATOM   1719 O  OG  . SER   A 1 236 ? 28.550  25.537  68.575 1.00 69.27  ?  243 SER   A OG  1 
ATOM   1720 N  N   . GLY   A 1 237 ? 27.015  24.983  65.024 1.00 74.69  ?  244 GLY   A N   1 
ATOM   1721 C  CA  . GLY   A 1 237 ? 27.485  25.340  63.686 1.00 79.95  ?  244 GLY   A CA  1 
ATOM   1722 C  C   . GLY   A 1 237 ? 28.815  24.809  63.175 1.00 78.16  ?  244 GLY   A C   1 
ATOM   1723 O  O   . GLY   A 1 237 ? 29.048  24.914  61.979 1.00 77.79  ?  244 GLY   A O   1 
ATOM   1724 N  N   . ASN   A 1 238 ? 29.682  24.252  64.036 1.00 86.21  ?  245 ASN   A N   1 
ATOM   1725 C  CA  . ASN   A 1 238 ? 31.021  23.760  63.585 1.00 73.65  ?  245 ASN   A CA  1 
ATOM   1726 C  C   . ASN   A 1 238 ? 30.886  22.498  62.718 1.00 74.75  ?  245 ASN   A C   1 
ATOM   1727 O  O   . ASN   A 1 238 ? 30.023  21.646  62.976 1.00 60.35  ?  245 ASN   A O   1 
ATOM   1728 C  CB  . ASN   A 1 238 ? 31.970  23.532  64.774 1.00 74.03  ?  245 ASN   A CB  1 
ATOM   1729 C  CG  . ASN   A 1 238 ? 32.315  24.843  65.509 1.00 92.74  ?  245 ASN   A CG  1 
ATOM   1730 O  OD1 . ASN   A 1 238 ? 31.813  25.105  66.609 1.00 102.51 ?  245 ASN   A OD1 1 
ATOM   1731 N  ND2 . ASN   A 1 238 ? 33.134  25.694  64.874 1.00 83.63  ?  245 ASN   A ND2 1 
ATOM   1732 N  N   . ARG   A 1 239 ? 31.732  22.404  61.686 1.00 68.64  ?  246 ARG   A N   1 
ATOM   1733 C  CA  . ARG   A 1 239 ? 31.616  21.398  60.599 1.00 58.08  ?  246 ARG   A CA  1 
ATOM   1734 C  C   . ARG   A 1 239 ? 33.012  20.839  60.268 1.00 63.71  ?  246 ARG   A C   1 
ATOM   1735 O  O   . ARG   A 1 239 ? 34.010  21.348  60.816 1.00 69.69  ?  246 ARG   A O   1 
ATOM   1736 C  CB  . ARG   A 1 239 ? 31.021  22.068  59.355 1.00 53.81  ?  246 ARG   A CB  1 
ATOM   1737 C  CG  . ARG   A 1 239 ? 29.603  22.541  59.519 1.00 56.39  ?  246 ARG   A CG  1 
ATOM   1738 C  CD  . ARG   A 1 239 ? 28.623  21.349  59.582 1.00 60.12  ?  246 ARG   A CD  1 
ATOM   1739 N  NE  . ARG   A 1 239 ? 27.236  21.821  59.680 1.00 53.29  ?  246 ARG   A NE  1 
ATOM   1740 C  CZ  . ARG   A 1 239 ? 26.559  22.067  60.806 1.00 52.32  ?  246 ARG   A CZ  1 
ATOM   1741 N  NH1 . ARG   A 1 239 ? 27.094  21.871  62.023 1.00 56.41  ?  246 ARG   A NH1 1 
ATOM   1742 N  NH2 . ARG   A 1 239 ? 25.303  22.509  60.710 1.00 57.20  ?  246 ARG   A NH2 1 
ATOM   1743 N  N   . PRO   A 1 240 ? 33.097  19.792  59.402 1.00 53.85  ?  247 PRO   A N   1 
ATOM   1744 C  CA  . PRO   A 1 240 ? 34.403  19.278  59.001 1.00 59.99  ?  247 PRO   A CA  1 
ATOM   1745 C  C   . PRO   A 1 240 ? 35.305  20.319  58.344 1.00 60.27  ?  247 PRO   A C   1 
ATOM   1746 O  O   . PRO   A 1 240 ? 34.816  21.225  57.647 1.00 63.90  ?  247 PRO   A O   1 
ATOM   1747 C  CB  . PRO   A 1 240 ? 34.035  18.172  58.002 1.00 56.18  ?  247 PRO   A CB  1 
ATOM   1748 C  CG  . PRO   A 1 240 ? 32.755  17.659  58.517 1.00 61.56  ?  247 PRO   A CG  1 
ATOM   1749 C  CD  . PRO   A 1 240 ? 32.033  18.930  58.848 1.00 64.79  ?  247 PRO   A CD  1 
ATOM   1750 N  N   . ASP   A 1 241 ? 36.600  20.187  58.575 1.00 65.28  ?  248 ASP   A N   1 
ATOM   1751 C  CA  . ASP   A 1 241 ? 37.552  21.221  58.185 1.00 70.08  ?  248 ASP   A CA  1 
ATOM   1752 C  C   . ASP   A 1 241 ? 37.843  21.153  56.686 1.00 69.93  ?  248 ASP   A C   1 
ATOM   1753 O  O   . ASP   A 1 241 ? 38.409  20.176  56.206 1.00 78.93  ?  248 ASP   A O   1 
ATOM   1754 C  CB  . ASP   A 1 241 ? 38.843  21.101  58.996 1.00 68.06  ?  248 ASP   A CB  1 
ATOM   1755 C  CG  . ASP   A 1 241 ? 39.782  22.284  58.797 1.00 72.54  ?  248 ASP   A CG  1 
ATOM   1756 O  OD1 . ASP   A 1 241 ? 39.339  23.382  58.396 1.00 77.74  ?  248 ASP   A OD1 1 
ATOM   1757 O  OD2 . ASP   A 1 241 ? 40.990  22.123  59.078 1.00 71.01  ?  248 ASP   A OD2 1 
ATOM   1758 N  N   . VAL   A 1 242 ? 37.411  22.171  55.948 1.00 72.08  ?  249 VAL   A N   1 
ATOM   1759 C  CA  . VAL   A 1 242 ? 37.604  22.260  54.488 1.00 72.14  ?  249 VAL   A CA  1 
ATOM   1760 C  C   . VAL   A 1 242 ? 39.104  22.448  54.115 1.00 84.42  ?  249 VAL   A C   1 
ATOM   1761 O  O   . VAL   A 1 242 ? 39.525  22.027  53.038 1.00 83.59  ?  249 VAL   A O   1 
ATOM   1762 C  CB  . VAL   A 1 242 ? 36.696  23.379  53.885 1.00 76.36  ?  249 VAL   A CB  1 
ATOM   1763 C  CG1 . VAL   A 1 242 ? 36.891  23.541  52.379 1.00 77.74  ?  249 VAL   A CG1 1 
ATOM   1764 C  CG2 . VAL   A 1 242 ? 35.224  23.070  54.156 1.00 76.02  ?  249 VAL   A CG2 1 
ATOM   1765 N  N   . ASP   A 1 243 ? 39.899  23.082  54.985 1.00 87.49  ?  250 ASP   A N   1 
ATOM   1766 C  CA  . ASP   A 1 243 ? 41.370  23.187  54.791 1.00 97.46  ?  250 ASP   A CA  1 
ATOM   1767 C  C   . ASP   A 1 243 ? 42.147  21.850  54.929 1.00 97.83  ?  250 ASP   A C   1 
ATOM   1768 O  O   . ASP   A 1 243 ? 43.286  21.744  54.450 1.00 97.01  ?  250 ASP   A O   1 
ATOM   1769 C  CB  . ASP   A 1 243 ? 41.973  24.241  55.733 1.00 100.03 ?  250 ASP   A CB  1 
ATOM   1770 C  CG  . ASP   A 1 243 ? 41.456  25.648  55.460 1.00 99.22  ?  250 ASP   A CG  1 
ATOM   1771 O  OD1 . ASP   A 1 243 ? 41.348  26.045  54.279 1.00 93.98  ?  250 ASP   A OD1 1 
ATOM   1772 O  OD2 . ASP   A 1 243 ? 41.169  26.368  56.439 1.00 108.15 ?  250 ASP   A OD2 1 
ATOM   1773 N  N   . ASP   A 1 244 ? 41.543  20.855  55.592 1.00 103.79 ?  251 ASP   A N   1 
ATOM   1774 C  CA  . ASP   A 1 244 ? 42.049  19.447  55.614 1.00 101.72 ?  251 ASP   A CA  1 
ATOM   1775 C  C   . ASP   A 1 244 ? 42.019  18.737  54.239 1.00 103.36 ?  251 ASP   A C   1 
ATOM   1776 O  O   . ASP   A 1 244 ? 42.690  17.716  54.078 1.00 121.42 ?  251 ASP   A O   1 
ATOM   1777 C  CB  . ASP   A 1 244 ? 41.290  18.552  56.656 1.00 105.90 ?  251 ASP   A CB  1 
ATOM   1778 C  CG  . ASP   A 1 244 ? 42.081  18.283  57.936 1.00 113.36 ?  251 ASP   A CG  1 
ATOM   1779 O  OD1 . ASP   A 1 244 ? 43.325  18.161  57.888 1.00 128.84 ?  251 ASP   A OD1 1 
ATOM   1780 O  OD2 . ASP   A 1 244 ? 41.427  18.142  58.999 1.00 113.26 ?  251 ASP   A OD2 1 
ATOM   1781 N  N   . ILE   A 1 245 ? 41.231  19.255  53.287 1.00 96.68  ?  252 ILE   A N   1 
ATOM   1782 C  CA  . ILE   A 1 245 ? 41.264  18.803  51.890 1.00 92.19  ?  252 ILE   A CA  1 
ATOM   1783 C  C   . ILE   A 1 245 ? 42.575  19.309  51.246 1.00 106.23 ?  252 ILE   A C   1 
ATOM   1784 O  O   . ILE   A 1 245 ? 42.670  20.486  50.866 1.00 98.94  ?  252 ILE   A O   1 
ATOM   1785 C  CB  . ILE   A 1 245 ? 40.000  19.282  51.097 1.00 88.80  ?  252 ILE   A CB  1 
ATOM   1786 C  CG1 . ILE   A 1 245 ? 38.713  18.644  51.655 1.00 82.38  ?  252 ILE   A CG1 1 
ATOM   1787 C  CG2 . ILE   A 1 245 ? 40.106  18.962  49.612 1.00 92.55  ?  252 ILE   A CG2 1 
ATOM   1788 C  CD1 . ILE   A 1 245 ? 37.437  19.391  51.305 1.00 75.50  ?  252 ILE   A CD1 1 
ATOM   1789 N  N   . THR   A 1 246 ? 43.576  18.418  51.157 1.00 114.54 ?  253 THR   A N   1 
ATOM   1790 C  CA  . THR   A 1 246 ? 44.804  18.621  50.347 1.00 113.44 ?  253 THR   A CA  1 
ATOM   1791 C  C   . THR   A 1 246 ? 44.857  17.696  49.089 1.00 113.10 ?  253 THR   A C   1 
ATOM   1792 O  O   . THR   A 1 246 ? 45.907  17.172  48.715 1.00 109.55 ?  253 THR   A O   1 
ATOM   1793 C  CB  . THR   A 1 246 ? 46.060  18.441  51.226 1.00 115.04 ?  253 THR   A CB  1 
ATOM   1794 O  OG1 . THR   A 1 246 ? 46.052  17.129  51.802 1.00 118.57 ?  253 THR   A OG1 1 
ATOM   1795 C  CG2 . THR   A 1 246 ? 46.097  19.492  52.332 1.00 109.94 ?  253 THR   A CG2 1 
ATOM   1796 N  N   . GLU   A 1 247 ? 43.695  17.473  48.484 1.00 118.29 ?  254 GLU   A N   1 
ATOM   1797 C  CA  . GLU   A 1 247 ? 43.537  17.051  47.097 1.00 120.29 ?  254 GLU   A CA  1 
ATOM   1798 C  C   . GLU   A 1 247 ? 42.689  18.125  46.401 1.00 113.35 ?  254 GLU   A C   1 
ATOM   1799 O  O   . GLU   A 1 247 ? 42.057  18.977  47.052 1.00 111.90 ?  254 GLU   A O   1 
ATOM   1800 C  CB  . GLU   A 1 247 ? 42.817  15.700  47.078 1.00 126.75 ?  254 GLU   A CB  1 
ATOM   1801 C  CG  . GLU   A 1 247 ? 42.550  15.049  45.723 1.00 128.96 ?  254 GLU   A CG  1 
ATOM   1802 C  CD  . GLU   A 1 247 ? 41.726  13.784  45.851 1.00 119.05 ?  254 GLU   A CD  1 
ATOM   1803 O  OE1 . GLU   A 1 247 ? 42.107  12.901  46.652 1.00 109.65 ?  254 GLU   A OE1 1 
ATOM   1804 O  OE2 . GLU   A 1 247 ? 40.682  13.664  45.162 1.00 100.81 ?  254 GLU   A OE2 1 
ATOM   1805 N  N   . TYR   A 1 248 ? 42.650  18.106  45.072 1.00 111.48 ?  255 TYR   A N   1 
ATOM   1806 C  CA  . TYR   A 1 248 ? 41.678  18.940  44.336 1.00 103.04 ?  255 TYR   A CA  1 
ATOM   1807 C  C   . TYR   A 1 248 ? 40.252  18.401  44.541 1.00 88.23  ?  255 TYR   A C   1 
ATOM   1808 O  O   . TYR   A 1 248 ? 39.868  17.411  43.924 1.00 79.77  ?  255 TYR   A O   1 
ATOM   1809 C  CB  . TYR   A 1 248 ? 42.009  19.066  42.842 1.00 110.03 ?  255 TYR   A CB  1 
ATOM   1810 C  CG  . TYR   A 1 248 ? 41.044  19.971  42.079 1.00 112.74 ?  255 TYR   A CG  1 
ATOM   1811 C  CD1 . TYR   A 1 248 ? 40.932  21.341  42.387 1.00 121.59 ?  255 TYR   A CD1 1 
ATOM   1812 C  CD2 . TYR   A 1 248 ? 40.248  19.468  41.037 1.00 118.23 ?  255 TYR   A CD2 1 
ATOM   1813 C  CE1 . TYR   A 1 248 ? 40.048  22.169  41.690 1.00 127.82 ?  255 TYR   A CE1 1 
ATOM   1814 C  CE2 . TYR   A 1 248 ? 39.366  20.287  40.331 1.00 115.11 ?  255 TYR   A CE2 1 
ATOM   1815 C  CZ  . TYR   A 1 248 ? 39.267  21.634  40.657 1.00 125.11 ?  255 TYR   A CZ  1 
ATOM   1816 O  OH  . TYR   A 1 248 ? 38.396  22.441  39.959 1.00 131.18 ?  255 TYR   A OH  1 
ATOM   1817 N  N   . CYS   A 1 249 ? 39.507  19.048  45.444 1.00 78.10  ?  256 CYS   A N   1 
ATOM   1818 C  CA  . CYS   A 1 249 ? 38.046  19.039  45.427 1.00 73.93  ?  256 CYS   A CA  1 
ATOM   1819 C  C   . CYS   A 1 249 ? 37.606  20.274  44.656 1.00 72.81  ?  256 CYS   A C   1 
ATOM   1820 O  O   . CYS   A 1 249 ? 38.033  21.369  45.012 1.00 87.39  ?  256 CYS   A O   1 
ATOM   1821 C  CB  . CYS   A 1 249 ? 37.440  19.094  46.826 1.00 65.90  ?  256 CYS   A CB  1 
ATOM   1822 S  SG  . CYS   A 1 249 ? 35.649  18.843  46.782 1.00 63.81  ?  256 CYS   A SG  1 
ATOM   1823 N  N   . PRO   A 1 250 ? 36.769  20.117  43.602 1.00 73.55  ?  257 PRO   A N   1 
ATOM   1824 C  CA  . PRO   A 1 250 ? 36.205  21.280  42.897 1.00 74.85  ?  257 PRO   A CA  1 
ATOM   1825 C  C   . PRO   A 1 250 ? 35.469  22.269  43.796 1.00 70.35  ?  257 PRO   A C   1 
ATOM   1826 O  O   . PRO   A 1 250 ? 34.989  21.877  44.885 1.00 60.34  ?  257 PRO   A O   1 
ATOM   1827 C  CB  . PRO   A 1 250 ? 35.194  20.645  41.929 1.00 82.05  ?  257 PRO   A CB  1 
ATOM   1828 C  CG  . PRO   A 1 250 ? 35.721  19.291  41.654 1.00 72.25  ?  257 PRO   A CG  1 
ATOM   1829 C  CD  . PRO   A 1 250 ? 36.456  18.857  42.890 1.00 68.66  ?  257 PRO   A CD  1 
ATOM   1830 N  N   . ARG   A 1 251 ? 35.393  23.526  43.339 1.00 76.90  ?  258 ARG   A N   1 
ATOM   1831 C  CA  . ARG   A 1 251 ? 34.670  24.593  44.065 1.00 79.63  ?  258 ARG   A CA  1 
ATOM   1832 C  C   . ARG   A 1 251 ? 33.191  24.255  44.305 1.00 69.56  ?  258 ARG   A C   1 
ATOM   1833 O  O   . ARG   A 1 251 ? 32.680  24.464  45.400 1.00 64.76  ?  258 ARG   A O   1 
ATOM   1834 C  CB  . ARG   A 1 251 ? 34.745  25.945  43.340 1.00 88.44  ?  258 ARG   A CB  1 
ATOM   1835 C  CG  . ARG   A 1 251 ? 36.133  26.539  43.223 1.00 101.29 ?  258 ARG   A CG  1 
ATOM   1836 C  CD  . ARG   A 1 251 ? 36.091  28.037  42.915 1.00 109.82 ?  258 ARG   A CD  1 
ATOM   1837 N  NE  . ARG   A 1 251 ? 35.502  28.381  41.606 1.00 112.89 ?  258 ARG   A NE  1 
ATOM   1838 C  CZ  . ARG   A 1 251 ? 34.227  28.727  41.346 1.00 110.74 ?  258 ARG   A CZ  1 
ATOM   1839 N  NH1 . ARG   A 1 251 ? 33.277  28.771  42.291 1.00 114.35 ?  258 ARG   A NH1 1 
ATOM   1840 N  NH2 . ARG   A 1 251 ? 33.886  29.028  40.088 1.00 105.54 ?  258 ARG   A NH2 1 
ATOM   1841 N  N   . GLU   A 1 252 ? 32.541  23.694  43.290 1.00 72.19  ?  259 GLU   A N   1 
ATOM   1842 C  CA  . GLU   A 1 252 ? 31.075  23.507  43.324 1.00 79.57  ?  259 GLU   A CA  1 
ATOM   1843 C  C   . GLU   A 1 252 ? 30.658  22.306  44.200 1.00 68.29  ?  259 GLU   A C   1 
ATOM   1844 O  O   . GLU   A 1 252 ? 29.550  22.297  44.704 1.00 75.22  ?  259 GLU   A O   1 
ATOM   1845 C  CB  . GLU   A 1 252 ? 30.382  23.582  41.929 1.00 84.00  ?  259 GLU   A CB  1 
ATOM   1846 C  CG  . GLU   A 1 252 ? 31.025  22.889  40.737 1.00 92.95  ?  259 GLU   A CG  1 
ATOM   1847 C  CD  . GLU   A 1 252 ? 32.073  23.738  40.017 1.00 101.82 ?  259 GLU   A CD  1 
ATOM   1848 O  OE1 . GLU   A 1 252 ? 33.190  23.856  40.572 1.00 101.56 ?  259 GLU   A OE1 1 
ATOM   1849 O  OE2 . GLU   A 1 252 ? 31.791  24.266  38.915 1.00 99.24  ?  259 GLU   A OE2 1 
ATOM   1850 N  N   . ILE   A 1 253 ? 31.532  21.315  44.393 1.00 81.85  ?  260 ILE   A N   1 
ATOM   1851 C  CA  . ILE   A 1 253 ? 31.321  20.225  45.378 1.00 76.27  ?  260 ILE   A CA  1 
ATOM   1852 C  C   . ILE   A 1 253 ? 31.477  20.730  46.828 1.00 74.90  ?  260 ILE   A C   1 
ATOM   1853 O  O   . ILE   A 1 253 ? 30.752  20.267  47.710 1.00 58.01  ?  260 ILE   A O   1 
ATOM   1854 C  CB  . ILE   A 1 253 ? 32.233  19.000  45.081 1.00 75.07  ?  260 ILE   A CB  1 
ATOM   1855 C  CG1 . ILE   A 1 253 ? 31.738  18.320  43.804 1.00 72.00  ?  260 ILE   A CG1 1 
ATOM   1856 C  CG2 . ILE   A 1 253 ? 32.223  17.973  46.223 1.00 75.28  ?  260 ILE   A CG2 1 
ATOM   1857 C  CD1 . ILE   A 1 253 ? 32.690  17.326  43.177 1.00 70.71  ?  260 ILE   A CD1 1 
ATOM   1858 N  N   . ILE   A 1 254 ? 32.419  21.650  47.074 1.00 71.41  ?  261 ILE   A N   1 
ATOM   1859 C  CA  . ILE   A 1 254 ? 32.530  22.346  48.379 1.00 69.51  ?  261 ILE   A CA  1 
ATOM   1860 C  C   . ILE   A 1 254 ? 31.247  23.172  48.646 1.00 67.79  ?  261 ILE   A C   1 
ATOM   1861 O  O   . ILE   A 1 254 ? 30.698  23.132  49.755 1.00 62.81  ?  261 ILE   A O   1 
ATOM   1862 C  CB  . ILE   A 1 254 ? 33.807  23.247  48.491 1.00 74.61  ?  261 ILE   A CB  1 
ATOM   1863 C  CG1 . ILE   A 1 254 ? 35.117  22.433  48.358 1.00 67.20  ?  261 ILE   A CG1 1 
ATOM   1864 C  CG2 . ILE   A 1 254 ? 33.829  24.012  49.817 1.00 75.18  ?  261 ILE   A CG2 1 
ATOM   1865 C  CD1 . ILE   A 1 254 ? 36.351  23.182  48.051 0.00 70.61  ?  261 ILE   A CD1 1 
ATOM   1866 N  N   . SER   A 1 255 ? 30.783  23.913  47.633 1.00 73.08  ?  262 SER   A N   1 
ATOM   1867 C  CA  . SER   A 1 255 ? 29.484  24.617  47.697 1.00 70.91  ?  262 SER   A CA  1 
ATOM   1868 C  C   . SER   A 1 255 ? 28.303  23.674  47.966 1.00 66.12  ?  262 SER   A C   1 
ATOM   1869 O  O   . SER   A 1 255 ? 27.407  24.009  48.742 1.00 66.01  ?  262 SER   A O   1 
ATOM   1870 C  CB  . SER   A 1 255 ? 29.230  25.413  46.419 1.00 72.59  ?  262 SER   A CB  1 
ATOM   1871 O  OG  . SER   A 1 255 ? 30.198  26.449  46.276 1.00 87.69  ?  262 SER   A OG  1 
ATOM   1872 N  N   . LEU   A 1 256 ? 28.322  22.504  47.337 1.00 66.40  ?  263 LEU   A N   1 
ATOM   1873 C  CA  . LEU   A 1 256 ? 27.283  21.488  47.540 1.00 70.55  ?  263 LEU   A CA  1 
ATOM   1874 C  C   . LEU   A 1 256 ? 27.273  20.927  48.974 1.00 71.97  ?  263 LEU   A C   1 
ATOM   1875 O  O   . LEU   A 1 256 ? 26.193  20.761  49.544 1.00 71.98  ?  263 LEU   A O   1 
ATOM   1876 C  CB  . LEU   A 1 256 ? 27.406  20.369  46.499 1.00 65.06  ?  263 LEU   A CB  1 
ATOM   1877 C  CG  . LEU   A 1 256 ? 26.432  19.192  46.557 1.00 61.03  ?  263 LEU   A CG  1 
ATOM   1878 C  CD1 . LEU   A 1 256 ? 24.986  19.634  46.526 1.00 61.33  ?  263 LEU   A CD1 1 
ATOM   1879 C  CD2 . LEU   A 1 256 ? 26.707  18.259  45.392 1.00 60.92  ?  263 LEU   A CD2 1 
ATOM   1880 N  N   . MET   A 1 257 ? 28.448  20.655  49.553 1.00 71.22  ?  264 MET   A N   1 
ATOM   1881 C  CA  . MET   A 1 257 ? 28.518  20.087  50.915 1.00 77.83  ?  264 MET   A CA  1 
ATOM   1882 C  C   . MET   A 1 257 ? 28.132  21.106  51.999 1.00 70.60  ?  264 MET   A C   1 
ATOM   1883 O  O   . MET   A 1 257 ? 27.486  20.750  52.979 1.00 88.50  ?  264 MET   A O   1 
ATOM   1884 C  CB  . MET   A 1 257 ? 29.876  19.396  51.205 1.00 73.47  ?  264 MET   A CB  1 
ATOM   1885 C  CG  . MET   A 1 257 ? 31.085  20.299  51.391 1.00 78.29  ?  264 MET   A CG  1 
ATOM   1886 S  SD  . MET   A 1 257 ? 32.575  19.387  51.874 1.00 71.78  ?  264 MET   A SD  1 
ATOM   1887 C  CE  . MET   A 1 257 ? 32.998  18.607  50.323 1.00 64.75  ?  264 MET   A CE  1 
ATOM   1888 N  N   . LYS   A 1 258 ? 28.544  22.357  51.828 1.00 74.12  ?  265 LYS   A N   1 
ATOM   1889 C  CA  . LYS   A 1 258 ? 28.098  23.471  52.688 1.00 66.81  ?  265 LYS   A CA  1 
ATOM   1890 C  C   . LYS   A 1 258 ? 26.587  23.725  52.646 1.00 60.56  ?  265 LYS   A C   1 
ATOM   1891 O  O   . LYS   A 1 258 ? 25.987  24.035  53.669 1.00 59.79  ?  265 LYS   A O   1 
ATOM   1892 C  CB  . LYS   A 1 258 ? 28.851  24.754  52.348 1.00 69.56  ?  265 LYS   A CB  1 
ATOM   1893 C  CG  . LYS   A 1 258 ? 30.311  24.733  52.771 1.00 67.57  ?  265 LYS   A CG  1 
ATOM   1894 C  CD  . LYS   A 1 258 ? 31.061  25.903  52.143 1.00 61.46  ?  265 LYS   A CD  1 
ATOM   1895 C  CE  . LYS   A 1 258 ? 32.477  26.036  52.668 1.00 63.44  ?  265 LYS   A CE  1 
ATOM   1896 N  NZ  . LYS   A 1 258 ? 32.996  27.420  52.425 1.00 67.55  ?  265 LYS   A NZ  1 
ATOM   1897 N  N   . LEU   A 1 259 ? 25.991  23.611  51.461 1.00 58.33  ?  266 LEU   A N   1 
ATOM   1898 C  CA  . LEU   A 1 259 ? 24.534  23.649  51.297 1.00 62.11  ?  266 LEU   A CA  1 
ATOM   1899 C  C   . LEU   A 1 259 ? 23.846  22.464  52.021 1.00 66.06  ?  266 LEU   A C   1 
ATOM   1900 O  O   . LEU   A 1 259 ? 22.855  22.654  52.720 1.00 73.86  ?  266 LEU   A O   1 
ATOM   1901 C  CB  . LEU   A 1 259 ? 24.180  23.627  49.808 1.00 65.26  ?  266 LEU   A CB  1 
ATOM   1902 C  CG  . LEU   A 1 259 ? 22.735  23.960  49.416 1.00 66.18  ?  266 LEU   A CG  1 
ATOM   1903 C  CD1 . LEU   A 1 259 ? 22.471  25.454  49.605 1.00 70.94  ?  266 LEU   A CD1 1 
ATOM   1904 C  CD2 . LEU   A 1 259 ? 22.471  23.532  47.979 1.00 60.18  ?  266 LEU   A CD2 1 
ATOM   1905 N  N   . CYS   A 1 260 ? 24.391  21.263  51.834 1.00 62.37  ?  267 CYS   A N   1 
ATOM   1906 C  CA  . CYS   A 1 260 ? 23.835  20.055  52.425 1.00 55.41  ?  267 CYS   A CA  1 
ATOM   1907 C  C   . CYS   A 1 260 ? 24.030  19.928  53.952 1.00 52.51  ?  267 CYS   A C   1 
ATOM   1908 O  O   . CYS   A 1 260 ? 23.188  19.302  54.594 1.00 52.36  ?  267 CYS   A O   1 
ATOM   1909 C  CB  . CYS   A 1 260 ? 24.346  18.810  51.688 1.00 65.27  ?  267 CYS   A CB  1 
ATOM   1910 S  SG  . CYS   A 1 260 ? 23.776  18.665  49.988 1.00 65.98  ?  267 CYS   A SG  1 
ATOM   1911 N  N   . TRP   A 1 261 ? 25.088  20.529  54.529 1.00 59.53  ?  268 TRP   A N   1 
ATOM   1912 C  CA  . TRP   A 1 261 ? 25.280  20.611  56.006 1.00 53.03  ?  268 TRP   A CA  1 
ATOM   1913 C  C   . TRP   A 1 261 ? 24.795  21.885  56.717 1.00 54.43  ?  268 TRP   A C   1 
ATOM   1914 O  O   . TRP   A 1 261 ? 25.258  22.192  57.832 1.00 51.48  ?  268 TRP   A O   1 
ATOM   1915 C  CB  . TRP   A 1 261 ? 26.729  20.240  56.425 1.00 50.50  ?  268 TRP   A CB  1 
ATOM   1916 C  CG  . TRP   A 1 261 ? 27.883  21.178  56.178 1.00 51.19  ?  268 TRP   A CG  1 
ATOM   1917 C  CD1 . TRP   A 1 261 ? 27.921  22.575  56.276 1.00 55.24  ?  268 TRP   A CD1 1 
ATOM   1918 C  CD2 . TRP   A 1 261 ? 29.223  20.781  55.890 1.00 48.62  ?  268 TRP   A CD2 1 
ATOM   1919 N  NE1 . TRP   A 1 261 ? 29.168  23.023  56.027 1.00 56.66  ?  268 TRP   A NE1 1 
ATOM   1920 C  CE2 . TRP   A 1 261 ? 29.997  21.958  55.788 1.00 53.77  ?  268 TRP   A CE2 1 
ATOM   1921 C  CE3 . TRP   A 1 261 ? 29.849  19.541  55.707 1.00 52.99  ?  268 TRP   A CE3 1 
ATOM   1922 C  CZ2 . TRP   A 1 261 ? 31.366  21.938  55.484 1.00 56.06  ?  268 TRP   A CZ2 1 
ATOM   1923 C  CZ3 . TRP   A 1 261 ? 31.224  19.518  55.391 1.00 51.65  ?  268 TRP   A CZ3 1 
ATOM   1924 C  CH2 . TRP   A 1 261 ? 31.963  20.714  55.307 1.00 57.21  ?  268 TRP   A CH2 1 
ATOM   1925 N  N   . GLU   A 1 262 ? 23.857  22.620  56.107 1.00 58.94  ?  269 GLU   A N   1 
ATOM   1926 C  CA  . GLU   A 1 262 ? 23.143  23.716  56.791 1.00 53.86  ?  269 GLU   A CA  1 
ATOM   1927 C  C   . GLU   A 1 262 ? 22.539  23.230  58.109 1.00 56.41  ?  269 GLU   A C   1 
ATOM   1928 O  O   . GLU   A 1 262 ? 21.980  22.124  58.168 1.00 63.91  ?  269 GLU   A O   1 
ATOM   1929 C  CB  . GLU   A 1 262 ? 22.017  24.257  55.910 1.00 62.66  ?  269 GLU   A CB  1 
ATOM   1930 C  CG  . GLU   A 1 262 ? 22.463  25.141  54.761 1.00 72.77  ?  269 GLU   A CG  1 
ATOM   1931 C  CD  . GLU   A 1 262 ? 23.018  26.483  55.188 1.00 78.58  ?  269 GLU   A CD  1 
ATOM   1932 O  OE1 . GLU   A 1 262 ? 23.948  26.957  54.504 1.00 88.93  ?  269 GLU   A OE1 1 
ATOM   1933 O  OE2 . GLU   A 1 262 ? 22.535  27.088  56.172 1.00 93.55  ?  269 GLU   A OE2 1 
ATOM   1934 N  N   . ALA   A 1 263 ? 22.668  24.051  59.152 1.00 61.34  ?  270 ALA   A N   1 
ATOM   1935 C  CA  . ALA   A 1 263 ? 22.082  23.794  60.483 1.00 64.37  ?  270 ALA   A CA  1 
ATOM   1936 C  C   . ALA   A 1 263 ? 20.566  23.542  60.435 1.00 69.49  ?  270 ALA   A C   1 
ATOM   1937 O  O   . ALA   A 1 263 ? 20.056  22.611  61.096 1.00 73.55  ?  270 ALA   A O   1 
ATOM   1938 C  CB  . ALA   A 1 263 ? 22.384  24.959  61.426 1.00 62.81  ?  270 ALA   A CB  1 
ATOM   1939 N  N   . ASN   A 1 264 ? 19.870  24.381  59.660 1.00 67.97  ?  271 ASN   A N   1 
ATOM   1940 C  CA  . ASN   A 1 264 ? 18.436  24.294  59.448 1.00 66.22  ?  271 ASN   A CA  1 
ATOM   1941 C  C   . ASN   A 1 264 ? 18.112  23.226  58.393 1.00 68.03  ?  271 ASN   A C   1 
ATOM   1942 O  O   . ASN   A 1 264 ? 18.572  23.365  57.257 1.00 67.50  ?  271 ASN   A O   1 
ATOM   1943 C  CB  . ASN   A 1 264 ? 17.929  25.663  58.988 1.00 75.30  ?  271 ASN   A CB  1 
ATOM   1944 C  CG  . ASN   A 1 264 ? 16.419  25.789  59.003 1.00 68.76  ?  271 ASN   A CG  1 
ATOM   1945 O  OD1 . ASN   A 1 264 ? 15.674  24.827  59.126 1.00 65.89  ?  271 ASN   A OD1 1 
ATOM   1946 N  ND2 . ASN   A 1 264 ? 15.959  27.023  58.892 1.00 65.16  ?  271 ASN   A ND2 1 
ATOM   1947 N  N   . PRO   A 1 265 ? 17.323  22.164  58.757 1.00 63.90  ?  272 PRO   A N   1 
ATOM   1948 C  CA  . PRO   A 1 265 ? 16.928  21.116  57.770 1.00 59.61  ?  272 PRO   A CA  1 
ATOM   1949 C  C   . PRO   A 1 265 ? 16.241  21.645  56.515 1.00 66.20  ?  272 PRO   A C   1 
ATOM   1950 O  O   . PRO   A 1 265 ? 16.572  21.209  55.419 1.00 60.55  ?  272 PRO   A O   1 
ATOM   1951 C  CB  . PRO   A 1 265 ? 15.953  20.207  58.541 1.00 61.32  ?  272 PRO   A CB  1 
ATOM   1952 C  CG  . PRO   A 1 265 ? 16.196  20.492  59.972 1.00 69.32  ?  272 PRO   A CG  1 
ATOM   1953 C  CD  . PRO   A 1 265 ? 16.807  21.859  60.106 1.00 63.45  ?  272 PRO   A CD  1 
ATOM   1954 N  N   . GLU   A 1 266 ? 15.310  22.593  56.686 1.00 74.83  ?  273 GLU   A N   1 
ATOM   1955 C  CA  . GLU   A 1 266 ? 14.586  23.237  55.577 1.00 74.57  ?  273 GLU   A CA  1 
ATOM   1956 C  C   . GLU   A 1 266 ? 15.496  23.950  54.552 1.00 73.50  ?  273 GLU   A C   1 
ATOM   1957 O  O   . GLU   A 1 266 ? 15.154  23.986  53.381 1.00 78.62  ?  273 GLU   A O   1 
ATOM   1958 C  CB  . GLU   A 1 266 ? 13.523  24.230  56.113 1.00 86.50  ?  273 GLU   A CB  1 
ATOM   1959 C  CG  . GLU   A 1 266 ? 12.339  23.612  56.864 1.00 89.11  ?  273 GLU   A CG  1 
ATOM   1960 C  CD  . GLU   A 1 266 ? 11.047  23.613  56.056 1.00 96.91  ?  273 GLU   A CD  1 
ATOM   1961 O  OE1 . GLU   A 1 266 ? 11.056  23.052  54.937 1.00 93.32  ?  273 GLU   A OE1 1 
ATOM   1962 O  OE2 . GLU   A 1 266 ? 10.028  24.180  56.530 1.00 104.22 ?  273 GLU   A OE2 1 
ATOM   1963 N  N   . ALA   A 1 267 ? 16.640  24.485  54.990 1.00 66.92  ?  274 ALA   A N   1 
ATOM   1964 C  CA  . ALA   A 1 267 ? 17.657  25.055  54.086 1.00 61.71  ?  274 ALA   A CA  1 
ATOM   1965 C  C   . ALA   A 1 267 ? 18.389  24.028  53.195 1.00 59.62  ?  274 ALA   A C   1 
ATOM   1966 O  O   . ALA   A 1 267 ? 18.984  24.401  52.187 1.00 55.34  ?  274 ALA   A O   1 
ATOM   1967 C  CB  . ALA   A 1 267 ? 18.673  25.882  54.879 1.00 62.79  ?  274 ALA   A CB  1 
ATOM   1968 N  N   . ARG   A 1 268 ? 18.366  22.749  53.565 1.00 62.85  ?  275 ARG   A N   1 
ATOM   1969 C  CA  . ARG   A 1 268 ? 19.067  21.717  52.803 1.00 59.70  ?  275 ARG   A CA  1 
ATOM   1970 C  C   . ARG   A 1 268 ? 18.247  21.332  51.572 1.00 56.96  ?  275 ARG   A C   1 
ATOM   1971 O  O   . ARG   A 1 268 ? 17.022  21.337  51.641 1.00 58.12  ?  275 ARG   A O   1 
ATOM   1972 C  CB  . ARG   A 1 268 ? 19.319  20.490  53.674 1.00 60.66  ?  275 ARG   A CB  1 
ATOM   1973 C  CG  . ARG   A 1 268 ? 20.190  20.779  54.890 1.00 59.43  ?  275 ARG   A CG  1 
ATOM   1974 C  CD  . ARG   A 1 268 ? 20.159  19.619  55.857 1.00 62.97  ?  275 ARG   A CD  1 
ATOM   1975 N  NE  . ARG   A 1 268 ? 20.515  20.022  57.212 1.00 66.73  ?  275 ARG   A NE  1 
ATOM   1976 C  CZ  . ARG   A 1 268 ? 20.343  19.284  58.313 1.00 70.53  ?  275 ARG   A CZ  1 
ATOM   1977 N  NH1 . ARG   A 1 268 ? 19.810  18.052  58.279 1.00 77.28  ?  275 ARG   A NH1 1 
ATOM   1978 N  NH2 . ARG   A 1 268 ? 20.708  19.791  59.481 1.00 72.16  ?  275 ARG   A NH2 1 
ATOM   1979 N  N   . PRO   A 1 269 ? 18.911  20.976  50.445 1.00 62.37  ?  276 PRO   A N   1 
ATOM   1980 C  CA  . PRO   A 1 269 ? 18.179  20.470  49.282 1.00 63.75  ?  276 PRO   A CA  1 
ATOM   1981 C  C   . PRO   A 1 269 ? 17.696  19.056  49.533 1.00 59.52  ?  276 PRO   A C   1 
ATOM   1982 O  O   . PRO   A 1 269 ? 18.029  18.475  50.538 1.00 54.41  ?  276 PRO   A O   1 
ATOM   1983 C  CB  . PRO   A 1 269 ? 19.242  20.478  48.168 1.00 63.03  ?  276 PRO   A CB  1 
ATOM   1984 C  CG  . PRO   A 1 269 ? 20.519  20.265  48.870 1.00 60.25  ?  276 PRO   A CG  1 
ATOM   1985 C  CD  . PRO   A 1 269 ? 20.365  20.783  50.272 1.00 60.80  ?  276 PRO   A CD  1 
ATOM   1986 N  N   . THR   A 1 270 ? 16.899  18.532  48.612 1.00 63.73  ?  277 THR   A N   1 
ATOM   1987 C  CA  . THR   A 1 270 ? 16.487  17.124  48.600 1.00 56.77  ?  277 THR   A CA  1 
ATOM   1988 C  C   . THR   A 1 270 ? 17.444  16.372  47.679 1.00 58.63  ?  277 THR   A C   1 
ATOM   1989 O  O   . THR   A 1 270 ? 18.268  16.999  46.988 1.00 60.70  ?  277 THR   A O   1 
ATOM   1990 C  CB  . THR   A 1 270 ? 15.037  16.973  48.075 1.00 54.62  ?  277 THR   A CB  1 
ATOM   1991 O  OG1 . THR   A 1 270 ? 14.936  17.534  46.770 1.00 54.87  ?  277 THR   A OG1 1 
ATOM   1992 C  CG2 . THR   A 1 270 ? 14.043  17.670  48.965 1.00 57.20  ?  277 THR   A CG2 1 
ATOM   1993 N  N   . PHE   A 1 271 ? 17.326  15.044  47.627 1.00 55.03  ?  278 PHE   A N   1 
ATOM   1994 C  CA  . PHE   A 1 271 ? 18.186  14.247  46.741 1.00 55.97  ?  278 PHE   A CA  1 
ATOM   1995 C  C   . PHE   A 1 271 ? 17.881  14.387  45.248 1.00 57.10  ?  278 PHE   A C   1 
ATOM   1996 O  O   . PHE   A 1 271 ? 18.817  14.320  44.444 1.00 72.95  ?  278 PHE   A O   1 
ATOM   1997 C  CB  . PHE   A 1 271 ? 18.245  12.782  47.173 1.00 64.50  ?  278 PHE   A CB  1 
ATOM   1998 C  CG  . PHE   A 1 271 ? 19.231  12.531  48.286 1.00 63.54  ?  278 PHE   A CG  1 
ATOM   1999 C  CD1 . PHE   A 1 271 ? 20.610  12.543  48.032 1.00 60.90  ?  278 PHE   A CD1 1 
ATOM   2000 C  CD2 . PHE   A 1 271 ? 18.793  12.318  49.594 1.00 61.57  ?  278 PHE   A CD2 1 
ATOM   2001 C  CE1 . PHE   A 1 271 ? 21.525  12.331  49.061 1.00 61.54  ?  278 PHE   A CE1 1 
ATOM   2002 C  CE2 . PHE   A 1 271 ? 19.703  12.105  50.626 1.00 57.61  ?  278 PHE   A CE2 1 
ATOM   2003 C  CZ  . PHE   A 1 271 ? 21.072  12.107  50.362 1.00 56.14  ?  278 PHE   A CZ  1 
ATOM   2004 N  N   . PRO   A 1 272 ? 16.595  14.550  44.870 1.00 59.50  ?  279 PRO   A N   1 
ATOM   2005 C  CA  . PRO   A 1 272 ? 16.288  14.956  43.492 1.00 61.47  ?  279 PRO   A CA  1 
ATOM   2006 C  C   . PRO   A 1 272 ? 16.835  16.323  43.115 1.00 64.22  ?  279 PRO   A C   1 
ATOM   2007 O  O   . PRO   A 1 272 ? 17.318  16.493  41.992 1.00 61.51  ?  279 PRO   A O   1 
ATOM   2008 C  CB  . PRO   A 1 272 ? 14.759  14.949  43.455 1.00 65.52  ?  279 PRO   A CB  1 
ATOM   2009 C  CG  . PRO   A 1 272 ? 14.381  13.916  44.444 1.00 61.85  ?  279 PRO   A CG  1 
ATOM   2010 C  CD  . PRO   A 1 272 ? 15.398  13.997  45.539 1.00 60.14  ?  279 PRO   A CD  1 
ATOM   2011 N  N   . GLY   A 1 273 ? 16.757  17.269  44.055 1.00 70.58  ?  280 GLY   A N   1 
ATOM   2012 C  CA  . GLY   A 1 273 ? 17.405  18.581  43.929 1.00 70.49  ?  280 GLY   A CA  1 
ATOM   2013 C  C   . GLY   A 1 273 ? 18.917  18.548  43.797 1.00 59.90  ?  280 GLY   A C   1 
ATOM   2014 O  O   . GLY   A 1 273 ? 19.490  19.352  43.053 1.00 61.68  ?  280 GLY   A O   1 
ATOM   2015 N  N   . ILE   A 1 274 ? 19.560  17.643  44.533 1.00 63.03  ?  281 ILE   A N   1 
ATOM   2016 C  CA  . ILE   A 1 274 ? 21.016  17.408  44.405 1.00 61.39  ?  281 ILE   A CA  1 
ATOM   2017 C  C   . ILE   A 1 274 ? 21.319  16.868  43.008 1.00 61.51  ?  281 ILE   A C   1 
ATOM   2018 O  O   . ILE   A 1 274 ? 22.151  17.442  42.309 1.00 70.87  ?  281 ILE   A O   1 
ATOM   2019 C  CB  . ILE   A 1 274 ? 21.576  16.486  45.523 1.00 59.98  ?  281 ILE   A CB  1 
ATOM   2020 C  CG1 . ILE   A 1 274 ? 21.605  17.249  46.844 1.00 58.59  ?  281 ILE   A CG1 1 
ATOM   2021 C  CG2 . ILE   A 1 274 ? 23.002  16.010  45.227 1.00 72.77  ?  281 ILE   A CG2 1 
ATOM   2022 C  CD1 . ILE   A 1 274 ? 21.747  16.393  48.077 1.00 60.30  ?  281 ILE   A CD1 1 
ATOM   2023 N  N   . GLU   A 1 275 ? 20.630  15.789  42.624 1.00 65.65  ?  282 GLU   A N   1 
ATOM   2024 C  CA  . GLU   A 1 275 ? 20.811  15.141  41.311 1.00 63.87  ?  282 GLU   A CA  1 
ATOM   2025 C  C   . GLU   A 1 275 ? 20.679  16.085  40.103 1.00 68.12  ?  282 GLU   A C   1 
ATOM   2026 O  O   . GLU   A 1 275 ? 21.495  16.017  39.170 1.00 59.30  ?  282 GLU   A O   1 
ATOM   2027 C  CB  . GLU   A 1 275 ? 19.840  13.970  41.141 1.00 68.81  ?  282 GLU   A CB  1 
ATOM   2028 C  CG  . GLU   A 1 275 ? 20.270  13.008  40.032 1.00 72.18  ?  282 GLU   A CG  1 
ATOM   2029 C  CD  . GLU   A 1 275 ? 19.420  11.764  39.902 1.00 71.21  ?  282 GLU   A CD  1 
ATOM   2030 O  OE1 . GLU   A 1 275 ? 19.905  10.851  39.210 1.00 72.69  ?  282 GLU   A OE1 1 
ATOM   2031 O  OE2 . GLU   A 1 275 ? 18.290  11.700  40.449 1.00 78.52  ?  282 GLU   A OE2 1 
ATOM   2032 N  N   . GLU   A 1 276 ? 19.645  16.934  40.127 1.00 73.97  ?  283 GLU   A N   1 
ATOM   2033 C  CA  . GLU   A 1 276 ? 19.389  17.940  39.068 1.00 78.38  ?  283 GLU   A CA  1 
ATOM   2034 C  C   . GLU   A 1 276 ? 20.572  18.894  38.845 1.00 76.15  ?  283 GLU   A C   1 
ATOM   2035 O  O   . GLU   A 1 276 ? 20.883  19.236  37.705 1.00 73.96  ?  283 GLU   A O   1 
ATOM   2036 C  CB  . GLU   A 1 276 ? 18.113  18.765  39.363 1.00 89.76  ?  283 GLU   A CB  1 
ATOM   2037 C  CG  . GLU   A 1 276 ? 16.810  18.047  39.046 1.00 93.24  ?  283 GLU   A CG  1 
ATOM   2038 C  CD  . GLU   A 1 276 ? 15.587  18.762  39.570 0.00 92.51  ?  283 GLU   A CD  1 
ATOM   2039 O  OE1 . GLU   A 1 276 ? 15.504  18.997  40.795 0.00 91.01  ?  283 GLU   A OE1 1 
ATOM   2040 O  OE2 . GLU   A 1 276 ? 14.692  19.086  38.760 0.00 95.45  ?  283 GLU   A OE2 1 
ATOM   2041 N  N   . LYS   A 1 277 ? 21.210  19.307  39.941 1.00 78.38  ?  284 LYS   A N   1 
ATOM   2042 C  CA  . LYS   A 1 277 ? 22.440  20.100  39.912 1.00 79.48  ?  284 LYS   A CA  1 
ATOM   2043 C  C   . LYS   A 1 277 ? 23.640  19.233  39.520 1.00 76.38  ?  284 LYS   A C   1 
ATOM   2044 O  O   . LYS   A 1 277 ? 24.359  19.572  38.588 1.00 73.67  ?  284 LYS   A O   1 
ATOM   2045 C  CB  . LYS   A 1 277 ? 22.725  20.723  41.285 1.00 89.82  ?  284 LYS   A CB  1 
ATOM   2046 C  CG  . LYS   A 1 277 ? 21.675  21.705  41.789 1.00 107.52 ?  284 LYS   A CG  1 
ATOM   2047 C  CD  . LYS   A 1 277 ? 21.848  22.003  43.273 1.00 111.60 ?  284 LYS   A CD  1 
ATOM   2048 C  CE  . LYS   A 1 277 ? 20.624  22.709  43.830 1.00 107.80 ?  284 LYS   A CE  1 
ATOM   2049 N  NZ  . LYS   A 1 277 ? 20.854  23.125  45.232 1.00 103.46 ?  284 LYS   A NZ  1 
ATOM   2050 N  N   . PHE   A 1 278 ? 23.828  18.121  40.237 1.00 67.66  ?  285 PHE   A N   1 
ATOM   2051 C  CA  . PHE   A 1 278 ? 25.085  17.367  40.212 1.00 69.18  ?  285 PHE   A CA  1 
ATOM   2052 C  C   . PHE   A 1 278 ? 25.321  16.517  38.968 1.00 63.80  ?  285 PHE   A C   1 
ATOM   2053 O  O   . PHE   A 1 278 ? 26.463  16.429  38.526 1.00 76.23  ?  285 PHE   A O   1 
ATOM   2054 C  CB  . PHE   A 1 278 ? 25.227  16.482  41.449 1.00 73.07  ?  285 PHE   A CB  1 
ATOM   2055 C  CG  . PHE   A 1 278 ? 26.625  15.948  41.640 1.00 74.87  ?  285 PHE   A CG  1 
ATOM   2056 C  CD1 . PHE   A 1 278 ? 27.629  16.768  42.167 1.00 68.19  ?  285 PHE   A CD1 1 
ATOM   2057 C  CD2 . PHE   A 1 278 ? 26.960  14.645  41.249 1.00 59.94  ?  285 PHE   A CD2 1 
ATOM   2058 C  CE1 . PHE   A 1 278 ? 28.926  16.286  42.324 1.00 68.34  ?  285 PHE   A CE1 1 
ATOM   2059 C  CE2 . PHE   A 1 278 ? 28.253  14.167  41.403 1.00 57.91  ?  285 PHE   A CE2 1 
ATOM   2060 C  CZ  . PHE   A 1 278 ? 29.239  14.980  41.950 1.00 62.67  ?  285 PHE   A CZ  1 
ATOM   2061 N  N   . ARG   A 1 279 ? 24.279  15.896  38.418 1.00 60.96  ?  286 ARG   A N   1 
ATOM   2062 C  CA  . ARG   A 1 279 ? 24.413  15.048  37.219 1.00 60.27  ?  286 ARG   A CA  1 
ATOM   2063 C  C   . ARG   A 1 279 ? 24.974  15.803  36.003 1.00 66.07  ?  286 ARG   A C   1 
ATOM   2064 O  O   . ARG   A 1 279 ? 25.948  15.326  35.414 1.00 67.59  ?  286 ARG   A O   1 
ATOM   2065 C  CB  . ARG   A 1 279 ? 23.097  14.337  36.869 1.00 59.68  ?  286 ARG   A CB  1 
ATOM   2066 C  CG  . ARG   A 1 279 ? 23.163  13.403  35.655 1.00 63.18  ?  286 ARG   A CG  1 
ATOM   2067 C  CD  . ARG   A 1 279 ? 21.853  12.675  35.470 1.00 64.81  ?  286 ARG   A CD  1 
ATOM   2068 N  NE  . ARG   A 1 279 ? 21.671  11.707  36.554 1.00 65.70  ?  286 ARG   A NE  1 
ATOM   2069 C  CZ  . ARG   A 1 279 ? 22.165  10.462  36.596 1.00 57.32  ?  286 ARG   A CZ  1 
ATOM   2070 N  NH1 . ARG   A 1 279 ? 22.887  9.951   35.591 1.00 56.86  ?  286 ARG   A NH1 1 
ATOM   2071 N  NH2 . ARG   A 1 279 ? 21.919  9.710   37.668 1.00 59.19  ?  286 ARG   A NH2 1 
ATOM   2072 N  N   . PRO   A 1 280 ? 24.379  16.968  35.639 1.00 61.76  ?  287 PRO   A N   1 
ATOM   2073 C  CA  . PRO   A 1 280 ? 24.978  17.699  34.517 1.00 65.41  ?  287 PRO   A CA  1 
ATOM   2074 C  C   . PRO   A 1 280 ? 26.382  18.246  34.822 1.00 64.70  ?  287 PRO   A C   1 
ATOM   2075 O  O   . PRO   A 1 280 ? 27.183  18.361  33.892 1.00 67.86  ?  287 PRO   A O   1 
ATOM   2076 C  CB  . PRO   A 1 280 ? 23.969  18.821  34.223 1.00 69.92  ?  287 PRO   A CB  1 
ATOM   2077 C  CG  . PRO   A 1 280 ? 23.132  18.940  35.431 1.00 67.37  ?  287 PRO   A CG  1 
ATOM   2078 C  CD  . PRO   A 1 280 ? 23.121  17.599  36.091 1.00 64.12  ?  287 PRO   A CD  1 
ATOM   2079 N  N   . PHE   A 1 281 ? 26.678  18.552  36.094 1.00 63.74  ?  288 PHE   A N   1 
ATOM   2080 C  CA  . PHE   A 1 281 ? 28.039  18.912  36.508 1.00 71.39  ?  288 PHE   A CA  1 
ATOM   2081 C  C   . PHE   A 1 281 ? 29.002  17.745  36.321 1.00 69.67  ?  288 PHE   A C   1 
ATOM   2082 O  O   . PHE   A 1 281 ? 30.091  17.930  35.756 1.00 76.01  ?  288 PHE   A O   1 
ATOM   2083 C  CB  . PHE   A 1 281 ? 28.104  19.462  37.955 1.00 71.37  ?  288 PHE   A CB  1 
ATOM   2084 C  CG  . PHE   A 1 281 ? 29.512  19.668  38.451 1.00 68.49  ?  288 PHE   A CG  1 
ATOM   2085 C  CD1 . PHE   A 1 281 ? 30.289  20.737  37.990 1.00 69.81  ?  288 PHE   A CD1 1 
ATOM   2086 C  CD2 . PHE   A 1 281 ? 30.102  18.730  39.312 1.00 64.76  ?  288 PHE   A CD2 1 
ATOM   2087 C  CE1 . PHE   A 1 281 ? 31.615  20.878  38.394 1.00 66.98  ?  288 PHE   A CE1 1 
ATOM   2088 C  CE2 . PHE   A 1 281 ? 31.417  18.884  39.739 1.00 65.65  ?  288 PHE   A CE2 1 
ATOM   2089 C  CZ  . PHE   A 1 281 ? 32.175  19.972  39.286 1.00 65.61  ?  288 PHE   A CZ  1 
ATOM   2090 N  N   . TYR   A 1 282 ? 28.595  16.565  36.794 1.00 70.27  ?  289 TYR   A N   1 
ATOM   2091 C  CA  . TYR   A 1 282 ? 29.355  15.331  36.579 1.00 69.15  ?  289 TYR   A CA  1 
ATOM   2092 C  C   . TYR   A 1 282 ? 29.640  15.082  35.095 1.00 76.52  ?  289 TYR   A C   1 
ATOM   2093 O  O   . TYR   A 1 282 ? 30.769  14.749  34.746 1.00 85.12  ?  289 TYR   A O   1 
ATOM   2094 C  CB  . TYR   A 1 282 ? 28.652  14.094  37.203 1.00 68.08  ?  289 TYR   A CB  1 
ATOM   2095 C  CG  . TYR   A 1 282 ? 29.328  12.806  36.821 1.00 61.73  ?  289 TYR   A CG  1 
ATOM   2096 C  CD1 . TYR   A 1 282 ? 30.577  12.481  37.348 1.00 62.82  ?  289 TYR   A CD1 1 
ATOM   2097 C  CD2 . TYR   A 1 282 ? 28.777  11.954  35.850 1.00 62.39  ?  289 TYR   A CD2 1 
ATOM   2098 C  CE1 . TYR   A 1 282 ? 31.243  11.315  36.971 1.00 60.83  ?  289 TYR   A CE1 1 
ATOM   2099 C  CE2 . TYR   A 1 282 ? 29.432  10.793  35.462 1.00 60.29  ?  289 TYR   A CE2 1 
ATOM   2100 C  CZ  . TYR   A 1 282 ? 30.670  10.477  36.021 1.00 62.13  ?  289 TYR   A CZ  1 
ATOM   2101 O  OH  . TYR   A 1 282 ? 31.331  9.328   35.640 1.00 65.78  ?  289 TYR   A OH  1 
ATOM   2102 N  N   . LEU   A 1 283 ? 28.616  15.237  34.248 1.00 81.69  ?  290 LEU   A N   1 
ATOM   2103 C  CA  . LEU   A 1 283 ? 28.713  14.943  32.809 1.00 86.96  ?  290 LEU   A CA  1 
ATOM   2104 C  C   . LEU   A 1 283 ? 29.606  15.920  32.040 1.00 91.15  ?  290 LEU   A C   1 
ATOM   2105 O  O   . LEU   A 1 283 ? 30.481  15.491  31.271 1.00 93.09  ?  290 LEU   A O   1 
ATOM   2106 C  CB  . LEU   A 1 283 ? 27.317  14.879  32.159 1.00 92.12  ?  290 LEU   A CB  1 
ATOM   2107 C  CG  . LEU   A 1 283 ? 26.459  13.668  32.550 1.00 96.94  ?  290 LEU   A CG  1 
ATOM   2108 C  CD1 . LEU   A 1 283 ? 24.987  13.908  32.232 1.00 92.76  ?  290 LEU   A CD1 1 
ATOM   2109 C  CD2 . LEU   A 1 283 ? 26.949  12.401  31.863 1.00 101.00 ?  290 LEU   A CD2 1 
ATOM   2110 N  N   . SER   A 1 284 ? 29.400  17.221  32.258 1.00 90.59  ?  291 SER   A N   1 
ATOM   2111 C  CA  . SER   A 1 284 ? 30.190  18.260  31.579 1.00 91.46  ?  291 SER   A CA  1 
ATOM   2112 C  C   . SER   A 1 284 ? 31.639  18.336  32.079 1.00 90.02  ?  291 SER   A C   1 
ATOM   2113 O  O   . SER   A 1 284 ? 32.539  18.338  31.260 1.00 101.32 ?  291 SER   A O   1 
ATOM   2114 C  CB  . SER   A 1 284 ? 29.512  19.636  31.652 1.00 88.90  ?  291 SER   A CB  1 
ATOM   2115 O  OG  . SER   A 1 284 ? 29.156  19.987  32.980 1.00 82.62  ?  291 SER   A OG  1 
ATOM   2116 N  N   . GLN   A 1 285 ? 31.852  18.329  33.402 1.00 89.58  ?  292 GLN   A N   1 
ATOM   2117 C  CA  . GLN   A 1 285 ? 33.156  18.624  34.012 1.00 87.83  ?  292 GLN   A CA  1 
ATOM   2118 C  C   . GLN   A 1 285 ? 34.006  17.416  34.425 1.00 83.20  ?  292 GLN   A C   1 
ATOM   2119 O  O   . GLN   A 1 285 ? 35.218  17.466  34.252 1.00 86.25  ?  292 GLN   A O   1 
ATOM   2120 C  CB  . GLN   A 1 285 ? 32.955  19.536  35.225 1.00 91.83  ?  292 GLN   A CB  1 
ATOM   2121 C  CG  . GLN   A 1 285 ? 32.362  20.901  34.880 1.00 97.48  ?  292 GLN   A CG  1 
ATOM   2122 C  CD  . GLN   A 1 285 ? 33.365  22.035  35.009 1.00 111.68 ?  292 GLN   A CD  1 
ATOM   2123 O  OE1 . GLN   A 1 285 ? 33.148  22.978  35.778 1.00 127.93 ?  292 GLN   A OE1 1 
ATOM   2124 N  NE2 . GLN   A 1 285 ? 34.479  21.947  34.273 1.00 106.19 ?  292 GLN   A NE2 1 
ATOM   2125 N  N   . LEU   A 1 286 ? 33.385  16.364  34.972 1.00 79.97  ?  293 LEU   A N   1 
ATOM   2126 C  CA  . LEU   A 1 286 ? 34.102  15.255  35.630 1.00 80.75  ?  293 LEU   A CA  1 
ATOM   2127 C  C   . LEU   A 1 286 ? 34.239  13.941  34.847 1.00 81.81  ?  293 LEU   A C   1 
ATOM   2128 O  O   . LEU   A 1 286 ? 35.253  13.270  35.004 1.00 70.49  ?  293 LEU   A O   1 
ATOM   2129 C  CB  . LEU   A 1 286 ? 33.493  14.979  36.996 1.00 78.04  ?  293 LEU   A CB  1 
ATOM   2130 C  CG  . LEU   A 1 286 ? 33.423  16.158  37.975 1.00 83.49  ?  293 LEU   A CG  1 
ATOM   2131 C  CD1 . LEU   A 1 286 ? 32.820  15.664  39.284 1.00 87.55  ?  293 LEU   A CD1 1 
ATOM   2132 C  CD2 . LEU   A 1 286 ? 34.775  16.813  38.232 1.00 82.35  ?  293 LEU   A CD2 1 
ATOM   2133 N  N   . GLU   A 1 287 ? 33.252  13.585  34.018 1.00 90.59  ?  294 GLU   A N   1 
ATOM   2134 C  CA  . GLU   A 1 287 ? 33.259  12.309  33.278 1.00 96.85  ?  294 GLU   A CA  1 
ATOM   2135 C  C   . GLU   A 1 287 ? 34.357  12.260  32.208 1.00 105.64 ?  294 GLU   A C   1 
ATOM   2136 O  O   . GLU   A 1 287 ? 35.414  11.653  32.420 1.00 93.66  ?  294 GLU   A O   1 
ATOM   2137 C  CB  . GLU   A 1 287 ? 31.887  12.044  32.630 1.00 101.33 ?  294 GLU   A CB  1 
ATOM   2138 C  CG  . GLU   A 1 287 ? 31.695  10.625  32.106 1.00 100.35 ?  294 GLU   A CG  1 
ATOM   2139 C  CD  . GLU   A 1 287 ? 30.289  10.309  31.660 0.00 100.63 ?  294 GLU   A CD  1 
ATOM   2140 O  OE1 . GLU   A 1 287 ? 29.806  10.961  30.709 0.00 102.70 ?  294 GLU   A OE1 1 
ATOM   2141 O  OE2 . GLU   A 1 287 ? 29.653  9.407   32.249 0.00 98.63  ?  294 GLU   A OE2 1 
ATOM   2142 N  N   . ASN   B 1 1   ? 5.824   20.914  41.598 1.00 105.62 ?  8   ASN   B N   1 
ATOM   2143 C  CA  . ASN   B 1 1   ? 4.765   21.769  40.936 1.00 108.93 ?  8   ASN   B CA  1 
ATOM   2144 C  C   . ASN   B 1 1   ? 5.047   22.024  39.451 1.00 105.93 ?  8   ASN   B C   1 
ATOM   2145 O  O   . ASN   B 1 1   ? 6.203   21.987  39.013 1.00 105.94 ?  8   ASN   B O   1 
ATOM   2146 C  CB  . ASN   B 1 1   ? 4.592   23.132  41.646 1.00 112.77 ?  8   ASN   B CB  1 
ATOM   2147 C  CG  . ASN   B 1 1   ? 3.971   23.022  43.044 1.00 114.45 ?  8   ASN   B CG  1 
ATOM   2148 O  OD1 . ASN   B 1 1   ? 3.988   21.962  43.678 1.00 112.16 ?  8   ASN   B OD1 1 
ATOM   2149 N  ND2 . ASN   B 1 1   ? 3.440   24.140  43.540 1.00 115.24 ?  8   ASN   B ND2 1 
ATOM   2150 N  N   . VAL   B 1 2   ? 3.979   22.301  38.704 1.00 111.51 ?  9   VAL   B N   1 
ATOM   2151 C  CA  . VAL   B 1 2   ? 4.046   22.560  37.253 1.00 116.44 ?  9   VAL   B CA  1 
ATOM   2152 C  C   . VAL   B 1 2   ? 4.383   24.039  37.040 1.00 112.57 ?  9   VAL   B C   1 
ATOM   2153 O  O   . VAL   B 1 2   ? 3.782   24.915  37.678 1.00 124.37 ?  9   VAL   B O   1 
ATOM   2154 C  CB  . VAL   B 1 2   ? 2.719   22.159  36.544 1.00 121.67 ?  9   VAL   B CB  1 
ATOM   2155 C  CG1 . VAL   B 1 2   ? 2.697   22.536  35.065 1.00 125.54 ?  9   VAL   B CG1 1 
ATOM   2156 C  CG2 . VAL   B 1 2   ? 2.495   20.664  36.680 1.00 122.75 ?  9   VAL   B CG2 1 
ATOM   2157 N  N   . ILE   B 1 3   ? 5.318   24.312  36.128 1.00 101.19 ?  10  ILE   B N   1 
ATOM   2158 C  CA  . ILE   B 1 3   ? 5.631   25.693  35.717 1.00 101.38 ?  10  ILE   B CA  1 
ATOM   2159 C  C   . ILE   B 1 3   ? 4.623   26.082  34.630 1.00 100.11 ?  10  ILE   B C   1 
ATOM   2160 O  O   . ILE   B 1 3   ? 4.553   25.427  33.591 1.00 98.26  ?  10  ILE   B O   1 
ATOM   2161 C  CB  . ILE   B 1 3   ? 7.089   25.853  35.229 1.00 99.15  ?  10  ILE   B CB  1 
ATOM   2162 C  CG1 . ILE   B 1 3   ? 8.070   25.554  36.371 1.00 100.57 ?  10  ILE   B CG1 1 
ATOM   2163 C  CG2 . ILE   B 1 3   ? 7.366   27.272  34.726 1.00 101.51 ?  10  ILE   B CG2 1 
ATOM   2164 C  CD1 . ILE   B 1 3   ? 9.498   25.273  35.992 0.00 101.12 ?  10  ILE   B CD1 1 
ATOM   2165 N  N   . LYS   B 1 4   ? 3.860   27.150  34.868 1.00 103.42 ?  11  LYS   B N   1 
ATOM   2166 C  CA  . LYS   B 1 4   ? 2.920   27.698  33.878 1.00 100.14 ?  11  LYS   B CA  1 
ATOM   2167 C  C   . LYS   B 1 4   ? 3.682   28.718  33.029 1.00 94.30  ?  11  LYS   B C   1 
ATOM   2168 O  O   . LYS   B 1 4   ? 4.159   29.723  33.558 1.00 92.45  ?  11  LYS   B O   1 
ATOM   2169 C  CB  . LYS   B 1 4   ? 1.697   28.340  34.557 1.00 104.36 ?  11  LYS   B CB  1 
ATOM   2170 C  CG  . LYS   B 1 4   ? 0.752   27.354  35.239 1.00 103.97 ?  11  LYS   B CG  1 
ATOM   2171 C  CD  . LYS   B 1 4   ? 0.139   27.890  36.513 0.00 108.45 ?  11  LYS   B CD  1 
ATOM   2172 C  CE  . LYS   B 1 4   ? -0.713  26.845  37.217 0.00 109.51 ?  11  LYS   B CE  1 
ATOM   2173 N  NZ  . LYS   B 1 4   ? -1.057  27.243  38.610 0.00 112.63 ?  11  LYS   B NZ  1 
ATOM   2174 N  N   . MET   B 1 5   ? 3.805   28.437  31.731 1.00 94.14  ?  12  MET   B N   1 
ATOM   2175 C  CA  . MET   B 1 5   ? 4.508   29.297  30.758 1.00 88.92  ?  12  MET   B CA  1 
ATOM   2176 C  C   . MET   B 1 5   ? 3.513   29.988  29.826 1.00 86.39  ?  12  MET   B C   1 
ATOM   2177 O  O   . MET   B 1 5   ? 2.336   29.603  29.754 1.00 81.65  ?  12  MET   B O   1 
ATOM   2178 C  CB  . MET   B 1 5   ? 5.481   28.457  29.925 1.00 82.77  ?  12  MET   B CB  1 
ATOM   2179 C  CG  . MET   B 1 5   ? 6.724   27.998  30.662 1.00 79.20  ?  12  MET   B CG  1 
ATOM   2180 S  SD  . MET   B 1 5   ? 7.542   26.748  29.661 1.00 79.76  ?  12  MET   B SD  1 
ATOM   2181 C  CE  . MET   B 1 5   ? 8.997   26.398  30.651 1.00 76.89  ?  12  MET   B CE  1 
ATOM   2182 N  N   . LYS   B 1 6   ? 4.012   30.997  29.108 1.00 85.67  ?  13  LYS   B N   1 
ATOM   2183 C  CA  . LYS   B 1 6   ? 3.240   31.784  28.142 1.00 85.75  ?  13  LYS   B CA  1 
ATOM   2184 C  C   . LYS   B 1 6   ? 3.855   31.624  26.755 1.00 85.50  ?  13  LYS   B C   1 
ATOM   2185 O  O   . LYS   B 1 6   ? 5.043   31.310  26.618 1.00 82.58  ?  13  LYS   B O   1 
ATOM   2186 C  CB  . LYS   B 1 6   ? 3.233   33.268  28.543 1.00 86.74  ?  13  LYS   B CB  1 
ATOM   2187 C  CG  . LYS   B 1 6   ? 2.624   33.559  29.918 1.00 89.08  ?  13  LYS   B CG  1 
ATOM   2188 C  CD  . LYS   B 1 6   ? 2.167   35.009  30.091 1.00 91.95  ?  13  LYS   B CD  1 
ATOM   2189 C  CE  . LYS   B 1 6   ? 0.767   35.257  29.530 1.00 94.68  ?  13  LYS   B CE  1 
ATOM   2190 N  NZ  . LYS   B 1 6   ? 0.272   36.585  29.488 0.00 94.13  ?  13  LYS   B NZ  1 
ATOM   2191 N  N   . SER   B 1 7   ? 3.035   31.842  25.727 1.00 89.16  ?  14  SER   B N   1 
ATOM   2192 C  CA  . SER   B 1 7   ? 3.487   31.782  24.324 1.00 94.03  ?  14  SER   B CA  1 
ATOM   2193 C  C   . SER   B 1 7   ? 4.456   32.922  23.955 1.00 94.75  ?  14  SER   B C   1 
ATOM   2194 O  O   . SER   B 1 7   ? 5.395   32.705  23.179 1.00 90.48  ?  14  SER   B O   1 
ATOM   2195 C  CB  . SER   B 1 7   ? 2.288   31.765  23.364 1.00 94.33  ?  14  SER   B CB  1 
ATOM   2196 O  OG  . SER   B 1 7   ? 1.480   30.602  23.553 1.00 91.80  ?  14  SER   B OG  1 
ATOM   2197 N  N   . SER   B 1 8   ? 4.215   34.115  24.516 1.00 98.98  ?  15  SER   B N   1 
ATOM   2198 C  CA  . SER   B 1 8   ? 5.121   35.284  24.419 1.00 100.09 ?  15  SER   B CA  1 
ATOM   2199 C  C   . SER   B 1 8   ? 6.533   35.072  24.975 1.00 101.21 ?  15  SER   B C   1 
ATOM   2200 O  O   . SER   B 1 8   ? 7.464   35.763  24.548 1.00 105.18 ?  15  SER   B O   1 
ATOM   2201 C  CB  . SER   B 1 8   ? 4.509   36.513  25.123 1.00 105.66 ?  15  SER   B CB  1 
ATOM   2202 O  OG  . SER   B 1 8   ? 4.443   36.330  26.532 1.00 101.93 ?  15  SER   B OG  1 
ATOM   2203 N  N   . ASP   B 1 9   ? 6.686   34.141  25.922 1.00 94.86  ?  16  ASP   B N   1 
ATOM   2204 C  CA  . ASP   B 1 9   ? 8.010   33.724  26.412 1.00 96.80  ?  16  ASP   B CA  1 
ATOM   2205 C  C   . ASP   B 1 9   ? 8.894   33.008  25.370 1.00 94.60  ?  16  ASP   B C   1 
ATOM   2206 O  O   . ASP   B 1 9   ? 10.104  32.918  25.590 1.00 89.24  ?  16  ASP   B O   1 
ATOM   2207 C  CB  . ASP   B 1 9   ? 7.906   32.815  27.658 1.00 100.77 ?  16  ASP   B CB  1 
ATOM   2208 C  CG  . ASP   B 1 9   ? 7.180   33.468  28.839 1.00 108.39 ?  16  ASP   B CG  1 
ATOM   2209 O  OD1 . ASP   B 1 9   ? 7.100   34.716  28.909 1.00 122.48 ?  16  ASP   B OD1 1 
ATOM   2210 O  OD2 . ASP   B 1 9   ? 6.682   32.710  29.701 1.00 104.09 ?  16  ASP   B OD2 1 
ATOM   2211 N  N   . PHE   B 1 10  ? 8.303   32.508  24.272 1.00 89.05  ?  17  PHE   B N   1 
ATOM   2212 C  CA  . PHE   B 1 10  ? 9.034   31.822  23.192 1.00 84.67  ?  17  PHE   B CA  1 
ATOM   2213 C  C   . PHE   B 1 10  ? 9.070   32.701  21.944 1.00 89.16  ?  17  PHE   B C   1 
ATOM   2214 O  O   . PHE   B 1 10  ? 8.033   33.286  21.556 1.00 95.93  ?  17  PHE   B O   1 
ATOM   2215 C  CB  . PHE   B 1 10  ? 8.379   30.475  22.889 1.00 80.95  ?  17  PHE   B CB  1 
ATOM   2216 C  CG  . PHE   B 1 10  ? 8.457   29.509  24.031 1.00 76.89  ?  17  PHE   B CG  1 
ATOM   2217 C  CD1 . PHE   B 1 10  ? 9.585   28.695  24.186 1.00 75.28  ?  17  PHE   B CD1 1 
ATOM   2218 C  CD2 . PHE   B 1 10  ? 7.432   29.440  24.987 1.00 74.65  ?  17  PHE   B CD2 1 
ATOM   2219 C  CE1 . PHE   B 1 10  ? 9.677   27.803  25.249 1.00 74.23  ?  17  PHE   B CE1 1 
ATOM   2220 C  CE2 . PHE   B 1 10  ? 7.522   28.551  26.050 1.00 74.36  ?  17  PHE   B CE2 1 
ATOM   2221 C  CZ  . PHE   B 1 10  ? 8.648   27.728  26.180 1.00 73.21  ?  17  PHE   B CZ  1 
ATOM   2222 N  N   . LEU   B 1 11  ? 10.252  32.789  21.312 1.00 92.37  ?  18  LEU   B N   1 
ATOM   2223 C  CA  . LEU   B 1 11  ? 10.486  33.733  20.197 1.00 92.68  ?  18  LEU   B CA  1 
ATOM   2224 C  C   . LEU   B 1 11  ? 9.996   33.192  18.861 1.00 97.99  ?  18  LEU   B C   1 
ATOM   2225 O  O   . LEU   B 1 11  ? 9.233   33.858  18.165 1.00 99.52  ?  18  LEU   B O   1 
ATOM   2226 C  CB  . LEU   B 1 11  ? 11.962  34.099  20.090 1.00 99.52  ?  18  LEU   B CB  1 
ATOM   2227 C  CG  . LEU   B 1 11  ? 12.710  34.516  21.356 1.00 99.19  ?  18  LEU   B CG  1 
ATOM   2228 C  CD1 . LEU   B 1 11  ? 14.118  34.960  20.971 1.00 95.78  ?  18  LEU   B CD1 1 
ATOM   2229 C  CD2 . LEU   B 1 11  ? 12.019  35.636  22.119 1.00 103.66 ?  18  LEU   B CD2 1 
ATOM   2230 N  N   . GLU   B 1 12  ? 10.465  31.989  18.521 1.00 105.61 ?  19  GLU   B N   1 
ATOM   2231 C  CA  . GLU   B 1 12  ? 10.086  31.267  17.294 1.00 105.44 ?  19  GLU   B CA  1 
ATOM   2232 C  C   . GLU   B 1 12  ? 9.960   29.762  17.576 1.00 103.72 ?  19  GLU   B C   1 
ATOM   2233 O  O   . GLU   B 1 12  ? 10.504  29.264  18.575 1.00 90.60  ?  19  GLU   B O   1 
ATOM   2234 C  CB  . GLU   B 1 12  ? 11.117  31.500  16.182 1.00 102.85 ?  19  GLU   B CB  1 
ATOM   2235 C  CG  . GLU   B 1 12  ? 11.338  32.957  15.775 1.00 103.74 ?  19  GLU   B CG  1 
ATOM   2236 C  CD  . GLU   B 1 12  ? 10.118  33.639  15.158 1.00 107.53 ?  19  GLU   B CD  1 
ATOM   2237 O  OE1 . GLU   B 1 12  ? 9.204   32.954  14.646 1.00 109.25 ?  19  GLU   B OE1 1 
ATOM   2238 O  OE2 . GLU   B 1 12  ? 10.072  34.885  15.190 1.00 102.83 ?  19  GLU   B OE2 1 
ATOM   2239 N  N   . SER   B 1 13  ? 9.245   29.069  16.680 1.00 107.45 ?  20  SER   B N   1 
ATOM   2240 C  CA  . SER   B 1 13  ? 8.878   27.647  16.828 1.00 106.26 ?  20  SER   B CA  1 
ATOM   2241 C  C   . SER   B 1 13  ? 8.892   26.905  15.471 1.00 108.69 ?  20  SER   B C   1 
ATOM   2242 O  O   . SER   B 1 13  ? 7.874   26.867  14.761 1.00 113.22 ?  20  SER   B O   1 
ATOM   2243 C  CB  . SER   B 1 13  ? 7.515   27.508  17.531 1.00 108.88 ?  20  SER   B CB  1 
ATOM   2244 O  OG  . SER   B 1 13  ? 6.473   28.124  16.790 1.00 118.67 ?  20  SER   B OG  1 
ATOM   2245 N  N   . ALA   B 1 14  ? 10.052  26.323  15.133 1.00 100.23 ?  21  ALA   B N   1 
ATOM   2246 C  CA  . ALA   B 1 14  ? 10.288  25.630  13.846 1.00 98.23  ?  21  ALA   B CA  1 
ATOM   2247 C  C   . ALA   B 1 14  ? 9.921   24.139  13.922 1.00 99.53  ?  21  ALA   B C   1 
ATOM   2248 O  O   . ALA   B 1 14  ? 10.571  23.372  14.661 1.00 92.65  ?  21  ALA   B O   1 
ATOM   2249 C  CB  . ALA   B 1 14  ? 11.740  25.788  13.410 1.00 96.16  ?  21  ALA   B CB  1 
ATOM   2250 N  N   . GLU   B 1 15  ? 8.911   23.742  13.134 1.00 99.79  ?  22  GLU   B N   1 
ATOM   2251 C  CA  . GLU   B 1 15  ? 8.331   22.377  13.142 1.00 96.50  ?  22  GLU   B CA  1 
ATOM   2252 C  C   . GLU   B 1 15  ? 9.336   21.359  12.611 1.00 89.82  ?  22  GLU   B C   1 
ATOM   2253 O  O   . GLU   B 1 15  ? 9.769   21.477  11.464 1.00 92.97  ?  22  GLU   B O   1 
ATOM   2254 C  CB  . GLU   B 1 15  ? 7.028   22.341  12.318 1.00 104.72 ?  22  GLU   B CB  1 
ATOM   2255 C  CG  . GLU   B 1 15  ? 5.886   23.164  12.924 1.00 111.43 ?  22  GLU   B CG  1 
ATOM   2256 C  CD  . GLU   B 1 15  ? 5.261   24.148  11.951 1.00 118.06 ?  22  GLU   B CD  1 
ATOM   2257 O  OE1 . GLU   B 1 15  ? 4.856   23.722  10.856 1.00 125.98 ?  22  GLU   B OE1 1 
ATOM   2258 O  OE2 . GLU   B 1 15  ? 5.168   25.349  12.284 1.00 125.64 ?  22  GLU   B OE2 1 
ATOM   2259 N  N   . LEU   B 1 16  ? 9.723   20.385  13.443 1.00 85.25  ?  23  LEU   B N   1 
ATOM   2260 C  CA  . LEU   B 1 16  ? 10.823  19.457  13.100 1.00 90.59  ?  23  LEU   B CA  1 
ATOM   2261 C  C   . LEU   B 1 16  ? 10.330  18.045  12.688 1.00 98.77  ?  23  LEU   B C   1 
ATOM   2262 O  O   . LEU   B 1 16  ? 9.283   17.576  13.152 1.00 98.90  ?  23  LEU   B O   1 
ATOM   2263 C  CB  . LEU   B 1 16  ? 11.918  19.457  14.186 1.00 82.79  ?  23  LEU   B CB  1 
ATOM   2264 C  CG  . LEU   B 1 16  ? 11.661  19.079  15.644 1.00 80.13  ?  23  LEU   B CG  1 
ATOM   2265 C  CD1 . LEU   B 1 16  ? 11.528  17.577  15.815 1.00 82.93  ?  23  LEU   B CD1 1 
ATOM   2266 C  CD2 . LEU   B 1 16  ? 12.792  19.572  16.529 1.00 77.89  ?  23  LEU   B CD2 1 
ATOM   2267 N  N   . ASP   B 1 17  ? 11.122  17.394  11.824 1.00 105.59 ?  24  ASP   B N   1 
ATOM   2268 C  CA  . ASP   B 1 17  ? 10.711  16.225  11.020 1.00 109.06 ?  24  ASP   B CA  1 
ATOM   2269 C  C   . ASP   B 1 17  ? 10.568  14.920  11.821 1.00 117.61 ?  24  ASP   B C   1 
ATOM   2270 O  O   . ASP   B 1 17  ? 11.566  14.284  12.166 1.00 121.23 ?  24  ASP   B O   1 
ATOM   2271 C  CB  . ASP   B 1 17  ? 11.721  16.029  9.860  1.00 114.54 ?  24  ASP   B CB  1 
ATOM   2272 C  CG  . ASP   B 1 17  ? 11.342  14.896  8.877  1.00 113.64 ?  24  ASP   B CG  1 
ATOM   2273 O  OD1 . ASP   B 1 17  ? 10.165  14.475  8.796  1.00 119.08 ?  24  ASP   B OD1 1 
ATOM   2274 O  OD2 . ASP   B 1 17  ? 12.251  14.445  8.149  1.00 104.82 ?  24  ASP   B OD2 1 
ATOM   2275 N  N   . SER   B 1 18  ? 9.318   14.538  12.097 1.00 119.59 ?  25  SER   B N   1 
ATOM   2276 C  CA  . SER   B 1 18  ? 8.965   13.158  12.472 1.00 118.41 ?  25  SER   B CA  1 
ATOM   2277 C  C   . SER   B 1 18  ? 7.482   12.849  12.221 1.00 126.69 ?  25  SER   B C   1 
ATOM   2278 O  O   . SER   B 1 18  ? 6.720   13.690  11.735 1.00 134.28 ?  25  SER   B O   1 
ATOM   2279 C  CB  . SER   B 1 18  ? 9.316   12.867  13.937 1.00 117.34 ?  25  SER   B CB  1 
ATOM   2280 O  OG  . SER   B 1 18  ? 9.211   11.481  14.215 1.00 110.85 ?  25  SER   B OG  1 
ATOM   2281 N  N   . LYS   B 1 23  ? 1.824   19.573  16.960 1.00 115.52 ?  30  LYS   B N   1 
ATOM   2282 C  CA  . LYS   B 1 23  ? 3.082   19.641  16.221 1.00 120.08 ?  30  LYS   B CA  1 
ATOM   2283 C  C   . LYS   B 1 23  ? 4.260   19.789  17.189 1.00 115.30 ?  30  LYS   B C   1 
ATOM   2284 O  O   . LYS   B 1 23  ? 4.249   20.696  18.027 1.00 116.21 ?  30  LYS   B O   1 
ATOM   2285 C  CB  . LYS   B 1 23  ? 3.089   20.819  15.232 1.00 131.10 ?  30  LYS   B CB  1 
ATOM   2286 C  CG  . LYS   B 1 23  ? 1.828   21.014  14.386 1.00 142.82 ?  30  LYS   B CG  1 
ATOM   2287 C  CD  . LYS   B 1 23  ? 1.533   19.845  13.458 1.00 148.18 ?  30  LYS   B CD  1 
ATOM   2288 C  CE  . LYS   B 1 23  ? 0.195   19.951  12.767 0.00 152.13 ?  30  LYS   B CE  1 
ATOM   2289 N  NZ  . LYS   B 1 23  ? -0.056  18.836  11.812 0.00 154.54 ?  30  LYS   B NZ  1 
ATOM   2290 N  N   . VAL   B 1 24  ? 5.242   18.890  17.079 1.00 110.99 ?  31  VAL   B N   1 
ATOM   2291 C  CA  . VAL   B 1 24  ? 6.493   18.953  17.862 1.00 100.35 ?  31  VAL   B CA  1 
ATOM   2292 C  C   . VAL   B 1 24  ? 7.424   19.921  17.131 1.00 91.02  ?  31  VAL   B C   1 
ATOM   2293 O  O   . VAL   B 1 24  ? 7.610   19.802  15.915 1.00 89.87  ?  31  VAL   B O   1 
ATOM   2294 C  CB  . VAL   B 1 24  ? 7.177   17.567  18.009 1.00 103.95 ?  31  VAL   B CB  1 
ATOM   2295 C  CG1 . VAL   B 1 24  ? 8.431   17.650  18.884 1.00 98.10  ?  31  VAL   B CG1 1 
ATOM   2296 C  CG2 . VAL   B 1 24  ? 6.213   16.536  18.598 1.00 110.33 ?  31  VAL   B CG2 1 
ATOM   2297 N  N   . SER   B 1 25  ? 8.026   20.853  17.876 1.00 84.24  ?  32  SER   B N   1 
ATOM   2298 C  CA  . SER   B 1 25  ? 8.847   21.925  17.301 1.00 81.01  ?  32  SER   B CA  1 
ATOM   2299 C  C   . SER   B 1 25  ? 9.890   22.466  18.278 1.00 74.87  ?  32  SER   B C   1 
ATOM   2300 O  O   . SER   B 1 25  ? 9.735   22.374  19.502 1.00 71.37  ?  32  SER   B O   1 
ATOM   2301 C  CB  . SER   B 1 25  ? 7.958   23.059  16.777 1.00 85.07  ?  32  SER   B CB  1 
ATOM   2302 O  OG  . SER   B 1 25  ? 7.091   23.557  17.772 1.00 86.77  ?  32  SER   B OG  1 
ATOM   2303 N  N   . LEU   B 1 26  ? 10.972  22.998  17.712 1.00 74.83  ?  33  LEU   B N   1 
ATOM   2304 C  CA  . LEU   B 1 26  ? 12.084  23.528  18.504 1.00 73.14  ?  33  LEU   B CA  1 
ATOM   2305 C  C   . LEU   B 1 26  ? 11.733  24.955  18.914 1.00 73.89  ?  33  LEU   B C   1 
ATOM   2306 O  O   . LEU   B 1 26  ? 11.383  25.777  18.064 1.00 75.47  ?  33  LEU   B O   1 
ATOM   2307 C  CB  . LEU   B 1 26  ? 13.382  23.488  17.706 1.00 74.89  ?  33  LEU   B CB  1 
ATOM   2308 C  CG  . LEU   B 1 26  ? 14.690  23.754  18.444 1.00 76.81  ?  33  LEU   B CG  1 
ATOM   2309 C  CD1 . LEU   B 1 26  ? 14.875  22.786  19.598 1.00 75.70  ?  33  LEU   B CD1 1 
ATOM   2310 C  CD2 . LEU   B 1 26  ? 15.862  23.650  17.474 1.00 80.95  ?  33  LEU   B CD2 1 
ATOM   2311 N  N   . ALA   B 1 27  ? 11.869  25.263  20.202 1.00 71.70  ?  34  ALA   B N   1 
ATOM   2312 C  CA  . ALA   B 1 27  ? 11.349  26.511  20.796 1.00 73.60  ?  34  ALA   B CA  1 
ATOM   2313 C  C   . ALA   B 1 27  ? 12.405  27.172  21.666 1.00 75.19  ?  34  ALA   B C   1 
ATOM   2314 O  O   . ALA   B 1 27  ? 12.948  26.506  22.546 1.00 82.15  ?  34  ALA   B O   1 
ATOM   2315 C  CB  . ALA   B 1 27  ? 10.118  26.197  21.632 1.00 72.78  ?  34  ALA   B CB  1 
ATOM   2316 N  N   . PHE   B 1 28  ? 12.698  28.454  21.418 1.00 82.76  ?  35  PHE   B N   1 
ATOM   2317 C  CA  . PHE   B 1 28  ? 13.655  29.221  22.223 1.00 87.61  ?  35  PHE   B CA  1 
ATOM   2318 C  C   . PHE   B 1 28  ? 12.913  30.068  23.266 1.00 83.63  ?  35  PHE   B C   1 
ATOM   2319 O  O   . PHE   B 1 28  ? 12.300  31.074  22.930 1.00 80.05  ?  35  PHE   B O   1 
ATOM   2320 C  CB  . PHE   B 1 28  ? 14.527  30.100  21.319 1.00 91.95  ?  35  PHE   B CB  1 
ATOM   2321 C  CG  . PHE   B 1 28  ? 15.687  30.746  22.033 1.00 97.69  ?  35  PHE   B CG  1 
ATOM   2322 C  CD1 . PHE   B 1 28  ? 16.871  30.033  22.276 1.00 95.75  ?  35  PHE   B CD1 1 
ATOM   2323 C  CD2 . PHE   B 1 28  ? 15.601  32.070  22.472 1.00 100.27 ?  35  PHE   B CD2 1 
ATOM   2324 C  CE1 . PHE   B 1 28  ? 17.940  30.633  22.941 1.00 96.24  ?  35  PHE   B CE1 1 
ATOM   2325 C  CE2 . PHE   B 1 28  ? 16.669  32.674  23.136 1.00 101.50 ?  35  PHE   B CE2 1 
ATOM   2326 C  CZ  . PHE   B 1 28  ? 17.839  31.954  23.370 1.00 100.95 ?  35  PHE   B CZ  1 
ATOM   2327 N  N   . HIS   B 1 29  ? 12.979  29.639  24.522 1.00 84.56  ?  36  HIS   B N   1 
ATOM   2328 C  CA  . HIS   B 1 29  ? 12.496  30.413  25.663 1.00 85.76  ?  36  HIS   B CA  1 
ATOM   2329 C  C   . HIS   B 1 29  ? 13.443  31.589  25.889 1.00 89.88  ?  36  HIS   B C   1 
ATOM   2330 O  O   . HIS   B 1 29  ? 14.677  31.402  25.865 1.00 90.10  ?  36  HIS   B O   1 
ATOM   2331 C  CB  . HIS   B 1 29  ? 12.454  29.530  26.918 1.00 88.77  ?  36  HIS   B CB  1 
ATOM   2332 C  CG  . HIS   B 1 29  ? 11.626  30.082  28.036 1.00 89.89  ?  36  HIS   B CG  1 
ATOM   2333 N  ND1 . HIS   B 1 29  ? 12.168  30.557  29.211 1.00 91.07  ?  36  HIS   B ND1 1 
ATOM   2334 C  CD2 . HIS   B 1 29  ? 10.285  30.178  28.182 1.00 93.32  ?  36  HIS   B CD2 1 
ATOM   2335 C  CE1 . HIS   B 1 29  ? 11.201  30.951  30.018 1.00 95.35  ?  36  HIS   B CE1 1 
ATOM   2336 N  NE2 . HIS   B 1 29  ? 10.047  30.732  29.418 1.00 98.05  ?  36  HIS   B NE2 1 
ATOM   2337 N  N   . ARG   B 1 30  ? 12.873  32.773  26.145 1.00 88.71  ?  37  ARG   B N   1 
ATOM   2338 C  CA  . ARG   B 1 30  ? 13.633  34.046  26.170 1.00 87.18  ?  37  ARG   B CA  1 
ATOM   2339 C  C   . ARG   B 1 30  ? 14.686  34.153  27.278 1.00 84.92  ?  37  ARG   B C   1 
ATOM   2340 O  O   . ARG   B 1 30  ? 15.652  34.900  27.110 1.00 88.58  ?  37  ARG   B O   1 
ATOM   2341 C  CB  . ARG   B 1 30  ? 12.698  35.282  26.218 1.00 92.20  ?  37  ARG   B CB  1 
ATOM   2342 C  CG  . ARG   B 1 30  ? 13.381  36.583  25.760 1.00 96.65  ?  37  ARG   B CG  1 
ATOM   2343 C  CD  . ARG   B 1 30  ? 12.510  37.831  25.783 1.00 96.87  ?  37  ARG   B CD  1 
ATOM   2344 N  NE  . ARG   B 1 30  ? 11.637  37.951  24.609 1.00 93.41  ?  37  ARG   B NE  1 
ATOM   2345 C  CZ  . ARG   B 1 30  ? 10.386  37.477  24.494 1.00 89.25  ?  37  ARG   B CZ  1 
ATOM   2346 N  NH1 . ARG   B 1 30  ? 9.779   36.807  25.482 1.00 88.20  ?  37  ARG   B NH1 1 
ATOM   2347 N  NH2 . ARG   B 1 30  ? 9.727   37.663  23.351 1.00 86.49  ?  37  ARG   B NH2 1 
ATOM   2348 N  N   . THR   B 1 31  ? 14.493  33.449  28.400 1.00 84.78  ?  38  THR   B N   1 
ATOM   2349 C  CA  . THR   B 1 31  ? 15.458  33.434  29.542 1.00 85.44  ?  38  THR   B CA  1 
ATOM   2350 C  C   . THR   B 1 31  ? 16.190  32.086  29.820 1.00 89.23  ?  38  THR   B C   1 
ATOM   2351 O  O   . THR   B 1 31  ? 17.265  32.091  30.442 1.00 86.90  ?  38  THR   B O   1 
ATOM   2352 C  CB  . THR   B 1 31  ? 14.771  33.921  30.843 1.00 86.27  ?  38  THR   B CB  1 
ATOM   2353 O  OG1 . THR   B 1 31  ? 13.774  32.983  31.264 1.00 83.98  ?  38  THR   B OG1 1 
ATOM   2354 C  CG2 . THR   B 1 31  ? 14.110  35.308  30.639 1.00 87.96  ?  38  THR   B CG2 1 
ATOM   2355 N  N   . GLN   B 1 32  ? 15.629  30.965  29.339 1.00 88.61  ?  39  GLN   B N   1 
ATOM   2356 C  CA  . GLN   B 1 32  ? 16.077  29.582  29.680 1.00 92.37  ?  39  GLN   B CA  1 
ATOM   2357 C  C   . GLN   B 1 32  ? 16.540  28.723  28.473 1.00 89.40  ?  39  GLN   B C   1 
ATOM   2358 O  O   . GLN   B 1 32  ? 16.861  27.539  28.647 1.00 86.00  ?  39  GLN   B O   1 
ATOM   2359 C  CB  . GLN   B 1 32  ? 14.976  28.807  30.427 1.00 96.59  ?  39  GLN   B CB  1 
ATOM   2360 C  CG  . GLN   B 1 32  ? 14.461  29.407  31.730 1.00 100.32 ?  39  GLN   B CG  1 
ATOM   2361 C  CD  . GLN   B 1 32  ? 13.328  28.577  32.333 1.00 104.27 ?  39  GLN   B CD  1 
ATOM   2362 O  OE1 . GLN   B 1 32  ? 13.276  27.348  32.161 1.00 111.85 ?  39  GLN   B OE1 1 
ATOM   2363 N  NE2 . GLN   B 1 32  ? 12.410  29.239  33.037 1.00 101.59 ?  39  GLN   B NE2 1 
ATOM   2364 N  N   . GLY   B 1 33  ? 16.568  29.297  27.266 1.00 87.67  ?  40  GLY   B N   1 
ATOM   2365 C  CA  . GLY   B 1 33  ? 17.185  28.659  26.119 1.00 81.96  ?  40  GLY   B CA  1 
ATOM   2366 C  C   . GLY   B 1 33  ? 16.285  27.676  25.390 1.00 77.44  ?  40  GLY   B C   1 
ATOM   2367 O  O   . GLY   B 1 33  ? 15.054  27.808  25.371 1.00 75.99  ?  40  GLY   B O   1 
ATOM   2368 N  N   . LEU   B 1 34  ? 16.923  26.666  24.811 1.00 72.74  ?  41  LEU   B N   1 
ATOM   2369 C  CA  . LEU   B 1 34  ? 16.320  25.826  23.775 1.00 69.59  ?  41  LEU   B CA  1 
ATOM   2370 C  C   . LEU   B 1 34  ? 15.476  24.725  24.430 1.00 68.06  ?  41  LEU   B C   1 
ATOM   2371 O  O   . LEU   B 1 34  ? 15.909  24.110  25.417 1.00 64.09  ?  41  LEU   B O   1 
ATOM   2372 C  CB  . LEU   B 1 34  ? 17.431  25.253  22.892 1.00 69.57  ?  41  LEU   B CB  1 
ATOM   2373 C  CG  . LEU   B 1 34  ? 17.299  25.056  21.381 1.00 69.69  ?  41  LEU   B CG  1 
ATOM   2374 C  CD1 . LEU   B 1 34  ? 16.753  26.275  20.652 1.00 68.54  ?  41  LEU   B CD1 1 
ATOM   2375 C  CD2 . LEU   B 1 34  ? 18.660  24.652  20.798 1.00 67.31  ?  41  LEU   B CD2 1 
ATOM   2376 N  N   . MET   B 1 35  ? 14.250  24.537  23.922 1.00 67.36  ?  42  MET   B N   1 
ATOM   2377 C  CA  . MET   B 1 35  ? 13.301  23.510  24.414 1.00 67.00  ?  42  MET   B CA  1 
ATOM   2378 C  C   . MET   B 1 35  ? 12.501  22.911  23.267 1.00 68.83  ?  42  MET   B C   1 
ATOM   2379 O  O   . MET   B 1 35  ? 12.482  23.451  22.161 1.00 70.32  ?  42  MET   B O   1 
ATOM   2380 C  CB  . MET   B 1 35  ? 12.301  24.094  25.413 1.00 68.66  ?  42  MET   B CB  1 
ATOM   2381 C  CG  . MET   B 1 35  ? 12.893  24.693  26.673 1.00 69.59  ?  42  MET   B CG  1 
ATOM   2382 S  SD  . MET   B 1 35  ? 11.612  25.512  27.635 1.00 62.84  ?  42  MET   B SD  1 
ATOM   2383 C  CE  . MET   B 1 35  ? 12.515  25.954  29.117 1.00 62.70  ?  42  MET   B CE  1 
ATOM   2384 N  N   . ILE   B 1 36  ? 11.841  21.794  23.562 1.00 74.27  ?  43  ILE   B N   1 
ATOM   2385 C  CA  . ILE   B 1 36  ? 10.884  21.141  22.658 1.00 77.64  ?  43  ILE   B CA  1 
ATOM   2386 C  C   . ILE   B 1 36  ? 9.480   21.480  23.162 1.00 77.39  ?  43  ILE   B C   1 
ATOM   2387 O  O   . ILE   B 1 36  ? 9.250   21.574  24.362 1.00 74.59  ?  43  ILE   B O   1 
ATOM   2388 C  CB  . ILE   B 1 36  ? 11.119  19.601  22.601 1.00 75.34  ?  43  ILE   B CB  1 
ATOM   2389 C  CG1 . ILE   B 1 36  ? 12.497  19.288  21.998 1.00 74.66  ?  43  ILE   B CG1 1 
ATOM   2390 C  CG2 . ILE   B 1 36  ? 10.033  18.839  21.822 1.00 78.60  ?  43  ILE   B CG2 1 
ATOM   2391 C  CD1 . ILE   B 1 36  ? 12.693  19.675  20.545 1.00 77.70  ?  43  ILE   B CD1 1 
ATOM   2392 N  N   . MET   B 1 37  ? 8.557   21.640  22.213 1.00 75.80  ?  44  MET   B N   1 
ATOM   2393 C  CA  . MET   B 1 37  ? 7.193   22.076  22.468 1.00 80.49  ?  44  MET   B CA  1 
ATOM   2394 C  C   . MET   B 1 37  ? 6.254   21.200  21.653 1.00 87.14  ?  44  MET   B C   1 
ATOM   2395 O  O   . MET   B 1 37  ? 6.254   21.282  20.428 1.00 86.85  ?  44  MET   B O   1 
ATOM   2396 C  CB  . MET   B 1 37  ? 7.011   23.555  22.096 1.00 81.74  ?  44  MET   B CB  1 
ATOM   2397 C  CG  . MET   B 1 37  ? 5.697   24.147  22.571 1.00 84.27  ?  44  MET   B CG  1 
ATOM   2398 S  SD  . MET   B 1 37  ? 5.659   25.940  22.407 1.00 87.51  ?  44  MET   B SD  1 
ATOM   2399 C  CE  . MET   B 1 37  ? 5.528   26.101  20.628 1.00 90.08  ?  44  MET   B CE  1 
ATOM   2400 N  N   . LYS   B 1 38  ? 5.514   20.325  22.337 1.00 89.73  ?  45  LYS   B N   1 
ATOM   2401 C  CA  . LYS   B 1 38  ? 4.396   19.611  21.729 1.00 83.60  ?  45  LYS   B CA  1 
ATOM   2402 C  C   . LYS   B 1 38  ? 3.161   20.483  21.955 1.00 86.36  ?  45  LYS   B C   1 
ATOM   2403 O  O   . LYS   B 1 38  ? 2.673   20.582  23.086 1.00 86.54  ?  45  LYS   B O   1 
ATOM   2404 C  CB  . LYS   B 1 38  ? 4.226   18.205  22.313 1.00 81.27  ?  45  LYS   B CB  1 
ATOM   2405 C  CG  . LYS   B 1 38  ? 3.122   17.424  21.618 1.00 86.42  ?  45  LYS   B CG  1 
ATOM   2406 C  CD  . LYS   B 1 38  ? 3.195   15.921  21.849 1.00 88.97  ?  45  LYS   B CD  1 
ATOM   2407 C  CE  . LYS   B 1 38  ? 2.153   15.191  20.997 1.00 92.49  ?  45  LYS   B CE  1 
ATOM   2408 N  NZ  . LYS   B 1 38  ? 2.586   14.949  19.640 0.00 90.21  ?  45  LYS   B NZ  1 
ATOM   2409 N  N   . THR   B 1 39  ? 2.694   21.141  20.881 1.00 88.66  ?  46  THR   B N   1 
ATOM   2410 C  CA  . THR   B 1 39  ? 1.442   21.902  20.872 1.00 86.61  ?  46  THR   B CA  1 
ATOM   2411 C  C   . THR   B 1 39  ? 0.324   20.932  20.522 1.00 85.38  ?  46  THR   B C   1 
ATOM   2412 O  O   . THR   B 1 39  ? 0.207   20.520  19.375 1.00 81.44  ?  46  THR   B O   1 
ATOM   2413 C  CB  . THR   B 1 39  ? 1.508   23.082  19.884 1.00 89.46  ?  46  THR   B CB  1 
ATOM   2414 O  OG1 . THR   B 1 39  ? 2.592   23.939  20.257 1.00 91.58  ?  46  THR   B OG1 1 
ATOM   2415 C  CG2 . THR   B 1 39  ? 0.217   23.907  19.885 1.00 91.96  ?  46  THR   B CG2 1 
ATOM   2416 N  N   . VAL   B 1 40  ? -0.493  20.596  21.519 1.00 86.33  ?  47  VAL   B N   1 
ATOM   2417 C  CA  . VAL   B 1 40  ? -1.414  19.448  21.440 1.00 89.60  ?  47  VAL   B CA  1 
ATOM   2418 C  C   . VAL   B 1 40  ? -2.721  19.842  20.757 1.00 89.85  ?  47  VAL   B C   1 
ATOM   2419 O  O   . VAL   B 1 40  ? -3.237  19.063  19.965 1.00 93.14  ?  47  VAL   B O   1 
ATOM   2420 C  CB  . VAL   B 1 40  ? -1.641  18.783  22.837 1.00 90.59  ?  47  VAL   B CB  1 
ATOM   2421 C  CG1 . VAL   B 1 40  ? -2.767  17.745  22.829 1.00 91.93  ?  47  VAL   B CG1 1 
ATOM   2422 C  CG2 . VAL   B 1 40  ? -0.343  18.130  23.329 1.00 92.31  ?  47  VAL   B CG2 1 
ATOM   2423 N  N   . TYR   B 1 41  ? -3.254  21.018  21.094 1.00 89.50  ?  48  TYR   B N   1 
ATOM   2424 C  CA  . TYR   B 1 41  ? -4.484  21.579  20.507 1.00 88.71  ?  48  TYR   B CA  1 
ATOM   2425 C  C   . TYR   B 1 41  ? -4.250  23.056  20.158 1.00 90.54  ?  48  TYR   B C   1 
ATOM   2426 O  O   . TYR   B 1 41  ? -3.627  23.788  20.931 1.00 89.49  ?  48  TYR   B O   1 
ATOM   2427 C  CB  . TYR   B 1 41  ? -5.643  21.410  21.506 1.00 89.65  ?  48  TYR   B CB  1 
ATOM   2428 C  CG  . TYR   B 1 41  ? -6.977  22.110  21.183 1.00 92.78  ?  48  TYR   B CG  1 
ATOM   2429 C  CD1 . TYR   B 1 41  ? -7.165  23.477  21.463 1.00 93.27  ?  48  TYR   B CD1 1 
ATOM   2430 C  CD2 . TYR   B 1 41  ? -8.057  21.403  20.629 1.00 93.35  ?  48  TYR   B CD2 1 
ATOM   2431 C  CE1 . TYR   B 1 41  ? -8.373  24.121  21.182 1.00 95.38  ?  48  TYR   B CE1 1 
ATOM   2432 C  CE2 . TYR   B 1 41  ? -9.276  22.044  20.346 1.00 98.25  ?  48  TYR   B CE2 1 
ATOM   2433 C  CZ  . TYR   B 1 41  ? -9.427  23.404  20.625 1.00 96.82  ?  48  TYR   B CZ  1 
ATOM   2434 O  OH  . TYR   B 1 41  ? -10.612 24.070  20.358 1.00 104.32 ?  48  TYR   B OH  1 
ATOM   2435 N  N   . LYS   B 1 42  ? -4.749  23.470  18.989 1.00 92.94  ?  49  LYS   B N   1 
ATOM   2436 C  CA  . LYS   B 1 42  ? -4.898  24.884  18.604 1.00 96.00  ?  49  LYS   B CA  1 
ATOM   2437 C  C   . LYS   B 1 42  ? -6.264  25.044  17.916 1.00 96.04  ?  49  LYS   B C   1 
ATOM   2438 O  O   . LYS   B 1 42  ? -6.573  24.300  16.985 1.00 95.04  ?  49  LYS   B O   1 
ATOM   2439 C  CB  . LYS   B 1 42  ? -3.764  25.340  17.676 1.00 98.58  ?  49  LYS   B CB  1 
ATOM   2440 C  CG  . LYS   B 1 42  ? -3.629  26.854  17.553 1.00 101.81 ?  49  LYS   B CG  1 
ATOM   2441 C  CD  . LYS   B 1 42  ? -2.366  27.255  16.796 1.00 103.87 ?  49  LYS   B CD  1 
ATOM   2442 C  CE  . LYS   B 1 42  ? -1.134  27.249  17.643 0.00 98.33  ?  49  LYS   B CE  1 
ATOM   2443 N  NZ  . LYS   B 1 42  ? 0.115   27.283  16.832 0.00 97.70  ?  49  LYS   B NZ  1 
ATOM   2444 N  N   . GLY   B 1 43  ? -7.066  26.001  18.382 1.00 93.88  ?  50  GLY   B N   1 
ATOM   2445 C  CA  . GLY   B 1 43  ? -8.445  26.171  17.909 1.00 96.02  ?  50  GLY   B CA  1 
ATOM   2446 C  C   . GLY   B 1 43  ? -9.250  27.227  18.662 1.00 96.81  ?  50  GLY   B C   1 
ATOM   2447 O  O   . GLY   B 1 43  ? -8.661  28.089  19.345 1.00 89.95  ?  50  GLY   B O   1 
ATOM   2448 N  N   . PRO   B 1 44  ? -10.604 27.187  18.532 1.00 103.77 ?  51  PRO   B N   1 
ATOM   2449 C  CA  . PRO   B 1 44  ? -11.470 28.066  19.344 1.00 109.22 ?  51  PRO   B CA  1 
ATOM   2450 C  C   . PRO   B 1 44  ? -11.474 27.726  20.837 1.00 110.94 ?  51  PRO   B C   1 
ATOM   2451 O  O   . PRO   B 1 44  ? -11.164 26.592  21.223 1.00 103.69 ?  51  PRO   B O   1 
ATOM   2452 C  CB  . PRO   B 1 44  ? -12.866 27.882  18.734 1.00 114.82 ?  51  PRO   B CB  1 
ATOM   2453 C  CG  . PRO   B 1 44  ? -12.819 26.586  18.015 1.00 112.91 ?  51  PRO   B CG  1 
ATOM   2454 C  CD  . PRO   B 1 44  ? -11.391 26.321  17.634 1.00 107.77 ?  51  PRO   B CD  1 
ATOM   2455 N  N   . ASN   B 1 45  ? -11.814 28.728  21.643 1.00 121.62 ?  52  ASN   B N   1 
ATOM   2456 C  CA  . ASN   B 1 45  ? -11.695 28.646  23.104 1.00 125.74 ?  52  ASN   B CA  1 
ATOM   2457 C  C   . ASN   B 1 45  ? -12.847 27.844  23.729 1.00 127.88 ?  52  ASN   B C   1 
ATOM   2458 O  O   . ASN   B 1 45  ? -14.005 28.273  23.674 1.00 135.02 ?  52  ASN   B O   1 
ATOM   2459 C  CB  . ASN   B 1 45  ? -11.628 30.061  23.714 1.00 132.10 ?  52  ASN   B CB  1 
ATOM   2460 C  CG  . ASN   B 1 45  ? -11.235 30.070  25.195 1.00 138.15 ?  52  ASN   B CG  1 
ATOM   2461 O  OD1 . ASN   B 1 45  ? -10.648 29.116  25.717 1.00 154.81 ?  52  ASN   B OD1 1 
ATOM   2462 N  ND2 . ASN   B 1 45  ? -11.539 31.173  25.873 1.00 140.18 ?  52  ASN   B ND2 1 
ATOM   2463 N  N   . CYS   B 1 46  ? -12.512 26.680  24.299 1.00 131.23 ?  53  CYS   B N   1 
ATOM   2464 C  CA  . CYS   B 1 46  ? -13.410 25.875  25.146 1.00 136.24 ?  53  CYS   B CA  1 
ATOM   2465 C  C   . CYS   B 1 46  ? -12.615 25.421  26.391 1.00 146.66 ?  53  CYS   B C   1 
ATOM   2466 O  O   . CYS   B 1 46  ? -11.715 24.570  26.294 1.00 130.54 ?  53  CYS   B O   1 
ATOM   2467 C  CB  . CYS   B 1 46  ? -13.987 24.658  24.393 1.00 127.80 ?  53  CYS   B CB  1 
ATOM   2468 S  SG  . CYS   B 1 46  ? -14.187 24.823  22.577 1.00 118.35 ?  53  CYS   B SG  1 
ATOM   2469 N  N   . ILE   B 1 47  ? -12.981 25.959  27.560 1.00 166.16 ?  54  ILE   B N   1 
ATOM   2470 C  CA  . ILE   B 1 47  ? -12.208 25.807  28.815 1.00 169.75 ?  54  ILE   B CA  1 
ATOM   2471 C  C   . ILE   B 1 47  ? -12.730 24.654  29.725 1.00 175.69 ?  54  ILE   B C   1 
ATOM   2472 O  O   . ILE   B 1 47  ? -12.725 24.748  30.965 1.00 177.20 ?  54  ILE   B O   1 
ATOM   2473 C  CB  . ILE   B 1 47  ? -12.174 27.167  29.564 1.00 169.69 ?  54  ILE   B CB  1 
ATOM   2474 C  CG1 . ILE   B 1 47  ? -11.013 27.395  30.478 0.00 179.93 ?  54  ILE   B CG1 1 
ATOM   2475 C  CG2 . ILE   B 1 47  ? -13.523 27.611  30.266 0.00 185.28 ?  54  ILE   B CG2 1 
ATOM   2476 C  CD1 . ILE   B 1 47  ? -11.014 28.679  31.278 0.00 181.18 ?  54  ILE   B CD1 1 
ATOM   2477 N  N   . GLU   B 1 48  ? -13.115 23.542  29.093 1.00 176.91 ?  55  GLU   B N   1 
ATOM   2478 C  CA  . GLU   B 1 48  ? -13.894 22.481  29.749 1.00 172.86 ?  55  GLU   B CA  1 
ATOM   2479 C  C   . GLU   B 1 48  ? -13.043 21.586  30.656 1.00 165.57 ?  55  GLU   B C   1 
ATOM   2480 O  O   . GLU   B 1 48  ? -13.404 21.377  31.816 1.00 176.90 ?  55  GLU   B O   1 
ATOM   2481 C  CB  . GLU   B 1 48  ? -14.636 21.620  28.711 1.00 171.51 ?  55  GLU   B CB  1 
ATOM   2482 C  CG  . GLU   B 1 48  ? -15.679 22.374  27.900 1.00 168.17 ?  55  GLU   B CG  1 
ATOM   2483 C  CD  . GLU   B 1 48  ? -16.440 21.469  26.932 0.00 183.64 ?  55  GLU   B CD  1 
ATOM   2484 O  OE1 . GLU   B 1 48  ? -15.803 20.679  26.203 0.00 181.64 ?  55  GLU   B OE1 1 
ATOM   2485 O  OE2 . GLU   B 1 48  ? -17.686 21.561  26.896 0.00 187.19 ?  55  GLU   B OE2 1 
ATOM   2486 N  N   . HIS   B 1 49  ? -11.931 21.072  30.122 1.00 140.43 ?  56  HIS   B N   1 
ATOM   2487 C  CA  . HIS   B 1 49  ? -11.078 20.083  30.809 1.00 138.73 ?  56  HIS   B CA  1 
ATOM   2488 C  C   . HIS   B 1 49  ? -9.816  20.651  31.519 1.00 136.18 ?  56  HIS   B C   1 
ATOM   2489 O  O   . HIS   B 1 49  ? -8.923  19.870  31.857 1.00 134.69 ?  56  HIS   B O   1 
ATOM   2490 C  CB  . HIS   B 1 49  ? -10.681 18.993  29.792 1.00 138.97 ?  56  HIS   B CB  1 
ATOM   2491 C  CG  . HIS   B 1 49  ? -11.825 18.152  29.331 1.00 140.77 ?  56  HIS   B CG  1 
ATOM   2492 N  ND1 . HIS   B 1 49  ? -12.595 18.474  28.235 1.00 147.88 ?  56  HIS   B ND1 1 
ATOM   2493 C  CD2 . HIS   B 1 49  ? -12.319 16.988  29.812 1.00 138.12 ?  56  HIS   B CD2 1 
ATOM   2494 C  CE1 . HIS   B 1 49  ? -13.523 17.548  28.067 1.00 152.66 ?  56  HIS   B CE1 1 
ATOM   2495 N  NE2 . HIS   B 1 49  ? -13.374 16.633  29.009 1.00 146.06 ?  56  HIS   B NE2 1 
ATOM   2496 N  N   . ASN   B 1 50  ? -9.752  21.970  31.749 1.00 136.03 ?  57  ASN   B N   1 
ATOM   2497 C  CA  . ASN   B 1 50  ? -8.519  22.637  32.237 1.00 134.31 ?  57  ASN   B CA  1 
ATOM   2498 C  C   . ASN   B 1 50  ? -8.028  22.154  33.613 1.00 131.72 ?  57  ASN   B C   1 
ATOM   2499 O  O   . ASN   B 1 50  ? -6.815  22.102  33.846 1.00 130.86 ?  57  ASN   B O   1 
ATOM   2500 C  CB  . ASN   B 1 50  ? -8.678  24.169  32.273 1.00 138.65 ?  57  ASN   B CB  1 
ATOM   2501 C  CG  . ASN   B 1 50  ? -8.676  24.793  30.889 1.00 142.43 ?  57  ASN   B CG  1 
ATOM   2502 O  OD1 . ASN   B 1 50  ? -9.157  24.202  29.925 1.00 153.92 ?  57  ASN   B OD1 1 
ATOM   2503 N  ND2 . ASN   B 1 50  ? -8.134  26.009  30.782 1.00 139.18 ?  57  ASN   B ND2 1 
ATOM   2504 N  N   . GLU   B 1 51  ? -8.967  21.800  34.497 1.00 137.64 ?  58  GLU   B N   1 
ATOM   2505 C  CA  . GLU   B 1 51  ? -8.650  21.219  35.817 1.00 137.16 ?  58  GLU   B CA  1 
ATOM   2506 C  C   . GLU   B 1 51  ? -7.990  19.836  35.711 1.00 129.20 ?  58  GLU   B C   1 
ATOM   2507 O  O   . GLU   B 1 51  ? -7.008  19.570  36.405 1.00 127.51 ?  58  GLU   B O   1 
ATOM   2508 C  CB  . GLU   B 1 51  ? -9.909  21.122  36.704 1.00 141.54 ?  58  GLU   B CB  1 
ATOM   2509 C  CG  . GLU   B 1 51  ? -10.523 22.460  37.084 1.00 141.04 ?  58  GLU   B CG  1 
ATOM   2510 C  CD  . GLU   B 1 51  ? -11.594 22.374  38.148 0.00 145.70 ?  58  GLU   B CD  1 
ATOM   2511 O  OE1 . GLU   B 1 51  ? -12.528 21.558  37.986 0.00 147.30 ?  58  GLU   B OE1 1 
ATOM   2512 O  OE2 . GLU   B 1 51  ? -11.524 23.124  39.146 0.00 147.34 ?  58  GLU   B OE2 1 
ATOM   2513 N  N   . ALA   B 1 52  ? -8.529  18.990  34.831 1.00 121.28 ?  59  ALA   B N   1 
ATOM   2514 C  CA  . ALA   B 1 52  ? -8.004  17.644  34.599 1.00 112.67 ?  59  ALA   B CA  1 
ATOM   2515 C  C   . ALA   B 1 52  ? -6.701  17.649  33.803 1.00 114.92 ?  59  ALA   B C   1 
ATOM   2516 O  O   . ALA   B 1 52  ? -5.845  16.824  34.073 1.00 121.94 ?  59  ALA   B O   1 
ATOM   2517 C  CB  . ALA   B 1 52  ? -9.038  16.769  33.907 1.00 110.42 ?  59  ALA   B CB  1 
ATOM   2518 N  N   . LEU   B 1 53  ? -6.566  18.556  32.831 1.00 111.55 ?  60  LEU   B N   1 
ATOM   2519 C  CA  . LEU   B 1 53  ? -5.306  18.735  32.077 1.00 101.68 ?  60  LEU   B CA  1 
ATOM   2520 C  C   . LEU   B 1 53  ? -4.149  19.198  32.963 1.00 97.69  ?  60  LEU   B C   1 
ATOM   2521 O  O   . LEU   B 1 53  ? -3.035  18.667  32.834 1.00 95.63  ?  60  LEU   B O   1 
ATOM   2522 C  CB  . LEU   B 1 53  ? -5.481  19.715  30.907 1.00 101.03 ?  60  LEU   B CB  1 
ATOM   2523 C  CG  . LEU   B 1 53  ? -6.367  19.257  29.745 1.00 101.24 ?  60  LEU   B CG  1 
ATOM   2524 C  CD1 . LEU   B 1 53  ? -6.753  20.446  28.878 1.00 99.75  ?  60  LEU   B CD1 1 
ATOM   2525 C  CD2 . LEU   B 1 53  ? -5.700  18.182  28.898 1.00 96.59  ?  60  LEU   B CD2 1 
ATOM   2526 N  N   . LEU   B 1 54  ? -4.409  20.167  33.845 1.00 97.21  ?  61  LEU   B N   1 
ATOM   2527 C  CA  . LEU   B 1 54  ? -3.390  20.640  34.802 1.00 99.13  ?  61  LEU   B CA  1 
ATOM   2528 C  C   . LEU   B 1 54  ? -3.023  19.581  35.862 1.00 101.47 ?  61  LEU   B C   1 
ATOM   2529 O  O   . LEU   B 1 54  ? -1.849  19.450  36.228 1.00 95.17  ?  61  LEU   B O   1 
ATOM   2530 C  CB  . LEU   B 1 54  ? -3.834  21.945  35.469 1.00 100.43 ?  61  LEU   B CB  1 
ATOM   2531 C  CG  . LEU   B 1 54  ? -2.875  22.665  36.425 1.00 102.45 ?  61  LEU   B CG  1 
ATOM   2532 C  CD1 . LEU   B 1 54  ? -1.567  23.063  35.763 1.00 99.28  ?  61  LEU   B CD1 1 
ATOM   2533 C  CD2 . LEU   B 1 54  ? -3.574  23.896  36.989 1.00 107.31 ?  61  LEU   B CD2 1 
ATOM   2534 N  N   . GLU   B 1 55  ? -4.019  18.839  36.353 1.00 106.36 ?  62  GLU   B N   1 
ATOM   2535 C  CA  . GLU   B 1 55  ? -3.778  17.727  37.300 1.00 109.57 ?  62  GLU   B CA  1 
ATOM   2536 C  C   . GLU   B 1 55  ? -3.022  16.563  36.640 1.00 102.05 ?  62  GLU   B C   1 
ATOM   2537 O  O   . GLU   B 1 55  ? -2.191  15.927  37.273 1.00 99.67  ?  62  GLU   B O   1 
ATOM   2538 C  CB  . GLU   B 1 55  ? -5.093  17.243  37.928 1.00 113.40 ?  62  GLU   B CB  1 
ATOM   2539 C  CG  . GLU   B 1 55  ? -4.930  16.404  39.205 1.00 115.69 ?  62  GLU   B CG  1 
ATOM   2540 C  CD  . GLU   B 1 55  ? -5.070  14.884  39.052 1.00 124.27 ?  62  GLU   B CD  1 
ATOM   2541 O  OE1 . GLU   B 1 55  ? -5.680  14.359  38.087 1.00 135.87 ?  62  GLU   B OE1 1 
ATOM   2542 O  OE2 . GLU   B 1 55  ? -4.573  14.181  39.958 1.00 127.26 ?  62  GLU   B OE2 1 
ATOM   2543 N  N   . GLU   B 1 56  ? -3.316  16.304  35.367 1.00 95.63  ?  63  GLU   B N   1 
ATOM   2544 C  CA  . GLU   B 1 56  ? -2.565  15.346  34.545 1.00 92.64  ?  63  GLU   B CA  1 
ATOM   2545 C  C   . GLU   B 1 56  ? -1.147  15.849  34.228 1.00 90.12  ?  63  GLU   B C   1 
ATOM   2546 O  O   . GLU   B 1 56  ? -0.213  15.049  34.185 1.00 82.54  ?  63  GLU   B O   1 
ATOM   2547 C  CB  . GLU   B 1 56  ? -3.342  15.034  33.262 1.00 92.92  ?  63  GLU   B CB  1 
ATOM   2548 C  CG  . GLU   B 1 56  ? -2.935  13.780  32.512 1.00 95.49  ?  63  GLU   B CG  1 
ATOM   2549 C  CD  . GLU   B 1 56  ? -4.073  13.259  31.649 1.00 103.46 ?  63  GLU   B CD  1 
ATOM   2550 O  OE1 . GLU   B 1 56  ? -4.079  13.514  30.432 1.00 105.21 ?  63  GLU   B OE1 1 
ATOM   2551 O  OE2 . GLU   B 1 56  ? -5.002  12.627  32.193 1.00 103.40 ?  63  GLU   B OE2 1 
ATOM   2552 N  N   . ALA   B 1 57  ? -0.997  17.162  34.015 1.00 87.09  ?  64  ALA   B N   1 
ATOM   2553 C  CA  . ALA   B 1 57  ? 0.326   17.798  33.903 1.00 82.50  ?  64  ALA   B CA  1 
ATOM   2554 C  C   . ALA   B 1 57  ? 1.160   17.681  35.198 1.00 84.08  ?  64  ALA   B C   1 
ATOM   2555 O  O   . ALA   B 1 57  ? 2.383   17.519  35.136 1.00 81.37  ?  64  ALA   B O   1 
ATOM   2556 C  CB  . ALA   B 1 57  ? 0.208   19.253  33.469 1.00 83.85  ?  64  ALA   B CB  1 
ATOM   2557 N  N   . LYS   B 1 58  ? 0.503   17.800  36.357 1.00 93.16  ?  65  LYS   B N   1 
ATOM   2558 C  CA  . LYS   B 1 58  ? 1.149   17.581  37.672 1.00 91.86  ?  65  LYS   B CA  1 
ATOM   2559 C  C   . LYS   B 1 58  ? 1.666   16.153  37.812 1.00 93.01  ?  65  LYS   B C   1 
ATOM   2560 O  O   . LYS   B 1 58  ? 2.790   15.958  38.260 1.00 98.45  ?  65  LYS   B O   1 
ATOM   2561 C  CB  . LYS   B 1 58  ? 0.210   17.940  38.850 1.00 93.73  ?  65  LYS   B CB  1 
ATOM   2562 C  CG  . LYS   B 1 58  ? 0.054   19.431  39.103 1.00 93.54  ?  65  LYS   B CG  1 
ATOM   2563 C  CD  . LYS   B 1 58  ? -1.038  19.689  40.120 0.00 96.23  ?  65  LYS   B CD  1 
ATOM   2564 C  CE  . LYS   B 1 58  ? -1.253  21.178  40.338 0.00 97.72  ?  65  LYS   B CE  1 
ATOM   2565 N  NZ  . LYS   B 1 58  ? -2.345  21.444  41.316 0.00 101.28 ?  65  LYS   B NZ  1 
ATOM   2566 N  N   . MET   B 1 59  ? 0.846   15.180  37.417 1.00 94.72  ?  66  MET   B N   1 
ATOM   2567 C  CA  . MET   B 1 59  ? 1.196   13.751  37.478 1.00 98.32  ?  66  MET   B CA  1 
ATOM   2568 C  C   . MET   B 1 59  ? 2.407   13.389  36.614 1.00 92.50  ?  66  MET   B C   1 
ATOM   2569 O  O   . MET   B 1 59  ? 3.272   12.624  37.039 1.00 89.92  ?  66  MET   B O   1 
ATOM   2570 C  CB  . MET   B 1 59  ? -0.010  12.874  37.088 1.00 109.48 ?  66  MET   B CB  1 
ATOM   2571 C  CG  . MET   B 1 59  ? -1.088  12.789  38.161 1.00 113.11 ?  66  MET   B CG  1 
ATOM   2572 S  SD  . MET   B 1 59  ? -2.363  11.537  37.849 1.00 123.97 ?  66  MET   B SD  1 
ATOM   2573 C  CE  . MET   B 1 59  ? -3.176  12.142  36.374 1.00 120.31 ?  66  MET   B CE  1 
ATOM   2574 N  N   . MET   B 1 60  ? 2.440   13.913  35.393 1.00 91.46  ?  67  MET   B N   1 
ATOM   2575 C  CA  . MET   B 1 60  ? 3.588   13.749  34.495 1.00 86.40  ?  67  MET   B CA  1 
ATOM   2576 C  C   . MET   B 1 60  ? 4.851   14.516  34.978 1.00 81.62  ?  67  MET   B C   1 
ATOM   2577 O  O   . MET   B 1 60  ? 5.957   14.121  34.661 1.00 85.71  ?  67  MET   B O   1 
ATOM   2578 C  CB  . MET   B 1 60  ? 3.190   14.053  33.027 1.00 81.64  ?  67  MET   B CB  1 
ATOM   2579 C  CG  . MET   B 1 60  ? 2.903   15.491  32.683 1.00 82.96  ?  67  MET   B CG  1 
ATOM   2580 S  SD  . MET   B 1 60  ? 2.505   15.943  30.980 1.00 84.00  ?  67  MET   B SD  1 
ATOM   2581 C  CE  . MET   B 1 60  ? 1.192   14.846  30.454 1.00 81.80  ?  67  MET   B CE  1 
ATOM   2582 N  N   . ASN   B 1 61  ? 4.679   15.599  35.736 1.00 83.47  ?  68  ASN   B N   1 
ATOM   2583 C  CA  . ASN   B 1 61  ? 5.808   16.305  36.394 1.00 82.14  ?  68  ASN   B CA  1 
ATOM   2584 C  C   . ASN   B 1 61  ? 6.421   15.534  37.581 1.00 81.87  ?  68  ASN   B C   1 
ATOM   2585 O  O   . ASN   B 1 61  ? 7.589   15.714  37.888 1.00 79.77  ?  68  ASN   B O   1 
ATOM   2586 C  CB  . ASN   B 1 61  ? 5.371   17.702  36.865 1.00 83.89  ?  68  ASN   B CB  1 
ATOM   2587 C  CG  . ASN   B 1 61  ? 6.542   18.616  37.148 1.00 81.43  ?  68  ASN   B CG  1 
ATOM   2588 O  OD1 . ASN   B 1 61  ? 6.854   18.881  38.293 1.00 84.52  ?  68  ASN   B OD1 1 
ATOM   2589 N  ND2 . ASN   B 1 61  ? 7.215   19.067  36.101 1.00 81.36  ?  68  ASN   B ND2 1 
ATOM   2590 N  N   . ARG   B 1 62  ? 5.617   14.722  38.264 1.00 85.25  ?  69  ARG   B N   1 
ATOM   2591 C  CA  . ARG   B 1 62  ? 6.070   13.866  39.377 1.00 86.91  ?  69  ARG   B CA  1 
ATOM   2592 C  C   . ARG   B 1 62  ? 7.062   12.757  38.954 1.00 81.81  ?  69  ARG   B C   1 
ATOM   2593 O  O   . ARG   B 1 62  ? 7.774   12.234  39.811 1.00 83.49  ?  69  ARG   B O   1 
ATOM   2594 C  CB  . ARG   B 1 62  ? 4.860   13.245  40.144 1.00 88.45  ?  69  ARG   B CB  1 
ATOM   2595 C  CG  . ARG   B 1 62  ? 4.092   14.199  41.070 1.00 94.40  ?  69  ARG   B CG  1 
ATOM   2596 C  CD  . ARG   B 1 62  ? 2.907   13.525  41.769 1.00 97.71  ?  69  ARG   B CD  1 
ATOM   2597 N  NE  . ARG   B 1 62  ? 2.155   14.424  42.601 0.00 99.13  ?  69  ARG   B NE  1 
ATOM   2598 C  CZ  . ARG   B 1 62  ? 1.045   14.114  43.279 0.00 101.83 ?  69  ARG   B CZ  1 
ATOM   2599 N  NH1 . ARG   B 1 62  ? 0.495   12.898  43.246 0.00 102.08 ?  69  ARG   B NH1 1 
ATOM   2600 N  NH2 . ARG   B 1 62  ? 0.464   15.052  44.015 0.00 104.52 ?  69  ARG   B NH2 1 
ATOM   2601 N  N   . LEU   B 1 63  ? 7.076   12.392  37.661 1.00 84.29  ?  70  LEU   B N   1 
ATOM   2602 C  CA  . LEU   B 1 63  ? 7.963   11.357  37.100 1.00 83.20  ?  70  LEU   B CA  1 
ATOM   2603 C  C   . LEU   B 1 63  ? 9.334   11.942  36.711 1.00 78.25  ?  70  LEU   B C   1 
ATOM   2604 O  O   . LEU   B 1 63  ? 9.556   12.370  35.571 1.00 74.50  ?  70  LEU   B O   1 
ATOM   2605 C  CB  . LEU   B 1 63  ? 7.282   10.675  35.899 1.00 83.50  ?  70  LEU   B CB  1 
ATOM   2606 C  CG  . LEU   B 1 63  ? 5.947   9.992   36.216 1.00 85.85  ?  70  LEU   B CG  1 
ATOM   2607 C  CD1 . LEU   B 1 63  ? 5.141   9.747   34.948 1.00 89.01  ?  70  LEU   B CD1 1 
ATOM   2608 C  CD2 . LEU   B 1 63  ? 6.175   8.689   36.967 1.00 85.01  ?  70  LEU   B CD2 1 
ATOM   2609 N  N   . ARG   B 1 64  ? 10.233  11.958  37.698 1.00 79.19  ?  71  ARG   B N   1 
ATOM   2610 C  CA  . ARG   B 1 64  ? 11.563  12.555  37.613 1.00 78.25  ?  71  ARG   B CA  1 
ATOM   2611 C  C   . ARG   B 1 64  ? 12.618  11.454  37.677 1.00 72.90  ?  71  ARG   B C   1 
ATOM   2612 O  O   . ARG   B 1 64  ? 12.712  10.725  38.672 1.00 77.72  ?  71  ARG   B O   1 
ATOM   2613 C  CB  . ARG   B 1 64  ? 11.772  13.529  38.773 1.00 82.92  ?  71  ARG   B CB  1 
ATOM   2614 C  CG  . ARG   B 1 64  ? 10.871  14.757  38.727 1.00 88.27  ?  71  ARG   B CG  1 
ATOM   2615 C  CD  . ARG   B 1 64  ? 11.463  15.901  37.908 1.00 91.31  ?  71  ARG   B CD  1 
ATOM   2616 N  NE  . ARG   B 1 64  ? 10.821  17.185  38.190 1.00 93.44  ?  71  ARG   B NE  1 
ATOM   2617 C  CZ  . ARG   B 1 64  ? 11.120  18.349  37.523 0.00 95.62  ?  71  ARG   B CZ  1 
ATOM   2618 N  NH1 . ARG   B 1 64  ? 12.065  18.420  36.584 0.00 94.31  ?  71  ARG   B NH1 1 
ATOM   2619 N  NH2 . ARG   B 1 64  ? 10.467  19.464  37.837 0.00 97.10  ?  71  ARG   B NH2 1 
ATOM   2620 N  N   . HIS   B 1 65  ? 13.398  11.320  36.608 1.00 68.97  ?  72  HIS   B N   1 
ATOM   2621 C  CA  . HIS   B 1 65  ? 14.481  10.331  36.534 1.00 65.90  ?  72  HIS   B CA  1 
ATOM   2622 C  C   . HIS   B 1 65  ? 15.445  10.695  35.415 1.00 64.17  ?  72  HIS   B C   1 
ATOM   2623 O  O   . HIS   B 1 65  ? 15.016  11.197  34.371 1.00 65.40  ?  72  HIS   B O   1 
ATOM   2624 C  CB  . HIS   B 1 65  ? 13.903  8.934   36.287 1.00 64.35  ?  72  HIS   B CB  1 
ATOM   2625 C  CG  . HIS   B 1 65  ? 14.850  7.819   36.590 1.00 64.42  ?  72  HIS   B CG  1 
ATOM   2626 N  ND1 . HIS   B 1 65  ? 15.312  6.957   35.622 1.00 66.40  ?  72  HIS   B ND1 1 
ATOM   2627 C  CD2 . HIS   B 1 65  ? 15.411  7.412   37.753 1.00 66.84  ?  72  HIS   B CD2 1 
ATOM   2628 C  CE1 . HIS   B 1 65  ? 16.132  6.077   36.170 1.00 66.08  ?  72  HIS   B CE1 1 
ATOM   2629 N  NE2 . HIS   B 1 65  ? 16.201  6.326   37.464 1.00 66.63  ?  72  HIS   B NE2 1 
ATOM   2630 N  N   . SER   B 1 66  ? 16.728  10.382  35.597 1.00 64.66  ?  73  SER   B N   1 
ATOM   2631 C  CA  . SER   B 1 66  ? 17.778  10.721  34.605 1.00 61.43  ?  73  SER   B CA  1 
ATOM   2632 C  C   . SER   B 1 66  ? 17.577  10.159  33.199 1.00 59.24  ?  73  SER   B C   1 
ATOM   2633 O  O   . SER   B 1 66  ? 18.103  10.732  32.220 1.00 57.37  ?  73  SER   B O   1 
ATOM   2634 C  CB  . SER   B 1 66  ? 19.151  10.298  35.117 1.00 65.49  ?  73  SER   B CB  1 
ATOM   2635 O  OG  . SER   B 1 66  ? 19.306  8.887   35.131 1.00 67.00  ?  73  SER   B OG  1 
ATOM   2636 N  N   . ARG   B 1 67  ? 16.841  9.039   33.110 1.00 57.68  ?  74  ARG   B N   1 
ATOM   2637 C  CA  . ARG   B 1 67  ? 16.485  8.390   31.839 1.00 57.35  ?  74  ARG   B CA  1 
ATOM   2638 C  C   . ARG   B 1 67  ? 15.049  8.615   31.382 1.00 57.19  ?  74  ARG   B C   1 
ATOM   2639 O  O   . ARG   B 1 67  ? 14.588  7.899   30.484 1.00 56.53  ?  74  ARG   B O   1 
ATOM   2640 C  CB  . ARG   B 1 67  ? 16.778  6.872   31.898 1.00 58.79  ?  74  ARG   B CB  1 
ATOM   2641 C  CG  . ARG   B 1 67  ? 18.045  6.461   32.621 1.00 58.53  ?  74  ARG   B CG  1 
ATOM   2642 C  CD  . ARG   B 1 67  ? 19.277  7.141   32.069 1.00 63.08  ?  74  ARG   B CD  1 
ATOM   2643 N  NE  . ARG   B 1 67  ? 20.459  6.740   32.834 1.00 69.76  ?  74  ARG   B NE  1 
ATOM   2644 C  CZ  . ARG   B 1 67  ? 21.648  7.357   32.833 1.00 69.21  ?  74  ARG   B CZ  1 
ATOM   2645 N  NH1 . ARG   B 1 67  ? 21.883  8.440   32.082 1.00 67.94  ?  74  ARG   B NH1 1 
ATOM   2646 N  NH2 . ARG   B 1 67  ? 22.626  6.875   33.612 1.00 68.53  ?  74  ARG   B NH2 1 
ATOM   2647 N  N   . VAL   B 1 68  ? 14.364  9.615   31.944 1.00 59.35  ?  75  VAL   B N   1 
ATOM   2648 C  CA  . VAL   B 1 68  ? 13.006  9.974   31.548 1.00 61.55  ?  75  VAL   B CA  1 
ATOM   2649 C  C   . VAL   B 1 68  ? 13.010  11.475  31.222 1.00 61.40  ?  75  VAL   B C   1 
ATOM   2650 O  O   . VAL   B 1 68  ? 13.549  12.289  31.986 1.00 62.20  ?  75  VAL   B O   1 
ATOM   2651 C  CB  . VAL   B 1 68  ? 11.988  9.624   32.659 1.00 65.06  ?  75  VAL   B CB  1 
ATOM   2652 C  CG1 . VAL   B 1 68  ? 10.567  10.035  32.280 1.00 66.82  ?  75  VAL   B CG1 1 
ATOM   2653 C  CG2 . VAL   B 1 68  ? 12.036  8.124   32.941 1.00 65.70  ?  75  VAL   B CG2 1 
ATOM   2654 N  N   . VAL   B 1 69  ? 12.358  11.814  30.114 1.00 59.50  ?  76  VAL   B N   1 
ATOM   2655 C  CA  . VAL   B 1 69  ? 12.255  13.193  29.634 1.00 61.95  ?  76  VAL   B CA  1 
ATOM   2656 C  C   . VAL   B 1 69  ? 11.401  13.987  30.617 1.00 65.90  ?  76  VAL   B C   1 
ATOM   2657 O  O   . VAL   B 1 69  ? 10.264  13.599  30.910 1.00 73.61  ?  76  VAL   B O   1 
ATOM   2658 C  CB  . VAL   B 1 69  ? 11.660  13.264  28.205 1.00 64.20  ?  76  VAL   B CB  1 
ATOM   2659 C  CG1 . VAL   B 1 69  ? 11.408  14.700  27.758 1.00 67.61  ?  76  VAL   B CG1 1 
ATOM   2660 C  CG2 . VAL   B 1 69  ? 12.598  12.601  27.196 1.00 63.04  ?  76  VAL   B CG2 1 
ATOM   2661 N  N   . LYS   B 1 70  ? 11.984  15.060  31.155 1.00 68.54  ?  77  LYS   B N   1 
ATOM   2662 C  CA  . LYS   B 1 70  ? 11.296  15.994  32.052 1.00 71.31  ?  77  LYS   B CA  1 
ATOM   2663 C  C   . LYS   B 1 70  ? 10.341  16.895  31.282 1.00 65.78  ?  77  LYS   B C   1 
ATOM   2664 O  O   . LYS   B 1 70  ? 10.699  17.430  30.237 1.00 65.26  ?  77  LYS   B O   1 
ATOM   2665 C  CB  . LYS   B 1 70  ? 12.301  16.873  32.825 1.00 79.03  ?  77  LYS   B CB  1 
ATOM   2666 C  CG  . LYS   B 1 70  ? 13.118  16.090  33.838 1.00 93.43  ?  77  LYS   B CG  1 
ATOM   2667 C  CD  . LYS   B 1 70  ? 14.394  16.779  34.303 1.00 98.44  ?  77  LYS   B CD  1 
ATOM   2668 C  CE  . LYS   B 1 70  ? 15.197  15.845  35.211 1.00 95.81  ?  77  LYS   B CE  1 
ATOM   2669 N  NZ  . LYS   B 1 70  ? 16.603  16.292  35.391 1.00 98.97  ?  77  LYS   B NZ  1 
ATOM   2670 N  N   . LEU   B 1 71  ? 9.120   17.016  31.788 1.00 63.77  ?  78  LEU   B N   1 
ATOM   2671 C  CA  . LEU   B 1 71  ? 8.208   18.088  31.399 1.00 65.76  ?  78  LEU   B CA  1 
ATOM   2672 C  C   . LEU   B 1 71  ? 8.707   19.344  32.120 1.00 68.12  ?  78  LEU   B C   1 
ATOM   2673 O  O   . LEU   B 1 71  ? 8.758   19.368  33.358 1.00 69.44  ?  78  LEU   B O   1 
ATOM   2674 C  CB  . LEU   B 1 71  ? 6.770   17.773  31.830 1.00 63.05  ?  78  LEU   B CB  1 
ATOM   2675 C  CG  . LEU   B 1 71  ? 5.717   18.814  31.396 1.00 65.84  ?  78  LEU   B CG  1 
ATOM   2676 C  CD1 . LEU   B 1 71  ? 5.192   18.525  29.996 1.00 64.24  ?  78  LEU   B CD1 1 
ATOM   2677 C  CD2 . LEU   B 1 71  ? 4.570   18.910  32.386 1.00 66.16  ?  78  LEU   B CD2 1 
ATOM   2678 N  N   . LEU   B 1 72  ? 9.052   20.379  31.358 1.00 71.26  ?  79  LEU   B N   1 
ATOM   2679 C  CA  . LEU   B 1 72  ? 9.567   21.643  31.930 1.00 72.59  ?  79  LEU   B CA  1 
ATOM   2680 C  C   . LEU   B 1 72  ? 8.444   22.631  32.232 1.00 71.16  ?  79  LEU   B C   1 
ATOM   2681 O  O   . LEU   B 1 72  ? 8.522   23.358  33.221 1.00 73.02  ?  79  LEU   B O   1 
ATOM   2682 C  CB  . LEU   B 1 72  ? 10.629  22.276  31.014 1.00 70.28  ?  79  LEU   B CB  1 
ATOM   2683 C  CG  . LEU   B 1 72  ? 11.886  21.432  30.796 1.00 67.44  ?  79  LEU   B CG  1 
ATOM   2684 C  CD1 . LEU   B 1 72  ? 12.702  21.996  29.638 1.00 67.55  ?  79  LEU   B CD1 1 
ATOM   2685 C  CD2 . LEU   B 1 72  ? 12.730  21.345  32.057 1.00 69.10  ?  79  LEU   B CD2 1 
ATOM   2686 N  N   . GLY   B 1 73  ? 7.429   22.672  31.371 1.00 70.36  ?  80  GLY   B N   1 
ATOM   2687 C  CA  . GLY   B 1 73  ? 6.267   23.511  31.571 1.00 71.57  ?  80  GLY   B CA  1 
ATOM   2688 C  C   . GLY   B 1 73  ? 5.066   23.178  30.704 1.00 72.40  ?  80  GLY   B C   1 
ATOM   2689 O  O   . GLY   B 1 73  ? 5.120   22.296  29.852 1.00 73.32  ?  80  GLY   B O   1 
ATOM   2690 N  N   . VAL   B 1 74  ? 3.980   23.895  30.956 1.00 76.07  ?  81  VAL   B N   1 
ATOM   2691 C  CA  . VAL   B 1 74  ? 2.748   23.832  30.157 1.00 80.52  ?  81  VAL   B CA  1 
ATOM   2692 C  C   . VAL   B 1 74  ? 2.321   25.245  29.761 1.00 79.95  ?  81  VAL   B C   1 
ATOM   2693 O  O   . VAL   B 1 74  ? 2.511   26.181  30.552 1.00 78.70  ?  81  VAL   B O   1 
ATOM   2694 C  CB  . VAL   B 1 74  ? 1.587   23.127  30.911 1.00 86.93  ?  81  VAL   B CB  1 
ATOM   2695 C  CG1 . VAL   B 1 74  ? 1.928   21.663  31.167 1.00 85.31  ?  81  VAL   B CG1 1 
ATOM   2696 C  CG2 . VAL   B 1 74  ? 1.233   23.808  32.237 1.00 90.67  ?  81  VAL   B CG2 1 
ATOM   2697 N  N   . ILE   B 1 75  ? 1.766   25.384  28.553 1.00 79.09  ?  82  ILE   B N   1 
ATOM   2698 C  CA  . ILE   B 1 75  ? 1.115   26.624  28.112 1.00 80.75  ?  82  ILE   B CA  1 
ATOM   2699 C  C   . ILE   B 1 75  ? -0.368  26.282  28.109 1.00 82.96  ?  82  ILE   B C   1 
ATOM   2700 O  O   . ILE   B 1 75  ? -0.800  25.467  27.304 1.00 78.83  ?  82  ILE   B O   1 
ATOM   2701 C  CB  . ILE   B 1 75  ? 1.601   27.099  26.725 1.00 78.25  ?  82  ILE   B CB  1 
ATOM   2702 C  CG1 . ILE   B 1 75  ? 3.114   27.317  26.741 1.00 74.78  ?  82  ILE   B CG1 1 
ATOM   2703 C  CG2 . ILE   B 1 75  ? 0.890   28.400  26.311 1.00 83.00  ?  82  ILE   B CG2 1 
ATOM   2704 C  CD1 . ILE   B 1 75  ? 3.705   27.505  25.361 1.00 75.20  ?  82  ILE   B CD1 1 
ATOM   2705 N  N   . ILE   B 1 76  ? -1.118  26.885  29.039 1.00 87.06  ?  83  ILE   B N   1 
ATOM   2706 C  CA  . ILE   B 1 76  ? -2.567  26.716  29.178 1.00 89.08  ?  83  ILE   B CA  1 
ATOM   2707 C  C   . ILE   B 1 76  ? -3.161  28.115  28.938 1.00 92.97  ?  83  ILE   B C   1 
ATOM   2708 O  O   . ILE   B 1 76  ? -3.263  28.918  29.872 1.00 94.41  ?  83  ILE   B O   1 
ATOM   2709 C  CB  . ILE   B 1 76  ? -2.952  26.160  30.586 1.00 92.13  ?  83  ILE   B CB  1 
ATOM   2710 C  CG1 . ILE   B 1 76  ? -2.309  24.791  30.863 1.00 91.28  ?  83  ILE   B CG1 1 
ATOM   2711 C  CG2 . ILE   B 1 76  ? -4.474  26.068  30.764 1.00 97.89  ?  83  ILE   B CG2 1 
ATOM   2712 C  CD1 . ILE   B 1 76  ? -2.717  23.658  29.936 1.00 93.26  ?  83  ILE   B CD1 1 
ATOM   2713 N  N   . GLU   B 1 77  ? -3.519  28.383  27.680 1.00 93.36  ?  84  GLU   B N   1 
ATOM   2714 C  CA  . GLU   B 1 77  ? -4.115  29.662  27.246 1.00 94.81  ?  84  GLU   B CA  1 
ATOM   2715 C  C   . GLU   B 1 77  ? -5.419  29.432  26.481 1.00 97.02  ?  84  GLU   B C   1 
ATOM   2716 O  O   . GLU   B 1 77  ? -5.777  28.283  26.175 1.00 94.18  ?  84  GLU   B O   1 
ATOM   2717 C  CB  . GLU   B 1 77  ? -3.116  30.436  26.381 1.00 93.36  ?  84  GLU   B CB  1 
ATOM   2718 C  CG  . GLU   B 1 77  ? -1.889  30.918  27.149 1.00 91.83  ?  84  GLU   B CG  1 
ATOM   2719 C  CD  . GLU   B 1 77  ? -0.805  31.559  26.282 1.00 89.93  ?  84  GLU   B CD  1 
ATOM   2720 O  OE1 . GLU   B 1 77  ? -0.796  31.410  25.035 1.00 85.54  ?  84  GLU   B OE1 1 
ATOM   2721 O  OE2 . GLU   B 1 77  ? 0.071   32.223  26.872 1.00 91.12  ?  84  GLU   B OE2 1 
ATOM   2722 N  N   . GLU   B 1 78  ? -6.130  30.536  26.212 1.00 101.67 ?  85  GLU   B N   1 
ATOM   2723 C  CA  . GLU   B 1 78  ? -7.410  30.521  25.467 1.00 101.68 ?  85  GLU   B CA  1 
ATOM   2724 C  C   . GLU   B 1 78  ? -7.243  29.988  24.033 1.00 97.88  ?  85  GLU   B C   1 
ATOM   2725 O  O   . GLU   B 1 78  ? -6.719  30.687  23.166 1.00 96.62  ?  85  GLU   B O   1 
ATOM   2726 C  CB  . GLU   B 1 78  ? -8.102  31.908  25.472 1.00 111.89 ?  85  GLU   B CB  1 
ATOM   2727 C  CG  . GLU   B 1 78  ? -7.355  33.079  24.829 1.00 114.07 ?  85  GLU   B CG  1 
ATOM   2728 C  CD  . GLU   B 1 78  ? -7.817  34.447  25.340 0.00 115.06 ?  85  GLU   B CD  1 
ATOM   2729 O  OE1 . GLU   B 1 78  ? -9.034  34.635  25.555 0.00 117.66 ?  85  GLU   B OE1 1 
ATOM   2730 O  OE2 . GLU   B 1 78  ? -6.955  35.333  25.524 0.00 114.53 ?  85  GLU   B OE2 1 
ATOM   2731 N  N   . GLY   B 1 79  ? -7.674  28.746  23.804 1.00 96.19  ?  86  GLY   B N   1 
ATOM   2732 C  CA  . GLY   B 1 79  ? -7.544  28.088  22.496 1.00 98.48  ?  86  GLY   B CA  1 
ATOM   2733 C  C   . GLY   B 1 79  ? -6.155  27.592  22.084 1.00 99.19  ?  86  GLY   B C   1 
ATOM   2734 O  O   . GLY   B 1 79  ? -5.931  27.370  20.892 1.00 100.68 ?  86  GLY   B O   1 
ATOM   2735 N  N   . LYS   B 1 80  ? -5.236  27.412  23.039 1.00 101.04 ?  87  LYS   B N   1 
ATOM   2736 C  CA  . LYS   B 1 80  ? -3.958  26.707  22.785 1.00 104.82 ?  87  LYS   B CA  1 
ATOM   2737 C  C   . LYS   B 1 80  ? -3.394  26.038  24.046 1.00 100.46 ?  87  LYS   B C   1 
ATOM   2738 O  O   . LYS   B 1 80  ? -3.168  26.700  25.061 1.00 105.07 ?  87  LYS   B O   1 
ATOM   2739 C  CB  . LYS   B 1 80  ? -2.901  27.620  22.140 1.00 110.00 ?  87  LYS   B CB  1 
ATOM   2740 C  CG  . LYS   B 1 80  ? -2.585  28.913  22.875 1.00 112.13 ?  87  LYS   B CG  1 
ATOM   2741 C  CD  . LYS   B 1 80  ? -1.725  29.861  22.039 1.00 111.80 ?  87  LYS   B CD  1 
ATOM   2742 C  CE  . LYS   B 1 80  ? -2.233  31.290  22.007 0.00 115.63 ?  87  LYS   B CE  1 
ATOM   2743 N  NZ  . LYS   B 1 80  ? -1.327  32.195  21.248 0.00 115.36 ?  87  LYS   B NZ  1 
ATOM   2744 N  N   . TYR   B 1 81  ? -3.206  24.718  23.961 1.00 96.50  ?  88  TYR   B N   1 
ATOM   2745 C  CA  . TYR   B 1 81  ? -2.699  23.877  25.043 1.00 93.51  ?  88  TYR   B CA  1 
ATOM   2746 C  C   . TYR   B 1 81  ? -1.426  23.182  24.525 1.00 87.29  ?  88  TYR   B C   1 
ATOM   2747 O  O   . TYR   B 1 81  ? -1.496  22.391  23.582 1.00 85.62  ?  88  TYR   B O   1 
ATOM   2748 C  CB  . TYR   B 1 81  ? -3.736  22.832  25.471 1.00 94.19  ?  88  TYR   B CB  1 
ATOM   2749 C  CG  . TYR   B 1 81  ? -5.097  23.390  25.826 1.00 102.77 ?  88  TYR   B CG  1 
ATOM   2750 C  CD1 . TYR   B 1 81  ? -5.388  23.835  27.125 1.00 108.63 ?  88  TYR   B CD1 1 
ATOM   2751 C  CD2 . TYR   B 1 81  ? -6.113  23.462  24.864 1.00 104.92 ?  88  TYR   B CD2 1 
ATOM   2752 C  CE1 . TYR   B 1 81  ? -6.657  24.341  27.452 1.00 109.94 ?  88  TYR   B CE1 1 
ATOM   2753 C  CE2 . TYR   B 1 81  ? -7.378  23.967  25.171 1.00 109.24 ?  88  TYR   B CE2 1 
ATOM   2754 C  CZ  . TYR   B 1 81  ? -7.650  24.406  26.461 1.00 111.53 ?  88  TYR   B CZ  1 
ATOM   2755 O  OH  . TYR   B 1 81  ? -8.903  24.891  26.746 1.00 118.89 ?  88  TYR   B OH  1 
ATOM   2756 N  N   . SER   B 1 82  ? -0.285  23.488  25.141 1.00 84.40  ?  89  SER   B N   1 
ATOM   2757 C  CA  . SER   B 1 82  ? 1.012   22.891  24.793 1.00 84.80  ?  89  SER   B CA  1 
ATOM   2758 C  C   . SER   B 1 82  ? 1.691   22.265  26.002 1.00 80.00  ?  89  SER   B C   1 
ATOM   2759 O  O   . SER   B 1 82  ? 1.567   22.758  27.117 1.00 85.19  ?  89  SER   B O   1 
ATOM   2760 C  CB  . SER   B 1 82  ? 1.947   23.941  24.198 1.00 83.00  ?  89  SER   B CB  1 
ATOM   2761 O  OG  . SER   B 1 82  ? 1.379   24.494  23.029 1.00 94.17  ?  89  SER   B OG  1 
ATOM   2762 N  N   . LEU   B 1 83  ? 2.404   21.175  25.746 1.00 77.14  ?  90  LEU   B N   1 
ATOM   2763 C  CA  . LEU   B 1 83  ? 3.394   20.601  26.660 1.00 74.89  ?  90  LEU   B CA  1 
ATOM   2764 C  C   . LEU   B 1 83  ? 4.774   21.108  26.216 1.00 74.56  ?  90  LEU   B C   1 
ATOM   2765 O  O   . LEU   B 1 83  ? 5.018   21.254  25.013 1.00 74.40  ?  90  LEU   B O   1 
ATOM   2766 C  CB  . LEU   B 1 83  ? 3.349   19.078  26.588 1.00 74.02  ?  90  LEU   B CB  1 
ATOM   2767 C  CG  . LEU   B 1 83  ? 2.000   18.455  26.984 1.00 74.61  ?  90  LEU   B CG  1 
ATOM   2768 C  CD1 . LEU   B 1 83  ? 1.906   16.997  26.570 1.00 76.16  ?  90  LEU   B CD1 1 
ATOM   2769 C  CD2 . LEU   B 1 83  ? 1.751   18.610  28.469 1.00 76.44  ?  90  LEU   B CD2 1 
ATOM   2770 N  N   . VAL   B 1 84  ? 5.642   21.387  27.188 1.00 74.08  ?  91  VAL   B N   1 
ATOM   2771 C  CA  . VAL   B 1 84  ? 6.994   21.907  26.963 1.00 71.05  ?  91  VAL   B CA  1 
ATOM   2772 C  C   . VAL   B 1 84  ? 7.945   20.967  27.686 1.00 67.63  ?  91  VAL   B C   1 
ATOM   2773 O  O   . VAL   B 1 84  ? 7.808   20.734  28.886 1.00 66.96  ?  91  VAL   B O   1 
ATOM   2774 C  CB  . VAL   B 1 84  ? 7.169   23.345  27.507 1.00 73.78  ?  91  VAL   B CB  1 
ATOM   2775 C  CG1 . VAL   B 1 84  ? 8.575   23.870  27.225 1.00 72.57  ?  91  VAL   B CG1 1 
ATOM   2776 C  CG2 . VAL   B 1 84  ? 6.146   24.286  26.881 1.00 78.99  ?  91  VAL   B CG2 1 
ATOM   2777 N  N   . MET   B 1 85  ? 8.942   20.475  26.963 1.00 70.47  ?  92  MET   B N   1 
ATOM   2778 C  CA  . MET   B 1 85  ? 9.866   19.440  27.444 1.00 72.79  ?  92  MET   B CA  1 
ATOM   2779 C  C   . MET   B 1 85  ? 11.286  19.778  27.049 1.00 70.35  ?  92  MET   B C   1 
ATOM   2780 O  O   . MET   B 1 85  ? 11.520  20.618  26.183 1.00 68.39  ?  92  MET   B O   1 
ATOM   2781 C  CB  . MET   B 1 85  ? 9.466   18.054  26.922 1.00 78.66  ?  92  MET   B CB  1 
ATOM   2782 C  CG  . MET   B 1 85  ? 8.892   18.056  25.522 1.00 83.50  ?  92  MET   B CG  1 
ATOM   2783 S  SD  . MET   B 1 85  ? 8.874   16.454  24.735 1.00 93.84  ?  92  MET   B SD  1 
ATOM   2784 C  CE  . MET   B 1 85  ? 10.610  16.218  24.329 1.00 101.67 ?  92  MET   B CE  1 
ATOM   2785 N  N   . GLU   B 1 86  ? 12.220  19.104  27.711 1.00 72.01  ?  93  GLU   B N   1 
ATOM   2786 C  CA  . GLU   B 1 86  ? 13.643  19.323  27.516 1.00 73.50  ?  93  GLU   B CA  1 
ATOM   2787 C  C   . GLU   B 1 86  ? 14.123  18.896  26.131 1.00 72.90  ?  93  GLU   B C   1 
ATOM   2788 O  O   . GLU   B 1 86  ? 13.483  18.073  25.465 1.00 67.41  ?  93  GLU   B O   1 
ATOM   2789 C  CB  . GLU   B 1 86  ? 14.480  18.679  28.645 1.00 80.32  ?  93  GLU   B CB  1 
ATOM   2790 C  CG  . GLU   B 1 86  ? 14.398  17.164  28.820 1.00 83.05  ?  93  GLU   B CG  1 
ATOM   2791 C  CD  . GLU   B 1 86  ? 15.250  16.659  29.978 1.00 89.70  ?  93  GLU   B CD  1 
ATOM   2792 O  OE1 . GLU   B 1 86  ? 16.291  17.269  30.292 1.00 97.14  ?  93  GLU   B OE1 1 
ATOM   2793 O  OE2 . GLU   B 1 86  ? 14.885  15.635  30.585 1.00 89.63  ?  93  GLU   B OE2 1 
ATOM   2794 N  N   . TYR   B 1 87  ? 15.250  19.485  25.728 1.00 72.07  ?  94  TYR   B N   1 
ATOM   2795 C  CA  . TYR   B 1 87  ? 15.774  19.368  24.375 1.00 68.84  ?  94  TYR   B CA  1 
ATOM   2796 C  C   . TYR   B 1 87  ? 16.861  18.304  24.355 1.00 65.79  ?  94  TYR   B C   1 
ATOM   2797 O  O   . TYR   B 1 87  ? 17.783  18.332  25.170 1.00 61.64  ?  94  TYR   B O   1 
ATOM   2798 C  CB  . TYR   B 1 87  ? 16.307  20.720  23.883 1.00 68.72  ?  94  TYR   B CB  1 
ATOM   2799 C  CG  . TYR   B 1 87  ? 16.931  20.699  22.502 1.00 66.47  ?  94  TYR   B CG  1 
ATOM   2800 C  CD1 . TYR   B 1 87  ? 16.248  20.164  21.393 1.00 67.42  ?  94  TYR   B CD1 1 
ATOM   2801 C  CD2 . TYR   B 1 87  ? 18.193  21.250  22.287 1.00 67.56  ?  94  TYR   B CD2 1 
ATOM   2802 C  CE1 . TYR   B 1 87  ? 16.824  20.154  20.118 1.00 67.36  ?  94  TYR   B CE1 1 
ATOM   2803 C  CE2 . TYR   B 1 87  ? 18.780  21.238  21.028 1.00 68.92  ?  94  TYR   B CE2 1 
ATOM   2804 C  CZ  . TYR   B 1 87  ? 18.100  20.709  19.938 1.00 70.40  ?  94  TYR   B CZ  1 
ATOM   2805 O  OH  . TYR   B 1 87  ? 18.717  20.713  18.703 1.00 69.35  ?  94  TYR   B OH  1 
ATOM   2806 N  N   . MET   B 1 88  ? 16.741  17.395  23.397 1.00 64.49  ?  95  MET   B N   1 
ATOM   2807 C  CA  . MET   B 1 88  ? 17.658  16.272  23.229 1.00 69.29  ?  95  MET   B CA  1 
ATOM   2808 C  C   . MET   B 1 88  ? 18.195  16.341  21.819 1.00 70.41  ?  95  MET   B C   1 
ATOM   2809 O  O   . MET   B 1 88  ? 17.492  16.028  20.854 1.00 64.50  ?  95  MET   B O   1 
ATOM   2810 C  CB  . MET   B 1 88  ? 16.921  14.958  23.476 1.00 73.60  ?  95  MET   B CB  1 
ATOM   2811 C  CG  . MET   B 1 88  ? 16.372  14.797  24.888 1.00 69.83  ?  95  MET   B CG  1 
ATOM   2812 S  SD  . MET   B 1 88  ? 17.677  14.667  26.115 1.00 65.12  ?  95  MET   B SD  1 
ATOM   2813 C  CE  . MET   B 1 88  ? 18.185  12.958  25.960 1.00 68.53  ?  95  MET   B CE  1 
ATOM   2814 N  N   . GLU   B 1 89  ? 19.464  16.736  21.722 1.00 71.08  ?  96  GLU   B N   1 
ATOM   2815 C  CA  . GLU   B 1 89  ? 20.047  17.317  20.497 1.00 75.18  ?  96  GLU   B CA  1 
ATOM   2816 C  C   . GLU   B 1 89  ? 20.073  16.369  19.277 1.00 68.97  ?  96  GLU   B C   1 
ATOM   2817 O  O   . GLU   B 1 89  ? 19.766  16.780  18.149 1.00 62.80  ?  96  GLU   B O   1 
ATOM   2818 C  CB  . GLU   B 1 89  ? 21.470  17.842  20.786 1.00 86.30  ?  96  GLU   B CB  1 
ATOM   2819 C  CG  . GLU   B 1 89  ? 21.559  18.916  21.884 1.00 97.96  ?  96  GLU   B CG  1 
ATOM   2820 C  CD  . GLU   B 1 89  ? 22.170  18.434  23.212 1.00 103.94 ?  96  GLU   B CD  1 
ATOM   2821 O  OE1 . GLU   B 1 89  ? 21.600  17.539  23.887 1.00 76.30  ?  96  GLU   B OE1 1 
ATOM   2822 O  OE2 . GLU   B 1 89  ? 23.230  18.975  23.599 1.00 118.11 ?  96  GLU   B OE2 1 
ATOM   2823 N  N   . LYS   B 1 90  ? 20.409  15.101  19.513 1.00 65.92  ?  97  LYS   B N   1 
ATOM   2824 C  CA  . LYS   B 1 90  ? 20.520  14.105  18.435 1.00 67.52  ?  97  LYS   B CA  1 
ATOM   2825 C  C   . LYS   B 1 90  ? 19.187  13.498  17.927 1.00 71.25  ?  97  LYS   B C   1 
ATOM   2826 O  O   . LYS   B 1 90  ? 19.201  12.659  17.016 1.00 78.71  ?  97  LYS   B O   1 
ATOM   2827 C  CB  . LYS   B 1 90  ? 21.482  13.000  18.871 1.00 71.61  ?  97  LYS   B CB  1 
ATOM   2828 C  CG  . LYS   B 1 90  ? 22.911  13.482  19.022 1.00 80.64  ?  97  LYS   B CG  1 
ATOM   2829 C  CD  . LYS   B 1 90  ? 23.901  12.344  19.209 1.00 81.61  ?  97  LYS   B CD  1 
ATOM   2830 C  CE  . LYS   B 1 90  ? 25.322  12.861  19.036 1.00 87.33  ?  97  LYS   B CE  1 
ATOM   2831 N  NZ  . LYS   B 1 90  ? 25.760  12.849  17.614 1.00 89.77  ?  97  LYS   B NZ  1 
ATOM   2832 N  N   . GLY   B 1 91  ? 18.056  13.907  18.499 1.00 64.93  ?  98  GLY   B N   1 
ATOM   2833 C  CA  . GLY   B 1 91  ? 16.744  13.471  18.054 1.00 67.76  ?  98  GLY   B CA  1 
ATOM   2834 C  C   . GLY   B 1 91  ? 16.443  12.107  18.635 1.00 66.88  ?  98  GLY   B C   1 
ATOM   2835 O  O   . GLY   B 1 91  ? 17.009  11.715  19.672 1.00 68.06  ?  98  GLY   B O   1 
ATOM   2836 N  N   . ASN   B 1 92  ? 15.557  11.372  17.961 1.00 72.65  ?  99  ASN   B N   1 
ATOM   2837 C  CA  . ASN   B 1 92  ? 15.169  10.042  18.430 1.00 68.14  ?  99  ASN   B CA  1 
ATOM   2838 C  C   . ASN   B 1 92  ? 16.233  8.954   18.133 1.00 68.70  ?  99  ASN   B C   1 
ATOM   2839 O  O   . ASN   B 1 92  ? 17.185  9.196   17.390 1.00 63.41  ?  99  ASN   B O   1 
ATOM   2840 C  CB  . ASN   B 1 92  ? 13.746  9.664   17.984 1.00 78.97  ?  99  ASN   B CB  1 
ATOM   2841 C  CG  . ASN   B 1 92  ? 13.591  9.457   16.482 1.00 82.81  ?  99  ASN   B CG  1 
ATOM   2842 O  OD1 . ASN   B 1 92  ? 14.471  8.928   15.801 1.00 84.37  ?  99  ASN   B OD1 1 
ATOM   2843 N  ND2 . ASN   B 1 92  ? 12.426  9.835   15.963 1.00 95.36  ?  99  ASN   B ND2 1 
ATOM   2844 N  N   . LEU   B 1 93  ? 16.037  7.770   18.714 1.00 58.63  ?  100 LEU   B N   1 
ATOM   2845 C  CA  . LEU   B 1 93  ? 16.995  6.658   18.589 1.00 62.82  ?  100 LEU   B CA  1 
ATOM   2846 C  C   . LEU   B 1 93  ? 17.214  6.169   17.154 1.00 59.00  ?  100 LEU   B C   1 
ATOM   2847 O  O   . LEU   B 1 93  ? 18.338  5.858   16.791 1.00 65.34  ?  100 LEU   B O   1 
ATOM   2848 C  CB  . LEU   B 1 93  ? 16.572  5.464   19.470 1.00 66.31  ?  100 LEU   B CB  1 
ATOM   2849 C  CG  . LEU   B 1 93  ? 17.457  4.202   19.462 1.00 63.72  ?  100 LEU   B CG  1 
ATOM   2850 C  CD1 . LEU   B 1 93  ? 18.844  4.534   19.981 1.00 69.50  ?  100 LEU   B CD1 1 
ATOM   2851 C  CD2 . LEU   B 1 93  ? 16.832  3.081   20.265 1.00 64.57  ?  100 LEU   B CD2 1 
ATOM   2852 N  N   . MET   B 1 94  ? 16.147  6.054   16.373 1.00 59.13  ?  101 MET   B N   1 
ATOM   2853 C  CA  . MET   B 1 94  ? 16.240  5.551   14.985 1.00 67.53  ?  101 MET   B CA  1 
ATOM   2854 C  C   . MET   B 1 94  ? 16.980  6.542   14.076 1.00 75.10  ?  101 MET   B C   1 
ATOM   2855 O  O   . MET   B 1 94  ? 17.740  6.127   13.201 1.00 83.18  ?  101 MET   B O   1 
ATOM   2856 C  CB  . MET   B 1 94  ? 14.843  5.255   14.422 1.00 72.71  ?  101 MET   B CB  1 
ATOM   2857 C  CG  . MET   B 1 94  ? 14.814  4.518   13.083 1.00 73.58  ?  101 MET   B CG  1 
ATOM   2858 S  SD  . MET   B 1 94  ? 15.532  2.869   13.122 1.00 73.07  ?  101 MET   B SD  1 
ATOM   2859 C  CE  . MET   B 1 94  ? 14.374  2.032   14.201 1.00 73.26  ?  101 MET   B CE  1 
ATOM   2860 N  N   . HIS   B 1 95  ? 16.740  7.839   14.280 1.00 73.51  ?  102 HIS   B N   1 
ATOM   2861 C  CA  . HIS   B 1 95  ? 17.505  8.911   13.620 1.00 72.89  ?  102 HIS   B CA  1 
ATOM   2862 C  C   . HIS   B 1 95  ? 19.027  8.835   13.867 1.00 66.85  ?  102 HIS   B C   1 
ATOM   2863 O  O   . HIS   B 1 95  ? 19.801  9.074   12.954 1.00 68.26  ?  102 HIS   B O   1 
ATOM   2864 C  CB  . HIS   B 1 95  ? 16.942  10.286  14.029 1.00 68.48  ?  102 HIS   B CB  1 
ATOM   2865 C  CG  . HIS   B 1 95  ? 17.563  11.432  13.304 1.00 76.76  ?  102 HIS   B CG  1 
ATOM   2866 N  ND1 . HIS   B 1 95  ? 18.647  12.122  13.804 1.00 78.92  ?  102 HIS   B ND1 1 
ATOM   2867 C  CD2 . HIS   B 1 95  ? 17.272  11.995  12.108 1.00 80.19  ?  102 HIS   B CD2 1 
ATOM   2868 C  CE1 . HIS   B 1 95  ? 18.990  13.069  12.952 1.00 80.85  ?  102 HIS   B CE1 1 
ATOM   2869 N  NE2 . HIS   B 1 95  ? 18.173  13.012  11.915 1.00 83.33  ?  102 HIS   B NE2 1 
ATOM   2870 N  N   . VAL   B 1 96  ? 19.430  8.489   15.086 1.00 67.16  ?  103 VAL   B N   1 
ATOM   2871 C  CA  . VAL   B 1 96  ? 20.843  8.303   15.444 1.00 66.39  ?  103 VAL   B CA  1 
ATOM   2872 C  C   . VAL   B 1 96  ? 21.427  7.024   14.831 1.00 62.15  ?  103 VAL   B C   1 
ATOM   2873 O  O   . VAL   B 1 96  ? 22.565  7.043   14.361 1.00 61.97  ?  103 VAL   B O   1 
ATOM   2874 C  CB  . VAL   B 1 96  ? 21.049  8.359   16.982 1.00 61.30  ?  103 VAL   B CB  1 
ATOM   2875 C  CG1 . VAL   B 1 96  ? 22.478  8.015   17.400 1.00 61.77  ?  103 VAL   B CG1 1 
ATOM   2876 C  CG2 . VAL   B 1 96  ? 20.726  9.757   17.467 1.00 67.72  ?  103 VAL   B CG2 1 
ATOM   2877 N  N   . LEU   B 1 97  ? 20.671  5.927   14.863 1.00 66.82  ?  104 LEU   B N   1 
ATOM   2878 C  CA  . LEU   B 1 97  ? 21.124  4.644   14.265 1.00 64.99  ?  104 LEU   B CA  1 
ATOM   2879 C  C   . LEU   B 1 97  ? 21.323  4.675   12.750 1.00 70.63  ?  104 LEU   B C   1 
ATOM   2880 O  O   . LEU   B 1 97  ? 22.143  3.908   12.234 1.00 75.07  ?  104 LEU   B O   1 
ATOM   2881 C  CB  . LEU   B 1 97  ? 20.176  3.487   14.613 1.00 64.01  ?  104 LEU   B CB  1 
ATOM   2882 C  CG  . LEU   B 1 97  ? 20.074  3.137   16.093 1.00 63.09  ?  104 LEU   B CG  1 
ATOM   2883 C  CD1 . LEU   B 1 97  ? 18.870  2.229   16.315 1.00 73.95  ?  104 LEU   B CD1 1 
ATOM   2884 C  CD2 . LEU   B 1 97  ? 21.345  2.519   16.647 1.00 64.16  ?  104 LEU   B CD2 1 
ATOM   2885 N  N   . LYS   B 1 98  ? 20.594  5.554   12.049 1.00 74.42  ?  105 LYS   B N   1 
ATOM   2886 C  CA  . LYS   B 1 98  ? 20.739  5.723   10.582 1.00 69.46  ?  105 LYS   B CA  1 
ATOM   2887 C  C   . LYS   B 1 98  ? 21.851  6.680   10.104 1.00 76.99  ?  105 LYS   B C   1 
ATOM   2888 O  O   . LYS   B 1 98  ? 22.144  6.694   8.916  1.00 87.21  ?  105 LYS   B O   1 
ATOM   2889 C  CB  . LYS   B 1 98  ? 19.397  6.121   9.963  1.00 72.00  ?  105 LYS   B CB  1 
ATOM   2890 C  CG  . LYS   B 1 98  ? 18.336  5.036   10.042 1.00 70.32  ?  105 LYS   B CG  1 
ATOM   2891 C  CD  . LYS   B 1 98  ? 16.999  5.497   9.479  1.00 77.09  ?  105 LYS   B CD  1 
ATOM   2892 C  CE  . LYS   B 1 98  ? 16.105  4.320   9.100  1.00 84.76  ?  105 LYS   B CE  1 
ATOM   2893 N  NZ  . LYS   B 1 98  ? 14.724  4.713   8.802  0.00 79.80  ?  105 LYS   B NZ  1 
ATOM   2894 N  N   . ALA   B 1 99  ? 22.469  7.443   11.013 1.00 81.42  ?  106 ALA   B N   1 
ATOM   2895 C  CA  . ALA   B 1 99  ? 23.459  8.481   10.671 1.00 90.68  ?  106 ALA   B CA  1 
ATOM   2896 C  C   . ALA   B 1 99  ? 24.773  7.943   10.091 1.00 100.66 ?  106 ALA   B C   1 
ATOM   2897 O  O   . ALA   B 1 99  ? 25.111  6.773   10.288 1.00 113.11 ?  106 ALA   B O   1 
ATOM   2898 C  CB  . ALA   B 1 99  ? 23.755  9.353   11.891 1.00 90.57  ?  106 ALA   B CB  1 
ATOM   2899 N  N   . GLU   B 1 100 ? 25.495  8.822   9.387  1.00 117.42 ?  107 GLU   B N   1 
ATOM   2900 C  CA  . GLU   B 1 100 ? 26.712  8.448   8.634  1.00 127.54 ?  107 GLU   B CA  1 
ATOM   2901 C  C   . GLU   B 1 100 ? 27.874  7.986   9.526  1.00 134.82 ?  107 GLU   B C   1 
ATOM   2902 O  O   . GLU   B 1 100 ? 28.567  7.021   9.179  1.00 147.12 ?  107 GLU   B O   1 
ATOM   2903 C  CB  . GLU   B 1 100 ? 27.165  9.577   7.680  1.00 131.75 ?  107 GLU   B CB  1 
ATOM   2904 C  CG  . GLU   B 1 100 ? 27.737  10.834  8.331  1.00 131.07 ?  107 GLU   B CG  1 
ATOM   2905 C  CD  . GLU   B 1 100 ? 27.914  11.992  7.358  0.00 148.76 ?  107 GLU   B CD  1 
ATOM   2906 O  OE1 . GLU   B 1 100 ? 28.417  11.771  6.235  0.00 151.20 ?  107 GLU   B OE1 1 
ATOM   2907 O  OE2 . GLU   B 1 100 ? 27.549  13.131  7.720  0.00 148.72 ?  107 GLU   B OE2 1 
ATOM   2908 N  N   . MET   B 1 101 ? 28.068  8.670   10.659 1.00 132.38 ?  108 MET   B N   1 
ATOM   2909 C  CA  . MET   B 1 101 ? 29.040  8.252   11.681 1.00 129.16 ?  108 MET   B CA  1 
ATOM   2910 C  C   . MET   B 1 101 ? 28.406  7.107   12.473 1.00 131.88 ?  108 MET   B C   1 
ATOM   2911 O  O   . MET   B 1 101 ? 27.353  7.301   13.088 1.00 143.80 ?  108 MET   B O   1 
ATOM   2912 C  CB  . MET   B 1 101 ? 29.410  9.420   12.605 1.00 126.20 ?  108 MET   B CB  1 
ATOM   2913 C  CG  . MET   B 1 101 ? 30.615  9.154   13.496 1.00 122.10 ?  108 MET   B CG  1 
ATOM   2914 S  SD  . MET   B 1 101 ? 31.157  10.596  14.410 0.00 133.29 ?  108 MET   B SD  1 
ATOM   2915 C  CE  . MET   B 1 101 ? 32.587  9.942   15.267 0.00 133.97 ?  108 MET   B CE  1 
ATOM   2916 N  N   . SER   B 1 102 ? 29.028  5.923   12.428 1.00 127.35 ?  109 SER   B N   1 
ATOM   2917 C  CA  . SER   B 1 102 ? 28.462  4.711   13.031 1.00 117.51 ?  109 SER   B CA  1 
ATOM   2918 C  C   . SER   B 1 102 ? 28.664  4.727   14.557 1.00 106.68 ?  109 SER   B C   1 
ATOM   2919 O  O   . SER   B 1 102 ? 29.669  5.247   15.061 1.00 125.49 ?  109 SER   B O   1 
ATOM   2920 C  CB  . SER   B 1 102 ? 29.069  3.445   12.406 1.00 116.16 ?  109 SER   B CB  1 
ATOM   2921 O  OG  . SER   B 1 102 ? 28.167  2.352   12.469 1.00 126.80 ?  109 SER   B OG  1 
ATOM   2922 N  N   . THR   B 1 103 ? 27.683  4.178   15.267 1.00 83.15  ?  110 THR   B N   1 
ATOM   2923 C  CA  . THR   B 1 103 ? 27.678  4.108   16.725 1.00 73.83  ?  110 THR   B CA  1 
ATOM   2924 C  C   . THR   B 1 103 ? 28.389  2.805   17.141 1.00 76.63  ?  110 THR   B C   1 
ATOM   2925 O  O   . THR   B 1 103 ? 27.979  1.728   16.688 1.00 82.59  ?  110 THR   B O   1 
ATOM   2926 C  CB  . THR   B 1 103 ? 26.236  4.055   17.287 1.00 68.06  ?  110 THR   B CB  1 
ATOM   2927 O  OG1 . THR   B 1 103 ? 25.389  5.007   16.624 1.00 68.99  ?  110 THR   B OG1 1 
ATOM   2928 C  CG2 . THR   B 1 103 ? 26.238  4.303   18.781 1.00 67.53  ?  110 THR   B CG2 1 
ATOM   2929 N  N   . PRO   B 1 104 ? 29.453  2.882   17.981 1.00 76.64  ?  111 PRO   B N   1 
ATOM   2930 C  CA  . PRO   B 1 104 ? 30.094  1.640   18.429 1.00 74.75  ?  111 PRO   B CA  1 
ATOM   2931 C  C   . PRO   B 1 104 ? 29.268  0.792   19.408 1.00 68.58  ?  111 PRO   B C   1 
ATOM   2932 O  O   . PRO   B 1 104 ? 28.239  1.233   19.927 1.00 75.72  ?  111 PRO   B O   1 
ATOM   2933 C  CB  . PRO   B 1 104 ? 31.379  2.136   19.092 1.00 78.10  ?  111 PRO   B CB  1 
ATOM   2934 C  CG  . PRO   B 1 104 ? 31.069  3.513   19.518 1.00 77.20  ?  111 PRO   B CG  1 
ATOM   2935 C  CD  . PRO   B 1 104 ? 30.251  4.049   18.395 1.00 78.75  ?  111 PRO   B CD  1 
ATOM   2936 N  N   . LEU   B 1 105 ? 29.754  -0.426  19.634 1.00 69.54  ?  112 LEU   B N   1 
ATOM   2937 C  CA  . LEU   B 1 105 ? 29.114  -1.407  20.512 1.00 64.71  ?  112 LEU   B CA  1 
ATOM   2938 C  C   . LEU   B 1 105 ? 28.977  -0.968  21.977 1.00 63.68  ?  112 LEU   B C   1 
ATOM   2939 O  O   . LEU   B 1 105 ? 27.986  -1.307  22.611 1.00 66.07  ?  112 LEU   B O   1 
ATOM   2940 C  CB  . LEU   B 1 105 ? 29.887  -2.721  20.442 1.00 64.15  ?  112 LEU   B CB  1 
ATOM   2941 C  CG  . LEU   B 1 105 ? 29.409  -3.923  21.262 1.00 65.31  ?  112 LEU   B CG  1 
ATOM   2942 C  CD1 . LEU   B 1 105 ? 27.958  -4.288  20.988 1.00 60.49  ?  112 LEU   B CD1 1 
ATOM   2943 C  CD2 . LEU   B 1 105 ? 30.300  -5.112  20.969 1.00 60.08  ?  112 LEU   B CD2 1 
ATOM   2944 N  N   . SER   B 1 106 ? 29.963  -0.229  22.499 1.00 60.21  ?  113 SER   B N   1 
ATOM   2945 C  CA  . SER   B 1 106 ? 29.941  0.268   23.878 1.00 56.01  ?  113 SER   B CA  1 
ATOM   2946 C  C   . SER   B 1 106 ? 28.821  1.269   24.111 1.00 58.51  ?  113 SER   B C   1 
ATOM   2947 O  O   . SER   B 1 106 ? 28.166  1.217   25.143 1.00 60.28  ?  113 SER   B O   1 
ATOM   2948 C  CB  . SER   B 1 106 ? 31.288  0.891   24.273 1.00 60.21  ?  113 SER   B CB  1 
ATOM   2949 O  OG  . SER   B 1 106 ? 31.654  1.942   23.386 1.00 73.90  ?  113 SER   B OG  1 
ATOM   2950 N  N   . VAL   B 1 107 ? 28.611  2.162   23.146 1.00 60.15  ?  114 VAL   B N   1 
ATOM   2951 C  CA  . VAL   B 1 107 ? 27.544  3.177   23.203 1.00 58.18  ?  114 VAL   B CA  1 
ATOM   2952 C  C   . VAL   B 1 107 ? 26.177  2.493   23.097 1.00 55.57  ?  114 VAL   B C   1 
ATOM   2953 O  O   . VAL   B 1 107 ? 25.272  2.828   23.869 1.00 56.20  ?  114 VAL   B O   1 
ATOM   2954 C  CB  . VAL   B 1 107 ? 27.739  4.278   22.114 1.00 62.51  ?  114 VAL   B CB  1 
ATOM   2955 C  CG1 . VAL   B 1 107 ? 26.576  5.251   22.062 1.00 58.39  ?  114 VAL   B CG1 1 
ATOM   2956 C  CG2 . VAL   B 1 107 ? 29.033  5.055   22.350 1.00 58.36  ?  114 VAL   B CG2 1 
ATOM   2957 N  N   . LYS   B 1 108 ? 26.043  1.548   22.160 1.00 54.27  ?  115 LYS   B N   1 
ATOM   2958 C  CA  . LYS   B 1 108 ? 24.830  0.722   22.044 1.00 60.66  ?  115 LYS   B CA  1 
ATOM   2959 C  C   . LYS   B 1 108 ? 24.482  -0.012  23.337 1.00 60.90  ?  115 LYS   B C   1 
ATOM   2960 O  O   . LYS   B 1 108 ? 23.331  0.035   23.787 1.00 60.91  ?  115 LYS   B O   1 
ATOM   2961 C  CB  . LYS   B 1 108 ? 24.934  -0.265  20.869 1.00 62.42  ?  115 LYS   B CB  1 
ATOM   2962 C  CG  . LYS   B 1 108 ? 24.806  0.461   19.540 1.00 63.98  ?  115 LYS   B CG  1 
ATOM   2963 C  CD  . LYS   B 1 108 ? 24.770  -0.476  18.347 1.00 57.04  ?  115 LYS   B CD  1 
ATOM   2964 C  CE  . LYS   B 1 108 ? 24.669  0.363   17.087 1.00 51.28  ?  115 LYS   B CE  1 
ATOM   2965 N  NZ  . LYS   B 1 108 ? 24.415  -0.490  15.912 1.00 57.75  ?  115 LYS   B NZ  1 
ATOM   2966 N  N   . GLY   B 1 109 ? 25.491  -0.648  23.937 1.00 59.44  ?  116 GLY   B N   1 
ATOM   2967 C  CA  . GLY   B 1 109 ? 25.363  -1.300  25.250 1.00 54.29  ?  116 GLY   B CA  1 
ATOM   2968 C  C   . GLY   B 1 109 ? 24.861  -0.379  26.358 1.00 55.03  ?  116 GLY   B C   1 
ATOM   2969 O  O   . GLY   B 1 109 ? 23.979  -0.746  27.150 1.00 57.82  ?  116 GLY   B O   1 
ATOM   2970 N  N   . ARG   B 1 110 ? 25.403  0.833   26.381 1.00 51.19  ?  117 ARG   B N   1 
ATOM   2971 C  CA  . ARG   B 1 110 ? 25.022  1.859   27.334 1.00 49.43  ?  117 ARG   B CA  1 
ATOM   2972 C  C   . ARG   B 1 110 ? 23.600  2.359   27.079 1.00 46.25  ?  117 ARG   B C   1 
ATOM   2973 O  O   . ARG   B 1 110 ? 22.843  2.522   28.022 1.00 51.82  ?  117 ARG   B O   1 
ATOM   2974 C  CB  . ARG   B 1 110 ? 26.030  3.031   27.310 1.00 50.67  ?  117 ARG   B CB  1 
ATOM   2975 C  CG  . ARG   B 1 110 ? 26.017  3.861   28.588 1.00 54.86  ?  117 ARG   B CG  1 
ATOM   2976 C  CD  . ARG   B 1 110 ? 27.061  4.962   28.570 1.00 58.06  ?  117 ARG   B CD  1 
ATOM   2977 N  NE  . ARG   B 1 110 ? 26.840  5.930   27.488 1.00 59.31  ?  117 ARG   B NE  1 
ATOM   2978 C  CZ  . ARG   B 1 110 ? 27.618  6.986   27.222 1.00 72.07  ?  117 ARG   B CZ  1 
ATOM   2979 N  NH1 . ARG   B 1 110 ? 28.694  7.277   27.970 1.00 73.78  ?  117 ARG   B NH1 1 
ATOM   2980 N  NH2 . ARG   B 1 110 ? 27.308  7.777   26.195 1.00 74.60  ?  117 ARG   B NH2 1 
ATOM   2981 N  N   . ILE   B 1 111 ? 23.249  2.586   25.812 1.00 54.77  ?  118 ILE   B N   1 
ATOM   2982 C  CA  . ILE   B 1 111 ? 21.872  2.905   25.395 1.00 52.89  ?  118 ILE   B CA  1 
ATOM   2983 C  C   . ILE   B 1 111 ? 20.871  1.858   25.920 1.00 51.39  ?  118 ILE   B C   1 
ATOM   2984 O  O   . ILE   B 1 111 ? 19.830  2.242   26.436 1.00 58.58  ?  118 ILE   B O   1 
ATOM   2985 C  CB  . ILE   B 1 111 ? 21.768  3.105   23.842 1.00 55.29  ?  118 ILE   B CB  1 
ATOM   2986 C  CG1 . ILE   B 1 111 ? 22.406  4.444   23.451 1.00 57.89  ?  118 ILE   B CG1 1 
ATOM   2987 C  CG2 . ILE   B 1 111 ? 20.314  3.101   23.325 1.00 51.67  ?  118 ILE   B CG2 1 
ATOM   2988 C  CD1 . ILE   B 1 111 ? 22.751  4.597   21.977 1.00 59.02  ?  118 ILE   B CD1 1 
ATOM   2989 N  N   . ILE   B 1 112 ? 21.197  0.570   25.808 1.00 47.92  ?  119 ILE   B N   1 
ATOM   2990 C  CA  . ILE   B 1 112 ? 20.275  -0.518  26.240 1.00 53.38  ?  119 ILE   B CA  1 
ATOM   2991 C  C   . ILE   B 1 112 ? 20.096  -0.524  27.766 1.00 55.51  ?  119 ILE   B C   1 
ATOM   2992 O  O   . ILE   B 1 112 ? 18.968  -0.688  28.258 1.00 54.95  ?  119 ILE   B O   1 
ATOM   2993 C  CB  . ILE   B 1 112 ? 20.734  -1.910  25.713 1.00 53.55  ?  119 ILE   B CB  1 
ATOM   2994 C  CG1 . ILE   B 1 112 ? 20.619  -1.956  24.179 1.00 56.27  ?  119 ILE   B CG1 1 
ATOM   2995 C  CG2 . ILE   B 1 112 ? 19.913  -3.053  26.304 1.00 57.67  ?  119 ILE   B CG2 1 
ATOM   2996 C  CD1 . ILE   B 1 112 ? 21.470  -3.021  23.506 1.00 58.96  ?  119 ILE   B CD1 1 
ATOM   2997 N  N   . LEU   B 1 113 ? 21.193  -0.351  28.505 1.00 53.27  ?  120 LEU   B N   1 
ATOM   2998 C  CA  . LEU   B 1 113 ? 21.125  -0.276  29.973 1.00 59.26  ?  120 LEU   B CA  1 
ATOM   2999 C  C   . LEU   B 1 113 ? 20.356  0.963   30.483 1.00 55.64  ?  120 LEU   B C   1 
ATOM   3000 O  O   . LEU   B 1 113 ? 19.607  0.880   31.468 1.00 56.12  ?  120 LEU   B O   1 
ATOM   3001 C  CB  . LEU   B 1 113 ? 22.523  -0.331  30.600 1.00 64.84  ?  120 LEU   B CB  1 
ATOM   3002 C  CG  . LEU   B 1 113 ? 22.653  -0.358  32.127 1.00 58.32  ?  120 LEU   B CG  1 
ATOM   3003 C  CD1 . LEU   B 1 113 ? 21.782  -1.425  32.771 1.00 58.16  ?  120 LEU   B CD1 1 
ATOM   3004 C  CD2 . LEU   B 1 113 ? 24.104  -0.576  32.502 1.00 64.15  ?  120 LEU   B CD2 1 
ATOM   3005 N  N   . GLU   B 1 114 ? 20.539  2.096   29.819 1.00 57.71  ?  121 GLU   B N   1 
ATOM   3006 C  CA  . GLU   B 1 114 ? 19.780  3.317   30.159 1.00 62.87  ?  121 GLU   B CA  1 
ATOM   3007 C  C   . GLU   B 1 114 ? 18.286  3.155   29.888 1.00 61.10  ?  121 GLU   B C   1 
ATOM   3008 O  O   . GLU   B 1 114 ? 17.470  3.617   30.687 1.00 61.46  ?  121 GLU   B O   1 
ATOM   3009 C  CB  . GLU   B 1 114 ? 20.368  4.537   29.444 1.00 63.95  ?  121 GLU   B CB  1 
ATOM   3010 C  CG  . GLU   B 1 114 ? 21.713  4.926   30.049 1.00 68.46  ?  121 GLU   B CG  1 
ATOM   3011 C  CD  . GLU   B 1 114 ? 22.399  6.104   29.378 1.00 73.99  ?  121 GLU   B CD  1 
ATOM   3012 O  OE1 . GLU   B 1 114 ? 21.972  6.537   28.286 1.00 82.87  ?  121 GLU   B OE1 1 
ATOM   3013 O  OE2 . GLU   B 1 114 ? 23.396  6.592   29.957 1.00 69.41  ?  121 GLU   B OE2 1 
ATOM   3014 N  N   . ILE   B 1 115 ? 17.952  2.481   28.778 1.00 61.99  ?  122 ILE   B N   1 
ATOM   3015 C  CA  . ILE   B 1 115 ? 16.571  2.083   28.454 1.00 56.14  ?  122 ILE   B CA  1 
ATOM   3016 C  C   . ILE   B 1 115 ? 15.990  1.209   29.580 1.00 58.54  ?  122 ILE   B C   1 
ATOM   3017 O  O   . ILE   B 1 115 ? 14.867  1.440   30.012 1.00 61.48  ?  122 ILE   B O   1 
ATOM   3018 C  CB  . ILE   B 1 115 ? 16.491  1.380   27.056 1.00 56.66  ?  122 ILE   B CB  1 
ATOM   3019 C  CG1 . ILE   B 1 115 ? 16.664  2.409   25.949 1.00 48.13  ?  122 ILE   B CG1 1 
ATOM   3020 C  CG2 . ILE   B 1 115 ? 15.181  0.595   26.835 1.00 53.23  ?  122 ILE   B CG2 1 
ATOM   3021 C  CD1 . ILE   B 1 115 ? 17.132  1.843   24.627 1.00 45.22  ?  122 ILE   B CD1 1 
ATOM   3022 N  N   . ILE   B 1 116 ? 16.765  0.233   30.045 1.00 62.72  ?  123 ILE   B N   1 
ATOM   3023 C  CA  . ILE   B 1 116 ? 16.345  -0.658  31.139 1.00 61.18  ?  123 ILE   B CA  1 
ATOM   3024 C  C   . ILE   B 1 116 ? 16.111  0.115   32.448 1.00 59.69  ?  123 ILE   B C   1 
ATOM   3025 O  O   . ILE   B 1 116 ? 15.106  -0.120  33.114 1.00 61.74  ?  123 ILE   B O   1 
ATOM   3026 C  CB  . ILE   B 1 116 ? 17.360  -1.809  31.359 1.00 53.82  ?  123 ILE   B CB  1 
ATOM   3027 C  CG1 . ILE   B 1 116 ? 17.375  -2.749  30.143 1.00 60.74  ?  123 ILE   B CG1 1 
ATOM   3028 C  CG2 . ILE   B 1 116 ? 17.041  -2.608  32.632 1.00 52.58  ?  123 ILE   B CG2 1 
ATOM   3029 C  CD1 . ILE   B 1 116 ? 18.687  -3.506  29.957 1.00 59.82  ?  123 ILE   B CD1 1 
ATOM   3030 N  N   . GLU   B 1 117 ? 17.057  0.990   32.809 1.00 57.95  ?  124 GLU   B N   1 
ATOM   3031 C  CA  . GLU   B 1 117 ? 16.956  1.859   33.997 1.00 55.92  ?  124 GLU   B CA  1 
ATOM   3032 C  C   . GLU   B 1 117 ? 15.671  2.691   33.993 1.00 55.90  ?  124 GLU   B C   1 
ATOM   3033 O  O   . GLU   B 1 117 ? 14.930  2.707   34.977 1.00 58.33  ?  124 GLU   B O   1 
ATOM   3034 C  CB  . GLU   B 1 117 ? 18.157  2.804   34.080 1.00 63.32  ?  124 GLU   B CB  1 
ATOM   3035 C  CG  . GLU   B 1 117 ? 19.452  2.152   34.581 1.00 64.26  ?  124 GLU   B CG  1 
ATOM   3036 C  CD  . GLU   B 1 117 ? 20.685  3.024   34.368 1.00 67.30  ?  124 GLU   B CD  1 
ATOM   3037 O  OE1 . GLU   B 1 117 ? 20.568  4.235   34.077 1.00 69.25  ?  124 GLU   B OE1 1 
ATOM   3038 O  OE2 . GLU   B 1 117 ? 21.798  2.488   34.497 1.00 75.34  ?  124 GLU   B OE2 1 
ATOM   3039 N  N   . GLY   B 1 118 ? 15.416  3.351   32.868 1.00 54.77  ?  125 GLY   B N   1 
ATOM   3040 C  CA  . GLY   B 1 118 ? 14.228  4.178   32.684 1.00 61.90  ?  125 GLY   B CA  1 
ATOM   3041 C  C   . GLY   B 1 118 ? 12.908  3.418   32.736 1.00 61.70  ?  125 GLY   B C   1 
ATOM   3042 O  O   . GLY   B 1 118 ? 11.944  3.884   33.369 1.00 53.86  ?  125 GLY   B O   1 
ATOM   3043 N  N   . MET   B 1 119 ? 12.858  2.261   32.076 1.00 62.97  ?  126 MET   B N   1 
ATOM   3044 C  CA  . MET   B 1 119 ? 11.673  1.384   32.140 1.00 65.24  ?  126 MET   B CA  1 
ATOM   3045 C  C   . MET   B 1 119 ? 11.415  0.813   33.539 1.00 64.86  ?  126 MET   B C   1 
ATOM   3046 O  O   . MET   B 1 119 ? 10.266  0.703   33.954 1.00 66.40  ?  126 MET   B O   1 
ATOM   3047 C  CB  . MET   B 1 119 ? 11.760  0.252   31.093 1.00 64.11  ?  126 MET   B CB  1 
ATOM   3048 C  CG  . MET   B 1 119 ? 11.714  0.698   29.644 1.00 64.42  ?  126 MET   B CG  1 
ATOM   3049 S  SD  . MET   B 1 119 ? 10.447  1.898   29.179 1.00 64.04  ?  126 MET   B SD  1 
ATOM   3050 C  CE  . MET   B 1 119 ? 8.967   1.007   29.666 1.00 69.75  ?  126 MET   B CE  1 
ATOM   3051 N  N   . ALA   B 1 120 ? 12.488  0.472   34.251 1.00 67.84  ?  127 ALA   B N   1 
ATOM   3052 C  CA  . ALA   B 1 120 ? 12.433  0.077   35.665 1.00 65.90  ?  127 ALA   B CA  1 
ATOM   3053 C  C   . ALA   B 1 120 ? 11.918  1.185   36.587 1.00 64.06  ?  127 ALA   B C   1 
ATOM   3054 O  O   . ALA   B 1 120 ? 11.178  0.899   37.535 1.00 68.10  ?  127 ALA   B O   1 
ATOM   3055 C  CB  . ALA   B 1 120 ? 13.809  -0.397  36.148 1.00 65.89  ?  127 ALA   B CB  1 
ATOM   3056 N  N   . TYR   B 1 121 ? 12.322  2.432   36.323 1.00 63.14  ?  128 TYR   B N   1 
ATOM   3057 C  CA  . TYR   B 1 121 ? 11.817  3.594   37.070 1.00 60.71  ?  128 TYR   B CA  1 
ATOM   3058 C  C   . TYR   B 1 121 ? 10.298  3.697   36.925 1.00 64.21  ?  128 TYR   B C   1 
ATOM   3059 O  O   . TYR   B 1 121 ? 9.589   3.738   37.925 1.00 71.27  ?  128 TYR   B O   1 
ATOM   3060 C  CB  . TYR   B 1 121 ? 12.470  4.920   36.614 1.00 60.68  ?  128 TYR   B CB  1 
ATOM   3061 C  CG  . TYR   B 1 121 ? 11.821  6.101   37.305 1.00 58.36  ?  128 TYR   B CG  1 
ATOM   3062 C  CD1 . TYR   B 1 121 ? 12.117  6.391   38.632 1.00 57.80  ?  128 TYR   B CD1 1 
ATOM   3063 C  CD2 . TYR   B 1 121 ? 10.854  6.883   36.657 1.00 61.00  ?  128 TYR   B CD2 1 
ATOM   3064 C  CE1 . TYR   B 1 121 ? 11.499  7.452   39.290 1.00 62.73  ?  128 TYR   B CE1 1 
ATOM   3065 C  CE2 . TYR   B 1 121 ? 10.210  7.931   37.314 1.00 62.65  ?  128 TYR   B CE2 1 
ATOM   3066 C  CZ  . TYR   B 1 121 ? 10.542  8.221   38.624 1.00 62.01  ?  128 TYR   B CZ  1 
ATOM   3067 O  OH  . TYR   B 1 121 ? 9.927   9.266   39.265 1.00 71.16  ?  128 TYR   B OH  1 
ATOM   3068 N  N   . LEU   B 1 122 ? 9.840   3.733   35.671 1.00 69.30  ?  129 LEU   B N   1 
ATOM   3069 C  CA  . LEU   B 1 122 ? 8.415   3.854   35.324 1.00 67.79  ?  129 LEU   B CA  1 
ATOM   3070 C  C   . LEU   B 1 122 ? 7.549   2.722   35.865 1.00 65.64  ?  129 LEU   B C   1 
ATOM   3071 O  O   . LEU   B 1 122 ? 6.504   2.983   36.444 1.00 78.91  ?  129 LEU   B O   1 
ATOM   3072 C  CB  . LEU   B 1 122 ? 8.235   3.966   33.798 1.00 72.25  ?  129 LEU   B CB  1 
ATOM   3073 C  CG  . LEU   B 1 122 ? 8.794   5.216   33.105 1.00 64.81  ?  129 LEU   B CG  1 
ATOM   3074 C  CD1 . LEU   B 1 122 ? 8.761   5.034   31.593 1.00 59.67  ?  129 LEU   B CD1 1 
ATOM   3075 C  CD2 . LEU   B 1 122 ? 8.037   6.472   33.528 1.00 71.01  ?  129 LEU   B CD2 1 
ATOM   3076 N  N   . HIS   B 1 123 ? 8.006   1.485   35.714 1.00 71.66  ?  130 HIS   B N   1 
ATOM   3077 C  CA  . HIS   B 1 123 ? 7.315   0.305   36.281 1.00 71.86  ?  130 HIS   B CA  1 
ATOM   3078 C  C   . HIS   B 1 123 ? 7.303   0.290   37.815 1.00 77.72  ?  130 HIS   B C   1 
ATOM   3079 O  O   . HIS   B 1 123 ? 6.311   -0.147  38.422 1.00 84.24  ?  130 HIS   B O   1 
ATOM   3080 C  CB  . HIS   B 1 123 ? 7.916   -0.995  35.729 1.00 68.44  ?  130 HIS   B CB  1 
ATOM   3081 C  CG  . HIS   B 1 123 ? 7.573   -1.244  34.294 1.00 73.73  ?  130 HIS   B CG  1 
ATOM   3082 N  ND1 . HIS   B 1 123 ? 7.703   -2.479  33.701 1.00 70.91  ?  130 HIS   B ND1 1 
ATOM   3083 C  CD2 . HIS   B 1 123 ? 7.077   -0.421  33.338 1.00 77.70  ?  130 HIS   B CD2 1 
ATOM   3084 C  CE1 . HIS   B 1 123 ? 7.319   -2.399  32.438 1.00 77.58  ?  130 HIS   B CE1 1 
ATOM   3085 N  NE2 . HIS   B 1 123 ? 6.923   -1.164  32.195 1.00 77.73  ?  130 HIS   B NE2 1 
ATOM   3086 N  N   . GLY   B 1 124 ? 8.384   0.789   38.422 1.00 77.08  ?  131 GLY   B N   1 
ATOM   3087 C  CA  . GLY   B 1 124 ? 8.468   1.015   39.865 1.00 77.34  ?  131 GLY   B CA  1 
ATOM   3088 C  C   . GLY   B 1 124 ? 7.466   2.007   40.443 1.00 80.27  ?  131 GLY   B C   1 
ATOM   3089 O  O   . GLY   B 1 124 ? 7.081   1.865   41.597 1.00 87.06  ?  131 GLY   B O   1 
ATOM   3090 N  N   . LYS   B 1 125 ? 7.063   3.002   39.644 1.00 81.27  ?  132 LYS   B N   1 
ATOM   3091 C  CA  . LYS   B 1 125 ? 5.995   3.961   39.989 1.00 81.57  ?  132 LYS   B CA  1 
ATOM   3092 C  C   . LYS   B 1 125 ? 4.612   3.560   39.405 1.00 87.45  ?  132 LYS   B C   1 
ATOM   3093 O  O   . LYS   B 1 125 ? 3.726   4.413   39.280 1.00 93.90  ?  132 LYS   B O   1 
ATOM   3094 C  CB  . LYS   B 1 125 ? 6.382   5.384   39.523 1.00 79.69  ?  132 LYS   B CB  1 
ATOM   3095 C  CG  . LYS   B 1 125 ? 7.766   5.882   39.943 1.00 74.63  ?  132 LYS   B CG  1 
ATOM   3096 C  CD  . LYS   B 1 125 ? 7.866   6.249   41.412 1.00 76.26  ?  132 LYS   B CD  1 
ATOM   3097 C  CE  . LYS   B 1 125 ? 7.481   7.700   41.664 1.00 83.75  ?  132 LYS   B CE  1 
ATOM   3098 N  NZ  . LYS   B 1 125 ? 7.707   8.146   43.032 0.00 82.46  ?  132 LYS   B NZ  1 
ATOM   3099 N  N   . GLY   B 1 126 ? 4.413   2.282   39.063 1.00 89.13  ?  133 GLY   B N   1 
ATOM   3100 C  CA  . GLY   B 1 126 ? 3.148   1.791   38.511 1.00 94.00  ?  133 GLY   B CA  1 
ATOM   3101 C  C   . GLY   B 1 126 ? 2.755   2.191   37.095 1.00 91.60  ?  133 GLY   B C   1 
ATOM   3102 O  O   . GLY   B 1 126 ? 1.650   1.875   36.678 1.00 99.42  ?  133 GLY   B O   1 
ATOM   3103 N  N   . VAL   B 1 127 ? 3.649   2.836   36.339 1.00 94.93  ?  134 VAL   B N   1 
ATOM   3104 C  CA  . VAL   B 1 127 ? 3.367   3.325   34.972 1.00 96.23  ?  134 VAL   B CA  1 
ATOM   3105 C  C   . VAL   B 1 127 ? 3.711   2.239   33.950 1.00 87.71  ?  134 VAL   B C   1 
ATOM   3106 O  O   . VAL   B 1 127 ? 4.841   1.777   33.920 1.00 100.98 ?  134 VAL   B O   1 
ATOM   3107 C  CB  . VAL   B 1 127 ? 4.195   4.603   34.619 1.00 91.50  ?  134 VAL   B CB  1 
ATOM   3108 C  CG1 . VAL   B 1 127 ? 3.861   5.110   33.216 1.00 92.84  ?  134 VAL   B CG1 1 
ATOM   3109 C  CG2 . VAL   B 1 127 ? 3.964   5.712   35.640 1.00 96.14  ?  134 VAL   B CG2 1 
ATOM   3110 N  N   . ILE   B 1 128 ? 2.738   1.846   33.127 1.00 90.14  ?  135 ILE   B N   1 
ATOM   3111 C  CA  . ILE   B 1 128 ? 2.980   1.058   31.913 1.00 84.66  ?  135 ILE   B CA  1 
ATOM   3112 C  C   . ILE   B 1 128 ? 3.084   2.088   30.791 1.00 84.13  ?  135 ILE   B C   1 
ATOM   3113 O  O   . ILE   B 1 128 ? 2.186   2.920   30.639 1.00 86.16  ?  135 ILE   B O   1 
ATOM   3114 C  CB  . ILE   B 1 128 ? 1.822   0.064   31.624 1.00 97.96  ?  135 ILE   B CB  1 
ATOM   3115 C  CG1 . ILE   B 1 128 ? 1.568   -0.849  32.848 1.00 104.74 ?  135 ILE   B CG1 1 
ATOM   3116 C  CG2 . ILE   B 1 128 ? 2.086   -0.778  30.367 1.00 94.95  ?  135 ILE   B CG2 1 
ATOM   3117 C  CD1 . ILE   B 1 128 ? 0.374   -0.457  33.698 1.00 117.16 ?  135 ILE   B CD1 1 
ATOM   3118 N  N   . HIS   B 1 129 ? 4.156   2.019   29.997 1.00 78.43  ?  136 HIS   B N   1 
ATOM   3119 C  CA  . HIS   B 1 129 ? 4.364   2.953   28.873 1.00 78.09  ?  136 HIS   B CA  1 
ATOM   3120 C  C   . HIS   B 1 129 ? 3.289   2.778   27.809 1.00 81.62  ?  136 HIS   B C   1 
ATOM   3121 O  O   . HIS   B 1 129 ? 2.707   3.765   27.355 1.00 80.82  ?  136 HIS   B O   1 
ATOM   3122 C  CB  . HIS   B 1 129 ? 5.735   2.746   28.210 1.00 71.24  ?  136 HIS   B CB  1 
ATOM   3123 C  CG  . HIS   B 1 129 ? 6.230   3.936   27.439 1.00 69.75  ?  136 HIS   B CG  1 
ATOM   3124 N  ND1 . HIS   B 1 129 ? 5.549   4.506   26.381 1.00 72.46  ?  136 HIS   B ND1 1 
ATOM   3125 C  CD2 . HIS   B 1 129 ? 7.369   4.656   27.574 1.00 70.17  ?  136 HIS   B CD2 1 
ATOM   3126 C  CE1 . HIS   B 1 129 ? 6.232   5.535   25.918 1.00 65.75  ?  136 HIS   B CE1 1 
ATOM   3127 N  NE2 . HIS   B 1 129 ? 7.345   5.643   26.618 1.00 65.17  ?  136 HIS   B NE2 1 
ATOM   3128 N  N   . LYS   B 1 130 ? 3.073   1.514   27.410 1.00 72.14  ?  137 LYS   B N   1 
ATOM   3129 C  CA  . LYS   B 1 130 ? 2.097   1.093   26.386 1.00 81.42  ?  137 LYS   B CA  1 
ATOM   3130 C  C   . LYS   B 1 130 ? 2.511   1.362   24.925 1.00 79.30  ?  137 LYS   B C   1 
ATOM   3131 O  O   . LYS   B 1 130 ? 1.802   0.935   24.012 1.00 84.61  ?  137 LYS   B O   1 
ATOM   3132 C  CB  . LYS   B 1 130 ? 0.673   1.658   26.639 1.00 84.42  ?  137 LYS   B CB  1 
ATOM   3133 C  CG  . LYS   B 1 130 ? 0.126   1.527   28.064 1.00 88.31  ?  137 LYS   B CG  1 
ATOM   3134 C  CD  . LYS   B 1 130 ? -0.949  2.571   28.355 1.00 96.40  ?  137 LYS   B CD  1 
ATOM   3135 C  CE  . LYS   B 1 130 ? -1.480  2.472   29.778 1.00 102.69 ?  137 LYS   B CE  1 
ATOM   3136 N  NZ  . LYS   B 1 130 ? -2.522  3.439   30.109 0.00 104.10 ?  137 LYS   B NZ  1 
ATOM   3137 N  N   . ASP   B 1 131 ? 3.650   2.027   24.697 1.00 82.38  ?  138 ASP   B N   1 
ATOM   3138 C  CA  . ASP   B 1 131 ? 4.075   2.505   23.366 1.00 76.74  ?  138 ASP   B CA  1 
ATOM   3139 C  C   . ASP   B 1 131 ? 5.605   2.751   23.302 1.00 66.48  ?  138 ASP   B C   1 
ATOM   3140 O  O   . ASP   B 1 131 ? 6.078   3.750   22.767 1.00 62.97  ?  138 ASP   B O   1 
ATOM   3141 C  CB  . ASP   B 1 131 ? 3.275   3.761   22.956 1.00 79.06  ?  138 ASP   B CB  1 
ATOM   3142 C  CG  . ASP   B 1 131 ? 3.313   4.044   21.440 1.00 78.24  ?  138 ASP   B CG  1 
ATOM   3143 O  OD1 . ASP   B 1 131 ? 3.787   3.213   20.627 1.00 83.05  ?  138 ASP   B OD1 1 
ATOM   3144 O  OD2 . ASP   B 1 131 ? 2.843   5.134   21.053 1.00 81.99  ?  138 ASP   B OD2 1 
ATOM   3145 N  N   . LEU   B 1 132 ? 6.383   1.806   23.838 1.00 76.81  ?  139 LEU   B N   1 
ATOM   3146 C  CA  . LEU   B 1 132 ? 7.853   1.896   23.803 1.00 65.65  ?  139 LEU   B CA  1 
ATOM   3147 C  C   . LEU   B 1 132 ? 8.284   1.600   22.363 1.00 64.93  ?  139 LEU   B C   1 
ATOM   3148 O  O   . LEU   B 1 132 ? 7.825   0.633   21.744 1.00 60.57  ?  139 LEU   B O   1 
ATOM   3149 C  CB  . LEU   B 1 132 ? 8.498   0.963   24.829 1.00 68.12  ?  139 LEU   B CB  1 
ATOM   3150 C  CG  . LEU   B 1 132 ? 10.026  0.818   24.896 1.00 72.33  ?  139 LEU   B CG  1 
ATOM   3151 C  CD1 . LEU   B 1 132 ? 10.706  2.125   25.256 1.00 69.89  ?  139 LEU   B CD1 1 
ATOM   3152 C  CD2 . LEU   B 1 132 ? 10.397  -0.252  25.904 1.00 74.75  ?  139 LEU   B CD2 1 
ATOM   3153 N  N   . LYS   B 1 133 ? 9.099   2.497   21.816 1.00 62.30  ?  140 LYS   B N   1 
ATOM   3154 C  CA  . LYS   B 1 133 ? 9.563   2.414   20.433 1.00 57.74  ?  140 LYS   B CA  1 
ATOM   3155 C  C   . LYS   B 1 133 ? 10.734  3.395   20.244 1.00 60.83  ?  140 LYS   B C   1 
ATOM   3156 O  O   . LYS   B 1 133 ? 10.831  4.381   21.000 1.00 67.37  ?  140 LYS   B O   1 
ATOM   3157 C  CB  . LYS   B 1 133 ? 8.421   2.735   19.443 1.00 59.56  ?  140 LYS   B CB  1 
ATOM   3158 C  CG  . LYS   B 1 133 ? 7.871   4.161   19.537 1.00 61.31  ?  140 LYS   B CG  1 
ATOM   3159 C  CD  . LYS   B 1 133 ? 6.520   4.372   18.853 1.00 63.54  ?  140 LYS   B CD  1 
ATOM   3160 C  CE  . LYS   B 1 133 ? 5.822   5.581   19.487 1.00 68.24  ?  140 LYS   B CE  1 
ATOM   3161 N  NZ  . LYS   B 1 133 ? 4.558   6.059   18.861 1.00 70.57  ?  140 LYS   B NZ  1 
ATOM   3162 N  N   . PRO   B 1 134 ? 11.596  3.171   19.219 1.00 58.11  ?  141 PRO   B N   1 
ATOM   3163 C  CA  . PRO   B 1 134 ? 12.718  4.079   18.955 1.00 56.48  ?  141 PRO   B CA  1 
ATOM   3164 C  C   . PRO   B 1 134 ? 12.358  5.575   18.899 1.00 54.62  ?  141 PRO   B C   1 
ATOM   3165 O  O   . PRO   B 1 134 ? 13.100  6.374   19.446 1.00 61.98  ?  141 PRO   B O   1 
ATOM   3166 C  CB  . PRO   B 1 134 ? 13.260  3.577   17.609 1.00 62.06  ?  141 PRO   B CB  1 
ATOM   3167 C  CG  . PRO   B 1 134 ? 12.943  2.122   17.612 1.00 64.45  ?  141 PRO   B CG  1 
ATOM   3168 C  CD  . PRO   B 1 134 ? 11.607  2.036   18.273 1.00 61.75  ?  141 PRO   B CD  1 
ATOM   3169 N  N   . GLU   B 1 135 ? 11.221  5.927   18.292 1.00 55.93  ?  142 GLU   B N   1 
ATOM   3170 C  CA  . GLU   B 1 135 ? 10.693  7.325   18.279 1.00 60.07  ?  142 GLU   B CA  1 
ATOM   3171 C  C   . GLU   B 1 135 ? 10.521  7.982   19.659 1.00 63.30  ?  142 GLU   B C   1 
ATOM   3172 O  O   . GLU   B 1 135 ? 10.670  9.192   19.779 1.00 80.47  ?  142 GLU   B O   1 
ATOM   3173 C  CB  . GLU   B 1 135 ? 9.363   7.426   17.511 1.00 60.71  ?  142 GLU   B CB  1 
ATOM   3174 C  CG  . GLU   B 1 135 ? 9.510   7.612   16.000 1.00 68.78  ?  142 GLU   B CG  1 
ATOM   3175 C  CD  . GLU   B 1 135 ? 8.248   8.117   15.336 0.00 66.78  ?  142 GLU   B CD  1 
ATOM   3176 O  OE1 . GLU   B 1 135 ? 7.763   7.397   14.443 0.00 67.42  ?  142 GLU   B OE1 1 
ATOM   3177 O  OE2 . GLU   B 1 135 ? 7.725   9.197   15.689 0.00 67.75  ?  142 GLU   B OE2 1 
ATOM   3178 N  N   . ASN   B 1 136 ? 10.233  7.167   20.675 1.00 70.49  ?  143 ASN   B N   1 
ATOM   3179 C  CA  . ASN   B 1 136 ? 10.113  7.609   22.084 1.00 66.22  ?  143 ASN   B CA  1 
ATOM   3180 C  C   . ASN   B 1 136 ? 11.422  7.535   22.912 1.00 66.56  ?  143 ASN   B C   1 
ATOM   3181 O  O   . ASN   B 1 136 ? 11.382  7.740   24.111 1.00 61.58  ?  143 ASN   B O   1 
ATOM   3182 C  CB  . ASN   B 1 136 ? 8.995   6.796   22.777 1.00 69.34  ?  143 ASN   B CB  1 
ATOM   3183 C  CG  . ASN   B 1 136 ? 7.609   7.411   22.608 1.00 64.73  ?  143 ASN   B CG  1 
ATOM   3184 O  OD1 . ASN   B 1 136 ? 7.456   8.621   22.544 1.00 59.15  ?  143 ASN   B OD1 1 
ATOM   3185 N  ND2 . ASN   B 1 136 ? 6.588   6.574   22.628 1.00 59.27  ?  143 ASN   B ND2 1 
ATOM   3186 N  N   . ILE   B 1 137 ? 12.565  7.275   22.275 1.00 69.17  ?  144 ILE   B N   1 
ATOM   3187 C  CA  . ILE   B 1 137 ? 13.867  7.230   22.939 1.00 57.41  ?  144 ILE   B CA  1 
ATOM   3188 C  C   . ILE   B 1 137 ? 14.633  8.368   22.309 1.00 56.32  ?  144 ILE   B C   1 
ATOM   3189 O  O   . ILE   B 1 137 ? 14.976  8.309   21.146 1.00 61.03  ?  144 ILE   B O   1 
ATOM   3190 C  CB  . ILE   B 1 137 ? 14.564  5.862   22.755 1.00 55.82  ?  144 ILE   B CB  1 
ATOM   3191 C  CG1 . ILE   B 1 137 ? 13.757  4.775   23.491 1.00 55.02  ?  144 ILE   B CG1 1 
ATOM   3192 C  CG2 . ILE   B 1 137 ? 16.005  5.886   23.283 1.00 49.69  ?  144 ILE   B CG2 1 
ATOM   3193 C  CD1 . ILE   B 1 137 ? 14.082  3.374   23.047 1.00 56.15  ?  144 ILE   B CD1 1 
ATOM   3194 N  N   . LEU   B 1 138 ? 14.873  9.400   23.095 1.00 61.73  ?  145 LEU   B N   1 
ATOM   3195 C  CA  . LEU   B 1 138 ? 15.537  10.608  22.640 1.00 61.30  ?  145 LEU   B CA  1 
ATOM   3196 C  C   . LEU   B 1 138 ? 16.967  10.558  23.139 1.00 59.15  ?  145 LEU   B C   1 
ATOM   3197 O  O   . LEU   B 1 138 ? 17.211  9.988   24.181 1.00 51.59  ?  145 LEU   B O   1 
ATOM   3198 C  CB  . LEU   B 1 138 ? 14.782  11.825  23.161 1.00 56.99  ?  145 LEU   B CB  1 
ATOM   3199 C  CG  . LEU   B 1 138 ? 13.264  11.849  22.855 1.00 59.62  ?  145 LEU   B CG  1 
ATOM   3200 C  CD1 . LEU   B 1 138 ? 12.672  13.203  23.195 1.00 57.73  ?  145 LEU   B CD1 1 
ATOM   3201 C  CD2 . LEU   B 1 138 ? 12.905  11.536  21.412 1.00 63.16  ?  145 LEU   B CD2 1 
ATOM   3202 N  N   . VAL   B 1 139 ? 17.879  11.198  22.402 1.00 57.96  ?  146 VAL   B N   1 
ATOM   3203 C  CA  . VAL   B 1 139 ? 19.322  11.066  22.577 1.00 53.39  ?  146 VAL   B CA  1 
ATOM   3204 C  C   . VAL   B 1 139 ? 19.922  12.467  22.676 1.00 57.45  ?  146 VAL   B C   1 
ATOM   3205 O  O   . VAL   B 1 139 ? 19.637  13.300  21.808 1.00 58.65  ?  146 VAL   B O   1 
ATOM   3206 C  CB  . VAL   B 1 139 ? 19.946  10.329  21.366 1.00 57.89  ?  146 VAL   B CB  1 
ATOM   3207 C  CG1 . VAL   B 1 139 ? 21.427  10.043  21.604 1.00 60.30  ?  146 VAL   B CG1 1 
ATOM   3208 C  CG2 . VAL   B 1 139 ? 19.199  9.027   21.033 1.00 54.95  ?  146 VAL   B CG2 1 
ATOM   3209 N  N   . ASP   B 1 140 ? 20.736  12.718  23.718 1.00 62.98  ?  147 ASP   B N   1 
ATOM   3210 C  CA  . ASP   B 1 140 ? 21.528  13.968  23.845 1.00 60.66  ?  147 ASP   B CA  1 
ATOM   3211 C  C   . ASP   B 1 140 ? 22.875  13.875  23.098 1.00 66.57  ?  147 ASP   B C   1 
ATOM   3212 O  O   . ASP   B 1 140 ? 23.216  12.803  22.591 1.00 68.39  ?  147 ASP   B O   1 
ATOM   3213 C  CB  . ASP   B 1 140 ? 21.654  14.432  25.324 1.00 57.54  ?  147 ASP   B CB  1 
ATOM   3214 C  CG  . ASP   B 1 140 ? 22.551  13.553  26.205 1.00 60.42  ?  147 ASP   B CG  1 
ATOM   3215 O  OD1 . ASP   B 1 140 ? 23.564  12.988  25.754 1.00 74.33  ?  147 ASP   B OD1 1 
ATOM   3216 O  OD2 . ASP   B 1 140 ? 22.269  13.474  27.424 1.00 59.75  ?  147 ASP   B OD2 1 
ATOM   3217 N  N   . ASN   B 1 141 ? 23.624  14.989  23.050 1.00 75.34  ?  148 ASN   B N   1 
ATOM   3218 C  CA  . ASN   B 1 141 ? 24.915  15.058  22.313 1.00 73.57  ?  148 ASN   B CA  1 
ATOM   3219 C  C   . ASN   B 1 141 ? 26.045  14.133  22.815 1.00 72.14  ?  148 ASN   B C   1 
ATOM   3220 O  O   . ASN   B 1 141 ? 26.925  13.752  22.027 1.00 68.53  ?  148 ASN   B O   1 
ATOM   3221 C  CB  . ASN   B 1 141 ? 25.433  16.505  22.168 1.00 83.54  ?  148 ASN   B CB  1 
ATOM   3222 C  CG  . ASN   B 1 141 ? 25.276  17.045  20.746 1.00 95.28  ?  148 ASN   B CG  1 
ATOM   3223 O  OD1 . ASN   B 1 141 ? 25.709  16.398  19.785 1.00 98.90  ?  148 ASN   B OD1 1 
ATOM   3224 N  ND2 . ASN   B 1 141 ? 24.677  18.237  20.601 1.00 103.03 ?  148 ASN   B ND2 1 
ATOM   3225 N  N   . ASP   B 1 142 ? 25.985  13.741  24.092 1.00 71.01  ?  149 ASP   B N   1 
ATOM   3226 C  CA  . ASP   B 1 142 ? 26.860  12.695  24.680 1.00 74.18  ?  149 ASP   B CA  1 
ATOM   3227 C  C   . ASP   B 1 142 ? 26.330  11.240  24.519 1.00 67.68  ?  149 ASP   B C   1 
ATOM   3228 O  O   . ASP   B 1 142 ? 26.838  10.334  25.176 1.00 73.32  ?  149 ASP   B O   1 
ATOM   3229 C  CB  . ASP   B 1 142 ? 27.100  13.001  26.177 1.00 82.00  ?  149 ASP   B CB  1 
ATOM   3230 C  CG  . ASP   B 1 142 ? 27.898  14.282  26.406 1.00 99.28  ?  149 ASP   B CG  1 
ATOM   3231 O  OD1 . ASP   B 1 142 ? 28.979  14.437  25.791 1.00 106.02 ?  149 ASP   B OD1 1 
ATOM   3232 O  OD2 . ASP   B 1 142 ? 27.463  15.120  27.237 1.00 99.10  ?  149 ASP   B OD2 1 
ATOM   3233 N  N   . PHE   B 1 143 ? 25.323  11.021  23.660 1.00 62.70  ?  150 PHE   B N   1 
ATOM   3234 C  CA  . PHE   B 1 143 ? 24.663  9.720   23.446 1.00 69.04  ?  150 PHE   B CA  1 
ATOM   3235 C  C   . PHE   B 1 143 ? 23.903  9.114   24.634 1.00 67.67  ?  150 PHE   B C   1 
ATOM   3236 O  O   . PHE   B 1 143 ? 23.504  7.941   24.565 1.00 73.95  ?  150 PHE   B O   1 
ATOM   3237 C  CB  . PHE   B 1 143 ? 25.631  8.700   22.803 1.00 70.54  ?  150 PHE   B CB  1 
ATOM   3238 C  CG  . PHE   B 1 143 ? 26.011  9.050   21.406 1.00 70.23  ?  150 PHE   B CG  1 
ATOM   3239 C  CD1 . PHE   B 1 143 ? 25.233  8.613   20.327 1.00 68.44  ?  150 PHE   B CD1 1 
ATOM   3240 C  CD2 . PHE   B 1 143 ? 27.141  9.833   21.151 1.00 83.57  ?  150 PHE   B CD2 1 
ATOM   3241 C  CE1 . PHE   B 1 143 ? 25.585  8.945   19.021 1.00 81.68  ?  150 PHE   B CE1 1 
ATOM   3242 C  CE2 . PHE   B 1 143 ? 27.505  10.157  19.842 1.00 87.53  ?  150 PHE   B CE2 1 
ATOM   3243 C  CZ  . PHE   B 1 143 ? 26.722  9.717   18.775 1.00 84.47  ?  150 PHE   B CZ  1 
ATOM   3244 N  N   . HIS   B 1 144 ? 23.643  9.904   25.685 1.00 68.26  ?  151 HIS   B N   1 
ATOM   3245 C  CA  . HIS   B 1 144 ? 22.807  9.447   26.784 1.00 64.09  ?  151 HIS   B CA  1 
ATOM   3246 C  C   . HIS   B 1 144 ? 21.359  9.631   26.333 1.00 66.68  ?  151 HIS   B C   1 
ATOM   3247 O  O   . HIS   B 1 144 ? 21.039  10.604  25.627 1.00 66.38  ?  151 HIS   B O   1 
ATOM   3248 C  CB  . HIS   B 1 144 ? 23.090  10.211  28.071 1.00 67.17  ?  151 HIS   B CB  1 
ATOM   3249 C  CG  . HIS   B 1 144 ? 24.478  10.032  28.596 1.00 68.52  ?  151 HIS   B CG  1 
ATOM   3250 N  ND1 . HIS   B 1 144 ? 24.917  8.848   29.150 1.00 65.49  ?  151 HIS   B ND1 1 
ATOM   3251 C  CD2 . HIS   B 1 144 ? 25.508  10.903  28.710 1.00 74.63  ?  151 HIS   B CD2 1 
ATOM   3252 C  CE1 . HIS   B 1 144 ? 26.166  8.989   29.555 1.00 64.01  ?  151 HIS   B CE1 1 
ATOM   3253 N  NE2 . HIS   B 1 144 ? 26.550  10.225  29.296 1.00 79.53  ?  151 HIS   B NE2 1 
ATOM   3254 N  N   . ILE   B 1 145 ? 20.515  8.673   26.712 1.00 59.32  ?  152 ILE   B N   1 
ATOM   3255 C  CA  . ILE   B 1 145 ? 19.111  8.630   26.287 1.00 60.10  ?  152 ILE   B CA  1 
ATOM   3256 C  C   . ILE   B 1 145 ? 18.111  9.002   27.379 1.00 55.49  ?  152 ILE   B C   1 
ATOM   3257 O  O   . ILE   B 1 145 ? 18.406  8.904   28.566 1.00 54.95  ?  152 ILE   B O   1 
ATOM   3258 C  CB  . ILE   B 1 145 ? 18.711  7.261   25.663 1.00 60.62  ?  152 ILE   B CB  1 
ATOM   3259 C  CG1 . ILE   B 1 145 ? 18.713  6.099   26.694 1.00 57.89  ?  152 ILE   B CG1 1 
ATOM   3260 C  CG2 . ILE   B 1 145 ? 19.629  6.953   24.491 1.00 57.27  ?  152 ILE   B CG2 1 
ATOM   3261 C  CD1 . ILE   B 1 145 ? 17.359  5.769   27.287 1.00 56.06  ?  152 ILE   B CD1 1 
ATOM   3262 N  N   . LYS   B 1 146 ? 16.928  9.427   26.942 1.00 55.57  ?  153 LYS   B N   1 
ATOM   3263 C  CA  . LYS   B 1 146 ? 15.769  9.613   27.814 1.00 54.32  ?  153 LYS   B CA  1 
ATOM   3264 C  C   . LYS   B 1 146 ? 14.506  9.111   27.121 1.00 56.65  ?  153 LYS   B C   1 
ATOM   3265 O  O   . LYS   B 1 146 ? 14.262  9.440   25.961 1.00 59.01  ?  153 LYS   B O   1 
ATOM   3266 C  CB  . LYS   B 1 146 ? 15.582  11.076  28.188 1.00 55.22  ?  153 LYS   B CB  1 
ATOM   3267 C  CG  . LYS   B 1 146 ? 16.689  11.647  29.067 1.00 58.12  ?  153 LYS   B CG  1 
ATOM   3268 C  CD  . LYS   B 1 146 ? 16.410  13.116  29.358 1.00 52.81  ?  153 LYS   B CD  1 
ATOM   3269 C  CE  . LYS   B 1 146 ? 17.610  13.845  29.928 1.00 56.99  ?  153 LYS   B CE  1 
ATOM   3270 N  NZ  . LYS   B 1 146 ? 17.828  13.541  31.360 1.00 63.36  ?  153 LYS   B NZ  1 
ATOM   3271 N  N   . ILE   B 1 147 ? 13.710  8.326   27.848 1.00 56.57  ?  154 ILE   B N   1 
ATOM   3272 C  CA  . ILE   B 1 147 ? 12.420  7.839   27.366 1.00 55.22  ?  154 ILE   B CA  1 
ATOM   3273 C  C   . ILE   B 1 147 ? 11.377  8.953   27.457 1.00 53.53  ?  154 ILE   B C   1 
ATOM   3274 O  O   . ILE   B 1 147 ? 11.295  9.633   28.497 1.00 55.20  ?  154 ILE   B O   1 
ATOM   3275 C  CB  . ILE   B 1 147 ? 11.952  6.578   28.135 1.00 57.21  ?  154 ILE   B CB  1 
ATOM   3276 C  CG1 . ILE   B 1 147 ? 12.969  5.430   27.902 1.00 62.01  ?  154 ILE   B CG1 1 
ATOM   3277 C  CG2 . ILE   B 1 147 ? 10.556  6.136   27.681 1.00 59.94  ?  154 ILE   B CG2 1 
ATOM   3278 C  CD1 . ILE   B 1 147 ? 13.119  4.478   29.065 1.00 56.82  ?  154 ILE   B CD1 1 
ATOM   3279 N  N   . ALA   B 1 148 ? 10.582  9.097   26.384 1.00 85.07  ?  155 ALA   B N   1 
ATOM   3280 C  CA  . ALA   B 1 148 ? 9.443   10.023  26.295 1.00 82.27  ?  155 ALA   B CA  1 
ATOM   3281 C  C   . ALA   B 1 148 ? 8.149   9.245   26.030 1.00 81.00  ?  155 ALA   B C   1 
ATOM   3282 O  O   . ALA   B 1 148 ? 8.214   8.069   25.731 1.00 81.02  ?  155 ALA   B O   1 
ATOM   3283 C  CB  . ALA   B 1 148 ? 9.679   11.005  25.177 1.00 80.29  ?  155 ALA   B CB  1 
ATOM   3284 N  N   A ASP   B 1 149 ? 7.003   9.913   26.158 0.50 80.76  ?  156 ASP   B N   1 
ATOM   3285 N  N   B ASP   B 1 149 ? 7.005   9.919   26.162 0.50 81.30  ?  156 ASP   B N   1 
ATOM   3286 C  CA  A ASP   B 1 149 ? 5.681   9.356   25.820 0.50 80.87  ?  156 ASP   B CA  1 
ATOM   3287 C  CA  B ASP   B 1 149 ? 5.671   9.366   25.837 0.50 81.76  ?  156 ASP   B CA  1 
ATOM   3288 C  C   A ASP   B 1 149 ? 5.023   10.375  24.912 0.50 79.30  ?  156 ASP   B C   1 
ATOM   3289 C  C   B ASP   B 1 149 ? 5.003   10.346  24.903 0.50 79.72  ?  156 ASP   B C   1 
ATOM   3290 O  O   A ASP   B 1 149 ? 4.069   11.045  25.287 0.50 79.95  ?  156 ASP   B O   1 
ATOM   3291 O  O   B ASP   B 1 149 ? 3.991   10.939  25.255 0.50 80.27  ?  156 ASP   B O   1 
ATOM   3292 C  CB  A ASP   B 1 149 ? 4.853   9.115   27.081 0.50 82.36  ?  156 ASP   B CB  1 
ATOM   3293 C  CB  B ASP   B 1 149 ? 4.814   9.183   27.094 0.50 84.05  ?  156 ASP   B CB  1 
ATOM   3294 C  CG  A ASP   B 1 149 ? 3.479   8.501   26.791 0.50 84.13  ?  156 ASP   B CG  1 
ATOM   3295 C  CG  B ASP   B 1 149 ? 3.529   8.384   26.836 0.50 86.84  ?  156 ASP   B CG  1 
ATOM   3296 O  OD1 A ASP   B 1 149 ? 3.295   7.876   25.723 0.50 84.75  ?  156 ASP   B OD1 1 
ATOM   3297 O  OD1 B ASP   B 1 149 ? 2.984   8.471   25.714 0.50 88.18  ?  156 ASP   B OD1 1 
ATOM   3298 O  OD2 A ASP   B 1 149 ? 2.572   8.628   27.647 0.50 81.85  ?  156 ASP   B OD2 1 
ATOM   3299 O  OD2 B ASP   B 1 149 ? 3.050   7.678   27.758 0.50 86.22  ?  156 ASP   B OD2 1 
ATOM   3300 N  N   . LEU   B 1 150 ? 5.583   10.500  23.713 1.00 79.50  ?  157 LEU   B N   1 
ATOM   3301 C  CA  . LEU   B 1 150 ? 5.116   11.461  22.697 1.00 79.27  ?  157 LEU   B CA  1 
ATOM   3302 C  C   . LEU   B 1 150 ? 3.713   11.165  22.119 1.00 80.55  ?  157 LEU   B C   1 
ATOM   3303 O  O   . LEU   B 1 150 ? 3.049   12.083  21.635 1.00 79.40  ?  157 LEU   B O   1 
ATOM   3304 C  CB  . LEU   B 1 150 ? 6.142   11.572  21.564 1.00 76.18  ?  157 LEU   B CB  1 
ATOM   3305 C  CG  . LEU   B 1 150 ? 7.546   12.072  21.955 1.00 76.53  ?  157 LEU   B CG  1 
ATOM   3306 C  CD1 . LEU   B 1 150 ? 8.541   11.913  20.811 1.00 74.43  ?  157 LEU   B CD1 1 
ATOM   3307 C  CD2 . LEU   B 1 150 ? 7.517   13.517  22.417 1.00 76.44  ?  157 LEU   B CD2 1 
ATOM   3308 N  N   . GLY   B 1 151 ? 3.271   9.901   22.167 1.00 85.13  ?  158 GLY   B N   1 
ATOM   3309 C  CA  . GLY   B 1 151 ? 1.871   9.517   21.830 1.00 84.59  ?  158 GLY   B CA  1 
ATOM   3310 C  C   . GLY   B 1 151 ? 0.831   9.708   22.929 1.00 88.86  ?  158 GLY   B C   1 
ATOM   3311 O  O   . GLY   B 1 151 ? -0.353  9.419   22.720 1.00 94.11  ?  158 GLY   B O   1 
ATOM   3312 N  N   . LEU   B 1 152 ? 1.272   10.146  24.113 1.00 89.87  ?  159 LEU   B N   1 
ATOM   3313 C  CA  . LEU   B 1 152 ? 0.426   10.439  25.270 1.00 88.16  ?  159 LEU   B CA  1 
ATOM   3314 C  C   . LEU   B 1 152 ? -0.405  9.239   25.742 1.00 90.48  ?  159 LEU   B C   1 
ATOM   3315 O  O   . LEU   B 1 152 ? -1.543  9.399   26.195 1.00 94.65  ?  159 LEU   B O   1 
ATOM   3316 C  CB  . LEU   B 1 152 ? -0.435  11.692  24.995 1.00 87.01  ?  159 LEU   B CB  1 
ATOM   3317 C  CG  . LEU   B 1 152 ? 0.300   12.976  24.579 1.00 83.04  ?  159 LEU   B CG  1 
ATOM   3318 C  CD1 . LEU   B 1 152 ? -0.691  14.025  24.123 1.00 83.97  ?  159 LEU   B CD1 1 
ATOM   3319 C  CD2 . LEU   B 1 152 ? 1.141   13.532  25.712 1.00 81.50  ?  159 LEU   B CD2 1 
ATOM   3320 N  N   . ALA   B 1 153 ? 0.193   8.046   25.650 1.00 91.17  ?  160 ALA   B N   1 
ATOM   3321 C  CA  . ALA   B 1 153 ? -0.457  6.787   26.028 1.00 94.02  ?  160 ALA   B CA  1 
ATOM   3322 C  C   . ALA   B 1 153 ? -0.816  6.679   27.514 1.00 95.67  ?  160 ALA   B C   1 
ATOM   3323 O  O   . ALA   B 1 153 ? -1.833  6.057   27.852 1.00 98.54  ?  160 ALA   B O   1 
ATOM   3324 C  CB  . ALA   B 1 153 ? 0.409   5.604   25.605 1.00 94.14  ?  160 ALA   B CB  1 
ATOM   3325 N  N   . SER   B 1 154 ? -0.004  7.300   28.379 1.00 93.73  ?  161 SER   B N   1 
ATOM   3326 C  CA  . SER   B 1 154 ? -0.238  7.332   29.834 1.00 99.32  ?  161 SER   B CA  1 
ATOM   3327 C  C   . SER   B 1 154 ? -1.156  8.478   30.332 1.00 104.97 ?  161 SER   B C   1 
ATOM   3328 O  O   . SER   B 1 154 ? -1.450  8.543   31.535 1.00 110.57 ?  161 SER   B O   1 
ATOM   3329 C  CB  . SER   B 1 154 ? 1.103   7.406   30.580 1.00 105.01 ?  161 SER   B CB  1 
ATOM   3330 O  OG  . SER   B 1 154 ? 1.965   6.319   30.269 1.00 112.20 ?  161 SER   B OG  1 
ATOM   3331 N  N   . PHE   B 1 155 ? -1.620  9.355   29.424 1.00 104.23 ?  162 PHE   B N   1 
ATOM   3332 C  CA  . PHE   B 1 155 ? -2.283  10.635  29.765 1.00 100.40 ?  162 PHE   B CA  1 
ATOM   3333 C  C   . PHE   B 1 155 ? -3.508  10.849  28.874 1.00 101.04 ?  162 PHE   B C   1 
ATOM   3334 O  O   . PHE   B 1 155 ? -3.410  11.443  27.792 1.00 100.19 ?  162 PHE   B O   1 
ATOM   3335 C  CB  . PHE   B 1 155 ? -1.243  11.762  29.656 1.00 98.22  ?  162 PHE   B CB  1 
ATOM   3336 C  CG  . PHE   B 1 155 ? -0.025  11.511  30.499 1.00 95.33  ?  162 PHE   B CG  1 
ATOM   3337 C  CD1 . PHE   B 1 155 ? -0.132  11.488  31.892 1.00 95.78  ?  162 PHE   B CD1 1 
ATOM   3338 C  CD2 . PHE   B 1 155 ? 1.207   11.197  29.919 1.00 95.83  ?  162 PHE   B CD2 1 
ATOM   3339 C  CE1 . PHE   B 1 155 ? 0.965   11.212  32.695 1.00 96.11  ?  162 PHE   B CE1 1 
ATOM   3340 C  CE2 . PHE   B 1 155 ? 2.318   10.935  30.720 1.00 95.21  ?  162 PHE   B CE2 1 
ATOM   3341 C  CZ  . PHE   B 1 155 ? 2.192   10.935  32.113 1.00 94.53  ?  162 PHE   B CZ  1 
ATOM   3342 N  N   . LYS   B 1 156 ? -4.654  10.352  29.356 1.00 110.72 ?  163 LYS   B N   1 
ATOM   3343 C  CA  . LYS   B 1 156 ? -5.893  10.243  28.563 1.00 115.08 ?  163 LYS   B CA  1 
ATOM   3344 C  C   . LYS   B 1 156 ? -6.521  11.570  28.145 1.00 115.04 ?  163 LYS   B C   1 
ATOM   3345 O  O   . LYS   B 1 156 ? -6.999  11.693  27.012 1.00 119.18 ?  163 LYS   B O   1 
ATOM   3346 C  CB  . LYS   B 1 156 ? -6.948  9.389   29.290 1.00 126.13 ?  163 LYS   B CB  1 
ATOM   3347 C  CG  . LYS   B 1 156 ? -6.622  7.903   29.371 1.00 134.98 ?  163 LYS   B CG  1 
ATOM   3348 C  CD  . LYS   B 1 156 ? -6.632  7.201   28.006 1.00 135.70 ?  163 LYS   B CD  1 
ATOM   3349 C  CE  . LYS   B 1 156 ? -5.229  6.992   27.433 1.00 134.12 ?  163 LYS   B CE  1 
ATOM   3350 N  NZ  . LYS   B 1 156 ? -5.210  6.943   25.945 1.00 130.66 ?  163 LYS   B NZ  1 
ATOM   3351 N  N   . MET   B 1 157 ? -6.532  12.534  29.059 1.00 112.35 ?  164 MET   B N   1 
ATOM   3352 C  CA  . MET   B 1 157 ? -7.144  13.853  28.817 1.00 110.61 ?  164 MET   B CA  1 
ATOM   3353 C  C   . MET   B 1 157 ? -6.399  14.691  27.781 1.00 107.46 ?  164 MET   B C   1 
ATOM   3354 O  O   . MET   B 1 157 ? -7.032  15.310  26.915 1.00 114.88 ?  164 MET   B O   1 
ATOM   3355 C  CB  . MET   B 1 157 ? -7.301  14.630  30.134 1.00 113.07 ?  164 MET   B CB  1 
ATOM   3356 C  CG  . MET   B 1 157 ? -8.181  13.947  31.178 1.00 119.97 ?  164 MET   B CG  1 
ATOM   3357 S  SD  . MET   B 1 157 ? -9.878  13.625  30.651 1.00 122.44 ?  164 MET   B SD  1 
ATOM   3358 C  CE  . MET   B 1 157 ? -9.771  11.923  30.088 1.00 122.64 ?  164 MET   B CE  1 
ATOM   3359 N  N   . TRP   B 1 158 ? -5.072  14.708  27.867 1.00 100.13 ?  165 TRP   B N   1 
ATOM   3360 C  CA  . TRP   B 1 158 ? -4.231  15.320  26.820 1.00 98.59  ?  165 TRP   B CA  1 
ATOM   3361 C  C   . TRP   B 1 158 ? -4.285  14.570  25.472 1.00 101.82 ?  165 TRP   B C   1 
ATOM   3362 O  O   . TRP   B 1 158 ? -4.213  15.212  24.420 1.00 103.09 ?  165 TRP   B O   1 
ATOM   3363 C  CB  . TRP   B 1 158 ? -2.784  15.474  27.290 1.00 94.36  ?  165 TRP   B CB  1 
ATOM   3364 C  CG  . TRP   B 1 158 ? -2.577  16.588  28.274 1.00 92.47  ?  165 TRP   B CG  1 
ATOM   3365 C  CD1 . TRP   B 1 158 ? -2.744  16.538  29.631 1.00 93.20  ?  165 TRP   B CD1 1 
ATOM   3366 C  CD2 . TRP   B 1 158 ? -2.125  17.918  27.977 1.00 90.07  ?  165 TRP   B CD2 1 
ATOM   3367 N  NE1 . TRP   B 1 158 ? -2.441  17.758  30.194 1.00 93.67  ?  165 TRP   B NE1 1 
ATOM   3368 C  CE2 . TRP   B 1 158 ? -2.054  18.623  29.205 1.00 89.93  ?  165 TRP   B CE2 1 
ATOM   3369 C  CE3 . TRP   B 1 158 ? -1.782  18.586  26.790 1.00 90.37  ?  165 TRP   B CE3 1 
ATOM   3370 C  CZ2 . TRP   B 1 158 ? -1.649  19.974  29.283 1.00 91.43  ?  165 TRP   B CZ2 1 
ATOM   3371 C  CZ3 . TRP   B 1 158 ? -1.369  19.943  26.863 1.00 90.39  ?  165 TRP   B CZ3 1 
ATOM   3372 C  CH2 . TRP   B 1 158 ? -1.307  20.614  28.107 1.00 90.62  ?  165 TRP   B CH2 1 
ATOM   3373 N  N   . SER   B 1 159 ? -4.415  13.237  25.499 1.00 106.02 ?  166 SER   B N   1 
ATOM   3374 C  CA  . SER   B 1 159 ? -4.543  12.447  24.256 1.00 110.88 ?  166 SER   B CA  1 
ATOM   3375 C  C   . SER   B 1 159 ? -5.906  12.649  23.572 1.00 112.81 ?  166 SER   B C   1 
ATOM   3376 O  O   . SER   B 1 159 ? -5.968  12.818  22.352 1.00 111.08 ?  166 SER   B O   1 
ATOM   3377 C  CB  . SER   B 1 159 ? -4.281  10.959  24.511 1.00 110.64 ?  166 SER   B CB  1 
ATOM   3378 O  OG  . SER   B 1 159 ? -5.358  10.356  25.199 1.00 112.99 ?  166 SER   B OG  1 
ATOM   3379 N  N   . LYS   B 1 160 ? -6.980  12.606  24.366 1.00 124.04 ?  167 LYS   B N   1 
ATOM   3380 C  CA  . LYS   B 1 160 ? -8.352  12.928  23.898 1.00 126.89 ?  167 LYS   B CA  1 
ATOM   3381 C  C   . LYS   B 1 160 ? -8.529  14.384  23.427 1.00 122.65 ?  167 LYS   B C   1 
ATOM   3382 O  O   . LYS   B 1 160 ? -9.344  14.644  22.539 1.00 124.17 ?  167 LYS   B O   1 
ATOM   3383 C  CB  . LYS   B 1 160 ? -9.405  12.602  24.974 1.00 138.42 ?  167 LYS   B CB  1 
ATOM   3384 C  CG  . LYS   B 1 160 ? -9.621  11.112  25.211 1.00 138.48 ?  167 LYS   B CG  1 
ATOM   3385 C  CD  . LYS   B 1 160 ? -10.505 10.482  24.166 0.00 140.16 ?  167 LYS   B CD  1 
ATOM   3386 C  CE  . LYS   B 1 160 ? -10.814 9.033   24.505 0.00 141.66 ?  167 LYS   B CE  1 
ATOM   3387 N  NZ  . LYS   B 1 160 ? -11.742 8.414   23.520 0.00 143.20 ?  167 LYS   B NZ  1 
ATOM   3388 N  N   . LEU   B 1 161 ? -7.790  15.317  24.037 1.00 117.05 ?  168 LEU   B N   1 
ATOM   3389 C  CA  . LEU   B 1 161 ? -7.727  16.722  23.581 1.00 112.24 ?  168 LEU   B CA  1 
ATOM   3390 C  C   . LEU   B 1 161 ? -7.197  16.904  22.146 1.00 112.07 ?  168 LEU   B C   1 
ATOM   3391 O  O   . LEU   B 1 161 ? -7.582  17.862  21.471 1.00 110.28 ?  168 LEU   B O   1 
ATOM   3392 C  CB  . LEU   B 1 161 ? -6.891  17.566  24.558 1.00 109.35 ?  168 LEU   B CB  1 
ATOM   3393 C  CG  . LEU   B 1 161 ? -6.677  19.057  24.284 1.00 106.65 ?  168 LEU   B CG  1 
ATOM   3394 C  CD1 . LEU   B 1 161 ? -8.003  19.807  24.208 1.00 109.23 ?  168 LEU   B CD1 1 
ATOM   3395 C  CD2 . LEU   B 1 161 ? -5.776  19.646  25.350 1.00 105.35 ?  168 LEU   B CD2 1 
ATOM   3396 N  N   . ASN   B 1 162 ? -6.307  16.010  21.704 1.00 116.61 ?  169 ASN   B N   1 
ATOM   3397 C  CA  . ASN   B 1 162 ? -5.813  15.991  20.313 1.00 121.09 ?  169 ASN   B CA  1 
ATOM   3398 C  C   . ASN   B 1 162 ? -6.960  15.615  19.367 1.00 127.88 ?  169 ASN   B C   1 
ATOM   3399 O  O   . ASN   B 1 162 ? -7.306  16.399  18.476 1.00 135.37 ?  169 ASN   B O   1 
ATOM   3400 C  CB  . ASN   B 1 162 ? -4.626  15.015  20.169 1.00 118.50 ?  169 ASN   B CB  1 
ATOM   3401 C  CG  . ASN   B 1 162 ? -3.850  15.182  18.866 1.00 116.05 ?  169 ASN   B CG  1 
ATOM   3402 O  OD1 . ASN   B 1 162 ? -4.338  15.740  17.880 1.00 118.33 ?  169 ASN   B OD1 1 
ATOM   3403 N  ND2 . ASN   B 1 162 ? -2.617  14.675  18.859 1.00 108.56 ?  169 ASN   B ND2 1 
ATOM   3404 N  N   . ASN   B 1 163 ? -7.562  14.447  19.598 1.00 133.70 ?  170 ASN   B N   1 
ATOM   3405 C  CA  . ASN   B 1 163 ? -8.688  13.950  18.791 1.00 141.15 ?  170 ASN   B CA  1 
ATOM   3406 C  C   . ASN   B 1 163 ? -9.996  14.685  19.153 1.00 139.40 ?  170 ASN   B C   1 
ATOM   3407 O  O   . ASN   B 1 163 ? -10.838 14.154  19.886 1.00 146.56 ?  170 ASN   B O   1 
ATOM   3408 C  CB  . ASN   B 1 163 ? -8.833  12.424  18.953 1.00 141.21 ?  170 ASN   B CB  1 
ATOM   3409 C  CG  . ASN   B 1 163 ? -7.647  11.644  18.465 0.00 142.10 ?  170 ASN   B CG  1 
ATOM   3410 O  OD1 . ASN   B 1 163 ? -6.944  10.999  19.243 0.00 141.15 ?  170 ASN   B OD1 1 
ATOM   3411 N  ND2 . ASN   B 1 163 ? -7.402  11.704  17.160 0.00 141.98 ?  170 ASN   B ND2 1 
ATOM   3412 N  N   . GLU   B 1 164 ? -10.137 15.910  18.635 1.00 133.98 ?  171 GLU   B N   1 
ATOM   3413 C  CA  . GLU   B 1 164 ? -11.315 16.769  18.853 1.00 137.79 ?  171 GLU   B CA  1 
ATOM   3414 C  C   . GLU   B 1 164 ? -11.716 17.473  17.551 1.00 140.69 ?  171 GLU   B C   1 
ATOM   3415 O  O   . GLU   B 1 164 ? -10.854 17.826  16.737 1.00 145.02 ?  171 GLU   B O   1 
ATOM   3416 C  CB  . GLU   B 1 164 ? -11.044 17.806  19.957 1.00 137.18 ?  171 GLU   B CB  1 
ATOM   3417 C  CG  . GLU   B 1 164 ? -12.311 18.433  20.546 1.00 143.61 ?  171 GLU   B CG  1 
ATOM   3418 C  CD  . GLU   B 1 164 ? -12.059 19.661  21.404 1.00 145.79 ?  171 GLU   B CD  1 
ATOM   3419 O  OE1 . GLU   B 1 164 ? -11.039 19.708  22.125 1.00 154.86 ?  171 GLU   B OE1 1 
ATOM   3420 O  OE2 . GLU   B 1 164 ? -12.903 20.585  21.372 1.00 145.03 ?  171 GLU   B OE2 1 
ATOM   3421 N  N   . GLU   B 1 165 ? -13.024 17.700  17.386 1.00 145.73 ?  172 GLU   B N   1 
ATOM   3422 C  CA  . GLU   B 1 165 ? -13.602 18.359  16.191 1.00 149.21 ?  172 GLU   B CA  1 
ATOM   3423 C  C   . GLU   B 1 165 ? -13.174 19.832  16.021 1.00 147.10 ?  172 GLU   B C   1 
ATOM   3424 O  O   . GLU   B 1 165 ? -12.902 20.269  14.900 1.00 140.48 ?  172 GLU   B O   1 
ATOM   3425 C  CB  . GLU   B 1 165 ? -15.144 18.260  16.199 1.00 155.67 ?  172 GLU   B CB  1 
ATOM   3426 C  CG  . GLU   B 1 165 ? -15.696 16.845  16.093 1.00 154.85 ?  172 GLU   B CG  1 
ATOM   3427 C  CD  . GLU   B 1 165 ? -17.241 16.814  16.068 0.00 167.27 ?  172 GLU   B CD  1 
ATOM   3428 O  OE1 . GLU   B 1 165 ? -17.886 17.454  16.928 0.00 168.63 ?  172 GLU   B OE1 1 
ATOM   3429 O  OE2 . GLU   B 1 165 ? -17.798 16.130  15.183 0.00 169.14 ?  172 GLU   B OE2 1 
ATOM   3430 N  N   . HIS   B 1 166 ? -13.106 20.571  17.134 1.00 147.11 ?  173 HIS   B N   1 
ATOM   3431 C  CA  . HIS   B 1 166 ? -12.649 21.983  17.152 1.00 146.22 ?  173 HIS   B CA  1 
ATOM   3432 C  C   . HIS   B 1 166 ? -11.162 22.193  16.777 1.00 138.32 ?  173 HIS   B C   1 
ATOM   3433 O  O   . HIS   B 1 166 ? -10.805 23.279  16.318 1.00 134.89 ?  173 HIS   B O   1 
ATOM   3434 C  CB  . HIS   B 1 166 ? -12.891 22.651  18.534 1.00 150.56 ?  173 HIS   B CB  1 
ATOM   3435 C  CG  . HIS   B 1 166 ? -14.333 22.714  18.955 1.00 157.23 ?  173 HIS   B CG  1 
ATOM   3436 N  ND1 . HIS   B 1 166 ? -14.809 22.048  20.065 1.00 158.94 ?  173 HIS   B ND1 1 
ATOM   3437 C  CD2 . HIS   B 1 166 ? -15.399 23.345  18.409 1.00 160.49 ?  173 HIS   B CD2 1 
ATOM   3438 C  CE1 . HIS   B 1 166 ? -16.104 22.275  20.191 1.00 160.79 ?  173 HIS   B CE1 1 
ATOM   3439 N  NE2 . HIS   B 1 166 ? -16.487 23.059  19.199 1.00 161.44 ?  173 HIS   B NE2 1 
ATOM   3440 N  N   . ASN   B 1 167 ? -10.319 21.170  16.971 1.00 131.38 ?  174 ASN   B N   1 
ATOM   3441 C  CA  . ASN   B 1 167 ? -8.866  21.285  16.794 1.00 127.01 ?  174 ASN   B CA  1 
ATOM   3442 C  C   . ASN   B 1 167 ? -8.454  21.447  15.324 1.00 124.21 ?  174 ASN   B C   1 
ATOM   3443 O  O   . ASN   B 1 167 ? -8.749  20.585  14.497 1.00 125.83 ?  174 ASN   B O   1 
ATOM   3444 C  CB  . ASN   B 1 167 ? -8.163  20.050  17.395 1.00 125.31 ?  174 ASN   B CB  1 
ATOM   3445 C  CG  . ASN   B 1 167 ? -6.667  20.248  17.625 1.00 121.26 ?  174 ASN   B CG  1 
ATOM   3446 O  OD1 . ASN   B 1 167 ? -6.105  21.342  17.476 1.00 125.40 ?  174 ASN   B OD1 1 
ATOM   3447 N  ND2 . ASN   B 1 167 ? -6.010  19.167  18.031 1.00 114.94 ?  174 ASN   B ND2 1 
ATOM   3448 N  N   . GLU   B 1 168 ? -7.784  22.559  15.006 1.00 123.16 ?  175 GLU   B N   1 
ATOM   3449 C  CA  . GLU   B 1 168 ? -7.108  22.762  13.708 1.00 125.71 ?  175 GLU   B CA  1 
ATOM   3450 C  C   . GLU   B 1 168 ? -5.927  21.796  13.518 1.00 124.18 ?  175 GLU   B C   1 
ATOM   3451 O  O   . GLU   B 1 168 ? -5.757  21.245  12.429 1.00 120.17 ?  175 GLU   B O   1 
ATOM   3452 C  CB  . GLU   B 1 168 ? -6.617  24.214  13.543 1.00 128.67 ?  175 GLU   B CB  1 
ATOM   3453 C  CG  . GLU   B 1 168 ? -7.715  25.257  13.346 1.00 131.65 ?  175 GLU   B CG  1 
ATOM   3454 C  CD  . GLU   B 1 168 ? -7.159  26.667  13.167 0.00 135.55 ?  175 GLU   B CD  1 
ATOM   3455 O  OE1 . GLU   B 1 168 ? -6.315  27.097  13.982 0.00 133.68 ?  175 GLU   B OE1 1 
ATOM   3456 O  OE2 . GLU   B 1 168 ? -7.584  27.353  12.213 0.00 137.96 ?  175 GLU   B OE2 1 
ATOM   3457 N  N   . LEU   B 1 169 ? -5.141  21.587  14.579 1.00 126.05 ?  176 LEU   B N   1 
ATOM   3458 C  CA  . LEU   B 1 169 ? -4.006  20.647  14.581 1.00 128.83 ?  176 LEU   B CA  1 
ATOM   3459 C  C   . LEU   B 1 169 ? -4.457  19.222  15.004 1.00 128.36 ?  176 LEU   B C   1 
ATOM   3460 O  O   . LEU   B 1 169 ? -3.859  18.599  15.896 1.00 122.59 ?  176 LEU   B O   1 
ATOM   3461 C  CB  . LEU   B 1 169 ? -2.869  21.189  15.482 1.00 128.90 ?  176 LEU   B CB  1 
ATOM   3462 C  CG  . LEU   B 1 169 ? -2.360  22.625  15.295 1.00 133.13 ?  176 LEU   B CG  1 
ATOM   3463 C  CD1 . LEU   B 1 169 ? -1.341  22.951  16.377 1.00 133.50 ?  176 LEU   B CD1 1 
ATOM   3464 C  CD2 . LEU   B 1 169 ? -1.766  22.859  13.911 1.00 136.25 ?  176 LEU   B CD2 1 
ATOM   3465 N  N   . ARG   B 1 170 ? -5.485  18.691  14.331 1.00 134.88 ?  177 ARG   B N   1 
ATOM   3466 C  CA  . ARG   B 1 170 ? -6.089  17.393  14.681 1.00 135.83 ?  177 ARG   B CA  1 
ATOM   3467 C  C   . ARG   B 1 170 ? -5.276  16.245  14.079 1.00 138.77 ?  177 ARG   B C   1 
ATOM   3468 O  O   . ARG   B 1 170 ? -4.747  16.371  12.966 1.00 137.25 ?  177 ARG   B O   1 
ATOM   3469 C  CB  . ARG   B 1 170 ? -7.543  17.304  14.183 1.00 135.03 ?  177 ARG   B CB  1 
ATOM   3470 C  CG  . ARG   B 1 170 ? -8.327  16.101  14.705 1.00 134.03 ?  177 ARG   B CG  1 
ATOM   3471 C  CD  . ARG   B 1 170 ? -9.734  16.034  14.135 1.00 131.17 ?  177 ARG   B CD  1 
ATOM   3472 N  NE  . ARG   B 1 170 ? -10.516 14.954  14.735 1.00 126.40 ?  177 ARG   B NE  1 
ATOM   3473 C  CZ  . ARG   B 1 170 ? -11.862 14.821  14.674 0.00 138.29 ?  177 ARG   B CZ  1 
ATOM   3474 N  NH1 . ARG   B 1 170 ? -12.611 15.620  13.910 0.00 140.25 ?  177 ARG   B NH1 1 
ATOM   3475 N  NH2 . ARG   B 1 170 ? -12.468 13.831  15.324 0.00 138.98 ?  177 ARG   B NH2 1 
ATOM   3476 N  N   . GLU   B 1 171 ? -5.204  15.134  14.819 1.00 141.75 ?  178 GLU   B N   1 
ATOM   3477 C  CA  . GLU   B 1 171 ? -4.632  13.876  14.326 1.00 148.41 ?  178 GLU   B CA  1 
ATOM   3478 C  C   . GLU   B 1 171 ? -5.710  13.140  13.516 1.00 150.60 ?  178 GLU   B C   1 
ATOM   3479 O  O   . GLU   B 1 171 ? -6.707  12.679  14.086 1.00 142.17 ?  178 GLU   B O   1 
ATOM   3480 C  CB  . GLU   B 1 171 ? -4.130  13.007  15.492 1.00 147.77 ?  178 GLU   B CB  1 
ATOM   3481 C  CG  . GLU   B 1 171 ? -3.290  11.808  15.071 1.00 142.30 ?  178 GLU   B CG  1 
ATOM   3482 C  CD  . GLU   B 1 171 ? -2.655  11.067  16.224 0.00 146.72 ?  178 GLU   B CD  1 
ATOM   3483 O  OE1 . GLU   B 1 171 ? -3.348  10.822  17.236 0.00 147.05 ?  178 GLU   B OE1 1 
ATOM   3484 O  OE2 . GLU   B 1 171 ? -1.456  10.726  16.130 0.00 145.70 ?  178 GLU   B OE2 1 
ATOM   3485 N  N   . VAL   B 1 172 ? -5.506  13.051  12.196 1.00 156.58 ?  179 VAL   B N   1 
ATOM   3486 C  CA  . VAL   B 1 172 ? -6.439  12.372  11.277 1.00 157.32 ?  179 VAL   B CA  1 
ATOM   3487 C  C   . VAL   B 1 172 ? -6.223  10.859  11.426 1.00 153.77 ?  179 VAL   B C   1 
ATOM   3488 O  O   . VAL   B 1 172 ? -5.173  10.342  11.024 1.00 141.29 ?  179 VAL   B O   1 
ATOM   3489 C  CB  . VAL   B 1 172 ? -6.245  12.824  9.797  1.00 157.49 ?  179 VAL   B CB  1 
ATOM   3490 C  CG1 . VAL   B 1 172 ? -7.194  12.086  8.847  1.00 156.44 ?  179 VAL   B CG1 1 
ATOM   3491 C  CG2 . VAL   B 1 172 ? -6.452  14.333  9.660  1.00 152.43 ?  179 VAL   B CG2 1 
ATOM   3492 N  N   . ASP   B 1 173 ? -7.210  10.174  12.014 1.00 153.57 ?  180 ASP   B N   1 
ATOM   3493 C  CA  . ASP   B 1 173 ? -7.170  8.719   12.221 1.00 153.01 ?  180 ASP   B CA  1 
ATOM   3494 C  C   . ASP   B 1 173 ? -8.582  8.131   12.271 1.00 146.29 ?  180 ASP   B C   1 
ATOM   3495 O  O   . ASP   B 1 173 ? -9.075  7.590   11.280 1.00 141.96 ?  180 ASP   B O   1 
ATOM   3496 C  CB  . ASP   B 1 173 ? -6.409  8.388   13.514 1.00 153.41 ?  180 ASP   B CB  1 
ATOM   3497 C  CG  . ASP   B 1 173 ? -6.028  6.914   13.613 1.00 157.24 ?  180 ASP   B CG  1 
ATOM   3498 O  OD1 . ASP   B 1 173 ? -5.152  6.468   12.841 1.00 153.57 ?  180 ASP   B OD1 1 
ATOM   3499 O  OD2 . ASP   B 1 173 ? -6.604  6.201   14.464 1.00 162.51 ?  180 ASP   B OD2 1 
ATOM   3500 N  N   . GLY   B 1 181 ? 4.259   2.298   12.256 1.00 108.21 ?  188 GLY   B N   1 
ATOM   3501 C  CA  . GLY   B 1 181 ? 5.288   2.798   13.160 1.00 97.31  ?  188 GLY   B CA  1 
ATOM   3502 C  C   . GLY   B 1 181 ? 5.142   2.245   14.559 1.00 100.70 ?  188 GLY   B C   1 
ATOM   3503 O  O   . GLY   B 1 181 ? 6.083   1.679   15.105 1.00 118.26 ?  188 GLY   B O   1 
ATOM   3504 N  N   . THR   B 1 182 ? 3.956   2.437   15.129 1.00 112.36 ?  189 THR   B N   1 
ATOM   3505 C  CA  . THR   B 1 182 ? 3.588   1.871   16.435 1.00 106.78 ?  189 THR   B CA  1 
ATOM   3506 C  C   . THR   B 1 182 ? 3.540   0.330   16.413 1.00 98.11  ?  189 THR   B C   1 
ATOM   3507 O  O   . THR   B 1 182 ? 4.055   -0.310  17.342 1.00 89.96  ?  189 THR   B O   1 
ATOM   3508 C  CB  . THR   B 1 182 ? 2.236   2.470   16.918 1.00 110.88 ?  189 THR   B CB  1 
ATOM   3509 O  OG1 . THR   B 1 182 ? 2.387   3.885   17.072 1.00 109.29 ?  189 THR   B OG1 1 
ATOM   3510 C  CG2 . THR   B 1 182 ? 1.752   1.862   18.250 1.00 105.62 ?  189 THR   B CG2 1 
ATOM   3511 N  N   . LEU   B 1 183 ? 2.949   -0.243  15.353 1.00 93.18  ?  190 LEU   B N   1 
ATOM   3512 C  CA  . LEU   B 1 183 ? 2.627   -1.687  15.277 1.00 81.10  ?  190 LEU   B CA  1 
ATOM   3513 C  C   . LEU   B 1 183 ? 3.810   -2.657  15.159 1.00 86.96  ?  190 LEU   B C   1 
ATOM   3514 O  O   . LEU   B 1 183 ? 3.663   -3.813  15.524 1.00 89.63  ?  190 LEU   B O   1 
ATOM   3515 C  CB  . LEU   B 1 183 ? 1.667   -1.991  14.122 1.00 91.16  ?  190 LEU   B CB  1 
ATOM   3516 C  CG  . LEU   B 1 183 ? 0.323   -1.258  14.085 1.00 104.31 ?  190 LEU   B CG  1 
ATOM   3517 C  CD1 . LEU   B 1 183 ? -0.382  -1.539  12.766 1.00 104.02 ?  190 LEU   B CD1 1 
ATOM   3518 C  CD2 . LEU   B 1 183 ? -0.564  -1.644  15.265 1.00 110.84 ?  190 LEU   B CD2 1 
ATOM   3519 N  N   . TYR   B 1 184 ? 4.984   -2.193  14.710 1.00 74.07  ?  191 TYR   B N   1 
ATOM   3520 C  CA  . TYR   B 1 184 ? 6.215   -3.012  14.763 1.00 64.46  ?  191 TYR   B CA  1 
ATOM   3521 C  C   . TYR   B 1 184 ? 6.651   -3.373  16.197 1.00 62.39  ?  191 TYR   B C   1 
ATOM   3522 O  O   . TYR   B 1 184 ? 7.276   -4.411  16.398 1.00 53.28  ?  191 TYR   B O   1 
ATOM   3523 C  CB  . TYR   B 1 184 ? 7.409   -2.322  14.077 1.00 70.82  ?  191 TYR   B CB  1 
ATOM   3524 C  CG  . TYR   B 1 184 ? 7.264   -1.926  12.610 1.00 73.60  ?  191 TYR   B CG  1 
ATOM   3525 C  CD1 . TYR   B 1 184 ? 6.499   -2.684  11.715 1.00 78.40  ?  191 TYR   B CD1 1 
ATOM   3526 C  CD2 . TYR   B 1 184 ? 7.905   -0.781  12.115 1.00 82.61  ?  191 TYR   B CD2 1 
ATOM   3527 C  CE1 . TYR   B 1 184 ? 6.386   -2.321  10.373 1.00 76.91  ?  191 TYR   B CE1 1 
ATOM   3528 C  CE2 . TYR   B 1 184 ? 7.795   -0.413  10.775 1.00 80.51  ?  191 TYR   B CE2 1 
ATOM   3529 C  CZ  . TYR   B 1 184 ? 7.038   -1.191  9.911  1.00 73.25  ?  191 TYR   B CZ  1 
ATOM   3530 O  OH  . TYR   B 1 184 ? 6.913   -0.847  8.598  1.00 69.22  ?  191 TYR   B OH  1 
ATOM   3531 N  N   . TYR   B 1 185 ? 6.337   -2.502  17.163 1.00 65.86  ?  192 TYR   B N   1 
ATOM   3532 C  CA  . TYR   B 1 185 ? 6.773   -2.614  18.565 1.00 65.00  ?  192 TYR   B CA  1 
ATOM   3533 C  C   . TYR   B 1 185 ? 5.644   -2.972  19.549 1.00 62.61  ?  192 TYR   B C   1 
ATOM   3534 O  O   . TYR   B 1 185 ? 5.894   -3.096  20.744 1.00 69.70  ?  192 TYR   B O   1 
ATOM   3535 C  CB  . TYR   B 1 185 ? 7.470   -1.309  18.999 1.00 65.86  ?  192 TYR   B CB  1 
ATOM   3536 C  CG  . TYR   B 1 185 ? 8.524   -0.902  18.008 1.00 64.88  ?  192 TYR   B CG  1 
ATOM   3537 C  CD1 . TYR   B 1 185 ? 9.815   -1.451  18.050 1.00 68.08  ?  192 TYR   B CD1 1 
ATOM   3538 C  CD2 . TYR   B 1 185 ? 8.227   -0.000  16.989 1.00 62.31  ?  192 TYR   B CD2 1 
ATOM   3539 C  CE1 . TYR   B 1 185 ? 10.791  -1.077  17.123 1.00 71.69  ?  192 TYR   B CE1 1 
ATOM   3540 C  CE2 . TYR   B 1 185 ? 9.196   0.381   16.053 1.00 64.90  ?  192 TYR   B CE2 1 
ATOM   3541 C  CZ  . TYR   B 1 185 ? 10.470  -0.175  16.112 1.00 64.80  ?  192 TYR   B CZ  1 
ATOM   3542 O  OH  . TYR   B 1 185 ? 11.434  0.172   15.199 1.00 72.48  ?  192 TYR   B OH  1 
ATOM   3543 N  N   . MET   B 1 186 ? 4.429   -3.173  19.041 1.00 60.70  ?  193 MET   B N   1 
ATOM   3544 C  CA  . MET   B 1 186 ? 3.259   -3.532  19.839 1.00 72.27  ?  193 MET   B CA  1 
ATOM   3545 C  C   . MET   B 1 186 ? 3.189   -5.056  19.946 1.00 68.48  ?  193 MET   B C   1 
ATOM   3546 O  O   . MET   B 1 186 ? 3.227   -5.762  18.934 1.00 74.63  ?  193 MET   B O   1 
ATOM   3547 C  CB  . MET   B 1 186 ? 1.979   -2.994  19.175 1.00 80.47  ?  193 MET   B CB  1 
ATOM   3548 C  CG  . MET   B 1 186 ? 0.684   -3.233  19.936 1.00 93.71  ?  193 MET   B CG  1 
ATOM   3549 S  SD  . MET   B 1 186 ? -0.679  -2.246  19.300 1.00 124.93 ?  193 MET   B SD  1 
ATOM   3550 C  CE  . MET   B 1 186 ? -0.332  -0.677  20.094 1.00 127.37 ?  193 MET   B CE  1 
ATOM   3551 N  N   . ALA   B 1 187 ? 3.088   -5.535  21.181 1.00 68.51  ?  194 ALA   B N   1 
ATOM   3552 C  CA  . ALA   B 1 187 ? 3.038   -6.962  21.481 1.00 72.95  ?  194 ALA   B CA  1 
ATOM   3553 C  C   . ALA   B 1 187 ? 1.833   -7.642  20.826 1.00 69.05  ?  194 ALA   B C   1 
ATOM   3554 O  O   . ALA   B 1 187 ? 0.774   -7.013  20.743 1.00 65.24  ?  194 ALA   B O   1 
ATOM   3555 C  CB  . ALA   B 1 187 ? 2.988   -7.176  22.989 1.00 76.90  ?  194 ALA   B CB  1 
ATOM   3556 N  N   . PRO   B 1 188 ? 1.992   -8.909  20.357 1.00 72.36  ?  195 PRO   B N   1 
ATOM   3557 C  CA  . PRO   B 1 188 ? 0.935   -9.599  19.579 1.00 73.20  ?  195 PRO   B CA  1 
ATOM   3558 C  C   . PRO   B 1 188 ? -0.425  -9.719  20.256 1.00 70.75  ?  195 PRO   B C   1 
ATOM   3559 O  O   . PRO   B 1 188 ? -1.432  -9.647  19.564 1.00 81.75  ?  195 PRO   B O   1 
ATOM   3560 C  CB  . PRO   B 1 188 ? 1.529   -10.993 19.325 1.00 71.30  ?  195 PRO   B CB  1 
ATOM   3561 C  CG  . PRO   B 1 188 ? 2.529   -11.175 20.390 1.00 74.03  ?  195 PRO   B CG  1 
ATOM   3562 C  CD  . PRO   B 1 188 ? 3.139   -9.814  20.569 1.00 72.62  ?  195 PRO   B CD  1 
ATOM   3563 N  N   . GLU   B 1 189 ? -0.434  -9.876  21.582 1.00 70.94  ?  196 GLU   B N   1 
ATOM   3564 C  CA  . GLU   B 1 189 ? -1.671  -9.801  22.377 1.00 76.84  ?  196 GLU   B CA  1 
ATOM   3565 C  C   . GLU   B 1 189 ? -2.540  -8.534  22.154 1.00 80.40  ?  196 GLU   B C   1 
ATOM   3566 O  O   . GLU   B 1 189 ? -3.746  -8.606  22.328 1.00 78.84  ?  196 GLU   B O   1 
ATOM   3567 C  CB  . GLU   B 1 189 ? -1.416  -10.030 23.890 1.00 77.84  ?  196 GLU   B CB  1 
ATOM   3568 C  CG  . GLU   B 1 189 ? -0.477  -9.037  24.605 1.00 77.38  ?  196 GLU   B CG  1 
ATOM   3569 C  CD  . GLU   B 1 189 ? 0.974   -9.503  24.719 1.00 75.76  ?  196 GLU   B CD  1 
ATOM   3570 O  OE1 . GLU   B 1 189 ? 1.681   -9.050  25.633 1.00 79.24  ?  196 GLU   B OE1 1 
ATOM   3571 O  OE2 . GLU   B 1 189 ? 1.434   -10.296 23.863 1.00 86.72  ?  196 GLU   B OE2 1 
ATOM   3572 N  N   . HIS   B 1 190 ? -1.925  -7.409  21.783 1.00 80.01  ?  197 HIS   B N   1 
ATOM   3573 C  CA  . HIS   B 1 190 ? -2.621  -6.133  21.486 1.00 83.68  ?  197 HIS   B CA  1 
ATOM   3574 C  C   . HIS   B 1 190 ? -2.964  -5.843  20.018 1.00 82.33  ?  197 HIS   B C   1 
ATOM   3575 O  O   . HIS   B 1 190 ? -3.748  -4.916  19.749 1.00 89.72  ?  197 HIS   B O   1 
ATOM   3576 C  CB  . HIS   B 1 190 ? -1.800  -4.965  22.047 1.00 78.90  ?  197 HIS   B CB  1 
ATOM   3577 C  CG  . HIS   B 1 190 ? -1.558  -5.074  23.517 1.00 82.94  ?  197 HIS   B CG  1 
ATOM   3578 N  ND1 . HIS   B 1 190 ? -2.587  -5.109  24.434 1.00 90.35  ?  197 HIS   B ND1 1 
ATOM   3579 C  CD2 . HIS   B 1 190 ? -0.416  -5.207  24.228 1.00 77.51  ?  197 HIS   B CD2 1 
ATOM   3580 C  CE1 . HIS   B 1 190 ? -2.089  -5.247  25.647 1.00 87.71  ?  197 HIS   B CE1 1 
ATOM   3581 N  NE2 . HIS   B 1 190 ? -0.774  -5.304  25.550 1.00 83.76  ?  197 HIS   B NE2 1 
ATOM   3582 N  N   . LEU   B 1 191 ? -2.373  -6.586  19.080 1.00 73.40  ?  198 LEU   B N   1 
ATOM   3583 C  CA  . LEU   B 1 191 ? -2.647  -6.386  17.645 1.00 70.46  ?  198 LEU   B CA  1 
ATOM   3584 C  C   . LEU   B 1 191 ? -4.053  -6.933  17.319 1.00 77.24  ?  198 LEU   B C   1 
ATOM   3585 O  O   . LEU   B 1 191 ? -4.341  -8.085  17.635 1.00 69.33  ?  198 LEU   B O   1 
ATOM   3586 C  CB  . LEU   B 1 191 ? -1.585  -7.076  16.782 1.00 65.74  ?  198 LEU   B CB  1 
ATOM   3587 C  CG  . LEU   B 1 191 ? -0.115  -6.651  16.953 1.00 65.25  ?  198 LEU   B CG  1 
ATOM   3588 C  CD1 . LEU   B 1 191 ? 0.847   -7.568  16.211 1.00 62.82  ?  198 LEU   B CD1 1 
ATOM   3589 C  CD2 . LEU   B 1 191 ? 0.088   -5.213  16.492 1.00 64.03  ?  198 LEU   B CD2 1 
ATOM   3590 N  N   . ASN   B 1 192 ? -4.908  -6.106  16.700 1.00 82.19  ?  199 ASN   B N   1 
ATOM   3591 C  CA  . ASN   B 1 192 ? -6.357  -6.405  16.507 1.00 96.08  ?  199 ASN   B CA  1 
ATOM   3592 C  C   . ASN   B 1 192 ? -7.095  -6.786  17.819 1.00 102.33 ?  199 ASN   B C   1 
ATOM   3593 O  O   . ASN   B 1 192 ? -7.868  -7.749  17.886 1.00 108.79 ?  199 ASN   B O   1 
ATOM   3594 C  CB  . ASN   B 1 192 ? -6.557  -7.464  15.398 1.00 102.99 ?  199 ASN   B CB  1 
ATOM   3595 C  CG  . ASN   B 1 192 ? -6.254  -6.936  14.004 1.00 113.06 ?  199 ASN   B CG  1 
ATOM   3596 O  OD1 . ASN   B 1 192 ? -5.688  -5.853  13.824 1.00 110.21 ?  199 ASN   B OD1 1 
ATOM   3597 N  ND2 . ASN   B 1 192 ? -6.636  -7.718  12.994 1.00 123.21 ?  199 ASN   B ND2 1 
ATOM   3598 N  N   . ASP   B 1 193 ? -6.789  -6.034  18.874 1.00 111.76 ?  200 ASP   B N   1 
ATOM   3599 C  CA  . ASP   B 1 193 ? -7.344  -6.262  20.219 1.00 120.82 ?  200 ASP   B CA  1 
ATOM   3600 C  C   . ASP   B 1 193 ? -7.232  -4.962  21.027 1.00 135.92 ?  200 ASP   B C   1 
ATOM   3601 O  O   . ASP   B 1 193 ? -6.340  -4.796  21.865 1.00 148.29 ?  200 ASP   B O   1 
ATOM   3602 C  CB  . ASP   B 1 193 ? -6.619  -7.449  20.883 1.00 115.95 ?  200 ASP   B CB  1 
ATOM   3603 C  CG  . ASP   B 1 193 ? -7.327  -7.990  22.124 1.00 120.79 ?  200 ASP   B CG  1 
ATOM   3604 O  OD1 . ASP   B 1 193 ? -8.236  -7.347  22.696 1.00 128.81 ?  200 ASP   B OD1 1 
ATOM   3605 O  OD2 . ASP   B 1 193 ? -6.953  -9.109  22.534 1.00 119.84 ?  200 ASP   B OD2 1 
ATOM   3606 N  N   . VAL   B 1 194 ? -8.142  -4.037  20.723 1.00 155.74 ?  201 VAL   B N   1 
ATOM   3607 C  CA  . VAL   B 1 194 ? -8.168  -2.686  21.339 1.00 163.68 ?  201 VAL   B CA  1 
ATOM   3608 C  C   . VAL   B 1 194 ? -8.611  -2.723  22.815 1.00 164.67 ?  201 VAL   B C   1 
ATOM   3609 O  O   . VAL   B 1 194 ? -8.213  -1.846  23.578 1.00 158.90 ?  201 VAL   B O   1 
ATOM   3610 C  CB  . VAL   B 1 194 ? -9.060  -1.680  20.532 1.00 166.09 ?  201 VAL   B CB  1 
ATOM   3611 C  CG1 . VAL   B 1 194 ? -9.095  -0.276  21.153 1.00 161.91 ?  201 VAL   B CG1 1 
ATOM   3612 C  CG2 . VAL   B 1 194 ? -8.584  -1.553  19.078 1.00 162.10 ?  201 VAL   B CG2 1 
ATOM   3613 N  N   . ASN   B 1 195 ? -9.405  -3.728  23.202 1.00 160.18 ?  202 ASN   B N   1 
ATOM   3614 C  CA  . ASN   B 1 195 ? -9.911  -3.860  24.579 1.00 162.80 ?  202 ASN   B CA  1 
ATOM   3615 C  C   . ASN   B 1 195 ? -8.882  -4.365  25.611 1.00 157.78 ?  202 ASN   B C   1 
ATOM   3616 O  O   . ASN   B 1 195 ? -9.009  -4.027  26.790 1.00 168.43 ?  202 ASN   B O   1 
ATOM   3617 C  CB  . ASN   B 1 195 ? -11.161 -4.760  24.608 1.00 168.34 ?  202 ASN   B CB  1 
ATOM   3618 C  CG  . ASN   B 1 195 ? -11.896 -4.747  25.931 0.00 173.97 ?  202 ASN   B CG  1 
ATOM   3619 O  OD1 . ASN   B 1 195 ? -12.219 -3.673  26.430 0.00 175.09 ?  202 ASN   B OD1 1 
ATOM   3620 N  ND2 . ASN   B 1 195 ? -12.156 -5.916  26.513 0.00 175.93 ?  202 ASN   B ND2 1 
ATOM   3621 N  N   . ALA   B 1 196 ? -7.888  -5.156  25.183 1.00 152.44 ?  203 ALA   B N   1 
ATOM   3622 C  CA  . ALA   B 1 196 ? -6.913  -5.775  26.113 1.00 142.55 ?  203 ALA   B CA  1 
ATOM   3623 C  C   . ALA   B 1 196 ? -6.070  -4.746  26.889 1.00 129.42 ?  203 ALA   B C   1 
ATOM   3624 O  O   . ALA   B 1 196 ? -5.553  -3.786  26.303 1.00 106.66 ?  203 ALA   B O   1 
ATOM   3625 C  CB  . ALA   B 1 196 ? -6.002  -6.757  25.380 1.00 135.13 ?  203 ALA   B CB  1 
ATOM   3626 N  N   . LYS   B 1 197 ? -5.962  -4.956  28.207 1.00 129.50 ?  204 LYS   B N   1 
ATOM   3627 C  CA  . LYS   B 1 197 ? -5.250  -4.043  29.111 1.00 127.44 ?  204 LYS   B CA  1 
ATOM   3628 C  C   . LYS   B 1 197 ? -3.756  -4.300  28.954 1.00 110.35 ?  204 LYS   B C   1 
ATOM   3629 O  O   . LYS   B 1 197 ? -3.329  -5.445  29.150 1.00 105.32 ?  204 LYS   B O   1 
ATOM   3630 C  CB  . LYS   B 1 197 ? -5.657  -4.267  30.574 1.00 132.21 ?  204 LYS   B CB  1 
ATOM   3631 C  CG  . LYS   B 1 197 ? -7.120  -3.975  30.868 1.00 134.89 ?  204 LYS   B CG  1 
ATOM   3632 C  CD  . LYS   B 1 197 ? -7.474  -4.383  32.301 0.00 143.95 ?  204 LYS   B CD  1 
ATOM   3633 C  CE  . LYS   B 1 197 ? -8.966  -4.260  32.562 0.00 148.71 ?  204 LYS   B CE  1 
ATOM   3634 N  NZ  . LYS   B 1 197 ? -9.333  -4.700  33.935 0.00 152.17 ?  204 LYS   B NZ  1 
ATOM   3635 N  N   . PRO   B 1 198 ? -2.953  -3.258  28.609 1.00 107.07 ?  205 PRO   B N   1 
ATOM   3636 C  CA  . PRO   B 1 198 ? -1.491  -3.454  28.628 1.00 93.50  ?  205 PRO   B CA  1 
ATOM   3637 C  C   . PRO   B 1 198 ? -0.908  -3.635  30.033 1.00 86.50  ?  205 PRO   B C   1 
ATOM   3638 O  O   . PRO   B 1 198 ? -1.478  -3.160  31.015 1.00 83.46  ?  205 PRO   B O   1 
ATOM   3639 C  CB  . PRO   B 1 198 ? -0.951  -2.185  27.966 1.00 89.36  ?  205 PRO   B CB  1 
ATOM   3640 C  CG  . PRO   B 1 198 ? -2.106  -1.592  27.234 1.00 87.59  ?  205 PRO   B CG  1 
ATOM   3641 C  CD  . PRO   B 1 198 ? -3.283  -1.913  28.093 1.00 103.23 ?  205 PRO   B CD  1 
ATOM   3642 N  N   . THR   B 1 199 ? 0.209   -4.346  30.089 1.00 76.88  ?  206 THR   B N   1 
ATOM   3643 C  CA  . THR   B 1 199 ? 0.895   -4.695  31.320 1.00 77.67  ?  206 THR   B CA  1 
ATOM   3644 C  C   . THR   B 1 199 ? 2.369   -4.310  31.183 1.00 79.90  ?  206 THR   B C   1 
ATOM   3645 O  O   . THR   B 1 199 ? 2.822   -3.874  30.115 1.00 65.05  ?  206 THR   B O   1 
ATOM   3646 C  CB  . THR   B 1 199 ? 0.783   -6.213  31.601 1.00 88.87  ?  206 THR   B CB  1 
ATOM   3647 O  OG1 . THR   B 1 199 ? 1.470   -6.957  30.586 1.00 93.43  ?  206 THR   B OG1 1 
ATOM   3648 C  CG2 . THR   B 1 199 ? -0.698  -6.672  31.652 1.00 91.95  ?  206 THR   B CG2 1 
ATOM   3649 N  N   . GLU   B 1 200 ? 3.110   -4.508  32.270 1.00 88.46  ?  207 GLU   B N   1 
ATOM   3650 C  CA  . GLU   B 1 200 ? 4.573   -4.422  32.260 1.00 83.84  ?  207 GLU   B CA  1 
ATOM   3651 C  C   . GLU   B 1 200 ? 5.188   -5.328  31.165 1.00 84.63  ?  207 GLU   B C   1 
ATOM   3652 O  O   . GLU   B 1 200 ? 6.141   -4.938  30.500 1.00 85.77  ?  207 GLU   B O   1 
ATOM   3653 C  CB  . GLU   B 1 200 ? 5.159   -4.767  33.650 1.00 84.42  ?  207 GLU   B CB  1 
ATOM   3654 C  CG  . GLU   B 1 200 ? 4.805   -3.794  34.778 1.00 83.66  ?  207 GLU   B CG  1 
ATOM   3655 C  CD  . GLU   B 1 200 ? 5.405   -4.084  36.126 0.00 84.25  ?  207 GLU   B CD  1 
ATOM   3656 O  OE1 . GLU   B 1 200 ? 6.223   -5.024  36.250 0.00 83.29  ?  207 GLU   B OE1 1 
ATOM   3657 O  OE2 . GLU   B 1 200 ? 5.051   -3.382  37.097 0.00 85.34  ?  207 GLU   B OE2 1 
ATOM   3658 N  N   . LYS   B 1 201 ? 4.599   -6.506  30.965 1.00 83.96  ?  208 LYS   B N   1 
ATOM   3659 C  CA  . LYS   B 1 201 ? 5.031   -7.454  29.919 1.00 83.91  ?  208 LYS   B CA  1 
ATOM   3660 C  C   . LYS   B 1 201 ? 4.855   -6.969  28.465 1.00 76.57  ?  208 LYS   B C   1 
ATOM   3661 O  O   . LYS   B 1 201 ? 5.623   -7.390  27.597 1.00 84.98  ?  208 LYS   B O   1 
ATOM   3662 C  CB  . LYS   B 1 201 ? 4.337   -8.822  30.088 1.00 83.49  ?  208 LYS   B CB  1 
ATOM   3663 C  CG  . LYS   B 1 201 ? 5.120   -9.847  30.870 1.00 83.23  ?  208 LYS   B CG  1 
ATOM   3664 C  CD  . LYS   B 1 201 ? 5.600   -9.441  32.248 1.00 86.65  ?  208 LYS   B CD  1 
ATOM   3665 C  CE  . LYS   B 1 201 ? 6.538   -10.519 32.782 1.00 86.56  ?  208 LYS   B CE  1 
ATOM   3666 N  NZ  . LYS   B 1 201 ? 6.752   -10.424 34.247 1.00 95.49  ?  208 LYS   B NZ  1 
ATOM   3667 N  N   . SER   B 1 202 ? 3.837   -6.147  28.209 1.00 60.54  ?  209 SER   B N   1 
ATOM   3668 C  CA  . SER   B 1 202 ? 3.659   -5.497  26.908 1.00 58.81  ?  209 SER   B CA  1 
ATOM   3669 C  C   . SER   B 1 202 ? 4.856   -4.605  26.503 1.00 59.22  ?  209 SER   B C   1 
ATOM   3670 O  O   . SER   B 1 202 ? 5.262   -4.619  25.348 1.00 58.54  ?  209 SER   B O   1 
ATOM   3671 C  CB  . SER   B 1 202 ? 2.402   -4.629  26.918 1.00 61.92  ?  209 SER   B CB  1 
ATOM   3672 O  OG  . SER   B 1 202 ? 1.284   -5.344  27.390 1.00 70.16  ?  209 SER   B OG  1 
ATOM   3673 N  N   . ASP   B 1 203 ? 5.376   -3.833  27.463 1.00 56.91  ?  210 ASP   B N   1 
ATOM   3674 C  CA  . ASP   B 1 203 ? 6.588   -3.033  27.285 1.00 61.09  ?  210 ASP   B CA  1 
ATOM   3675 C  C   . ASP   B 1 203 ? 7.867   -3.839  27.089 1.00 65.28  ?  210 ASP   B C   1 
ATOM   3676 O  O   . ASP   B 1 203 ? 8.750   -3.405  26.349 1.00 81.34  ?  210 ASP   B O   1 
ATOM   3677 C  CB  . ASP   B 1 203 ? 6.801   -2.086  28.472 1.00 63.87  ?  210 ASP   B CB  1 
ATOM   3678 C  CG  . ASP   B 1 203 ? 5.781   -0.970  28.541 1.00 62.05  ?  210 ASP   B CG  1 
ATOM   3679 O  OD1 . ASP   B 1 203 ? 5.137   -0.656  27.525 1.00 65.05  ?  210 ASP   B OD1 1 
ATOM   3680 O  OD2 . ASP   B 1 203 ? 5.634   -0.393  29.636 1.00 69.12  ?  210 ASP   B OD2 1 
ATOM   3681 N  N   . VAL   B 1 204 ? 7.973   -4.987  27.755 1.00 71.51  ?  211 VAL   B N   1 
ATOM   3682 C  CA  . VAL   B 1 204 ? 9.116   -5.896  27.574 1.00 72.53  ?  211 VAL   B CA  1 
ATOM   3683 C  C   . VAL   B 1 204 ? 9.165   -6.430  26.124 1.00 78.58  ?  211 VAL   B C   1 
ATOM   3684 O  O   . VAL   B 1 204 ? 10.257  -6.585  25.567 1.00 63.10  ?  211 VAL   B O   1 
ATOM   3685 C  CB  . VAL   B 1 204 ? 9.120   -7.028  28.634 1.00 75.46  ?  211 VAL   B CB  1 
ATOM   3686 C  CG1 . VAL   B 1 204 ? 10.181  -8.098  28.351 1.00 78.84  ?  211 VAL   B CG1 1 
ATOM   3687 C  CG2 . VAL   B 1 204 ? 9.373   -6.437  30.020 1.00 70.18  ?  211 VAL   B CG2 1 
ATOM   3688 N  N   . TYR   B 1 205 ? 8.000   -6.701  25.518 1.00 80.23  ?  212 TYR   B N   1 
ATOM   3689 C  CA  . TYR   B 1 205 ? 7.951   -7.017  24.078 1.00 75.23  ?  212 TYR   B CA  1 
ATOM   3690 C  C   . TYR   B 1 205 ? 8.516   -5.889  23.202 1.00 63.60  ?  212 TYR   B C   1 
ATOM   3691 O  O   . TYR   B 1 205 ? 9.308   -6.140  22.294 1.00 56.08  ?  212 TYR   B O   1 
ATOM   3692 C  CB  . TYR   B 1 205 ? 6.533   -7.386  23.595 1.00 70.16  ?  212 TYR   B CB  1 
ATOM   3693 C  CG  . TYR   B 1 205 ? 6.527   -7.866  22.152 1.00 67.72  ?  212 TYR   B CG  1 
ATOM   3694 C  CD1 . TYR   B 1 205 ? 6.458   -6.955  21.090 1.00 68.64  ?  212 TYR   B CD1 1 
ATOM   3695 C  CD2 . TYR   B 1 205 ? 6.674   -9.216  21.837 1.00 64.70  ?  212 TYR   B CD2 1 
ATOM   3696 C  CE1 . TYR   B 1 205 ? 6.493   -7.383  19.770 1.00 69.42  ?  212 TYR   B CE1 1 
ATOM   3697 C  CE2 . TYR   B 1 205 ? 6.709   -9.645  20.519 1.00 64.05  ?  212 TYR   B CE2 1 
ATOM   3698 C  CZ  . TYR   B 1 205 ? 6.625   -8.729  19.490 1.00 62.31  ?  212 TYR   B CZ  1 
ATOM   3699 O  OH  . TYR   B 1 205 ? 6.654   -9.153  18.186 1.00 72.85  ?  212 TYR   B OH  1 
ATOM   3700 N  N   . SER   B 1 206 ? 8.069   -4.664  23.453 1.00 61.55  ?  213 SER   B N   1 
ATOM   3701 C  CA  . SER   B 1 206 ? 8.508   -3.497  22.688 1.00 65.93  ?  213 SER   B CA  1 
ATOM   3702 C  C   . SER   B 1 206 ? 10.048  -3.358  22.747 1.00 61.75  ?  213 SER   B C   1 
ATOM   3703 O  O   . SER   B 1 206 ? 10.705  -3.311  21.699 1.00 71.29  ?  213 SER   B O   1 
ATOM   3704 C  CB  . SER   B 1 206 ? 7.861   -2.243  23.243 1.00 65.84  ?  213 SER   B CB  1 
ATOM   3705 O  OG  . SER   B 1 206 ? 6.447   -2.266  23.177 1.00 62.98  ?  213 SER   B OG  1 
ATOM   3706 N  N   . PHE   B 1 207 ? 10.583  -3.382  23.976 1.00 57.19  ?  214 PHE   B N   1 
ATOM   3707 C  CA  . PHE   B 1 207 ? 12.022  -3.459  24.277 1.00 54.98  ?  214 PHE   B CA  1 
ATOM   3708 C  C   . PHE   B 1 207 ? 12.772  -4.502  23.454 1.00 51.63  ?  214 PHE   B C   1 
ATOM   3709 O  O   . PHE   B 1 207 ? 13.830  -4.211  22.911 1.00 53.58  ?  214 PHE   B O   1 
ATOM   3710 C  CB  . PHE   B 1 207 ? 12.217  -3.717  25.775 1.00 54.83  ?  214 PHE   B CB  1 
ATOM   3711 C  CG  . PHE   B 1 207 ? 13.647  -3.909  26.187 1.00 60.96  ?  214 PHE   B CG  1 
ATOM   3712 C  CD1 . PHE   B 1 207 ? 14.493  -2.814  26.302 1.00 55.96  ?  214 PHE   B CD1 1 
ATOM   3713 C  CD2 . PHE   B 1 207 ? 14.148  -5.181  26.486 1.00 60.26  ?  214 PHE   B CD2 1 
ATOM   3714 C  CE1 . PHE   B 1 207 ? 15.826  -2.970  26.697 1.00 63.61  ?  214 PHE   B CE1 1 
ATOM   3715 C  CE2 . PHE   B 1 207 ? 15.478  -5.345  26.868 1.00 65.55  ?  214 PHE   B CE2 1 
ATOM   3716 C  CZ  . PHE   B 1 207 ? 16.322  -4.243  26.976 1.00 63.16  ?  214 PHE   B CZ  1 
ATOM   3717 N  N   . ALA   B 1 208 ? 12.214  -5.703  23.374 1.00 62.09  ?  215 ALA   B N   1 
ATOM   3718 C  CA  . ALA   B 1 208 ? 12.761  -6.806  22.546 1.00 58.58  ?  215 ALA   B CA  1 
ATOM   3719 C  C   . ALA   B 1 208 ? 12.966  -6.388  21.106 1.00 57.89  ?  215 ALA   B C   1 
ATOM   3720 O  O   . ALA   B 1 208 ? 14.011  -6.658  20.526 1.00 57.16  ?  215 ALA   B O   1 
ATOM   3721 C  CB  . ALA   B 1 208 ? 11.836  -8.021  22.575 1.00 64.01  ?  215 ALA   B CB  1 
ATOM   3722 N  N   . VAL   B 1 209 ? 11.956  -5.718  20.548 1.00 59.58  ?  216 VAL   B N   1 
ATOM   3723 C  CA  . VAL   B 1 209 ? 12.019  -5.247  19.170 1.00 58.47  ?  216 VAL   B CA  1 
ATOM   3724 C  C   . VAL   B 1 209 ? 12.993  -4.044  19.058 1.00 60.92  ?  216 VAL   B C   1 
ATOM   3725 O  O   . VAL   B 1 209 ? 13.723  -3.946  18.061 1.00 62.21  ?  216 VAL   B O   1 
ATOM   3726 C  CB  . VAL   B 1 209 ? 10.613  -4.946  18.590 1.00 55.66  ?  216 VAL   B CB  1 
ATOM   3727 C  CG1 . VAL   B 1 209 ? 10.712  -4.602  17.109 1.00 51.77  ?  216 VAL   B CG1 1 
ATOM   3728 C  CG2 . VAL   B 1 209 ? 9.682   -6.150  18.750 1.00 59.43  ?  216 VAL   B CG2 1 
ATOM   3729 N  N   . VAL   B 1 210 ? 13.014  -3.173  20.078 1.00 59.11  ?  217 VAL   B N   1 
ATOM   3730 C  CA  . VAL   B 1 210 ? 14.019  -2.077  20.185 1.00 61.94  ?  217 VAL   B CA  1 
ATOM   3731 C  C   . VAL   B 1 210 ? 15.469  -2.618  20.195 1.00 55.67  ?  217 VAL   B C   1 
ATOM   3732 O  O   . VAL   B 1 210 ? 16.357  -1.981  19.625 1.00 59.60  ?  217 VAL   B O   1 
ATOM   3733 C  CB  . VAL   B 1 210 ? 13.768  -1.145  21.413 1.00 58.80  ?  217 VAL   B CB  1 
ATOM   3734 C  CG1 . VAL   B 1 210 ? 14.857  -0.082  21.566 1.00 65.84  ?  217 VAL   B CG1 1 
ATOM   3735 C  CG2 . VAL   B 1 210 ? 12.440  -0.411  21.290 1.00 61.62  ?  217 VAL   B CG2 1 
ATOM   3736 N  N   . LEU   B 1 211 ? 15.698  -3.771  20.834 1.00 54.26  ?  218 LEU   B N   1 
ATOM   3737 C  CA  . LEU   B 1 211 ? 17.035  -4.393  20.881 1.00 61.07  ?  218 LEU   B CA  1 
ATOM   3738 C  C   . LEU   B 1 211 ? 17.491  -4.770  19.493 1.00 60.72  ?  218 LEU   B C   1 
ATOM   3739 O  O   . LEU   B 1 211 ? 18.559  -4.336  19.084 1.00 58.82  ?  218 LEU   B O   1 
ATOM   3740 C  CB  . LEU   B 1 211 ? 17.093  -5.630  21.780 1.00 69.27  ?  218 LEU   B CB  1 
ATOM   3741 C  CG  . LEU   B 1 211 ? 17.053  -5.472  23.295 1.00 71.11  ?  218 LEU   B CG  1 
ATOM   3742 C  CD1 . LEU   B 1 211 ? 17.125  -6.850  23.935 1.00 74.26  ?  218 LEU   B CD1 1 
ATOM   3743 C  CD2 . LEU   B 1 211 ? 18.189  -4.599  23.799 1.00 75.48  ?  218 LEU   B CD2 1 
ATOM   3744 N  N   . TRP   B 1 212 ? 16.657  -5.542  18.783 1.00 63.76  ?  219 TRP   B N   1 
ATOM   3745 C  CA  . TRP   B 1 212 ? 16.874  -5.897  17.366 1.00 60.41  ?  219 TRP   B CA  1 
ATOM   3746 C  C   . TRP   B 1 212 ? 17.219  -4.671  16.490 1.00 59.90  ?  219 TRP   B C   1 
ATOM   3747 O  O   . TRP   B 1 212 ? 18.206  -4.691  15.743 1.00 67.08  ?  219 TRP   B O   1 
ATOM   3748 C  CB  . TRP   B 1 212 ? 15.633  -6.595  16.778 1.00 60.63  ?  219 TRP   B CB  1 
ATOM   3749 C  CG  . TRP   B 1 212 ? 15.886  -7.105  15.397 1.00 65.21  ?  219 TRP   B CG  1 
ATOM   3750 C  CD1 . TRP   B 1 212 ? 16.420  -8.307  15.054 1.00 63.25  ?  219 TRP   B CD1 1 
ATOM   3751 C  CD2 . TRP   B 1 212 ? 15.677  -6.393  14.176 1.00 69.52  ?  219 TRP   B CD2 1 
ATOM   3752 N  NE1 . TRP   B 1 212 ? 16.544  -8.400  13.696 1.00 65.08  ?  219 TRP   B NE1 1 
ATOM   3753 C  CE2 . TRP   B 1 212 ? 16.111  -7.231  13.128 1.00 69.65  ?  219 TRP   B CE2 1 
ATOM   3754 C  CE3 . TRP   B 1 212 ? 15.203  -5.104  13.868 1.00 73.19  ?  219 TRP   B CE3 1 
ATOM   3755 C  CZ2 . TRP   B 1 212 ? 16.049  -6.842  11.777 1.00 76.21  ?  219 TRP   B CZ2 1 
ATOM   3756 C  CZ3 . TRP   B 1 212 ? 15.144  -4.708  12.522 1.00 69.40  ?  219 TRP   B CZ3 1 
ATOM   3757 C  CH2 . TRP   B 1 212 ? 15.562  -5.578  11.495 1.00 73.30  ?  219 TRP   B CH2 1 
ATOM   3758 N  N   . ALA   B 1 213 ? 16.382  -3.639  16.589 1.00 54.74  ?  220 ALA   B N   1 
ATOM   3759 C  CA  . ALA   B 1 213 ? 16.578  -2.375  15.850 1.00 58.62  ?  220 ALA   B CA  1 
ATOM   3760 C  C   . ALA   B 1 213 ? 17.933  -1.713  16.120 1.00 62.71  ?  220 ALA   B C   1 
ATOM   3761 O  O   . ALA   B 1 213 ? 18.558  -1.167  15.198 1.00 71.28  ?  220 ALA   B O   1 
ATOM   3762 C  CB  . ALA   B 1 213 ? 15.459  -1.406  16.165 1.00 56.24  ?  220 ALA   B CB  1 
ATOM   3763 N  N   . ILE   B 1 214 ? 18.374  -1.769  17.381 1.00 59.88  ?  221 ILE   B N   1 
ATOM   3764 C  CA  . ILE   B 1 214 ? 19.685  -1.225  17.784 1.00 58.25  ?  221 ILE   B CA  1 
ATOM   3765 C  C   . ILE   B 1 214 ? 20.849  -1.932  17.059 1.00 56.72  ?  221 ILE   B C   1 
ATOM   3766 O  O   . ILE   B 1 214 ? 21.823  -1.270  16.697 1.00 67.41  ?  221 ILE   B O   1 
ATOM   3767 C  CB  . ILE   B 1 214 ? 19.852  -1.189  19.345 1.00 53.27  ?  221 ILE   B CB  1 
ATOM   3768 C  CG1 . ILE   B 1 214 ? 19.008  -0.020  19.916 1.00 51.00  ?  221 ILE   B CG1 1 
ATOM   3769 C  CG2 . ILE   B 1 214 ? 21.316  -1.013  19.771 1.00 52.86  ?  221 ILE   B CG2 1 
ATOM   3770 C  CD1 . ILE   B 1 214 ? 18.772  0.011   21.423 1.00 48.04  ?  221 ILE   B CD1 1 
ATOM   3771 N  N   . PHE   B 1 215 ? 20.749  -3.243  16.850 1.00 59.58  ?  222 PHE   B N   1 
ATOM   3772 C  CA  . PHE   B 1 215 ? 21.788  -4.001  16.095 1.00 60.19  ?  222 PHE   B CA  1 
ATOM   3773 C  C   . PHE   B 1 215 ? 21.566  -4.125  14.592 1.00 61.79  ?  222 PHE   B C   1 
ATOM   3774 O  O   . PHE   B 1 215 ? 22.509  -4.463  13.859 1.00 62.09  ?  222 PHE   B O   1 
ATOM   3775 C  CB  . PHE   B 1 215 ? 22.098  -5.335  16.791 1.00 57.35  ?  222 PHE   B CB  1 
ATOM   3776 C  CG  . PHE   B 1 215 ? 22.769  -5.131  18.105 1.00 59.09  ?  222 PHE   B CG  1 
ATOM   3777 C  CD1 . PHE   B 1 215 ? 24.146  -4.908  18.163 1.00 71.07  ?  222 PHE   B CD1 1 
ATOM   3778 C  CD2 . PHE   B 1 215 ? 22.024  -5.020  19.270 1.00 61.91  ?  222 PHE   B CD2 1 
ATOM   3779 C  CE1 . PHE   B 1 215 ? 24.771  -4.642  19.369 1.00 71.74  ?  222 PHE   B CE1 1 
ATOM   3780 C  CE2 . PHE   B 1 215 ? 22.645  -4.745  20.481 1.00 68.47  ?  222 PHE   B CE2 1 
ATOM   3781 C  CZ  . PHE   B 1 215 ? 24.026  -4.563  20.535 1.00 70.86  ?  222 PHE   B CZ  1 
ATOM   3782 N  N   . ALA   B 1 216 ? 20.353  -3.830  14.126 1.00 59.85  ?  223 ALA   B N   1 
ATOM   3783 C  CA  . ALA   B 1 216 ? 20.049  -3.776  12.689 1.00 61.09  ?  223 ALA   B CA  1 
ATOM   3784 C  C   . ALA   B 1 216 ? 20.306  -2.412  12.036 1.00 58.79  ?  223 ALA   B C   1 
ATOM   3785 O  O   . ALA   B 1 216 ? 20.515  -2.368  10.826 1.00 57.66  ?  223 ALA   B O   1 
ATOM   3786 C  CB  . ALA   B 1 216 ? 18.620  -4.213  12.437 1.00 61.05  ?  223 ALA   B CB  1 
ATOM   3787 N  N   . ASN   B 1 217 ? 20.261  -1.319  12.802 1.00 58.01  ?  224 ASN   B N   1 
ATOM   3788 C  CA  . ASN   B 1 217 ? 20.340  0.058   12.254 1.00 68.80  ?  224 ASN   B CA  1 
ATOM   3789 C  C   . ASN   B 1 217 ? 19.213  0.393   11.267 1.00 57.89  ?  224 ASN   B C   1 
ATOM   3790 O  O   . ASN   B 1 217 ? 19.430  1.082   10.268 1.00 70.41  ?  224 ASN   B O   1 
ATOM   3791 C  CB  . ASN   B 1 217 ? 21.729  0.344   11.633 1.00 68.66  ?  224 ASN   B CB  1 
ATOM   3792 C  CG  . ASN   B 1 217 ? 22.844  0.163   12.623 1.00 67.47  ?  224 ASN   B CG  1 
ATOM   3793 O  OD1 . ASN   B 1 217 ? 22.755  0.663   13.740 1.00 72.48  ?  224 ASN   B OD1 1 
ATOM   3794 N  ND2 . ASN   B 1 217 ? 23.895  -0.547  12.235 1.00 69.61  ?  224 ASN   B ND2 1 
ATOM   3795 N  N   . LYS   B 1 218 ? 18.018  -0.107  11.579 1.00 63.00  ?  225 LYS   B N   1 
ATOM   3796 C  CA  . LYS   B 1 218 ? 16.791  0.111   10.784 1.00 60.89  ?  225 LYS   B CA  1 
ATOM   3797 C  C   . LYS   B 1 218 ? 15.527  -0.414  11.500 1.00 58.75  ?  225 LYS   B C   1 
ATOM   3798 O  O   . LYS   B 1 218 ? 15.624  -1.141  12.494 1.00 66.10  ?  225 LYS   B O   1 
ATOM   3799 C  CB  . LYS   B 1 218 ? 16.900  -0.552  9.398  1.00 62.40  ?  225 LYS   B CB  1 
ATOM   3800 C  CG  . LYS   B 1 218 ? 17.168  -2.040  9.395  1.00 64.38  ?  225 LYS   B CG  1 
ATOM   3801 C  CD  . LYS   B 1 218 ? 17.350  -2.511  7.970  1.00 72.38  ?  225 LYS   B CD  1 
ATOM   3802 C  CE  . LYS   B 1 218 ? 17.411  -4.022  7.909  1.00 73.41  ?  225 LYS   B CE  1 
ATOM   3803 N  NZ  . LYS   B 1 218 ? 17.419  -4.496  6.498  1.00 81.55  ?  225 LYS   B NZ  1 
ATOM   3804 N  N   . GLU   B 1 219 ? 14.358  -0.074  10.961 1.00 61.29  ?  226 GLU   B N   1 
ATOM   3805 C  CA  . GLU   B 1 219 ? 13.071  -0.612  11.438 1.00 64.07  ?  226 GLU   B CA  1 
ATOM   3806 C  C   . GLU   B 1 219 ? 12.961  -2.092  10.997 1.00 66.52  ?  226 GLU   B C   1 
ATOM   3807 O  O   . GLU   B 1 219 ? 13.484  -2.457  9.942  1.00 69.22  ?  226 GLU   B O   1 
ATOM   3808 C  CB  . GLU   B 1 219 ? 11.882  0.199   10.878 1.00 71.09  ?  226 GLU   B CB  1 
ATOM   3809 C  CG  . GLU   B 1 219 ? 11.863  1.702   11.212 1.00 71.82  ?  226 GLU   B CG  1 
ATOM   3810 C  CD  . GLU   B 1 219 ? 10.653  2.195   12.031 1.00 79.25  ?  226 GLU   B CD  1 
ATOM   3811 O  OE1 . GLU   B 1 219 ? 10.550  1.904   13.254 1.00 62.44  ?  226 GLU   B OE1 1 
ATOM   3812 O  OE2 . GLU   B 1 219 ? 9.810   2.928   11.451 1.00 80.33  ?  226 GLU   B OE2 1 
ATOM   3813 N  N   . PRO   B 1 220 ? 12.287  -2.957  11.793 1.00 69.50  ?  227 PRO   B N   1 
ATOM   3814 C  CA  . PRO   B 1 220 ? 11.996  -4.328  11.336 1.00 62.81  ?  227 PRO   B CA  1 
ATOM   3815 C  C   . PRO   B 1 220 ? 10.950  -4.437  10.218 1.00 64.51  ?  227 PRO   B C   1 
ATOM   3816 O  O   . PRO   B 1 220 ? 10.239  -3.464  9.903  1.00 71.36  ?  227 PRO   B O   1 
ATOM   3817 C  CB  . PRO   B 1 220 ? 11.466  -4.992  12.604 1.00 67.47  ?  227 PRO   B CB  1 
ATOM   3818 C  CG  . PRO   B 1 220 ? 10.795  -3.873  13.320 1.00 68.63  ?  227 PRO   B CG  1 
ATOM   3819 C  CD  . PRO   B 1 220 ? 11.764  -2.744  13.156 1.00 68.48  ?  227 PRO   B CD  1 
ATOM   3820 N  N   . TYR   B 1 221 ? 10.874  -5.641  9.646  1.00 71.94  ?  228 TYR   B N   1 
ATOM   3821 C  CA  . TYR   B 1 221 ? 9.795   -6.072  8.734  1.00 65.20  ?  228 TYR   B CA  1 
ATOM   3822 C  C   . TYR   B 1 221 ? 9.704   -5.282  7.413  1.00 66.06  ?  228 TYR   B C   1 
ATOM   3823 O  O   . TYR   B 1 221 ? 8.608   -5.023  6.895  1.00 73.56  ?  228 TYR   B O   1 
ATOM   3824 C  CB  . TYR   B 1 221 ? 8.443   -6.022  9.444  1.00 64.61  ?  228 TYR   B CB  1 
ATOM   3825 C  CG  . TYR   B 1 221 ? 8.352   -6.686  10.805 1.00 66.25  ?  228 TYR   B CG  1 
ATOM   3826 C  CD1 . TYR   B 1 221 ? 8.508   -8.066  10.948 1.00 75.27  ?  228 TYR   B CD1 1 
ATOM   3827 C  CD2 . TYR   B 1 221 ? 7.983   -5.949  11.940 1.00 65.80  ?  228 TYR   B CD2 1 
ATOM   3828 C  CE1 . TYR   B 1 221 ? 8.360   -8.685  12.190 1.00 71.07  ?  228 TYR   B CE1 1 
ATOM   3829 C  CE2 . TYR   B 1 221 ? 7.829   -6.554  13.183 1.00 65.01  ?  228 TYR   B CE2 1 
ATOM   3830 C  CZ  . TYR   B 1 221 ? 8.030   -7.919  13.309 1.00 67.52  ?  228 TYR   B CZ  1 
ATOM   3831 O  OH  . TYR   B 1 221 ? 7.866   -8.503  14.544 1.00 70.06  ?  228 TYR   B OH  1 
ATOM   3832 N  N   . GLU   B 1 222 ? 10.862  -4.909  6.873  1.00 65.05  ?  229 GLU   B N   1 
ATOM   3833 C  CA  . GLU   B 1 222 ? 10.968  -4.172  5.602  1.00 62.15  ?  229 GLU   B CA  1 
ATOM   3834 C  C   . GLU   B 1 222 ? 10.210  -4.815  4.426  1.00 70.32  ?  229 GLU   B C   1 
ATOM   3835 O  O   . GLU   B 1 222 ? 9.615   -4.091  3.620  1.00 66.86  ?  229 GLU   B O   1 
ATOM   3836 C  CB  . GLU   B 1 222 ? 12.443  -3.957  5.223  1.00 64.11  ?  229 GLU   B CB  1 
ATOM   3837 C  CG  . GLU   B 1 222 ? 13.212  -5.236  4.844  1.00 72.65  ?  229 GLU   B CG  1 
ATOM   3838 C  CD  . GLU   B 1 222 ? 14.711  -5.058  4.621  1.00 78.72  ?  229 GLU   B CD  1 
ATOM   3839 O  OE1 . GLU   B 1 222 ? 15.371  -6.083  4.334  1.00 83.36  ?  229 GLU   B OE1 1 
ATOM   3840 O  OE2 . GLU   B 1 222 ? 15.256  -3.930  4.735  1.00 91.31  ?  229 GLU   B OE2 1 
ATOM   3841 N  N   . ASN   B 1 223 ? 10.223  -6.158  4.353  1.00 65.31  ?  230 ASN   B N   1 
ATOM   3842 C  CA  . ASN   B 1 223 ? 9.560   -6.923  3.278  1.00 67.62  ?  230 ASN   B CA  1 
ATOM   3843 C  C   . ASN   B 1 223 ? 8.044   -7.130  3.384  1.00 66.41  ?  230 ASN   B C   1 
ATOM   3844 O  O   . ASN   B 1 223 ? 7.438   -7.607  2.407  1.00 61.52  ?  230 ASN   B O   1 
ATOM   3845 C  CB  . ASN   B 1 223 ? 10.263  -8.272  3.055  1.00 65.99  ?  230 ASN   B CB  1 
ATOM   3846 C  CG  . ASN   B 1 223 ? 11.699  -8.113  2.546  1.00 73.78  ?  230 ASN   B CG  1 
ATOM   3847 O  OD1 . ASN   B 1 223 ? 12.059  -7.111  1.881  1.00 65.40  ?  230 ASN   B OD1 1 
ATOM   3848 N  ND2 . ASN   B 1 223 ? 12.536  -9.103  2.857  1.00 67.41  ?  230 ASN   B ND2 1 
ATOM   3849 N  N   . ALA   B 1 224 ? 7.424   -6.751  4.508  1.00 64.50  ?  231 ALA   B N   1 
ATOM   3850 C  CA  . ALA   B 1 224 ? 5.948   -6.769  4.615  1.00 70.74  ?  231 ALA   B CA  1 
ATOM   3851 C  C   . ALA   B 1 224 ? 5.304   -5.769  3.626  1.00 72.62  ?  231 ALA   B C   1 
ATOM   3852 O  O   . ALA   B 1 224 ? 5.850   -4.697  3.389  1.00 79.79  ?  231 ALA   B O   1 
ATOM   3853 C  CB  . ALA   B 1 224 ? 5.487   -6.479  6.040  1.00 64.38  ?  231 ALA   B CB  1 
ATOM   3854 N  N   . ILE   B 1 225 ? 4.183   -6.186  3.038  1.00 78.54  ?  232 ILE   B N   1 
ATOM   3855 C  CA  . ILE   B 1 225 ? 3.470   -5.496  1.953  1.00 74.32  ?  232 ILE   B CA  1 
ATOM   3856 C  C   . ILE   B 1 225 ? 2.241   -4.759  2.476  1.00 78.30  ?  232 ILE   B C   1 
ATOM   3857 O  O   . ILE   B 1 225 ? 2.037   -3.581  2.154  1.00 93.60  ?  232 ILE   B O   1 
ATOM   3858 C  CB  . ILE   B 1 225 ? 2.957   -6.498  0.880  1.00 77.29  ?  232 ILE   B CB  1 
ATOM   3859 C  CG1 . ILE   B 1 225 ? 4.014   -7.564  0.501  1.00 79.36  ?  232 ILE   B CG1 1 
ATOM   3860 C  CG2 . ILE   B 1 225 ? 2.464   -5.772  -0.367 1.00 74.36  ?  232 ILE   B CG2 1 
ATOM   3861 C  CD1 . ILE   B 1 225 ? 5.332   -7.004  0.007  1.00 83.84  ?  232 ILE   B CD1 1 
ATOM   3862 N  N   . ALA   B 1 226 ? 1.423   -5.470  3.245  1.00 75.78  ?  233 ALA   B N   1 
ATOM   3863 C  CA  . ALA   B 1 226 ? 0.190   -4.941  3.807  1.00 73.39  ?  233 ALA   B CA  1 
ATOM   3864 C  C   . ALA   B 1 226 ? 0.173   -5.089  5.323  1.00 70.54  ?  233 ALA   B C   1 
ATOM   3865 O  O   . ALA   B 1 226 ? 0.908   -5.898  5.898  1.00 62.28  ?  233 ALA   B O   1 
ATOM   3866 C  CB  . ALA   B 1 226 ? -0.985  -5.665  3.195  1.00 76.80  ?  233 ALA   B CB  1 
ATOM   3867 N  N   . GLU   B 1 227 ? -0.698  -4.299  5.939  1.00 70.48  ?  234 GLU   B N   1 
ATOM   3868 C  CA  . GLU   B 1 227 ? -0.769  -4.126  7.386  1.00 73.11  ?  234 GLU   B CA  1 
ATOM   3869 C  C   . GLU   B 1 227 ? -1.321  -5.376  8.070  1.00 75.04  ?  234 GLU   B C   1 
ATOM   3870 O  O   . GLU   B 1 227 ? -0.723  -5.894  9.026  1.00 73.28  ?  234 GLU   B O   1 
ATOM   3871 C  CB  . GLU   B 1 227 ? -1.653  -2.911  7.702  1.00 75.68  ?  234 GLU   B CB  1 
ATOM   3872 C  CG  . GLU   B 1 227 ? -1.583  -2.416  9.137  1.00 82.45  ?  234 GLU   B CG  1 
ATOM   3873 C  CD  . GLU   B 1 227 ? -2.087  -0.984  9.286  1.00 93.70  ?  234 GLU   B CD  1 
ATOM   3874 O  OE1 . GLU   B 1 227 ? -3.203  -0.790  9.826  1.00 104.77 ?  234 GLU   B OE1 1 
ATOM   3875 O  OE2 . GLU   B 1 227 ? -1.372  -0.053  8.844  1.00 80.07  ?  234 GLU   B OE2 1 
ATOM   3876 N  N   . GLN   B 1 228 ? -2.441  -5.867  7.535  1.00 77.77  ?  235 GLN   B N   1 
ATOM   3877 C  CA  . GLN   B 1 228 ? -3.046  -7.130  7.951  1.00 77.12  ?  235 GLN   B CA  1 
ATOM   3878 C  C   . GLN   B 1 228 ? -2.170  -8.362  7.742  1.00 73.87  ?  235 GLN   B C   1 
ATOM   3879 O  O   . GLN   B 1 228 ? -2.247  -9.300  8.542  1.00 74.43  ?  235 GLN   B O   1 
ATOM   3880 C  CB  . GLN   B 1 228 ? -4.415  -7.326  7.263  1.00 81.54  ?  235 GLN   B CB  1 
ATOM   3881 C  CG  . GLN   B 1 228 ? -5.495  -6.370  7.749  1.00 89.44  ?  235 GLN   B CG  1 
ATOM   3882 C  CD  . GLN   B 1 228 ? -5.708  -6.419  9.262  1.00 95.63  ?  235 GLN   B CD  1 
ATOM   3883 O  OE1 . GLN   B 1 228 ? -5.634  -7.488  9.869  1.00 92.32  ?  235 GLN   B OE1 1 
ATOM   3884 N  NE2 . GLN   B 1 228 ? -5.945  -5.258  9.879  1.00 104.58 ?  235 GLN   B NE2 1 
ATOM   3885 N  N   . GLN   B 1 229 ? -1.359  -8.376  6.682  1.00 70.11  ?  236 GLN   B N   1 
ATOM   3886 C  CA  . GLN   B 1 229 ? -0.327  -9.423  6.495  1.00 74.09  ?  236 GLN   B CA  1 
ATOM   3887 C  C   . GLN   B 1 229 ? 0.618   -9.488  7.697  1.00 73.41  ?  236 GLN   B C   1 
ATOM   3888 O  O   . GLN   B 1 229 ? 0.845   -10.561 8.260  1.00 78.88  ?  236 GLN   B O   1 
ATOM   3889 C  CB  . GLN   B 1 229 ? 0.492   -9.177  5.215  1.00 71.49  ?  236 GLN   B CB  1 
ATOM   3890 C  CG  . GLN   B 1 229 ? 1.623   -10.183 4.929  1.00 73.52  ?  236 GLN   B CG  1 
ATOM   3891 C  CD  . GLN   B 1 229 ? 2.847   -9.594  4.229  1.00 72.40  ?  236 GLN   B CD  1 
ATOM   3892 O  OE1 . GLN   B 1 229 ? 2.995   -8.376  4.106  1.00 66.36  ?  236 GLN   B OE1 1 
ATOM   3893 N  NE2 . GLN   B 1 229 ? 3.762   -10.474 3.792  1.00 68.92  ?  236 GLN   B NE2 1 
ATOM   3894 N  N   . LEU   B 1 230 ? 1.140   -8.326  8.067  1.00 72.11  ?  237 LEU   B N   1 
ATOM   3895 C  CA  . LEU   B 1 230 ? 2.071   -8.169  9.173  1.00 73.18  ?  237 LEU   B CA  1 
ATOM   3896 C  C   . LEU   B 1 230 ? 1.468   -8.465  10.539 1.00 64.30  ?  237 LEU   B C   1 
ATOM   3897 O  O   . LEU   B 1 230 ? 2.113   -9.138  11.343 1.00 57.84  ?  237 LEU   B O   1 
ATOM   3898 C  CB  . LEU   B 1 230 ? 2.654   -6.745  9.151  1.00 74.73  ?  237 LEU   B CB  1 
ATOM   3899 C  CG  . LEU   B 1 230 ? 3.713   -6.375  10.174 1.00 74.85  ?  237 LEU   B CG  1 
ATOM   3900 C  CD1 . LEU   B 1 230 ? 4.945   -7.259  10.047 1.00 75.72  ?  237 LEU   B CD1 1 
ATOM   3901 C  CD2 . LEU   B 1 230 ? 4.073   -4.917  9.983  1.00 71.04  ?  237 LEU   B CD2 1 
ATOM   3902 N  N   . ILE   B 1 231 ? 0.266   -7.937  10.797 1.00 65.80  ?  238 ILE   B N   1 
ATOM   3903 C  CA  . ILE   B 1 231 ? -0.442  -8.137  12.083 1.00 67.86  ?  238 ILE   B CA  1 
ATOM   3904 C  C   . ILE   B 1 231 ? -0.615  -9.622  12.352 1.00 70.61  ?  238 ILE   B C   1 
ATOM   3905 O  O   . ILE   B 1 231 ? -0.188  -10.116 13.398 1.00 81.78  ?  238 ILE   B O   1 
ATOM   3906 C  CB  . ILE   B 1 231 ? -1.834  -7.433  12.110 1.00 72.33  ?  238 ILE   B CB  1 
ATOM   3907 C  CG1 . ILE   B 1 231 ? -1.669  -5.910  12.189 1.00 73.73  ?  238 ILE   B CG1 1 
ATOM   3908 C  CG2 . ILE   B 1 231 ? -2.720  -7.926  13.264 1.00 74.31  ?  238 ILE   B CG2 1 
ATOM   3909 C  CD1 . ILE   B 1 231 ? -2.862  -5.157  11.640 1.00 77.85  ?  238 ILE   B CD1 1 
ATOM   3910 N  N   . MET   B 1 232 ? -1.239  -10.305 11.394 1.00 74.47  ?  239 MET   B N   1 
ATOM   3911 C  CA  . MET   B 1 232 ? -1.498  -11.747 11.489 1.00 76.67  ?  239 MET   B CA  1 
ATOM   3912 C  C   . MET   B 1 232 ? -0.225  -12.576 11.546 1.00 72.50  ?  239 MET   B C   1 
ATOM   3913 O  O   . MET   B 1 232 ? -0.185  -13.523 12.326 1.00 71.85  ?  239 MET   B O   1 
ATOM   3914 C  CB  . MET   B 1 232 ? -2.458  -12.251 10.393 1.00 80.27  ?  239 MET   B CB  1 
ATOM   3915 C  CG  . MET   B 1 232 ? -3.790  -12.764 10.958 1.00 96.91  ?  239 MET   B CG  1 
ATOM   3916 S  SD  . MET   B 1 232 ? -4.851  -11.571 11.806 1.00 99.80  ?  239 MET   B SD  1 
ATOM   3917 C  CE  . MET   B 1 232 ? -5.352  -10.550 10.423 1.00 102.70 ?  239 MET   B CE  1 
ATOM   3918 N  N   . ALA   B 1 233 ? 0.805   -12.179 10.786 1.00 65.88  ?  240 ALA   B N   1 
ATOM   3919 C  CA  . ALA   B 1 233 ? 2.130   -12.816 10.868 1.00 65.92  ?  240 ALA   B CA  1 
ATOM   3920 C  C   . ALA   B 1 233 ? 2.715   -12.749 12.262 1.00 68.13  ?  240 ALA   B C   1 
ATOM   3921 O  O   . ALA   B 1 233 ? 3.127   -13.783 12.801 1.00 76.80  ?  240 ALA   B O   1 
ATOM   3922 C  CB  . ALA   B 1 233 ? 3.106   -12.205 9.874  1.00 66.17  ?  240 ALA   B CB  1 
ATOM   3923 N  N   . ILE   B 1 234 ? 2.695   -11.552 12.855 1.00 73.18  ?  241 ILE   B N   1 
ATOM   3924 C  CA  . ILE   B 1 234 ? 3.245   -11.357 14.209 1.00 72.41  ?  241 ILE   B CA  1 
ATOM   3925 C  C   . ILE   B 1 234 ? 2.435   -12.139 15.266 1.00 70.83  ?  241 ILE   B C   1 
ATOM   3926 O  O   . ILE   B 1 234 ? 3.036   -12.802 16.128 1.00 64.83  ?  241 ILE   B O   1 
ATOM   3927 C  CB  . ILE   B 1 234 ? 3.413   -9.863  14.581 1.00 65.93  ?  241 ILE   B CB  1 
ATOM   3928 C  CG1 . ILE   B 1 234 ? 4.427   -9.185  13.639 1.00 68.73  ?  241 ILE   B CG1 1 
ATOM   3929 C  CG2 . ILE   B 1 234 ? 3.914   -9.693  16.021 1.00 64.16  ?  241 ILE   B CG2 1 
ATOM   3930 C  CD1 . ILE   B 1 234 ? 4.210   -7.689  13.508 1.00 73.73  ?  241 ILE   B CD1 1 
ATOM   3931 N  N   . LYS   B 1 235 ? 1.099   -12.077 15.175 1.00 70.31  ?  242 LYS   B N   1 
ATOM   3932 C  CA  . LYS   B 1 235 ? 0.215   -12.845 16.072 1.00 71.87  ?  242 LYS   B CA  1 
ATOM   3933 C  C   . LYS   B 1 235 ? 0.428   -14.358 16.012 1.00 67.86  ?  242 LYS   B C   1 
ATOM   3934 O  O   . LYS   B 1 235 ? 0.297   -15.020 17.036 1.00 74.18  ?  242 LYS   B O   1 
ATOM   3935 C  CB  . LYS   B 1 235 ? -1.265  -12.513 15.828 1.00 74.00  ?  242 LYS   B CB  1 
ATOM   3936 C  CG  . LYS   B 1 235 ? -1.652  -11.140 16.352 1.00 76.32  ?  242 LYS   B CG  1 
ATOM   3937 C  CD  . LYS   B 1 235 ? -3.123  -10.837 16.135 1.00 80.95  ?  242 LYS   B CD  1 
ATOM   3938 C  CE  . LYS   B 1 235 ? -4.006  -11.433 17.232 1.00 83.52  ?  242 LYS   B CE  1 
ATOM   3939 N  NZ  . LYS   B 1 235 ? -3.899  -10.768 18.568 1.00 81.19  ?  242 LYS   B NZ  1 
ATOM   3940 N  N   . SER   B 1 236 ? 0.795   -14.871 14.836 1.00 71.26  ?  243 SER   B N   1 
ATOM   3941 C  CA  . SER   B 1 236 ? 1.137   -16.288 14.631 1.00 82.43  ?  243 SER   B CA  1 
ATOM   3942 C  C   . SER   B 1 236 ? 2.646   -16.607 14.746 1.00 79.15  ?  243 SER   B C   1 
ATOM   3943 O  O   . SER   B 1 236 ? 3.108   -17.562 14.113 1.00 94.49  ?  243 SER   B O   1 
ATOM   3944 C  CB  . SER   B 1 236 ? 0.611   -16.736 13.261 1.00 84.85  ?  243 SER   B CB  1 
ATOM   3945 O  OG  . SER   B 1 236 ? 1.446   -16.225 12.234 1.00 89.41  ?  243 SER   B OG  1 
ATOM   3946 N  N   . GLY   B 1 237 ? 3.400   -15.832 15.523 1.00 77.50  ?  244 GLY   B N   1 
ATOM   3947 C  CA  . GLY   B 1 237 ? 4.810   -16.133 15.829 1.00 78.23  ?  244 GLY   B CA  1 
ATOM   3948 C  C   . GLY   B 1 237 ? 5.941   -15.394 15.119 1.00 75.43  ?  244 GLY   B C   1 
ATOM   3949 O  O   . GLY   B 1 237 ? 7.081   -15.495 15.579 1.00 71.54  ?  244 GLY   B O   1 
ATOM   3950 N  N   . ASN   B 1 238 ? 5.668   -14.681 14.020 1.00 78.18  ?  245 ASN   B N   1 
ATOM   3951 C  CA  . ASN   B 1 238 ? 6.744   -13.998 13.246 1.00 81.94  ?  245 ASN   B CA  1 
ATOM   3952 C  C   . ASN   B 1 238 ? 7.325   -12.815 14.024 1.00 73.46  ?  245 ASN   B C   1 
ATOM   3953 O  O   . ASN   B 1 238 ? 6.599   -12.076 14.699 1.00 70.93  ?  245 ASN   B O   1 
ATOM   3954 C  CB  . ASN   B 1 238 ? 6.316   -13.549 11.821 1.00 83.57  ?  245 ASN   B CB  1 
ATOM   3955 C  CG  . ASN   B 1 238 ? 6.730   -14.536 10.751 1.00 90.94  ?  245 ASN   B CG  1 
ATOM   3956 O  OD1 . ASN   B 1 238 ? 6.355   -15.709 10.810 1.00 92.11  ?  245 ASN   B OD1 1 
ATOM   3957 N  ND2 . ASN   B 1 238 ? 7.518   -14.077 9.773  1.00 88.32  ?  245 ASN   B ND2 1 
ATOM   3958 N  N   . ARG   B 1 239 ? 8.643   -12.694 13.937 1.00 72.59  ?  246 ARG   B N   1 
ATOM   3959 C  CA  . ARG   B 1 239 ? 9.433   -11.706 14.671 1.00 71.54  ?  246 ARG   B CA  1 
ATOM   3960 C  C   . ARG   B 1 239 ? 10.399  -11.026 13.715 1.00 65.47  ?  246 ARG   B C   1 
ATOM   3961 O  O   . ARG   B 1 239 ? 10.472  -11.417 12.549 1.00 68.27  ?  246 ARG   B O   1 
ATOM   3962 C  CB  . ARG   B 1 239 ? 10.179  -12.420 15.810 1.00 69.06  ?  246 ARG   B CB  1 
ATOM   3963 C  CG  . ARG   B 1 239 ? 9.270   -13.106 16.849 1.00 66.36  ?  246 ARG   B CG  1 
ATOM   3964 C  CD  . ARG   B 1 239 ? 8.458   -12.090 17.622 1.00 63.45  ?  246 ARG   B CD  1 
ATOM   3965 N  NE  . ARG   B 1 239 ? 7.671   -12.668 18.700 1.00 62.44  ?  246 ARG   B NE  1 
ATOM   3966 C  CZ  . ARG   B 1 239 ? 6.415   -13.099 18.625 1.00 61.45  ?  246 ARG   B CZ  1 
ATOM   3967 N  NH1 . ARG   B 1 239 ? 5.712   -13.106 17.478 1.00 67.33  ?  246 ARG   B NH1 1 
ATOM   3968 N  NH2 . ARG   B 1 239 ? 5.843   -13.550 19.736 1.00 66.69  ?  246 ARG   B NH2 1 
ATOM   3969 N  N   . PRO   B 1 240 ? 11.135  -9.991  14.178 1.00 66.31  ?  247 PRO   B N   1 
ATOM   3970 C  CA  . PRO   B 1 240 ? 12.206  -9.433  13.331 1.00 62.73  ?  247 PRO   B CA  1 
ATOM   3971 C  C   . PRO   B 1 240 ? 13.258  -10.475 12.912 1.00 69.12  ?  247 PRO   B C   1 
ATOM   3972 O  O   . PRO   B 1 240 ? 13.553  -11.388 13.687 1.00 65.75  ?  247 PRO   B O   1 
ATOM   3973 C  CB  . PRO   B 1 240 ? 12.815  -8.359  14.215 1.00 58.13  ?  247 PRO   B CB  1 
ATOM   3974 C  CG  . PRO   B 1 240 ? 11.676  -7.897  15.067 1.00 60.41  ?  247 PRO   B CG  1 
ATOM   3975 C  CD  . PRO   B 1 240 ? 10.929  -9.162  15.383 1.00 65.89  ?  247 PRO   B CD  1 
ATOM   3976 N  N   . ASP   B 1 241 ? 13.786  -10.346 11.692 1.00 73.46  ?  248 ASP   B N   1 
ATOM   3977 C  CA  . ASP   B 1 241 ? 14.708  -11.359 11.130 1.00 74.12  ?  248 ASP   B CA  1 
ATOM   3978 C  C   . ASP   B 1 241 ? 16.090  -11.188 11.774 1.00 76.22  ?  248 ASP   B C   1 
ATOM   3979 O  O   . ASP   B 1 241 ? 16.771  -10.174 11.554 1.00 66.57  ?  248 ASP   B O   1 
ATOM   3980 C  CB  . ASP   B 1 241 ? 14.807  -11.253 9.600  1.00 77.90  ?  248 ASP   B CB  1 
ATOM   3981 C  CG  . ASP   B 1 241 ? 15.737  -12.310 8.981  1.00 76.09  ?  248 ASP   B CG  1 
ATOM   3982 O  OD1 . ASP   B 1 241 ? 15.826  -13.435 9.524  1.00 77.64  ?  248 ASP   B OD1 1 
ATOM   3983 O  OD2 . ASP   B 1 241 ? 16.394  -11.994 7.969  1.00 71.22  ?  248 ASP   B OD2 1 
ATOM   3984 N  N   . VAL   B 1 242 ? 16.479  -12.192 12.554 1.00 71.98  ?  249 VAL   B N   1 
ATOM   3985 C  CA  . VAL   B 1 242 ? 17.729  -12.175 13.309 1.00 73.69  ?  249 VAL   B CA  1 
ATOM   3986 C  C   . VAL   B 1 242 ? 18.954  -12.296 12.375 1.00 72.63  ?  249 VAL   B C   1 
ATOM   3987 O  O   . VAL   B 1 242 ? 19.993  -11.725 12.687 1.00 68.12  ?  249 VAL   B O   1 
ATOM   3988 C  CB  . VAL   B 1 242 ? 17.712  -13.251 14.435 1.00 78.32  ?  249 VAL   B CB  1 
ATOM   3989 C  CG1 . VAL   B 1 242 ? 19.032  -13.300 15.208 1.00 80.03  ?  249 VAL   B CG1 1 
ATOM   3990 C  CG2 . VAL   B 1 242 ? 16.561  -12.970 15.403 1.00 77.86  ?  249 VAL   B CG2 1 
ATOM   3991 N  N   . ASP   B 1 243 ? 18.812  -12.993 11.241 1.00 77.21  ?  250 ASP   B N   1 
ATOM   3992 C  CA  . ASP   B 1 243 ? 19.881  -13.087 10.224 1.00 87.09  ?  250 ASP   B CA  1 
ATOM   3993 C  C   . ASP   B 1 243 ? 20.165  -11.776 9.457  1.00 87.00  ?  250 ASP   B C   1 
ATOM   3994 O  O   . ASP   B 1 243 ? 21.251  -11.616 8.891  1.00 88.85  ?  250 ASP   B O   1 
ATOM   3995 C  CB  . ASP   B 1 243 ? 19.587  -14.226 9.226  1.00 89.86  ?  250 ASP   B CB  1 
ATOM   3996 C  CG  . ASP   B 1 243 ? 19.548  -15.588 9.888  0.00 90.00  ?  250 ASP   B CG  1 
ATOM   3997 O  OD1 . ASP   B 1 243 ? 20.435  -15.904 10.710 0.00 90.35  ?  250 ASP   B OD1 1 
ATOM   3998 O  OD2 . ASP   B 1 243 ? 18.617  -16.361 9.573  0.00 90.29  ?  250 ASP   B OD2 1 
ATOM   3999 N  N   . ASP   B 1 244 ? 19.194  -10.862 9.449  1.00 97.54  ?  251 ASP   B N   1 
ATOM   4000 C  CA  . ASP   B 1 244 ? 19.359  -9.501  8.910  1.00 87.28  ?  251 ASP   B CA  1 
ATOM   4001 C  C   . ASP   B 1 244 ? 20.272  -8.582  9.765  1.00 84.42  ?  251 ASP   B C   1 
ATOM   4002 O  O   . ASP   B 1 244 ? 20.604  -7.470  9.333  1.00 83.88  ?  251 ASP   B O   1 
ATOM   4003 C  CB  . ASP   B 1 244 ? 17.964  -8.876  8.746  1.00 80.24  ?  251 ASP   B CB  1 
ATOM   4004 C  CG  . ASP   B 1 244 ? 17.878  -7.811  7.672  1.00 89.98  ?  251 ASP   B CG  1 
ATOM   4005 O  OD1 . ASP   B 1 244 ? 18.688  -7.755  6.713  1.00 93.99  ?  251 ASP   B OD1 1 
ATOM   4006 O  OD2 . ASP   B 1 244 ? 16.917  -7.021  7.783  1.00 78.13  ?  251 ASP   B OD2 1 
ATOM   4007 N  N   . ILE   B 1 245 ? 20.623  -9.000  10.988 1.00 84.93  ?  252 ILE   B N   1 
ATOM   4008 C  CA  . ILE   B 1 245 ? 21.702  -8.372  11.773 1.00 82.63  ?  252 ILE   B CA  1 
ATOM   4009 C  C   . ILE   B 1 245 ? 23.051  -8.678  11.094 1.00 93.17  ?  252 ILE   B C   1 
ATOM   4010 O  O   . ILE   B 1 245 ? 23.586  -9.787  11.246 1.00 90.43  ?  252 ILE   B O   1 
ATOM   4011 C  CB  . ILE   B 1 245 ? 21.681  -8.814  13.271 1.00 77.36  ?  252 ILE   B CB  1 
ATOM   4012 C  CG1 . ILE   B 1 245 ? 20.403  -8.284  13.952 1.00 73.86  ?  252 ILE   B CG1 1 
ATOM   4013 C  CG2 . ILE   B 1 245 ? 22.899  -8.269  14.029 1.00 79.05  ?  252 ILE   B CG2 1 
ATOM   4014 C  CD1 . ILE   B 1 245 ? 20.037  -8.953  15.262 1.00 75.91  ?  252 ILE   B CD1 1 
ATOM   4015 N  N   . THR   B 1 246 ? 23.569  -7.685  10.360 1.00 97.40  ?  253 THR   B N   1 
ATOM   4016 C  CA  . THR   B 1 246 ? 24.843  -7.779  9.613  1.00 101.48 ?  253 THR   B CA  1 
ATOM   4017 C  C   . THR   B 1 246 ? 26.031  -7.720  10.573 1.00 102.48 ?  253 THR   B C   1 
ATOM   4018 O  O   . THR   B 1 246 ? 26.883  -8.617  10.581 1.00 119.05 ?  253 THR   B O   1 
ATOM   4019 C  CB  . THR   B 1 246 ? 24.993  -6.623  8.574  1.00 106.39 ?  253 THR   B CB  1 
ATOM   4020 O  OG1 . THR   B 1 246 ? 23.805  -6.513  7.778  1.00 106.91 ?  253 THR   B OG1 1 
ATOM   4021 C  CG2 . THR   B 1 246 ? 26.192  -6.845  7.639  1.00 115.43 ?  253 THR   B CG2 1 
ATOM   4022 N  N   . GLU   B 1 247 ? 26.061  -6.652  11.375 1.00 102.21 ?  254 GLU   B N   1 
ATOM   4023 C  CA  . GLU   B 1 247 ? 27.178  -6.342  12.293 1.00 90.93  ?  254 GLU   B CA  1 
ATOM   4024 C  C   . GLU   B 1 247 ? 27.135  -7.227  13.538 1.00 89.98  ?  254 GLU   B C   1 
ATOM   4025 O  O   . GLU   B 1 247 ? 26.113  -7.846  13.795 1.00 92.27  ?  254 GLU   B O   1 
ATOM   4026 C  CB  . GLU   B 1 247 ? 27.199  -4.842  12.671 1.00 87.03  ?  254 GLU   B CB  1 
ATOM   4027 C  CG  . GLU   B 1 247 ? 25.986  -4.300  13.432 1.00 88.15  ?  254 GLU   B CG  1 
ATOM   4028 C  CD  . GLU   B 1 247 ? 26.231  -2.945  14.064 1.00 81.20  ?  254 GLU   B CD  1 
ATOM   4029 O  OE1 . GLU   B 1 247 ? 26.154  -2.849  15.308 1.00 76.12  ?  254 GLU   B OE1 1 
ATOM   4030 O  OE2 . GLU   B 1 247 ? 26.485  -1.970  13.326 1.00 79.37  ?  254 GLU   B OE2 1 
ATOM   4031 N  N   . TYR   B 1 248 ? 28.251  -7.271  14.268 1.00 86.24  ?  255 TYR   B N   1 
ATOM   4032 C  CA  . TYR   B 1 248 ? 28.403  -8.073  15.477 1.00 84.29  ?  255 TYR   B CA  1 
ATOM   4033 C  C   . TYR   B 1 248 ? 27.440  -7.646  16.592 1.00 77.28  ?  255 TYR   B C   1 
ATOM   4034 O  O   . TYR   B 1 248 ? 27.640  -6.612  17.232 1.00 83.26  ?  255 TYR   B O   1 
ATOM   4035 C  CB  . TYR   B 1 248 ? 29.863  -8.010  15.970 1.00 91.51  ?  255 TYR   B CB  1 
ATOM   4036 C  CG  . TYR   B 1 248 ? 30.141  -8.835  17.207 1.00 98.29  ?  255 TYR   B CG  1 
ATOM   4037 C  CD1 . TYR   B 1 248 ? 30.024  -10.234 17.183 1.00 105.48 ?  255 TYR   B CD1 1 
ATOM   4038 C  CD2 . TYR   B 1 248 ? 30.492  -8.221  18.419 1.00 97.46  ?  255 TYR   B CD2 1 
ATOM   4039 C  CE1 . TYR   B 1 248 ? 30.264  -10.998 18.330 1.00 104.05 ?  255 TYR   B CE1 1 
ATOM   4040 C  CE2 . TYR   B 1 248 ? 30.737  -8.973  19.568 1.00 100.12 ?  255 TYR   B CE2 1 
ATOM   4041 C  CZ  . TYR   B 1 248 ? 30.622  -10.358 19.525 1.00 101.80 ?  255 TYR   B CZ  1 
ATOM   4042 O  OH  . TYR   B 1 248 ? 30.859  -11.081 20.667 1.00 98.19  ?  255 TYR   B OH  1 
ATOM   4043 N  N   . CYS   B 1 249 ? 26.355  -8.410  16.726 1.00 76.84  ?  256 CYS   B N   1 
ATOM   4044 C  CA  . CYS   B 1 249 ? 25.536  -8.440  17.939 1.00 73.16  ?  256 CYS   B CA  1 
ATOM   4045 C  C   . CYS   B 1 249 ? 25.971  -9.662  18.729 1.00 76.81  ?  256 CYS   B C   1 
ATOM   4046 O  O   . CYS   B 1 249 ? 25.968  -10.761 18.172 1.00 83.71  ?  256 CYS   B O   1 
ATOM   4047 C  CB  . CYS   B 1 249 ? 24.057  -8.570  17.611 1.00 76.20  ?  256 CYS   B CB  1 
ATOM   4048 S  SG  . CYS   B 1 249 ? 22.989  -8.483  19.073 1.00 81.62  ?  256 CYS   B SG  1 
ATOM   4049 N  N   . PRO   B 1 250 ? 26.344  -9.498  20.021 1.00 80.14  ?  257 PRO   B N   1 
ATOM   4050 C  CA  . PRO   B 1 250 ? 26.678  -10.656 20.863 1.00 77.18  ?  257 PRO   B CA  1 
ATOM   4051 C  C   . PRO   B 1 250 ? 25.570  -11.694 20.980 1.00 84.63  ?  257 PRO   B C   1 
ATOM   4052 O  O   . PRO   B 1 250 ? 24.402  -11.370 20.777 1.00 97.28  ?  257 PRO   B O   1 
ATOM   4053 C  CB  . PRO   B 1 250 ? 26.939  -10.024 22.226 1.00 78.55  ?  257 PRO   B CB  1 
ATOM   4054 C  CG  . PRO   B 1 250 ? 27.491  -8.695  21.891 1.00 79.22  ?  257 PRO   B CG  1 
ATOM   4055 C  CD  . PRO   B 1 250 ? 26.656  -8.242  20.728 1.00 81.53  ?  257 PRO   B CD  1 
ATOM   4056 N  N   . ARG   B 1 251 ? 25.963  -12.927 21.299 1.00 89.06  ?  258 ARG   B N   1 
ATOM   4057 C  CA  . ARG   B 1 251 ? 25.036  -14.049 21.514 1.00 91.47  ?  258 ARG   B CA  1 
ATOM   4058 C  C   . ARG   B 1 251 ? 24.021  -13.769 22.623 1.00 85.80  ?  258 ARG   B C   1 
ATOM   4059 O  O   . ARG   B 1 251 ? 22.847  -14.071 22.460 1.00 93.79  ?  258 ARG   B O   1 
ATOM   4060 C  CB  . ARG   B 1 251 ? 25.800  -15.337 21.840 1.00 99.76  ?  258 ARG   B CB  1 
ATOM   4061 C  CG  . ARG   B 1 251 ? 26.610  -15.892 20.675 1.00 115.04 ?  258 ARG   B CG  1 
ATOM   4062 C  CD  . ARG   B 1 251 ? 27.387  -17.145 21.063 1.00 125.43 ?  258 ARG   B CD  1 
ATOM   4063 N  NE  . ARG   B 1 251 ? 28.208  -17.652 19.964 1.00 134.78 ?  258 ARG   B NE  1 
ATOM   4064 C  CZ  . ARG   B 1 251 ? 28.967  -18.747 19.898 0.00 147.35 ?  258 ARG   B CZ  1 
ATOM   4065 N  NH1 . ARG   B 1 251 ? 29.098  -19.535 20.968 0.00 149.08 ?  258 ARG   B NH1 1 
ATOM   4066 N  NH2 . ARG   B 1 251 ? 29.642  -19.072 18.798 0.00 149.30 ?  258 ARG   B NH2 1 
ATOM   4067 N  N   . GLU   B 1 252 ? 24.478  -13.156 23.717 1.00 82.99  ?  259 GLU   B N   1 
ATOM   4068 C  CA  . GLU   B 1 252 ? 23.652  -12.879 24.901 1.00 79.87  ?  259 GLU   B CA  1 
ATOM   4069 C  C   . GLU   B 1 252 ? 22.528  -11.869 24.681 1.00 76.09  ?  259 GLU   B C   1 
ATOM   4070 O  O   . GLU   B 1 252 ? 21.449  -12.012 25.264 1.00 77.79  ?  259 GLU   B O   1 
ATOM   4071 C  CB  . GLU   B 1 252 ? 24.531  -12.374 26.060 1.00 79.69  ?  259 GLU   B CB  1 
ATOM   4072 C  CG  . GLU   B 1 252 ? 25.485  -13.424 26.631 1.00 86.31  ?  259 GLU   B CG  1 
ATOM   4073 C  CD  . GLU   B 1 252 ? 26.882  -13.443 26.018 1.00 83.05  ?  259 GLU   B CD  1 
ATOM   4074 O  OE1 . GLU   B 1 252 ? 27.836  -13.743 26.765 1.00 84.87  ?  259 GLU   B OE1 1 
ATOM   4075 O  OE2 . GLU   B 1 252 ? 27.060  -13.135 24.822 1.00 74.73  ?  259 GLU   B OE2 1 
ATOM   4076 N  N   . ILE   B 1 253 ? 22.794  -10.871 23.842 1.00 71.47  ?  260 ILE   B N   1 
ATOM   4077 C  CA  . ILE   B 1 253 ? 21.769  -9.880  23.451 1.00 71.93  ?  260 ILE   B CA  1 
ATOM   4078 C  C   . ILE   B 1 253 ? 20.716  -10.471 22.486 1.00 63.47  ?  260 ILE   B C   1 
ATOM   4079 O  O   . ILE   B 1 253 ? 19.544  -10.109 22.573 1.00 66.63  ?  260 ILE   B O   1 
ATOM   4080 C  CB  . ILE   B 1 253 ? 22.417  -8.574  22.914 1.00 68.10  ?  260 ILE   B CB  1 
ATOM   4081 C  CG1 . ILE   B 1 253 ? 23.105  -7.833  24.066 1.00 68.17  ?  260 ILE   B CG1 1 
ATOM   4082 C  CG2 . ILE   B 1 253 ? 21.384  -7.632  22.305 1.00 72.02  ?  260 ILE   B CG2 1 
ATOM   4083 C  CD1 . ILE   B 1 253 ? 24.094  -6.757  23.652 1.00 76.81  ?  260 ILE   B CD1 1 
ATOM   4084 N  N   . ILE   B 1 254 ? 21.137  -11.353 21.582 1.00 66.12  ?  261 ILE   B N   1 
ATOM   4085 C  CA  . ILE   B 1 254 ? 20.200  -12.103 20.716 1.00 75.51  ?  261 ILE   B CA  1 
ATOM   4086 C  C   . ILE   B 1 254 ? 19.291  -13.010 21.566 1.00 69.68  ?  261 ILE   B C   1 
ATOM   4087 O  O   . ILE   B 1 254 ? 18.076  -13.044 21.361 1.00 61.68  ?  261 ILE   B O   1 
ATOM   4088 C  CB  . ILE   B 1 254 ? 20.932  -12.879 19.580 1.00 78.00  ?  261 ILE   B CB  1 
ATOM   4089 C  CG1 . ILE   B 1 254 ? 21.505  -11.872 18.565 1.00 82.88  ?  261 ILE   B CG1 1 
ATOM   4090 C  CG2 . ILE   B 1 254 ? 19.993  -13.829 18.829 1.00 83.66  ?  261 ILE   B CG2 1 
ATOM   4091 C  CD1 . ILE   B 1 254 ? 22.598  -12.408 17.665 1.00 93.12  ?  261 ILE   B CD1 1 
ATOM   4092 N  N   . SER   B 1 255 ? 19.893  -13.728 22.510 1.00 67.56  ?  262 SER   B N   1 
ATOM   4093 C  CA  . SER   B 1 255 ? 19.148  -14.518 23.501 1.00 69.00  ?  262 SER   B CA  1 
ATOM   4094 C  C   . SER   B 1 255 ? 18.189  -13.687 24.335 1.00 68.76  ?  262 SER   B C   1 
ATOM   4095 O  O   . SER   B 1 255 ? 17.064  -14.128 24.590 1.00 78.89  ?  262 SER   B O   1 
ATOM   4096 C  CB  . SER   B 1 255 ? 20.098  -15.287 24.418 1.00 68.91  ?  262 SER   B CB  1 
ATOM   4097 O  OG  . SER   B 1 255 ? 20.745  -16.273 23.660 1.00 65.79  ?  262 SER   B OG  1 
ATOM   4098 N  N   . LEU   B 1 256 ? 18.620  -12.486 24.727 1.00 68.46  ?  263 LEU   B N   1 
ATOM   4099 C  CA  . LEU   B 1 256 ? 17.767  -11.576 25.482 1.00 67.90  ?  263 LEU   B CA  1 
ATOM   4100 C  C   . LEU   B 1 256 ? 16.548  -11.087 24.679 1.00 66.26  ?  263 LEU   B C   1 
ATOM   4101 O  O   . LEU   B 1 256 ? 15.449  -11.026 25.238 1.00 59.44  ?  263 LEU   B O   1 
ATOM   4102 C  CB  . LEU   B 1 256 ? 18.567  -10.375 26.047 1.00 69.77  ?  263 LEU   B CB  1 
ATOM   4103 C  CG  . LEU   B 1 256 ? 17.804  -9.332  26.900 1.00 61.82  ?  263 LEU   B CG  1 
ATOM   4104 C  CD1 . LEU   B 1 256 ? 17.109  -10.004 28.080 1.00 68.27  ?  263 LEU   B CD1 1 
ATOM   4105 C  CD2 . LEU   B 1 256 ? 18.694  -8.200  27.395 1.00 63.04  ?  263 LEU   B CD2 1 
ATOM   4106 N  N   . MET   B 1 257 ? 16.731  -10.752 23.395 1.00 65.23  ?  264 MET   B N   1 
ATOM   4107 C  CA  . MET   B 1 257 ? 15.596  -10.256 22.571 1.00 66.84  ?  264 MET   B CA  1 
ATOM   4108 C  C   . MET   B 1 257 ? 14.578  -11.361 22.244 1.00 71.10  ?  264 MET   B C   1 
ATOM   4109 O  O   . MET   B 1 257 ? 13.367  -11.106 22.273 1.00 81.76  ?  264 MET   B O   1 
ATOM   4110 C  CB  . MET   B 1 257 ? 16.058  -9.496  21.309 1.00 67.04  ?  264 MET   B CB  1 
ATOM   4111 C  CG  . MET   B 1 257 ? 16.680  -10.321 20.192 1.00 68.55  ?  264 MET   B CG  1 
ATOM   4112 S  SD  . MET   B 1 257 ? 17.226  -9.372  18.771 1.00 68.52  ?  264 MET   B SD  1 
ATOM   4113 C  CE  . MET   B 1 257 ? 18.645  -8.509  19.444 1.00 70.91  ?  264 MET   B CE  1 
ATOM   4114 N  N   . LYS   B 1 258 ? 15.065  -12.573 21.963 1.00 66.55  ?  265 LYS   B N   1 
ATOM   4115 C  CA  . LYS   B 1 258 ? 14.186  -13.761 21.806 1.00 74.49  ?  265 LYS   B CA  1 
ATOM   4116 C  C   . LYS   B 1 258 ? 13.372  -14.113 23.061 1.00 74.70  ?  265 LYS   B C   1 
ATOM   4117 O  O   . LYS   B 1 258 ? 12.207  -14.511 22.962 1.00 76.12  ?  265 LYS   B O   1 
ATOM   4118 C  CB  . LYS   B 1 258 ? 14.981  -15.003 21.360 1.00 73.83  ?  265 LYS   B CB  1 
ATOM   4119 C  CG  . LYS   B 1 258 ? 15.542  -14.895 19.952 1.00 72.80  ?  265 LYS   B CG  1 
ATOM   4120 C  CD  . LYS   B 1 258 ? 16.362  -16.116 19.593 1.00 69.60  ?  265 LYS   B CD  1 
ATOM   4121 C  CE  . LYS   B 1 258 ? 16.794  -16.066 18.139 1.00 67.21  ?  265 LYS   B CE  1 
ATOM   4122 N  NZ  . LYS   B 1 258 ? 17.371  -17.364 17.732 1.00 61.89  ?  265 LYS   B NZ  1 
ATOM   4123 N  N   . LEU   B 1 259 ? 14.003  -13.977 24.223 1.00 74.81  ?  266 LEU   B N   1 
ATOM   4124 C  CA  . LEU   B 1 259 ? 13.323  -14.149 25.513 1.00 78.14  ?  266 LEU   B CA  1 
ATOM   4125 C  C   . LEU   B 1 259 ? 12.260  -13.065 25.752 1.00 75.42  ?  266 LEU   B C   1 
ATOM   4126 O  O   . LEU   B 1 259 ? 11.140  -13.359 26.198 1.00 66.19  ?  266 LEU   B O   1 
ATOM   4127 C  CB  . LEU   B 1 259 ? 14.349  -14.143 26.649 1.00 78.36  ?  266 LEU   B CB  1 
ATOM   4128 C  CG  . LEU   B 1 259 ? 13.958  -14.564 28.066 1.00 80.49  ?  266 LEU   B CG  1 
ATOM   4129 C  CD1 . LEU   B 1 259 ? 13.289  -15.932 28.167 1.00 81.76  ?  266 LEU   B CD1 1 
ATOM   4130 C  CD2 . LEU   B 1 259 ? 15.208  -14.523 28.945 1.00 79.95  ?  266 LEU   B CD2 1 
ATOM   4131 N  N   . CYS   B 1 260 ? 12.614  -11.817 25.449 1.00 62.97  ?  267 CYS   B N   1 
ATOM   4132 C  CA  . CYS   B 1 260 ? 11.701  -10.687 25.625 1.00 59.89  ?  267 CYS   B CA  1 
ATOM   4133 C  C   . CYS   B 1 260 ? 10.545  -10.629 24.598 1.00 60.13  ?  267 CYS   B C   1 
ATOM   4134 O  O   . CYS   B 1 260 ? 9.490   -10.097 24.938 1.00 60.92  ?  267 CYS   B O   1 
ATOM   4135 C  CB  . CYS   B 1 260 ? 12.477  -9.375  25.686 1.00 62.72  ?  267 CYS   B CB  1 
ATOM   4136 S  SG  . CYS   B 1 260 ? 13.583  -9.200  27.110 1.00 68.46  ?  267 CYS   B SG  1 
ATOM   4137 N  N   . TRP   B 1 261 ? 10.715  -11.187 23.383 1.00 67.02  ?  268 TRP   B N   1 
ATOM   4138 C  CA  . TRP   B 1 261 ? 9.589   -11.344 22.392 1.00 63.68  ?  268 TRP   B CA  1 
ATOM   4139 C  C   . TRP   B 1 261 ? 8.832   -12.687 22.360 1.00 80.72  ?  268 TRP   B C   1 
ATOM   4140 O  O   . TRP   B 1 261 ? 8.196   -13.040 21.345 1.00 76.80  ?  268 TRP   B O   1 
ATOM   4141 C  CB  . TRP   B 1 261 ? 9.991   -10.895 20.974 1.00 67.87  ?  268 TRP   B CB  1 
ATOM   4142 C  CG  . TRP   B 1 261 ? 10.951  -11.723 20.139 1.00 67.02  ?  268 TRP   B CG  1 
ATOM   4143 C  CD1 . TRP   B 1 261 ? 10.989  -13.098 19.962 1.00 67.51  ?  268 TRP   B CD1 1 
ATOM   4144 C  CD2 . TRP   B 1 261 ? 11.922  -11.190 19.239 1.00 59.96  ?  268 TRP   B CD2 1 
ATOM   4145 N  NE1 . TRP   B 1 261 ? 11.969  -13.433 19.055 1.00 60.04  ?  268 TRP   B NE1 1 
ATOM   4146 C  CE2 . TRP   B 1 261 ? 12.559  -12.285 18.601 1.00 69.11  ?  268 TRP   B CE2 1 
ATOM   4147 C  CE3 . TRP   B 1 261 ? 12.348  -9.889  18.937 1.00 67.76  ?  268 TRP   B CE3 1 
ATOM   4148 C  CZ2 . TRP   B 1 261 ? 13.602  -12.111 17.673 1.00 73.90  ?  268 TRP   B CZ2 1 
ATOM   4149 C  CZ3 . TRP   B 1 261 ? 13.395  -9.717  18.016 1.00 64.28  ?  268 TRP   B CZ3 1 
ATOM   4150 C  CH2 . TRP   B 1 261 ? 13.996  -10.822 17.389 1.00 63.21  ?  268 TRP   B CH2 1 
ATOM   4151 N  N   . GLU   B 1 262 ? 8.875   -13.420 23.471 1.00 84.55  ?  269 GLU   B N   1 
ATOM   4152 C  CA  . GLU   B 1 262 ? 8.039   -14.590 23.667 1.00 75.68  ?  269 GLU   B CA  1 
ATOM   4153 C  C   . GLU   B 1 262 ? 6.562   -14.297 23.423 1.00 76.31  ?  269 GLU   B C   1 
ATOM   4154 O  O   . GLU   B 1 262 ? 6.073   -13.253 23.854 1.00 69.73  ?  269 GLU   B O   1 
ATOM   4155 C  CB  . GLU   B 1 262 ? 8.217   -15.145 25.092 1.00 79.25  ?  269 GLU   B CB  1 
ATOM   4156 C  CG  . GLU   B 1 262 ? 9.467   -15.986 25.276 1.00 80.38  ?  269 GLU   B CG  1 
ATOM   4157 C  CD  . GLU   B 1 262 ? 9.423   -17.301 24.508 1.00 90.03  ?  269 GLU   B CD  1 
ATOM   4158 O  OE1 . GLU   B 1 262 ? 10.454  -17.638 23.904 1.00 99.24  ?  269 GLU   B OE1 1 
ATOM   4159 O  OE2 . GLU   B 1 262 ? 8.360   -17.966 24.465 1.00 85.02  ?  269 GLU   B OE2 1 
ATOM   4160 N  N   . ALA   B 1 263 ? 5.884   -15.227 22.731 1.00 73.77  ?  270 ALA   B N   1 
ATOM   4161 C  CA  . ALA   B 1 263 ? 4.440   -15.150 22.473 1.00 75.99  ?  270 ALA   B CA  1 
ATOM   4162 C  C   . ALA   B 1 263 ? 3.611   -14.984 23.754 1.00 78.26  ?  270 ALA   B C   1 
ATOM   4163 O  O   . ALA   B 1 263 ? 2.769   -14.083 23.815 1.00 75.40  ?  270 ALA   B O   1 
ATOM   4164 C  CB  . ALA   B 1 263 ? 3.972   -16.371 21.700 1.00 76.92  ?  270 ALA   B CB  1 
ATOM   4165 N  N   . ASN   B 1 264 ? 3.922   -15.804 24.766 1.00 74.84  ?  271 ASN   B N   1 
ATOM   4166 C  CA  . ASN   B 1 264 ? 3.251   -15.766 26.095 1.00 84.13  ?  271 ASN   B CA  1 
ATOM   4167 C  C   . ASN   B 1 264 ? 3.934   -14.694 26.946 1.00 83.04  ?  271 ASN   B C   1 
ATOM   4168 O  O   . ASN   B 1 264 ? 5.146   -14.831 27.197 1.00 88.17  ?  271 ASN   B O   1 
ATOM   4169 C  CB  . ASN   B 1 264 ? 3.336   -17.143 26.824 1.00 92.37  ?  271 ASN   B CB  1 
ATOM   4170 C  CG  . ASN   B 1 264 ? 2.675   -17.150 28.231 1.00 94.10  ?  271 ASN   B CG  1 
ATOM   4171 O  OD1 . ASN   B 1 264 ? 1.864   -16.283 28.552 1.00 101.54 ?  271 ASN   B OD1 1 
ATOM   4172 N  ND2 . ASN   B 1 264 ? 3.061   -18.109 29.074 1.00 87.62  ?  271 ASN   B ND2 1 
ATOM   4173 N  N   . PRO   B 1 265 ? 3.173   -13.671 27.434 1.00 81.05  ?  272 PRO   B N   1 
ATOM   4174 C  CA  . PRO   B 1 265 ? 3.709   -12.657 28.345 1.00 83.13  ?  272 PRO   B CA  1 
ATOM   4175 C  C   . PRO   B 1 265 ? 4.433   -13.177 29.573 1.00 85.82  ?  272 PRO   B C   1 
ATOM   4176 O  O   . PRO   B 1 265 ? 5.514   -12.676 29.857 1.00 89.95  ?  272 PRO   B O   1 
ATOM   4177 C  CB  . PRO   B 1 265 ? 2.463   -11.875 28.774 1.00 83.42  ?  272 PRO   B CB  1 
ATOM   4178 C  CG  . PRO   B 1 265 ? 1.594   -11.939 27.583 1.00 84.20  ?  272 PRO   B CG  1 
ATOM   4179 C  CD  . PRO   B 1 265 ? 1.786   -13.326 27.053 1.00 84.28  ?  272 PRO   B CD  1 
ATOM   4180 N  N   . GLU   B 1 266 ? 3.876   -14.183 30.251 1.00 94.35  ?  273 GLU   B N   1 
ATOM   4181 C  CA  . GLU   B 1 266 ? 4.516   -14.711 31.476 1.00 105.91 ?  273 GLU   B CA  1 
ATOM   4182 C  C   . GLU   B 1 266 ? 5.896   -15.378 31.254 1.00 104.09 ?  273 GLU   B C   1 
ATOM   4183 O  O   . GLU   B 1 266 ? 6.734   -15.373 32.168 1.00 109.16 ?  273 GLU   B O   1 
ATOM   4184 C  CB  . GLU   B 1 266 ? 3.575   -15.626 32.256 1.00 127.00 ?  273 GLU   B CB  1 
ATOM   4185 C  CG  . GLU   B 1 266 ? 3.874   -15.695 33.759 1.00 143.49 ?  273 GLU   B CG  1 
ATOM   4186 C  CD  . GLU   B 1 266 ? 3.785   -14.363 34.504 1.00 147.02 ?  273 GLU   B CD  1 
ATOM   4187 O  OE1 . GLU   B 1 266 ? 2.806   -13.611 34.290 1.00 167.44 ?  273 GLU   B OE1 1 
ATOM   4188 O  OE2 . GLU   B 1 266 ? 4.695   -14.078 35.319 1.00 123.35 ?  273 GLU   B OE2 1 
ATOM   4189 N  N   . ALA   B 1 267 ? 6.145   -15.900 30.049 1.00 94.83  ?  274 ALA   B N   1 
ATOM   4190 C  CA  . ALA   B 1 267 ? 7.505   -16.357 29.646 1.00 88.23  ?  274 ALA   B CA  1 
ATOM   4191 C  C   . ALA   B 1 267 ? 8.573   -15.233 29.507 1.00 82.54  ?  274 ALA   B C   1 
ATOM   4192 O  O   . ALA   B 1 267 ? 9.773   -15.506 29.522 1.00 74.06  ?  274 ALA   B O   1 
ATOM   4193 C  CB  . ALA   B 1 267 ? 7.438   -17.162 28.351 1.00 83.84  ?  274 ALA   B CB  1 
ATOM   4194 N  N   . ARG   B 1 268 ? 8.145   -13.983 29.349 1.00 78.01  ?  275 ARG   B N   1 
ATOM   4195 C  CA  . ARG   B 1 268 ? 9.066   -12.856 29.247 1.00 76.74  ?  275 ARG   B CA  1 
ATOM   4196 C  C   . ARG   B 1 268 ? 9.561   -12.486 30.655 1.00 82.25  ?  275 ARG   B C   1 
ATOM   4197 O  O   . ARG   B 1 268 ? 8.790   -12.597 31.615 1.00 77.73  ?  275 ARG   B O   1 
ATOM   4198 C  CB  . ARG   B 1 268 ? 8.391   -11.641 28.599 1.00 73.66  ?  275 ARG   B CB  1 
ATOM   4199 C  CG  . ARG   B 1 268 ? 7.780   -11.897 27.214 1.00 73.88  ?  275 ARG   B CG  1 
ATOM   4200 C  CD  . ARG   B 1 268 ? 6.843   -10.769 26.774 1.00 70.66  ?  275 ARG   B CD  1 
ATOM   4201 N  NE  . ARG   B 1 268 ? 5.967   -11.180 25.667 1.00 70.62  ?  275 ARG   B NE  1 
ATOM   4202 C  CZ  . ARG   B 1 268 ? 4.850   -10.550 25.267 1.00 70.30  ?  275 ARG   B CZ  1 
ATOM   4203 N  NH1 . ARG   B 1 268 ? 4.428   -9.424  25.855 1.00 69.39  ?  275 ARG   B NH1 1 
ATOM   4204 N  NH2 . ARG   B 1 268 ? 4.135   -11.062 24.258 1.00 74.18  ?  275 ARG   B NH2 1 
ATOM   4205 N  N   . PRO   B 1 269 ? 10.828  -12.012 30.787 1.00 81.44  ?  276 PRO   B N   1 
ATOM   4206 C  CA  . PRO   B 1 269 ? 11.288  -11.514 32.082 1.00 79.45  ?  276 PRO   B CA  1 
ATOM   4207 C  C   . PRO   B 1 269 ? 10.691  -10.145 32.375 1.00 74.75  ?  276 PRO   B C   1 
ATOM   4208 O  O   . PRO   B 1 269 ? 10.000  -9.598  31.531 1.00 72.99  ?  276 PRO   B O   1 
ATOM   4209 C  CB  . PRO   B 1 269 ? 12.796  -11.414 31.895 1.00 87.14  ?  276 PRO   B CB  1 
ATOM   4210 C  CG  . PRO   B 1 269 ? 12.984  -11.147 30.453 1.00 84.02  ?  276 PRO   B CG  1 
ATOM   4211 C  CD  . PRO   B 1 269 ? 11.782  -11.666 29.720 1.00 83.85  ?  276 PRO   B CD  1 
ATOM   4212 N  N   . THR   B 1 270 ? 10.915  -9.641  33.580 1.00 83.25  ?  277 THR   B N   1 
ATOM   4213 C  CA  . THR   B 1 270 ? 10.564  -8.249  33.926 1.00 89.25  ?  277 THR   B CA  1 
ATOM   4214 C  C   . THR   B 1 270 ? 11.838  -7.410  33.836 1.00 78.94  ?  277 THR   B C   1 
ATOM   4215 O  O   . THR   B 1 270 ? 12.920  -7.951  33.605 1.00 92.56  ?  277 THR   B O   1 
ATOM   4216 C  CB  . THR   B 1 270 ? 9.816   -8.121  35.275 1.00 99.95  ?  277 THR   B CB  1 
ATOM   4217 O  OG1 . THR   B 1 270 ? 9.566   -6.739  35.555 1.00 129.37 ?  277 THR   B OG1 1 
ATOM   4218 C  CG2 . THR   B 1 270 ? 10.557  -8.763  36.445 1.00 102.46 ?  277 THR   B CG2 1 
ATOM   4219 N  N   . PHE   B 1 271 ? 11.703  -6.098  33.971 1.00 66.33  ?  278 PHE   B N   1 
ATOM   4220 C  CA  . PHE   B 1 271 ? 12.841  -5.184  33.726 1.00 69.82  ?  278 PHE   B CA  1 
ATOM   4221 C  C   . PHE   B 1 271 ? 13.918  -5.199  34.817 1.00 70.34  ?  278 PHE   B C   1 
ATOM   4222 O  O   . PHE   B 1 271 ? 15.084  -4.982  34.503 1.00 83.88  ?  278 PHE   B O   1 
ATOM   4223 C  CB  . PHE   B 1 271 ? 12.384  -3.741  33.431 1.00 62.43  ?  278 PHE   B CB  1 
ATOM   4224 C  CG  . PHE   B 1 271 ? 11.896  -3.535  32.031 1.00 62.96  ?  278 PHE   B CG  1 
ATOM   4225 C  CD1 . PHE   B 1 271 ? 12.794  -3.487  30.966 1.00 65.68  ?  278 PHE   B CD1 1 
ATOM   4226 C  CD2 . PHE   B 1 271 ? 10.533  -3.385  31.765 1.00 69.40  ?  278 PHE   B CD2 1 
ATOM   4227 C  CE1 . PHE   B 1 271 ? 12.340  -3.292  29.661 1.00 69.87  ?  278 PHE   B CE1 1 
ATOM   4228 C  CE2 . PHE   B 1 271 ? 10.072  -3.184  30.466 1.00 67.44  ?  278 PHE   B CE2 1 
ATOM   4229 C  CZ  . PHE   B 1 271 ? 10.977  -3.133  29.409 1.00 59.82  ?  278 PHE   B CZ  1 
ATOM   4230 N  N   . PRO   B 1 272 ? 13.538  -5.389  36.094 1.00 75.81  ?  279 PRO   B N   1 
ATOM   4231 C  CA  . PRO   B 1 272 ? 14.543  -5.687  37.130 1.00 75.25  ?  279 PRO   B CA  1 
ATOM   4232 C  C   . PRO   B 1 272 ? 15.325  -6.977  36.895 1.00 69.02  ?  279 PRO   B C   1 
ATOM   4233 O  O   . PRO   B 1 272 ? 16.529  -7.020  37.137 1.00 86.37  ?  279 PRO   B O   1 
ATOM   4234 C  CB  . PRO   B 1 272 ? 13.695  -5.785  38.394 1.00 74.36  ?  279 PRO   B CB  1 
ATOM   4235 C  CG  . PRO   B 1 272 ? 12.641  -4.752  38.154 1.00 71.72  ?  279 PRO   B CG  1 
ATOM   4236 C  CD  . PRO   B 1 272 ? 12.277  -4.931  36.712 1.00 72.27  ?  279 PRO   B CD  1 
ATOM   4237 N  N   . GLY   B 1 273 ? 14.625  -8.010  36.437 1.00 75.91  ?  280 GLY   B N   1 
ATOM   4238 C  CA  . GLY   B 1 273 ? 15.224  -9.265  35.988 1.00 73.11  ?  280 GLY   B CA  1 
ATOM   4239 C  C   . GLY   B 1 273 ? 16.134  -9.111  34.786 1.00 72.07  ?  280 GLY   B C   1 
ATOM   4240 O  O   . GLY   B 1 273 ? 17.162  -9.773  34.735 1.00 78.84  ?  280 GLY   B O   1 
ATOM   4241 N  N   . ILE   B 1 274 ? 15.760  -8.248  33.827 1.00 72.39  ?  281 ILE   B N   1 
ATOM   4242 C  CA  . ILE   B 1 274 ? 16.636  -7.898  32.691 1.00 70.08  ?  281 ILE   B CA  1 
ATOM   4243 C  C   . ILE   B 1 274 ? 17.897  -7.206  33.210 1.00 67.84  ?  281 ILE   B C   1 
ATOM   4244 O  O   . ILE   B 1 274 ? 18.995  -7.649  32.890 1.00 81.57  ?  281 ILE   B O   1 
ATOM   4245 C  CB  . ILE   B 1 274 ? 15.926  -7.033  31.601 1.00 70.46  ?  281 ILE   B CB  1 
ATOM   4246 C  CG1 . ILE   B 1 274 ? 14.867  -7.863  30.870 1.00 69.09  ?  281 ILE   B CG1 1 
ATOM   4247 C  CG2 . ILE   B 1 274 ? 16.915  -6.494  30.553 1.00 66.01  ?  281 ILE   B CG2 1 
ATOM   4248 C  CD1 . ILE   B 1 274 ? 13.877  -7.049  30.052 1.00 65.27  ?  281 ILE   B CD1 1 
ATOM   4249 N  N   . GLU   B 1 275 ? 17.721  -6.151  34.013 1.00 64.60  ?  282 GLU   B N   1 
ATOM   4250 C  CA  . GLU   B 1 275 ? 18.830  -5.350  34.572 1.00 67.96  ?  282 GLU   B CA  1 
ATOM   4251 C  C   . GLU   B 1 275 ? 19.879  -6.182  35.317 1.00 69.81  ?  282 GLU   B C   1 
ATOM   4252 O  O   . GLU   B 1 275 ? 21.079  -5.978  35.110 1.00 78.55  ?  282 GLU   B O   1 
ATOM   4253 C  CB  . GLU   B 1 275 ? 18.312  -4.245  35.519 1.00 72.95  ?  282 GLU   B CB  1 
ATOM   4254 C  CG  . GLU   B 1 275 ? 19.343  -3.175  35.859 1.00 70.40  ?  282 GLU   B CG  1 
ATOM   4255 C  CD  . GLU   B 1 275 ? 18.841  -2.075  36.796 1.00 80.43  ?  282 GLU   B CD  1 
ATOM   4256 O  OE1 . GLU   B 1 275 ? 19.690  -1.237  37.186 1.00 73.92  ?  282 GLU   B OE1 1 
ATOM   4257 O  OE2 . GLU   B 1 275 ? 17.632  -2.022  37.144 1.00 79.42  ?  282 GLU   B OE2 1 
ATOM   4258 N  N   . GLU   B 1 276 ? 19.413  -7.091  36.178 1.00 73.83  ?  283 GLU   B N   1 
ATOM   4259 C  CA  . GLU   B 1 276 ? 20.285  -8.001  36.950 1.00 78.57  ?  283 GLU   B CA  1 
ATOM   4260 C  C   . GLU   B 1 276 ? 21.192  -8.858  36.054 1.00 76.08  ?  283 GLU   B C   1 
ATOM   4261 O  O   . GLU   B 1 276 ? 22.359  -9.053  36.381 1.00 78.88  ?  283 GLU   B O   1 
ATOM   4262 C  CB  . GLU   B 1 276 ? 19.459  -8.906  37.889 1.00 90.88  ?  283 GLU   B CB  1 
ATOM   4263 C  CG  . GLU   B 1 276 ? 18.944  -8.217  39.150 1.00 96.58  ?  283 GLU   B CG  1 
ATOM   4264 C  CD  . GLU   B 1 276 ? 17.952  -9.042  39.926 0.00 96.24  ?  283 GLU   B CD  1 
ATOM   4265 O  OE1 . GLU   B 1 276 ? 16.920  -9.447  39.348 0.00 96.58  ?  283 GLU   B OE1 1 
ATOM   4266 O  OE2 . GLU   B 1 276 ? 18.191  -9.291  41.127 0.00 98.21  ?  283 GLU   B OE2 1 
ATOM   4267 N  N   . LYS   B 1 277 ? 20.634  -9.351  34.947 1.00 78.15  ?  284 LYS   B N   1 
ATOM   4268 C  CA  . LYS   B 1 277 ? 21.387  -10.077 33.915 1.00 80.81  ?  284 LYS   B CA  1 
ATOM   4269 C  C   . LYS   B 1 277 ? 22.289  -9.155  33.085 1.00 73.83  ?  284 LYS   B C   1 
ATOM   4270 O  O   . LYS   B 1 277 ? 23.479  -9.453  32.867 1.00 69.32  ?  284 LYS   B O   1 
ATOM   4271 C  CB  . LYS   B 1 277 ? 20.430  -10.807 32.955 1.00 91.69  ?  284 LYS   B CB  1 
ATOM   4272 C  CG  . LYS   B 1 277 ? 19.603  -11.918 33.586 1.00 117.26 ?  284 LYS   B CG  1 
ATOM   4273 C  CD  . LYS   B 1 277 ? 18.597  -12.505 32.591 1.00 122.53 ?  284 LYS   B CD  1 
ATOM   4274 C  CE  . LYS   B 1 277 ? 17.775  -13.637 33.199 1.00 119.41 ?  284 LYS   B CE  1 
ATOM   4275 N  NZ  . LYS   B 1 277 ? 16.918  -14.316 32.217 0.00 124.27 ?  284 LYS   B NZ  1 
ATOM   4276 N  N   . PHE   B 1 278 ? 21.700  -8.063  32.596 1.00 62.34  ?  285 PHE   B N   1 
ATOM   4277 C  CA  . PHE   B 1 278 ? 22.336  -7.185  31.608 1.00 62.36  ?  285 PHE   B CA  1 
ATOM   4278 C  C   . PHE   B 1 278 ? 23.475  -6.303  32.124 1.00 59.68  ?  285 PHE   B C   1 
ATOM   4279 O  O   . PHE   B 1 278 ? 24.425  -6.062  31.394 1.00 66.08  ?  285 PHE   B O   1 
ATOM   4280 C  CB  . PHE   B 1 278 ? 21.294  -6.292  30.912 1.00 58.76  ?  285 PHE   B CB  1 
ATOM   4281 C  CG  . PHE   B 1 278 ? 21.819  -5.624  29.682 1.00 63.68  ?  285 PHE   B CG  1 
ATOM   4282 C  CD1 . PHE   B 1 278 ? 21.988  -6.348  28.492 1.00 66.97  ?  285 PHE   B CD1 1 
ATOM   4283 C  CD2 . PHE   B 1 278 ? 22.211  -4.285  29.714 1.00 66.59  ?  285 PHE   B CD2 1 
ATOM   4284 C  CE1 . PHE   B 1 278 ? 22.508  -5.734  27.357 1.00 66.02  ?  285 PHE   B CE1 1 
ATOM   4285 C  CE2 . PHE   B 1 278 ? 22.722  -3.663  28.571 1.00 63.22  ?  285 PHE   B CE2 1 
ATOM   4286 C  CZ  . PHE   B 1 278 ? 22.884  -4.392  27.398 1.00 67.74  ?  285 PHE   B CZ  1 
ATOM   4287 N  N   . ARG   B 1 279 ? 23.343  -5.774  33.339 1.00 62.38  ?  286 ARG   B N   1 
ATOM   4288 C  CA  . ARG   B 1 279 ? 24.308  -4.806  33.876 1.00 57.29  ?  286 ARG   B CA  1 
ATOM   4289 C  C   . ARG   B 1 279 ? 25.714  -5.397  34.036 1.00 58.88  ?  286 ARG   B C   1 
ATOM   4290 O  O   . ARG   B 1 279 ? 26.683  -4.789  33.549 1.00 60.05  ?  286 ARG   B O   1 
ATOM   4291 C  CB  . ARG   B 1 279 ? 23.802  -4.165  35.176 1.00 58.48  ?  286 ARG   B CB  1 
ATOM   4292 C  CG  . ARG   B 1 279 ? 24.745  -3.147  35.819 1.00 57.01  ?  286 ARG   B CG  1 
ATOM   4293 C  CD  . ARG   B 1 279 ? 24.124  -2.566  37.069 1.00 60.48  ?  286 ARG   B CD  1 
ATOM   4294 N  NE  . ARG   B 1 279 ? 22.950  -1.742  36.755 1.00 56.91  ?  286 ARG   B NE  1 
ATOM   4295 C  CZ  . ARG   B 1 279 ? 22.976  -0.473  36.346 1.00 59.94  ?  286 ARG   B CZ  1 
ATOM   4296 N  NH1 . ARG   B 1 279 ? 24.120  0.213   36.193 1.00 67.20  ?  286 ARG   B NH1 1 
ATOM   4297 N  NH2 . ARG   B 1 279 ? 21.825  0.140   36.088 1.00 65.92  ?  286 ARG   B NH2 1 
ATOM   4298 N  N   . PRO   B 1 280 ? 25.840  -6.573  34.696 1.00 64.50  ?  287 PRO   B N   1 
ATOM   4299 C  CA  . PRO   B 1 280 ? 27.158  -7.204  34.726 1.00 61.21  ?  287 PRO   B CA  1 
ATOM   4300 C  C   . PRO   B 1 280 ? 27.696  -7.612  33.351 1.00 58.01  ?  287 PRO   B C   1 
ATOM   4301 O  O   . PRO   B 1 280 ? 28.911  -7.568  33.162 1.00 67.14  ?  287 PRO   B O   1 
ATOM   4302 C  CB  . PRO   B 1 280 ? 26.954  -8.410  35.664 1.00 68.32  ?  287 PRO   B CB  1 
ATOM   4303 C  CG  . PRO   B 1 280 ? 25.486  -8.657  35.666 1.00 66.33  ?  287 PRO   B CG  1 
ATOM   4304 C  CD  . PRO   B 1 280 ? 24.895  -7.294  35.571 1.00 63.58  ?  287 PRO   B CD  1 
ATOM   4305 N  N   . PHE   B 1 281 ? 26.816  -7.968  32.413 1.00 58.24  ?  288 PHE   B N   1 
ATOM   4306 C  CA  . PHE   B 1 281 ? 27.225  -8.253  31.025 1.00 61.52  ?  288 PHE   B CA  1 
ATOM   4307 C  C   . PHE   B 1 281 ? 27.747  -6.982  30.353 1.00 64.09  ?  288 PHE   B C   1 
ATOM   4308 O  O   . PHE   B 1 281 ? 28.789  -7.024  29.700 1.00 73.89  ?  288 PHE   B O   1 
ATOM   4309 C  CB  . PHE   B 1 281 ? 26.087  -8.883  30.194 1.00 58.33  ?  288 PHE   B CB  1 
ATOM   4310 C  CG  . PHE   B 1 281 ? 26.432  -9.069  28.743 1.00 53.27  ?  288 PHE   B CG  1 
ATOM   4311 C  CD1 . PHE   B 1 281 ? 27.184  -10.153 28.343 1.00 59.39  ?  288 PHE   B CD1 1 
ATOM   4312 C  CD2 . PHE   B 1 281 ? 26.009  -8.150  27.772 1.00 57.91  ?  288 PHE   B CD2 1 
ATOM   4313 C  CE1 . PHE   B 1 281 ? 27.509  -10.338 26.997 1.00 63.71  ?  288 PHE   B CE1 1 
ATOM   4314 C  CE2 . PHE   B 1 281 ? 26.351  -8.307  26.433 1.00 57.35  ?  288 PHE   B CE2 1 
ATOM   4315 C  CZ  . PHE   B 1 281 ? 27.100  -9.407  26.041 1.00 66.86  ?  288 PHE   B CZ  1 
ATOM   4316 N  N   . TYR   B 1 282 ? 27.020  -5.875  30.509 1.00 59.32  ?  289 TYR   B N   1 
ATOM   4317 C  CA  . TYR   B 1 282 ? 27.463  -4.555  30.019 1.00 58.34  ?  289 TYR   B CA  1 
ATOM   4318 C  C   . TYR   B 1 282 ? 28.859  -4.196  30.546 1.00 54.88  ?  289 TYR   B C   1 
ATOM   4319 O  O   . TYR   B 1 282 ? 29.700  -3.752  29.764 1.00 55.99  ?  289 TYR   B O   1 
ATOM   4320 C  CB  . TYR   B 1 282 ? 26.459  -3.433  30.368 1.00 55.36  ?  289 TYR   B CB  1 
ATOM   4321 C  CG  . TYR   B 1 282 ? 27.030  -2.043  30.075 1.00 53.04  ?  289 TYR   B CG  1 
ATOM   4322 C  CD1 . TYR   B 1 282 ? 27.221  -1.611  28.762 1.00 51.28  ?  289 TYR   B CD1 1 
ATOM   4323 C  CD2 . TYR   B 1 282 ? 27.462  -1.212  31.109 1.00 65.91  ?  289 TYR   B CD2 1 
ATOM   4324 C  CE1 . TYR   B 1 282 ? 27.799  -0.372  28.485 1.00 65.96  ?  289 TYR   B CE1 1 
ATOM   4325 C  CE2 . TYR   B 1 282 ? 28.030  0.043   30.846 1.00 70.52  ?  289 TYR   B CE2 1 
ATOM   4326 C  CZ  . TYR   B 1 282 ? 28.197  0.460   29.534 1.00 69.26  ?  289 TYR   B CZ  1 
ATOM   4327 O  OH  . TYR   B 1 282 ? 28.760  1.694   29.281 1.00 70.60  ?  289 TYR   B OH  1 
ATOM   4328 N  N   . LEU   B 1 283 ? 29.090  -4.386  31.848 1.00 58.50  ?  290 LEU   B N   1 
ATOM   4329 C  CA  . LEU   B 1 283 ? 30.365  -3.966  32.475 1.00 66.21  ?  290 LEU   B CA  1 
ATOM   4330 C  C   . LEU   B 1 283 ? 31.550  -4.865  32.093 1.00 68.82  ?  290 LEU   B C   1 
ATOM   4331 O  O   . LEU   B 1 283 ? 32.591  -4.354  31.685 1.00 86.97  ?  290 LEU   B O   1 
ATOM   4332 C  CB  . LEU   B 1 283 ? 30.227  -3.840  33.996 1.00 68.47  ?  290 LEU   B CB  1 
ATOM   4333 C  CG  . LEU   B 1 283 ? 29.218  -2.800  34.548 1.00 66.61  ?  290 LEU   B CG  1 
ATOM   4334 C  CD1 . LEU   B 1 283 ? 29.113  -2.933  36.060 1.00 67.82  ?  290 LEU   B CD1 1 
ATOM   4335 C  CD2 . LEU   B 1 283 ? 29.549  -1.363  34.168 1.00 57.11  ?  290 LEU   B CD2 1 
ATOM   4336 N  N   . SER   B 1 284 ? 31.386  -6.176  32.212 1.00 64.72  ?  291 SER   B N   1 
ATOM   4337 C  CA  . SER   B 1 284 ? 32.452  -7.141  31.839 1.00 72.72  ?  291 SER   B CA  1 
ATOM   4338 C  C   . SER   B 1 284 ? 32.754  -7.222  30.331 1.00 76.00  ?  291 SER   B C   1 
ATOM   4339 O  O   . SER   B 1 284 ? 33.926  -7.252  29.947 1.00 91.83  ?  291 SER   B O   1 
ATOM   4340 C  CB  . SER   B 1 284 ? 32.169  -8.547  32.408 1.00 66.62  ?  291 SER   B CB  1 
ATOM   4341 O  OG  . SER   B 1 284 ? 30.887  -9.009  32.058 1.00 68.07  ?  291 SER   B OG  1 
ATOM   4342 N  N   . GLN   B 1 285 ? 31.716  -7.253  29.492 1.00 83.38  ?  292 GLN   B N   1 
ATOM   4343 C  CA  . GLN   B 1 285 ? 31.870  -7.493  28.018 1.00 81.21  ?  292 GLN   B CA  1 
ATOM   4344 C  C   . GLN   B 1 285 ? 31.897  -6.245  27.114 1.00 84.36  ?  292 GLN   B C   1 
ATOM   4345 O  O   . GLN   B 1 285 ? 32.651  -6.217  26.129 1.00 82.32  ?  292 GLN   B O   1 
ATOM   4346 C  CB  . GLN   B 1 285 ? 30.783  -8.450  27.485 1.00 77.78  ?  292 GLN   B CB  1 
ATOM   4347 C  CG  . GLN   B 1 285 ? 30.525  -9.719  28.300 1.00 77.74  ?  292 GLN   B CG  1 
ATOM   4348 C  CD  . GLN   B 1 285 ? 31.785  -10.471 28.673 1.00 78.51  ?  292 GLN   B CD  1 
ATOM   4349 O  OE1 . GLN   B 1 285 ? 32.669  -10.639 27.837 1.00 82.45  ?  292 GLN   B OE1 1 
ATOM   4350 N  NE2 . GLN   B 1 285 ? 31.877  -10.926 29.929 1.00 78.23  ?  292 GLN   B NE2 1 
ATOM   4351 N  N   . LEU   B 1 286 ? 31.074  -5.239  27.425 1.00 81.69  ?  293 LEU   B N   1 
ATOM   4352 C  CA  . LEU   B 1 286 ? 30.826  -4.088  26.506 1.00 77.56  ?  293 LEU   B CA  1 
ATOM   4353 C  C   . LEU   B 1 286 ? 31.486  -2.751  26.871 1.00 76.38  ?  293 LEU   B C   1 
ATOM   4354 O  O   . LEU   B 1 286 ? 31.828  -1.997  25.953 1.00 77.29  ?  293 LEU   B O   1 
ATOM   4355 C  CB  . LEU   B 1 286 ? 29.322  -3.872  26.321 1.00 66.43  ?  293 LEU   B CB  1 
ATOM   4356 C  CG  . LEU   B 1 286 ? 28.451  -5.098  25.968 1.00 62.96  ?  293 LEU   B CG  1 
ATOM   4357 C  CD1 . LEU   B 1 286 ? 27.034  -4.645  25.653 1.00 56.59  ?  293 LEU   B CD1 1 
ATOM   4358 C  CD2 . LEU   B 1 286 ? 28.999  -5.936  24.810 1.00 66.48  ?  293 LEU   B CD2 1 
ATOM   4359 N  N   . GLU   B 1 287 ? 31.661  -2.448  28.167 1.00 74.84  ?  294 GLU   B N   1 
ATOM   4360 C  CA  . GLU   B 1 287 ? 32.206  -1.132  28.585 1.00 86.19  ?  294 GLU   B CA  1 
ATOM   4361 C  C   . GLU   B 1 287 ? 33.695  -1.010  28.244 1.00 98.84  ?  294 GLU   B C   1 
ATOM   4362 O  O   . GLU   B 1 287 ? 34.057  -0.352  27.263 1.00 95.56  ?  294 GLU   B O   1 
ATOM   4363 C  CB  . GLU   B 1 287 ? 31.961  -0.826  30.079 1.00 86.18  ?  294 GLU   B CB  1 
ATOM   4364 C  CG  . GLU   B 1 287 ? 32.243  0.635   30.455 1.00 81.02  ?  294 GLU   B CG  1 
ATOM   4365 C  CD  . GLU   B 1 287 ? 31.690  1.048   31.814 1.00 88.41  ?  294 GLU   B CD  1 
ATOM   4366 O  OE1 . GLU   B 1 287 ? 32.138  0.494   32.846 1.00 85.66  ?  294 GLU   B OE1 1 
ATOM   4367 O  OE2 . GLU   B 1 287 ? 30.816  1.952   31.851 1.00 92.77  ?  294 GLU   B OE2 1 
HETATM 4368 C  C1  . A1BU6 C 2 .   ? 19.579  1.109   53.147 1.00 77.90  ?  301 A1BU6 A C1  1 
HETATM 4369 C  C2  . A1BU6 C 2 .   ? 18.396  1.245   53.883 1.00 74.59  ?  301 A1BU6 A C2  1 
HETATM 4370 C  C3  . A1BU6 C 2 .   ? 17.495  0.186   53.956 1.00 61.96  ?  301 A1BU6 A C3  1 
HETATM 4371 C  C4  . A1BU6 C 2 .   ? 17.795  -1.014  53.294 1.00 67.15  ?  301 A1BU6 A C4  1 
HETATM 4372 C  C5  . A1BU6 C 2 .   ? 18.986  -1.145  52.568 1.00 62.07  ?  301 A1BU6 A C5  1 
HETATM 4373 C  C6  . A1BU6 C 2 .   ? 19.873  -0.085  52.490 1.00 64.64  ?  301 A1BU6 A C6  1 
HETATM 4374 C  C7  . A1BU6 C 2 .   ? 19.268  -2.458  51.837 1.00 60.07  ?  301 A1BU6 A C7  1 
HETATM 4375 C  C11 . A1BU6 C 2 .   ? 17.087  -3.173  52.425 1.00 57.34  ?  301 A1BU6 A C11 1 
HETATM 4376 C  C15 . A1BU6 C 2 .   ? 20.623  -3.959  53.410 1.00 61.02  ?  301 A1BU6 A C15 1 
HETATM 4377 C  C17 . A1BU6 C 2 .   ? 20.780  -5.110  54.430 1.00 66.79  ?  301 A1BU6 A C17 1 
HETATM 4378 C  C18 . A1BU6 C 2 .   ? 20.126  -4.701  55.775 1.00 69.26  ?  301 A1BU6 A C18 1 
HETATM 4379 C  C19 . A1BU6 C 2 .   ? 22.276  -5.388  54.671 1.00 65.72  ?  301 A1BU6 A C19 1 
HETATM 4380 N  N9  . A1BU6 C 2 .   ? 19.444  -3.567  52.829 1.00 57.68  ?  301 A1BU6 A N9  1 
HETATM 4381 C  C10 . A1BU6 C 2 .   ? 18.097  -4.138  53.042 1.00 58.27  ?  301 A1BU6 A C10 1 
HETATM 4382 O  O13 . A1BU6 C 2 .   ? 16.928  -2.060  53.337 1.00 64.63  ?  301 A1BU6 A O13 1 
HETATM 4383 C  C14 . A1BU6 C 2 .   ? 17.896  -2.808  51.143 1.00 53.69  ?  301 A1BU6 A C14 1 
HETATM 4384 O  O16 . A1BU6 C 2 .   ? 21.605  -3.336  53.078 1.00 69.99  ?  301 A1BU6 A O16 1 
HETATM 4385 F  F20 . A1BU6 C 2 .   ? 22.891  -4.269  55.211 1.00 71.63  ?  301 A1BU6 A F20 1 
HETATM 4386 F  F21 . A1BU6 C 2 .   ? 22.510  -6.463  55.540 1.00 78.72  ?  301 A1BU6 A F21 1 
HETATM 4387 C  C22 . A1BU6 C 2 .   ? 20.185  -6.430  53.846 1.00 66.47  ?  301 A1BU6 A C22 1 
HETATM 4388 I  I   . IOD   D 3 .   ? 26.755  20.671  41.977 0.75 104.65 -1 302 IOD   A I   1 
HETATM 4389 I  I   . IOD   E 3 .   ? 21.416  -4.418  39.033 0.80 103.91 -1 303 IOD   A I   1 
HETATM 4390 I  I   . IOD   F 3 .   ? 35.931  19.755  70.308 0.80 95.96  -1 304 IOD   A I   1 
HETATM 4391 N  N   . GLY   G 4 .   ? 40.133  23.265  48.986 1.00 74.42  ?  305 GLY   A N   1 
HETATM 4392 C  CA  . GLY   G 4 .   ? 40.349  22.467  47.735 1.00 80.87  ?  305 GLY   A CA  1 
HETATM 4393 C  C   . GLY   G 4 .   ? 41.805  22.207  47.373 1.00 81.83  ?  305 GLY   A C   1 
HETATM 4394 O  O   . GLY   G 4 .   ? 42.589  21.692  48.175 1.00 78.74  ?  305 GLY   A O   1 
HETATM 4395 O  OXT . GLY   G 4 .   ? 42.240  22.499  46.258 1.00 84.12  ?  305 GLY   A OXT 1 
HETATM 4396 C  C1  . A1BU6 H 2 .   ? 7.282   7.808   29.493 1.00 68.65  ?  301 A1BU6 B C1  1 
HETATM 4397 C  C2  . A1BU6 H 2 .   ? 6.093   7.472   30.148 1.00 77.79  ?  301 A1BU6 B C2  1 
HETATM 4398 C  C3  . A1BU6 H 2 .   ? 5.432   8.432   30.911 1.00 78.18  ?  301 A1BU6 B C3  1 
HETATM 4399 C  C4  . A1BU6 H 2 .   ? 5.962   9.728   31.012 1.00 73.15  ?  301 A1BU6 B C4  1 
HETATM 4400 C  C5  . A1BU6 H 2 .   ? 7.147   10.059  30.344 1.00 62.54  ?  301 A1BU6 B C5  1 
HETATM 4401 C  C6  . A1BU6 H 2 .   ? 7.805   9.103   29.588 1.00 69.87  ?  301 A1BU6 B C6  1 
HETATM 4402 C  C7  . A1BU6 H 2 .   ? 7.711   11.469  30.500 1.00 60.13  ?  301 A1BU6 B C7  1 
HETATM 4403 C  C11 . A1BU6 H 2 .   ? 6.010   11.905  32.095 1.00 60.26  ?  301 A1BU6 B C11 1 
HETATM 4404 C  C15 . A1BU6 H 2 .   ? 6.884   12.942  28.572 1.00 64.64  ?  301 A1BU6 B C15 1 
HETATM 4405 C  C17 . A1BU6 H 2 .   ? 5.922   13.985  27.968 1.00 61.63  ?  301 A1BU6 B C17 1 
HETATM 4406 C  C18 . A1BU6 H 2 .   ? 6.045   15.316  28.758 1.00 66.32  ?  301 A1BU6 B C18 1 
HETATM 4407 C  C19 . A1BU6 H 2 .   ? 6.351   14.289  26.516 1.00 63.51  ?  301 A1BU6 B C19 1 
HETATM 4408 N  N9  . A1BU6 H 2 .   ? 6.801   12.471  29.860 1.00 58.10  ?  301 A1BU6 B N9  1 
HETATM 4409 C  C10 . A1BU6 H 2 .   ? 5.832   12.848  30.906 1.00 64.22  ?  301 A1BU6 B C10 1 
HETATM 4410 O  O13 . A1BU6 H 2 .   ? 5.340   10.661  31.776 1.00 60.59  ?  301 A1BU6 B O13 1 
HETATM 4411 C  C14 . A1BU6 H 2 .   ? 7.559   11.799  32.039 1.00 50.28  ?  301 A1BU6 B C14 1 
HETATM 4412 O  O16 . A1BU6 H 2 .   ? 7.779   12.494  27.884 1.00 74.21  ?  301 A1BU6 B O16 1 
HETATM 4413 F  F20 . A1BU6 H 2 .   ? 5.494   15.208  25.894 1.00 68.43  ?  301 A1BU6 B F20 1 
HETATM 4414 F  F21 . A1BU6 H 2 .   ? 6.370   13.112  25.756 1.00 68.67  ?  301 A1BU6 B F21 1 
HETATM 4415 C  C22 . A1BU6 H 2 .   ? 4.466   13.439  27.924 1.00 66.91  ?  301 A1BU6 B C22 1 
HETATM 4416 CL CL  . CL    I 5 .   ? 18.633  14.096  36.380 1.00 57.50  -1 302 CL    B CL  1 
HETATM 4417 I  I   . IOD   J 3 .   ? 22.158  -10.484 29.208 0.75 104.77 -1 303 IOD   B I   1 
HETATM 4418 O  O   . HOH   K 6 .   ? 22.909  0.874   59.606 1.00 72.14  ?  401 HOH   A O   1 
HETATM 4419 O  O   . HOH   K 6 .   ? 16.299  12.331  66.842 1.00 55.26  ?  402 HOH   A O   1 
HETATM 4420 O  O   . HOH   K 6 .   ? 18.355  2.376   57.060 1.00 71.72  ?  403 HOH   A O   1 
HETATM 4421 O  O   . HOH   K 6 .   ? 22.087  -4.174  43.639 1.00 53.27  ?  404 HOH   A O   1 
HETATM 4422 O  O   . HOH   K 6 .   ? 21.937  12.664  59.917 1.00 50.41  ?  405 HOH   A O   1 
HETATM 4423 O  O   . HOH   K 6 .   ? 32.080  -6.877  44.285 1.00 68.68  ?  406 HOH   A O   1 
HETATM 4424 O  O   . HOH   K 6 .   ? 42.870  0.626   52.416 1.00 67.19  ?  407 HOH   A O   1 
HETATM 4425 O  O   . HOH   K 6 .   ? 23.344  -6.117  64.134 1.00 77.95  ?  408 HOH   A O   1 
HETATM 4426 O  O   . HOH   K 6 .   ? 30.994  -1.935  56.502 1.00 55.78  ?  409 HOH   A O   1 
HETATM 4427 O  O   . HOH   K 6 .   ? 21.581  9.128   57.659 1.00 53.26  ?  410 HOH   A O   1 
HETATM 4428 O  O   . HOH   K 6 .   ? 19.749  -26.078 57.691 1.00 60.15  ?  411 HOH   A O   1 
HETATM 4429 O  O   . HOH   K 6 .   ? 29.033  16.200  61.950 1.00 57.07  ?  412 HOH   A O   1 
HETATM 4430 O  O   . HOH   K 6 .   ? 26.176  6.159   63.643 1.00 52.63  ?  413 HOH   A O   1 
HETATM 4431 O  O   . HOH   K 6 .   ? 15.486  16.552  60.053 1.00 56.13  ?  414 HOH   A O   1 
HETATM 4432 O  O   . HOH   K 6 .   ? 39.707  13.050  36.455 1.00 59.89  ?  415 HOH   A O   1 
HETATM 4433 O  O   . HOH   K 6 .   ? 11.702  -1.701  61.419 1.00 65.24  ?  416 HOH   A O   1 
HETATM 4434 O  O   . HOH   K 6 .   ? 38.125  12.031  67.156 1.00 67.49  ?  417 HOH   A O   1 
HETATM 4435 O  O   . HOH   K 6 .   ? 19.486  -14.957 79.987 1.00 80.77  ?  418 HOH   A O   1 
HETATM 4436 O  O   . HOH   K 6 .   ? 10.954  8.211   73.972 1.00 52.92  ?  419 HOH   A O   1 
HETATM 4437 O  O   . HOH   K 6 .   ? 30.357  27.625  43.674 1.00 71.03  ?  420 HOH   A O   1 
HETATM 4438 O  O   . HOH   K 6 .   ? 40.091  15.534  60.608 1.00 69.77  ?  421 HOH   A O   1 
HETATM 4439 O  O   . HOH   K 6 .   ? 25.241  8.473   60.109 1.00 51.64  ?  422 HOH   A O   1 
HETATM 4440 O  O   . HOH   K 6 .   ? 36.755  -7.390  51.081 1.00 72.95  ?  423 HOH   A O   1 
HETATM 4441 O  O   . HOH   K 6 .   ? 42.914  5.616   47.696 1.00 69.83  ?  424 HOH   A O   1 
HETATM 4442 O  O   . HOH   K 6 .   ? 32.207  5.047   58.567 1.00 58.92  ?  425 HOH   A O   1 
HETATM 4443 O  O   . HOH   K 6 .   ? 38.388  17.620  60.229 1.00 59.56  ?  426 HOH   A O   1 
HETATM 4444 O  O   . HOH   K 6 .   ? 31.419  -7.171  51.461 1.00 65.64  ?  427 HOH   A O   1 
HETATM 4445 O  O   . HOH   K 6 .   ? 8.770   -8.418  49.104 1.00 81.63  ?  428 HOH   A O   1 
HETATM 4446 O  O   . HOH   K 6 .   ? 40.467  11.093  66.248 1.00 78.01  ?  429 HOH   A O   1 
HETATM 4447 O  O   . HOH   K 6 .   ? 15.982  20.946  46.562 1.00 55.74  ?  430 HOH   A O   1 
HETATM 4448 O  O   . HOH   K 6 .   ? 35.803  11.907  69.940 1.00 53.90  ?  431 HOH   A O   1 
HETATM 4449 O  O   . HOH   K 6 .   ? 11.139  -0.508  53.931 1.00 71.65  ?  432 HOH   A O   1 
HETATM 4450 O  O   . HOH   K 6 .   ? 10.495  -2.261  58.862 1.00 62.93  ?  433 HOH   A O   1 
HETATM 4451 O  O   . HOH   K 6 .   ? 38.733  -5.510  51.959 1.00 70.17  ?  434 HOH   A O   1 
HETATM 4452 O  O   . HOH   K 6 .   ? 32.490  -3.783  54.974 1.00 63.97  ?  435 HOH   A O   1 
HETATM 4453 O  O   . HOH   K 6 .   ? 16.366  -14.869 80.158 1.00 75.51  ?  436 HOH   A O   1 
HETATM 4454 O  O   . HOH   L 6 .   ? -8.618  27.286  27.779 1.00 77.29  ?  401 HOH   B O   1 
HETATM 4455 O  O   . HOH   L 6 .   ? 3.630   2.061   9.675  1.00 66.03  ?  402 HOH   B O   1 
HETATM 4456 O  O   . HOH   L 6 .   ? 6.298   5.262   15.130 1.00 65.35  ?  403 HOH   B O   1 
HETATM 4457 O  O   . HOH   L 6 .   ? 8.391   14.991  33.889 1.00 60.64  ?  404 HOH   B O   1 
HETATM 4458 O  O   . HOH   L 6 .   ? 20.633  10.273  30.542 1.00 63.24  ?  405 HOH   B O   1 
HETATM 4459 O  O   . HOH   L 6 .   ? -11.250 22.689  24.372 1.00 75.47  ?  406 HOH   B O   1 
HETATM 4460 O  O   . HOH   L 6 .   ? 12.674  13.032  34.480 1.00 58.04  ?  407 HOH   B O   1 
HETATM 4461 O  O   . HOH   L 6 .   ? 2.961   -1.358  23.043 1.00 74.54  ?  408 HOH   B O   1 
HETATM 4462 O  O   . HOH   L 6 .   ? 12.162  34.343  33.048 1.00 70.20  ?  409 HOH   B O   1 
HETATM 4463 O  O   . HOH   L 6 .   ? 23.835  10.312  32.712 1.00 56.16  ?  410 HOH   B O   1 
HETATM 4464 O  O   . HOH   L 6 .   ? 26.893  0.166   35.983 1.00 74.98  ?  411 HOH   B O   1 
HETATM 4465 O  O   . HOH   L 6 .   ? 6.183   -6.977  16.403 1.00 62.86  ?  412 HOH   B O   1 
HETATM 4466 O  O   . HOH   L 6 .   ? 14.610  12.446  15.525 1.00 60.95  ?  413 HOH   B O   1 
HETATM 4467 O  O   . HOH   L 6 .   ? 29.211  -11.247 32.478 1.00 82.22  ?  414 HOH   B O   1 
HETATM 4468 O  O   . HOH   L 6 .   ? 18.939  0.512   39.335 1.00 66.70  ?  415 HOH   B O   1 
HETATM 4469 O  O   . HOH   L 6 .   ? 12.019  -16.166 18.077 1.00 42.53  ?  416 HOH   B O   1 
HETATM 4470 O  O   . HOH   L 6 .   ? -11.306 17.463  25.821 1.00 63.73  ?  417 HOH   B O   1 
HETATM 4471 O  O   . HOH   L 6 .   ? 11.785  11.355  12.539 1.00 61.20  ?  418 HOH   B O   1 
HETATM 4472 O  O   . HOH   L 6 .   ? -16.673 27.158  22.925 1.00 71.13  ?  419 HOH   B O   1 
HETATM 4473 O  O   . HOH   L 6 .   ? 7.998   34.739  12.546 1.00 80.02  ?  420 HOH   B O   1 
HETATM 4474 O  O   . HOH   L 6 .   ? 16.242  21.888  27.465 1.00 71.06  ?  421 HOH   B O   1 
HETATM 4475 O  O   . HOH   L 6 .   ? 4.857   0.193   21.135 1.00 64.38  ?  422 HOH   B O   1 
HETATM 4476 O  O   . HOH   L 6 .   ? 14.458  16.335  21.175 1.00 57.66  ?  423 HOH   B O   1 
HETATM 4477 O  O   . HOH   L 6 .   ? 23.411  -17.076 25.008 1.00 63.78  ?  424 HOH   B O   1 
HETATM 4478 O  O   . HOH   L 6 .   ? -3.938  -3.106  16.068 1.00 67.25  ?  425 HOH   B O   1 
HETATM 4479 O  O   . HOH   L 6 .   ? 15.077  8.432   11.411 1.00 62.70  ?  426 HOH   B O   1 
HETATM 4480 O  O   . HOH   L 6 .   ? 7.510   -4.616  0.400  1.00 65.16  ?  427 HOH   B O   1 
HETATM 4481 O  O   . HOH   L 6 .   ? 25.530  -11.527 13.529 1.00 75.82  ?  428 HOH   B O   1 
HETATM 4482 O  O   . HOH   L 6 .   ? 16.239  13.607  37.699 1.00 71.99  ?  429 HOH   B O   1 
HETATM 4483 O  O   . HOH   L 6 .   ? 26.819  2.538   34.725 1.00 59.55  ?  430 HOH   B O   1 
HETATM 4484 O  O   . HOH   L 6 .   ? 9.254   -17.475 18.079 1.00 68.54  ?  431 HOH   B O   1 
HETATM 4485 O  O   . HOH   L 6 .   ? 15.124  16.333  16.481 1.00 62.63  ?  432 HOH   B O   1 
HETATM 4486 O  O   . HOH   L 6 .   ? 12.840  14.856  16.621 1.00 66.11  ?  433 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   . ASN A 1   ? 1.2733 1.4631 1.7348 -0.2381 -0.0656 -0.0121 8   ASN A N   
2    C CA  . ASN A 1   ? 1.2994 1.4381 1.7474 -0.2282 -0.0313 -0.0183 8   ASN A CA  
3    C C   . ASN A 1   ? 1.2680 1.3300 1.6512 -0.2095 -0.0202 -0.0381 8   ASN A C   
4    O O   . ASN A 1   ? 1.1873 1.2232 1.5316 -0.2169 -0.0352 -0.0543 8   ASN A O   
5    C CB  . ASN A 1   ? 1.3755 1.5102 1.8373 -0.2712 -0.0250 -0.0227 8   ASN A CB  
6    C CG  . ASN A 1   ? 1.4179 1.6305 1.9568 -0.2840 -0.0246 0.0027  8   ASN A CG  
7    O OD1 . ASN A 1   ? 1.5942 1.8781 2.1792 -0.2778 -0.0445 0.0221  8   ASN A OD1 
8    N ND2 . ASN A 1   ? 1.4648 1.6666 2.0232 -0.3005 0.0001  0.0063  8   ASN A ND2 
9    N N   . VAL A 2   ? 1.1910 1.2218 1.5647 -0.1861 0.0068  -0.0339 9   VAL A N   
10   C CA  . VAL A 2   ? 1.0216 0.9896 1.3443 -0.1685 0.0182  -0.0451 9   VAL A CA  
11   C C   . VAL A 2   ? 0.9737 0.8923 1.2748 -0.1938 0.0281  -0.0561 9   VAL A C   
12   O O   . VAL A 2   ? 1.0841 1.0062 1.4072 -0.2175 0.0392  -0.0512 9   VAL A O   
13   C CB  . VAL A 2   ? 1.0006 0.9585 1.3158 -0.1373 0.0403  -0.0331 9   VAL A CB  
14   C CG1 . VAL A 2   ? 0.9904 0.9441 1.3214 -0.1455 0.0650  -0.0203 9   VAL A CG1 
15   C CG2 . VAL A 2   ? 1.0361 0.9494 1.3043 -0.1172 0.0414  -0.0400 9   VAL A CG2 
16   N N   . ILE A 3   ? 0.9163 0.7875 1.1778 -0.1887 0.0276  -0.0699 10  ILE A N   
17   C CA  . ILE A 3   ? 1.0435 0.8544 1.2814 -0.2051 0.0452  -0.0798 10  ILE A CA  
18   C C   . ILE A 3   ? 1.0359 0.8167 1.2694 -0.1809 0.0702  -0.0624 10  ILE A C   
19   O O   . ILE A 3   ? 0.9770 0.7575 1.1974 -0.1487 0.0693  -0.0536 10  ILE A O   
20   C CB  . ILE A 3   ? 1.0590 0.8312 1.2602 -0.2042 0.0411  -0.0983 10  ILE A CB  
21   C CG1 . ILE A 3   ? 1.0344 0.8331 1.2296 -0.2340 0.0162  -0.1142 10  ILE A CG1 
22   C CG2 . ILE A 3   ? 1.1849 0.8836 1.3624 -0.2132 0.0692  -0.1065 10  ILE A CG2 
23   C CD1 . ILE A 3   ? 1.0711 0.8448 1.2294 -0.2281 0.0104  -0.1296 10  ILE A CD1 
24   N N   . LYS A 4   ? 1.0596 0.8180 1.3030 -0.1994 0.0911  -0.0560 11  LYS A N   
25   C CA  . LYS A 4   ? 1.0985 0.8223 1.3335 -0.1792 0.1169  -0.0355 11  LYS A CA  
26   C C   . LYS A 4   ? 1.0411 0.6976 1.2512 -0.1738 0.1341  -0.0391 11  LYS A C   
27   O O   . LYS A 4   ? 1.1988 0.8138 1.4033 -0.2034 0.1466  -0.0550 11  LYS A O   
28   C CB  . LYS A 4   ? 1.1540 0.8816 1.4129 -0.2001 0.1362  -0.0235 11  LYS A CB  
29   C CG  . LYS A 4   ? 1.1879 0.9790 1.4749 -0.1933 0.1302  -0.0116 11  LYS A CG  
30   C CD  . LYS A 4   ? 1.2826 1.0815 1.6001 -0.2158 0.1528  0.0015  11  LYS A CD  
31   C CE  . LYS A 4   ? 1.2336 1.0987 1.5896 -0.2119 0.1513  0.0123  11  LYS A CE  
32   N NZ  . LYS A 4   ? 1.2637 1.1434 1.6595 -0.2388 0.1739  0.0251  11  LYS A NZ  
33   N N   . MET A 5   ? 0.9789 0.6267 1.1750 -0.1373 0.1351  -0.0241 12  MET A N   
34   C CA  . MET A 5   ? 1.0619 0.6562 1.2450 -0.1210 0.1527  -0.0198 12  MET A CA  
35   C C   . MET A 5   ? 1.0885 0.6534 1.2717 -0.1000 0.1772  0.0134  12  MET A C   
36   O O   . MET A 5   ? 1.2170 0.8090 1.4012 -0.0935 0.1754  0.0329  12  MET A O   
37   C CB  . MET A 5   ? 1.0156 0.6332 1.1929 -0.0942 0.1335  -0.0207 12  MET A CB  
38   C CG  . MET A 5   ? 1.0399 0.6724 1.2112 -0.1110 0.1149  -0.0504 12  MET A CG  
39   S SD  . MET A 5   ? 1.0524 0.7104 1.2202 -0.0822 0.0967  -0.0504 12  MET A SD  
40   C CE  . MET A 5   ? 0.9487 0.5806 1.0986 -0.1073 0.0973  -0.0836 12  MET A CE  
41   N N   . LYS A 6   ? 1.1048 0.6117 1.2853 -0.0882 0.2030  0.0215  13  LYS A N   
42   C CA  . LYS A 6   ? 1.2382 0.7095 1.4213 -0.0642 0.2300  0.0591  13  LYS A CA  
43   C C   . LYS A 6   ? 1.2443 0.7247 1.4339 -0.0222 0.2261  0.0851  13  LYS A C   
44   O O   . LYS A 6   ? 1.2516 0.7405 1.4449 -0.0168 0.2161  0.0681  13  LYS A O   
45   C CB  . LYS A 6   ? 1.3541 0.7419 1.5362 -0.0844 0.2720  0.0528  13  LYS A CB  
46   C CG  . LYS A 6   ? 1.4245 0.8052 1.6058 -0.1325 0.2763  0.0293  13  LYS A CG  
47   C CD  . LYS A 6   ? 1.4816 0.7720 1.6582 -0.1543 0.3220  0.0274  13  LYS A CD  
48   C CE  . LYS A 6   ? 1.5590 0.8558 1.7420 -0.2050 0.3231  0.0100  13  LYS A CE  
49   N NZ  . LYS A 6   ? 1.6568 0.8608 1.8326 -0.2325 0.3692  0.0061  13  LYS A NZ  
50   N N   . SER A 7   ? 1.3377 0.8192 1.5303 0.0064  0.2342  0.1290  14  SER A N   
51   C CA  . SER A 7   ? 1.3217 0.8161 1.5308 0.0470  0.2321  0.1634  14  SER A CA  
52   C C   . SER A 7   ? 1.3616 0.7881 1.5910 0.0606  0.2716  0.1652  14  SER A C   
53   O O   . SER A 7   ? 1.3607 0.8037 1.6116 0.0855  0.2683  0.1736  14  SER A O   
54   C CB  . SER A 7   ? 1.3545 0.8705 1.5590 0.0722  0.2289  0.2154  14  SER A CB  
55   O OG  . SER A 7   ? 1.2672 0.8459 1.4466 0.0635  0.1932  0.2123  14  SER A OG  
56   N N   . SER A 8   ? 1.4852 0.8337 1.7082 0.0431  0.3119  0.1571  15  SER A N   
57   C CA  . SER A 8   ? 1.5085 0.7708 1.7393 0.0472  0.3594  0.1478  15  SER A CA  
58   C C   . SER A 8   ? 1.4828 0.7347 1.7026 0.0266  0.3562  0.0987  15  SER A C   
59   O O   . SER A 8   ? 1.4745 0.6690 1.7012 0.0408  0.3925  0.0949  15  SER A O   
60   C CB  . SER A 8   ? 1.5079 0.6842 1.7240 0.0201  0.4018  0.1404  15  SER A CB  
61   O OG  . SER A 8   ? 1.5101 0.6896 1.7021 -0.0337 0.3870  0.0932  15  SER A OG  
62   N N   . ASP A 9   ? 1.3750 0.6790 1.5766 -0.0053 0.3168  0.0637  16  ASP A N   
63   C CA  . ASP A 9   ? 1.3745 0.6848 1.5627 -0.0218 0.3050  0.0237  16  ASP A CA  
64   C C   . ASP A 9   ? 1.2771 0.6321 1.4884 0.0156  0.2916  0.0395  16  ASP A C   
65   O O   . ASP A 9   ? 1.2182 0.5645 1.4190 0.0072  0.2932  0.0110  16  ASP A O   
66   C CB  . ASP A 9   ? 1.3608 0.7239 1.5304 -0.0600 0.2643  -0.0084 16  ASP A CB  
67   C CG  . ASP A 9   ? 1.4722 0.8031 1.6257 -0.1050 0.2738  -0.0288 16  ASP A CG  
68   O OD1 . ASP A 9   ? 1.6146 0.8668 1.7601 -0.1169 0.3147  -0.0301 16  ASP A OD1 
69   O OD2 . ASP A 9   ? 1.3873 0.7739 1.5393 -0.1298 0.2408  -0.0428 16  ASP A OD2 
70   N N   . PHE A 10  ? 1.2568 0.6632 1.4970 0.0524  0.2765  0.0844  17  PHE A N   
71   C CA  . PHE A 10  ? 1.3104 0.7734 1.5803 0.0842  0.2585  0.1049  17  PHE A CA  
72   C C   . PHE A 10  ? 1.3393 0.7964 1.6527 0.1305  0.2835  0.1567  17  PHE A C   
73   O O   . PHE A 10  ? 1.3721 0.8013 1.6915 0.1442  0.3029  0.1889  17  PHE A O   
74   C CB  . PHE A 10  ? 1.1731 0.7233 1.4387 0.0817  0.2065  0.1133  17  PHE A CB  
75   C CG  . PHE A 10  ? 1.1181 0.6907 1.3555 0.0474  0.1795  0.0699  17  PHE A CG  
76   C CD1 . PHE A 10  ? 1.1142 0.7152 1.3538 0.0447  0.1630  0.0490  17  PHE A CD1 
77   C CD2 . PHE A 10  ? 1.1023 0.6703 1.3155 0.0192  0.1723  0.0536  17  PHE A CD2 
78   C CE1 . PHE A 10  ? 1.1131 0.7350 1.3288 0.0165  0.1388  0.0146  17  PHE A CE1 
79   C CE2 . PHE A 10  ? 1.0921 0.6874 1.2880 -0.0082 0.1477  0.0201  17  PHE A CE2 
80   C CZ  . PHE A 10  ? 1.0558 0.6765 1.2516 -0.0085 0.1307  0.0016  17  PHE A CZ  
81   N N   . LEU A 11  ? 1.4017 0.8912 1.7490 0.1545  0.2822  0.1672  18  LEU A N   
82   C CA  . LEU A 11  ? 1.4605 0.9845 1.8643 0.2013  0.2897  0.2244  18  LEU A CA  
83   C C   . LEU A 11  ? 1.5475 1.1778 1.9659 0.2015  0.2335  0.2337  18  LEU A C   
84   O O   . LEU A 11  ? 1.5397 1.1898 1.9496 0.1836  0.2187  0.1978  18  LEU A O   
85   C CB  . LEU A 11  ? 1.4007 0.8727 1.8400 0.2271  0.3423  0.2270  18  LEU A CB  
86   C CG  . LEU A 11  ? 1.5142 0.8668 1.9186 0.2095  0.3999  0.1891  18  LEU A CG  
87   C CD1 . LEU A 11  ? 1.5299 0.8361 1.9619 0.2336  0.4513  0.1862  18  LEU A CD1 
88   C CD2 . LEU A 11  ? 1.7103 1.0024 2.1098 0.2170  0.4295  0.2151  18  LEU A CD2 
89   N N   . GLU A 12  ? 1.6667 1.3616 2.1009 0.2181  0.2027  0.2805  19  GLU A N   
90   C CA  . GLU A 12  ? 1.6446 1.4387 2.0918 0.2157  0.1506  0.2929  19  GLU A CA  
91   C C   . GLU A 12  ? 1.6153 1.4561 2.1349 0.2499  0.1571  0.3314  19  GLU A C   
92   O O   . GLU A 12  ? 1.7001 1.5436 2.2658 0.2870  0.1777  0.3854  19  GLU A O   
93   C CB  . GLU A 12  ? 1.6991 1.5426 2.1204 0.2115  0.1125  0.3234  19  GLU A CB  
94   C CG  . GLU A 12  ? 1.6812 1.4966 2.0351 0.1754  0.1014  0.2830  19  GLU A CG  
95   C CD  . GLU A 12  ? 1.6097 1.4802 1.9253 0.1636  0.0601  0.3003  19  GLU A CD  
96   O OE1 . GLU A 12  ? 1.4978 1.4408 1.8201 0.1620  0.0219  0.3144  19  GLU A OE1 
97   O OE2 . GLU A 12  ? 1.5021 1.3412 1.7764 0.1519  0.0672  0.2969  19  GLU A OE2 
98   N N   . LYS A 23  ? 1.6406 1.7058 1.6387 0.0176  -0.1256 0.2289  30  LYS A N   
99   C CA  . LYS A 23  ? 1.5123 1.6220 1.5694 0.0226  -0.1447 0.2350  30  LYS A CA  
100  C C   . LYS A 23  ? 1.4124 1.4883 1.5078 0.0239  -0.1228 0.1937  30  LYS A C   
101  O O   . LYS A 23  ? 1.3876 1.4149 1.5022 0.0379  -0.0900 0.1855  30  LYS A O   
102  C CB  . LYS A 23  ? 1.4659 1.6060 1.5844 0.0560  -0.1441 0.2929  30  LYS A CB  
103  C CG  . LYS A 23  ? 1.5319 1.7097 1.6185 0.0600  -0.1664 0.3449  30  LYS A CG  
104  C CD  . LYS A 23  ? 1.4872 1.7217 1.6469 0.0914  -0.1778 0.4074  30  LYS A CD  
105  C CE  . LYS A 23  ? 1.6656 1.9441 1.7898 0.0950  -0.2046 0.4655  30  LYS A CE  
106  N NZ  . LYS A 23  ? 1.6809 2.0205 1.8856 0.1312  -0.2146 0.5360  30  LYS A NZ  
107  N N   . VAL A 24  ? 1.3175 1.4189 1.4206 0.0063  -0.1413 0.1691  31  VAL A N   
108  C CA  . VAL A 24  ? 1.1552 1.2356 1.2994 0.0094  -0.1246 0.1391  31  VAL A CA  
109  C C   . VAL A 24  ? 1.0942 1.2009 1.3121 0.0356  -0.1189 0.1717  31  VAL A C   
110  O O   . VAL A 24  ? 1.1999 1.3679 1.4446 0.0386  -0.1439 0.2058  31  VAL A O   
111  C CB  . VAL A 24  ? 1.0594 1.1520 1.1845 -0.0185 -0.1419 0.1034  31  VAL A CB  
112  C CG1 . VAL A 24  ? 0.9287 0.9955 1.0897 -0.0140 -0.1225 0.0760  31  VAL A CG1 
113  C CG2 . VAL A 24  ? 1.2007 1.2633 1.2527 -0.0414 -0.1418 0.0742  31  VAL A CG2 
114  N N   . SER A 25  ? 1.0073 1.0688 1.2569 0.0529  -0.0850 0.1617  32  SER A N   
115  C CA  . SER A 25  ? 1.0091 1.0776 1.3252 0.0817  -0.0661 0.1905  32  SER A CA  
116  C C   . SER A 25  ? 0.9400 0.9547 1.2731 0.0858  -0.0318 0.1589  32  SER A C   
117  O O   . SER A 25  ? 0.8934 0.8630 1.1888 0.0696  -0.0221 0.1219  32  SER A O   
118  C CB  . SER A 25  ? 1.0637 1.1224 1.3926 0.1083  -0.0516 0.2357  32  SER A CB  
119  O OG  . SER A 25  ? 1.0712 1.0659 1.3613 0.1044  -0.0279 0.2187  32  SER A OG  
120  N N   . LEU A 26  ? 0.9073 0.9290 1.2970 0.1074  -0.0127 0.1762  33  LEU A N   
121  C CA  . LEU A 26  ? 0.8817 0.8444 1.2816 0.1133  0.0264  0.1510  33  LEU A CA  
122  C C   . LEU A 26  ? 0.9322 0.8266 1.3198 0.1251  0.0615  0.1547  33  LEU A C   
123  O O   . LEU A 26  ? 0.9335 0.8324 1.3441 0.1484  0.0700  0.1956  33  LEU A O   
124  C CB  . LEU A 26  ? 0.8177 0.8052 1.2816 0.1351  0.0434  0.1713  33  LEU A CB  
125  C CG  . LEU A 26  ? 0.7534 0.8055 1.2375 0.1204  0.0144  0.1665  33  LEU A CG  
126  C CD1 . LEU A 26  ? 0.6989 0.7935 1.2622 0.1468  0.0302  0.2020  33  LEU A CD1 
127  C CD2 . LEU A 26  ? 0.7122 0.7303 1.1563 0.0943  0.0167  0.1159  33  LEU A CD2 
128  N N   . ALA A 27  ? 0.8696 0.7044 1.2204 0.1064  0.0794  0.1139  34  ALA A N   
129  C CA  . ALA A 27  ? 0.8935 0.6619 1.2244 0.1052  0.1092  0.1085  34  ALA A CA  
130  C C   . ALA A 27  ? 0.8908 0.5955 1.2155 0.0992  0.1459  0.0782  34  ALA A C   
131  O O   . ALA A 27  ? 0.8836 0.5852 1.1836 0.0769  0.1371  0.0427  34  ALA A O   
132  C CB  . ALA A 27  ? 0.8702 0.6358 1.1553 0.0788  0.0894  0.0874  34  ALA A CB  
133  N N   . PHE A 28  ? 0.9461 0.5957 1.2884 0.1183  0.1891  0.0930  35  PHE A N   
134  C CA  . PHE A 28  ? 0.9857 0.5570 1.3075 0.1077  0.2312  0.0607  35  PHE A CA  
135  C C   . PHE A 28  ? 0.9908 0.5001 1.2693 0.0802  0.2442  0.0378  35  PHE A C   
136  O O   . PHE A 28  ? 1.0514 0.5218 1.3391 0.0929  0.2698  0.0603  35  PHE A O   
137  C CB  . PHE A 28  ? 1.0631 0.5983 1.4281 0.1440  0.2806  0.0872  35  PHE A CB  
138  C CG  . PHE A 28  ? 1.0310 0.6106 1.4349 0.1616  0.2805  0.0952  35  PHE A CG  
139  C CD1 . PHE A 28  ? 1.0272 0.5701 1.4045 0.1455  0.3012  0.0566  35  PHE A CD1 
140  C CD2 . PHE A 28  ? 0.9978 0.6595 1.4642 0.1915  0.2590  0.1427  35  PHE A CD2 
141  C CE1 . PHE A 28  ? 0.9785 0.5620 1.3933 0.1607  0.3048  0.0646  35  PHE A CE1 
142  C CE2 . PHE A 28  ? 0.9789 0.6873 1.4885 0.2044  0.2595  0.1511  35  PHE A CE2 
143  C CZ  . PHE A 28  ? 0.9841 0.6516 1.4695 0.1901  0.2847  0.1118  35  PHE A CZ  
144  N N   . HIS A 29  ? 0.9798 0.4828 1.2151 0.0421  0.2266  -0.0035 36  HIS A N   
145  C CA  . HIS A 29  ? 1.1212 0.5664 1.3185 0.0087  0.2407  -0.0295 36  HIS A CA  
146  C C   . HIS A 29  ? 1.2248 0.5789 1.4041 0.0043  0.2933  -0.0475 36  HIS A C   
147  O O   . HIS A 29  ? 1.2765 0.6168 1.4477 0.0067  0.3070  -0.0636 36  HIS A O   
148  C CB  . HIS A 29  ? 1.1142 0.5867 1.2775 -0.0299 0.2062  -0.0633 36  HIS A CB  
149  C CG  . HIS A 29  ? 1.1181 0.5597 1.2577 -0.0646 0.2093  -0.0794 36  HIS A CG  
150  N ND1 . HIS A 29  ? 1.1483 0.5346 1.2493 -0.1026 0.2255  -0.1144 36  HIS A ND1 
151  C CD2 . HIS A 29  ? 1.1151 0.5737 1.2641 -0.0696 0.1998  -0.0643 36  HIS A CD2 
152  C CE1 . HIS A 29  ? 1.1340 0.5114 1.2280 -0.1313 0.2225  -0.1197 36  HIS A CE1 
153  N NE2 . HIS A 29  ? 1.1215 0.5415 1.2463 -0.1101 0.2092  -0.0891 36  HIS A NE2 
154  N N   . ARG A 30  ? 1.3573 0.6458 1.5275 -0.0036 0.3254  -0.0453 37  ARG A N   
155  C CA  . ARG A 30  ? 1.4253 0.6112 1.5799 -0.0029 0.3865  -0.0569 37  ARG A CA  
156  C C   . ARG A 30  ? 1.4558 0.5863 1.5510 -0.0442 0.4011  -0.1097 37  ARG A C   
157  O O   . ARG A 30  ? 1.5013 0.5558 1.5828 -0.0360 0.4525  -0.1204 37  ARG A O   
158  C CB  . ARG A 30  ? 1.5003 0.6230 1.6527 -0.0092 0.4169  -0.0449 37  ARG A CB  
159  C CG  . ARG A 30  ? 1.5786 0.7152 1.7851 0.0421  0.4311  0.0136  37  ARG A CG  
160  C CD  . ARG A 30  ? 1.7525 0.8056 1.9512 0.0353  0.4733  0.0235  37  ARG A CD  
161  N NE  . ARG A 30  ? 1.7582 0.8108 2.0067 0.0885  0.4962  0.0842  37  ARG A NE  
162  C CZ  . ARG A 30  ? 1.8710 0.8756 2.1524 0.1309  0.5457  0.1128  37  ARG A CZ  
163  N NH1 . ARG A 30  ? 1.9212 0.8651 2.1901 0.1302  0.5860  0.0833  37  ARG A NH1 
164  N NH2 . ARG A 30  ? 1.8877 0.9067 2.2177 0.1784  0.5578  0.1757  37  ARG A NH2 
165  N N   . THR A 31  ? 1.4244 0.5915 1.4840 -0.0876 0.3586  -0.1399 38  THR A N   
166  C CA  . THR A 31  ? 1.4895 0.6224 1.4871 -0.1304 0.3599  -0.1865 38  THR A CA  
167  C C   . THR A 31  ? 1.3579 0.5632 1.3515 -0.1288 0.3198  -0.1928 38  THR A C   
168  O O   . THR A 31  ? 1.3197 0.4896 1.2660 -0.1484 0.3331  -0.2221 38  THR A O   
169  C CB  . THR A 31  ? 1.4778 0.5883 1.4314 -0.1904 0.3456  -0.2172 38  THR A CB  
170  O OG1 . THR A 31  ? 1.5344 0.7382 1.5138 -0.1985 0.2899  -0.2042 38  THR A OG1 
171  C CG2 . THR A 31  ? 1.6117 0.6400 1.5638 -0.1983 0.3899  -0.2149 38  THR A CG2 
172  N N   . GLN A 32  ? 1.3516 0.6483 1.3894 -0.1054 0.2767  -0.1656 39  GLN A N   
173  C CA  . GLN A 32  ? 1.3254 0.6923 1.3592 -0.1097 0.2341  -0.1711 39  GLN A CA  
174  C C   . GLN A 32  ? 1.2594 0.6737 1.3353 -0.0680 0.2296  -0.1463 39  GLN A C   
175  O O   . GLN A 32  ? 1.1644 0.6316 1.2391 -0.0705 0.1978  -0.1491 39  GLN A O   
176  C CB  . GLN A 32  ? 1.2989 0.7326 1.3431 -0.1258 0.1861  -0.1656 39  GLN A CB  
177  C CG  . GLN A 32  ? 1.4279 0.8415 1.4354 -0.1747 0.1775  -0.1907 39  GLN A CG  
178  C CD  . GLN A 32  ? 1.4702 0.9586 1.4974 -0.1871 0.1328  -0.1821 39  GLN A CD  
179  O OE1 . GLN A 32  ? 1.3062 0.8502 1.3693 -0.1587 0.1130  -0.1588 39  GLN A OE1 
180  N NE2 . GLN A 32  ? 1.5814 1.0711 1.5848 -0.2316 0.1183  -0.2006 39  GLN A NE2 
181  N N   . GLY A 33  ? 1.2508 0.6492 1.3671 -0.0310 0.2608  -0.1196 40  GLY A N   
182  C CA  . GLY A 33  ? 1.1743 0.6220 1.3375 0.0049  0.2579  -0.0939 40  GLY A CA  
183  C C   . GLY A 33  ? 1.0528 0.5851 1.2560 0.0208  0.2141  -0.0649 40  GLY A C   
184  O O   . GLY A 33  ? 1.0717 0.6176 1.2778 0.0176  0.1974  -0.0536 40  GLY A O   
185  N N   . LEU A 34  ? 1.0830 0.6686 1.3123 0.0344  0.1979  -0.0549 41  LEU A N   
186  C CA  . LEU A 34  ? 1.0328 0.6934 1.3030 0.0518  0.1644  -0.0246 41  LEU A CA  
187  C C   . LEU A 34  ? 0.9732 0.6723 1.2179 0.0293  0.1208  -0.0370 41  LEU A C   
188  O O   . LEU A 34  ? 0.9937 0.6880 1.2063 0.0072  0.1098  -0.0638 41  LEU A O   
189  C CB  . LEU A 34  ? 1.1340 0.8345 1.4434 0.0690  0.1665  -0.0115 41  LEU A CB  
190  C CG  . LEU A 34  ? 1.0969 0.8766 1.4555 0.0855  0.1365  0.0230  41  LEU A CG  
191  C CD1 . LEU A 34  ? 1.0964 0.8875 1.4925 0.1119  0.1433  0.0635  41  LEU A CD1 
192  C CD2 . LEU A 34  ? 1.1805 0.9926 1.5787 0.0958  0.1452  0.0307  41  LEU A CD2 
193  N N   . MET A 35  ? 0.8989 0.6323 1.1563 0.0364  0.0998  -0.0152 42  MET A N   
194  C CA  . MET A 35  ? 0.8342 0.6037 1.0720 0.0211  0.0648  -0.0218 42  MET A CA  
195  C C   . MET A 35  ? 0.8244 0.6454 1.0833 0.0350  0.0431  0.0076  42  MET A C   
196  O O   . MET A 35  ? 0.9365 0.7701 1.2291 0.0569  0.0521  0.0377  42  MET A O   
197  C CB  . MET A 35  ? 0.9283 0.6701 1.1409 0.0060  0.0674  -0.0308 42  MET A CB  
198  C CG  . MET A 35  ? 0.9985 0.6976 1.1842 -0.0173 0.0804  -0.0604 42  MET A CG  
199  S SD  . MET A 35  ? 1.0194 0.6813 1.1917 -0.0341 0.0938  -0.0628 42  MET A SD  
200  C CE  . MET A 35  ? 1.0304 0.6565 1.1680 -0.0690 0.0995  -0.0995 42  MET A CE  
201  N N   . ILE A 36  ? 0.7280 0.5779 0.9654 0.0217  0.0158  0.0001  43  ILE A N   
202  C CA  . ILE A 36  ? 0.7772 0.6683 1.0141 0.0257  -0.0064 0.0224  43  ILE A CA  
203  C C   . ILE A 36  ? 0.8669 0.7401 1.0762 0.0207  -0.0041 0.0243  43  ILE A C   
204  O O   . ILE A 36  ? 0.8528 0.7008 1.0434 0.0071  0.0025  0.0015  43  ILE A O   
205  C CB  . ILE A 36  ? 0.7561 0.6835 0.9802 0.0112  -0.0330 0.0104  43  ILE A CB  
206  C CG1 . ILE A 36  ? 0.7854 0.7293 1.0383 0.0124  -0.0326 0.0066  43  ILE A CG1 
207  C CG2 . ILE A 36  ? 0.7007 0.6686 0.9165 0.0103  -0.0561 0.0330  43  ILE A CG2 
208  C CD1 . ILE A 36  ? 0.7400 0.6905 0.9699 -0.0070 -0.0475 -0.0178 43  ILE A CD1 
209  N N   . MET A 37  ? 0.9112 0.8019 1.1208 0.0314  -0.0097 0.0547  44  MET A N   
210  C CA  . MET A 37  ? 1.0337 0.9109 1.2157 0.0277  -0.0059 0.0621  44  MET A CA  
211  C C   . MET A 37  ? 1.0136 0.9299 1.1669 0.0227  -0.0316 0.0753  44  MET A C   
212  O O   . MET A 37  ? 1.1473 1.0960 1.3118 0.0335  -0.0449 0.1069  44  MET A O   
213  C CB  . MET A 37  ? 1.0755 0.9239 1.2762 0.0451  0.0183  0.0895  44  MET A CB  
214  C CG  . MET A 37  ? 1.1551 0.9798 1.3306 0.0399  0.0300  0.0967  44  MET A CG  
215  S SD  . MET A 37  ? 1.1953 0.9633 1.3935 0.0543  0.0689  0.1183  44  MET A SD  
216  C CE  . MET A 37  ? 1.3396 1.1389 1.5643 0.0875  0.0631  0.1731  44  MET A CE  
217  N N   . LYS A 38  ? 1.0508 0.9647 1.1669 0.0052  -0.0378 0.0514  45  LYS A N   
218  C CA  . LYS A 38  ? 1.1302 1.0627 1.2009 -0.0045 -0.0532 0.0578  45  LYS A CA  
219  C C   . LYS A 38  ? 1.1345 1.0452 1.1844 0.0002  -0.0358 0.0747  45  LYS A C   
220  O O   . LYS A 38  ? 0.9672 0.8504 1.0122 -0.0050 -0.0161 0.0578  45  LYS A O   
221  C CB  . LYS A 38  ? 1.1263 1.0543 1.1647 -0.0232 -0.0580 0.0239  45  LYS A CB  
222  C CG  . LYS A 38  ? 1.2766 1.2129 1.2554 -0.0377 -0.0692 0.0248  45  LYS A CG  
223  C CD  . LYS A 38  ? 1.3312 1.2646 1.2804 -0.0574 -0.0771 -0.0061 45  LYS A CD  
224  C CE  . LYS A 38  ? 1.3469 1.2823 1.2256 -0.0775 -0.0875 -0.0080 45  LYS A CE  
225  N NZ  . LYS A 38  ? 1.3575 1.2938 1.2011 -0.1018 -0.1009 -0.0309 45  LYS A NZ  
226  N N   . THR A 39  ? 1.2260 1.1532 1.2696 0.0105  -0.0431 0.1119  46  THR A N   
227  C CA  . THR A 39  ? 1.2208 1.1298 1.2385 0.0155  -0.0278 0.1357  46  THR A CA  
228  C C   . THR A 39  ? 1.2340 1.1557 1.1841 -0.0016 -0.0410 0.1315  46  THR A C   
229  O O   . THR A 39  ? 1.2073 1.1656 1.1323 -0.0065 -0.0691 0.1498  46  THR A O   
230  C CB  . THR A 39  ? 1.1308 1.0505 1.1747 0.0382  -0.0282 0.1840  46  THR A CB  
231  O OG1 . THR A 39  ? 1.0920 0.9907 1.1936 0.0531  -0.0101 0.1830  46  THR A OG1 
232  C CG2 . THR A 39  ? 1.2199 1.1155 1.2361 0.0440  -0.0094 0.2122  46  THR A CG2 
233  N N   . VAL A 40  ? 1.2249 1.1178 1.1455 -0.0120 -0.0196 0.1084  47  VAL A N   
234  C CA  . VAL A 40  ? 1.3254 1.2168 1.1756 -0.0295 -0.0223 0.0954  47  VAL A CA  
235  C C   . VAL A 40  ? 1.3488 1.2392 1.1459 -0.0293 -0.0195 0.1283  47  VAL A C   
236  O O   . VAL A 40  ? 1.4404 1.3444 1.1718 -0.0451 -0.0375 0.1304  47  VAL A O   
237  C CB  . VAL A 40  ? 1.3357 1.1988 1.1800 -0.0375 0.0037  0.0587  47  VAL A CB  
238  C CG1 . VAL A 40  ? 1.2762 1.1437 1.1660 -0.0380 -0.0032 0.0313  47  VAL A CG1 
239  C CG2 . VAL A 40  ? 1.3656 1.2051 1.2303 -0.0304 0.0371  0.0655  47  VAL A CG2 
240  N N   . TYR A 41  ? 1.3601 1.2316 1.1813 -0.0144 0.0034  0.1534  48  TYR A N   
241  C CA  . TYR A 41  ? 1.4438 1.3091 1.2196 -0.0107 0.0114  0.1907  48  TYR A CA  
242  C C   . TYR A 41  ? 1.4038 1.2688 1.2283 0.0126  0.0149  0.2343  48  TYR A C   
243  O O   . TYR A 41  ? 1.2520 1.0954 1.1379 0.0221  0.0335  0.2268  48  TYR A O   
244  C CB  . TYR A 41  ? 1.5058 1.3344 1.2551 -0.0178 0.0505  0.1769  48  TYR A CB  
245  C CG  . TYR A 41  ? 1.6442 1.4587 1.3400 -0.0159 0.0665  0.2129  48  TYR A CG  
246  C CD1 . TYR A 41  ? 1.6437 1.4398 1.3741 -0.0003 0.0869  0.2483  48  TYR A CD1 
247  C CD2 . TYR A 41  ? 1.7342 1.5462 1.3381 -0.0319 0.0658  0.2106  48  TYR A CD2 
248  C CE1 . TYR A 41  ? 1.7554 1.5361 1.4357 0.0020  0.1037  0.2849  48  TYR A CE1 
249  C CE2 . TYR A 41  ? 1.7588 1.5560 1.3056 -0.0311 0.0821  0.2453  48  TYR A CE2 
250  C CZ  . TYR A 41  ? 1.8175 1.6011 1.4051 -0.0129 0.1005  0.2844  48  TYR A CZ  
251  O OH  . TYR A 41  ? 1.8570 1.6238 1.3876 -0.0114 0.1185  0.3221  48  TYR A OH  
252  N N   . LYS A 42  ? 1.4739 1.3619 1.2683 0.0206  -0.0029 0.2800  49  LYS A N   
253  C CA  . LYS A 42  ? 1.5538 1.4309 1.3792 0.0457  0.0105  0.3314  49  LYS A CA  
254  C C   . LYS A 42  ? 1.6525 1.5315 1.4040 0.0435  0.0100  0.3706  49  LYS A C   
255  O O   . LYS A 42  ? 1.6895 1.6081 1.3819 0.0303  -0.0242 0.3799  49  LYS A O   
256  C CB  . LYS A 42  ? 1.5741 1.4893 1.4567 0.0670  -0.0145 0.3618  49  LYS A CB  
257  C CG  . LYS A 42  ? 1.5370 1.4237 1.5003 0.0829  0.0085  0.3484  49  LYS A CG  
258  C CD  . LYS A 42  ? 1.5293 1.4557 1.5493 0.1064  -0.0111 0.3805  49  LYS A CD  
259  C CE  . LYS A 42  ? 1.4503 1.3395 1.5400 0.1209  0.0174  0.3639  49  LYS A CE  
260  N NZ  . LYS A 42  ? 1.3983 1.3294 1.5440 0.1392  0.0005  0.3806  49  LYS A NZ  
261  N N   . GLY A 43  ? 1.7015 1.5372 1.4522 0.0526  0.0476  0.3928  50  GLY A N   
262  C CA  . GLY A 43  ? 1.8632 1.6925 1.5393 0.0504  0.0544  0.4306  50  GLY A CA  
263  C C   . GLY A 43  ? 1.9352 1.7074 1.6150 0.0539  0.1055  0.4409  50  GLY A C   
264  O O   . GLY A 43  ? 1.8726 1.6122 1.6222 0.0647  0.1316  0.4383  50  GLY A O   
265  N N   . PRO A 44  ? 2.0519 1.8096 1.6531 0.0424  0.1216  0.4538  51  PRO A N   
266  C CA  . PRO A 44  ? 2.0467 1.7532 1.6473 0.0389  0.1737  0.4564  51  PRO A CA  
267  C C   . PRO A 44  ? 1.9030 1.5891 1.5465 0.0222  0.2023  0.3993  51  PRO A C   
268  O O   . PRO A 44  ? 1.7075 1.4156 1.3554 0.0110  0.1842  0.3547  51  PRO A O   
269  C CB  . PRO A 44  ? 2.2115 1.9178 1.7040 0.0270  0.1776  0.4763  51  PRO A CB  
270  C CG  . PRO A 44  ? 2.2827 2.0346 1.7347 0.0353  0.1283  0.5169  51  PRO A CG  
271  C CD  . PRO A 44  ? 2.1850 1.9760 1.6969 0.0374  0.0903  0.4883  51  PRO A CD  
272  N N   . ASN A 45  ? 1.8829 1.5294 1.5560 0.0192  0.2472  0.4049  52  ASN A N   
273  C CA  . ASN A 45  ? 1.8056 1.4407 1.5329 0.0029  0.2741  0.3609  52  ASN A CA  
274  C C   . ASN A 45  ? 1.7811 1.4246 1.4625 -0.0131 0.2908  0.3318  52  ASN A C   
275  O O   . ASN A 45  ? 1.7707 1.3963 1.3973 -0.0171 0.3202  0.3522  52  ASN A O   
276  C CB  . ASN A 45  ? 1.8088 1.4018 1.5840 0.0000  0.3161  0.3800  52  ASN A CB  
277  C CG  . ASN A 45  ? 1.7863 1.3766 1.6300 -0.0203 0.3369  0.3401  52  ASN A CG  
278  O OD1 . ASN A 45  ? 1.7159 1.3340 1.5909 -0.0262 0.3150  0.3005  52  ASN A OD1 
279  N ND2 . ASN A 45  ? 1.8188 1.3787 1.6889 -0.0330 0.3785  0.3526  52  ASN A ND2 
280  N N   . CYS A 46  ? 1.7639 1.4312 1.4660 -0.0204 0.2753  0.2865  53  CYS A N   
281  C CA  . CYS A 46  ? 1.8221 1.4931 1.5042 -0.0320 0.2990  0.2542  53  CYS A CA  
282  C C   . CYS A 46  ? 1.8253 1.5023 1.5997 -0.0397 0.3223  0.2313  53  CYS A C   
283  O O   . CYS A 46  ? 1.8799 1.5762 1.7098 -0.0405 0.2991  0.2058  53  CYS A O   
284  C CB  . CYS A 46  ? 1.7843 1.4749 1.4238 -0.0345 0.2675  0.2231  53  CYS A CB  
285  S SG  . CYS A 46  ? 1.5312 1.2501 1.2314 -0.0285 0.2174  0.2048  53  CYS A SG  
286  N N   . ILE A 47  ? 1.9805 1.6449 1.7701 -0.0473 0.3670  0.2425  54  ILE A N   
287  C CA  . ILE A 47  ? 1.9984 1.6735 1.8821 -0.0597 0.3874  0.2325  54  ILE A CA  
288  C C   . ILE A 47  ? 1.9059 1.6118 1.8317 -0.0654 0.4061  0.2049  54  ILE A C   
289  O O   . ILE A 47  ? 1.7579 1.4875 1.7682 -0.0773 0.4082  0.1948  54  ILE A O   
290  C CB  . ILE A 47  ? 2.1727 1.8216 2.0679 -0.0687 0.4284  0.2646  54  ILE A CB  
291  C CG1 . ILE A 47  ? 2.2969 1.9083 2.1317 -0.0571 0.4228  0.3054  54  ILE A CG1 
292  C CG2 . ILE A 47  ? 2.1938 1.8458 2.1802 -0.0878 0.4397  0.2611  54  ILE A CG2 
293  C CD1 . ILE A 47  ? 2.3451 1.9217 2.2049 -0.0660 0.4602  0.3378  54  ILE A CD1 
294  N N   . GLU A 48  ? 1.8820 1.5866 1.7503 -0.0580 0.4217  0.1946  55  GLU A N   
295  C CA  . GLU A 48  ? 1.9073 1.6339 1.8151 -0.0581 0.4568  0.1785  55  GLU A CA  
296  C C   . GLU A 48  ? 1.7407 1.5032 1.7121 -0.0548 0.4318  0.1492  55  GLU A C   
297  O O   . GLU A 48  ? 1.7213 1.5202 1.7810 -0.0601 0.4451  0.1470  55  GLU A O   
298  C CB  . GLU A 48  ? 2.0874 1.7873 1.9032 -0.0508 0.4904  0.1755  55  GLU A CB  
299  C CG  . GLU A 48  ? 2.1826 1.8496 1.9345 -0.0548 0.5249  0.2070  55  GLU A CG  
300  C CD  . GLU A 48  ? 2.3329 1.9665 1.9740 -0.0514 0.5560  0.1999  55  GLU A CD  
301  O OE1 . GLU A 48  ? 2.3399 1.9759 1.9922 -0.0459 0.5896  0.1775  55  GLU A OE1 
302  O OE2 . GLU A 48  ? 2.4087 2.0120 1.9499 -0.0547 0.5491  0.2183  55  GLU A OE2 
303  N N   . HIS A 49  ? 1.6057 1.3617 1.5341 -0.0477 0.3944  0.1303  56  HIS A N   
304  C CA  . HIS A 49  ? 1.5170 1.2985 1.4872 -0.0421 0.3731  0.1032  56  HIS A CA  
305  C C   . HIS A 49  ? 1.4162 1.2190 1.4418 -0.0475 0.3273  0.0961  56  HIS A C   
306  O O   . HIS A 49  ? 1.3732 1.1918 1.4175 -0.0426 0.3043  0.0755  56  HIS A O   
307  C CB  . HIS A 49  ? 1.6017 1.3582 1.4884 -0.0340 0.3687  0.0827  56  HIS A CB  
308  C CG  . HIS A 49  ? 1.7141 1.4455 1.5493 -0.0295 0.4204  0.0805  56  HIS A CG  
309  N ND1 . HIS A 49  ? 1.7762 1.4723 1.5198 -0.0347 0.4401  0.0938  56  HIS A ND1 
310  C CD2 . HIS A 49  ? 1.6996 1.4336 1.5608 -0.0190 0.4603  0.0681  56  HIS A CD2 
311  C CE1 . HIS A 49  ? 1.8448 1.5182 1.5534 -0.0300 0.4917  0.0857  56  HIS A CE1 
312  N NE2 . HIS A 49  ? 1.8099 1.5048 1.5924 -0.0187 0.5070  0.0704  56  HIS A NE2 
313  N N   . ASN A 50  ? 1.3652 1.1643 1.4184 -0.0585 0.3196  0.1125  57  ASN A N   
314  C CA  . ASN A 50  ? 1.2300 1.0432 1.3386 -0.0679 0.2866  0.1039  57  ASN A CA  
315  C C   . ASN A 50  ? 1.1342 0.9919 1.3223 -0.0762 0.2828  0.0898  57  ASN A C   
316  O O   . ASN A 50  ? 1.0134 0.8845 1.2264 -0.0800 0.2509  0.0749  57  ASN A O   
317  C CB  . ASN A 50  ? 1.2355 1.0251 1.3580 -0.0810 0.2922  0.1235  57  ASN A CB  
318  C CG  . ASN A 50  ? 1.2719 1.0232 1.3274 -0.0691 0.2857  0.1432  57  ASN A CG  
319  O OD1 . ASN A 50  ? 1.3560 1.1033 1.3495 -0.0554 0.2752  0.1435  57  ASN A OD1 
320  N ND2 . ASN A 50  ? 1.3012 1.0244 1.3694 -0.0757 0.2928  0.1620  57  ASN A ND2 
321  N N   . GLU A 51  ? 1.2330 1.1166 1.4619 -0.0790 0.3160  0.0982  58  GLU A N   
322  C CA  . GLU A 51  ? 1.2244 1.1628 1.5343 -0.0828 0.3141  0.0930  58  GLU A CA  
323  C C   . GLU A 51  ? 1.1271 1.0757 1.4267 -0.0617 0.3021  0.0764  58  GLU A C   
324  O O   . GLU A 51  ? 1.0836 1.0682 1.4337 -0.0641 0.2770  0.0692  58  GLU A O   
325  C CB  . GLU A 51  ? 1.2608 1.2287 1.6221 -0.0870 0.3580  0.1120  58  GLU A CB  
326  C CG  . GLU A 51  ? 1.2905 1.2594 1.6864 -0.1156 0.3673  0.1275  58  GLU A CG  
327  C CD  . GLU A 51  ? 1.3989 1.3740 1.8125 -0.1170 0.4193  0.1496  58  GLU A CD  
328  O OE1 . GLU A 51  ? 1.5073 1.4402 1.8481 -0.1001 0.4476  0.1553  58  GLU A OE1 
329  O OE2 . GLU A 51  ? 1.4256 1.4495 1.9242 -0.1377 0.4318  0.1619  58  GLU A OE2 
330  N N   . ALA A 52  ? 1.0887 1.0029 1.3194 -0.0436 0.3217  0.0710  59  ALA A N   
331  C CA  . ALA A 52  ? 1.0634 0.9710 1.2708 -0.0258 0.3163  0.0528  59  ALA A CA  
332  C C   . ALA A 52  ? 1.0669 0.9595 1.2405 -0.0277 0.2700  0.0359  59  ALA A C   
333  O O   . ALA A 52  ? 0.9698 0.8738 1.1602 -0.0196 0.2546  0.0231  59  ALA A O   
334  C CB  . ALA A 52  ? 1.1627 1.0295 1.2963 -0.0130 0.3547  0.0481  59  ALA A CB  
335  N N   . LEU A 53  ? 1.0695 0.9367 1.1978 -0.0364 0.2514  0.0392  60  LEU A N   
336  C CA  . LEU A 53  ? 1.0370 0.8957 1.1460 -0.0384 0.2104  0.0282  60  LEU A CA  
337  C C   . LEU A 53  ? 1.0013 0.8883 1.1754 -0.0476 0.1854  0.0234  60  LEU A C   
338  O O   . LEU A 53  ? 0.9602 0.8516 1.1347 -0.0441 0.1602  0.0093  60  LEU A O   
339  C CB  . LEU A 53  ? 1.0546 0.8862 1.1151 -0.0420 0.2009  0.0411  60  LEU A CB  
340  C CG  . LEU A 53  ? 1.1353 0.9403 1.1125 -0.0367 0.2106  0.0455  60  LEU A CG  
341  C CD1 . LEU A 53  ? 1.2240 1.0122 1.1711 -0.0388 0.2064  0.0709  60  LEU A CD1 
342  C CD2 . LEU A 53  ? 1.0856 0.8846 1.0184 -0.0337 0.1864  0.0259  60  LEU A CD2 
343  N N   . LEU A 54  ? 1.0462 0.9505 1.2701 -0.0627 0.1931  0.0346  61  LEU A N   
344  C CA  . LEU A 54  ? 0.9927 0.9247 1.2722 -0.0793 0.1703  0.0290  61  LEU A CA  
345  C C   . LEU A 54  ? 0.9160 0.8936 1.2438 -0.0736 0.1650  0.0256  61  LEU A C   
346  O O   . LEU A 54  ? 0.7923 0.7850 1.1361 -0.0788 0.1368  0.0161  61  LEU A O   
347  C CB  . LEU A 54  ? 0.9996 0.9366 1.3162 -0.1040 0.1817  0.0405  61  LEU A CB  
348  C CG  . LEU A 54  ? 0.9828 0.9380 1.3404 -0.1312 0.1576  0.0314  61  LEU A CG  
349  C CD1 . LEU A 54  ? 0.9767 0.9009 1.3041 -0.1345 0.1341  0.0167  61  LEU A CD1 
350  C CD2 . LEU A 54  ? 1.0129 0.9740 1.4093 -0.1609 0.1772  0.0434  61  LEU A CD2 
351  N N   . GLU A 55  ? 0.9799 0.9774 1.3302 -0.0610 0.1950  0.0360  62  GLU A N   
352  C CA  . GLU A 55  ? 0.9738 1.0133 1.3746 -0.0476 0.1970  0.0398  62  GLU A CA  
353  C C   . GLU A 55  ? 0.9158 0.9296 1.2742 -0.0283 0.1853  0.0237  62  GLU A C   
354  O O   . GLU A 55  ? 0.9936 1.0349 1.3862 -0.0229 0.1680  0.0240  62  GLU A O   
355  C CB  . GLU A 55  ? 1.0510 1.1119 1.4883 -0.0346 0.2417  0.0572  62  GLU A CB  
356  C CG  . GLU A 55  ? 1.1297 1.2483 1.6457 -0.0204 0.2475  0.0722  62  GLU A CG  
357  C CD  . GLU A 55  ? 1.2059 1.3952 1.8068 -0.0452 0.2256  0.0897  62  GLU A CD  
358  O OE1 . GLU A 55  ? 1.2625 1.4730 1.8986 -0.0604 0.2460  0.1035  62  GLU A OE1 
359  O OE2 . GLU A 55  ? 1.2230 1.4463 1.8519 -0.0525 0.1883  0.0898  62  GLU A OE2 
360  N N   . GLU A 56  ? 0.9559 0.9192 1.2398 -0.0207 0.1937  0.0117  63  GLU A N   
361  C CA  . GLU A 56  ? 0.8817 0.8158 1.1182 -0.0103 0.1800  -0.0063 63  GLU A CA  
362  C C   . GLU A 56  ? 0.8852 0.8200 1.1173 -0.0215 0.1383  -0.0155 63  GLU A C   
363  O O   . GLU A 56  ? 0.8978 0.8303 1.1261 -0.0152 0.1230  -0.0255 63  GLU A O   
364  C CB  . GLU A 56  ? 0.9301 0.8168 1.0862 -0.0072 0.1973  -0.0153 63  GLU A CB  
365  C CG  . GLU A 56  ? 0.9746 0.8290 1.0808 0.0004  0.1963  -0.0347 63  GLU A CG  
366  C CD  . GLU A 56  ? 1.1271 0.9383 1.1544 -0.0005 0.2227  -0.0431 63  GLU A CD  
367  O OE1 . GLU A 56  ? 1.2304 1.0215 1.1960 -0.0121 0.2017  -0.0501 63  GLU A OE1 
368  O OE2 . GLU A 56  ? 1.1058 0.9049 1.1318 0.0097  0.2656  -0.0412 63  GLU A OE2 
369  N N   . ALA A 57  ? 0.8897 0.8222 1.1212 -0.0371 0.1252  -0.0116 64  ALA A N   
370  C CA  . ALA A 57  ? 0.7937 0.7252 1.0283 -0.0484 0.0939  -0.0193 64  ALA A CA  
371  C C   . ALA A 57  ? 0.7594 0.7284 1.0457 -0.0567 0.0779  -0.0190 64  ALA A C   
372  O O   . ALA A 57  ? 0.8415 0.8081 1.1200 -0.0578 0.0558  -0.0288 64  ALA A O   
373  C CB  . ALA A 57  ? 0.7582 0.6702 0.9826 -0.0617 0.0927  -0.0139 64  ALA A CB  
374  N N   . LYS A 58  ? 0.7431 0.7504 1.0817 -0.0634 0.0888  -0.0052 65  LYS A N   
375  C CA  . LYS A 58  ? 0.7247 0.7818 1.1170 -0.0723 0.0705  0.0018  65  LYS A CA  
376  C C   . LYS A 58  ? 0.7646 0.8318 1.1620 -0.0492 0.0670  0.0030  65  LYS A C   
377  O O   . LYS A 58  ? 0.7415 0.8255 1.1473 -0.0546 0.0409  0.0016  65  LYS A O   
378  C CB  . LYS A 58  ? 0.8171 0.9248 1.2744 -0.0837 0.0834  0.0217  65  LYS A CB  
379  C CG  . LYS A 58  ? 0.9159 1.0219 1.3809 -0.1176 0.0790  0.0203  65  LYS A CG  
380  C CD  . LYS A 58  ? 0.9717 1.1298 1.5041 -0.1311 0.0953  0.0411  65  LYS A CD  
381  C CE  . LYS A 58  ? 0.9547 1.1030 1.4929 -0.1655 0.0988  0.0398  65  LYS A CE  
382  N NZ  . LYS A 58  ? 0.9655 1.1691 1.5750 -0.1789 0.1179  0.0620  65  LYS A NZ  
383  N N   . MET A 59  ? 0.8007 0.8500 1.1857 -0.0251 0.0960  0.0048  66  MET A N   
384  C CA  . MET A 59  ? 0.9401 0.9822 1.3228 -0.0017 0.1024  0.0044  66  MET A CA  
385  C C   . MET A 59  ? 0.9253 0.9329 1.2592 -0.0032 0.0794  -0.0143 66  MET A C   
386  O O   . MET A 59  ? 0.8193 0.8385 1.1683 0.0042  0.0670  -0.0105 66  MET A O   
387  C CB  . MET A 59  ? 1.0681 1.0791 1.4297 0.0195  0.1449  0.0030  66  MET A CB  
388  C CG  . MET A 59  ? 1.1305 1.1786 1.5523 0.0302  0.1774  0.0257  66  MET A CG  
389  S SD  . MET A 59  ? 1.3351 1.4452 1.8460 0.0499  0.1757  0.0545  66  MET A SD  
390  C CE  . MET A 59  ? 1.3746 1.4227 1.8444 0.0822  0.2088  0.0434  66  MET A CE  
391  N N   . MET A 60  ? 0.9262 0.8960 1.2067 -0.0122 0.0742  -0.0305 67  MET A N   
392  C CA  . MET A 60  ? 0.9089 0.8534 1.1517 -0.0157 0.0526  -0.0458 67  MET A CA  
393  C C   . MET A 60  ? 0.8955 0.8582 1.1545 -0.0310 0.0241  -0.0463 67  MET A C   
394  O O   . MET A 60  ? 0.8606 0.8123 1.1032 -0.0308 0.0094  -0.0544 67  MET A O   
395  C CB  . MET A 60  ? 0.9312 0.8397 1.1194 -0.0188 0.0550  -0.0573 67  MET A CB  
396  C CG  . MET A 60  ? 0.9424 0.8487 1.1239 -0.0302 0.0508  -0.0527 67  MET A CG  
397  S SD  . MET A 60  ? 0.9264 0.8028 1.0501 -0.0308 0.0439  -0.0581 67  MET A SD  
398  C CE  . MET A 60  ? 0.8995 0.7588 0.9831 -0.0253 0.0703  -0.0579 67  MET A CE  
399  N N   . ASN A 61  ? 0.8827 0.8702 1.1705 -0.0470 0.0189  -0.0386 68  ASN A N   
400  C CA  . ASN A 61  ? 0.7830 0.7845 1.0792 -0.0675 -0.0052 -0.0414 68  ASN A CA  
401  C C   . ASN A 61  ? 0.7180 0.7588 1.0442 -0.0672 -0.0214 -0.0303 68  ASN A C   
402  O O   . ASN A 61  ? 0.7229 0.7646 1.0350 -0.0821 -0.0428 -0.0363 68  ASN A O   
403  C CB  . ASN A 61  ? 0.8307 0.8406 1.1428 -0.0915 -0.0042 -0.0393 68  ASN A CB  
404  C CG  . ASN A 61  ? 0.7924 0.7863 1.0847 -0.1162 -0.0213 -0.0524 68  ASN A CG  
405  O OD1 . ASN A 61  ? 0.8226 0.8455 1.1330 -0.1393 -0.0376 -0.0506 68  ASN A OD1 
406  N ND2 . ASN A 61  ? 0.8726 0.8209 1.1268 -0.1123 -0.0168 -0.0650 68  ASN A ND2 
407  N N   . ARG A 62  ? 0.6863 0.7577 1.0516 -0.0491 -0.0092 -0.0120 69  ARG A N   
408  C CA  . ARG A 62  ? 0.7081 0.8216 1.1087 -0.0421 -0.0233 0.0072  69  ARG A CA  
409  C C   . ARG A 62  ? 0.7382 0.8237 1.1068 -0.0284 -0.0299 0.0016  69  ARG A C   
410  O O   . ARG A 62  ? 0.8403 0.9558 1.2266 -0.0270 -0.0472 0.0179  69  ARG A O   
411  C CB  . ARG A 62  ? 0.7536 0.9065 1.2136 -0.0207 -0.0016 0.0332  69  ARG A CB  
412  C CG  . ARG A 62  ? 0.8738 0.9911 1.3233 0.0131  0.0296  0.0334  69  ARG A CG  
413  C CD  . ARG A 62  ? 0.9213 1.0560 1.4153 0.0330  0.0660  0.0505  69  ARG A CD  
414  N NE  . ARG A 62  ? 0.9580 1.0515 1.4391 0.0643  0.1002  0.0498  69  ARG A NE  
415  C CZ  . ARG A 62  ? 1.0620 1.1673 1.5769 0.0893  0.1078  0.0711  69  ARG A CZ  
416  N NH1 . ARG A 62  ? 1.0170 1.1845 1.5830 0.0880  0.0783  0.0995  69  ARG A NH1 
417  N NH2 . ARG A 62  ? 1.0610 1.1118 1.5545 0.1148  0.1465  0.0649  69  ARG A NH2 
418  N N   . LEU A 63  ? 0.7192 0.7514 1.0427 -0.0201 -0.0168 -0.0185 70  LEU A N   
419  C CA  . LEU A 63  ? 0.8076 0.8086 1.1005 -0.0107 -0.0191 -0.0262 70  LEU A CA  
420  C C   . LEU A 63  ? 0.8372 0.8247 1.0970 -0.0303 -0.0407 -0.0404 70  LEU A C   
421  O O   . LEU A 63  ? 0.7571 0.7131 0.9857 -0.0366 -0.0380 -0.0584 70  LEU A O   
422  C CB  . LEU A 63  ? 0.7534 0.7084 1.0157 0.0026  0.0051  -0.0408 70  LEU A CB  
423  C CG  . LEU A 63  ? 0.6883 0.6427 0.9720 0.0219  0.0358  -0.0311 70  LEU A CG  
424  C CD1 . LEU A 63  ? 0.7096 0.6136 0.9448 0.0237  0.0562  -0.0518 70  LEU A CD1 
425  C CD2 . LEU A 63  ? 0.6907 0.6611 1.0136 0.0443  0.0471  -0.0084 70  LEU A CD2 
426  N N   . ARG A 64  ? 0.8772 0.8907 1.1447 -0.0390 -0.0606 -0.0294 71  ARG A N   
427  C CA  . ARG A 64  ? 0.9340 0.9315 1.1650 -0.0572 -0.0765 -0.0418 71  ARG A CA  
428  C C   . ARG A 64  ? 0.8837 0.8700 1.1001 -0.0457 -0.0788 -0.0350 71  ARG A C   
429  O O   . ARG A 64  ? 0.7757 0.7924 1.0135 -0.0381 -0.0874 -0.0117 71  ARG A O   
430  C CB  . ARG A 64  ? 0.9950 1.0250 1.2306 -0.0846 -0.0978 -0.0376 71  ARG A CB  
431  C CG  . ARG A 64  ? 1.1543 1.1868 1.4011 -0.1010 -0.0928 -0.0461 71  ARG A CG  
432  C CD  . ARG A 64  ? 1.4061 1.4244 1.6215 -0.1352 -0.1040 -0.0626 71  ARG A CD  
433  N NE  . ARG A 64  ? 1.4318 1.4381 1.6546 -0.1495 -0.0927 -0.0716 71  ARG A NE  
434  C CZ  . ARG A 64  ? 1.3765 1.3416 1.5870 -0.1390 -0.0718 -0.0827 71  ARG A CZ  
435  N NH1 . ARG A 64  ? 1.3049 1.2417 1.4975 -0.1163 -0.0619 -0.0877 71  ARG A NH1 
436  N NH2 . ARG A 64  ? 1.6209 1.5761 1.8394 -0.1530 -0.0614 -0.0860 71  ARG A NH2 
437  N N   . HIS A 65  ? 0.8461 0.7923 1.0310 -0.0439 -0.0704 -0.0517 72  HIS A N   
438  C CA  . HIS A 65  ? 0.7833 0.7131 0.9515 -0.0366 -0.0695 -0.0465 72  HIS A CA  
439  C C   . HIS A 65  ? 0.7161 0.6112 0.8527 -0.0444 -0.0635 -0.0665 72  HIS A C   
440  O O   . HIS A 65  ? 0.6928 0.5739 0.8284 -0.0450 -0.0552 -0.0806 72  HIS A O   
441  C CB  . HIS A 65  ? 0.6869 0.6063 0.8737 -0.0131 -0.0523 -0.0356 72  HIS A CB  
442  C CG  . HIS A 65  ? 0.7676 0.6766 0.9477 -0.0035 -0.0508 -0.0201 72  HIS A CG  
443  N ND1 . HIS A 65  ? 0.7617 0.6290 0.9242 0.0017  -0.0342 -0.0292 72  HIS A ND1 
444  C CD2 . HIS A 65  ? 0.7264 0.6628 0.9154 0.0007  -0.0641 0.0068  72  HIS A CD2 
445  C CE1 . HIS A 65  ? 0.7617 0.6248 0.9217 0.0102  -0.0337 -0.0091 72  HIS A CE1 
446  N NE2 . HIS A 65  ? 0.6883 0.5944 0.8632 0.0112  -0.0528 0.0146  72  HIS A NE2 
447  N N   . SER A 66  ? 0.7615 0.6459 0.8751 -0.0491 -0.0664 -0.0642 73  SER A N   
448  C CA  . SER A 66  ? 0.8108 0.6668 0.9011 -0.0562 -0.0569 -0.0804 73  SER A CA  
449  C C   . SER A 66  ? 0.8170 0.6552 0.9170 -0.0482 -0.0433 -0.0887 73  SER A C   
450  O O   . SER A 66  ? 0.7819 0.6103 0.8784 -0.0536 -0.0371 -0.1001 73  SER A O   
451  C CB  . SER A 66  ? 0.8792 0.7255 0.9409 -0.0620 -0.0582 -0.0738 73  SER A CB  
452  O OG  . SER A 66  ? 0.9824 0.8226 1.0504 -0.0487 -0.0531 -0.0583 73  SER A OG  
453  N N   . ARG A 67  ? 0.7248 0.5591 0.8372 -0.0366 -0.0376 -0.0819 74  ARG A N   
454  C CA  . ARG A 67  ? 0.6989 0.5134 0.8126 -0.0353 -0.0259 -0.0923 74  ARG A CA  
455  C C   . ARG A 67  ? 0.6705 0.4891 0.7912 -0.0324 -0.0233 -0.0987 74  ARG A C   
456  O O   . ARG A 67  ? 0.7126 0.5115 0.8255 -0.0337 -0.0133 -0.1073 74  ARG A O   
457  C CB  . ARG A 67  ? 0.7285 0.5181 0.8392 -0.0278 -0.0129 -0.0845 74  ARG A CB  
458  C CG  . ARG A 67  ? 0.7044 0.4896 0.8057 -0.0269 -0.0138 -0.0704 74  ARG A CG  
459  C CD  . ARG A 67  ? 0.7782 0.5613 0.8660 -0.0413 -0.0152 -0.0806 74  ARG A CD  
460  N NE  . ARG A 67  ? 0.9073 0.6835 0.9770 -0.0415 -0.0140 -0.0666 74  ARG A NE  
461  C CZ  . ARG A 67  ? 0.9498 0.7247 0.9998 -0.0519 -0.0131 -0.0702 74  ARG A CZ  
462  N NH1 . ARG A 67  ? 0.8335 0.6134 0.8868 -0.0605 -0.0108 -0.0863 74  ARG A NH1 
463  N NH2 . ARG A 67  ? 1.0666 0.8324 1.0921 -0.0523 -0.0112 -0.0549 74  ARG A NH2 
464  N N   . VAL A 68  ? 0.7081 0.5481 0.8381 -0.0319 -0.0307 -0.0957 75  VAL A N   
465  C CA  . VAL A 68  ? 0.6942 0.5381 0.8273 -0.0302 -0.0267 -0.1000 75  VAL A CA  
466  C C   . VAL A 68  ? 0.7349 0.5907 0.8687 -0.0381 -0.0349 -0.1035 75  VAL A C   
467  O O   . VAL A 68  ? 0.7685 0.6318 0.9051 -0.0434 -0.0413 -0.1011 75  VAL A O   
468  C CB  . VAL A 68  ? 0.6750 0.5310 0.8265 -0.0186 -0.0199 -0.0879 75  VAL A CB  
469  C CG1 . VAL A 68  ? 0.7006 0.5533 0.8481 -0.0169 -0.0094 -0.0931 75  VAL A CG1 
470  C CG2 . VAL A 68  ? 0.8221 0.6624 0.9787 -0.0052 -0.0064 -0.0792 75  VAL A CG2 
471  N N   . VAL A 69  ? 0.6834 0.5375 0.8107 -0.0401 -0.0335 -0.1082 76  VAL A N   
472  C CA  . VAL A 69  ? 0.6873 0.5493 0.8189 -0.0428 -0.0370 -0.1059 76  VAL A CA  
473  C C   . VAL A 69  ? 0.6973 0.5671 0.8389 -0.0427 -0.0348 -0.1002 76  VAL A C   
474  O O   . VAL A 69  ? 0.8077 0.6819 0.9519 -0.0382 -0.0285 -0.0967 76  VAL A O   
475  C CB  . VAL A 69  ? 0.6894 0.5540 0.8113 -0.0439 -0.0388 -0.1055 76  VAL A CB  
476  C CG1 . VAL A 69  ? 0.6379 0.5089 0.7667 -0.0415 -0.0388 -0.0961 76  VAL A CG1 
477  C CG2 . VAL A 69  ? 0.6226 0.4902 0.7445 -0.0495 -0.0446 -0.1090 76  VAL A CG2 
478  N N   . LYS A 70  ? 0.7635 0.6330 0.9098 -0.0499 -0.0372 -0.1003 77  LYS A N   
479  C CA  . LYS A 70  ? 0.8477 0.7252 1.0045 -0.0574 -0.0363 -0.0964 77  LYS A CA  
480  C C   . LYS A 70  ? 0.7624 0.6320 0.9198 -0.0560 -0.0279 -0.0925 77  LYS A C   
481  O O   . LYS A 70  ? 0.7609 0.6168 0.9127 -0.0529 -0.0245 -0.0924 77  LYS A O   
482  C CB  . LYS A 70  ? 0.9440 0.8170 1.0952 -0.0731 -0.0415 -0.1016 77  LYS A CB  
483  C CG  . LYS A 70  ? 1.1907 1.0801 1.3411 -0.0757 -0.0530 -0.0982 77  LYS A CG  
484  C CD  . LYS A 70  ? 1.1988 1.0801 1.3272 -0.0945 -0.0600 -0.1052 77  LYS A CD  
485  C CE  . LYS A 70  ? 1.0997 1.0037 1.2263 -0.0954 -0.0745 -0.0947 77  LYS A CE  
486  N NZ  . LYS A 70  ? 1.1124 0.9960 1.2046 -0.1028 -0.0751 -0.1017 77  LYS A NZ  
487  N N   . LEU A 71  ? 0.7957 0.6761 0.9634 -0.0564 -0.0225 -0.0858 78  LEU A N   
488  C CA  . LEU A 71  ? 0.6964 0.5677 0.8652 -0.0586 -0.0125 -0.0791 78  LEU A CA  
489  C C   . LEU A 71  ? 0.7326 0.5928 0.9077 -0.0757 -0.0110 -0.0835 78  LEU A C   
490  O O   . LEU A 71  ? 0.7667 0.6440 0.9544 -0.0900 -0.0171 -0.0854 78  LEU A O   
491  C CB  . LEU A 71  ? 0.7116 0.5969 0.8891 -0.0556 -0.0029 -0.0706 78  LEU A CB  
492  C CG  . LEU A 71  ? 0.7523 0.6270 0.9284 -0.0579 0.0105  -0.0604 78  LEU A CG  
493  C CD1 . LEU A 71  ? 0.7403 0.6035 0.8891 -0.0460 0.0129  -0.0533 78  LEU A CD1 
494  C CD2 . LEU A 71  ? 0.6990 0.5917 0.8955 -0.0620 0.0227  -0.0527 78  LEU A CD2 
495  N N   . LEU A 72  ? 0.7249 0.5562 0.8910 -0.0753 -0.0021 -0.0842 79  LEU A N   
496  C CA  . LEU A 72  ? 0.7450 0.5490 0.9067 -0.0937 0.0062  -0.0930 79  LEU A CA  
497  C C   . LEU A 72  ? 0.7967 0.5885 0.9673 -0.1041 0.0199  -0.0861 79  LEU A C   
498  O O   . LEU A 72  ? 0.8486 0.6299 1.0192 -0.1298 0.0225  -0.0954 79  LEU A O   
499  C CB  . LEU A 72  ? 0.8240 0.5953 0.9744 -0.0852 0.0175  -0.0968 79  LEU A CB  
500  C CG  . LEU A 72  ? 0.8379 0.6172 0.9792 -0.0813 0.0078  -0.1057 79  LEU A CG  
501  C CD1 . LEU A 72  ? 0.7744 0.5312 0.9170 -0.0661 0.0229  -0.1026 79  LEU A CD1 
502  C CD2 . LEU A 72  ? 0.8359 0.6113 0.9590 -0.1053 0.0005  -0.1216 79  LEU A CD2 
503  N N   . GLY A 73  ? 0.7862 0.5788 0.9608 -0.0876 0.0283  -0.0696 80  GLY A N   
504  C CA  . GLY A 73  ? 0.8146 0.6021 0.9987 -0.0959 0.0421  -0.0591 80  GLY A CA  
505  C C   . GLY A 73  ? 0.8304 0.6247 1.0087 -0.0759 0.0483  -0.0393 80  GLY A C   
506  O O   . GLY A 73  ? 0.7983 0.6036 0.9637 -0.0582 0.0389  -0.0347 80  GLY A O   
507  N N   . VAL A 74  ? 0.8599 0.6470 1.0443 -0.0827 0.0643  -0.0277 81  VAL A N   
508  C CA  . VAL A 74  ? 0.9019 0.6904 1.0722 -0.0676 0.0740  -0.0066 81  VAL A CA  
509  C C   . VAL A 74  ? 0.9271 0.6788 1.0978 -0.0698 0.0965  0.0106  81  VAL A C   
510  O O   . VAL A 74  ? 1.0237 0.7549 1.2104 -0.0907 0.1088  0.0034  81  VAL A O   
511  C CB  . VAL A 74  ? 0.8744 0.6923 1.0493 -0.0705 0.0783  -0.0053 81  VAL A CB  
512  C CG1 . VAL A 74  ? 0.8905 0.7345 1.0603 -0.0625 0.0620  -0.0182 81  VAL A CG1 
513  C CG2 . VAL A 74  ? 0.8225 0.6511 1.0319 -0.0934 0.0880  -0.0088 81  VAL A CG2 
514  N N   . ILE A 75  ? 0.9380 0.6815 1.0891 -0.0498 0.1007  0.0346  82  ILE A N   
515  C CA  . ILE A 75  ? 0.9146 0.6240 1.0626 -0.0450 0.1237  0.0601  82  ILE A CA  
516  C C   . ILE A 75  ? 1.0129 0.7388 1.1414 -0.0440 0.1311  0.0754  82  ILE A C   
517  O O   . ILE A 75  ? 1.0422 0.7915 1.1415 -0.0312 0.1174  0.0828  82  ILE A O   
518  C CB  . ILE A 75  ? 0.9425 0.6391 1.0844 -0.0194 0.1215  0.0841  82  ILE A CB  
519  C CG1 . ILE A 75  ? 0.9270 0.6068 1.0881 -0.0189 0.1197  0.0662  82  ILE A CG1 
520  C CG2 . ILE A 75  ? 1.0273 0.6866 1.1666 -0.0098 0.1480  0.1183  82  ILE A CG2 
521  C CD1 . ILE A 75  ? 0.9555 0.6217 1.1271 0.0080  0.1250  0.0908  82  ILE A CD1 
522  N N   . ILE A 76  ? 1.0445 0.7574 1.1870 -0.0612 0.1539  0.0778  83  ILE A N   
523  C CA  . ILE A 76  ? 1.0355 0.7564 1.1615 -0.0613 0.1709  0.0945  83  ILE A CA  
524  C C   . ILE A 76  ? 1.1359 0.8134 1.2637 -0.0641 0.1993  0.1201  83  ILE A C   
525  O O   . ILE A 76  ? 1.1162 0.7773 1.2734 -0.0875 0.2186  0.1138  83  ILE A O   
526  C CB  . ILE A 76  ? 1.0343 0.7870 1.1872 -0.0792 0.1763  0.0766  83  ILE A CB  
527  C CG1 . ILE A 76  ? 1.0420 0.8301 1.1931 -0.0724 0.1525  0.0552  83  ILE A CG1 
528  C CG2 . ILE A 76  ? 1.0981 0.8549 1.2364 -0.0785 0.2024  0.0944  83  ILE A CG2 
529  C CD1 . ILE A 76  ? 0.9701 0.7935 1.1622 -0.0859 0.1539  0.0405  83  ILE A CD1 
530  N N   . GLU A 77  ? 1.1436 0.8044 1.2411 -0.0417 0.2010  0.1511  84  GLU A N   
531  C CA  . GLU A 77  ? 1.2576 0.8714 1.3542 -0.0363 0.2285  0.1832  84  GLU A CA  
532  C C   . GLU A 77  ? 1.3403 0.9580 1.3924 -0.0210 0.2360  0.2206  84  GLU A C   
533  O O   . GLU A 77  ? 1.3099 0.9640 1.3257 -0.0158 0.2180  0.2184  84  GLU A O   
534  C CB  . GLU A 77  ? 1.2615 0.8476 1.3706 -0.0182 0.2246  0.1929  84  GLU A CB  
535  C CG  . GLU A 77  ? 1.2288 0.7931 1.3707 -0.0366 0.2269  0.1576  84  GLU A CG  
536  C CD  . GLU A 77  ? 1.2893 0.8186 1.4428 -0.0164 0.2329  0.1670  84  GLU A CD  
537  O OE1 . GLU A 77  ? 1.2692 0.8191 1.4157 0.0146  0.2188  0.1948  84  GLU A OE1 
538  O OE2 . GLU A 77  ? 1.2626 0.7444 1.4326 -0.0331 0.2526  0.1461  84  GLU A OE2 
539  N N   . GLU A 78  ? 1.4061 0.9804 1.4564 -0.0160 0.2649  0.2545  85  GLU A N   
540  C CA  . GLU A 78  ? 1.5005 1.0703 1.5047 -0.0013 0.2758  0.2981  85  GLU A CA  
541  C C   . GLU A 78  ? 1.4394 1.0413 1.4066 0.0252  0.2419  0.3234  85  GLU A C   
542  O O   . GLU A 78  ? 1.4404 1.0324 1.4254 0.0468  0.2352  0.3483  85  GLU A O   
543  C CB  . GLU A 78  ? 1.5936 1.1028 1.6108 0.0010  0.3152  0.3324  85  GLU A CB  
544  C CG  . GLU A 78  ? 1.7439 1.2418 1.7144 0.0095  0.3356  0.3777  85  GLU A CG  
545  C CD  . GLU A 78  ? 1.8012 1.2944 1.7698 -0.0176 0.3664  0.3658  85  GLU A CD  
546  O OE1 . GLU A 78  ? 1.7486 1.2784 1.7294 -0.0356 0.3571  0.3265  85  GLU A OE1 
547  O OE2 . GLU A 78  ? 1.8774 1.3309 1.8357 -0.0191 0.4023  0.3994  85  GLU A OE2 
548  N N   . GLY A 79  ? 1.4304 1.0716 1.3488 0.0214  0.2221  0.3156  86  GLY A N   
549  C CA  . GLY A 79  ? 1.4280 1.1073 1.3037 0.0359  0.1853  0.3345  86  GLY A CA  
550  C C   . GLY A 79  ? 1.3552 1.0689 1.2569 0.0408  0.1487  0.3120  86  GLY A C   
551  O O   . GLY A 79  ? 1.4000 1.1469 1.2825 0.0537  0.1183  0.3365  86  GLY A O   
552  N N   . LYS A 80  ? 1.2651 0.9752 1.2109 0.0293  0.1505  0.2686  87  LYS A N   
553  C CA  . LYS A 80  ? 1.2340 0.9716 1.2064 0.0330  0.1207  0.2460  87  LYS A CA  
554  C C   . LYS A 80  ? 1.2139 0.9545 1.2094 0.0139  0.1213  0.1954  87  LYS A C   
555  O O   . LYS A 80  ? 1.1627 0.8770 1.1923 0.0027  0.1438  0.1801  87  LYS A O   
556  C CB  . LYS A 80  ? 1.2134 0.9335 1.2337 0.0530  0.1250  0.2675  87  LYS A CB  
557  C CG  . LYS A 80  ? 1.1125 0.8663 1.1584 0.0619  0.0960  0.2569  87  LYS A CG  
558  C CD  . LYS A 80  ? 1.0911 0.8129 1.1907 0.0778  0.1146  0.2638  87  LYS A CD  
559  C CE  . LYS A 80  ? 1.0589 0.8074 1.1868 0.0802  0.0942  0.2404  87  LYS A CE  
560  N NZ  . LYS A 80  ? 1.0871 0.7950 1.2608 0.0946  0.1204  0.2431  87  LYS A NZ  
561  N N   . TYR A 81  ? 1.2645 1.0384 1.2412 0.0088  0.0953  0.1720  88  TYR A N   
562  C CA  . TYR A 81  ? 1.2152 0.9971 1.2063 -0.0059 0.0944  0.1301  88  TYR A CA  
563  C C   . TYR A 81  ? 1.0876 0.8935 1.0898 -0.0035 0.0653  0.1120  88  TYR A C   
564  O O   . TYR A 81  ? 1.1365 0.9659 1.1043 -0.0023 0.0432  0.1168  88  TYR A O   
565  C CB  . TYR A 81  ? 1.3434 1.1307 1.2904 -0.0154 0.1047  0.1202  88  TYR A CB  
566  C CG  . TYR A 81  ? 1.3907 1.1562 1.3263 -0.0182 0.1374  0.1404  88  TYR A CG  
567  C CD1 . TYR A 81  ? 1.4560 1.2130 1.3429 -0.0112 0.1414  0.1755  88  TYR A CD1 
568  C CD2 . TYR A 81  ? 1.4240 1.1812 1.3995 -0.0293 0.1638  0.1278  88  TYR A CD2 
569  C CE1 . TYR A 81  ? 1.6348 1.3683 1.5098 -0.0139 0.1747  0.1962  88  TYR A CE1 
570  C CE2 . TYR A 81  ? 1.5117 1.2506 1.4824 -0.0341 0.1963  0.1474  88  TYR A CE2 
571  C CZ  . TYR A 81  ? 1.5800 1.3033 1.4987 -0.0257 0.2038  0.1809  88  TYR A CZ  
572  O OH  . TYR A 81  ? 1.6610 1.3632 1.5726 -0.0306 0.2389  0.2020  88  TYR A OH  
573  N N   . SER A 82  ? 1.0276 0.8267 1.0745 -0.0055 0.0655  0.0930  89  SER A N   
574  C CA  . SER A 82  ? 0.9787 0.7964 1.0410 -0.0027 0.0429  0.0777  89  SER A CA  
575  C C   . SER A 82  ? 0.9266 0.7448 1.0099 -0.0149 0.0427  0.0434  89  SER A C   
576  O O   . SER A 82  ? 0.9048 0.7072 1.0089 -0.0246 0.0588  0.0346  89  SER A O   
577  C CB  . SER A 82  ? 0.9611 0.7686 1.0554 0.0118  0.0442  0.0958  89  SER A CB  
578  O OG  . SER A 82  ? 1.0341 0.8456 1.1184 0.0275  0.0441  0.1355  89  SER A OG  
579  N N   . LEU A 83  ? 0.9527 0.7911 1.0303 -0.0161 0.0233  0.0267  90  LEU A N   
580  C CA  . LEU A 83  ? 0.8535 0.6945 0.9516 -0.0238 0.0193  -0.0001 90  LEU A CA  
581  C C   . LEU A 83  ? 0.8810 0.7203 1.0008 -0.0184 0.0112  -0.0010 90  LEU A C   
582  O O   . LEU A 83  ? 0.8011 0.6541 0.9192 -0.0085 -0.0001 0.0140  90  LEU A O   
583  C CB  . LEU A 83  ? 0.7889 0.6445 0.8650 -0.0278 0.0098  -0.0167 90  LEU A CB  
584  C CG  . LEU A 83  ? 0.7885 0.6409 0.8375 -0.0307 0.0245  -0.0170 90  LEU A CG  
585  C CD1 . LEU A 83  ? 0.7576 0.6118 0.7783 -0.0341 0.0200  -0.0349 90  LEU A CD1 
586  C CD2 . LEU A 83  ? 0.7782 0.6279 0.8570 -0.0345 0.0440  -0.0189 90  LEU A CD2 
587  N N   . VAL A 84  ? 0.8403 0.6655 0.9807 -0.0261 0.0176  -0.0168 91  VAL A N   
588  C CA  . VAL A 84  ? 0.8825 0.6954 1.0392 -0.0227 0.0186  -0.0211 91  VAL A CA  
589  C C   . VAL A 84  ? 0.8314 0.6542 0.9884 -0.0318 0.0077  -0.0441 91  VAL A C   
590  O O   . VAL A 84  ? 0.7688 0.5924 0.9266 -0.0448 0.0078  -0.0567 91  VAL A O   
591  C CB  . VAL A 84  ? 0.9314 0.7054 1.0989 -0.0279 0.0407  -0.0205 91  VAL A CB  
592  C CG1 . VAL A 84  ? 0.9909 0.7429 1.1677 -0.0245 0.0493  -0.0284 91  VAL A CG1 
593  C CG2 . VAL A 84  ? 1.0411 0.8004 1.2092 -0.0163 0.0551  0.0071  91  VAL A CG2 
594  N N   . MET A 85  ? 0.7887 0.6224 0.9492 -0.0249 -0.0014 -0.0455 92  MET A N   
595  C CA  . MET A 85  ? 0.8466 0.6901 1.0040 -0.0313 -0.0117 -0.0630 92  MET A CA  
596  C C   . MET A 85  ? 0.8663 0.7020 1.0350 -0.0273 -0.0074 -0.0656 92  MET A C   
597  O O   . MET A 85  ? 0.7671 0.5965 0.9510 -0.0158 0.0028  -0.0514 92  MET A O   
598  C CB  . MET A 85  ? 0.8047 0.6704 0.9489 -0.0306 -0.0254 -0.0640 92  MET A CB  
599  C CG  . MET A 85  ? 0.9263 0.8081 1.0646 -0.0244 -0.0327 -0.0468 92  MET A CG  
600  S SD  . MET A 85  ? 1.1092 1.0105 1.2238 -0.0334 -0.0497 -0.0547 92  MET A SD  
601  C CE  . MET A 85  ? 0.8780 0.7905 1.0185 -0.0345 -0.0560 -0.0598 92  MET A CE  
602  N N   . GLU A 86  ? 0.8339 0.6701 0.9968 -0.0349 -0.0122 -0.0808 93  GLU A N   
603  C CA  . GLU A 86  ? 0.7710 0.5962 0.9393 -0.0333 -0.0038 -0.0858 93  GLU A CA  
604  C C   . GLU A 86  ? 0.6914 0.5398 0.8800 -0.0221 -0.0074 -0.0737 93  GLU A C   
605  O O   . GLU A 86  ? 0.7419 0.6164 0.9311 -0.0220 -0.0228 -0.0671 93  GLU A O   
606  C CB  . GLU A 86  ? 0.8059 0.6235 0.9569 -0.0457 -0.0069 -0.1022 93  GLU A CB  
607  C CG  . GLU A 86  ? 0.9308 0.7681 1.0760 -0.0485 -0.0224 -0.1052 93  GLU A CG  
608  C CD  . GLU A 86  ? 0.9786 0.8102 1.1079 -0.0588 -0.0261 -0.1138 93  GLU A CD  
609  O OE1 . GLU A 86  ? 1.0391 0.8513 1.1537 -0.0678 -0.0185 -0.1210 93  GLU A OE1 
610  O OE2 . GLU A 86  ? 0.7909 0.6359 0.9196 -0.0580 -0.0353 -0.1118 93  GLU A OE2 
611  N N   . TYR A 87  ? 0.8218 0.6601 1.0273 -0.0143 0.0092  -0.0699 94  TYR A N   
612  C CA  . TYR A 87  ? 0.8831 0.7516 1.1231 -0.0022 0.0090  -0.0525 94  TYR A CA  
613  C C   . TYR A 87  ? 0.7957 0.6788 1.0359 -0.0115 0.0021  -0.0629 94  TYR A C   
614  O O   . TYR A 87  ? 0.7886 0.6456 1.0085 -0.0189 0.0122  -0.0794 94  TYR A O   
615  C CB  . TYR A 87  ? 0.8324 0.6798 1.0980 0.0145  0.0389  -0.0409 94  TYR A CB  
616  C CG  . TYR A 87  ? 0.7741 0.6605 1.0897 0.0304  0.0425  -0.0169 94  TYR A CG  
617  C CD1 . TYR A 87  ? 0.7844 0.7243 1.1265 0.0353  0.0180  0.0083  94  TYR A CD1 
618  C CD2 . TYR A 87  ? 0.8446 0.7186 1.1811 0.0385  0.0703  -0.0180 94  TYR A CD2 
619  C CE1 . TYR A 87  ? 0.9395 0.9288 1.3359 0.0472  0.0164  0.0349  94  TYR A CE1 
620  C CE2 . TYR A 87  ? 0.9399 0.8592 1.3348 0.0542  0.0751  0.0084  94  TYR A CE2 
621  C CZ  . TYR A 87  ? 0.9712 0.9528 1.4002 0.0582  0.0459  0.0363  94  TYR A CZ  
622  O OH  . TYR A 87  ? 0.9695 1.0085 1.4638 0.0708  0.0459  0.0665  94  TYR A OH  
623  N N   . MET A 88  ? 0.8076 0.7314 1.0671 -0.0140 -0.0153 -0.0526 95  MET A N   
624  C CA  . MET A 88  ? 0.7273 0.6644 0.9903 -0.0258 -0.0205 -0.0610 95  MET A CA  
625  C C   . MET A 88  ? 0.7135 0.6959 1.0261 -0.0212 -0.0224 -0.0401 95  MET A C   
626  O O   . MET A 88  ? 0.7631 0.7853 1.0882 -0.0267 -0.0445 -0.0267 95  MET A O   
627  C CB  . MET A 88  ? 0.6856 0.6241 0.9182 -0.0420 -0.0403 -0.0737 95  MET A CB  
628  C CG  . MET A 88  ? 0.7676 0.6712 0.9646 -0.0436 -0.0369 -0.0888 95  MET A CG  
629  S SD  . MET A 88  ? 0.9005 0.7743 1.0831 -0.0460 -0.0219 -0.1010 95  MET A SD  
630  C CE  . MET A 88  ? 0.8764 0.7528 1.0526 -0.0578 -0.0281 -0.1075 95  MET A CE  
631  N N   . GLU A 89  ? 0.8302 0.5687 1.1360 0.1008  0.0364  -0.1058 96  GLU A N   
632  C CA  . GLU A 89  ? 0.9335 0.6818 1.2682 0.1295  0.0354  -0.1110 96  GLU A CA  
633  C C   . GLU A 89  ? 0.9214 0.7158 1.2792 0.1388  0.0245  -0.0996 96  GLU A C   
634  O O   . GLU A 89  ? 0.9091 0.7007 1.2833 0.1620  0.0131  -0.0917 96  GLU A O   
635  C CB  . GLU A 89  ? 0.8899 0.6521 1.2365 0.1344  0.0522  -0.1375 96  GLU A CB  
636  C CG  . GLU A 89  ? 0.9472 0.7186 1.3271 0.1657  0.0542  -0.1474 96  GLU A CG  
637  C CD  . GLU A 89  ? 1.0508 0.8206 1.4369 0.1716  0.0734  -0.1762 96  GLU A CD  
638  O OE1 . GLU A 89  ? 1.0150 0.7962 1.4320 0.1987  0.0774  -0.1870 96  GLU A OE1 
639  O OE2 . GLU A 89  ? 1.0752 0.8346 1.4360 0.1505  0.0843  -0.1893 96  GLU A OE2 
640  N N   . LYS A 90  ? 0.8854 0.7199 1.2432 0.1203  0.0270  -0.0984 97  LYS A N   
641  C CA  . LYS A 90  ? 0.8632 0.7430 1.2440 0.1239  0.0189  -0.0913 97  LYS A CA  
642  C C   . LYS A 90  ? 0.7800 0.6523 1.1482 0.1197  0.0016  -0.0700 97  LYS A C   
643  O O   . LYS A 90  ? 0.9187 0.8277 1.3047 0.1209  -0.0064 -0.0659 97  LYS A O   
644  C CB  . LYS A 90  ? 0.7980 0.7207 1.1853 0.1067  0.0322  -0.1006 97  LYS A CB  
645  C CG  . LYS A 90  ? 0.8855 0.8274 1.2915 0.1152  0.0493  -0.1223 97  LYS A CG  
646  C CD  . LYS A 90  ? 0.9899 0.9764 1.4033 0.0992  0.0634  -0.1288 97  LYS A CD  
647  C CE  . LYS A 90  ? 1.0137 1.0323 1.4571 0.1116  0.0801  -0.1499 97  LYS A CE  
648  N NZ  . LYS A 90  ? 0.9895 1.0447 1.4775 0.1289  0.0743  -0.1527 97  LYS A NZ  
649  N N   . GLY A 91  ? 0.7485 0.5753 1.0869 0.1140  -0.0031 -0.0581 98  GLY A N   
650  C CA  . GLY A 91  ? 0.7604 0.5770 1.0822 0.1105  -0.0174 -0.0383 98  GLY A CA  
651  C C   . GLY A 91  ? 0.6822 0.5211 0.9935 0.0867  -0.0155 -0.0343 98  GLY A C   
652  O O   . GLY A 91  ? 0.6277 0.4751 0.9350 0.0718  -0.0036 -0.0428 98  GLY A O   
653  N N   . ASN A 92  ? 0.6537 0.5005 0.9586 0.0845  -0.0275 -0.0217 99  ASN A N   
654  C CA  . ASN A 92  ? 0.6509 0.5127 0.9445 0.0635  -0.0254 -0.0178 99  ASN A CA  
655  C C   . ASN A 92  ? 0.6438 0.5492 0.9602 0.0569  -0.0199 -0.0275 99  ASN A C   
656  O O   . ASN A 92  ? 0.6168 0.5491 0.9614 0.0680  -0.0192 -0.0372 99  ASN A O   
657  C CB  . ASN A 92  ? 0.6090 0.4588 0.8822 0.0610  -0.0375 -0.0029 99  ASN A CB  
658  C CG  . ASN A 92  ? 0.6808 0.5523 0.9675 0.0759  -0.0537 0.0001  99  ASN A CG  
659  O OD1 . ASN A 92  ? 0.6824 0.5937 0.9980 0.0786  -0.0553 -0.0098 99  ASN A OD1 
660  N ND2 . ASN A 92  ? 0.7982 0.6447 1.0630 0.0850  -0.0660 0.0139  99  ASN A ND2 
661  N N   . LEU A 93  ? 0.6482 0.5593 0.9531 0.0389  -0.0147 -0.0249 100 LEU A N   
662  C CA  . LEU A 93  ? 0.6565 0.5987 0.9758 0.0286  -0.0066 -0.0316 100 LEU A CA  
663  C C   . LEU A 93  ? 0.6577 0.6333 1.0026 0.0316  -0.0144 -0.0352 100 LEU A C   
664  O O   . LEU A 93  ? 0.5833 0.5889 0.9521 0.0289  -0.0059 -0.0452 100 LEU A O   
665  C CB  . LEU A 93  ? 0.6548 0.5882 0.9534 0.0116  -0.0012 -0.0255 100 LEU A CB  
666  C CG  . LEU A 93  ? 0.5671 0.5209 0.8725 -0.0009 0.0098  -0.0291 100 LEU A CG  
667  C CD1 . LEU A 93  ? 0.5815 0.5470 0.8940 -0.0004 0.0233  -0.0378 100 LEU A CD1 
668  C CD2 . LEU A 93  ? 0.6056 0.5421 0.8877 -0.0121 0.0128  -0.0209 100 LEU A CD2 
669  N N   . MET A 94  ? 0.7289 0.7008 1.0678 0.0357  -0.0301 -0.0281 101 MET A N   
670  C CA  . MET A 94  ? 0.7433 0.7503 1.1056 0.0377  -0.0413 -0.0330 101 MET A CA  
671  C C   . MET A 94  ? 0.7641 0.7984 1.1601 0.0575  -0.0470 -0.0412 101 MET A C   
672  O O   . MET A 94  ? 0.7409 0.8179 1.1700 0.0549  -0.0467 -0.0524 101 MET A O   
673  C CB  . MET A 94  ? 0.7363 0.7319 1.0773 0.0381  -0.0581 -0.0237 101 MET A CB  
674  C CG  . MET A 94  ? 0.6989 0.7322 1.0590 0.0343  -0.0707 -0.0310 101 MET A CG  
675  S SD  . MET A 94  ? 0.8170 0.8791 1.1977 0.0083  -0.0561 -0.0442 101 MET A SD  
676  C CE  . MET A 94  ? 0.6851 0.7036 1.0265 -0.0085 -0.0420 -0.0351 101 MET A CE  
677  N N   . HIS A 95  ? 0.7272 0.7362 1.1164 0.0767  -0.0510 -0.0366 102 HIS A N   
678  C CA  . HIS A 95  ? 0.7164 0.7450 1.1376 0.1000  -0.0545 -0.0449 102 HIS A CA  
679  C C   . HIS A 95  ? 0.7556 0.8139 1.2061 0.0955  -0.0349 -0.0616 102 HIS A C   
680  O O   . HIS A 95  ? 0.7184 0.8192 1.2090 0.1069  -0.0365 -0.0732 102 HIS A O   
681  C CB  . HIS A 95  ? 0.7633 0.7462 1.1655 0.1197  -0.0590 -0.0362 102 HIS A CB  
682  C CG  . HIS A 95  ? 0.7486 0.7451 1.1817 0.1487  -0.0652 -0.0428 102 HIS A CG  
683  N ND1 . HIS A 95  ? 0.8294 0.8280 1.2819 0.1569  -0.0494 -0.0569 102 HIS A ND1 
684  C CD2 . HIS A 95  ? 0.8315 0.8403 1.2789 0.1735  -0.0859 -0.0376 102 HIS A CD2 
685  C CE1 . HIS A 95  ? 0.7467 0.7582 1.2276 0.1863  -0.0587 -0.0610 102 HIS A CE1 
686  N NE2 . HIS A 95  ? 0.7785 0.7968 1.2573 0.1978  -0.0821 -0.0484 102 HIS A NE2 
687  N N   . VAL A 96  ? 0.7423 0.7819 1.1728 0.0789  -0.0168 -0.0629 103 VAL A N   
688  C CA  . VAL A 96  ? 0.7598 0.8236 1.2078 0.0719  0.0039  -0.0771 103 VAL A CA  
689  C C   . VAL A 96  ? 0.7546 0.8593 1.2230 0.0534  0.0107  -0.0824 103 VAL A C   
690  O O   . VAL A 96  ? 0.7148 0.8578 1.2158 0.0537  0.0225  -0.0960 103 VAL A O   
691  C CB  . VAL A 96  ? 0.8628 0.8936 1.2780 0.0613  0.0186  -0.0761 103 VAL A CB  
692  C CG1 . VAL A 96  ? 0.8591 0.9132 1.2832 0.0523  0.0404  -0.0889 103 VAL A CG1 
693  C CG2 . VAL A 96  ? 0.9574 0.9509 1.3596 0.0777  0.0146  -0.0758 103 VAL A CG2 
694  N N   . LEU A 97  ? 0.7689 0.8641 1.2186 0.0367  0.0051  -0.0729 104 LEU A N   
695  C CA  . LEU A 97  ? 0.7807 0.9070 1.2475 0.0169  0.0108  -0.0779 104 LEU A CA  
696  C C   . LEU A 97  ? 0.7378 0.9135 1.2487 0.0232  -0.0009 -0.0887 104 LEU A C   
697  O O   . LEU A 97  ? 0.7522 0.9629 1.2888 0.0066  0.0095  -0.0987 104 LEU A O   
698  C CB  . LEU A 97  ? 0.6723 0.7716 1.1078 0.0000  0.0068  -0.0667 104 LEU A CB  
699  C CG  . LEU A 97  ? 0.6629 0.7259 1.0626 -0.0099 0.0206  -0.0581 104 LEU A CG  
700  C CD1 . LEU A 97  ? 0.7375 0.7704 1.1075 -0.0176 0.0127  -0.0467 104 LEU A CD1 
701  C CD2 . LEU A 97  ? 0.6512 0.7257 1.0541 -0.0262 0.0424  -0.0623 104 LEU A CD2 
702  N N   . LYS A 98  ? 0.8039 0.9821 1.3226 0.0464  -0.0223 -0.0862 105 LYS A N   
703  C CA  . LYS A 98  ? 0.7492 0.9785 1.3112 0.0583  -0.0385 -0.0961 105 LYS A CA  
704  C C   . LYS A 98  ? 0.6876 0.9560 1.2952 0.0786  -0.0329 -0.1103 105 LYS A C   
705  O O   . LYS A 98  ? 0.7082 1.0289 1.3593 0.0881  -0.0457 -0.1207 105 LYS A O   
706  C CB  . LYS A 98  ? 0.7602 0.9738 1.3039 0.0746  -0.0672 -0.0843 105 LYS A CB  
707  C CG  . LYS A 98  ? 0.8630 1.0599 1.3760 0.0529  -0.0736 -0.0774 105 LYS A CG  
708  C CD  . LYS A 98  ? 0.9438 1.1296 1.4360 0.0679  -0.1009 -0.0668 105 LYS A CD  
709  C CE  . LYS A 98  ? 0.9816 1.1636 1.4511 0.0457  -0.1071 -0.0661 105 LYS A CE  
710  N NZ  . LYS A 98  ? 1.0824 1.2548 1.5267 0.0606  -0.1333 -0.0559 105 LYS A NZ  
711  N N   . ALA A 99  ? 0.6761 0.9248 1.2769 0.0845  -0.0137 -0.1132 106 ALA A N   
712  C CA  . ALA A 99  ? 0.7218 1.0030 1.3639 0.1065  -0.0060 -0.1285 106 ALA A CA  
713  C C   . ALA A 99  ? 0.8607 1.2076 1.5526 0.0930  0.0103  -0.1475 106 ALA A C   
714  O O   . ALA A 99  ? 0.8691 1.2249 1.5554 0.0624  0.0230  -0.1483 106 ALA A O   
715  C CB  . ALA A 99  ? 0.6906 0.9308 1.3075 0.1134  0.0116  -0.1292 106 ALA A CB  
716  N N   . GLU A 100 ? 1.0128 1.4039 1.7539 0.1163  0.0113  -0.1630 107 GLU A N   
717  C CA  . GLU A 100 ? 1.0936 1.5570 1.8919 0.1057  0.0277  -0.1840 107 GLU A CA  
718  C C   . GLU A 100 ? 1.2221 1.6818 2.0078 0.0793  0.0651  -0.1911 107 GLU A C   
719  O O   . GLU A 100 ? 1.2313 1.7291 2.0387 0.0517  0.0813  -0.1996 107 GLU A O   
720  C CB  . GLU A 100 ? 1.1522 1.6651 2.0086 0.1414  0.0204  -0.1998 107 GLU A CB  
721  C CG  . GLU A 100 ? 1.0922 1.6332 1.9751 0.1648  -0.0168 -0.1960 107 GLU A CG  
722  C CD  . GLU A 100 ? 1.2178 1.7997 2.1545 0.2071  -0.0255 -0.2090 107 GLU A CD  
723  O OE1 . GLU A 100 ? 1.2146 1.8506 2.2016 0.2079  -0.0033 -0.2309 107 GLU A OE1 
724  O OE2 . GLU A 100 ? 1.2386 1.7978 2.1666 0.2404  -0.0539 -0.1968 107 GLU A OE2 
725  N N   . MET A 101 ? 1.3570 1.7701 2.1057 0.0871  0.0786  -0.1878 108 MET A N   
726  C CA  . MET A 101 ? 1.3398 1.7365 2.0587 0.0631  0.1102  -0.1897 108 MET A CA  
727  C C   . MET A 101 ? 1.2812 1.6323 1.9479 0.0368  0.1069  -0.1698 108 MET A C   
728  O O   . MET A 101 ? 1.3175 1.6203 1.9472 0.0449  0.0885  -0.1548 108 MET A O   
729  C CB  . MET A 101 ? 1.3893 1.7514 2.0835 0.0812  0.1216  -0.1944 108 MET A CB  
730  C CG  . MET A 101 ? 1.4878 1.8873 2.2311 0.1110  0.1268  -0.2153 108 MET A CG  
731  S SD  . MET A 101 ? 1.5711 2.0566 2.3812 0.1037  0.1525  -0.2401 108 MET A SD  
732  C CE  . MET A 101 ? 1.5810 2.0501 2.3453 0.0668  0.1916  -0.2404 108 MET A CE  
733  N N   . SER A 102 ? 1.2447 1.6099 1.9090 0.0059  0.1261  -0.1699 109 SER A N   
734  C CA  . SER A 102 ? 1.1940 1.5172 1.8126 -0.0183 0.1247  -0.1517 109 SER A CA  
735  C C   . SER A 102 ? 0.9574 1.2281 1.5183 -0.0206 0.1359  -0.1405 109 SER A C   
736  O O   . SER A 102 ? 0.8199 1.0946 1.3753 -0.0165 0.1551  -0.1493 109 SER A O   
737  C CB  . SER A 102 ? 1.2539 1.6042 1.8889 -0.0507 0.1420  -0.1550 109 SER A CB  
738  O OG  . SER A 102 ? 1.2713 1.6061 1.8771 -0.0702 0.1724  -0.1517 109 SER A OG  
739  N N   . THR A 103 ? 0.9175 1.1427 1.4366 -0.0276 0.1238  -0.1227 110 THR A N   
740  C CA  . THR A 103 ? 0.7633 0.9435 1.2290 -0.0322 0.1315  -0.1111 110 THR A CA  
741  C C   . THR A 103 ? 0.7663 0.9421 1.2118 -0.0589 0.1534  -0.1042 110 THR A C   
742  O O   . THR A 103 ? 0.8249 0.9984 1.2745 -0.0746 0.1503  -0.0974 110 THR A O   
743  C CB  . THR A 103 ? 0.7087 0.8467 1.1440 -0.0263 0.1088  -0.0959 110 THR A CB  
744  O OG1 . THR A 103 ? 0.5838 0.7234 1.0374 -0.0037 0.0891  -0.1001 110 THR A OG1 
745  C CG2 . THR A 103 ? 0.7678 0.8677 1.1550 -0.0275 0.1135  -0.0871 110 THR A CG2 
746  N N   . PRO A 104 ? 0.7383 0.9094 1.1586 -0.0643 0.1757  -0.1055 111 PRO A N   
747  C CA  . PRO A 104 ? 0.8011 0.9582 1.1926 -0.0886 0.1961  -0.0941 111 PRO A CA  
748  C C   . PRO A 104 ? 0.7877 0.8957 1.1325 -0.0933 0.1853  -0.0725 111 PRO A C   
749  O O   . PRO A 104 ? 0.7642 0.8500 1.0944 -0.0787 0.1644  -0.0672 111 PRO A O   
750  C CB  . PRO A 104 ? 0.8787 1.0430 1.2497 -0.0894 0.2204  -0.1010 111 PRO A CB  
751  C CG  . PRO A 104 ? 0.8340 0.9942 1.2028 -0.0650 0.2069  -0.1108 111 PRO A CG  
752  C CD  . PRO A 104 ? 0.7838 0.9632 1.2005 -0.0501 0.1858  -0.1187 111 PRO A CD  
753  N N   . LEU A 105 ? 0.8863 0.9783 1.2102 -0.1140 0.2015  -0.0605 112 LEU A N   
754  C CA  . LEU A 105 ? 0.7982 0.8438 1.0803 -0.1182 0.1945  -0.0395 112 LEU A CA  
755  C C   . LEU A 105 ? 0.8118 0.8300 1.0465 -0.1046 0.1874  -0.0293 112 LEU A C   
756  O O   . LEU A 105 ? 0.9063 0.8961 1.1208 -0.0974 0.1702  -0.0172 112 LEU A O   
757  C CB  . LEU A 105 ? 0.8141 0.8447 1.0816 -0.1426 0.2177  -0.0289 112 LEU A CB  
758  C CG  . LEU A 105 ? 0.7910 0.7700 1.0137 -0.1474 0.2165  -0.0058 112 LEU A CG  
759  C CD1 . LEU A 105 ? 0.7196 0.6827 0.9542 -0.1412 0.1932  -0.0035 112 LEU A CD1 
760  C CD2 . LEU A 105 ? 0.8823 0.8478 1.0958 -0.1734 0.2443  0.0020  112 LEU A CD2 
761  N N   . SER A 106 ? 0.8363 0.8656 1.0540 -0.1019 0.2011  -0.0356 113 SER A N   
762  C CA  . SER A 106 ? 0.8522 0.8619 1.0252 -0.0905 0.1938  -0.0298 113 SER A CA  
763  C C   . SER A 106 ? 0.8024 0.8114 0.9874 -0.0724 0.1689  -0.0378 113 SER A C   
764  O O   . SER A 106 ? 0.7384 0.7253 0.8953 -0.0655 0.1540  -0.0282 113 SER A O   
765  C CB  . SER A 106 ? 0.9158 0.9408 1.0688 -0.0927 0.2147  -0.0392 113 SER A CB  
766  O OG  . SER A 106 ? 1.1764 1.1961 1.3091 -0.1109 0.2395  -0.0284 113 SER A OG  
767  N N   . VAL A 107 ? 0.7018 0.7352 0.9295 -0.0649 0.1650  -0.0548 114 VAL A N   
768  C CA  . VAL A 107 ? 0.7799 0.8086 1.0209 -0.0488 0.1436  -0.0617 114 VAL A CA  
769  C C   . VAL A 107 ? 0.7092 0.7186 0.9527 -0.0483 0.1244  -0.0486 114 VAL A C   
770  O O   . VAL A 107 ? 0.5589 0.5501 0.7874 -0.0406 0.1093  -0.0447 114 VAL A O   
771  C CB  . VAL A 107 ? 0.6799 0.7364 0.9645 -0.0381 0.1448  -0.0811 114 VAL A CB  
772  C CG1 . VAL A 107 ? 0.6018 0.6464 0.8998 -0.0221 0.1231  -0.0844 114 VAL A CG1 
773  C CG2 . VAL A 107 ? 0.6795 0.7510 0.9571 -0.0356 0.1636  -0.0966 114 VAL A CG2 
774  N N   . LYS A 108 ? 0.7329 0.7480 0.9960 -0.0579 0.1266  -0.0440 115 LYS A N   
775  C CA  . LYS A 108 ? 0.6388 0.6348 0.9007 -0.0598 0.1121  -0.0327 115 LYS A CA  
776  C C   . LYS A 108 ? 0.6456 0.6111 0.8681 -0.0605 0.1090  -0.0169 115 LYS A C   
777  O O   . LYS A 108 ? 0.7586 0.7094 0.9752 -0.0530 0.0931  -0.0122 115 LYS A O   
778  C CB  . LYS A 108 ? 0.6795 0.6866 0.9656 -0.0738 0.1182  -0.0332 115 LYS A CB  
779  C CG  . LYS A 108 ? 0.6889 0.7293 1.0190 -0.0683 0.1113  -0.0483 115 LYS A CG  
780  C CD  . LYS A 108 ? 0.6698 0.7266 1.0274 -0.0825 0.1122  -0.0520 115 LYS A CD  
781  C CE  . LYS A 108 ? 0.6476 0.7437 1.0492 -0.0726 0.1018  -0.0671 115 LYS A CE  
782  N NZ  . LYS A 108 ? 0.7079 0.8255 1.1386 -0.0846 0.0959  -0.0733 115 LYS A NZ  
783  N N   . GLY A 109 ? 0.6310 0.5883 0.8265 -0.0684 0.1243  -0.0087 116 GLY A N   
784  C CA  . GLY A 109 ? 0.7066 0.6376 0.8621 -0.0652 0.1204  0.0073  116 GLY A CA  
785  C C   . GLY A 109 ? 0.7679 0.6991 0.9092 -0.0521 0.1054  0.0040  116 GLY A C   
786  O O   . GLY A 109 ? 0.8547 0.7716 0.9839 -0.0457 0.0922  0.0129  116 GLY A O   
787  N N   . ARG A 110 ? 0.7423 0.6911 0.8881 -0.0487 0.1085  -0.0109 117 ARG A N   
788  C CA  . ARG A 110 ? 0.7567 0.7063 0.8919 -0.0395 0.0961  -0.0186 117 ARG A CA  
789  C C   . ARG A 110 ? 0.7436 0.6892 0.9035 -0.0334 0.0796  -0.0226 117 ARG A C   
790  O O   . ARG A 110 ? 0.5600 0.4984 0.7097 -0.0294 0.0671  -0.0206 117 ARG A O   
791  C CB  . ARG A 110 ? 0.8042 0.7697 0.9381 -0.0384 0.1066  -0.0362 117 ARG A CB  
792  C CG  . ARG A 110 ? 0.8263 0.7905 0.9380 -0.0332 0.0977  -0.0456 117 ARG A CG  
793  C CD  . ARG A 110 ? 0.8409 0.8177 0.9557 -0.0314 0.1093  -0.0670 117 ARG A CD  
794  N NE  . ARG A 110 ? 0.8336 0.8151 0.9895 -0.0252 0.1095  -0.0792 117 ARG A NE  
795  C CZ  . ARG A 110 ? 0.9092 0.9023 1.0804 -0.0203 0.1212  -0.0979 117 ARG A CZ  
796  N NH1 . ARG A 110 ? 0.9881 0.9898 1.1353 -0.0227 0.1358  -0.1097 117 ARG A NH1 
797  N NH2 . ARG A 110 ? 0.9196 0.9152 1.1291 -0.0110 0.1178  -0.1056 117 ARG A NH2 
798  N N   . ILE A 111 ? 0.6623 0.6144 0.8539 -0.0330 0.0799  -0.0280 118 ILE A N   
799  C CA  . ILE A 111 ? 0.5750 0.5197 0.7849 -0.0281 0.0653  -0.0277 118 ILE A CA  
800  C C   . ILE A 111 ? 0.5942 0.5237 0.7923 -0.0300 0.0569  -0.0140 118 ILE A C   
801  O O   . ILE A 111 ? 0.7149 0.6366 0.9123 -0.0263 0.0461  -0.0135 118 ILE A O   
802  C CB  . ILE A 111 ? 0.4864 0.4434 0.7286 -0.0267 0.0656  -0.0334 118 ILE A CB  
803  C CG1 . ILE A 111 ? 0.5350 0.5052 0.7935 -0.0184 0.0697  -0.0485 118 ILE A CG1 
804  C CG2 . ILE A 111 ? 0.4463 0.3936 0.6992 -0.0234 0.0511  -0.0287 118 ILE A CG2 
805  C CD1 . ILE A 111 ? 0.5739 0.5672 0.8662 -0.0160 0.0730  -0.0556 118 ILE A CD1 
806  N N   . ILE A 112 ? 0.7246 0.6485 0.9142 -0.0360 0.0637  -0.0036 119 ILE A N   
807  C CA  . ILE A 112 ? 0.6229 0.5301 0.8024 -0.0358 0.0581  0.0086  119 ILE A CA  
808  C C   . ILE A 112 ? 0.6438 0.5473 0.8014 -0.0292 0.0512  0.0138  119 ILE A C   
809  O O   . ILE A 112 ? 0.6490 0.5480 0.8092 -0.0250 0.0415  0.0164  119 ILE A O   
810  C CB  . ILE A 112 ? 0.6761 0.5718 0.8505 -0.0441 0.0691  0.0177  119 ILE A CB  
811  C CG1 . ILE A 112 ? 0.8041 0.7085 1.0060 -0.0519 0.0716  0.0100  119 ILE A CG1 
812  C CG2 . ILE A 112 ? 0.7303 0.6043 0.8910 -0.0406 0.0649  0.0300  119 ILE A CG2 
813  C CD1 . ILE A 112 ? 0.8995 0.8001 1.1030 -0.0654 0.0868  0.0128  119 ILE A CD1 
814  N N   . LEU A 113 ? 0.7224 0.6311 0.8591 -0.0287 0.0561  0.0142  120 LEU A N   
815  C CA  . LEU A 113 ? 0.7357 0.6477 0.8511 -0.0222 0.0470  0.0170  120 LEU A CA  
816  C C   . LEU A 113 ? 0.7743 0.6971 0.9019 -0.0203 0.0357  0.0039  120 LEU A C   
817  O O   . LEU A 113 ? 0.7461 0.6732 0.8714 -0.0162 0.0249  0.0060  120 LEU A O   
818  C CB  . LEU A 113 ? 0.7732 0.6893 0.8585 -0.0229 0.0547  0.0190  120 LEU A CB  
819  C CG  . LEU A 113 ? 0.8084 0.7305 0.8659 -0.0153 0.0432  0.0241  120 LEU A CG  
820  C CD1 . LEU A 113 ? 0.8837 0.7948 0.9366 -0.0064 0.0346  0.0408  120 LEU A CD1 
821  C CD2 . LEU A 113 ? 0.8147 0.7386 0.8358 -0.0167 0.0523  0.0272  120 LEU A CD2 
822  N N   . GLU A 114 ? 0.6899 0.6165 0.8323 -0.0231 0.0389  -0.0096 121 GLU A N   
823  C CA  . GLU A 114 ? 0.6850 0.6133 0.8387 -0.0232 0.0309  -0.0214 121 GLU A CA  
824  C C   . GLU A 114 ? 0.7612 0.6817 0.9313 -0.0231 0.0238  -0.0164 121 GLU A C   
825  O O   . GLU A 114 ? 0.7461 0.6689 0.9189 -0.0246 0.0165  -0.0205 121 GLU A O   
826  C CB  . GLU A 114 ? 0.7867 0.7146 0.9510 -0.0234 0.0373  -0.0357 121 GLU A CB  
827  C CG  . GLU A 114 ? 0.7549 0.6922 0.9004 -0.0242 0.0446  -0.0458 121 GLU A CG  
828  C CD  . GLU A 114 ? 0.8352 0.7728 0.9934 -0.0219 0.0533  -0.0618 121 GLU A CD  
829  O OE1 . GLU A 114 ? 1.0603 0.9936 1.2430 -0.0181 0.0545  -0.0618 121 GLU A OE1 
830  O OE2 . GLU A 114 ? 0.8701 0.8132 1.0129 -0.0228 0.0586  -0.0750 121 GLU A OE2 
831  N N   . ILE A 115 ? 0.6323 0.5452 0.8125 -0.0229 0.0270  -0.0091 122 ILE A N   
832  C CA  . ILE A 115 ? 0.6384 0.5433 0.8281 -0.0230 0.0220  -0.0035 122 ILE A CA  
833  C C   . ILE A 115 ? 0.6789 0.5868 0.8609 -0.0205 0.0177  0.0037  122 ILE A C   
834  O O   . ILE A 115 ? 0.8167 0.7265 1.0057 -0.0212 0.0129  0.0022  122 ILE A O   
835  C CB  . ILE A 115 ? 0.6133 0.5120 0.8121 -0.0243 0.0255  0.0009  122 ILE A CB  
836  C CG1 . ILE A 115 ? 0.6853 0.5865 0.8979 -0.0235 0.0259  -0.0069 122 ILE A CG1 
837  C CG2 . ILE A 115 ? 0.5756 0.4657 0.7780 -0.0247 0.0212  0.0054  122 ILE A CG2 
838  C CD1 . ILE A 115 ? 0.5543 0.4610 0.7782 -0.0258 0.0298  -0.0063 122 ILE A CD1 
839  N N   . ILE A 116 ? 0.7401 0.6488 0.9078 -0.0171 0.0202  0.0116  123 ILE A N   
840  C CA  . ILE A 116 ? 0.7227 0.6349 0.8829 -0.0100 0.0148  0.0197  123 ILE A CA  
841  C C   . ILE A 116 ? 0.6603 0.5928 0.8210 -0.0087 0.0051  0.0121  123 ILE A C   
842  O O   . ILE A 116 ? 0.7573 0.6996 0.9283 -0.0054 -0.0009 0.0125  123 ILE A O   
843  C CB  . ILE A 116 ? 0.7621 0.6649 0.9015 -0.0051 0.0196  0.0323  123 ILE A CB  
844  C CG1 . ILE A 116 ? 0.8017 0.6836 0.9446 -0.0094 0.0298  0.0384  123 ILE A CG1 
845  C CG2 . ILE A 116 ? 0.8508 0.7575 0.9816 0.0069  0.0117  0.0417  123 ILE A CG2 
846  C CD1 . ILE A 116 ? 0.8621 0.7314 0.9859 -0.0121 0.0405  0.0473  123 ILE A CD1 
847  N N   . GLU A 117 ? 0.6822 0.6230 0.8328 -0.0121 0.0044  0.0036  124 GLU A N   
848  C CA  . GLU A 117 ? 0.7393 0.7002 0.8901 -0.0145 -0.0048 -0.0082 124 GLU A CA  
849  C C   . GLU A 117 ? 0.6889 0.6521 0.8628 -0.0220 -0.0069 -0.0175 124 GLU A C   
850  O O   . GLU A 117 ? 0.9168 0.8987 1.1006 -0.0227 -0.0144 -0.0212 124 GLU A O   
851  C CB  . GLU A 117 ? 0.8264 0.7896 0.9630 -0.0194 -0.0018 -0.0202 124 GLU A CB  
852  C CG  . GLU A 117 ? 0.9145 0.8823 1.0213 -0.0141 -0.0007 -0.0136 124 GLU A CG  
853  C CD  . GLU A 117 ? 0.9641 0.9320 1.0567 -0.0194 0.0071  -0.0268 124 GLU A CD  
854  O OE1 . GLU A 117 ? 0.9954 0.9614 1.1015 -0.0257 0.0088  -0.0434 124 GLU A OE1 
855  O OE2 . GLU A 117 ? 0.9891 0.9568 1.0550 -0.0170 0.0130  -0.0204 124 GLU A OE2 
856  N N   . GLY A 118 ? 0.7024 0.6470 0.8847 -0.0272 0.0001  -0.0206 125 GLY A N   
857  C CA  . GLY A 118 ? 0.6889 0.6267 0.8867 -0.0349 0.0007  -0.0264 125 GLY A CA  
858  C C   . GLY A 118 ? 0.6891 0.6297 0.8978 -0.0341 0.0005  -0.0189 125 GLY A C   
859  O O   . GLY A 118 ? 0.6203 0.5695 0.8406 -0.0414 -0.0005 -0.0248 125 GLY A O   
860  N N   . MET A 119 ? 0.6557 0.5887 0.8612 -0.0268 0.0032  -0.0076 126 MET A N   
861  C CA  . MET A 119 ? 0.6454 0.5801 0.8595 -0.0245 0.0047  -0.0020 126 MET A CA  
862  C C   . MET A 119 ? 0.6384 0.5988 0.8596 -0.0182 -0.0013 -0.0022 126 MET A C   
863  O O   . MET A 119 ? 0.6583 0.6305 0.8945 -0.0198 0.0000  -0.0047 126 MET A O   
864  C CB  . MET A 119 ? 0.7213 0.6388 0.9291 -0.0191 0.0093  0.0073  126 MET A CB  
865  C CG  . MET A 119 ? 0.6580 0.5577 0.8641 -0.0243 0.0127  0.0066  126 MET A CG  
866  S SD  . MET A 119 ? 0.7102 0.6010 0.9207 -0.0323 0.0141  0.0032  126 MET A SD  
867  C CE  . MET A 119 ? 0.7516 0.6455 0.9645 -0.0304 0.0183  0.0069  126 MET A CE  
868  N N   . ALA A 120 ? 0.5817 0.5527 0.7921 -0.0108 -0.0077 0.0002  127 ALA A N   
869  C CA  . ALA A 120 ? 0.6451 0.6455 0.8613 -0.0026 -0.0176 -0.0005 127 ALA A CA  
870  C C   . ALA A 120 ? 0.6628 0.6905 0.8957 -0.0139 -0.0231 -0.0162 127 ALA A C   
871  O O   . ALA A 120 ? 0.5565 0.6133 0.8089 -0.0110 -0.0283 -0.0200 127 ALA A O   
872  C CB  . ALA A 120 ? 0.6248 0.6270 0.8180 0.0078  -0.0239 0.0071  127 ALA A CB  
873  N N   . TYR A 121 ? 0.6989 0.7174 0.9263 -0.0268 -0.0211 -0.0264 128 TYR A N   
874  C CA  . TYR A 121 ? 0.6741 0.7089 0.9165 -0.0420 -0.0231 -0.0428 128 TYR A CA  
875  C C   . TYR A 121 ? 0.7120 0.7470 0.9763 -0.0509 -0.0151 -0.0443 128 TYR A C   
876  O O   . TYR A 121 ? 0.7541 0.8206 1.0399 -0.0565 -0.0182 -0.0529 128 TYR A O   
877  C CB  . TYR A 121 ? 0.6985 0.7126 0.9297 -0.0533 -0.0195 -0.0536 128 TYR A CB  
878  C CG  . TYR A 121 ? 0.6519 0.6745 0.8989 -0.0717 -0.0189 -0.0709 128 TYR A CG  
879  C CD1 . TYR A 121 ? 0.6629 0.7216 0.9174 -0.0777 -0.0297 -0.0854 128 TYR A CD1 
880  C CD2 . TYR A 121 ? 0.6510 0.6464 0.9055 -0.0839 -0.0078 -0.0721 128 TYR A CD2 
881  C CE1 . TYR A 121 ? 0.7402 0.8077 1.0122 -0.0983 -0.0280 -0.1034 128 TYR A CE1 
882  C CE2 . TYR A 121 ? 0.6378 0.6361 0.9062 -0.1036 -0.0045 -0.0871 128 TYR A CE2 
883  C CZ  . TYR A 121 ? 0.6720 0.7067 0.9510 -0.1121 -0.0140 -0.1039 128 TYR A CZ  
884  O OH  . TYR A 121 ? 0.7448 0.7836 1.0399 -0.1350 -0.0099 -0.1212 128 TYR A OH  
885  N N   . LEU A 122 ? 0.6153 0.6177 0.8733 -0.0524 -0.0048 -0.0364 129 LEU A N   
886  C CA  . LEU A 122 ? 0.6237 0.6189 0.8930 -0.0610 0.0052  -0.0354 129 LEU A CA  
887  C C   . LEU A 122 ? 0.6024 0.6231 0.8886 -0.0537 0.0065  -0.0326 129 LEU A C   
888  O O   . LEU A 122 ? 0.8220 0.8594 1.1270 -0.0643 0.0129  -0.0393 129 LEU A O   
889  C CB  . LEU A 122 ? 0.6061 0.5628 0.8591 -0.0600 0.0125  -0.0258 129 LEU A CB  
890  C CG  . LEU A 122 ? 0.6565 0.5852 0.8983 -0.0667 0.0139  -0.0289 129 LEU A CG  
891  C CD1 . LEU A 122 ? 0.6483 0.5483 0.8772 -0.0611 0.0175  -0.0181 129 LEU A CD1 
892  C CD2 . LEU A 122 ? 0.7676 0.6891 1.0163 -0.0842 0.0194  -0.0381 129 LEU A CD2 
893  N N   . HIS A 123 ? 0.6866 0.7086 0.9666 -0.0360 0.0024  -0.0231 130 HIS A N   
894  C CA  . HIS A 123 ? 0.6103 0.6553 0.9067 -0.0238 0.0028  -0.0207 130 HIS A CA  
895  C C   . HIS A 123 ? 0.6319 0.7241 0.9518 -0.0210 -0.0074 -0.0300 130 HIS A C   
896  O O   . HIS A 123 ? 0.5903 0.7108 0.9357 -0.0184 -0.0041 -0.0347 130 HIS A O   
897  C CB  . HIS A 123 ? 0.5635 0.5899 0.8444 -0.0052 0.0013  -0.0078 130 HIS A CB  
898  C CG  . HIS A 123 ? 0.6522 0.6424 0.9184 -0.0081 0.0116  -0.0020 130 HIS A CG  
899  N ND1 . HIS A 123 ? 0.6696 0.6407 0.9261 0.0039  0.0145  0.0064  130 HIS A ND1 
900  C CD2 . HIS A 123 ? 0.6973 0.6674 0.9562 -0.0218 0.0187  -0.0037 130 HIS A CD2 
901  C CE1 . HIS A 123 ? 0.7135 0.6587 0.9588 -0.0037 0.0220  0.0074  130 HIS A CE1 
902  N NE2 . HIS A 123 ? 0.6619 0.6068 0.9075 -0.0177 0.0237  0.0025  130 HIS A NE2 
903  N N   . GLY A 124 ? 0.6966 0.8001 1.0086 -0.0216 -0.0197 -0.0340 131 GLY A N   
904  C CA  . GLY A 124 ? 0.6694 0.8210 1.0021 -0.0233 -0.0323 -0.0465 131 GLY A CA  
905  C C   . GLY A 124 ? 0.6797 0.8547 1.0404 -0.0462 -0.0261 -0.0636 131 GLY A C   
906  O O   . GLY A 124 ? 0.6289 0.8533 1.0193 -0.0465 -0.0335 -0.0744 131 GLY A O   
907  N N   . LYS A 125 ? 0.6582 0.7980 1.0099 -0.0653 -0.0126 -0.0656 132 LYS A N   
908  C CA  . LYS A 125 ? 0.7195 0.8674 1.0921 -0.0900 -0.0012 -0.0785 132 LYS A CA  
909  C C   . LYS A 125 ? 0.7179 0.8587 1.1002 -0.0926 0.0161  -0.0725 132 LYS A C   
910  O O   . LYS A 125 ? 0.7410 0.8716 1.1291 -0.1143 0.0303  -0.0780 132 LYS A O   
911  C CB  . LYS A 125 ? 0.7041 0.8112 1.0571 -0.1085 0.0043  -0.0830 132 LYS A CB  
912  C CG  . LYS A 125 ? 0.6833 0.7905 1.0221 -0.1081 -0.0089 -0.0914 132 LYS A CG  
913  C CD  . LYS A 125 ? 0.7318 0.8880 1.0923 -0.1184 -0.0208 -0.1114 132 LYS A CD  
914  C CE  . LYS A 125 ? 0.8208 0.9769 1.1989 -0.1493 -0.0115 -0.1302 132 LYS A CE  
915  N NZ  . LYS A 125 ? 0.7723 0.9878 1.1844 -0.1609 -0.0201 -0.1493 132 LYS A NZ  
916  N N   . GLY A 126 ? 0.7211 0.8637 1.1021 -0.0715 0.0165  -0.0617 133 GLY A N   
917  C CA  . GLY A 126 ? 0.6408 0.7767 1.0271 -0.0723 0.0334  -0.0579 133 GLY A CA  
918  C C   . GLY A 126 ? 0.6940 0.7778 1.0501 -0.0811 0.0465  -0.0483 133 GLY A C   
919  O O   . GLY A 126 ? 0.8086 0.8882 1.1656 -0.0859 0.0617  -0.0470 133 GLY A O   
920  N N   . VAL A 127 ? 0.5637 0.6111 0.8932 -0.0820 0.0405  -0.0421 134 VAL A N   
921  C CA  . VAL A 127 ? 0.6416 0.6427 0.9432 -0.0878 0.0488  -0.0327 134 VAL A CA  
922  C C   . VAL A 127 ? 0.6059 0.5881 0.8892 -0.0697 0.0457  -0.0219 134 VAL A C   
923  O O   . VAL A 127 ? 0.5301 0.5110 0.8081 -0.0574 0.0348  -0.0188 134 VAL A O   
924  C CB  . VAL A 127 ? 0.6641 0.6380 0.9514 -0.0971 0.0442  -0.0337 134 VAL A CB  
925  C CG1 . VAL A 127 ? 0.7206 0.6487 0.9795 -0.0965 0.0482  -0.0224 134 VAL A CG1 
926  C CG2 . VAL A 127 ? 0.6564 0.6408 0.9596 -0.1191 0.0504  -0.0458 134 VAL A CG2 
927  N N   . ILE A 128 ? 0.6629 0.6288 0.9343 -0.0705 0.0563  -0.0170 135 ILE A N   
928  C CA  . ILE A 128 ? 0.6688 0.6094 0.9185 -0.0594 0.0541  -0.0087 135 ILE A CA  
929  C C   . ILE A 128 ? 0.6660 0.5729 0.8922 -0.0673 0.0532  -0.0026 135 ILE A C   
930  O O   . ILE A 128 ? 0.6838 0.5790 0.9022 -0.0802 0.0617  -0.0015 135 ILE A O   
931  C CB  . ILE A 128 ? 0.7006 0.6420 0.9472 -0.0557 0.0653  -0.0093 135 ILE A CB  
932  C CG1 . ILE A 128 ? 0.6383 0.6165 0.9139 -0.0480 0.0696  -0.0170 135 ILE A CG1 
933  C CG2 . ILE A 128 ? 0.7326 0.6513 0.9604 -0.0449 0.0611  -0.0042 135 ILE A CG2 
934  C CD1 . ILE A 128 ? 0.6606 0.6550 0.9500 -0.0313 0.0565  -0.0164 135 ILE A CD1 
935  N N   . HIS A 129 ? 0.6432 0.5349 0.8586 -0.0593 0.0435  0.0018  136 HIS A N   
936  C CA  . HIS A 129 ? 0.6367 0.5000 0.8334 -0.0622 0.0403  0.0075  136 HIS A CA  
937  C C   . HIS A 129 ? 0.6639 0.5095 0.8394 -0.0643 0.0453  0.0133  136 HIS A C   
938  O O   . HIS A 129 ? 0.7538 0.5789 0.9137 -0.0715 0.0484  0.0186  136 HIS A O   
939  C CB  . HIS A 129 ? 0.6449 0.5038 0.8400 -0.0523 0.0301  0.0090  136 HIS A CB  
940  C CG  . HIS A 129 ? 0.6937 0.5326 0.8802 -0.0524 0.0253  0.0117  136 HIS A CG  
941  N ND1 . HIS A 129 ? 0.7653 0.5820 0.9342 -0.0531 0.0248  0.0186  136 HIS A ND1 
942  C CD2 . HIS A 129 ? 0.7336 0.5712 0.9261 -0.0499 0.0205  0.0081  136 HIS A CD2 
943  C CE1 . HIS A 129 ? 0.6668 0.4693 0.8341 -0.0490 0.0191  0.0199  136 HIS A CE1 
944  N NE2 . HIS A 129 ? 0.7805 0.5954 0.9630 -0.0475 0.0176  0.0124  136 HIS A NE2 
945  N N   . LYS A 130 ? 0.5833 0.4338 0.7555 -0.0577 0.0458  0.0124  137 LYS A N   
946  C CA  . LYS A 130 ? 0.6437 0.4810 0.7932 -0.0590 0.0496  0.0148  137 LYS A CA  
947  C C   . LYS A 130 ? 0.6849 0.5038 0.8148 -0.0558 0.0386  0.0204  137 LYS A C   
948  O O   . LYS A 130 ? 0.8342 0.6454 0.9437 -0.0563 0.0388  0.0209  137 LYS A O   
949  C CB  . LYS A 130 ? 0.7287 0.5626 0.8673 -0.0699 0.0632  0.0158  137 LYS A CB  
950  C CG  . LYS A 130 ? 0.7221 0.5823 0.8856 -0.0734 0.0747  0.0080  137 LYS A CG  
951  C CD  . LYS A 130 ? 0.7766 0.6340 0.9337 -0.0890 0.0894  0.0091  137 LYS A CD  
952  C CE  . LYS A 130 ? 0.8236 0.6760 0.9904 -0.0987 0.0875  0.0108  137 LYS A CE  
953  N NZ  . LYS A 130 ? 0.8104 0.6978 1.0133 -0.1032 0.0910  0.0000  137 LYS A NZ  
954  N N   . ASP A 131 ? 0.7272 0.5433 0.8649 -0.0515 0.0289  0.0226  138 ASP A N   
955  C CA  . ASP A 131 ? 0.7106 0.5160 0.8372 -0.0459 0.0171  0.0269  138 ASP A CA  
956  C C   . ASP A 131 ? 0.7706 0.5845 0.9171 -0.0392 0.0093  0.0241  138 ASP A C   
957  O O   . ASP A 131 ? 0.6166 0.4224 0.7628 -0.0339 0.0020  0.0273  138 ASP A O   
958  C CB  . ASP A 131 ? 0.7426 0.5252 0.8465 -0.0477 0.0161  0.0365  138 ASP A CB  
959  C CG  . ASP A 131 ? 0.9498 0.7248 1.0372 -0.0392 0.0020  0.0418  138 ASP A CG  
960  O OD1 . ASP A 131 ? 0.9656 0.7559 1.0583 -0.0358 -0.0056 0.0358  138 ASP A OD1 
961  O OD2 . ASP A 131 ? 1.0120 0.7654 1.0822 -0.0358 -0.0022 0.0519  138 ASP A OD2 
962  N N   . LEU A 132 ? 0.6603 0.4896 0.8225 -0.0382 0.0116  0.0185  139 LEU A N   
963  C CA  . LEU A 132 ? 0.7284 0.5668 0.9059 -0.0336 0.0074  0.0156  139 LEU A CA  
964  C C   . LEU A 132 ? 0.6816 0.5236 0.8595 -0.0306 -0.0002 0.0144  139 LEU A C   
965  O O   . LEU A 132 ? 0.7589 0.6017 0.9304 -0.0335 -0.0005 0.0124  139 LEU A O   
966  C CB  . LEU A 132 ? 0.7445 0.5947 0.9324 -0.0335 0.0126  0.0128  139 LEU A CB  
967  C CG  . LEU A 132 ? 0.7672 0.6263 0.9652 -0.0304 0.0115  0.0107  139 LEU A CG  
968  C CD1 . LEU A 132 ? 0.7477 0.6078 0.9502 -0.0291 0.0098  0.0082  139 LEU A CD1 
969  C CD2 . LEU A 132 ? 0.8098 0.6750 1.0096 -0.0290 0.0162  0.0116  139 LEU A CD2 
970  N N   . LYS A 133 ? 0.6534 0.4987 0.8402 -0.0250 -0.0064 0.0139  140 LYS A N   
971  C CA  . LYS A 133 ? 0.6332 0.4897 0.8273 -0.0210 -0.0154 0.0113  140 LYS A CA  
972  C C   . LYS A 133 ? 0.7342 0.5984 0.9456 -0.0127 -0.0182 0.0087  140 LYS A C   
973  O O   . LYS A 133 ? 0.6397 0.4919 0.8494 -0.0097 -0.0150 0.0101  140 LYS A O   
974  C CB  . LYS A 133 ? 0.7729 0.6210 0.9489 -0.0186 -0.0248 0.0160  140 LYS A CB  
975  C CG  . LYS A 133 ? 0.8235 0.6509 0.9861 -0.0119 -0.0279 0.0248  140 LYS A CG  
976  C CD  . LYS A 133 ? 0.8633 0.6770 0.9975 -0.0115 -0.0342 0.0326  140 LYS A CD  
977  C CE  . LYS A 133 ? 0.9266 0.7112 1.0427 -0.0080 -0.0326 0.0438  140 LYS A CE  
978  N NZ  . LYS A 133 ? 0.9794 0.7466 1.0605 -0.0084 -0.0366 0.0540  140 LYS A NZ  
979  N N   . PRO A 134 ? 0.6591 0.5442 0.8886 -0.0095 -0.0231 0.0029  141 PRO A N   
980  C CA  . PRO A 134 ? 0.6398 0.5362 0.8892 -0.0002 -0.0236 -0.0018 141 PRO A CA  
981  C C   . PRO A 134 ? 0.5990 0.4767 0.8428 0.0125  -0.0293 0.0028  141 PRO A C   
982  O O   . PRO A 134 ? 0.5928 0.4661 0.8442 0.0169  -0.0234 -0.0014 141 PRO A O   
983  C CB  . PRO A 134 ? 0.5919 0.5178 0.8628 0.0009  -0.0303 -0.0087 141 PRO A CB  
984  C CG  . PRO A 134 ? 0.6293 0.5578 0.8936 -0.0136 -0.0266 -0.0103 141 PRO A CG  
985  C CD  . PRO A 134 ? 0.7099 0.6118 0.9457 -0.0161 -0.0265 -0.0021 141 PRO A CD  
986  N N   . GLU A 135 ? 0.7274 0.5905 0.9544 0.0174  -0.0395 0.0113  142 GLU A N   
987  C CA  . GLU A 135 ? 0.7837 0.6173 0.9975 0.0285  -0.0435 0.0196  142 GLU A CA  
988  C C   . GLU A 135 ? 0.7569 0.5637 0.9605 0.0214  -0.0313 0.0204  142 GLU A C   
989  O O   . GLU A 135 ? 0.7893 0.5717 0.9901 0.0295  -0.0308 0.0224  142 GLU A O   
990  C CB  . GLU A 135 ? 0.8742 0.6919 1.0611 0.0312  -0.0541 0.0317  142 GLU A CB  
991  C CG  . GLU A 135 ? 0.9724 0.8056 1.1653 0.0473  -0.0723 0.0339  142 GLU A CG  
992  C CD  . GLU A 135 ? 1.1982 1.0192 1.3573 0.0471  -0.0829 0.0452  142 GLU A CD  
993  O OE1 . GLU A 135 ? 1.2328 1.0289 1.3714 0.0610  -0.0923 0.0584  142 GLU A OE1 
994  O OE2 . GLU A 135 ? 1.1935 1.0264 1.3431 0.0331  -0.0809 0.0412  142 GLU A OE2 
995  N N   . ASN A 136 ? 0.6101 0.4209 0.8084 0.0067  -0.0222 0.0183  143 ASN A N   
996  C CA  . ASN A 136 ? 0.6366 0.4334 0.8301 -0.0026 -0.0118 0.0161  143 ASN A CA  
997  C C   . ASN A 136 ? 0.6282 0.4412 0.8373 -0.0048 -0.0054 0.0049  143 ASN A C   
998  O O   . ASN A 136 ? 0.5911 0.4011 0.7973 -0.0138 0.0012  0.0011  143 ASN A O   
999  C CB  . ASN A 136 ? 0.5795 0.3745 0.7588 -0.0153 -0.0065 0.0206  143 ASN A CB  
1000 C CG  . ASN A 136 ? 0.6421 0.4095 0.7991 -0.0180 -0.0060 0.0307  143 ASN A CG  
1001 O OD1 . ASN A 136 ? 0.7563 0.4975 0.9070 -0.0148 -0.0055 0.0343  143 ASN A OD1 
1002 N ND2 . ASN A 136 ? 0.5972 0.3665 0.7396 -0.0241 -0.0043 0.0354  143 ASN A ND2 
1003 N N   . ILE A 137 ? 0.5648 0.3977 0.7900 0.0025  -0.0070 -0.0011 144 ILE A N   
1004 C CA  . ILE A 137 ? 0.5979 0.4459 0.8327 0.0004  0.0004  -0.0109 144 ILE A CA  
1005 C C   . ILE A 137 ? 0.6248 0.4705 0.8723 0.0129  0.0000  -0.0182 144 ILE A C   
1006 O O   . ILE A 137 ? 0.6564 0.5172 0.9189 0.0222  -0.0045 -0.0190 144 ILE A O   
1007 C CB  . ILE A 137 ? 0.7110 0.5835 0.9518 -0.0044 0.0034  -0.0114 144 ILE A CB  
1008 C CG1 . ILE A 137 ? 0.7796 0.6490 1.0075 -0.0137 0.0045  -0.0049 144 ILE A CG1 
1009 C CG2 . ILE A 137 ? 0.7888 0.6751 1.0346 -0.0055 0.0120  -0.0198 144 ILE A CG2 
1010 C CD1 . ILE A 137 ? 0.7458 0.6283 0.9761 -0.0183 0.0073  -0.0031 144 ILE A CD1 
1011 N N   . LEU A 138 ? 0.5732 0.4008 0.8165 0.0130  0.0047  -0.0250 145 LEU A N   
1012 C CA  . LEU A 138 ? 0.6260 0.4444 0.8801 0.0263  0.0060  -0.0337 145 LEU A CA  
1013 C C   . LEU A 138 ? 0.6016 0.4416 0.8640 0.0252  0.0156  -0.0480 145 LEU A C   
1014 O O   . LEU A 138 ? 0.5647 0.4134 0.8165 0.0130  0.0204  -0.0507 145 LEU A O   
1015 C CB  . LEU A 138 ? 0.6145 0.3926 0.8559 0.0254  0.0073  -0.0340 145 LEU A CB  
1016 C CG  . LEU A 138 ? 0.5925 0.3449 0.8174 0.0211  0.0019  -0.0184 145 LEU A CG  
1017 C CD1 . LEU A 138 ? 0.7477 0.4561 0.9608 0.0184  0.0065  -0.0192 145 LEU A CD1 
1018 C CD2 . LEU A 138 ? 0.5920 0.3476 0.8198 0.0357  -0.0090 -0.0069 145 LEU A CD2 
1019 N N   . VAL A 139 ? 0.7025 0.5504 0.9827 0.0392  0.0183  -0.0573 146 VAL A N   
1020 C CA  . VAL A 139 ? 0.7185 0.5924 1.0087 0.0397  0.0296  -0.0712 146 VAL A CA  
1021 C C   . VAL A 139 ? 0.7059 0.5629 1.0019 0.0517  0.0358  -0.0867 146 VAL A C   
1022 O O   . VAL A 139 ? 0.7882 0.6290 1.0964 0.0682  0.0302  -0.0853 146 VAL A O   
1023 C CB  . VAL A 139 ? 0.6637 0.5729 0.9785 0.0456  0.0293  -0.0701 146 VAL A CB  
1024 C CG1 . VAL A 139 ? 0.6049 0.5426 0.9293 0.0434  0.0445  -0.0836 146 VAL A CG1 
1025 C CG2 . VAL A 139 ? 0.5842 0.5030 0.8929 0.0340  0.0228  -0.0563 146 VAL A CG2 
1026 N N   . ASP A 140 ? 0.7715 0.6303 1.0562 0.0444  0.0468  -0.1012 147 ASP A N   
1027 C CA  . ASP A 140 ? 0.7501 0.5952 1.0395 0.0548  0.0561  -0.1209 147 ASP A CA  
1028 C C   . ASP A 140 ? 0.7837 0.6635 1.0955 0.0657  0.0673  -0.1328 147 ASP A C   
1029 O O   . ASP A 140 ? 0.7375 0.6505 1.0591 0.0614  0.0684  -0.1256 147 ASP A O   
1030 C CB  . ASP A 140 ? 0.7735 0.6011 1.0376 0.0406  0.0617  -0.1342 147 ASP A CB  
1031 C CG  . ASP A 140 ? 0.8593 0.7172 1.1058 0.0265  0.0682  -0.1385 147 ASP A CG  
1032 O OD1 . ASP A 140 ? 0.8668 0.7543 1.1204 0.0297  0.0774  -0.1414 147 ASP A OD1 
1033 O OD2 . ASP A 140 ? 0.8283 0.6800 1.0531 0.0118  0.0640  -0.1387 147 ASP A OD2 
1034 N N   . ASN A 141 ? 0.8566 0.7274 1.1769 0.0785  0.0772  -0.1521 148 ASN A N   
1035 C CA  . ASN A 141 ? 0.8661 0.7706 1.2123 0.0913  0.0908  -0.1673 148 ASN A CA  
1036 C C   . ASN A 141 ? 0.8921 0.8329 1.2268 0.0753  0.1059  -0.1733 148 ASN A C   
1037 O O   . ASN A 141 ? 0.9194 0.8964 1.2783 0.0809  0.1170  -0.1800 148 ASN A O   
1038 C CB  . ASN A 141 ? 0.8187 0.6982 1.1721 0.1088  0.1000  -0.1893 148 ASN A CB  
1039 C CG  . ASN A 141 ? 0.8699 0.7791 1.2640 0.1327  0.1084  -0.2015 148 ASN A CG  
1040 O OD1 . ASN A 141 ? 0.8302 0.7506 1.2291 0.1380  0.1267  -0.2245 148 ASN A OD1 
1041 N ND2 . ASN A 141 ? 0.8157 0.7388 1.2397 0.1484  0.0948  -0.1877 148 ASN A ND2 
1042 N N   . ASP A 142 ? 0.8700 0.8013 1.1682 0.0563  0.1064  -0.1712 149 ASP A N   
1043 C CA  . ASP A 142 ? 0.9146 0.8730 1.1920 0.0405  0.1174  -0.1698 149 ASP A CA  
1044 C C   . ASP A 142 ? 0.8585 0.8302 1.1328 0.0286  0.1094  -0.1460 149 ASP A C   
1045 O O   . ASP A 142 ? 0.8525 0.8359 1.1023 0.0151  0.1161  -0.1401 149 ASP A O   
1046 C CB  . ASP A 142 ? 1.0252 0.9677 1.2622 0.0284  0.1190  -0.1793 149 ASP A CB  
1047 C CG  . ASP A 142 ? 1.0453 0.9773 1.2786 0.0358  0.1312  -0.2070 149 ASP A CG  
1048 O OD1 . ASP A 142 ? 1.0845 1.0379 1.3315 0.0440  0.1484  -0.2208 149 ASP A OD1 
1049 O OD2 . ASP A 142 ? 1.1377 1.0407 1.3540 0.0318  0.1249  -0.2167 149 ASP A OD2 
1050 N N   . PHE A 143 ? 0.8123 0.7787 1.1073 0.0340  0.0953  -0.1323 150 PHE A N   
1051 C CA  . PHE A 143 ? 0.7828 0.7563 1.0760 0.0238  0.0870  -0.1122 150 PHE A CA  
1052 C C   . PHE A 143 ? 0.7482 0.7032 1.0090 0.0111  0.0786  -0.1001 150 PHE A C   
1053 O O   . PHE A 143 ? 0.6778 0.6371 0.9342 0.0030  0.0744  -0.0850 150 PHE A O   
1054 C CB  . PHE A 143 ? 0.7531 0.7602 1.0588 0.0166  0.0999  -0.1105 150 PHE A CB  
1055 C CG  . PHE A 143 ? 0.8309 0.8651 1.1785 0.0288  0.1046  -0.1209 150 PHE A CG  
1056 C CD1 . PHE A 143 ? 0.8114 0.8563 1.1871 0.0340  0.0914  -0.1130 150 PHE A CD1 
1057 C CD2 . PHE A 143 ? 0.8363 0.8883 1.1963 0.0365  0.1216  -0.1404 150 PHE A CD2 
1058 C CE1 . PHE A 143 ? 0.7382 0.8149 1.1565 0.0472  0.0930  -0.1235 150 PHE A CE1 
1059 C CE2 . PHE A 143 ? 0.8149 0.8977 1.2196 0.0504  0.1256  -0.1514 150 PHE A CE2 
1060 C CZ  . PHE A 143 ? 0.8332 0.9300 1.2685 0.0562  0.1101  -0.1425 150 PHE A CZ  
1061 N N   . HIS A 144 ? 0.7349 0.6699 0.9767 0.0099  0.0755  -0.1077 151 HIS A N   
1062 C CA  . HIS A 144 ? 0.7037 0.6265 0.9225 -0.0004 0.0655  -0.0983 151 HIS A CA  
1063 C C   . HIS A 144 ? 0.7406 0.6441 0.9713 0.0022  0.0526  -0.0881 151 HIS A C   
1064 O O   . HIS A 144 ? 0.7779 0.6677 1.0251 0.0125  0.0506  -0.0922 151 HIS A O   
1065 C CB  . HIS A 144 ? 0.7219 0.6371 0.9178 -0.0055 0.0668  -0.1130 151 HIS A CB  
1066 C CG  . HIS A 144 ? 0.7406 0.6739 0.9175 -0.0082 0.0796  -0.1230 151 HIS A CG  
1067 N ND1 . HIS A 144 ? 0.7638 0.7122 0.9186 -0.0152 0.0821  -0.1111 151 HIS A ND1 
1068 C CD2 . HIS A 144 ? 0.8209 0.7575 0.9952 -0.0041 0.0923  -0.1433 151 HIS A CD2 
1069 C CE1 . HIS A 144 ? 0.8019 0.7623 0.9380 -0.0167 0.0955  -0.1225 151 HIS A CE1 
1070 N NE2 . HIS A 144 ? 0.9063 0.8617 1.0547 -0.0103 0.1025  -0.1434 151 HIS A NE2 
1071 N N   . ILE A 145 ? 0.7047 0.6059 0.9252 -0.0058 0.0445  -0.0745 152 ILE A N   
1072 C CA  . ILE A 145 ? 0.7051 0.5918 0.9337 -0.0050 0.0347  -0.0629 152 ILE A CA  
1073 C C   . ILE A 145 ? 0.6638 0.5354 0.8812 -0.0132 0.0286  -0.0617 152 ILE A C   
1074 O O   . ILE A 145 ? 0.6603 0.5399 0.8645 -0.0205 0.0287  -0.0671 152 ILE A O   
1075 C CB  . ILE A 145 ? 0.6576 0.5562 0.8907 -0.0067 0.0323  -0.0485 152 ILE A CB  
1076 C CG1 . ILE A 145 ? 0.6860 0.5922 0.9020 -0.0151 0.0326  -0.0407 152 ILE A CG1 
1077 C CG2 . ILE A 145 ? 0.6525 0.5695 0.9020 -0.0018 0.0390  -0.0516 152 ILE A CG2 
1078 C CD1 . ILE A 145 ? 0.6292 0.5263 0.8405 -0.0191 0.0246  -0.0318 152 ILE A CD1 
1079 N N   . LYS A 146 ? 0.6241 0.4766 0.8466 -0.0123 0.0233  -0.0546 153 LYS A N   
1080 C CA  . LYS A 146 ? 0.6913 0.5322 0.9067 -0.0226 0.0196  -0.0516 153 LYS A CA  
1081 C C   . LYS A 146 ? 0.6976 0.5308 0.9143 -0.0223 0.0153  -0.0366 153 LYS A C   
1082 O O   . LYS A 146 ? 0.7813 0.6023 1.0025 -0.0136 0.0130  -0.0312 153 LYS A O   
1083 C CB  . LYS A 146 ? 0.6668 0.4817 0.8808 -0.0261 0.0219  -0.0625 153 LYS A CB  
1084 C CG  . LYS A 146 ? 0.7071 0.5273 0.9164 -0.0293 0.0262  -0.0813 153 LYS A CG  
1085 C CD  . LYS A 146 ? 0.6883 0.4765 0.8963 -0.0355 0.0294  -0.0938 153 LYS A CD  
1086 C CE  . LYS A 146 ? 0.6628 0.4466 0.8678 -0.0324 0.0357  -0.1149 153 LYS A CE  
1087 N NZ  . LYS A 146 ? 0.6453 0.4557 0.8385 -0.0432 0.0348  -0.1282 153 LYS A NZ  
1088 N N   . ILE A 147 ? 0.5466 0.3884 0.7592 -0.0307 0.0139  -0.0309 154 ILE A N   
1089 C CA  . ILE A 147 ? 0.5588 0.3924 0.7691 -0.0323 0.0121  -0.0191 154 ILE A CA  
1090 C C   . ILE A 147 ? 0.6287 0.4347 0.8343 -0.0383 0.0140  -0.0184 154 ILE A C   
1091 O O   . ILE A 147 ? 0.6043 0.4059 0.8107 -0.0480 0.0173  -0.0274 154 ILE A O   
1092 C CB  . ILE A 147 ? 0.5556 0.4080 0.7652 -0.0374 0.0121  -0.0150 154 ILE A CB  
1093 C CG1 . ILE A 147 ? 0.5360 0.4056 0.7459 -0.0314 0.0116  -0.0125 154 ILE A CG1 
1094 C CG2 . ILE A 147 ? 0.5542 0.3982 0.7599 -0.0402 0.0128  -0.0060 154 ILE A CG2 
1095 C CD1 . ILE A 147 ? 0.6148 0.5023 0.8225 -0.0333 0.0110  -0.0137 154 ILE A CD1 
1096 N N   . ALA A 148 ? 0.6571 0.7371 0.7321 0.0795  -0.0570 -0.0077 155 ALA A N   
1097 C CA  . ALA A 148 ? 0.6590 0.7383 0.7311 0.0877  -0.0514 -0.0062 155 ALA A CA  
1098 C C   . ALA A 148 ? 0.7016 0.7772 0.7686 0.0830  -0.0555 -0.0116 155 ALA A C   
1099 O O   . ALA A 148 ? 0.7640 0.8359 0.8246 0.0741  -0.0622 -0.0147 155 ALA A O   
1100 C CB  . ALA A 148 ? 0.7027 0.8037 0.7772 0.0972  -0.0473 0.0063  155 ALA A CB  
1101 N N   . ASP A 149 ? 0.7203 0.7892 0.7827 0.0884  -0.0497 -0.0127 156 ASP A N   
1102 C CA  . ASP A 149 ? 0.7302 0.7926 0.7833 0.0866  -0.0499 -0.0165 156 ASP A CA  
1103 C C   . ASP A 149 ? 0.7509 0.8174 0.7967 0.0925  -0.0465 -0.0107 156 ASP A C   
1104 O O   . ASP A 149 ? 0.7911 0.8454 0.8301 0.0959  -0.0387 -0.0128 156 ASP A O   
1105 C CB  . ASP A 149 ? 0.6965 0.7476 0.7518 0.0882  -0.0441 -0.0229 156 ASP A CB  
1106 C CG  . ASP A 149 ? 0.8180 0.8586 0.8601 0.0899  -0.0397 -0.0260 156 ASP A CG  
1107 O OD1 . ASP A 149 ? 0.8887 0.9208 0.9130 0.0856  -0.0446 -0.0261 156 ASP A OD1 
1108 O OD2 . ASP A 149 ? 0.9412 0.9819 0.9881 0.0939  -0.0311 -0.0272 156 ASP A OD2 
1109 N N   . LEU A 150 ? 0.7496 0.8364 0.7966 0.0931  -0.0524 -0.0015 157 LEU A N   
1110 C CA  . LEU A 150 ? 0.7595 0.8553 0.7999 0.1037  -0.0496 0.0082  157 LEU A CA  
1111 C C   . LEU A 150 ? 0.7678 0.8524 0.7907 0.1002  -0.0516 0.0057  157 LEU A C   
1112 O O   . LEU A 150 ? 0.9990 1.0774 1.0106 0.1105  -0.0458 0.0104  157 LEU A O   
1113 C CB  . LEU A 150 ? 0.7283 0.8627 0.7812 0.1080  -0.0555 0.0238  157 LEU A CB  
1114 C CG  . LEU A 150 ? 0.7423 0.8846 0.8077 0.1169  -0.0483 0.0288  157 LEU A CG  
1115 C CD1 . LEU A 150 ? 0.7391 0.9309 0.8229 0.1189  -0.0538 0.0463  157 LEU A CD1 
1116 C CD2 . LEU A 150 ? 0.8147 0.9294 0.8644 0.1362  -0.0321 0.0308  157 LEU A CD2 
1117 N N   . GLY A 151 ? 0.7769 0.8512 0.7902 0.0867  -0.0582 -0.0014 158 GLY A N   
1118 C CA  . GLY A 151 ? 0.7390 0.7915 0.7278 0.0829  -0.0573 -0.0057 158 GLY A CA  
1119 C C   . GLY A 151 ? 0.7385 0.7656 0.7224 0.0879  -0.0433 -0.0154 158 GLY A C   
1120 O O   . GLY A 151 ? 0.8859 0.8923 0.8475 0.0865  -0.0392 -0.0188 158 GLY A O   
1121 N N   . LEU A 152 ? 0.7999 0.8307 0.8031 0.0924  -0.0361 -0.0182 159 LEU A N   
1122 C CA  . LEU A 152 ? 0.8552 0.8774 0.8620 0.0947  -0.0238 -0.0230 159 LEU A CA  
1123 C C   . LEU A 152 ? 0.8763 0.8853 0.8738 0.0960  -0.0181 -0.0282 159 LEU A C   
1124 O O   . LEU A 152 ? 0.8739 0.8755 0.8647 0.0995  -0.0063 -0.0293 159 LEU A O   
1125 C CB  . LEU A 152 ? 0.8543 0.8676 0.8486 0.0966  -0.0158 -0.0206 159 LEU A CB  
1126 C CG  . LEU A 152 ? 0.8957 0.9086 0.8872 0.1006  -0.0160 -0.0144 159 LEU A CG  
1127 C CD1 . LEU A 152 ? 0.9164 0.9100 0.8819 0.1049  -0.0089 -0.0111 159 LEU A CD1 
1128 C CD2 . LEU A 152 ? 0.8839 0.8965 0.8859 0.0955  -0.0125 -0.0156 159 LEU A CD2 
1129 N N   . ALA A 153 ? 0.9545 0.9565 0.9463 0.0941  -0.0248 -0.0303 160 ALA A N   
1130 C CA  . ALA A 153 ? 0.9461 0.9230 0.9174 0.0995  -0.0171 -0.0344 160 ALA A CA  
1131 C C   . ALA A 153 ? 0.8778 0.8681 0.8709 0.1127  -0.0035 -0.0332 160 ALA A C   
1132 O O   . ALA A 153 ? 0.9648 0.9389 0.9422 0.1241  0.0106  -0.0333 160 ALA A O   
1133 C CB  . ALA A 153 ? 0.9767 0.9359 0.9296 0.0922  -0.0274 -0.0364 160 ALA A CB  
1134 N N   . SER A 154 ? 0.8796 0.9000 0.9062 0.1111  -0.0074 -0.0301 161 SER A N   
1135 C CA  . SER A 154 ? 0.8716 0.9194 0.9256 0.1186  0.0012  -0.0249 161 SER A CA  
1136 C C   . SER A 154 ? 0.8777 0.9472 0.9456 0.1129  0.0097  -0.0206 161 SER A C   
1137 O O   . SER A 154 ? 0.7463 0.8485 0.8398 0.1148  0.0158  -0.0133 161 SER A O   
1138 C CB  . SER A 154 ? 0.8366 0.9028 0.9129 0.1146  -0.0096 -0.0228 161 SER A CB  
1139 O OG  . SER A 154 ? 0.8162 0.8630 0.8792 0.1216  -0.0137 -0.0254 161 SER A OG  
1140 N N   . PHE A 155 ? 0.9006 0.9541 0.9505 0.1050  0.0097  -0.0233 162 PHE A N   
1141 C CA  . PHE A 155 ? 1.0211 1.0838 1.0738 0.0944  0.0156  -0.0201 162 PHE A CA  
1142 C C   . PHE A 155 ? 1.0659 1.1043 1.0907 0.0965  0.0245  -0.0225 162 PHE A C   
1143 O O   . PHE A 155 ? 1.0420 1.0595 1.0455 0.0934  0.0187  -0.0244 162 PHE A O   
1144 C CB  . PHE A 155 ? 1.0454 1.1037 1.0960 0.0823  0.0056  -0.0198 162 PHE A CB  
1145 C CG  . PHE A 155 ? 0.9207 0.9948 0.9911 0.0794  -0.0038 -0.0182 162 PHE A CG  
1146 C CD1 . PHE A 155 ? 0.8788 0.9837 0.9729 0.0725  -0.0030 -0.0122 162 PHE A CD1 
1147 C CD2 . PHE A 155 ? 0.7889 0.8521 0.8554 0.0833  -0.0137 -0.0209 162 PHE A CD2 
1148 C CE1 . PHE A 155 ? 0.8660 0.9847 0.9756 0.0698  -0.0132 -0.0098 162 PHE A CE1 
1149 C CE2 . PHE A 155 ? 0.7778 0.8514 0.8588 0.0807  -0.0215 -0.0197 162 PHE A CE2 
1150 C CZ  . PHE A 155 ? 0.7656 0.8640 0.8662 0.0744  -0.0219 -0.0146 162 PHE A CZ  
1151 N N   . LYS A 156 ? 1.0775 1.1202 1.1019 0.1042  0.0398  -0.0204 163 LYS A N   
1152 C CA  . LYS A 156 ? 1.1305 1.1429 1.1218 0.1086  0.0502  -0.0232 163 LYS A CA  
1153 C C   . LYS A 156 ? 1.1542 1.1568 1.1304 0.0969  0.0533  -0.0226 163 LYS A C   
1154 O O   . LYS A 156 ? 1.1801 1.1512 1.1236 0.0976  0.0511  -0.0256 163 LYS A O   
1155 C CB  . LYS A 156 ? 1.1828 1.2003 1.1748 0.1233  0.0708  -0.0194 163 LYS A CB  
1156 C CG  . LYS A 156 ? 1.2824 1.2884 1.2685 0.1408  0.0727  -0.0202 163 LYS A CG  
1157 C CD  . LYS A 156 ? 1.3296 1.3430 1.3166 0.1620  0.0980  -0.0128 163 LYS A CD  
1158 C CE  . LYS A 156 ? 1.3520 1.3455 1.3251 0.1836  0.1026  -0.0122 163 LYS A CE  
1159 N NZ  . LYS A 156 ? 1.3818 1.3860 1.3568 0.2122  0.1314  -0.0013 163 LYS A NZ  
1160 N N   . MET A 157 ? 1.1976 1.2246 1.1926 0.0843  0.0575  -0.0176 164 MET A N   
1161 C CA  . MET A 157 ? 1.1715 1.1813 1.1439 0.0703  0.0627  -0.0166 164 MET A CA  
1162 C C   . MET A 157 ? 1.1245 1.1031 1.0712 0.0688  0.0502  -0.0192 164 MET A C   
1163 O O   . MET A 157 ? 1.1971 1.1444 1.1102 0.0701  0.0533  -0.0199 164 MET A O   
1164 C CB  . MET A 157 ? 1.2771 1.3189 1.2699 0.0505  0.0688  -0.0093 164 MET A CB  
1165 C CG  . MET A 157 ? 1.5119 1.5414 1.4817 0.0360  0.0832  -0.0067 164 MET A CG  
1166 S SD  . MET A 157 ? 1.5557 1.5884 1.5222 0.0516  0.1051  -0.0053 164 MET A SD  
1167 C CE  . MET A 157 ? 1.4617 1.5654 1.4853 0.0594  0.1144  0.0063  164 MET A CE  
1168 N N   . TRP A 158 ? 1.0461 1.0336 1.0074 0.0689  0.0379  -0.0191 165 TRP A N   
1169 C CA  . TRP A 158 ? 0.9557 0.9202 0.8971 0.0751  0.0285  -0.0187 165 TRP A CA  
1170 C C   . TRP A 158 ? 1.0068 0.9645 0.9382 0.0892  0.0209  -0.0192 165 TRP A C   
1171 O O   . TRP A 158 ? 1.0947 1.0355 1.0035 0.0964  0.0176  -0.0152 165 TRP A O   
1172 C CB  . TRP A 158 ? 0.9756 0.9515 0.9340 0.0724  0.0197  -0.0176 165 TRP A CB  
1173 C CG  . TRP A 158 ? 0.9839 0.9496 0.9312 0.0545  0.0237  -0.0154 165 TRP A CG  
1174 C CD1 . TRP A 158 ? 0.9691 0.9607 0.9371 0.0365  0.0247  -0.0133 165 TRP A CD1 
1175 C CD2 . TRP A 158 ? 0.9834 0.9065 0.8888 0.0509  0.0273  -0.0131 165 TRP A CD2 
1176 N NE1 . TRP A 158 ? 0.9442 0.9116 0.8842 0.0155  0.0260  -0.0107 165 TRP A NE1 
1177 C CE2 . TRP A 158 ? 1.0083 0.9258 0.9042 0.0248  0.0292  -0.0116 165 TRP A CE2 
1178 C CE3 . TRP A 158 ? 0.9643 0.8527 0.8358 0.0683  0.0297  -0.0102 165 TRP A CE3 
1179 C CZ2 . TRP A 158 ? 0.9945 0.8584 0.8370 0.0127  0.0342  -0.0097 165 TRP A CZ2 
1180 C CZ3 . TRP A 158 ? 1.0053 0.8430 0.8273 0.0640  0.0376  -0.0072 165 TRP A CZ3 
1181 C CH2 . TRP A 158 ? 1.0524 0.8714 0.8551 0.0350  0.0402  -0.0082 165 TRP A CH2 
1182 N N   . SER A 159 ? 1.1339 1.1032 1.0776 0.0926  0.0179  -0.0223 166 SER A N   
1183 C CA  . SER A 159 ? 1.2117 1.1715 1.1384 0.0977  0.0083  -0.0222 166 SER A CA  
1184 C C   . SER A 159 ? 1.2407 1.1744 1.1333 0.0983  0.0145  -0.0221 166 SER A C   
1185 O O   . SER A 159 ? 1.2412 1.1669 1.1137 0.1009  0.0047  -0.0175 166 SER A O   
1186 C CB  . SER A 159 ? 1.1790 1.1433 1.1136 0.0978  0.0045  -0.0262 166 SER A CB  
1187 O OG  . SER A 159 ? 1.3377 1.2902 1.2640 0.1008  0.0193  -0.0296 166 SER A OG  
1188 N N   . LYS A 160 ? 1.1830 1.1078 1.0705 0.0964  0.0307  -0.0253 167 LYS A N   
1189 C CA  . LYS A 160 ? 1.2765 1.1724 1.1289 0.0960  0.0406  -0.0256 167 LYS A CA  
1190 C C   . LYS A 160 ? 1.3984 1.2791 1.2310 0.0946  0.0417  -0.0215 167 LYS A C   
1191 O O   . LYS A 160 ? 1.5032 1.3571 1.3007 0.0969  0.0419  -0.0199 167 LYS A O   
1192 C CB  . LYS A 160 ? 1.4144 1.3110 1.2703 0.0957  0.0618  -0.0276 167 LYS A CB  
1193 C CG  . LYS A 160 ? 1.4956 1.3864 1.3484 0.1042  0.0668  -0.0305 167 LYS A CG  
1194 C CD  . LYS A 160 ? 1.5096 1.4188 1.3810 0.1106  0.0901  -0.0278 167 LYS A CD  
1195 C CE  . LYS A 160 ? 1.5288 1.4249 1.3906 0.1259  0.0984  -0.0290 167 LYS A CE  
1196 N NZ  . LYS A 160 ? 1.5295 1.4558 1.4173 0.1389  0.1228  -0.0218 167 LYS A NZ  
1197 N N   . LEU A 161 ? 1.3994 1.2897 1.2465 0.0906  0.0432  -0.0195 168 LEU A N   
1198 C CA  . LEU A 161 ? 1.3821 1.2458 1.1997 0.0916  0.0455  -0.0150 168 LEU A CA  
1199 C C   . LEU A 161 ? 1.4245 1.2819 1.2261 0.1080  0.0327  -0.0078 168 LEU A C   
1200 O O   . LEU A 161 ? 1.5826 1.4102 1.3479 0.1155  0.0365  -0.0024 168 LEU A O   
1201 C CB  . LEU A 161 ? 1.4401 1.3065 1.2671 0.0818  0.0490  -0.0143 168 LEU A CB  
1202 C CG  . LEU A 161 ? 1.4671 1.2918 1.2519 0.0819  0.0546  -0.0099 168 LEU A CG  
1203 C CD1 . LEU A 161 ? 1.4956 1.2829 1.2382 0.0739  0.0677  -0.0101 168 LEU A CD1 
1204 C CD2 . LEU A 161 ? 1.4738 1.2982 1.2641 0.0663  0.0561  -0.0103 168 LEU A CD2 
1205 N N   . ASN A 162 ? 1.3594 1.2465 1.1869 0.1134  0.0180  -0.0057 169 ASN A N   
1206 C CA  . ASN A 162 ? 1.4435 1.3423 1.2650 0.1267  0.0039  0.0050  169 ASN A CA  
1207 C C   . ASN A 162 ? 1.7235 1.6088 1.5163 0.1256  -0.0017 0.0072  169 ASN A C   
1208 O O   . ASN A 162 ? 1.7177 1.5887 1.4827 0.1370  -0.0027 0.0163  169 ASN A O   
1209 C CB  . ASN A 162 ? 1.4478 1.3858 1.3047 0.1257  -0.0102 0.0071  169 ASN A CB  
1210 C CG  . ASN A 162 ? 1.5335 1.5009 1.3950 0.1382  -0.0247 0.0227  169 ASN A CG  
1211 O OD1 . ASN A 162 ? 1.6151 1.6158 1.5023 0.1329  -0.0368 0.0254  169 ASN A OD1 
1212 N ND2 . ASN A 162 ? 1.5394 1.4984 1.3770 0.1549  -0.0233 0.0348  169 ASN A ND2 
1213 N N   . ASN A 163 ? 2.0466 1.9300 1.8395 0.1132  -0.0040 -0.0007 170 ASN A N   
1214 C CA  . ASN A 163 ? 2.0013 1.8623 1.7579 0.1080  -0.0094 -0.0001 170 ASN A CA  
1215 C C   . ASN A 163 ? 2.0307 1.8518 1.7547 0.1080  0.0094  -0.0049 170 ASN A C   
1216 O O   . ASN A 163 ? 1.9934 1.7965 1.7096 0.1009  0.0231  -0.0138 170 ASN A O   
1217 C CB  . ASN A 163 ? 1.8802 1.7383 1.6345 0.0951  -0.0152 -0.0071 170 ASN A CB  
1218 C CG  . ASN A 163 ? 2.1052 1.9378 1.8143 0.0850  -0.0270 -0.0046 170 ASN A CG  
1219 O OD1 . ASN A 163 ? 2.1263 1.9497 1.8095 0.0880  -0.0331 0.0033  170 ASN A OD1 
1220 N ND2 . ASN A 163 ? 2.1190 1.9331 1.8104 0.0723  -0.0302 -0.0110 170 ASN A ND2 
1221 N N   . GLU A 164 ? 2.0717 1.8783 1.7746 0.1179  0.0118  0.0025  171 GLU A N   
1222 C CA  . GLU A 164 ? 2.1502 1.9146 1.8156 0.1164  0.0295  -0.0005 171 GLU A CA  
1223 C C   . GLU A 164 ? 2.4156 2.1575 2.0393 0.1283  0.0217  0.0105  171 GLU A C   
1224 O O   . GLU A 164 ? 2.5344 2.2986 2.1653 0.1432  0.0079  0.0232  171 GLU A O   
1225 C CB  . GLU A 164 ? 2.0368 1.7943 1.7108 0.1134  0.0463  -0.0036 171 GLU A CB  
1226 C CG  . GLU A 164 ? 2.0932 1.8150 1.7367 0.1021  0.0671  -0.0086 171 GLU A CG  
1227 C CD  . GLU A 164 ? 2.1518 1.8645 1.7954 0.0912  0.0807  -0.0097 171 GLU A CD  
1228 O OE1 . GLU A 164 ? 2.3866 2.1291 2.0672 0.0861  0.0778  -0.0111 171 GLU A OE1 
1229 O OE2 . GLU A 164 ? 2.0468 1.7183 1.6475 0.0847  0.0937  -0.0089 171 GLU A OE2 
1230 N N   . GLU A 165 ? 2.5228 2.2231 2.1034 0.1235  0.0317  0.0073  172 GLU A N   
1231 C CA  . GLU A 165 ? 2.4515 2.1259 1.9858 0.1336  0.0233  0.0178  172 GLU A CA  
1232 C C   . GLU A 165 ? 2.4101 2.0668 1.9239 0.1532  0.0290  0.0282  172 GLU A C   
1233 O O   . GLU A 165 ? 2.3352 1.9994 1.8337 0.1722  0.0150  0.0440  172 GLU A O   
1234 C CB  . GLU A 165 ? 2.4052 2.0321 1.8934 0.1224  0.0355  0.0104  172 GLU A CB  
1235 C CG  . GLU A 165 ? 2.3011 1.9077 1.7436 0.1266  0.0188  0.0203  172 GLU A CG  
1236 C CD  . GLU A 165 ? 2.5185 2.0730 1.9116 0.1137  0.0320  0.0115  172 GLU A CD  
1237 O OE1 . GLU A 165 ? 2.5053 2.0544 1.9052 0.1010  0.0429  0.0001  172 GLU A OE1 
1238 O OE2 . GLU A 165 ? 2.5656 2.0810 1.9087 0.1192  0.0330  0.0173  172 GLU A OE2 
1239 N N   . HIS A 166 ? 2.3442 1.9763 1.8534 0.1482  0.0497  0.0212  173 HIS A N   
1240 C CA  . HIS A 166 ? 2.2810 1.8801 1.7580 0.1650  0.0589  0.0295  173 HIS A CA  
1241 C C   . HIS A 166 ? 2.2542 1.8861 1.7577 0.1877  0.0495  0.0414  173 HIS A C   
1242 O O   . HIS A 166 ? 1.9249 1.5270 1.3921 0.2120  0.0557  0.0535  173 HIS A O   
1243 C CB  . HIS A 166 ? 2.2292 1.7905 1.6884 0.1448  0.0818  0.0188  173 HIS A CB  
1244 C CG  . HIS A 166 ? 2.2463 1.7607 1.6597 0.1295  0.0970  0.0131  173 HIS A CG  
1245 N ND1 . HIS A 166 ? 2.1705 1.6368 1.5245 0.1432  0.0985  0.0204  173 HIS A ND1 
1246 C CD2 . HIS A 166 ? 2.2113 1.7203 1.6283 0.1020  0.1132  0.0026  173 HIS A CD2 
1247 C CE1 . HIS A 166 ? 2.1079 1.5368 1.4286 0.1232  0.1150  0.0128  173 HIS A CE1 
1248 N NE2 . HIS A 166 ? 2.1789 1.6362 1.5391 0.0980  0.1249  0.0027  173 HIS A NE2 
1249 N N   . ASN A 167 ? 2.3138 2.0012 1.8746 0.1816  0.0377  0.0388  174 ASN A N   
1250 C CA  . ASN A 167 ? 2.2433 1.9654 1.8346 0.1996  0.0318  0.0488  174 ASN A CA  
1251 C C   . ASN A 167 ? 2.2008 1.9519 1.7896 0.2297  0.0175  0.0711  174 ASN A C   
1252 O O   . ASN A 167 ? 2.0443 1.8341 1.6499 0.2246  -0.0024 0.0769  174 ASN A O   
1253 C CB  . ASN A 167 ? 2.2067 1.9802 1.8574 0.1822  0.0217  0.0400  174 ASN A CB  
1254 C CG  . ASN A 167 ? 2.1632 1.9679 1.8452 0.1959  0.0192  0.0474  174 ASN A CG  
1255 O OD1 . ASN A 167 ? 2.1344 1.9121 1.7912 0.2154  0.0311  0.0552  174 ASN A OD1 
1256 N ND2 . ASN A 167 ? 2.0683 1.9232 1.7982 0.1862  0.0056  0.0451  174 ASN A ND2 
1257 N N   . GLU A 168 ? 2.3296 2.0617 1.8947 0.2602  0.0283  0.0850  175 GLU A N   
1258 C CA  . GLU A 168 ? 2.3537 2.1193 1.9172 0.2968  0.0187  0.1118  175 GLU A CA  
1259 C C   . GLU A 168 ? 2.2694 2.1072 1.8883 0.3125  0.0095  0.1264  175 GLU A C   
1260 O O   . GLU A 168 ? 2.3612 2.2294 1.9804 0.3490  0.0079  0.1522  175 GLU A O   
1261 C CB  . GLU A 168 ? 2.3126 2.0099 1.8064 0.3295  0.0386  0.1232  175 GLU A CB  
1262 C CG  . GLU A 168 ? 2.2426 1.8889 1.7062 0.3460  0.0633  0.1225  175 GLU A CG  
1263 C CD  . GLU A 168 ? 2.4876 2.0581 1.8699 0.3825  0.0833  0.1368  175 GLU A CD  
1264 O OE1 . GLU A 168 ? 2.5313 2.0460 1.8621 0.3729  0.0881  0.1306  175 GLU A OE1 
1265 O OE2 . GLU A 168 ? 2.5158 2.0777 1.8810 0.4224  0.0966  0.1547  175 GLU A OE2 
1266 N N   . LEU A 169 ? 2.2010 2.0691 1.8663 0.2866  0.0040  0.1121  176 LEU A N   
1267 C CA  . LEU A 169 ? 2.1269 2.0651 1.8466 0.2938  -0.0060 0.1237  176 LEU A CA  
1268 C C   . LEU A 169 ? 2.0833 2.0918 1.8409 0.2761  -0.0349 0.1320  176 LEU A C   
1269 O O   . LEU A 169 ? 2.0097 2.0781 1.8137 0.2689  -0.0467 0.1379  176 LEU A O   
1270 C CB  . LEU A 169 ? 1.9981 1.9278 1.7419 0.2729  0.0017  0.1043  176 LEU A CB  
1271 C CG  . LEU A 169 ? 1.9344 1.7954 1.6381 0.2823  0.0272  0.0968  176 LEU A CG  
1272 C CD1 . LEU A 169 ? 1.8897 1.7403 1.6134 0.2509  0.0300  0.0752  176 LEU A CD1 
1273 C CD2 . LEU A 169 ? 1.8069 1.6722 1.5020 0.3222  0.0398  0.1175  176 LEU A CD2 
1274 N N   . GLY A 181 ? 0.9161 0.8318 0.9900 -0.0111 -0.1254 0.0008  188 GLY A N   
1275 C CA  . GLY A 181 ? 0.9772 0.8874 1.0823 -0.0050 -0.1141 0.0065  188 GLY A CA  
1276 C C   . GLY A 181 ? 1.0285 0.9042 1.1197 -0.0095 -0.0926 0.0157  188 GLY A C   
1277 O O   . GLY A 181 ? 0.9708 0.8458 1.0873 -0.0132 -0.0787 0.0127  188 GLY A O   
1278 N N   . THR A 182 ? 1.0902 0.9396 1.1408 -0.0095 -0.0900 0.0266  189 THR A N   
1279 C CA  . THR A 182 ? 1.1832 1.0063 1.2206 -0.0178 -0.0686 0.0318  189 THR A CA  
1280 C C   . THR A 182 ? 1.1417 0.9711 1.1872 -0.0319 -0.0542 0.0175  189 THR A C   
1281 O O   . THR A 182 ? 0.9590 0.7844 1.0234 -0.0355 -0.0394 0.0161  189 THR A O   
1282 C CB  . THR A 182 ? 1.3064 1.1016 1.2969 -0.0171 -0.0669 0.0461  189 THR A CB  
1283 O OG1 . THR A 182 ? 1.2588 1.0608 1.2176 -0.0194 -0.0777 0.0421  189 THR A OG1 
1284 C CG2 . THR A 182 ? 1.2659 1.0420 1.2483 -0.0022 -0.0762 0.0636  189 THR A CG2 
1285 N N   . LEU A 183 ? 1.1148 0.9544 1.1473 -0.0385 -0.0600 0.0062  190 LEU A N   
1286 C CA  . LEU A 183 ? 1.0268 0.8649 1.0613 -0.0506 -0.0459 -0.0079 190 LEU A CA  
1287 C C   . LEU A 183 ? 0.9100 0.7597 0.9824 -0.0553 -0.0406 -0.0184 190 LEU A C   
1288 O O   . LEU A 183 ? 1.0146 0.8552 1.0887 -0.0625 -0.0266 -0.0269 190 LEU A O   
1289 C CB  . LEU A 183 ? 1.0446 0.8862 1.0494 -0.0575 -0.0534 -0.0193 190 LEU A CB  
1290 C CG  . LEU A 183 ? 1.0713 0.8984 1.0279 -0.0558 -0.0553 -0.0105 190 LEU A CG  
1291 C CD1 . LEU A 183 ? 1.1139 0.9511 1.0432 -0.0626 -0.0671 -0.0250 190 LEU A CD1 
1292 C CD2 . LEU A 183 ? 1.0129 0.8187 0.9552 -0.0601 -0.0315 -0.0066 190 LEU A CD2 
1293 N N   . TYR A 184 ? 0.8716 0.7400 0.9722 -0.0512 -0.0504 -0.0183 191 TYR A N   
1294 C CA  . TYR A 184 ? 0.8196 0.7000 0.9514 -0.0590 -0.0451 -0.0291 191 TYR A CA  
1295 C C   . TYR A 184 ? 0.7451 0.6112 0.8895 -0.0598 -0.0270 -0.0254 191 TYR A C   
1296 O O   . TYR A 184 ? 0.7878 0.6514 0.9446 -0.0681 -0.0183 -0.0332 191 TYR A O   
1297 C CB  . TYR A 184 ? 0.7638 0.6720 0.9254 -0.0547 -0.0573 -0.0306 191 TYR A CB  
1298 C CG  . TYR A 184 ? 0.7856 0.7195 0.9462 -0.0527 -0.0788 -0.0370 191 TYR A CG  
1299 C CD1 . TYR A 184 ? 0.7771 0.7121 0.9123 -0.0605 -0.0872 -0.0465 191 TYR A CD1 
1300 C CD2 . TYR A 184 ? 0.8985 0.8595 1.0859 -0.0421 -0.0917 -0.0355 191 TYR A CD2 
1301 C CE1 . TYR A 184 ? 0.7865 0.7501 0.9209 -0.0576 -0.1101 -0.0527 191 TYR A CE1 
1302 C CE2 . TYR A 184 ? 0.8078 0.7988 0.9991 -0.0374 -0.1140 -0.0414 191 TYR A CE2 
1303 C CZ  . TYR A 184 ? 0.7957 0.7888 0.9598 -0.0452 -0.1244 -0.0495 191 TYR A CZ  
1304 O OH  . TYR A 184 ? 0.8841 0.9110 1.0515 -0.0394 -0.1495 -0.0555 191 TYR A OH  
1305 N N   . TYR A 185 ? 0.7997 0.6554 0.9393 -0.0518 -0.0218 -0.0137 192 TYR A N   
1306 C CA  . TYR A 185 ? 0.7173 0.5648 0.8683 -0.0504 -0.0082 -0.0096 192 TYR A CA  
1307 C C   . TYR A 185 ? 0.6569 0.4891 0.7929 -0.0507 0.0037  -0.0085 192 TYR A C   
1308 O O   . TYR A 185 ? 0.5695 0.3991 0.7150 -0.0474 0.0124  -0.0047 192 TYR A O   
1309 C CB  . TYR A 185 ? 0.6875 0.5405 0.8509 -0.0426 -0.0109 -0.0013 192 TYR A CB  
1310 C CG  . TYR A 185 ? 0.6589 0.5304 0.8411 -0.0406 -0.0204 -0.0046 192 TYR A CG  
1311 C CD1 . TYR A 185 ? 0.6504 0.5307 0.8290 -0.0347 -0.0350 -0.0036 192 TYR A CD1 
1312 C CD2 . TYR A 185 ? 0.6414 0.5234 0.8451 -0.0442 -0.0144 -0.0089 192 TYR A CD2 
1313 C CE1 . TYR A 185 ? 0.7110 0.6152 0.9128 -0.0312 -0.0442 -0.0086 192 TYR A CE1 
1314 C CE2 . TYR A 185 ? 0.6268 0.5312 0.8519 -0.0437 -0.0206 -0.0141 192 TYR A CE2 
1315 C CZ  . TYR A 185 ? 0.6229 0.5412 0.8504 -0.0367 -0.0358 -0.0151 192 TYR A CZ  
1316 O OH  . TYR A 185 ? 0.6292 0.5758 0.8841 -0.0343 -0.0418 -0.0218 192 TYR A OH  
1317 N N   . MET A 186 ? 0.6396 0.4651 0.7535 -0.0545 0.0040  -0.0135 193 MET A N   
1318 C CA  . MET A 186 ? 0.6938 0.5091 0.7935 -0.0543 0.0163  -0.0135 193 MET A CA  
1319 C C   . MET A 186 ? 0.7256 0.5322 0.8281 -0.0564 0.0269  -0.0242 193 MET A C   
1320 O O   . MET A 186 ? 0.8758 0.6784 0.9718 -0.0629 0.0239  -0.0350 193 MET A O   
1321 C CB  . MET A 186 ? 0.7503 0.5611 0.8190 -0.0569 0.0127  -0.0123 193 MET A CB  
1322 C CG  . MET A 186 ? 0.7651 0.5686 0.8193 -0.0581 0.0276  -0.0109 193 MET A CG  
1323 S SD  . MET A 186 ? 0.9534 0.7480 0.9640 -0.0619 0.0234  -0.0047 193 MET A SD  
1324 C CE  . MET A 186 ? 0.8580 0.6481 0.8742 -0.0575 0.0173  0.0134  193 MET A CE  
1325 N N   . ALA A 187 ? 0.7296 0.5331 0.8421 -0.0507 0.0388  -0.0224 194 ALA A N   
1326 C CA  . ALA A 187 ? 0.6303 0.4214 0.7464 -0.0483 0.0499  -0.0310 194 ALA A CA  
1327 C C   . ALA A 187 ? 0.7300 0.5112 0.8233 -0.0531 0.0564  -0.0440 194 ALA A C   
1328 O O   . ALA A 187 ? 0.7642 0.5506 0.8395 -0.0553 0.0576  -0.0431 194 ALA A O   
1329 C CB  . ALA A 187 ? 0.6917 0.4869 0.8240 -0.0376 0.0589  -0.0258 194 ALA A CB  
1330 N N   . PRO A 188 ? 0.7346 0.4986 0.8255 -0.0562 0.0614  -0.0566 195 PRO A N   
1331 C CA  . PRO A 188 ? 0.7081 0.4611 0.7745 -0.0623 0.0675  -0.0729 195 PRO A CA  
1332 C C   . PRO A 188 ? 0.6971 0.4508 0.7532 -0.0560 0.0824  -0.0766 195 PRO A C   
1333 O O   . PRO A 188 ? 0.6907 0.4429 0.7187 -0.0624 0.0856  -0.0864 195 PRO A O   
1334 C CB  . PRO A 188 ? 0.7440 0.4727 0.8172 -0.0650 0.0739  -0.0852 195 PRO A CB  
1335 C CG  . PRO A 188 ? 0.7486 0.4730 0.8473 -0.0546 0.0770  -0.0722 195 PRO A CG  
1336 C CD  . PRO A 188 ? 0.6975 0.4469 0.8058 -0.0545 0.0641  -0.0566 195 PRO A CD  
1337 N N   . GLU A 189 ? 0.6974 0.4560 0.7759 -0.0437 0.0918  -0.0700 196 GLU A N   
1338 C CA  . GLU A 189 ? 0.7698 0.5396 0.8475 -0.0379 0.1064  -0.0724 196 GLU A CA  
1339 C C   . GLU A 189 ? 0.8245 0.6087 0.8815 -0.0470 0.1052  -0.0661 196 GLU A C   
1340 O O   . GLU A 189 ? 0.9883 0.7770 1.0324 -0.0483 0.1198  -0.0727 196 GLU A O   
1341 C CB  . GLU A 189 ? 0.7695 0.5514 0.8808 -0.0227 0.1124  -0.0654 196 GLU A CB  
1342 C CG  . GLU A 189 ? 0.8242 0.6228 0.9548 -0.0211 0.1001  -0.0488 196 GLU A CG  
1343 C CD  . GLU A 189 ? 0.7965 0.5833 0.9406 -0.0151 0.0915  -0.0423 196 GLU A CD  
1344 O OE1 . GLU A 189 ? 0.6934 0.4934 0.8576 -0.0066 0.0869  -0.0320 196 GLU A OE1 
1345 O OE2 . GLU A 189 ? 0.7878 0.5524 0.9211 -0.0204 0.0896  -0.0480 196 GLU A OE2 
1346 N N   . HIS A 190 ? 0.7982 0.5873 0.8514 -0.0526 0.0895  -0.0534 197 HIS A N   
1347 C CA  . HIS A 190 ? 0.8357 0.6296 0.8649 -0.0603 0.0867  -0.0443 197 HIS A CA  
1348 C C   . HIS A 190 ? 0.8469 0.6316 0.8385 -0.0683 0.0757  -0.0472 197 HIS A C   
1349 O O   . HIS A 190 ? 0.8938 0.6768 0.8561 -0.0734 0.0768  -0.0405 197 HIS A O   
1350 C CB  . HIS A 190 ? 0.7638 0.5661 0.8108 -0.0591 0.0764  -0.0283 197 HIS A CB  
1351 C CG  . HIS A 190 ? 0.7596 0.5755 0.8402 -0.0525 0.0841  -0.0257 197 HIS A CG  
1352 N ND1 . HIS A 190 ? 0.8170 0.6451 0.9039 -0.0533 0.1003  -0.0280 197 HIS A ND1 
1353 C CD2 . HIS A 190 ? 0.6925 0.5152 0.8017 -0.0452 0.0778  -0.0218 197 HIS A CD2 
1354 C CE1 . HIS A 190 ? 0.7122 0.5569 0.8328 -0.0461 0.1013  -0.0264 197 HIS A CE1 
1355 N NE2 . HIS A 190 ? 0.7237 0.5637 0.8553 -0.0407 0.0874  -0.0219 197 HIS A NE2 
1356 N N   . LEU A 191 ? 0.9113 0.6905 0.9029 -0.0701 0.0651  -0.0569 198 LEU A N   
1357 C CA  . LEU A 191 ? 0.9343 0.7108 0.8926 -0.0778 0.0525  -0.0637 198 LEU A CA  
1358 C C   . LEU A 191 ? 0.9908 0.7588 0.9157 -0.0827 0.0668  -0.0787 198 LEU A C   
1359 O O   . LEU A 191 ? 0.9592 0.7189 0.8944 -0.0810 0.0816  -0.0936 198 LEU A O   
1360 C CB  . LEU A 191 ? 0.9487 0.7257 0.9228 -0.0815 0.0396  -0.0738 198 LEU A CB  
1361 C CG  . LEU A 191 ? 0.9662 0.7532 0.9735 -0.0781 0.0274  -0.0630 198 LEU A CG  
1362 C CD1 . LEU A 191 ? 0.9515 0.7388 0.9710 -0.0860 0.0200  -0.0768 198 LEU A CD1 
1363 C CD2 . LEU A 191 ? 1.0347 0.8337 1.0351 -0.0748 0.0115  -0.0473 198 LEU A CD2 
1364 N N   . ASN A 192 ? 1.0176 0.7854 0.9005 -0.0876 0.0634  -0.0742 199 ASN A N   
1365 C CA  . ASN A 192 ? 1.0793 0.8400 0.9231 -0.0930 0.0798  -0.0867 199 ASN A CA  
1366 C C   . ASN A 192 ? 1.0287 0.7900 0.8883 -0.0892 0.1083  -0.0901 199 ASN A C   
1367 O O   . ASN A 192 ? 1.0720 0.8282 0.9174 -0.0907 0.1257  -0.1084 199 ASN A O   
1368 C CB  . ASN A 192 ? 1.0714 0.8259 0.8962 -0.0997 0.0748  -0.1115 199 ASN A CB  
1369 C CG  . ASN A 192 ? 1.0448 0.8069 0.8444 -0.1053 0.0468  -0.1102 199 ASN A CG  
1370 O OD1 . ASN A 192 ? 1.0810 0.8510 0.8778 -0.1013 0.0308  -0.0898 199 ASN A OD1 
1371 N ND2 . ASN A 192 ? 1.1695 0.9299 0.9519 -0.1140 0.0407  -0.1334 199 ASN A ND2 
1372 N N   . ASP A 193 ? 1.1057 0.8758 0.9948 -0.0845 0.1124  -0.0738 200 ASP A N   
1373 C CA  . ASP A 193 ? 1.1006 0.8806 1.0118 -0.0812 0.1365  -0.0755 200 ASP A CA  
1374 C C   . ASP A 193 ? 1.0828 0.8725 1.0128 -0.0820 0.1345  -0.0549 200 ASP A C   
1375 O O   . ASP A 193 ? 1.0575 0.8574 1.0294 -0.0751 0.1309  -0.0504 200 ASP A O   
1376 C CB  . ASP A 193 ? 1.1812 0.9635 1.1323 -0.0699 0.1446  -0.0896 200 ASP A CB  
1377 C CG  . ASP A 193 ? 1.2062 1.0035 1.1779 -0.0640 0.1704  -0.0972 200 ASP A CG  
1378 O OD1 . ASP A 193 ? 1.2771 1.0878 1.2419 -0.0707 0.1832  -0.0904 200 ASP A OD1 
1379 O OD2 . ASP A 193 ? 1.1338 0.9296 1.1306 -0.0522 0.1785  -0.1103 200 ASP A OD2 
1380 N N   . VAL A 194 ? 1.0369 0.8201 0.9310 -0.0913 0.1367  -0.0427 201 VAL A N   
1381 C CA  . VAL A 194 ? 1.0094 0.7941 0.9132 -0.0956 0.1374  -0.0241 201 VAL A CA  
1382 C C   . VAL A 194 ? 0.9020 0.7060 0.8379 -0.0987 0.1607  -0.0272 201 VAL A C   
1383 O O   . VAL A 194 ? 0.8107 0.6209 0.7711 -0.1016 0.1595  -0.0164 201 VAL A O   
1384 C CB  . VAL A 194 ? 1.1633 0.9277 1.0144 -0.1044 0.1337  -0.0078 201 VAL A CB  
1385 C CG1 . VAL A 194 ? 1.1982 0.9513 1.0284 -0.0984 0.1054  -0.0026 201 VAL A CG1 
1386 C CG2 . VAL A 194 ? 1.2710 1.0306 1.0780 -0.1141 0.1557  -0.0133 201 VAL A CG2 
1387 N N   . ASN A 195 ? 0.9014 0.7170 0.8387 -0.0984 0.1818  -0.0435 202 ASN A N   
1388 C CA  . ASN A 195 ? 0.9157 0.7579 0.8882 -0.1002 0.2048  -0.0496 202 ASN A CA  
1389 C C   . ASN A 195 ? 0.8929 0.7586 0.9249 -0.0861 0.1996  -0.0557 202 ASN A C   
1390 O O   . ASN A 195 ? 0.9464 0.8378 1.0134 -0.0886 0.2093  -0.0552 202 ASN A O   
1391 C CB  . ASN A 195 ? 0.9681 0.8167 0.9201 -0.1040 0.2315  -0.0655 202 ASN A CB  
1392 C CG  . ASN A 195 ? 1.0541 0.8831 0.9449 -0.1208 0.2415  -0.0561 202 ASN A CG  
1393 O OD1 . ASN A 195 ? 1.0388 0.8572 0.9156 -0.1322 0.2392  -0.0369 202 ASN A OD1 
1394 N ND2 . ASN A 195 ? 1.0764 0.8977 0.9274 -0.1224 0.2534  -0.0695 202 ASN A ND2 
1395 N N   . ALA A 196 ? 0.9773 0.8342 1.0192 -0.0725 0.1842  -0.0610 203 ALA A N   
1396 C CA  . ALA A 196 ? 0.9157 0.7891 1.0065 -0.0570 0.1778  -0.0641 203 ALA A CA  
1397 C C   . ALA A 196 ? 0.8622 0.7486 0.9803 -0.0587 0.1648  -0.0504 203 ALA A C   
1398 O O   . ALA A 196 ? 0.9390 0.8092 1.0394 -0.0660 0.1502  -0.0379 203 ALA A O   
1399 C CB  . ALA A 196 ? 0.8176 0.6698 0.9050 -0.0457 0.1647  -0.0696 203 ALA A CB  
1400 N N   . LYS A 197 ? 0.7831 0.7003 0.9448 -0.0507 0.1697  -0.0545 204 LYS A N   
1401 C CA  . LYS A 197 ? 0.7922 0.7283 0.9823 -0.0535 0.1597  -0.0460 204 LYS A CA  
1402 C C   . LYS A 197 ? 0.7705 0.6931 0.9656 -0.0427 0.1370  -0.0386 204 LYS A C   
1403 O O   . LYS A 197 ? 0.8026 0.7217 1.0074 -0.0269 0.1335  -0.0431 204 LYS A O   
1404 C CB  . LYS A 197 ? 0.8220 0.8018 1.0596 -0.0459 0.1692  -0.0554 204 LYS A CB  
1405 C CG  . LYS A 197 ? 0.9967 1.0009 1.2423 -0.0537 0.1956  -0.0669 204 LYS A CG  
1406 C CD  . LYS A 197 ? 1.0720 1.0892 1.3190 -0.0778 0.2058  -0.0628 204 LYS A CD  
1407 C CE  . LYS A 197 ? 1.0915 1.1280 1.3383 -0.0880 0.2358  -0.0740 204 LYS A CE  
1408 N NZ  . LYS A 197 ? 1.1062 1.1483 1.3488 -0.1153 0.2495  -0.0687 204 LYS A NZ  
1409 N N   . PRO A 198 ? 0.8505 0.7624 1.0372 -0.0511 0.1233  -0.0275 205 PRO A N   
1410 C CA  . PRO A 198 ? 0.7527 0.6581 0.9480 -0.0416 0.1048  -0.0217 205 PRO A CA  
1411 C C   . PRO A 198 ? 0.6898 0.6231 0.9213 -0.0301 0.0999  -0.0234 205 PRO A C   
1412 O O   . PRO A 198 ? 0.6998 0.6628 0.9551 -0.0331 0.1069  -0.0282 205 PRO A O   
1413 C CB  . PRO A 198 ? 0.7622 0.6528 0.9414 -0.0530 0.0951  -0.0119 205 PRO A CB  
1414 C CG  . PRO A 198 ? 0.8895 0.7649 1.0386 -0.0654 0.1052  -0.0101 205 PRO A CG  
1415 C CD  . PRO A 198 ? 0.9009 0.7976 1.0623 -0.0681 0.1247  -0.0191 205 PRO A CD  
1416 N N   . THR A 199 ? 0.7258 0.6501 0.9602 -0.0176 0.0880  -0.0196 206 THR A N   
1417 C CA  . THR A 199 ? 0.7353 0.6817 0.9962 -0.0036 0.0801  -0.0184 206 THR A CA  
1418 C C   . THR A 199 ? 0.7263 0.6621 0.9798 -0.0040 0.0650  -0.0096 206 THR A C   
1419 O O   . THR A 199 ? 0.6852 0.5986 0.9183 -0.0132 0.0615  -0.0057 206 THR A O   
1420 C CB  . THR A 199 ? 0.6834 0.6246 0.9515 0.0162  0.0840  -0.0213 206 THR A CB  
1421 O OG1 . THR A 199 ? 0.7526 0.6564 0.9970 0.0175  0.0809  -0.0174 206 THR A OG1 
1422 C CG2 . THR A 199 ? 0.5638 0.5163 0.8398 0.0179  0.1018  -0.0329 206 THR A CG2 
1423 N N   . GLU A 200 ? 0.7405 0.6948 1.0107 0.0075  0.0560  -0.0070 207 GLU A N   
1424 C CA  . GLU A 200 ? 0.6823 0.6264 0.9429 0.0100  0.0437  0.0010  207 GLU A CA  
1425 C C   . GLU A 200 ? 0.7284 0.6368 0.9680 0.0126  0.0447  0.0063  207 GLU A C   
1426 O O   . GLU A 200 ? 0.8075 0.7024 1.0344 0.0055  0.0396  0.0104  207 GLU A O   
1427 C CB  . GLU A 200 ? 0.7911 0.7595 1.0671 0.0252  0.0341  0.0038  207 GLU A CB  
1428 C CG  . GLU A 200 ? 0.7983 0.8087 1.0984 0.0205  0.0297  -0.0037 207 GLU A CG  
1429 C CD  . GLU A 200 ? 0.9052 0.9452 1.2204 0.0384  0.0171  -0.0016 207 GLU A CD  
1430 O OE1 . GLU A 200 ? 1.1721 1.1994 1.4809 0.0582  0.0140  0.0072  207 GLU A OE1 
1431 O OE2 . GLU A 200 ? 1.0501 1.1260 1.3828 0.0326  0.0096  -0.0087 207 GLU A OE2 
1432 N N   . LYS A 201 ? 0.6619 0.5563 0.8999 0.0211  0.0527  0.0039  208 LYS A N   
1433 C CA  . LYS A 201 ? 0.7681 0.6278 0.9882 0.0205  0.0555  0.0058  208 LYS A CA  
1434 C C   . LYS A 201 ? 0.6732 0.5188 0.8771 0.0040  0.0570  0.0014  208 LYS A C   
1435 O O   . LYS A 201 ? 0.8615 0.6865 1.0542 -0.0006 0.0555  0.0027  208 LYS A O   
1436 C CB  . LYS A 201 ? 0.7028 0.5472 0.9254 0.0345  0.0646  0.0022  208 LYS A CB  
1437 C CG  . LYS A 201 ? 0.7567 0.6123 0.9948 0.0564  0.0612  0.0085  208 LYS A CG  
1438 C CD  . LYS A 201 ? 0.7357 0.5842 0.9656 0.0615  0.0507  0.0221  208 LYS A CD  
1439 C CE  . LYS A 201 ? 0.7917 0.6500 1.0319 0.0860  0.0450  0.0303  208 LYS A CE  
1440 N NZ  . LYS A 201 ? 0.8655 0.6907 1.1022 0.1033  0.0534  0.0325  208 LYS A NZ  
1441 N N   . SER A 202 ? 0.6737 0.5304 0.8758 -0.0048 0.0602  -0.0035 209 SER A N   
1442 C CA  . SER A 202 ? 0.6912 0.5373 0.8753 -0.0183 0.0578  -0.0047 209 SER A CA  
1443 C C   . SER A 202 ? 0.7194 0.5648 0.9020 -0.0232 0.0469  0.0016  209 SER A C   
1444 O O   . SER A 202 ? 0.8477 0.6816 1.0198 -0.0288 0.0425  0.0009  209 SER A O   
1445 C CB  . SER A 202 ? 0.6976 0.5536 0.8770 -0.0261 0.0636  -0.0070 209 SER A CB  
1446 O OG  . SER A 202 ? 0.7951 0.6562 0.9777 -0.0219 0.0763  -0.0146 209 SER A OG  
1447 N N   . ASP A 203 ? 0.6095 0.4701 0.8043 -0.0209 0.0427  0.0056  210 ASP A N   
1448 C CA  . ASP A 203 ? 0.5523 0.4136 0.7474 -0.0235 0.0344  0.0096  210 ASP A CA  
1449 C C   . ASP A 203 ? 0.6278 0.4808 0.8222 -0.0193 0.0327  0.0127  210 ASP A C   
1450 O O   . ASP A 203 ? 0.6125 0.4627 0.8047 -0.0237 0.0288  0.0135  210 ASP A O   
1451 C CB  . ASP A 203 ? 0.5245 0.4036 0.7307 -0.0232 0.0313  0.0101  210 ASP A CB  
1452 C CG  . ASP A 203 ? 0.6300 0.5128 0.8363 -0.0322 0.0341  0.0076  210 ASP A CG  
1453 O OD1 . ASP A 203 ? 0.7193 0.5887 0.9125 -0.0378 0.0370  0.0082  210 ASP A OD1 
1454 O OD2 . ASP A 203 ? 0.5344 0.4331 0.7525 -0.0348 0.0333  0.0051  210 ASP A OD2 
1455 N N   . VAL A 204 ? 0.6484 0.4973 0.8450 -0.0103 0.0365  0.0150  211 VAL A N   
1456 C CA  . VAL A 204 ? 0.6666 0.4999 0.8579 -0.0074 0.0380  0.0200  211 VAL A CA  
1457 C C   . VAL A 204 ? 0.6649 0.4805 0.8495 -0.0174 0.0413  0.0153  211 VAL A C   
1458 O O   . VAL A 204 ? 0.9258 0.7357 1.1089 -0.0229 0.0415  0.0173  211 VAL A O   
1459 C CB  . VAL A 204 ? 0.6439 0.4697 0.8361 0.0070  0.0416  0.0252  211 VAL A CB  
1460 C CG1 . VAL A 204 ? 0.6760 0.4761 0.8573 0.0085  0.0458  0.0327  211 VAL A CG1 
1461 C CG2 . VAL A 204 ? 0.5904 0.4409 0.7912 0.0171  0.0350  0.0292  211 VAL A CG2 
1462 N N   . TYR A 205 ? 0.6450 0.4546 0.8255 -0.0209 0.0440  0.0076  212 TYR A N   
1463 C CA  . TYR A 205 ? 0.6532 0.4522 0.8271 -0.0321 0.0439  0.0002  212 TYR A CA  
1464 C C   . TYR A 205 ? 0.6272 0.4415 0.8042 -0.0393 0.0347  0.0001  212 TYR A C   
1465 O O   . TYR A 205 ? 0.6477 0.4615 0.8283 -0.0468 0.0332  -0.0029 212 TYR A O   
1466 C CB  . TYR A 205 ? 0.5918 0.3842 0.7557 -0.0344 0.0474  -0.0091 212 TYR A CB  
1467 C CG  . TYR A 205 ? 0.6566 0.4401 0.8123 -0.0464 0.0454  -0.0191 212 TYR A CG  
1468 C CD1 . TYR A 205 ? 0.7168 0.5146 0.8689 -0.0538 0.0347  -0.0216 212 TYR A CD1 
1469 C CD2 . TYR A 205 ? 0.7282 0.4889 0.8803 -0.0500 0.0534  -0.0268 212 TYR A CD2 
1470 C CE1 . TYR A 205 ? 0.6791 0.4757 0.8262 -0.0647 0.0302  -0.0323 212 TYR A CE1 
1471 C CE2 . TYR A 205 ? 0.8535 0.6091 1.0000 -0.0640 0.0509  -0.0391 212 TYR A CE2 
1472 C CZ  . TYR A 205 ? 0.7365 0.5140 0.8815 -0.0714 0.0381  -0.0422 212 TYR A CZ  
1473 O OH  . TYR A 205 ? 0.8489 0.6289 0.9903 -0.0848 0.0326  -0.0557 212 TYR A OH  
1474 N N   . SER A 206 ? 0.6246 0.4515 0.8015 -0.0371 0.0295  0.0026  213 SER A N   
1475 C CA  . SER A 206 ? 0.5524 0.3900 0.7324 -0.0398 0.0207  0.0033  213 SER A CA  
1476 C C   . SER A 206 ? 0.5464 0.3913 0.7382 -0.0397 0.0203  0.0052  213 SER A C   
1477 O O   . SER A 206 ? 0.4691 0.3206 0.6678 -0.0445 0.0171  0.0013  213 SER A O   
1478 C CB  . SER A 206 ? 0.6392 0.4812 0.8162 -0.0370 0.0180  0.0071  213 SER A CB  
1479 O OG  . SER A 206 ? 0.6006 0.4365 0.7642 -0.0390 0.0208  0.0060  213 SER A OG  
1480 N N   . PHE A 207 ? 0.5901 0.4361 0.7840 -0.0346 0.0242  0.0102  214 PHE A N   
1481 C CA  . PHE A 207 ? 0.6707 0.5210 0.8690 -0.0343 0.0269  0.0131  214 PHE A CA  
1482 C C   . PHE A 207 ? 0.7225 0.5649 0.9223 -0.0418 0.0329  0.0117  214 PHE A C   
1483 O O   . PHE A 207 ? 0.5983 0.4503 0.8059 -0.0465 0.0345  0.0098  214 PHE A O   
1484 C CB  . PHE A 207 ? 0.6909 0.5406 0.8842 -0.0267 0.0293  0.0194  214 PHE A CB  
1485 C CG  . PHE A 207 ? 0.6453 0.4961 0.8345 -0.0261 0.0330  0.0242  214 PHE A CG  
1486 C CD1 . PHE A 207 ? 0.7757 0.6404 0.9678 -0.0272 0.0312  0.0213  214 PHE A CD1 
1487 C CD2 . PHE A 207 ? 0.6778 0.5128 0.8575 -0.0242 0.0397  0.0315  214 PHE A CD2 
1488 C CE1 . PHE A 207 ? 0.6983 0.5647 0.8824 -0.0275 0.0367  0.0249  214 PHE A CE1 
1489 C CE2 . PHE A 207 ? 0.6798 0.5130 0.8496 -0.0246 0.0447  0.0379  214 PHE A CE2 
1490 C CZ  . PHE A 207 ? 0.6022 0.4530 0.7734 -0.0267 0.0435  0.0343  214 PHE A CZ  
1491 N N   . ALA A 208 ? 0.7787 0.6034 0.9723 -0.0435 0.0378  0.0112  215 ALA A N   
1492 C CA  . ALA A 208 ? 0.7130 0.5244 0.9075 -0.0541 0.0452  0.0078  215 ALA A CA  
1493 C C   . ALA A 208 ? 0.7216 0.5501 0.9287 -0.0650 0.0400  -0.0023 215 ALA A C   
1494 O O   . ALA A 208 ? 0.6799 0.5141 0.8970 -0.0749 0.0453  -0.0051 215 ALA A O   
1495 C CB  . ALA A 208 ? 0.7952 0.5820 0.9808 -0.0540 0.0505  0.0053  215 ALA A CB  
1496 N N   . VAL A 209 ? 0.6929 0.5314 0.8995 -0.0629 0.0298  -0.0075 216 VAL A N   
1497 C CA  . VAL A 209 ? 0.6827 0.5414 0.9007 -0.0693 0.0206  -0.0165 216 VAL A CA  
1498 C C   . VAL A 209 ? 0.7034 0.5848 0.9366 -0.0641 0.0163  -0.0145 216 VAL A C   
1499 O O   . VAL A 209 ? 0.6434 0.5457 0.8951 -0.0700 0.0137  -0.0218 216 VAL A O   
1500 C CB  . VAL A 209 ? 0.6521 0.5105 0.8578 -0.0676 0.0106  -0.0209 216 VAL A CB  
1501 C CG1 . VAL A 209 ? 0.6317 0.5132 0.8475 -0.0724 -0.0021 -0.0298 216 VAL A CG1 
1502 C CG2 . VAL A 209 ? 0.6719 0.5076 0.8632 -0.0731 0.0179  -0.0262 216 VAL A CG2 
1503 N N   . VAL A 210 ? 0.6865 0.5655 0.9145 -0.0538 0.0164  -0.0068 217 VAL A N   
1504 C CA  . VAL A 210 ? 0.6646 0.5594 0.9045 -0.0484 0.0156  -0.0064 217 VAL A CA  
1505 C C   . VAL A 210 ? 0.7176 0.6202 0.9676 -0.0555 0.0269  -0.0080 217 VAL A C   
1506 O O   . VAL A 210 ? 0.7236 0.6477 0.9914 -0.0549 0.0270  -0.0136 217 VAL A O   
1507 C CB  . VAL A 210 ? 0.6887 0.5762 0.9187 -0.0391 0.0150  -0.0004 217 VAL A CB  
1508 C CG1 . VAL A 210 ? 0.6641 0.5638 0.9036 -0.0344 0.0167  -0.0026 217 VAL A CG1 
1509 C CG2 . VAL A 210 ? 0.6704 0.5510 0.8920 -0.0344 0.0062  0.0013  217 VAL A CG2 
1510 N N   . LEU A 211 ? 0.5906 0.4753 0.8291 -0.0612 0.0374  -0.0029 218 LEU A N   
1511 C CA  . LEU A 211 ? 0.6765 0.5620 0.9182 -0.0703 0.0510  -0.0018 218 LEU A CA  
1512 C C   . LEU A 211 ? 0.6173 0.5199 0.8807 -0.0838 0.0533  -0.0125 218 LEU A C   
1513 O O   . LEU A 211 ? 0.6919 0.6168 0.9721 -0.0878 0.0590  -0.0174 218 LEU A O   
1514 C CB  . LEU A 211 ? 0.6531 0.5083 0.8741 -0.0726 0.0613  0.0084  218 LEU A CB  
1515 C CG  . LEU A 211 ? 0.7253 0.5684 0.9263 -0.0598 0.0606  0.0197  218 LEU A CG  
1516 C CD1 . LEU A 211 ? 0.8665 0.6786 1.0491 -0.0595 0.0693  0.0303  218 LEU A CD1 
1517 C CD2 . LEU A 211 ? 0.8015 0.6602 1.0000 -0.0567 0.0635  0.0212  218 LEU A CD2 
1518 N N   . TRP A 212 ? 0.6558 0.5503 0.9198 -0.0913 0.0491  -0.0180 219 TRP A N   
1519 C CA  . TRP A 212 ? 0.5963 0.5120 0.8830 -0.1057 0.0471  -0.0317 219 TRP A CA  
1520 C C   . TRP A 212 ? 0.5444 0.5011 0.8575 -0.0996 0.0361  -0.0399 219 TRP A C   
1521 O O   . TRP A 212 ? 0.4398 0.4247 0.7795 -0.1095 0.0418  -0.0490 219 TRP A O   
1522 C CB  . TRP A 212 ? 0.6037 0.5069 0.8818 -0.1102 0.0386  -0.0384 219 TRP A CB  
1523 C CG  . TRP A 212 ? 0.6252 0.5490 0.9240 -0.1273 0.0360  -0.0541 219 TRP A CG  
1524 C CD1 . TRP A 212 ? 0.6934 0.6040 0.9965 -0.1480 0.0491  -0.0613 219 TRP A CD1 
1525 C CD2 . TRP A 212 ? 0.6423 0.6051 0.9618 -0.1258 0.0186  -0.0657 219 TRP A CD2 
1526 N NE1 . TRP A 212 ? 0.6452 0.5880 0.9731 -0.1622 0.0412  -0.0789 219 TRP A NE1 
1527 C CE2 . TRP A 212 ? 0.6524 0.6301 0.9908 -0.1475 0.0209  -0.0817 219 TRP A CE2 
1528 C CE3 . TRP A 212 ? 0.6101 0.5951 0.9330 -0.1078 0.0008  -0.0635 219 TRP A CE3 
1529 C CZ2 . TRP A 212 ? 0.7265 0.7482 1.0900 -0.1509 0.0037  -0.0969 219 TRP A CZ2 
1530 C CZ3 . TRP A 212 ? 0.6330 0.6557 0.9771 -0.1083 -0.0159 -0.0755 219 TRP A CZ3 
1531 C CH2 . TRP A 212 ? 0.6919 0.7366 1.0574 -0.1294 -0.0157 -0.0927 219 TRP A CH2 
1532 N N   . ALA A 213 ? 0.5097 0.4688 0.8161 -0.0830 0.0215  -0.0366 220 ALA A N   
1533 C CA  . ALA A 213 ? 0.5151 0.5045 0.8417 -0.0712 0.0094  -0.0412 220 ALA A CA  
1534 C C   . ALA A 213 ? 0.5438 0.5510 0.8879 -0.0678 0.0200  -0.0428 220 ALA A C   
1535 O O   . ALA A 213 ? 0.7292 0.7711 1.1032 -0.0650 0.0162  -0.0524 220 ALA A O   
1536 C CB  . ALA A 213 ? 0.4760 0.4509 0.7838 -0.0547 -0.0037 -0.0334 220 ALA A CB  
1537 N N   . ILE A 214 ? 0.5670 0.5531 0.8926 -0.0672 0.0329  -0.0344 221 ILE A N   
1538 C CA  . ILE A 214 ? 0.5882 0.5878 0.9226 -0.0650 0.0454  -0.0363 221 ILE A CA  
1539 C C   . ILE A 214 ? 0.6235 0.6475 0.9815 -0.0812 0.0596  -0.0449 221 ILE A C   
1540 O O   . ILE A 214 ? 0.6054 0.6592 0.9871 -0.0779 0.0651  -0.0535 221 ILE A O   
1541 C CB  . ILE A 214 ? 0.6347 0.6073 0.9386 -0.0615 0.0539  -0.0256 221 ILE A CB  
1542 C CG1 . ILE A 214 ? 0.6394 0.6011 0.9321 -0.0458 0.0415  -0.0225 221 ILE A CG1 
1543 C CG2 . ILE A 214 ? 0.6534 0.6368 0.9580 -0.0649 0.0709  -0.0276 221 ILE A CG2 
1544 C CD1 . ILE A 214 ? 0.6202 0.5568 0.8842 -0.0440 0.0436  -0.0128 221 ILE A CD1 
1545 N N   . PHE A 215 ? 0.6475 0.6585 1.0004 -0.0991 0.0669  -0.0439 222 PHE A N   
1546 C CA  . PHE A 215 ? 0.6359 0.6676 1.0121 -0.1196 0.0828  -0.0528 222 PHE A CA  
1547 C C   . PHE A 215 ? 0.5817 0.6517 0.9955 -0.1274 0.0721  -0.0691 222 PHE A C   
1548 O O   . PHE A 215 ? 0.8723 0.9747 1.3169 -0.1419 0.0838  -0.0803 222 PHE A O   
1549 C CB  . PHE A 215 ? 0.7058 0.6992 1.0559 -0.1364 0.1002  -0.0429 222 PHE A CB  
1550 C CG  . PHE A 215 ? 0.7550 0.7251 1.0745 -0.1299 0.1128  -0.0287 222 PHE A CG  
1551 C CD1 . PHE A 215 ? 0.8528 0.8378 1.1768 -0.1383 0.1326  -0.0299 222 PHE A CD1 
1552 C CD2 . PHE A 215 ? 0.7304 0.6701 1.0181 -0.1146 0.1042  -0.0160 222 PHE A CD2 
1553 C CE1 . PHE A 215 ? 0.8530 0.8190 1.1442 -0.1317 0.1427  -0.0175 222 PHE A CE1 
1554 C CE2 . PHE A 215 ? 0.7400 0.6646 0.9999 -0.1076 0.1124  -0.0045 222 PHE A CE2 
1555 C CZ  . PHE A 215 ? 0.8492 0.7856 1.1081 -0.1159 0.1310  -0.0049 222 PHE A CZ  
1556 N N   . ALA A 216 ? 0.5600 0.6294 0.9712 -0.1181 0.0502  -0.0709 223 ALA A N   
1557 C CA  . ALA A 216 ? 0.5475 0.6564 0.9905 -0.1214 0.0342  -0.0860 223 ALA A CA  
1558 C C   . ALA A 216 ? 0.5835 0.7340 1.0555 -0.1004 0.0198  -0.0919 223 ALA A C   
1559 O O   . ALA A 216 ? 0.5802 0.7769 1.0897 -0.1040 0.0108  -0.1065 223 ALA A O   
1560 C CB  . ALA A 216 ? 0.6129 0.7008 1.0339 -0.1217 0.0176  -0.0853 223 ALA A CB  
1561 N N   . ASN A 217 ? 0.5592 0.6938 1.0155 -0.0785 0.0169  -0.0818 224 ASN A N   
1562 C CA  . ASN A 217 ? 0.6051 0.7675 1.0836 -0.0545 0.0025  -0.0855 224 ASN A CA  
1563 C C   . ASN A 217 ? 0.5536 0.7288 1.0354 -0.0431 -0.0251 -0.0869 224 ASN A C   
1564 O O   . ASN A 217 ? 0.5029 0.7184 1.0174 -0.0286 -0.0389 -0.0951 224 ASN A O   
1565 C CB  . ASN A 217 ? 0.6335 0.8452 1.1580 -0.0555 0.0142  -0.0998 224 ASN A CB  
1566 C CG  . ASN A 217 ? 0.7542 0.9538 1.2701 -0.0666 0.0427  -0.0980 224 ASN A CG  
1567 O OD1 . ASN A 217 ? 1.1067 1.2675 1.5881 -0.0800 0.0545  -0.0876 224 ASN A OD1 
1568 N ND2 . ASN A 217 ? 0.8095 1.0434 1.3559 -0.0598 0.0539  -0.1083 224 ASN A ND2 
1569 N N   . LYS A 218 ? 0.5502 0.6920 0.9970 -0.0486 -0.0328 -0.0790 225 LYS A N   
1570 C CA  . LYS A 218 ? 0.6175 0.7650 1.0553 -0.0407 -0.0577 -0.0790 225 LYS A CA  
1571 C C   . LYS A 218 ? 0.7229 0.8244 1.1148 -0.0464 -0.0586 -0.0688 225 LYS A C   
1572 O O   . LYS A 218 ? 0.7241 0.7949 1.0977 -0.0590 -0.0409 -0.0644 225 LYS A O   
1573 C CB  . LYS A 218 ? 0.6868 0.8823 1.1576 -0.0539 -0.0680 -0.0967 225 LYS A CB  
1574 C CG  . LYS A 218 ? 0.7250 0.9166 1.1986 -0.0855 -0.0514 -0.1067 225 LYS A CG  
1575 C CD  . LYS A 218 ? 0.8556 1.1038 1.3729 -0.1004 -0.0592 -0.1279 225 LYS A CD  
1576 C CE  . LYS A 218 ? 0.8924 1.1304 1.4077 -0.1340 -0.0460 -0.1395 225 LYS A CE  
1577 N NZ  . LYS A 218 ? 0.8672 1.1600 1.4214 -0.1504 -0.0583 -0.1624 225 LYS A NZ  
1578 N N   . GLU A 219 ? 0.7650 0.8632 1.1381 -0.0355 -0.0792 -0.0647 226 GLU A N   
1579 C CA  . GLU A 219 ? 0.8117 0.8723 1.1422 -0.0407 -0.0804 -0.0574 226 GLU A CA  
1580 C C   . GLU A 219 ? 0.7632 0.8276 1.0929 -0.0644 -0.0763 -0.0709 226 GLU A C   
1581 O O   . GLU A 219 ? 0.7741 0.8770 1.1328 -0.0740 -0.0837 -0.0860 226 GLU A O   
1582 C CB  . GLU A 219 ? 0.8313 0.8871 1.1377 -0.0235 -0.1021 -0.0489 226 GLU A CB  
1583 C CG  . GLU A 219 ? 0.8730 0.9102 1.1718 -0.0013 -0.1039 -0.0339 226 GLU A CG  
1584 C CD  . GLU A 219 ? 0.9386 0.9312 1.2100 -0.0034 -0.0870 -0.0222 226 GLU A CD  
1585 O OE1 . GLU A 219 ? 1.0412 1.0202 1.3147 0.0092  -0.0828 -0.0145 226 GLU A OE1 
1586 O OE2 . GLU A 219 ? 1.0408 1.0132 1.2902 -0.0170 -0.0779 -0.0219 226 GLU A OE2 
1587 N N   . PRO A 220 ? 0.7350 0.7606 1.0351 -0.0743 -0.0636 -0.0670 227 PRO A N   
1588 C CA  . PRO A 220 ? 0.6299 0.6510 0.9257 -0.0958 -0.0590 -0.0808 227 PRO A CA  
1589 C C   . PRO A 220 ? 0.7278 0.7609 1.0073 -0.0985 -0.0787 -0.0907 227 PRO A C   
1590 O O   . PRO A 220 ? 0.7611 0.7995 1.0238 -0.0820 -0.0960 -0.0828 227 PRO A O   
1591 C CB  . PRO A 220 ? 0.6112 0.5858 0.8795 -0.0989 -0.0407 -0.0721 227 PRO A CB  
1592 C CG  . PRO A 220 ? 0.6834 0.6430 0.9313 -0.0794 -0.0449 -0.0560 227 PRO A CG  
1593 C CD  . PRO A 220 ? 0.6567 0.6426 0.9298 -0.0668 -0.0517 -0.0520 227 PRO A CD  
1594 N N   . TYR A 221 ? 0.8072 0.8435 1.0908 -0.1203 -0.0753 -0.1084 228 TYR A N   
1595 C CA  . TYR A 221 ? 0.7852 0.8280 1.0482 -0.1285 -0.0905 -0.1223 228 TYR A CA  
1596 C C   . TYR A 221 ? 0.7868 0.8794 1.0627 -0.1204 -0.1196 -0.1292 228 TYR A C   
1597 O O   . TYR A 221 ? 0.7167 0.8103 0.9607 -0.1162 -0.1370 -0.1316 228 TYR A O   
1598 C CB  . TYR A 221 ? 0.7445 0.7469 0.9587 -0.1201 -0.0879 -0.1125 228 TYR A CB  
1599 C CG  . TYR A 221 ? 0.7812 0.7386 0.9822 -0.1230 -0.0628 -0.1054 228 TYR A CG  
1600 C CD1 . TYR A 221 ? 0.7861 0.7223 0.9888 -0.1421 -0.0470 -0.1190 228 TYR A CD1 
1601 C CD2 . TYR A 221 ? 0.7548 0.6893 0.9403 -0.1062 -0.0554 -0.0856 228 TYR A CD2 
1602 C CE1 . TYR A 221 ? 0.8294 0.7236 1.0193 -0.1405 -0.0258 -0.1112 228 TYR A CE1 
1603 C CE2 . TYR A 221 ? 0.7109 0.6104 0.8866 -0.1067 -0.0351 -0.0797 228 TYR A CE2 
1604 C CZ  . TYR A 221 ? 0.7646 0.6443 0.9423 -0.1217 -0.0211 -0.0915 228 TYR A CZ  
1605 O OH  . TYR A 221 ? 0.7022 0.5479 0.8709 -0.1178 -0.0030 -0.0842 228 TYR A OH  
1606 N N   . GLU A 222 ? 0.8999 1.0351 1.2213 -0.1176 -0.1249 -0.1330 229 GLU A N   
1607 C CA  . GLU A 222 ? 0.9938 1.1829 1.3352 -0.1055 -0.1542 -0.1392 229 GLU A CA  
1608 C C   . GLU A 222 ? 1.1337 1.3501 1.4679 -0.1213 -0.1740 -0.1612 229 GLU A C   
1609 O O   . GLU A 222 ? 1.3234 1.5642 1.6430 -0.1057 -0.2021 -0.1596 229 GLU A O   
1610 C CB  . GLU A 222 ? 1.0507 1.2858 1.4503 -0.1032 -0.1522 -0.1447 229 GLU A CB  
1611 C CG  . GLU A 222 ? 1.1374 1.3980 1.5762 -0.1346 -0.1382 -0.1675 229 GLU A CG  
1612 C CD  . GLU A 222 ? 1.0758 1.3637 1.5636 -0.1350 -0.1222 -0.1681 229 GLU A CD  
1613 O OE1 . GLU A 222 ? 0.9430 1.2816 1.4772 -0.1523 -0.1230 -0.1884 229 GLU A OE1 
1614 O OE2 . GLU A 222 ? 0.9772 1.2377 1.4572 -0.1197 -0.1079 -0.1501 229 GLU A OE2 
1615 N N   . ASN A 223 ? 1.1518 1.3606 1.4930 -0.1517 -0.1592 -0.1810 230 ASN A N   
1616 C CA  . ASN A 223 ? 1.1956 1.4288 1.5321 -0.1726 -0.1749 -0.2074 230 ASN A CA  
1617 C C   . ASN A 223 ? 1.1452 1.3398 1.4201 -0.1736 -0.1796 -0.2085 230 ASN A C   
1618 O O   . ASN A 223 ? 1.0720 1.2869 1.3370 -0.1895 -0.1947 -0.2314 230 ASN A O   
1619 C CB  . ASN A 223 ? 1.0507 1.2894 1.4226 -0.2079 -0.1552 -0.2310 230 ASN A CB  
1620 C CG  . ASN A 223 ? 1.0918 1.2671 1.4422 -0.2229 -0.1240 -0.2281 230 ASN A CG  
1621 O OD1 . ASN A 223 ? 1.0669 1.1987 1.3936 -0.2059 -0.1095 -0.2048 230 ASN A OD1 
1622 N ND2 . ASN A 223 ? 1.1158 1.2818 1.4739 -0.2551 -0.1123 -0.2520 230 ASN A ND2 
1623 N N   . ALA A 224 ? 1.1407 1.2832 1.3756 -0.1585 -0.1660 -0.1865 231 ALA A N   
1624 C CA  . ALA A 224 ? 1.1652 1.2758 1.3409 -0.1560 -0.1698 -0.1857 231 ALA A CA  
1625 C C   . ALA A 224 ? 1.2155 1.3583 1.3665 -0.1383 -0.2034 -0.1810 231 ALA A C   
1626 O O   . ALA A 224 ? 1.1225 1.2910 1.2920 -0.1162 -0.2186 -0.1650 231 ALA A O   
1627 C CB  . ALA A 224 ? 1.1116 1.1672 1.2578 -0.1436 -0.1470 -0.1632 231 ALA A CB  
1628 N N   . ILE A 225 ? 1.3131 1.4521 1.4202 -0.1468 -0.2146 -0.1948 232 ILE A N   
1629 C CA  . ILE A 225 ? 1.4424 1.6129 1.5180 -0.1327 -0.2491 -0.1929 232 ILE A CA  
1630 C C   . ILE A 225 ? 1.4166 1.5465 1.4202 -0.1190 -0.2486 -0.1749 232 ILE A C   
1631 O O   . ILE A 225 ? 1.4476 1.5969 1.4181 -0.1040 -0.2763 -0.1672 232 ILE A O   
1632 C CB  . ILE A 225 ? 1.6656 1.8851 1.7540 -0.1551 -0.2710 -0.2279 232 ILE A CB  
1633 C CG1 . ILE A 225 ? 1.6909 1.9700 1.7823 -0.1361 -0.3131 -0.2255 232 ILE A CG1 
1634 C CG2 . ILE A 225 ? 1.6794 1.8696 1.7191 -0.1770 -0.2627 -0.2500 232 ILE A CG2 
1635 C CD1 . ILE A 225 ? 1.6632 1.9853 1.8175 -0.1184 -0.3230 -0.2146 232 ILE A CD1 
1636 N N   . ALA A 226 ? 1.4033 1.4796 1.3819 -0.1242 -0.2178 -0.1688 233 ALA A N   
1637 C CA  . ALA A 226 ? 1.5073 1.5451 1.4228 -0.1125 -0.2112 -0.1504 233 ALA A CA  
1638 C C   . ALA A 226 ? 1.6273 1.6194 1.5464 -0.1084 -0.1782 -0.1333 233 ALA A C   
1639 O O   . ALA A 226 ? 1.7039 1.6864 1.6622 -0.1186 -0.1581 -0.1409 233 ALA A O   
1640 C CB  . ALA A 226 ? 1.5967 1.6252 1.4606 -0.1285 -0.2117 -0.1724 233 ALA A CB  
1641 N N   . GLU A 227 ? 1.6630 1.6273 1.5388 -0.0945 -0.1728 -0.1106 234 GLU A N   
1642 C CA  . GLU A 227 ? 1.5367 1.4626 1.4138 -0.0902 -0.1435 -0.0943 234 GLU A CA  
1643 C C   . GLU A 227 ? 1.3592 1.2588 1.2227 -0.1061 -0.1173 -0.1121 234 GLU A C   
1644 O O   . GLU A 227 ? 1.2075 1.0918 1.1038 -0.1100 -0.0960 -0.1142 234 GLU A O   
1645 C CB  . GLU A 227 ? 1.7224 1.6273 1.5574 -0.0740 -0.1446 -0.0663 234 GLU A CB  
1646 C CG  . GLU A 227 ? 1.8236 1.7415 1.6763 -0.0541 -0.1641 -0.0446 234 GLU A CG  
1647 C CD  . GLU A 227 ? 1.7733 1.6785 1.6689 -0.0480 -0.1471 -0.0319 234 GLU A CD  
1648 O OE1 . GLU A 227 ? 1.9134 1.7918 1.7917 -0.0377 -0.1387 -0.0098 234 GLU A OE1 
1649 O OE2 . GLU A 227 ? 1.5451 1.4660 1.4895 -0.0549 -0.1415 -0.0447 234 GLU A OE2 
1650 N N   . GLN A 228 ? 1.2821 1.1760 1.0953 -0.1133 -0.1195 -0.1244 235 GLN A N   
1651 C CA  . GLN A 228 ? 1.3569 1.2250 1.1515 -0.1265 -0.0944 -0.1441 235 GLN A CA  
1652 C C   . GLN A 228 ? 1.3015 1.1715 1.1339 -0.1431 -0.0877 -0.1715 235 GLN A C   
1653 O O   . GLN A 228 ? 1.1533 0.9953 0.9955 -0.1477 -0.0616 -0.1797 235 GLN A O   
1654 C CB  . GLN A 228 ? 1.4438 1.3083 1.1721 -0.1311 -0.0995 -0.1535 235 GLN A CB  
1655 C CG  . GLN A 228 ? 1.5220 1.3586 1.2254 -0.1418 -0.0712 -0.1736 235 GLN A CG  
1656 C CD  . GLN A 228 ? 1.4845 1.2943 1.1971 -0.1350 -0.0404 -0.1611 235 GLN A CD  
1657 O OE1 . GLN A 228 ? 1.4651 1.2718 1.1802 -0.1229 -0.0381 -0.1335 235 GLN A OE1 
1658 N NE2 . GLN A 228 ? 1.4879 1.2772 1.2062 -0.1421 -0.0155 -0.1818 235 GLN A NE2 
1659 N N   . GLN A 229 ? 1.2566 1.1589 1.1108 -0.1515 -0.1108 -0.1851 236 GLN A N   
1660 C CA  . GLN A 229 ? 1.2579 1.1621 1.1534 -0.1697 -0.1041 -0.2086 236 GLN A CA  
1661 C C   . GLN A 229 ? 1.1803 1.0684 1.1226 -0.1643 -0.0847 -0.1938 236 GLN A C   
1662 O O   . GLN A 229 ? 1.2952 1.1539 1.2506 -0.1731 -0.0619 -0.2044 236 GLN A O   
1663 C CB  . GLN A 229 ? 1.2688 1.2194 1.1864 -0.1798 -0.1331 -0.2236 236 GLN A CB  
1664 C CG  . GLN A 229 ? 1.3336 1.3024 1.2069 -0.1898 -0.1534 -0.2459 236 GLN A CG  
1665 C CD  . GLN A 229 ? 1.3775 1.3970 1.2829 -0.2045 -0.1805 -0.2679 236 GLN A CD  
1666 O OE1 . GLN A 229 ? 1.3435 1.3966 1.2933 -0.1968 -0.1941 -0.2564 236 GLN A OE1 
1667 N NE2 . GLN A 229 ? 1.4247 1.4526 1.3086 -0.2259 -0.1884 -0.3013 236 GLN A NE2 
1668 N N   . LEU A 230 ? 1.0619 0.9673 1.0258 -0.1488 -0.0940 -0.1693 237 LEU A N   
1669 C CA  . LEU A 230 ? 0.9401 0.8356 0.9454 -0.1427 -0.0788 -0.1542 237 LEU A CA  
1670 C C   . LEU A 230 ? 0.9659 0.8233 0.9606 -0.1342 -0.0529 -0.1422 237 LEU A C   
1671 O O   . LEU A 230 ? 0.9417 0.7805 0.9621 -0.1366 -0.0351 -0.1422 237 LEU A O   
1672 C CB  . LEU A 230 ? 0.9478 0.8710 0.9745 -0.1272 -0.0955 -0.1335 237 LEU A CB  
1673 C CG  . LEU A 230 ? 0.8958 0.8147 0.9617 -0.1194 -0.0833 -0.1176 237 LEU A CG  
1674 C CD1 . LEU A 230 ? 0.9573 0.8754 1.0594 -0.1357 -0.0711 -0.1317 237 LEU A CD1 
1675 C CD2 . LEU A 230 ? 0.8289 0.7771 0.9122 -0.1042 -0.1021 -0.1026 237 LEU A CD2 
1676 N N   . ILE A 231 ? 0.9941 0.8417 0.9515 -0.1242 -0.0510 -0.1312 238 ILE A N   
1677 C CA  . ILE A 231 ? 0.9985 0.8178 0.9466 -0.1167 -0.0271 -0.1219 238 ILE A CA  
1678 C C   . ILE A 231 ? 1.0216 0.8161 0.9700 -0.1258 -0.0071 -0.1423 238 ILE A C   
1679 O O   . ILE A 231 ? 1.0755 0.8525 1.0480 -0.1209 0.0101  -0.1375 238 ILE A O   
1680 C CB  . ILE A 231 ? 1.0954 0.9100 0.9985 -0.1095 -0.0268 -0.1107 238 ILE A CB  
1681 C CG1 . ILE A 231 ? 1.0155 0.8413 0.9229 -0.0968 -0.0397 -0.0849 238 ILE A CG1 
1682 C CG2 . ILE A 231 ? 1.1446 0.9355 1.0376 -0.1063 0.0004  -0.1100 238 ILE A CG2 
1683 C CD1 . ILE A 231 ? 0.9824 0.8054 0.8404 -0.0920 -0.0474 -0.0732 238 ILE A CD1 
1684 N N   . MET A 232 ? 1.0513 0.8434 0.9708 -0.1376 -0.0103 -0.1648 239 MET A N   
1685 C CA  . MET A 232 ? 1.1260 0.8896 1.0420 -0.1467 0.0091  -0.1883 239 MET A CA  
1686 C C   . MET A 232 ? 1.0434 0.7961 0.9995 -0.1559 0.0140  -0.1964 239 MET A C   
1687 O O   . MET A 232 ? 1.1256 0.8461 1.0915 -0.1541 0.0351  -0.2017 239 MET A O   
1688 C CB  . MET A 232 ? 1.2010 0.9649 1.0744 -0.1595 0.0037  -0.2140 239 MET A CB  
1689 C CG  . MET A 232 ? 1.2508 1.0160 1.0762 -0.1517 0.0063  -0.2072 239 MET A CG  
1690 S SD  . MET A 232 ? 1.3607 1.0953 1.1794 -0.1409 0.0419  -0.2068 239 MET A SD  
1691 C CE  . MET A 232 ? 1.4357 1.1425 1.2398 -0.1546 0.0568  -0.2465 239 MET A CE  
1692 N N   . ALA A 233 ? 1.0020 0.7810 0.9809 -0.1649 -0.0044 -0.1967 240 ALA A N   
1693 C CA  . ALA A 233 ? 0.9541 0.7267 0.9726 -0.1750 0.0011  -0.1999 240 ALA A CA  
1694 C C   . ALA A 233 ? 0.9696 0.7240 1.0112 -0.1600 0.0169  -0.1769 240 ALA A C   
1695 O O   . ALA A 233 ? 0.9858 0.7083 1.0400 -0.1629 0.0345  -0.1802 240 ALA A O   
1696 C CB  . ALA A 233 ? 0.9076 0.7223 0.9497 -0.1842 -0.0214 -0.2012 240 ALA A CB  
1697 N N   . ILE A 234 ? 0.9596 0.7324 1.0040 -0.1438 0.0102  -0.1537 241 ILE A N   
1698 C CA  . ILE A 234 ? 0.8598 0.6218 0.9232 -0.1291 0.0220  -0.1325 241 ILE A CA  
1699 C C   . ILE A 234 ? 0.8681 0.5980 0.9202 -0.1193 0.0427  -0.1331 241 ILE A C   
1700 O O   . ILE A 234 ? 0.8789 0.5884 0.9485 -0.1132 0.0555  -0.1262 241 ILE A O   
1701 C CB  . ILE A 234 ? 0.8363 0.6247 0.9040 -0.1161 0.0097  -0.1110 241 ILE A CB  
1702 C CG1 . ILE A 234 ? 0.7829 0.6019 0.8727 -0.1222 -0.0078 -0.1102 241 ILE A CG1 
1703 C CG2 . ILE A 234 ? 0.8037 0.5827 0.8870 -0.1020 0.0214  -0.0921 241 ILE A CG2 
1704 C CD1 . ILE A 234 ? 0.8486 0.6927 0.9332 -0.1107 -0.0247 -0.0960 241 ILE A CD1 
1705 N N   . LYS A 235 ? 0.8887 0.6162 0.9115 -0.1166 0.0458  -0.1407 242 LYS A N   
1706 C CA  . LYS A 235 ? 0.8394 0.5418 0.8531 -0.1069 0.0665  -0.1458 242 LYS A CA  
1707 C C   . LYS A 235 ? 0.9796 0.6461 0.9987 -0.1120 0.0810  -0.1631 242 LYS A C   
1708 O O   . LYS A 235 ? 0.9619 0.6059 0.9893 -0.0984 0.0977  -0.1604 242 LYS A O   
1709 C CB  . LYS A 235 ? 0.8388 0.5474 0.8166 -0.1066 0.0688  -0.1539 242 LYS A CB  
1710 C CG  . LYS A 235 ? 0.8733 0.6042 0.8453 -0.0972 0.0639  -0.1328 242 LYS A CG  
1711 C CD  . LYS A 235 ? 0.8816 0.6135 0.8157 -0.0974 0.0722  -0.1391 242 LYS A CD  
1712 C CE  . LYS A 235 ? 0.9884 0.7072 0.9272 -0.0875 0.0975  -0.1449 242 LYS A CE  
1713 N NZ  . LYS A 235 ? 0.9476 0.6760 0.9167 -0.0739 0.1051  -0.1261 242 LYS A NZ  
1714 N N   . SER A 236 ? 1.0293 0.6909 1.0450 -0.1314 0.0743  -0.1813 243 SER A N   
1715 C CA  . SER A 236 ? 1.0608 0.6836 1.0819 -0.1414 0.0877  -0.1988 243 SER A CA  
1716 C C   . SER A 236 ? 1.0889 0.7030 1.1400 -0.1482 0.0877  -0.1881 243 SER A C   
1717 O O   . SER A 236 ? 1.0637 0.6572 1.1196 -0.1674 0.0916  -0.2044 243 SER A O   
1718 C CB  . SER A 236 ? 1.1103 0.7330 1.1083 -0.1630 0.0817  -0.2291 243 SER A CB  
1719 O OG  . SER A 236 ? 0.9894 0.6441 0.9985 -0.1802 0.0613  -0.2314 243 SER A OG  
1720 N N   . GLY A 237 ? 1.0458 0.6766 1.1157 -0.1351 0.0838  -0.1621 244 GLY A N   
1721 C CA  . GLY A 237 ? 1.1086 0.7271 1.2019 -0.1377 0.0884  -0.1488 244 GLY A CA  
1722 C C   . GLY A 237 ? 1.0691 0.7193 1.1815 -0.1526 0.0752  -0.1449 244 GLY A C   
1723 O O   . GLY A 237 ? 1.0609 0.7045 1.1902 -0.1518 0.0807  -0.1302 244 GLY A O   
1724 N N   . ASN A 238 ? 1.1600 0.8458 1.2698 -0.1649 0.0581  -0.1575 245 ASN A N   
1725 C CA  . ASN A 238 ? 0.9806 0.7031 1.1148 -0.1778 0.0450  -0.1563 245 ASN A CA  
1726 C C   . ASN A 238 ? 0.9813 0.7305 1.1283 -0.1604 0.0377  -0.1315 245 ASN A C   
1727 O O   . ASN A 238 ? 0.8013 0.5568 0.9347 -0.1427 0.0334  -0.1201 245 ASN A O   
1728 C CB  . ASN A 238 ? 0.9758 0.7323 1.1048 -0.1926 0.0259  -0.1772 245 ASN A CB  
1729 C CG  . ASN A 238 ? 1.2238 0.9561 1.3438 -0.2155 0.0329  -0.2063 245 ASN A CG  
1730 O OD1 . ASN A 238 ? 1.3612 1.0816 1.4522 -0.2153 0.0324  -0.2212 245 ASN A OD1 
1731 N ND2 . ASN A 238 ? 1.1041 0.8258 1.2476 -0.2365 0.0421  -0.2151 245 ASN A ND2 
1732 N N   . ARG A 239 ? 0.8906 0.6539 1.0636 -0.1673 0.0385  -0.1249 246 ARG A N   
1733 C CA  . ARG A 239 ? 0.7465 0.5274 0.9327 -0.1523 0.0365  -0.1031 246 ARG A CA  
1734 C C   . ARG A 239 ? 0.7946 0.6178 1.0085 -0.1622 0.0259  -0.1066 246 ARG A C   
1735 O O   . ARG A 239 ? 0.8613 0.7000 1.0866 -0.1815 0.0209  -0.1256 246 ARG A O   
1736 C CB  . ARG A 239 ? 0.7037 0.4498 0.8910 -0.1476 0.0554  -0.0891 246 ARG A CB  
1737 C CG  . ARG A 239 ? 0.7552 0.4655 0.9218 -0.1327 0.0650  -0.0837 246 ARG A CG  
1738 C CD  . ARG A 239 ? 0.7987 0.5271 0.9585 -0.1117 0.0569  -0.0706 246 ARG A CD  
1739 N NE  . ARG A 239 ? 0.7256 0.4268 0.8722 -0.0969 0.0671  -0.0666 246 ARG A NE  
1740 C CZ  . ARG A 239 ? 0.7216 0.4136 0.8526 -0.0940 0.0693  -0.0779 246 ARG A CZ  
1741 N NH1 . ARG A 239 ? 0.7726 0.4783 0.8925 -0.1051 0.0607  -0.0935 246 ARG A NH1 
1742 N NH2 . ARG A 239 ? 0.7921 0.4634 0.9179 -0.0784 0.0802  -0.0739 246 ARG A NH2 
1743 N N   . PRO A 240 ? 0.6583 0.5028 0.8850 -0.1492 0.0222  -0.0910 247 PRO A N   
1744 C CA  . PRO A 240 ? 0.7124 0.5980 0.9691 -0.1560 0.0147  -0.0951 247 PRO A CA  
1745 C C   . PRO A 240 ? 0.7094 0.5931 0.9875 -0.1792 0.0293  -0.1045 247 PRO A C   
1746 O O   . PRO A 240 ? 0.7720 0.6158 1.0402 -0.1845 0.0485  -0.0980 247 PRO A O   
1747 C CB  . PRO A 240 ? 0.6601 0.5536 0.9208 -0.1372 0.0152  -0.0764 247 PRO A CB  
1748 C CG  . PRO A 240 ? 0.7436 0.6180 0.9773 -0.1204 0.0110  -0.0668 247 PRO A CG  
1749 C CD  . PRO A 240 ? 0.8030 0.6398 1.0188 -0.1278 0.0233  -0.0717 247 PRO A CD  
1750 N N   . ASP A 241 ? 0.7490 0.6753 1.0561 -0.1924 0.0203  -0.1192 248 ASP A N   
1751 C CA  . ASP A 241 ? 0.8011 0.7302 1.1312 -0.2203 0.0342  -0.1329 248 ASP A CA  
1752 C C   . ASP A 241 ? 0.7941 0.7234 1.1396 -0.2220 0.0526  -0.1199 248 ASP A C   
1753 O O   . ASP A 241 ? 0.8873 0.8569 1.2549 -0.2126 0.0466  -0.1165 248 ASP A O   
1754 C CB  . ASP A 241 ? 0.7473 0.7307 1.1079 -0.2349 0.0170  -0.1559 248 ASP A CB  
1755 C CG  . ASP A 241 ? 0.7950 0.7810 1.1801 -0.2694 0.0318  -0.1750 248 ASP A CG  
1756 O OD1 . ASP A 241 ? 0.8839 0.8173 1.2527 -0.2837 0.0540  -0.1728 248 ASP A OD1 
1757 O OD2 . ASP A 241 ? 0.7449 0.7864 1.1669 -0.2828 0.0209  -0.1931 248 ASP A OD2 
1758 N N   . VAL A 242 ? 0.8425 0.7238 1.1726 -0.2321 0.0755  -0.1119 249 VAL A N   
1759 C CA  . VAL A 242 ? 0.8445 0.7175 1.1791 -0.2353 0.0958  -0.0975 249 VAL A CA  
1760 C C   . VAL A 242 ? 0.9730 0.8870 1.3474 -0.2612 0.1048  -0.1123 249 VAL A C   
1761 O O   . VAL A 242 ? 0.9525 0.8846 1.3391 -0.2602 0.1159  -0.1041 249 VAL A O   
1762 C CB  . VAL A 242 ? 0.9315 0.7363 1.2333 -0.2373 0.1165  -0.0828 249 VAL A CB  
1763 C CG1 . VAL A 242 ? 0.9545 0.7467 1.2527 -0.2413 0.1377  -0.0661 249 VAL A CG1 
1764 C CG2 . VAL A 242 ? 0.9470 0.7237 1.2178 -0.2093 0.1074  -0.0691 249 VAL A CG2 
1765 N N   . ASP A 243 ? 0.9994 0.9302 1.3944 -0.2853 0.1008  -0.1357 250 ASP A N   
1766 C CA  . ASP A 243 ? 1.0931 1.0758 1.5344 -0.3110 0.1063  -0.1542 250 ASP A CA  
1767 C C   . ASP A 243 ? 1.0607 1.1181 1.5383 -0.2950 0.0856  -0.1608 250 ASP A C   
1768 O O   . ASP A 243 ? 1.0205 1.1259 1.5397 -0.3097 0.0933  -0.1719 250 ASP A O   
1769 C CB  . ASP A 243 ? 1.1209 1.1040 1.5758 -0.3427 0.1057  -0.1804 250 ASP A CB  
1770 C CG  . ASP A 243 ? 1.1454 1.0531 1.5714 -0.3628 0.1313  -0.1764 250 ASP A CG  
1771 O OD1 . ASP A 243 ? 1.0938 0.9676 1.5094 -0.3683 0.1569  -0.1590 250 ASP A OD1 
1772 O OD2 . ASP A 243 ? 1.2724 1.1527 1.6841 -0.3725 0.1260  -0.1909 250 ASP A OD2 
1773 N N   . ASP A 244 ? 1.1383 1.2042 1.6009 -0.2653 0.0610  -0.1543 251 ASP A N   
1774 C CA  . ASP A 244 ? 1.0850 1.2071 1.5730 -0.2420 0.0419  -0.1539 251 ASP A CA  
1775 C C   . ASP A 244 ? 1.1031 1.2285 1.5957 -0.2285 0.0572  -0.1384 251 ASP A C   
1776 O O   . ASP A 244 ? 1.3056 1.4798 1.8280 -0.2141 0.0476  -0.1422 251 ASP A O   
1777 C CB  . ASP A 244 ? 1.1479 1.2658 1.6101 -0.2138 0.0144  -0.1472 251 ASP A CB  
1778 C CG  . ASP A 244 ? 1.2193 1.3859 1.7018 -0.2142 -0.0134 -0.1660 251 ASP A CG  
1779 O OD1 . ASP A 244 ? 1.3807 1.6053 1.9093 -0.2232 -0.0187 -0.1820 251 ASP A OD1 
1780 O OD2 . ASP A 244 ? 1.2345 1.3834 1.6856 -0.2039 -0.0307 -0.1644 251 ASP A OD2 
1781 N N   . ILE A 245 ? 1.0460 1.1198 1.5076 -0.2313 0.0796  -0.1215 252 ILE A N   
1782 C CA  . ILE A 245 ? 0.9888 1.0637 1.4502 -0.2246 0.0976  -0.1090 252 ILE A CA  
1783 C C   . ILE A 245 ? 1.1420 1.2522 1.6421 -0.2518 0.1184  -0.1225 252 ILE A C   
1784 O O   . ILE A 245 ? 1.0630 1.1421 1.5542 -0.2784 0.1408  -0.1218 252 ILE A O   
1785 C CB  . ILE A 245 ? 0.9838 0.9936 1.3965 -0.2190 0.1129  -0.0864 252 ILE A CB  
1786 C CG1 . ILE A 245 ? 0.9210 0.9062 1.3029 -0.1919 0.0937  -0.0748 252 ILE A CG1 
1787 C CG2 . ILE A 245 ? 1.0327 1.0434 1.4403 -0.2162 0.1328  -0.0749 252 ILE A CG2 
1788 C CD1 . ILE A 245 ? 0.8682 0.7928 1.2076 -0.1881 0.1035  -0.0575 252 ILE A CD1 
1789 N N   . THR A 246 ? 1.2115 1.3855 1.7550 -0.2450 0.1117  -0.1350 253 THR A N   
1790 C CA  . THR A 246 ? 1.1691 1.3868 1.7541 -0.2661 0.1341  -0.1474 253 THR A CA  
1791 C C   . THR A 246 ? 1.1606 1.3911 1.7454 -0.2488 0.1480  -0.1383 253 THR A C   
1792 O O   . THR A 246 ? 1.0815 1.3700 1.7110 -0.2492 0.1541  -0.1523 253 THR A O   
1793 C CB  . THR A 246 ? 1.1453 1.4363 1.7895 -0.2743 0.1174  -0.1740 253 THR A CB  
1794 O OG1 . THR A 246 ? 1.1750 1.4993 1.8310 -0.2395 0.0880  -0.1747 253 THR A OG1 
1795 C CG2 . THR A 246 ? 1.0853 1.3639 1.7282 -0.2980 0.1080  -0.1866 253 THR A CG2 
1796 N N   . GLU A 247 ? 1.2603 1.4388 1.7954 -0.2323 0.1517  -0.1167 254 GLU A N   
1797 C CA  . GLU A 247 ? 1.2943 1.4645 1.8116 -0.2252 0.1723  -0.1058 254 GLU A CA  
1798 C C   . GLU A 247 ? 1.2456 1.3498 1.7114 -0.2389 0.1923  -0.0857 254 GLU A C   
1799 O O   . GLU A 247 ? 1.2486 1.3109 1.6922 -0.2460 0.1865  -0.0795 254 GLU A O   
1800 C CB  . GLU A 247 ? 1.3817 1.5502 1.8840 -0.1898 0.1531  -0.0987 254 GLU A CB  
1801 C CG  . GLU A 247 ? 1.4190 1.5805 1.9002 -0.1783 0.1692  -0.0904 254 GLU A CG  
1802 C CD  . GLU A 247 ? 1.3021 1.4544 1.7669 -0.1467 0.1487  -0.0850 254 GLU A CD  
1803 O OE1 . GLU A 247 ? 1.1627 1.3459 1.6576 -0.1301 0.1284  -0.0954 254 GLU A OE1 
1804 O OE2 . GLU A 247 ? 1.0987 1.2119 1.5199 -0.1384 0.1522  -0.0702 254 GLU A OE2 
1805 N N   . TYR A 248 ? 1.2332 1.3255 1.6769 -0.2412 0.2160  -0.0752 255 TYR A N   
1806 C CA  . TYR A 248 ? 1.1672 1.1939 1.5539 -0.2453 0.2302  -0.0515 255 TYR A CA  
1807 C C   . TYR A 248 ? 1.0031 0.9966 1.3526 -0.2156 0.2074  -0.0370 255 TYR A C   
1808 O O   . TYR A 248 ? 0.8970 0.8996 1.2342 -0.1955 0.2027  -0.0333 255 TYR A O   
1809 C CB  . TYR A 248 ? 1.2639 1.2867 1.6302 -0.2555 0.2610  -0.0428 255 TYR A CB  
1810 C CG  . TYR A 248 ? 1.3419 1.2959 1.6459 -0.2580 0.2740  -0.0160 255 TYR A CG  
1811 C CD1 . TYR A 248 ? 1.4749 1.3814 1.7636 -0.2789 0.2846  -0.0073 255 TYR A CD1 
1812 C CD2 . TYR A 248 ? 1.4325 1.3679 1.6919 -0.2387 0.2751  0.0002  255 TYR A CD2 
1813 C CE1 . TYR A 248 ? 1.5949 1.4357 1.8261 -0.2771 0.2953  0.0192  255 TYR A CE1 
1814 C CE2 . TYR A 248 ? 1.4319 1.3078 1.6338 -0.2377 0.2838  0.0259  255 TYR A CE2 
1815 C CZ  . TYR A 248 ? 1.5794 1.4071 1.7673 -0.2553 0.2938  0.0366  255 TYR A CZ  
1816 O OH  . TYR A 248 ? 1.6959 1.4621 1.8264 -0.2504 0.3014  0.0639  255 TYR A OH  
1817 N N   . CYS A 249 ? 0.8915 0.8493 1.2265 -0.2146 0.1942  -0.0316 256 CYS A N   
1818 C CA  . CYS A 249 ? 0.8676 0.7813 1.1602 -0.1939 0.1821  -0.0138 256 CYS A CA  
1819 C C   . CYS A 249 ? 0.8849 0.7442 1.1376 -0.2050 0.2023  0.0053  256 CYS A C   
1820 O O   . CYS A 249 ? 1.0749 0.9129 1.3326 -0.2270 0.2143  0.0028  256 CYS A O   
1821 C CB  . CYS A 249 ? 0.7674 0.6715 1.0648 -0.1853 0.1591  -0.0186 256 CYS A CB  
1822 S SG  . CYS A 249 ? 0.7682 0.6330 1.0234 -0.1578 0.1444  -0.0001 256 CYS A SG  
1823 N N   . PRO A 250 ? 0.9158 0.7511 1.1278 -0.1901 0.2057  0.0242  257 PRO A N   
1824 C CA  . PRO A 250 ? 0.9661 0.7443 1.1338 -0.1946 0.2210  0.0465  257 PRO A CA  
1825 C C   . PRO A 250 ? 0.9275 0.6603 1.0853 -0.1928 0.2137  0.0520  257 PRO A C   
1826 O O   . PRO A 250 ? 0.7912 0.5355 0.9660 -0.1807 0.1923  0.0419  257 PRO A O   
1827 C CB  . PRO A 250 ? 1.0719 0.8436 1.2021 -0.1701 0.2131  0.0622  257 PRO A CB  
1828 C CG  . PRO A 250 ? 0.9222 0.7473 1.0757 -0.1646 0.2085  0.0469  257 PRO A CG  
1829 C CD  . PRO A 250 ? 0.8474 0.7092 1.0521 -0.1703 0.1978  0.0246  257 PRO A CD  
1830 N N   . ARG A 251 ? 1.0380 0.7174 1.1665 -0.2045 0.2328  0.0679  258 ARG A N   
1831 C CA  . ARG A 251 ? 1.0947 0.7214 1.2096 -0.2015 0.2297  0.0741  258 ARG A CA  
1832 C C   . ARG A 251 ? 0.9770 0.5926 1.0735 -0.1681 0.2067  0.0838  258 ARG A C   
1833 O O   . ARG A 251 ? 0.9152 0.5221 1.0231 -0.1614 0.1943  0.0752  258 ARG A O   
1834 C CB  . ARG A 251 ? 1.2395 0.8020 1.3188 -0.2155 0.2552  0.0940  258 ARG A CB  
1835 C CG  . ARG A 251 ? 1.3957 0.9593 1.4935 -0.2539 0.2820  0.0840  258 ARG A CG  
1836 C CD  . ARG A 251 ? 1.5407 1.0266 1.6054 -0.2696 0.3059  0.1013  258 ARG A CD  
1837 N NE  . ARG A 251 ? 1.6134 1.0541 1.6218 -0.2558 0.3173  0.1344  258 ARG A NE  
1838 C CZ  . ARG A 251 ? 1.6148 1.0099 1.5829 -0.2249 0.3056  0.1578  258 ARG A CZ  
1839 N NH1 . ARG A 251 ? 1.6601 1.0468 1.6377 -0.2023 0.2834  0.1521  258 ARG A NH1 
1840 N NH2 . ARG A 251 ? 1.5781 0.9375 1.4943 -0.2153 0.3165  0.1876  258 ARG A NH2 
1841 N N   . GLU A 252 ? 1.0173 0.6383 1.0871 -0.1487 0.2015  0.0994  259 GLU A N   
1842 C CA  . GLU A 252 ? 1.1208 0.7307 1.1717 -0.1181 0.1819  0.1107  259 GLU A CA  
1843 C C   . GLU A 252 ? 0.9526 0.6088 1.0333 -0.1055 0.1588  0.0931  259 GLU A C   
1844 O O   . GLU A 252 ? 1.0438 0.6924 1.1217 -0.0864 0.1442  0.0956  259 GLU A O   
1845 C CB  . GLU A 252 ? 1.1981 0.7896 1.2040 -0.1013 0.1832  0.1355  259 GLU A CB  
1846 C CG  . GLU A 252 ? 1.3069 0.9256 1.2992 -0.1086 0.1926  0.1380  259 GLU A CG  
1847 C CD  . GLU A 252 ? 1.4348 1.0254 1.4084 -0.1335 0.2222  0.1476  259 GLU A CD  
1848 O OE1 . GLU A 252 ? 1.4159 1.0204 1.4227 -0.1589 0.2354  0.1307  259 GLU A OE1 
1849 O OE2 . GLU A 252 ? 1.4292 0.9861 1.3554 -0.1285 0.2322  0.1715  259 GLU A OE2 
1850 N N   . ILE A 253 ? 1.0994 0.8018 1.2086 -0.1155 0.1565  0.0761  260 ILE A N   
1851 C CA  . ILE A 253 ? 1.0069 0.7467 1.1443 -0.1067 0.1367  0.0597  260 ILE A CA  
1852 C C   . ILE A 253 ? 0.9851 0.7176 1.1432 -0.1147 0.1322  0.0467  260 ILE A C   
1853 O O   . ILE A 253 ? 0.7660 0.5069 0.9310 -0.1022 0.1164  0.0411  260 ILE A O   
1854 C CB  . ILE A 253 ? 0.9685 0.7558 1.1282 -0.1114 0.1356  0.0469  260 ILE A CB  
1855 C CG1 . ILE A 253 ? 0.9350 0.7298 1.0707 -0.0987 0.1352  0.0565  260 ILE A CG1 
1856 C CG2 . ILE A 253 ? 0.9510 0.7698 1.1394 -0.1046 0.1170  0.0311  260 ILE A CG2 
1857 C CD1 . ILE A 253 ? 0.9015 0.7339 1.0515 -0.1040 0.1412  0.0455  260 ILE A CD1 
1858 N N   . ILE A 254 ? 0.9428 0.6609 1.1097 -0.1372 0.1467  0.0407  261 ILE A N   
1859 C CA  . ILE A 254 ? 0.9191 0.6231 1.0990 -0.1470 0.1441  0.0276  261 ILE A CA  
1860 C C   . ILE A 254 ? 0.9213 0.5780 1.0763 -0.1315 0.1425  0.0384  261 ILE A C   
1861 O O   . ILE A 254 ? 0.8560 0.5132 1.0173 -0.1242 0.1312  0.0287  261 ILE A O   
1862 C CB  . ILE A 254 ? 0.9813 0.6778 1.1760 -0.1780 0.1617  0.0171  261 ILE A CB  
1863 C CG1 . ILE A 254 ? 0.8576 0.6099 1.0858 -0.1922 0.1624  0.0027  261 ILE A CG1 
1864 C CG2 . ILE A 254 ? 0.9914 0.6700 1.1950 -0.1885 0.1583  0.0014  261 ILE A CG2 
1865 C CD1 . ILE A 254 ? 0.8951 0.6487 1.1392 -0.2228 0.1834  -0.0050 261 ILE A CD1 
1866 N N   . SER A 255 ? 1.0112 0.6282 1.1372 -0.1252 0.1542  0.0587  262 SER A N   
1867 C CA  . SER A 255 ? 1.0050 0.5807 1.1084 -0.1038 0.1514  0.0716  262 SER A CA  
1868 C C   . SER A 255 ? 0.9339 0.5380 1.0406 -0.0780 0.1311  0.0719  262 SER A C   
1869 O O   . SER A 255 ? 0.9369 0.5269 1.0441 -0.0649 0.1252  0.0688  262 SER A O   
1870 C CB  . SER A 255 ? 1.0521 0.5848 1.1211 -0.0979 0.1647  0.0966  262 SER A CB  
1871 O OG  . SER A 255 ? 1.2577 0.7531 1.3211 -0.1235 0.1868  0.0973  262 SER A OG  
1872 N N   . LEU A 256 ? 0.9230 0.5669 1.0330 -0.0725 0.1224  0.0737  263 LEU A N   
1873 C CA  . LEU A 256 ? 0.9638 0.6373 1.0795 -0.0528 0.1045  0.0720  263 LEU A CA  
1874 C C   . LEU A 256 ? 0.9666 0.6620 1.1058 -0.0559 0.0948  0.0535  263 LEU A C   
1875 O O   . LEU A 256 ? 0.9655 0.6633 1.1060 -0.0412 0.0860  0.0523  263 LEU A O   
1876 C CB  . LEU A 256 ? 0.8844 0.5909 0.9967 -0.0494 0.0994  0.0757  263 LEU A CB  
1877 C CG  . LEU A 256 ? 0.8206 0.5589 0.9395 -0.0336 0.0825  0.0724  263 LEU A CG  
1878 C CD1 . LEU A 256 ? 0.8320 0.5576 0.9406 -0.0130 0.0751  0.0819  263 LEU A CD1 
1879 C CD2 . LEU A 256 ? 0.8135 0.5762 0.9248 -0.0334 0.0811  0.0745  263 LEU A CD2 
1880 N N   . MET A 257 ? 0.9455 0.6582 1.1025 -0.0743 0.0963  0.0395  264 MET A N   
1881 C CA  . MET A 257 ? 1.0167 0.7501 1.1903 -0.0767 0.0854  0.0236  264 MET A CA  
1882 C C   . MET A 257 ? 0.9361 0.6407 1.1055 -0.0787 0.0885  0.0163  264 MET A C   
1883 O O   . MET A 257 ? 1.1596 0.8723 1.3309 -0.0713 0.0801  0.0093  264 MET A O   
1884 C CB  . MET A 257 ? 0.9435 0.7099 1.1383 -0.0918 0.0822  0.0110  264 MET A CB  
1885 C CG  . MET A 257 ? 1.0034 0.7627 1.2084 -0.1142 0.0930  0.0018  264 MET A CG  
1886 S SD  . MET A 257 ? 0.8932 0.7034 1.1305 -0.1270 0.0845  -0.0153 264 MET A SD  
1887 C CE  . MET A 257 ? 0.7961 0.6271 1.0371 -0.1231 0.0919  -0.0060 264 MET A CE  
1888 N N   . LYS A 258 ? 0.9949 0.6642 1.1573 -0.0898 0.1023  0.0172  265 LYS A N   
1889 C CA  . LYS A 258 ? 0.9171 0.5494 1.0721 -0.0903 0.1083  0.0102  265 LYS A CA  
1890 C C   . LYS A 258 ? 0.8484 0.4616 0.9910 -0.0649 0.1067  0.0201  265 LYS A C   
1891 O O   . LYS A 258 ? 0.8418 0.4457 0.9843 -0.0596 0.1058  0.0096  265 LYS A O   
1892 C CB  . LYS A 258 ? 0.9676 0.5591 1.1164 -0.1084 0.1258  0.0105  265 LYS A CB  
1893 C CG  . LYS A 258 ? 0.9292 0.5413 1.0969 -0.1370 0.1280  -0.0067 265 LYS A CG  
1894 C CD  . LYS A 258 ? 0.8665 0.4399 1.0288 -0.1578 0.1486  -0.0036 265 LYS A CD  
1895 C CE  . LYS A 258 ? 0.8761 0.4721 1.0624 -0.1891 0.1517  -0.0248 265 LYS A CE  
1896 N NZ  . LYS A 258 ? 0.9470 0.4929 1.1266 -0.2126 0.1738  -0.0267 265 LYS A NZ  
1897 N N   . LEU A 259 ? 0.8245 0.4348 0.9570 -0.0492 0.1063  0.0390  266 LEU A N   
1898 C CA  . LEU A 259 ? 0.8754 0.4821 1.0024 -0.0227 0.1009  0.0484  266 LEU A CA  
1899 C C   . LEU A 259 ? 0.9064 0.5559 1.0477 -0.0152 0.0877  0.0390  266 LEU A C   
1900 O O   . LEU A 259 ? 1.0047 0.6523 1.1495 -0.0024 0.0868  0.0341  266 LEU A O   
1901 C CB  . LEU A 259 ? 0.9213 0.5247 1.0335 -0.0093 0.0997  0.0698  266 LEU A CB  
1902 C CG  . LEU A 259 ? 0.9377 0.5335 1.0432 0.0198  0.0940  0.0822  266 LEU A CG  
1903 C CD1 . LEU A 259 ? 1.0208 0.5603 1.1142 0.0284  0.1060  0.0875  266 LEU A CD1 
1904 C CD2 . LEU A 259 ? 0.8618 0.4718 0.9529 0.0308  0.0869  0.1002  266 LEU A CD2 
1905 N N   . CYS A 260 ? 0.8448 0.5305 0.9943 -0.0236 0.0796  0.0366  267 CYS A N   
1906 C CA  . CYS A 260 ? 0.7416 0.4622 0.9017 -0.0190 0.0687  0.0299  267 CYS A CA  
1907 C C   . CYS A 260 ? 0.7018 0.4265 0.8667 -0.0280 0.0677  0.0140  267 CYS A C   
1908 O O   . CYS A 260 ? 0.6934 0.4345 0.8616 -0.0210 0.0632  0.0102  267 CYS A O   
1909 C CB  . CYS A 260 ? 0.8546 0.6056 1.0197 -0.0233 0.0612  0.0328  267 CYS A CB  
1910 S SG  . CYS A 260 ? 0.8655 0.6212 1.0204 -0.0102 0.0591  0.0490  267 CYS A SG  
1911 N N   . TRP A 261 ? 0.7959 0.5065 0.9596 -0.0442 0.0722  0.0043  268 TRP A N   
1912 C CA  . TRP A 261 ? 0.7138 0.4251 0.8762 -0.0528 0.0707  -0.0121 268 TRP A CA  
1913 C C   . TRP A 261 ? 0.7458 0.4229 0.8993 -0.0513 0.0812  -0.0210 268 TRP A C   
1914 O O   . TRP A 261 ? 0.7116 0.3840 0.8603 -0.0634 0.0816  -0.0371 268 TRP A O   
1915 C CB  . TRP A 261 ? 0.6738 0.4024 0.8428 -0.0715 0.0646  -0.0219 268 TRP A CB  
1916 C CG  . TRP A 261 ? 0.6860 0.3995 0.8594 -0.0892 0.0720  -0.0279 268 TRP A CG  
1917 C CD1 . TRP A 261 ? 0.7526 0.4273 0.9190 -0.0968 0.0848  -0.0332 268 TRP A CD1 
1918 C CD2 . TRP A 261 ? 0.6404 0.3782 0.8287 -0.1038 0.0681  -0.0319 268 TRP A CD2 
1919 N NE1 . TRP A 261 ? 0.7678 0.4415 0.9434 -0.1174 0.0896  -0.0395 268 TRP A NE1 
1920 C CE2 . TRP A 261 ? 0.7121 0.4277 0.9031 -0.1219 0.0795  -0.0393 268 TRP A CE2 
1921 C CE3 . TRP A 261 ? 0.6787 0.4546 0.8801 -0.1028 0.0570  -0.0307 268 TRP A CE3 
1922 C CZ2 . TRP A 261 ? 0.7281 0.4644 0.9375 -0.1407 0.0806  -0.0461 268 TRP A CZ2 
1923 C CZ3 . TRP A 261 ? 0.6485 0.4451 0.8687 -0.1178 0.0573  -0.0372 268 TRP A CZ3 
1924 C CH2 . TRP A 261 ? 0.7227 0.5027 0.9482 -0.1374 0.0691  -0.0455 268 TRP A CH2 
1925 N N   . GLU A 262 ? 0.8119 0.4652 0.9622 -0.0352 0.0889  -0.0116 269 GLU A N   
1926 C CA  . GLU A 262 ? 0.7605 0.3815 0.9042 -0.0272 0.0993  -0.0202 269 GLU A CA  
1927 C C   . GLU A 262 ? 0.7868 0.4270 0.9294 -0.0256 0.0974  -0.0345 269 GLU A C   
1928 O O   . GLU A 262 ? 0.8686 0.5426 1.0169 -0.0194 0.0898  -0.0301 269 GLU A O   
1929 C CB  . GLU A 262 ? 0.8774 0.4817 1.0219 -0.0027 0.1036  -0.0054 269 GLU A CB  
1930 C CG  . GLU A 262 ? 1.0203 0.5883 1.1561 -0.0020 0.1101  0.0092  269 GLU A CG  
1931 C CD  . GLU A 262 ? 1.1145 0.6308 1.2404 -0.0131 0.1243  -0.0001 269 GLU A CD  
1932 O OE1 . GLU A 262 ? 1.2557 0.7485 1.3747 -0.0275 0.1305  0.0068  269 GLU A OE1 
1933 O OE2 . GLU A 262 ? 1.3108 0.8082 1.4353 -0.0087 0.1311  -0.0150 269 GLU A OE2 
1934 N N   . ALA A 263 ? 0.8602 0.4769 0.9933 -0.0329 0.1055  -0.0521 270 ALA A N   
1935 C CA  . ALA A 263 ? 0.8973 0.5259 1.0226 -0.0320 0.1073  -0.0674 270 ALA A CA  
1936 C C   . ALA A 263 ? 0.9548 0.5969 1.0886 -0.0095 0.1120  -0.0622 270 ALA A C   
1937 O O   . ALA A 263 ? 0.9966 0.6687 1.1293 -0.0094 0.1094  -0.0650 270 ALA A O   
1938 C CB  . ALA A 263 ? 0.8937 0.4874 1.0054 -0.0417 0.1179  -0.0887 270 ALA A CB  
1939 N N   . ASN A 264 ? 0.9401 0.5600 1.0823 0.0093  0.1191  -0.0542 271 ASN A N   
1940 C CA  . ASN A 264 ? 0.9077 0.5438 1.0647 0.0334  0.1224  -0.0494 271 ASN A CA  
1941 C C   . ASN A 264 ? 0.9137 0.5867 1.0845 0.0396  0.1097  -0.0314 271 ASN A C   
1942 O O   . ASN A 264 ? 0.9104 0.5735 1.0807 0.0413  0.1038  -0.0168 271 ASN A O   
1943 C CB  . ASN A 264 ? 1.0353 0.6308 1.1951 0.0535  0.1325  -0.0469 271 ASN A CB  
1944 C CG  . ASN A 264 ? 0.9403 0.5531 1.1189 0.0813  0.1374  -0.0473 271 ASN A CG  
1945 O OD1 . ASN A 264 ? 0.8839 0.5427 1.0769 0.0850  0.1331  -0.0469 271 ASN A OD1 
1946 N ND2 . ASN A 264 ? 0.9071 0.4814 1.0872 0.1011  0.1477  -0.0489 271 ASN A ND2 
1947 N N   . PRO A 265 ? 0.8443 0.5581 1.0256 0.0413  0.1070  -0.0333 272 PRO A N   
1948 C CA  . PRO A 265 ? 0.7734 0.5225 0.9690 0.0457  0.0954  -0.0195 272 PRO A CA  
1949 C C   . PRO A 265 ? 0.8527 0.6016 1.0611 0.0680  0.0913  -0.0064 272 PRO A C   
1950 O O   . PRO A 265 ? 0.7786 0.5358 0.9863 0.0672  0.0808  0.0066  272 PRO A O   
1951 C CB  . PRO A 265 ? 0.7793 0.5647 0.9858 0.0447  0.0989  -0.0274 272 PRO A CB  
1952 C CG  . PRO A 265 ? 0.8912 0.6618 1.0810 0.0342  0.1098  -0.0430 272 PRO A CG  
1953 C CD  . PRO A 265 ? 0.8351 0.5627 1.0128 0.0364  0.1158  -0.0489 272 PRO A CD  
1954 N N   . GLU A 266 ? 0.9620 0.7009 1.1803 0.0890  0.0995  -0.0102 273 GLU A N   
1955 C CA  . GLU A 266 ? 0.9561 0.6923 1.1850 0.1155  0.0945  0.0032  273 GLU A CA  
1956 C C   . GLU A 266 ? 0.9632 0.6578 1.1716 0.1160  0.0910  0.0194  273 GLU A C   
1957 O O   . GLU A 266 ? 1.0252 0.7269 1.2349 0.1314  0.0810  0.0355  273 GLU A O   
1958 C CB  . GLU A 266 ? 1.1053 0.8325 1.3488 0.1401  0.1058  -0.0057 273 GLU A CB  
1959 C CG  . GLU A 266 ? 1.1131 0.8893 1.3833 0.1452  0.1108  -0.0197 273 GLU A CG  
1960 C CD  . GLU A 266 ? 1.1885 1.0038 1.4899 0.1733  0.1024  -0.0131 273 GLU A CD  
1961 O OE1 . GLU A 266 ? 1.1350 0.9717 1.4389 0.1747  0.0859  0.0012  273 GLU A OE1 
1962 O OE2 . GLU A 266 ? 1.2696 1.0965 1.5938 0.1946  0.1119  -0.0234 273 GLU A OE2 
1963 N N   . ALA A 267 ? 0.8998 0.5540 1.0887 0.0979  0.0991  0.0146  274 ALA A N   
1964 C CA  . ALA A 267 ? 0.8529 0.4694 1.0224 0.0909  0.0990  0.0285  274 ALA A CA  
1965 C C   . ALA A 267 ? 0.8195 0.4617 0.9842 0.0763  0.0878  0.0391  274 ALA A C   
1966 O O   . ALA A 267 ? 0.7777 0.3976 0.9276 0.0750  0.0875  0.0537  274 ALA A O   
1967 C CB  . ALA A 267 ? 0.8862 0.4581 1.0413 0.0718  0.1118  0.0163  274 ALA A CB  
1968 N N   . ARG A 268 ? 0.8424 0.5279 1.0176 0.0652  0.0805  0.0315  275 ARG A N   
1969 C CA  . ARG A 268 ? 0.7959 0.5043 0.9680 0.0522  0.0711  0.0382  275 ARG A CA  
1970 C C   . ARG A 268 ? 0.7519 0.4843 0.9279 0.0693  0.0604  0.0516  275 ARG A C   
1971 O O   . ARG A 268 ? 0.7549 0.5075 0.9457 0.0871  0.0570  0.0505  275 ARG A O   
1972 C CB  . ARG A 268 ? 0.7952 0.5344 0.9751 0.0360  0.0674  0.0259  275 ARG A CB  
1973 C CG  . ARG A 268 ? 0.7880 0.5093 0.9608 0.0190  0.0743  0.0125  275 ARG A CG  
1974 C CD  . ARG A 268 ? 0.8221 0.5716 0.9987 0.0089  0.0702  0.0028  275 ARG A CD  
1975 N NE  . ARG A 268 ? 0.8774 0.6130 1.0450 -0.0010 0.0764  -0.0115 275 ARG A NE  
1976 C CZ  . ARG A 268 ? 0.9215 0.6734 1.0851 -0.0079 0.0758  -0.0202 275 ARG A CZ  
1977 N NH1 . ARG A 268 ? 0.9955 0.7757 1.1652 -0.0073 0.0707  -0.0160 275 ARG A NH1 
1978 N NH2 . ARG A 268 ? 0.9515 0.6887 1.1018 -0.0165 0.0809  -0.0336 275 ARG A NH2 
1979 N N   . PRO A 269 ? 0.8239 0.5584 0.9876 0.0634  0.0551  0.0626  276 PRO A N   
1980 C CA  . PRO A 269 ? 0.8320 0.5942 0.9960 0.0770  0.0429  0.0726  276 PRO A CA  
1981 C C   . PRO A 269 ? 0.7568 0.5655 0.9393 0.0702  0.0344  0.0616  276 PRO A C   
1982 O O   . PRO A 269 ? 0.6875 0.5020 0.8780 0.0557  0.0385  0.0496  276 PRO A O   
1983 C CB  . PRO A 269 ? 0.8356 0.5827 0.9766 0.0676  0.0436  0.0842  276 PRO A CB  
1984 C CG  . PRO A 269 ? 0.8037 0.5401 0.9454 0.0438  0.0524  0.0743  276 PRO A CG  
1985 C CD  . PRO A 269 ? 0.8119 0.5340 0.9642 0.0417  0.0594  0.0623  276 PRO A CD  
1986 N N   . THR A 270 ? 0.7983 0.6379 0.9854 0.0807  0.0225  0.0658  277 THR A N   
1987 C CA  . THR A 270 ? 0.6913 0.5722 0.8937 0.0713  0.0147  0.0554  277 THR A CA  
1988 C C   . THR A 270 ? 0.7199 0.6019 0.9059 0.0586  0.0110  0.0580  277 THR A C   
1989 O O   . THR A 270 ? 0.7619 0.6183 0.9260 0.0588  0.0145  0.0687  277 THR A O   
1990 C CB  . THR A 270 ? 0.6453 0.5648 0.8652 0.0883  0.0030  0.0549  277 THR A CB  
1991 O OG1 . THR A 270 ? 0.6558 0.5715 0.8576 0.1041  -0.0066 0.0694  277 THR A OG1 
1992 C CG2 . THR A 270 ? 0.6692 0.5938 0.9105 0.1028  0.0080  0.0503  277 THR A CG2 
1993 N N   . PHE A 271 ? 0.6618 0.5715 0.8576 0.0473  0.0058  0.0479  278 PHE A N   
1994 C CA  . PHE A 271 ? 0.6776 0.5895 0.8594 0.0367  0.0033  0.0473  278 PHE A CA  
1995 C C   . PHE A 271 ? 0.6938 0.6170 0.8586 0.0468  -0.0061 0.0553  278 PHE A C   
1996 O O   . PHE A 271 ? 0.9054 0.8170 1.0494 0.0413  -0.0032 0.0597  278 PHE A O   
1997 C CB  . PHE A 271 ? 0.7755 0.7047 0.9704 0.0217  0.0022  0.0337  278 PHE A CB  
1998 C CG  . PHE A 271 ? 0.7692 0.6790 0.9661 0.0098  0.0108  0.0298  278 PHE A CG  
1999 C CD1 . PHE A 271 ? 0.7450 0.6383 0.9305 0.0030  0.0153  0.0317  278 PHE A CD1 
2000 C CD2 . PHE A 271 ? 0.7397 0.6501 0.9493 0.0057  0.0146  0.0240  278 PHE A CD2 
2001 C CE1 . PHE A 271 ? 0.7559 0.6370 0.9454 -0.0061 0.0202  0.0276  278 PHE A CE1 
2002 C CE2 . PHE A 271 ? 0.6961 0.5898 0.9031 -0.0037 0.0199  0.0213  278 PHE A CE2 
2003 C CZ  . PHE A 271 ? 0.6848 0.5653 0.8830 -0.0088 0.0212  0.0230  278 PHE A CZ  
2004 N N   . PRO A 272 ? 0.7128 0.6617 0.8862 0.0615  -0.0175 0.0565  279 PRO A N   
2005 C CA  . PRO A 272 ? 0.7427 0.6990 0.8940 0.0754  -0.0284 0.0676  279 PRO A CA  
2006 C C   . PRO A 272 ? 0.7998 0.7162 0.9240 0.0871  -0.0219 0.0874  279 PRO A C   
2007 O O   . PRO A 272 ? 0.7791 0.6858 0.8723 0.0886  -0.0233 0.0978  279 PRO A O   
2008 C CB  . PRO A 272 ? 0.7733 0.7687 0.9474 0.0906  -0.0425 0.0635  279 PRO A CB  
2009 C CG  . PRO A 272 ? 0.7088 0.7265 0.9145 0.0748  -0.0390 0.0450  279 PRO A CG  
2010 C CD  . PRO A 272 ? 0.6994 0.6816 0.9038 0.0620  -0.0224 0.0443  279 PRO A CD  
2011 N N   . GLY A 273 ? 0.8855 0.7768 1.0195 0.0939  -0.0133 0.0916  280 GLY A N   
2012 C CA  . GLY A 273 ? 0.9082 0.7515 1.0187 0.1000  -0.0027 0.1081  280 GLY A CA  
2013 C C   . GLY A 273 ? 0.7893 0.6052 0.8816 0.0792  0.0113  0.1094  280 GLY A C   
2014 O O   . GLY A 273 ? 0.8320 0.6163 0.8953 0.0811  0.0181  0.1251  280 GLY A O   
2015 N N   . ILE A 274 ? 0.8192 0.6468 0.9289 0.0599  0.0160  0.0936  281 ILE A N   
2016 C CA  . ILE A 274 ? 0.8060 0.6200 0.9064 0.0405  0.0274  0.0912  281 ILE A CA  
2017 C C   . ILE A 274 ? 0.8108 0.6376 0.8887 0.0388  0.0244  0.0954  281 ILE A C   
2018 O O   . ILE A 274 ? 0.9448 0.7492 0.9989 0.0338  0.0347  0.1059  281 ILE A O   
2019 C CB  . ILE A 274 ? 0.7757 0.6026 0.9005 0.0246  0.0300  0.0739  281 ILE A CB  
2020 C CG1 . ILE A 274 ? 0.7610 0.5674 0.8977 0.0231  0.0365  0.0707  281 ILE A CG1 
2021 C CG2 . ILE A 274 ? 0.9395 0.7652 1.0603 0.0081  0.0381  0.0694  281 ILE A CG2 
2022 C CD1 . ILE A 274 ? 0.7710 0.5919 0.9281 0.0130  0.0353  0.0560  281 ILE A CD1 
2023 N N   . GLU A 275 ? 0.8494 0.7113 0.9339 0.0413  0.0116  0.0862  282 GLU A N   
2024 C CA  . GLU A 275 ? 0.8288 0.7069 0.8911 0.0393  0.0075  0.0857  282 GLU A CA  
2025 C C   . GLU A 275 ? 0.9008 0.7630 0.9245 0.0516  0.0064  0.1057  282 GLU A C   
2026 O O   . GLU A 275 ? 0.8006 0.6557 0.7969 0.0441  0.0145  0.1098  282 GLU A O   
2027 C CB  . GLU A 275 ? 0.8737 0.7907 0.9502 0.0408  -0.0078 0.0712  282 GLU A CB  
2028 C CG  . GLU A 275 ? 0.9172 0.8500 0.9754 0.0326  -0.0093 0.0624  282 GLU A CG  
2029 C CD  . GLU A 275 ? 0.8883 0.8557 0.9618 0.0293  -0.0224 0.0443  282 GLU A CD  
2030 O OE1 . GLU A 275 ? 0.9078 0.8836 0.9706 0.0199  -0.0207 0.0325  282 GLU A OE1 
2031 O OE2 . GLU A 275 ? 0.9669 0.9532 1.0632 0.0350  -0.0328 0.0406  282 GLU A OE2 
2032 N N   . GLU A 276 ? 0.9775 0.8345 0.9986 0.0714  -0.0031 0.1181  283 GLU A N   
2033 C CA  . GLU A 276 ? 1.0533 0.8897 1.0352 0.0882  -0.0063 0.1413  283 GLU A CA  
2034 C C   . GLU A 276 ? 1.0505 0.8381 1.0049 0.0790  0.0147  0.1569  283 GLU A C   
2035 O O   . GLU A 276 ? 1.0413 0.8144 0.9543 0.0811  0.0181  0.1723  283 GLU A O   
2036 C CB  . GLU A 276 ? 1.1944 1.0302 1.1858 0.1143  -0.0192 0.1516  283 GLU A CB  
2037 C CG  . GLU A 276 ? 1.2157 1.1039 1.2230 0.1275  -0.0426 0.1423  283 GLU A CG  
2038 C CD  . GLU A 276 ? 1.1962 1.0922 1.2265 0.1525  -0.0533 0.1473  283 GLU A CD  
2039 O OE1 . GLU A 276 ? 1.1701 1.0565 1.2314 0.1500  -0.0440 0.1395  283 GLU A OE1 
2040 O OE2 . GLU A 276 ? 1.2318 1.1458 1.2491 0.1758  -0.0716 0.1584  283 GLU A OE2 
2041 N N   . LYS A 277 ? 1.0792 0.8431 1.0557 0.0675  0.0290  0.1518  284 LYS A N   
2042 C CA  . LYS A 277 ? 1.1121 0.8350 1.0727 0.0521  0.0509  0.1605  284 LYS A CA  
2043 C C   . LYS A 277 ? 1.0674 0.8076 1.0273 0.0295  0.0619  0.1486  284 LYS A C   
2044 O O   . LYS A 277 ? 1.0491 0.7724 0.9775 0.0219  0.0749  0.1597  284 LYS A O   
2045 C CB  . LYS A 277 ? 1.2417 0.9410 1.2302 0.0450  0.0604  0.1536  284 LYS A CB  
2046 C CG  . LYS A 277 ? 1.4726 1.1483 1.4642 0.0667  0.0546  0.1631  284 LYS A CG  
2047 C CD  . LYS A 277 ? 1.5177 1.1820 1.5405 0.0585  0.0617  0.1485  284 LYS A CD  
2048 C CE  . LYS A 277 ? 1.4701 1.1232 1.5025 0.0826  0.0544  0.1522  284 LYS A CE  
2049 N NZ  . LYS A 277 ? 1.4133 1.0492 1.4685 0.0735  0.0641  0.1378  284 LYS A NZ  
2050 N N   . PHE A 278 ? 0.9346 0.7074 0.9287 0.0202  0.0574  0.1266  285 PHE A N   
2051 C CA  . PHE A 278 ? 0.9456 0.7325 0.9506 0.0003  0.0692  0.1126  285 PHE A CA  
2052 C C   . PHE A 278 ? 0.8772 0.6863 0.8604 -0.0019 0.0693  0.1089  285 PHE A C   
2053 O O   . PHE A 278 ? 1.0372 0.8452 1.0141 -0.0162 0.0857  0.1060  285 PHE A O   
2054 C CB  . PHE A 278 ? 0.9739 0.7825 1.0199 -0.0061 0.0639  0.0924  285 PHE A CB  
2055 C CG  . PHE A 278 ? 0.9877 0.8065 1.0503 -0.0236 0.0761  0.0796  285 PHE A CG  
2056 C CD1 . PHE A 278 ? 0.9063 0.7067 0.9781 -0.0370 0.0905  0.0805  285 PHE A CD1 
2057 C CD2 . PHE A 278 ? 0.7865 0.6341 0.8567 -0.0265 0.0736  0.0654  285 PHE A CD2 
2058 C CE1 . PHE A 278 ? 0.8957 0.7132 0.9878 -0.0519 0.1004  0.0676  285 PHE A CE1 
2059 C CE2 . PHE A 278 ? 0.7507 0.6103 0.8394 -0.0389 0.0845  0.0534  285 PHE A CE2 
2060 C CZ  . PHE A 278 ? 0.8105 0.6585 0.9121 -0.0512 0.0971  0.0545  285 PHE A CZ  
2061 N N   . ARG A 279 ? 0.8371 0.6686 0.8105 0.0108  0.0519  0.1068  286 ARG A N   
2062 C CA  . ARG A 279 ? 0.8291 0.6823 0.7787 0.0086  0.0506  0.1001  286 ARG A CA  
2063 C C   . ARG A 279 ? 0.9253 0.7576 0.8274 0.0064  0.0645  0.1177  286 ARG A C   
2064 O O   . ARG A 279 ? 0.9451 0.7851 0.8380 -0.0066 0.0793  0.1093  286 ARG A O   
2065 C CB  . ARG A 279 ? 0.8126 0.6946 0.7603 0.0212  0.0277  0.0934  286 ARG A CB  
2066 C CG  . ARG A 279 ? 0.8577 0.7631 0.7798 0.0179  0.0248  0.0823  286 ARG A CG  
2067 C CD  . ARG A 279 ? 0.8658 0.8028 0.7939 0.0267  0.0013  0.0715  286 ARG A CD  
2068 N NE  . ARG A 279 ? 0.8569 0.8084 0.8309 0.0195  -0.0022 0.0516  286 ARG A NE  
2069 C CZ  . ARG A 279 ? 0.7422 0.7052 0.7304 0.0074  0.0023  0.0299  286 ARG A CZ  
2070 N NH1 . ARG A 279 ? 0.7435 0.7101 0.7070 0.0008  0.0111  0.0212  286 ARG A NH1 
2071 N NH2 . ARG A 279 ? 0.7512 0.7201 0.7775 0.0025  -0.0010 0.0168  286 ARG A NH2 
2072 N N   . PRO A 280 ? 0.8901 0.6949 0.7617 0.0196  0.0612  0.1422  287 PRO A N   
2073 C CA  . PRO A 280 ? 0.9618 0.7401 0.7832 0.0157  0.0772  0.1615  287 PRO A CA  
2074 C C   . PRO A 280 ? 0.9586 0.7119 0.7879 -0.0060 0.1058  0.1629  287 PRO A C   
2075 O O   . PRO A 280 ? 1.0117 0.7577 0.8089 -0.0175 0.1245  0.1686  287 PRO A O   
2076 C CB  . PRO A 280 ? 1.0388 0.7886 0.8293 0.0378  0.0653  0.1887  287 PRO A CB  
2077 C CG  . PRO A 280 ? 0.9906 0.7451 0.8240 0.0493  0.0507  0.1828  287 PRO A CG  
2078 C CD  . PRO A 280 ? 0.9205 0.7179 0.7977 0.0402  0.0432  0.1536  287 PRO A CD  
2079 N N   . PHE A 281 ? 0.9356 0.6794 0.8068 -0.0127 0.1097  0.1560  288 PHE A N   
2080 C CA  . PHE A 281 ? 1.0305 0.7621 0.9198 -0.0357 0.1341  0.1508  288 PHE A CA  
2081 C C   . PHE A 281 ? 0.9889 0.7593 0.8989 -0.0496 0.1425  0.1280  288 PHE A C   
2082 O O   . PHE A 281 ? 1.0733 0.8414 0.9735 -0.0664 0.1656  0.1281  288 PHE A O   
2083 C CB  . PHE A 281 ? 1.0221 0.7387 0.9507 -0.0396 0.1333  0.1456  288 PHE A CB  
2084 C CG  . PHE A 281 ? 0.9773 0.6932 0.9319 -0.0646 0.1543  0.1347  288 PHE A CG  
2085 C CD1 . PHE A 281 ? 1.0128 0.6941 0.9458 -0.0809 0.1786  0.1484  288 PHE A CD1 
2086 C CD2 . PHE A 281 ? 0.9026 0.6552 0.9030 -0.0724 0.1502  0.1104  288 PHE A CD2 
2087 C CE1 . PHE A 281 ? 0.9646 0.6539 0.9265 -0.1063 0.1981  0.1354  288 PHE A CE1 
2088 C CE2 . PHE A 281 ? 0.9019 0.6626 0.9299 -0.0939 0.1670  0.0989  288 PHE A CE2 
2089 C CZ  . PHE A 281 ? 0.9166 0.6483 0.9279 -0.1120 0.1911  0.1100  288 PHE A CZ  
2090 N N   . TYR A 282 ? 0.9756 0.7799 0.9145 -0.0426 0.1252  0.1086  289 TYR A N   
2091 C CA  . TYR A 282 ? 0.9437 0.7826 0.9012 -0.0504 0.1304  0.0864  289 TYR A CA  
2092 C C   . TYR A 282 ? 1.0488 0.8943 0.9644 -0.0530 0.1419  0.0884  289 TYR A C   
2093 O O   . TYR A 282 ? 1.1506 1.0101 1.0735 -0.0661 0.1615  0.0773  289 TYR A O   
2094 C CB  . TYR A 282 ? 0.9119 0.7769 0.8978 -0.0404 0.1090  0.0684  289 TYR A CB  
2095 C CG  . TYR A 282 ? 0.8179 0.7114 0.8162 -0.0450 0.1141  0.0466  289 TYR A CG  
2096 C CD1 . TYR A 282 ? 0.8158 0.7220 0.8490 -0.0552 0.1272  0.0333  289 TYR A CD1 
2097 C CD2 . TYR A 282 ? 0.8293 0.7378 0.8034 -0.0388 0.1068  0.0385  289 TYR A CD2 
2098 C CE1 . TYR A 282 ? 0.7781 0.7089 0.8244 -0.0563 0.1332  0.0130  289 TYR A CE1 
2099 C CE2 . TYR A 282 ? 0.7923 0.7221 0.7763 -0.0425 0.1139  0.0168  289 TYR A CE2 
2100 C CZ  . TYR A 282 ? 0.8000 0.7398 0.8207 -0.0499 0.1277  0.0047  289 TYR A CZ  
2101 O OH  . TYR A 282 ? 0.8355 0.7954 0.8684 -0.0502 0.1354  -0.0172 289 TYR A OH  
2102 N N   . LEU A 283 ? 1.1310 0.9694 1.0036 -0.0399 0.1295  0.1015  290 LEU A N   
2103 C CA  . LEU A 283 ? 1.2112 1.0572 1.0358 -0.0405 0.1366  0.1029  290 LEU A CA  
2104 C C   . LEU A 283 ? 1.2852 1.1055 1.0728 -0.0535 0.1644  0.1208  290 LEU A C   
2105 O O   . LEU A 283 ? 1.3093 1.1441 1.0836 -0.0653 0.1843  0.1109  290 LEU A O   
2106 C CB  . LEU A 283 ? 1.2876 1.1368 1.0759 -0.0219 0.1117  0.1121  290 LEU A CB  
2107 C CG  . LEU A 283 ? 1.3280 1.2100 1.1454 -0.0137 0.0877  0.0898  290 LEU A CG  
2108 C CD1 . LEU A 283 ? 1.2810 1.1673 1.0761 0.0047  0.0611  0.1011  290 LEU A CD1 
2109 C CD2 . LEU A 283 ? 1.3717 1.2809 1.1852 -0.0215 0.0938  0.0644  290 LEU A CD2 
2110 N N   . SER A 284 ? 1.2965 1.0771 1.0682 -0.0520 0.1677  0.1463  291 SER A N   
2111 C CA  . SER A 284 ? 1.3314 1.0783 1.0653 -0.0663 0.1960  0.1666  291 SER A CA  
2112 C C   . SER A 284 ? 1.2975 1.0514 1.0713 -0.0917 0.2238  0.1529  291 SER A C   
2113 O O   . SER A 284 ? 1.4460 1.2043 1.1993 -0.1075 0.2497  0.1521  291 SER A O   
2114 C CB  . SER A 284 ? 1.3265 1.0217 1.0298 -0.0561 0.1918  0.1985  291 SER A CB  
2115 O OG  . SER A 284 ? 1.2349 0.9204 0.9841 -0.0513 0.1800  0.1951  291 SER A OG  
2116 N N   . GLN A 285 ? 1.2707 1.0311 1.1017 -0.0955 0.2179  0.1403  292 GLN A N   
2117 C CA  . GLN A 285 ? 1.2332 0.9992 1.1048 -0.1191 0.2406  0.1292  292 GLN A CA  
2118 C C   . GLN A 285 ? 1.1398 0.9579 1.0637 -0.1249 0.2421  0.0979  292 GLN A C   
2119 O O   . GLN A 285 ? 1.1669 1.0013 1.1090 -0.1443 0.2668  0.0883  292 GLN A O   
2120 C CB  . GLN A 285 ? 1.2846 1.0220 1.1825 -0.1210 0.2342  0.1354  292 GLN A CB  
2121 C CG  . GLN A 285 ? 1.3914 1.0697 1.2426 -0.1175 0.2390  0.1663  292 GLN A CG  
2122 C CD  . GLN A 285 ? 1.5818 1.2269 1.4349 -0.1443 0.2686  0.1738  292 GLN A CD  
2123 O OE1 . GLN A 285 ? 1.7973 1.4048 1.6586 -0.1462 0.2676  0.1815  292 GLN A OE1 
2124 N NE2 . GLN A 285 ? 1.5093 1.1687 1.3568 -0.1665 0.2967  0.1694  292 GLN A NE2 
2125 N N   . LEU A 286 ? 1.0824 0.9251 1.0310 -0.1083 0.2170  0.0827  293 LEU A N   
2126 C CA  . LEU A 286 ? 1.0607 0.9447 1.0628 -0.1096 0.2142  0.0553  293 LEU A CA  
2127 C C   . LEU A 286 ? 1.0649 0.9805 1.0629 -0.1026 0.2147  0.0370  293 LEU A C   
2128 O O   . LEU A 286 ? 0.8989 0.8456 0.9338 -0.1079 0.2253  0.0169  293 LEU A O   
2129 C CB  . LEU A 286 ? 1.0141 0.8994 1.0517 -0.0988 0.1890  0.0495  293 LEU A CB  
2130 C CG  . LEU A 286 ? 1.0885 0.9460 1.1377 -0.1056 0.1877  0.0609  293 LEU A CG  
2131 C CD1 . LEU A 286 ? 1.1267 0.9916 1.2081 -0.0940 0.1635  0.0521  293 LEU A CD1 
2132 C CD2 . LEU A 286 ? 1.0639 0.9264 1.1387 -0.1286 0.2104  0.0557  293 LEU A CD2 
2133 N N   . GLU A 287 ? 1.1926 1.1016 1.1478 -0.0903 0.2033  0.0424  294 GLU A N   
2134 C CA  . GLU A 287 ? 1.2655 1.2006 1.2135 -0.0839 0.2023  0.0224  294 GLU A CA  
2135 C C   . GLU A 287 ? 1.3778 1.3272 1.3088 -0.0965 0.2329  0.0151  294 GLU A C   
2136 O O   . GLU A 287 ? 1.2033 1.1807 1.1747 -0.1017 0.2466  -0.0055 294 GLU A O   
2137 C CB  . GLU A 287 ? 1.3397 1.2662 1.2441 -0.0702 0.1813  0.0290  294 GLU A CB  
2138 C CG  . GLU A 287 ? 1.3197 1.2705 1.2227 -0.0636 0.1747  0.0042  294 GLU A CG  
2139 C CD  . GLU A 287 ? 1.3348 1.2833 1.2052 -0.0520 0.1502  0.0067  294 GLU A CD  
2140 O OE1 . GLU A 287 ? 1.3824 1.3201 1.1998 -0.0502 0.1496  0.0235  294 GLU A OE1 
2141 O OE2 . GLU A 287 ? 1.2974 1.2556 1.1946 -0.0450 0.1312  -0.0079 294 GLU A OE2 
2142 N N   . ASN B 1   ? 1.4167 1.4914 1.1049 0.2934  0.1385  -0.1344 8   ASN B N   
2143 C CA  . ASN B 1   ? 1.4403 1.5281 1.1703 0.2970  0.1594  -0.1265 8   ASN B CA  
2144 C C   . ASN B 1   ? 1.3707 1.4868 1.1676 0.2721  0.1422  -0.1242 8   ASN B C   
2145 O O   . ASN B 1   ? 1.3692 1.4826 1.1736 0.2556  0.1137  -0.1360 8   ASN B O   
2146 C CB  . ASN B 1   ? 1.5179 1.5624 1.2045 0.3188  0.1659  -0.1462 8   ASN B CB  
2147 C CG  . ASN B 1   ? 1.5732 1.5858 1.1896 0.3501  0.1941  -0.1446 8   ASN B CG  
2148 O OD1 . ASN B 1   ? 1.5529 1.5684 1.1402 0.3559  0.2016  -0.1334 8   ASN B OD1 
2149 N ND2 . ASN B 1   ? 1.6045 1.5832 1.1907 0.3722  0.2114  -0.1554 8   ASN B ND2 
2150 N N   . VAL B 2   ? 1.4170 1.5581 1.2619 0.2715  0.1604  -0.1076 9   VAL B N   
2151 C CA  . VAL B 2   ? 1.4516 1.6180 1.3545 0.2515  0.1473  -0.1020 9   VAL B CA  
2152 C C   . VAL B 2   ? 1.4099 1.5532 1.3140 0.2551  0.1391  -0.1193 9   VAL B C   
2153 O O   . VAL B 2   ? 1.5723 1.6950 1.4582 0.2743  0.1560  -0.1246 9   VAL B O   
2154 C CB  . VAL B 2   ? 1.4885 1.6910 1.4434 0.2491  0.1655  -0.0752 9   VAL B CB  
2155 C CG1 . VAL B 2   ? 1.5144 1.7369 1.5186 0.2323  0.1510  -0.0697 9   VAL B CG1 
2156 C CG2 . VAL B 2   ? 1.4926 1.7169 1.4543 0.2428  0.1697  -0.0589 9   VAL B CG2 
2157 N N   . ILE B 3   ? 1.2568 1.4027 1.1852 0.2380  0.1159  -0.1263 10  ILE B N   
2158 C CA  . ILE B 3   ? 1.2594 1.3886 1.2041 0.2390  0.1086  -0.1383 10  ILE B CA  
2159 C C   . ILE B 3   ? 1.2180 1.3741 1.2116 0.2366  0.1215  -0.1190 10  ILE B C   
2160 O O   . ILE B 3   ? 1.1755 1.3589 1.1991 0.2221  0.1160  -0.1039 10  ILE B O   
2161 C CB  . ILE B 3   ? 1.2306 1.3499 1.1865 0.2236  0.0812  -0.1505 10  ILE B CB  
2162 C CG1 . ILE B 3   ? 1.2730 1.3639 1.1844 0.2265  0.0637  -0.1696 10  ILE B CG1 
2163 C CG2 . ILE B 3   ? 1.2563 1.3608 1.2397 0.2244  0.0758  -0.1591 10  ILE B CG2 
2164 C CD1 . ILE B 3   ? 1.2751 1.3632 1.2038 0.2099  0.0376  -0.1754 10  ILE B CD1 
2165 N N   . LYS B 4   ? 1.2616 1.4070 1.2608 0.2516  0.1375  -0.1199 11  LYS B N   
2166 C CA  . LYS B 4   ? 1.1960 1.3644 1.2444 0.2510  0.1476  -0.1015 11  LYS B CA  
2167 C C   . LYS B 4   ? 1.1173 1.2765 1.1892 0.2434  0.1327  -0.1091 11  LYS B C   
2168 O O   . LYS B 4   ? 1.1083 1.2368 1.1674 0.2517  0.1304  -0.1278 11  LYS B O   
2169 C CB  . LYS B 4   ? 1.2512 1.4133 1.3006 0.2724  0.1758  -0.0953 11  LYS B CB  
2170 C CG  . LYS B 4   ? 1.2441 1.4206 1.2855 0.2815  0.1970  -0.0793 11  LYS B CG  
2171 C CD  . LYS B 4   ? 1.3220 1.4699 1.3288 0.3083  0.2257  -0.0847 11  LYS B CD  
2172 C CE  . LYS B 4   ? 1.3330 1.4944 1.3333 0.3188  0.2502  -0.0656 11  LYS B CE  
2173 N NZ  . LYS B 4   ? 1.4035 1.5268 1.3491 0.3480  0.2792  -0.0739 11  LYS B NZ  
2174 N N   . MET B 5   ? 1.0967 1.2793 1.2009 0.2288  0.1228  -0.0946 12  MET B N   
2175 C CA  . MET B 5   ? 1.0238 1.2009 1.1540 0.2222  0.1123  -0.0954 12  MET B CA  
2176 C C   . MET B 5   ? 0.9731 1.1677 1.1416 0.2260  0.1213  -0.0761 12  MET B C   
2177 O O   . MET B 5   ? 0.9018 1.1178 1.0826 0.2295  0.1309  -0.0599 12  MET B O   
2178 C CB  . MET B 5   ? 0.9430 1.1280 1.0738 0.2057  0.0965  -0.0917 12  MET B CB  
2179 C CG  . MET B 5   ? 0.9125 1.0787 1.0180 0.2005  0.0840  -0.1096 12  MET B CG  
2180 S SD  . MET B 5   ? 0.9140 1.0946 1.0221 0.1833  0.0732  -0.0991 12  MET B SD  
2181 C CE  . MET B 5   ? 0.8913 1.0496 0.9805 0.1789  0.0582  -0.1186 12  MET B CE  
2182 N N   . LYS B 6   ? 0.9592 1.1449 1.1510 0.2252  0.1174  -0.0759 13  LYS B N   
2183 C CA  . LYS B 6   ? 0.9435 1.1426 1.1718 0.2292  0.1236  -0.0569 13  LYS B CA  
2184 C C   . LYS B 6   ? 0.9344 1.1410 1.1734 0.2185  0.1120  -0.0441 13  LYS B C   
2185 O O   . LYS B 6   ? 0.9052 1.1000 1.1324 0.2105  0.1034  -0.0526 13  LYS B O   
2186 C CB  . LYS B 6   ? 0.9572 1.1347 1.2036 0.2416  0.1336  -0.0661 13  LYS B CB  
2187 C CG  . LYS B 6   ? 0.9987 1.1598 1.2262 0.2564  0.1486  -0.0800 13  LYS B CG  
2188 C CD  . LYS B 6   ? 1.0324 1.1770 1.2844 0.2709  0.1629  -0.0822 13  LYS B CD  
2189 C CE  . LYS B 6   ? 1.0455 1.2170 1.3348 0.2781  0.1783  -0.0555 13  LYS B CE  
2190 N NZ  . LYS B 6   ? 1.0314 1.1925 1.3525 0.2910  0.1929  -0.0521 13  LYS B NZ  
2191 N N   . SER B 7   ? 0.9675 1.1918 1.2284 0.2198  0.1124  -0.0223 14  SER B N   
2192 C CA  . SER B 7   ? 1.0277 1.2544 1.2906 0.2139  0.1036  -0.0077 14  SER B CA  
2193 C C   . SER B 7   ? 1.0371 1.2442 1.3186 0.2178  0.1087  -0.0096 14  SER B C   
2194 O O   . SER B 7   ? 0.9882 1.1873 1.2624 0.2129  0.1052  -0.0049 14  SER B O   
2195 C CB  . SER B 7   ? 1.0197 1.2672 1.2973 0.2159  0.0987  0.0162  14  SER B CB  
2196 O OG  . SER B 7   ? 0.9847 1.2503 1.2529 0.2100  0.0905  0.0203  14  SER B OG  
2197 N N   . SER B 8   ? 1.0851 1.2830 1.3927 0.2276  0.1187  -0.0153 15  SER B N   
2198 C CA  . SER B 8   ? 1.0973 1.2740 1.4318 0.2315  0.1235  -0.0203 15  SER B CA  
2199 C C   . SER B 8   ? 1.1208 1.2766 1.4481 0.2244  0.1163  -0.0398 15  SER B C   
2200 O O   . SER B 8   ? 1.1665 1.3083 1.5217 0.2243  0.1176  -0.0374 15  SER B O   
2201 C CB  . SER B 8   ? 1.1624 1.3293 1.5231 0.2436  0.1346  -0.0273 15  SER B CB  
2202 O OG  . SER B 8   ? 1.1272 1.2804 1.4654 0.2463  0.1351  -0.0516 15  SER B OG  
2203 N N   . ASP B 9   ? 1.0517 1.2057 1.3469 0.2191  0.1088  -0.0569 16  ASP B N   
2204 C CA  . ASP B 9   ? 1.0845 1.2219 1.3718 0.2110  0.0978  -0.0728 16  ASP B CA  
2205 C C   . ASP B 9   ? 1.0545 1.1972 1.3426 0.2019  0.0953  -0.0587 16  ASP B C   
2206 O O   . ASP B 9   ? 0.9877 1.1161 1.2868 0.1962  0.0886  -0.0668 16  ASP B O   
2207 C CB  . ASP B 9   ? 1.1487 1.2835 1.3967 0.2088  0.0905  -0.0916 16  ASP B CB  
2208 C CG  . ASP B 9   ? 1.2537 1.3744 1.4902 0.2208  0.0957  -0.1079 16  ASP B CG  
2209 O OD1 . ASP B 9   ? 1.4289 1.5340 1.6906 0.2289  0.1006  -0.1124 16  ASP B OD1 
2210 O OD2 . ASP B 9   ? 1.2102 1.3335 1.4111 0.2233  0.0970  -0.1154 16  ASP B OD2 
2211 N N   . PHE B 10  ? 0.9825 1.1424 1.2586 0.2016  0.0999  -0.0380 17  PHE B N   
2212 C CA  . PHE B 10  ? 0.9305 1.0898 1.1968 0.1965  0.1010  -0.0238 17  PHE B CA  
2213 C C   . PHE B 10  ? 0.9814 1.1370 1.2691 0.2045  0.1120  -0.0017 17  PHE B C   
2214 O O   . PHE B 10  ? 1.0623 1.2274 1.3553 0.2117  0.1147  0.0093  17  PHE B O   
2215 C CB  . PHE B 10  ? 0.8918 1.0662 1.1177 0.1909  0.0949  -0.0190 17  PHE B CB  
2216 C CG  . PHE B 10  ? 0.8460 1.0238 1.0517 0.1837  0.0868  -0.0369 17  PHE B CG  
2217 C CD1 . PHE B 10  ? 0.8317 1.0010 1.0277 0.1758  0.0831  -0.0432 17  PHE B CD1 
2218 C CD2 . PHE B 10  ? 0.8164 1.0048 1.0152 0.1863  0.0853  -0.0454 17  PHE B CD2 
2219 C CE1 . PHE B 10  ? 0.8239 0.9959 1.0006 0.1700  0.0753  -0.0579 17  PHE B CE1 
2220 C CE2 . PHE B 10  ? 0.8196 1.0092 0.9966 0.1819  0.0803  -0.0595 17  PHE B CE2 
2221 C CZ  . PHE B 10  ? 0.8117 0.9934 0.9764 0.1734  0.0740  -0.0660 17  PHE B CZ  
2222 N N   . LEU B 11  ? 1.0220 1.1635 1.3241 0.2046  0.1197  0.0074  18  LEU B N   
2223 C CA  . LEU B 11  ? 1.0204 1.1539 1.3472 0.2147  0.1346  0.0303  18  LEU B CA  
2224 C C   . LEU B 11  ? 1.1007 1.2366 1.3860 0.2201  0.1388  0.0521  18  LEU B C   
2225 O O   . LEU B 11  ? 1.1182 1.2581 1.4048 0.2293  0.1421  0.0681  18  LEU B O   
2226 C CB  . LEU B 11  ? 1.0995 1.2154 1.4664 0.2145  0.1445  0.0344  18  LEU B CB  
2227 C CG  . LEU B 11  ? 1.0845 1.1917 1.4925 0.2075  0.1340  0.0118  18  LEU B CG  
2228 C CD1 . LEU B 11  ? 1.0289 1.1203 1.4898 0.2084  0.1446  0.0240  18  LEU B CD1 
2229 C CD2 . LEU B 11  ? 1.1335 1.2396 1.5654 0.2115  0.1284  -0.0015 18  LEU B CD2 
2230 N N   . GLU B 12  ? 1.2115 1.3421 1.4589 0.2151  0.1374  0.0522  19  GLU B N   
2231 C CA  . GLU B 12  ? 1.2288 1.3539 1.4235 0.2199  0.1376  0.0682  19  GLU B CA  
2232 C C   . GLU B 12  ? 1.2200 1.3487 1.3720 0.2090  0.1243  0.0548  19  GLU B C   
2233 O O   . GLU B 12  ? 1.0485 1.1809 1.2131 0.1993  0.1209  0.0376  19  GLU B O   
2234 C CB  . GLU B 12  ? 1.2049 1.3063 1.3965 0.2310  0.1598  0.0896  19  GLU B CB  
2235 C CG  . GLU B 12  ? 1.2028 1.2987 1.4403 0.2431  0.1765  0.1075  19  GLU B CG  
2236 C CD  . GLU B 12  ? 1.2521 1.3558 1.4779 0.2524  0.1709  0.1211  19  GLU B CD  
2237 O OE1 . GLU B 12  ? 1.2900 1.3973 1.4638 0.2524  0.1557  0.1234  19  GLU B OE1 
2238 O OE2 . GLU B 12  ? 1.1759 1.2818 1.4493 0.2594  0.1802  0.1301  19  GLU B OE2 
2239 N N   . SER B 13  ? 1.2849 1.4105 1.3872 0.2111  0.1151  0.0630  20  SER B N   
2240 C CA  . SER B 13  ? 1.2818 1.4109 1.3446 0.2009  0.0993  0.0517  20  SER B CA  
2241 C C   . SER B 13  ? 1.3411 1.4461 1.3426 0.2071  0.0974  0.0633  20  SER B C   
2242 O O   . SER B 13  ? 1.4079 1.5128 1.3811 0.2107  0.0810  0.0711  20  SER B O   
2243 C CB  . SER B 13  ? 1.3028 1.4582 1.3759 0.1940  0.0794  0.0433  20  SER B CB  
2244 O OG  . SER B 13  ? 1.4259 1.5863 1.4966 0.2015  0.0707  0.0582  20  SER B OG  
2245 N N   . ALA B 14  ? 1.2482 1.3305 1.2296 0.2091  0.1136  0.0645  21  ALA B N   
2246 C CA  . ALA B 14  ? 1.2557 1.3052 1.1712 0.2185  0.1182  0.0746  21  ALA B CA  
2247 C C   . ALA B 14  ? 1.2876 1.3334 1.1608 0.2076  0.0990  0.0597  21  ALA B C   
2248 O O   . ALA B 14  ? 1.1947 1.2445 1.0809 0.1978  0.1038  0.0475  21  ALA B O   
2249 C CB  . ALA B 14  ? 1.2367 1.2608 1.1560 0.2290  0.1510  0.0866  21  ALA B CB  
2250 N N   . GLU B 15  ? 1.3101 1.3465 1.1350 0.2095  0.0760  0.0617  22  GLU B N   
2251 C CA  . GLU B 15  ? 1.2814 1.3142 1.0709 0.1984  0.0513  0.0478  22  GLU B CA  
2252 C C   . GLU B 15  ? 1.2256 1.2221 0.9651 0.2021  0.0661  0.0442  22  GLU B C   
2253 O O   . GLU B 15  ? 1.2958 1.2544 0.9821 0.2183  0.0793  0.0560  22  GLU B O   
2254 C CB  . GLU B 15  ? 1.3989 1.4264 1.1535 0.2007  0.0193  0.0527  22  GLU B CB  
2255 C CG  . GLU B 15  ? 1.4521 1.5187 1.2630 0.1955  0.0030  0.0566  22  GLU B CG  
2256 C CD  . GLU B 15  ? 1.5437 1.6024 1.3397 0.2090  -0.0058 0.0751  22  GLU B CD  
2257 O OE1 . GLU B 15  ? 1.6737 1.7041 1.4089 0.2151  -0.0267 0.0796  22  GLU B OE1 
2258 O OE2 . GLU B 15  ? 1.6172 1.6958 1.4605 0.2141  0.0068  0.0849  22  GLU B OE2 
2259 N N   . LEU B 16  ? 1.1592 1.1652 0.9148 0.1890  0.0667  0.0298  23  LEU B N   
2260 C CA  . LEU B 16  ? 1.2489 1.2231 0.9701 0.1923  0.0863  0.0273  23  LEU B CA  
2261 C C   . LEU B 16  ? 1.3778 1.3305 1.0443 0.1860  0.0644  0.0145  23  LEU B C   
2262 O O   . LEU B 16  ? 1.3675 1.3425 1.0476 0.1725  0.0345  0.0042  23  LEU B O   
2263 C CB  . LEU B 16  ? 1.1247 1.1172 0.9037 0.1855  0.1079  0.0241  23  LEU B CB  
2264 C CG  . LEU B 16  ? 1.0614 1.0921 0.8910 0.1677  0.0944  0.0095  23  LEU B CG  
2265 C CD1 . LEU B 16  ? 1.1071 1.1320 0.9117 0.1573  0.0828  -0.0029 23  LEU B CD1 
2266 C CD2 . LEU B 16  ? 1.0104 1.0537 0.8955 0.1662  0.1140  0.0108  23  LEU B CD2 
2267 N N   . ASP B 17  ? 1.4986 1.4062 1.1072 0.1970  0.0818  0.0162  24  ASP B N   
2268 C CA  . ASP B 17  ? 1.5797 1.4489 1.1152 0.1976  0.0624  0.0055  24  ASP B CA  
2269 C C   . ASP B 17  ? 1.6771 1.5598 1.2316 0.1788  0.0480  -0.0122 24  ASP B C   
2270 O O   . ASP B 17  ? 1.7227 1.5978 1.2857 0.1775  0.0716  -0.0149 24  ASP B O   
2271 C CB  . ASP B 17  ? 1.6924 1.5032 1.1563 0.2193  0.0935  0.0143  24  ASP B CB  
2272 C CG  . ASP B 17  ? 1.7294 1.4875 1.1011 0.2242  0.0738  0.0018  24  ASP B CG  
2273 O OD1 . ASP B 17  ? 1.8021 1.5642 1.1583 0.2133  0.0303  -0.0105 24  ASP B OD1 
2274 O OD2 . ASP B 17  ? 1.6532 1.3619 0.9677 0.2405  0.1028  0.0052  24  ASP B OD2 
2275 N N   . SER B 18  ? 1.6917 1.5946 1.2576 0.1651  0.0098  -0.0218 25  SER B N   
2276 C CA  . SER B 18  ? 1.6768 1.5794 1.2429 0.1500  -0.0098 -0.0375 25  SER B CA  
2277 C C   . SER B 18  ? 1.7811 1.6896 1.3430 0.1404  -0.0560 -0.0436 25  SER B C   
2278 O O   . SER B 18  ? 1.8779 1.7902 1.4341 0.1458  -0.0740 -0.0355 25  SER B O   
2279 C CB  . SER B 18  ? 1.6243 1.5707 1.2631 0.1358  0.0025  -0.0408 25  SER B CB  
2280 O OG  . SER B 18  ? 1.5452 1.4855 1.1810 0.1240  -0.0087 -0.0532 25  SER B OG  
2281 N N   . LYS B 23  ? 1.4050 1.6002 1.3839 0.1294  -0.0785 0.0207  30  LYS B N   
2282 C CA  . LYS B 23  ? 1.4930 1.6533 1.4161 0.1368  -0.0642 0.0163  30  LYS B CA  
2283 C C   . LYS B 23  ? 1.4266 1.5915 1.3628 0.1372  -0.0324 0.0079  30  LYS B C   
2284 O O   . LYS B 23  ? 1.4178 1.6038 1.3938 0.1404  -0.0177 0.0096  30  LYS B O   
2285 C CB  . LYS B 23  ? 1.6442 1.7898 1.5471 0.1507  -0.0629 0.0293  30  LYS B CB  
2286 C CG  . LYS B 23  ? 1.7932 1.9396 1.6936 0.1522  -0.0962 0.0411  30  LYS B CG  
2287 C CD  . LYS B 23  ? 1.8883 2.0051 1.7366 0.1472  -0.1281 0.0353  30  LYS B CD  
2288 C CE  . LYS B 23  ? 1.9346 2.0550 1.7907 0.1460  -0.1689 0.0461  30  LYS B CE  
2289 N NZ  . LYS B 23  ? 1.9963 2.0804 1.7952 0.1416  -0.2052 0.0379  30  LYS B NZ  
2290 N N   . VAL B 24  ? 1.3901 1.5334 1.2937 0.1343  -0.0240 -0.0012 31  VAL B N   
2291 C CA  . VAL B 24  ? 1.2515 1.3949 1.1664 0.1346  0.0024  -0.0077 31  VAL B CA  
2292 C C   . VAL B 24  ? 1.1462 1.2676 1.0446 0.1474  0.0215  0.0003  31  VAL B C   
2293 O O   . VAL B 24  ? 1.1574 1.2486 1.0088 0.1552  0.0202  0.0064  31  VAL B O   
2294 C CB  . VAL B 24  ? 1.3089 1.4386 1.2022 0.1268  0.0048  -0.0176 31  VAL B CB  
2295 C CG1 . VAL B 24  ? 1.2273 1.3600 1.1401 0.1266  0.0281  -0.0224 31  VAL B CG1 
2296 C CG2 . VAL B 24  ? 1.3774 1.5264 1.2883 0.1147  -0.0143 -0.0229 31  VAL B CG2 
2297 N N   . SER B 25  ? 1.0439 1.1773 0.9797 0.1506  0.0394  0.0005  32  SER B N   
2298 C CA  . SER B 25  ? 1.0077 1.1249 0.9453 0.1626  0.0585  0.0108  32  SER B CA  
2299 C C   . SER B 25  ? 0.9134 1.0378 0.8935 0.1617  0.0759  0.0058  32  SER B C   
2300 O O   . SER B 25  ? 0.8528 0.9977 0.8610 0.1540  0.0709  -0.0055 32  SER B O   
2301 C CB  . SER B 25  ? 1.0543 1.1779 1.0002 0.1711  0.0522  0.0226  32  SER B CB  
2302 O OG  . SER B 25  ? 1.0513 1.2055 1.0401 0.1666  0.0444  0.0183  32  SER B OG  
2303 N N   . LEU B 26  ? 0.9186 1.0229 0.9019 0.1704  0.0958  0.0154  33  LEU B N   
2304 C CA  . LEU B 26  ? 0.8810 0.9878 0.9104 0.1694  0.1091  0.0126  33  LEU B CA  
2305 C C   . LEU B 26  ? 0.8727 0.9921 0.9426 0.1738  0.1088  0.0140  33  LEU B C   
2306 O O   . LEU B 26  ? 0.8959 1.0091 0.9626 0.1838  0.1143  0.0277  33  LEU B O   
2307 C CB  . LEU B 26  ? 0.9127 0.9931 0.9395 0.1774  0.1324  0.0256  33  LEU B CB  
2308 C CG  . LEU B 26  ? 0.9194 0.9999 0.9991 0.1744  0.1436  0.0245  33  LEU B CG  
2309 C CD1 . LEU B 26  ? 0.8988 0.9926 0.9850 0.1609  0.1301  0.0075  33  LEU B CD1 
2310 C CD2 . LEU B 26  ? 0.9811 1.0344 1.0601 0.1847  0.1709  0.0430  33  LEU B CD2 
2311 N N   . ALA B 27  ? 0.8285 0.9620 0.9338 0.1675  0.1029  0.0001  34  ALA B N   
2312 C CA  . ALA B 27  ? 0.8379 0.9820 0.9765 0.1711  0.0998  -0.0037 34  ALA B CA  
2313 C C   . ALA B 27  ? 0.8454 0.9836 1.0279 0.1696  0.1023  -0.0124 34  ALA B C   
2314 O O   . ALA B 27  ? 0.9327 1.0719 1.1166 0.1618  0.0950  -0.0251 34  ALA B O   
2315 C CB  . ALA B 27  ? 0.8241 0.9883 0.9529 0.1667  0.0858  -0.0149 34  ALA B CB  
2316 N N   . PHE B 28  ? 0.9314 1.0624 1.1509 0.1769  0.1105  -0.0052 35  PHE B N   
2317 C CA  . PHE B 28  ? 0.9792 1.1017 1.2478 0.1752  0.1082  -0.0142 35  PHE B CA  
2318 C C   . PHE B 28  ? 0.9231 1.0507 1.2035 0.1765  0.0970  -0.0310 35  PHE B C   
2319 O O   . PHE B 28  ? 0.8726 1.0011 1.1677 0.1842  0.1027  -0.0246 35  PHE B O   
2320 C CB  . PHE B 28  ? 1.0251 1.1334 1.3351 0.1828  0.1257  0.0053  35  PHE B CB  
2321 C CG  . PHE B 28  ? 1.0812 1.1790 1.4517 0.1791  0.1209  -0.0015 35  PHE B CG  
2322 C CD1 . PHE B 28  ? 1.0525 1.1440 1.4414 0.1722  0.1192  -0.0016 35  PHE B CD1 
2323 C CD2 . PHE B 28  ? 1.1013 1.1940 1.5144 0.1824  0.1161  -0.0077 35  PHE B CD2 
2324 C CE1 . PHE B 28  ? 1.0411 1.1226 1.4929 0.1678  0.1094  -0.0072 35  PHE B CE1 
2325 C CE2 . PHE B 28  ? 1.1015 1.1814 1.5738 0.1781  0.1062  -0.0156 35  PHE B CE2 
2326 C CZ  . PHE B 28  ? 1.0893 1.1641 1.5824 0.1704  0.1012  -0.0150 35  PHE B CZ  
2327 N N   . HIS B 29  ? 0.9380 1.0663 1.2087 0.1704  0.0823  -0.0517 36  HIS B N   
2328 C CA  . HIS B 29  ? 0.9529 1.0768 1.2288 0.1736  0.0727  -0.0706 36  HIS B CA  
2329 C C   . HIS B 29  ? 0.9946 1.0989 1.3217 0.1751  0.0685  -0.0758 36  HIS B C   
2330 O O   . HIS B 29  ? 0.9909 1.0860 1.3464 0.1692  0.0636  -0.0741 36  HIS B O   
2331 C CB  . HIS B 29  ? 1.0016 1.1261 1.2450 0.1688  0.0588  -0.0897 36  HIS B CB  
2332 C CG  . HIS B 29  ? 1.0231 1.1421 1.2502 0.1759  0.0541  -0.1072 36  HIS B CG  
2333 N ND1 . HIS B 29  ? 1.0451 1.1419 1.2732 0.1774  0.0391  -0.1291 36  HIS B ND1 
2334 C CD2 . HIS B 29  ? 1.0695 1.1998 1.2763 0.1833  0.0629  -0.1054 36  HIS B CD2 
2335 C CE1 . HIS B 29  ? 1.1096 1.2010 1.3120 0.1871  0.0418  -0.1408 36  HIS B CE1 
2336 N NE2 . HIS B 29  ? 1.1395 1.2529 1.3332 0.1908  0.0580  -0.1254 36  HIS B NE2 
2337 N N   . ARG B 30  ? 0.9766 1.0740 1.3201 0.1828  0.0698  -0.0817 37  ARG B N   
2338 C CA  . ARG B 30  ? 0.9447 1.0229 1.3448 0.1850  0.0672  -0.0839 37  ARG B CA  
2339 C C   . ARG B 30  ? 0.9169 0.9734 1.3365 0.1786  0.0436  -0.1061 37  ARG B C   
2340 O O   . ARG B 30  ? 0.9484 0.9906 1.4265 0.1766  0.0390  -0.1030 37  ARG B O   
2341 C CB  . ARG B 30  ? 1.0057 1.0797 1.4178 0.1954  0.0745  -0.0860 37  ARG B CB  
2342 C CG  . ARG B 30  ? 1.0450 1.1038 1.5234 0.1986  0.0789  -0.0781 37  ARG B CG  
2343 C CD  . ARG B 30  ? 1.0440 1.0973 1.5393 0.2092  0.0872  -0.0792 37  ARG B CD  
2344 N NE  . ARG B 30  ? 0.9947 1.0686 1.4856 0.2166  0.1081  -0.0520 37  ARG B NE  
2345 C CZ  . ARG B 30  ? 0.9499 1.0428 1.3983 0.2205  0.1136  -0.0472 37  ARG B CZ  
2346 N NH1 . ARG B 30  ? 0.9499 1.0458 1.3554 0.2189  0.1051  -0.0659 37  ARG B NH1 
2347 N NH2 . ARG B 30  ? 0.9091 1.0174 1.3597 0.2268  0.1276  -0.0212 37  ARG B NH2 
2348 N N   . THR B 31  ? 0.9315 0.9843 1.3053 0.1762  0.0278  -0.1270 38  THR B N   
2349 C CA  . THR B 31  ? 0.9455 0.9749 1.3260 0.1706  -0.0006 -0.1496 38  THR B CA  
2350 C C   . THR B 31  ? 0.9970 1.0338 1.3596 0.1610  -0.0118 -0.1490 38  THR B C   
2351 O O   . THR B 31  ? 0.9646 0.9846 1.3524 0.1545  -0.0359 -0.1597 38  THR B O   
2352 C CB  . THR B 31  ? 0.9775 0.9847 1.3157 0.1791  -0.0138 -0.1782 38  THR B CB  
2353 O OG1 . THR B 31  ? 0.9654 0.9869 1.2386 0.1834  -0.0049 -0.1802 38  THR B OG1 
2354 C CG2 . THR B 31  ? 0.9950 0.9912 1.3558 0.1891  -0.0027 -0.1801 38  THR B CG2 
2355 N N   . GLN B 32  ? 0.9937 1.0544 1.3185 0.1598  0.0039  -0.1358 39  GLN B N   
2356 C CA  . GLN B 32  ? 1.0473 1.1163 1.3459 0.1521  -0.0038 -0.1358 39  GLN B CA  
2357 C C   . GLN B 32  ? 0.9991 1.0851 1.3127 0.1464  0.0136  -0.1110 39  GLN B C   
2358 O O   . GLN B 32  ? 0.9602 1.0536 1.2538 0.1404  0.0105  -0.1092 39  GLN B O   
2359 C CB  . GLN B 32  ? 1.1199 1.1977 1.3526 0.1563  -0.0024 -0.1455 39  GLN B CB  
2360 C CG  . GLN B 32  ? 1.1849 1.2421 1.3848 0.1653  -0.0151 -0.1698 39  GLN B CG  
2361 C CD  . GLN B 32  ? 1.2509 1.3194 1.3914 0.1717  -0.0055 -0.1722 39  GLN B CD  
2362 O OE1 . GLN B 32  ? 1.3464 1.4338 1.4696 0.1659  -0.0008 -0.1620 39  GLN B OE1 
2363 N NE2 . GLN B 32  ? 1.2307 1.2865 1.3429 0.1844  -0.0004 -0.1844 39  GLN B NE2 
2364 N N   . GLY B 33  ? 0.9660 1.0550 1.3103 0.1499  0.0329  -0.0917 40  GLY B N   
2365 C CA  . GLY B 33  ? 0.8869 0.9819 1.2453 0.1478  0.0507  -0.0685 40  GLY B CA  
2366 C C   . GLY B 33  ? 0.8423 0.9524 1.1476 0.1493  0.0655  -0.0586 40  GLY B C   
2367 O O   . GLY B 33  ? 0.8318 0.9512 1.1044 0.1536  0.0674  -0.0619 40  GLY B O   
2368 N N   . LEU B 34  ? 0.7844 0.8951 1.0845 0.1457  0.0746  -0.0464 41  LEU B N   
2369 C CA  . LEU B 34  ? 0.7568 0.8734 1.0137 0.1481  0.0901  -0.0335 41  LEU B CA  
2370 C C   . LEU B 34  ? 0.7489 0.8789 0.9583 0.1425  0.0789  -0.0461 41  LEU B C   
2371 O O   . LEU B 34  ? 0.6981 0.8298 0.9073 0.1359  0.0663  -0.0575 41  LEU B O   
2372 C CB  . LEU B 34  ? 0.7557 0.8610 1.0268 0.1488  0.1075  -0.0155 41  LEU B CB  
2373 C CG  . LEU B 34  ? 0.7694 0.8646 1.0140 0.1581  0.1316  0.0053  41  LEU B CG  
2374 C CD1 . LEU B 34  ? 0.7536 0.8456 1.0051 0.1686  0.1408  0.0159  41  LEU B CD1 
2375 C CD2 . LEU B 34  ? 0.7355 0.8149 1.0071 0.1608  0.1517  0.0225  41  LEU B CD2 
2376 N N   . MET B 35  ? 0.7488 0.8881 0.9226 0.1455  0.0820  -0.0429 42  MET B N   
2377 C CA  . MET B 35  ? 0.7519 0.9053 0.8885 0.1408  0.0735  -0.0508 42  MET B CA  
2378 C C   . MET B 35  ? 0.7849 0.9409 0.8893 0.1421  0.0786  -0.0394 42  MET B C   
2379 O O   . MET B 35  ? 0.8075 0.9542 0.9102 0.1487  0.0876  -0.0267 42  MET B O   
2380 C CB  . MET B 35  ? 0.7700 0.9341 0.9047 0.1438  0.0650  -0.0627 42  MET B CB  
2381 C CG  . MET B 35  ? 0.7785 0.9344 0.9312 0.1443  0.0552  -0.0783 42  MET B CG  
2382 S SD  . MET B 35  ? 0.6951 0.8557 0.8370 0.1530  0.0526  -0.0901 42  MET B SD  
2383 C CE  . MET B 35  ? 0.6985 0.8391 0.8449 0.1539  0.0367  -0.1119 42  MET B CE  
2384 N N   . ILE B 36  ? 0.8588 1.0254 0.9375 0.1362  0.0712  -0.0438 43  ILE B N   
2385 C CA  . ILE B 36  ? 0.9106 1.0799 0.9597 0.1355  0.0680  -0.0366 43  ILE B CA  
2386 C C   . ILE B 36  ? 0.8989 1.0881 0.9534 0.1368  0.0594  -0.0386 43  ILE B C   
2387 O O   . ILE B 36  ? 0.8558 1.0561 0.9221 0.1363  0.0576  -0.0476 43  ILE B O   
2388 C CB  . ILE B 36  ? 0.8902 1.0563 0.9159 0.1275  0.0654  -0.0389 43  ILE B CB  
2389 C CG1 . ILE B 36  ? 0.8899 1.0341 0.9126 0.1284  0.0782  -0.0339 43  ILE B CG1 
2390 C CG2 . ILE B 36  ? 0.9404 1.1078 0.9380 0.1250  0.0554  -0.0349 43  ILE B CG2 
2391 C CD1 . ILE B 36  ? 0.9423 1.0645 0.9453 0.1374  0.0893  -0.0211 43  ILE B CD1 
2392 N N   . MET B 37  ? 0.8816 1.0726 0.9258 0.1396  0.0544  -0.0288 44  MET B N   
2393 C CA  . MET B 37  ? 0.9299 1.1398 0.9884 0.1421  0.0476  -0.0255 44  MET B CA  
2394 C C   . MET B 37  ? 1.0187 1.2322 1.0598 0.1375  0.0329  -0.0180 44  MET B C   
2395 O O   . MET B 37  ? 1.0273 1.2259 1.0466 0.1403  0.0277  -0.0100 44  MET B O   
2396 C CB  . MET B 37  ? 0.9402 1.1481 1.0174 0.1519  0.0532  -0.0185 44  MET B CB  
2397 C CG  . MET B 37  ? 0.9578 1.1854 1.0586 0.1561  0.0505  -0.0150 44  MET B CG  
2398 S SD  . MET B 37  ? 0.9909 1.2144 1.1195 0.1680  0.0605  -0.0095 44  MET B SD  
2399 C CE  . MET B 37  ? 1.0330 1.2462 1.1434 0.1716  0.0543  0.0093  44  MET B CE  
2400 N N   . LYS B 38  ? 1.0432 1.2735 1.0928 0.1310  0.0257  -0.0205 45  LYS B N   
2401 C CA  . LYS B 38  ? 0.9632 1.2010 1.0121 0.1259  0.0075  -0.0129 45  LYS B CA  
2402 C C   . LYS B 38  ? 0.9793 1.2381 1.0640 0.1315  0.0050  -0.0029 45  LYS B C   
2403 O O   . LYS B 38  ? 0.9663 1.2433 1.0785 0.1334  0.0144  -0.0036 45  LYS B O   
2404 C CB  . LYS B 38  ? 0.9307 1.1763 0.9810 0.1161  0.0024  -0.0175 45  LYS B CB  
2405 C CG  . LYS B 38  ? 0.9926 1.2428 1.0481 0.1092  -0.0206 -0.0102 45  LYS B CG  
2406 C CD  . LYS B 38  ? 1.0270 1.2756 1.0777 0.0986  -0.0272 -0.0153 45  LYS B CD  
2407 C CE  . LYS B 38  ? 1.0703 1.3174 1.1266 0.0910  -0.0559 -0.0095 45  LYS B CE  
2408 N NZ  . LYS B 38  ? 1.0695 1.2827 1.0754 0.0907  -0.0711 -0.0141 45  LYS B NZ  
2409 N N   . THR B 39  ? 1.0111 1.2647 1.0930 0.1359  -0.0057 0.0075  46  THR B N   
2410 C CA  . THR B 39  ? 0.9661 1.2393 1.0856 0.1408  -0.0115 0.0206  46  THR B CA  
2411 C C   . THR B 39  ? 0.9416 1.2266 1.0760 0.1322  -0.0361 0.0287  46  THR B C   
2412 O O   . THR B 39  ? 0.9057 1.1751 1.0135 0.1287  -0.0589 0.0318  46  THR B O   
2413 C CB  . THR B 39  ? 1.0083 1.2704 1.1204 0.1500  -0.0127 0.0299  46  THR B CB  
2414 O OG1 . THR B 39  ? 1.0403 1.2913 1.1478 0.1568  0.0097  0.0225  46  THR B OG1 
2415 C CG2 . THR B 39  ? 1.0181 1.3015 1.1744 0.1556  -0.0182 0.0453  46  THR B CG2 
2416 N N   . VAL B 40  ? 0.9312 1.2408 1.1083 0.1302  -0.0312 0.0329  47  VAL B N   
2417 C CA  . VAL B 40  ? 0.9601 1.2822 1.1619 0.1200  -0.0517 0.0399  47  VAL B CA  
2418 C C   . VAL B 40  ? 0.9454 1.2815 1.1872 0.1205  -0.0746 0.0583  47  VAL B C   
2419 O O   . VAL B 40  ? 0.9882 1.3198 1.2308 0.1113  -0.1059 0.0622  47  VAL B O   
2420 C CB  . VAL B 40  ? 0.9562 1.2976 1.1884 0.1187  -0.0330 0.0393  47  VAL B CB  
2421 C CG1 . VAL B 40  ? 0.9520 1.3113 1.2296 0.1095  -0.0513 0.0518  47  VAL B CG1 
2422 C CG2 . VAL B 40  ? 0.9975 1.3226 1.1872 0.1155  -0.0200 0.0219  47  VAL B CG2 
2423 N N   . TYR B 41  ? 0.9241 1.2756 1.2007 0.1311  -0.0603 0.0693  48  TYR B N   
2424 C CA  . TYR B 41  ? 0.8935 1.2608 1.2162 0.1335  -0.0792 0.0899  48  TYR B CA  
2425 C C   . TYR B 41  ? 0.9214 1.2827 1.2358 0.1461  -0.0674 0.0938  48  TYR B C   
2426 O O   . TYR B 41  ? 0.9114 1.2699 1.2190 0.1548  -0.0367 0.0853  48  TYR B O   
2427 C CB  . TYR B 41  ? 0.8699 1.2693 1.2669 0.1350  -0.0677 0.1056  48  TYR B CB  
2428 C CG  . TYR B 41  ? 0.8800 1.3017 1.3435 0.1396  -0.0792 0.1308  48  TYR B CG  
2429 C CD1 . TYR B 41  ? 0.8776 1.3058 1.3606 0.1541  -0.0558 0.1387  48  TYR B CD1 
2430 C CD2 . TYR B 41  ? 0.8659 1.3020 1.3789 0.1295  -0.1142 0.1473  48  TYR B CD2 
2431 C CE1 . TYR B 41  ? 0.8754 1.3247 1.4240 0.1590  -0.0645 0.1637  48  TYR B CE1 
2432 C CE2 . TYR B 41  ? 0.8975 1.3557 1.4799 0.1336  -0.1264 0.1729  48  TYR B CE2 
2433 C CZ  . TYR B 41  ? 0.8710 1.3367 1.4710 0.1488  -0.0999 0.1818  48  TYR B CZ  
2434 O OH  . TYR B 41  ? 0.9344 1.4224 1.6067 0.1538  -0.1095 0.2089  48  TYR B OH  
2435 N N   . LYS B 42  ? 0.9533 1.3103 1.2678 0.1471  -0.0941 0.1066  49  LYS B N   
2436 C CA  . LYS B 42  ? 0.9880 1.3459 1.3135 0.1594  -0.0864 0.1180  49  LYS B CA  
2437 C C   . LYS B 42  ? 0.9664 1.3417 1.3410 0.1585  -0.1174 0.1420  49  LYS B C   
2438 O O   . LYS B 42  ? 0.9630 1.3284 1.3197 0.1499  -0.1558 0.1448  49  LYS B O   
2439 C CB  . LYS B 42  ? 1.0534 1.3797 1.3126 0.1643  -0.0861 0.1099  49  LYS B CB  
2440 C CG  . LYS B 42  ? 1.0903 1.4161 1.3620 0.1782  -0.0671 0.1187  49  LYS B CG  
2441 C CD  . LYS B 42  ? 1.1465 1.4412 1.3587 0.1840  -0.0589 0.1117  49  LYS B CD  
2442 C CE  . LYS B 42  ? 1.0855 1.3698 1.2806 0.1839  -0.0294 0.0921  49  LYS B CE  
2443 N NZ  . LYS B 42  ? 1.1062 1.3595 1.2466 0.1874  -0.0238 0.0871  49  LYS B NZ  
2444 N N   . GLY B 43  ? 0.9108 1.3092 1.3468 0.1677  -0.1020 0.1588  50  GLY B N   
2445 C CA  . GLY B 43  ? 0.9091 1.3297 1.4094 0.1671  -0.1288 0.1850  50  GLY B CA  
2446 C C   . GLY B 43  ? 0.8862 1.3326 1.4595 0.1793  -0.1005 0.2032  50  GLY B C   
2447 O O   . GLY B 43  ? 0.8053 1.2456 1.3669 0.1905  -0.0624 0.1940  50  GLY B O   
2448 N N   . PRO B 44  ? 0.9392 1.4125 1.5910 0.1779  -0.1195 0.2296  51  PRO B N   
2449 C CA  . PRO B 44  ? 0.9738 1.4725 1.7037 0.1906  -0.0880 0.2496  51  PRO B CA  
2450 C C   . PRO B 44  ? 0.9855 1.4932 1.7366 0.1955  -0.0449 0.2425  51  PRO B C   
2451 O O   . PRO B 44  ? 0.9016 1.4062 1.6320 0.1857  -0.0477 0.2298  51  PRO B O   
2452 C CB  . PRO B 44  ? 1.0091 1.5335 1.8200 0.1855  -0.1250 0.2810  51  PRO B CB  
2453 C CG  . PRO B 44  ? 0.9970 1.5123 1.7807 0.1677  -0.1721 0.2736  51  PRO B CG  
2454 C CD  . PRO B 44  ? 0.9803 1.4594 1.6549 0.1647  -0.1720 0.2426  51  PRO B CD  
2455 N N   . ASN B 45  ? 1.1060 1.6213 1.8939 0.2120  -0.0050 0.2509  52  ASN B N   
2456 C CA  . ASN B 45  ? 1.1579 1.6719 1.9476 0.2223  0.0419  0.2418  52  ASN B CA  
2457 C C   . ASN B 45  ? 1.1500 1.6916 2.0174 0.2219  0.0490  0.2652  52  ASN B C   
2458 O O   . ASN B 45  ? 1.2048 1.7698 2.1556 0.2287  0.0520  0.2954  52  ASN B O   
2459 C CB  . ASN B 45  ? 1.2404 1.7449 2.0340 0.2424  0.0823  0.2405  52  ASN B CB  
2460 C CG  . ASN B 45  ? 1.3311 1.8206 2.0974 0.2553  0.1287  0.2232  52  ASN B CG  
2461 O OD1 . ASN B 45  ? 1.5590 2.0400 2.2831 0.2488  0.1306  0.2060  52  ASN B OD1 
2462 N ND2 . ASN B 45  ? 1.3526 1.8352 2.1384 0.2750  0.1658  0.2271  52  ASN B ND2 
2463 N N   . CYS B 46  ? 1.2009 1.7398 2.0454 0.2143  0.0523  0.2534  53  CYS B N   
2464 C CA  . CYS B 46  ? 1.2349 1.7958 2.1457 0.2168  0.0706  0.2734  53  CYS B CA  
2465 C C   . CYS B 46  ? 1.3925 1.9352 2.2446 0.2242  0.1086  0.2515  53  CYS B C   
2466 O O   . CYS B 46  ? 1.2128 1.7417 2.0053 0.2116  0.0925  0.2292  53  CYS B O   
2467 C CB  . CYS B 46  ? 1.1067 1.6860 2.0633 0.1963  0.0240  0.2872  53  CYS B CB  
2468 S SG  . CYS B 46  ? 0.9861 1.5653 1.9452 0.1799  -0.0441 0.2926  53  CYS B SG  
2469 N N   . ILE B 47  ? 1.6346 2.1755 2.5034 0.2460  0.1587  0.2591  54  ILE B N   
2470 C CA  . ILE B 47  ? 1.7107 2.2270 2.5122 0.2584  0.1970  0.2371  54  ILE B CA  
2471 C C   . ILE B 47  ? 1.7709 2.3001 2.6044 0.2619  0.2191  0.2527  54  ILE B C   
2472 O O   . ILE B 47  ? 1.8021 2.3173 2.6134 0.2824  0.2649  0.2516  54  ILE B O   
2473 C CB  . ILE B 47  ? 1.7234 2.2190 2.5051 0.2831  0.2389  0.2313  54  ILE B CB  
2474 C CG1 . ILE B 47  ? 1.8970 2.3553 2.5843 0.2928  0.2609  0.1974  54  ILE B CG1 
2475 C CG2 . ILE B 47  ? 1.8892 2.3998 2.7506 0.3054  0.2811  0.2650  54  ILE B CG2 
2476 C CD1 . ILE B 47  ? 1.9291 2.3609 2.5941 0.3178  0.3001  0.1893  54  ILE B CD1 
2477 N N   . GLU B 48  ? 1.7636 2.3153 2.6430 0.2423  0.1850  0.2659  55  GLU B N   
2478 C CA  . GLU B 48  ? 1.6847 2.2567 2.6265 0.2441  0.2019  0.2908  55  GLU B CA  
2479 C C   . GLU B 48  ? 1.6208 2.1751 2.4950 0.2457  0.2206  0.2716  55  GLU B C   
2480 O O   . GLU B 48  ? 1.7610 2.3143 2.6462 0.2648  0.2659  0.2852  55  GLU B O   
2481 C CB  . GLU B 48  ? 1.6313 2.2318 2.6535 0.2213  0.1535  0.3113  55  GLU B CB  
2482 C CG  . GLU B 48  ? 1.5538 2.1761 2.6598 0.2206  0.1336  0.3378  55  GLU B CG  
2483 C CD  . GLU B 48  ? 1.7147 2.3617 2.9010 0.1980  0.0805  0.3575  55  GLU B CD  
2484 O OE1 . GLU B 48  ? 1.7085 2.3443 2.8487 0.1773  0.0371  0.3364  55  GLU B OE1 
2485 O OE2 . GLU B 48  ? 1.7131 2.3886 3.0107 0.2014  0.0814  0.3945  55  GLU B OE2 
2486 N N   . HIS B 49  ? 1.3305 1.8697 2.1355 0.2275  0.1873  0.2424  56  HIS B N   
2487 C CA  . HIS B 49  ? 1.3331 1.8582 2.0798 0.2247  0.1959  0.2252  56  HIS B CA  
2488 C C   . HIS B 49  ? 1.3472 1.8373 1.9898 0.2361  0.2157  0.1924  56  HIS B C   
2489 O O   . HIS B 49  ? 1.3507 1.8277 1.9390 0.2299  0.2120  0.1747  56  HIS B O   
2490 C CB  . HIS B 49  ? 1.3352 1.8653 2.0796 0.1971  0.1466  0.2160  56  HIS B CB  
2491 C CG  . HIS B 49  ? 1.3155 1.8751 2.1581 0.1853  0.1257  0.2454  56  HIS B CG  
2492 N ND1 . HIS B 49  ? 1.3803 1.9555 2.2829 0.1748  0.0896  0.2597  56  HIS B ND1 
2493 C CD2 . HIS B 49  ? 1.2593 1.8345 2.1539 0.1818  0.1333  0.2636  56  HIS B CD2 
2494 C CE1 . HIS B 49  ? 1.4038 2.0027 2.3939 0.1646  0.0731  0.2847  56  HIS B CE1 
2495 N NE2 . HIS B 49  ? 1.3200 1.9200 2.3095 0.1684  0.1004  0.2879  56  HIS B NE2 
2496 N N   . ASN B 50  ? 1.3580 1.8325 1.9779 0.2522  0.2348  0.1852  57  ASN B N   
2497 C CA  . ASN B 50  ? 1.3789 1.8180 1.9061 0.2599  0.2432  0.1518  57  ASN B CA  
2498 C C   . ASN B 50  ? 1.3722 1.7901 1.8425 0.2747  0.2740  0.1418  57  ASN B C   
2499 O O   . ASN B 50  ? 1.3940 1.7875 1.7907 0.2710  0.2642  0.1135  57  ASN B O   
2500 C CB  . ASN B 50  ? 1.4399 1.8649 1.9633 0.2757  0.2591  0.1479  57  ASN B CB  
2501 C CG  . ASN B 50  ? 1.4760 1.9111 2.0246 0.2611  0.2243  0.1481  57  ASN B CG  
2502 O OD1 . ASN B 50  ? 1.5974 2.0569 2.1940 0.2443  0.1941  0.1636  57  ASN B OD1 
2503 N ND2 . ASN B 50  ? 1.4532 1.8668 1.9681 0.2682  0.2273  0.1311  57  ASN B ND2 
2504 N N   . GLU B 51  ? 1.4320 1.8590 1.9387 0.2922  0.3106  0.1669  58  GLU B N   
2505 C CA  . GLU B 51  ? 1.4498 1.8573 1.9042 0.3089  0.3422  0.1635  58  GLU B CA  
2506 C C   . GLU B 51  ? 1.3520 1.7671 1.7899 0.2900  0.3195  0.1576  58  GLU B C   
2507 O O   . GLU B 51  ? 1.3642 1.7542 1.7264 0.2942  0.3226  0.1366  58  GLU B O   
2508 C CB  . GLU B 51  ? 1.4852 1.9018 1.9907 0.3340  0.3912  0.1981  58  GLU B CB  
2509 C CG  . GLU B 51  ? 1.4822 1.8835 1.9930 0.3590  0.4246  0.2037  58  GLU B CG  
2510 C CD  . GLU B 51  ? 1.5309 1.9312 2.0738 0.3895  0.4819  0.2359  58  GLU B CD  
2511 O OE1 . GLU B 51  ? 1.5097 1.9451 2.1421 0.3852  0.4891  0.2714  58  GLU B OE1 
2512 O OE2 . GLU B 51  ? 1.5850 1.9474 2.0658 0.4189  0.5205  0.2268  58  GLU B OE2 
2513 N N   . ALA B 52  ? 1.2171 1.6645 1.7266 0.2694  0.2947  0.1759  59  ALA B N   
2514 C CA  . ALA B 52  ? 1.1072 1.5623 1.6113 0.2501  0.2716  0.1718  59  ALA B CA  
2515 C C   . ALA B 52  ? 1.1607 1.6005 1.6054 0.2301  0.2325  0.1392  59  ALA B C   
2516 O O   . ALA B 52  ? 1.2668 1.6970 1.6692 0.2231  0.2257  0.1263  59  ALA B O   
2517 C CB  . ALA B 52  ? 1.0347 1.5246 1.6364 0.2349  0.2552  0.2005  59  ALA B CB  
2518 N N   . LEU B 53  ? 1.1186 1.5561 1.5637 0.2222  0.2093  0.1289  60  LEU B N   
2519 C CA  . LEU B 53  ? 1.0183 1.4380 1.4071 0.2072  0.1785  0.1003  60  LEU B CA  
2520 C C   . LEU B 53  ? 1.0043 1.3930 1.3143 0.2184  0.1923  0.0749  60  LEU B C   
2521 O O   . LEU B 53  ? 0.9967 1.3733 1.2634 0.2070  0.1753  0.0567  60  LEU B O   
2522 C CB  . LEU B 53  ? 1.0031 1.4254 1.4101 0.2008  0.1564  0.0987  60  LEU B CB  
2523 C CG  . LEU B 53  ? 0.9761 1.4227 1.4479 0.1852  0.1271  0.1177  60  LEU B CG  
2524 C CD1 . LEU B 53  ? 0.9498 1.3986 1.4415 0.1868  0.1149  0.1218  60  LEU B CD1 
2525 C CD2 . LEU B 53  ? 0.9256 1.3680 1.3762 0.1637  0.0928  0.1064  60  LEU B CD2 
2526 N N   . LEU B 54  ? 1.0088 1.3828 1.3019 0.2406  0.2215  0.0738  61  LEU B N   
2527 C CA  . LEU B 54  ? 1.0700 1.4096 1.2869 0.2532  0.2320  0.0490  61  LEU B CA  
2528 C C   . LEU B 54  ? 1.1146 1.4463 1.2946 0.2591  0.2451  0.0487  61  LEU B C   
2529 O O   . LEU B 54  ? 1.0616 1.3712 1.1831 0.2565  0.2336  0.0266  61  LEU B O   
2530 C CB  . LEU B 54  ? 1.0971 1.4172 1.3017 0.2770  0.2593  0.0468  61  LEU B CB  
2531 C CG  . LEU B 54  ? 1.1630 1.4409 1.2889 0.2916  0.2659  0.0185  61  LEU B CG  
2532 C CD1 . LEU B 54  ? 1.1368 1.4009 1.2345 0.2748  0.2319  -0.0077 61  LEU B CD1 
2533 C CD2 . LEU B 54  ? 1.2316 1.4906 1.3549 0.3162  0.2952  0.0200  61  LEU B CD2 
2534 N N   . GLU B 55  ? 1.1577 1.5074 1.3761 0.2677  0.2691  0.0752  62  GLU B N   
2535 C CA  . GLU B 55  ? 1.2087 1.5544 1.4000 0.2738  0.2835  0.0806  62  GLU B CA  
2536 C C   . GLU B 55  ? 1.1081 1.4660 1.3033 0.2482  0.2521  0.0746  62  GLU B C   
2537 O O   . GLU B 55  ? 1.0983 1.4424 1.2461 0.2491  0.2513  0.0650  62  GLU B O   
2538 C CB  . GLU B 55  ? 1.2341 1.5976 1.4769 0.2903  0.3206  0.1151  62  GLU B CB  
2539 C CG  . GLU B 55  ? 1.2813 1.6318 1.4828 0.3074  0.3484  0.1229  62  GLU B CG  
2540 C CD  . GLU B 55  ? 1.3663 1.7430 1.6123 0.2928  0.3426  0.1419  62  GLU B CD  
2541 O OE1 . GLU B 55  ? 1.4762 1.8844 1.8018 0.2731  0.3249  0.1574  62  GLU B OE1 
2542 O OE2 . GLU B 55  ? 1.4242 1.7873 1.6236 0.3023  0.3557  0.1419  62  GLU B OE2 
2543 N N   . GLU B 56  ? 1.0013 1.3820 1.2504 0.2268  0.2258  0.0804  63  GLU B N   
2544 C CA  . GLU B 56  ? 0.9620 1.3480 1.2100 0.2027  0.1941  0.0714  63  GLU B CA  
2545 C C   . GLU B 56  ? 0.9581 1.3200 1.1461 0.1954  0.1734  0.0418  63  GLU B C   
2546 O O   . GLU B 56  ? 0.8728 1.2283 1.0351 0.1846  0.1602  0.0318  63  GLU B O   
2547 C CB  . GLU B 56  ? 0.9354 1.3452 1.2499 0.1848  0.1705  0.0846  63  GLU B CB  
2548 C CG  . GLU B 56  ? 0.9629 1.3783 1.2871 0.1629  0.1434  0.0818  63  GLU B CG  
2549 C CD  . GLU B 56  ? 1.0309 1.4697 1.4303 0.1506  0.1259  0.1018  63  GLU B CD  
2550 O OE1 . GLU B 56  ? 1.0514 1.4886 1.4575 0.1373  0.0956  0.0951  63  GLU B OE1 
2551 O OE2 . GLU B 56  ? 1.0057 1.4632 1.4598 0.1553  0.1422  0.1256  63  GLU B OE2 
2552 N N   . ALA B 57  ? 0.9292 1.2782 1.1016 0.2016  0.1719  0.0300  64  ALA B N   
2553 C CA  . ALA B 57  ? 0.8962 1.2204 1.0181 0.1984  0.1570  0.0042  64  ALA B CA  
2554 C C   . ALA B 57  ? 0.9432 1.2438 1.0077 0.2103  0.1669  -0.0093 64  ALA B C   
2555 O O   . ALA B 57  ? 0.9242 1.2105 0.9572 0.2017  0.1494  -0.0260 64  ALA B O   
2556 C CB  . ALA B 57  ? 0.9151 1.2305 1.0404 0.2041  0.1556  -0.0030 64  ALA B CB  
2557 N N   . LYS B 58  ? 1.0652 1.3592 1.1154 0.2316  0.1948  -0.0010 65  LYS B N   
2558 C CA  . LYS B 58  ? 1.0778 1.3463 1.0663 0.2462  0.2044  -0.0111 65  LYS B CA  
2559 C C   . LYS B 58  ? 1.0902 1.3684 1.0752 0.2353  0.1968  -0.0054 65  LYS B C   
2560 O O   . LYS B 58  ? 1.1804 1.4398 1.1206 0.2336  0.1833  -0.0211 65  LYS B O   
2561 C CB  . LYS B 58  ? 1.1117 1.3681 1.0814 0.2748  0.2411  0.0002  65  LYS B CB  
2562 C CG  . LYS B 58  ? 1.1256 1.3565 1.0719 0.2909  0.2496  -0.0135 65  LYS B CG  
2563 C CD  . LYS B 58  ? 1.1668 1.3872 1.1024 0.3203  0.2914  0.0024  65  LYS B CD  
2564 C CE  . LYS B 58  ? 1.2020 1.3946 1.1162 0.3371  0.3018  -0.0113 65  LYS B CE  
2565 N NZ  . LYS B 58  ? 1.2557 1.4344 1.1582 0.3686  0.3477  0.0057  65  LYS B NZ  
2566 N N   . MET B 59  ? 1.0849 1.3920 1.1221 0.2275  0.2038  0.0174  66  MET B N   
2567 C CA  . MET B 59  ? 1.1243 1.4427 1.1688 0.2165  0.1986  0.0256  66  MET B CA  
2568 C C   . MET B 59  ? 1.0542 1.3694 1.0909 0.1943  0.1670  0.0087  66  MET B C   
2569 O O   . MET B 59  ? 1.0326 1.3406 1.0435 0.1910  0.1611  0.0043  66  MET B O   
2570 C CB  . MET B 59  ? 1.2321 1.5813 1.3462 0.2109  0.2089  0.0531  66  MET B CB  
2571 C CG  . MET B 59  ? 1.2724 1.6262 1.3989 0.2344  0.2471  0.0770  66  MET B CG  
2572 S SD  . MET B 59  ? 1.3666 1.7573 1.5862 0.2267  0.2583  0.1126  66  MET B SD  
2573 C CE  . MET B 59  ? 1.2907 1.7017 1.5788 0.2096  0.2347  0.1154  66  MET B CE  
2574 N N   . MET B 60  ? 1.0315 1.3515 1.0920 0.1807  0.1487  0.0020  67  MET B N   
2575 C CA  . MET B 60  ? 0.9731 1.2856 1.0241 0.1630  0.1236  -0.0129 67  MET B CA  
2576 C C   . MET B 60  ? 0.9367 1.2233 0.9410 0.1679  0.1154  -0.0339 67  MET B C   
2577 O O   . MET B 60  ? 0.9944 1.2735 0.9886 0.1569  0.1003  -0.0427 67  MET B O   
2578 C CB  . MET B 60  ? 0.8982 1.2202 0.9834 0.1498  0.1085  -0.0113 67  MET B CB  
2579 C CG  . MET B 60  ? 0.9163 1.2328 1.0030 0.1568  0.1086  -0.0167 67  MET B CG  
2580 S SD  . MET B 60  ? 0.9170 1.2405 1.0342 0.1444  0.0896  -0.0136 67  MET B SD  
2581 C CE  . MET B 60  ? 0.8637 1.2122 1.0319 0.1354  0.0842  0.0075  67  MET B CE  
2582 N N   . ASN B 61  ? 0.9736 1.2449 0.9531 0.1846  0.1248  -0.0412 68  ASN B N   
2583 C CA  . ASN B 61  ? 0.9808 1.2237 0.9163 0.1907  0.1141  -0.0617 68  ASN B CA  
2584 C C   . ASN B 61  ? 0.9950 1.2255 0.8903 0.1979  0.1144  -0.0636 68  ASN B C   
2585 O O   . ASN B 61  ? 0.9833 1.1946 0.8530 0.1956  0.0960  -0.0786 68  ASN B O   
2586 C CB  . ASN B 61  ? 1.0148 1.2399 0.9327 0.2076  0.1231  -0.0708 68  ASN B CB  
2587 C CG  . ASN B 61  ? 1.0036 1.1990 0.8914 0.2089  0.1039  -0.0941 68  ASN B CG  
2588 O OD1 . ASN B 61  ? 1.0669 1.2363 0.9082 0.2231  0.1034  -0.1055 68  ASN B OD1 
2589 N ND2 . ASN B 61  ? 0.9932 1.1903 0.9077 0.1944  0.0872  -0.1004 68  ASN B ND2 
2590 N N   . ARG B 62  ? 1.0352 1.2760 0.9280 0.2078  0.1351  -0.0467 69  ARG B N   
2591 C CA  . ARG B 62  ? 1.0720 1.3031 0.9270 0.2163  0.1385  -0.0435 69  ARG B CA  
2592 C C   . ARG B 62  ? 0.9997 1.2400 0.8689 0.1975  0.1206  -0.0424 69  ARG B C   
2593 O O   . ARG B 62  ? 1.0362 1.2643 0.8717 0.2027  0.1152  -0.0440 69  ARG B O   
2594 C CB  . ARG B 62  ? 1.0873 1.3291 0.9442 0.2332  0.1710  -0.0203 69  ARG B CB  
2595 C CG  . ARG B 62  ? 1.1817 1.4029 1.0021 0.2602  0.1948  -0.0206 69  ARG B CG  
2596 C CD  . ARG B 62  ? 1.2162 1.4491 1.0471 0.2780  0.2321  0.0073  69  ARG B CD  
2597 N NE  . ARG B 62  ? 1.2532 1.4639 1.0494 0.3060  0.2598  0.0089  69  ARG B NE  
2598 C CZ  . ARG B 62  ? 1.2835 1.4987 1.0869 0.3274  0.2994  0.0345  69  ARG B CZ  
2599 N NH1 . ARG B 62  ? 1.2611 1.5052 1.1122 0.3233  0.3153  0.0625  69  ARG B NH1 
2600 N NH2 . ARG B 62  ? 1.3395 1.5279 1.1040 0.3547  0.3256  0.0332  69  ARG B NH2 
2601 N N   . LEU B 63  ? 1.0092 1.2685 0.9251 0.1777  0.1122  -0.0390 70  LEU B N   
2602 C CA  . LEU B 63  ? 0.9877 1.2533 0.9200 0.1603  0.0986  -0.0377 70  LEU B CA  
2603 C C   . LEU B 63  ? 0.9337 1.1823 0.8571 0.1519  0.0764  -0.0551 70  LEU B C   
2604 O O   . LEU B 63  ? 0.8780 1.1280 0.8247 0.1408  0.0686  -0.0601 70  LEU B O   
2605 C CB  . LEU B 63  ? 0.9687 1.2557 0.9483 0.1454  0.1007  -0.0266 70  LEU B CB  
2606 C CG  . LEU B 63  ? 0.9835 1.2898 0.9888 0.1510  0.1201  -0.0064 70  LEU B CG  
2607 C CD1 . LEU B 63  ? 1.0022 1.3248 1.0548 0.1373  0.1147  0.0005  70  LEU B CD1 
2608 C CD2 . LEU B 63  ? 0.9720 1.2831 0.9746 0.1522  0.1279  0.0056  70  LEU B CD2 
2609 N N   . ARG B 64  ? 0.9624 1.1938 0.8528 0.1586  0.0663  -0.0625 71  ARG B N   
2610 C CA  . ARG B 64  ? 0.9578 1.1712 0.8440 0.1531  0.0434  -0.0774 71  ARG B CA  
2611 C C   . ARG B 64  ? 0.8862 1.1019 0.7818 0.1433  0.0333  -0.0718 71  ARG B C   
2612 O O   . ARG B 64  ? 0.9559 1.1697 0.8275 0.1506  0.0342  -0.0655 71  ARG B O   
2613 C CB  . ARG B 64  ? 1.0407 1.2278 0.8820 0.1693  0.0336  -0.0918 71  ARG B CB  
2614 C CG  . ARG B 64  ? 1.1139 1.2937 0.9464 0.1800  0.0435  -0.0994 71  ARG B CG  
2615 C CD  . ARG B 64  ? 1.1472 1.3180 1.0041 0.1718  0.0285  -0.1128 71  ARG B CD  
2616 N NE  . ARG B 64  ? 1.1851 1.3404 1.0248 0.1850  0.0337  -0.1235 71  ARG B NE  
2617 C CZ  . ARG B 64  ? 1.2079 1.3547 1.0703 0.1809  0.0247  -0.1340 71  ARG B CZ  
2618 N NH1 . ARG B 64  ? 1.1772 1.3281 1.0779 0.1654  0.0114  -0.1343 71  ARG B NH1 
2619 N NH2 . ARG B 64  ? 1.2368 1.3689 1.0837 0.1941  0.0316  -0.1429 71  ARG B NH2 
2620 N N   . HIS B 65  ? 0.8240 1.0426 0.7541 0.1283  0.0261  -0.0722 72  HIS B N   
2621 C CA  . HIS B 65  ? 0.7792 0.9988 0.7261 0.1187  0.0186  -0.0659 72  HIS B CA  
2622 C C   . HIS B 65  ? 0.7476 0.9616 0.7288 0.1071  0.0119  -0.0691 72  HIS B C   
2623 O O   . HIS B 65  ? 0.7582 0.9742 0.7524 0.1036  0.0197  -0.0706 72  HIS B O   
2624 C CB  . HIS B 65  ? 0.7499 0.9869 0.7082 0.1136  0.0347  -0.0509 72  HIS B CB  
2625 C CG  . HIS B 65  ? 0.7473 0.9850 0.7155 0.1082  0.0301  -0.0425 72  HIS B CG  
2626 N ND1 . HIS B 65  ? 0.7606 1.0025 0.7598 0.0955  0.0354  -0.0360 72  HIS B ND1 
2627 C CD2 . HIS B 65  ? 0.7857 1.0187 0.7352 0.1148  0.0208  -0.0388 72  HIS B CD2 
2628 C CE1 . HIS B 65  ? 0.7545 0.9963 0.7600 0.0938  0.0310  -0.0279 72  HIS B CE1 
2629 N NE2 . HIS B 65  ? 0.7725 1.0102 0.7488 0.1051  0.0209  -0.0288 72  HIS B NE2 
2630 N N   . SER B 66  ? 0.7506 0.9575 0.7486 0.1021  -0.0010 -0.0674 73  SER B N   
2631 C CA  . SER B 66  ? 0.6990 0.8989 0.7360 0.0933  -0.0040 -0.0667 73  SER B CA  
2632 C C   . SER B 66  ? 0.6637 0.8684 0.7186 0.0856  0.0157  -0.0587 73  SER B C   
2633 O O   . SER B 66  ? 0.6355 0.8316 0.7128 0.0826  0.0197  -0.0584 73  SER B O   
2634 C CB  . SER B 66  ? 0.7447 0.9387 0.8048 0.0896  -0.0198 -0.0618 73  SER B CB  
2635 O OG  . SER B 66  ? 0.7588 0.9621 0.8247 0.0852  -0.0103 -0.0490 73  SER B OG  
2636 N N   . ARG B 67  ? 0.6440 0.8595 0.6881 0.0834  0.0276  -0.0519 74  ARG B N   
2637 C CA  . ARG B 67  ? 0.6376 0.8528 0.6886 0.0768  0.0427  -0.0470 74  ARG B CA  
2638 C C   . ARG B 67  ? 0.6384 0.8609 0.6737 0.0784  0.0483  -0.0497 74  ARG B C   
2639 O O   . ARG B 67  ? 0.6303 0.8516 0.6661 0.0729  0.0557  -0.0464 74  ARG B O   
2640 C CB  . ARG B 67  ? 0.6521 0.8703 0.7114 0.0712  0.0495  -0.0374 74  ARG B CB  
2641 C CG  . ARG B 67  ? 0.6435 0.8595 0.7208 0.0704  0.0424  -0.0314 74  ARG B CG  
2642 C CD  . ARG B 67  ? 0.6964 0.8990 0.8012 0.0689  0.0397  -0.0310 74  ARG B CD  
2643 N NE  . ARG B 67  ? 0.7729 0.9751 0.9027 0.0676  0.0290  -0.0235 74  ARG B NE  
2644 C CZ  . ARG B 67  ? 0.7571 0.9511 0.9215 0.0669  0.0191  -0.0209 74  ARG B CZ  
2645 N NH1 . ARG B 67  ? 0.7392 0.9237 0.9186 0.0679  0.0217  -0.0246 74  ARG B NH1 
2646 N NH2 . ARG B 67  ? 0.7397 0.9354 0.9289 0.0653  0.0057  -0.0125 74  ARG B NH2 
2647 N N   . VAL B 68  ? 0.6683 0.8957 0.6911 0.0860  0.0437  -0.0556 75  VAL B N   
2648 C CA  . VAL B 68  ? 0.6955 0.9313 0.7116 0.0884  0.0485  -0.0560 75  VAL B CA  
2649 C C   . VAL B 68  ? 0.6965 0.9248 0.7116 0.0935  0.0447  -0.0638 75  VAL B C   
2650 O O   . VAL B 68  ? 0.7102 0.9317 0.7215 0.0993  0.0373  -0.0708 75  VAL B O   
2651 C CB  . VAL B 68  ? 0.7385 0.9888 0.7446 0.0953  0.0528  -0.0514 75  VAL B CB  
2652 C CG1 . VAL B 68  ? 0.7559 1.0168 0.7664 0.0981  0.0582  -0.0488 75  VAL B CG1 
2653 C CG2 . VAL B 68  ? 0.7418 0.9995 0.7550 0.0901  0.0577  -0.0415 75  VAL B CG2 
2654 N N   . VAL B 69  ? 0.6716 0.8996 0.6894 0.0917  0.0480  -0.0627 76  VAL B N   
2655 C CA  . VAL B 69  ? 0.7040 0.9258 0.7240 0.0965  0.0466  -0.0672 76  VAL B CA  
2656 C C   . VAL B 69  ? 0.7537 0.9837 0.7668 0.1060  0.0461  -0.0713 76  VAL B C   
2657 O O   . VAL B 69  ? 0.8474 1.0911 0.8583 0.1084  0.0510  -0.0660 76  VAL B O   
2658 C CB  . VAL B 69  ? 0.7338 0.9525 0.7530 0.0937  0.0491  -0.0629 76  VAL B CB  
2659 C CG1 . VAL B 69  ? 0.7771 0.9919 0.8000 0.1001  0.0488  -0.0649 76  VAL B CG1 
2660 C CG2 . VAL B 69  ? 0.7255 0.9274 0.7422 0.0881  0.0532  -0.0599 76  VAL B CG2 
2661 N N   . LYS B 70  ? 0.7910 1.0103 0.8030 0.1121  0.0407  -0.0802 77  LYS B N   
2662 C CA  . LYS B 70  ? 0.8304 1.0489 0.8301 0.1235  0.0412  -0.0868 77  LYS B CA  
2663 C C   . LYS B 70  ? 0.7554 0.9788 0.7652 0.1269  0.0471  -0.0842 77  LYS B C   
2664 O O   . LYS B 70  ? 0.7460 0.9638 0.7698 0.1232  0.0456  -0.0831 77  LYS B O   
2665 C CB  . LYS B 70  ? 0.9362 1.1356 0.9310 0.1283  0.0288  -0.0997 77  LYS B CB  
2666 C CG  . LYS B 70  ? 1.1251 1.3188 1.1059 0.1276  0.0190  -0.1024 77  LYS B CG  
2667 C CD  . LYS B 70  ? 1.1929 1.3665 1.1810 0.1275  -0.0006 -0.1134 77  LYS B CD  
2668 C CE  . LYS B 70  ? 1.1645 1.3344 1.1412 0.1258  -0.0130 -0.1128 77  LYS B CE  
2669 N NZ  . LYS B 70  ? 1.2019 1.3557 1.2027 0.1213  -0.0354 -0.1190 77  LYS B NZ  
2670 N N   . LEU B 71  ? 0.7282 0.9619 0.7327 0.1349  0.0555  -0.0807 78  LEU B N   
2671 C CA  . LEU B 71  ? 0.7487 0.9857 0.7643 0.1416  0.0609  -0.0789 78  LEU B CA  
2672 C C   . LEU B 71  ? 0.7885 1.0062 0.7937 0.1513  0.0582  -0.0930 78  LEU B C   
2673 O O   . LEU B 71  ? 0.8169 1.0245 0.7971 0.1606  0.0591  -0.1009 78  LEU B O   
2674 C CB  . LEU B 71  ? 0.7071 0.9611 0.7275 0.1484  0.0731  -0.0682 78  LEU B CB  
2675 C CG  . LEU B 71  ? 0.7337 0.9942 0.7736 0.1553  0.0795  -0.0627 78  LEU B CG  
2676 C CD1 . LEU B 71  ? 0.7009 0.9746 0.7653 0.1451  0.0721  -0.0510 78  LEU B CD1 
2677 C CD2 . LEU B 71  ? 0.7349 1.0031 0.7758 0.1693  0.0968  -0.0556 78  LEU B CD2 
2678 N N   . LEU B 72  ? 0.8253 1.0349 0.8473 0.1504  0.0545  -0.0960 79  LEU B N   
2679 C CA  . LEU B 72  ? 0.8498 1.0385 0.8697 0.1582  0.0492  -0.1102 79  LEU B CA  
2680 C C   . LEU B 72  ? 0.8323 1.0202 0.8513 0.1712  0.0604  -0.1112 79  LEU B C   
2681 O O   . LEU B 72  ? 0.8686 1.0367 0.8690 0.1821  0.0593  -0.1250 79  LEU B O   
2682 C CB  . LEU B 72  ? 0.8150 0.9938 0.8616 0.1513  0.0414  -0.1111 79  LEU B CB  
2683 C CG  . LEU B 72  ? 0.7780 0.9534 0.8310 0.1407  0.0328  -0.1097 79  LEU B CG  
2684 C CD1 . LEU B 72  ? 0.7711 0.9398 0.8559 0.1361  0.0337  -0.1032 79  LEU B CD1 
2685 C CD2 . LEU B 72  ? 0.8084 0.9684 0.8486 0.1422  0.0181  -0.1232 79  LEU B CD2 
2686 N N   . GLY B 73  ? 0.8093 1.0160 0.8481 0.1705  0.0696  -0.0967 80  GLY B N   
2687 C CA  . GLY B 73  ? 0.8209 1.0310 0.8676 0.1826  0.0824  -0.0929 80  GLY B CA  
2688 C C   . GLY B 73  ? 0.8144 1.0500 0.8864 0.1799  0.0887  -0.0733 80  GLY B C   
2689 O O   . GLY B 73  ? 0.8195 1.0676 0.8987 0.1682  0.0809  -0.0641 80  GLY B O   
2690 N N   . VAL B 74  ? 0.8546 1.0953 0.9405 0.1916  0.1019  -0.0671 81  VAL B N   
2691 C CA  . VAL B 74  ? 0.8916 1.1561 1.0117 0.1906  0.1053  -0.0470 81  VAL B CA  
2692 C C   . VAL B 74  ? 0.8782 1.1389 1.0205 0.1992  0.1107  -0.0442 81  VAL B C   
2693 O O   . VAL B 74  ? 0.8725 1.1138 1.0037 0.2111  0.1204  -0.0567 81  VAL B O   
2694 C CB  . VAL B 74  ? 0.9640 1.2450 1.0942 0.1975  0.1201  -0.0341 81  VAL B CB  
2695 C CG1 . VAL B 74  ? 0.9461 1.2337 1.0618 0.1880  0.1146  -0.0333 81  VAL B CG1 
2696 C CG2 . VAL B 74  ? 1.0219 1.2877 1.1353 0.2173  0.1424  -0.0405 81  VAL B CG2 
2697 N N   . ILE B 75  ? 0.8526 1.1289 1.0234 0.1937  0.1028  -0.0285 82  ILE B N   
2698 C CA  . ILE B 75  ? 0.8634 1.1418 1.0630 0.2024  0.1087  -0.0198 82  ILE B CA  
2699 C C   . ILE B 75  ? 0.8714 1.1750 1.1057 0.2058  0.1146  0.0008  82  ILE B C   
2700 O O   . ILE B 75  ? 0.8086 1.1293 1.0573 0.1953  0.0993  0.0140  82  ILE B O   
2701 C CB  . ILE B 75  ? 0.8304 1.1059 1.0367 0.1957  0.0947  -0.0145 82  ILE B CB  
2702 C CG1 . ILE B 75  ? 0.8022 1.0545 0.9844 0.1919  0.0909  -0.0314 82  ILE B CG1 
2703 C CG2 . ILE B 75  ? 0.8787 1.1574 1.1175 0.2057  0.1015  -0.0034 82  ILE B CG2 
2704 C CD1 . ILE B 75  ? 0.8088 1.0564 0.9920 0.1861  0.0812  -0.0233 82  ILE B CD1 
2705 N N   . ILE B 76  ? 0.9191 1.2218 1.1670 0.2213  0.1368  0.0035  83  ILE B N   
2706 C CA  . ILE B 76  ? 0.9221 1.2483 1.2142 0.2280  0.1486  0.0263  83  ILE B CA  
2707 C C   . ILE B 76  ? 0.9614 1.2862 1.2849 0.2400  0.1594  0.0343  83  ILE B C   
2708 O O   . ILE B 76  ? 0.9881 1.2956 1.3033 0.2565  0.1831  0.0263  83  ILE B O   
2709 C CB  . ILE B 76  ? 0.9657 1.2891 1.2458 0.2398  0.1733  0.0257  83  ILE B CB  
2710 C CG1 . ILE B 76  ? 0.9647 1.2888 1.2145 0.2285  0.1633  0.0185  83  ILE B CG1 
2711 C CG2 . ILE B 76  ? 1.0116 1.3593 1.3485 0.2491  0.1911  0.0534  83  ILE B CG2 
2712 C CD1 . ILE B 76  ? 0.9711 1.3209 1.2514 0.2113  0.1422  0.0343  83  ILE B CD1 
2713 N N   . GLU B 77  ? 0.9507 1.2907 1.3059 0.2325  0.1411  0.0495  84  GLU B N   
2714 C CA  . GLU B 77  ? 0.9560 1.2986 1.3477 0.2423  0.1478  0.0616  84  GLU B CA  
2715 C C   . GLU B 77  ? 0.9544 1.3279 1.4042 0.2393  0.1365  0.0916  84  GLU B C   
2716 O O   . GLU B 77  ? 0.9094 1.2999 1.3692 0.2278  0.1192  0.1009  84  GLU B O   
2717 C CB  . GLU B 77  ? 0.9497 1.2758 1.3216 0.2379  0.1344  0.0517  84  GLU B CB  
2718 C CG  . GLU B 77  ? 0.9545 1.2494 1.2854 0.2420  0.1443  0.0241  84  GLU B CG  
2719 C CD  . GLU B 77  ? 0.9392 1.2188 1.2588 0.2366  0.1321  0.0171  84  GLU B CD  
2720 O OE1 . GLU B 77  ? 0.8780 1.1676 1.2044 0.2288  0.1154  0.0312  84  GLU B OE1 
2721 O OE2 . GLU B 77  ? 0.9682 1.2227 1.2712 0.2412  0.1393  -0.0026 84  GLU B OE2 
2722 N N   . GLU B 78  ? 0.9974 1.3769 1.4888 0.2499  0.1451  0.1067  85  GLU B N   
2723 C CA  . GLU B 78  ? 0.9663 1.3750 1.5221 0.2485  0.1323  0.1377  85  GLU B CA  
2724 C C   . GLU B 78  ? 0.9185 1.3345 1.4660 0.2319  0.0909  0.1447  85  GLU B C   
2725 O O   . GLU B 78  ? 0.9125 1.3172 1.4414 0.2314  0.0793  0.1427  85  GLU B O   
2726 C CB  . GLU B 78  ? 1.0797 1.4908 1.6810 0.2645  0.1512  0.1524  85  GLU B CB  
2727 C CG  . GLU B 78  ? 1.1200 1.5124 1.7016 0.2674  0.1477  0.1438  85  GLU B CG  
2728 C CD  . GLU B 78  ? 1.1240 1.5089 1.7391 0.2865  0.1781  0.1489  85  GLU B CD  
2729 O OE1 . GLU B 78  ? 1.1307 1.5352 1.8048 0.2958  0.1916  0.1727  85  GLU B OE1 
2730 O OE2 . GLU B 78  ? 1.1357 1.4940 1.7220 0.2923  0.1887  0.1297  85  GLU B OE2 
2731 N N   . GLY B 79  ? 0.8882 1.3197 1.4470 0.2195  0.0697  0.1525  86  GLY B N   
2732 C CA  . GLY B 79  ? 0.9228 1.3547 1.4643 0.2044  0.0282  0.1562  86  GLY B CA  
2733 C C   . GLY B 79  ? 0.9654 1.3717 1.4315 0.1954  0.0174  0.1322  86  GLY B C   
2734 O O   . GLY B 79  ? 0.9958 1.3934 1.4361 0.1880  -0.0119 0.1345  86  GLY B O   
2735 N N   . LYS B 80  ? 1.0058 1.3976 1.4357 0.1971  0.0402  0.1104  87  LYS B N   
2736 C CA  . LYS B 80  ? 1.0811 1.4519 1.4495 0.1874  0.0312  0.0899  87  LYS B CA  
2737 C C   . LYS B 80  ? 1.0346 1.4002 1.3821 0.1868  0.0506  0.0724  87  LYS B C   
2738 O O   . LYS B 80  ? 1.0960 1.4545 1.4417 0.1978  0.0764  0.0633  87  LYS B O   
2739 C CB  . LYS B 80  ? 1.1662 1.5141 1.4993 0.1913  0.0332  0.0811  87  LYS B CB  
2740 C CG  . LYS B 80  ? 1.1925 1.5319 1.5358 0.2044  0.0605  0.0740  87  LYS B CG  
2741 C CD  . LYS B 80  ? 1.2008 1.5213 1.5258 0.2080  0.0598  0.0724  87  LYS B CD  
2742 C CE  . LYS B 80  ? 1.2357 1.5589 1.5987 0.2210  0.0729  0.0835  87  LYS B CE  
2743 N NZ  . LYS B 80  ? 1.2432 1.5474 1.5926 0.2250  0.0750  0.0832  87  LYS B NZ  
2744 N N   . TYR B 81  ? 0.9897 1.3567 1.3202 0.1747  0.0364  0.0683  88  TYR B N   
2745 C CA  . TYR B 81  ? 0.9598 1.3233 1.2700 0.1728  0.0503  0.0549  88  TYR B CA  
2746 C C   . TYR B 81  ? 0.9047 1.2485 1.1632 0.1619  0.0371  0.0387  88  TYR B C   
2747 O O   . TYR B 81  ? 0.8867 1.2295 1.1368 0.1513  0.0137  0.0425  88  TYR B O   
2748 C CB  . TYR B 81  ? 0.9480 1.3338 1.2971 0.1687  0.0485  0.0690  88  TYR B CB  
2749 C CG  . TYR B 81  ? 1.0285 1.4361 1.4400 0.1791  0.0611  0.0909  88  TYR B CG  
2750 C CD1 . TYR B 81  ? 1.0988 1.5075 1.5211 0.1949  0.0963  0.0920  88  TYR B CD1 
2751 C CD2 . TYR B 81  ? 1.0341 1.4589 1.4934 0.1743  0.0376  0.1118  88  TYR B CD2 
2752 C CE1 . TYR B 81  ? 1.0889 1.5162 1.5721 0.2066  0.1129  0.1148  88  TYR B CE1 
2753 C CE2 . TYR B 81  ? 1.0590 1.5058 1.5858 0.1839  0.0495  0.1354  88  TYR B CE2 
2754 C CZ  . TYR B 81  ? 1.0827 1.5313 1.6235 0.2004  0.0897  0.1376  88  TYR B CZ  
2755 O OH  . TYR B 81  ? 1.1459 1.6149 1.7564 0.2116  0.1056  0.1632  88  TYR B OH  
2756 N N   . SER B 82  ? 0.8850 1.2110 1.1109 0.1654  0.0515  0.0210  89  SER B N   
2757 C CA  . SER B 82  ? 0.9102 1.2176 1.0944 0.1570  0.0443  0.0072  89  SER B CA  
2758 C C   . SER B 82  ? 0.8572 1.1597 1.0229 0.1564  0.0562  -0.0065 89  SER B C   
2759 O O   . SER B 82  ? 0.9216 1.2238 1.0913 0.1663  0.0728  -0.0115 89  SER B O   
2760 C CB  . SER B 82  ? 0.8991 1.1873 1.0672 0.1612  0.0468  0.0017  89  SER B CB  
2761 O OG  . SER B 82  ? 1.0363 1.3267 1.2151 0.1631  0.0357  0.0159  89  SER B OG  
2762 N N   . LEU B 83  ? 0.8311 1.1267 0.9731 0.1460  0.0472  -0.0123 90  LEU B N   
2763 C CA  . LEU B 83  ? 0.8135 1.0997 0.9324 0.1442  0.0544  -0.0258 90  LEU B CA  
2764 C C   . LEU B 83  ? 0.8235 1.0881 0.9216 0.1431  0.0532  -0.0361 90  LEU B C   
2765 O O   . LEU B 83  ? 0.8261 1.0826 0.9184 0.1402  0.0458  -0.0311 90  LEU B O   
2766 C CB  . LEU B 83  ? 0.8023 1.0945 0.9156 0.1335  0.0464  -0.0234 90  LEU B CB  
2767 C CG  . LEU B 83  ? 0.7918 1.1065 0.9366 0.1334  0.0472  -0.0100 90  LEU B CG  
2768 C CD1 . LEU B 83  ? 0.8098 1.1280 0.9557 0.1206  0.0338  -0.0066 90  LEU B CD1 
2769 C CD2 . LEU B 83  ? 0.8116 1.1322 0.9605 0.1446  0.0682  -0.0107 90  LEU B CD2 
2770 N N   . VAL B 84  ? 0.8243 1.0780 0.9123 0.1467  0.0603  -0.0489 91  VAL B N   
2771 C CA  . VAL B 84  ? 0.7947 1.0290 0.8760 0.1458  0.0592  -0.0575 91  VAL B CA  
2772 C C   . VAL B 84  ? 0.7587 0.9868 0.8243 0.1401  0.0570  -0.0664 91  VAL B C   
2773 O O   . VAL B 84  ? 0.7523 0.9825 0.8095 0.1439  0.0594  -0.0731 91  VAL B O   
2774 C CB  . VAL B 84  ? 0.8289 1.0528 0.9216 0.1557  0.0646  -0.0654 91  VAL B CB  
2775 C CG1 . VAL B 84  ? 0.8181 1.0229 0.9164 0.1537  0.0618  -0.0717 91  VAL B CG1 
2776 C CG2 . VAL B 84  ? 0.8858 1.1176 0.9979 0.1625  0.0686  -0.0548 91  VAL B CG2 
2777 N N   . MET B 85  ? 0.7994 1.0176 0.8603 0.1330  0.0539  -0.0652 92  MET B N   
2778 C CA  . MET B 85  ? 0.8337 1.0473 0.8848 0.1264  0.0515  -0.0700 92  MET B CA  
2779 C C   . MET B 85  ? 0.8052 1.0016 0.8662 0.1246  0.0518  -0.0717 92  MET B C   
2780 O O   . MET B 85  ? 0.7794 0.9673 0.8518 0.1278  0.0559  -0.0665 92  MET B O   
2781 C CB  . MET B 85  ? 0.9092 1.1304 0.9490 0.1186  0.0497  -0.0630 92  MET B CB  
2782 C CG  . MET B 85  ? 0.9727 1.1917 1.0082 0.1171  0.0472  -0.0538 92  MET B CG  
2783 S SD  . MET B 85  ? 1.1117 1.3255 1.1282 0.1074  0.0416  -0.0501 92  MET B SD  
2784 C CE  . MET B 85  ? 1.2219 1.4120 1.2291 0.1063  0.0507  -0.0521 92  MET B CE  
2785 N N   . GLU B 86  ? 0.8279 1.0197 0.8883 0.1201  0.0482  -0.0766 93  GLU B N   
2786 C CA  . GLU B 86  ? 0.8450 1.0222 0.9255 0.1179  0.0478  -0.0762 93  GLU B CA  
2787 C C   . GLU B 86  ? 0.8400 1.0084 0.9214 0.1156  0.0588  -0.0639 93  GLU B C   
2788 O O   . GLU B 86  ? 0.7773 0.9487 0.8355 0.1133  0.0621  -0.0588 93  GLU B O   
2789 C CB  . GLU B 86  ? 0.9313 1.1066 1.0137 0.1140  0.0382  -0.0832 93  GLU B CB  
2790 C CG  . GLU B 86  ? 0.9689 1.1526 1.0341 0.1080  0.0397  -0.0794 93  GLU B CG  
2791 C CD  . GLU B 86  ? 1.0529 1.2342 1.1209 0.1058  0.0287  -0.0846 93  GLU B CD  
2792 O OE1 . GLU B 86  ? 1.1432 1.3132 1.2346 0.1057  0.0191  -0.0883 93  GLU B OE1 
2793 O OE2 . GLU B 86  ? 1.0551 1.2456 1.1048 0.1041  0.0282  -0.0839 93  GLU B OE2 
2794 N N   . TYR B 87  ? 0.8250 0.9796 0.9338 0.1173  0.0643  -0.0588 94  TYR B N   
2795 C CA  . TYR B 87  ? 0.7888 0.9291 0.8978 0.1200  0.0805  -0.0448 94  TYR B CA  
2796 C C   . TYR B 87  ? 0.7503 0.8827 0.8667 0.1153  0.0866  -0.0399 94  TYR B C   
2797 O O   . TYR B 87  ? 0.6869 0.8200 0.8353 0.1117  0.0798  -0.0424 94  TYR B O   
2798 C CB  . TYR B 87  ? 0.7797 0.9096 0.9216 0.1270  0.0884  -0.0374 94  TYR B CB  
2799 C CG  . TYR B 87  ? 0.7575 0.8688 0.8991 0.1337  0.1102  -0.0196 94  TYR B CG  
2800 C CD1 . TYR B 87  ? 0.7883 0.8910 0.8824 0.1380  0.1187  -0.0130 94  TYR B CD1 
2801 C CD2 . TYR B 87  ? 0.7597 0.8590 0.9482 0.1371  0.1224  -0.0082 94  TYR B CD2 
2802 C CE1 . TYR B 87  ? 0.7995 0.8784 0.8816 0.1477  0.1410  0.0034  94  TYR B CE1 
2803 C CE2 . TYR B 87  ? 0.7842 0.8636 0.9710 0.1465  0.1482  0.0112  94  TYR B CE2 
2804 C CZ  . TYR B 87  ? 0.8264 0.8937 0.9547 0.1530  0.1588  0.0167  94  TYR B CZ  
2805 O OH  . TYR B 87  ? 0.8255 0.8667 0.9427 0.1656  0.1867  0.0361  94  TYR B OH  
2806 N N   . MET B 88  ? 0.7471 0.8695 0.8336 0.1158  0.0983  -0.0328 95  MET B N   
2807 C CA  . MET B 88  ? 0.8109 0.9228 0.8989 0.1128  0.1082  -0.0272 95  MET B CA  
2808 C C   . MET B 88  ? 0.8372 0.9232 0.9148 0.1221  0.1321  -0.0125 95  MET B C   
2809 O O   . MET B 88  ? 0.7822 0.8552 0.8135 0.1266  0.1369  -0.0112 95  MET B O   
2810 C CB  . MET B 88  ? 0.8743 0.9934 0.9287 0.1060  0.1006  -0.0343 95  MET B CB  
2811 C CG  . MET B 88  ? 0.8166 0.9593 0.8773 0.0996  0.0820  -0.0454 95  MET B CG  
2812 S SD  . MET B 88  ? 0.7424 0.8893 0.8425 0.0956  0.0749  -0.0465 95  MET B SD  
2813 C CE  . MET B 88  ? 0.7898 0.9318 0.8822 0.0899  0.0837  -0.0405 95  MET B CE  
2814 N N   . GLU B 89  ? 1.0514 0.6435 1.0058 -0.0737 -0.0264 0.0547  96  GLU B N   
2815 C CA  . GLU B 89  ? 1.1326 0.6774 1.0467 -0.0967 -0.0254 0.0675  96  GLU B CA  
2816 C C   . GLU B 89  ? 1.0529 0.6075 0.9602 -0.1036 -0.0093 0.0757  96  GLU B C   
2817 O O   . GLU B 89  ? 1.0042 0.5126 0.8691 -0.1086 -0.0166 0.0829  96  GLU B O   
2818 C CB  . GLU B 89  ? 1.2739 0.8157 1.1894 -0.1256 -0.0162 0.0734  96  GLU B CB  
2819 C CG  . GLU B 89  ? 1.4291 0.9500 1.3431 -0.1223 -0.0345 0.0663  96  GLU B CG  
2820 C CD  . GLU B 89  ? 1.4716 1.0459 1.4319 -0.1203 -0.0254 0.0584  96  GLU B CD  
2821 O OE1 . GLU B 89  ? 1.0966 0.7148 1.0876 -0.0994 -0.0212 0.0502  96  GLU B OE1 
2822 O OE2 . GLU B 89  ? 1.6513 1.2215 1.6150 -0.1413 -0.0239 0.0605  96  GLU B OE2 
2823 N N   . LYS B 90  ? 0.9828 0.5935 0.9283 -0.1026 0.0102  0.0739  97  LYS B N   
2824 C CA  . LYS B 90  ? 0.9998 0.6237 0.9420 -0.1078 0.0258  0.0793  97  LYS B CA  
2825 C C   . LYS B 90  ? 1.0498 0.6712 0.9863 -0.0858 0.0164  0.0762  97  LYS B C   
2826 O O   . LYS B 90  ? 1.1437 0.7722 1.0746 -0.0883 0.0269  0.0798  97  LYS B O   
2827 C CB  . LYS B 90  ? 1.0191 0.6993 1.0025 -0.1144 0.0471  0.0771  97  LYS B CB  
2828 C CG  . LYS B 90  ? 1.1291 0.8164 1.1186 -0.1396 0.0591  0.0799  97  LYS B CG  
2829 C CD  . LYS B 90  ? 1.1100 0.8523 1.1386 -0.1442 0.0788  0.0757  97  LYS B CD  
2830 C CE  . LYS B 90  ? 1.1780 0.9295 1.2106 -0.1722 0.0925  0.0775  97  LYS B CE  
2831 N NZ  . LYS B 90  ? 1.2221 0.9624 1.2265 -0.1915 0.1085  0.0837  97  LYS B NZ  
2832 N N   . GLY B 91  ? 0.9714 0.5853 0.9105 -0.0642 -0.0033 0.0678  98  GLY B N   
2833 C CA  . GLY B 91  ? 1.0081 0.6217 0.9447 -0.0440 -0.0148 0.0627  98  GLY B CA  
2834 C C   . GLY B 91  ? 0.9639 0.6346 0.9424 -0.0356 -0.0033 0.0577  98  GLY B C   
2835 O O   . GLY B 91  ? 0.9571 0.6633 0.9657 -0.0391 0.0070  0.0555  98  GLY B O   
2836 N N   . ASN B 92  ? 1.0356 0.7115 1.0132 -0.0256 -0.0069 0.0563  99  ASN B N   
2837 C CA  . ASN B 92  ? 0.9511 0.6746 0.9632 -0.0199 0.0015  0.0526  99  ASN B CA  
2838 C C   . ASN B 92  ? 0.9493 0.6909 0.9700 -0.0339 0.0213  0.0596  99  ASN B C   
2839 O O   . ASN B 92  ? 0.8957 0.6174 0.8962 -0.0475 0.0304  0.0662  99  ASN B O   
2840 C CB  . ASN B 92  ? 1.0865 0.8138 1.1001 -0.0042 -0.0120 0.0463  99  ASN B CB  
2841 C CG  . ASN B 92  ? 1.1567 0.8510 1.1388 -0.0061 -0.0159 0.0521  99  ASN B CG  
2842 O OD1 . ASN B 92  ? 1.1829 0.8703 1.1525 -0.0194 -0.0018 0.0604  99  ASN B OD1 
2843 N ND2 . ASN B 92  ? 1.3257 1.0020 1.2955 0.0088  -0.0359 0.0459  99  ASN B ND2 
2844 N N   . LEU B 93  ? 0.7999 0.5787 0.8490 -0.0305 0.0270  0.0572  100 LEU B N   
2845 C CA  . LEU B 93  ? 0.8432 0.6401 0.9035 -0.0391 0.0418  0.0608  100 LEU B CA  
2846 C C   . LEU B 93  ? 0.8086 0.5870 0.8462 -0.0428 0.0469  0.0646  100 LEU B C   
2847 O O   . LEU B 93  ? 0.8878 0.6706 0.9244 -0.0521 0.0603  0.0664  100 LEU B O   
2848 C CB  . LEU B 93  ? 0.8671 0.6977 0.9548 -0.0343 0.0419  0.0581  100 LEU B CB  
2849 C CG  . LEU B 93  ? 0.8252 0.6713 0.9245 -0.0389 0.0515  0.0598  100 LEU B CG  
2850 C CD1 . LEU B 93  ? 0.8920 0.7470 1.0016 -0.0462 0.0607  0.0595  100 LEU B CD1 
2851 C CD2 . LEU B 93  ? 0.8233 0.6906 0.9396 -0.0358 0.0471  0.0590  100 LEU B CD2 
2852 N N   . MET B 94  ? 0.8213 0.5827 0.8426 -0.0350 0.0361  0.0641  101 MET B N   
2853 C CA  . MET B 94  ? 0.9432 0.6841 0.9386 -0.0372 0.0390  0.0671  101 MET B CA  
2854 C C   . MET B 94  ? 1.0627 0.7691 1.0216 -0.0486 0.0447  0.0725  101 MET B C   
2855 O O   . MET B 94  ? 1.1720 0.8737 1.1148 -0.0570 0.0576  0.0746  101 MET B O   
2856 C CB  . MET B 94  ? 1.0154 0.7452 1.0021 -0.0256 0.0226  0.0644  101 MET B CB  
2857 C CG  . MET B 94  ? 1.0412 0.7520 1.0027 -0.0259 0.0234  0.0661  101 MET B CG  
2858 S SD  . MET B 94  ? 1.0195 0.7571 0.9999 -0.0282 0.0365  0.0644  101 MET B SD  
2859 C CE  . MET B 94  ? 1.0003 0.7672 1.0160 -0.0214 0.0243  0.0609  101 MET B CE  
2860 N N   . HIS B 95  ? 1.0559 0.7374 0.9996 -0.0494 0.0346  0.0741  102 HIS B N   
2861 C CA  . HIS B 95  ? 1.0727 0.7175 0.9794 -0.0651 0.0390  0.0811  102 HIS B CA  
2862 C C   . HIS B 95  ? 0.9841 0.6518 0.9039 -0.0835 0.0613  0.0830  102 HIS B C   
2863 O O   . HIS B 95  ? 1.0168 0.6682 0.9085 -0.1000 0.0736  0.0880  102 HIS B O   
2864 C CB  . HIS B 95  ? 1.0327 0.6452 0.9241 -0.0607 0.0199  0.0810  102 HIS B CB  
2865 C CG  . HIS B 95  ? 1.1695 0.7327 1.0143 -0.0784 0.0194  0.0898  102 HIS B CG  
2866 N ND1 . HIS B 95  ? 1.1959 0.7598 1.0431 -0.0968 0.0295  0.0935  102 HIS B ND1 
2867 C CD2 . HIS B 95  ? 1.2487 0.7580 1.0402 -0.0831 0.0094  0.0965  102 HIS B CD2 
2868 C CE1 . HIS B 95  ? 1.2540 0.7667 1.0511 -0.1142 0.0267  0.1027  102 HIS B CE1 
2869 N NE2 . HIS B 95  ? 1.3098 0.7865 1.0699 -0.1060 0.0144  0.1052  102 HIS B NE2 
2870 N N   . VAL B 96  ? 0.9610 0.6679 0.9228 -0.0809 0.0661  0.0782  103 VAL B N   
2871 C CA  . VAL B 96  ? 0.9343 0.6708 0.9175 -0.0948 0.0844  0.0769  103 VAL B CA  
2872 C C   . VAL B 96  ? 0.8685 0.6312 0.8618 -0.0943 0.0993  0.0730  103 VAL B C   
2873 O O   . VAL B 96  ? 0.8626 0.6375 0.8544 -0.1086 0.1165  0.0719  103 VAL B O   
2874 C CB  . VAL B 96  ? 0.8474 0.6128 0.8689 -0.0901 0.0808  0.0723  103 VAL B CB  
2875 C CG1 . VAL B 96  ? 0.8323 0.6328 0.8817 -0.1010 0.0964  0.0686  103 VAL B CG1 
2876 C CG2 . VAL B 96  ? 0.9430 0.6799 0.9500 -0.0927 0.0678  0.0744  103 VAL B CG2 
2877 N N   . LEU B 97  ? 0.9206 0.6934 0.9250 -0.0783 0.0925  0.0696  104 LEU B N   
2878 C CA  . LEU B 97  ? 0.8890 0.6805 0.8998 -0.0742 0.1025  0.0643  104 LEU B CA  
2879 C C   . LEU B 97  ? 0.9804 0.7500 0.9531 -0.0814 0.1118  0.0659  104 LEU B C   
2880 O O   . LEU B 97  ? 1.0284 0.8182 1.0058 -0.0824 0.1258  0.0593  104 LEU B O   
2881 C CB  . LEU B 97  ? 0.8692 0.6683 0.8947 -0.0580 0.0900  0.0617  104 LEU B CB  
2882 C CG  . LEU B 97  ? 0.8375 0.6617 0.8980 -0.0523 0.0834  0.0597  104 LEU B CG  
2883 C CD1 . LEU B 97  ? 0.9738 0.7973 1.0387 -0.0418 0.0699  0.0598  104 LEU B CD1 
2884 C CD2 . LEU B 97  ? 0.8322 0.6863 0.9195 -0.0533 0.0927  0.0537  104 LEU B CD2 
2885 N N   . LYS B 98  ? 1.0555 0.7834 0.9888 -0.0853 0.1031  0.0732  105 LYS B N   
2886 C CA  . LYS B 98  ? 1.0180 0.7165 0.9045 -0.0945 0.1106  0.0765  105 LYS B CA  
2887 C C   . LYS B 98  ? 1.1239 0.8146 0.9867 -0.1194 0.1284  0.0811  105 LYS B C   
2888 O O   . LYS B 98  ? 1.2721 0.9453 1.0963 -0.1299 0.1392  0.0830  105 LYS B O   
2889 C CB  . LYS B 98  ? 1.0776 0.7301 0.9279 -0.0860 0.0895  0.0820  105 LYS B CB  
2890 C CG  . LYS B 98  ? 1.0480 0.7090 0.9149 -0.0660 0.0752  0.0768  105 LYS B CG  
2891 C CD  . LYS B 98  ? 1.1571 0.7778 0.9940 -0.0568 0.0523  0.0798  105 LYS B CD  
2892 C CE  . LYS B 98  ? 1.2506 0.8763 1.0937 -0.0423 0.0414  0.0745  105 LYS B CE  
2893 N NZ  . LYS B 98  ? 1.2017 0.8002 1.0299 -0.0310 0.0165  0.0744  105 LYS B NZ  
2894 N N   . ALA B 99  ? 1.1684 0.8725 1.0526 -0.1304 0.1316  0.0826  106 ALA B N   
2895 C CA  . ALA B 99  ? 1.2964 0.9906 1.1585 -0.1583 0.1461  0.0882  106 ALA B CA  
2896 C C   . ALA B 99  ? 1.4063 1.1407 1.2775 -0.1730 0.1745  0.0809  106 ALA B C   
2897 O O   . ALA B 99  ? 1.5375 1.3151 1.4450 -0.1585 0.1817  0.0690  106 ALA B O   
2898 C CB  . ALA B 99  ? 1.2844 0.9849 1.1719 -0.1648 0.1396  0.0899  106 ALA B CB  
2899 N N   . GLU B 100 ? 1.6352 1.3542 1.4720 -0.2023 0.1896  0.0874  107 GLU B N   
2900 C CA  . GLU B 100 ? 1.7501 1.5079 1.5880 -0.2203 0.2197  0.0797  107 GLU B CA  
2901 C C   . GLU B 100 ? 1.7972 1.6251 1.7005 -0.2205 0.2339  0.0654  107 GLU B C   
2902 O O   . GLU B 100 ? 1.9293 1.8044 1.8561 -0.2141 0.2510  0.0507  107 GLU B O   
2903 C CB  . GLU B 100 ? 1.8345 1.5568 1.6147 -0.2569 0.2331  0.0917  107 GLU B CB  
2904 C CG  . GLU B 100 ? 1.8280 1.5414 1.6108 -0.2840 0.2327  0.1000  107 GLU B CG  
2905 C CD  . GLU B 100 ? 2.0938 1.7526 1.8058 -0.3207 0.2388  0.1159  107 GLU B CD  
2906 O OE1 . GLU B 100 ? 2.1333 1.7989 1.8127 -0.3389 0.2621  0.1153  107 GLU B OE1 
2907 O OE2 . GLU B 100 ? 2.1197 1.7259 1.8051 -0.3315 0.2195  0.1287  107 GLU B OE2 
2908 N N   . MET B 101 ? 1.7553 1.5882 1.6864 -0.2258 0.2245  0.0683  108 MET B N   
2909 C CA  . MET B 101 ? 1.6728 1.5671 1.6676 -0.2220 0.2309  0.0549  108 MET B CA  
2910 C C   . MET B 101 ? 1.6909 1.5995 1.7204 -0.1864 0.2138  0.0471  108 MET B C   
2911 O O   . MET B 101 ? 1.8551 1.7308 1.8780 -0.1728 0.1920  0.0550  108 MET B O   
2912 C CB  . MET B 101 ? 1.6337 1.5215 1.6400 -0.2406 0.2243  0.0613  108 MET B CB  
2913 C CG  . MET B 101 ? 1.5399 1.4918 1.6075 -0.2434 0.2331  0.0472  108 MET B CG  
2914 S SD  . MET B 101 ? 1.6823 1.6242 1.7578 -0.2705 0.2266  0.0544  108 MET B SD  
2915 C CE  . MET B 101 ? 1.6370 1.6641 1.7891 -0.2682 0.2371  0.0333  108 MET B CE  
2916 N N   . SER B 102 ? 1.6063 1.5626 1.6699 -0.1719 0.2231  0.0311  109 SER B N   
2917 C CA  . SER B 102 ? 1.4709 1.4347 1.5593 -0.1405 0.2067  0.0243  109 SER B CA  
2918 C C   . SER B 102 ? 1.3128 1.2962 1.4445 -0.1324 0.1929  0.0218  109 SER B C   
2919 O O   . SER B 102 ? 1.5317 1.5455 1.6906 -0.1461 0.2005  0.0167  109 SER B O   
2920 C CB  . SER B 102 ? 1.4364 1.4366 1.5405 -0.1263 0.2180  0.0070  109 SER B CB  
2921 O OG  . SER B 102 ? 1.5783 1.5605 1.6790 -0.1003 0.2009  0.0057  109 SER B OG  
2922 N N   . THR B 103 ? 1.0196 0.9847 1.1549 -0.1122 0.1725  0.0254  110 THR B N   
2923 C CA  . THR B 103 ? 0.8873 0.8636 1.0545 -0.1032 0.1576  0.0244  110 THR B CA  
2924 C C   . THR B 103 ? 0.8981 0.9116 1.1018 -0.0854 0.1552  0.0094  110 THR B C   
2925 O O   . THR B 103 ? 0.9781 0.9855 1.1744 -0.0695 0.1508  0.0056  110 THR B O   
2926 C CB  . THR B 103 ? 0.8310 0.7726 0.9825 -0.0911 0.1380  0.0346  110 THR B CB  
2927 O OG1 . THR B 103 ? 0.8686 0.7711 0.9815 -0.1004 0.1367  0.0458  110 THR B OG1 
2928 C CG2 . THR B 103 ? 0.8134 0.7632 0.9891 -0.0876 0.1254  0.0352  110 THR B CG2 
2929 N N   . PRO B 104 ? 0.8736 0.9229 1.1153 -0.0870 0.1554  -0.0001 111 PRO B N   
2930 C CA  . PRO B 104 ? 0.8289 0.9081 1.1033 -0.0666 0.1478  -0.0154 111 PRO B CA  
2931 C C   . PRO B 104 ? 0.7587 0.8152 1.0319 -0.0478 0.1243  -0.0107 111 PRO B C   
2932 O O   . PRO B 104 ? 0.8656 0.8918 1.1197 -0.0511 0.1151  0.0032  111 PRO B O   
2933 C CB  . PRO B 104 ? 0.8443 0.9651 1.1581 -0.0753 0.1520  -0.0260 111 PRO B CB  
2934 C CG  . PRO B 104 ? 0.8442 0.9445 1.1446 -0.0959 0.1523  -0.0121 111 PRO B CG  
2935 C CD  . PRO B 104 ? 0.8900 0.9557 1.1465 -0.1077 0.1626  0.0003  111 PRO B CD  
2936 N N   . LEU B 105 ? 0.7593 0.8312 1.0519 -0.0285 0.1146  -0.0236 112 LEU B N   
2937 C CA  . LEU B 105 ? 0.7073 0.7559 0.9953 -0.0124 0.0916  -0.0198 112 LEU B CA  
2938 C C   . LEU B 105 ? 0.6937 0.7364 0.9896 -0.0157 0.0780  -0.0124 112 LEU B C   
2939 O O   . LEU B 105 ? 0.7396 0.7540 1.0169 -0.0128 0.0647  -0.0015 112 LEU B O   
2940 C CB  . LEU B 105 ? 0.6888 0.7531 0.9953 0.0091  0.0818  -0.0374 112 LEU B CB  
2941 C CG  . LEU B 105 ? 0.7161 0.7516 1.0138 0.0258  0.0553  -0.0351 112 LEU B CG  
2942 C CD1 . LEU B 105 ? 0.6812 0.6749 0.9421 0.0226  0.0499  -0.0192 112 LEU B CD1 
2943 C CD2 . LEU B 105 ? 0.6396 0.6892 0.9541 0.0486  0.0454  -0.0556 112 LEU B CD2 
2944 N N   . SER B 106 ? 0.6313 0.7023 0.9540 -0.0229 0.0818  -0.0191 113 SER B N   
2945 C CA  . SER B 106 ? 0.5775 0.6437 0.9068 -0.0261 0.0689  -0.0138 113 SER B CA  
2946 C C   . SER B 106 ? 0.6273 0.6659 0.9299 -0.0393 0.0714  0.0024  113 SER B C   
2947 O O   . SER B 106 ? 0.6590 0.6800 0.9513 -0.0365 0.0583  0.0097  113 SER B O   
2948 C CB  . SER B 106 ? 0.6061 0.7101 0.9714 -0.0322 0.0721  -0.0260 113 SER B CB  
2949 O OG  . SER B 106 ? 0.7735 0.8932 1.1412 -0.0518 0.0937  -0.0261 113 SER B OG  
2950 N N   . VAL B 107 ? 0.6538 0.6882 0.9434 -0.0530 0.0874  0.0070  114 VAL B N   
2951 C CA  . VAL B 107 ? 0.6471 0.6531 0.9103 -0.0628 0.0880  0.0199  114 VAL B CA  
2952 C C   . VAL B 107 ? 0.6305 0.6110 0.8698 -0.0535 0.0805  0.0280  114 VAL B C   
2953 O O   . VAL B 107 ? 0.6472 0.6129 0.8754 -0.0532 0.0721  0.0348  114 VAL B O   
2954 C CB  . VAL B 107 ? 0.7079 0.7092 0.9581 -0.0801 0.1041  0.0228  114 VAL B CB  
2955 C CG1 . VAL B 107 ? 0.6775 0.6437 0.8972 -0.0858 0.1004  0.0344  114 VAL B CG1 
2956 C CG2 . VAL B 107 ? 0.6387 0.6660 0.9129 -0.0946 0.1111  0.0159  114 VAL B CG2 
2957 N N   . LYS B 108 ? 0.6171 0.5953 0.8497 -0.0464 0.0836  0.0257  115 LYS B N   
2958 C CA  . LYS B 108 ? 0.7118 0.6681 0.9249 -0.0387 0.0749  0.0320  115 LYS B CA  
2959 C C   . LYS B 108 ? 0.7148 0.6675 0.9316 -0.0322 0.0590  0.0345  115 LYS B C   
2960 O O   . LYS B 108 ? 0.7243 0.6632 0.9266 -0.0343 0.0533  0.0426  115 LYS B O   
2961 C CB  . LYS B 108 ? 0.7372 0.6910 0.9434 -0.0312 0.0785  0.0269  115 LYS B CB  
2962 C CG  . LYS B 108 ? 0.7654 0.7121 0.9536 -0.0397 0.0931  0.0286  115 LYS B CG  
2963 C CD  . LYS B 108 ? 0.6836 0.6245 0.8591 -0.0319 0.0965  0.0235  115 LYS B CD  
2964 C CE  . LYS B 108 ? 0.6222 0.5526 0.7737 -0.0427 0.1110  0.0264  115 LYS B CE  
2965 N NZ  . LYS B 108 ? 0.7144 0.6334 0.8465 -0.0350 0.1128  0.0223  115 LYS B NZ  
2966 N N   . GLY B 109 ? 0.6857 0.6517 0.9210 -0.0250 0.0518  0.0266  116 GLY B N   
2967 C CA  . GLY B 109 ? 0.6233 0.5818 0.8576 -0.0204 0.0350  0.0291  116 GLY B CA  
2968 C C   . GLY B 109 ? 0.6349 0.5917 0.8643 -0.0287 0.0330  0.0358  116 GLY B C   
2969 O O   . GLY B 109 ? 0.6799 0.6236 0.8933 -0.0304 0.0247  0.0432  116 GLY B O   
2970 N N   . ARG B 110 ? 0.5780 0.5478 0.8193 -0.0351 0.0413  0.0327  117 ARG B N   
2971 C CA  . ARG B 110 ? 0.5581 0.5254 0.7946 -0.0414 0.0393  0.0363  117 ARG B CA  
2972 C C   . ARG B 110 ? 0.5293 0.4829 0.7451 -0.0449 0.0434  0.0437  117 ARG B C   
2973 O O   . ARG B 110 ? 0.6042 0.5545 0.8104 -0.0455 0.0380  0.0467  117 ARG B O   
2974 C CB  . ARG B 110 ? 0.5636 0.5445 0.8171 -0.0486 0.0453  0.0305  117 ARG B CB  
2975 C CG  . ARG B 110 ? 0.6176 0.5965 0.8702 -0.0516 0.0375  0.0306  117 ARG B CG  
2976 C CD  . ARG B 110 ? 0.6488 0.6388 0.9183 -0.0608 0.0411  0.0248  117 ARG B CD  
2977 N NE  . ARG B 110 ? 0.6710 0.6516 0.9309 -0.0713 0.0532  0.0280  117 ARG B NE  
2978 C CZ  . ARG B 110 ? 0.8290 0.8129 1.0964 -0.0848 0.0584  0.0255  117 ARG B CZ  
2979 N NH1 . ARG B 110 ? 0.8372 0.8386 1.1274 -0.0894 0.0530  0.0184  117 ARG B NH1 
2980 N NH2 . ARG B 110 ? 0.8727 0.8395 1.1224 -0.0952 0.0675  0.0305  117 ARG B NH2 
2981 N N   . ILE B 111 ? 0.6416 0.5888 0.8504 -0.0467 0.0522  0.0451  118 ILE B N   
2982 C CA  . ILE B 111 ? 0.6281 0.5625 0.8190 -0.0471 0.0531  0.0501  118 ILE B CA  
2983 C C   . ILE B 111 ? 0.6119 0.5452 0.7954 -0.0443 0.0459  0.0541  118 ILE B C   
2984 O O   . ILE B 111 ? 0.7047 0.6396 0.8813 -0.0454 0.0440  0.0556  118 ILE B O   
2985 C CB  . ILE B 111 ? 0.6654 0.5890 0.8464 -0.0486 0.0613  0.0510  118 ILE B CB  
2986 C CG1 . ILE B 111 ? 0.7006 0.6193 0.8797 -0.0566 0.0680  0.0498  118 ILE B CG1 
2987 C CG2 . ILE B 111 ? 0.6294 0.5402 0.7937 -0.0459 0.0582  0.0548  118 ILE B CG2 
2988 C CD1 . ILE B 111 ? 0.7220 0.6313 0.8892 -0.0620 0.0781  0.0505  118 ILE B CD1 
2989 N N   . ILE B 112 ? 0.5684 0.4995 0.7529 -0.0416 0.0415  0.0548  119 ILE B N   
2990 C CA  . ILE B 112 ? 0.6437 0.5682 0.8165 -0.0432 0.0335  0.0602  119 ILE B CA  
2991 C C   . ILE B 112 ? 0.6703 0.5996 0.8393 -0.0476 0.0274  0.0627  119 ILE B C   
2992 O O   . ILE B 112 ? 0.6659 0.5979 0.8243 -0.0539 0.0267  0.0669  119 ILE B O   
2993 C CB  . ILE B 112 ? 0.6506 0.5632 0.8207 -0.0385 0.0267  0.0599  119 ILE B CB  
2994 C CG1 . ILE B 112 ? 0.6878 0.5948 0.8553 -0.0350 0.0334  0.0576  119 ILE B CG1 
2995 C CG2 . ILE B 112 ? 0.7125 0.6120 0.8666 -0.0440 0.0158  0.0671  119 ILE B CG2 
2996 C CD1 . ILE B 112 ? 0.7236 0.6236 0.8929 -0.0262 0.0293  0.0518  119 ILE B CD1 
2997 N N   . LEU B 113 ? 0.6382 0.5705 0.8153 -0.0449 0.0233  0.0592  120 LEU B N   
2998 C CA  . LEU B 113 ? 0.7162 0.6501 0.8854 -0.0486 0.0168  0.0610  120 LEU B CA  
2999 C C   . LEU B 113 ? 0.6671 0.6128 0.8341 -0.0518 0.0236  0.0591  120 LEU B C   
3000 O O   . LEU B 113 ? 0.6761 0.6262 0.8298 -0.0572 0.0223  0.0614  120 LEU B O   
3001 C CB  . LEU B 113 ? 0.7833 0.7172 0.9629 -0.0433 0.0080  0.0560  120 LEU B CB  
3002 C CG  . LEU B 113 ? 0.7062 0.6363 0.8735 -0.0460 -0.0021 0.0575  120 LEU B CG  
3003 C CD1 . LEU B 113 ? 0.7186 0.6333 0.8581 -0.0537 -0.0089 0.0668  120 LEU B CD1 
3004 C CD2 . LEU B 113 ? 0.7758 0.7049 0.9569 -0.0381 -0.0141 0.0509  120 LEU B CD2 
3005 N N   . GLU B 114 ? 0.6886 0.6381 0.8659 -0.0488 0.0303  0.0543  121 GLU B N   
3006 C CA  . GLU B 114 ? 0.7531 0.7087 0.9270 -0.0482 0.0337  0.0504  121 GLU B CA  
3007 C C   . GLU B 114 ? 0.7308 0.6933 0.8973 -0.0490 0.0369  0.0514  121 GLU B C   
3008 O O   . GLU B 114 ? 0.7328 0.7079 0.8946 -0.0488 0.0376  0.0474  121 GLU B O   
3009 C CB  . GLU B 114 ? 0.7664 0.7157 0.9478 -0.0463 0.0368  0.0461  121 GLU B CB  
3010 C CG  . GLU B 114 ? 0.8198 0.7699 1.0113 -0.0480 0.0332  0.0428  121 GLU B CG  
3011 C CD  . GLU B 114 ? 0.8903 0.8333 1.0878 -0.0514 0.0365  0.0397  121 GLU B CD  
3012 O OE1 . GLU B 114 ? 1.0086 0.9411 1.1991 -0.0524 0.0416  0.0414  121 GLU B OE1 
3013 O OE2 . GLU B 114 ? 0.8280 0.7740 1.0352 -0.0547 0.0328  0.0359  121 GLU B OE2 
3014 N N   . ILE B 115 ? 0.7440 0.7008 0.9105 -0.0494 0.0385  0.0551  122 ILE B N   
3015 C CA  . ILE B 115 ? 0.6685 0.6335 0.8310 -0.0517 0.0397  0.0561  122 ILE B CA  
3016 C C   . ILE B 115 ? 0.6977 0.6745 0.8521 -0.0614 0.0384  0.0599  122 ILE B C   
3017 O O   . ILE B 115 ? 0.7282 0.7253 0.8824 -0.0644 0.0417  0.0562  122 ILE B O   
3018 C CB  . ILE B 115 ? 0.6797 0.6318 0.8412 -0.0510 0.0393  0.0597  122 ILE B CB  
3019 C CG1 . ILE B 115 ? 0.5750 0.5165 0.7374 -0.0442 0.0418  0.0561  122 ILE B CG1 
3020 C CG2 . ILE B 115 ? 0.6346 0.5949 0.7930 -0.0566 0.0377  0.0620  122 ILE B CG2 
3021 C CD1 . ILE B 115 ? 0.5448 0.4704 0.7030 -0.0432 0.0432  0.0589  122 ILE B CD1 
3022 N N   . ILE B 116 ? 0.7574 0.7215 0.9042 -0.0663 0.0330  0.0662  123 ILE B N   
3023 C CA  . ILE B 116 ? 0.7428 0.7085 0.8733 -0.0786 0.0298  0.0723  123 ILE B CA  
3024 C C   . ILE B 116 ? 0.7202 0.7029 0.8449 -0.0808 0.0334  0.0678  123 ILE B C   
3025 O O   . ILE B 116 ? 0.7437 0.7436 0.8586 -0.0917 0.0381  0.0686  123 ILE B O   
3026 C CB  . ILE B 116 ? 0.6620 0.6015 0.7812 -0.0803 0.0183  0.0793  123 ILE B CB  
3027 C CG1 . ILE B 116 ? 0.7548 0.6780 0.8751 -0.0787 0.0140  0.0825  123 ILE B CG1 
3028 C CG2 . ILE B 116 ? 0.6572 0.5898 0.7508 -0.0947 0.0126  0.0871  123 ILE B CG2 
3029 C CD1 . ILE B 116 ? 0.7510 0.6512 0.8707 -0.0702 0.0025  0.0825  123 ILE B CD1 
3030 N N   . GLU B 117 ? 0.6975 0.6764 0.8279 -0.0716 0.0314  0.0624  124 GLU B N   
3031 C CA  . GLU B 117 ? 0.6697 0.6611 0.7939 -0.0706 0.0332  0.0559  124 GLU B CA  
3032 C C   . GLU B 117 ? 0.6589 0.6768 0.7884 -0.0679 0.0420  0.0467  124 GLU B C   
3033 O O   . GLU B 117 ? 0.6866 0.7244 0.8052 -0.0741 0.0469  0.0433  124 GLU B O   
3034 C CB  . GLU B 117 ? 0.7635 0.7450 0.8973 -0.0606 0.0284  0.0503  124 GLU B CB  
3035 C CG  . GLU B 117 ? 0.7825 0.7467 0.9123 -0.0615 0.0177  0.0547  124 GLU B CG  
3036 C CD  . GLU B 117 ? 0.8166 0.7764 0.9640 -0.0537 0.0139  0.0484  124 GLU B CD  
3037 O OE1 . GLU B 117 ? 0.8371 0.8015 0.9928 -0.0497 0.0183  0.0419  124 GLU B OE1 
3038 O OE2 . GLU B 117 ? 0.9196 0.8705 1.0724 -0.0521 0.0049  0.0494  124 GLU B OE2 
3039 N N   . GLY B 118 ? 0.6394 0.6575 0.7842 -0.0585 0.0433  0.0417  125 GLY B N   
3040 C CA  . GLY B 118 ? 0.7197 0.7600 0.8723 -0.0513 0.0474  0.0305  125 GLY B CA  
3041 C C   . GLY B 118 ? 0.7075 0.7755 0.8615 -0.0609 0.0536  0.0304  125 GLY B C   
3042 O O   . GLY B 118 ? 0.5966 0.6961 0.7537 -0.0592 0.0590  0.0191  125 GLY B O   
3043 N N   . MET B 119 ? 0.7274 0.7855 0.8798 -0.0711 0.0525  0.0413  126 MET B N   
3044 C CA  . MET B 119 ? 0.7482 0.8301 0.9006 -0.0856 0.0573  0.0433  126 MET B CA  
3045 C C   . MET B 119 ? 0.7442 0.8415 0.8787 -0.1030 0.0631  0.0470  126 MET B C   
3046 O O   . MET B 119 ? 0.7505 0.8841 0.8883 -0.1132 0.0717  0.0413  126 MET B O   
3047 C CB  . MET B 119 ? 0.7415 0.8018 0.8925 -0.0929 0.0520  0.0545  126 MET B CB  
3048 C CG  . MET B 119 ? 0.7446 0.7941 0.9090 -0.0790 0.0480  0.0506  126 MET B CG  
3049 S SD  . MET B 119 ? 0.7231 0.8030 0.9070 -0.0652 0.0491  0.0338  126 MET B SD  
3050 C CE  . MET B 119 ? 0.7785 0.9015 0.9703 -0.0838 0.0551  0.0317  126 MET B CE  
3051 N N   . ALA B 120 ? 0.7972 0.8680 0.9123 -0.1067 0.0581  0.0555  127 ALA B N   
3052 C CA  . ALA B 120 ? 0.7793 0.8556 0.8692 -0.1219 0.0613  0.0594  127 ALA B CA  
3053 C C   . ALA B 120 ? 0.7440 0.8541 0.8358 -0.1156 0.0706  0.0444  127 ALA B C   
3054 O O   . ALA B 120 ? 0.7917 0.9273 0.8683 -0.1312 0.0801  0.0432  127 ALA B O   
3055 C CB  . ALA B 120 ? 0.7992 0.8352 0.8690 -0.1218 0.0493  0.0696  127 ALA B CB  
3056 N N   . TYR B 121 ? 0.7277 0.8363 0.8351 -0.0938 0.0675  0.0326  128 TYR B N   
3057 C CA  . TYR B 121 ? 0.6863 0.8236 0.7968 -0.0828 0.0733  0.0150  128 TYR B CA  
3058 C C   . TYR B 121 ? 0.7092 0.8946 0.8358 -0.0847 0.0843  0.0026  128 TYR B C   
3059 O O   . TYR B 121 ? 0.7896 1.0103 0.9079 -0.0925 0.0951  -0.0058 128 TYR B O   
3060 C CB  . TYR B 121 ? 0.6874 0.8071 0.8109 -0.0596 0.0647  0.0051  128 TYR B CB  
3061 C CG  . TYR B 121 ? 0.6482 0.7951 0.7742 -0.0457 0.0679  -0.0153 128 TYR B CG  
3062 C CD1 . TYR B 121 ? 0.6466 0.7971 0.7525 -0.0469 0.0695  -0.0204 128 TYR B CD1 
3063 C CD2 . TYR B 121 ? 0.6672 0.8365 0.8141 -0.0301 0.0678  -0.0313 128 TYR B CD2 
3064 C CE1 . TYR B 121 ? 0.7001 0.8764 0.8068 -0.0323 0.0722  -0.0416 128 TYR B CE1 
3065 C CE2 . TYR B 121 ? 0.6782 0.8741 0.8279 -0.0142 0.0690  -0.0532 128 TYR B CE2 
3066 C CZ  . TYR B 121 ? 0.6755 0.8754 0.8053 -0.0151 0.0718  -0.0587 128 TYR B CZ  
3067 O OH  . TYR B 121 ? 0.7825 1.0077 0.9137 0.0028  0.0723  -0.0826 128 TYR B OH  
3068 N N   . LEU B 122 ? 0.7653 0.9531 0.9147 -0.0775 0.0810  0.0008  129 LEU B N   
3069 C CA  . LEU B 122 ? 0.7233 0.9574 0.8950 -0.0761 0.0877  -0.0129 129 LEU B CA  
3070 C C   . LEU B 122 ? 0.6868 0.9547 0.8527 -0.1038 0.1001  -0.0074 129 LEU B C   
3071 O O   . LEU B 122 ? 0.8339 1.1541 1.0101 -0.1066 0.1115  -0.0229 129 LEU B O   
3072 C CB  . LEU B 122 ? 0.7780 0.9975 0.9697 -0.0645 0.0782  -0.0128 129 LEU B CB  
3073 C CG  . LEU B 122 ? 0.6917 0.8821 0.8888 -0.0388 0.0663  -0.0204 129 LEU B CG  
3074 C CD1 . LEU B 122 ? 0.6314 0.7986 0.8374 -0.0339 0.0575  -0.0146 129 LEU B CD1 
3075 C CD2 . LEU B 122 ? 0.7564 0.9766 0.9652 -0.0183 0.0651  -0.0445 129 LEU B CD2 
3076 N N   . HIS B 123 ? 0.7789 1.0169 0.9271 -0.1246 0.0974  0.0136  130 HIS B N   
3077 C CA  . HIS B 123 ? 0.7797 1.0376 0.9131 -0.1566 0.1070  0.0231  130 HIS B CA  
3078 C C   . HIS B 123 ? 0.8579 1.1318 0.9632 -0.1713 0.1181  0.0225  130 HIS B C   
3079 O O   . HIS B 123 ? 0.9278 1.2442 1.0287 -0.1943 0.1325  0.0197  130 HIS B O   
3080 C CB  . HIS B 123 ? 0.7583 0.9682 0.8737 -0.1727 0.0965  0.0457  130 HIS B CB  
3081 C CG  . HIS B 123 ? 0.8192 1.0237 0.9584 -0.1664 0.0892  0.0460  130 HIS B CG  
3082 N ND1 . HIS B 123 ? 0.7979 0.9711 0.9253 -0.1825 0.0810  0.0622  130 HIS B ND1 
3083 C CD2 . HIS B 123 ? 0.8529 1.0762 1.0232 -0.1455 0.0870  0.0316  130 HIS B CD2 
3084 C CE1 . HIS B 123 ? 0.8739 1.0489 1.0250 -0.1718 0.0754  0.0575  130 HIS B CE1 
3085 N NE2 . HIS B 123 ? 0.8573 1.0621 1.0339 -0.1498 0.0787  0.0395  130 HIS B NE2 
3086 N N   . GLY B 124 ? 0.8668 1.1088 0.9530 -0.1590 0.1117  0.0242  131 GLY B N   
3087 C CA  . GLY B 124 ? 0.8758 1.1292 0.9336 -0.1667 0.1199  0.0206  131 GLY B CA  
3088 C C   . GLY B 124 ? 0.8872 1.2018 0.9607 -0.1573 0.1349  -0.0045 131 GLY B C   
3089 O O   . GLY B 124 ? 0.9727 1.3129 1.0221 -0.1737 0.1481  -0.0076 131 GLY B O   
3090 N N   . LYS B 125 ? 0.8805 1.2160 0.9914 -0.1304 0.1317  -0.0231 132 LYS B N   
3091 C CA  . LYS B 125 ? 0.8564 1.2532 0.9898 -0.1158 0.1426  -0.0515 132 LYS B CA  
3092 C C   . LYS B 125 ? 0.9011 1.3546 1.0668 -0.1258 0.1525  -0.0609 132 LYS B C   
3093 O O   . LYS B 125 ? 0.9562 1.4589 1.1528 -0.1059 0.1559  -0.0872 132 LYS B O   
3094 C CB  . LYS B 125 ? 0.8320 1.2125 0.9836 -0.0777 0.1286  -0.0685 132 LYS B CB  
3095 C CG  . LYS B 125 ? 0.7944 1.1203 0.9211 -0.0673 0.1165  -0.0608 132 LYS B CG  
3096 C CD  . LYS B 125 ? 0.8193 1.1592 0.9190 -0.0690 0.1244  -0.0702 132 LYS B CD  
3097 C CE  . LYS B 125 ? 0.9019 1.2646 1.0155 -0.0382 0.1214  -0.0997 132 LYS B CE  
3098 N NZ  . LYS B 125 ? 0.8930 1.2622 0.9780 -0.0362 0.1263  -0.1099 132 LYS B NZ  
3099 N N   . GLY B 126 ? 0.9269 1.3737 1.0861 -0.1556 0.1553  -0.0412 133 GLY B N   
3100 C CA  . GLY B 126 ? 0.9612 1.4598 1.1505 -0.1696 0.1635  -0.0482 133 GLY B CA  
3101 C C   . GLY B 126 ? 0.9167 1.4177 1.1461 -0.1465 0.1501  -0.0578 133 GLY B C   
3102 O O   . GLY B 126 ? 0.9899 1.5394 1.2480 -0.1557 0.1554  -0.0671 133 GLY B O   
3103 N N   . VAL B 127 ? 0.9763 1.4246 1.2060 -0.1191 0.1324  -0.0548 134 VAL B N   
3104 C CA  . VAL B 127 ? 0.9854 1.4261 1.2447 -0.0955 0.1175  -0.0632 134 VAL B CA  
3105 C C   . VAL B 127 ? 0.8932 1.2927 1.1465 -0.1111 0.1090  -0.0403 134 VAL B C   
3106 O O   . VAL B 127 ? 1.0885 1.4333 1.3149 -0.1172 0.1035  -0.0200 134 VAL B O   
3107 C CB  . VAL B 127 ? 0.9402 1.3393 1.1968 -0.0611 0.1025  -0.0703 134 VAL B CB  
3108 C CG1 . VAL B 127 ? 0.9538 1.3404 1.2334 -0.0390 0.0863  -0.0780 134 VAL B CG1 
3109 C CG2 . VAL B 127 ? 0.9882 1.4184 1.2462 -0.0431 0.1075  -0.0935 134 VAL B CG2 
3110 N N   . ILE B 128 ? 0.9061 1.3335 1.1854 -0.1159 0.1066  -0.0455 135 ILE B N   
3111 C CA  . ILE B 128 ? 0.8509 1.2377 1.1283 -0.1217 0.0944  -0.0292 135 ILE B CA  
3112 C C   . ILE B 128 ? 0.8461 1.2117 1.1388 -0.0877 0.0783  -0.0404 135 ILE B C   
3113 O O   . ILE B 128 ? 0.8493 1.2551 1.1694 -0.0689 0.0753  -0.0634 135 ILE B O   
3114 C CB  . ILE B 128 ? 0.9998 1.4268 1.2953 -0.1473 0.0986  -0.0292 135 ILE B CB  
3115 C CG1 . ILE B 128 ? 1.0832 1.5360 1.3603 -0.1849 0.1160  -0.0196 135 ILE B CG1 
3116 C CG2 . ILE B 128 ? 0.9789 1.3596 1.2690 -0.1525 0.0841  -0.0131 135 ILE B CG2 
3117 C CD1 . ILE B 128 ? 1.2043 1.7408 1.5063 -0.1923 0.1336  -0.0422 135 ILE B CD1 
3118 N N   . HIS B 129 ? 0.8010 1.1040 1.0748 -0.0802 0.0674  -0.0251 136 HIS B N   
3119 C CA  . HIS B 129 ? 0.8050 1.0781 1.0838 -0.0523 0.0521  -0.0319 136 HIS B CA  
3120 C C   . HIS B 129 ? 0.8358 1.1279 1.1375 -0.0479 0.0424  -0.0408 136 HIS B C   
3121 O O   . HIS B 129 ? 0.8164 1.1201 1.1343 -0.0237 0.0318  -0.0591 136 HIS B O   
3122 C CB  . HIS B 129 ? 0.7487 0.9563 1.0019 -0.0510 0.0458  -0.0128 136 HIS B CB  
3123 C CG  . HIS B 129 ? 0.7430 0.9160 0.9911 -0.0259 0.0341  -0.0184 136 HIS B CG  
3124 N ND1 . HIS B 129 ? 0.7752 0.9449 1.0332 -0.0088 0.0209  -0.0289 136 HIS B ND1 
3125 C CD2 . HIS B 129 ? 0.7661 0.9027 0.9972 -0.0172 0.0325  -0.0139 136 HIS B CD2 
3126 C CE1 . HIS B 129 ? 0.7086 0.8380 0.9517 0.0083  0.0119  -0.0297 136 HIS B CE1 
3127 N NE2 . HIS B 129 ? 0.7124 0.8230 0.9406 0.0024  0.0196  -0.0206 136 HIS B NE2 
3128 N N   . LYS B 130 ? 0.7171 1.0068 1.0172 -0.0706 0.0433  -0.0277 137 LYS B N   
3129 C CA  . LYS B 130 ? 0.8231 1.1277 1.1427 -0.0718 0.0331  -0.0333 137 LYS B CA  
3130 C C   . LYS B 130 ? 0.8177 1.0695 1.1258 -0.0533 0.0157  -0.0291 137 LYS B C   
3131 O O   . LYS B 130 ? 0.8799 1.1359 1.1991 -0.0545 0.0051  -0.0319 137 LYS B O   
3132 C CB  . LYS B 130 ? 0.8247 1.1997 1.1830 -0.0634 0.0333  -0.0595 137 LYS B CB  
3133 C CG  . LYS B 130 ? 0.8488 1.2864 1.2203 -0.0809 0.0530  -0.0682 137 LYS B CG  
3134 C CD  . LYS B 130 ? 0.9178 1.4193 1.3257 -0.0588 0.0521  -0.1000 137 LYS B CD  
3135 C CE  . LYS B 130 ? 0.9715 1.5397 1.3907 -0.0763 0.0745  -0.1106 137 LYS B CE  
3136 N NZ  . LYS B 130 ? 0.9538 1.5907 1.4107 -0.0536 0.0748  -0.1448 137 LYS B NZ  
3137 N N   . ASP B 131 ? 0.8809 1.0838 1.1654 -0.0387 0.0128  -0.0222 138 ASP B N   
3138 C CA  . ASP B 131 ? 0.8311 0.9845 1.0999 -0.0211 -0.0018 -0.0196 138 ASP B CA  
3139 C C   . ASP B 131 ? 0.7284 0.8300 0.9677 -0.0192 0.0022  -0.0051 138 ASP B C   
3140 O O   . ASP B 131 ? 0.6991 0.7685 0.9248 -0.0026 -0.0052 -0.0073 138 ASP B O   
3141 C CB  . ASP B 131 ? 0.8523 1.0169 1.1347 0.0053  -0.0162 -0.0401 138 ASP B CB  
3142 C CG  . ASP B 131 ? 0.8633 0.9811 1.1285 0.0194  -0.0345 -0.0381 138 ASP B CG  
3143 O OD1 . ASP B 131 ? 0.9412 1.0260 1.1884 0.0087  -0.0352 -0.0233 138 ASP B OD1 
3144 O OD2 . ASP B 131 ? 0.9123 1.0240 1.1792 0.0425  -0.0500 -0.0527 138 ASP B OD2 
3145 N N   . LEU B 132 ? 0.8657 0.9586 1.0943 -0.0374 0.0127  0.0094  139 LEU B N   
3146 C CA  . LEU B 132 ? 0.7454 0.7972 0.9520 -0.0366 0.0165  0.0213  139 LEU B CA  
3147 C C   . LEU B 132 ? 0.7551 0.7665 0.9454 -0.0326 0.0091  0.0282  139 LEU B C   
3148 O O   . LEU B 132 ? 0.7005 0.7100 0.8908 -0.0403 0.0046  0.0317  139 LEU B O   
3149 C CB  . LEU B 132 ? 0.7773 0.8327 0.9781 -0.0543 0.0263  0.0321  139 LEU B CB  
3150 C CG  . LEU B 132 ? 0.8481 0.8685 1.0317 -0.0547 0.0292  0.0428  139 LEU B CG  
3151 C CD1 . LEU B 132 ? 0.8201 0.8337 1.0019 -0.0425 0.0312  0.0376  139 LEU B CD1 
3152 C CD2 . LEU B 132 ? 0.8796 0.9035 1.0568 -0.0714 0.0337  0.0520  139 LEU B CD2 
3153 N N   . LYS B 133 ? 0.7375 0.7170 0.9125 -0.0214 0.0074  0.0292  140 LYS B N   
3154 C CA  . LYS B 133 ? 0.6995 0.6403 0.8541 -0.0175 0.0024  0.0346  140 LYS B CA  
3155 C C   . LYS B 133 ? 0.7543 0.6655 0.8915 -0.0125 0.0062  0.0377  140 LYS B C   
3156 O O   . LYS B 133 ? 0.8334 0.7512 0.9751 -0.0075 0.0067  0.0327  140 LYS B O   
3157 C CB  . LYS B 133 ? 0.7239 0.6613 0.8780 -0.0072 -0.0120 0.0265  140 LYS B CB  
3158 C CG  . LYS B 133 ? 0.7447 0.6837 0.9012 0.0092  -0.0215 0.0145  140 LYS B CG  
3159 C CD  . LYS B 133 ? 0.7669 0.7153 0.9321 0.0212  -0.0387 0.0024  140 LYS B CD  
3160 C CE  . LYS B 133 ? 0.8147 0.7836 0.9946 0.0380  -0.0472 -0.0141 140 LYS B CE  
3161 N NZ  . LYS B 133 ? 0.8381 0.8153 1.0278 0.0558  -0.0680 -0.0300 140 LYS B NZ  
3162 N N   . PRO B 134 ? 0.7373 0.6168 0.8539 -0.0146 0.0087  0.0449  141 PRO B N   
3163 C CA  . PRO B 134 ? 0.7307 0.5848 0.8305 -0.0146 0.0140  0.0482  141 PRO B CA  
3164 C C   . PRO B 134 ? 0.7159 0.5540 0.8055 -0.0054 0.0048  0.0427  141 PRO B C   
3165 O O   . PRO B 134 ? 0.8120 0.6439 0.8992 -0.0075 0.0088  0.0433  141 PRO B O   
3166 C CB  . PRO B 134 ? 0.8179 0.6447 0.8953 -0.0174 0.0165  0.0537  141 PRO B CB  
3167 C CG  . PRO B 134 ? 0.8398 0.6811 0.9277 -0.0207 0.0163  0.0549  141 PRO B CG  
3168 C CD  . PRO B 134 ? 0.7906 0.6578 0.8979 -0.0185 0.0076  0.0495  141 PRO B CD  
3169 N N   . GLU B 135 ? 0.7368 0.5674 0.8208 0.0053  -0.0098 0.0363  142 GLU B N   
3170 C CA  . GLU B 135 ? 0.7985 0.6115 0.8725 0.0183  -0.0243 0.0282  142 GLU B CA  
3171 C C   . GLU B 135 ? 0.8237 0.6631 0.9185 0.0239  -0.0241 0.0192  142 GLU B C   
3172 O O   . GLU B 135 ? 1.0536 0.8693 1.1347 0.0313  -0.0327 0.0152  142 GLU B O   
3173 C CB  . GLU B 135 ? 0.8087 0.6174 0.8803 0.0321  -0.0431 0.0194  142 GLU B CB  
3174 C CG  . GLU B 135 ? 0.9405 0.6994 0.9735 0.0328  -0.0521 0.0260  142 GLU B CG  
3175 C CD  . GLU B 135 ? 0.9220 0.6675 0.9479 0.0506  -0.0769 0.0152  142 GLU B CD  
3176 O OE1 . GLU B 135 ? 0.9339 0.6743 0.9536 0.0510  -0.0829 0.0161  142 GLU B OE1 
3177 O OE2 . GLU B 135 ? 0.9361 0.6756 0.9626 0.0656  -0.0922 0.0045  142 GLU B OE2 
3178 N N   . ASN B 136 ? 0.8902 0.7745 1.0135 0.0193  -0.0149 0.0164  143 ASN B N   
3179 C CA  . ASN B 136 ? 0.8201 0.7342 0.9616 0.0224  -0.0115 0.0080  143 ASN B CA  
3180 C C   . ASN B 136 ? 0.8256 0.7376 0.9656 0.0106  0.0015  0.0163  143 ASN B C   
3181 O O   . ASN B 136 ? 0.7504 0.6865 0.9027 0.0114  0.0051  0.0104  143 ASN B O   
3182 C CB  . ASN B 136 ? 0.8331 0.7987 1.0028 0.0213  -0.0085 -0.0001 143 ASN B CB  
3183 C CG  . ASN B 136 ? 0.7640 0.7488 0.9467 0.0389  -0.0230 -0.0178 143 ASN B CG  
3184 O OD1 . ASN B 136 ? 0.7021 0.6687 0.8764 0.0554  -0.0356 -0.0278 143 ASN B OD1 
3185 N ND2 . ASN B 136 ? 0.6745 0.6984 0.8793 0.0351  -0.0222 -0.0232 143 ASN B ND2 
3186 N N   . ILE B 137 ? 0.8724 0.7579 0.9977 0.0004  0.0081  0.0281  144 ILE B N   
3187 C CA  . ILE B 137 ? 0.7232 0.6080 0.8501 -0.0096 0.0183  0.0342  144 ILE B CA  
3188 C C   . ILE B 137 ? 0.7292 0.5762 0.8346 -0.0109 0.0151  0.0368  144 ILE B C   
3189 O O   . ILE B 137 ? 0.8030 0.6251 0.8906 -0.0156 0.0163  0.0432  144 ILE B O   
3190 C CB  . ILE B 137 ? 0.6987 0.5913 0.8308 -0.0205 0.0285  0.0431  144 ILE B CB  
3191 C CG1 . ILE B 137 ? 0.6729 0.5968 0.8208 -0.0227 0.0295  0.0419  144 ILE B CG1 
3192 C CG2 . ILE B 137 ? 0.6207 0.5116 0.7559 -0.0287 0.0365  0.0472  144 ILE B CG2 
3193 C CD1 . ILE B 137 ? 0.6877 0.6103 0.8352 -0.0304 0.0331  0.0494  144 ILE B CD1 
3194 N N   . LEU B 138 ? 0.7998 0.6415 0.9042 -0.0081 0.0106  0.0318  145 LEU B N   
3195 C CA  . LEU B 138 ? 0.8152 0.6173 0.8966 -0.0118 0.0051  0.0342  145 LEU B CA  
3196 C C   . LEU B 138 ? 0.7843 0.5908 0.8725 -0.0266 0.0163  0.0399  145 LEU B C   
3197 O O   . LEU B 138 ? 0.6715 0.5080 0.7806 -0.0273 0.0218  0.0378  145 LEU B O   
3198 C CB  . LEU B 138 ? 0.7671 0.5566 0.8418 0.0031  -0.0114 0.0227  145 LEU B CB  
3199 C CG  . LEU B 138 ? 0.7971 0.5941 0.8742 0.0217  -0.0243 0.0121  145 LEU B CG  
3200 C CD1 . LEU B 138 ? 0.7837 0.5599 0.8499 0.0391  -0.0437 -0.0013 145 LEU B CD1 
3201 C CD2 . LEU B 138 ? 0.8555 0.6291 0.9151 0.0215  -0.0287 0.0181  145 LEU B CD2 
3202 N N   . VAL B 139 ? 0.7857 0.5618 0.8547 -0.0393 0.0184  0.0465  146 VAL B N   
3203 C CA  . VAL B 139 ? 0.7219 0.5065 0.8001 -0.0559 0.0307  0.0514  146 VAL B CA  
3204 C C   . VAL B 139 ? 0.7899 0.5425 0.8504 -0.0657 0.0239  0.0521  146 VAL B C   
3205 O O   . VAL B 139 ? 0.8292 0.5409 0.8583 -0.0684 0.0156  0.0556  146 VAL B O   
3206 C CB  . VAL B 139 ? 0.7810 0.5653 0.8532 -0.0669 0.0440  0.0585  146 VAL B CB  
3207 C CG1 . VAL B 139 ? 0.7983 0.6039 0.8889 -0.0816 0.0575  0.0596  146 VAL B CG1 
3208 C CG2 . VAL B 139 ? 0.7346 0.5378 0.8156 -0.0568 0.0464  0.0580  146 VAL B CG2 
3209 N N   . ASP B 140 ? 0.8493 0.6166 0.9270 -0.0716 0.0252  0.0492  147 ASP B N   
3210 C CA  . ASP B 140 ? 0.8342 0.5729 0.8978 -0.0859 0.0195  0.0505  147 ASP B CA  
3211 C C   . ASP B 140 ? 0.9076 0.6494 0.9724 -0.1109 0.0348  0.0580  147 ASP B C   
3212 O O   . ASP B 140 ? 0.9166 0.6862 0.9959 -0.1132 0.0493  0.0599  147 ASP B O   
3213 C CB  . ASP B 140 ? 0.7864 0.5353 0.8646 -0.0795 0.0102  0.0419  147 ASP B CB  
3214 C CG  . ASP B 140 ? 0.7974 0.5892 0.9092 -0.0838 0.0202  0.0400  147 ASP B CG  
3215 O OD1 . ASP B 140 ? 0.9629 0.7725 1.0888 -0.0977 0.0330  0.0442  147 ASP B OD1 
3216 O OD2 . ASP B 140 ? 0.7798 0.5875 0.9029 -0.0724 0.0138  0.0327  147 ASP B OD2 
3217 N N   . ASN B 141 ? 1.0327 0.7475 1.0823 -0.1297 0.0311  0.0610  148 ASN B N   
3218 C CA  . ASN B 141 ? 1.0083 0.7289 1.0583 -0.1580 0.0470  0.0672  148 ASN B CA  
3219 C C   . ASN B 141 ? 0.9563 0.7336 1.0511 -0.1636 0.0621  0.0618  148 ASN B C   
3220 O O   . ASN B 141 ? 0.9013 0.6989 1.0036 -0.1804 0.0795  0.0636  148 ASN B O   
3221 C CB  . ASN B 141 ? 1.1590 0.8350 1.1800 -0.1811 0.0385  0.0723  148 ASN B CB  
3222 C CG  . ASN B 141 ? 1.3391 0.9684 1.3127 -0.1976 0.0403  0.0835  148 ASN B CG  
3223 O OD1 . ASN B 141 ? 1.3791 1.0265 1.3520 -0.2095 0.0596  0.0880  148 ASN B OD1 
3224 N ND2 . ASN B 141 ? 1.4726 1.0390 1.4032 -0.1978 0.0191  0.0874  148 ASN B ND2 
3225 N N   . ASP B 142 ? 0.9242 0.7270 1.0469 -0.1483 0.0549  0.0540  149 ASP B N   
3226 C CA  . ASP B 142 ? 0.9338 0.7870 1.0975 -0.1462 0.0634  0.0475  149 ASP B CA  
3227 C C   . ASP B 142 ? 0.8393 0.7170 1.0150 -0.1277 0.0690  0.0461  149 ASP B C   
3228 O O   . ASP B 142 ? 0.8901 0.8011 1.0946 -0.1205 0.0700  0.0403  149 ASP B O   
3229 C CB  . ASP B 142 ? 1.0241 0.8861 1.2054 -0.1402 0.0502  0.0406  149 ASP B CB  
3230 C CG  . ASP B 142 ? 1.2505 1.0945 1.4271 -0.1610 0.0443  0.0404  149 ASP B CG  
3231 O OD1 . ASP B 142 ? 1.3278 1.1855 1.5150 -0.1839 0.0559  0.0416  149 ASP B OD1 
3232 O OD2 . ASP B 142 ? 1.2614 1.0795 1.4245 -0.1549 0.0280  0.0378  149 ASP B OD2 
3233 N N   . PHE B 143 ? 0.7907 0.6487 0.9427 -0.1201 0.0701  0.0511  150 PHE B N   
3234 C CA  . PHE B 143 ? 0.8638 0.7374 1.0218 -0.1042 0.0729  0.0506  150 PHE B CA  
3235 C C   . PHE B 143 ? 0.8386 0.7245 1.0080 -0.0868 0.0627  0.0472  150 PHE B C   
3236 O O   . PHE B 143 ? 0.9114 0.8112 1.0873 -0.0773 0.0643  0.0472  150 PHE B O   
3237 C CB  . PHE B 143 ? 0.8667 0.7699 1.0436 -0.1088 0.0871  0.0479  150 PHE B CB  
3238 C CG  . PHE B 143 ? 0.8729 0.7647 1.0307 -0.1241 0.1002  0.0517  150 PHE B CG  
3239 C CD1 . PHE B 143 ? 0.8641 0.7386 0.9977 -0.1185 0.1033  0.0559  150 PHE B CD1 
3240 C CD2 . PHE B 143 ? 1.0389 0.9364 1.2001 -0.1463 0.1095  0.0511  150 PHE B CD2 
3241 C CE1 . PHE B 143 ? 1.0444 0.9053 1.1538 -0.1337 0.1157  0.0598  150 PHE B CE1 
3242 C CE2 . PHE B 143 ? 1.1001 0.9871 1.2386 -0.1642 0.1239  0.0554  150 PHE B CE2 
3243 C CZ  . PHE B 143 ? 1.0774 0.9444 1.1876 -0.1575 0.1270  0.0600  150 PHE B CZ  
3244 N N   . HIS B 144 ? 0.8492 0.7275 1.0169 -0.0837 0.0519  0.0443  151 HIS B N   
3245 C CA  . HIS B 144 ? 0.7913 0.6804 0.9634 -0.0695 0.0441  0.0409  151 HIS B CA  
3246 C C   . HIS B 144 ? 0.8354 0.7093 0.9887 -0.0594 0.0399  0.0416  151 HIS B C   
3247 O O   . HIS B 144 ? 0.8475 0.6935 0.9812 -0.0611 0.0360  0.0427  151 HIS B O   
3248 C CB  . HIS B 144 ? 0.8291 0.7181 1.0050 -0.0689 0.0348  0.0354  151 HIS B CB  
3249 C CG  . HIS B 144 ? 0.8333 0.7395 1.0305 -0.0776 0.0357  0.0330  151 HIS B CG  
3250 N ND1 . HIS B 144 ? 0.7809 0.7116 0.9959 -0.0730 0.0361  0.0316  151 HIS B ND1 
3251 C CD2 . HIS B 144 ? 0.9099 0.8119 1.1137 -0.0904 0.0339  0.0308  151 HIS B CD2 
3252 C CE1 . HIS B 144 ? 0.7515 0.6949 0.9857 -0.0802 0.0341  0.0272  151 HIS B CE1 
3253 N NE2 . HIS B 144 ? 0.9543 0.8835 1.1840 -0.0921 0.0338  0.0266  151 HIS B NE2 
3254 N N   . ILE B 145 ? 0.7348 0.6259 0.8932 -0.0501 0.0396  0.0410  152 ILE B N   
3255 C CA  . ILE B 145 ? 0.7496 0.6364 0.8975 -0.0407 0.0362  0.0399  152 ILE B CA  
3256 C C   . ILE B 145 ? 0.6872 0.5856 0.8357 -0.0304 0.0291  0.0318  152 ILE B C   
3257 O O   . ILE B 145 ? 0.6731 0.5861 0.8286 -0.0308 0.0286  0.0289  152 ILE B O   
3258 C CB  . ILE B 145 ? 0.7510 0.6494 0.9029 -0.0402 0.0415  0.0444  152 ILE B CB  
3259 C CG1 . ILE B 145 ? 0.7043 0.6266 0.8686 -0.0405 0.0426  0.0451  152 ILE B CG1 
3260 C CG2 . ILE B 145 ? 0.7130 0.6011 0.8620 -0.0478 0.0490  0.0495  152 ILE B CG2 
3261 C CD1 . ILE B 145 ? 0.6762 0.6141 0.8397 -0.0357 0.0397  0.0423  152 ILE B CD1 
3262 N N   . LYS B 146 ? 0.6927 0.5856 0.8332 -0.0205 0.0233  0.0269  153 LYS B N   
3263 C CA  . LYS B 146 ? 0.6684 0.5823 0.8133 -0.0091 0.0187  0.0163  153 LYS B CA  
3264 C C   . LYS B 146 ? 0.6930 0.6188 0.8409 -0.0026 0.0176  0.0140  153 LYS B C   
3265 O O   . LYS B 146 ? 0.7339 0.6367 0.8716 0.0009  0.0121  0.0155  153 LYS B O   
3266 C CB  . LYS B 146 ? 0.6890 0.5852 0.8240 0.0015  0.0072  0.0056  153 LYS B CB  
3267 C CG  . LYS B 146 ? 0.7294 0.6165 0.8625 -0.0045 0.0059  0.0054  153 LYS B CG  
3268 C CD  . LYS B 146 ? 0.6747 0.5378 0.7940 0.0071  -0.0086 -0.0061 153 LYS B CD  
3269 C CE  . LYS B 146 ? 0.7363 0.5792 0.8500 -0.0016 -0.0129 -0.0049 153 LYS B CE  
3270 N NZ  . LYS B 146 ? 0.8049 0.6744 0.9280 -0.0006 -0.0101 -0.0105 153 LYS B NZ  
3271 N N   . ILE B 147 ? 0.6760 0.6371 0.8361 -0.0028 0.0223  0.0104  154 ILE B N   
3272 C CA  . ILE B 147 ? 0.6496 0.6307 0.8177 0.0016  0.0211  0.0059  154 ILE B CA  
3273 C C   . ILE B 147 ? 0.6249 0.6133 0.7956 0.0196  0.0107  -0.0111 154 ILE B C   
3274 O O   . ILE B 147 ? 0.6414 0.6422 0.8137 0.0266  0.0095  -0.0217 154 ILE B O   
3275 C CB  . ILE B 147 ? 0.6593 0.6763 0.8380 -0.0096 0.0304  0.0087  154 ILE B CB  
3276 C CG1 . ILE B 147 ? 0.7267 0.7289 0.9003 -0.0238 0.0358  0.0242  154 ILE B CG1 
3277 C CG2 . ILE B 147 ? 0.6813 0.7244 0.8719 -0.0075 0.0290  0.0024  154 ILE B CG2 
3278 C CD1 . ILE B 147 ? 0.6551 0.6755 0.8285 -0.0360 0.0418  0.0292  154 ILE B CD1 
3279 N N   . ALA B 148 ? 0.6787 1.2429 1.3107 -0.1338 0.0649  0.2435  155 ALA B N   
3280 C CA  . ALA B 148 ? 0.6538 1.2188 1.2533 -0.1367 0.0787  0.2596  155 ALA B CA  
3281 C C   . ALA B 148 ? 0.6402 1.1996 1.2380 -0.1412 0.0723  0.2914  155 ALA B C   
3282 O O   . ALA B 148 ? 0.6364 1.1865 1.2553 -0.1446 0.0603  0.2987  155 ALA B O   
3283 C CB  . ALA B 148 ? 0.6413 1.1842 1.2250 -0.1475 0.0987  0.2344  155 ALA B CB  
3284 N N   A ASP B 149 ? 0.6417 1.2082 1.2185 -0.1409 0.0797  0.3072  156 ASP B N   
3285 N N   B ASP B 149 ? 0.6486 1.2151 1.2253 -0.1409 0.0797  0.3072  156 ASP B N   
3286 C CA  A ASP B 149 ? 0.6426 1.2067 1.2235 -0.1459 0.0759  0.3310  156 ASP B CA  
3287 C CA  B ASP B 149 ? 0.6537 1.2182 1.2344 -0.1458 0.0760  0.3312  156 ASP B CA  
3288 C C   A ASP B 149 ? 0.6347 1.1840 1.1942 -0.1490 0.0850  0.3213  156 ASP B C   
3289 C C   B ASP B 149 ? 0.6399 1.1892 1.1999 -0.1491 0.0848  0.3217  156 ASP B C   
3290 O O   A ASP B 149 ? 0.6420 1.2057 1.1898 -0.1447 0.0887  0.3305  156 ASP B O   
3291 O O   B ASP B 149 ? 0.6455 1.2090 1.1955 -0.1452 0.0878  0.3322  156 ASP B O   
3292 C CB  A ASP B 149 ? 0.6532 1.2431 1.2330 -0.1407 0.0743  0.3584  156 ASP B CB  
3293 C CB  B ASP B 149 ? 0.6747 1.2654 1.2534 -0.1405 0.0750  0.3583  156 ASP B CB  
3294 C CG  A ASP B 149 ? 0.6704 1.2622 1.2642 -0.1479 0.0730  0.3792  156 ASP B CG  
3295 C CG  B ASP B 149 ? 0.7043 1.2958 1.2995 -0.1480 0.0721  0.3804  156 ASP B CG  
3296 O OD1 A ASP B 149 ? 0.6793 1.2520 1.2890 -0.1551 0.0665  0.3765  156 ASP B OD1 
3297 O OD1 B ASP B 149 ? 0.7241 1.3014 1.3251 -0.1533 0.0711  0.3736  156 ASP B OD1 
3298 O OD2 A ASP B 149 ? 0.6352 1.2484 1.2263 -0.1466 0.0792  0.3965  156 ASP B OD2 
3299 O OD2 B ASP B 149 ? 0.6907 1.2942 1.2913 -0.1487 0.0712  0.4032  156 ASP B OD2 
3300 N N   . LEU B 150 ? 0.6509 1.1675 1.2023 -0.1560 0.0885  0.3003  157 LEU B N   
3301 C CA  . LEU B 150 ? 0.6693 1.1553 1.1875 -0.1585 0.0954  0.2880  157 LEU B CA  
3302 C C   . LEU B 150 ? 0.6876 1.1654 1.2074 -0.1578 0.0842  0.3026  157 LEU B C   
3303 O O   . LEU B 150 ? 0.6888 1.1483 1.1796 -0.1541 0.0845  0.2964  157 LEU B O   
3304 C CB  . LEU B 150 ? 0.6489 1.0940 1.1516 -0.1683 0.1049  0.2613  157 LEU B CB  
3305 C CG  . LEU B 150 ? 0.6509 1.1015 1.1552 -0.1705 0.1193  0.2373  157 LEU B CG  
3306 C CD1 . LEU B 150 ? 0.6387 1.0512 1.1382 -0.1840 0.1316  0.2095  157 LEU B CD1 
3307 C CD2 . LEU B 150 ? 0.6589 1.1130 1.1323 -0.1657 0.1317  0.2291  157 LEU B CD2 
3308 N N   . GLY B 151 ? 0.7303 1.2196 1.2845 -0.1607 0.0727  0.3197  158 GLY B N   
3309 C CA  . GLY B 151 ? 0.7175 1.2096 1.2869 -0.1598 0.0615  0.3329  158 GLY B CA  
3310 C C   . GLY B 151 ? 0.7524 1.2855 1.3383 -0.1549 0.0632  0.3499  158 GLY B C   
3311 O O   . GLY B 151 ? 0.8092 1.3504 1.4163 -0.1548 0.0557  0.3568  158 GLY B O   
3312 N N   . LEU B 152 ? 0.7589 1.3181 1.3378 -0.1510 0.0734  0.3548  159 LEU B N   
3313 C CA  . LEU B 152 ? 0.7221 1.3186 1.3091 -0.1470 0.0798  0.3690  159 LEU B CA  
3314 C C   . LEU B 152 ? 0.7333 1.3487 1.3559 -0.1542 0.0782  0.3909  159 LEU B C   
3315 O O   . LEU B 152 ? 0.7726 1.4128 1.4110 -0.1546 0.0835  0.3979  159 LEU B O   
3316 C CB  . LEU B 152 ? 0.7119 1.3106 1.2835 -0.1395 0.0807  0.3571  159 LEU B CB  
3317 C CG  . LEU B 152 ? 0.6839 1.2580 1.2132 -0.1336 0.0847  0.3362  159 LEU B CG  
3318 C CD1 . LEU B 152 ? 0.7037 1.2698 1.2169 -0.1252 0.0792  0.3251  159 LEU B CD1 
3319 C CD2 . LEU B 152 ? 0.6618 1.2573 1.1777 -0.1296 0.0965  0.3361  159 LEU B CD2 
3320 N N   . ALA B 153 ? 0.7418 1.3444 1.3777 -0.1606 0.0721  0.3998  160 ALA B N   
3321 C CA  . ALA B 153 ? 0.7654 1.3761 1.4310 -0.1696 0.0710  0.4209  160 ALA B CA  
3322 C C   . ALA B 153 ? 0.7798 1.4148 1.4403 -0.1711 0.0844  0.4406  160 ALA B C   
3323 O O   . ALA B 153 ? 0.8043 1.4515 1.4882 -0.1804 0.0915  0.4549  160 ALA B O   
3324 C CB  . ALA B 153 ? 0.7718 1.3581 1.4470 -0.1743 0.0594  0.4242  160 ALA B CB  
3325 N N   . SER B 154 ? 0.7641 1.4039 1.3934 -0.1626 0.0891  0.4393  161 SER B N   
3326 C CA  . SER B 154 ? 0.8353 1.4917 1.4467 -0.1617 0.1017  0.4564  161 SER B CA  
3327 C C   . SER B 154 ? 0.8982 1.5850 1.5051 -0.1587 0.1172  0.4521  161 SER B C   
3328 O O   . SER B 154 ? 0.9702 1.6707 1.5604 -0.1592 0.1310  0.4653  161 SER B O   
3329 C CB  . SER B 154 ? 0.9216 1.5669 1.5014 -0.1513 0.0952  0.4552  161 SER B CB  
3330 O OG  . SER B 154 ? 1.0192 1.6384 1.6056 -0.1523 0.0794  0.4574  161 SER B OG  
3331 N N   . PHE B 155 ? 0.8830 1.5762 1.5010 -0.1550 0.1143  0.4330  162 PHE B N   
3332 C CA  . PHE B 155 ? 0.8284 1.5469 1.4395 -0.1479 0.1237  0.4224  162 PHE B CA  
3333 C C   . PHE B 155 ? 0.8228 1.5495 1.4667 -0.1497 0.1193  0.4106  162 PHE B C   
3334 O O   . PHE B 155 ? 0.8204 1.5282 1.4583 -0.1430 0.1061  0.3925  162 PHE B O   
3335 C CB  . PHE B 155 ? 0.8153 1.5242 1.3925 -0.1357 0.1196  0.4054  162 PHE B CB  
3336 C CG  . PHE B 155 ? 0.7889 1.4914 1.3419 -0.1318 0.1197  0.4120  162 PHE B CG  
3337 C CD1 . PHE B 155 ? 0.7943 1.5140 1.3307 -0.1295 0.1303  0.4266  162 PHE B CD1 
3338 C CD2 . PHE B 155 ? 0.8054 1.4825 1.3534 -0.1305 0.1086  0.4023  162 PHE B CD2 
3339 C CE1 . PHE B 155 ? 0.8105 1.5195 1.3219 -0.1228 0.1253  0.4314  162 PHE B CE1 
3340 C CE2 . PHE B 155 ? 0.8043 1.4770 1.3364 -0.1245 0.1045  0.4040  162 PHE B CE2 
3341 C CZ  . PHE B 155 ? 0.7974 1.4845 1.3097 -0.1193 0.1105  0.4190  162 PHE B CZ  
3342 N N   . LYS B 156 ? 0.9262 1.6778 1.6030 -0.1589 0.1306  0.4194  163 LYS B N   
3343 C CA  . LYS B 156 ? 0.9627 1.7250 1.6849 -0.1618 0.1244  0.4072  163 LYS B CA  
3344 C C   . LYS B 156 ? 0.9578 1.7319 1.6813 -0.1482 0.1167  0.3828  163 LYS B C   
3345 O O   . LYS B 156 ? 1.0096 1.7692 1.7496 -0.1427 0.0977  0.3662  163 LYS B O   
3346 C CB  . LYS B 156 ? 1.0801 1.8695 1.8428 -0.1776 0.1432  0.4194  163 LYS B CB  
3347 C CG  . LYS B 156 ? 1.1966 1.9657 1.9663 -0.1923 0.1457  0.4412  163 LYS B CG  
3348 C CD  . LYS B 156 ? 1.2044 1.9504 2.0013 -0.1937 0.1237  0.4340  163 LYS B CD  
3349 C CE  . LYS B 156 ? 1.2088 1.9172 1.9697 -0.1873 0.1071  0.4368  163 LYS B CE  
3350 N NZ  . LYS B 156 ? 1.1689 1.8537 1.9418 -0.1823 0.0847  0.4201  163 LYS B NZ  
3351 N N   . MET B 157 ? 0.9228 1.7194 1.6264 -0.1417 0.1293  0.3802  164 MET B N   
3352 C CA  . MET B 157 ? 0.8971 1.7057 1.6001 -0.1275 0.1220  0.3569  164 MET B CA  
3353 C C   . MET B 157 ? 0.8845 1.6521 1.5466 -0.1144 0.1018  0.3420  164 MET B C   
3354 O O   . MET B 157 ? 0.9812 1.7362 1.6476 -0.1039 0.0839  0.3217  164 MET B O   
3355 C CB  . MET B 157 ? 0.9205 1.7639 1.6117 -0.1246 0.1422  0.3586  164 MET B CB  
3356 C CG  . MET B 157 ? 0.9837 1.8644 1.7100 -0.1391 0.1671  0.3699  164 MET B CG  
3357 S SD  . MET B 157 ? 0.9792 1.8903 1.7828 -0.1451 0.1654  0.3503  164 MET B SD  
3358 C CE  . MET B 157 ? 0.9812 1.8689 1.8098 -0.1629 0.1629  0.3683  164 MET B CE  
3359 N N   . TRP B 158 ? 0.8131 1.5567 1.4347 -0.1150 0.1047  0.3499  165 TRP B N   
3360 C CA  . TRP B 158 ? 0.8223 1.5199 1.4038 -0.1080 0.0913  0.3361  165 TRP B CA  
3361 C C   . TRP B 158 ? 0.8730 1.5333 1.4623 -0.1119 0.0745  0.3320  165 TRP B C   
3362 O O   . TRP B 158 ? 0.9123 1.5324 1.4721 -0.1044 0.0606  0.3153  165 TRP B O   
3363 C CB  . TRP B 158 ? 0.7840 1.4705 1.3307 -0.1094 0.1011  0.3411  165 TRP B CB  
3364 C CG  . TRP B 158 ? 0.7601 1.4684 1.2848 -0.1009 0.1119  0.3369  165 TRP B CG  
3365 C CD1 . TRP B 158 ? 0.7539 1.5008 1.2863 -0.1011 0.1259  0.3492  165 TRP B CD1 
3366 C CD2 . TRP B 158 ? 0.7492 1.4370 1.2359 -0.0914 0.1100  0.3187  165 TRP B CD2 
3367 N NE1 . TRP B 158 ? 0.7660 1.5218 1.2714 -0.0909 0.1312  0.3391  165 TRP B NE1 
3368 C CE2 . TRP B 158 ? 0.7389 1.4600 1.2180 -0.0852 0.1218  0.3203  165 TRP B CE2 
3369 C CE3 . TRP B 158 ? 0.7802 1.4198 1.2337 -0.0883 0.1006  0.3011  165 TRP B CE3 
3370 C CZ2 . TRP B 158 ? 0.7722 1.4840 1.2177 -0.0756 0.1234  0.3043  165 TRP B CZ2 
3371 C CZ3 . TRP B 158 ? 0.7981 1.4232 1.2129 -0.0803 0.1042  0.2858  165 TRP B CZ3 
3372 C CH2 . TRP B 158 ? 0.7884 1.4519 1.2029 -0.0739 0.1149  0.2874  165 TRP B CH2 
3373 N N   . SER B 159 ? 0.9119 1.5805 1.5357 -0.1234 0.0756  0.3468  166 SER B N   
3374 C CA  . SER B 159 ? 0.9801 1.6166 1.6161 -0.1269 0.0589  0.3428  166 SER B CA  
3375 C C   . SER B 159 ? 0.9947 1.6331 1.6584 -0.1193 0.0417  0.3273  166 SER B C   
3376 O O   . SER B 159 ? 0.9932 1.5893 1.6381 -0.1125 0.0219  0.3129  166 SER B O   
3377 C CB  . SER B 159 ? 0.9647 1.6086 1.6305 -0.1408 0.0639  0.3624  166 SER B CB  
3378 O OG  . SER B 159 ? 0.9663 1.6481 1.6786 -0.1479 0.0718  0.3724  166 SER B OG  
3379 N N   . LYS B 160 ? 1.1065 1.7919 1.8146 -0.1206 0.0494  0.3285  167 LYS B N   
3380 C CA  . LYS B 160 ? 1.1260 1.8240 1.8714 -0.1113 0.0329  0.3077  167 LYS B CA  
3381 C C   . LYS B 160 ? 1.0925 1.7680 1.7997 -0.0916 0.0164  0.2849  167 LYS B C   
3382 O O   . LYS B 160 ? 1.1143 1.7717 1.8320 -0.0791 -0.0093 0.2639  167 LYS B O   
3383 C CB  . LYS B 160 ? 1.2320 1.9900 2.0373 -0.1198 0.0512  0.3108  167 LYS B CB  
3384 C CG  . LYS B 160 ? 1.2128 1.9858 2.0630 -0.1391 0.0631  0.3282  167 LYS B CG  
3385 C CD  . LYS B 160 ? 1.2202 1.9863 2.1188 -0.1381 0.0413  0.3126  167 LYS B CD  
3386 C CE  . LYS B 160 ? 1.2169 2.0010 2.1646 -0.1591 0.0564  0.3290  167 LYS B CE  
3387 N NZ  . LYS B 160 ? 1.2185 2.0006 2.2217 -0.1581 0.0349  0.3109  167 LYS B NZ  
3388 N N   . LEU B 161 ? 1.0367 1.7110 1.6996 -0.0880 0.0292  0.2878  168 LEU B N   
3389 C CA  . LEU B 161 ? 1.0031 1.6449 1.6167 -0.0708 0.0153  0.2686  168 LEU B CA  
3390 C C   . LEU B 161 ? 1.0437 1.6113 1.6033 -0.0650 -0.0052 0.2586  168 LEU B C   
3391 O O   . LEU B 161 ? 1.0450 1.5751 1.5700 -0.0489 -0.0257 0.2390  168 LEU B O   
3392 C CB  . LEU B 161 ? 0.9739 1.6287 1.5522 -0.0710 0.0362  0.2753  168 LEU B CB  
3393 C CG  . LEU B 161 ? 0.9688 1.5910 1.4925 -0.0560 0.0276  0.2580  168 LEU B CG  
3394 C CD1 . LEU B 161 ? 0.9892 1.6261 1.5348 -0.0391 0.0085  0.2367  168 LEU B CD1 
3395 C CD2 . LEU B 161 ? 0.9536 1.5959 1.4534 -0.0591 0.0507  0.2665  168 LEU B CD2 
3396 N N   . ASN B 162 ? 1.1133 1.6559 1.6614 -0.0777 0.0008  0.2711  169 ASN B N   
3397 C CA  . ASN B 162 ? 1.2105 1.6813 1.7091 -0.0756 -0.0147 0.2619  169 ASN B CA  
3398 C C   . ASN B 162 ? 1.2944 1.7478 1.8165 -0.0654 -0.0449 0.2484  169 ASN B C   
3399 O O   . ASN B 162 ? 1.4216 1.8225 1.8992 -0.0498 -0.0683 0.2295  169 ASN B O   
3400 C CB  . ASN B 162 ? 1.1835 1.6420 1.6770 -0.0926 0.0005  0.2765  169 ASN B CB  
3401 C CG  . ASN B 162 ? 1.1984 1.5811 1.6300 -0.0937 -0.0057 0.2656  169 ASN B CG  
3402 O OD1 . ASN B 162 ? 1.2577 1.5883 1.6500 -0.0820 -0.0263 0.2498  169 ASN B OD1 
3403 N ND2 . ASN B 162 ? 1.1103 1.4833 1.5312 -0.1077 0.0121  0.2725  169 ASN B ND2 
3404 N N   . ASN B 163 ? 1.3316 1.8264 1.9219 -0.0734 -0.0453 0.2567  170 ASN B N   
3405 C CA  . ASN B 163 ? 1.4156 1.9036 2.0437 -0.0647 -0.0738 0.2420  170 ASN B CA  
3406 C C   . ASN B 163 ? 1.3693 1.8920 2.0352 -0.0488 -0.0883 0.2219  170 ASN B C   
3407 O O   . ASN B 163 ? 1.4142 1.9993 2.1553 -0.0550 -0.0800 0.2224  170 ASN B O   
3408 C CB  . ASN B 163 ? 1.3842 1.9052 2.0757 -0.0812 -0.0661 0.2570  170 ASN B CB  
3409 C CG  . ASN B 163 ? 1.4176 1.9030 2.0785 -0.0939 -0.0582 0.2718  170 ASN B CG  
3410 O OD1 . ASN B 163 ? 1.3918 1.9042 2.0672 -0.1094 -0.0347 0.2923  170 ASN B OD1 
3411 N ND2 . ASN B 163 ? 1.4531 1.8734 2.0682 -0.0866 -0.0786 0.2598  170 ASN B ND2 
3412 N N   . GLU B 164 ? 1.3334 1.8123 1.9451 -0.0292 -0.1087 0.2026  171 GLU B N   
3413 C CA  . GLU B 164 ? 1.3647 1.8669 2.0039 -0.0097 -0.1285 0.1781  171 GLU B CA  
3414 C C   . GLU B 164 ? 1.4450 1.8707 2.0297 0.0153  -0.1715 0.1523  171 GLU B C   
3415 O O   . GLU B 164 ? 1.5544 1.9033 2.0525 0.0170  -0.1761 0.1558  171 GLU B O   
3416 C CB  . GLU B 164 ? 1.3516 1.8855 1.9749 -0.0092 -0.1063 0.1819  171 GLU B CB  
3417 C CG  . GLU B 164 ? 1.3974 1.9827 2.0763 0.0052  -0.1169 0.1589  171 GLU B CG  
3418 C CD  . GLU B 164 ? 1.4300 2.0308 2.0787 0.0111  -0.1029 0.1576  171 GLU B CD  
3419 O OE1 . GLU B 164 ? 1.5510 2.1617 2.1713 -0.0035 -0.0716 0.1804  171 GLU B OE1 
3420 O OE2 . GLU B 164 ? 1.4166 2.0208 2.0729 0.0318  -0.1254 0.1314  171 GLU B OE2 
3421 N N   . GLU B 165 ? 1.4861 1.9307 2.1200 0.0348  -0.2024 0.1244  172 GLU B N   
3422 C CA  . GLU B 165 ? 1.5702 1.9418 2.1573 0.0638  -0.2516 0.0954  172 GLU B CA  
3423 C C   . GLU B 165 ? 1.5962 1.9056 2.0874 0.0796  -0.2604 0.0885  172 GLU B C   
3424 O O   . GLU B 165 ? 1.5736 1.7876 1.9762 0.0933  -0.2866 0.0804  172 GLU B O   
3425 C CB  . GLU B 165 ? 1.6066 2.0243 2.2838 0.0823  -0.2837 0.0623  172 GLU B CB  
3426 C CG  . GLU B 165 ? 1.5513 2.0140 2.3184 0.0699  -0.2830 0.0620  172 GLU B CG  
3427 C CD  . GLU B 165 ? 1.6611 2.1703 2.5241 0.0885  -0.3150 0.0224  172 GLU B CD  
3428 O OE1 . GLU B 165 ? 1.6428 2.2095 2.5547 0.0936  -0.3082 0.0064  172 GLU B OE1 
3429 O OE2 . GLU B 165 ? 1.6816 2.1707 2.5742 0.0978  -0.3469 0.0051  172 GLU B OE2 
3430 N N   . HIS B 166 ? 1.5749 1.9343 2.0802 0.0766  -0.2373 0.0921  173 HIS B N   
3431 C CA  . HIS B 166 ? 1.6086 1.9177 2.0292 0.0885  -0.2400 0.0874  173 HIS B CA  
3432 C C   . HIS B 166 ? 1.5641 1.8047 1.8868 0.0728  -0.2153 0.1095  173 HIS B C   
3433 O O   . HIS B 166 ? 1.5749 1.7419 1.8086 0.0841  -0.2256 0.1017  173 HIS B O   
3434 C CB  . HIS B 166 ? 1.6223 2.0095 2.0886 0.0871  -0.2174 0.0868  173 HIS B CB  
3435 C CG  . HIS B 166 ? 1.6547 2.1071 2.2123 0.1030  -0.2384 0.0589  173 HIS B CG  
3436 N ND1 . HIS B 166 ? 1.6102 2.1620 2.2666 0.0869  -0.2096 0.0641  173 HIS B ND1 
3437 C CD2 . HIS B 166 ? 1.7004 2.1308 2.2665 0.1331  -0.2848 0.0231  173 HIS B CD2 
3438 C CE1 . HIS B 166 ? 1.5962 2.1894 2.3235 0.1043  -0.2336 0.0312  173 HIS B CE1 
3439 N NE2 . HIS B 166 ? 1.6442 2.1675 2.3221 0.1339  -0.2817 0.0048  173 HIS B NE2 
3440 N N   . ASN B 167 ? 1.4628 1.7260 1.8031 0.0470  -0.1832 0.1343  174 ASN B N   
3441 C CA  . ASN B 167 ? 1.4473 1.6637 1.7150 0.0290  -0.1539 0.1522  174 ASN B CA  
3442 C C   . ASN B 167 ? 1.4808 1.5852 1.6533 0.0342  -0.1727 0.1444  174 ASN B C   
3443 O O   . ASN B 167 ? 1.5063 1.5867 1.6880 0.0357  -0.1912 0.1417  174 ASN B O   
3444 C CB  . ASN B 167 ? 1.3887 1.6623 1.7102 0.0027  -0.1199 0.1769  174 ASN B CB  
3445 C CG  . ASN B 167 ? 1.3609 1.6143 1.6321 -0.0160 -0.0850 0.1918  174 ASN B CG  
3446 O OD1 . ASN B 167 ? 1.4529 1.6578 1.6539 -0.0129 -0.0792 0.1852  174 ASN B OD1 
3447 N ND2 . ASN B 167 ? 1.2544 1.5468 1.5659 -0.0358 -0.0614 0.2103  174 ASN B ND2 
3448 N N   . GLU B 168 ? 1.5227 1.5555 1.6013 0.0363  -0.1668 0.1401  175 GLU B N   
3449 C CA  . GLU B 168 ? 1.6287 1.5468 1.6010 0.0338  -0.1709 0.1360  175 GLU B CA  
3450 C C   . GLU B 168 ? 1.6094 1.5272 1.5819 0.0054  -0.1359 0.1529  175 GLU B C   
3451 O O   . GLU B 168 ? 1.5933 1.4473 1.5251 0.0028  -0.1454 0.1503  175 GLU B O   
3452 C CB  . GLU B 168 ? 1.7245 1.5676 1.5968 0.0385  -0.1655 0.1278  175 GLU B CB  
3453 C CG  . GLU B 168 ? 1.7845 1.5914 1.6262 0.0703  -0.2085 0.1066  175 GLU B CG  
3454 C CD  . GLU B 168 ? 1.8967 1.6212 1.6325 0.0730  -0.2013 0.1002  175 GLU B CD  
3455 O OE1 . GLU B 168 ? 1.8601 1.6190 1.6002 0.0556  -0.1628 0.1100  175 GLU B OE1 
3456 O OE2 . GLU B 168 ? 1.9913 1.6131 1.6375 0.0935  -0.2358 0.0843  175 GLU B OE2 
3457 N N   . LEU B 169 ? 1.5940 1.5822 1.6131 -0.0140 -0.0982 0.1681  176 LEU B N   
3458 C CA  . LEU B 169 ? 1.6197 1.6213 1.6540 -0.0395 -0.0662 0.1817  176 LEU B CA  
3459 C C   . LEU B 169 ? 1.5549 1.6346 1.6875 -0.0445 -0.0702 0.1946  176 LEU B C   
3460 O O   . LEU B 169 ? 1.4423 1.5868 1.6289 -0.0601 -0.0443 0.2096  176 LEU B O   
3461 C CB  . LEU B 169 ? 1.6128 1.6425 1.6424 -0.0555 -0.0274 0.1877  176 LEU B CB  
3462 C CG  . LEU B 169 ? 1.7168 1.6814 1.6601 -0.0541 -0.0169 0.1757  176 LEU B CG  
3463 C CD1 . LEU B 169 ? 1.6965 1.7125 1.6634 -0.0690 0.0193  0.1810  176 LEU B CD1 
3464 C CD2 . LEU B 169 ? 1.8275 1.6781 1.6715 -0.0618 -0.0130 0.1649  176 LEU B CD2 
3465 N N   . ARG B 170 ? 1.6350 1.7025 1.7872 -0.0309 -0.1036 0.1876  177 ARG B N   
3466 C CA  . ARG B 170 ? 1.5925 1.7296 1.8388 -0.0348 -0.1097 0.1970  177 ARG B CA  
3467 C C   . ARG B 170 ? 1.6364 1.7538 1.8823 -0.0524 -0.0977 0.2065  177 ARG B C   
3468 O O   . ARG B 170 ? 1.6691 1.7043 1.8414 -0.0540 -0.1009 0.1985  177 ARG B O   
3469 C CB  . ARG B 170 ? 1.5736 1.7078 1.8490 -0.0125 -0.1516 0.1806  177 ARG B CB  
3470 C CG  . ARG B 170 ? 1.4987 1.7131 1.8807 -0.0171 -0.1552 0.1871  177 ARG B CG  
3471 C CD  . ARG B 170 ? 1.4526 1.6628 1.8685 0.0051  -0.1976 0.1647  177 ARG B CD  
3472 N NE  . ARG B 170 ? 1.3290 1.6206 1.8530 -0.0022 -0.1956 0.1686  177 ARG B NE  
3473 C CZ  . ARG B 170 ? 1.4472 1.7701 2.0372 0.0131  -0.2241 0.1473  177 ARG B CZ  
3474 N NH1 . ARG B 170 ? 1.4989 1.7732 2.0569 0.0407  -0.2652 0.1191  177 ARG B NH1 
3475 N NH2 . ARG B 170 ? 1.3979 1.7963 2.0864 0.0008  -0.2130 0.1521  177 ARG B NH2 
3476 N N   . GLU B 171 ? 1.6238 1.8131 1.9489 -0.0656 -0.0840 0.2228  178 GLU B N   
3477 C CA  . GLU B 171 ? 1.7047 1.8868 2.0474 -0.0801 -0.0782 0.2313  178 GLU B CA  
3478 C C   . GLU B 171 ? 1.7266 1.8967 2.0988 -0.0692 -0.1118 0.2234  178 GLU B C   
3479 O O   . GLU B 171 ? 1.5747 1.8050 2.0221 -0.0648 -0.1223 0.2256  178 GLU B O   
3480 C CB  . GLU B 171 ? 1.6489 1.9065 2.0591 -0.0967 -0.0530 0.2518  178 GLU B CB  
3481 C CG  . GLU B 171 ? 1.5789 1.8267 2.0012 -0.1122 -0.0442 0.2597  178 GLU B CG  
3482 C CD  . GLU B 171 ? 1.5970 1.9065 2.0712 -0.1262 -0.0220 0.2783  178 GLU B CD  
3483 O OE1 . GLU B 171 ? 1.5635 1.9325 2.0914 -0.1252 -0.0207 0.2901  178 GLU B OE1 
3484 O OE2 . GLU B 171 ? 1.5934 1.8894 2.0533 -0.1381 -0.0057 0.2795  178 GLU B OE2 
3485 N N   . VAL B 172 ? 1.8489 1.9396 2.1610 -0.0653 -0.1272 0.2123  179 VAL B N   
3486 C CA  . VAL B 172 ? 1.8598 1.9273 2.1903 -0.0529 -0.1626 0.2016  179 VAL B CA  
3487 C C   . VAL B 172 ? 1.7764 1.8887 2.1775 -0.0693 -0.1536 0.2160  179 VAL B C   
3488 O O   . VAL B 172 ? 1.6363 1.7212 2.0110 -0.0840 -0.1365 0.2221  179 VAL B O   
3489 C CB  . VAL B 172 ? 1.9331 1.8895 2.1614 -0.0425 -0.1824 0.1849  179 VAL B CB  
3490 C CG1 . VAL B 172 ? 1.9219 1.8530 2.1693 -0.0274 -0.2226 0.1723  179 VAL B CG1 
3491 C CG2 . VAL B 172 ? 1.9126 1.8157 2.0632 -0.0261 -0.1924 0.1714  179 VAL B CG2 
3492 N N   . ASP B 173 ? 1.7215 1.9011 2.2123 -0.0674 -0.1639 0.2196  180 ASP B N   
3493 C CA  . ASP B 173 ? 1.6766 1.8988 2.2383 -0.0823 -0.1575 0.2335  180 ASP B CA  
3494 C C   . ASP B 173 ? 1.5509 1.8142 2.1932 -0.0738 -0.1819 0.2248  180 ASP B C   
3495 O O   . ASP B 173 ? 1.5047 1.7360 2.1533 -0.0652 -0.2100 0.2119  180 ASP B O   
3496 C CB  . ASP B 173 ? 1.6504 1.9324 2.2462 -0.1016 -0.1213 0.2567  180 ASP B CB  
3497 C CG  . ASP B 173 ? 1.6745 1.9800 2.3200 -0.1181 -0.1132 0.2722  180 ASP B CG  
3498 O OD1 . ASP B 173 ? 1.6537 1.9160 2.2654 -0.1242 -0.1118 0.2714  180 ASP B OD1 
3499 O OD2 . ASP B 173 ? 1.6978 2.0622 2.4145 -0.1255 -0.1073 0.2842  180 ASP B OD2 
3500 N N   . GLY B 181 ? 1.4042 1.2236 1.4838 0.0386  -0.1113 0.0041  188 GLY B N   
3501 C CA  . GLY B 181 ? 1.2655 1.0872 1.3446 0.0338  -0.0921 0.0106  188 GLY B CA  
3502 C C   . GLY B 181 ? 1.2774 1.1525 1.3963 0.0226  -0.0782 0.0089  188 GLY B C   
3503 O O   . GLY B 181 ? 1.4999 1.3762 1.6172 0.0098  -0.0609 0.0189  188 GLY B O   
3504 N N   . THR B 182 ? 1.3988 1.3182 1.5521 0.0277  -0.0866 -0.0049 189 THR B N   
3505 C CA  . THR B 182 ? 1.2974 1.2725 1.4874 0.0144  -0.0738 -0.0079 189 THR B CA  
3506 C C   . THR B 182 ? 1.1830 1.1669 1.3779 -0.0069 -0.0683 0.0011  189 THR B C   
3507 O O   . THR B 182 ? 1.0733 1.0712 1.2736 -0.0228 -0.0530 0.0094  189 THR B O   
3508 C CB  . THR B 182 ? 1.3200 1.3460 1.5467 0.0255  -0.0841 -0.0283 189 THR B CB  
3509 O OG1 . THR B 182 ? 1.3071 1.3195 1.5260 0.0461  -0.0904 -0.0368 189 THR B OG1 
3510 C CG2 . THR B 182 ? 1.2206 1.3094 1.4832 0.0083  -0.0689 -0.0322 189 THR B CG2 
3511 N N   . LEU B 183 ? 1.1269 1.0973 1.3162 -0.0066 -0.0833 -0.0006 190 LEU B N   
3512 C CA  . LEU B 183 ? 0.9687 0.9479 1.1646 -0.0264 -0.0839 0.0050  190 LEU B CA  
3513 C C   . LEU B 183 ? 1.0647 1.0066 1.2330 -0.0379 -0.0741 0.0208  190 LEU B C   
3514 O O   . LEU B 183 ? 1.0934 1.0443 1.2679 -0.0564 -0.0725 0.0264  190 LEU B O   
3515 C CB  . LEU B 183 ? 1.0985 1.0703 1.2948 -0.0215 -0.1056 -0.0026 190 LEU B CB  
3516 C CG  . LEU B 183 ? 1.2407 1.2532 1.4694 -0.0092 -0.1210 -0.0218 190 LEU B CG  
3517 C CD1 . LEU B 183 ? 1.2471 1.2382 1.4670 -0.0018 -0.1453 -0.0277 190 LEU B CD1 
3518 C CD2 . LEU B 183 ? 1.2844 1.3675 1.5593 -0.0261 -0.1125 -0.0299 190 LEU B CD2 
3519 N N   . TYR B 184 ? 0.9246 0.8264 1.0632 -0.0277 -0.0679 0.0272  191 TYR B N   
3520 C CA  . TYR B 184 ? 0.8185 0.6938 0.9370 -0.0355 -0.0570 0.0387  191 TYR B CA  
3521 C C   . TYR B 184 ? 0.7788 0.6788 0.9131 -0.0487 -0.0433 0.0442  191 TYR B C   
3522 O O   . TYR B 184 ? 0.6713 0.5569 0.7961 -0.0584 -0.0404 0.0519  191 TYR B O   
3523 C CB  . TYR B 184 ? 0.9215 0.7594 1.0099 -0.0235 -0.0502 0.0422  191 TYR B CB  
3524 C CG  . TYR B 184 ? 0.9783 0.7805 1.0377 -0.0117 -0.0615 0.0393  191 TYR B CG  
3525 C CD1 . TYR B 184 ? 1.0455 0.8357 1.0975 -0.0119 -0.0772 0.0363  191 TYR B CD1 
3526 C CD2 . TYR B 184 ? 1.1090 0.8856 1.1442 -0.0021 -0.0576 0.0403  191 TYR B CD2 
3527 C CE1 . TYR B 184 ? 1.0495 0.8031 1.0695 -0.0010 -0.0886 0.0339  191 TYR B CE1 
3528 C CE2 . TYR B 184 ? 1.1066 0.8450 1.1074 0.0066  -0.0681 0.0392  191 TYR B CE2 
3529 C CZ  . TYR B 184 ? 1.0212 0.7482 1.0138 0.0080  -0.0836 0.0358  191 TYR B CZ  
3530 O OH  . TYR B 184 ? 0.9963 0.6830 0.9509 0.0166  -0.0954 0.0346  191 TYR B OH  
3531 N N   . TYR B 185 ? 0.8046 0.7380 0.9596 -0.0473 -0.0368 0.0393  192 TYR B N   
3532 C CA  . TYR B 185 ? 0.7828 0.7383 0.9485 -0.0579 -0.0237 0.0437  192 TYR B CA  
3533 C C   . TYR B 185 ? 0.7281 0.7308 0.9200 -0.0735 -0.0223 0.0397  192 TYR B C   
3534 O O   . TYR B 185 ? 0.8100 0.8311 1.0069 -0.0842 -0.0118 0.0434  192 TYR B O   
3535 C CB  . TYR B 185 ? 0.7944 0.7493 0.9587 -0.0452 -0.0152 0.0412  192 TYR B CB  
3536 C CG  . TYR B 185 ? 0.8044 0.7175 0.9431 -0.0343 -0.0148 0.0449  192 TYR B CG  
3537 C CD1 . TYR B 185 ? 0.8566 0.7487 0.9815 -0.0380 -0.0064 0.0530  192 TYR B CD1 
3538 C CD2 . TYR B 185 ? 0.7823 0.6764 0.9088 -0.0207 -0.0234 0.0396  192 TYR B CD2 
3539 C CE1 . TYR B 185 ? 0.9198 0.7810 1.0231 -0.0302 -0.0031 0.0548  192 TYR B CE1 
3540 C CE2 . TYR B 185 ? 0.8375 0.6928 0.9355 -0.0148 -0.0210 0.0440  192 TYR B CE2 
3541 C CZ  . TYR B 185 ? 0.8439 0.6863 0.9319 -0.0206 -0.0092 0.0512  192 TYR B CZ  
3542 O OH  . TYR B 185 ? 0.9599 0.7719 1.0221 -0.0171 -0.0038 0.0540  192 TYR B OH  
3543 N N   . MET B 186 ? 0.6919 0.7149 0.8993 -0.0761 -0.0330 0.0319  193 MET B N   
3544 C CA  . MET B 186 ? 0.8118 0.8868 1.0473 -0.0936 -0.0309 0.0260  193 MET B CA  
3545 C C   . MET B 186 ? 0.7707 0.8346 0.9967 -0.1197 -0.0332 0.0378  193 MET B C   
3546 O O   . MET B 186 ? 0.8646 0.8950 1.0760 -0.1200 -0.0456 0.0416  193 MET B O   
3547 C CB  . MET B 186 ? 0.8973 1.0024 1.1579 -0.0830 -0.0436 0.0094  193 MET B CB  
3548 C CG  . MET B 186 ? 1.0307 1.2019 1.3278 -0.0999 -0.0404 -0.0013 193 MET B CG  
3549 S SD  . MET B 186 ? 1.4000 1.6138 1.7330 -0.0780 -0.0562 -0.0267 193 MET B SD  
3550 C CE  . MET B 186 ? 1.4241 1.6530 1.7624 -0.0531 -0.0475 -0.0382 193 MET B CE  
3551 N N   . ALA B 187 ? 0.7615 0.8500 0.9918 -0.1418 -0.0224 0.0433  194 ALA B N   
3552 C CA  . ALA B 187 ? 0.8275 0.9008 1.0433 -0.1701 -0.0254 0.0562  194 ALA B CA  
3553 C C   . ALA B 187 ? 0.7678 0.8576 0.9984 -0.1855 -0.0376 0.0519  194 ALA B C   
3554 O O   . ALA B 187 ? 0.6920 0.8318 0.9551 -0.1822 -0.0375 0.0371  194 ALA B O   
3555 C CB  . ALA B 187 ? 0.8684 0.9692 1.0841 -0.1927 -0.0112 0.0620  194 ALA B CB  
3556 N N   . PRO B 188 ? 0.8312 0.8793 1.0390 -0.2008 -0.0499 0.0630  195 PRO B N   
3557 C CA  . PRO B 188 ? 0.8359 0.8908 1.0546 -0.2147 -0.0651 0.0591  195 PRO B CA  
3558 C C   . PRO B 188 ? 0.7716 0.8926 1.0239 -0.2426 -0.0596 0.0524  195 PRO B C   
3559 O O   . PRO B 188 ? 0.8930 1.0420 1.1711 -0.2426 -0.0699 0.0405  195 PRO B O   
3560 C CB  . PRO B 188 ? 0.8445 0.8382 1.0264 -0.2295 -0.0776 0.0742  195 PRO B CB  
3561 C CG  . PRO B 188 ? 0.8931 0.8672 1.0526 -0.2346 -0.0669 0.0861  195 PRO B CG  
3562 C CD  . PRO B 188 ? 0.8655 0.8573 1.0362 -0.2061 -0.0530 0.0784  195 PRO B CD  
3563 N N   . GLU B 189 ? 0.7656 0.9126 1.0171 -0.2656 -0.0436 0.0589  196 GLU B N   
3564 C CA  . GLU B 189 ? 0.8041 1.0261 1.0896 -0.2918 -0.0320 0.0500  196 GLU B CA  
3565 C C   . GLU B 189 ? 0.8111 1.0998 1.1440 -0.2686 -0.0283 0.0253  196 GLU B C   
3566 O O   . GLU B 189 ? 0.7584 1.1103 1.1270 -0.2867 -0.0259 0.0131  196 GLU B O   
3567 C CB  . GLU B 189 ? 0.8170 1.0537 1.0870 -0.3176 -0.0130 0.0608  196 GLU B CB  
3568 C CG  . GLU B 189 ? 0.8151 1.0486 1.0763 -0.2929 0.0009  0.0596  196 GLU B CG  
3569 C CD  . GLU B 189 ? 0.8346 0.9932 1.0505 -0.2859 -0.0043 0.0776  196 GLU B CD  
3570 O OE1 . GLU B 189 ? 0.8836 1.0402 1.0870 -0.2802 0.0074  0.0810  196 GLU B OE1 
3571 O OE2 . GLU B 189 ? 0.9997 1.1019 1.1935 -0.2836 -0.0212 0.0865  196 GLU B OE2 
3572 N N   . HIS B 190 ? 0.8114 1.0851 1.1436 -0.2298 -0.0290 0.0175  197 HIS B N   
3573 C CA  . HIS B 190 ? 0.8295 1.1511 1.1989 -0.2016 -0.0309 -0.0062 197 HIS B CA  
3574 C C   . HIS B 190 ? 0.8168 1.1180 1.1933 -0.1772 -0.0538 -0.0162 197 HIS B C   
3575 O O   . HIS B 190 ? 0.8855 1.2285 1.2948 -0.1564 -0.0602 -0.0374 197 HIS B O   
3576 C CB  . HIS B 190 ? 0.7738 1.0891 1.1348 -0.1752 -0.0197 -0.0094 197 HIS B CB  
3577 C CG  . HIS B 190 ? 0.8183 1.1591 1.1739 -0.1953 0.0016  -0.0033 197 HIS B CG  
3578 N ND1 . HIS B 190 ? 0.8776 1.2922 1.2630 -0.2167 0.0152  -0.0145 197 HIS B ND1 
3579 C CD2 . HIS B 190 ? 0.7733 1.0760 1.0957 -0.1987 0.0112  0.0125  197 HIS B CD2 
3580 C CE1 . HIS B 190 ? 0.8498 1.2669 1.2158 -0.2329 0.0326  -0.0048 197 HIS B CE1 
3581 N NE2 . HIS B 190 ? 0.8353 1.1838 1.1635 -0.2215 0.0291  0.0116  197 HIS B NE2 
3582 N N   . LEU B 191 ? 0.7363 0.9724 1.0803 -0.1773 -0.0672 -0.0026 198 LEU B N   
3583 C CA  . LEU B 191 ? 0.7085 0.9179 1.0508 -0.1556 -0.0895 -0.0105 198 LEU B CA  
3584 C C   . LEU B 191 ? 0.7671 1.0229 1.1447 -0.1735 -0.1024 -0.0224 198 LEU B C   
3585 O O   . LEU B 191 ? 0.6657 0.9264 1.0423 -0.2078 -0.1011 -0.0128 198 LEU B O   
3586 C CB  . LEU B 191 ? 0.6910 0.8205 0.9865 -0.1514 -0.0983 0.0059  198 LEU B CB  
3587 C CG  . LEU B 191 ? 0.7114 0.7945 0.9731 -0.1350 -0.0869 0.0169  198 LEU B CG  
3588 C CD1 . LEU B 191 ? 0.7168 0.7324 0.9378 -0.1354 -0.0941 0.0306  198 LEU B CD1 
3589 C CD2 . LEU B 191 ? 0.6969 0.7764 0.9595 -0.1020 -0.0886 0.0062  198 LEU B CD2 
3590 N N   . ASN B 192 ? 0.8092 1.0968 1.2169 -0.1509 -0.1166 -0.0434 199 ASN B N   
3591 C CA  . ASN B 192 ? 0.9489 1.2988 1.4029 -0.1646 -0.1285 -0.0608 199 ASN B CA  
3592 C C   . ASN B 192 ? 0.9892 1.4184 1.4803 -0.1994 -0.1079 -0.0651 199 ASN B C   
3593 O O   . ASN B 192 ? 1.0549 1.5142 1.5645 -0.2334 -0.1105 -0.0644 199 ASN B O   
3594 C CB  . ASN B 192 ? 1.0562 1.3635 1.4934 -0.1767 -0.1505 -0.0536 199 ASN B CB  
3595 C CG  . ASN B 192 ? 1.2115 1.4612 1.6229 -0.1412 -0.1736 -0.0575 199 ASN B CG  
3596 O OD1 . ASN B 192 ? 1.1880 1.4154 1.5842 -0.1097 -0.1723 -0.0607 199 ASN B OD1 
3597 N ND2 . ASN B 192 ? 1.3523 1.5743 1.7547 -0.1479 -0.1957 -0.0569 199 ASN B ND2 
3598 N N   . ASP B 193 ? 1.0968 1.5557 1.5940 -0.1925 -0.0868 -0.0685 200 ASP B N   
3599 C CA  . ASP B 193 ? 1.1781 1.7100 1.7025 -0.2236 -0.0630 -0.0724 200 ASP B CA  
3600 C C   . ASP B 193 ? 1.3511 1.9218 1.8913 -0.1973 -0.0483 -0.0881 200 ASP B C   
3601 O O   . ASP B 193 ? 1.5244 2.0731 2.0366 -0.1991 -0.0308 -0.0754 200 ASP B O   
3602 C CB  . ASP B 193 ? 1.1436 1.6348 1.6271 -0.2621 -0.0497 -0.0439 200 ASP B CB  
3603 C CG  . ASP B 193 ? 1.1753 1.7350 1.6792 -0.3054 -0.0280 -0.0441 200 ASP B CG  
3604 O OD1 . ASP B 193 ? 1.2325 1.8789 1.7827 -0.3048 -0.0162 -0.0670 200 ASP B OD1 
3605 O OD2 . ASP B 193 ? 1.1865 1.7106 1.6564 -0.3417 -0.0232 -0.0210 200 ASP B OD2 
3606 N N   . VAL B 194 ? 1.5692 2.1945 2.1536 -0.1706 -0.0589 -0.1171 201 VAL B N   
3607 C CA  . VAL B 194 ? 1.6518 2.3131 2.2541 -0.1386 -0.0514 -0.1375 201 VAL B CA  
3608 C C   . VAL B 194 ? 1.6292 2.3708 2.2568 -0.1630 -0.0222 -0.1461 201 VAL B C   
3609 O O   . VAL B 194 ? 1.5548 2.3053 2.1775 -0.1445 -0.0099 -0.1530 201 VAL B O   
3610 C CB  . VAL B 194 ? 1.6590 2.3516 2.3002 -0.0989 -0.0766 -0.1689 201 VAL B CB  
3611 C CG1 . VAL B 194 ? 1.5904 2.3141 2.2473 -0.0634 -0.0727 -0.1918 201 VAL B CG1 
3612 C CG2 . VAL B 194 ? 1.6480 2.2556 2.2556 -0.0742 -0.1054 -0.1598 201 VAL B CG2 
3613 N N   . ASN B 195 ? 1.5463 2.3427 2.1972 -0.2057 -0.0114 -0.1452 202 ASN B N   
3614 C CA  . ASN B 195 ? 1.5455 2.4224 2.2178 -0.2354 0.0183  -0.1530 202 ASN B CA  
3615 C C   . ASN B 195 ? 1.5135 2.3476 2.1337 -0.2620 0.0410  -0.1245 202 ASN B C   
3616 O O   . ASN B 195 ? 1.6290 2.5149 2.2558 -0.2708 0.0649  -0.1327 202 ASN B O   
3617 C CB  . ASN B 195 ? 1.5762 2.5291 2.2910 -0.2765 0.0222  -0.1620 202 ASN B CB  
3618 C CG  . ASN B 195 ? 1.6035 2.6570 2.3495 -0.3051 0.0533  -0.1772 202 ASN B CG  
3619 O OD1 . ASN B 195 ? 1.5879 2.7002 2.3645 -0.2758 0.0615  -0.2050 202 ASN B OD1 
3620 N ND2 . ASN B 195 ? 1.6258 2.6978 2.3611 -0.3623 0.0705  -0.1598 202 ASN B ND2 
3621 N N   . ALA B 196 ? 1.4936 2.2357 2.0625 -0.2732 0.0326  -0.0933 203 ALA B N   
3622 C CA  . ALA B 196 ? 1.4006 2.0969 1.9187 -0.2993 0.0492  -0.0658 203 ALA B CA  
3623 C C   . ALA B 196 ? 1.2444 1.9286 1.7445 -0.2717 0.0614  -0.0684 203 ALA B C   
3624 O O   . ALA B 196 ? 0.9677 1.6189 1.4659 -0.2293 0.0487  -0.0758 203 ALA B O   
3625 C CB  . ALA B 196 ? 1.3546 1.9544 1.8253 -0.3086 0.0331  -0.0367 203 ALA B CB  
3626 N N   . LYS B 197 ? 1.2421 1.9518 1.7267 -0.2981 0.0851  -0.0621 204 LYS B N   
3627 C CA  . LYS B 197 ? 1.2231 1.9285 1.6908 -0.2770 0.0980  -0.0657 204 LYS B CA  
3628 C C   . LYS B 197 ? 1.0575 1.6637 1.4716 -0.2692 0.0894  -0.0384 204 LYS B C   
3629 O O   . LYS B 197 ? 1.0198 1.5835 1.3985 -0.3014 0.0898  -0.0136 204 LYS B O   
3630 C CB  . LYS B 197 ? 1.2648 2.0297 1.7291 -0.3107 0.1261  -0.0677 204 LYS B CB  
3631 C CG  . LYS B 197 ? 1.2427 2.1189 1.7635 -0.3196 0.1393  -0.0982 204 LYS B CG  
3632 C CD  . LYS B 197 ? 1.3434 2.2740 1.8521 -0.3614 0.1698  -0.0963 204 LYS B CD  
3633 C CE  . LYS B 197 ? 1.3444 2.3938 1.9120 -0.3771 0.1854  -0.1268 204 LYS B CE  
3634 N NZ  . LYS B 197 ? 1.3751 2.4797 1.9271 -0.4226 0.2178  -0.1243 204 LYS B NZ  
3635 N N   . PRO B 198 ? 1.0307 1.5994 1.4379 -0.2275 0.0805  -0.0434 205 PRO B N   
3636 C CA  . PRO B 198 ? 0.9021 1.3881 1.2623 -0.2218 0.0759  -0.0199 205 PRO B CA  
3637 C C   . PRO B 198 ? 0.8247 1.3076 1.1542 -0.2407 0.0934  -0.0088 205 PRO B C   
3638 O O   . PRO B 198 ? 0.7616 1.3045 1.1050 -0.2459 0.1103  -0.0233 205 PRO B O   
3639 C CB  . PRO B 198 ? 0.8565 1.3165 1.2222 -0.1765 0.0642  -0.0313 205 PRO B CB  
3640 C CG  . PRO B 198 ? 0.8034 1.3120 1.2126 -0.1585 0.0547  -0.0559 205 PRO B CG  
3641 C CD  . PRO B 198 ? 0.9637 1.5559 1.4026 -0.1846 0.0711  -0.0693 205 PRO B CD  
3642 N N   . THR B 199 ? 0.7402 1.1533 1.0276 -0.2497 0.0878  0.0155  206 THR B N   
3643 C CA  . THR B 199 ? 0.7690 1.1630 1.0192 -0.2682 0.0986  0.0299  206 THR B CA  
3644 C C   . THR B 199 ? 0.8278 1.1559 1.0522 -0.2421 0.0890  0.0394  206 THR B C   
3645 O O   . THR B 199 ? 0.6467 0.9449 0.8801 -0.2146 0.0762  0.0366  206 THR B O   
3646 C CB  . THR B 199 ? 0.9291 1.2987 1.1487 -0.3118 0.0975  0.0520  206 THR B CB  
3647 O OG1 . THR B 199 ? 1.0156 1.3166 1.2176 -0.3070 0.0773  0.0672  206 THR B OG1 
3648 C CG2 . THR B 199 ? 0.9366 1.3735 1.1837 -0.3435 0.1070  0.0433  206 THR B CG2 
3649 N N   . GLU B 200 ? 0.9546 1.2609 1.1456 -0.2528 0.0952  0.0508  207 GLU B N   
3650 C CA  . GLU B 200 ? 0.9261 1.1692 1.0904 -0.2353 0.0852  0.0623  207 GLU B CA  
3651 C C   . GLU B 200 ? 0.9597 1.1441 1.1116 -0.2342 0.0674  0.0767  207 GLU B C   
3652 O O   . GLU B 200 ? 0.9865 1.1346 1.1378 -0.2086 0.0583  0.0770  207 GLU B O   
3653 C CB  . GLU B 200 ? 0.9514 1.1784 1.0777 -0.2531 0.0914  0.0739  207 GLU B CB  
3654 C CG  . GLU B 200 ? 0.9233 1.2001 1.0552 -0.2496 0.1084  0.0591  207 GLU B CG  
3655 C CD  . GLU B 200 ? 0.9512 1.2085 1.0413 -0.2657 0.1132  0.0701  207 GLU B CD  
3656 O OE1 . GLU B 200 ? 0.9702 1.1696 1.0248 -0.2778 0.1010  0.0902  207 GLU B OE1 
3657 O OE2 . GLU B 200 ? 0.9511 1.2499 1.0414 -0.2657 0.1280  0.0578  207 GLU B OE2 
3658 N N   . LYS B 201 ? 0.9565 1.1346 1.0989 -0.2625 0.0629  0.0870  208 LYS B N   
3659 C CA  . LYS B 201 ? 0.9782 1.1023 1.1078 -0.2623 0.0449  0.0985  208 LYS B CA  
3660 C C   . LYS B 201 ? 0.8755 1.0005 1.0333 -0.2366 0.0368  0.0874  208 LYS B C   
3661 O O   . LYS B 201 ? 1.0027 1.0783 1.1479 -0.2243 0.0234  0.0938  208 LYS B O   
3662 C CB  . LYS B 201 ? 0.9822 1.0975 1.0924 -0.3016 0.0402  0.1118  208 LYS B CB  
3663 C CG  . LYS B 201 ? 1.0138 1.0732 1.0753 -0.3212 0.0316  0.1317  208 LYS B CG  
3664 C CD  . LYS B 201 ? 1.0623 1.1272 1.1027 -0.3250 0.0424  0.1345  208 LYS B CD  
3665 C CE  . LYS B 201 ? 1.1018 1.0961 1.0909 -0.3377 0.0259  0.1543  208 LYS B CE  
3666 N NZ  . LYS B 201 ? 1.2246 1.2209 1.1825 -0.3534 0.0345  0.1607  208 LYS B NZ  
3667 N N   . SER B 202 ? 0.6426 0.8223 0.8355 -0.2291 0.0438  0.0704  209 SER B N   
3668 C CA  . SER B 202 ? 0.6131 0.7922 0.8290 -0.2022 0.0349  0.0587  209 SER B CA  
3669 C C   . SER B 202 ? 0.6327 0.7763 0.8410 -0.1702 0.0317  0.0573  209 SER B C   
3670 O O   . SER B 202 ? 0.6365 0.7464 0.8413 -0.1548 0.0211  0.0583  209 SER B O   
3671 C CB  . SER B 202 ? 0.6175 0.8633 0.8720 -0.1962 0.0413  0.0380  209 SER B CB  
3672 O OG  . SER B 202 ? 0.7028 0.9935 0.9695 -0.2278 0.0476  0.0369  209 SER B OG  
3673 N N   . ASP B 203 ? 0.6013 0.7546 0.8064 -0.1625 0.0415  0.0544  210 ASP B N   
3674 C CA  . ASP B 203 ? 0.6680 0.7890 0.8643 -0.1383 0.0397  0.0544  210 ASP B CA  
3675 C C   . ASP B 203 ? 0.7477 0.8149 0.9178 -0.1396 0.0327  0.0694  210 ASP B C   
3676 O O   . ASP B 203 ? 0.9614 1.0005 1.1288 -0.1206 0.0285  0.0688  210 ASP B O   
3677 C CB  . ASP B 203 ? 0.6947 0.8393 0.8928 -0.1325 0.0502  0.0474  210 ASP B CB  
3678 C CG  . ASP B 203 ? 0.6464 0.8395 0.8718 -0.1195 0.0547  0.0276  210 ASP B CG  
3679 O OD1 . ASP B 203 ? 0.6759 0.8766 0.9190 -0.1077 0.0470  0.0186  210 ASP B OD1 
3680 O OD2 . ASP B 203 ? 0.7253 0.9479 0.9530 -0.1195 0.0644  0.0196  210 ASP B OD2 
3681 N N   . VAL B 204 ? 0.8380 0.8912 0.9880 -0.1620 0.0309  0.0817  211 VAL B N   
3682 C CA  . VAL B 204 ? 0.8765 0.8777 1.0017 -0.1618 0.0204  0.0937  211 VAL B CA  
3683 C C   . VAL B 204 ? 0.9622 0.9358 1.0877 -0.1536 0.0092  0.0941  211 VAL B C   
3684 O O   . VAL B 204 ? 0.7808 0.7198 0.8968 -0.1387 0.0031  0.0958  211 VAL B O   
3685 C CB  . VAL B 204 ? 0.9280 0.9135 1.0256 -0.1882 0.0169  0.1070  211 VAL B CB  
3686 C CG1 . VAL B 204 ? 0.9986 0.9268 1.0703 -0.1857 0.0007  0.1173  211 VAL B CG1 
3687 C CG2 . VAL B 204 ? 0.8574 0.8612 0.9482 -0.1917 0.0270  0.1065  211 VAL B CG2 
3688 N N   . TYR B 205 ? 0.9734 0.9647 1.1102 -0.1630 0.0066  0.0910  212 TYR B N   
3689 C CA  . TYR B 205 ? 0.9178 0.8856 1.0550 -0.1526 -0.0041 0.0889  212 TYR B CA  
3690 C C   . TYR B 205 ? 0.7692 0.7323 0.9150 -0.1248 -0.0016 0.0800  212 TYR B C   
3691 O O   . TYR B 205 ? 0.6895 0.6182 0.8231 -0.1125 -0.0074 0.0811  212 TYR B O   
3692 C CB  . TYR B 205 ? 0.8410 0.8328 0.9920 -0.1671 -0.0087 0.0852  212 TYR B CB  
3693 C CG  . TYR B 205 ? 0.8226 0.7828 0.9675 -0.1578 -0.0224 0.0840  212 TYR B CG  
3694 C CD1 . TYR B 205 ? 0.8301 0.7925 0.9855 -0.1350 -0.0237 0.0738  212 TYR B CD1 
3695 C CD2 . TYR B 205 ? 0.8046 0.7261 0.9275 -0.1705 -0.0357 0.0931  212 TYR B CD2 
3696 C CE1 . TYR B 205 ? 0.8541 0.7851 0.9984 -0.1263 -0.0359 0.0727  212 TYR B CE1 
3697 C CE2 . TYR B 205 ? 0.8094 0.7005 0.9238 -0.1602 -0.0484 0.0905  212 TYR B CE2 
3698 C CZ  . TYR B 205 ? 0.7818 0.6791 0.9067 -0.1384 -0.0476 0.0803  212 TYR B CZ  
3699 O OH  . TYR B 205 ? 0.9301 0.7959 1.0420 -0.1287 -0.0599 0.0776  212 TYR B OH  
3700 N N   . SER B 206 ? 0.7258 0.7225 0.8903 -0.1159 0.0065  0.0704  213 SER B N   
3701 C CA  . SER B 206 ? 0.7827 0.7714 0.9510 -0.0928 0.0074  0.0629  213 SER B CA  
3702 C C   . SER B 206 ? 0.7446 0.7033 0.8983 -0.0835 0.0109  0.0679  213 SER B C   
3703 O O   . SER B 206 ? 0.8776 0.8093 1.0217 -0.0723 0.0082  0.0679  213 SER B O   
3704 C CB  . SER B 206 ? 0.7630 0.7887 0.9501 -0.0852 0.0133  0.0517  213 SER B CB  
3705 O OG  . SER B 206 ? 0.7080 0.7700 0.9147 -0.0909 0.0103  0.0430  213 SER B OG  
3706 N N   . PHE B 207 ? 0.6851 0.6506 0.8371 -0.0898 0.0166  0.0717  214 PHE B N   
3707 C CA  . PHE B 207 ? 0.6681 0.6110 0.8101 -0.0840 0.0179  0.0758  214 PHE B CA  
3708 C C   . PHE B 207 ? 0.6413 0.5504 0.7699 -0.0812 0.0102  0.0801  214 PHE B C   
3709 O O   . PHE B 207 ? 0.6714 0.5661 0.7982 -0.0688 0.0123  0.0775  214 PHE B O   
3710 C CB  . PHE B 207 ? 0.6644 0.6169 0.8019 -0.0955 0.0204  0.0805  214 PHE B CB  
3711 C CG  . PHE B 207 ? 0.7521 0.6828 0.8812 -0.0896 0.0181  0.0836  214 PHE B CG  
3712 C CD1 . PHE B 207 ? 0.6845 0.6196 0.8221 -0.0773 0.0239  0.0782  214 PHE B CD1 
3713 C CD2 . PHE B 207 ? 0.7574 0.6624 0.8700 -0.0964 0.0081  0.0912  214 PHE B CD2 
3714 C CE1 . PHE B 207 ? 0.7870 0.7081 0.9220 -0.0720 0.0212  0.0791  214 PHE B CE1 
3715 C CE2 . PHE B 207 ? 0.8314 0.7193 0.9398 -0.0879 0.0034  0.0912  214 PHE B CE2 
3716 C CZ  . PHE B 207 ? 0.7928 0.6922 0.9148 -0.0759 0.0107  0.0847  214 PHE B CZ  
3717 N N   . ALA B 208 ? 0.7808 0.6786 0.8998 -0.0934 0.0012  0.0854  215 ALA B N   
3718 C CA  . ALA B 208 ? 0.7531 0.6159 0.8570 -0.0895 -0.0094 0.0875  215 ALA B CA  
3719 C C   . ALA B 208 ? 0.7472 0.6007 0.8515 -0.0742 -0.0080 0.0807  215 ALA B C   
3720 O O   . ALA B 208 ? 0.7470 0.5808 0.8439 -0.0626 -0.0089 0.0778  215 ALA B O   
3721 C CB  . ALA B 208 ? 0.8295 0.6807 0.9220 -0.1074 -0.0210 0.0939  215 ALA B CB  
3722 N N   . VAL B 209 ? 0.7609 0.6299 0.8730 -0.0741 -0.0061 0.0771  216 VAL B N   
3723 C CA  . VAL B 209 ? 0.7531 0.6093 0.8593 -0.0612 -0.0062 0.0717  216 VAL B CA  
3724 C C   . VAL B 209 ? 0.7828 0.6411 0.8906 -0.0496 0.0053  0.0683  216 VAL B C   
3725 O O   . VAL B 209 ? 0.8092 0.6494 0.9051 -0.0407 0.0080  0.0656  216 VAL B O   
3726 C CB  . VAL B 209 ? 0.7116 0.5795 0.8236 -0.0634 -0.0122 0.0681  216 VAL B CB  
3727 C CG1 . VAL B 209 ? 0.6748 0.5201 0.7719 -0.0506 -0.0154 0.0638  216 VAL B CG1 
3728 C CG2 . VAL B 209 ? 0.7587 0.6279 0.8713 -0.0792 -0.0230 0.0716  216 VAL B CG2 
3729 N N   . VAL B 210 ? 0.7485 0.6282 0.8691 -0.0514 0.0119  0.0681  217 VAL B N   
3730 C CA  . VAL B 210 ? 0.7836 0.6639 0.9059 -0.0441 0.0214  0.0658  217 VAL B CA  
3731 C C   . VAL B 210 ? 0.7088 0.5782 0.8282 -0.0412 0.0251  0.0663  217 VAL B C   
3732 O O   . VAL B 210 ? 0.7612 0.6257 0.8779 -0.0358 0.0328  0.0633  217 VAL B O   
3733 C CB  . VAL B 210 ? 0.7316 0.6352 0.8671 -0.0464 0.0253  0.0645  217 VAL B CB  
3734 C CG1 . VAL B 210 ? 0.8216 0.7220 0.9579 -0.0412 0.0328  0.0626  217 VAL B CG1 
3735 C CG2 . VAL B 210 ? 0.7606 0.6786 0.9021 -0.0442 0.0216  0.0594  217 VAL B CG2 
3736 N N   . LEU B 211 ? 0.6921 0.5580 0.8116 -0.0452 0.0187  0.0691  218 LEU B N   
3737 C CA  . LEU B 211 ? 0.7815 0.6382 0.9007 -0.0389 0.0182  0.0666  218 LEU B CA  
3738 C C   . LEU B 211 ? 0.7854 0.6270 0.8947 -0.0300 0.0193  0.0611  218 LEU B C   
3739 O O   . LEU B 211 ? 0.7583 0.6050 0.8717 -0.0235 0.0285  0.0552  218 LEU B O   
3740 C CB  . LEU B 211 ? 0.8903 0.7368 1.0049 -0.0436 0.0059  0.0707  218 LEU B CB  
3741 C CG  . LEU B 211 ? 0.9084 0.7661 1.0273 -0.0521 0.0045  0.0757  218 LEU B CG  
3742 C CD1 . LEU B 211 ? 0.9606 0.7960 1.0647 -0.0577 -0.0108 0.0810  218 LEU B CD1 
3743 C CD2 . LEU B 211 ? 0.9549 0.8261 1.0871 -0.0452 0.0118  0.0709  218 LEU B CD2 
3744 N N   . TRP B 212 ? 0.8336 0.6589 0.9299 -0.0311 0.0105  0.0623  219 TRP B N   
3745 C CA  . TRP B 212 ? 0.8019 0.6101 0.8834 -0.0225 0.0106  0.0565  219 TRP B CA  
3746 C C   . TRP B 212 ? 0.7952 0.6085 0.8723 -0.0192 0.0247  0.0533  219 TRP B C   
3747 O O   . TRP B 212 ? 0.8886 0.7000 0.9599 -0.0125 0.0331  0.0465  219 TRP B O   
3748 C CB  . TRP B 212 ? 0.8148 0.6061 0.8830 -0.0268 -0.0019 0.0592  219 TRP B CB  
3749 C CG  . TRP B 212 ? 0.8862 0.6561 0.9354 -0.0171 -0.0041 0.0525  219 TRP B CG  
3750 C CD1 . TRP B 212 ? 0.8713 0.6218 0.9102 -0.0092 -0.0130 0.0468  219 TRP B CD1 
3751 C CD2 . TRP B 212 ? 0.9479 0.7113 0.9823 -0.0131 0.0021  0.0496  219 TRP B CD2 
3752 N NE1 . TRP B 212 ? 0.9056 0.6417 0.9256 -0.0003 -0.0110 0.0396  219 TRP B NE1 
3753 C CE2 . TRP B 212 ? 0.9629 0.7057 0.9781 -0.0036 -0.0012 0.0420  219 TRP B CE2 
3754 C CE3 . TRP B 212 ? 0.9931 0.7625 1.0251 -0.0157 0.0088  0.0521  219 TRP B CE3 
3755 C CZ2 . TRP B 212 ? 1.0583 0.7873 1.0499 0.0013  0.0035  0.0379  219 TRP B CZ2 
3756 C CZ3 . TRP B 212 ? 0.9595 0.7107 0.9666 -0.0110 0.0112  0.0491  219 TRP B CZ3 
3757 C CH2 . TRP B 212 ? 1.0222 0.7542 1.0086 -0.0036 0.0096  0.0426  219 TRP B CH2 
3758 N N   . ALA B 213 ? 0.7275 0.5466 0.8056 -0.0245 0.0264  0.0574  220 ALA B N   
3759 C CA  . ALA B 213 ? 0.7814 0.5968 0.8491 -0.0237 0.0360  0.0566  220 ALA B CA  
3760 C C   . ALA B 213 ? 0.8266 0.6539 0.9022 -0.0248 0.0499  0.0542  220 ALA B C   
3761 O O   . ALA B 213 ? 0.9423 0.7627 1.0035 -0.0256 0.0602  0.0520  220 ALA B O   
3762 C CB  . ALA B 213 ? 0.7493 0.5682 0.8194 -0.0265 0.0309  0.0597  220 ALA B CB  
3763 N N   . ILE B 214 ? 0.7777 0.6230 0.8746 -0.0267 0.0499  0.0547  221 ILE B N   
3764 C CA  . ILE B 214 ? 0.7476 0.6082 0.8576 -0.0282 0.0607  0.0512  221 ILE B CA  
3765 C C   . ILE B 214 ? 0.7264 0.5915 0.8371 -0.0225 0.0677  0.0425  221 ILE B C   
3766 O O   . ILE B 214 ? 0.8569 0.7337 0.9709 -0.0262 0.0812  0.0383  221 ILE B O   
3767 C CB  . ILE B 214 ? 0.6722 0.5490 0.8029 -0.0302 0.0560  0.0529  221 ILE B CB  
3768 C CG1 . ILE B 214 ? 0.6430 0.5214 0.7733 -0.0353 0.0550  0.0574  221 ILE B CG1 
3769 C CG2 . ILE B 214 ? 0.6554 0.5496 0.8037 -0.0296 0.0631  0.0469  221 ILE B CG2 
3770 C CD1 . ILE B 214 ? 0.5966 0.4886 0.7402 -0.0376 0.0496  0.0593  221 ILE B CD1 
3771 N N   . PHE B 215 ? 0.7664 0.6234 0.8740 -0.0141 0.0586  0.0389  222 PHE B N   
3772 C CA  . PHE B 215 ? 0.7724 0.6342 0.8802 -0.0044 0.0634  0.0270  222 PHE B CA  
3773 C C   . PHE B 215 ? 0.8066 0.6530 0.8883 -0.0019 0.0691  0.0235  222 PHE B C   
3774 O O   . PHE B 215 ? 0.8075 0.6638 0.8880 0.0047  0.0786  0.0118  222 PHE B O   
3775 C CB  . PHE B 215 ? 0.7337 0.5931 0.8522 0.0063  0.0481  0.0218  222 PHE B CB  
3776 C CG  . PHE B 215 ? 0.7417 0.6193 0.8840 0.0054  0.0455  0.0216  222 PHE B CG  
3777 C CD1 . PHE B 215 ? 0.8773 0.7818 1.0411 0.0107  0.0545  0.0098  222 PHE B CD1 
3778 C CD2 . PHE B 215 ? 0.7790 0.6507 0.9227 -0.0023 0.0359  0.0325  222 PHE B CD2 
3779 C CE1 . PHE B 215 ? 0.8730 0.7939 1.0589 0.0099  0.0505  0.0091  222 PHE B CE1 
3780 C CE2 . PHE B 215 ? 0.8513 0.7376 1.0128 -0.0034 0.0333  0.0323  222 PHE B CE2 
3781 C CZ  . PHE B 215 ? 0.8669 0.7759 1.0495 0.0033  0.0392  0.0208  222 PHE B CZ  
3782 N N   . ALA B 216 ? 0.7961 0.6206 0.8571 -0.0067 0.0634  0.0320  223 ALA B N   
3783 C CA  . ALA B 216 ? 0.8284 0.6334 0.8591 -0.0055 0.0673  0.0301  223 ALA B CA  
3784 C C   . ALA B 216 ? 0.8056 0.6087 0.8194 -0.0158 0.0825  0.0335  223 ALA B C   
3785 O O   . ALA B 216 ? 0.8044 0.5954 0.7911 -0.0160 0.0906  0.0299  223 ALA B O   
3786 C CB  . ALA B 216 ? 0.8410 0.6216 0.8569 -0.0046 0.0502  0.0360  223 ALA B CB  
3787 N N   . ASN B 217 ? 0.7895 0.6000 0.8145 -0.0248 0.0850  0.0405  224 ASN B N   
3788 C CA  . ASN B 217 ? 0.9376 0.7357 0.9408 -0.0364 0.0944  0.0460  224 ASN B CA  
3789 C C   . ASN B 217 ? 0.8233 0.5859 0.7904 -0.0358 0.0848  0.0515  224 ASN B C   
3790 O O   . ASN B 217 ? 0.9997 0.7421 0.9336 -0.0434 0.0926  0.0538  224 ASN B O   
3791 C CB  . ASN B 217 ? 0.9325 0.7457 0.9307 -0.0446 0.1158  0.0399  224 ASN B CB  
3792 C CG  . ASN B 217 ? 0.8917 0.7426 0.9291 -0.0447 0.1232  0.0330  224 ASN B CG  
3793 O OD1 . ASN B 217 ? 0.9458 0.8044 1.0038 -0.0477 0.1174  0.0376  224 ASN B OD1 
3794 N ND2 . ASN B 217 ? 0.9071 0.7825 0.9553 -0.0400 0.1346  0.0203  224 ASN B ND2 
3795 N N   . LYS B 218 ? 0.8884 0.6438 0.8616 -0.0281 0.0670  0.0533  225 LYS B N   
3796 C CA  . LYS B 218 ? 0.8803 0.6063 0.8269 -0.0248 0.0527  0.0565  225 LYS B CA  
3797 C C   . LYS B 218 ? 0.8434 0.5772 0.8116 -0.0190 0.0347  0.0569  225 LYS B C   
3798 O O   . LYS B 218 ? 0.9193 0.6759 0.9161 -0.0187 0.0339  0.0558  225 LYS B O   
3799 C CB  . LYS B 218 ? 0.9174 0.6223 0.8313 -0.0213 0.0543  0.0525  225 LYS B CB  
3800 C CG  . LYS B 218 ? 0.9346 0.6507 0.8611 -0.0132 0.0528  0.0449  225 LYS B CG  
3801 C CD  . LYS B 218 ? 1.0555 0.7493 0.9451 -0.0091 0.0557  0.0394  225 LYS B CD  
3802 C CE  . LYS B 218 ? 1.0649 0.7615 0.9629 0.0017  0.0481  0.0307  225 LYS B CE  
3803 N NZ  . LYS B 218 ? 1.1893 0.8609 1.0482 0.0076  0.0480  0.0239  225 LYS B NZ  
3804 N N   . GLU B 219 ? 0.8871 0.6018 0.8399 -0.0154 0.0198  0.0579  226 GLU B N   
3805 C CA  . GLU B 219 ? 0.9118 0.6378 0.8848 -0.0118 0.0032  0.0563  226 GLU B CA  
3806 C C   . GLU B 219 ? 0.9450 0.6669 0.9156 -0.0102 -0.0022 0.0536  226 GLU B C   
3807 O O   . GLU B 219 ? 0.9952 0.6960 0.9388 -0.0073 0.0015  0.0514  226 GLU B O   
3808 C CB  . GLU B 219 ? 1.0111 0.7198 0.9701 -0.0062 -0.0133 0.0552  226 GLU B CB  
3809 C CG  . GLU B 219 ? 1.0236 0.7265 0.9786 -0.0050 -0.0138 0.0565  226 GLU B CG  
3810 C CD  . GLU B 219 ? 1.1016 0.8258 1.0836 0.0015  -0.0280 0.0512  226 GLU B CD  
3811 O OE1 . GLU B 219 ? 0.8652 0.6256 0.8818 -0.0017 -0.0231 0.0496  226 GLU B OE1 
3812 O OE2 . GLU B 219 ? 1.1269 0.8315 1.0938 0.0105  -0.0448 0.0475  226 GLU B OE2 
3813 N N   . PRO B 220 ? 0.9682 0.7085 0.9641 -0.0131 -0.0111 0.0534  227 PRO B N   
3814 C CA  . PRO B 220 ? 0.8894 0.6181 0.8791 -0.0129 -0.0214 0.0513  227 PRO B CA  
3815 C C   . PRO B 220 ? 0.9244 0.6318 0.8947 -0.0091 -0.0376 0.0484  227 PRO B C   
3816 O O   . PRO B 220 ? 1.0137 0.7182 0.9794 -0.0060 -0.0440 0.0478  227 PRO B O   
3817 C CB  . PRO B 220 ? 0.9304 0.6833 0.9498 -0.0219 -0.0268 0.0540  227 PRO B CB  
3818 C CG  . PRO B 220 ? 0.9307 0.7078 0.9693 -0.0241 -0.0255 0.0547  227 PRO B CG  
3819 C CD  . PRO B 220 ? 0.9345 0.7052 0.9623 -0.0186 -0.0123 0.0552  227 PRO B CD  
3820 N N   . TYR B 221 ? 1.0282 0.7185 0.9865 -0.0083 -0.0466 0.0458  228 TYR B N   
3821 C CA  . TYR B 221 ? 0.9538 0.6255 0.8982 -0.0066 -0.0660 0.0424  228 TYR B CA  
3822 C C   . TYR B 221 ? 0.9861 0.6292 0.8946 0.0025  -0.0691 0.0398  228 TYR B C   
3823 O O   . TYR B 221 ? 1.0853 0.7204 0.9891 0.0050  -0.0865 0.0374  228 TYR B O   
3824 C CB  . TYR B 221 ? 0.9272 0.6252 0.9026 -0.0148 -0.0790 0.0429  228 TYR B CB  
3825 C CG  . TYR B 221 ? 0.9282 0.6544 0.9347 -0.0280 -0.0761 0.0470  228 TYR B CG  
3826 C CD1 . TYR B 221 ? 1.0477 0.7613 1.0507 -0.0355 -0.0828 0.0487  228 TYR B CD1 
3827 C CD2 . TYR B 221 ? 0.9005 0.6630 0.9365 -0.0338 -0.0693 0.0486  228 TYR B CD2 
3828 C CE1 . TYR B 221 ? 0.9810 0.7139 1.0053 -0.0504 -0.0824 0.0541  228 TYR B CE1 
3829 C CE2 . TYR B 221 ? 0.8747 0.6617 0.9337 -0.0482 -0.0665 0.0529  228 TYR B CE2 
3830 C CZ  . TYR B 221 ? 0.9144 0.6850 0.9659 -0.0576 -0.0730 0.0567  228 TYR B CZ  
3831 O OH  . TYR B 221 ? 0.9354 0.7241 1.0026 -0.0743 -0.0715 0.0626  228 TYR B OH  
3832 N N   . GLU B 222 ? 0.9870 0.6152 0.8693 0.0066  -0.0528 0.0398  229 GLU B N   
3833 C CA  . GLU B 222 ? 0.9757 0.5715 0.8142 0.0119  -0.0526 0.0391  229 GLU B CA  
3834 C C   . GLU B 222 ? 1.0994 0.6639 0.9085 0.0178  -0.0722 0.0341  229 GLU B C   
3835 O O   . GLU B 222 ? 1.0730 0.6128 0.8545 0.0217  -0.0837 0.0344  229 GLU B O   
3836 C CB  . GLU B 222 ? 1.0097 0.6004 0.8258 0.0113  -0.0287 0.0386  229 GLU B CB  
3837 C CG  . GLU B 222 ? 1.1213 0.7093 0.9297 0.0162  -0.0230 0.0308  229 GLU B CG  
3838 C CD  . GLU B 222 ? 1.1989 0.7961 0.9963 0.0160  0.0027  0.0268  229 GLU B CD  
3839 O OE1 . GLU B 222 ? 1.2583 0.8569 1.0522 0.0233  0.0067  0.0172  229 GLU B OE1 
3840 O OE2 . GLU B 222 ? 1.3573 0.9616 1.1506 0.0085  0.0183  0.0319  229 GLU B OE2 
3841 N N   . ASN B 223 ? 1.0354 0.5976 0.8486 0.0187  -0.0786 0.0294  230 ASN B N   
3842 C CA  . ASN B 223 ? 1.0841 0.6153 0.8698 0.0240  -0.0987 0.0235  230 ASN B CA  
3843 C C   . ASN B 223 ? 1.0608 0.5962 0.8664 0.0208  -0.1250 0.0228  230 ASN B C   
3844 O O   . ASN B 223 ? 1.0164 0.5239 0.7971 0.0253  -0.1440 0.0176  230 ASN B O   
3845 C CB  . ASN B 223 ? 1.0701 0.5906 0.8464 0.0279  -0.0968 0.0169  230 ASN B CB  
3846 C CG  . ASN B 223 ? 1.1795 0.6947 0.9290 0.0343  -0.0728 0.0124  230 ASN B CG  
3847 O OD1 . ASN B 223 ? 1.0865 0.5916 0.8067 0.0346  -0.0606 0.0143  230 ASN B OD1 
3848 N ND2 . ASN B 223 ? 1.0934 0.6156 0.8522 0.0390  -0.0666 0.0058  230 ASN B ND2 
3849 N N   . ALA B 224 ? 1.0100 0.5815 0.8592 0.0133  -0.1264 0.0263  231 ALA B N   
3850 C CA  . ALA B 224 ? 1.0761 0.6621 0.9495 0.0099  -0.1494 0.0232  231 ALA B CA  
3851 C C   . ALA B 224 ? 1.1161 0.6795 0.9638 0.0210  -0.1644 0.0194  231 ALA B C   
3852 O O   . ALA B 224 ? 1.2191 0.7687 1.0440 0.0272  -0.1542 0.0225  231 ALA B O   
3853 C CB  . ALA B 224 ? 0.9625 0.5971 0.8867 -0.0001 -0.1441 0.0257  231 ALA B CB  
3854 N N   . ILE B 225 ? 1.1932 0.7493 1.0417 0.0225  -0.1903 0.0129  232 ILE B N   
3855 C CA  . ILE B 225 ? 1.1591 0.6862 0.9785 0.0348  -0.2121 0.0075  232 ILE B CA  
3856 C C   . ILE B 225 ? 1.1841 0.7461 1.0447 0.0377  -0.2289 0.0012  232 ILE B C   
3857 O O   . ILE B 225 ? 1.3880 0.9357 1.2327 0.0499  -0.2367 -0.0006 232 ILE B O   
3858 C CB  . ILE B 225 ? 1.2157 0.7114 1.0098 0.0366  -0.2348 0.0013  232 ILE B CB  
3859 C CG1 . ILE B 225 ? 1.2607 0.7302 1.0244 0.0341  -0.2215 0.0033  232 ILE B CG1 
3860 C CG2 . ILE B 225 ? 1.2069 0.6612 0.9571 0.0508  -0.2564 -0.0032 232 ILE B CG2 
3861 C CD1 . ILE B 225 ? 1.3413 0.7842 1.0601 0.0407  -0.1979 0.0076  232 ILE B CD1 
3862 N N   . ALA B 226 ? 1.1208 0.7269 1.0315 0.0262  -0.2355 -0.0031 233 ALA B N   
3863 C CA  . ALA B 226 ? 1.0593 0.7114 1.0178 0.0276  -0.2501 -0.0127 233 ALA B CA  
3864 C C   . ALA B 226 ? 0.9868 0.6965 0.9970 0.0126  -0.2310 -0.0103 233 ALA B C   
3865 O O   . ALA B 226 ? 0.8809 0.5930 0.8924 -0.0015 -0.2129 -0.0013 233 ALA B O   
3866 C CB  . ALA B 226 ? 1.0969 0.7533 1.0679 0.0250  -0.2788 -0.0227 233 ALA B CB  
3867 N N   . GLU B 227 ? 0.9576 0.7122 1.0082 0.0174  -0.2370 -0.0200 234 GLU B N   
3868 C CA  . GLU B 227 ? 0.9568 0.7680 1.0531 0.0066  -0.2185 -0.0199 234 GLU B CA  
3869 C C   . GLU B 227 ? 0.9560 0.8070 1.0881 -0.0189 -0.2162 -0.0193 234 GLU B C   
3870 O O   . GLU B 227 ? 0.9265 0.7911 1.0666 -0.0354 -0.1955 -0.0095 234 GLU B O   
3871 C CB  . GLU B 227 ? 0.9669 0.8144 1.0942 0.0225  -0.2293 -0.0347 234 GLU B CB  
3872 C CG  . GLU B 227 ? 1.0228 0.9222 1.1878 0.0174  -0.2088 -0.0362 234 GLU B CG  
3873 C CD  . GLU B 227 ? 1.1554 1.0707 1.3341 0.0409  -0.2193 -0.0505 234 GLU B CD  
3874 O OE1 . GLU B 227 ? 1.2591 1.2344 1.4872 0.0431  -0.2276 -0.0675 234 GLU B OE1 
3875 O OE2 . GLU B 227 ? 1.0120 0.8791 1.1511 0.0569  -0.2202 -0.0456 234 GLU B OE2 
3876 N N   . GLN B 228 ? 0.9801 0.8449 1.1299 -0.0230 -0.2394 -0.0294 235 GLN B N   
3877 C CA  . GLN B 228 ? 0.9532 0.8468 1.1302 -0.0506 -0.2421 -0.0285 235 GLN B CA  
3878 C C   . GLN B 228 ? 0.9398 0.7860 1.0808 -0.0649 -0.2367 -0.0139 235 GLN B C   
3879 O O   . GLN B 228 ? 0.9350 0.8004 1.0925 -0.0907 -0.2293 -0.0073 235 GLN B O   
3880 C CB  . GLN B 228 ? 0.9937 0.9089 1.1957 -0.0507 -0.2714 -0.0440 235 GLN B CB  
3881 C CG  . GLN B 228 ? 1.0540 1.0360 1.3084 -0.0416 -0.2775 -0.0624 235 GLN B CG  
3882 C CD  . GLN B 228 ? 1.0941 1.1450 1.3946 -0.0624 -0.2534 -0.0625 235 GLN B CD  
3883 O OE1 . GLN B 228 ? 1.0461 1.1085 1.3532 -0.0929 -0.2420 -0.0522 235 GLN B OE1 
3884 N NE2 . GLN B 228 ? 1.1848 1.2767 1.5122 -0.0460 -0.2465 -0.0740 235 GLN B NE2 
3885 N N   . GLN B 229 ? 0.9298 0.7138 1.0201 -0.0486 -0.2411 -0.0098 236 GLN B N   
3886 C CA  . GLN B 229 ? 1.0077 0.7458 1.0614 -0.0556 -0.2340 0.0013  236 GLN B CA  
3887 C C   . GLN B 229 ? 0.9925 0.7439 1.0530 -0.0648 -0.2074 0.0121  236 GLN B C   
3888 O O   . GLN B 229 ? 1.0627 0.8102 1.1243 -0.0835 -0.2045 0.0194  236 GLN B O   
3889 C CB  . GLN B 229 ? 1.0133 0.6911 1.0120 -0.0337 -0.2375 0.0015  236 GLN B CB  
3890 C CG  . GLN B 229 ? 1.0665 0.6995 1.0274 -0.0352 -0.2300 0.0085  236 GLN B CG  
3891 C CD  . GLN B 229 ? 1.0799 0.6749 0.9961 -0.0157 -0.2158 0.0104  236 GLN B CD  
3892 O OE1 . GLN B 229 ? 1.0037 0.6029 0.9147 -0.0040 -0.2081 0.0101  236 GLN B OE1 
3893 N NE2 . GLN B 229 ? 1.0591 0.6174 0.9423 -0.0130 -0.2120 0.0118  236 GLN B NE2 
3894 N N   . LEU B 230 ? 0.9714 0.7345 1.0340 -0.0513 -0.1910 0.0128  237 LEU B N   
3895 C CA  . LEU B 230 ? 0.9786 0.7546 1.0472 -0.0564 -0.1667 0.0215  237 LEU B CA  
3896 C C   . LEU B 230 ? 0.8352 0.6629 0.9451 -0.0785 -0.1595 0.0233  237 LEU B C   
3897 O O   . LEU B 230 ? 0.7557 0.5798 0.8623 -0.0920 -0.1480 0.0329  237 LEU B O   
3898 C CB  . LEU B 230 ? 1.0013 0.7762 1.0618 -0.0372 -0.1544 0.0204  237 LEU B CB  
3899 C CG  . LEU B 230 ? 0.9984 0.7832 1.0623 -0.0388 -0.1304 0.0280  237 LEU B CG  
3900 C CD1 . LEU B 230 ? 1.0302 0.7805 1.0665 -0.0411 -0.1215 0.0359  237 LEU B CD1 
3901 C CD2 . LEU B 230 ? 0.9549 0.7350 1.0094 -0.0214 -0.1239 0.0256  237 LEU B CD2 
3902 N N   . ILE B 231 ? 0.8258 0.7014 0.9728 -0.0812 -0.1663 0.0132  238 ILE B N   
3903 C CA  . ILE B 231 ? 0.8186 0.7529 1.0068 -0.1039 -0.1575 0.0124  238 ILE B CA  
3904 C C   . ILE B 231 ? 0.8574 0.7831 1.0422 -0.1332 -0.1624 0.0212  238 ILE B C   
3905 O O   . ILE B 231 ? 0.9970 0.9290 1.1815 -0.1515 -0.1486 0.0315  238 ILE B O   
3906 C CB  . ILE B 231 ? 0.8416 0.8334 1.0733 -0.1007 -0.1675 -0.0047 238 ILE B CB  
3907 C CG1 . ILE B 231 ? 0.8537 0.8569 1.0907 -0.0734 -0.1621 -0.0134 238 ILE B CG1 
3908 C CG2 . ILE B 231 ? 0.8312 0.8873 1.1051 -0.1303 -0.1595 -0.0071 238 ILE B CG2 
3909 C CD1 . ILE B 231 ? 0.8868 0.9202 1.1510 -0.0573 -0.1822 -0.0328 238 ILE B CD1 
3910 N N   . MET B 232 ? 0.9146 0.8215 1.0933 -0.1374 -0.1842 0.0171  239 MET B N   
3911 C CA  . MET B 232 ? 0.9504 0.8408 1.1218 -0.1660 -0.1945 0.0247  239 MET B CA  
3912 C C   . MET B 232 ? 0.9316 0.7629 1.0603 -0.1664 -0.1904 0.0382  239 MET B C   
3913 O O   . MET B 232 ? 0.9259 0.7528 1.0514 -0.1925 -0.1893 0.0482  239 MET B O   
3914 C CB  . MET B 232 ? 0.9983 0.8794 1.1722 -0.1690 -0.2215 0.0158  239 MET B CB  
3915 C CG  . MET B 232 ? 1.1761 1.1132 1.3927 -0.2023 -0.2279 0.0113  239 MET B CG  
3916 S SD  . MET B 232 ? 1.1595 1.1935 1.4391 -0.2028 -0.2149 -0.0041 239 MET B SD  
3917 C CE  . MET B 232 ? 1.1963 1.2252 1.4808 -0.1643 -0.2373 -0.0230 239 MET B CE  
3918 N N   . ALA B 233 ? 0.8723 0.6615 0.9692 -0.1382 -0.1879 0.0377  240 ALA B N   
3919 C CA  . ALA B 233 ? 0.9006 0.6419 0.9621 -0.1330 -0.1820 0.0465  240 ALA B CA  
3920 C C   . ALA B 233 ? 0.9187 0.6797 0.9901 -0.1438 -0.1629 0.0558  240 ALA B C   
3921 O O   . ALA B 233 ? 1.0421 0.7780 1.0978 -0.1589 -0.1663 0.0648  240 ALA B O   
3922 C CB  . ALA B 233 ? 0.9250 0.6324 0.9569 -0.1022 -0.1776 0.0421  240 ALA B CB  
3923 N N   . ILE B 234 ? 0.9609 0.7637 1.0560 -0.1364 -0.1457 0.0532  241 ILE B N   
3924 C CA  . ILE B 234 ? 0.9413 0.7648 1.0452 -0.1451 -0.1272 0.0609  241 ILE B CA  
3925 C C   . ILE B 234 ? 0.9071 0.7573 1.0270 -0.1797 -0.1283 0.0676  241 ILE B C   
3926 O O   . ILE B 234 ? 0.8420 0.6748 0.9465 -0.1933 -0.1242 0.0785  241 ILE B O   
3927 C CB  . ILE B 234 ? 0.8412 0.6998 0.9641 -0.1283 -0.1102 0.0554  241 ILE B CB  
3928 C CG1 . ILE B 234 ? 0.8961 0.7206 0.9948 -0.1000 -0.1071 0.0526  241 ILE B CG1 
3929 C CG2 . ILE B 234 ? 0.8087 0.6892 0.9401 -0.1384 -0.0927 0.0626  241 ILE B CG2 
3930 C CD1 . ILE B 234 ? 0.9466 0.7955 1.0592 -0.0830 -0.1004 0.0447  241 ILE B CD1 
3931 N N   . LYS B 235 ? 0.8772 0.7682 1.0259 -0.1943 -0.1349 0.0605  242 LYS B N   
3932 C CA  . LYS B 235 ? 0.8818 0.8030 1.0461 -0.2322 -0.1352 0.0660  242 LYS B CA  
3933 C C   . LYS B 235 ? 0.8597 0.7276 0.9912 -0.2548 -0.1511 0.0784  242 LYS B C   
3934 O O   . LYS B 235 ? 0.9400 0.8121 1.0662 -0.2853 -0.1471 0.0894  242 LYS B O   
3935 C CB  . LYS B 235 ? 0.8756 0.8550 1.0812 -0.2424 -0.1408 0.0528  242 LYS B CB  
3936 C CG  . LYS B 235 ? 0.8716 0.9142 1.1138 -0.2282 -0.1244 0.0404  242 LYS B CG  
3937 C CD  . LYS B 235 ? 0.8942 0.9997 1.1816 -0.2357 -0.1317 0.0238  242 LYS B CD  
3938 C CE  . LYS B 235 ? 0.8995 1.0609 1.2129 -0.2773 -0.1218 0.0257  242 LYS B CE  
3939 N NZ  . LYS B 235 ? 0.8491 1.0583 1.1776 -0.2821 -0.0963 0.0249  242 LYS B NZ  
3940 N N   . SER B 236 ? 0.9292 0.7436 1.0346 -0.2390 -0.1693 0.0763  243 SER B N   
3941 C CA  . SER B 236 ? 1.1037 0.8560 1.1722 -0.2529 -0.1884 0.0856  243 SER B CA  
3942 C C   . SER B 236 ? 1.0924 0.7905 1.1243 -0.2331 -0.1869 0.0916  243 SER B C   
3943 O O   . SER B 236 ? 1.3172 0.9568 1.3163 -0.2276 -0.2057 0.0924  243 SER B O   
3944 C CB  . SER B 236 ? 1.1459 0.8714 1.2065 -0.2465 -0.2117 0.0771  243 SER B CB  
3945 O OG  . SER B 236 ? 1.2198 0.9157 1.2618 -0.2083 -0.2120 0.0691  243 SER B OG  
3946 N N   . GLY B 237 ? 1.0628 0.7805 1.1012 -0.2213 -0.1663 0.0937  244 GLY B N   
3947 C CA  . GLY B 237 ? 1.0954 0.7712 1.1057 -0.2053 -0.1645 0.0985  244 GLY B CA  
3948 C C   . GLY B 237 ? 1.0656 0.7304 1.0700 -0.1674 -0.1555 0.0895  244 GLY B C   
3949 O O   . GLY B 237 ? 1.0273 0.6727 1.0182 -0.1558 -0.1506 0.0919  244 GLY B O   
3950 N N   . ASN B 238 ? 1.0942 0.7698 1.1065 -0.1493 -0.1541 0.0791  245 ASN B N   
3951 C CA  . ASN B 238 ? 1.1500 0.8125 1.1510 -0.1171 -0.1447 0.0712  245 ASN B CA  
3952 C C   . ASN B 238 ? 1.0247 0.7223 1.0442 -0.1089 -0.1216 0.0723  245 ASN B C   
3953 O O   . ASN B 238 ? 0.9696 0.7101 1.0153 -0.1196 -0.1125 0.0738  245 ASN B O   
3954 C CB  . ASN B 238 ? 1.1745 0.8310 1.1696 -0.1015 -0.1507 0.0612  245 ASN B CB  
3955 C CG  . ASN B 238 ? 1.2966 0.9010 1.2577 -0.0904 -0.1675 0.0559  245 ASN B CG  
3956 O OD1 . ASN B 238 ? 1.3243 0.9016 1.2739 -0.1052 -0.1865 0.0589  245 ASN B OD1 
3957 N ND2 . ASN B 238 ? 1.2750 0.8635 1.2172 -0.0654 -0.1608 0.0476  245 ASN B ND2 
3958 N N   . ARG B 239 ? 1.0239 0.7039 1.0302 -0.0901 -0.1135 0.0701  246 ARG B N   
3959 C CA  . ARG B 239 ? 0.9976 0.7031 1.0175 -0.0821 -0.0937 0.0710  246 ARG B CA  
3960 C C   . ARG B 239 ? 0.9271 0.6238 0.9365 -0.0581 -0.0837 0.0628  246 ARG B C   
3961 O O   . ARG B 239 ? 0.9782 0.6483 0.9673 -0.0478 -0.0917 0.0566  246 ARG B O   
3962 C CB  . ARG B 239 ? 0.9716 0.6657 0.9867 -0.0890 -0.0951 0.0777  246 ARG B CB  
3963 C CG  . ARG B 239 ? 0.9343 0.6341 0.9528 -0.1178 -0.1034 0.0881  246 ARG B CG  
3964 C CD  . ARG B 239 ? 0.8712 0.6223 0.9174 -0.1301 -0.0888 0.0901  246 ARG B CD  
3965 N NE  . ARG B 239 ? 0.8533 0.6170 0.9023 -0.1597 -0.0919 0.0994  246 ARG B NE  
3966 C CZ  . ARG B 239 ? 0.8337 0.6112 0.8901 -0.1823 -0.0995 0.1011  246 ARG B CZ  
3967 N NH1 . ARG B 239 ? 0.9064 0.6835 0.9685 -0.1776 -0.1087 0.0938  246 ARG B NH1 
3968 N NH2 . ARG B 239 ? 0.8948 0.6873 0.9518 -0.2120 -0.0981 0.1103  246 ARG B NH2 
3969 N N   . PRO B 240 ? 0.9267 0.6453 0.9477 -0.0507 -0.0659 0.0626  247 PRO B N   
3970 C CA  . PRO B 240 ? 0.8881 0.5984 0.8971 -0.0323 -0.0546 0.0555  247 PRO B CA  
3971 C C   . PRO B 240 ? 0.9839 0.6668 0.9753 -0.0207 -0.0594 0.0492  247 PRO B C   
3972 O O   . PRO B 240 ? 0.9442 0.6172 0.9369 -0.0244 -0.0685 0.0515  247 PRO B O   
3973 C CB  . PRO B 240 ? 0.8144 0.5527 0.8417 -0.0320 -0.0376 0.0579  247 PRO B CB  
3974 C CG  . PRO B 240 ? 0.8283 0.5921 0.8750 -0.0458 -0.0392 0.0635  247 PRO B CG  
3975 C CD  . PRO B 240 ? 0.9019 0.6554 0.9464 -0.0597 -0.0548 0.0676  247 PRO B CD  
3976 N N   . ASP B 241 ? 1.0497 0.7192 1.0223 -0.0065 -0.0546 0.0403  248 ASP B N   
3977 C CA  . ASP B 241 ? 1.0717 0.7176 1.0270 0.0079  -0.0599 0.0300  248 ASP B CA  
3978 C C   . ASP B 241 ? 1.0873 0.7515 1.0571 0.0167  -0.0469 0.0251  248 ASP B C   
3979 O O   . ASP B 241 ? 0.9557 0.6422 0.9316 0.0205  -0.0270 0.0221  248 ASP B O   
3980 C CB  . ASP B 241 ? 1.1341 0.7635 1.0623 0.0196  -0.0569 0.0205  248 ASP B CB  
3981 C CG  . ASP B 241 ? 1.1242 0.7325 1.0345 0.0371  -0.0621 0.0062  248 ASP B CG  
3982 O OD1 . ASP B 241 ? 1.1494 0.7396 1.0608 0.0391  -0.0794 0.0047  248 ASP B OD1 
3983 O OD2 . ASP B 241 ? 1.0677 0.6773 0.9612 0.0487  -0.0489 -0.0042 248 ASP B OD2 
3984 N N   . VAL B 242 ? 1.0363 0.6887 1.0100 0.0189  -0.0601 0.0242  249 VAL B N   
3985 C CA  . VAL B 242 ? 1.0470 0.7156 1.0371 0.0281  -0.0536 0.0188  249 VAL B CA  
3986 C C   . VAL B 242 ? 1.0334 0.7073 1.0189 0.0494  -0.0441 0.0004  249 VAL B C   
3987 O O   . VAL B 242 ? 0.9601 0.6634 0.9647 0.0553  -0.0289 -0.0058 249 VAL B O   
3988 C CB  . VAL B 242 ? 1.1129 0.7600 1.1028 0.0241  -0.0750 0.0238  249 VAL B CB  
3989 C CG1 . VAL B 242 ? 1.1247 0.7853 1.1307 0.0367  -0.0729 0.0162  249 VAL B CG1 
3990 C CG2 . VAL B 242 ? 1.1032 0.7558 1.0993 -0.0003 -0.0779 0.0413  249 VAL B CG2 
3991 N N   . ASP B 243 ? 1.1079 0.7567 1.0689 0.0598  -0.0521 -0.0092 250 ASP B N   
3992 C CA  . ASP B 243 ? 1.2326 0.8902 1.1861 0.0796  -0.0405 -0.0289 250 ASP B CA  
3993 C C   . ASP B 243 ? 1.2224 0.9087 1.1745 0.0748  -0.0120 -0.0296 250 ASP B C   
3994 O O   . ASP B 243 ? 1.2379 0.9461 1.1918 0.0862  0.0047  -0.0449 250 ASP B O   
3995 C CB  . ASP B 243 ? 1.2908 0.9099 1.2137 0.0925  -0.0586 -0.0397 250 ASP B CB  
3996 C CG  . ASP B 243 ? 1.3054 0.8900 1.2243 0.0994  -0.0884 -0.0418 250 ASP B CG  
3997 O OD1 . ASP B 243 ? 1.3008 0.8945 1.2374 0.1093  -0.0928 -0.0480 250 ASP B OD1 
3998 O OD2 . ASP B 243 ? 1.3299 0.8749 1.2257 0.0943  -0.1098 -0.0372 250 ASP B OD2 
3999 N N   . ASP B 244 ? 1.3575 1.0431 1.3055 0.0576  -0.0074 -0.0140 251 ASP B N   
4000 C CA  . ASP B 244 ? 1.2228 0.9274 1.1659 0.0495  0.0156  -0.0107 251 ASP B CA  
4001 C C   . ASP B 244 ? 1.1645 0.9062 1.1368 0.0438  0.0337  -0.0091 251 ASP B C   
4002 O O   . ASP B 244 ? 1.1546 0.9106 1.1216 0.0358  0.0532  -0.0072 251 ASP B O   
4003 C CB  . ASP B 244 ? 1.1433 0.8314 1.0742 0.0361  0.0083  0.0039  251 ASP B CB  
4004 C CG  . ASP B 244 ? 1.2767 0.9604 1.1816 0.0317  0.0225  0.0054  251 ASP B CG  
4005 O OD1 . ASP B 244 ? 1.3341 1.0188 1.2184 0.0376  0.0369  -0.0048 251 ASP B OD1 
4006 O OD2 . ASP B 244 ? 1.1295 0.8071 1.0321 0.0218  0.0177  0.0166  251 ASP B OD2 
4007 N N   . ILE B 245 ? 1.1581 0.9112 1.1578 0.0458  0.0255  -0.0085 252 ILE B N   
4008 C CA  . ILE B 245 ? 1.1075 0.8958 1.1362 0.0445  0.0395  -0.0115 252 ILE B CA  
4009 C C   . ILE B 245 ? 1.2322 1.0425 1.2654 0.0589  0.0525  -0.0320 252 ILE B C   
4010 O O   . ILE B 245 ? 1.1959 1.0037 1.2364 0.0763  0.0399  -0.0455 252 ILE B O   
4011 C CB  . ILE B 245 ? 1.0325 0.8224 1.0843 0.0438  0.0241  -0.0058 252 ILE B CB  
4012 C CG1 . ILE B 245 ? 0.9919 0.7723 1.0421 0.0270  0.0179  0.0126  252 ILE B CG1 
4013 C CG2 . ILE B 245 ? 1.0321 0.8577 1.1139 0.0453  0.0357  -0.0119 252 ILE B CG2 
4014 C CD1 . ILE B 245 ? 1.0176 0.7893 1.0774 0.0229  0.0002  0.0202  252 ILE B CD1 
4015 N N   . THR B 246 ? 1.2806 1.1120 1.3083 0.0509  0.0769  -0.0346 253 THR B N   
4016 C CA  . THR B 246 ? 1.3203 1.1826 1.3527 0.0598  0.0957  -0.0548 253 THR B CA  
4017 C C   . THR B 246 ? 1.3048 1.2087 1.3802 0.0644  0.1005  -0.0650 253 THR B C   
4018 O O   . THR B 246 ? 1.5033 1.4246 1.5956 0.0843  0.0957  -0.0852 253 THR B O   
4019 C CB  . THR B 246 ? 1.3877 1.2583 1.3962 0.0431  0.1218  -0.0514 253 THR B CB  
4020 O OG1 . THR B 246 ? 1.4219 1.2506 1.3897 0.0379  0.1143  -0.0399 253 THR B OG1 
4021 C CG2 . THR B 246 ? 1.4917 1.3952 1.4990 0.0505  0.1433  -0.0737 253 THR B CG2 
4022 N N   . GLU B 247 ? 1.2911 1.2092 1.3834 0.0474  0.1076  -0.0521 254 GLU B N   
4023 C CA  . GLU B 247 ? 1.1210 1.0799 1.2539 0.0475  0.1134  -0.0600 254 GLU B CA  
4024 C C   . GLU B 247 ? 1.1054 1.0548 1.2587 0.0613  0.0873  -0.0606 254 GLU B C   
4025 O O   . GLU B 247 ? 1.1535 1.0642 1.2883 0.0638  0.0676  -0.0499 254 GLU B O   
4026 C CB  . GLU B 247 ? 1.0655 1.0371 1.2041 0.0233  0.1286  -0.0458 254 GLU B CB  
4027 C CG  . GLU B 247 ? 1.0939 1.0337 1.2217 0.0123  0.1155  -0.0238 254 GLU B CG  
4028 C CD  . GLU B 247 ? 0.9968 0.9514 1.1372 -0.0061 0.1257  -0.0145 254 GLU B CD  
4029 O OE1 . GLU B 247 ? 0.9247 0.8822 1.0854 -0.0060 0.1142  -0.0093 254 GLU B OE1 
4030 O OE2 . GLU B 247 ? 0.9768 0.9361 1.1029 -0.0216 0.1442  -0.0120 254 GLU B OE2 
4031 N N   . TYR B 248 ? 1.0342 1.0187 1.2238 0.0688  0.0871  -0.0733 255 TYR B N   
4032 C CA  . TYR B 248 ? 1.0069 0.9819 1.2137 0.0825  0.0613  -0.0753 255 TYR B CA  
4033 C C   . TYR B 248 ? 0.9294 0.8782 1.1287 0.0673  0.0498  -0.0518 255 TYR B C   
4034 O O   . TYR B 248 ? 0.9935 0.9616 1.2085 0.0533  0.0592  -0.0445 255 TYR B O   
4035 C CB  . TYR B 248 ? 1.0681 1.0914 1.3176 0.0928  0.0647  -0.0952 255 TYR B CB  
4036 C CG  . TYR B 248 ? 1.1530 1.1638 1.4176 0.1090  0.0353  -0.0990 255 TYR B CG  
4037 C CD1 . TYR B 248 ? 1.2596 1.2377 1.5104 0.1320  0.0092  -0.1080 255 TYR B CD1 
4038 C CD2 . TYR B 248 ? 1.1301 1.1555 1.4176 0.1009  0.0310  -0.0929 255 TYR B CD2 
4039 C CE1 . TYR B 248 ? 1.2462 1.2039 1.5032 0.1457  -0.0210 -0.1099 255 TYR B CE1 
4040 C CE2 . TYR B 248 ? 1.1668 1.1754 1.4618 0.1151  0.0022  -0.0954 255 TYR B CE2 
4041 C CZ  . TYR B 248 ? 1.2054 1.1787 1.4838 0.1370  -0.0240 -0.1032 255 TYR B CZ  
4042 O OH  . TYR B 248 ? 1.1675 1.1168 1.4466 0.1495  -0.0548 -0.1041 255 TYR B OH  
4043 N N   . CYS B 249 ? 0.9468 0.8526 1.1202 0.0685  0.0310  -0.0407 256 CYS B N   
4044 C CA  . CYS B 249 ? 0.9099 0.7923 1.0774 0.0586  0.0151  -0.0231 256 CYS B CA  
4045 C C   . CYS B 249 ? 0.9611 0.8257 1.1316 0.0747  -0.0112 -0.0302 256 CYS B C   
4046 O O   . CYS B 249 ? 1.0610 0.9025 1.2172 0.0895  -0.0251 -0.0392 256 CYS B O   
4047 C CB  . CYS B 249 ? 0.9695 0.8184 1.1074 0.0471  0.0103  -0.0072 256 CYS B CB  
4048 S SG  . CYS B 249 ? 1.0461 0.8770 1.1780 0.0307  -0.0033 0.0131  256 CYS B SG  
4049 N N   . PRO B 250 ? 0.9966 0.8668 1.1815 0.0728  -0.0207 -0.0266 257 PRO B N   
4050 C CA  . PRO B 250 ? 0.9697 0.8132 1.1497 0.0869  -0.0500 -0.0308 257 PRO B CA  
4051 C C   . PRO B 250 ? 1.0940 0.8845 1.2370 0.0820  -0.0711 -0.0178 257 PRO B C   
4052 O O   . PRO B 250 ? 1.2635 1.0431 1.3896 0.0634  -0.0630 -0.0020 257 PRO B O   
4053 C CB  . PRO B 250 ? 0.9787 0.8336 1.1720 0.0781  -0.0530 -0.0231 257 PRO B CB  
4054 C CG  . PRO B 250 ? 0.9621 0.8644 1.1834 0.0710  -0.0259 -0.0280 257 PRO B CG  
4055 C CD  . PRO B 250 ? 0.9971 0.8977 1.2030 0.0599  -0.0065 -0.0213 257 PRO B CD  
4056 N N   . ARG B 251 ? 1.1648 0.9228 1.2962 0.0986  -0.0994 -0.0255 258 ARG B N   
4057 C CA  . ARG B 251 ? 1.2273 0.9279 1.3202 0.0924  -0.1243 -0.0132 258 ARG B CA  
4058 C C   . ARG B 251 ? 1.1670 0.8513 1.2420 0.0647  -0.1263 0.0114  258 ARG B C   
4059 O O   . ARG B 251 ? 1.2844 0.9441 1.3352 0.0470  -0.1284 0.0257  258 ARG B O   
4060 C CB  . ARG B 251 ? 1.3481 1.0123 1.4300 0.1162  -0.1583 -0.0264 258 ARG B CB  
4061 C CG  . ARG B 251 ? 1.5349 1.2080 1.6279 0.1456  -0.1608 -0.0530 258 ARG B CG  
4062 C CD  . ARG B 251 ? 1.6824 1.3180 1.7655 0.1732  -0.1985 -0.0688 258 ARG B CD  
4063 N NE  . ARG B 251 ? 1.7911 1.4418 1.8882 0.2047  -0.2002 -0.0985 258 ARG B NE  
4064 C CZ  . ARG B 251 ? 1.9602 1.5854 2.0531 0.2371  -0.2310 -0.1209 258 ARG B CZ  
4065 N NH1 . ARG B 251 ? 2.0062 1.5805 2.0778 0.2434  -0.2686 -0.1161 258 ARG B NH1 
4066 N NH2 . ARG B 251 ? 1.9719 1.6209 2.0800 0.2649  -0.2264 -0.1498 258 ARG B NH2 
4067 N N   . GLU B 252 ? 1.1208 0.8231 1.2094 0.0608  -0.1244 0.0147  259 GLU B N   
4068 C CA  . GLU B 252 ? 1.0911 0.7816 1.1621 0.0363  -0.1259 0.0353  259 GLU B CA  
4069 C C   . GLU B 252 ? 1.0336 0.7492 1.1082 0.0140  -0.1002 0.0479  259 GLU B C   
4070 O O   . GLU B 252 ? 1.0677 0.7673 1.1206 -0.0075 -0.1027 0.0641  259 GLU B O   
4071 C CB  . GLU B 252 ? 1.0785 0.7852 1.1643 0.0407  -0.1297 0.0327  259 GLU B CB  
4072 C CG  . GLU B 252 ? 1.1767 0.8504 1.2525 0.0607  -0.1622 0.0231  259 GLU B CG  
4073 C CD  . GLU B 252 ? 1.1137 0.8165 1.2253 0.0912  -0.1640 -0.0033 259 GLU B CD  
4074 O OE1 . GLU B 252 ? 1.1361 0.8336 1.2549 0.1074  -0.1849 -0.0133 259 GLU B OE1 
4075 O OE2 . GLU B 252 ? 0.9909 0.7244 1.1241 0.0990  -0.1446 -0.0153 259 GLU B OE2 
4076 N N   . ILE B 253 ? 0.9535 0.7078 1.0542 0.0192  -0.0768 0.0394  260 ILE B N   
4077 C CA  . ILE B 253 ? 0.9514 0.7263 1.0552 0.0028  -0.0553 0.0484  260 ILE B CA  
4078 C C   . ILE B 253 ? 0.8575 0.6116 0.9425 -0.0032 -0.0578 0.0527  260 ILE B C   
4079 O O   . ILE B 253 ? 0.8984 0.6563 0.9770 -0.0205 -0.0514 0.0637  260 ILE B O   
4080 C CB  . ILE B 253 ? 0.8804 0.6955 1.0117 0.0079  -0.0322 0.0395  260 ILE B CB  
4081 C CG1 . ILE B 253 ? 0.8690 0.7042 1.0169 0.0064  -0.0301 0.0392  260 ILE B CG1 
4082 C CG2 . ILE B 253 ? 0.9266 0.7537 1.0559 -0.0047 -0.0149 0.0467  260 ILE B CG2 
4083 C CD1 . ILE B 253 ? 0.9573 0.8282 1.1331 0.0120  -0.0126 0.0283  260 ILE B CD1 
4084 N N   . ILE B 254 ? 0.8998 0.6347 0.9777 0.0121  -0.0677 0.0423  261 ILE B N   
4085 C CA  . ILE B 254 ? 1.0351 0.7427 1.0913 0.0075  -0.0756 0.0456  261 ILE B CA  
4086 C C   . ILE B 254 ? 0.9814 0.6539 1.0121 -0.0109 -0.0954 0.0605  261 ILE B C   
4087 O O   . ILE B 254 ? 0.8847 0.5532 0.9057 -0.0289 -0.0937 0.0704  261 ILE B O   
4088 C CB  . ILE B 254 ? 1.0731 0.7659 1.1247 0.0302  -0.0832 0.0287  261 ILE B CB  
4089 C CG1 . ILE B 254 ? 1.1158 0.8463 1.1870 0.0397  -0.0581 0.0171  261 ILE B CG1 
4090 C CG2 . ILE B 254 ? 1.1661 0.8217 1.1908 0.0257  -0.0976 0.0321  261 ILE B CG2 
4091 C CD1 . ILE B 254 ? 1.2433 0.9764 1.3185 0.0642  -0.0594 -0.0041 261 ILE B CD1 
4092 N N   . SER B 255 ? 0.9665 0.6143 0.9860 -0.0073 -0.1145 0.0616  262 SER B N   
4093 C CA  . SER B 255 ? 1.0064 0.6188 0.9963 -0.0288 -0.1327 0.0777  262 SER B CA  
4094 C C   . SER B 255 ? 0.9930 0.6327 0.9868 -0.0548 -0.1163 0.0921  262 SER B C   
4095 O O   . SER B 255 ? 1.1323 0.7582 1.1072 -0.0790 -0.1207 0.1048  262 SER B O   
4096 C CB  . SER B 255 ? 1.0216 0.6006 0.9959 -0.0183 -0.1571 0.0758  262 SER B CB  
4097 O OG  . SER B 255 ? 0.9960 0.5426 0.9612 0.0046  -0.1773 0.0622  262 SER B OG  
4098 N N   . LEU B 256 ? 0.9673 0.6475 0.9864 -0.0502 -0.0975 0.0885  263 LEU B N   
4099 C CA  . LEU B 256 ? 0.9481 0.6584 0.9734 -0.0701 -0.0812 0.0981  263 LEU B CA  
4100 C C   . LEU B 256 ? 0.9170 0.6494 0.9514 -0.0808 -0.0669 0.1000  263 LEU B C   
4101 O O   . LEU B 256 ? 0.8291 0.5718 0.8576 -0.1028 -0.0631 0.1093  263 LEU B O   
4102 C CB  . LEU B 256 ? 0.9527 0.6967 1.0016 -0.0606 -0.0670 0.0922  263 LEU B CB  
4103 C CG  . LEU B 256 ? 0.8392 0.6148 0.8947 -0.0767 -0.0510 0.0988  263 LEU B CG  
4104 C CD1 . LEU B 256 ? 0.9361 0.6944 0.9636 -0.0993 -0.0604 0.1121  263 LEU B CD1 
4105 C CD2 . LEU B 256 ? 0.8391 0.6407 0.9153 -0.0659 -0.0408 0.0919  263 LEU B CD2 
4106 N N   . MET B 257 ? 0.8967 0.6374 0.9443 -0.0659 -0.0597 0.0902  264 MET B N   
4107 C CA  . MET B 257 ? 0.9089 0.6673 0.9636 -0.0733 -0.0496 0.0907  264 MET B CA  
4108 C C   . MET B 257 ? 0.9775 0.7106 1.0132 -0.0884 -0.0641 0.0972  264 MET B C   
4109 O O   . MET B 257 ? 1.1047 0.8566 1.1454 -0.1050 -0.0590 0.1018  264 MET B O   
4110 C CB  . MET B 257 ? 0.9029 0.6735 0.9706 -0.0552 -0.0380 0.0798  264 MET B CB  
4111 C CG  . MET B 257 ? 0.9344 0.6789 0.9913 -0.0397 -0.0469 0.0713  264 MET B CG  
4112 S SD  . MET B 257 ? 0.9257 0.6863 0.9915 -0.0233 -0.0298 0.0596  264 MET B SD  
4113 C CE  . MET B 257 ? 0.9403 0.7270 1.0271 -0.0143 -0.0169 0.0537  264 MET B CE  
4114 N N   . LYS B 258 ? 0.9406 0.6323 0.9558 -0.0825 -0.0831 0.0962  265 LYS B N   
4115 C CA  . LYS B 258 ? 1.0601 0.7183 1.0517 -0.0999 -0.1013 0.1038  265 LYS B CA  
4116 C C   . LYS B 258 ? 1.0676 0.7244 1.0460 -0.1304 -0.1051 0.1187  265 LYS B C   
4117 O O   . LYS B 258 ? 1.0877 0.7447 1.0600 -0.1533 -0.1085 0.1255  265 LYS B O   
4118 C CB  . LYS B 258 ? 1.0767 0.6838 1.0448 -0.0851 -0.1246 0.0986  265 LYS B CB  
4119 C CG  . LYS B 258 ? 1.0612 0.6681 1.0367 -0.0591 -0.1216 0.0831  265 LYS B CG  
4120 C CD  . LYS B 258 ? 1.0437 0.6035 0.9975 -0.0412 -0.1453 0.0745  265 LYS B CD  
4121 C CE  . LYS B 258 ? 1.0116 0.5731 0.9691 -0.0176 -0.1408 0.0580  265 LYS B CE  
4122 N NZ  . LYS B 258 ? 0.9681 0.4814 0.9019 -0.0004 -0.1666 0.0479  265 LYS B NZ  
4123 N N   . LEU B 259 ? 1.0710 0.7273 1.0440 -0.1316 -0.1047 0.1230  266 LEU B N   
4124 C CA  . LEU B 259 ? 1.1175 0.7767 1.0750 -0.1611 -0.1043 0.1368  266 LEU B CA  
4125 C C   . LEU B 259 ? 1.0552 0.7721 1.0382 -0.1754 -0.0806 0.1369  266 LEU B C   
4126 O O   . LEU B 259 ? 0.9369 0.6652 0.9129 -0.2043 -0.0786 0.1454  266 LEU B O   
4127 C CB  . LEU B 259 ? 1.1293 0.7739 1.0739 -0.1549 -0.1099 0.1394  266 LEU B CB  
4128 C CG  . LEU B 259 ? 1.1713 0.8015 1.0854 -0.1835 -0.1151 0.1546  266 LEU B CG  
4129 C CD1 . LEU B 259 ? 1.2167 0.7982 1.0914 -0.2107 -0.1358 0.1681  266 LEU B CD1 
4130 C CD2 . LEU B 259 ? 1.1748 0.7852 1.0776 -0.1680 -0.1248 0.1534  266 LEU B CD2 
4131 N N   . CYS B 260 ? 0.8757 0.6291 0.8878 -0.1553 -0.0637 0.1265  267 CYS B N   
4132 C CA  . CYS B 260 ? 0.8109 0.6166 0.8480 -0.1621 -0.0441 0.1231  267 CYS B CA  
4133 C C   . CYS B 260 ? 0.8032 0.6267 0.8547 -0.1672 -0.0424 0.1189  267 CYS B C   
4134 O O   . CYS B 260 ? 0.7943 0.6585 0.8619 -0.1807 -0.0316 0.1174  267 CYS B O   
4135 C CB  . CYS B 260 ? 0.8315 0.6619 0.8897 -0.1400 -0.0304 0.1140  267 CYS B CB  
4136 S SG  . CYS B 260 ? 0.9102 0.7334 0.9575 -0.1375 -0.0308 0.1174  267 CYS B SG  
4137 N N   . TRP B 261 ? 0.9017 0.6969 0.9478 -0.1562 -0.0537 0.1156  268 TRP B N   
4138 C CA  . TRP B 261 ? 0.8536 0.6576 0.9081 -0.1629 -0.0573 0.1123  268 TRP B CA  
4139 C C   . TRP B 261 ? 1.0847 0.8626 1.1198 -0.1882 -0.0739 0.1209  268 TRP B C   
4140 O O   . TRP B 261 ? 1.0367 0.8076 1.0737 -0.1894 -0.0827 0.1173  268 TRP B O   
4141 C CB  . TRP B 261 ? 0.9074 0.7030 0.9683 -0.1369 -0.0576 0.1019  268 TRP B CB  
4142 C CG  . TRP B 261 ? 0.9188 0.6684 0.9591 -0.1210 -0.0705 0.0993  268 TRP B CG  
4143 C CD1 . TRP B 261 ? 0.9477 0.6540 0.9634 -0.1281 -0.0903 0.1035  268 TRP B CD1 
4144 C CD2 . TRP B 261 ? 0.8307 0.5744 0.8730 -0.0949 -0.0648 0.0898  268 TRP B CD2 
4145 N NE1 . TRP B 261 ? 0.8666 0.5435 0.8712 -0.1044 -0.0970 0.0951  268 TRP B NE1 
4146 C CE2 . TRP B 261 ? 0.9675 0.6696 0.9886 -0.0851 -0.0799 0.0866  268 TRP B CE2 
4147 C CE3 . TRP B 261 ? 0.9161 0.6847 0.9738 -0.0800 -0.0484 0.0833  268 TRP B CE3 
4148 C CZ2 . TRP B 261 ? 1.0324 0.7248 1.0505 -0.0608 -0.0761 0.0758  268 TRP B CZ2 
4149 C CZ3 . TRP B 261 ? 0.8784 0.6337 0.9304 -0.0595 -0.0448 0.0750  268 TRP B CZ3 
4150 C CH2 . TRP B 261 ? 0.8822 0.6035 0.9160 -0.0501 -0.0572 0.0707  268 TRP B CH2 
4151 N N   . GLU B 262 ? 1.1460 0.9071 1.1596 -0.2102 -0.0793 0.1325  269 GLU B N   
4152 C CA  . GLU B 262 ? 1.0476 0.7872 1.0405 -0.2422 -0.0931 0.1430  269 GLU B CA  
4153 C C   . GLU B 262 ? 1.0309 0.8189 1.0495 -0.2626 -0.0848 0.1397  269 GLU B C   
4154 O O   . GLU B 262 ? 0.9196 0.7637 0.9663 -0.2626 -0.0658 0.1336  269 GLU B O   
4155 C CB  . GLU B 262 ? 1.1083 0.8303 1.0726 -0.2667 -0.0957 0.1570  269 GLU B CB  
4156 C CG  . GLU B 262 ? 1.1560 0.8128 1.0851 -0.2537 -0.1161 0.1621  269 GLU B CG  
4157 C CD  . GLU B 262 ? 1.3072 0.9048 1.2086 -0.2582 -0.1428 0.1654  269 GLU B CD  
4158 O OE1 . GLU B 262 ? 1.4398 0.9990 1.3318 -0.2291 -0.1569 0.1581  269 GLU B OE1 
4159 O OE2 . GLU B 262 ? 1.2489 0.8411 1.1401 -0.2900 -0.1497 0.1735  269 GLU B OE2 
4160 N N   . ALA B 263 ? 1.0093 0.7749 1.0188 -0.2784 -0.1010 0.1423  270 ALA B N   
4161 C CA  . ALA B 263 ? 1.0141 0.8244 1.0487 -0.3011 -0.0973 0.1386  270 ALA B CA  
4162 C C   . ALA B 263 ? 1.0233 0.8828 1.0673 -0.3351 -0.0812 0.1442  270 ALA B C   
4163 O O   . ALA B 263 ? 0.9524 0.8780 1.0344 -0.3356 -0.0653 0.1331  270 ALA B O   
4164 C CB  . ALA B 263 ? 1.0461 0.8145 1.0620 -0.3176 -0.1207 0.1430  270 ALA B CB  
4165 N N   . ASN B 264 ? 1.0035 0.8294 1.0109 -0.3604 -0.0858 0.1599  271 ASN B N   
4166 C CA  . ASN B 264 ? 1.1088 0.9742 1.1137 -0.3969 -0.0697 0.1675  271 ASN B CA  
4167 C C   . ASN B 264 ? 1.0837 0.9755 1.0959 -0.3764 -0.0509 0.1631  271 ASN B C   
4168 O O   . ASN B 264 ? 1.1738 1.0171 1.1592 -0.3580 -0.0591 0.1687  271 ASN B O   
4169 C CB  . ASN B 264 ? 1.2505 1.0568 1.2022 -0.4351 -0.0855 0.1885  271 ASN B CB  
4170 C CG  . ASN B 264 ? 1.2637 1.1074 1.2043 -0.4771 -0.0673 0.1980  271 ASN B CG  
4171 O OD1 . ASN B 264 ? 1.3188 1.2416 1.2979 -0.4833 -0.0433 0.1869  271 ASN B OD1 
4172 N ND2 . ASN B 264 ? 1.2195 1.0046 1.1049 -0.5042 -0.0795 0.2175  271 ASN B ND2 
4173 N N   . PRO B 265 ? 1.0214 0.9890 1.0690 -0.3796 -0.0276 0.1521  272 PRO B N   
4174 C CA  . PRO B 265 ? 1.0375 1.0312 1.0899 -0.3637 -0.0102 0.1474  272 PRO B CA  
4175 C C   . PRO B 265 ? 1.0994 1.0549 1.1065 -0.3800 -0.0117 0.1633  272 PRO B C   
4176 O O   . PRO B 265 ? 1.1611 1.0963 1.1602 -0.3536 -0.0119 0.1621  272 PRO B O   
4177 C CB  . PRO B 265 ? 0.9997 1.0792 1.0904 -0.3770 0.0116  0.1341  272 PRO B CB  
4178 C CG  . PRO B 265 ? 0.9917 1.0926 1.1147 -0.3744 0.0040  0.1239  272 PRO B CG  
4179 C CD  . PRO B 265 ? 1.0259 1.0609 1.1154 -0.3926 -0.0183 0.1395  272 PRO B CD  
4180 N N   . GLU B 266 ? 1.2226 1.1644 1.1980 -0.4235 -0.0146 0.1781  273 GLU B N   
4181 C CA  . GLU B 266 ? 1.4003 1.2995 1.3244 -0.4418 -0.0183 0.1947  273 GLU B CA  
4182 C C   . GLU B 266 ? 1.4185 1.2310 1.3053 -0.4198 -0.0450 0.2040  273 GLU B C   
4183 O O   . GLU B 266 ? 1.5028 1.2859 1.3587 -0.4158 -0.0482 0.2110  273 GLU B O   
4184 C CB  . GLU B 266 ? 1.6771 1.5784 1.5699 -0.4974 -0.0152 0.2098  273 GLU B CB  
4185 C CG  . GLU B 266 ? 1.9045 1.7946 1.7527 -0.5197 -0.0069 0.2222  273 GLU B CG  
4186 C CD  . GLU B 266 ? 1.9164 1.8770 1.7927 -0.5047 0.0210  0.2073  273 GLU B CD  
4187 O OE1 . GLU B 266 ? 2.1320 2.1729 2.0570 -0.5052 0.0421  0.1905  273 GLU B OE1 
4188 O OE2 . GLU B 266 ? 1.6344 1.5688 1.4834 -0.4916 0.0199  0.2113  273 GLU B OE2 
4189 N N   . ALA B 267 ? 1.3122 1.0873 1.2037 -0.4031 -0.0642 0.2016  274 ALA B N   
4190 C CA  . ALA B 267 ? 1.2594 0.9651 1.1280 -0.3722 -0.0878 0.2031  274 ALA B CA  
4191 C C   . ALA B 267 ? 1.1724 0.8959 1.0677 -0.3278 -0.0789 0.1894  274 ALA B C   
4192 O O   . ALA B 267 ? 1.0866 0.7636 0.9639 -0.3050 -0.0946 0.1898  274 ALA B O   
4193 C CB  . ALA B 267 ? 1.2170 0.8839 1.0846 -0.3649 -0.1087 0.2012  274 ALA B CB  
4194 N N   . ARG B 268 ? 1.0785 0.8685 1.0170 -0.3155 -0.0557 0.1762  275 ARG B N   
4195 C CA  . ARG B 268 ? 1.0487 0.8560 1.0109 -0.2788 -0.0467 0.1642  275 ARG B CA  
4196 C C   . ARG B 268 ? 1.1232 0.9343 1.0675 -0.2837 -0.0396 0.1689  275 ARG B C   
4197 O O   . ARG B 268 ? 1.0637 0.8958 0.9937 -0.3143 -0.0299 0.1760  275 ARG B O   
4198 C CB  . ARG B 268 ? 0.9737 0.8427 0.9825 -0.2647 -0.0280 0.1488  275 ARG B CB  
4199 C CG  . ARG B 268 ? 0.9704 0.8399 0.9968 -0.2602 -0.0349 0.1430  275 ARG B CG  
4200 C CD  . ARG B 268 ? 0.8950 0.8268 0.9630 -0.2526 -0.0190 0.1287  275 ARG B CD  
4201 N NE  . ARG B 268 ? 0.8889 0.8244 0.9698 -0.2579 -0.0273 0.1250  275 ARG B NE  
4202 C CZ  . ARG B 268 ? 0.8564 0.8437 0.9708 -0.2591 -0.0195 0.1133  275 ARG B CZ  
4203 N NH1 . ARG B 268 ? 0.8180 0.8603 0.9581 -0.2534 -0.0025 0.1027  275 ARG B NH1 
4204 N NH2 . ARG B 268 ? 0.9042 0.8876 1.0266 -0.2645 -0.0310 0.1107  275 ARG B NH2 
4205 N N   . PRO B 269 ? 1.1180 0.9127 1.0638 -0.2546 -0.0435 0.1639  276 PRO B N   
4206 C CA  . PRO B 269 ? 1.0948 0.8969 1.0271 -0.2564 -0.0370 0.1661  276 PRO B CA  
4207 C C   . PRO B 269 ? 1.0023 0.8704 0.9674 -0.2524 -0.0119 0.1546  276 PRO B C   
4208 O O   . PRO B 269 ? 0.9569 0.8612 0.9552 -0.2457 -0.0020 0.1447  276 PRO B O   
4209 C CB  . PRO B 269 ? 1.2031 0.9722 1.1358 -0.2245 -0.0505 0.1612  276 PRO B CB  
4210 C CG  . PRO B 269 ? 1.1505 0.9268 1.1151 -0.2008 -0.0499 0.1501  276 PRO B CG  
4211 C CD  . PRO B 269 ? 1.1450 0.9284 1.1126 -0.2191 -0.0491 0.1530  276 PRO B CD  
4212 N N   . THR B 270 ? 1.1100 0.9905 1.0625 -0.2565 -0.0040 0.1552  277 THR B N   
4213 C CA  . THR B 270 ? 1.1575 1.0948 1.1390 -0.2460 0.0167  0.1415  277 THR B CA  
4214 C C   . THR B 270 ? 1.0260 0.9525 1.0207 -0.2136 0.0129  0.1333  277 THR B C   
4215 O O   . THR B 270 ? 1.2171 1.0997 1.2000 -0.2017 -0.0039 0.1378  277 THR B O   
4216 C CB  . THR B 270 ? 1.2894 1.2571 1.2513 -0.2724 0.0312  0.1441  277 THR B CB  
4217 O OG1 . THR B 270 ? 1.6351 1.6546 1.6258 -0.2563 0.0484  0.1277  277 THR B OG1 
4218 C CG2 . THR B 270 ? 1.3526 1.2752 1.2651 -0.2853 0.0199  0.1579  277 THR B CG2 
4219 N N   . PHE B 271 ? 0.8441 0.8113 0.8647 -0.1991 0.0271  0.1201  278 PHE B N   
4220 C CA  . PHE B 271 ? 0.8851 0.8453 0.9226 -0.1705 0.0244  0.1116  278 PHE B CA  
4221 C C   . PHE B 271 ? 0.9074 0.8431 0.9220 -0.1675 0.0160  0.1154  278 PHE B C   
4222 O O   . PHE B 271 ? 1.0825 0.9986 1.1061 -0.1480 0.0070  0.1121  278 PHE B O   
4223 C CB  . PHE B 271 ? 0.7666 0.7693 0.8361 -0.1550 0.0383  0.0962  278 PHE B CB  
4224 C CG  . PHE B 271 ? 0.7618 0.7737 0.8567 -0.1452 0.0394  0.0904  278 PHE B CG  
4225 C CD1 . PHE B 271 ? 0.8020 0.7878 0.9058 -0.1278 0.0317  0.0898  278 PHE B CD1 
4226 C CD2 . PHE B 271 ? 0.8261 0.8748 0.9359 -0.1535 0.0478  0.0844  278 PHE B CD2 
4227 C CE1 . PHE B 271 ? 0.8478 0.8381 0.9689 -0.1194 0.0322  0.0850  278 PHE B CE1 
4228 C CE2 . PHE B 271 ? 0.7925 0.8465 0.9233 -0.1433 0.0459  0.0786  278 PHE B CE2 
4229 C CZ  . PHE B 271 ? 0.7059 0.7276 0.8395 -0.1264 0.0378  0.0798  278 PHE B CZ  
4230 N N   . PRO B 272 ? 0.9849 0.9247 0.9707 -0.1866 0.0195  0.1209  279 PRO B N   
4231 C CA  . PRO B 272 ? 0.9997 0.9050 0.9544 -0.1864 0.0062  0.1272  279 PRO B CA  
4232 C C   . PRO B 272 ? 0.9470 0.7970 0.8785 -0.1874 -0.0170 0.1386  279 PRO B C   
4233 O O   . PRO B 272 ? 1.1774 1.0000 1.1044 -0.1714 -0.0324 0.1372  279 PRO B O   
4234 C CB  . PRO B 272 ? 0.9939 0.9148 0.9166 -0.2124 0.0165  0.1323  279 PRO B CB  
4235 C CG  . PRO B 272 ? 0.9299 0.9103 0.8850 -0.2100 0.0387  0.1184  279 PRO B CG  
4236 C CD  . PRO B 272 ? 0.9245 0.9106 0.9109 -0.2030 0.0382  0.1161  279 PRO B CD  
4237 N N   . GLY B 273 ? 1.0440 0.8786 0.9616 -0.2055 -0.0209 0.1483  280 GLY B N   
4238 C CA  . GLY B 273 ? 1.0334 0.8137 0.9307 -0.2043 -0.0446 0.1570  280 GLY B CA  
4239 C C   . GLY B 273 ? 1.0108 0.7854 0.9419 -0.1741 -0.0518 0.1465  280 GLY B C   
4240 O O   . GLY B 273 ? 1.1137 0.8485 1.0335 -0.1610 -0.0729 0.1470  280 GLY B O   
4241 N N   . ILE B 274 ? 0.9888 0.8026 0.9592 -0.1630 -0.0351 0.1360  281 ILE B N   
4242 C CA  . ILE B 274 ? 0.9489 0.7634 0.9505 -0.1362 -0.0373 0.1252  281 ILE B CA  
4243 C C   . ILE B 274 ? 0.9164 0.7326 0.9285 -0.1178 -0.0408 0.1175  281 ILE B C   
4244 O O   . ILE B 274 ? 1.0965 0.8902 1.1125 -0.1017 -0.0553 0.1134  281 ILE B O   
4245 C CB  . ILE B 274 ? 0.9303 0.7819 0.9648 -0.1304 -0.0195 0.1169  281 ILE B CB  
4246 C CG1 . ILE B 274 ? 0.9171 0.7629 0.9452 -0.1448 -0.0210 0.1225  281 ILE B CG1 
4247 C CG2 . ILE B 274 ? 0.8644 0.7180 0.9258 -0.1056 -0.0188 0.1062  281 ILE B CG2 
4248 C CD1 . ILE B 274 ? 0.8472 0.7309 0.9019 -0.1435 -0.0056 0.1152  281 ILE B CD1 
4249 N N   . GLU B 275 ? 0.8644 0.7084 0.8817 -0.1201 -0.0286 0.1141  282 GLU B N   
4250 C CA  . GLU B 275 ? 0.9016 0.7505 0.9300 -0.1051 -0.0315 0.1063  282 GLU B CA  
4251 C C   . GLU B 275 ? 0.9451 0.7566 0.9510 -0.1008 -0.0545 0.1097  282 GLU B C   
4252 O O   . GLU B 275 ? 1.0497 0.8591 1.0755 -0.0821 -0.0632 0.1007  282 GLU B O   
4253 C CB  . GLU B 275 ? 0.9557 0.8333 0.9827 -0.1113 -0.0179 0.1031  282 GLU B CB  
4254 C CG  . GLU B 275 ? 0.9142 0.8014 0.9594 -0.0955 -0.0188 0.0929  282 GLU B CG  
4255 C CD  . GLU B 275 ? 1.0345 0.9460 1.0756 -0.0992 -0.0077 0.0879  282 GLU B CD  
4256 O OE1 . GLU B 275 ? 0.9474 0.8620 0.9992 -0.0882 -0.0111 0.0801  282 GLU B OE1 
4257 O OE2 . GLU B 275 ? 1.0197 0.9492 1.0486 -0.1126 0.0040  0.0899  282 GLU B OE2 
4258 N N   . GLU B 276 ? 1.0193 0.8023 0.9835 -0.1189 -0.0648 0.1221  283 GLU B N   
4259 C CA  . GLU B 276 ? 1.1051 0.8423 1.0378 -0.1161 -0.0916 0.1272  283 GLU B CA  
4260 C C   . GLU B 276 ? 1.0789 0.7890 1.0228 -0.0969 -0.1112 0.1219  283 GLU B C   
4261 O O   . GLU B 276 ? 1.1196 0.8120 1.0654 -0.0796 -0.1307 0.1152  283 GLU B O   
4262 C CB  . GLU B 276 ? 1.2900 0.9950 1.1681 -0.1442 -0.0988 0.1441  283 GLU B CB  
4263 C CG  . GLU B 276 ? 1.3633 1.0867 1.2196 -0.1604 -0.0861 0.1475  283 GLU B CG  
4264 C CD  . GLU B 276 ? 1.3838 1.0851 1.1878 -0.1937 -0.0862 0.1642  283 GLU B CD  
4265 O OE1 . GLU B 276 ? 1.3841 1.0963 1.1892 -0.2114 -0.0750 0.1699  283 GLU B OE1 
4266 O OE2 . GLU B 276 ? 1.4331 1.1059 1.1927 -0.2041 -0.0976 0.1719  283 GLU B OE2 
4267 N N   . LYS B 277 ? 1.1028 0.8119 1.0547 -0.0990 -0.1065 0.1232  284 LYS B N   
4268 C CA  . LYS B 277 ? 1.1381 0.8284 1.1040 -0.0790 -0.1210 0.1151  284 LYS B CA  
4269 C C   . LYS B 277 ? 1.0204 0.7491 1.0357 -0.0556 -0.1094 0.0978  284 LYS B C   
4270 O O   . LYS B 277 ? 0.9606 0.6824 0.9909 -0.0342 -0.1243 0.0862  284 LYS B O   
4271 C CB  . LYS B 277 ? 1.2826 0.9611 1.2402 -0.0898 -0.1183 0.1212  284 LYS B CB  
4272 C CG  . LYS B 277 ? 1.6376 1.2725 1.5452 -0.1155 -0.1325 0.1385  284 LYS B CG  
4273 C CD  . LYS B 277 ? 1.7068 1.3368 1.6119 -0.1280 -0.1281 0.1433  284 LYS B CD  
4274 C CE  . LYS B 277 ? 1.6992 1.2844 1.5534 -0.1583 -0.1426 0.1614  284 LYS B CE  
4275 N NZ  . LYS B 277 ? 1.7649 1.3400 1.6166 -0.1697 -0.1434 0.1651  284 LYS B NZ  
4276 N N   . PHE B 278 ? 0.8535 0.6224 0.8930 -0.0605 -0.0836 0.0956  285 PHE B N   
4277 C CA  . PHE B 278 ? 0.8291 0.6310 0.9093 -0.0447 -0.0697 0.0822  285 PHE B CA  
4278 C C   . PHE B 278 ? 0.7805 0.6029 0.8840 -0.0334 -0.0695 0.0719  285 PHE B C   
4279 O O   . PHE B 278 ? 0.8462 0.6853 0.9792 -0.0185 -0.0673 0.0595  285 PHE B O   
4280 C CB  . PHE B 278 ? 0.7701 0.6001 0.8626 -0.0538 -0.0460 0.0838  285 PHE B CB  
4281 C CG  . PHE B 278 ? 0.8149 0.6668 0.9380 -0.0412 -0.0336 0.0730  285 PHE B CG  
4282 C CD1 . PHE B 278 ? 0.8587 0.7007 0.9853 -0.0325 -0.0363 0.0687  285 PHE B CD1 
4283 C CD2 . PHE B 278 ? 0.8352 0.7147 0.9802 -0.0386 -0.0203 0.0667  285 PHE B CD2 
4284 C CE1 . PHE B 278 ? 0.8321 0.6943 0.9822 -0.0229 -0.0233 0.0588  285 PHE B CE1 
4285 C CE2 . PHE B 278 ? 0.7793 0.6757 0.9472 -0.0309 -0.0085 0.0582  285 PHE B CE2 
4286 C CZ  . PHE B 278 ? 0.8383 0.7274 1.0081 -0.0236 -0.0090 0.0544  285 PHE B CZ  
4287 N N   . ARG B 279 ? 0.8182 0.6427 0.9092 -0.0418 -0.0703 0.0763  286 ARG B N   
4288 C CA  . ARG B 279 ? 0.7399 0.5845 0.8525 -0.0336 -0.0700 0.0669  286 ARG B CA  
4289 C C   . ARG B 279 ? 0.7593 0.5941 0.8839 -0.0161 -0.0915 0.0566  286 ARG B C   
4290 O O   . ARG B 279 ? 0.7526 0.6150 0.9140 -0.0049 -0.0867 0.0433  286 ARG B O   
4291 C CB  . ARG B 279 ? 0.7615 0.6074 0.8532 -0.0457 -0.0676 0.0729  286 ARG B CB  
4292 C CG  . ARG B 279 ? 0.7311 0.5936 0.8415 -0.0384 -0.0698 0.0633  286 ARG B CG  
4293 C CD  . ARG B 279 ? 0.7840 0.6455 0.8685 -0.0497 -0.0672 0.0685  286 ARG B CD  
4294 N NE  . ARG B 279 ? 0.7310 0.6141 0.8173 -0.0590 -0.0450 0.0703  286 ARG B NE  
4295 C CZ  . ARG B 279 ? 0.7531 0.6604 0.8641 -0.0553 -0.0319 0.0624  286 ARG B CZ  
4296 N NH1 . ARG B 279 ? 0.8332 0.7494 0.9706 -0.0462 -0.0354 0.0529  286 ARG B NH1 
4297 N NH2 . ARG B 279 ? 0.8244 0.7468 0.9334 -0.0613 -0.0160 0.0632  286 ARG B NH2 
4298 N N   . PRO B 280 ? 0.8537 0.6496 0.9475 -0.0140 -0.1162 0.0618  287 PRO B N   
4299 C CA  . PRO B 280 ? 0.8104 0.5969 0.9183 0.0072  -0.1399 0.0488  287 PRO B CA  
4300 C C   . PRO B 280 ? 0.7547 0.5559 0.8934 0.0234  -0.1369 0.0357  287 PRO B C   
4301 O O   . PRO B 280 ? 0.8527 0.6740 1.0243 0.0418  -0.1450 0.0185  287 PRO B O   
4302 C CB  . PRO B 280 ? 0.9355 0.6669 0.9936 0.0040  -0.1685 0.0597  287 PRO B CB  
4303 C CG  . PRO B 280 ? 0.9274 0.6425 0.9504 -0.0201 -0.1559 0.0779  287 PRO B CG  
4304 C CD  . PRO B 280 ? 0.8710 0.6299 0.9149 -0.0311 -0.1255 0.0783  287 PRO B CD  
4305 N N   . PHE B 281 ? 0.7627 0.5578 0.8923 0.0166  -0.1249 0.0421  288 PHE B N   
4306 C CA  . PHE B 281 ? 0.7904 0.6012 0.9458 0.0306  -0.1182 0.0295  288 PHE B CA  
4307 C C   . PHE B 281 ? 0.7920 0.6538 0.9894 0.0317  -0.0931 0.0188  288 PHE B C   
4308 O O   . PHE B 281 ? 0.8973 0.7837 1.1264 0.0472  -0.0925 0.0016  288 PHE B O   
4309 C CB  . PHE B 281 ? 0.7647 0.5543 0.8972 0.0215  -0.1123 0.0395  288 PHE B CB  
4310 C CG  . PHE B 281 ? 0.6877 0.4938 0.8426 0.0349  -0.1031 0.0266  288 PHE B CG  
4311 C CD1 . PHE B 281 ? 0.7703 0.5595 0.9268 0.0561  -0.1232 0.0134  288 PHE B CD1 
4312 C CD2 . PHE B 281 ? 0.7309 0.5673 0.9022 0.0273  -0.0754 0.0265  288 PHE B CD2 
4313 C CE1 . PHE B 281 ? 0.8131 0.6195 0.9881 0.0692  -0.1134 -0.0005 288 PHE B CE1 
4314 C CE2 . PHE B 281 ? 0.7140 0.5644 0.9008 0.0383  -0.0660 0.0147  288 PHE B CE2 
4315 C CZ  . PHE B 281 ? 0.8378 0.6756 1.0271 0.0591  -0.0836 0.0007  288 PHE B CZ  
4316 N N   . TYR B 282 ? 0.7271 0.6039 0.9230 0.0146  -0.0732 0.0282  289 TYR B N   
4317 C CA  . TYR B 282 ? 0.6909 0.6071 0.9187 0.0116  -0.0519 0.0208  289 TYR B CA  
4318 C C   . TYR B 282 ? 0.6292 0.5686 0.8873 0.0213  -0.0603 0.0066  289 TYR B C   
4319 O O   . TYR B 282 ? 0.6212 0.5936 0.9124 0.0257  -0.0489 -0.0064 289 TYR B O   
4320 C CB  . TYR B 282 ? 0.6556 0.5759 0.8719 -0.0056 -0.0363 0.0322  289 TYR B CB  
4321 C CG  . TYR B 282 ? 0.6069 0.5580 0.8503 -0.0095 -0.0204 0.0253  289 TYR B CG  
4322 C CD1 . TYR B 282 ? 0.5734 0.5420 0.8328 -0.0105 -0.0033 0.0202  289 TYR B CD1 
4323 C CD2 . TYR B 282 ? 0.7649 0.7243 1.0149 -0.0131 -0.0244 0.0234  289 TYR B CD2 
4324 C CE1 . TYR B 282 ? 0.7449 0.7368 1.0246 -0.0176 0.0100  0.0150  289 TYR B CE1 
4325 C CE2 . TYR B 282 ? 0.8079 0.7909 1.0808 -0.0188 -0.0123 0.0173  289 TYR B CE2 
4326 C CZ  . TYR B 282 ? 0.7821 0.7805 1.0692 -0.0223 0.0049  0.0138  289 TYR B CZ  
4327 O OH  . TYR B 282 ? 0.7871 0.8039 1.0917 -0.0319 0.0160  0.0094  289 TYR B OH  
4328 N N   . LEU B 283 ? 0.6846 0.6077 0.9303 0.0231  -0.0800 0.0088  290 LEU B N   
4329 C CA  . LEU B 283 ? 0.7652 0.7105 1.0400 0.0315  -0.0906 -0.0049 290 LEU B CA  
4330 C C   . LEU B 283 ? 0.7857 0.7422 1.0871 0.0535  -0.1071 -0.0236 290 LEU B C   
4331 O O   . LEU B 283 ? 0.9874 0.9859 1.3313 0.0588  -0.1001 -0.0402 290 LEU B O   
4332 C CB  . LEU B 283 ? 0.8097 0.7322 1.0595 0.0270  -0.1078 0.0028  290 LEU B CB  
4333 C CG  . LEU B 283 ? 0.7941 0.7139 1.0230 0.0082  -0.0924 0.0160  290 LEU B CG  
4334 C CD1 . LEU B 283 ? 0.8285 0.7222 1.0260 0.0056  -0.1114 0.0223  290 LEU B CD1 
4335 C CD2 . LEU B 283 ? 0.6520 0.6064 0.9113 0.0011  -0.0732 0.0097  290 LEU B CD2 
4336 N N   . SER B 284 ? 0.7542 0.6742 1.0307 0.0657  -0.1290 -0.0221 291 SER B N   
4337 C CA  . SER B 284 ? 0.8460 0.7720 1.1449 0.0914  -0.1487 -0.0425 291 SER B CA  
4338 C C   . SER B 284 ? 0.8664 0.8263 1.1948 0.0989  -0.1291 -0.0564 291 SER B C   
4339 O O   . SER B 284 ? 1.0397 1.0393 1.4102 0.1150  -0.1308 -0.0793 291 SER B O   
4340 C CB  . SER B 284 ? 0.8025 0.6696 1.0593 0.1026  -0.1821 -0.0366 291 SER B CB  
4341 O OG  . SER B 284 ? 0.8461 0.6777 1.0627 0.0886  -0.1749 -0.0180 291 SER B OG  
4342 N N   . GLN B 285 ? 0.9715 0.9183 1.2782 0.0872  -0.1106 -0.0439 292 GLN B N   
4343 C CA  . GLN B 285 ? 0.9312 0.9000 1.2544 0.0947  -0.0940 -0.0556 292 GLN B CA  
4344 C C   . GLN B 285 ? 0.9491 0.9611 1.2952 0.0787  -0.0589 -0.0564 292 GLN B C   
4345 O O   . GLN B 285 ? 0.9014 0.9503 1.2761 0.0865  -0.0457 -0.0739 292 GLN B O   
4346 C CB  . GLN B 285 ? 0.9159 0.8400 1.1993 0.0942  -0.0990 -0.0439 292 GLN B CB  
4347 C CG  . GLN B 285 ? 0.9456 0.8143 1.1937 0.1037  -0.1337 -0.0379 292 GLN B CG  
4348 C CD  . GLN B 285 ? 0.9487 0.8186 1.2156 0.1316  -0.1624 -0.0594 292 GLN B CD  
4349 O OE1 . GLN B 285 ? 0.9754 0.8803 1.2768 0.1508  -0.1584 -0.0826 292 GLN B OE1 
4350 N NE2 . GLN B 285 ? 0.9655 0.7979 1.2090 0.1346  -0.1919 -0.0531 292 GLN B NE2 
4351 N N   . LEU B 286 ? 0.9224 0.9281 1.2533 0.0567  -0.0445 -0.0386 293 LEU B N   
4352 C CA  . LEU B 286 ? 0.8596 0.8895 1.1981 0.0397  -0.0143 -0.0350 293 LEU B CA  
4353 C C   . LEU B 286 ? 0.8251 0.8875 1.1895 0.0266  -0.0026 -0.0380 293 LEU B C   
4354 O O   . LEU B 286 ? 0.8223 0.9123 1.2019 0.0165  0.0194  -0.0426 293 LEU B O   
4355 C CB  . LEU B 286 ? 0.7414 0.7394 1.0432 0.0257  -0.0064 -0.0147 293 LEU B CB  
4356 C CG  . LEU B 286 ? 0.7193 0.6815 0.9915 0.0324  -0.0173 -0.0083 293 LEU B CG  
4357 C CD1 . LEU B 286 ? 0.6534 0.5977 0.8992 0.0166  -0.0055 0.0085  293 LEU B CD1 
4358 C CD2 . LEU B 286 ? 0.7583 0.7282 1.0395 0.0482  -0.0165 -0.0233 293 LEU B CD2 
4359 N N   . GLU B 287 ? 0.8071 0.8636 1.1728 0.0251  -0.0174 -0.0350 294 GLU B N   
4360 C CA  . GLU B 287 ? 0.9356 1.0171 1.3222 0.0112  -0.0088 -0.0369 294 GLU B CA  
4361 C C   . GLU B 287 ? 1.0638 1.1942 1.4976 0.0159  -0.0055 -0.0584 294 GLU B C   
4362 O O   . GLU B 287 ? 1.0070 1.1666 1.4573 0.0038  0.0172  -0.0633 294 GLU B O   
4363 C CB  . GLU B 287 ? 0.9472 1.0079 1.3194 0.0086  -0.0261 -0.0289 294 GLU B CB  
4364 C CG  . GLU B 287 ? 0.8723 0.9490 1.2569 -0.0078 -0.0170 -0.0282 294 GLU B CG  
4365 C CD  . GLU B 287 ? 0.9826 1.0336 1.3430 -0.0115 -0.0301 -0.0184 294 GLU B CD  
4366 O OE1 . GLU B 287 ? 0.9503 0.9939 1.3104 -0.0011 -0.0522 -0.0227 294 GLU B OE1 
4367 O OE2 . GLU B 287 ? 1.0489 1.0866 1.3892 -0.0241 -0.0192 -0.0077 294 GLU B OE2 
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