data_9N9L
# 
_entry.id   9N9L 
# 
_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   9N9L         pdb_00009n9l 10.2210/pdb9n9l/pdb 
WWPDB D_1000292793 ?            ?                   
# 
loop_
_pdbx_audit_revision_history.ordinal 
_pdbx_audit_revision_history.data_content_type 
_pdbx_audit_revision_history.major_revision 
_pdbx_audit_revision_history.minor_revision 
_pdbx_audit_revision_history.revision_date 
_pdbx_audit_revision_history.part_number 
1 'Structure model' 1 0 2025-04-30 ? 
2 'Structure model' 1 1 2025-05-07 ? 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
_pdbx_audit_revision_group.ordinal             1 
_pdbx_audit_revision_group.revision_ordinal    2 
_pdbx_audit_revision_group.data_content_type   'Structure model' 
_pdbx_audit_revision_group.group               'Database references' 
# 
loop_
_pdbx_audit_revision_category.ordinal 
_pdbx_audit_revision_category.revision_ordinal 
_pdbx_audit_revision_category.data_content_type 
_pdbx_audit_revision_category.category 
1 2 'Structure model' citation        
2 2 'Structure model' citation_author 
# 
loop_
_pdbx_audit_revision_item.ordinal 
_pdbx_audit_revision_item.revision_ordinal 
_pdbx_audit_revision_item.data_content_type 
_pdbx_audit_revision_item.item 
1 2 'Structure model' '_citation.journal_volume'          
2 2 'Structure model' '_citation.page_first'              
3 2 'Structure model' '_citation.page_last'               
4 2 'Structure model' '_citation_author.identifier_ORCID' 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        9N9L 
_pdbx_database_status.recvd_initial_deposition_date   2025-02-11 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           N 
# 
_pdbx_contact_author.id                 3 
_pdbx_contact_author.email              John@spurlino.com 
_pdbx_contact_author.name_first         John 
_pdbx_contact_author.name_last          Spurlino 
_pdbx_contact_author.name_mi            C 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0003-1308-2570 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Spurlino, J.C.' 1 0000-0003-1308-2570 
'Milligan, C.'   2 ?                   
# 
_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            J.Med.Chem. 
_citation.journal_id_ASTM           JMCMAR 
_citation.journal_id_CSD            0151 
_citation.journal_id_ISSN           0022-2623 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            68 
_citation.language                  ? 
_citation.page_first                8713 
_citation.page_last                 8728 
_citation.title                     'Identification of JNJ-61803534, a ROR gamma t Inverse Agonist for the Treatment of Psoriasis.' 
_citation.year                      2025 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1021/acs.jmedchem.5c00390 
_citation.pdbx_database_id_PubMed   40237323 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Kinzel, O.'     1  ? 
primary 'Goldberg, S.D.' 2  ? 
primary 'Cummings, M.D.' 3  ? 
primary 'Gege, C.'       4  ? 
primary 'Steeneck, C.'   5  ? 
primary 'Xue, X.'        6  ? 
primary 'Albers, M.'     7  ? 
primary 'Schluter, T.'   8  ? 
primary 'Kleymann, G.'   9  ? 
primary 'Scott, B.'      10 ? 
primary 'Sepassi, K.'    11 ? 
primary 'Schoetens, F.'  12 ? 
primary 'Venkatesan, H.' 13 ? 
primary 'Tanis, V.M.'    14 ? 
primary 'Coe, K.'        15 ? 
primary 'Sales, Z.S.'    16 ? 
primary 'Spurlino, J.'   17 ? 
primary 'Milligan, C.'   18 ? 
primary 'Fourie, A.M.'   19 ? 
primary 'Edwards, J.P.'  20 ? 
primary 'Hoffmann, T.'   21 ? 
# 
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 'Nuclear receptor ROR-gamma' 28307.824 2   ? ? ? ? 
2 non-polymer syn 
;(5P)-5-[2,3-dichloro-4-(1,1,1,3,3,3-hexafluoro-2-hydroxypropan-2-yl)phenyl]-N-(2-hydroxy-2-methylpropyl)-4-[(2S)-2-methylpyrrolidine-1-carbonyl]-1,3-thiazole-2-carboxamide
;
622.408   2   ? ? ? ? 
3 water       nat water 18.015    156 ? ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        
;Nuclear receptor RZR-gamma,Nuclear receptor subfamily 1 group F member 3,RAR-related orphan receptor C,Retinoid-related orphan receptor-gamma
;
# 
_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       
;ASLTEIEHLVQSVCKSYRETCQLRLEDLLRQRSNIFSREEVTGYQRKSMWEMWERCAHHLTEAIQYVVEFAKRLSGFMEL
CQNDQIVLLKAGAMEVVLVRMCRAYNADNRTVFFEGKYGGMELFRALGCSELISSIFDFSHSLSALHFSEDEIALYTALV
LINAHRPGLQEKRKVEQLQYNLELAFHHHLCKTHRQSILAKLPPKGKLRSLCSQHVERLQIFQHLHPIVVQAAFPPLYKE
LFS
;
_entity_poly.pdbx_seq_one_letter_code_can   
;ASLTEIEHLVQSVCKSYRETCQLRLEDLLRQRSNIFSREEVTGYQRKSMWEMWERCAHHLTEAIQYVVEFAKRLSGFMEL
CQNDQIVLLKAGAMEVVLVRMCRAYNADNRTVFFEGKYGGMELFRALGCSELISSIFDFSHSLSALHFSEDEIALYTALV
LINAHRPGLQEKRKVEQLQYNLELAFHHHLCKTHRQSILAKLPPKGKLRSLCSQHVERLQIFQHLHPIVVQAAFPPLYKE
LFS
;
_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 
;(5P)-5-[2,3-dichloro-4-(1,1,1,3,3,3-hexafluoro-2-hydroxypropan-2-yl)phenyl]-N-(2-hydroxy-2-methylpropyl)-4-[(2S)-2-methylpyrrolidine-1-carbonyl]-1,3-thiazole-2-carboxamide
;
A1BW2 
3 water HOH   
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   ALA n 
1 2   SER n 
1 3   LEU n 
1 4   THR n 
1 5   GLU n 
1 6   ILE n 
1 7   GLU n 
1 8   HIS n 
1 9   LEU n 
1 10  VAL n 
1 11  GLN n 
1 12  SER n 
1 13  VAL n 
1 14  CYS n 
1 15  LYS n 
1 16  SER n 
1 17  TYR n 
1 18  ARG n 
1 19  GLU n 
1 20  THR n 
1 21  CYS n 
1 22  GLN n 
1 23  LEU n 
1 24  ARG n 
1 25  LEU n 
1 26  GLU n 
1 27  ASP n 
1 28  LEU n 
1 29  LEU n 
1 30  ARG n 
1 31  GLN n 
1 32  ARG n 
1 33  SER n 
1 34  ASN n 
1 35  ILE n 
1 36  PHE n 
1 37  SER n 
1 38  ARG n 
1 39  GLU n 
1 40  GLU n 
1 41  VAL n 
1 42  THR n 
1 43  GLY n 
1 44  TYR n 
1 45  GLN n 
1 46  ARG n 
1 47  LYS n 
1 48  SER n 
1 49  MET n 
1 50  TRP n 
1 51  GLU n 
1 52  MET n 
1 53  TRP n 
1 54  GLU n 
1 55  ARG n 
1 56  CYS n 
1 57  ALA n 
1 58  HIS n 
1 59  HIS n 
1 60  LEU n 
1 61  THR n 
1 62  GLU n 
1 63  ALA n 
1 64  ILE n 
1 65  GLN n 
1 66  TYR n 
1 67  VAL n 
1 68  VAL n 
1 69  GLU n 
1 70  PHE n 
1 71  ALA n 
1 72  LYS n 
1 73  ARG n 
1 74  LEU n 
1 75  SER n 
1 76  GLY n 
1 77  PHE n 
1 78  MET n 
1 79  GLU n 
1 80  LEU n 
1 81  CYS n 
1 82  GLN n 
1 83  ASN n 
1 84  ASP n 
1 85  GLN n 
1 86  ILE n 
1 87  VAL n 
1 88  LEU n 
1 89  LEU n 
1 90  LYS n 
1 91  ALA n 
1 92  GLY n 
1 93  ALA n 
1 94  MET n 
1 95  GLU n 
1 96  VAL n 
1 97  VAL n 
1 98  LEU n 
1 99  VAL n 
1 100 ARG n 
1 101 MET n 
1 102 CYS n 
1 103 ARG n 
1 104 ALA n 
1 105 TYR n 
1 106 ASN n 
1 107 ALA n 
1 108 ASP n 
1 109 ASN n 
1 110 ARG n 
1 111 THR n 
1 112 VAL n 
1 113 PHE n 
1 114 PHE n 
1 115 GLU n 
1 116 GLY n 
1 117 LYS n 
1 118 TYR n 
1 119 GLY n 
1 120 GLY n 
1 121 MET n 
1 122 GLU n 
1 123 LEU n 
1 124 PHE n 
1 125 ARG n 
1 126 ALA n 
1 127 LEU n 
1 128 GLY n 
1 129 CYS n 
1 130 SER n 
1 131 GLU n 
1 132 LEU n 
1 133 ILE n 
1 134 SER n 
1 135 SER n 
1 136 ILE n 
1 137 PHE n 
1 138 ASP n 
1 139 PHE n 
1 140 SER n 
1 141 HIS n 
1 142 SER n 
1 143 LEU n 
1 144 SER n 
1 145 ALA n 
1 146 LEU n 
1 147 HIS n 
1 148 PHE n 
1 149 SER n 
1 150 GLU n 
1 151 ASP n 
1 152 GLU n 
1 153 ILE n 
1 154 ALA n 
1 155 LEU n 
1 156 TYR n 
1 157 THR n 
1 158 ALA n 
1 159 LEU n 
1 160 VAL n 
1 161 LEU n 
1 162 ILE n 
1 163 ASN n 
1 164 ALA n 
1 165 HIS n 
1 166 ARG n 
1 167 PRO n 
1 168 GLY n 
1 169 LEU n 
1 170 GLN n 
1 171 GLU n 
1 172 LYS n 
1 173 ARG n 
1 174 LYS n 
1 175 VAL n 
1 176 GLU n 
1 177 GLN n 
1 178 LEU n 
1 179 GLN n 
1 180 TYR n 
1 181 ASN n 
1 182 LEU n 
1 183 GLU n 
1 184 LEU n 
1 185 ALA n 
1 186 PHE n 
1 187 HIS n 
1 188 HIS n 
1 189 HIS n 
1 190 LEU n 
1 191 CYS n 
1 192 LYS n 
1 193 THR n 
1 194 HIS n 
1 195 ARG n 
1 196 GLN n 
1 197 SER n 
1 198 ILE n 
1 199 LEU n 
1 200 ALA n 
1 201 LYS n 
1 202 LEU n 
1 203 PRO n 
1 204 PRO n 
1 205 LYS n 
1 206 GLY n 
1 207 LYS n 
1 208 LEU n 
1 209 ARG n 
1 210 SER n 
1 211 LEU n 
1 212 CYS n 
1 213 SER n 
1 214 GLN n 
1 215 HIS n 
1 216 VAL n 
1 217 GLU n 
1 218 ARG n 
1 219 LEU n 
1 220 GLN n 
1 221 ILE n 
1 222 PHE n 
1 223 GLN n 
1 224 HIS n 
1 225 LEU n 
1 226 HIS n 
1 227 PRO n 
1 228 ILE n 
1 229 VAL n 
1 230 VAL n 
1 231 GLN n 
1 232 ALA n 
1 233 ALA n 
1 234 PHE n 
1 235 PRO n 
1 236 PRO n 
1 237 LEU n 
1 238 TYR n 
1 239 LYS n 
1 240 GLU n 
1 241 LEU n 
1 242 PHE n 
1 243 SER 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                   243 
_entity_src_gen.gene_src_common_name               human 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 'RORC, NR1F3, RORG, RZRG' 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    ? 
_entity_src_gen.gene_src_tissue                    ? 
_entity_src_gen.gene_src_tissue_fraction           ? 
_entity_src_gen.gene_src_details                   ? 
_entity_src_gen.pdbx_gene_src_fragment             ? 
_entity_src_gen.pdbx_gene_src_scientific_name      'Homo sapiens' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     9606 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     562 
_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 
A1BW2 non-polymer         . 
;(5P)-5-[2,3-dichloro-4-(1,1,1,3,3,3-hexafluoro-2-hydroxypropan-2-yl)phenyl]-N-(2-hydroxy-2-methylpropyl)-4-[(2S)-2-methylpyrrolidine-1-carbonyl]-1,3-thiazole-2-carboxamide
;
? 'C23 H23 Cl2 F6 N3 O4 S' 622.408 
ALA   'L-peptide linking' y ALANINE ? 'C3 H7 N O2'             89.093  
ARG   'L-peptide linking' y ARGININE ? 'C6 H15 N4 O2 1'         175.209 
ASN   'L-peptide linking' y ASPARAGINE ? 'C4 H8 N2 O3'            132.118 
ASP   'L-peptide linking' y 'ASPARTIC ACID' ? 'C4 H7 N O4'             133.103 
CYS   'L-peptide linking' y CYSTEINE ? 'C3 H7 N O2 S'           121.158 
GLN   'L-peptide linking' y GLUTAMINE ? 'C5 H10 N2 O3'           146.144 
GLU   'L-peptide linking' y 'GLUTAMIC ACID' ? 'C5 H9 N O4'             147.129 
GLY   'peptide linking'   y GLYCINE ? 'C2 H5 N O2'             75.067  
HIS   'L-peptide linking' y HISTIDINE ? 'C6 H10 N3 O2 1'         156.162 
HOH   non-polymer         . WATER ? 'H2 O'                   18.015  
ILE   'L-peptide linking' y ISOLEUCINE ? 'C6 H13 N O2'            131.173 
LEU   'L-peptide linking' y LEUCINE ? 'C6 H13 N O2'            131.173 
LYS   'L-peptide linking' y LYSINE ? 'C6 H15 N2 O2 1'         147.195 
MET   'L-peptide linking' y METHIONINE ? 'C5 H11 N O2 S'          149.211 
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   ALA 1   265 265 ALA ALA A . n 
A 1 2   SER 2   266 266 SER SER A . n 
A 1 3   LEU 3   267 267 LEU LEU A . n 
A 1 4   THR 4   268 268 THR THR A . n 
A 1 5   GLU 5   269 269 GLU GLU A . n 
A 1 6   ILE 6   270 270 ILE ILE A . n 
A 1 7   GLU 7   271 271 GLU GLU A . n 
A 1 8   HIS 8   272 272 HIS HIS A . n 
A 1 9   LEU 9   273 273 LEU LEU A . n 
A 1 10  VAL 10  274 274 VAL VAL A . n 
A 1 11  GLN 11  275 275 GLN GLN A . n 
A 1 12  SER 12  276 276 SER SER A . n 
A 1 13  VAL 13  277 277 VAL VAL A . n 
A 1 14  CYS 14  278 278 CYS CYS A . n 
A 1 15  LYS 15  279 279 LYS LYS A . n 
A 1 16  SER 16  280 280 SER SER A . n 
A 1 17  TYR 17  281 281 TYR TYR A . n 
A 1 18  ARG 18  282 282 ARG ARG A . n 
A 1 19  GLU 19  283 283 GLU GLU A . n 
A 1 20  THR 20  284 284 THR THR A . n 
A 1 21  CYS 21  285 285 CYS CYS A . n 
A 1 22  GLN 22  286 286 GLN GLN A . n 
A 1 23  LEU 23  287 287 LEU LEU A . n 
A 1 24  ARG 24  288 288 ARG ARG A . n 
A 1 25  LEU 25  289 289 LEU LEU A . n 
A 1 26  GLU 26  290 290 GLU GLU A . n 
A 1 27  ASP 27  291 291 ASP ASP A . n 
A 1 28  LEU 28  292 292 LEU LEU A . n 
A 1 29  LEU 29  293 293 LEU LEU A . n 
A 1 30  ARG 30  294 294 ARG ARG A . n 
A 1 31  GLN 31  295 295 GLN GLN A . n 
A 1 32  ARG 32  296 296 ARG ARG A . n 
A 1 33  SER 33  297 297 SER SER A . n 
A 1 34  ASN 34  298 298 ASN ASN A . n 
A 1 35  ILE 35  299 299 ILE ILE A . n 
A 1 36  PHE 36  300 300 PHE PHE A . n 
A 1 37  SER 37  301 301 SER SER A . n 
A 1 38  ARG 38  302 302 ARG ARG A . n 
A 1 39  GLU 39  303 303 GLU GLU A . n 
A 1 40  GLU 40  304 304 GLU GLU A . n 
A 1 41  VAL 41  305 305 VAL VAL A . n 
A 1 42  THR 42  306 306 THR THR A . n 
A 1 43  GLY 43  307 307 GLY GLY A . n 
A 1 44  TYR 44  308 308 TYR TYR A . n 
A 1 45  GLN 45  309 309 GLN GLN A . n 
A 1 46  ARG 46  310 310 ARG ARG A . n 
A 1 47  LYS 47  311 311 LYS LYS A . n 
A 1 48  SER 48  312 312 SER SER A . n 
A 1 49  MET 49  313 313 MET MET A . n 
A 1 50  TRP 50  314 314 TRP TRP A . n 
A 1 51  GLU 51  315 315 GLU GLU A . n 
A 1 52  MET 52  316 316 MET MET A . n 
A 1 53  TRP 53  317 317 TRP TRP A . n 
A 1 54  GLU 54  318 318 GLU GLU A . n 
A 1 55  ARG 55  319 319 ARG ARG A . n 
A 1 56  CYS 56  320 320 CYS CYS A . n 
A 1 57  ALA 57  321 321 ALA ALA A . n 
A 1 58  HIS 58  322 322 HIS HIS A . n 
A 1 59  HIS 59  323 323 HIS HIS A . n 
A 1 60  LEU 60  324 324 LEU LEU A . n 
A 1 61  THR 61  325 325 THR THR A . n 
A 1 62  GLU 62  326 326 GLU GLU A . n 
A 1 63  ALA 63  327 327 ALA ALA A . n 
A 1 64  ILE 64  328 328 ILE ILE A . n 
A 1 65  GLN 65  329 329 GLN GLN A . n 
A 1 66  TYR 66  330 330 TYR TYR A . n 
A 1 67  VAL 67  331 331 VAL VAL A . n 
A 1 68  VAL 68  332 332 VAL VAL A . n 
A 1 69  GLU 69  333 333 GLU GLU A . n 
A 1 70  PHE 70  334 334 PHE PHE A . n 
A 1 71  ALA 71  335 335 ALA ALA A . n 
A 1 72  LYS 72  336 336 LYS LYS A . n 
A 1 73  ARG 73  337 337 ARG ARG A . n 
A 1 74  LEU 74  338 338 LEU LEU A . n 
A 1 75  SER 75  339 339 SER SER A . n 
A 1 76  GLY 76  340 340 GLY GLY A . n 
A 1 77  PHE 77  341 341 PHE PHE A . n 
A 1 78  MET 78  342 342 MET MET A . n 
A 1 79  GLU 79  343 343 GLU GLU A . n 
A 1 80  LEU 80  344 344 LEU LEU A . n 
A 1 81  CYS 81  345 345 CYS CYS A . n 
A 1 82  GLN 82  346 346 GLN GLN A . n 
A 1 83  ASN 83  347 347 ASN ASN A . n 
A 1 84  ASP 84  348 348 ASP ASP A . n 
A 1 85  GLN 85  349 349 GLN GLN A . n 
A 1 86  ILE 86  350 350 ILE ILE A . n 
A 1 87  VAL 87  351 351 VAL VAL A . n 
A 1 88  LEU 88  352 352 LEU LEU A . n 
A 1 89  LEU 89  353 353 LEU LEU A . n 
A 1 90  LYS 90  354 354 LYS LYS A . n 
A 1 91  ALA 91  355 355 ALA ALA A . n 
A 1 92  GLY 92  356 356 GLY GLY A . n 
A 1 93  ALA 93  357 357 ALA ALA A . n 
A 1 94  MET 94  358 358 MET MET A . n 
A 1 95  GLU 95  359 359 GLU GLU A . n 
A 1 96  VAL 96  360 360 VAL VAL A . n 
A 1 97  VAL 97  361 361 VAL VAL A . n 
A 1 98  LEU 98  362 362 LEU LEU A . n 
A 1 99  VAL 99  363 363 VAL VAL A . n 
A 1 100 ARG 100 364 364 ARG ARG A . n 
A 1 101 MET 101 365 365 MET MET A . n 
A 1 102 CYS 102 366 366 CYS CYS A . n 
A 1 103 ARG 103 367 367 ARG ARG A . n 
A 1 104 ALA 104 368 368 ALA ALA A . n 
A 1 105 TYR 105 369 369 TYR TYR A . n 
A 1 106 ASN 106 370 370 ASN ASN A . n 
A 1 107 ALA 107 371 371 ALA ALA A . n 
A 1 108 ASP 108 372 372 ASP ASP A . n 
A 1 109 ASN 109 373 373 ASN ASN A . n 
A 1 110 ARG 110 374 374 ARG ARG A . n 
A 1 111 THR 111 375 375 THR THR A . n 
A 1 112 VAL 112 376 376 VAL VAL A . n 
A 1 113 PHE 113 377 377 PHE PHE A . n 
A 1 114 PHE 114 378 378 PHE PHE A . n 
A 1 115 GLU 115 379 379 GLU GLU A . n 
A 1 116 GLY 116 380 380 GLY GLY A . n 
A 1 117 LYS 117 381 381 LYS LYS A . n 
A 1 118 TYR 118 382 382 TYR TYR A . n 
A 1 119 GLY 119 383 383 GLY GLY A . n 
A 1 120 GLY 120 384 384 GLY GLY A . n 
A 1 121 MET 121 385 385 MET MET A . n 
A 1 122 GLU 122 386 386 GLU GLU A . n 
A 1 123 LEU 123 387 387 LEU LEU A . n 
A 1 124 PHE 124 388 388 PHE PHE A . n 
A 1 125 ARG 125 389 389 ARG ARG A . n 
A 1 126 ALA 126 390 390 ALA ALA A . n 
A 1 127 LEU 127 391 391 LEU LEU A . n 
A 1 128 GLY 128 392 392 GLY GLY A . n 
A 1 129 CYS 129 393 393 CYS CYS A . n 
A 1 130 SER 130 394 394 SER SER A . n 
A 1 131 GLU 131 395 395 GLU GLU A . n 
A 1 132 LEU 132 396 396 LEU LEU A . n 
A 1 133 ILE 133 397 397 ILE ILE A . n 
A 1 134 SER 134 398 398 SER SER A . n 
A 1 135 SER 135 399 399 SER SER A . n 
A 1 136 ILE 136 400 400 ILE ILE A . n 
A 1 137 PHE 137 401 401 PHE PHE A . n 
A 1 138 ASP 138 402 402 ASP ASP A . n 
A 1 139 PHE 139 403 403 PHE PHE A . n 
A 1 140 SER 140 404 404 SER SER A . n 
A 1 141 HIS 141 405 405 HIS HIS A . n 
A 1 142 SER 142 406 406 SER SER A . n 
A 1 143 LEU 143 407 407 LEU LEU A . n 
A 1 144 SER 144 408 408 SER SER A . n 
A 1 145 ALA 145 409 409 ALA ALA A . n 
A 1 146 LEU 146 410 410 LEU LEU A . n 
A 1 147 HIS 147 411 411 HIS HIS A . n 
A 1 148 PHE 148 412 412 PHE PHE A . n 
A 1 149 SER 149 413 413 SER SER A . n 
A 1 150 GLU 150 414 414 GLU GLU A . n 
A 1 151 ASP 151 415 415 ASP ASP A . n 
A 1 152 GLU 152 416 416 GLU GLU A . n 
A 1 153 ILE 153 417 417 ILE ILE A . n 
A 1 154 ALA 154 418 418 ALA ALA A . n 
A 1 155 LEU 155 419 419 LEU LEU A . n 
A 1 156 TYR 156 420 420 TYR TYR A . n 
A 1 157 THR 157 421 421 THR THR A . n 
A 1 158 ALA 158 422 422 ALA ALA A . n 
A 1 159 LEU 159 423 423 LEU LEU A . n 
A 1 160 VAL 160 424 424 VAL VAL A . n 
A 1 161 LEU 161 425 425 LEU LEU A . n 
A 1 162 ILE 162 426 426 ILE ILE A . n 
A 1 163 ASN 163 427 427 ASN ASN A . n 
A 1 164 ALA 164 428 428 ALA ALA A . n 
A 1 165 HIS 165 429 429 HIS HIS A . n 
A 1 166 ARG 166 430 430 ARG ARG A . n 
A 1 167 PRO 167 431 431 PRO PRO A . n 
A 1 168 GLY 168 432 432 GLY GLY A . n 
A 1 169 LEU 169 433 433 LEU LEU A . n 
A 1 170 GLN 170 434 434 GLN GLN A . n 
A 1 171 GLU 171 435 435 GLU GLU A . n 
A 1 172 LYS 172 436 436 LYS LYS A . n 
A 1 173 ARG 173 437 437 ARG ARG A . n 
A 1 174 LYS 174 438 438 LYS LYS A . n 
A 1 175 VAL 175 439 439 VAL VAL A . n 
A 1 176 GLU 176 440 440 GLU GLU A . n 
A 1 177 GLN 177 441 441 GLN GLN A . n 
A 1 178 LEU 178 442 442 LEU LEU A . n 
A 1 179 GLN 179 443 443 GLN GLN A . n 
A 1 180 TYR 180 444 444 TYR TYR A . n 
A 1 181 ASN 181 445 445 ASN ASN A . n 
A 1 182 LEU 182 446 446 LEU LEU A . n 
A 1 183 GLU 183 447 447 GLU GLU A . n 
A 1 184 LEU 184 448 448 LEU LEU A . n 
A 1 185 ALA 185 449 449 ALA ALA A . n 
A 1 186 PHE 186 450 450 PHE PHE A . n 
A 1 187 HIS 187 451 451 HIS HIS A . n 
A 1 188 HIS 188 452 452 HIS HIS A . n 
A 1 189 HIS 189 453 453 HIS HIS A . n 
A 1 190 LEU 190 454 454 LEU LEU A . n 
A 1 191 CYS 191 455 455 CYS CYS A . n 
A 1 192 LYS 192 456 456 LYS LYS A . n 
A 1 193 THR 193 457 457 THR THR A . n 
A 1 194 HIS 194 458 458 HIS HIS A . n 
A 1 195 ARG 195 459 459 ARG ARG A . n 
A 1 196 GLN 196 460 460 GLN GLN A . n 
A 1 197 SER 197 461 461 SER SER A . n 
A 1 198 ILE 198 462 462 ILE ILE A . n 
A 1 199 LEU 199 463 463 LEU LEU A . n 
A 1 200 ALA 200 464 464 ALA ALA A . n 
A 1 201 LYS 201 465 465 LYS LYS A . n 
A 1 202 LEU 202 466 466 LEU LEU A . n 
A 1 203 PRO 203 467 467 PRO PRO A . n 
A 1 204 PRO 204 468 468 PRO PRO A . n 
A 1 205 LYS 205 469 469 LYS LYS A . n 
A 1 206 GLY 206 470 470 GLY GLY A . n 
A 1 207 LYS 207 471 471 LYS LYS A . n 
A 1 208 LEU 208 472 472 LEU LEU A . n 
A 1 209 ARG 209 473 473 ARG ARG A . n 
A 1 210 SER 210 474 474 SER SER A . n 
A 1 211 LEU 211 475 475 LEU LEU A . n 
A 1 212 CYS 212 476 476 CYS CYS A . n 
A 1 213 SER 213 477 477 SER SER A . n 
A 1 214 GLN 214 478 478 GLN GLN A . n 
A 1 215 HIS 215 479 479 HIS HIS A . n 
A 1 216 VAL 216 480 480 VAL VAL A . n 
A 1 217 GLU 217 481 481 GLU GLU A . n 
A 1 218 ARG 218 482 482 ARG ARG A . n 
A 1 219 LEU 219 483 483 LEU LEU A . n 
A 1 220 GLN 220 484 484 GLN GLN A . n 
A 1 221 ILE 221 485 485 ILE ILE A . n 
A 1 222 PHE 222 486 486 PHE PHE A . n 
A 1 223 GLN 223 487 487 GLN GLN A . n 
A 1 224 HIS 224 488 488 HIS HIS A . n 
A 1 225 LEU 225 489 489 LEU LEU A . n 
A 1 226 HIS 226 490 490 HIS HIS A . n 
A 1 227 PRO 227 491 491 PRO PRO A . n 
A 1 228 ILE 228 492 492 ILE ILE A . n 
A 1 229 VAL 229 493 ?   ?   ?   A . n 
A 1 230 VAL 230 494 ?   ?   ?   A . n 
A 1 231 GLN 231 495 ?   ?   ?   A . n 
A 1 232 ALA 232 496 ?   ?   ?   A . n 
A 1 233 ALA 233 497 ?   ?   ?   A . n 
A 1 234 PHE 234 498 ?   ?   ?   A . n 
A 1 235 PRO 235 499 ?   ?   ?   A . n 
A 1 236 PRO 236 500 ?   ?   ?   A . n 
A 1 237 LEU 237 501 ?   ?   ?   A . n 
A 1 238 TYR 238 502 ?   ?   ?   A . n 
A 1 239 LYS 239 503 ?   ?   ?   A . n 
A 1 240 GLU 240 504 ?   ?   ?   A . n 
A 1 241 LEU 241 505 ?   ?   ?   A . n 
A 1 242 PHE 242 506 ?   ?   ?   A . n 
A 1 243 SER 243 507 ?   ?   ?   A . n 
B 1 1   ALA 1   265 265 ALA ALA B . n 
B 1 2   SER 2   266 266 SER SER B . n 
B 1 3   LEU 3   267 267 LEU LEU B . n 
B 1 4   THR 4   268 268 THR THR B . n 
B 1 5   GLU 5   269 269 GLU GLU B . n 
B 1 6   ILE 6   270 270 ILE ILE B . n 
B 1 7   GLU 7   271 271 GLU GLU B . n 
B 1 8   HIS 8   272 272 HIS HIS B . n 
B 1 9   LEU 9   273 273 LEU LEU B . n 
B 1 10  VAL 10  274 274 VAL VAL B . n 
B 1 11  GLN 11  275 275 GLN GLN B . n 
B 1 12  SER 12  276 276 SER SER B . n 
B 1 13  VAL 13  277 277 VAL VAL B . n 
B 1 14  CYS 14  278 278 CYS CYS B . n 
B 1 15  LYS 15  279 279 LYS LYS B . n 
B 1 16  SER 16  280 280 SER SER B . n 
B 1 17  TYR 17  281 281 TYR TYR B . n 
B 1 18  ARG 18  282 282 ARG ARG B . n 
B 1 19  GLU 19  283 283 GLU GLU B . n 
B 1 20  THR 20  284 284 THR THR B . n 
B 1 21  CYS 21  285 285 CYS CYS B . n 
B 1 22  GLN 22  286 286 GLN GLN B . n 
B 1 23  LEU 23  287 287 LEU LEU B . n 
B 1 24  ARG 24  288 288 ARG ARG B . n 
B 1 25  LEU 25  289 289 LEU LEU B . n 
B 1 26  GLU 26  290 290 GLU GLU B . n 
B 1 27  ASP 27  291 291 ASP ASP B . n 
B 1 28  LEU 28  292 292 LEU LEU B . n 
B 1 29  LEU 29  293 293 LEU LEU B . n 
B 1 30  ARG 30  294 294 ARG ARG B . n 
B 1 31  GLN 31  295 295 GLN GLN B . n 
B 1 32  ARG 32  296 296 ARG ARG B . n 
B 1 33  SER 33  297 297 SER SER B . n 
B 1 34  ASN 34  298 298 ASN ASN B . n 
B 1 35  ILE 35  299 299 ILE ILE B . n 
B 1 36  PHE 36  300 300 PHE PHE B . n 
B 1 37  SER 37  301 301 SER SER B . n 
B 1 38  ARG 38  302 302 ARG ARG B . n 
B 1 39  GLU 39  303 303 GLU GLU B . n 
B 1 40  GLU 40  304 304 GLU GLU B . n 
B 1 41  VAL 41  305 305 VAL VAL B . n 
B 1 42  THR 42  306 306 THR THR B . n 
B 1 43  GLY 43  307 307 GLY GLY B . n 
B 1 44  TYR 44  308 308 TYR TYR B . n 
B 1 45  GLN 45  309 309 GLN GLN B . n 
B 1 46  ARG 46  310 310 ARG ARG B . n 
B 1 47  LYS 47  311 311 LYS LYS B . n 
B 1 48  SER 48  312 312 SER SER B . n 
B 1 49  MET 49  313 313 MET MET B . n 
B 1 50  TRP 50  314 314 TRP TRP B . n 
B 1 51  GLU 51  315 315 GLU GLU B . n 
B 1 52  MET 52  316 316 MET MET B . n 
B 1 53  TRP 53  317 317 TRP TRP B . n 
B 1 54  GLU 54  318 318 GLU GLU B . n 
B 1 55  ARG 55  319 319 ARG ARG B . n 
B 1 56  CYS 56  320 320 CYS CYS B . n 
B 1 57  ALA 57  321 321 ALA ALA B . n 
B 1 58  HIS 58  322 322 HIS HIS B . n 
B 1 59  HIS 59  323 323 HIS HIS B . n 
B 1 60  LEU 60  324 324 LEU LEU B . n 
B 1 61  THR 61  325 325 THR THR B . n 
B 1 62  GLU 62  326 326 GLU GLU B . n 
B 1 63  ALA 63  327 327 ALA ALA B . n 
B 1 64  ILE 64  328 328 ILE ILE B . n 
B 1 65  GLN 65  329 329 GLN GLN B . n 
B 1 66  TYR 66  330 330 TYR TYR B . n 
B 1 67  VAL 67  331 331 VAL VAL B . n 
B 1 68  VAL 68  332 332 VAL VAL B . n 
B 1 69  GLU 69  333 333 GLU GLU B . n 
B 1 70  PHE 70  334 334 PHE PHE B . n 
B 1 71  ALA 71  335 335 ALA ALA B . n 
B 1 72  LYS 72  336 336 LYS LYS B . n 
B 1 73  ARG 73  337 337 ARG ARG B . n 
B 1 74  LEU 74  338 338 LEU LEU B . n 
B 1 75  SER 75  339 339 SER SER B . n 
B 1 76  GLY 76  340 340 GLY GLY B . n 
B 1 77  PHE 77  341 341 PHE PHE B . n 
B 1 78  MET 78  342 342 MET MET B . n 
B 1 79  GLU 79  343 343 GLU GLU B . n 
B 1 80  LEU 80  344 344 LEU LEU B . n 
B 1 81  CYS 81  345 345 CYS CYS B . n 
B 1 82  GLN 82  346 346 GLN GLN B . n 
B 1 83  ASN 83  347 347 ASN ASN B . n 
B 1 84  ASP 84  348 348 ASP ASP B . n 
B 1 85  GLN 85  349 349 GLN GLN B . n 
B 1 86  ILE 86  350 350 ILE ILE B . n 
B 1 87  VAL 87  351 351 VAL VAL B . n 
B 1 88  LEU 88  352 352 LEU LEU B . n 
B 1 89  LEU 89  353 353 LEU LEU B . n 
B 1 90  LYS 90  354 354 LYS LYS B . n 
B 1 91  ALA 91  355 355 ALA ALA B . n 
B 1 92  GLY 92  356 356 GLY GLY B . n 
B 1 93  ALA 93  357 357 ALA ALA B . n 
B 1 94  MET 94  358 358 MET MET B . n 
B 1 95  GLU 95  359 359 GLU GLU B . n 
B 1 96  VAL 96  360 360 VAL VAL B . n 
B 1 97  VAL 97  361 361 VAL VAL B . n 
B 1 98  LEU 98  362 362 LEU LEU B . n 
B 1 99  VAL 99  363 363 VAL VAL B . n 
B 1 100 ARG 100 364 364 ARG ARG B . n 
B 1 101 MET 101 365 365 MET MET B . n 
B 1 102 CYS 102 366 366 CYS CYS B . n 
B 1 103 ARG 103 367 367 ARG ARG B . n 
B 1 104 ALA 104 368 368 ALA ALA B . n 
B 1 105 TYR 105 369 369 TYR TYR B . n 
B 1 106 ASN 106 370 370 ASN ASN B . n 
B 1 107 ALA 107 371 371 ALA ALA B . n 
B 1 108 ASP 108 372 372 ASP ASP B . n 
B 1 109 ASN 109 373 373 ASN ASN B . n 
B 1 110 ARG 110 374 374 ARG ARG B . n 
B 1 111 THR 111 375 375 THR THR B . n 
B 1 112 VAL 112 376 376 VAL VAL B . n 
B 1 113 PHE 113 377 377 PHE PHE B . n 
B 1 114 PHE 114 378 378 PHE PHE B . n 
B 1 115 GLU 115 379 379 GLU GLU B . n 
B 1 116 GLY 116 380 380 GLY GLY B . n 
B 1 117 LYS 117 381 381 LYS LYS B . n 
B 1 118 TYR 118 382 382 TYR TYR B . n 
B 1 119 GLY 119 383 383 GLY GLY B . n 
B 1 120 GLY 120 384 384 GLY GLY B . n 
B 1 121 MET 121 385 385 MET MET B . n 
B 1 122 GLU 122 386 386 GLU GLU B . n 
B 1 123 LEU 123 387 387 LEU LEU B . n 
B 1 124 PHE 124 388 388 PHE PHE B . n 
B 1 125 ARG 125 389 389 ARG ARG B . n 
B 1 126 ALA 126 390 390 ALA ALA B . n 
B 1 127 LEU 127 391 391 LEU LEU B . n 
B 1 128 GLY 128 392 392 GLY GLY B . n 
B 1 129 CYS 129 393 393 CYS CYS B . n 
B 1 130 SER 130 394 394 SER SER B . n 
B 1 131 GLU 131 395 395 GLU GLU B . n 
B 1 132 LEU 132 396 396 LEU LEU B . n 
B 1 133 ILE 133 397 397 ILE ILE B . n 
B 1 134 SER 134 398 398 SER SER B . n 
B 1 135 SER 135 399 399 SER SER B . n 
B 1 136 ILE 136 400 400 ILE ILE B . n 
B 1 137 PHE 137 401 401 PHE PHE B . n 
B 1 138 ASP 138 402 402 ASP ASP B . n 
B 1 139 PHE 139 403 403 PHE PHE B . n 
B 1 140 SER 140 404 404 SER SER B . n 
B 1 141 HIS 141 405 405 HIS HIS B . n 
B 1 142 SER 142 406 406 SER SER B . n 
B 1 143 LEU 143 407 407 LEU LEU B . n 
B 1 144 SER 144 408 408 SER SER B . n 
B 1 145 ALA 145 409 409 ALA ALA B . n 
B 1 146 LEU 146 410 410 LEU LEU B . n 
B 1 147 HIS 147 411 411 HIS HIS B . n 
B 1 148 PHE 148 412 412 PHE PHE B . n 
B 1 149 SER 149 413 413 SER SER B . n 
B 1 150 GLU 150 414 414 GLU GLU B . n 
B 1 151 ASP 151 415 415 ASP ASP B . n 
B 1 152 GLU 152 416 416 GLU GLU B . n 
B 1 153 ILE 153 417 417 ILE ILE B . n 
B 1 154 ALA 154 418 418 ALA ALA B . n 
B 1 155 LEU 155 419 419 LEU LEU B . n 
B 1 156 TYR 156 420 420 TYR TYR B . n 
B 1 157 THR 157 421 421 THR THR B . n 
B 1 158 ALA 158 422 422 ALA ALA B . n 
B 1 159 LEU 159 423 423 LEU LEU B . n 
B 1 160 VAL 160 424 424 VAL VAL B . n 
B 1 161 LEU 161 425 425 LEU LEU B . n 
B 1 162 ILE 162 426 426 ILE ILE B . n 
B 1 163 ASN 163 427 427 ASN ASN B . n 
B 1 164 ALA 164 428 428 ALA ALA B . n 
B 1 165 HIS 165 429 429 HIS HIS B . n 
B 1 166 ARG 166 430 430 ARG ARG B . n 
B 1 167 PRO 167 431 431 PRO PRO B . n 
B 1 168 GLY 168 432 432 GLY GLY B . n 
B 1 169 LEU 169 433 433 LEU LEU B . n 
B 1 170 GLN 170 434 434 GLN GLN B . n 
B 1 171 GLU 171 435 435 GLU GLU B . n 
B 1 172 LYS 172 436 436 LYS LYS B . n 
B 1 173 ARG 173 437 437 ARG ARG B . n 
B 1 174 LYS 174 438 438 LYS LYS B . n 
B 1 175 VAL 175 439 439 VAL VAL B . n 
B 1 176 GLU 176 440 440 GLU GLU B . n 
B 1 177 GLN 177 441 441 GLN GLN B . n 
B 1 178 LEU 178 442 442 LEU LEU B . n 
B 1 179 GLN 179 443 443 GLN GLN B . n 
B 1 180 TYR 180 444 444 TYR TYR B . n 
B 1 181 ASN 181 445 445 ASN ASN B . n 
B 1 182 LEU 182 446 446 LEU LEU B . n 
B 1 183 GLU 183 447 447 GLU GLU B . n 
B 1 184 LEU 184 448 448 LEU LEU B . n 
B 1 185 ALA 185 449 449 ALA ALA B . n 
B 1 186 PHE 186 450 450 PHE PHE B . n 
B 1 187 HIS 187 451 451 HIS HIS B . n 
B 1 188 HIS 188 452 452 HIS HIS B . n 
B 1 189 HIS 189 453 453 HIS HIS B . n 
B 1 190 LEU 190 454 454 LEU LEU B . n 
B 1 191 CYS 191 455 455 CYS CYS B . n 
B 1 192 LYS 192 456 456 LYS LYS B . n 
B 1 193 THR 193 457 457 THR THR B . n 
B 1 194 HIS 194 458 458 HIS HIS B . n 
B 1 195 ARG 195 459 459 ARG ARG B . n 
B 1 196 GLN 196 460 460 GLN GLN B . n 
B 1 197 SER 197 461 461 SER SER B . n 
B 1 198 ILE 198 462 462 ILE ILE B . n 
B 1 199 LEU 199 463 463 LEU LEU B . n 
B 1 200 ALA 200 464 464 ALA ALA B . n 
B 1 201 LYS 201 465 465 LYS LYS B . n 
B 1 202 LEU 202 466 466 LEU LEU B . n 
B 1 203 PRO 203 467 467 PRO PRO B . n 
B 1 204 PRO 204 468 468 PRO PRO B . n 
B 1 205 LYS 205 469 469 LYS LYS B . n 
B 1 206 GLY 206 470 470 GLY GLY B . n 
B 1 207 LYS 207 471 471 LYS LYS B . n 
B 1 208 LEU 208 472 472 LEU LEU B . n 
B 1 209 ARG 209 473 473 ARG ARG B . n 
B 1 210 SER 210 474 474 SER SER B . n 
B 1 211 LEU 211 475 475 LEU LEU B . n 
B 1 212 CYS 212 476 476 CYS CYS B . n 
B 1 213 SER 213 477 477 SER SER B . n 
B 1 214 GLN 214 478 478 GLN GLN B . n 
B 1 215 HIS 215 479 479 HIS HIS B . n 
B 1 216 VAL 216 480 480 VAL VAL B . n 
B 1 217 GLU 217 481 481 GLU GLU B . n 
B 1 218 ARG 218 482 482 ARG ARG B . n 
B 1 219 LEU 219 483 483 LEU LEU B . n 
B 1 220 GLN 220 484 484 GLN GLN B . n 
B 1 221 ILE 221 485 485 ILE ILE B . n 
B 1 222 PHE 222 486 486 PHE PHE B . n 
B 1 223 GLN 223 487 487 GLN GLN B . n 
B 1 224 HIS 224 488 488 HIS HIS B . n 
B 1 225 LEU 225 489 489 LEU LEU B . n 
B 1 226 HIS 226 490 490 HIS HIS B . n 
B 1 227 PRO 227 491 491 PRO PRO B . n 
B 1 228 ILE 228 492 492 ILE ILE B . n 
B 1 229 VAL 229 493 ?   ?   ?   B . n 
B 1 230 VAL 230 494 ?   ?   ?   B . n 
B 1 231 GLN 231 495 ?   ?   ?   B . n 
B 1 232 ALA 232 496 ?   ?   ?   B . n 
B 1 233 ALA 233 497 ?   ?   ?   B . n 
B 1 234 PHE 234 498 ?   ?   ?   B . n 
B 1 235 PRO 235 499 ?   ?   ?   B . n 
B 1 236 PRO 236 500 ?   ?   ?   B . n 
B 1 237 LEU 237 501 ?   ?   ?   B . n 
B 1 238 TYR 238 502 ?   ?   ?   B . n 
B 1 239 LYS 239 503 ?   ?   ?   B . n 
B 1 240 GLU 240 504 ?   ?   ?   B . n 
B 1 241 LEU 241 505 ?   ?   ?   B . n 
B 1 242 PHE 242 506 ?   ?   ?   B . n 
B 1 243 SER 243 507 ?   ?   ?   B . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        A1BW2 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1BW2 
_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 A1BW2 1  601 1   A1BW2 UNL A . 
D 2 A1BW2 1  601 2   A1BW2 UNL B . 
E 3 HOH   1  701 10  HOH   HOH A . 
E 3 HOH   2  702 124 HOH   HOH A . 
E 3 HOH   3  703 119 HOH   HOH A . 
E 3 HOH   4  704 130 HOH   HOH A . 
E 3 HOH   5  705 97  HOH   HOH A . 
E 3 HOH   6  706 19  HOH   HOH A . 
E 3 HOH   7  707 99  HOH   HOH A . 
E 3 HOH   8  708 102 HOH   HOH A . 
E 3 HOH   9  709 79  HOH   HOH A . 
E 3 HOH   10 710 16  HOH   HOH A . 
E 3 HOH   11 711 12  HOH   HOH A . 
E 3 HOH   12 712 87  HOH   HOH A . 
E 3 HOH   13 713 8   HOH   HOH A . 
E 3 HOH   14 714 49  HOH   HOH A . 
E 3 HOH   15 715 116 HOH   HOH A . 
E 3 HOH   16 716 37  HOH   HOH A . 
E 3 HOH   17 717 129 HOH   HOH A . 
E 3 HOH   18 718 121 HOH   HOH A . 
E 3 HOH   19 719 138 HOH   HOH A . 
E 3 HOH   20 720 76  HOH   HOH A . 
E 3 HOH   21 721 86  HOH   HOH A . 
E 3 HOH   22 722 44  HOH   HOH A . 
E 3 HOH   23 723 73  HOH   HOH A . 
E 3 HOH   24 724 38  HOH   HOH A . 
E 3 HOH   25 725 80  HOH   HOH A . 
E 3 HOH   26 726 43  HOH   HOH A . 
E 3 HOH   27 727 57  HOH   HOH A . 
E 3 HOH   28 728 127 HOH   HOH A . 
E 3 HOH   29 729 100 HOH   HOH A . 
E 3 HOH   30 730 96  HOH   HOH A . 
E 3 HOH   31 731 94  HOH   HOH A . 
E 3 HOH   32 732 36  HOH   HOH A . 
E 3 HOH   33 733 56  HOH   HOH A . 
E 3 HOH   34 734 5   HOH   HOH A . 
E 3 HOH   35 735 15  HOH   HOH A . 
E 3 HOH   36 736 1   HOH   HOH A . 
E 3 HOH   37 737 136 HOH   HOH A . 
E 3 HOH   38 738 61  HOH   HOH A . 
E 3 HOH   39 739 126 HOH   HOH A . 
E 3 HOH   40 740 39  HOH   HOH A . 
E 3 HOH   41 741 147 HOH   HOH A . 
E 3 HOH   42 742 2   HOH   HOH A . 
E 3 HOH   43 743 142 HOH   HOH A . 
E 3 HOH   44 744 34  HOH   HOH A . 
E 3 HOH   45 745 104 HOH   HOH A . 
E 3 HOH   46 746 68  HOH   HOH A . 
E 3 HOH   47 747 125 HOH   HOH A . 
E 3 HOH   48 748 47  HOH   HOH A . 
E 3 HOH   49 749 62  HOH   HOH A . 
E 3 HOH   50 750 81  HOH   HOH A . 
E 3 HOH   51 751 118 HOH   HOH A . 
E 3 HOH   52 752 144 HOH   HOH A . 
E 3 HOH   53 753 88  HOH   HOH A . 
E 3 HOH   54 754 22  HOH   HOH A . 
E 3 HOH   55 755 83  HOH   HOH A . 
E 3 HOH   56 756 93  HOH   HOH A . 
E 3 HOH   57 757 54  HOH   HOH A . 
E 3 HOH   58 758 32  HOH   HOH A . 
E 3 HOH   59 759 25  HOH   HOH A . 
E 3 HOH   60 760 91  HOH   HOH A . 
E 3 HOH   61 761 132 HOH   HOH A . 
E 3 HOH   62 762 78  HOH   HOH A . 
E 3 HOH   63 763 17  HOH   HOH A . 
E 3 HOH   64 764 123 HOH   HOH A . 
E 3 HOH   65 765 160 HOH   HOH A . 
E 3 HOH   66 766 84  HOH   HOH A . 
E 3 HOH   67 767 60  HOH   HOH A . 
E 3 HOH   68 768 133 HOH   HOH A . 
E 3 HOH   69 769 143 HOH   HOH A . 
E 3 HOH   70 770 122 HOH   HOH A . 
E 3 HOH   71 771 59  HOH   HOH A . 
E 3 HOH   72 772 120 HOH   HOH A . 
E 3 HOH   73 773 158 HOH   HOH A . 
E 3 HOH   74 774 131 HOH   HOH A . 
E 3 HOH   75 775 55  HOH   HOH A . 
E 3 HOH   76 776 152 HOH   HOH A . 
E 3 HOH   77 777 112 HOH   HOH A . 
E 3 HOH   78 778 46  HOH   HOH A . 
E 3 HOH   79 779 108 HOH   HOH A . 
E 3 HOH   80 780 109 HOH   HOH A . 
E 3 HOH   81 781 162 HOH   HOH A . 
E 3 HOH   82 782 113 HOH   HOH A . 
F 3 HOH   1  701 149 HOH   HOH B . 
F 3 HOH   2  702 157 HOH   HOH B . 
F 3 HOH   3  703 33  HOH   HOH B . 
F 3 HOH   4  704 134 HOH   HOH B . 
F 3 HOH   5  705 101 HOH   HOH B . 
F 3 HOH   6  706 146 HOH   HOH B . 
F 3 HOH   7  707 26  HOH   HOH B . 
F 3 HOH   8  708 40  HOH   HOH B . 
F 3 HOH   9  709 30  HOH   HOH B . 
F 3 HOH   10 710 48  HOH   HOH B . 
F 3 HOH   11 711 20  HOH   HOH B . 
F 3 HOH   12 712 161 HOH   HOH B . 
F 3 HOH   13 713 11  HOH   HOH B . 
F 3 HOH   14 714 45  HOH   HOH B . 
F 3 HOH   15 715 4   HOH   HOH B . 
F 3 HOH   16 716 7   HOH   HOH B . 
F 3 HOH   17 717 18  HOH   HOH B . 
F 3 HOH   18 718 135 HOH   HOH B . 
F 3 HOH   19 719 31  HOH   HOH B . 
F 3 HOH   20 720 92  HOH   HOH B . 
F 3 HOH   21 721 28  HOH   HOH B . 
F 3 HOH   22 722 77  HOH   HOH B . 
F 3 HOH   23 723 51  HOH   HOH B . 
F 3 HOH   24 724 137 HOH   HOH B . 
F 3 HOH   25 725 13  HOH   HOH B . 
F 3 HOH   26 726 107 HOH   HOH B . 
F 3 HOH   27 727 163 HOH   HOH B . 
F 3 HOH   28 728 141 HOH   HOH B . 
F 3 HOH   29 729 3   HOH   HOH B . 
F 3 HOH   30 730 159 HOH   HOH B . 
F 3 HOH   31 731 6   HOH   HOH B . 
F 3 HOH   32 732 82  HOH   HOH B . 
F 3 HOH   33 733 52  HOH   HOH B . 
F 3 HOH   34 734 58  HOH   HOH B . 
F 3 HOH   35 735 66  HOH   HOH B . 
F 3 HOH   36 736 153 HOH   HOH B . 
F 3 HOH   37 737 35  HOH   HOH B . 
F 3 HOH   38 738 53  HOH   HOH B . 
F 3 HOH   39 739 69  HOH   HOH B . 
F 3 HOH   40 740 106 HOH   HOH B . 
F 3 HOH   41 741 151 HOH   HOH B . 
F 3 HOH   42 742 24  HOH   HOH B . 
F 3 HOH   43 743 23  HOH   HOH B . 
F 3 HOH   44 744 72  HOH   HOH B . 
F 3 HOH   45 745 140 HOH   HOH B . 
F 3 HOH   46 746 63  HOH   HOH B . 
F 3 HOH   47 747 14  HOH   HOH B . 
F 3 HOH   48 748 148 HOH   HOH B . 
F 3 HOH   49 749 156 HOH   HOH B . 
F 3 HOH   50 750 155 HOH   HOH B . 
F 3 HOH   51 751 139 HOH   HOH B . 
F 3 HOH   52 752 74  HOH   HOH B . 
F 3 HOH   53 753 75  HOH   HOH B . 
F 3 HOH   54 754 128 HOH   HOH B . 
F 3 HOH   55 755 29  HOH   HOH B . 
F 3 HOH   56 756 27  HOH   HOH B . 
F 3 HOH   57 757 65  HOH   HOH B . 
F 3 HOH   58 758 41  HOH   HOH B . 
F 3 HOH   59 759 105 HOH   HOH B . 
F 3 HOH   60 760 95  HOH   HOH B . 
F 3 HOH   61 761 89  HOH   HOH B . 
F 3 HOH   62 762 85  HOH   HOH B . 
F 3 HOH   63 763 90  HOH   HOH B . 
F 3 HOH   64 764 103 HOH   HOH B . 
F 3 HOH   65 765 64  HOH   HOH B . 
F 3 HOH   66 766 110 HOH   HOH B . 
F 3 HOH   67 767 150 HOH   HOH B . 
F 3 HOH   68 768 98  HOH   HOH B . 
F 3 HOH   69 769 21  HOH   HOH B . 
F 3 HOH   70 770 67  HOH   HOH B . 
F 3 HOH   71 771 111 HOH   HOH B . 
F 3 HOH   72 772 9   HOH   HOH B . 
F 3 HOH   73 773 114 HOH   HOH B . 
F 3 HOH   74 774 70  HOH   HOH B . 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement       ? ? ? ? ? ? ? ? ? ? ? PHENIX   ? ? ? dev-2026_1692 1 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? HKL-2000 ? ? ? .             2 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? HKL-2000 ? ? ? .             3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHENIX   ? ? ? .             4 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   91.38 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9N9L 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     41.503 
_cell.length_a_esd                 ? 
_cell.length_b                     128.898 
_cell.length_b_esd                 ? 
_cell.length_c                     51.832 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        4 
_cell.reciprocal_angle_alpha       ? 
_cell.reciprocal_angle_beta        ? 
_cell.reciprocal_angle_gamma       ? 
_cell.reciprocal_angle_alpha_esd   ? 
_cell.reciprocal_angle_beta_esd    ? 
_cell.reciprocal_angle_gamma_esd   ? 
_cell.reciprocal_length_a          ? 
_cell.reciprocal_length_b          ? 
_cell.reciprocal_length_c          ? 
_cell.reciprocal_length_a_esd      ? 
_cell.reciprocal_length_b_esd      ? 
_cell.reciprocal_length_c_esd      ? 
_cell.pdbx_unique_axis             ? 
_cell.pdbx_esd_method              ? 
# 
_symmetry.entry_id                         9N9L 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                4 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 1 21 1' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
_exptl.absorpt_coefficient_mu     ? 
_exptl.absorpt_correction_T_max   ? 
_exptl.absorpt_correction_T_min   ? 
_exptl.absorpt_correction_type    ? 
_exptl.absorpt_process_details    ? 
_exptl.entry_id                   9N9L 
_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             2.45 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          49.76 
_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    '18% PEG 4000, 0.1 M Hepes pH 7.5 and 0.1 M Ammonium Acetate' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            293 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     80 
_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 EIGER X 9M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2015-05-16 
_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   1.0 
_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                        'CLSI BEAMLINE 08ID-1' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        1.0 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   08ID-1 
_diffrn_source.pdbx_synchrotron_site       CLSI 
# 
_reflns.B_iso_Wilson_estimate                          23.12 
_reflns.entry_id                                       9N9L 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.637 
_reflns.d_resolution_low                               40.383 
_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                                     66034 
_reflns.observed_criterion                             ? 
_reflns.observed_criterion_F_max                       ? 
_reflns.observed_criterion_F_min                       ? 
_reflns.observed_criterion_I_max                       ? 
_reflns.observed_criterion_I_min                       ? 
_reflns.observed_criterion_sigma_F                     ? 
_reflns.observed_criterion_sigma_I                     ? 
_reflns.percent_possible_obs                           98.81 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                3.8 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          22.2 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               ? 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                ? 
_reflns.pdbx_Rpim_I_all                                ? 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   ? 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.052 
_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                                    1.637 
_reflns_shell.d_res_low                                     1.696 
_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                             6394 
_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                                  ? 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          96.13 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  0.509 
_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]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               ? 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.details                                  ? 
_refine.diff_density_max                         ? 
_refine.diff_density_max_esd                     ? 
_refine.diff_density_min                         ? 
_refine.diff_density_min_esd                     ? 
_refine.diff_density_rms                         ? 
_refine.diff_density_rms_esd                     ? 
_refine.entry_id                                 9N9L 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            1.637 
_refine.ls_d_res_low                             40.383 
_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                     66024 
_refine.ls_number_reflns_R_free                  1998 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    98.77 
_refine.ls_percent_reflns_R_free                 3.03 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1919 
_refine.ls_R_factor_R_free                       0.2248 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1908 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    'FLAT BULK SOLVENT MODEL' 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          1.34 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               'FREE R-VALUE' 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       ML 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             1.11 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.90 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 23.49 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_diffrn_id                           1 
_refine.overall_SU_B                             ? 
_refine.overall_SU_ML                            0.16 
_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.pdbx_number_atoms_protein        3730 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         78 
_refine_hist.number_atoms_solvent             156 
_refine_hist.number_atoms_total               3964 
_refine_hist.d_res_high                       1.637 
_refine_hist.d_res_low                        40.383 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.criterion 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.number 
_refine_ls_restr.rejects 
_refine_ls_restr.type 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' ? 0.014  ? 3900 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 1.483  ? 5269 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 14.990 ? 1451 ? f_dihedral_angle_d ? ? 
'X-RAY DIFFRACTION' ? 0.067  ? 563  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.007  ? 675  ? f_plane_restr      ? ? 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_obs 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.redundancy_reflns_all 
_refine_ls_shell.redundancy_reflns_obs 
_refine_ls_shell.wR_factor_all 
_refine_ls_shell.wR_factor_obs 
_refine_ls_shell.wR_factor_R_free 
_refine_ls_shell.wR_factor_R_work 
_refine_ls_shell.pdbx_R_complete 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.pdbx_phase_error 
_refine_ls_shell.pdbx_fsc_work 
_refine_ls_shell.pdbx_fsc_free 
_refine_ls_shell.R_factor_R_free 
'X-RAY DIFFRACTION' 1.637  1.6776 . . 135 4392 95.00  . . . . 0.2477 . . . . . . . . . . . 0.2738 
'X-RAY DIFFRACTION' 1.6776 1.7230 . . 142 4563 98.00  . . . . 0.2238 . . . . . . . . . . . 0.2687 
'X-RAY DIFFRACTION' 1.7230 1.7737 . . 139 4502 99.00  . . . . 0.2068 . . . . . . . . . . . 0.2442 
'X-RAY DIFFRACTION' 1.7737 1.8309 . . 143 4568 99.00  . . . . 0.1986 . . . . . . . . . . . 0.2450 
'X-RAY DIFFRACTION' 1.8309 1.8964 . . 148 4567 99.00  . . . . 0.1953 . . . . . . . . . . . 0.2202 
'X-RAY DIFFRACTION' 1.8964 1.9723 . . 144 4617 99.00  . . . . 0.2040 . . . . . . . . . . . 0.2309 
'X-RAY DIFFRACTION' 1.9723 2.0621 . . 139 4568 99.00  . . . . 0.1991 . . . . . . . . . . . 0.2497 
'X-RAY DIFFRACTION' 2.0621 2.1708 . . 137 4593 99.00  . . . . 0.1887 . . . . . . . . . . . 0.2034 
'X-RAY DIFFRACTION' 2.1708 2.3068 . . 146 4585 99.00  . . . . 0.1810 . . . . . . . . . . . 0.2408 
'X-RAY DIFFRACTION' 2.3068 2.4848 . . 147 4583 99.00  . . . . 0.1981 . . . . . . . . . . . 0.2238 
'X-RAY DIFFRACTION' 2.4848 2.7349 . . 149 4627 100.00 . . . . 0.2063 . . . . . . . . . . . 0.2323 
'X-RAY DIFFRACTION' 2.7349 3.1305 . . 137 4604 100.00 . . . . 0.2060 . . . . . . . . . . . 0.2662 
'X-RAY DIFFRACTION' 3.1305 3.9435 . . 150 4633 100.00 . . . . 0.1856 . . . . . . . . . . . 0.2339 
'X-RAY DIFFRACTION' 3.9435 10     . . 142 4624 98.00  . . . . 0.1697 . . . . . . . . . . . 0.1773 
# 
_struct.entry_id                     9N9L 
_struct.title                        'An RORgt Inverse agonist for treatment of Psoriasis' 
_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        9N9L 
_struct_keywords.text            'Nuclear Hormone Receptor, NUCLEAR PROTEIN' 
_struct_keywords.pdbx_keywords   'NUCLEAR PROTEIN' 
# 
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 2 ? 
E N N 3 ? 
F N N 3 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    RORG_HUMAN 
_struct_ref.pdbx_db_accession          P51449 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;ASLTEIEHLVQSVCKSYRETCQLRLEDLLRQRSNIFSREEVTGYQRKSMWEMWERCAHHLTEAIQYVVEFAKRLSGFMEL
CQNDQIVLLKAGAMEVVLVRMCRAYNADNRTVFFEGKYGGMELFRALGCSELISSIFDFSHSLSALHFSEDEIALYTALV
LINAHRPGLQEKRKVEQLQYNLELAFHHHLCKTHRQSILAKLPPKGKLRSLCSQHVERLQIFQHLHPIVVQAAFPPLYKE
LFS
;
_struct_ref.pdbx_align_begin           265 
# 
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 9N9L A 1 ? 243 ? P51449 265 ? 507 ? 265 507 
2 1 9N9L B 1 ? 243 ? P51449 265 ? 507 ? 265 507 
# 
loop_
_pdbx_struct_assembly.id 
_pdbx_struct_assembly.details 
_pdbx_struct_assembly.method_details 
_pdbx_struct_assembly.oligomeric_details 
_pdbx_struct_assembly.oligomeric_count 
1 author_defined_assembly ? monomeric 1 
2 author_defined_assembly ? monomeric 1 
# 
loop_
_pdbx_struct_assembly_gen.assembly_id 
_pdbx_struct_assembly_gen.oper_expression 
_pdbx_struct_assembly_gen.asym_id_list 
1 1 A,C,E 
2 1 B,D,F 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   none 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 SER A 2   ? THR A 20  ? SER A 266 THR A 284 1 ? 19 
HELX_P HELX_P2  AA2 ARG A 24  ? GLN A 31  ? ARG A 288 GLN A 295 1 ? 8  
HELX_P HELX_P3  AA3 SER A 37  ? ARG A 46  ? SER A 301 ARG A 310 1 ? 10 
HELX_P HELX_P4  AA4 SER A 48  ? LEU A 74  ? SER A 312 LEU A 338 1 ? 27 
HELX_P HELX_P5  AA5 GLY A 76  ? LEU A 80  ? GLY A 340 LEU A 344 5 ? 5  
HELX_P HELX_P6  AA6 CYS A 81  ? MET A 101 ? CYS A 345 MET A 365 1 ? 21 
HELX_P HELX_P7  AA7 GLY A 120 ? GLY A 128 ? GLY A 384 GLY A 392 5 ? 9  
HELX_P HELX_P8  AA8 CYS A 129 ? ALA A 145 ? CYS A 393 ALA A 409 1 ? 17 
HELX_P HELX_P9  AA9 SER A 149 ? ILE A 162 ? SER A 413 ILE A 426 1 ? 14 
HELX_P HELX_P10 AB1 GLU A 171 ? THR A 193 ? GLU A 435 THR A 457 1 ? 23 
HELX_P HELX_P11 AB2 ARG A 195 ? LEU A 202 ? ARG A 459 LEU A 466 5 ? 8  
HELX_P HELX_P12 AB3 PRO A 204 ? HIS A 226 ? PRO A 468 HIS A 490 1 ? 23 
HELX_P HELX_P13 AB4 SER B 2   ? CYS B 21  ? SER B 266 CYS B 285 1 ? 20 
HELX_P HELX_P14 AB5 ARG B 24  ? GLN B 31  ? ARG B 288 GLN B 295 1 ? 8  
HELX_P HELX_P15 AB6 ARG B 32  ? ASN B 34  ? ARG B 296 ASN B 298 5 ? 3  
HELX_P HELX_P16 AB7 SER B 37  ? ARG B 46  ? SER B 301 ARG B 310 1 ? 10 
HELX_P HELX_P17 AB8 SER B 48  ? LEU B 74  ? SER B 312 LEU B 338 1 ? 27 
HELX_P HELX_P18 AB9 GLY B 76  ? LEU B 80  ? GLY B 340 LEU B 344 5 ? 5  
HELX_P HELX_P19 AC1 CYS B 81  ? MET B 101 ? CYS B 345 MET B 365 1 ? 21 
HELX_P HELX_P20 AC2 GLY B 120 ? GLY B 128 ? GLY B 384 GLY B 392 5 ? 9  
HELX_P HELX_P21 AC3 CYS B 129 ? ALA B 145 ? CYS B 393 ALA B 409 1 ? 17 
HELX_P HELX_P22 AC4 SER B 149 ? ILE B 162 ? SER B 413 ILE B 426 1 ? 14 
HELX_P HELX_P23 AC5 GLU B 171 ? THR B 193 ? GLU B 435 THR B 457 1 ? 23 
HELX_P HELX_P24 AC6 SER B 197 ? LEU B 202 ? SER B 461 LEU B 466 1 ? 6  
HELX_P HELX_P25 AC7 PRO B 204 ? HIS B 226 ? PRO B 468 HIS B 490 1 ? 23 
# 
_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 ? 3 ? 
AA2 ? 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 
AA2 1 2 ? anti-parallel 
AA2 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 TYR A 105 ? ASN A 106 ? TYR A 369 ASN A 370 
AA1 2 THR A 111 ? PHE A 114 ? THR A 375 PHE A 378 
AA1 3 LYS A 117 ? GLY A 119 ? LYS A 381 GLY A 383 
AA2 1 TYR B 105 ? ASN B 106 ? TYR B 369 ASN B 370 
AA2 2 THR B 111 ? PHE B 114 ? THR B 375 PHE B 378 
AA2 3 LYS B 117 ? GLY B 119 ? LYS B 381 GLY B 383 
# 
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 ASN A 106 ? N ASN A 370 O THR A 111 ? O THR A 375 
AA1 2 3 N PHE A 114 ? N PHE A 378 O LYS A 117 ? O LYS A 381 
AA2 1 2 N ASN B 106 ? N ASN B 370 O THR B 111 ? O THR B 375 
AA2 2 3 N PHE B 114 ? N PHE B 378 O LYS B 117 ? O LYS B 381 
# 
_pdbx_entry_details.entry_id                   9N9L 
_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 GLN A 286 ? ? 77.12   -61.81 
2 1 GLN B 286 ? ? 87.03   -61.90 
3 1 CYS B 393 ? ? -142.64 57.83  
# 
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 -14.0923 1.9887   67.8543 0.2859 ? -0.0346 ? -0.0806 ? 0.2879 ? 0.0847  ? 0.2861 ? 2.8335 ? 
2.4142  ? -2.9388 ? 3.9547 ? -3.4423 ? 4.9491 ? -0.1890 ? 0.2971  ? -0.0259 ? -0.5631 ? 0.5270  ? 0.4310  ? 0.4816  ? -0.6757 ? 
-0.4213 ? 
2  'X-RAY DIFFRACTION' ? refined 7.6048   15.0040  54.5399 0.1951 ? -0.0068 ? -0.0196 ? 0.1914 ? 0.0029  ? 0.1926 ? 0.8250 ? 
0.1056  ? -0.1530 ? 0.9470 ? 0.1816  ? 0.6186 ? -0.0478 ? 0.1083  ? 0.0613  ? -0.0755 ? 0.0975  ? -0.0575 ? 0.1107  ? 0.0334  ? 
-0.0498 ? 
3  'X-RAY DIFFRACTION' ? refined -6.3822  16.7153  69.0297 0.1831 ? -0.0132 ? -0.0001 ? 0.2074 ? 0.0377  ? 0.1839 ? 2.3387 ? 
-1.1183 ? -1.2539 ? 3.0684 ? 0.8700  ? 2.5008 ? 0.0699  ? -0.0927 ? 0.0027  ? 0.0963  ? 0.0155  ? 0.1696  ? -0.0994 ? -0.0721 ? 
-0.0876 ? 
4  'X-RAY DIFFRACTION' ? refined 10.3692  9.6530   64.1166 0.2251 ? -0.0011 ? -0.0549 ? 0.2321 ? 0.0279  ? 0.2270 ? 1.7470 ? 
0.0703  ? -1.0467 ? 1.1037 ? -0.4242 ? 0.7001 ? -0.0425 ? -0.2565 ? -0.1209 ? 0.1014  ? -0.0003 ? -0.1942 ? 0.1194  ? 0.1155  ? 
0.0439  ? 
5  'X-RAY DIFFRACTION' ? refined -7.9423  6.7460   78.4565 0.2544 ? 0.0008  ? -0.0235 ? 0.2859 ? 0.0710  ? 0.2297 ? 1.3561 ? 
-0.3323 ? -0.7320 ? 3.4154 ? -0.1766 ? 1.4285 ? -0.1176 ? -0.2547 ? -0.1944 ? 0.4667  ? 0.1539  ? 0.2485  ? -0.0100 ? -0.1007 ? 
-0.0429 ? 
6  'X-RAY DIFFRACTION' ? refined 7.7051   12.2306  77.6884 1.1391 ? 0.1600  ? 0.1393  ? 0.4917 ? -0.0976 ? 0.1019 ? 0.8247 ? 
0.3308  ? -0.1426 ? 0.9233 ? 0.2307  ? 0.1285 ? 0.0646  ? -0.3127 ? 0.1487  ? 0.1106  ? 0.0349  ? -0.0449 ? -0.4776 ? 0.1326  ? 
0.1246  ? 
7  'X-RAY DIFFRACTION' ? refined 9.4669   28.9143  65.5228 0.2575 ? 0.0123  ? -0.0255 ? 0.2528 ? -0.0320 ? 0.2896 ? 2.0080 ? 
0.6622  ? -0.5333 ? 4.7199 ? -1.3573 ? 1.8754 ? -0.0222 ? -0.2433 ? 0.2339  ? 0.4224  ? 0.0110  ? 0.1284  ? -0.2356 ? 0.0352  ? 
0.0282  ? 
8  'X-RAY DIFFRACTION' ? refined -15.9686 -5.0567  44.0527 0.3607 ? 0.0621  ? 0.1080  ? 0.3479 ? 0.0658  ? 0.3339 ? 2.8798 ? 
-1.6097 ? 1.9927  ? 3.6008 ? -2.5918 ? 3.5464 ? -0.2455 ? -0.3611 ? 0.1823  ? 0.6758  ? 0.5220  ? 0.6161  ? -0.4469 ? -0.7867 ? 
-0.1982 ? 
9  'X-RAY DIFFRACTION' ? refined 2.6768   -9.4014  56.6704 0.4767 ? 0.0228  ? 0.0372  ? 0.2559 ? -0.0540 ? 0.3115 ? 4.9282 ? 
1.9891  ? 1.9542  ? 2.9956 ? 0.5671  ? 3.2241 ? 0.1403  ? -0.5799 ? 0.4496  ? 0.8401  ? -0.2007 ? 0.4984  ? 0.1483  ? -0.2193 ? 
-0.1365 ? 
10 'X-RAY DIFFRACTION' ? refined 19.0135  -23.9690 57.0993 0.2683 ? 0.0140  ? -0.0692 ? 0.3097 ? -0.0231 ? 0.2429 ? 1.0003 ? 
-0.1007 ? 0.1777  ? 5.4477 ? 1.7455  ? 2.0196 ? -0.0454 ? -0.2745 ? 0.0189  ? 0.7140  ? -0.0345 ? -0.3365 ? 0.0148  ? 0.1321  ? 
-0.0254 ? 
11 'X-RAY DIFFRACTION' ? refined -0.2190  -26.1099 48.5488 0.2015 ? -0.0088 ? 0.0132  ? 0.1973 ? -0.0095 ? 0.2016 ? 4.2622 ? 
-2.0080 ? 1.3529  ? 1.9790 ? -0.8387 ? 1.3983 ? -0.0916 ? -0.3298 ? -0.1365 ? 0.1680  ? 0.1976  ? 0.1199  ? -0.0689 ? -0.0656 ? 
-0.0486 ? 
12 'X-RAY DIFFRACTION' ? refined -1.2348  -17.1502 43.2544 0.1883 ? 0.0159  ? 0.0255  ? 0.2003 ? 0.0033  ? 0.1900 ? 2.2089 ? 
-0.0082 ? 1.5651  ? 1.1548 ? -0.0914 ? 1.8535 ? -0.0188 ? 0.0437  ? 0.2069  ? -0.0027 ? -0.0113 ? 0.0751  ? -0.0508 ? -0.0744 ? 
0.0129  ? 
13 'X-RAY DIFFRACTION' ? refined 13.4771  -17.4312 42.9494 0.2140 ? -0.0215 ? 0.0442  ? 0.2479 ? -0.0054 ? 0.2523 ? 1.8761 ? 
-0.9113 ? 0.9736  ? 3.0253 ? -0.9808 ? 1.1873 ? -0.0165 ? 0.2430  ? 0.0805  ? -0.2274 ? -0.0058 ? -0.3633 ? -0.0844 ? 0.1624  ? 
0.0726  ? 
14 'X-RAY DIFFRACTION' ? refined -6.8176  -11.9213 35.9611 0.2482 ? 0.0270  ? 0.0013  ? 0.2162 ? 0.0513  ? 0.2349 ? 2.0207 ? 
1.0454  ? 1.2679  ? 3.1474 ? 1.4751  ? 2.9900 ? 0.0107  ? 0.1626  ? 0.0999  ? 0.0840  ? 0.0617  ? 0.1008  ? 0.1104  ? 0.0394  ? 
-0.1294 ? 
15 'X-RAY DIFFRACTION' ? refined -13.1062 -5.2285  32.2961 0.2131 ? 0.0081  ? 0.0041  ? 0.2465 ? 0.0974  ? 0.2536 ? 2.1813 ? 
1.2052  ? 1.3950  ? 4.2083 ? 1.2883  ? 2.9333 ? -0.0361 ? 0.1338  ? 0.1948  ? -0.2354 ? 0.0684  ? 0.3077  ? -0.1803 ? -0.2082 ? 
0.0008  ? 
16 'X-RAY DIFFRACTION' ? refined 0.5220   -0.8969  35.5270 0.4575 ? 0.0195  ? 0.1040  ? 0.3172 ? 0.0712  ? 0.2833 ? 4.1335 ? 
-1.1273 ? 0.0173  ? 3.8336 ? 1.5131  ? 3.4992 ? 0.0134  ? 0.7188  ? 0.5386  ? -0.4759 ? 0.1244  ? -0.4962 ? 0.3703  ? 0.2014  ? 
-0.0801 ? 
17 'X-RAY DIFFRACTION' ? refined 7.0945   -29.1846 37.5334 0.3544 ? -0.0054 ? 0.0033  ? 0.3261 ? -0.0846 ? 0.2404 ? 2.6590 ? 
-0.0781 ? -0.1178 ? 5.1918 ? 0.3627  ? 0.9889 ? -0.0364 ? 0.2297  ? -0.2283 ? -0.5947 ? 0.0740  ? 0.2385  ? -0.3226 ? 0.0139  ? 
0.0632  ? 
# 
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  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 265 through 284 )
;
2  'X-RAY DIFFRACTION' 2  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 285 through 337 )
;
3  'X-RAY DIFFRACTION' 3  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 338 through 368 )
;
4  'X-RAY DIFFRACTION' 4  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 369 through 425 )
;
5  'X-RAY DIFFRACTION' 5  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 426 through 465 )
;
6  'X-RAY DIFFRACTION' 6  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 466 through 474 )
;
7  'X-RAY DIFFRACTION' 7  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 475 through 492 )
;
8  'X-RAY DIFFRACTION' 8  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'B' and (resid 265 through 284 )
;
9  'X-RAY DIFFRACTION' 9  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'B' and (resid 285 through 297 )
;
10 'X-RAY DIFFRACTION' 10 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'B' and (resid 298 through 312 )
;
11 'X-RAY DIFFRACTION' 11 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'B' and (resid 313 through 337 )
;
12 'X-RAY DIFFRACTION' 12 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'B' and (resid 338 through 384 )
;
13 'X-RAY DIFFRACTION' 13 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'B' and (resid 385 through 410 )
;
14 'X-RAY DIFFRACTION' 14 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'B' and (resid 411 through 435 )
;
15 'X-RAY DIFFRACTION' 15 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'B' and (resid 436 through 456 )
;
16 'X-RAY DIFFRACTION' 16 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'B' and (resid 457 through 470 )
;
17 'X-RAY DIFFRACTION' 17 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'B' and (resid 471 through 492 )
;
# 
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 VAL 493 ? A VAL 229 
2  1 Y 1 A VAL 494 ? A VAL 230 
3  1 Y 1 A GLN 495 ? A GLN 231 
4  1 Y 1 A ALA 496 ? A ALA 232 
5  1 Y 1 A ALA 497 ? A ALA 233 
6  1 Y 1 A PHE 498 ? A PHE 234 
7  1 Y 1 A PRO 499 ? A PRO 235 
8  1 Y 1 A PRO 500 ? A PRO 236 
9  1 Y 1 A LEU 501 ? A LEU 237 
10 1 Y 1 A TYR 502 ? A TYR 238 
11 1 Y 1 A LYS 503 ? A LYS 239 
12 1 Y 1 A GLU 504 ? A GLU 240 
13 1 Y 1 A LEU 505 ? A LEU 241 
14 1 Y 1 A PHE 506 ? A PHE 242 
15 1 Y 1 A SER 507 ? A SER 243 
16 1 Y 1 B VAL 493 ? B VAL 229 
17 1 Y 1 B VAL 494 ? B VAL 230 
18 1 Y 1 B GLN 495 ? B GLN 231 
19 1 Y 1 B ALA 496 ? B ALA 232 
20 1 Y 1 B ALA 497 ? B ALA 233 
21 1 Y 1 B PHE 498 ? B PHE 234 
22 1 Y 1 B PRO 499 ? B PRO 235 
23 1 Y 1 B PRO 500 ? B PRO 236 
24 1 Y 1 B LEU 501 ? B LEU 237 
25 1 Y 1 B TYR 502 ? B TYR 238 
26 1 Y 1 B LYS 503 ? B LYS 239 
27 1 Y 1 B GLU 504 ? B GLU 240 
28 1 Y 1 B LEU 505 ? B LEU 241 
29 1 Y 1 B PHE 506 ? B PHE 242 
30 1 Y 1 B SER 507 ? B SER 243 
# 
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 
A1BW2 C16  C  Y N 1   
A1BW2 C17  C  Y N 2   
A1BW2 C15  C  Y N 3   
A1BW2 C18  C  Y N 4   
A1BW2 C21  C  Y N 5   
A1BW2 C19  C  Y N 6   
A1BW2 C14  C  Y N 7   
A1BW2 C10  C  Y N 8   
A1BW2 C12  C  Y N 9   
A1BW2 C8   C  N N 10  
A1BW2 C33  C  N N 11  
A1BW2 C5   C  N N 12  
A1BW2 C4   C  N N 13  
A1BW2 C6   C  N N 14  
A1BW2 C2   C  N S 15  
A1BW2 C1   C  N N 16  
A1BW2 C38  C  N N 17  
A1BW2 C39  C  N N 18  
A1BW2 C36  C  N N 19  
A1BW2 C23  C  N N 20  
A1BW2 C37  C  N N 21  
A1BW2 C25  C  N N 22  
A1BW2 C29  C  N N 23  
A1BW2 N11  N  Y N 24  
A1BW2 N7   N  N N 25  
A1BW2 N35  N  N N 26  
A1BW2 O9   O  N N 27  
A1BW2 O34  O  N N 28  
A1BW2 O24  O  N N 29  
A1BW2 O40  O  N N 30  
A1BW2 F26  F  N N 31  
A1BW2 F27  F  N N 32  
A1BW2 F28  F  N N 33  
A1BW2 F30  F  N N 34  
A1BW2 F31  F  N N 35  
A1BW2 F32  F  N N 36  
A1BW2 S13  S  Y N 37  
A1BW2 CL22 CL N N 38  
A1BW2 CL20 CL N N 39  
A1BW2 H50  H  N N 40  
A1BW2 H51  H  N N 41  
A1BW2 H46  H  N N 42  
A1BW2 H47  H  N N 43  
A1BW2 H45  H  N N 44  
A1BW2 H44  H  N N 45  
A1BW2 H48  H  N N 46  
A1BW2 H49  H  N N 47  
A1BW2 H3   H  N N 48  
A1BW2 H41  H  N N 49  
A1BW2 H42  H  N N 50  
A1BW2 H43  H  N N 51  
A1BW2 H56  H  N N 52  
A1BW2 H58  H  N N 53  
A1BW2 H57  H  N N 54  
A1BW2 H60  H  N N 55  
A1BW2 H61  H  N N 56  
A1BW2 H59  H  N N 57  
A1BW2 H54  H  N N 58  
A1BW2 H55  H  N N 59  
A1BW2 H53  H  N N 60  
A1BW2 H52  H  N N 61  
A1BW2 H62  H  N N 62  
ALA   N    N  N N 63  
ALA   CA   C  N S 64  
ALA   C    C  N N 65  
ALA   O    O  N N 66  
ALA   CB   C  N N 67  
ALA   OXT  O  N N 68  
ALA   H    H  N N 69  
ALA   H2   H  N N 70  
ALA   HA   H  N N 71  
ALA   HB1  H  N N 72  
ALA   HB2  H  N N 73  
ALA   HB3  H  N N 74  
ALA   HXT  H  N N 75  
ARG   N    N  N N 76  
ARG   CA   C  N S 77  
ARG   C    C  N N 78  
ARG   O    O  N N 79  
ARG   CB   C  N N 80  
ARG   CG   C  N N 81  
ARG   CD   C  N N 82  
ARG   NE   N  N N 83  
ARG   CZ   C  N N 84  
ARG   NH1  N  N N 85  
ARG   NH2  N  N N 86  
ARG   OXT  O  N N 87  
ARG   H    H  N N 88  
ARG   H2   H  N N 89  
ARG   HA   H  N N 90  
ARG   HB2  H  N N 91  
ARG   HB3  H  N N 92  
ARG   HG2  H  N N 93  
ARG   HG3  H  N N 94  
ARG   HD2  H  N N 95  
ARG   HD3  H  N N 96  
ARG   HE   H  N N 97  
ARG   HH11 H  N N 98  
ARG   HH12 H  N N 99  
ARG   HH21 H  N N 100 
ARG   HH22 H  N N 101 
ARG   HXT  H  N N 102 
ASN   N    N  N N 103 
ASN   CA   C  N S 104 
ASN   C    C  N N 105 
ASN   O    O  N N 106 
ASN   CB   C  N N 107 
ASN   CG   C  N N 108 
ASN   OD1  O  N N 109 
ASN   ND2  N  N N 110 
ASN   OXT  O  N N 111 
ASN   H    H  N N 112 
ASN   H2   H  N N 113 
ASN   HA   H  N N 114 
ASN   HB2  H  N N 115 
ASN   HB3  H  N N 116 
ASN   HD21 H  N N 117 
ASN   HD22 H  N N 118 
ASN   HXT  H  N N 119 
ASP   N    N  N N 120 
ASP   CA   C  N S 121 
ASP   C    C  N N 122 
ASP   O    O  N N 123 
ASP   CB   C  N N 124 
ASP   CG   C  N N 125 
ASP   OD1  O  N N 126 
ASP   OD2  O  N N 127 
ASP   OXT  O  N N 128 
ASP   H    H  N N 129 
ASP   H2   H  N N 130 
ASP   HA   H  N N 131 
ASP   HB2  H  N N 132 
ASP   HB3  H  N N 133 
ASP   HD2  H  N N 134 
ASP   HXT  H  N N 135 
CYS   N    N  N N 136 
CYS   CA   C  N R 137 
CYS   C    C  N N 138 
CYS   O    O  N N 139 
CYS   CB   C  N N 140 
CYS   SG   S  N N 141 
CYS   OXT  O  N N 142 
CYS   H    H  N N 143 
CYS   H2   H  N N 144 
CYS   HA   H  N N 145 
CYS   HB2  H  N N 146 
CYS   HB3  H  N N 147 
CYS   HG   H  N N 148 
CYS   HXT  H  N N 149 
GLN   N    N  N N 150 
GLN   CA   C  N S 151 
GLN   C    C  N N 152 
GLN   O    O  N N 153 
GLN   CB   C  N N 154 
GLN   CG   C  N N 155 
GLN   CD   C  N N 156 
GLN   OE1  O  N N 157 
GLN   NE2  N  N N 158 
GLN   OXT  O  N N 159 
GLN   H    H  N N 160 
GLN   H2   H  N N 161 
GLN   HA   H  N N 162 
GLN   HB2  H  N N 163 
GLN   HB3  H  N N 164 
GLN   HG2  H  N N 165 
GLN   HG3  H  N N 166 
GLN   HE21 H  N N 167 
GLN   HE22 H  N N 168 
GLN   HXT  H  N N 169 
GLU   N    N  N N 170 
GLU   CA   C  N S 171 
GLU   C    C  N N 172 
GLU   O    O  N N 173 
GLU   CB   C  N N 174 
GLU   CG   C  N N 175 
GLU   CD   C  N N 176 
GLU   OE1  O  N N 177 
GLU   OE2  O  N N 178 
GLU   OXT  O  N N 179 
GLU   H    H  N N 180 
GLU   H2   H  N N 181 
GLU   HA   H  N N 182 
GLU   HB2  H  N N 183 
GLU   HB3  H  N N 184 
GLU   HG2  H  N N 185 
GLU   HG3  H  N N 186 
GLU   HE2  H  N N 187 
GLU   HXT  H  N N 188 
GLY   N    N  N N 189 
GLY   CA   C  N N 190 
GLY   C    C  N N 191 
GLY   O    O  N N 192 
GLY   OXT  O  N N 193 
GLY   H    H  N N 194 
GLY   H2   H  N N 195 
GLY   HA2  H  N N 196 
GLY   HA3  H  N N 197 
GLY   HXT  H  N N 198 
HIS   N    N  N N 199 
HIS   CA   C  N S 200 
HIS   C    C  N N 201 
HIS   O    O  N N 202 
HIS   CB   C  N N 203 
HIS   CG   C  Y N 204 
HIS   ND1  N  Y N 205 
HIS   CD2  C  Y N 206 
HIS   CE1  C  Y N 207 
HIS   NE2  N  Y N 208 
HIS   OXT  O  N N 209 
HIS   H    H  N N 210 
HIS   H2   H  N N 211 
HIS   HA   H  N N 212 
HIS   HB2  H  N N 213 
HIS   HB3  H  N N 214 
HIS   HD1  H  N N 215 
HIS   HD2  H  N N 216 
HIS   HE1  H  N N 217 
HIS   HE2  H  N N 218 
HIS   HXT  H  N N 219 
HOH   O    O  N N 220 
HOH   H1   H  N N 221 
HOH   H2   H  N N 222 
ILE   N    N  N N 223 
ILE   CA   C  N S 224 
ILE   C    C  N N 225 
ILE   O    O  N N 226 
ILE   CB   C  N S 227 
ILE   CG1  C  N N 228 
ILE   CG2  C  N N 229 
ILE   CD1  C  N N 230 
ILE   OXT  O  N N 231 
ILE   H    H  N N 232 
ILE   H2   H  N N 233 
ILE   HA   H  N N 234 
ILE   HB   H  N N 235 
ILE   HG12 H  N N 236 
ILE   HG13 H  N N 237 
ILE   HG21 H  N N 238 
ILE   HG22 H  N N 239 
ILE   HG23 H  N N 240 
ILE   HD11 H  N N 241 
ILE   HD12 H  N N 242 
ILE   HD13 H  N N 243 
ILE   HXT  H  N N 244 
LEU   N    N  N N 245 
LEU   CA   C  N S 246 
LEU   C    C  N N 247 
LEU   O    O  N N 248 
LEU   CB   C  N N 249 
LEU   CG   C  N N 250 
LEU   CD1  C  N N 251 
LEU   CD2  C  N N 252 
LEU   OXT  O  N N 253 
LEU   H    H  N N 254 
LEU   H2   H  N N 255 
LEU   HA   H  N N 256 
LEU   HB2  H  N N 257 
LEU   HB3  H  N N 258 
LEU   HG   H  N N 259 
LEU   HD11 H  N N 260 
LEU   HD12 H  N N 261 
LEU   HD13 H  N N 262 
LEU   HD21 H  N N 263 
LEU   HD22 H  N N 264 
LEU   HD23 H  N N 265 
LEU   HXT  H  N N 266 
LYS   N    N  N N 267 
LYS   CA   C  N S 268 
LYS   C    C  N N 269 
LYS   O    O  N N 270 
LYS   CB   C  N N 271 
LYS   CG   C  N N 272 
LYS   CD   C  N N 273 
LYS   CE   C  N N 274 
LYS   NZ   N  N N 275 
LYS   OXT  O  N N 276 
LYS   H    H  N N 277 
LYS   H2   H  N N 278 
LYS   HA   H  N N 279 
LYS   HB2  H  N N 280 
LYS   HB3  H  N N 281 
LYS   HG2  H  N N 282 
LYS   HG3  H  N N 283 
LYS   HD2  H  N N 284 
LYS   HD3  H  N N 285 
LYS   HE2  H  N N 286 
LYS   HE3  H  N N 287 
LYS   HZ1  H  N N 288 
LYS   HZ2  H  N N 289 
LYS   HZ3  H  N N 290 
LYS   HXT  H  N N 291 
MET   N    N  N N 292 
MET   CA   C  N S 293 
MET   C    C  N N 294 
MET   O    O  N N 295 
MET   CB   C  N N 296 
MET   CG   C  N N 297 
MET   SD   S  N N 298 
MET   CE   C  N N 299 
MET   OXT  O  N N 300 
MET   H    H  N N 301 
MET   H2   H  N N 302 
MET   HA   H  N N 303 
MET   HB2  H  N N 304 
MET   HB3  H  N N 305 
MET   HG2  H  N N 306 
MET   HG3  H  N N 307 
MET   HE1  H  N N 308 
MET   HE2  H  N N 309 
MET   HE3  H  N N 310 
MET   HXT  H  N N 311 
PHE   N    N  N N 312 
PHE   CA   C  N S 313 
PHE   C    C  N N 314 
PHE   O    O  N N 315 
PHE   CB   C  N N 316 
PHE   CG   C  Y N 317 
PHE   CD1  C  Y N 318 
PHE   CD2  C  Y N 319 
PHE   CE1  C  Y N 320 
PHE   CE2  C  Y N 321 
PHE   CZ   C  Y N 322 
PHE   OXT  O  N N 323 
PHE   H    H  N N 324 
PHE   H2   H  N N 325 
PHE   HA   H  N N 326 
PHE   HB2  H  N N 327 
PHE   HB3  H  N N 328 
PHE   HD1  H  N N 329 
PHE   HD2  H  N N 330 
PHE   HE1  H  N N 331 
PHE   HE2  H  N N 332 
PHE   HZ   H  N N 333 
PHE   HXT  H  N N 334 
PRO   N    N  N N 335 
PRO   CA   C  N S 336 
PRO   C    C  N N 337 
PRO   O    O  N N 338 
PRO   CB   C  N N 339 
PRO   CG   C  N N 340 
PRO   CD   C  N N 341 
PRO   OXT  O  N N 342 
PRO   H    H  N N 343 
PRO   HA   H  N N 344 
PRO   HB2  H  N N 345 
PRO   HB3  H  N N 346 
PRO   HG2  H  N N 347 
PRO   HG3  H  N N 348 
PRO   HD2  H  N N 349 
PRO   HD3  H  N N 350 
PRO   HXT  H  N N 351 
SER   N    N  N N 352 
SER   CA   C  N S 353 
SER   C    C  N N 354 
SER   O    O  N N 355 
SER   CB   C  N N 356 
SER   OG   O  N N 357 
SER   OXT  O  N N 358 
SER   H    H  N N 359 
SER   H2   H  N N 360 
SER   HA   H  N N 361 
SER   HB2  H  N N 362 
SER   HB3  H  N N 363 
SER   HG   H  N N 364 
SER   HXT  H  N N 365 
THR   N    N  N N 366 
THR   CA   C  N S 367 
THR   C    C  N N 368 
THR   O    O  N N 369 
THR   CB   C  N R 370 
THR   OG1  O  N N 371 
THR   CG2  C  N N 372 
THR   OXT  O  N N 373 
THR   H    H  N N 374 
THR   H2   H  N N 375 
THR   HA   H  N N 376 
THR   HB   H  N N 377 
THR   HG1  H  N N 378 
THR   HG21 H  N N 379 
THR   HG22 H  N N 380 
THR   HG23 H  N N 381 
THR   HXT  H  N N 382 
TRP   N    N  N N 383 
TRP   CA   C  N S 384 
TRP   C    C  N N 385 
TRP   O    O  N N 386 
TRP   CB   C  N N 387 
TRP   CG   C  Y N 388 
TRP   CD1  C  Y N 389 
TRP   CD2  C  Y N 390 
TRP   NE1  N  Y N 391 
TRP   CE2  C  Y N 392 
TRP   CE3  C  Y N 393 
TRP   CZ2  C  Y N 394 
TRP   CZ3  C  Y N 395 
TRP   CH2  C  Y N 396 
TRP   OXT  O  N N 397 
TRP   H    H  N N 398 
TRP   H2   H  N N 399 
TRP   HA   H  N N 400 
TRP   HB2  H  N N 401 
TRP   HB3  H  N N 402 
TRP   HD1  H  N N 403 
TRP   HE1  H  N N 404 
TRP   HE3  H  N N 405 
TRP   HZ2  H  N N 406 
TRP   HZ3  H  N N 407 
TRP   HH2  H  N N 408 
TRP   HXT  H  N N 409 
TYR   N    N  N N 410 
TYR   CA   C  N S 411 
TYR   C    C  N N 412 
TYR   O    O  N N 413 
TYR   CB   C  N N 414 
TYR   CG   C  Y N 415 
TYR   CD1  C  Y N 416 
TYR   CD2  C  Y N 417 
TYR   CE1  C  Y N 418 
TYR   CE2  C  Y N 419 
TYR   CZ   C  Y N 420 
TYR   OH   O  N N 421 
TYR   OXT  O  N N 422 
TYR   H    H  N N 423 
TYR   H2   H  N N 424 
TYR   HA   H  N N 425 
TYR   HB2  H  N N 426 
TYR   HB3  H  N N 427 
TYR   HD1  H  N N 428 
TYR   HD2  H  N N 429 
TYR   HE1  H  N N 430 
TYR   HE2  H  N N 431 
TYR   HH   H  N N 432 
TYR   HXT  H  N N 433 
VAL   N    N  N N 434 
VAL   CA   C  N S 435 
VAL   C    C  N N 436 
VAL   O    O  N N 437 
VAL   CB   C  N N 438 
VAL   CG1  C  N N 439 
VAL   CG2  C  N N 440 
VAL   OXT  O  N N 441 
VAL   H    H  N N 442 
VAL   H2   H  N N 443 
VAL   HA   H  N N 444 
VAL   HB   H  N N 445 
VAL   HG11 H  N N 446 
VAL   HG12 H  N N 447 
VAL   HG13 H  N N 448 
VAL   HG21 H  N N 449 
VAL   HG22 H  N N 450 
VAL   HG23 H  N N 451 
VAL   HXT  H  N N 452 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
A1BW2 O40 C37  sing N N 1   
A1BW2 C38 C37  sing N N 2   
A1BW2 C37 C36  sing N N 3   
A1BW2 C37 C39  sing N N 4   
A1BW2 C36 N35  sing N N 5   
A1BW2 N35 C33  sing N N 6   
A1BW2 O9  C8   doub N N 7   
A1BW2 N11 C10  sing Y N 8   
A1BW2 N11 C12  doub Y N 9   
A1BW2 C8  C10  sing N N 10  
A1BW2 C8  N7   sing N N 11  
A1BW2 C33 C12  sing N N 12  
A1BW2 C33 O34  doub N N 13  
A1BW2 C6  N7   sing N N 14  
A1BW2 C6  C5   sing N N 15  
A1BW2 C10 C14  doub Y N 16  
A1BW2 C12 S13  sing Y N 17  
A1BW2 N7  C2   sing N N 18  
A1BW2 C1  C2   sing N N 19  
A1BW2 C5  C4   sing N N 20  
A1BW2 C14 S13  sing Y N 21  
A1BW2 C14 C15  sing N N 22  
A1BW2 C2  C4   sing N N 23  
A1BW2 C16 C15  doub Y N 24  
A1BW2 C16 C17  sing Y N 25  
A1BW2 C15 C21  sing Y N 26  
A1BW2 C17 C18  doub Y N 27  
A1BW2 F27 C25  sing N N 28  
A1BW2 F30 C29  sing N N 29  
A1BW2 C21 C19  doub Y N 30  
A1BW2 C21 CL22 sing N N 31  
A1BW2 C18 C19  sing Y N 32  
A1BW2 C18 C23  sing N N 33  
A1BW2 C25 F26  sing N N 34  
A1BW2 C25 C23  sing N N 35  
A1BW2 C25 F28  sing N N 36  
A1BW2 C29 C23  sing N N 37  
A1BW2 C29 F31  sing N N 38  
A1BW2 C29 F32  sing N N 39  
A1BW2 C19 CL20 sing N N 40  
A1BW2 C23 O24  sing N N 41  
A1BW2 C16 H50  sing N N 42  
A1BW2 C17 H51  sing N N 43  
A1BW2 C5  H46  sing N N 44  
A1BW2 C5  H47  sing N N 45  
A1BW2 C4  H45  sing N N 46  
A1BW2 C4  H44  sing N N 47  
A1BW2 C6  H48  sing N N 48  
A1BW2 C6  H49  sing N N 49  
A1BW2 C2  H3   sing N N 50  
A1BW2 C1  H41  sing N N 51  
A1BW2 C1  H42  sing N N 52  
A1BW2 C1  H43  sing N N 53  
A1BW2 C38 H56  sing N N 54  
A1BW2 C38 H58  sing N N 55  
A1BW2 C38 H57  sing N N 56  
A1BW2 C39 H60  sing N N 57  
A1BW2 C39 H61  sing N N 58  
A1BW2 C39 H59  sing N N 59  
A1BW2 C36 H54  sing N N 60  
A1BW2 C36 H55  sing N N 61  
A1BW2 N35 H53  sing N N 62  
A1BW2 O24 H52  sing N N 63  
A1BW2 O40 H62  sing N N 64  
ALA   N   CA   sing N N 65  
ALA   N   H    sing N N 66  
ALA   N   H2   sing N N 67  
ALA   CA  C    sing N N 68  
ALA   CA  CB   sing N N 69  
ALA   CA  HA   sing N N 70  
ALA   C   O    doub N N 71  
ALA   C   OXT  sing N N 72  
ALA   CB  HB1  sing N N 73  
ALA   CB  HB2  sing N N 74  
ALA   CB  HB3  sing N N 75  
ALA   OXT HXT  sing N N 76  
ARG   N   CA   sing N N 77  
ARG   N   H    sing N N 78  
ARG   N   H2   sing N N 79  
ARG   CA  C    sing N N 80  
ARG   CA  CB   sing N N 81  
ARG   CA  HA   sing N N 82  
ARG   C   O    doub N N 83  
ARG   C   OXT  sing N N 84  
ARG   CB  CG   sing N N 85  
ARG   CB  HB2  sing N N 86  
ARG   CB  HB3  sing N N 87  
ARG   CG  CD   sing N N 88  
ARG   CG  HG2  sing N N 89  
ARG   CG  HG3  sing N N 90  
ARG   CD  NE   sing N N 91  
ARG   CD  HD2  sing N N 92  
ARG   CD  HD3  sing N N 93  
ARG   NE  CZ   sing N N 94  
ARG   NE  HE   sing N N 95  
ARG   CZ  NH1  sing N N 96  
ARG   CZ  NH2  doub N N 97  
ARG   NH1 HH11 sing N N 98  
ARG   NH1 HH12 sing N N 99  
ARG   NH2 HH21 sing N N 100 
ARG   NH2 HH22 sing N N 101 
ARG   OXT HXT  sing N N 102 
ASN   N   CA   sing N N 103 
ASN   N   H    sing N N 104 
ASN   N   H2   sing N N 105 
ASN   CA  C    sing N N 106 
ASN   CA  CB   sing N N 107 
ASN   CA  HA   sing N N 108 
ASN   C   O    doub N N 109 
ASN   C   OXT  sing N N 110 
ASN   CB  CG   sing N N 111 
ASN   CB  HB2  sing N N 112 
ASN   CB  HB3  sing N N 113 
ASN   CG  OD1  doub N N 114 
ASN   CG  ND2  sing N N 115 
ASN   ND2 HD21 sing N N 116 
ASN   ND2 HD22 sing N N 117 
ASN   OXT HXT  sing N N 118 
ASP   N   CA   sing N N 119 
ASP   N   H    sing N N 120 
ASP   N   H2   sing N N 121 
ASP   CA  C    sing N N 122 
ASP   CA  CB   sing N N 123 
ASP   CA  HA   sing N N 124 
ASP   C   O    doub N N 125 
ASP   C   OXT  sing N N 126 
ASP   CB  CG   sing N N 127 
ASP   CB  HB2  sing N N 128 
ASP   CB  HB3  sing N N 129 
ASP   CG  OD1  doub N N 130 
ASP   CG  OD2  sing N N 131 
ASP   OD2 HD2  sing N N 132 
ASP   OXT HXT  sing N N 133 
CYS   N   CA   sing N N 134 
CYS   N   H    sing N N 135 
CYS   N   H2   sing N N 136 
CYS   CA  C    sing N N 137 
CYS   CA  CB   sing N N 138 
CYS   CA  HA   sing N N 139 
CYS   C   O    doub N N 140 
CYS   C   OXT  sing N N 141 
CYS   CB  SG   sing N N 142 
CYS   CB  HB2  sing N N 143 
CYS   CB  HB3  sing N N 144 
CYS   SG  HG   sing N N 145 
CYS   OXT HXT  sing N N 146 
GLN   N   CA   sing N N 147 
GLN   N   H    sing N N 148 
GLN   N   H2   sing N N 149 
GLN   CA  C    sing N N 150 
GLN   CA  CB   sing N N 151 
GLN   CA  HA   sing N N 152 
GLN   C   O    doub N N 153 
GLN   C   OXT  sing N N 154 
GLN   CB  CG   sing N N 155 
GLN   CB  HB2  sing N N 156 
GLN   CB  HB3  sing N N 157 
GLN   CG  CD   sing N N 158 
GLN   CG  HG2  sing N N 159 
GLN   CG  HG3  sing N N 160 
GLN   CD  OE1  doub N N 161 
GLN   CD  NE2  sing N N 162 
GLN   NE2 HE21 sing N N 163 
GLN   NE2 HE22 sing N N 164 
GLN   OXT HXT  sing N N 165 
GLU   N   CA   sing N N 166 
GLU   N   H    sing N N 167 
GLU   N   H2   sing N N 168 
GLU   CA  C    sing N N 169 
GLU   CA  CB   sing N N 170 
GLU   CA  HA   sing N N 171 
GLU   C   O    doub N N 172 
GLU   C   OXT  sing N N 173 
GLU   CB  CG   sing N N 174 
GLU   CB  HB2  sing N N 175 
GLU   CB  HB3  sing N N 176 
GLU   CG  CD   sing N N 177 
GLU   CG  HG2  sing N N 178 
GLU   CG  HG3  sing N N 179 
GLU   CD  OE1  doub N N 180 
GLU   CD  OE2  sing N N 181 
GLU   OE2 HE2  sing N N 182 
GLU   OXT HXT  sing N N 183 
GLY   N   CA   sing N N 184 
GLY   N   H    sing N N 185 
GLY   N   H2   sing N N 186 
GLY   CA  C    sing N N 187 
GLY   CA  HA2  sing N N 188 
GLY   CA  HA3  sing N N 189 
GLY   C   O    doub N N 190 
GLY   C   OXT  sing N N 191 
GLY   OXT HXT  sing N N 192 
HIS   N   CA   sing N N 193 
HIS   N   H    sing N N 194 
HIS   N   H2   sing N N 195 
HIS   CA  C    sing N N 196 
HIS   CA  CB   sing N N 197 
HIS   CA  HA   sing N N 198 
HIS   C   O    doub N N 199 
HIS   C   OXT  sing N N 200 
HIS   CB  CG   sing N N 201 
HIS   CB  HB2  sing N N 202 
HIS   CB  HB3  sing N N 203 
HIS   CG  ND1  sing Y N 204 
HIS   CG  CD2  doub Y N 205 
HIS   ND1 CE1  doub Y N 206 
HIS   ND1 HD1  sing N N 207 
HIS   CD2 NE2  sing Y N 208 
HIS   CD2 HD2  sing N N 209 
HIS   CE1 NE2  sing Y N 210 
HIS   CE1 HE1  sing N N 211 
HIS   NE2 HE2  sing N N 212 
HIS   OXT HXT  sing N N 213 
HOH   O   H1   sing N N 214 
HOH   O   H2   sing N N 215 
ILE   N   CA   sing N N 216 
ILE   N   H    sing N N 217 
ILE   N   H2   sing N N 218 
ILE   CA  C    sing N N 219 
ILE   CA  CB   sing N N 220 
ILE   CA  HA   sing N N 221 
ILE   C   O    doub N N 222 
ILE   C   OXT  sing N N 223 
ILE   CB  CG1  sing N N 224 
ILE   CB  CG2  sing N N 225 
ILE   CB  HB   sing N N 226 
ILE   CG1 CD1  sing N N 227 
ILE   CG1 HG12 sing N N 228 
ILE   CG1 HG13 sing N N 229 
ILE   CG2 HG21 sing N N 230 
ILE   CG2 HG22 sing N N 231 
ILE   CG2 HG23 sing N N 232 
ILE   CD1 HD11 sing N N 233 
ILE   CD1 HD12 sing N N 234 
ILE   CD1 HD13 sing N N 235 
ILE   OXT HXT  sing N N 236 
LEU   N   CA   sing N N 237 
LEU   N   H    sing N N 238 
LEU   N   H2   sing N N 239 
LEU   CA  C    sing N N 240 
LEU   CA  CB   sing N N 241 
LEU   CA  HA   sing N N 242 
LEU   C   O    doub N N 243 
LEU   C   OXT  sing N N 244 
LEU   CB  CG   sing N N 245 
LEU   CB  HB2  sing N N 246 
LEU   CB  HB3  sing N N 247 
LEU   CG  CD1  sing N N 248 
LEU   CG  CD2  sing N N 249 
LEU   CG  HG   sing N N 250 
LEU   CD1 HD11 sing N N 251 
LEU   CD1 HD12 sing N N 252 
LEU   CD1 HD13 sing N N 253 
LEU   CD2 HD21 sing N N 254 
LEU   CD2 HD22 sing N N 255 
LEU   CD2 HD23 sing N N 256 
LEU   OXT HXT  sing N N 257 
LYS   N   CA   sing N N 258 
LYS   N   H    sing N N 259 
LYS   N   H2   sing N N 260 
LYS   CA  C    sing N N 261 
LYS   CA  CB   sing N N 262 
LYS   CA  HA   sing N N 263 
LYS   C   O    doub N N 264 
LYS   C   OXT  sing N N 265 
LYS   CB  CG   sing N N 266 
LYS   CB  HB2  sing N N 267 
LYS   CB  HB3  sing N N 268 
LYS   CG  CD   sing N N 269 
LYS   CG  HG2  sing N N 270 
LYS   CG  HG3  sing N N 271 
LYS   CD  CE   sing N N 272 
LYS   CD  HD2  sing N N 273 
LYS   CD  HD3  sing N N 274 
LYS   CE  NZ   sing N N 275 
LYS   CE  HE2  sing N N 276 
LYS   CE  HE3  sing N N 277 
LYS   NZ  HZ1  sing N N 278 
LYS   NZ  HZ2  sing N N 279 
LYS   NZ  HZ3  sing N N 280 
LYS   OXT HXT  sing N N 281 
MET   N   CA   sing N N 282 
MET   N   H    sing N N 283 
MET   N   H2   sing N N 284 
MET   CA  C    sing N N 285 
MET   CA  CB   sing N N 286 
MET   CA  HA   sing N N 287 
MET   C   O    doub N N 288 
MET   C   OXT  sing N N 289 
MET   CB  CG   sing N N 290 
MET   CB  HB2  sing N N 291 
MET   CB  HB3  sing N N 292 
MET   CG  SD   sing N N 293 
MET   CG  HG2  sing N N 294 
MET   CG  HG3  sing N N 295 
MET   SD  CE   sing N N 296 
MET   CE  HE1  sing N N 297 
MET   CE  HE2  sing N N 298 
MET   CE  HE3  sing N N 299 
MET   OXT HXT  sing N N 300 
PHE   N   CA   sing N N 301 
PHE   N   H    sing N N 302 
PHE   N   H2   sing N N 303 
PHE   CA  C    sing N N 304 
PHE   CA  CB   sing N N 305 
PHE   CA  HA   sing N N 306 
PHE   C   O    doub N N 307 
PHE   C   OXT  sing N N 308 
PHE   CB  CG   sing N N 309 
PHE   CB  HB2  sing N N 310 
PHE   CB  HB3  sing N N 311 
PHE   CG  CD1  doub Y N 312 
PHE   CG  CD2  sing Y N 313 
PHE   CD1 CE1  sing Y N 314 
PHE   CD1 HD1  sing N N 315 
PHE   CD2 CE2  doub Y N 316 
PHE   CD2 HD2  sing N N 317 
PHE   CE1 CZ   doub Y N 318 
PHE   CE1 HE1  sing N N 319 
PHE   CE2 CZ   sing Y N 320 
PHE   CE2 HE2  sing N N 321 
PHE   CZ  HZ   sing N N 322 
PHE   OXT HXT  sing N N 323 
PRO   N   CA   sing N N 324 
PRO   N   CD   sing N N 325 
PRO   N   H    sing N N 326 
PRO   CA  C    sing N N 327 
PRO   CA  CB   sing N N 328 
PRO   CA  HA   sing N N 329 
PRO   C   O    doub N N 330 
PRO   C   OXT  sing N N 331 
PRO   CB  CG   sing N N 332 
PRO   CB  HB2  sing N N 333 
PRO   CB  HB3  sing N N 334 
PRO   CG  CD   sing N N 335 
PRO   CG  HG2  sing N N 336 
PRO   CG  HG3  sing N N 337 
PRO   CD  HD2  sing N N 338 
PRO   CD  HD3  sing N N 339 
PRO   OXT HXT  sing N N 340 
SER   N   CA   sing N N 341 
SER   N   H    sing N N 342 
SER   N   H2   sing N N 343 
SER   CA  C    sing N N 344 
SER   CA  CB   sing N N 345 
SER   CA  HA   sing N N 346 
SER   C   O    doub N N 347 
SER   C   OXT  sing N N 348 
SER   CB  OG   sing N N 349 
SER   CB  HB2  sing N N 350 
SER   CB  HB3  sing N N 351 
SER   OG  HG   sing N N 352 
SER   OXT HXT  sing N N 353 
THR   N   CA   sing N N 354 
THR   N   H    sing N N 355 
THR   N   H2   sing N N 356 
THR   CA  C    sing N N 357 
THR   CA  CB   sing N N 358 
THR   CA  HA   sing N N 359 
THR   C   O    doub N N 360 
THR   C   OXT  sing N N 361 
THR   CB  OG1  sing N N 362 
THR   CB  CG2  sing N N 363 
THR   CB  HB   sing N N 364 
THR   OG1 HG1  sing N N 365 
THR   CG2 HG21 sing N N 366 
THR   CG2 HG22 sing N N 367 
THR   CG2 HG23 sing N N 368 
THR   OXT HXT  sing N N 369 
TRP   N   CA   sing N N 370 
TRP   N   H    sing N N 371 
TRP   N   H2   sing N N 372 
TRP   CA  C    sing N N 373 
TRP   CA  CB   sing N N 374 
TRP   CA  HA   sing N N 375 
TRP   C   O    doub N N 376 
TRP   C   OXT  sing N N 377 
TRP   CB  CG   sing N N 378 
TRP   CB  HB2  sing N N 379 
TRP   CB  HB3  sing N N 380 
TRP   CG  CD1  doub Y N 381 
TRP   CG  CD2  sing Y N 382 
TRP   CD1 NE1  sing Y N 383 
TRP   CD1 HD1  sing N N 384 
TRP   CD2 CE2  doub Y N 385 
TRP   CD2 CE3  sing Y N 386 
TRP   NE1 CE2  sing Y N 387 
TRP   NE1 HE1  sing N N 388 
TRP   CE2 CZ2  sing Y N 389 
TRP   CE3 CZ3  doub Y N 390 
TRP   CE3 HE3  sing N N 391 
TRP   CZ2 CH2  doub Y N 392 
TRP   CZ2 HZ2  sing N N 393 
TRP   CZ3 CH2  sing Y N 394 
TRP   CZ3 HZ3  sing N N 395 
TRP   CH2 HH2  sing N N 396 
TRP   OXT HXT  sing N N 397 
TYR   N   CA   sing N N 398 
TYR   N   H    sing N N 399 
TYR   N   H2   sing N N 400 
TYR   CA  C    sing N N 401 
TYR   CA  CB   sing N N 402 
TYR   CA  HA   sing N N 403 
TYR   C   O    doub N N 404 
TYR   C   OXT  sing N N 405 
TYR   CB  CG   sing N N 406 
TYR   CB  HB2  sing N N 407 
TYR   CB  HB3  sing N N 408 
TYR   CG  CD1  doub Y N 409 
TYR   CG  CD2  sing Y N 410 
TYR   CD1 CE1  sing Y N 411 
TYR   CD1 HD1  sing N N 412 
TYR   CD2 CE2  doub Y N 413 
TYR   CD2 HD2  sing N N 414 
TYR   CE1 CZ   doub Y N 415 
TYR   CE1 HE1  sing N N 416 
TYR   CE2 CZ   sing Y N 417 
TYR   CE2 HE2  sing N N 418 
TYR   CZ  OH   sing N N 419 
TYR   OH  HH   sing N N 420 
TYR   OXT HXT  sing N N 421 
VAL   N   CA   sing N N 422 
VAL   N   H    sing N N 423 
VAL   N   H2   sing N N 424 
VAL   CA  C    sing N N 425 
VAL   CA  CB   sing N N 426 
VAL   CA  HA   sing N N 427 
VAL   C   O    doub N N 428 
VAL   C   OXT  sing N N 429 
VAL   CB  CG1  sing N N 430 
VAL   CB  CG2  sing N N 431 
VAL   CB  HB   sing N N 432 
VAL   CG1 HG11 sing N N 433 
VAL   CG1 HG12 sing N N 434 
VAL   CG1 HG13 sing N N 435 
VAL   CG2 HG21 sing N N 436 
VAL   CG2 HG22 sing N N 437 
VAL   CG2 HG23 sing N N 438 
VAL   OXT HXT  sing N N 439 
# 
_pdbx_audit_support.funding_organization   'Not funded' 
_pdbx_audit_support.country                ? 
_pdbx_audit_support.grant_number           ? 
_pdbx_audit_support.ordinal                1 
# 
_atom_sites.entry_id                    9N9L 
_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]   0.024095 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000581 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.007758 
_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]   0.019299 
_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  
H  
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    . ALA   A 1 1   ? -22.118 1.731   80.760 1.00 35.19 ? 265 ALA   A N    1 
ATOM   2    C  CA   . ALA   A 1 1   ? -20.831 1.709   80.013 1.00 38.38 ? 265 ALA   A CA   1 
ATOM   3    C  C    . ALA   A 1 1   ? -20.465 0.239   79.773 1.00 35.20 ? 265 ALA   A C    1 
ATOM   4    O  O    . ALA   A 1 1   ? -19.706 -0.373  80.528 1.00 33.70 ? 265 ALA   A O    1 
ATOM   5    C  CB   . ALA   A 1 1   ? -19.828 2.401   80.753 1.00 30.54 ? 265 ALA   A CB   1 
ATOM   6    N  N    . SER   A 1 2   ? -21.118 -0.343  78.770 1.00 33.77 ? 266 SER   A N    1 
ATOM   7    C  CA   . SER   A 1 2   ? -21.181 -1.799  78.597 1.00 35.02 ? 266 SER   A CA   1 
ATOM   8    C  C    . SER   A 1 2   ? -19.985 -2.341  77.834 1.00 32.91 ? 266 SER   A C    1 
ATOM   9    O  O    . SER   A 1 2   ? -19.239 -1.579  77.228 1.00 32.13 ? 266 SER   A O    1 
ATOM   10   C  CB   . SER   A 1 2   ? -22.458 -2.194  77.850 1.00 37.35 ? 266 SER   A CB   1 
ATOM   11   O  OG   . SER   A 1 2   ? -22.389 -1.808  76.487 1.00 38.48 ? 266 SER   A OG   1 
ATOM   12   N  N    . LEU   A 1 3   ? -19.848 -3.667  77.844 1.00 32.95 ? 267 LEU   A N    1 
ATOM   13   C  CA   . LEU   A 1 3   ? -18.801 -4.302  77.077 1.00 28.56 ? 267 LEU   A CA   1 
ATOM   14   C  C    . LEU   A 1 3   ? -19.018 -3.999  75.608 1.00 28.16 ? 267 LEU   A C    1 
ATOM   15   O  O    . LEU   A 1 3   ? -18.073 -3.623  74.918 1.00 29.90 ? 267 LEU   A O    1 
ATOM   16   C  CB   . LEU   A 1 3   ? -18.745 -5.817  77.343 1.00 26.17 ? 267 LEU   A CB   1 
ATOM   17   C  CG   . LEU   A 1 3   ? -17.822 -6.652  76.442 1.00 30.14 ? 267 LEU   A CG   1 
ATOM   18   C  CD1  . LEU   A 1 3   ? -16.416 -6.129  76.502 1.00 27.57 ? 267 LEU   A CD1  1 
ATOM   19   C  CD2  . LEU   A 1 3   ? -17.815 -8.167  76.790 1.00 32.25 ? 267 LEU   A CD2  1 
ATOM   20   N  N    . THR   A 1 4   ? -20.258 -4.086  75.132 1.00 34.62 ? 268 THR   A N    1 
ATOM   21   C  CA   . THR   A 1 4   ? -20.489 -3.788  73.728 1.00 35.59 ? 268 THR   A CA   1 
ATOM   22   C  C    . THR   A 1 4   ? -20.170 -2.336  73.392 1.00 31.80 ? 268 THR   A C    1 
ATOM   23   O  O    . THR   A 1 4   ? -19.617 -2.028  72.325 1.00 32.06 ? 268 THR   A O    1 
ATOM   24   C  CB   . THR   A 1 4   ? -21.962 -4.141  73.333 1.00 35.07 ? 268 THR   A CB   1 
ATOM   25   O  OG1  . THR   A 1 4   ? -22.134 -5.559  73.458 1.00 42.72 ? 268 THR   A OG1  1 
ATOM   26   C  CG2  . THR   A 1 4   ? -22.187 -3.770  71.930 1.00 41.25 ? 268 THR   A CG2  1 
ATOM   27   N  N    . GLU   A 1 5   ? -20.504 -1.423  74.295 1.00 32.26 ? 269 GLU   A N    1 
ATOM   28   C  CA   . GLU   A 1 5   ? -20.146 -0.006  74.103 1.00 29.05 ? 269 GLU   A CA   1 
ATOM   29   C  C    . GLU   A 1 5   ? -18.632 0.238   74.029 1.00 29.50 ? 269 GLU   A C    1 
ATOM   30   O  O    . GLU   A 1 5   ? -18.174 1.035   73.199 1.00 28.68 ? 269 GLU   A O    1 
ATOM   31   C  CB   . GLU   A 1 5   ? -20.799 0.829   75.216 1.00 31.02 ? 269 GLU   A CB   1 
ATOM   32   C  CG   . GLU   A 1 5   ? -22.313 0.943   74.964 1.00 39.75 ? 269 GLU   A CG   1 
ATOM   33   C  CD   . GLU   A 1 5   ? -23.134 1.499   76.120 1.00 48.11 ? 269 GLU   A CD   1 
ATOM   34   O  OE1  . GLU   A 1 5   ? -22.599 1.716   77.222 1.00 45.44 ? 269 GLU   A OE1  1 
ATOM   35   O  OE2  . GLU   A 1 5   ? -24.354 1.721   75.911 1.00 45.96 ? 269 GLU   A OE2  1 
ATOM   36   N  N    . ILE   A 1 6   ? -17.869 -0.490  74.842 1.00 25.91 ? 270 ILE   A N    1 
ATOM   37   C  CA   . ILE   A 1 6   ? -16.429 -0.314  74.835 1.00 24.15 ? 270 ILE   A CA   1 
ATOM   38   C  C    . ILE   A 1 6   ? -15.858 -0.931  73.546 1.00 29.57 ? 270 ILE   A C    1 
ATOM   39   O  O    . ILE   A 1 6   ? -14.939 -0.368  72.931 1.00 25.13 ? 270 ILE   A O    1 
ATOM   40   C  CB   . ILE   A 1 6   ? -15.779 -0.895  76.098 1.00 26.47 ? 270 ILE   A CB   1 
ATOM   41   C  CG1  . ILE   A 1 6   ? -16.072 0.017   77.296 1.00 31.15 ? 270 ILE   A CG1  1 
ATOM   42   C  CG2  . ILE   A 1 6   ? -14.270 -1.027  75.917 1.00 29.08 ? 270 ILE   A CG2  1 
ATOM   43   C  CD1  . ILE   A 1 6   ? -15.345 1.422   77.246 1.00 30.12 ? 270 ILE   A CD1  1 
ATOM   44   N  N    . GLU   A 1 7   ? -16.396 -2.065  73.123 1.00 30.38 ? 271 GLU   A N    1 
ATOM   45   C  CA   . GLU   A 1 7   ? -15.972 -2.682  71.864 1.00 27.01 ? 271 GLU   A CA   1 
ATOM   46   C  C    . GLU   A 1 7   ? -16.249 -1.752  70.695 1.00 30.62 ? 271 GLU   A C    1 
ATOM   47   O  O    . GLU   A 1 7   ? -15.400 -1.578  69.829 1.00 28.69 ? 271 GLU   A O    1 
ATOM   48   C  CB   . GLU   A 1 7   ? -16.673 -4.024  71.651 1.00 26.38 ? 271 GLU   A CB   1 
ATOM   49   C  CG   . GLU   A 1 7   ? -16.217 -5.084  72.664 1.00 30.84 ? 271 GLU   A CG   1 
ATOM   50   C  CD   . GLU   A 1 7   ? -16.990 -6.412  72.575 1.00 31.72 ? 271 GLU   A CD   1 
ATOM   51   O  OE1  . GLU   A 1 7   ? -18.215 -6.438  72.199 1.00 33.61 ? 271 GLU   A OE1  1 
ATOM   52   O  OE2  . GLU   A 1 7   ? -16.358 -7.466  72.901 1.00 32.99 ? 271 GLU   A OE2  1 
ATOM   53   N  N    . HIS   A 1 8   ? -17.442 -1.169  70.644 1.00 29.66 ? 272 HIS   A N    1 
ATOM   54   C  CA   . HIS   A 1 8   ? -17.755 -0.241  69.559 1.00 30.44 ? 272 HIS   A CA   1 
ATOM   55   C  C    . HIS   A 1 8   ? -16.867 1.019   69.617 1.00 32.90 ? 272 HIS   A C    1 
ATOM   56   O  O    . HIS   A 1 8   ? -16.506 1.600   68.591 1.00 32.43 ? 272 HIS   A O    1 
ATOM   57   C  CB   . HIS   A 1 8   ? -19.225 0.124   69.616 1.00 30.42 ? 272 HIS   A CB   1 
ATOM   58   C  CG   . HIS   A 1 8   ? -20.117 -0.998  69.202 1.00 42.01 ? 272 HIS   A CG   1 
ATOM   59   N  ND1  . HIS   A 1 8   ? -19.622 -2.204  68.761 1.00 48.13 ? 272 HIS   A ND1  1 
ATOM   60   C  CD2  . HIS   A 1 8   ? -21.466 -1.102  69.161 1.00 48.28 ? 272 HIS   A CD2  1 
ATOM   61   C  CE1  . HIS   A 1 8   ? -20.628 -3.008  68.462 1.00 52.67 ? 272 HIS   A CE1  1 
ATOM   62   N  NE2  . HIS   A 1 8   ? -21.756 -2.361  68.691 1.00 55.57 ? 272 HIS   A NE2  1 
ATOM   63   N  N    . LEU   A 1 9   ? -16.459 1.422   70.818 1.00 27.04 ? 273 LEU   A N    1 
ATOM   64   C  CA   . LEU   A 1 9   ? -15.612 2.593   70.963 1.00 29.49 ? 273 LEU   A CA   1 
ATOM   65   C  C    . LEU   A 1 9   ? -14.234 2.313   70.400 1.00 25.13 ? 273 LEU   A C    1 
ATOM   66   O  O    . LEU   A 1 9   ? -13.700 3.117   69.632 1.00 27.21 ? 273 LEU   A O    1 
ATOM   67   C  CB   . LEU   A 1 9   ? -15.502 3.030   72.428 1.00 25.52 ? 273 LEU   A CB   1 
ATOM   68   C  CG   . LEU   A 1 9   ? -14.639 4.272   72.618 1.00 29.34 ? 273 LEU   A CG   1 
ATOM   69   C  CD1  . LEU   A 1 9   ? -15.094 5.490   71.782 1.00 26.68 ? 273 LEU   A CD1  1 
ATOM   70   C  CD2  . LEU   A 1 9   ? -14.535 4.638   74.099 1.00 32.53 ? 273 LEU   A CD2  1 
ATOM   71   N  N    . VAL   A 1 10  ? -13.679 1.145   70.727 1.00 25.24 ? 274 VAL   A N    1 
ATOM   72   C  CA   . VAL   A 1 10  ? -12.413 0.749   70.095 1.00 25.35 ? 274 VAL   A CA   1 
ATOM   73   C  C    . VAL   A 1 10  ? -12.553 0.781   68.571 1.00 26.53 ? 274 VAL   A C    1 
ATOM   74   O  O    . VAL   A 1 10  ? -11.732 1.381   67.891 1.00 26.36 ? 274 VAL   A O    1 
ATOM   75   C  CB   . VAL   A 1 10  ? -11.939 -0.628  70.541 1.00 27.59 ? 274 VAL   A CB   1 
ATOM   76   C  CG1  . VAL   A 1 10  ? -10.726 -1.061  69.726 1.00 26.37 ? 274 VAL   A CG1  1 
ATOM   77   C  CG2  . VAL   A 1 10  ? -11.622 -0.614  71.995 1.00 24.80 ? 274 VAL   A CG2  1 
ATOM   78   N  N    . GLN   A 1 11  ? -13.604 0.155   68.050 1.00 26.45 ? 275 GLN   A N    1 
ATOM   79   C  CA   . GLN   A 1 11  ? -13.810 0.105   66.621 1.00 25.55 ? 275 GLN   A CA   1 
ATOM   80   C  C    . GLN   A 1 11  ? -13.932 1.506   66.018 1.00 26.66 ? 275 GLN   A C    1 
ATOM   81   O  O    . GLN   A 1 11  ? -13.423 1.738   64.931 1.00 28.63 ? 275 GLN   A O    1 
ATOM   82   C  CB   . GLN   A 1 11  ? -15.069 -0.722  66.275 1.00 27.91 ? 275 GLN   A CB   1 
ATOM   83   C  CG   . GLN   A 1 11  ? -14.874 -2.195  66.547 1.00 42.04 ? 275 GLN   A CG   1 
ATOM   84   C  CD   . GLN   A 1 11  ? -16.206 -2.969  66.583 1.00 53.28 ? 275 GLN   A CD   1 
ATOM   85   O  OE1  . GLN   A 1 11  ? -17.213 -2.530  66.020 1.00 54.59 ? 275 GLN   A OE1  1 
ATOM   86   N  NE2  . GLN   A 1 11  ? -16.207 -4.114  67.253 1.00 57.90 ? 275 GLN   A NE2  1 
ATOM   87   N  N    . SER   A 1 12  ? -14.653 2.423   66.673 1.00 27.02 ? 276 SER   A N    1 
ATOM   88   C  CA   . SER   A 1 12  ? -14.851 3.723   66.025 1.00 24.87 ? 276 SER   A CA   1 
ATOM   89   C  C    . SER   A 1 12  ? -13.538 4.512   66.032 1.00 26.90 ? 276 SER   A C    1 
ATOM   90   O  O    . SER   A 1 12  ? -13.211 5.184   65.053 1.00 29.23 ? 276 SER   A O    1 
ATOM   91   C  CB   . SER   A 1 12  ? -15.969 4.533   66.680 1.00 39.22 ? 276 SER   A CB   1 
ATOM   92   O  OG   . SER   A 1 12  ? -15.726 4.764   68.045 1.00 46.69 ? 276 SER   A OG   1 
ATOM   93   N  N    . VAL   A 1 13  ? -12.775 4.390   67.120 1.00 26.72 ? 277 VAL   A N    1 
ATOM   94   C  CA   . VAL   A 1 13  ? -11.547 5.161   67.223 1.00 24.88 ? 277 VAL   A CA   1 
ATOM   95   C  C    . VAL   A 1 13  ? -10.570 4.669   66.181 1.00 23.94 ? 277 VAL   A C    1 
ATOM   96   O  O    . VAL   A 1 13  ? -9.896  5.478   65.530 1.00 25.17 ? 277 VAL   A O    1 
ATOM   97   C  CB   . VAL   A 1 13  ? -10.943 5.087   68.638 1.00 26.74 ? 277 VAL   A CB   1 
ATOM   98   C  CG1  . VAL   A 1 13  ? -9.519  5.693   68.659 1.00 26.97 ? 277 VAL   A CG1  1 
ATOM   99   C  CG2  . VAL   A 1 13  ? -11.853 5.767   69.633 1.00 27.66 ? 277 VAL   A CG2  1 
ATOM   100  N  N    . CYS   A 1 14  ? -10.506 3.349   66.005 1.00 22.91 ? 278 CYS   A N    1 
ATOM   101  C  CA   . CYS   A 1 14  ? -9.645  2.756   65.005 1.00 22.49 ? 278 CYS   A CA   1 
ATOM   102  C  C    . CYS   A 1 14  ? -10.034 3.175   63.591 1.00 25.50 ? 278 CYS   A C    1 
ATOM   103  O  O    . CYS   A 1 14  ? -9.171  3.465   62.774 1.00 27.72 ? 278 CYS   A O    1 
ATOM   104  C  CB   . CYS   A 1 14  ? -9.639  1.234   65.136 1.00 22.91 ? 278 CYS   A CB   1 
ATOM   105  S  SG   . CYS   A 1 14  ? -8.700  0.699   66.638 1.00 29.84 ? 278 CYS   A SG   1 
ATOM   106  N  N    . LYS   A 1 15  ? -11.341 3.197   63.299 1.00 26.21 ? 279 LYS   A N    1 
ATOM   107  C  CA   . LYS   A 1 15  ? -11.836 3.637   62.005 1.00 27.60 ? 279 LYS   A CA   1 
ATOM   108  C  C    . LYS   A 1 15  ? -11.484 5.097   61.739 1.00 24.37 ? 279 LYS   A C    1 
ATOM   109  O  O    . LYS   A 1 15  ? -11.036 5.444   60.645 1.00 28.18 ? 279 LYS   A O    1 
ATOM   110  C  CB   . LYS   A 1 15  ? -13.356 3.448   61.932 1.00 27.24 ? 279 LYS   A CB   1 
ATOM   111  C  CG   . LYS   A 1 15  ? -14.013 3.968   60.625 1.00 32.19 ? 279 LYS   A CG   1 
ATOM   112  C  CD   . LYS   A 1 15  ? -15.540 3.698   60.660 1.00 41.27 ? 279 LYS   A CD   1 
ATOM   113  C  CE   . LYS   A 1 15  ? -16.331 4.547   59.658 1.00 50.28 ? 279 LYS   A CE   1 
ATOM   114  N  NZ   . LYS   A 1 15  ? -17.808 4.346   59.858 1.00 61.51 ? 279 LYS   A NZ   1 
ATOM   115  N  N    . SER   A 1 16  ? -11.647 5.931   62.754 1.00 24.65 ? 280 SER   A N    1 
ATOM   116  C  CA   . SER   A 1 16  ? -11.352 7.375   62.633 1.00 23.25 ? 280 SER   A CA   1 
ATOM   117  C  C    . SER   A 1 16  ? -9.888  7.559   62.258 1.00 22.44 ? 280 SER   A C    1 
ATOM   118  O  O    . SER   A 1 16  ? -9.570  8.321   61.362 1.00 25.83 ? 280 SER   A O    1 
ATOM   119  C  CB   . SER   A 1 16  ? -11.669 8.113   63.938 1.00 27.67 ? 280 SER   A CB   1 
ATOM   120  O  OG   . SER   A 1 16  ? -13.084 8.101   64.163 1.00 33.55 ? 280 SER   A OG   1 
ATOM   121  N  N    . TYR   A 1 17  ? -9.034  6.785   62.918 1.00 22.73 ? 281 TYR   A N    1 
ATOM   122  C  CA   . TYR   A 1 17  ? -7.609  6.816   62.637 1.00 21.91 ? 281 TYR   A CA   1 
ATOM   123  C  C    . TYR   A 1 17  ? -7.324  6.354   61.189 1.00 23.30 ? 281 TYR   A C    1 
ATOM   124  O  O    . TYR   A 1 17  ? -6.610  7.037   60.454 1.00 22.15 ? 281 TYR   A O    1 
ATOM   125  C  CB   . TYR   A 1 17  ? -6.819  5.967   63.649 1.00 20.72 ? 281 TYR   A CB   1 
ATOM   126  C  CG   . TYR   A 1 17  ? -5.358  5.983   63.290 1.00 26.27 ? 281 TYR   A CG   1 
ATOM   127  C  CD1  . TYR   A 1 17  ? -4.626  7.123   63.481 1.00 30.37 ? 281 TYR   A CD1  1 
ATOM   128  C  CD2  . TYR   A 1 17  ? -4.740  4.895   62.683 1.00 29.80 ? 281 TYR   A CD2  1 
ATOM   129  C  CE1  . TYR   A 1 17  ? -3.289  7.197   63.122 1.00 36.72 ? 281 TYR   A CE1  1 
ATOM   130  C  CE2  . TYR   A 1 17  ? -3.385  4.961   62.326 1.00 35.56 ? 281 TYR   A CE2  1 
ATOM   131  C  CZ   . TYR   A 1 17  ? -2.687  6.114   62.543 1.00 38.59 ? 281 TYR   A CZ   1 
ATOM   132  O  OH   . TYR   A 1 17  ? -1.368  6.223   62.192 1.00 45.61 ? 281 TYR   A OH   1 
ATOM   133  N  N    . ARG   A 1 18  ? -7.873  5.211   60.771 1.00 24.52 ? 282 ARG   A N    1 
ATOM   134  C  CA   . ARG   A 1 18  ? -7.635  4.726   59.414 1.00 28.01 ? 282 ARG   A CA   1 
ATOM   135  C  C    . ARG   A 1 18  ? -8.064  5.774   58.369 1.00 30.19 ? 282 ARG   A C    1 
ATOM   136  O  O    . ARG   A 1 18  ? -7.396  5.961   57.354 1.00 32.07 ? 282 ARG   A O    1 
ATOM   137  C  CB   . ARG   A 1 18  ? -8.384  3.406   59.146 1.00 29.92 ? 282 ARG   A CB   1 
ATOM   138  C  CG   . ARG   A 1 18  ? -7.887  2.169   59.872 1.00 40.08 ? 282 ARG   A CG   1 
ATOM   139  C  CD   . ARG   A 1 18  ? -8.572  0.918   59.295 1.00 42.74 ? 282 ARG   A CD   1 
ATOM   140  N  NE   . ARG   A 1 18  ? -10.030 1.057   59.238 1.00 56.87 ? 282 ARG   A NE   1 
ATOM   141  C  CZ   . ARG   A 1 18  ? -10.714 1.501   58.173 1.00 72.93 ? 282 ARG   A CZ   1 
ATOM   142  N  NH1  . ARG   A 1 18  ? -12.041 1.601   58.217 1.00 80.30 ? 282 ARG   A NH1  1 
ATOM   143  N  NH2  . ARG   A 1 18  ? -10.081 1.844   57.054 1.00 74.85 ? 282 ARG   A NH2  1 
ATOM   144  N  N    . GLU   A 1 19  ? -9.180  6.457   58.624 1.00 26.31 ? 283 GLU   A N    1 
ATOM   145  C  CA   . GLU   A 1 19  ? -9.699  7.461   57.696 1.00 26.40 ? 283 GLU   A CA   1 
ATOM   146  C  C    . GLU   A 1 19  ? -8.827  8.718   57.593 1.00 26.03 ? 283 GLU   A C    1 
ATOM   147  O  O    . GLU   A 1 19  ? -9.016  9.492   56.675 1.00 26.40 ? 283 GLU   A O    1 
ATOM   148  C  CB   . GLU   A 1 19  ? -11.131 7.870   58.102 1.00 27.90 ? 283 GLU   A CB   1 
ATOM   149  C  CG   . GLU   A 1 19  ? -12.189 6.792   57.846 1.00 32.71 ? 283 GLU   A CG   1 
ATOM   150  C  CD   . GLU   A 1 19  ? -13.506 7.092   58.535 1.00 42.91 ? 283 GLU   A CD   1 
ATOM   151  O  OE1  . GLU   A 1 19  ? -13.542 7.971   59.425 1.00 38.94 ? 283 GLU   A OE1  1 
ATOM   152  O  OE2  . GLU   A 1 19  ? -14.521 6.431   58.195 1.00 44.37 ? 283 GLU   A OE2  1 
ATOM   153  N  N    . THR   A 1 20  ? -7.912  8.932   58.531 1.00 23.71 ? 284 THR   A N    1 
ATOM   154  C  CA   . THR   A 1 20  ? -7.149  10.171  58.566 1.00 21.97 ? 284 THR   A CA   1 
ATOM   155  C  C    . THR   A 1 20  ? -5.654  9.969   58.770 1.00 23.22 ? 284 THR   A C    1 
ATOM   156  O  O    . THR   A 1 20  ? -4.968  10.879  59.181 1.00 22.97 ? 284 THR   A O    1 
ATOM   157  C  CB   . THR   A 1 20  ? -7.653  11.028  59.737 1.00 21.12 ? 284 THR   A CB   1 
ATOM   158  O  OG1  . THR   A 1 20  ? -7.435  10.330  60.966 1.00 21.72 ? 284 THR   A OG1  1 
ATOM   159  C  CG2  . THR   A 1 20  ? -9.132  11.319  59.592 1.00 22.65 ? 284 THR   A CG2  1 
ATOM   160  N  N    . CYS   A 1 21  ? -5.153  8.787   58.463 1.00 23.35 ? 285 CYS   A N    1 
ATOM   161  C  CA   . CYS   A 1 21  ? -3.748  8.461   58.775 1.00 24.57 ? 285 CYS   A CA   1 
ATOM   162  C  C    . CYS   A 1 21  ? -2.696  9.050   57.852 1.00 27.83 ? 285 CYS   A C    1 
ATOM   163  O  O    . CYS   A 1 21  ? -1.520  8.897   58.119 1.00 27.52 ? 285 CYS   A O    1 
ATOM   164  C  CB   . CYS   A 1 21  ? -3.550  6.922   58.896 1.00 30.89 ? 285 CYS   A CB   1 
ATOM   165  S  SG   . CYS   A 1 21  ? -3.781  6.012   57.376 1.00 34.41 ? 285 CYS   A SG   1 
ATOM   166  N  N    . GLN   A 1 22  ? -3.118  9.696   56.791 1.00 24.66 ? 286 GLN   A N    1 
ATOM   167  C  CA   . GLN   A 1 22  ? -2.196  10.394  55.890 1.00 25.51 ? 286 GLN   A CA   1 
ATOM   168  C  C    . GLN   A 1 22  ? -1.433  9.499   54.947 1.00 30.04 ? 286 GLN   A C    1 
ATOM   169  O  O    . GLN   A 1 22  ? -1.552  9.652   53.744 1.00 31.19 ? 286 GLN   A O    1 
ATOM   170  C  CB   . GLN   A 1 22  ? -1.244  11.317  56.684 1.00 32.20 ? 286 GLN   A CB   1 
ATOM   171  C  CG   . GLN   A 1 22  ? -0.644  12.422  55.847 1.00 34.51 ? 286 GLN   A CG   1 
ATOM   172  C  CD   . GLN   A 1 22  ? 0.136   13.441  56.658 1.00 39.30 ? 286 GLN   A CD   1 
ATOM   173  O  OE1  . GLN   A 1 22  ? 0.193   13.376  57.882 1.00 41.69 ? 286 GLN   A OE1  1 
ATOM   174  N  NE2  . GLN   A 1 22  ? 0.744   14.389  55.968 1.00 33.46 ? 286 GLN   A NE2  1 
ATOM   175  N  N    . LEU   A 1 23  ? -0.626  8.603   55.482 1.00 26.96 ? 287 LEU   A N    1 
ATOM   176  C  CA   . LEU   A 1 23  ? 0.071   7.646   54.659 1.00 22.96 ? 287 LEU   A CA   1 
ATOM   177  C  C    . LEU   A 1 23  ? -0.232  6.267   55.183 1.00 23.26 ? 287 LEU   A C    1 
ATOM   178  O  O    . LEU   A 1 23  ? -0.365  6.097   56.372 1.00 26.76 ? 287 LEU   A O    1 
ATOM   179  C  CB   . LEU   A 1 23  ? 1.563   7.864   54.699 1.00 24.49 ? 287 LEU   A CB   1 
ATOM   180  C  CG   . LEU   A 1 23  ? 2.102   9.099   53.977 1.00 33.37 ? 287 LEU   A CG   1 
ATOM   181  C  CD1  . LEU   A 1 23  ? 3.613   9.117   54.028 1.00 33.61 ? 287 LEU   A CD1  1 
ATOM   182  C  CD2  . LEU   A 1 23  ? 1.618   9.132   52.544 1.00 35.24 ? 287 LEU   A CD2  1 
ATOM   183  N  N    . ARG   A 1 24  ? -0.369  5.303   54.282 1.00 23.50 ? 288 ARG   A N    1 
ATOM   184  C  CA   . ARG   A 1 24  ? -0.590  3.924   54.688 1.00 22.18 ? 288 ARG   A CA   1 
ATOM   185  C  C    . ARG   A 1 24  ? 0.700   3.289   55.176 1.00 24.17 ? 288 ARG   A C    1 
ATOM   186  O  O    . ARG   A 1 24  ? 1.749   3.531   54.618 1.00 23.35 ? 288 ARG   A O    1 
ATOM   187  C  CB   . ARG   A 1 24  ? -1.151  3.094   53.540 1.00 30.35 ? 288 ARG   A CB   1 
ATOM   188  C  CG   . ARG   A 1 24  ? -2.489  3.650   53.017 1.00 39.50 ? 288 ARG   A CG   1 
ATOM   189  C  CD   . ARG   A 1 24  ? -3.169  2.707   52.031 1.00 53.31 ? 288 ARG   A CD   1 
ATOM   190  N  NE   . ARG   A 1 24  ? -2.245  1.763   51.399 1.00 64.00 ? 288 ARG   A NE   1 
ATOM   191  C  CZ   . ARG   A 1 24  ? -2.039  1.664   50.086 1.00 70.73 ? 288 ARG   A CZ   1 
ATOM   192  N  NH1  . ARG   A 1 24  ? -2.697  2.462   49.250 1.00 72.33 ? 288 ARG   A NH1  1 
ATOM   193  N  NH2  . ARG   A 1 24  ? -1.176  0.765   49.608 1.00 70.54 ? 288 ARG   A NH2  1 
ATOM   194  N  N    . LEU   A 1 25  ? 0.596   2.518   56.252 1.00 25.68 ? 289 LEU   A N    1 
ATOM   195  C  CA   . LEU   A 1 25  ? 1.796   1.907   56.826 1.00 23.19 ? 289 LEU   A CA   1 
ATOM   196  C  C    . LEU   A 1 25  ? 2.444   0.999   55.807 1.00 25.95 ? 289 LEU   A C    1 
ATOM   197  O  O    . LEU   A 1 25  ? 3.693   0.949   55.726 1.00 25.50 ? 289 LEU   A O    1 
ATOM   198  C  CB   . LEU   A 1 25  ? 1.443   1.144   58.088 1.00 25.36 ? 289 LEU   A CB   1 
ATOM   199  C  CG   . LEU   A 1 25  ? 2.637   0.489   58.777 1.00 27.51 ? 289 LEU   A CG   1 
ATOM   200  C  CD1  . LEU   A 1 25  ? 3.535   1.568   59.359 1.00 28.62 ? 289 LEU   A CD1  1 
ATOM   201  C  CD2  . LEU   A 1 25  ? 2.104   -0.494  59.843 1.00 35.19 ? 289 LEU   A CD2  1 
ATOM   202  N  N    . GLU   A 1 26  ? 1.660   0.240   55.032 1.00 27.21 ? 290 GLU   A N    1 
ATOM   203  C  CA   . GLU   A 1 26  ? 2.312   -0.615  54.047 1.00 27.67 ? 290 GLU   A CA   1 
ATOM   204  C  C    . GLU   A 1 26  ? 3.206   0.162   53.071 1.00 26.12 ? 290 GLU   A C    1 
ATOM   205  O  O    . GLU   A 1 26  ? 4.222   -0.384  52.586 1.00 27.83 ? 290 GLU   A O    1 
ATOM   206  C  CB   . GLU   A 1 26  ? 1.305   -1.454  53.227 1.00 27.72 ? 290 GLU   A CB   1 
ATOM   207  C  CG   . GLU   A 1 26  ? -0.158  -0.997  53.196 1.00 43.98 ? 290 GLU   A CG   1 
ATOM   208  C  CD   . GLU   A 1 26  ? -0.845  -1.186  54.534 1.00 46.33 ? 290 GLU   A CD   1 
ATOM   209  O  OE1  . GLU   A 1 26  ? -1.197  -2.332  54.902 1.00 52.53 ? 290 GLU   A OE1  1 
ATOM   210  O  OE2  . GLU   A 1 26  ? -1.025  -0.189  55.231 1.00 42.03 ? 290 GLU   A OE2  1 
ATOM   211  N  N    . ASP   A 1 27  ? 2.818   1.396   52.726 1.00 24.04 ? 291 ASP   A N    1 
ATOM   212  C  CA   . ASP   A 1 27  ? 3.590   2.217   51.806 1.00 25.30 ? 291 ASP   A CA   1 
ATOM   213  C  C    . ASP   A 1 27  ? 4.875   2.659   52.492 1.00 24.76 ? 291 ASP   A C    1 
ATOM   214  O  O    . ASP   A 1 27  ? 5.930   2.578   51.897 1.00 26.95 ? 291 ASP   A O    1 
ATOM   215  C  CB   . ASP   A 1 27  ? 2.824   3.458   51.344 1.00 31.03 ? 291 ASP   A CB   1 
ATOM   216  C  CG   . ASP   A 1 27  ? 1.548   3.097   50.562 1.00 49.37 ? 291 ASP   A CG   1 
ATOM   217  O  OD1  . ASP   A 1 27  ? 1.505   2.029   49.899 1.00 55.10 ? 291 ASP   A OD1  1 
ATOM   218  O  OD2  . ASP   A 1 27  ? 0.577   3.878   50.618 1.00 61.19 ? 291 ASP   A OD2  1 
ATOM   219  N  N    . LEU   A 1 28  ? 4.765   3.104   53.737 1.00 21.35 ? 292 LEU   A N    1 
ATOM   220  C  CA   . LEU   A 1 28  ? 5.931   3.533   54.499 1.00 23.92 ? 292 LEU   A CA   1 
ATOM   221  C  C    . LEU   A 1 28  ? 6.921   2.388   54.659 1.00 25.47 ? 292 LEU   A C    1 
ATOM   222  O  O    . LEU   A 1 28  ? 8.141   2.614   54.536 1.00 25.84 ? 292 LEU   A O    1 
ATOM   223  C  CB   . LEU   A 1 28  ? 5.515   4.077   55.861 1.00 24.43 ? 292 LEU   A CB   1 
ATOM   224  C  CG   . LEU   A 1 28  ? 4.777   5.424   55.873 1.00 24.47 ? 292 LEU   A CG   1 
ATOM   225  C  CD1  . LEU   A 1 28  ? 4.242   5.694   57.262 1.00 28.37 ? 292 LEU   A CD1  1 
ATOM   226  C  CD2  . LEU   A 1 28  ? 5.672   6.574   55.446 1.00 27.65 ? 292 LEU   A CD2  1 
ATOM   227  N  N    . LEU   A 1 29  ? 6.419   1.172   54.923 1.00 24.11 ? 293 LEU   A N    1 
ATOM   228  C  CA   . LEU   A 1 29  ? 7.307   0.033   55.159 1.00 23.23 ? 293 LEU   A CA   1 
ATOM   229  C  C    . LEU   A 1 29  ? 7.995   -0.385  53.881 1.00 23.83 ? 293 LEU   A C    1 
ATOM   230  O  O    . LEU   A 1 29  ? 9.200   -0.701  53.889 1.00 23.15 ? 293 LEU   A O    1 
ATOM   231  C  CB   . LEU   A 1 29  ? 6.557   -1.177  55.746 1.00 20.83 ? 293 LEU   A CB   1 
ATOM   232  C  CG   . LEU   A 1 29  ? 6.044   -0.936  57.177 1.00 23.00 ? 293 LEU   A CG   1 
ATOM   233  C  CD1  . LEU   A 1 29  ? 5.286   -2.123  57.732 1.00 24.13 ? 293 LEU   A CD1  1 
ATOM   234  C  CD2  . LEU   A 1 29  ? 7.177   -0.588  58.117 1.00 27.28 ? 293 LEU   A CD2  1 
ATOM   235  N  N    . ARG   A 1 30  ? 7.269   -0.350  52.766 1.00 22.46 ? 294 ARG   A N    1 
ATOM   236  C  CA   . ARG   A 1 30  ? 7.889   -0.750  51.491 1.00 22.34 ? 294 ARG   A CA   1 
ATOM   237  C  C    . ARG   A 1 30  ? 8.908   0.274   50.975 1.00 24.87 ? 294 ARG   A C    1 
ATOM   238  O  O    . ARG   A 1 30  ? 9.755   -0.081  50.176 1.00 27.97 ? 294 ARG   A O    1 
ATOM   239  C  CB   . ARG   A 1 30  ? 6.807   -1.013  50.429 1.00 23.72 ? 294 ARG   A CB   1 
ATOM   240  C  CG   . ARG   A 1 30  ? 6.125   -2.346  50.739 1.00 28.86 ? 294 ARG   A CG   1 
ATOM   241  C  CD   . ARG   A 1 30  ? 5.036   -2.754  49.750 1.00 33.61 ? 294 ARG   A CD   1 
ATOM   242  N  NE   . ARG   A 1 30  ? 3.931   -1.830  49.751 1.00 40.29 ? 294 ARG   A NE   1 
ATOM   243  C  CZ   . ARG   A 1 30  ? 2.818   -2.038  49.055 1.00 40.40 ? 294 ARG   A CZ   1 
ATOM   244  N  NH1  . ARG   A 1 30  ? 2.718   -3.140  48.347 1.00 33.69 ? 294 ARG   A NH1  1 
ATOM   245  N  NH2  . ARG   A 1 30  ? 1.827   -1.157  49.083 1.00 44.69 ? 294 ARG   A NH2  1 
ATOM   246  N  N    . GLN   A 1 31  ? 8.850   1.500   51.469 1.00 23.85 ? 295 GLN   A N    1 
ATOM   247  C  CA   . GLN   A 1 31  ? 9.768   2.539   51.064 1.00 20.05 ? 295 GLN   A CA   1 
ATOM   248  C  C    . GLN   A 1 31  ? 11.051  2.577   51.860 1.00 24.55 ? 295 GLN   A C    1 
ATOM   249  O  O    . GLN   A 1 31  ? 11.919  3.388   51.560 1.00 24.33 ? 295 GLN   A O    1 
ATOM   250  C  CB   . GLN   A 1 31  ? 9.091   3.909   51.175 1.00 24.16 ? 295 GLN   A CB   1 
ATOM   251  C  CG   . GLN   A 1 31  ? 8.013   4.153   50.098 1.00 28.08 ? 295 GLN   A CG   1 
ATOM   252  C  CD   . GLN   A 1 31  ? 8.583   4.433   48.708 1.00 38.30 ? 295 GLN   A CD   1 
ATOM   253  O  OE1  . GLN   A 1 31  ? 9.783   4.278   48.451 1.00 40.20 ? 295 GLN   A OE1  1 
ATOM   254  N  NE2  . GLN   A 1 31  ? 7.716   4.838   47.800 1.00 44.74 ? 295 GLN   A NE2  1 
ATOM   255  N  N    . ARG   A 1 32  ? 11.168  1.718   52.870 1.00 26.65 ? 296 ARG   A N    1 
ATOM   256  C  CA   . ARG   A 1 32  ? 12.346  1.779   53.754 1.00 24.14 ? 296 ARG   A CA   1 
ATOM   257  C  C    . ARG   A 1 32  ? 13.667  1.683   53.010 1.00 24.32 ? 296 ARG   A C    1 
ATOM   258  O  O    . ARG   A 1 32  ? 14.640  2.255   53.462 1.00 30.16 ? 296 ARG   A O    1 
ATOM   259  C  CB   . ARG   A 1 32  ? 12.262  0.675   54.806 1.00 27.26 ? 296 ARG   A CB   1 
ATOM   260  C  CG   . ARG   A 1 32  ? 11.366  1.079   55.941 1.00 28.02 ? 296 ARG   A CG   1 
ATOM   261  C  CD   . ARG   A 1 32  ? 11.179  0.006   56.976 1.00 35.14 ? 296 ARG   A CD   1 
ATOM   262  N  NE   . ARG   A 1 32  ? 10.489  0.622   58.107 1.00 46.61 ? 296 ARG   A NE   1 
ATOM   263  C  CZ   . ARG   A 1 32  ? 10.856  0.493   59.374 1.00 51.71 ? 296 ARG   A CZ   1 
ATOM   264  N  NH1  . ARG   A 1 32  ? 10.162  1.106   60.335 1.00 49.51 ? 296 ARG   A NH1  1 
ATOM   265  N  NH2  . ARG   A 1 32  ? 11.905  -0.256  59.670 1.00 51.41 ? 296 ARG   A NH2  1 
ATOM   266  N  N    . SER   A 1 33  ? 13.742  0.937   51.901 1.00 25.56 ? 297 SER   A N    1 
ATOM   267  C  CA   . SER   A 1 33  ? 15.020  0.827   51.202 1.00 29.85 ? 297 SER   A CA   1 
ATOM   268  C  C    . SER   A 1 33  ? 15.267  1.998   50.264 1.00 32.59 ? 297 SER   A C    1 
ATOM   269  O  O    . SER   A 1 33  ? 16.342  2.117   49.695 1.00 33.63 ? 297 SER   A O    1 
ATOM   270  C  CB   . SER   A 1 33  ? 15.110  -0.481  50.415 1.00 31.10 ? 297 SER   A CB   1 
ATOM   271  O  OG   . SER   A 1 33  ? 14.080  -0.574  49.439 1.00 36.12 ? 297 SER   A OG   1 
ATOM   272  N  N    . ASN   A 1 34  ? 14.274  2.877   50.131 1.00 29.63 ? 298 ASN   A N    1 
ATOM   273  C  CA   . ASN   A 1 34  ? 14.383  4.073   49.291 1.00 28.59 ? 298 ASN   A CA   1 
ATOM   274  C  C    . ASN   A 1 34  ? 14.974  5.229   50.108 1.00 26.87 ? 298 ASN   A C    1 
ATOM   275  O  O    . ASN   A 1 34  ? 14.230  5.985   50.755 1.00 26.79 ? 298 ASN   A O    1 
ATOM   276  C  CB   . ASN   A 1 34  ? 12.990  4.403   48.740 1.00 29.37 ? 298 ASN   A CB   1 
ATOM   277  C  CG   . ASN   A 1 34  ? 13.012  5.407   47.625 1.00 32.48 ? 298 ASN   A CG   1 
ATOM   278  O  OD1  . ASN   A 1 34  ? 14.066  5.803   47.141 1.00 35.43 ? 298 ASN   A OD1  1 
ATOM   279  N  ND2  . ASN   A 1 34  ? 11.820  5.834   47.201 1.00 31.33 ? 298 ASN   A ND2  1 
ATOM   280  N  N    . ILE   A 1 35  ? 16.322  5.330   50.124 1.00 28.33 ? 299 ILE   A N    1 
ATOM   281  C  CA   . ILE   A 1 35  ? 17.052  6.250   50.991 1.00 27.09 ? 299 ILE   A CA   1 
ATOM   282  C  C    . ILE   A 1 35  ? 17.742  7.343   50.164 1.00 25.43 ? 299 ILE   A C    1 
ATOM   283  O  O    . ILE   A 1 35  ? 18.275  7.079   49.073 1.00 27.76 ? 299 ILE   A O    1 
ATOM   284  C  CB   . ILE   A 1 35  ? 18.086  5.470   51.824 1.00 27.26 ? 299 ILE   A CB   1 
ATOM   285  C  CG1  . ILE   A 1 35  ? 17.352  4.504   52.774 1.00 30.27 ? 299 ILE   A CG1  1 
ATOM   286  C  CG2  . ILE   A 1 35  ? 19.023  6.438   52.516 1.00 26.31 ? 299 ILE   A CG2  1 
ATOM   287  C  CD1  . ILE   A 1 35  ? 18.130  3.231   53.069 1.00 31.69 ? 299 ILE   A CD1  1 
ATOM   288  N  N    . PHE   A 1 36  ? 17.733  8.570   50.668 1.00 25.39 ? 300 PHE   A N    1 
ATOM   289  C  CA   . PHE   A 1 36  ? 18.455  9.637   49.978 1.00 25.72 ? 300 PHE   A CA   1 
ATOM   290  C  C    . PHE   A 1 36  ? 19.919  9.293   49.826 1.00 25.81 ? 300 PHE   A C    1 
ATOM   291  O  O    . PHE   A 1 36  ? 20.593  8.861   50.780 1.00 27.46 ? 300 PHE   A O    1 
ATOM   292  C  CB   . PHE   A 1 36  ? 18.331  10.985  50.727 1.00 22.79 ? 300 PHE   A CB   1 
ATOM   293  C  CG   . PHE   A 1 36  ? 16.968  11.613  50.618 1.00 24.32 ? 300 PHE   A CG   1 
ATOM   294  C  CD1  . PHE   A 1 36  ? 16.515  12.132  49.414 1.00 20.91 ? 300 PHE   A CD1  1 
ATOM   295  C  CD2  . PHE   A 1 36  ? 16.152  11.707  51.722 1.00 24.11 ? 300 PHE   A CD2  1 
ATOM   296  C  CE1  . PHE   A 1 36  ? 15.239  12.725  49.311 1.00 22.83 ? 300 PHE   A CE1  1 
ATOM   297  C  CE2  . PHE   A 1 36  ? 14.855  12.291  51.635 1.00 25.09 ? 300 PHE   A CE2  1 
ATOM   298  C  CZ   . PHE   A 1 36  ? 14.405  12.808  50.443 1.00 21.24 ? 300 PHE   A CZ   1 
ATOM   299  N  N    . SER   A 1 37  ? 20.408  9.490   48.605 1.00 26.01 ? 301 SER   A N    1 
ATOM   300  C  CA   . SER   A 1 37  ? 21.839  9.323   48.313 1.00 27.26 ? 301 SER   A CA   1 
ATOM   301  C  C    . SER   A 1 37  ? 22.677  10.400  48.957 1.00 29.77 ? 301 SER   A C    1 
ATOM   302  O  O    . SER   A 1 37  ? 22.178  11.441  49.360 1.00 31.00 ? 301 SER   A O    1 
ATOM   303  C  CB   . SER   A 1 37  ? 22.084  9.358   46.817 1.00 32.25 ? 301 SER   A CB   1 
ATOM   304  O  OG   . SER   A 1 37  ? 21.840  10.665  46.303 1.00 32.36 ? 301 SER   A OG   1 
ATOM   305  N  N    . ARG   A 1 38  ? 23.974  10.157  49.029 1.00 29.03 ? 302 ARG   A N    1 
ATOM   306  C  CA   . ARG   A 1 38  ? 24.898  11.140  49.544 1.00 30.59 ? 302 ARG   A CA   1 
ATOM   307  C  C    . ARG   A 1 38  ? 24.776  12.463  48.793 1.00 30.88 ? 302 ARG   A C    1 
ATOM   308  O  O    . ARG   A 1 38  ? 24.797  13.509  49.400 1.00 33.43 ? 302 ARG   A O    1 
ATOM   309  C  CB   . ARG   A 1 38  ? 26.318  10.579  49.461 1.00 35.77 ? 302 ARG   A CB   1 
ATOM   310  C  CG   . ARG   A 1 38  ? 27.346  11.419  50.186 1.00 49.13 ? 302 ARG   A CG   1 
ATOM   311  C  CD   . ARG   A 1 38  ? 28.648  10.610  50.408 1.00 64.72 ? 302 ARG   A CD   1 
ATOM   312  N  NE   . ARG   A 1 38  ? 28.414  9.383   51.181 1.00 72.46 ? 302 ARG   A NE   1 
ATOM   313  C  CZ   . ARG   A 1 38  ? 28.635  8.149   50.733 1.00 73.64 ? 302 ARG   A CZ   1 
ATOM   314  N  NH1  . ARG   A 1 38  ? 29.118  7.959   49.512 1.00 73.33 ? 302 ARG   A NH1  1 
ATOM   315  N  NH2  . ARG   A 1 38  ? 28.379  7.102   51.512 1.00 73.64 ? 302 ARG   A NH2  1 
ATOM   316  N  N    . GLU   A 1 39  ? 24.620  12.418  47.476 1.00 29.96 ? 303 GLU   A N    1 
ATOM   317  C  CA   . GLU   A 1 39  ? 24.466  13.633  46.712 1.00 33.48 ? 303 GLU   A CA   1 
ATOM   318  C  C    . GLU   A 1 39  ? 23.157  14.378  47.057 1.00 29.87 ? 303 GLU   A C    1 
ATOM   319  O  O    . GLU   A 1 39  ? 23.146  15.610  47.121 1.00 30.38 ? 303 GLU   A O    1 
ATOM   320  C  CB   . GLU   A 1 39  ? 24.503  13.340  45.218 1.00 41.68 ? 303 GLU   A CB   1 
ATOM   321  C  CG   . GLU   A 1 39  ? 24.491  14.647  44.421 1.00 60.99 ? 303 GLU   A CG   1 
ATOM   322  C  CD   . GLU   A 1 39  ? 24.102  14.485  42.956 1.00 76.47 ? 303 GLU   A CD   1 
ATOM   323  O  OE1  . GLU   A 1 39  ? 23.657  13.387  42.557 1.00 80.89 ? 303 GLU   A OE1  1 
ATOM   324  O  OE2  . GLU   A 1 39  ? 24.238  15.475  42.204 1.00 82.26 ? 303 GLU   A OE2  1 
ATOM   325  N  N    . GLU   A 1 40  ? 22.064  13.646  47.283 1.00 28.83 ? 304 GLU   A N    1 
ATOM   326  C  CA   . GLU   A 1 40  ? 20.785  14.270  47.603 1.00 28.85 ? 304 GLU   A CA   1 
ATOM   327  C  C    . GLU   A 1 40  ? 20.833  14.875  48.983 1.00 28.16 ? 304 GLU   A C    1 
ATOM   328  O  O    . GLU   A 1 40  ? 20.269  15.929  49.207 1.00 27.85 ? 304 GLU   A O    1 
ATOM   329  C  CB   . GLU   A 1 40  ? 19.636  13.281  47.517 1.00 27.79 ? 304 GLU   A CB   1 
ATOM   330  C  CG   . GLU   A 1 40  ? 19.454  12.759  46.105 1.00 34.21 ? 304 GLU   A CG   1 
ATOM   331  C  CD   . GLU   A 1 40  ? 18.400  11.687  46.014 1.00 40.94 ? 304 GLU   A CD   1 
ATOM   332  O  OE1  . GLU   A 1 40  ? 17.382  11.897  45.317 1.00 49.68 ? 304 GLU   A OE1  1 
ATOM   333  O  OE2  . GLU   A 1 40  ? 18.583  10.638  46.651 1.00 32.10 ? 304 GLU   A OE2  1 
ATOM   334  N  N    . VAL   A 1 41  ? 21.524  14.215  49.901 1.00 25.41 ? 305 VAL   A N    1 
ATOM   335  C  CA   . VAL   A 1 41  ? 21.691  14.758  51.246 1.00 25.29 ? 305 VAL   A CA   1 
ATOM   336  C  C    . VAL   A 1 41  ? 22.456  16.082  51.184 1.00 25.70 ? 305 VAL   A C    1 
ATOM   337  O  O    . VAL   A 1 41  ? 22.069  17.088  51.781 1.00 24.78 ? 305 VAL   A O    1 
ATOM   338  C  CB   . VAL   A 1 41  ? 22.431  13.770  52.151 1.00 26.96 ? 305 VAL   A CB   1 
ATOM   339  C  CG1  . VAL   A 1 41  ? 22.881  14.474  53.422 1.00 27.26 ? 305 VAL   A CG1  1 
ATOM   340  C  CG2  . VAL   A 1 41  ? 21.566  12.556  52.454 1.00 26.02 ? 305 VAL   A CG2  1 
ATOM   341  N  N    . THR   A 1 42  ? 23.555  16.087  50.449 1.00 27.19 ? 306 THR   A N    1 
ATOM   342  C  CA   . THR   A 1 42  ? 24.329  17.317  50.295 1.00 31.30 ? 306 THR   A CA   1 
ATOM   343  C  C    . THR   A 1 42  ? 23.448  18.414  49.700 1.00 31.29 ? 306 THR   A C    1 
ATOM   344  O  O    . THR   A 1 42  ? 23.523  19.575  50.112 1.00 27.81 ? 306 THR   A O    1 
ATOM   345  C  CB   . THR   A 1 42  ? 25.560  17.115  49.428 1.00 31.74 ? 306 THR   A CB   1 
ATOM   346  O  OG1  . THR   A 1 42  ? 26.423  16.164  50.068 1.00 30.71 ? 306 THR   A OG1  1 
ATOM   347  C  CG2  . THR   A 1 42  ? 26.287  18.467  49.252 1.00 29.80 ? 306 THR   A CG2  1 
ATOM   348  N  N    . GLY   A 1 43  ? 22.598  18.030  48.756 1.00 27.27 ? 307 GLY   A N    1 
ATOM   349  C  CA   . GLY   A 1 43  ? 21.664  18.971  48.145 1.00 28.70 ? 307 GLY   A CA   1 
ATOM   350  C  C    . GLY   A 1 43  ? 20.776  19.638  49.164 1.00 28.63 ? 307 GLY   A C    1 
ATOM   351  O  O    . GLY   A 1 43  ? 20.651  20.853  49.171 1.00 26.75 ? 307 GLY   A O    1 
ATOM   352  N  N    . TYR   A 1 44  ? 20.194  18.843  50.064 1.00 24.56 ? 308 TYR   A N    1 
ATOM   353  C  CA   . TYR   A 1 44  ? 19.362  19.418  51.125 1.00 22.63 ? 308 TYR   A CA   1 
ATOM   354  C  C    . TYR   A 1 44  ? 20.202  20.302  52.104 1.00 21.92 ? 308 TYR   A C    1 
ATOM   355  O  O    . TYR   A 1 44  ? 19.716  21.327  52.609 1.00 22.99 ? 308 TYR   A O    1 
ATOM   356  C  CB   . TYR   A 1 44  ? 18.675  18.297  51.887 1.00 20.90 ? 308 TYR   A CB   1 
ATOM   357  C  CG   . TYR   A 1 44  ? 17.361  17.831  51.283 1.00 22.00 ? 308 TYR   A CG   1 
ATOM   358  C  CD1  . TYR   A 1 44  ? 16.224  18.597  51.419 1.00 22.21 ? 308 TYR   A CD1  1 
ATOM   359  C  CD2  . TYR   A 1 44  ? 17.277  16.624  50.584 1.00 21.88 ? 308 TYR   A CD2  1 
ATOM   360  C  CE1  . TYR   A 1 44  ? 15.042  18.183  50.887 1.00 24.01 ? 308 TYR   A CE1  1 
ATOM   361  C  CE2  . TYR   A 1 44  ? 16.048  16.198  50.038 1.00 21.44 ? 308 TYR   A CE2  1 
ATOM   362  C  CZ   . TYR   A 1 44  ? 14.973  16.994  50.190 1.00 19.75 ? 308 TYR   A CZ   1 
ATOM   363  O  OH   . TYR   A 1 44  ? 13.807  16.548  49.616 1.00 23.87 ? 308 TYR   A OH   1 
ATOM   364  N  N    . GLN   A 1 45  ? 21.403  19.847  52.406 1.00 26.42 ? 309 GLN   A N    1 
ATOM   365  C  CA   . GLN   A 1 45  ? 22.273  20.582  53.319 1.00 26.52 ? 309 GLN   A CA   1 
ATOM   366  C  C    . GLN   A 1 45  ? 22.683  21.921  52.737 1.00 28.01 ? 309 GLN   A C    1 
ATOM   367  O  O    . GLN   A 1 45  ? 22.972  22.889  53.481 1.00 28.03 ? 309 GLN   A O    1 
ATOM   368  C  CB   . GLN   A 1 45  ? 23.508  19.742  53.664 1.00 25.54 ? 309 GLN   A CB   1 
ATOM   369  C  CG   . GLN   A 1 45  ? 23.157  18.601  54.588 1.00 23.45 ? 309 GLN   A CG   1 
ATOM   370  C  CD   . GLN   A 1 45  ? 24.335  17.682  54.844 1.00 28.41 ? 309 GLN   A CD   1 
ATOM   371  O  OE1  . GLN   A 1 45  ? 25.265  17.606  54.037 1.00 29.63 ? 309 GLN   A OE1  1 
ATOM   372  N  NE2  . GLN   A 1 45  ? 24.274  16.930  55.934 1.00 24.38 ? 309 GLN   A NE2  1 
ATOM   373  N  N    . ARG   A 1 46  ? 22.689  22.002  51.412 1.00 23.82 ? 310 ARG   A N    1 
ATOM   374  C  CA   . ARG   A 1 46  ? 23.018  23.266  50.760 1.00 26.34 ? 310 ARG   A CA   1 
ATOM   375  C  C    . ARG   A 1 46  ? 21.844  24.244  50.575 1.00 24.52 ? 310 ARG   A C    1 
ATOM   376  O  O    . ARG   A 1 46  ? 22.053  25.396  50.159 1.00 25.67 ? 310 ARG   A O    1 
ATOM   377  C  CB   . ARG   A 1 46  ? 23.660  22.997  49.381 1.00 26.49 ? 310 ARG   A CB   1 
ATOM   378  C  CG   . ARG   A 1 46  ? 25.057  22.399  49.408 1.00 33.47 ? 310 ARG   A CG   1 
ATOM   379  C  CD   . ARG   A 1 46  ? 25.665  22.466  47.999 1.00 50.13 ? 310 ARG   A CD   1 
ATOM   380  N  NE   . ARG   A 1 46  ? 25.214  21.416  47.082 1.00 62.16 ? 310 ARG   A NE   1 
ATOM   381  C  CZ   . ARG   A 1 46  ? 24.255  21.548  46.160 1.00 69.08 ? 310 ARG   A CZ   1 
ATOM   382  N  NH1  . ARG   A 1 46  ? 23.588  22.693  46.011 1.00 73.61 ? 310 ARG   A NH1  1 
ATOM   383  N  NH2  . ARG   A 1 46  ? 23.957  20.519  45.380 1.00 66.71 ? 310 ARG   A NH2  1 
ATOM   384  N  N    . LYS   A 1 47  ? 20.620  23.805  50.880 1.00 23.15 ? 311 LYS   A N    1 
ATOM   385  C  CA   . LYS   A 1 47  ? 19.471  24.687  50.733 1.00 20.28 ? 311 LYS   A CA   1 
ATOM   386  C  C    . LYS   A 1 47  ? 19.527  25.772  51.774 1.00 21.23 ? 311 LYS   A C    1 
ATOM   387  O  O    . LYS   A 1 47  ? 20.171  25.589  52.827 1.00 27.66 ? 311 LYS   A O    1 
ATOM   388  C  CB   . LYS   A 1 47  ? 18.145  23.934  50.864 1.00 23.76 ? 311 LYS   A CB   1 
ATOM   389  C  CG   . LYS   A 1 47  ? 17.903  22.909  49.731 1.00 25.02 ? 311 LYS   A CG   1 
ATOM   390  C  CD   . LYS   A 1 47  ? 16.518  22.307  49.934 1.00 24.37 ? 311 LYS   A CD   1 
ATOM   391  C  CE   . LYS   A 1 47  ? 16.139  21.266  48.848 1.00 28.00 ? 311 LYS   A CE   1 
ATOM   392  N  NZ   . LYS   A 1 47  ? 16.107  21.883  47.501 1.00 30.09 ? 311 LYS   A NZ   1 
ATOM   393  N  N    . SER   A 1 48  ? 18.899  26.900  51.505 1.00 21.58 ? 312 SER   A N    1 
ATOM   394  C  CA   . SER   A 1 48  ? 18.810  27.920  52.535 1.00 22.50 ? 312 SER   A CA   1 
ATOM   395  C  C    . SER   A 1 48  ? 17.832  27.536  53.641 1.00 22.26 ? 312 SER   A C    1 
ATOM   396  O  O    . SER   A 1 48  ? 16.881  26.743  53.466 1.00 23.79 ? 312 SER   A O    1 
ATOM   397  C  CB   . SER   A 1 48  ? 18.415  29.265  51.944 1.00 20.81 ? 312 SER   A CB   1 
ATOM   398  O  OG   . SER   A 1 48  ? 17.035  29.177  51.493 1.00 23.13 ? 312 SER   A OG   1 
ATOM   399  N  N    . MET   A 1 49  ? 18.016  28.170  54.782 1.00 25.44 ? 313 MET   A N    1 
ATOM   400  C  CA   . MET   A 1 49  ? 17.093  27.947  55.852 1.00 20.15 ? 313 MET   A CA   1 
ATOM   401  C  C    . MET   A 1 49  ? 15.717  28.393  55.413 1.00 20.81 ? 313 MET   A C    1 
ATOM   402  O  O    . MET   A 1 49  ? 14.730  27.761  55.710 1.00 22.22 ? 313 MET   A O    1 
ATOM   403  C  CB   . MET   A 1 49  ? 17.463  28.756  57.060 1.00 25.92 ? 313 MET   A CB   1 
ATOM   404  C  CG   . MET   A 1 49  ? 16.532  28.508  58.191 1.00 34.62 ? 313 MET   A CG   1 
ATOM   405  S  SD   . MET   A 1 49  ? 15.544  29.960  58.452 1.00 45.56 ? 313 MET   A SD   1 
ATOM   406  C  CE   . MET   A 1 49  ? 16.642  30.610  59.682 1.00 23.32 ? 313 MET   A CE   1 
ATOM   407  N  N    . TRP   A 1 50  ? 15.686  29.508  54.720 1.00 20.18 ? 314 TRP   A N    1 
ATOM   408  C  CA   . TRP   A 1 50  ? 14.404  30.044  54.256 1.00 24.76 ? 314 TRP   A CA   1 
ATOM   409  C  C    . TRP   A 1 50  ? 13.623  29.020  53.440 1.00 23.71 ? 314 TRP   A C    1 
ATOM   410  O  O    . TRP   A 1 50  ? 12.442  28.753  53.711 1.00 21.46 ? 314 TRP   A O    1 
ATOM   411  C  CB   . TRP   A 1 50  ? 14.706  31.308  53.447 1.00 23.10 ? 314 TRP   A CB   1 
ATOM   412  C  CG   . TRP   A 1 50  ? 13.570  32.106  52.978 1.00 23.54 ? 314 TRP   A CG   1 
ATOM   413  C  CD1  . TRP   A 1 50  ? 12.234  31.887  53.167 1.00 27.68 ? 314 TRP   A CD1  1 
ATOM   414  C  CD2  . TRP   A 1 50  ? 13.689  33.333  52.265 1.00 25.28 ? 314 TRP   A CD2  1 
ATOM   415  N  NE1  . TRP   A 1 50  ? 11.501  32.905  52.558 1.00 30.04 ? 314 TRP   A NE1  1 
ATOM   416  C  CE2  . TRP   A 1 50  ? 12.382  33.807  52.017 1.00 30.33 ? 314 TRP   A CE2  1 
ATOM   417  C  CE3  . TRP   A 1 50  ? 14.779  34.059  51.778 1.00 30.26 ? 314 TRP   A CE3  1 
ATOM   418  C  CZ2  . TRP   A 1 50  ? 12.146  34.995  51.303 1.00 32.33 ? 314 TRP   A CZ2  1 
ATOM   419  C  CZ3  . TRP   A 1 50  ? 14.552  35.240  51.088 1.00 29.14 ? 314 TRP   A CZ3  1 
ATOM   420  C  CH2  . TRP   A 1 50  ? 13.243  35.695  50.848 1.00 28.66 ? 314 TRP   A CH2  1 
ATOM   421  N  N    . GLU   A 1 51  ? 14.299  28.424  52.464 1.00 21.04 ? 315 GLU   A N    1 
ATOM   422  C  CA   . GLU   A 1 51  ? 13.672  27.421  51.638 1.00 21.57 ? 315 GLU   A CA   1 
ATOM   423  C  C    . GLU   A 1 51  ? 13.237  26.182  52.448 1.00 22.65 ? 315 GLU   A C    1 
ATOM   424  O  O    . GLU   A 1 51  ? 12.144  25.647  52.219 1.00 19.82 ? 315 GLU   A O    1 
ATOM   425  C  CB   . GLU   A 1 51  ? 14.594  26.995  50.490 1.00 23.32 ? 315 GLU   A CB   1 
ATOM   426  C  CG   . GLU   A 1 51  ? 14.061  25.721  49.828 1.00 33.21 ? 315 GLU   A CG   1 
ATOM   427  C  CD   . GLU   A 1 51  ? 14.819  25.266  48.591 1.00 43.13 ? 315 GLU   A CD   1 
ATOM   428  O  OE1  . GLU   A 1 51  ? 15.811  25.926  48.199 1.00 34.05 ? 315 GLU   A OE1  1 
ATOM   429  O  OE2  . GLU   A 1 51  ? 14.415  24.226  48.019 1.00 46.84 ? 315 GLU   A OE2  1 
ATOM   430  N  N    . MET   A 1 52  ? 14.088  25.681  53.334 1.00 20.28 ? 316 MET   A N    1 
ATOM   431  C  CA   . MET   A 1 52  ? 13.742  24.527  54.142 1.00 19.38 ? 316 MET   A CA   1 
ATOM   432  C  C    . MET   A 1 52  ? 12.561  24.840  55.076 1.00 22.12 ? 316 MET   A C    1 
ATOM   433  O  O    . MET   A 1 52  ? 11.685  23.997  55.271 1.00 20.23 ? 316 MET   A O    1 
ATOM   434  C  CB   . MET   A 1 52  ? 14.963  24.053  54.943 1.00 24.45 ? 316 MET   A CB   1 
ATOM   435  C  CG   . MET   A 1 52  ? 15.901  23.225  54.102 1.00 26.05 ? 316 MET   A CG   1 
ATOM   436  S  SD   . MET   A 1 52  ? 15.197  21.699  53.456 1.00 28.75 ? 316 MET   A SD   1 
ATOM   437  C  CE   . MET   A 1 52  ? 15.024  20.689  54.918 1.00 29.98 ? 316 MET   A CE   1 
ATOM   438  N  N    . TRP   A 1 53  ? 12.519  26.060  55.622 1.00 20.96 ? 317 TRP   A N    1 
ATOM   439  C  CA   . TRP   A 1 53  ? 11.385  26.444  56.464 1.00 18.67 ? 317 TRP   A CA   1 
ATOM   440  C  C    . TRP   A 1 53  ? 10.119  26.468  55.629 1.00 20.74 ? 317 TRP   A C    1 
ATOM   441  O  O    . TRP   A 1 53  ? 9.114   26.001  56.114 1.00 21.32 ? 317 TRP   A O    1 
ATOM   442  C  CB   . TRP   A 1 53  ? 11.660  27.802  57.112 1.00 18.23 ? 317 TRP   A CB   1 
ATOM   443  C  CG   . TRP   A 1 53  ? 10.457  28.619  57.505 1.00 20.94 ? 317 TRP   A CG   1 
ATOM   444  C  CD1  . TRP   A 1 53  ? 10.174  29.895  57.069 1.00 22.17 ? 317 TRP   A CD1  1 
ATOM   445  C  CD2  . TRP   A 1 53  ? 9.451   28.298  58.469 1.00 22.76 ? 317 TRP   A CD2  1 
ATOM   446  N  NE1  . TRP   A 1 53  ? 9.026   30.348  57.668 1.00 22.28 ? 317 TRP   A NE1  1 
ATOM   447  C  CE2  . TRP   A 1 53  ? 8.571   29.394  58.534 1.00 20.67 ? 317 TRP   A CE2  1 
ATOM   448  C  CE3  . TRP   A 1 53  ? 9.198   27.180  59.276 1.00 24.02 ? 317 TRP   A CE3  1 
ATOM   449  C  CZ2  . TRP   A 1 53  ? 7.464   29.409  59.359 1.00 22.53 ? 317 TRP   A CZ2  1 
ATOM   450  C  CZ3  . TRP   A 1 53  ? 8.061   27.179  60.073 1.00 23.36 ? 317 TRP   A CZ3  1 
ATOM   451  C  CH2  . TRP   A 1 53  ? 7.239   28.312  60.142 1.00 22.01 ? 317 TRP   A CH2  1 
ATOM   452  N  N    . GLU   A 1 54  ? 10.160  26.993  54.396 1.00 18.51 ? 318 GLU   A N    1 
ATOM   453  C  CA   . GLU   A 1 54  ? 8.900   27.025  53.596 1.00 20.72 ? 318 GLU   A CA   1 
ATOM   454  C  C    . GLU   A 1 54  ? 8.438   25.587  53.363 1.00 20.05 ? 318 GLU   A C    1 
ATOM   455  O  O    . GLU   A 1 54  ? 7.221   25.307  53.418 1.00 20.99 ? 318 GLU   A O    1 
ATOM   456  C  CB   . GLU   A 1 54  ? 9.090   27.729  52.245 1.00 23.36 ? 318 GLU   A CB   1 
ATOM   457  C  CG   . GLU   A 1 54  ? 9.349   29.225  52.322 1.00 30.29 ? 318 GLU   A CG   1 
ATOM   458  C  CD   . GLU   A 1 54  ? 9.616   29.820  50.941 1.00 42.26 ? 318 GLU   A CD   1 
ATOM   459  O  OE1  . GLU   A 1 54  ? 9.257   30.988  50.727 1.00 45.93 ? 318 GLU   A OE1  1 
ATOM   460  O  OE2  . GLU   A 1 54  ? 10.219  29.126  50.082 1.00 49.70 ? 318 GLU   A OE2  1 
ATOM   461  N  N    . ARG   A 1 55  ? 9.388   24.699  53.101 1.00 19.42 ? 319 ARG   A N    1 
ATOM   462  C  CA   . ARG   A 1 55  ? 9.050   23.302  52.834 1.00 19.14 ? 319 ARG   A CA   1 
ATOM   463  C  C    . ARG   A 1 55  ? 8.447   22.651  54.058 1.00 20.47 ? 319 ARG   A C    1 
ATOM   464  O  O    . ARG   A 1 55  ? 7.413   21.952  53.970 1.00 21.19 ? 319 ARG   A O    1 
ATOM   465  C  CB   . ARG   A 1 55  ? 10.294  22.519  52.375 1.00 22.26 ? 319 ARG   A CB   1 
ATOM   466  C  CG   . ARG   A 1 55  ? 10.703  22.815  50.927 1.00 22.66 ? 319 ARG   A CG   1 
ATOM   467  C  CD   . ARG   A 1 55  ? 11.971  21.972  50.579 1.00 26.57 ? 319 ARG   A CD   1 
ATOM   468  N  NE   . ARG   A 1 55  ? 12.330  22.213  49.193 1.00 35.86 ? 319 ARG   A NE   1 
ATOM   469  C  CZ   . ARG   A 1 55  ? 12.265  21.314  48.224 1.00 37.51 ? 319 ARG   A CZ   1 
ATOM   470  N  NH1  . ARG   A 1 55  ? 11.943  20.050  48.496 1.00 34.67 ? 319 ARG   A NH1  1 
ATOM   471  N  NH2  . ARG   A 1 55  ? 12.594  21.690  46.994 1.00 37.88 ? 319 ARG   A NH2  1 
ATOM   472  N  N    . CYS   A 1 56  ? 9.091   22.844  55.193 1.00 19.29 ? 320 CYS   A N    1 
ATOM   473  C  CA   . CYS   A 1 56  ? 8.719   22.151  56.405 1.00 20.85 ? 320 CYS   A CA   1 
ATOM   474  C  C    . CYS   A 1 56  ? 7.450   22.754  57.014 1.00 19.71 ? 320 CYS   A C    1 
ATOM   475  O  O    . CYS   A 1 56  ? 6.649   22.017  57.607 1.00 22.78 ? 320 CYS   A O    1 
ATOM   476  C  CB   . CYS   A 1 56  ? 9.876   22.163  57.387 1.00 22.94 ? 320 CYS   A CB   1 
ATOM   477  S  SG   . CYS   A 1 56  ? 11.258  21.076  56.733 1.00 23.43 ? 320 CYS   A SG   1 
ATOM   478  N  N    . ALA   A 1 57  ? 7.220   24.059  56.822 1.00 18.34 ? 321 ALA   A N    1 
ATOM   479  C  CA   . ALA   A 1 57  ? 5.939   24.688  57.235 1.00 20.67 ? 321 ALA   A CA   1 
ATOM   480  C  C    . ALA   A 1 57  ? 4.776   24.021  56.502 1.00 22.71 ? 321 ALA   A C    1 
ATOM   481  O  O    . ALA   A 1 57  ? 3.717   23.765  57.087 1.00 22.53 ? 321 ALA   A O    1 
ATOM   482  C  CB   . ALA   A 1 57  ? 5.960   26.200  56.952 1.00 20.73 ? 321 ALA   A CB   1 
ATOM   483  N  N    . HIS   A 1 58  ? 4.984   23.738  55.218 1.00 21.03 ? 322 HIS   A N    1 
ATOM   484  C  CA   . HIS   A 1 58  ? 3.961   23.032  54.445 1.00 21.92 ? 322 HIS   A CA   1 
ATOM   485  C  C    . HIS   A 1 58  ? 3.704   21.643  55.028 1.00 20.05 ? 322 HIS   A C    1 
ATOM   486  O  O    . HIS   A 1 58  ? 2.548   21.227  55.189 1.00 20.12 ? 322 HIS   A O    1 
ATOM   487  C  CB   . HIS   A 1 58  ? 4.403   22.888  52.988 1.00 25.38 ? 322 HIS   A CB   1 
ATOM   488  C  CG   . HIS   A 1 58  ? 3.556   21.920  52.206 1.00 37.64 ? 322 HIS   A CG   1 
ATOM   489  N  ND1  . HIS   A 1 58  ? 2.343   22.276  51.653 1.00 39.33 ? 322 HIS   A ND1  1 
ATOM   490  C  CD2  . HIS   A 1 58  ? 3.729   20.606  51.918 1.00 44.59 ? 322 HIS   A CD2  1 
ATOM   491  C  CE1  . HIS   A 1 58  ? 1.816   21.232  51.041 1.00 41.50 ? 322 HIS   A CE1  1 
ATOM   492  N  NE2  . HIS   A 1 58  ? 2.628   20.199  51.196 1.00 45.31 ? 322 HIS   A NE2  1 
ATOM   493  N  N    . HIS   A 1 59  ? 4.772   20.880  55.320 1.00 20.40 ? 323 HIS   A N    1 
ATOM   494  C  CA   . HIS   A 1 59  ? 4.570   19.523  55.856 1.00 19.06 ? 323 HIS   A CA   1 
ATOM   495  C  C    . HIS   A 1 59  ? 3.900   19.557  57.225 1.00 20.03 ? 323 HIS   A C    1 
ATOM   496  O  O    . HIS   A 1 59  ? 3.052   18.708  57.541 1.00 21.79 ? 323 HIS   A O    1 
ATOM   497  C  CB   . HIS   A 1 59  ? 5.920   18.783  55.954 1.00 20.70 ? 323 HIS   A CB   1 
ATOM   498  C  CG   . HIS   A 1 59  ? 6.598   18.655  54.634 1.00 23.74 ? 323 HIS   A CG   1 
ATOM   499  N  ND1  . HIS   A 1 59  ? 5.939   18.331  53.471 1.00 30.44 ? 323 HIS   A ND1  1 
ATOM   500  C  CD2  . HIS   A 1 59  ? 7.914   18.843  54.291 1.00 21.31 ? 323 HIS   A CD2  1 
ATOM   501  C  CE1  . HIS   A 1 59  ? 6.802   18.322  52.463 1.00 28.65 ? 323 HIS   A CE1  1 
ATOM   502  N  NE2  . HIS   A 1 59  ? 8.006   18.611  52.946 1.00 23.04 ? 323 HIS   A NE2  1 
ATOM   503  N  N    . LEU   A 1 60  ? 4.280   20.547  58.035 1.00 18.98 ? 324 LEU   A N    1 
ATOM   504  C  CA   . LEU   A 1 60  ? 3.687   20.690  59.372 1.00 17.02 ? 324 LEU   A CA   1 
ATOM   505  C  C    . LEU   A 1 60  ? 2.207   20.997  59.262 1.00 18.83 ? 324 LEU   A C    1 
ATOM   506  O  O    . LEU   A 1 60  ? 1.382   20.317  59.896 1.00 21.47 ? 324 LEU   A O    1 
ATOM   507  C  CB   . LEU   A 1 60  ? 4.365   21.819  60.135 1.00 21.17 ? 324 LEU   A CB   1 
ATOM   508  C  CG   . LEU   A 1 60  ? 3.828   22.054  61.543 1.00 29.30 ? 324 LEU   A CG   1 
ATOM   509  C  CD1  . LEU   A 1 60  ? 3.828   20.742  62.326 1.00 30.58 ? 324 LEU   A CD1  1 
ATOM   510  C  CD2  . LEU   A 1 60  ? 4.621   23.155  62.264 1.00 36.06 ? 324 LEU   A CD2  1 
ATOM   511  N  N    . THR   A 1 61  ? 1.855   22.007  58.468 1.00 20.34 ? 325 THR   A N    1 
ATOM   512  C  CA   . THR   A 1 61  ? 0.438   22.371  58.411 1.00 19.37 ? 325 THR   A CA   1 
ATOM   513  C  C    . THR   A 1 61  ? -0.410  21.245  57.798 1.00 20.05 ? 325 THR   A C    1 
ATOM   514  O  O    . THR   A 1 61  ? -1.543  21.020  58.258 1.00 21.84 ? 325 THR   A O    1 
ATOM   515  C  CB   . THR   A 1 61  ? 0.204   23.703  57.676 1.00 27.04 ? 325 THR   A CB   1 
ATOM   516  O  OG1  . THR   A 1 61  ? 0.795   23.691  56.394 1.00 32.93 ? 325 THR   A OG1  1 
ATOM   517  C  CG2  . THR   A 1 61  ? 0.779   24.808  58.433 1.00 22.51 ? 325 THR   A CG2  1 
ATOM   518  N  N    . GLU   A 1 62  ? 0.142   20.485  56.839 1.00 19.76 ? 326 GLU   A N    1 
ATOM   519  C  CA   . GLU   A 1 62  ? -0.579  19.342  56.262 1.00 18.72 ? 326 GLU   A CA   1 
ATOM   520  C  C    . GLU   A 1 62  ? -0.814  18.279  57.349 1.00 19.05 ? 326 GLU   A C    1 
ATOM   521  O  O    . GLU   A 1 62  ? -1.900  17.717  57.494 1.00 20.57 ? 326 GLU   A O    1 
ATOM   522  C  CB   . GLU   A 1 62  ? 0.230   18.759  55.077 1.00 21.95 ? 326 GLU   A CB   1 
ATOM   523  C  CG   . GLU   A 1 62  ? -0.385  17.495  54.457 1.00 29.39 ? 326 GLU   A CG   1 
ATOM   524  C  CD   . GLU   A 1 62  ? -0.158  17.457  52.960 1.00 50.29 ? 326 GLU   A CD   1 
ATOM   525  O  OE1  . GLU   A 1 62  ? 0.585   18.333  52.472 1.00 60.19 ? 326 GLU   A OE1  1 
ATOM   526  O  OE2  . GLU   A 1 62  ? -0.707  16.576  52.270 1.00 55.55 ? 326 GLU   A OE2  1 
ATOM   527  N  N    . ALA   A 1 63  ? 0.219   17.955  58.118 1.00 17.47 ? 327 ALA   A N    1 
ATOM   528  C  CA   . ALA   A 1 63  ? 0.047   16.956  59.173 1.00 19.67 ? 327 ALA   A CA   1 
ATOM   529  C  C    . ALA   A 1 63  ? -0.984  17.381  60.198 1.00 20.29 ? 327 ALA   A C    1 
ATOM   530  O  O    . ALA   A 1 63  ? -1.786  16.542  60.663 1.00 21.34 ? 327 ALA   A O    1 
ATOM   531  C  CB   . ALA   A 1 63  ? 1.425   16.698  59.869 1.00 19.83 ? 327 ALA   A CB   1 
ATOM   532  N  N    . ILE   A 1 64  ? -0.988  18.667  60.550 1.00 21.08 ? 328 ILE   A N    1 
ATOM   533  C  CA   . ILE   A 1 64  ? -1.928  19.158  61.548 1.00 18.15 ? 328 ILE   A CA   1 
ATOM   534  C  C    . ILE   A 1 64  ? -3.383  19.017  61.004 1.00 20.92 ? 328 ILE   A C    1 
ATOM   535  O  O    . ILE   A 1 64  ? -4.309  18.679  61.756 1.00 20.80 ? 328 ILE   A O    1 
ATOM   536  C  CB   . ILE   A 1 64  ? -1.595  20.603  61.935 1.00 16.87 ? 328 ILE   A CB   1 
ATOM   537  C  CG1  . ILE   A 1 64  ? -0.333  20.603  62.802 1.00 21.00 ? 328 ILE   A CG1  1 
ATOM   538  C  CG2  . ILE   A 1 64  ? -2.810  21.265  62.638 1.00 22.24 ? 328 ILE   A CG2  1 
ATOM   539  C  CD1  . ILE   A 1 64  ? -0.566  20.078  64.189 1.00 26.25 ? 328 ILE   A CD1  1 
ATOM   540  N  N    . GLN   A 1 65  ? -3.549  19.255  59.711 1.00 18.39 ? 329 GLN   A N    1 
ATOM   541  C  CA   . GLN   A 1 65  ? -4.889  19.146  59.070 1.00 19.06 ? 329 GLN   A CA   1 
ATOM   542  C  C    . GLN   A 1 65  ? -5.487  17.745  59.277 1.00 18.55 ? 329 GLN   A C    1 
ATOM   543  O  O    . GLN   A 1 65  ? -6.690  17.609  59.534 1.00 20.32 ? 329 GLN   A O    1 
ATOM   544  C  CB   . GLN   A 1 65  ? -4.725  19.478  57.586 1.00 22.21 ? 329 GLN   A CB   1 
ATOM   545  C  CG   . GLN   A 1 65  ? -5.923  19.488  56.696 1.00 39.90 ? 329 GLN   A CG   1 
ATOM   546  C  CD   . GLN   A 1 65  ? -5.514  20.152  55.410 1.00 50.84 ? 329 GLN   A CD   1 
ATOM   547  O  OE1  . GLN   A 1 65  ? -4.365  20.624  55.294 1.00 47.43 ? 329 GLN   A OE1  1 
ATOM   548  N  NE2  . GLN   A 1 65  ? -6.424  20.232  54.455 1.00 54.85 ? 329 GLN   A NE2  1 
ATOM   549  N  N    . TYR   A 1 66  ? -4.673  16.704  59.132 1.00 19.33 ? 330 TYR   A N    1 
ATOM   550  C  CA   . TYR   A 1 66  ? -5.168  15.355  59.299 1.00 19.12 ? 330 TYR   A CA   1 
ATOM   551  C  C    . TYR   A 1 66  ? -5.499  15.099  60.761 1.00 20.74 ? 330 TYR   A C    1 
ATOM   552  O  O    . TYR   A 1 66  ? -6.460  14.402  61.056 1.00 21.27 ? 330 TYR   A O    1 
ATOM   553  C  CB   . TYR   A 1 66  ? -4.134  14.358  58.750 1.00 23.81 ? 330 TYR   A CB   1 
ATOM   554  C  CG   . TYR   A 1 66  ? -4.129  14.241  57.241 1.00 23.03 ? 330 TYR   A CG   1 
ATOM   555  C  CD1  . TYR   A 1 66  ? -3.367  15.099  56.467 1.00 26.44 ? 330 TYR   A CD1  1 
ATOM   556  C  CD2  . TYR   A 1 66  ? -4.866  13.289  56.596 1.00 22.38 ? 330 TYR   A CD2  1 
ATOM   557  C  CE1  . TYR   A 1 66  ? -3.369  15.009  55.087 1.00 31.72 ? 330 TYR   A CE1  1 
ATOM   558  C  CE2  . TYR   A 1 66  ? -4.876  13.186  55.208 1.00 27.62 ? 330 TYR   A CE2  1 
ATOM   559  C  CZ   . TYR   A 1 66  ? -4.109  14.036  54.463 1.00 32.10 ? 330 TYR   A CZ   1 
ATOM   560  O  OH   . TYR   A 1 66  ? -4.100  13.956  53.091 1.00 35.32 ? 330 TYR   A OH   1 
ATOM   561  N  N    . VAL   A 1 67  ? -4.694  15.628  61.671 1.00 21.87 ? 331 VAL   A N    1 
ATOM   562  C  CA   . VAL   A 1 67  ? -4.942  15.414  63.098 1.00 20.67 ? 331 VAL   A CA   1 
ATOM   563  C  C    . VAL   A 1 67  ? -6.239  16.089  63.529 1.00 19.01 ? 331 VAL   A C    1 
ATOM   564  O  O    . VAL   A 1 67  ? -7.014  15.533  64.341 1.00 18.85 ? 331 VAL   A O    1 
ATOM   565  C  CB   . VAL   A 1 67  ? -3.753  15.916  63.947 1.00 18.53 ? 331 VAL   A CB   1 
ATOM   566  C  CG1  . VAL   A 1 67  ? -4.098  15.923  65.427 1.00 20.81 ? 331 VAL   A CG1  1 
ATOM   567  C  CG2  . VAL   A 1 67  ? -2.566  14.940  63.706 1.00 18.86 ? 331 VAL   A CG2  1 
ATOM   568  N  N    . VAL   A 1 68  ? -6.495  17.296  63.007 1.00 20.38 ? 332 VAL   A N    1 
ATOM   569  C  CA   . VAL   A 1 68  ? -7.764  17.993  63.324 1.00 17.51 ? 332 VAL   A CA   1 
ATOM   570  C  C    . VAL   A 1 68  ? -8.949  17.193  62.841 1.00 20.65 ? 332 VAL   A C    1 
ATOM   571  O  O    . VAL   A 1 68  ? -9.963  17.077  63.531 1.00 19.91 ? 332 VAL   A O    1 
ATOM   572  C  CB   . VAL   A 1 68  ? -7.742  19.401  62.721 1.00 17.75 ? 332 VAL   A CB   1 
ATOM   573  C  CG1  . VAL   A 1 68  ? -9.122  20.030  62.813 1.00 22.65 ? 332 VAL   A CG1  1 
ATOM   574  C  CG2  . VAL   A 1 68  ? -6.728  20.243  63.446 1.00 20.65 ? 332 VAL   A CG2  1 
ATOM   575  N  N    . GLU   A 1 69  ? -8.838  16.614  61.664 1.00 20.22 ? 333 GLU   A N    1 
ATOM   576  C  CA   . GLU   A 1 69  ? -9.946  15.819  61.130 1.00 18.11 ? 333 GLU   A CA   1 
ATOM   577  C  C    . GLU   A 1 69  ? -10.113 14.530  61.949 1.00 17.28 ? 333 GLU   A C    1 
ATOM   578  O  O    . GLU   A 1 69  ? -11.240 14.097  62.213 1.00 21.41 ? 333 GLU   A O    1 
ATOM   579  C  CB   . GLU   A 1 69  ? -9.718  15.517  59.662 1.00 20.43 ? 333 GLU   A CB   1 
ATOM   580  C  CG   . GLU   A 1 69  ? -10.869 14.683  59.033 1.00 20.16 ? 333 GLU   A CG   1 
ATOM   581  C  CD   . GLU   A 1 69  ? -12.148 15.453  58.896 1.00 23.80 ? 333 GLU   A CD   1 
ATOM   582  O  OE1  . GLU   A 1 69  ? -12.094 16.704  58.916 1.00 25.99 ? 333 GLU   A OE1  1 
ATOM   583  O  OE2  . GLU   A 1 69  ? -13.209 14.784  58.777 1.00 24.09 ? 333 GLU   A OE2  1 
ATOM   584  N  N    . PHE   A 1 70  ? -9.001  13.925  62.379 1.00 19.09 ? 334 PHE   A N    1 
ATOM   585  C  CA   . PHE   A 1 70  ? -9.089  12.760  63.260 1.00 19.45 ? 334 PHE   A CA   1 
ATOM   586  C  C    . PHE   A 1 70  ? -9.895  13.081  64.524 1.00 20.80 ? 334 PHE   A C    1 
ATOM   587  O  O    . PHE   A 1 70  ? -10.800 12.315  64.931 1.00 23.26 ? 334 PHE   A O    1 
ATOM   588  C  CB   . PHE   A 1 70  ? -7.678  12.318  63.666 1.00 17.84 ? 334 PHE   A CB   1 
ATOM   589  C  CG   . PHE   A 1 70  ? -7.657  11.307  64.776 1.00 21.39 ? 334 PHE   A CG   1 
ATOM   590  C  CD1  . PHE   A 1 70  ? -8.155  10.036  64.590 1.00 20.23 ? 334 PHE   A CD1  1 
ATOM   591  C  CD2  . PHE   A 1 70  ? -7.059  11.652  66.006 1.00 22.59 ? 334 PHE   A CD2  1 
ATOM   592  C  CE1  . PHE   A 1 70  ? -8.127  9.090   65.616 1.00 24.06 ? 334 PHE   A CE1  1 
ATOM   593  C  CE2  . PHE   A 1 70  ? -7.018  10.701  67.064 1.00 23.68 ? 334 PHE   A CE2  1 
ATOM   594  C  CZ   . PHE   A 1 70  ? -7.543  9.411   66.853 1.00 22.09 ? 334 PHE   A CZ   1 
ATOM   595  N  N    . ALA   A 1 71  ? -9.577  14.228  65.132 1.00 19.21 ? 335 ALA   A N    1 
ATOM   596  C  CA   . ALA   A 1 71  ? -10.280 14.648  66.356 1.00 20.13 ? 335 ALA   A CA   1 
ATOM   597  C  C    . ALA   A 1 71  ? -11.778 14.817  66.085 1.00 20.16 ? 335 ALA   A C    1 
ATOM   598  O  O    . ALA   A 1 71  ? -12.632 14.357  66.856 1.00 22.53 ? 335 ALA   A O    1 
ATOM   599  C  CB   . ALA   A 1 71  ? -9.661  15.961  66.895 1.00 23.91 ? 335 ALA   A CB   1 
ATOM   600  N  N    . LYS   A 1 72  ? -12.112 15.436  64.968 1.00 19.68 ? 336 LYS   A N    1 
ATOM   601  C  CA   . LYS   A 1 72  ? -13.535 15.696  64.676 1.00 22.04 ? 336 LYS   A CA   1 
ATOM   602  C  C    . LYS   A 1 72  ? -14.341 14.439  64.409 1.00 26.48 ? 336 LYS   A C    1 
ATOM   603  O  O    . LYS   A 1 72  ? -15.598 14.463  64.524 1.00 24.52 ? 336 LYS   A O    1 
ATOM   604  C  CB   . LYS   A 1 72  ? -13.655 16.625  63.480 1.00 22.09 ? 336 LYS   A CB   1 
ATOM   605  C  CG   . LYS   A 1 72  ? -13.259 18.047  63.828 1.00 20.61 ? 336 LYS   A CG   1 
ATOM   606  C  CD   . LYS   A 1 72  ? -13.186 18.881  62.553 1.00 24.12 ? 336 LYS   A CD   1 
ATOM   607  C  CE   . LYS   A 1 72  ? -12.819 20.312  62.895 1.00 27.96 ? 336 LYS   A CE   1 
ATOM   608  N  NZ   . LYS   A 1 72  ? -12.578 21.069  61.624 1.00 30.67 ? 336 LYS   A NZ   1 
ATOM   609  N  N    . ARG   A 1 73  ? -13.671 13.369  64.022 1.00 23.59 ? 337 ARG   A N    1 
ATOM   610  C  CA   . ARG   A 1 73  ? -14.354 12.115  63.766 1.00 24.26 ? 337 ARG   A CA   1 
ATOM   611  C  C    . ARG   A 1 73  ? -14.323 11.243  64.984 1.00 26.45 ? 337 ARG   A C    1 
ATOM   612  O  O    . ARG   A 1 73  ? -15.011 10.245  65.049 1.00 33.39 ? 337 ARG   A O    1 
ATOM   613  C  CB   . ARG   A 1 73  ? -13.681 11.371  62.621 1.00 22.54 ? 337 ARG   A CB   1 
ATOM   614  C  CG   . ARG   A 1 73  ? -13.759 12.102  61.310 1.00 26.87 ? 337 ARG   A CG   1 
ATOM   615  C  CD   . ARG   A 1 73  ? -13.082 11.360  60.191 1.00 28.62 ? 337 ARG   A CD   1 
ATOM   616  N  NE   . ARG   A 1 73  ? -13.460 11.961  58.923 1.00 42.36 ? 337 ARG   A NE   1 
ATOM   617  C  CZ   . ARG   A 1 73  ? -14.346 11.438  58.087 1.00 52.74 ? 337 ARG   A CZ   1 
ATOM   618  N  NH1  . ARG   A 1 73  ? -14.926 10.285  58.374 1.00 54.50 ? 337 ARG   A NH1  1 
ATOM   619  N  NH2  . ARG   A 1 73  ? -14.651 12.066  56.962 1.00 42.44 ? 337 ARG   A NH2  1 
ATOM   620  N  N    . LEU   A 1 74  ? -13.568 11.647  65.978 1.00 33.36 ? 338 LEU   A N    1 
ATOM   621  C  CA   . LEU   A 1 74  ? -13.351 10.811  67.145 1.00 35.63 ? 338 LEU   A CA   1 
ATOM   622  C  C    . LEU   A 1 74  ? -14.642 10.784  67.938 1.00 34.78 ? 338 LEU   A C    1 
ATOM   623  O  O    . LEU   A 1 74  ? -15.239 11.835  68.234 1.00 35.02 ? 338 LEU   A O    1 
ATOM   624  C  CB   . LEU   A 1 74  ? -12.210 11.347  67.959 1.00 37.71 ? 338 LEU   A CB   1 
ATOM   625  C  CG   . LEU   A 1 74  ? -11.599 10.478  69.021 1.00 44.32 ? 338 LEU   A CG   1 
ATOM   626  C  CD1  . LEU   A 1 74  ? -10.939 9.271   68.381 1.00 44.84 ? 338 LEU   A CD1  1 
ATOM   627  C  CD2  . LEU   A 1 74  ? -10.596 11.347  69.731 1.00 45.87 ? 338 LEU   A CD2  1 
ATOM   628  N  N    . SER   A 1 75  ? -15.109 9.574   68.256 1.00 34.41 ? 339 SER   A N    1 
ATOM   629  C  CA   . SER   A 1 75  ? -16.328 9.419   69.038 1.00 34.75 ? 339 SER   A CA   1 
ATOM   630  C  C    . SER   A 1 75  ? -16.268 10.267  70.319 1.00 41.07 ? 339 SER   A C    1 
ATOM   631  O  O    . SER   A 1 75  ? -15.371 10.099  71.137 1.00 45.68 ? 339 SER   A O    1 
ATOM   632  C  CB   . SER   A 1 75  ? -16.553 7.941   69.370 1.00 36.13 ? 339 SER   A CB   1 
ATOM   633  O  OG   . SER   A 1 75  ? -17.774 7.742   70.090 1.00 44.58 ? 339 SER   A OG   1 
ATOM   634  N  N    . GLY   A 1 76  ? -17.197 11.208  70.468 1.00 29.70 ? 340 GLY   A N    1 
ATOM   635  C  CA   . GLY   A 1 76  ? -17.306 11.994  71.688 1.00 29.44 ? 340 GLY   A CA   1 
ATOM   636  C  C    . GLY   A 1 76  ? -16.714 13.378  71.639 1.00 31.50 ? 340 GLY   A C    1 
ATOM   637  O  O    . GLY   A 1 76  ? -17.064 14.228  72.435 1.00 31.29 ? 340 GLY   A O    1 
ATOM   638  N  N    . PHE   A 1 77  ? -15.836 13.626  70.682 1.00 29.37 ? 341 PHE   A N    1 
ATOM   639  C  CA   . PHE   A 1 77  ? -15.191 14.925  70.600 1.00 24.14 ? 341 PHE   A CA   1 
ATOM   640  C  C    . PHE   A 1 77  ? -16.133 16.046  70.196 1.00 25.36 ? 341 PHE   A C    1 
ATOM   641  O  O    . PHE   A 1 77  ? -16.060 17.148  70.742 1.00 24.10 ? 341 PHE   A O    1 
ATOM   642  C  CB   . PHE   A 1 77  ? -13.994 14.843  69.629 1.00 22.71 ? 341 PHE   A CB   1 
ATOM   643  C  CG   . PHE   A 1 77  ? -13.182 16.099  69.570 1.00 23.17 ? 341 PHE   A CG   1 
ATOM   644  C  CD1  . PHE   A 1 77  ? -12.160 16.305  70.470 1.00 22.77 ? 341 PHE   A CD1  1 
ATOM   645  C  CD2  . PHE   A 1 77  ? -13.388 17.033  68.571 1.00 23.49 ? 341 PHE   A CD2  1 
ATOM   646  C  CE1  . PHE   A 1 77  ? -11.358 17.492  70.373 1.00 20.82 ? 341 PHE   A CE1  1 
ATOM   647  C  CE2  . PHE   A 1 77  ? -12.625 18.202  68.463 1.00 25.68 ? 341 PHE   A CE2  1 
ATOM   648  C  CZ   . PHE   A 1 77  ? -11.590 18.427  69.358 1.00 20.36 ? 341 PHE   A CZ   1 
ATOM   649  N  N    . MET   A 1 78  ? -17.012 15.768  69.231 1.00 28.09 ? 342 MET   A N    1 
ATOM   650  C  CA   . MET   A 1 78  ? -17.936 16.784  68.773 1.00 31.09 ? 342 MET   A CA   1 
ATOM   651  C  C    . MET   A 1 78  ? -19.009 17.070  69.809 1.00 33.01 ? 342 MET   A C    1 
ATOM   652  O  O    . MET   A 1 78  ? -19.750 18.042  69.660 1.00 37.11 ? 342 MET   A O    1 
ATOM   653  C  CB   . MET   A 1 78  ? -18.556 16.363  67.459 1.00 34.87 ? 342 MET   A CB   1 
ATOM   654  C  CG   . MET   A 1 78  ? -17.586 16.314  66.348 1.00 36.20 ? 342 MET   A CG   1 
ATOM   655  S  SD   . MET   A 1 78  ? -16.647 17.845  66.156 1.00 37.98 ? 342 MET   A SD   1 
ATOM   656  C  CE   . MET   A 1 78  ? -17.007 18.209  64.412 1.00 43.68 ? 342 MET   A CE   1 
ATOM   657  N  N    . GLU   A 1 79  ? -19.083 16.275  70.873 1.00 32.64 ? 343 GLU   A N    1 
ATOM   658  C  CA   . GLU   A 1 79  ? -20.013 16.592  71.970 1.00 37.94 ? 343 GLU   A CA   1 
ATOM   659  C  C    . GLU   A 1 79  ? -19.485 17.725  72.851 1.00 32.27 ? 343 GLU   A C    1 
ATOM   660  O  O    . GLU   A 1 79  ? -20.259 18.410  73.536 1.00 38.48 ? 343 GLU   A O    1 
ATOM   661  C  CB   . GLU   A 1 79  ? -20.280 15.358  72.830 1.00 50.39 ? 343 GLU   A CB   1 
ATOM   662  C  CG   . GLU   A 1 79  ? -21.110 14.286  72.130 1.00 63.73 ? 343 GLU   A CG   1 
ATOM   663  C  CD   . GLU   A 1 79  ? -20.997 12.926  72.806 1.00 73.88 ? 343 GLU   A CD   1 
ATOM   664  O  OE1  . GLU   A 1 79  ? -20.597 12.878  73.992 1.00 74.90 ? 343 GLU   A OE1  1 
ATOM   665  O  OE2  . GLU   A 1 79  ? -21.297 11.903  72.146 1.00 78.41 ? 343 GLU   A OE2  1 
ATOM   666  N  N    . LEU   A 1 80  ? -18.164 17.920  72.837 1.00 28.13 ? 344 LEU   A N    1 
ATOM   667  C  CA   . LEU   A 1 80  ? -17.605 18.990  73.627 1.00 27.21 ? 344 LEU   A CA   1 
ATOM   668  C  C    . LEU   A 1 80  ? -17.930 20.326  73.024 1.00 30.81 ? 344 LEU   A C    1 
ATOM   669  O  O    . LEU   A 1 80  ? -18.011 20.458  71.793 1.00 29.01 ? 344 LEU   A O    1 
ATOM   670  C  CB   . LEU   A 1 80  ? -16.100 18.845  73.723 1.00 24.34 ? 344 LEU   A CB   1 
ATOM   671  C  CG   . LEU   A 1 80  ? -15.609 17.487  74.197 1.00 29.36 ? 344 LEU   A CG   1 
ATOM   672  C  CD1  . LEU   A 1 80  ? -14.074 17.424  74.180 1.00 27.92 ? 344 LEU   A CD1  1 
ATOM   673  C  CD2  . LEU   A 1 80  ? -16.142 17.188  75.586 1.00 35.00 ? 344 LEU   A CD2  1 
ATOM   674  N  N    . CYS   A 1 81  ? -18.004 21.353  73.868 1.00 31.06 ? 345 CYS   A N    1 
ATOM   675  C  CA   . CYS   A 1 81  ? -18.239 22.694  73.345 1.00 31.61 ? 345 CYS   A CA   1 
ATOM   676  C  C    . CYS   A 1 81  ? -17.040 23.169  72.520 1.00 32.69 ? 345 CYS   A C    1 
ATOM   677  O  O    . CYS   A 1 81  ? -15.907 22.698  72.683 1.00 28.09 ? 345 CYS   A O    1 
ATOM   678  C  CB   . CYS   A 1 81  ? -18.538 23.681  74.478 1.00 34.03 ? 345 CYS   A CB   1 
ATOM   679  S  SG   . CYS   A 1 81  ? -17.059 24.044  75.499 1.00 36.14 ? 345 CYS   A SG   1 
ATOM   680  N  N    . GLN   A 1 82  ? -17.297 24.108  71.619 1.00 32.09 ? 346 GLN   A N    1 
ATOM   681  C  CA   . GLN   A 1 82  ? -16.240 24.499  70.694 1.00 29.32 ? 346 GLN   A CA   1 
ATOM   682  C  C    . GLN   A 1 82  ? -15.010 24.986  71.433 1.00 28.20 ? 346 GLN   A C    1 
ATOM   683  O  O    . GLN   A 1 82  ? -13.891 24.682  71.012 1.00 25.19 ? 346 GLN   A O    1 
ATOM   684  C  CB   . GLN   A 1 82  ? -16.748 25.577  69.748 1.00 36.57 ? 346 GLN   A CB   1 
ATOM   685  C  CG   . GLN   A 1 82  ? -17.691 25.012  68.733 1.00 59.80 ? 346 GLN   A CG   1 
ATOM   686  C  CD   . GLN   A 1 82  ? -16.962 24.562  67.487 1.00 73.22 ? 346 GLN   A CD   1 
ATOM   687  O  OE1  . GLN   A 1 82  ? -15.887 25.077  67.183 1.00 77.84 ? 346 GLN   A OE1  1 
ATOM   688  N  NE2  . GLN   A 1 82  ? -17.542 23.610  66.751 1.00 75.30 ? 346 GLN   A NE2  1 
ATOM   689  N  N    . ASN   A 1 83  ? -15.200 25.700  72.542 1.00 30.04 ? 347 ASN   A N    1 
ATOM   690  C  CA   . ASN   A 1 83  ? -14.030 26.192  73.286 1.00 30.18 ? 347 ASN   A CA   1 
ATOM   691  C  C    . ASN   A 1 83  ? -13.104 25.041  73.703 1.00 25.78 ? 347 ASN   A C    1 
ATOM   692  O  O    . ASN   A 1 83  ? -11.857 25.128  73.615 1.00 27.58 ? 347 ASN   A O    1 
ATOM   693  C  CB   . ASN   A 1 83  ? -14.461 26.972  74.534 1.00 33.94 ? 347 ASN   A CB   1 
ATOM   694  C  CG   . ASN   A 1 83  ? -13.291 27.316  75.437 1.00 43.90 ? 347 ASN   A CG   1 
ATOM   695  O  OD1  . ASN   A 1 83  ? -12.933 26.551  76.349 1.00 43.07 ? 347 ASN   A OD1  1 
ATOM   696  N  ND2  . ASN   A 1 83  ? -12.662 28.450  75.171 1.00 48.62 ? 347 ASN   A ND2  1 
ATOM   697  N  N    . ASP   A 1 84  ? -13.725 23.988  74.198 1.00 26.47 ? 348 ASP   A N    1 
ATOM   698  C  CA   . ASP   A 1 84  ? -12.978 22.873  74.733 1.00 26.05 ? 348 ASP   A CA   1 
ATOM   699  C  C    . ASP   A 1 84  ? -12.317 22.060  73.605 1.00 26.26 ? 348 ASP   A C    1 
ATOM   700  O  O    . ASP   A 1 84  ? -11.179 21.609  73.761 1.00 24.00 ? 348 ASP   A O    1 
ATOM   701  C  CB   . ASP   A 1 84  ? -13.900 22.035  75.603 1.00 23.26 ? 348 ASP   A CB   1 
ATOM   702  C  CG   . ASP   A 1 84  ? -14.109 22.641  76.975 1.00 29.95 ? 348 ASP   A CG   1 
ATOM   703  O  OD1  . ASP   A 1 84  ? -13.636 23.772  77.214 1.00 30.91 ? 348 ASP   A OD1  1 
ATOM   704  O  OD2  . ASP   A 1 84  ? -14.761 21.982  77.807 1.00 33.16 ? 348 ASP   A OD2  1 
ATOM   705  N  N    . GLN   A 1 85  ? -12.995 21.903  72.453 1.00 21.29 ? 349 GLN   A N    1 
ATOM   706  C  CA   . GLN   A 1 85  ? -12.349 21.311  71.280 1.00 22.76 ? 349 GLN   A CA   1 
ATOM   707  C  C    . GLN   A 1 85  ? -11.084 22.046  70.903 1.00 18.70 ? 349 GLN   A C    1 
ATOM   708  O  O    . GLN   A 1 85  ? -10.060 21.412  70.601 1.00 22.48 ? 349 GLN   A O    1 
ATOM   709  C  CB   . GLN   A 1 85  ? -13.285 21.338  70.080 1.00 23.83 ? 349 GLN   A CB   1 
ATOM   710  C  CG   . GLN   A 1 85  ? -14.584 20.559  70.302 1.00 24.06 ? 349 GLN   A CG   1 
ATOM   711  C  CD   . GLN   A 1 85  ? -15.507 20.706  69.112 1.00 30.85 ? 349 GLN   A CD   1 
ATOM   712  O  OE1  . GLN   A 1 85  ? -15.051 20.996  68.007 1.00 28.23 ? 349 GLN   A OE1  1 
ATOM   713  N  NE2  . GLN   A 1 85  ? -16.834 20.578  69.339 1.00 31.03 ? 349 GLN   A NE2  1 
ATOM   714  N  N    . ILE   A 1 86  ? -11.185 23.380  70.884 1.00 20.78 ? 350 ILE   A N    1 
ATOM   715  C  CA   . ILE   A 1 86  ? -10.046 24.229  70.542 1.00 22.16 ? 350 ILE   A CA   1 
ATOM   716  C  C    . ILE   A 1 86  ? -8.918  24.075  71.590 1.00 21.01 ? 350 ILE   A C    1 
ATOM   717  O  O    . ILE   A 1 86  ? -7.772  23.925  71.221 1.00 23.41 ? 350 ILE   A O    1 
ATOM   718  C  CB   . ILE   A 1 86  ? -10.483 25.689  70.362 1.00 23.48 ? 350 ILE   A CB   1 
ATOM   719  C  CG1  . ILE   A 1 86  ? -11.314 25.749  69.094 1.00 26.41 ? 350 ILE   A CG1  1 
ATOM   720  C  CG2  . ILE   A 1 86  ? -9.237  26.609  70.277 1.00 23.70 ? 350 ILE   A CG2  1 
ATOM   721  C  CD1  . ILE   A 1 86  ? -12.043 27.074  68.916 1.00 24.84 ? 350 ILE   A CD1  1 
ATOM   722  N  N    . VAL   A 1 87  ? -9.277  24.076  72.865 1.00 23.10 ? 351 VAL   A N    1 
ATOM   723  C  CA   . VAL   A 1 87  ? -8.274  23.888  73.909 1.00 22.95 ? 351 VAL   A CA   1 
ATOM   724  C  C    . VAL   A 1 87  ? -7.550  22.561  73.730 1.00 22.11 ? 351 VAL   A C    1 
ATOM   725  O  O    . VAL   A 1 87  ? -6.301  22.518  73.767 1.00 23.17 ? 351 VAL   A O    1 
ATOM   726  C  CB   . VAL   A 1 87  ? -8.906  23.971  75.270 1.00 26.03 ? 351 VAL   A CB   1 
ATOM   727  C  CG1  . VAL   A 1 87  ? -7.937  23.483  76.362 1.00 24.30 ? 351 VAL   A CG1  1 
ATOM   728  C  CG2  . VAL   A 1 87  ? -9.406  25.410  75.524 1.00 28.62 ? 351 VAL   A CG2  1 
ATOM   729  N  N    . LEU   A 1 88  ? -8.305  21.484  73.507 1.00 20.94 ? 352 LEU   A N    1 
ATOM   730  C  CA   . LEU   A 1 88  ? -7.655  20.185  73.396 1.00 20.09 ? 352 LEU   A CA   1 
ATOM   731  C  C    . LEU   A 1 88  ? -6.772  20.102  72.190 1.00 20.88 ? 352 LEU   A C    1 
ATOM   732  O  O    . LEU   A 1 88  ? -5.673  19.546  72.279 1.00 21.06 ? 352 LEU   A O    1 
ATOM   733  C  CB   . LEU   A 1 88  ? -8.715  19.055  73.384 1.00 21.04 ? 352 LEU   A CB   1 
ATOM   734  C  CG   . LEU   A 1 88  ? -9.506  18.925  74.674 1.00 21.02 ? 352 LEU   A CG   1 
ATOM   735  C  CD1  . LEU   A 1 88  ? -10.552 17.808  74.505 1.00 22.24 ? 352 LEU   A CD1  1 
ATOM   736  C  CD2  . LEU   A 1 88  ? -8.600  18.594  75.855 1.00 22.99 ? 352 LEU   A CD2  1 
ATOM   737  N  N    . LEU   A 1 89  ? -7.199  20.634  71.040 1.00 21.07 ? 353 LEU   A N    1 
ATOM   738  C  CA   . LEU   A 1 89  ? -6.345  20.571  69.850 1.00 21.47 ? 353 LEU   A CA   1 
ATOM   739  C  C    . LEU   A 1 89  ? -5.112  21.498  69.934 1.00 22.17 ? 353 LEU   A C    1 
ATOM   740  O  O    . LEU   A 1 89  ? -4.025  21.186  69.411 1.00 23.66 ? 353 LEU   A O    1 
ATOM   741  C  CB   . LEU   A 1 89  ? -7.159  20.874  68.597 1.00 26.08 ? 353 LEU   A CB   1 
ATOM   742  C  CG   . LEU   A 1 89  ? -7.884  19.614  68.137 1.00 24.72 ? 353 LEU   A CG   1 
ATOM   743  C  CD1  . LEU   A 1 89  ? -8.890  20.019  67.098 1.00 24.60 ? 353 LEU   A CD1  1 
ATOM   744  C  CD2  . LEU   A 1 89  ? -6.946  18.608  67.505 1.00 25.56 ? 353 LEU   A CD2  1 
ATOM   745  N  N    . LYS   A 1 90  ? -5.279  22.677  70.513 1.00 22.94 ? 354 LYS   A N    1 
ATOM   746  C  CA   . LYS   A 1 90  ? -4.160  23.602  70.594 1.00 25.52 ? 354 LYS   A CA   1 
ATOM   747  C  C    . LYS   A 1 90  ? -3.071  22.944  71.442 1.00 31.35 ? 354 LYS   A C    1 
ATOM   748  O  O    . LYS   A 1 90  ? -1.880  23.054  71.146 1.00 29.10 ? 354 LYS   A O    1 
ATOM   749  C  CB   . LYS   A 1 90  ? -4.635  24.932  71.176 1.00 30.58 ? 354 LYS   A CB   1 
ATOM   750  C  CG   . LYS   A 1 90  ? -3.619  26.043  71.044 1.00 49.78 ? 354 LYS   A CG   1 
ATOM   751  C  CD   . LYS   A 1 90  ? -4.312  27.405  71.093 1.00 58.81 ? 354 LYS   A CD   1 
ATOM   752  C  CE   . LYS   A 1 90  ? -4.763  27.723  72.490 1.00 60.74 ? 354 LYS   A CE   1 
ATOM   753  N  NZ   . LYS   A 1 90  ? -5.127  29.158  72.626 1.00 62.91 ? 354 LYS   A NZ   1 
ATOM   754  N  N    . ALA   A 1 91  ? -3.515  22.234  72.479 1.00 28.13 ? 355 ALA   A N    1 
ATOM   755  C  CA   . ALA   A 1 91  ? -2.621  21.618  73.446 1.00 28.20 ? 355 ALA   A CA   1 
ATOM   756  C  C    . ALA   A 1 91  ? -2.019  20.292  72.957 1.00 30.69 ? 355 ALA   A C    1 
ATOM   757  O  O    . ALA   A 1 91  ? -0.882  19.941  73.334 1.00 30.91 ? 355 ALA   A O    1 
ATOM   758  C  CB   . ALA   A 1 91  ? -3.363  21.381  74.716 1.00 27.05 ? 355 ALA   A CB   1 
ATOM   759  N  N    . GLY   A 1 92  ? -2.779  19.561  72.131 1.00 24.49 ? 356 GLY   A N    1 
ATOM   760  C  CA   . GLY   A 1 92  ? -2.452  18.190  71.785 1.00 26.46 ? 356 GLY   A CA   1 
ATOM   761  C  C    . GLY   A 1 92  ? -2.179  17.828  70.335 1.00 23.44 ? 356 GLY   A C    1 
ATOM   762  O  O    . GLY   A 1 92  ? -1.682  16.743  70.074 1.00 22.69 ? 356 GLY   A O    1 
ATOM   763  N  N    . ALA   A 1 93  ? -2.496  18.685  69.384 1.00 23.63 ? 357 ALA   A N    1 
ATOM   764  C  CA   . ALA   A 1 93  ? -2.402  18.269  67.990 1.00 22.61 ? 357 ALA   A CA   1 
ATOM   765  C  C    . ALA   A 1 93  ? -0.955  18.011  67.572 1.00 22.02 ? 357 ALA   A C    1 
ATOM   766  O  O    . ALA   A 1 93  ? -0.687  17.023  66.880 1.00 22.57 ? 357 ALA   A O    1 
ATOM   767  C  CB   . ALA   A 1 93  ? -3.041  19.294  67.087 1.00 26.31 ? 357 ALA   A CB   1 
ATOM   768  N  N    . MET   A 1 94  ? -0.030  18.891  67.976 1.00 25.00 ? 358 MET   A N    1 
ATOM   769  C  CA   . MET   A 1 94  ? 1.377   18.694  67.645 1.00 21.54 ? 358 MET   A CA   1 
ATOM   770  C  C    . MET   A 1 94  ? 1.892   17.413  68.295 1.00 24.92 ? 358 MET   A C    1 
ATOM   771  O  O    . MET   A 1 94  ? 2.716   16.659  67.730 1.00 23.85 ? 358 MET   A O    1 
ATOM   772  C  CB   . MET   A 1 94  ? 2.208   19.912  68.119 1.00 28.30 ? 358 MET   A CB   1 
ATOM   773  C  CG   . MET   A 1 94  ? 3.550   19.934  67.502 1.00 28.39 ? 358 MET   A CG   1 
ATOM   774  S  SD   . MET   A 1 94  ? 3.472   19.966  65.720 1.00 31.74 ? 358 MET   A SD   1 
ATOM   775  C  CE   . MET   A 1 94  ? 5.061   19.180  65.411 1.00 29.55 ? 358 MET   A CE   1 
ATOM   776  N  N    . GLU   A 1 95  ? 1.440   17.146  69.514 1.00 24.74 ? 359 GLU   A N    1 
ATOM   777  C  CA   . GLU   A 1 95  ? 1.844   15.922  70.173 1.00 24.21 ? 359 GLU   A CA   1 
ATOM   778  C  C    . GLU   A 1 95  ? 1.397   14.703  69.365 1.00 23.51 ? 359 GLU   A C    1 
ATOM   779  O  O    . GLU   A 1 95  ? 2.130   13.752  69.195 1.00 25.28 ? 359 GLU   A O    1 
ATOM   780  C  CB   . GLU   A 1 95  ? 1.319   15.919  71.616 1.00 28.23 ? 359 GLU   A CB   1 
ATOM   781  C  CG   . GLU   A 1 95  ? 1.705   17.241  72.390 1.00 38.85 ? 359 GLU   A CG   1 
ATOM   782  C  CD   . GLU   A 1 95  ? 1.191   17.320  73.858 1.00 44.89 ? 359 GLU   A CD   1 
ATOM   783  O  OE1  . GLU   A 1 95  ? 0.401   16.463  74.288 1.00 32.38 ? 359 GLU   A OE1  1 
ATOM   784  O  OE2  . GLU   A 1 95  ? 1.585   18.255  74.586 1.00 50.82 ? 359 GLU   A OE2  1 
ATOM   785  N  N    . VAL   A 1 96  ? 0.191   14.737  68.805 1.00 18.09 ? 360 VAL   A N    1 
ATOM   786  C  CA   . VAL   A 1 96  ? -0.214  13.637  67.966 1.00 17.34 ? 360 VAL   A CA   1 
ATOM   787  C  C    . VAL   A 1 96  ? 0.627   13.563  66.697 1.00 19.06 ? 360 VAL   A C    1 
ATOM   788  O  O    . VAL   A 1 96  ? 0.914   12.462  66.210 1.00 20.41 ? 360 VAL   A O    1 
ATOM   789  C  CB   . VAL   A 1 96  ? -1.715  13.739  67.618 1.00 17.21 ? 360 VAL   A CB   1 
ATOM   790  C  CG1  . VAL   A 1 96  ? -2.117  12.658  66.563 1.00 19.32 ? 360 VAL   A CG1  1 
ATOM   791  C  CG2  . VAL   A 1 96  ? -2.542  13.592  68.921 1.00 22.22 ? 360 VAL   A CG2  1 
ATOM   792  N  N    . VAL   A 1 97  ? 0.956   14.700  66.105 1.00 20.48 ? 361 VAL   A N    1 
ATOM   793  C  CA   . VAL   A 1 97  ? 1.775   14.704  64.896 1.00 19.43 ? 361 VAL   A CA   1 
ATOM   794  C  C    . VAL   A 1 97  ? 3.087   13.966  65.207 1.00 20.84 ? 361 VAL   A C    1 
ATOM   795  O  O    . VAL   A 1 97  ? 3.512   13.119  64.450 1.00 22.04 ? 361 VAL   A O    1 
ATOM   796  C  CB   . VAL   A 1 97  ? 2.067   16.120  64.413 1.00 20.15 ? 361 VAL   A CB   1 
ATOM   797  C  CG1  . VAL   A 1 97  ? 3.194   16.115  63.345 1.00 20.08 ? 361 VAL   A CG1  1 
ATOM   798  C  CG2  . VAL   A 1 97  ? 0.768   16.718  63.830 1.00 21.14 ? 361 VAL   A CG2  1 
ATOM   799  N  N    . LEU   A 1 98  ? 3.688   14.303  66.336 1.00 21.19 ? 362 LEU   A N    1 
ATOM   800  C  CA   . LEU   A 1 98  ? 4.974   13.706  66.686 1.00 23.03 ? 362 LEU   A CA   1 
ATOM   801  C  C    . LEU   A 1 98  ? 4.883   12.218  66.974 1.00 22.89 ? 362 LEU   A C    1 
ATOM   802  O  O    . LEU   A 1 98  ? 5.843   11.474  66.698 1.00 29.40 ? 362 LEU   A O    1 
ATOM   803  C  CB   . LEU   A 1 98  ? 5.554   14.436  67.882 1.00 22.83 ? 362 LEU   A CB   1 
ATOM   804  C  CG   . LEU   A 1 98  ? 5.999   15.888  67.595 1.00 24.79 ? 362 LEU   A CG   1 
ATOM   805  C  CD1  . LEU   A 1 98  ? 6.223   16.680  68.898 1.00 27.48 ? 362 LEU   A CD1  1 
ATOM   806  C  CD2  . LEU   A 1 98  ? 7.280   15.901  66.782 1.00 27.68 ? 362 LEU   A CD2  1 
ATOM   807  N  N    . VAL   A 1 99  ? 3.775   11.768  67.552 1.00 22.46 ? 363 VAL   A N    1 
ATOM   808  C  CA   . VAL   A 1 99  ? 3.565   10.343  67.762 1.00 22.77 ? 363 VAL   A CA   1 
ATOM   809  C  C    . VAL   A 1 99  ? 3.357   9.623   66.443 1.00 24.45 ? 363 VAL   A C    1 
ATOM   810  O  O    . VAL   A 1 99  ? 3.905   8.560   66.225 1.00 22.59 ? 363 VAL   A O    1 
ATOM   811  C  CB   . VAL   A 1 99  ? 2.379   10.094  68.748 1.00 23.23 ? 363 VAL   A CB   1 
ATOM   812  C  CG1  . VAL   A 1 99  ? 1.949   8.601   68.788 1.00 23.21 ? 363 VAL   A CG1  1 
ATOM   813  C  CG2  . VAL   A 1 99  ? 2.784   10.573  70.152 1.00 25.38 ? 363 VAL   A CG2  1 
ATOM   814  N  N    . ARG   A 1 100 ? 2.517   10.179  65.573 1.00 25.17 ? 364 ARG   A N    1 
ATOM   815  C  CA   . ARG   A 1 100 ? 2.244   9.615   64.254 1.00 22.17 ? 364 ARG   A CA   1 
ATOM   816  C  C    . ARG   A 1 100 ? 3.529   9.417   63.448 1.00 24.87 ? 364 ARG   A C    1 
ATOM   817  O  O    . ARG   A 1 100 ? 3.651   8.492   62.646 1.00 23.10 ? 364 ARG   A O    1 
ATOM   818  C  CB   . ARG   A 1 100 ? 1.295   10.527  63.497 1.00 19.15 ? 364 ARG   A CB   1 
ATOM   819  C  CG   . ARG   A 1 100 ? -0.148  10.350  63.890 1.00 20.40 ? 364 ARG   A CG   1 
ATOM   820  C  CD   . ARG   A 1 100 ? -1.054  11.410  63.191 1.00 21.80 ? 364 ARG   A CD   1 
ATOM   821  N  NE   . ARG   A 1 100 ? -2.443  11.011  63.272 1.00 20.32 ? 364 ARG   A NE   1 
ATOM   822  C  CZ   . ARG   A 1 100 ? -3.300  11.076  62.276 1.00 22.64 ? 364 ARG   A CZ   1 
ATOM   823  N  NH1  . ARG   A 1 100 ? -2.958  11.636  61.121 1.00 25.39 ? 364 ARG   A NH1  1 
ATOM   824  N  NH2  . ARG   A 1 100 ? -4.531  10.629  62.453 1.00 23.80 ? 364 ARG   A NH2  1 
ATOM   825  N  N    . MET   A 1 101 ? 4.490   10.313  63.664 1.00 23.45 ? 365 MET   A N    1 
ATOM   826  C  CA   . MET   A 1 101 ? 5.725   10.282  62.919 1.00 23.37 ? 365 MET   A CA   1 
ATOM   827  C  C    . MET   A 1 101 ? 6.517   8.973   63.100 1.00 24.52 ? 365 MET   A C    1 
ATOM   828  O  O    . MET   A 1 101 ? 7.282   8.591   62.224 1.00 22.61 ? 365 MET   A O    1 
ATOM   829  C  CB   . MET   A 1 101 ? 6.558   11.487  63.306 1.00 28.34 ? 365 MET   A CB   1 
ATOM   830  C  CG   . MET   A 1 101 ? 7.915   11.453  62.741 1.00 27.33 ? 365 MET   A CG   1 
ATOM   831  S  SD   . MET   A 1 101 ? 8.720   13.039  63.029 1.00 33.81 ? 365 MET   A SD   1 
ATOM   832  C  CE   . MET   A 1 101 ? 7.437   14.130  62.412 1.00 29.13 ? 365 MET   A CE   1 
ATOM   833  N  N    . CYS   A 1 102 ? 6.355   8.288   64.222 1.00 23.49 ? 366 CYS   A N    1 
ATOM   834  C  CA   . CYS   A 1 102 ? 7.146   7.052   64.408 1.00 23.81 ? 366 CYS   A CA   1 
ATOM   835  C  C    . CYS   A 1 102 ? 6.795   5.986   63.360 1.00 24.36 ? 366 CYS   A C    1 
ATOM   836  O  O    . CYS   A 1 102 ? 7.610   5.107   63.109 1.00 24.46 ? 366 CYS   A O    1 
ATOM   837  C  CB   . CYS   A 1 102 ? 6.978   6.507   65.817 1.00 25.66 ? 366 CYS   A CB   1 
ATOM   838  S  SG   . CYS   A 1 102 ? 5.413   5.617   66.169 1.00 29.78 ? 366 CYS   A SG   1 
ATOM   839  N  N    . ARG   A 1 103 ? 5.596   6.058   62.747 1.00 21.67 ? 367 ARG   A N    1 
ATOM   840  C  CA   . ARG   A 1 103 ? 5.277   5.123   61.666 1.00 24.77 ? 367 ARG   A CA   1 
ATOM   841  C  C    . ARG   A 1 103 ? 6.208   5.271   60.473 1.00 25.03 ? 367 ARG   A C    1 
ATOM   842  O  O    . ARG   A 1 103 ? 6.395   4.344   59.659 1.00 24.11 ? 367 ARG   A O    1 
ATOM   843  C  CB   . ARG   A 1 103 ? 3.828   5.338   61.192 1.00 21.61 ? 367 ARG   A CB   1 
ATOM   844  C  CG   . ARG   A 1 103 ? 2.785   5.087   62.260 1.00 24.16 ? 367 ARG   A CG   1 
ATOM   845  C  CD   . ARG   A 1 103 ? 1.434   5.656   61.852 1.00 25.38 ? 367 ARG   A CD   1 
ATOM   846  N  NE   . ARG   A 1 103 ? 0.725   4.878   60.839 1.00 25.14 ? 367 ARG   A NE   1 
ATOM   847  C  CZ   . ARG   A 1 103 ? 0.502   5.259   59.573 1.00 23.28 ? 367 ARG   A CZ   1 
ATOM   848  N  NH1  . ARG   A 1 103 ? 0.970   6.421   59.114 1.00 22.89 ? 367 ARG   A NH1  1 
ATOM   849  N  NH2  . ARG   A 1 103 ? -0.261  4.476   58.773 1.00 26.18 ? 367 ARG   A NH2  1 
ATOM   850  N  N    . ALA   A 1 104 ? 6.757   6.471   60.324 1.00 21.64 ? 368 ALA   A N    1 
ATOM   851  C  CA   . ALA   A 1 104 ? 7.576   6.869   59.190 1.00 21.75 ? 368 ALA   A CA   1 
ATOM   852  C  C    . ALA   A 1 104 ? 9.069   6.853   59.555 1.00 20.46 ? 368 ALA   A C    1 
ATOM   853  O  O    . ALA   A 1 104 ? 9.942   7.230   58.777 1.00 22.38 ? 368 ALA   A O    1 
ATOM   854  C  CB   . ALA   A 1 104 ? 7.135   8.277   58.695 1.00 19.01 ? 368 ALA   A CB   1 
ATOM   855  N  N    . TYR   A 1 105 ? 9.336   6.272   60.708 1.00 19.09 ? 369 TYR   A N    1 
ATOM   856  C  CA   . TYR   A 1 105 ? 10.705  6.193   61.231 1.00 19.78 ? 369 TYR   A CA   1 
ATOM   857  C  C    . TYR   A 1 105 ? 11.254  4.772   61.154 1.00 24.08 ? 369 TYR   A C    1 
ATOM   858  O  O    . TYR   A 1 105 ? 10.603  3.823   61.608 1.00 24.09 ? 369 TYR   A O    1 
ATOM   859  C  CB   . TYR   A 1 105 ? 10.734  6.694   62.680 1.00 21.63 ? 369 TYR   A CB   1 
ATOM   860  C  CG   . TYR   A 1 105 ? 12.134  6.647   63.314 1.00 20.22 ? 369 TYR   A CG   1 
ATOM   861  C  CD1  . TYR   A 1 105 ? 13.082  7.613   63.030 1.00 21.73 ? 369 TYR   A CD1  1 
ATOM   862  C  CD2  . TYR   A 1 105 ? 12.488  5.602   64.166 1.00 21.17 ? 369 TYR   A CD2  1 
ATOM   863  C  CE1  . TYR   A 1 105 ? 14.357  7.565   63.598 1.00 23.10 ? 369 TYR   A CE1  1 
ATOM   864  C  CE2  . TYR   A 1 105 ? 13.744  5.545   64.748 1.00 21.94 ? 369 TYR   A CE2  1 
ATOM   865  C  CZ   . TYR   A 1 105 ? 14.678  6.526   64.467 1.00 23.59 ? 369 TYR   A CZ   1 
ATOM   866  O  OH   . TYR   A 1 105 ? 15.912  6.419   65.056 1.00 30.40 ? 369 TYR   A OH   1 
ATOM   867  N  N    . ASN   A 1 106 ? 12.507  4.655   60.682 1.00 20.74 ? 370 ASN   A N    1 
ATOM   868  C  CA   . ASN   A 1 106 ? 13.164  3.348   60.566 1.00 22.02 ? 370 ASN   A CA   1 
ATOM   869  C  C    . ASN   A 1 106 ? 14.278  3.300   61.610 1.00 23.30 ? 370 ASN   A C    1 
ATOM   870  O  O    . ASN   A 1 106 ? 15.293  3.959   61.456 1.00 24.52 ? 370 ASN   A O    1 
ATOM   871  C  CB   . ASN   A 1 106 ? 13.703  3.129   59.134 1.00 24.81 ? 370 ASN   A CB   1 
ATOM   872  C  CG   . ASN   A 1 106 ? 14.379  1.773   58.975 1.00 26.65 ? 370 ASN   A CG   1 
ATOM   873  O  OD1  . ASN   A 1 106 ? 14.370  0.985   59.892 1.00 30.75 ? 370 ASN   A OD1  1 
ATOM   874  N  ND2  . ASN   A 1 106 ? 14.969  1.521   57.823 1.00 29.39 ? 370 ASN   A ND2  1 
ATOM   875  N  N    . ALA   A 1 107 ? 14.054  2.562   62.694 1.00 25.82 ? 371 ALA   A N    1 
ATOM   876  C  CA   . ALA   A 1 107 ? 15.055  2.537   63.774 1.00 27.67 ? 371 ALA   A CA   1 
ATOM   877  C  C    . ALA   A 1 107 ? 16.338  1.818   63.384 1.00 28.41 ? 371 ALA   A C    1 
ATOM   878  O  O    . ALA   A 1 107 ? 17.367  2.003   64.038 1.00 29.66 ? 371 ALA   A O    1 
ATOM   879  C  CB   . ALA   A 1 107 ? 14.493  1.891   65.016 1.00 28.48 ? 371 ALA   A CB   1 
ATOM   880  N  N    . ASP   A 1 108 ? 16.294  0.981   62.352 1.00 25.36 ? 372 ASP   A N    1 
ATOM   881  C  CA   . ASP   A 1 108 ? 17.492  0.219   61.962 1.00 29.51 ? 372 ASP   A CA   1 
ATOM   882  C  C    . ASP   A 1 108 ? 18.631  1.095   61.431 1.00 29.44 ? 372 ASP   A C    1 
ATOM   883  O  O    . ASP   A 1 108 ? 19.810  0.774   61.653 1.00 34.35 ? 372 ASP   A O    1 
ATOM   884  C  CB   . ASP   A 1 108 ? 17.115  -0.821  60.906 1.00 37.23 ? 372 ASP   A CB   1 
ATOM   885  C  CG   . ASP   A 1 108 ? 16.123  -1.845  61.426 1.00 50.86 ? 372 ASP   A CG   1 
ATOM   886  O  OD1  . ASP   A 1 108 ? 16.142  -2.137  62.645 1.00 55.37 ? 372 ASP   A OD1  1 
ATOM   887  O  OD2  . ASP   A 1 108 ? 15.331  -2.364  60.613 1.00 58.58 ? 372 ASP   A OD2  1 
ATOM   888  N  N    . ASN   A 1 109 ? 18.300  2.180   60.734 1.00 26.48 ? 373 ASN   A N    1 
ATOM   889  C  CA   . ASN   A 1 109 ? 19.291  3.105   60.235 1.00 27.84 ? 373 ASN   A CA   1 
ATOM   890  C  C    . ASN   A 1 109 ? 18.999  4.552   60.662 1.00 24.68 ? 373 ASN   A C    1 
ATOM   891  O  O    . ASN   A 1 109 ? 19.679  5.465   60.214 1.00 28.68 ? 373 ASN   A O    1 
ATOM   892  C  CB   . ASN   A 1 109 ? 19.417  2.997   58.716 1.00 30.64 ? 373 ASN   A CB   1 
ATOM   893  C  CG   . ASN   A 1 109 ? 18.144  3.331   57.999 1.00 28.04 ? 373 ASN   A CG   1 
ATOM   894  O  OD1  . ASN   A 1 109 ? 17.177  3.771   58.605 1.00 27.14 ? 373 ASN   A OD1  1 
ATOM   895  N  ND2  . ASN   A 1 109 ? 18.134  3.141   56.695 1.00 32.57 ? 373 ASN   A ND2  1 
ATOM   896  N  N    . ARG   A 1 110 ? 18.057  4.731   61.584 1.00 23.92 ? 374 ARG   A N    1 
ATOM   897  C  CA   . ARG   A 1 110 ? 17.758  6.080   62.124 1.00 22.24 ? 374 ARG   A CA   1 
ATOM   898  C  C    . ARG   A 1 110 ? 17.422  7.086   61.013 1.00 25.83 ? 374 ARG   A C    1 
ATOM   899  O  O    . ARG   A 1 110 ? 17.946  8.201   60.931 1.00 27.17 ? 374 ARG   A O    1 
ATOM   900  C  CB   . ARG   A 1 110 ? 18.940  6.562   62.994 1.00 27.27 ? 374 ARG   A CB   1 
ATOM   901  C  CG   . ARG   A 1 110 ? 19.249  5.570   64.111 1.00 35.20 ? 374 ARG   A CG   1 
ATOM   902  C  CD   . ARG   A 1 110 ? 20.162  6.165   65.211 1.00 52.45 ? 374 ARG   A CD   1 
ATOM   903  N  NE   . ARG   A 1 110 ? 19.467  7.215   65.973 1.00 62.87 ? 374 ARG   A NE   1 
ATOM   904  C  CZ   . ARG   A 1 110 ? 18.986  7.078   67.213 1.00 64.12 ? 374 ARG   A CZ   1 
ATOM   905  N  NH1  . ARG   A 1 110 ? 18.367  8.098   67.816 1.00 58.46 ? 374 ARG   A NH1  1 
ATOM   906  N  NH2  . ARG   A 1 110 ? 19.130  5.929   67.859 1.00 66.37 ? 374 ARG   A NH2  1 
ATOM   907  N  N    . THR   A 1 111 ? 16.486  6.694   60.162 1.00 21.66 ? 375 THR   A N    1 
ATOM   908  C  CA   . THR   A 1 111 ? 15.991  7.589   59.130 1.00 21.28 ? 375 THR   A CA   1 
ATOM   909  C  C    . THR   A 1 111 ? 14.471  7.754   59.220 1.00 22.87 ? 375 THR   A C    1 
ATOM   910  O  O    . THR   A 1 111 ? 13.770  6.965   59.841 1.00 22.44 ? 375 THR   A O    1 
ATOM   911  C  CB   . THR   A 1 111 ? 16.321  7.095   57.696 1.00 23.89 ? 375 THR   A CB   1 
ATOM   912  O  OG1  . THR   A 1 111 ? 15.749  5.805   57.476 1.00 25.51 ? 375 THR   A OG1  1 
ATOM   913  C  CG2  . THR   A 1 111 ? 17.830  6.969   57.520 1.00 23.47 ? 375 THR   A CG2  1 
ATOM   914  N  N    . VAL   A 1 112 ? 14.008  8.862   58.632 1.00 20.42 ? 376 VAL   A N    1 
ATOM   915  C  CA   . VAL   A 1 112 ? 12.588  9.192   58.609 1.00 20.02 ? 376 VAL   A CA   1 
ATOM   916  C  C    . VAL   A 1 112 ? 12.169  9.446   57.168 1.00 25.18 ? 376 VAL   A C    1 
ATOM   917  O  O    . VAL   A 1 112 ? 12.949  9.968   56.375 1.00 20.72 ? 376 VAL   A O    1 
ATOM   918  C  CB   . VAL   A 1 112 ? 12.292  10.414  59.520 1.00 18.97 ? 376 VAL   A CB   1 
ATOM   919  C  CG1  . VAL   A 1 112 ? 12.808  11.669  58.923 1.00 22.16 ? 376 VAL   A CG1  1 
ATOM   920  C  CG2  . VAL   A 1 112 ? 10.754  10.528  59.769 1.00 21.11 ? 376 VAL   A CG2  1 
ATOM   921  N  N    . PHE   A 1 113 ? 10.950  9.041   56.817 1.00 20.89 ? 377 PHE   A N    1 
ATOM   922  C  CA   . PHE   A 1 113 ? 10.437  9.306   55.479 1.00 20.80 ? 377 PHE   A CA   1 
ATOM   923  C  C    . PHE   A 1 113 ? 10.109  10.801  55.336 1.00 22.48 ? 377 PHE   A C    1 
ATOM   924  O  O    . PHE   A 1 113 ? 9.328   11.354  56.120 1.00 23.91 ? 377 PHE   A O    1 
ATOM   925  C  CB   . PHE   A 1 113 ? 9.173   8.472   55.235 1.00 22.30 ? 377 PHE   A CB   1 
ATOM   926  C  CG   . PHE   A 1 113 ? 8.705   8.463   53.801 1.00 23.32 ? 377 PHE   A CG   1 
ATOM   927  C  CD1  . PHE   A 1 113 ? 9.441   7.812   52.832 1.00 23.72 ? 377 PHE   A CD1  1 
ATOM   928  C  CD2  . PHE   A 1 113 ? 7.502   9.058   53.434 1.00 34.21 ? 377 PHE   A CD2  1 
ATOM   929  C  CE1  . PHE   A 1 113 ? 9.000   7.735   51.506 1.00 24.17 ? 377 PHE   A CE1  1 
ATOM   930  C  CE2  . PHE   A 1 113 ? 7.085   8.997   52.120 1.00 29.30 ? 377 PHE   A CE2  1 
ATOM   931  C  CZ   . PHE   A 1 113 ? 7.853   8.354   51.162 1.00 25.88 ? 377 PHE   A CZ   1 
ATOM   932  N  N    . PHE   A 1 114 ? 10.697  11.442  54.332 1.00 21.19 ? 378 PHE   A N    1 
ATOM   933  C  CA   . PHE   A 1 114 ? 10.580  12.886  54.152 1.00 19.49 ? 378 PHE   A CA   1 
ATOM   934  C  C    . PHE   A 1 114 ? 10.668  13.156  52.662 1.00 22.16 ? 378 PHE   A C    1 
ATOM   935  O  O    . PHE   A 1 114 ? 11.649  12.806  52.012 1.00 19.77 ? 378 PHE   A O    1 
ATOM   936  C  CB   . PHE   A 1 114 ? 11.702  13.606  54.916 1.00 21.19 ? 378 PHE   A CB   1 
ATOM   937  C  CG   . PHE   A 1 114 ? 11.677  15.116  54.762 1.00 21.64 ? 378 PHE   A CG   1 
ATOM   938  C  CD1  . PHE   A 1 114 ? 10.790  15.883  55.526 1.00 25.87 ? 378 PHE   A CD1  1 
ATOM   939  C  CD2  . PHE   A 1 114 ? 12.470  15.732  53.847 1.00 20.59 ? 378 PHE   A CD2  1 
ATOM   940  C  CE1  . PHE   A 1 114 ? 10.736  17.288  55.389 1.00 23.32 ? 378 PHE   A CE1  1 
ATOM   941  C  CE2  . PHE   A 1 114 ? 12.431  17.157  53.691 1.00 25.69 ? 378 PHE   A CE2  1 
ATOM   942  C  CZ   . PHE   A 1 114 ? 11.542  17.925  54.457 1.00 23.25 ? 378 PHE   A CZ   1 
ATOM   943  N  N    . GLU   A 1 115 ? 9.635   13.792  52.108 1.00 21.04 ? 379 GLU   A N    1 
ATOM   944  C  CA   . GLU   A 1 115 ? 9.695   14.181  50.682 1.00 21.29 ? 379 GLU   A CA   1 
ATOM   945  C  C    . GLU   A 1 115 ? 10.121  13.026  49.783 1.00 23.90 ? 379 GLU   A C    1 
ATOM   946  O  O    . GLU   A 1 115 ? 10.932  13.197  48.861 1.00 23.99 ? 379 GLU   A O    1 
ATOM   947  C  CB   . GLU   A 1 115 ? 10.601  15.395  50.446 1.00 22.72 ? 379 GLU   A CB   1 
ATOM   948  C  CG   . GLU   A 1 115 ? 10.026  16.622  51.195 1.00 22.34 ? 379 GLU   A CG   1 
ATOM   949  C  CD   . GLU   A 1 115 ? 10.669  17.980  50.828 1.00 24.34 ? 379 GLU   A CD   1 
ATOM   950  O  OE1  . GLU   A 1 115 ? 11.738  17.993  50.177 1.00 25.83 ? 379 GLU   A OE1  1 
ATOM   951  O  OE2  . GLU   A 1 115 ? 10.053  19.015  51.193 1.00 25.47 ? 379 GLU   A OE2  1 
ATOM   952  N  N    . GLY   A 1 116 ? 9.528   11.863  50.044 1.00 22.38 ? 380 GLY   A N    1 
ATOM   953  C  CA   . GLY   A 1 116 ? 9.620   10.786  49.085 1.00 21.66 ? 380 GLY   A CA   1 
ATOM   954  C  C    . GLY   A 1 116 ? 10.638  9.706   49.363 1.00 25.61 ? 380 GLY   A C    1 
ATOM   955  O  O    . GLY   A 1 116 ? 10.595  8.656   48.714 1.00 24.40 ? 380 GLY   A O    1 
ATOM   956  N  N    . LYS   A 1 117 ? 11.608  9.997   50.231 1.00 21.98 ? 381 LYS   A N    1 
ATOM   957  C  CA   . LYS   A 1 117 ? 12.624  9.004   50.571 1.00 22.30 ? 381 LYS   A CA   1 
ATOM   958  C  C    . LYS   A 1 117 ? 12.954  9.081   52.058 1.00 24.62 ? 381 LYS   A C    1 
ATOM   959  O  O    . LYS   A 1 117 ? 12.567  10.019  52.736 1.00 22.24 ? 381 LYS   A O    1 
ATOM   960  C  CB   . LYS   A 1 117 ? 13.925  9.195   49.777 1.00 23.81 ? 381 LYS   A CB   1 
ATOM   961  C  CG   . LYS   A 1 117 ? 13.768  9.220   48.275 1.00 27.53 ? 381 LYS   A CG   1 
ATOM   962  C  CD   . LYS   A 1 117 ? 15.157  9.171   47.597 1.00 27.62 ? 381 LYS   A CD   1 
ATOM   963  C  CE   . LYS   A 1 117 ? 15.022  9.294   46.083 1.00 33.05 ? 381 LYS   A CE   1 
ATOM   964  N  NZ   . LYS   A 1 117 ? 16.304  8.917   45.409 1.00 41.06 ? 381 LYS   A NZ   1 
ATOM   965  N  N    . TYR   A 1 118 ? 13.700  8.096   52.550 1.00 23.97 ? 382 TYR   A N    1 
ATOM   966  C  CA   . TYR   A 1 118 ? 14.161  8.111   53.940 1.00 19.47 ? 382 TYR   A CA   1 
ATOM   967  C  C    . TYR   A 1 118 ? 15.479  8.866   54.108 1.00 22.28 ? 382 TYR   A C    1 
ATOM   968  O  O    . TYR   A 1 118 ? 16.419  8.713   53.305 1.00 24.54 ? 382 TYR   A O    1 
ATOM   969  C  CB   . TYR   A 1 118 ? 14.335  6.671   54.450 1.00 19.77 ? 382 TYR   A CB   1 
ATOM   970  C  CG   . TYR   A 1 118 ? 13.036  6.036   54.891 1.00 21.06 ? 382 TYR   A CG   1 
ATOM   971  C  CD1  . TYR   A 1 118 ? 12.147  5.493   53.954 1.00 23.10 ? 382 TYR   A CD1  1 
ATOM   972  C  CD2  . TYR   A 1 118 ? 12.680  6.000   56.237 1.00 20.54 ? 382 TYR   A CD2  1 
ATOM   973  C  CE1  . TYR   A 1 118 ? 10.943  4.935   54.353 1.00 22.83 ? 382 TYR   A CE1  1 
ATOM   974  C  CE2  . TYR   A 1 118 ? 11.484  5.441   56.664 1.00 24.55 ? 382 TYR   A CE2  1 
ATOM   975  C  CZ   . TYR   A 1 118 ? 10.595  4.911   55.703 1.00 23.85 ? 382 TYR   A CZ   1 
ATOM   976  O  OH   . TYR   A 1 118 ? 9.409   4.366   56.099 1.00 27.69 ? 382 TYR   A OH   1 
ATOM   977  N  N    . GLY   A 1 119 ? 15.540  9.724   55.129 1.00 21.95 ? 383 GLY   A N    1 
ATOM   978  C  CA   . GLY   A 1 119 ? 16.805  10.441  55.391 1.00 22.87 ? 383 GLY   A CA   1 
ATOM   979  C  C    . GLY   A 1 119 ? 17.081  10.537  56.882 1.00 23.02 ? 383 GLY   A C    1 
ATOM   980  O  O    . GLY   A 1 119 ? 16.153  10.509  57.694 1.00 24.25 ? 383 GLY   A O    1 
ATOM   981  N  N    . GLY   A 1 120 ? 18.358  10.705  57.244 1.00 25.84 ? 384 GLY   A N    1 
ATOM   982  C  CA   . GLY   A 1 120 ? 18.697  10.847  58.645 1.00 22.49 ? 384 GLY   A CA   1 
ATOM   983  C  C    . GLY   A 1 120 ? 18.686  12.269  59.099 1.00 24.80 ? 384 GLY   A C    1 
ATOM   984  O  O    . GLY   A 1 120 ? 18.366  13.174  58.331 1.00 25.03 ? 384 GLY   A O    1 
ATOM   985  N  N    . MET   A 1 121 ? 19.082  12.490  60.348 1.00 24.28 ? 385 MET   A N    1 
ATOM   986  C  CA   . MET   A 1 121 ? 18.900  13.831  60.875 1.00 22.89 ? 385 MET   A CA   1 
ATOM   987  C  C    . MET   A 1 121 ? 19.761  14.849  60.151 1.00 24.51 ? 385 MET   A C    1 
ATOM   988  O  O    . MET   A 1 121 ? 19.474  16.055  60.203 1.00 21.16 ? 385 MET   A O    1 
ATOM   989  C  CB   . MET   A 1 121 ? 19.204  13.848  62.363 1.00 26.03 ? 385 MET   A CB   1 
ATOM   990  C  CG   . MET   A 1 121 ? 20.572  13.412  62.725 1.00 28.25 ? 385 MET   A CG   1 
ATOM   991  S  SD   . MET   A 1 121 ? 20.658  13.487  64.521 1.00 42.08 ? 385 MET   A SD   1 
ATOM   992  C  CE   . MET   A 1 121 ? 22.330  13.006  64.803 1.00 40.45 ? 385 MET   A CE   1 
ATOM   993  N  N    . GLU   A 1 122 ? 20.866  14.389  59.558 1.00 24.04 ? 386 GLU   A N    1 
ATOM   994  C  CA   . GLU   A 1 122 ? 21.713  15.341  58.854 1.00 24.52 ? 386 GLU   A CA   1 
ATOM   995  C  C    . GLU   A 1 122 ? 21.030  15.957  57.623 1.00 23.95 ? 386 GLU   A C    1 
ATOM   996  O  O    . GLU   A 1 122 ? 21.534  16.964  57.130 1.00 23.40 ? 386 GLU   A O    1 
ATOM   997  C  CB   . GLU   A 1 122 ? 23.035  14.680  58.443 1.00 25.79 ? 386 GLU   A CB   1 
ATOM   998  C  CG   . GLU   A 1 122 ? 22.923  13.676  57.310 1.00 27.50 ? 386 GLU   A CG   1 
ATOM   999  C  CD   . GLU   A 1 122 ? 22.483  12.277  57.783 1.00 36.24 ? 386 GLU   A CD   1 
ATOM   1000 O  OE1  . GLU   A 1 122 ? 22.507  11.345  56.940 1.00 40.40 ? 386 GLU   A OE1  1 
ATOM   1001 O  OE2  . GLU   A 1 122 ? 22.138  12.086  58.981 1.00 38.31 ? 386 GLU   A OE2  1 
ATOM   1002 N  N    . LEU   A 1 123 ? 19.916  15.395  57.140 1.00 24.06 ? 387 LEU   A N    1 
ATOM   1003 C  CA   . LEU   A 1 123 ? 19.217  15.979  56.001 1.00 23.18 ? 387 LEU   A CA   1 
ATOM   1004 C  C    . LEU   A 1 123 ? 18.773  17.418  56.343 1.00 23.27 ? 387 LEU   A C    1 
ATOM   1005 O  O    . LEU   A 1 123 ? 18.649  18.291  55.458 1.00 25.15 ? 387 LEU   A O    1 
ATOM   1006 C  CB   . LEU   A 1 123 ? 17.982  15.125  55.608 1.00 22.57 ? 387 LEU   A CB   1 
ATOM   1007 C  CG   . LEU   A 1 123 ? 17.576  15.351  54.159 1.00 25.85 ? 387 LEU   A CG   1 
ATOM   1008 C  CD1  . LEU   A 1 123 ? 18.323  14.451  53.217 1.00 26.29 ? 387 LEU   A CD1  1 
ATOM   1009 C  CD2  . LEU   A 1 123 ? 16.077  14.970  54.038 1.00 31.41 ? 387 LEU   A CD2  1 
ATOM   1010 N  N    . PHE   A 1 124 ? 18.524  17.665  57.638 1.00 22.38 ? 388 PHE   A N    1 
ATOM   1011 C  CA   . PHE   A 1 124 ? 17.799  18.870  58.093 1.00 24.19 ? 388 PHE   A CA   1 
ATOM   1012 C  C    . PHE   A 1 124 ? 18.678  20.003  58.626 1.00 24.13 ? 388 PHE   A C    1 
ATOM   1013 O  O    . PHE   A 1 124 ? 18.201  20.968  59.275 1.00 21.47 ? 388 PHE   A O    1 
ATOM   1014 C  CB   . PHE   A 1 124 ? 16.762  18.436  59.152 1.00 22.56 ? 388 PHE   A CB   1 
ATOM   1015 C  CG   . PHE   A 1 124 ? 15.844  17.396  58.630 1.00 20.91 ? 388 PHE   A CG   1 
ATOM   1016 C  CD1  . PHE   A 1 124 ? 14.890  17.741  57.682 1.00 19.75 ? 388 PHE   A CD1  1 
ATOM   1017 C  CD2  . PHE   A 1 124 ? 15.999  16.085  59.005 1.00 22.08 ? 388 PHE   A CD2  1 
ATOM   1018 C  CE1  . PHE   A 1 124 ? 14.051  16.764  57.147 1.00 20.05 ? 388 PHE   A CE1  1 
ATOM   1019 C  CE2  . PHE   A 1 124 ? 15.180  15.094  58.493 1.00 22.19 ? 388 PHE   A CE2  1 
ATOM   1020 C  CZ   . PHE   A 1 124 ? 14.181  15.463  57.564 1.00 20.09 ? 388 PHE   A CZ   1 
ATOM   1021 N  N    . ARG   A 1 125 ? 19.981  19.922  58.350 1.00 22.68 ? 389 ARG   A N    1 
ATOM   1022 C  CA   . ARG   A 1 125 ? 20.894  20.884  58.979 1.00 22.54 ? 389 ARG   A CA   1 
ATOM   1023 C  C    . ARG   A 1 125 ? 20.648  22.342  58.618 1.00 22.81 ? 389 ARG   A C    1 
ATOM   1024 O  O    . ARG   A 1 125 ? 20.953  23.223  59.402 1.00 23.85 ? 389 ARG   A O    1 
ATOM   1025 C  CB   . ARG   A 1 125 ? 22.343  20.550  58.656 1.00 21.98 ? 389 ARG   A CB   1 
ATOM   1026 C  CG   . ARG   A 1 125 ? 22.809  19.292  59.369 1.00 23.30 ? 389 ARG   A CG   1 
ATOM   1027 C  CD   . ARG   A 1 125 ? 24.301  19.086  59.228 1.00 23.69 ? 389 ARG   A CD   1 
ATOM   1028 N  NE   . ARG   A 1 125 ? 24.689  17.816  59.819 1.00 27.21 ? 389 ARG   A NE   1 
ATOM   1029 C  CZ   . ARG   A 1 125 ? 25.848  17.236  59.584 1.00 26.47 ? 389 ARG   A CZ   1 
ATOM   1030 N  NH1  . ARG   A 1 125 ? 26.146  16.083  60.176 1.00 25.76 ? 389 ARG   A NH1  1 
ATOM   1031 N  NH2  . ARG   A 1 125 ? 26.742  17.854  58.783 1.00 26.07 ? 389 ARG   A NH2  1 
ATOM   1032 N  N    . ALA   A 1 126 ? 20.118  22.579  57.426 1.00 22.12 ? 390 ALA   A N    1 
ATOM   1033 C  CA   . ALA   A 1 126 ? 19.930  23.941  56.985 1.00 24.29 ? 390 ALA   A CA   1 
ATOM   1034 C  C    . ALA   A 1 126 ? 18.844  24.666  57.796 1.00 24.19 ? 390 ALA   A C    1 
ATOM   1035 O  O    . ALA   A 1 126 ? 18.843  25.894  57.821 1.00 25.41 ? 390 ALA   A O    1 
ATOM   1036 C  CB   . ALA   A 1 126 ? 19.593  23.947  55.502 1.00 29.33 ? 390 ALA   A CB   1 
ATOM   1037 N  N    . LEU   A 1 127 ? 17.987  23.916  58.493 1.00 22.50 ? 391 LEU   A N    1 
ATOM   1038 C  CA   . LEU   A 1 127 ? 17.003  24.553  59.370 1.00 23.36 ? 391 LEU   A CA   1 
ATOM   1039 C  C    . LEU   A 1 127 ? 17.634  25.240  60.547 1.00 27.07 ? 391 LEU   A C    1 
ATOM   1040 O  O    . LEU   A 1 127 ? 17.051  26.131  61.120 1.00 27.48 ? 391 LEU   A O    1 
ATOM   1041 C  CB   . LEU   A 1 127 ? 15.975  23.534  59.862 1.00 21.13 ? 391 LEU   A CB   1 
ATOM   1042 C  CG   . LEU   A 1 127 ? 14.945  23.050  58.845 1.00 22.78 ? 391 LEU   A CG   1 
ATOM   1043 C  CD1  . LEU   A 1 127 ? 14.183  21.889  59.382 1.00 23.91 ? 391 LEU   A CD1  1 
ATOM   1044 C  CD2  . LEU   A 1 127 ? 13.939  24.164  58.542 1.00 21.90 ? 391 LEU   A CD2  1 
ATOM   1045 N  N    . GLY   A 1 128 ? 18.873  24.863  60.899 1.00 23.39 ? 392 GLY   A N    1 
ATOM   1046 C  CA   . GLY   A 1 128 ? 19.511  25.580  61.987 1.00 29.81 ? 392 GLY   A CA   1 
ATOM   1047 C  C    . GLY   A 1 128 ? 18.940  25.353  63.381 1.00 28.21 ? 392 GLY   A C    1 
ATOM   1048 O  O    . GLY   A 1 128 ? 19.029  26.221  64.241 1.00 31.87 ? 392 GLY   A O    1 
ATOM   1049 N  N    . CYS   A 1 129 ? 18.384  24.177  63.621 1.00 27.74 ? 393 CYS   A N    1 
ATOM   1050 C  CA   . CYS   A 1 129 ? 17.902  23.789  64.952 1.00 29.00 ? 393 CYS   A CA   1 
ATOM   1051 C  C    . CYS   A 1 129 ? 18.266  22.329  65.225 1.00 29.55 ? 393 CYS   A C    1 
ATOM   1052 O  O    . CYS   A 1 129 ? 17.426  21.467  65.398 1.00 28.20 ? 393 CYS   A O    1 
ATOM   1053 C  CB   . CYS   A 1 129 ? 16.387  24.011  65.094 1.00 31.40 ? 393 CYS   A CB   1 
ATOM   1054 S  SG   . CYS   A 1 129 ? 15.376  23.445  63.696 1.00 31.84 ? 393 CYS   A SG   1 
ATOM   1055 N  N    . SER   A 1 130 ? 19.559  22.080  65.239 1.00 36.70 ? 394 SER   A N    1 
ATOM   1056 C  CA   . SER   A 1 130 ? 20.094  20.738  65.450 1.00 38.49 ? 394 SER   A CA   1 
ATOM   1057 C  C    . SER   A 1 130 ? 19.564  19.981  66.672 1.00 24.87 ? 394 SER   A C    1 
ATOM   1058 O  O    . SER   A 1 130 ? 19.206  18.776  66.541 1.00 26.88 ? 394 SER   A O    1 
ATOM   1059 C  CB   . SER   A 1 130 ? 21.632  20.844  65.550 1.00 51.99 ? 394 SER   A CB   1 
ATOM   1060 O  OG   . SER   A 1 130 ? 22.228  19.570  65.697 1.00 65.62 ? 394 SER   A OG   1 
ATOM   1061 N  N    . GLU   A 1 131 ? 19.524  20.629  67.838 1.00 28.56 ? 395 GLU   A N    1 
ATOM   1062 C  CA   . GLU   A 1 131 ? 18.965  20.045  69.064 1.00 33.81 ? 395 GLU   A CA   1 
ATOM   1063 C  C    . GLU   A 1 131 ? 17.542  19.535  68.905 1.00 33.28 ? 395 GLU   A C    1 
ATOM   1064 O  O    . GLU   A 1 131 ? 17.181  18.423  69.302 1.00 30.68 ? 395 GLU   A O    1 
ATOM   1065 C  CB   . GLU   A 1 131 ? 18.948  21.070  70.202 1.00 42.53 ? 395 GLU   A CB   1 
ATOM   1066 C  CG   . GLU   A 1 131 ? 20.184  21.090  71.115 1.00 59.89 ? 395 GLU   A CG   1 
ATOM   1067 C  CD   . GLU   A 1 131 ? 19.997  22.016  72.321 1.00 72.05 ? 395 GLU   A CD   1 
ATOM   1068 O  OE1  . GLU   A 1 131 ? 20.145  23.249  72.150 1.00 77.44 ? 395 GLU   A OE1  1 
ATOM   1069 O  OE2  . GLU   A 1 131 ? 19.704  21.514  73.432 1.00 72.95 ? 395 GLU   A OE2  1 
ATOM   1070 N  N    . LEU   A 1 132 ? 16.691  20.397  68.372 1.00 29.64 ? 396 LEU   A N    1 
ATOM   1071 C  CA   . LEU   A 1 132 ? 15.325  20.009  68.115 1.00 25.48 ? 396 LEU   A CA   1 
ATOM   1072 C  C    . LEU   A 1 132 ? 15.189  18.802  67.155 1.00 25.50 ? 396 LEU   A C    1 
ATOM   1073 O  O    . LEU   A 1 132 ? 14.442  17.854  67.422 1.00 25.67 ? 396 LEU   A O    1 
ATOM   1074 C  CB   . LEU   A 1 132 ? 14.537  21.205  67.540 1.00 28.84 ? 396 LEU   A CB   1 
ATOM   1075 C  CG   . LEU   A 1 132 ? 13.093  20.902  67.181 1.00 32.00 ? 396 LEU   A CG   1 
ATOM   1076 C  CD1  . LEU   A 1 132 ? 12.346  20.235  68.316 1.00 31.43 ? 396 LEU   A CD1  1 
ATOM   1077 C  CD2  . LEU   A 1 132 ? 12.417  22.233  66.784 1.00 27.74 ? 396 LEU   A CD2  1 
ATOM   1078 N  N    . ILE   A 1 133 ? 15.906  18.846  66.028 1.00 22.14 ? 397 ILE   A N    1 
ATOM   1079 C  CA   . ILE   A 1 133 ? 15.833  17.751  65.087 1.00 21.71 ? 397 ILE   A CA   1 
ATOM   1080 C  C    . ILE   A 1 133 ? 16.266  16.433  65.754 1.00 23.99 ? 397 ILE   A C    1 
ATOM   1081 O  O    . ILE   A 1 133 ? 15.571  15.418  65.628 1.00 23.91 ? 397 ILE   A O    1 
ATOM   1082 C  CB   . ILE   A 1 133 ? 16.695  17.997  63.856 1.00 26.30 ? 397 ILE   A CB   1 
ATOM   1083 C  CG1  . ILE   A 1 133 ? 16.233  19.251  63.104 1.00 25.81 ? 397 ILE   A CG1  1 
ATOM   1084 C  CG2  . ILE   A 1 133 ? 16.666  16.763  62.983 1.00 26.20 ? 397 ILE   A CG2  1 
ATOM   1085 C  CD1  . ILE   A 1 133 ? 14.785  19.203  62.716 1.00 25.65 ? 397 ILE   A CD1  1 
ATOM   1086 N  N    . SER   A 1 134 ? 17.408  16.439  66.445 1.00 24.87 ? 398 SER   A N    1 
ATOM   1087 C  CA   . SER   A 1 134 ? 17.810  15.194  67.089 1.00 24.67 ? 398 SER   A CA   1 
ATOM   1088 C  C    . SER   A 1 134 ? 16.776  14.828  68.231 1.00 29.04 ? 398 SER   A C    1 
ATOM   1089 O  O    . SER   A 1 134 ? 16.554  13.634  68.467 1.00 26.94 ? 398 SER   A O    1 
ATOM   1090 C  CB   . SER   A 1 134 ? 19.299  15.279  67.564 1.00 32.39 ? 398 SER   A CB   1 
ATOM   1091 O  OG   . SER   A 1 134 ? 19.340  15.538  68.936 1.00 46.01 ? 398 SER   A OG   1 
ATOM   1092 N  N    . SER   A 1 135 ? 16.082  15.798  68.870 1.00 25.86 ? 399 SER   A N    1 
ATOM   1093 C  CA   . SER   A 1 135 ? 15.068  15.450  69.895 1.00 24.26 ? 399 SER   A CA   1 
ATOM   1094 C  C    . SER   A 1 135 ? 13.876  14.731  69.237 1.00 25.37 ? 399 SER   A C    1 
ATOM   1095 O  O    . SER   A 1 135 ? 13.297  13.817  69.822 1.00 29.16 ? 399 SER   A O    1 
ATOM   1096 C  CB   . SER   A 1 135 ? 14.535  16.665  70.639 1.00 28.71 ? 399 SER   A CB   1 
ATOM   1097 O  OG   . SER   A 1 135 ? 15.493  17.230  71.525 1.00 39.28 ? 399 SER   A OG   1 
ATOM   1098 N  N    . ILE   A 1 136 ? 13.536  15.135  68.014 1.00 22.48 ? 400 ILE   A N    1 
ATOM   1099 C  CA   . ILE   A 1 136 ? 12.446  14.498  67.271 1.00 24.70 ? 400 ILE   A CA   1 
ATOM   1100 C  C    . ILE   A 1 136 ? 12.820  13.037  66.948 1.00 24.45 ? 400 ILE   A C    1 
ATOM   1101 O  O    . ILE   A 1 136 ? 12.021  12.095  67.091 1.00 23.93 ? 400 ILE   A O    1 
ATOM   1102 C  CB   . ILE   A 1 136 ? 12.163  15.290  65.995 1.00 22.28 ? 400 ILE   A CB   1 
ATOM   1103 C  CG1  . ILE   A 1 136 ? 11.566  16.658  66.328 1.00 23.44 ? 400 ILE   A CG1  1 
ATOM   1104 C  CG2  . ILE   A 1 136 ? 11.276  14.523  65.070 1.00 22.65 ? 400 ILE   A CG2  1 
ATOM   1105 C  CD1  . ILE   A 1 136 ? 11.513  17.570  65.072 1.00 26.04 ? 400 ILE   A CD1  1 
ATOM   1106 N  N    . PHE   A 1 137 ? 14.037  12.877  66.429 1.00 21.54 ? 401 PHE   A N    1 
ATOM   1107 C  CA   . PHE   A 1 137 ? 14.531  11.559  66.066 1.00 24.24 ? 401 PHE   A CA   1 
ATOM   1108 C  C    . PHE   A 1 137 ? 14.565  10.708  67.308 1.00 23.28 ? 401 PHE   A C    1 
ATOM   1109 O  O    . PHE   A 1 137 ? 14.242  9.522   67.249 1.00 25.20 ? 401 PHE   A O    1 
ATOM   1110 C  CB   . PHE   A 1 137 ? 15.925  11.637  65.408 1.00 22.45 ? 401 PHE   A CB   1 
ATOM   1111 C  CG   . PHE   A 1 137 ? 15.869  11.825  63.907 1.00 20.63 ? 401 PHE   A CG   1 
ATOM   1112 C  CD1  . PHE   A 1 137 ? 15.363  13.014  63.356 1.00 22.85 ? 401 PHE   A CD1  1 
ATOM   1113 C  CD2  . PHE   A 1 137 ? 16.235  10.785  63.044 1.00 22.39 ? 401 PHE   A CD2  1 
ATOM   1114 C  CE1  . PHE   A 1 137 ? 15.248  13.173  61.965 1.00 23.55 ? 401 PHE   A CE1  1 
ATOM   1115 C  CE2  . PHE   A 1 137 ? 16.153  10.941  61.655 1.00 22.35 ? 401 PHE   A CE2  1 
ATOM   1116 C  CZ   . PHE   A 1 137 ? 15.653  12.141  61.124 1.00 24.56 ? 401 PHE   A CZ   1 
ATOM   1117 N  N    . ASP   A 1 138 ? 15.009  11.271  68.442 1.00 22.78 ? 402 ASP   A N    1 
ATOM   1118 C  CA   . ASP   A 1 138 ? 15.155  10.440  69.652 1.00 28.58 ? 402 ASP   A CA   1 
ATOM   1119 C  C    . ASP   A 1 138 ? 13.794  9.994   70.177 1.00 29.61 ? 402 ASP   A C    1 
ATOM   1120 O  O    . ASP   A 1 138 ? 13.640  8.880   70.672 1.00 30.49 ? 402 ASP   A O    1 
ATOM   1121 C  CB   . ASP   A 1 138 ? 15.928  11.204  70.728 1.00 35.21 ? 402 ASP   A CB   1 
ATOM   1122 C  CG   . ASP   A 1 138 ? 17.405  11.362  70.366 1.00 60.07 ? 402 ASP   A CG   1 
ATOM   1123 O  OD1  . ASP   A 1 138 ? 17.905  10.554  69.543 1.00 64.87 ? 402 ASP   A OD1  1 
ATOM   1124 O  OD2  . ASP   A 1 138 ? 18.063  12.285  70.896 1.00 66.89 ? 402 ASP   A OD2  1 
ATOM   1125 N  N    . PHE   A 1 139 ? 12.824  10.875  70.053 1.00 28.73 ? 403 PHE   A N    1 
ATOM   1126 C  CA   . PHE   A 1 139 ? 11.469  10.575  70.483 1.00 25.66 ? 403 PHE   A CA   1 
ATOM   1127 C  C    . PHE   A 1 139 ? 10.927  9.471   69.605 1.00 27.36 ? 403 PHE   A C    1 
ATOM   1128 O  O    . PHE   A 1 139 ? 10.286  8.523   70.098 1.00 30.93 ? 403 PHE   A O    1 
ATOM   1129 C  CB   . PHE   A 1 139 ? 10.563  11.801  70.431 1.00 26.18 ? 403 PHE   A CB   1 
ATOM   1130 C  CG   . PHE   A 1 139 ? 9.176   11.519  70.935 1.00 24.11 ? 403 PHE   A CG   1 
ATOM   1131 C  CD1  . PHE   A 1 139 ? 8.965   11.272  72.284 1.00 30.13 ? 403 PHE   A CD1  1 
ATOM   1132 C  CD2  . PHE   A 1 139 ? 8.102   11.465  70.069 1.00 29.31 ? 403 PHE   A CD2  1 
ATOM   1133 C  CE1  . PHE   A 1 139 ? 7.702   11.009  72.757 1.00 31.90 ? 403 PHE   A CE1  1 
ATOM   1134 C  CE2  . PHE   A 1 139 ? 6.818   11.203  70.544 1.00 26.34 ? 403 PHE   A CE2  1 
ATOM   1135 C  CZ   . PHE   A 1 139 ? 6.627   10.956  71.891 1.00 28.78 ? 403 PHE   A CZ   1 
ATOM   1136 N  N    . SER   A 1 140 ? 11.142  9.582   68.294 1.00 24.22 ? 404 SER   A N    1 
ATOM   1137 C  CA   . SER   A 1 140 ? 10.638  8.558   67.369 1.00 20.94 ? 404 SER   A CA   1 
ATOM   1138 C  C    . SER   A 1 140 ? 11.316  7.241   67.680 1.00 23.14 ? 404 SER   A C    1 
ATOM   1139 O  O    . SER   A 1 140 ? 10.695  6.181   67.592 1.00 25.83 ? 404 SER   A O    1 
ATOM   1140 C  CB   . SER   A 1 140 ? 10.896  8.948   65.934 1.00 24.88 ? 404 SER   A CB   1 
ATOM   1141 O  OG   . SER   A 1 140 ? 9.986   9.973   65.599 1.00 34.51 ? 404 SER   A OG   1 
ATOM   1142 N  N    . HIS   A 1 141 ? 12.619  7.295   67.994 1.00 26.29 ? 405 HIS   A N    1 
ATOM   1143 C  CA   . HIS   A 1 141 ? 13.341  6.054   68.250 1.00 22.68 ? 405 HIS   A CA   1 
ATOM   1144 C  C    . HIS   A 1 141 ? 12.735  5.408   69.483 1.00 26.02 ? 405 HIS   A C    1 
ATOM   1145 O  O    . HIS   A 1 141 ? 12.568  4.183   69.527 1.00 28.48 ? 405 HIS   A O    1 
ATOM   1146 C  CB   . HIS   A 1 141 ? 14.838  6.314   68.441 1.00 24.51 ? 405 HIS   A CB   1 
ATOM   1147 C  CG   . HIS   A 1 141 ? 15.695  5.096   68.256 1.00 28.87 ? 405 HIS   A CG   1 
ATOM   1148 N  ND1  . HIS   A 1 141 ? 16.195  4.724   67.021 1.00 28.76 ? 405 HIS   A ND1  1 
ATOM   1149 C  CD2  . HIS   A 1 141 ? 16.124  4.179   69.136 1.00 35.44 ? 405 HIS   A CD2  1 
ATOM   1150 C  CE1  . HIS   A 1 141 ? 16.901  3.624   67.163 1.00 33.54 ? 405 HIS   A CE1  1 
ATOM   1151 N  NE2  . HIS   A 1 141 ? 16.884  3.265   68.431 1.00 37.23 ? 405 HIS   A NE2  1 
ATOM   1152 N  N    . SER   A 1 142 ? 12.388  6.215   70.483 1.00 25.50 ? 406 SER   A N    1 
ATOM   1153 C  CA   . SER   A 1 142 ? 11.883  5.636   71.729 1.00 26.06 ? 406 SER   A CA   1 
ATOM   1154 C  C    . SER   A 1 142 ? 10.514  4.978   71.478 1.00 28.52 ? 406 SER   A C    1 
ATOM   1155 O  O    . SER   A 1 142 ? 10.235  3.900   72.042 1.00 31.45 ? 406 SER   A O    1 
ATOM   1156 C  CB   . SER   A 1 142 ? 11.790  6.688   72.839 1.00 32.13 ? 406 SER   A CB   1 
ATOM   1157 O  OG   . SER   A 1 142 ? 10.712  7.575   72.667 1.00 43.60 ? 406 SER   A OG   1 
ATOM   1158 N  N    . LEU   A 1 143 ? 9.691   5.583   70.630 1.00 27.70 ? 407 LEU   A N    1 
ATOM   1159 C  CA   . LEU   A 1 143 ? 8.392   4.946   70.286 1.00 24.08 ? 407 LEU   A CA   1 
ATOM   1160 C  C    . LEU   A 1 143 ? 8.553   3.723   69.414 1.00 30.44 ? 407 LEU   A C    1 
ATOM   1161 O  O    . LEU   A 1 143 ? 7.720   2.796   69.472 1.00 30.59 ? 407 LEU   A O    1 
ATOM   1162 C  CB   . LEU   A 1 143 ? 7.476   5.916   69.562 1.00 24.58 ? 407 LEU   A CB   1 
ATOM   1163 C  CG   . LEU   A 1 143 ? 6.965   7.059   70.420 1.00 27.95 ? 407 LEU   A CG   1 
ATOM   1164 C  CD1  . LEU   A 1 143 ? 5.988   7.850   69.591 1.00 28.13 ? 407 LEU   A CD1  1 
ATOM   1165 C  CD2  . LEU   A 1 143 ? 6.306   6.535   71.668 1.00 31.62 ? 407 LEU   A CD2  1 
ATOM   1166 N  N    . SER   A 1 144 ? 9.571   3.740   68.570 1.00 31.87 ? 408 SER   A N    1 
ATOM   1167 C  CA   . SER   A 1 144 ? 9.853   2.636   67.665 1.00 36.25 ? 408 SER   A CA   1 
ATOM   1168 C  C    . SER   A 1 144 ? 9.975   1.307   68.414 1.00 33.67 ? 408 SER   A C    1 
ATOM   1169 O  O    . SER   A 1 144 ? 9.576   0.262   67.872 1.00 32.39 ? 408 SER   A O    1 
ATOM   1170 C  CB   . SER   A 1 144 ? 11.135  2.902   66.871 1.00 36.02 ? 408 SER   A CB   1 
ATOM   1171 O  OG   . SER   A 1 144 ? 12.266  2.682   67.694 1.00 37.93 ? 408 SER   A OG   1 
ATOM   1172 N  N    . ALA   A 1 145 ? 10.500  1.355   69.651 1.00 30.50 ? 409 ALA   A N    1 
ATOM   1173 C  CA   . ALA   A 1 145 ? 10.689  0.183   70.509 1.00 34.85 ? 409 ALA   A CA   1 
ATOM   1174 C  C    . ALA   A 1 145 ? 9.403   -0.568  70.822 1.00 34.96 ? 409 ALA   A C    1 
ATOM   1175 O  O    . ALA   A 1 145 ? 9.443   -1.742  71.192 1.00 36.18 ? 409 ALA   A O    1 
ATOM   1176 C  CB   . ALA   A 1 145 ? 11.340  0.594   71.812 1.00 37.97 ? 409 ALA   A CB   1 
ATOM   1177 N  N    . LEU   A 1 146 ? 8.267   0.103   70.714 1.00 30.66 ? 410 LEU   A N    1 
ATOM   1178 C  CA   . LEU   A 1 146 ? 6.984   -0.513  71.113 1.00 29.67 ? 410 LEU   A CA   1 
ATOM   1179 C  C    . LEU   A 1 146 ? 6.349   -1.327  69.994 1.00 33.97 ? 410 LEU   A C    1 
ATOM   1180 O  O    . LEU   A 1 146 ? 5.458   -2.154  70.252 1.00 32.64 ? 410 LEU   A O    1 
ATOM   1181 C  CB   . LEU   A 1 146 ? 5.979   0.538   71.570 1.00 35.12 ? 410 LEU   A CB   1 
ATOM   1182 C  CG   . LEU   A 1 146 ? 6.178   1.073   72.978 1.00 43.53 ? 410 LEU   A CG   1 
ATOM   1183 C  CD1  . LEU   A 1 146 ? 7.614   1.464   73.151 1.00 48.75 ? 410 LEU   A CD1  1 
ATOM   1184 C  CD2  . LEU   A 1 146 ? 5.288   2.261   73.162 1.00 48.17 ? 410 LEU   A CD2  1 
ATOM   1185 N  N    . HIS   A 1 147 ? 6.799   -1.078  68.766 1.00 31.08 ? 411 HIS   A N    1 
ATOM   1186 C  CA   . HIS   A 1 147 ? 6.234   -1.705  67.581 1.00 27.07 ? 411 HIS   A CA   1 
ATOM   1187 C  C    . HIS   A 1 147 ? 4.717   -1.583  67.599 1.00 27.78 ? 411 HIS   A C    1 
ATOM   1188 O  O    . HIS   A 1 147 ? 4.019   -2.585  67.449 1.00 29.56 ? 411 HIS   A O    1 
ATOM   1189 C  CB   . HIS   A 1 147 ? 6.658   -3.162  67.498 1.00 29.34 ? 411 HIS   A CB   1 
ATOM   1190 C  CG   . HIS   A 1 147 ? 8.125   -3.318  67.300 1.00 38.07 ? 411 HIS   A CG   1 
ATOM   1191 N  ND1  . HIS   A 1 147 ? 9.011   -3.401  68.351 1.00 46.61 ? 411 HIS   A ND1  1 
ATOM   1192 C  CD2  . HIS   A 1 147 ? 8.874   -3.300  66.175 1.00 44.21 ? 411 HIS   A CD2  1 
ATOM   1193 C  CE1  . HIS   A 1 147 ? 10.241  -3.482  67.877 1.00 45.82 ? 411 HIS   A CE1  1 
ATOM   1194 N  NE2  . HIS   A 1 147 ? 10.185  -3.423  66.560 1.00 45.11 ? 411 HIS   A NE2  1 
ATOM   1195 N  N    . PHE   A 1 148 ? 4.232   -0.368  67.840 1.00 25.87 ? 412 PHE   A N    1 
ATOM   1196 C  CA   . PHE   A 1 148 ? 2.782   -0.107  67.848 1.00 24.25 ? 412 PHE   A CA   1 
ATOM   1197 C  C    . PHE   A 1 148 ? 2.066   -0.752  66.682 1.00 29.09 ? 412 PHE   A C    1 
ATOM   1198 O  O    . PHE   A 1 148 ? 2.493   -0.619  65.531 1.00 29.34 ? 412 PHE   A O    1 
ATOM   1199 C  CB   . PHE   A 1 148 ? 2.491   1.383   67.722 1.00 27.93 ? 412 PHE   A CB   1 
ATOM   1200 C  CG   . PHE   A 1 148 ? 2.529   2.169   68.990 1.00 33.57 ? 412 PHE   A CG   1 
ATOM   1201 C  CD1  . PHE   A 1 148 ? 1.903   1.744   70.139 1.00 38.55 ? 412 PHE   A CD1  1 
ATOM   1202 C  CD2  . PHE   A 1 148 ? 3.157   3.407   68.990 1.00 38.80 ? 412 PHE   A CD2  1 
ATOM   1203 C  CE1  . PHE   A 1 148 ? 1.923   2.530   71.292 1.00 40.74 ? 412 PHE   A CE1  1 
ATOM   1204 C  CE2  . PHE   A 1 148 ? 3.177   4.185   70.122 1.00 42.73 ? 412 PHE   A CE2  1 
ATOM   1205 C  CZ   . PHE   A 1 148 ? 2.554   3.744   71.279 1.00 42.02 ? 412 PHE   A CZ   1 
ATOM   1206 N  N    . SER   A 1 149 ? 0.932   -1.376  66.951 1.00 25.82 ? 413 SER   A N    1 
ATOM   1207 C  CA   . SER   A 1 149 ? -0.005  -1.652  65.863 1.00 24.36 ? 413 SER   A CA   1 
ATOM   1208 C  C    . SER   A 1 149 ? -0.717  -0.392  65.454 1.00 26.68 ? 413 SER   A C    1 
ATOM   1209 O  O    . SER   A 1 149 ? -0.742  0.586   66.192 1.00 27.48 ? 413 SER   A O    1 
ATOM   1210 C  CB   . SER   A 1 149 ? -1.039  -2.708  66.266 1.00 25.80 ? 413 SER   A CB   1 
ATOM   1211 O  OG   . SER   A 1 149 ? -1.907  -2.239  67.290 1.00 26.86 ? 413 SER   A OG   1 
ATOM   1212 N  N    . GLU   A 1 150 ? -1.378  -0.442  64.293 1.00 25.08 ? 414 GLU   A N    1 
ATOM   1213 C  CA   . GLU   A 1 150 ? -2.169  0.696   63.856 1.00 24.84 ? 414 GLU   A CA   1 
ATOM   1214 C  C    . GLU   A 1 150 ? -3.277  0.945   64.874 1.00 24.62 ? 414 GLU   A C    1 
ATOM   1215 O  O    . GLU   A 1 150 ? -3.569  2.088   65.154 1.00 27.83 ? 414 GLU   A O    1 
ATOM   1216 C  CB   . GLU   A 1 150 ? -2.750  0.465   62.470 1.00 28.33 ? 414 GLU   A CB   1 
ATOM   1217 C  CG   . GLU   A 1 150 ? -1.752  0.478   61.322 1.00 26.52 ? 414 GLU   A CG   1 
ATOM   1218 C  CD   . GLU   A 1 150 ? -1.112  1.847   61.132 1.00 26.56 ? 414 GLU   A CD   1 
ATOM   1219 O  OE1  . GLU   A 1 150 ? -1.697  2.654   60.364 1.00 32.79 ? 414 GLU   A OE1  1 
ATOM   1220 O  OE2  . GLU   A 1 150 ? -0.025  2.097   61.708 1.00 29.05 ? 414 GLU   A OE2  1 
ATOM   1221 N  N    . ASP   A 1 151 ? -3.887  -0.114  65.421 1.00 26.04 ? 415 ASP   A N    1 
ATOM   1222 C  CA   . ASP   A 1 151 ? -4.972  0.088   66.398 1.00 22.88 ? 415 ASP   A CA   1 
ATOM   1223 C  C    . ASP   A 1 151 ? -4.471  0.718   67.698 1.00 23.78 ? 415 ASP   A C    1 
ATOM   1224 O  O    . ASP   A 1 151 ? -5.094  1.616   68.267 1.00 24.79 ? 415 ASP   A O    1 
ATOM   1225 C  CB   . ASP   A 1 151 ? -5.672  -1.239  66.719 1.00 27.25 ? 415 ASP   A CB   1 
ATOM   1226 C  CG   . ASP   A 1 151 ? -6.550  -1.753  65.578 1.00 32.13 ? 415 ASP   A CG   1 
ATOM   1227 O  OD1  . ASP   A 1 151 ? -6.796  -1.033  64.601 1.00 34.63 ? 415 ASP   A OD1  1 
ATOM   1228 O  OD2  . ASP   A 1 151 ? -6.981  -2.912  65.660 1.00 36.30 ? 415 ASP   A OD2  1 
ATOM   1229 N  N    . GLU   A 1 152 ? -3.291  0.307   68.143 1.00 24.69 ? 416 GLU   A N    1 
ATOM   1230 C  CA   . GLU   A 1 152 ? -2.688  0.938   69.311 1.00 25.51 ? 416 GLU   A CA   1 
ATOM   1231 C  C    . GLU   A 1 152 ? -2.360  2.407   69.097 1.00 22.88 ? 416 GLU   A C    1 
ATOM   1232 O  O    . GLU   A 1 152 ? -2.564  3.197   70.000 1.00 23.82 ? 416 GLU   A O    1 
ATOM   1233 C  CB   . GLU   A 1 152 ? -1.427  0.173   69.720 1.00 25.20 ? 416 GLU   A CB   1 
ATOM   1234 C  CG   . GLU   A 1 152 ? -1.755  -1.212  70.319 1.00 26.14 ? 416 GLU   A CG   1 
ATOM   1235 C  CD   . GLU   A 1 152 ? -0.591  -2.195  70.245 1.00 31.27 ? 416 GLU   A CD   1 
ATOM   1236 O  OE1  . GLU   A 1 152 ? 0.487   -1.856  69.717 1.00 28.46 ? 416 GLU   A OE1  1 
ATOM   1237 O  OE2  . GLU   A 1 152 ? -0.762  -3.328  70.720 1.00 30.05 ? 416 GLU   A OE2  1 
ATOM   1238 N  N    . ILE   A 1 153 ? -1.784  2.777   67.942 1.00 21.76 ? 417 ILE   A N    1 
ATOM   1239 C  CA   . ILE   A 1 153 ? -1.551  4.179   67.621 1.00 24.02 ? 417 ILE   A CA   1 
ATOM   1240 C  C    . ILE   A 1 153 ? -2.861  4.983   67.666 1.00 26.28 ? 417 ILE   A C    1 
ATOM   1241 O  O    . ILE   A 1 153 ? -2.894  6.081   68.228 1.00 25.40 ? 417 ILE   A O    1 
ATOM   1242 C  CB   . ILE   A 1 153 ? -0.876  4.288   66.243 1.00 26.69 ? 417 ILE   A CB   1 
ATOM   1243 C  CG1  . ILE   A 1 153 ? 0.558   3.822   66.407 1.00 33.12 ? 417 ILE   A CG1  1 
ATOM   1244 C  CG2  . ILE   A 1 153 ? -1.005  5.705   65.695 1.00 33.24 ? 417 ILE   A CG2  1 
ATOM   1245 C  CD1  . ILE   A 1 153 ? 1.448   4.078   65.223 1.00 39.66 ? 417 ILE   A CD1  1 
ATOM   1246 N  N    . ALA   A 1 154 ? -3.937  4.415   67.119 1.00 22.65 ? 418 ALA   A N    1 
ATOM   1247 C  CA   . ALA   A 1 154 ? -5.230  5.076   67.125 1.00 19.18 ? 418 ALA   A CA   1 
ATOM   1248 C  C    . ALA   A 1 154 ? -5.658  5.397   68.548 1.00 22.93 ? 418 ALA   A C    1 
ATOM   1249 O  O    . ALA   A 1 154 ? -6.068  6.527   68.875 1.00 23.47 ? 418 ALA   A O    1 
ATOM   1250 C  CB   . ALA   A 1 154 ? -6.302  4.201   66.452 1.00 23.41 ? 418 ALA   A CB   1 
ATOM   1251 N  N    . LEU   A 1 155 ? -5.624  4.380   69.402 1.00 21.04 ? 419 LEU   A N    1 
ATOM   1252 C  CA   . LEU   A 1 155 ? -6.122  4.549   70.767 1.00 19.92 ? 419 LEU   A CA   1 
ATOM   1253 C  C    . LEU   A 1 155 ? -5.190  5.450   71.583 1.00 25.16 ? 419 LEU   A C    1 
ATOM   1254 O  O    . LEU   A 1 155 ? -5.656  6.276   72.363 1.00 24.94 ? 419 LEU   A O    1 
ATOM   1255 C  CB   . LEU   A 1 155 ? -6.268  3.201   71.448 1.00 22.79 ? 419 LEU   A CB   1 
ATOM   1256 C  CG   . LEU   A 1 155 ? -7.287  2.298   70.800 1.00 25.73 ? 419 LEU   A CG   1 
ATOM   1257 C  CD1  . LEU   A 1 155 ? -7.024  0.825   71.100 1.00 27.09 ? 419 LEU   A CD1  1 
ATOM   1258 C  CD2  . LEU   A 1 155 ? -8.677  2.729   71.248 1.00 25.77 ? 419 LEU   A CD2  1 
ATOM   1259 N  N    . TYR   A 1 156 ? -3.884  5.276   71.415 1.00 23.34 ? 420 TYR   A N    1 
ATOM   1260 C  CA   . TYR   A 1 156 ? -2.946  6.090   72.156 1.00 22.78 ? 420 TYR   A CA   1 
ATOM   1261 C  C    . TYR   A 1 156 ? -3.038  7.549   71.741 1.00 22.84 ? 420 TYR   A C    1 
ATOM   1262 O  O    . TYR   A 1 156 ? -3.048  8.419   72.617 1.00 22.99 ? 420 TYR   A O    1 
ATOM   1263 C  CB   . TYR   A 1 156 ? -1.528  5.582   71.965 1.00 21.39 ? 420 TYR   A CB   1 
ATOM   1264 C  CG   . TYR   A 1 156 ? -0.505  6.325   72.775 1.00 25.99 ? 420 TYR   A CG   1 
ATOM   1265 C  CD1  . TYR   A 1 156 ? -0.447  6.164   74.149 1.00 29.61 ? 420 TYR   A CD1  1 
ATOM   1266 C  CD2  . TYR   A 1 156 ? 0.395   7.159   72.165 1.00 30.75 ? 420 TYR   A CD2  1 
ATOM   1267 C  CE1  . TYR   A 1 156 ? 0.519   6.838   74.909 1.00 33.10 ? 420 TYR   A CE1  1 
ATOM   1268 C  CE2  . TYR   A 1 156 ? 1.356   7.849   72.919 1.00 30.30 ? 420 TYR   A CE2  1 
ATOM   1269 C  CZ   . TYR   A 1 156 ? 1.393   7.675   74.279 1.00 33.67 ? 420 TYR   A CZ   1 
ATOM   1270 O  OH   . TYR   A 1 156 ? 2.344   8.339   75.025 1.00 32.66 ? 420 TYR   A OH   1 
ATOM   1271 N  N    . THR   A 1 157 ? -3.132  7.826   70.438 1.00 21.05 ? 421 THR   A N    1 
ATOM   1272 C  CA   . THR   A 1 157 ? -3.221  9.254   70.037 1.00 20.29 ? 421 THR   A CA   1 
ATOM   1273 C  C    . THR   A 1 157 ? -4.558  9.863   70.417 1.00 24.04 ? 421 THR   A C    1 
ATOM   1274 O  O    . THR   A 1 157 ? -4.622  11.054  70.653 1.00 22.69 ? 421 THR   A O    1 
ATOM   1275 C  CB   . THR   A 1 157 ? -2.985  9.464   68.533 1.00 21.19 ? 421 THR   A CB   1 
ATOM   1276 O  OG1  . THR   A 1 157 ? -3.855  8.614   67.802 1.00 23.51 ? 421 THR   A OG1  1 
ATOM   1277 C  CG2  . THR   A 1 157 ? -1.535  9.090   68.201 1.00 22.82 ? 421 THR   A CG2  1 
ATOM   1278 N  N    . ALA   A 1 158 ? -5.614  9.051   70.488 1.00 21.77 ? 422 ALA   A N    1 
ATOM   1279 C  CA   . ALA   A 1 158 ? -6.881  9.580   70.996 1.00 20.82 ? 422 ALA   A CA   1 
ATOM   1280 C  C    . ALA   A 1 158 ? -6.721  10.075  72.438 1.00 23.99 ? 422 ALA   A C    1 
ATOM   1281 O  O    . ALA   A 1 158 ? -7.219  11.152  72.795 1.00 23.39 ? 422 ALA   A O    1 
ATOM   1282 C  CB   . ALA   A 1 158 ? -7.988  8.535   70.898 1.00 26.24 ? 422 ALA   A CB   1 
ATOM   1283 N  N    . LEU   A 1 159 ? -5.983  9.324   73.248 1.00 23.77 ? 423 LEU   A N    1 
ATOM   1284 C  CA   . LEU   A 1 159 ? -5.743  9.698   74.639 1.00 23.22 ? 423 LEU   A CA   1 
ATOM   1285 C  C    . LEU   A 1 159 ? -4.789  10.884  74.765 1.00 24.72 ? 423 LEU   A C    1 
ATOM   1286 O  O    . LEU   A 1 159 ? -4.819  11.613  75.775 1.00 27.05 ? 423 LEU   A O    1 
ATOM   1287 C  CB   . LEU   A 1 159 ? -5.177  8.513   75.417 1.00 24.61 ? 423 LEU   A CB   1 
ATOM   1288 C  CG   . LEU   A 1 159 ? -6.280  7.500   75.724 1.00 24.55 ? 423 LEU   A CG   1 
ATOM   1289 C  CD1  . LEU   A 1 159 ? -5.679  6.132   76.087 1.00 28.27 ? 423 LEU   A CD1  1 
ATOM   1290 C  CD2  . LEU   A 1 159 ? -7.178  8.009   76.860 1.00 29.07 ? 423 LEU   A CD2  1 
ATOM   1291 N  N    . VAL   A 1 160 ? -3.901  11.058  73.789 1.00 22.26 ? 424 VAL   A N    1 
ATOM   1292 C  CA   . VAL   A 1 160 ? -3.029  12.238  73.828 1.00 22.61 ? 424 VAL   A CA   1 
ATOM   1293 C  C    . VAL   A 1 160 ? -3.933  13.474  73.736 1.00 23.02 ? 424 VAL   A C    1 
ATOM   1294 O  O    . VAL   A 1 160 ? -3.699  14.485  74.418 1.00 21.70 ? 424 VAL   A O    1 
ATOM   1295 C  CB   . VAL   A 1 160 ? -1.978  12.230  72.689 1.00 23.90 ? 424 VAL   A CB   1 
ATOM   1296 C  CG1  . VAL   A 1 160 ? -1.333  13.633  72.518 1.00 26.66 ? 424 VAL   A CG1  1 
ATOM   1297 C  CG2  . VAL   A 1 160 ? -0.924  11.166  72.904 1.00 21.37 ? 424 VAL   A CG2  1 
ATOM   1298 N  N    . LEU   A 1 161 ? -4.962  13.384  72.886 1.00 21.60 ? 425 LEU   A N    1 
ATOM   1299 C  CA   . LEU   A 1 161 ? -5.853  14.539  72.661 1.00 19.81 ? 425 LEU   A CA   1 
ATOM   1300 C  C    . LEU   A 1 161 ? -6.866  14.704  73.788 1.00 25.88 ? 425 LEU   A C    1 
ATOM   1301 O  O    . LEU   A 1 161 ? -7.122  15.822  74.246 1.00 25.65 ? 425 LEU   A O    1 
ATOM   1302 C  CB   . LEU   A 1 161 ? -6.636  14.409  71.321 1.00 23.39 ? 425 LEU   A CB   1 
ATOM   1303 C  CG   . LEU   A 1 161 ? -5.837  14.540  70.050 1.00 26.03 ? 425 LEU   A CG   1 
ATOM   1304 C  CD1  . LEU   A 1 161 ? -6.669  14.228  68.827 1.00 28.77 ? 425 LEU   A CD1  1 
ATOM   1305 C  CD2  . LEU   A 1 161 ? -5.309  15.948  69.977 1.00 25.63 ? 425 LEU   A CD2  1 
ATOM   1306 N  N    . ILE   A 1 162 ? -7.463  13.612  74.260 1.00 23.32 ? 426 ILE   A N    1 
ATOM   1307 C  CA   . ILE   A 1 162 ? -8.559  13.734  75.237 1.00 25.37 ? 426 ILE   A CA   1 
ATOM   1308 C  C    . ILE   A 1 162 ? -7.989  13.678  76.643 1.00 26.14 ? 426 ILE   A C    1 
ATOM   1309 O  O    . ILE   A 1 162 ? -7.963  12.609  77.275 1.00 26.68 ? 426 ILE   A O    1 
ATOM   1310 C  CB   . ILE   A 1 162 ? -9.616  12.646  75.007 1.00 22.82 ? 426 ILE   A CB   1 
ATOM   1311 C  CG1  . ILE   A 1 162 ? -10.042 12.618  73.537 1.00 24.07 ? 426 ILE   A CG1  1 
ATOM   1312 C  CG2  . ILE   A 1 162 ? -10.810 12.833  75.963 1.00 28.49 ? 426 ILE   A CG2  1 
ATOM   1313 C  CD1  . ILE   A 1 162 ? -10.663 13.975  72.980 1.00 29.53 ? 426 ILE   A CD1  1 
ATOM   1314 N  N    . ASN   A 1 163 ? -7.513  14.834  77.103 1.00 24.35 ? 427 ASN   A N    1 
ATOM   1315 C  CA   . ASN   A 1 163 ? -6.771  14.996  78.350 1.00 27.54 ? 427 ASN   A CA   1 
ATOM   1316 C  C    . ASN   A 1 163 ? -7.475  16.078  79.175 1.00 28.62 ? 427 ASN   A C    1 
ATOM   1317 O  O    . ASN   A 1 163 ? -7.433  17.268  78.807 1.00 27.02 ? 427 ASN   A O    1 
ATOM   1318 C  CB   . ASN   A 1 163 ? -5.316  15.391  78.029 1.00 31.43 ? 427 ASN   A CB   1 
ATOM   1319 C  CG   . ASN   A 1 163 ? -4.469  15.652  79.263 1.00 31.90 ? 427 ASN   A CG   1 
ATOM   1320 O  OD1  . ASN   A 1 163 ? -4.971  15.837  80.361 1.00 33.79 ? 427 ASN   A OD1  1 
ATOM   1321 N  ND2  . ASN   A 1 163 ? -3.157  15.665  79.069 1.00 34.01 ? 427 ASN   A ND2  1 
ATOM   1322 N  N    . ALA   A 1 164 ? -8.139  15.675  80.257 1.00 26.47 ? 428 ALA   A N    1 
ATOM   1323 C  CA   . ALA   A 1 164 ? -9.009  16.585  81.019 1.00 29.07 ? 428 ALA   A CA   1 
ATOM   1324 C  C    . ALA   A 1 164 ? -8.208  17.541  81.897 1.00 33.73 ? 428 ALA   A C    1 
ATOM   1325 O  O    . ALA   A 1 164 ? -8.792  18.382  82.593 1.00 34.45 ? 428 ALA   A O    1 
ATOM   1326 C  CB   . ALA   A 1 164 ? -9.987  15.783  81.874 1.00 31.73 ? 428 ALA   A CB   1 
ATOM   1327 N  N    . HIS   A 1 165 ? -6.882  17.425  81.859 1.00 30.88 ? 429 HIS   A N    1 
ATOM   1328 C  CA   . HIS   A 1 165 ? -6.020  18.290  82.670 1.00 34.30 ? 429 HIS   A CA   1 
ATOM   1329 C  C    . HIS   A 1 165 ? -5.558  19.564  81.955 1.00 33.93 ? 429 HIS   A C    1 
ATOM   1330 O  O    . HIS   A 1 165 ? -4.960  20.427  82.592 1.00 37.70 ? 429 HIS   A O    1 
ATOM   1331 C  CB   . HIS   A 1 165 ? -4.807  17.517  83.171 1.00 36.97 ? 429 HIS   A CB   1 
ATOM   1332 C  CG   . HIS   A 1 165 ? -5.171  16.289  83.936 1.00 42.30 ? 429 HIS   A CG   1 
ATOM   1333 N  ND1  . HIS   A 1 165 ? -5.486  16.312  85.276 1.00 49.35 ? 429 HIS   A ND1  1 
ATOM   1334 C  CD2  . HIS   A 1 165 ? -5.310  14.997  83.538 1.00 47.15 ? 429 HIS   A CD2  1 
ATOM   1335 C  CE1  . HIS   A 1 165 ? -5.779  15.087  85.679 1.00 52.38 ? 429 HIS   A CE1  1 
ATOM   1336 N  NE2  . HIS   A 1 165 ? -5.685  14.273  84.641 1.00 51.62 ? 429 HIS   A NE2  1 
ATOM   1337 N  N    . ARG   A 1 166 ? -5.856  19.708  80.666 1.00 29.02 ? 430 ARG   A N    1 
ATOM   1338 C  CA   . ARG   A 1 166 ? -5.444  20.880  79.919 1.00 27.63 ? 430 ARG   A CA   1 
ATOM   1339 C  C    . ARG   A 1 166 ? -6.075  22.110  80.530 1.00 30.69 ? 430 ARG   A C    1 
ATOM   1340 O  O    . ARG   A 1 166 ? -7.270  22.150  80.809 1.00 32.56 ? 430 ARG   A O    1 
ATOM   1341 C  CB   . ARG   A 1 166 ? -5.844  20.806  78.438 1.00 25.17 ? 430 ARG   A CB   1 
ATOM   1342 C  CG   . ARG   A 1 166 ? -5.456  19.542  77.716 1.00 26.70 ? 430 ARG   A CG   1 
ATOM   1343 C  CD   . ARG   A 1 166 ? -3.955  19.401  77.586 1.00 27.93 ? 430 ARG   A CD   1 
ATOM   1344 N  NE   . ARG   A 1 166 ? -3.604  18.463  76.520 1.00 26.55 ? 430 ARG   A NE   1 
ATOM   1345 C  CZ   . ARG   A 1 166 ? -2.370  18.054  76.249 1.00 30.90 ? 430 ARG   A CZ   1 
ATOM   1346 N  NH1  . ARG   A 1 166 ? -1.346  18.492  76.982 1.00 32.17 ? 430 ARG   A NH1  1 
ATOM   1347 N  NH2  . ARG   A 1 166 ? -2.156  17.220  75.238 1.00 28.11 ? 430 ARG   A NH2  1 
ATOM   1348 N  N    . PRO   A 1 167 ? -5.269  23.145  80.725 1.00 35.46 ? 431 PRO   A N    1 
ATOM   1349 C  CA   . PRO   A 1 167 ? -5.832  24.364  81.299 1.00 36.59 ? 431 PRO   A CA   1 
ATOM   1350 C  C    . PRO   A 1 167 ? -6.803  25.034  80.355 1.00 31.63 ? 431 PRO   A C    1 
ATOM   1351 O  O    . PRO   A 1 167 ? -6.615  25.015  79.136 1.00 33.02 ? 431 PRO   A O    1 
ATOM   1352 C  CB   . PRO   A 1 167 ? -4.594  25.244  81.534 1.00 37.12 ? 431 PRO   A CB   1 
ATOM   1353 C  CG   . PRO   A 1 167 ? -3.462  24.261  81.663 1.00 40.63 ? 431 PRO   A CG   1 
ATOM   1354 C  CD   . PRO   A 1 167 ? -3.798  23.183  80.654 1.00 32.66 ? 431 PRO   A CD   1 
ATOM   1355 N  N    . GLY   A 1 168 ? -7.825  25.645  80.927 1.00 34.51 ? 432 GLY   A N    1 
ATOM   1356 C  CA   . GLY   A 1 168 ? -8.772  26.408  80.145 1.00 35.96 ? 432 GLY   A CA   1 
ATOM   1357 C  C    . GLY   A 1 168 ? -10.026 25.681  79.700 1.00 34.00 ? 432 GLY   A C    1 
ATOM   1358 O  O    . GLY   A 1 168 ? -10.841 26.267  79.002 1.00 33.71 ? 432 GLY   A O    1 
ATOM   1359 N  N    . LEU   A 1 169 ? -10.175 24.409  80.060 1.00 33.42 ? 433 LEU   A N    1 
ATOM   1360 C  CA   . LEU   A 1 169 ? -11.407 23.689  79.705 1.00 30.92 ? 433 LEU   A CA   1 
ATOM   1361 C  C    . LEU   A 1 169 ? -12.571 24.273  80.460 1.00 30.68 ? 433 LEU   A C    1 
ATOM   1362 O  O    . LEU   A 1 169 ? -12.463 24.517  81.657 1.00 35.48 ? 433 LEU   A O    1 
ATOM   1363 C  CB   . LEU   A 1 169 ? -11.304 22.206  80.032 1.00 26.86 ? 433 LEU   A CB   1 
ATOM   1364 C  CG   . LEU   A 1 169 ? -10.298 21.442  79.192 1.00 28.95 ? 433 LEU   A CG   1 
ATOM   1365 C  CD1  . LEU   A 1 169 ? -10.170 20.028  79.701 1.00 28.92 ? 433 LEU   A CD1  1 
ATOM   1366 C  CD2  . LEU   A 1 169 ? -10.706 21.446  77.730 1.00 28.71 ? 433 LEU   A CD2  1 
ATOM   1367 N  N    . GLN   A 1 170 ? -13.705 24.456  79.786 1.00 33.55 ? 434 GLN   A N    1 
ATOM   1368 C  CA   . GLN   A 1 170 ? -14.915 24.943  80.453 1.00 34.40 ? 434 GLN   A CA   1 
ATOM   1369 C  C    . GLN   A 1 170 ? -15.811 23.836  80.992 1.00 37.70 ? 434 GLN   A C    1 
ATOM   1370 O  O    . GLN   A 1 170 ? -16.613 24.053  81.908 1.00 41.52 ? 434 GLN   A O    1 
ATOM   1371 C  CB   . GLN   A 1 170 ? -15.708 25.816  79.492 1.00 37.53 ? 434 GLN   A CB   1 
ATOM   1372 C  CG   . GLN   A 1 170 ? -14.971 27.098  79.186 1.00 44.15 ? 434 GLN   A CG   1 
ATOM   1373 C  CD   . GLN   A 1 170 ? -15.647 27.943  78.125 1.00 54.58 ? 434 GLN   A CD   1 
ATOM   1374 O  OE1  . GLN   A 1 170 ? -16.634 27.531  77.507 1.00 60.77 ? 434 GLN   A OE1  1 
ATOM   1375 N  NE2  . GLN   A 1 170 ? -15.106 29.132  77.898 1.00 55.43 ? 434 GLN   A NE2  1 
ATOM   1376 N  N    . GLU   A 1 171 ? -15.703 22.665  80.393 1.00 32.42 ? 435 GLU   A N    1 
ATOM   1377 C  CA   . GLU   A 1 171 ? -16.528 21.531  80.778 1.00 35.13 ? 435 GLU   A CA   1 
ATOM   1378 C  C    . GLU   A 1 171 ? -15.627 20.368  81.126 1.00 33.52 ? 435 GLU   A C    1 
ATOM   1379 O  O    . GLU   A 1 171 ? -15.606 19.356  80.449 1.00 32.83 ? 435 GLU   A O    1 
ATOM   1380 C  CB   . GLU   A 1 171 ? -17.501 21.159  79.657 1.00 42.33 ? 435 GLU   A CB   1 
ATOM   1381 C  CG   . GLU   A 1 171 ? -18.632 22.168  79.468 1.00 44.03 ? 435 GLU   A CG   1 
ATOM   1382 C  CD   . GLU   A 1 171 ? -19.497 21.868  78.255 1.00 50.30 ? 435 GLU   A CD   1 
ATOM   1383 O  OE1  . GLU   A 1 171 ? -19.008 21.269  77.270 1.00 52.07 ? 435 GLU   A OE1  1 
ATOM   1384 O  OE2  . GLU   A 1 171 ? -20.682 22.241  78.293 1.00 57.67 ? 435 GLU   A OE2  1 
ATOM   1385 N  N    . LYS   A 1 172 ? -14.869 20.528  82.197 1.00 33.43 ? 436 LYS   A N    1 
ATOM   1386 C  CA   . LYS   A 1 172 ? -13.822 19.564  82.508 1.00 36.13 ? 436 LYS   A CA   1 
ATOM   1387 C  C    . LYS   A 1 172 ? -14.436 18.186  82.750 1.00 35.57 ? 436 LYS   A C    1 
ATOM   1388 O  O    . LYS   A 1 172 ? -13.867 17.165  82.346 1.00 30.16 ? 436 LYS   A O    1 
ATOM   1389 C  CB   . LYS   A 1 172 ? -13.018 20.027  83.728 1.00 42.02 ? 436 LYS   A CB   1 
ATOM   1390 C  CG   . LYS   A 1 172 ? -11.855 19.113  84.085 1.00 41.04 ? 436 LYS   A CG   1 
ATOM   1391 C  CD   . LYS   A 1 172 ? -11.221 19.509  85.403 1.00 42.29 ? 436 LYS   A CD   1 
ATOM   1392 C  CE   . LYS   A 1 172 ? -10.100 18.547  85.786 1.00 42.75 ? 436 LYS   A CE   1 
ATOM   1393 N  NZ   . LYS   A 1 172 ? -9.302  19.111  86.912 1.00 47.94 ? 436 LYS   A NZ   1 
ATOM   1394 N  N    . ARG   A 1 173 ? -15.599 18.171  83.392 1.00 38.70 ? 437 ARG   A N    1 
ATOM   1395 C  CA   . ARG   A 1 173 ? -16.269 16.931  83.724 1.00 42.07 ? 437 ARG   A CA   1 
ATOM   1396 C  C    . ARG   A 1 173 ? -16.508 16.100  82.479 1.00 36.12 ? 437 ARG   A C    1 
ATOM   1397 O  O    . ARG   A 1 173 ? -16.320 14.886  82.489 1.00 35.56 ? 437 ARG   A O    1 
ATOM   1398 C  CB   . ARG   A 1 173 ? -17.607 17.212  84.428 1.00 49.20 ? 437 ARG   A CB   1 
ATOM   1399 C  CG   . ARG   A 1 173 ? -18.000 16.120  85.386 1.00 59.17 ? 437 ARG   A CG   1 
ATOM   1400 C  CD   . ARG   A 1 173 ? -19.489 15.851  85.404 1.00 68.74 ? 437 ARG   A CD   1 
ATOM   1401 N  NE   . ARG   A 1 173 ? -19.736 14.472  85.819 1.00 75.43 ? 437 ARG   A NE   1 
ATOM   1402 C  CZ   . ARG   A 1 173 ? -20.014 14.105  87.063 1.00 79.79 ? 437 ARG   A CZ   1 
ATOM   1403 N  NH1  . ARG   A 1 173 ? -20.108 15.024  88.013 1.00 84.12 ? 437 ARG   A NH1  1 
ATOM   1404 N  NH2  . ARG   A 1 173 ? -20.208 12.825  87.355 1.00 78.10 ? 437 ARG   A NH2  1 
ATOM   1405 N  N    . LYS   A 1 174 ? -16.973 16.767  81.431 1.00 31.35 ? 438 LYS   A N    1 
ATOM   1406 C  CA   . LYS   A 1 174 ? -17.269 16.125  80.153 1.00 31.98 ? 438 LYS   A CA   1 
ATOM   1407 C  C    . LYS   A 1 174 ? -16.021 15.470  79.565 1.00 29.56 ? 438 LYS   A C    1 
ATOM   1408 O  O    . LYS   A 1 174 ? -16.079 14.346  79.057 1.00 32.33 ? 438 LYS   A O    1 
ATOM   1409 C  CB   . LYS   A 1 174 ? -17.819 17.146  79.182 1.00 31.68 ? 438 LYS   A CB   1 
ATOM   1410 C  CG   . LYS   A 1 174 ? -18.642 16.580  78.053 1.00 43.84 ? 438 LYS   A CG   1 
ATOM   1411 C  CD   . LYS   A 1 174 ? -19.775 17.540  77.670 1.00 51.80 ? 438 LYS   A CD   1 
ATOM   1412 C  CE   . LYS   A 1 174 ? -20.776 16.881  76.725 1.00 58.45 ? 438 LYS   A CE   1 
ATOM   1413 N  NZ   . LYS   A 1 174 ? -21.956 17.764  76.418 1.00 59.58 ? 438 LYS   A NZ   1 
ATOM   1414 N  N    . VAL   A 1 175 ? -14.892 16.161  79.634 1.00 26.02 ? 439 VAL   A N    1 
ATOM   1415 C  CA   . VAL   A 1 175 ? -13.671 15.635  79.036 1.00 23.87 ? 439 VAL   A CA   1 
ATOM   1416 C  C    . VAL   A 1 175 ? -13.186 14.454  79.883 1.00 27.65 ? 439 VAL   A C    1 
ATOM   1417 O  O    . VAL   A 1 175 ? -12.693 13.449  79.348 1.00 27.87 ? 439 VAL   A O    1 
ATOM   1418 C  CB   . VAL   A 1 175 ? -12.589 16.715  78.894 1.00 27.59 ? 439 VAL   A CB   1 
ATOM   1419 C  CG1  . VAL   A 1 175 ? -11.408 16.114  78.180 1.00 25.61 ? 439 VAL   A CG1  1 
ATOM   1420 C  CG2  . VAL   A 1 175 ? -13.166 17.939  78.116 1.00 29.90 ? 439 VAL   A CG2  1 
ATOM   1421 N  N    . GLU   A 1 176 ? -13.321 14.584  81.204 1.00 27.47 ? 440 GLU   A N    1 
ATOM   1422 C  CA   . GLU   A 1 176 ? -12.936 13.500  82.116 1.00 28.98 ? 440 GLU   A CA   1 
ATOM   1423 C  C    . GLU   A 1 176 ? -13.679 12.226  81.769 1.00 30.06 ? 440 GLU   A C    1 
ATOM   1424 O  O    . GLU   A 1 176 ? -13.105 11.146  81.824 1.00 29.07 ? 440 GLU   A O    1 
ATOM   1425 C  CB   . GLU   A 1 176 ? -13.215 13.882  83.571 1.00 31.93 ? 440 GLU   A CB   1 
ATOM   1426 C  CG   . GLU   A 1 176 ? -12.254 14.927  84.112 1.00 38.36 ? 440 GLU   A CG   1 
ATOM   1427 C  CD   . GLU   A 1 176 ? -12.547 15.303  85.549 1.00 51.80 ? 440 GLU   A CD   1 
ATOM   1428 O  OE1  . GLU   A 1 176 ? -13.674 15.045  86.011 1.00 53.10 ? 440 GLU   A OE1  1 
ATOM   1429 O  OE2  . GLU   A 1 176 ? -11.645 15.863  86.219 1.00 58.11 ? 440 GLU   A OE2  1 
ATOM   1430 N  N    . GLN   A 1 177 ? -14.960 12.349  81.450 1.00 30.88 ? 441 GLN   A N    1 
ATOM   1431 C  CA   . GLN   A 1 177 ? -15.778 11.168  81.150 1.00 34.68 ? 441 GLN   A CA   1 
ATOM   1432 C  C    . GLN   A 1 177 ? -15.299 10.523  79.872 1.00 33.50 ? 441 GLN   A C    1 
ATOM   1433 O  O    . GLN   A 1 177 ? -15.219 9.293   79.778 1.00 32.36 ? 441 GLN   A O    1 
ATOM   1434 C  CB   . GLN   A 1 177 ? -17.269 11.526  81.031 1.00 39.23 ? 441 GLN   A CB   1 
ATOM   1435 C  CG   . GLN   A 1 177 ? -17.937 11.846  82.364 1.00 63.57 ? 441 GLN   A CG   1 
ATOM   1436 C  CD   . GLN   A 1 177 ? -17.659 10.787  83.420 1.00 81.00 ? 441 GLN   A CD   1 
ATOM   1437 O  OE1  . GLN   A 1 177 ? -17.850 9.588   83.182 1.00 82.93 ? 441 GLN   A OE1  1 
ATOM   1438 N  NE2  . GLN   A 1 177 ? -17.187 11.224  84.590 1.00 88.27 ? 441 GLN   A NE2  1 
ATOM   1439 N  N    . LEU   A 1 178 ? -15.003 11.347  78.874 1.00 26.31 ? 442 LEU   A N    1 
ATOM   1440 C  CA   . LEU   A 1 178 ? -14.492 10.818  77.619 1.00 25.06 ? 442 LEU   A CA   1 
ATOM   1441 C  C    . LEU   A 1 178 ? -13.142 10.132  77.832 1.00 27.76 ? 442 LEU   A C    1 
ATOM   1442 O  O    . LEU   A 1 178 ? -12.861 9.049   77.305 1.00 26.25 ? 442 LEU   A O    1 
ATOM   1443 C  CB   . LEU   A 1 178 ? -14.338 11.936  76.613 1.00 24.09 ? 442 LEU   A CB   1 
ATOM   1444 C  CG   . LEU   A 1 178 ? -13.943 11.451  75.240 1.00 29.72 ? 442 LEU   A CG   1 
ATOM   1445 C  CD1  . LEU   A 1 178 ? -14.734 10.238  74.836 1.00 34.29 ? 442 LEU   A CD1  1 
ATOM   1446 C  CD2  . LEU   A 1 178 ? -14.158 12.586  74.233 1.00 36.02 ? 442 LEU   A CD2  1 
ATOM   1447 N  N    . GLN   A 1 179 ? -12.273 10.784  78.581 1.00 26.66 ? 443 GLN   A N    1 
ATOM   1448 C  CA   . GLN   A 1 179 ? -10.966 10.202  78.851 1.00 24.11 ? 443 GLN   A CA   1 
ATOM   1449 C  C    . GLN   A 1 179 ? -11.087 8.872   79.565 1.00 26.55 ? 443 GLN   A C    1 
ATOM   1450 O  O    . GLN   A 1 179 ? -10.361 7.943   79.261 1.00 26.49 ? 443 GLN   A O    1 
ATOM   1451 C  CB   . GLN   A 1 179 ? -10.145 11.167  79.680 1.00 26.12 ? 443 GLN   A CB   1 
ATOM   1452 C  CG   . GLN   A 1 179 ? -8.736  10.632  79.985 1.00 25.80 ? 443 GLN   A CG   1 
ATOM   1453 C  CD   . GLN   A 1 179 ? -7.934  11.590  80.828 1.00 33.39 ? 443 GLN   A CD   1 
ATOM   1454 O  OE1  . GLN   A 1 179 ? -8.235  12.771  80.898 1.00 30.26 ? 443 GLN   A OE1  1 
ATOM   1455 N  NE2  . GLN   A 1 179 ? -6.908  11.077  81.488 1.00 39.25 ? 443 GLN   A NE2  1 
ATOM   1456 N  N    . TYR   A 1 180 ? -11.969 8.818   80.556 1.00 25.77 ? 444 TYR   A N    1 
ATOM   1457 C  CA   . TYR   A 1 180 ? -12.175 7.609   81.382 1.00 24.30 ? 444 TYR   A CA   1 
ATOM   1458 C  C    . TYR   A 1 180 ? -12.565 6.455   80.459 1.00 29.33 ? 444 TYR   A C    1 
ATOM   1459 O  O    . TYR   A 1 180 ? -12.056 5.345   80.584 1.00 28.40 ? 444 TYR   A O    1 
ATOM   1460 C  CB   . TYR   A 1 180 ? -13.261 7.932   82.425 1.00 28.14 ? 444 TYR   A CB   1 
ATOM   1461 C  CG   . TYR   A 1 180 ? -13.818 6.837   83.322 1.00 30.08 ? 444 TYR   A CG   1 
ATOM   1462 C  CD1  . TYR   A 1 180 ? -14.749 5.904   82.845 1.00 32.08 ? 444 TYR   A CD1  1 
ATOM   1463 C  CD2  . TYR   A 1 180 ? -13.530 6.832   84.678 1.00 32.46 ? 444 TYR   A CD2  1 
ATOM   1464 C  CE1  . TYR   A 1 180 ? -15.302 4.955   83.689 1.00 35.33 ? 444 TYR   A CE1  1 
ATOM   1465 C  CE2  . TYR   A 1 180 ? -14.086 5.884   85.534 1.00 35.88 ? 444 TYR   A CE2  1 
ATOM   1466 C  CZ   . TYR   A 1 180 ? -14.975 4.960   85.035 1.00 37.21 ? 444 TYR   A CZ   1 
ATOM   1467 O  OH   . TYR   A 1 180 ? -15.514 4.054   85.920 1.00 35.23 ? 444 TYR   A OH   1 
ATOM   1468 N  N    . ASN   A 1 181 ? -13.479 6.711   79.520 1.00 26.80 ? 445 ASN   A N    1 
ATOM   1469 C  CA   . ASN   A 1 181 ? -13.919 5.631   78.635 1.00 26.49 ? 445 ASN   A CA   1 
ATOM   1470 C  C    . ASN   A 1 181 ? -12.842 5.223   77.627 1.00 27.27 ? 445 ASN   A C    1 
ATOM   1471 O  O    . ASN   A 1 181 ? -12.651 4.025   77.397 1.00 27.81 ? 445 ASN   A O    1 
ATOM   1472 C  CB   . ASN   A 1 181 ? -15.198 6.034   77.889 1.00 24.48 ? 445 ASN   A CB   1 
ATOM   1473 C  CG   . ASN   A 1 181 ? -16.397 6.035   78.784 1.00 29.80 ? 445 ASN   A CG   1 
ATOM   1474 O  OD1  . ASN   A 1 181 ? -16.441 5.348   79.815 1.00 31.37 ? 445 ASN   A OD1  1 
ATOM   1475 N  ND2  . ASN   A 1 181 ? -17.391 6.797   78.395 1.00 38.93 ? 445 ASN   A ND2  1 
ATOM   1476 N  N    . LEU   A 1 182 ? -12.110 6.187   77.056 1.00 22.73 ? 446 LEU   A N    1 
ATOM   1477 C  CA   . LEU   A 1 182 ? -10.997 5.847   76.166 1.00 22.94 ? 446 LEU   A CA   1 
ATOM   1478 C  C    . LEU   A 1 182 ? -9.893  5.094   76.906 1.00 24.68 ? 446 LEU   A C    1 
ATOM   1479 O  O    . LEU   A 1 182 ? -9.225  4.247   76.312 1.00 25.60 ? 446 LEU   A O    1 
ATOM   1480 C  CB   . LEU   A 1 182 ? -10.373 7.089   75.529 1.00 22.23 ? 446 LEU   A CB   1 
ATOM   1481 C  CG   . LEU   A 1 182 ? -11.254 7.713   74.449 1.00 29.57 ? 446 LEU   A CG   1 
ATOM   1482 C  CD1  . LEU   A 1 182 ? -10.792 9.168   74.152 1.00 26.78 ? 446 LEU   A CD1  1 
ATOM   1483 C  CD2  . LEU   A 1 182 ? -11.169 6.852   73.209 1.00 34.36 ? 446 LEU   A CD2  1 
ATOM   1484 N  N    . GLU   A 1 183 ? -9.637  5.435   78.170 1.00 25.86 ? 447 GLU   A N    1 
ATOM   1485 C  CA   . GLU   A 1 183 ? -8.599  4.712   78.905 1.00 28.28 ? 447 GLU   A CA   1 
ATOM   1486 C  C    . GLU   A 1 183 ? -9.047  3.249   79.094 1.00 25.91 ? 447 GLU   A C    1 
ATOM   1487 O  O    . GLU   A 1 183 ? -8.281  2.316   78.883 1.00 25.67 ? 447 GLU   A O    1 
ATOM   1488 C  CB   . GLU   A 1 183 ? -8.288  5.367   80.256 1.00 29.82 ? 447 GLU   A CB   1 
ATOM   1489 C  CG   . GLU   A 1 183 ? -7.548  6.712   80.143 1.00 30.03 ? 447 GLU   A CG   1 
ATOM   1490 C  CD   . GLU   A 1 183 ? -7.373  7.415   81.482 1.00 35.86 ? 447 GLU   A CD   1 
ATOM   1491 O  OE1  . GLU   A 1 183 ? -7.980  6.972   82.481 1.00 39.35 ? 447 GLU   A OE1  1 
ATOM   1492 O  OE2  . GLU   A 1 183 ? -6.614  8.415   81.536 1.00 36.45 ? 447 GLU   A OE2  1 
ATOM   1493 N  N    . LEU   A 1 184 ? -10.306 3.067   79.473 1.00 25.90 ? 448 LEU   A N    1 
ATOM   1494 C  CA   . LEU   A 1 184 ? -10.853 1.731   79.663 1.00 24.81 ? 448 LEU   A CA   1 
ATOM   1495 C  C    . LEU   A 1 184 ? -10.770 0.951   78.344 1.00 24.95 ? 448 LEU   A C    1 
ATOM   1496 O  O    . LEU   A 1 184 ? -10.384 -0.219  78.323 1.00 28.57 ? 448 LEU   A O    1 
ATOM   1497 C  CB   . LEU   A 1 184 ? -12.306 1.847   80.157 1.00 29.21 ? 448 LEU   A CB   1 
ATOM   1498 C  CG   . LEU   A 1 184 ? -13.042 0.549   80.427 1.00 35.12 ? 448 LEU   A CG   1 
ATOM   1499 C  CD1  . LEU   A 1 184 ? -12.193 -0.439  81.230 1.00 40.96 ? 448 LEU   A CD1  1 
ATOM   1500 C  CD2  . LEU   A 1 184 ? -14.304 0.931   81.164 1.00 40.11 ? 448 LEU   A CD2  1 
ATOM   1501 N  N    . ALA   A 1 185 ? -11.103 1.611   77.247 1.00 26.86 ? 449 ALA   A N    1 
ATOM   1502 C  CA   . ALA   A 1 185 ? -11.061 0.996   75.914 1.00 22.54 ? 449 ALA   A CA   1 
ATOM   1503 C  C    . ALA   A 1 185 ? -9.626  0.568   75.568 1.00 23.44 ? 449 ALA   A C    1 
ATOM   1504 O  O    . ALA   A 1 185 ? -9.398  -0.538  75.066 1.00 24.78 ? 449 ALA   A O    1 
ATOM   1505 C  CB   . ALA   A 1 185 ? -11.560 1.971   74.874 1.00 25.20 ? 449 ALA   A CB   1 
ATOM   1506 N  N    . PHE   A 1 186 ? -8.671  1.479   75.766 1.00 24.03 ? 450 PHE   A N    1 
ATOM   1507 C  CA   . PHE   A 1 186 ? -7.282  1.185   75.503 1.00 24.25 ? 450 PHE   A CA   1 
ATOM   1508 C  C    . PHE   A 1 186 ? -6.830  -0.022  76.282 1.00 25.06 ? 450 PHE   A C    1 
ATOM   1509 O  O    . PHE   A 1 186 ? -6.279  -0.988  75.725 1.00 23.35 ? 450 PHE   A O    1 
ATOM   1510 C  CB   . PHE   A 1 186 ? -6.412  2.402   75.877 1.00 23.30 ? 450 PHE   A CB   1 
ATOM   1511 C  CG   . PHE   A 1 186 ? -4.982  2.308   75.463 1.00 25.23 ? 450 PHE   A CG   1 
ATOM   1512 C  CD1  . PHE   A 1 186 ? -4.617  1.783   74.249 1.00 25.17 ? 450 PHE   A CD1  1 
ATOM   1513 C  CD2  . PHE   A 1 186 ? -4.011  2.883   76.260 1.00 31.76 ? 450 PHE   A CD2  1 
ATOM   1514 C  CE1  . PHE   A 1 186 ? -3.261  1.789   73.857 1.00 25.07 ? 450 PHE   A CE1  1 
ATOM   1515 C  CE2  . PHE   A 1 186 ? -2.656  2.869   75.894 1.00 32.79 ? 450 PHE   A CE2  1 
ATOM   1516 C  CZ   . PHE   A 1 186 ? -2.298  2.331   74.670 1.00 29.35 ? 450 PHE   A CZ   1 
ATOM   1517 N  N    . HIS   A 1 187 ? -7.072  -0.008  77.589 1.00 22.58 ? 451 HIS   A N    1 
ATOM   1518 C  CA   . HIS   A 1 187 ? -6.579  -1.119  78.407 1.00 24.43 ? 451 HIS   A CA   1 
ATOM   1519 C  C    . HIS   A 1 187 ? -7.306  -2.409  78.136 1.00 23.58 ? 451 HIS   A C    1 
ATOM   1520 O  O    . HIS   A 1 187 ? -6.697  -3.461  78.139 1.00 27.66 ? 451 HIS   A O    1 
ATOM   1521 C  CB   . HIS   A 1 187 ? -6.671  -0.781  79.886 1.00 24.82 ? 451 HIS   A CB   1 
ATOM   1522 C  CG   . HIS   A 1 187 ? -5.668  0.243   80.301 1.00 28.89 ? 451 HIS   A CG   1 
ATOM   1523 N  ND1  . HIS   A 1 187 ? -4.354  -0.078  80.597 1.00 35.69 ? 451 HIS   A ND1  1 
ATOM   1524 C  CD2  . HIS   A 1 187 ? -5.781  1.577   80.455 1.00 30.28 ? 451 HIS   A CD2  1 
ATOM   1525 C  CE1  . HIS   A 1 187 ? -3.707  1.031   80.907 1.00 35.35 ? 451 HIS   A CE1  1 
ATOM   1526 N  NE2  . HIS   A 1 187 ? -4.539  2.051   80.812 1.00 33.04 ? 451 HIS   A NE2  1 
ATOM   1527 N  N    . HIS   A 1 188 ? -8.612  -2.314  77.848 1.00 23.53 ? 452 HIS   A N    1 
ATOM   1528 C  CA   . HIS   A 1 188 ? -9.385  -3.501  77.474 1.00 25.67 ? 452 HIS   A CA   1 
ATOM   1529 C  C    . HIS   A 1 188 ? -8.777  -4.140  76.235 1.00 23.91 ? 452 HIS   A C    1 
ATOM   1530 O  O    . HIS   A 1 188 ? -8.604  -5.381  76.153 1.00 28.34 ? 452 HIS   A O    1 
ATOM   1531 C  CB   . HIS   A 1 188 ? -10.855 -3.119  77.211 1.00 27.20 ? 452 HIS   A CB   1 
ATOM   1532 C  CG   . HIS   A 1 188 ? -11.691 -4.258  76.708 1.00 30.15 ? 452 HIS   A CG   1 
ATOM   1533 N  ND1  . HIS   A 1 188 ? -12.187 -5.234  77.540 1.00 27.33 ? 452 HIS   A ND1  1 
ATOM   1534 C  CD2  . HIS   A 1 188 ? -12.078 -4.599  75.455 1.00 32.15 ? 452 HIS   A CD2  1 
ATOM   1535 C  CE1  . HIS   A 1 188 ? -12.874 -6.110  76.831 1.00 32.10 ? 452 HIS   A CE1  1 
ATOM   1536 N  NE2  . HIS   A 1 188 ? -12.801 -5.761  75.556 1.00 30.37 ? 452 HIS   A NE2  1 
ATOM   1537 N  N    . HIS   A 1 189 ? -8.466  -3.287  75.276 1.00 24.71 ? 453 HIS   A N    1 
ATOM   1538 C  CA   . HIS   A 1 189 ? -7.942  -3.781  74.024 1.00 25.64 ? 453 HIS   A CA   1 
ATOM   1539 C  C    . HIS   A 1 189 ? -6.533  -4.363  74.147 1.00 25.62 ? 453 HIS   A C    1 
ATOM   1540 O  O    . HIS   A 1 189 ? -6.233  -5.393  73.546 1.00 26.20 ? 453 HIS   A O    1 
ATOM   1541 C  CB   . HIS   A 1 189 ? -7.941  -2.694  72.988 1.00 28.22 ? 453 HIS   A CB   1 
ATOM   1542 C  CG   . HIS   A 1 189 ? -7.752  -3.229  71.607 1.00 29.62 ? 453 HIS   A CG   1 
ATOM   1543 N  ND1  . HIS   A 1 189 ? -8.670  -4.085  71.028 1.00 38.61 ? 453 HIS   A ND1  1 
ATOM   1544 C  CD2  . HIS   A 1 189 ? -6.736  -3.111  70.735 1.00 31.07 ? 453 HIS   A CD2  1 
ATOM   1545 C  CE1  . HIS   A 1 189 ? -8.237  -4.434  69.837 1.00 38.19 ? 453 HIS   A CE1  1 
ATOM   1546 N  NE2  . HIS   A 1 189 ? -7.083  -3.844  69.618 1.00 31.33 ? 453 HIS   A NE2  1 
ATOM   1547 N  N    . LEU   A 1 190 ? -5.672  -3.682  74.884 1.00 23.93 ? 454 LEU   A N    1 
ATOM   1548 C  CA   . LEU   A 1 190 ? -4.357  -4.250  75.182 1.00 22.74 ? 454 LEU   A CA   1 
ATOM   1549 C  C    . LEU   A 1 190 ? -4.447  -5.631  75.844 1.00 26.16 ? 454 LEU   A C    1 
ATOM   1550 O  O    . LEU   A 1 190 ? -3.699  -6.528  75.473 1.00 27.82 ? 454 LEU   A O    1 
ATOM   1551 C  CB   . LEU   A 1 190 ? -3.579  -3.288  76.062 1.00 25.14 ? 454 LEU   A CB   1 
ATOM   1552 C  CG   . LEU   A 1 190 ? -3.190  -1.970  75.425 1.00 24.22 ? 454 LEU   A CG   1 
ATOM   1553 C  CD1  . LEU   A 1 190 ? -2.442  -1.101  76.439 1.00 26.83 ? 454 LEU   A CD1  1 
ATOM   1554 C  CD2  . LEU   A 1 190 ? -2.304  -2.158  74.183 1.00 23.89 ? 454 LEU   A CD2  1 
ATOM   1555 N  N    . CYS   A 1 191 ? -5.342  -5.820  76.824 1.00 27.28 ? 455 CYS   A N    1 
ATOM   1556 C  CA   . CYS   A 1 191 ? -5.432  -7.144  77.477 1.00 27.64 ? 455 CYS   A CA   1 
ATOM   1557 C  C    . CYS   A 1 191 ? -5.965  -8.191  76.512 1.00 30.65 ? 455 CYS   A C    1 
ATOM   1558 O  O    . CYS   A 1 191 ? -5.479  -9.329  76.470 1.00 33.57 ? 455 CYS   A O    1 
ATOM   1559 C  CB   . CYS   A 1 191 ? -6.307  -7.035  78.715 1.00 38.47 ? 455 CYS   A CB   1 
ATOM   1560 S  SG   . CYS   A 1 191 ? -5.571  -5.994  79.988 1.00 54.66 ? 455 CYS   A SG   1 
ATOM   1561 N  N    . LYS   A 1 192 ? -6.965  -7.798  75.726 1.00 31.48 ? 456 LYS   A N    1 
ATOM   1562 C  CA   . LYS   A 1 192 ? -7.537  -8.684  74.733 1.00 34.03 ? 456 LYS   A CA   1 
ATOM   1563 C  C    . LYS   A 1 192 ? -6.491  -9.193  73.748 1.00 31.48 ? 456 LYS   A C    1 
ATOM   1564 O  O    . LYS   A 1 192 ? -6.537  -10.356 73.328 1.00 32.80 ? 456 LYS   A O    1 
ATOM   1565 C  CB   . LYS   A 1 192 ? -8.660  -7.965  73.984 1.00 32.89 ? 456 LYS   A CB   1 
ATOM   1566 C  CG   . LYS   A 1 192 ? -9.506  -8.869  73.159 1.00 37.34 ? 456 LYS   A CG   1 
ATOM   1567 C  CD   . LYS   A 1 192 ? -10.816 -8.171  72.796 1.00 42.99 ? 456 LYS   A CD   1 
ATOM   1568 C  CE   . LYS   A 1 192 ? -11.519 -8.935  71.706 1.00 53.80 ? 456 LYS   A CE   1 
ATOM   1569 N  NZ   . LYS   A 1 192 ? -11.389 -10.398 71.951 1.00 62.29 ? 456 LYS   A NZ   1 
ATOM   1570 N  N    . THR   A 1 193 ? -5.539  -8.330  73.404 1.00 30.93 ? 457 THR   A N    1 
ATOM   1571 C  CA   . THR   A 1 193 ? -4.565  -8.649  72.372 1.00 31.25 ? 457 THR   A CA   1 
ATOM   1572 C  C    . THR   A 1 193 ? -3.218  -9.067  72.946 1.00 32.04 ? 457 THR   A C    1 
ATOM   1573 O  O    . THR   A 1 193 ? -2.240  -9.179  72.212 1.00 33.81 ? 457 THR   A O    1 
ATOM   1574 C  CB   . THR   A 1 193 ? -4.369  -7.463  71.403 1.00 31.39 ? 457 THR   A CB   1 
ATOM   1575 O  OG1  . THR   A 1 193 ? -3.932  -6.291  72.122 1.00 30.60 ? 457 THR   A OG1  1 
ATOM   1576 C  CG2  . THR   A 1 193 ? -5.690  -7.164  70.675 1.00 33.72 ? 457 THR   A CG2  1 
ATOM   1577 N  N    . HIS   A 1 194 ? -3.163  -9.305  74.250 1.00 32.56 ? 458 HIS   A N    1 
ATOM   1578 C  CA   . HIS   A 1 194 ? -1.912  -9.673  74.925 1.00 28.05 ? 458 HIS   A CA   1 
ATOM   1579 C  C    . HIS   A 1 194 ? -0.803  -8.680  74.708 1.00 28.19 ? 458 HIS   A C    1 
ATOM   1580 O  O    . HIS   A 1 194 ? 0.345   -9.076  74.460 1.00 35.59 ? 458 HIS   A O    1 
ATOM   1581 C  CB   . HIS   A 1 194 ? -1.441  -11.058 74.461 1.00 36.17 ? 458 HIS   A CB   1 
ATOM   1582 C  CG   . HIS   A 1 194 ? -2.500  -12.095 74.569 1.00 39.99 ? 458 HIS   A CG   1 
ATOM   1583 N  ND1  . HIS   A 1 194 ? -2.855  -12.654 75.777 1.00 46.91 ? 458 HIS   A ND1  1 
ATOM   1584 C  CD2  . HIS   A 1 194 ? -3.324  -12.630 73.643 1.00 47.54 ? 458 HIS   A CD2  1 
ATOM   1585 C  CE1  . HIS   A 1 194 ? -3.833  -13.519 75.583 1.00 52.64 ? 458 HIS   A CE1  1 
ATOM   1586 N  NE2  . HIS   A 1 194 ? -4.139  -13.524 74.298 1.00 52.63 ? 458 HIS   A NE2  1 
ATOM   1587 N  N    . ARG   A 1 195 ? -1.110  -7.397  74.855 1.00 25.49 ? 459 ARG   A N    1 
ATOM   1588 C  CA   . ARG   A 1 195 ? -0.125  -6.353  74.617 1.00 25.55 ? 459 ARG   A CA   1 
ATOM   1589 C  C    . ARG   A 1 195 ? 0.020   -5.376  75.761 1.00 29.61 ? 459 ARG   A C    1 
ATOM   1590 O  O    . ARG   A 1 195 ? 0.539   -4.273  75.567 1.00 29.63 ? 459 ARG   A O    1 
ATOM   1591 C  CB   . ARG   A 1 195 ? -0.459  -5.591  73.353 1.00 28.95 ? 459 ARG   A CB   1 
ATOM   1592 C  CG   . ARG   A 1 195 ? -0.385  -6.422  72.121 1.00 30.27 ? 459 ARG   A CG   1 
ATOM   1593 C  CD   . ARG   A 1 195 ? 0.993   -6.452  71.568 1.00 31.03 ? 459 ARG   A CD   1 
ATOM   1594 N  NE   . ARG   A 1 195 ? 1.352   -5.144  71.019 1.00 29.65 ? 459 ARG   A NE   1 
ATOM   1595 C  CZ   . ARG   A 1 195 ? 2.600   -4.785  70.725 1.00 29.25 ? 459 ARG   A CZ   1 
ATOM   1596 N  NH1  . ARG   A 1 195 ? 3.606   -5.632  70.913 1.00 38.39 ? 459 ARG   A NH1  1 
ATOM   1597 N  NH2  . ARG   A 1 195 ? 2.837   -3.597  70.202 1.00 29.14 ? 459 ARG   A NH2  1 
ATOM   1598 N  N    . GLN   A 1 196 ? -0.397  -5.774  76.959 1.00 31.95 ? 460 GLN   A N    1 
ATOM   1599 C  CA   . GLN   A 1 196 ? -0.314  -4.898  78.141 1.00 35.76 ? 460 GLN   A CA   1 
ATOM   1600 C  C    . GLN   A 1 196 ? 1.109   -4.406  78.345 1.00 35.61 ? 460 GLN   A C    1 
ATOM   1601 O  O    . GLN   A 1 196 ? 1.333   -3.292  78.819 1.00 38.08 ? 460 GLN   A O    1 
ATOM   1602 C  CB   . GLN   A 1 196 ? -0.743  -5.619  79.427 1.00 42.47 ? 460 GLN   A CB   1 
ATOM   1603 C  CG   . GLN   A 1 196 ? -2.090  -6.282  79.386 1.00 48.15 ? 460 GLN   A CG   1 
ATOM   1604 C  CD   . GLN   A 1 196 ? -2.009  -7.768  79.086 1.00 48.98 ? 460 GLN   A CD   1 
ATOM   1605 O  OE1  . GLN   A 1 196 ? -1.506  -8.184  78.032 1.00 47.07 ? 460 GLN   A OE1  1 
ATOM   1606 N  NE2  . GLN   A 1 196 ? -2.486  -8.582  80.026 1.00 47.29 ? 460 GLN   A NE2  1 
ATOM   1607 N  N    . SER   A 1 197 ? 2.060   -5.246  77.978 1.00 35.85 ? 461 SER   A N    1 
ATOM   1608 C  CA   . SER   A 1 197 ? 3.448   -4.977  78.326 1.00 42.75 ? 461 SER   A CA   1 
ATOM   1609 C  C    . SER   A 1 197 ? 3.992   -3.725  77.651 1.00 43.09 ? 461 SER   A C    1 
ATOM   1610 O  O    . SER   A 1 197 ? 5.033   -3.218  78.061 1.00 45.15 ? 461 SER   A O    1 
ATOM   1611 C  CB   . SER   A 1 197 ? 4.310   -6.161  77.953 1.00 46.94 ? 461 SER   A CB   1 
ATOM   1612 O  OG   . SER   A 1 197 ? 4.514   -6.123  76.553 1.00 53.78 ? 461 SER   A OG   1 
ATOM   1613 N  N    . ILE   A 1 198 ? 3.325   -3.216  76.620 1.00 41.50 ? 462 ILE   A N    1 
ATOM   1614 C  CA   . ILE   A 1 198 ? 3.843   -1.995  76.006 1.00 42.88 ? 462 ILE   A CA   1 
ATOM   1615 C  C    . ILE   A 1 198 ? 3.663   -0.782  76.928 1.00 42.96 ? 462 ILE   A C    1 
ATOM   1616 O  O    . ILE   A 1 198 ? 4.241   0.274   76.692 1.00 46.05 ? 462 ILE   A O    1 
ATOM   1617 C  CB   . ILE   A 1 198 ? 3.185   -1.694  74.652 1.00 43.15 ? 462 ILE   A CB   1 
ATOM   1618 C  CG1  . ILE   A 1 198 ? 1.751   -1.230  74.861 1.00 36.68 ? 462 ILE   A CG1  1 
ATOM   1619 C  CG2  . ILE   A 1 198 ? 3.259   -2.902  73.742 1.00 48.82 ? 462 ILE   A CG2  1 
ATOM   1620 C  CD1  . ILE   A 1 198 ? 1.241   -0.359  73.759 1.00 41.06 ? 462 ILE   A CD1  1 
ATOM   1621 N  N    . LEU   A 1 199 ? 2.830   -0.893  77.946 1.00 38.94 ? 463 LEU   A N    1 
ATOM   1622 C  CA   . LEU   A 1 199 ? 2.565   0.272   78.773 1.00 37.79 ? 463 LEU   A CA   1 
ATOM   1623 C  C    . LEU   A 1 199 ? 3.862   0.692   79.474 1.00 40.56 ? 463 LEU   A C    1 
ATOM   1624 O  O    . LEU   A 1 199 ? 4.175   1.874   79.548 1.00 42.82 ? 463 LEU   A O    1 
ATOM   1625 C  CB   . LEU   A 1 199 ? 1.485   -0.027  79.799 1.00 35.79 ? 463 LEU   A CB   1 
ATOM   1626 C  CG   . LEU   A 1 199 ? 0.078   -0.324  79.269 1.00 37.92 ? 463 LEU   A CG   1 
ATOM   1627 C  CD1  . LEU   A 1 199 ? -0.727  -1.067  80.335 1.00 46.18 ? 463 LEU   A CD1  1 
ATOM   1628 C  CD2  . LEU   A 1 199 ? -0.586  0.938   78.879 1.00 32.75 ? 463 LEU   A CD2  1 
ATOM   1629 N  N    . ALA   A 1 200 ? 4.630   -0.282  79.955 1.00 40.88 ? 464 ALA   A N    1 
ATOM   1630 C  CA   . ALA   A 1 200 ? 5.806   0.027   80.752 1.00 41.48 ? 464 ALA   A CA   1 
ATOM   1631 C  C    . ALA   A 1 200 ? 6.931   0.581   79.884 1.00 40.88 ? 464 ALA   A C    1 
ATOM   1632 O  O    . ALA   A 1 200 ? 7.963   1.031   80.401 1.00 43.80 ? 464 ALA   A O    1 
ATOM   1633 C  CB   . ALA   A 1 200 ? 6.263   -1.213  81.526 1.00 42.87 ? 464 ALA   A CB   1 
ATOM   1634 N  N    . LYS   A 1 201 ? 6.737   0.542   78.571 1.00 36.80 ? 465 LYS   A N    1 
ATOM   1635 C  CA   . LYS   A 1 201 ? 7.710   1.064   77.628 1.00 39.00 ? 465 LYS   A CA   1 
ATOM   1636 C  C    . LYS   A 1 201 ? 7.323   2.389   76.991 1.00 41.74 ? 465 LYS   A C    1 
ATOM   1637 O  O    . LYS   A 1 201 ? 8.071   2.897   76.167 1.00 55.15 ? 465 LYS   A O    1 
ATOM   1638 C  CB   . LYS   A 1 201 ? 7.965   0.038   76.539 1.00 43.61 ? 465 LYS   A CB   1 
ATOM   1639 C  CG   . LYS   A 1 201 ? 8.639   -1.193  77.107 1.00 52.22 ? 465 LYS   A CG   1 
ATOM   1640 C  CD   . LYS   A 1 201 ? 8.430   -2.405  76.260 1.00 55.74 ? 465 LYS   A CD   1 
ATOM   1641 C  CE   . LYS   A 1 201 ? 9.039   -2.227  74.909 1.00 59.84 ? 465 LYS   A CE   1 
ATOM   1642 N  NZ   . LYS   A 1 201 ? 9.243   -3.573  74.314 1.00 63.76 ? 465 LYS   A NZ   1 
ATOM   1643 N  N    . LEU   A 1 202 ? 6.184   2.930   77.368 1.00 48.66 ? 466 LEU   A N    1 
ATOM   1644 C  CA   . LEU   A 1 202 ? 5.807   4.246   76.879 1.00 45.55 ? 466 LEU   A CA   1 
ATOM   1645 C  C    . LEU   A 1 202 ? 6.765   5.205   77.544 1.00 50.90 ? 466 LEU   A C    1 
ATOM   1646 O  O    . LEU   A 1 202 ? 7.188   4.993   78.670 1.00 51.50 ? 466 LEU   A O    1 
ATOM   1647 C  CB   . LEU   A 1 202 ? 4.331   4.539   77.130 1.00 45.40 ? 466 LEU   A CB   1 
ATOM   1648 C  CG   . LEU   A 1 202 ? 3.342   3.798   76.251 1.00 41.06 ? 466 LEU   A CG   1 
ATOM   1649 C  CD1  . LEU   A 1 202 ? 1.995   3.719   76.919 1.00 44.54 ? 466 LEU   A CD1  1 
ATOM   1650 C  CD2  . LEU   A 1 202 ? 3.242   4.513   74.925 1.00 46.56 ? 466 LEU   A CD2  1 
ATOM   1651 N  N    . PRO   A 1 203 ? 7.170   6.269   76.837 1.00 57.71 ? 467 PRO   A N    1 
ATOM   1652 C  CA   . PRO   A 1 203 ? 8.224   7.101   77.435 1.00 59.47 ? 467 PRO   A CA   1 
ATOM   1653 C  C    . PRO   A 1 203 ? 7.842   8.074   78.572 1.00 58.99 ? 467 PRO   A C    1 
ATOM   1654 O  O    . PRO   A 1 203 ? 6.678   8.383   78.758 1.00 56.96 ? 467 PRO   A O    1 
ATOM   1655 C  CB   . PRO   A 1 203 ? 8.721   7.899   76.223 1.00 61.46 ? 467 PRO   A CB   1 
ATOM   1656 C  CG   . PRO   A 1 203 ? 7.543   8.070   75.395 1.00 62.63 ? 467 PRO   A CG   1 
ATOM   1657 C  CD   . PRO   A 1 203 ? 6.766   6.796   75.515 1.00 58.55 ? 467 PRO   A CD   1 
ATOM   1658 N  N    . PRO   A 1 204 ? 8.845   8.561   79.303 1.00 62.08 ? 468 PRO   A N    1 
ATOM   1659 C  CA   . PRO   A 1 204 ? 8.587   9.529   80.379 1.00 63.88 ? 468 PRO   A CA   1 
ATOM   1660 C  C    . PRO   A 1 204 ? 8.100   10.872  79.889 1.00 69.36 ? 468 PRO   A C    1 
ATOM   1661 O  O    . PRO   A 1 204 ? 8.700   11.380  78.954 1.00 71.18 ? 468 PRO   A O    1 
ATOM   1662 C  CB   . PRO   A 1 204 ? 9.952   9.723   81.016 1.00 60.65 ? 468 PRO   A CB   1 
ATOM   1663 C  CG   . PRO   A 1 204 ? 10.831  8.658   80.477 1.00 57.90 ? 468 PRO   A CG   1 
ATOM   1664 C  CD   . PRO   A 1 204 ? 10.274  8.233   79.177 1.00 59.19 ? 468 PRO   A CD   1 
ATOM   1665 N  N    . LYS   A 1 205 ? 7.032   11.414  80.450 1.00 70.67 ? 469 LYS   A N    1 
ATOM   1666 C  CA   . LYS   A 1 205 ? 6.519   12.754  80.086 1.00 72.81 ? 469 LYS   A CA   1 
ATOM   1667 C  C    . LYS   A 1 205 ? 7.539   13.835  79.680 1.00 74.03 ? 469 LYS   A C    1 
ATOM   1668 O  O    . LYS   A 1 205 ? 7.387   14.464  78.646 1.00 78.27 ? 469 LYS   A O    1 
ATOM   1669 C  CB   . LYS   A 1 205 ? 5.683   13.293  81.245 1.00 73.48 ? 469 LYS   A CB   1 
ATOM   1670 C  CG   . LYS   A 1 205 ? 6.447   13.489  82.545 1.00 74.86 ? 469 LYS   A CG   1 
ATOM   1671 C  CD   . LYS   A 1 205 ? 5.561   14.025  83.654 1.00 75.79 ? 469 LYS   A CD   1 
ATOM   1672 C  CE   . LYS   A 1 205 ? 6.351   14.210  84.938 1.00 74.79 ? 469 LYS   A CE   1 
ATOM   1673 N  NZ   . LYS   A 1 205 ? 6.834   12.911  85.471 1.00 74.67 ? 469 LYS   A NZ   1 
ATOM   1674 N  N    . GLY   A 1 206 ? 8.566   14.046  80.499 1.00 73.00 ? 470 GLY   A N    1 
ATOM   1675 C  CA   . GLY   A 1 206 ? 9.572   15.056  80.205 1.00 73.22 ? 470 GLY   A CA   1 
ATOM   1676 C  C    . GLY   A 1 206 ? 10.208  15.113  78.841 1.00 73.20 ? 470 GLY   A C    1 
ATOM   1677 O  O    . GLY   A 1 206 ? 10.810  16.108  78.486 1.00 71.18 ? 470 GLY   A O    1 
ATOM   1678 N  N    . LYS   A 1 207 ? 10.087  14.039  78.084 1.00 76.94 ? 471 LYS   A N    1 
ATOM   1679 C  CA   . LYS   A 1 207 ? 10.645  13.997  76.758 1.00 75.90 ? 471 LYS   A CA   1 
ATOM   1680 C  C    . LYS   A 1 207 ? 9.755   14.749  75.792 1.00 69.35 ? 471 LYS   A C    1 
ATOM   1681 O  O    . LYS   A 1 207 ? 10.207  15.673  75.134 1.00 67.04 ? 471 LYS   A O    1 
ATOM   1682 C  CB   . LYS   A 1 207 ? 10.777  12.555  76.303 1.00 77.53 ? 471 LYS   A CB   1 
ATOM   1683 C  CG   . LYS   A 1 207 ? 11.810  12.346  75.217 1.00 77.72 ? 471 LYS   A CG   1 
ATOM   1684 C  CD   . LYS   A 1 207 ? 13.102  11.788  75.777 1.00 75.75 ? 471 LYS   A CD   1 
ATOM   1685 C  CE   . LYS   A 1 207 ? 13.999  12.891  76.315 1.00 74.35 ? 471 LYS   A CE   1 
ATOM   1686 N  NZ   . LYS   A 1 207 ? 14.540  12.572  77.660 1.00 72.74 ? 471 LYS   A NZ   1 
ATOM   1687 N  N    . LEU   A 1 208 ? 8.501   14.360  75.722 1.00 62.52 ? 472 LEU   A N    1 
ATOM   1688 C  CA   . LEU   A 1 208 ? 7.598   14.972  74.781 1.00 60.60 ? 472 LEU   A CA   1 
ATOM   1689 C  C    . LEU   A 1 208 ? 7.318   16.389  75.133 1.00 60.80 ? 472 LEU   A C    1 
ATOM   1690 O  O    . LEU   A 1 208 ? 7.139   17.227  74.259 1.00 61.88 ? 472 LEU   A O    1 
ATOM   1691 C  CB   . LEU   A 1 208 ? 6.268   14.214  74.767 1.00 58.01 ? 472 LEU   A CB   1 
ATOM   1692 C  CG   . LEU   A 1 208 ? 5.138   14.550  73.801 1.00 60.65 ? 472 LEU   A CG   1 
ATOM   1693 C  CD1  . LEU   A 1 208 ? 4.354   13.309  73.479 1.00 60.25 ? 472 LEU   A CD1  1 
ATOM   1694 C  CD2  . LEU   A 1 208 ? 4.227   15.574  74.402 1.00 61.28 ? 472 LEU   A CD2  1 
ATOM   1695 N  N    . ARG   A 1 209 ? 7.219   16.666  76.414 1.00 65.98 ? 473 ARG   A N    1 
ATOM   1696 C  CA   . ARG   A 1 209 ? 6.871   17.989  76.839 1.00 67.16 ? 473 ARG   A CA   1 
ATOM   1697 C  C    . ARG   A 1 209 ? 7.971   18.889  76.430 1.00 65.12 ? 473 ARG   A C    1 
ATOM   1698 O  O    . ARG   A 1 209 ? 7.731   19.941  75.888 1.00 71.53 ? 473 ARG   A O    1 
ATOM   1699 C  CB   . ARG   A 1 209 ? 6.673   17.992  78.368 1.00 69.05 ? 473 ARG   A CB   1 
ATOM   1700 C  CG   . ARG   A 1 209 ? 6.201   19.310  78.943 1.00 65.23 ? 473 ARG   A CG   1 
ATOM   1701 C  CD   . ARG   A 1 209 ? 6.547   19.414  80.414 1.00 67.41 ? 473 ARG   A CD   1 
ATOM   1702 N  NE   . ARG   A 1 209 ? 5.661   18.597  81.234 1.00 74.49 ? 473 ARG   A NE   1 
ATOM   1703 C  CZ   . ARG   A 1 209 ? 6.072   17.775  82.192 1.00 81.26 ? 473 ARG   A CZ   1 
ATOM   1704 N  NH1  . ARG   A 1 209 ? 7.366   17.650  82.458 1.00 81.88 ? 473 ARG   A NH1  1 
ATOM   1705 N  NH2  . ARG   A 1 209 ? 5.185   17.075  82.885 1.00 83.00 ? 473 ARG   A NH2  1 
ATOM   1706 N  N    . SER   A 1 210 ? 9.189   18.481  76.700 1.00 52.21 ? 474 SER   A N    1 
ATOM   1707 C  CA   . SER   A 1 210 ? 10.285  19.260  76.264 1.00 49.60 ? 474 SER   A CA   1 
ATOM   1708 C  C    . SER   A 1 210 ? 10.180  19.424  74.749 1.00 56.73 ? 474 SER   A C    1 
ATOM   1709 O  O    . SER   A 1 210 ? 10.390  20.513  74.244 1.00 50.03 ? 474 SER   A O    1 
ATOM   1710 C  CB   . SER   A 1 210 ? 11.593  18.583  76.617 1.00 50.08 ? 474 SER   A CB   1 
ATOM   1711 O  OG   . SER   A 1 210 ? 12.689  19.460  76.452 1.00 54.05 ? 474 SER   A OG   1 
ATOM   1712 N  N    . LEU   A 1 211 ? 9.824   18.350  74.040 1.00 41.65 ? 475 LEU   A N    1 
ATOM   1713 C  CA   . LEU   A 1 211 ? 9.808   18.386  72.571 1.00 39.60 ? 475 LEU   A CA   1 
ATOM   1714 C  C    . LEU   A 1 211 ? 8.844   19.403  72.039 1.00 34.32 ? 475 LEU   A C    1 
ATOM   1715 O  O    . LEU   A 1 211 ? 9.197   20.236  71.236 1.00 30.98 ? 475 LEU   A O    1 
ATOM   1716 C  CB   . LEU   A 1 211 ? 9.479   17.016  71.992 1.00 34.28 ? 475 LEU   A CB   1 
ATOM   1717 C  CG   . LEU   A 1 211 ? 9.696   16.818  70.498 1.00 31.78 ? 475 LEU   A CG   1 
ATOM   1718 C  CD1  . LEU   A 1 211 ? 11.058  17.327  70.103 1.00 37.96 ? 475 LEU   A CD1  1 
ATOM   1719 C  CD2  . LEU   A 1 211 ? 9.545   15.357  70.134 1.00 25.94 ? 475 LEU   A CD2  1 
ATOM   1720 N  N    . CYS   A 1 212 ? 7.621   19.336  72.513 1.00 35.59 ? 476 CYS   A N    1 
ATOM   1721 C  CA   . CYS   A 1 212 ? 6.620   20.247  72.003 1.00 36.60 ? 476 CYS   A CA   1 
ATOM   1722 C  C    . CYS   A 1 212 ? 6.976   21.696  72.393 1.00 36.78 ? 476 CYS   A C    1 
ATOM   1723 O  O    . CYS   A 1 212 ? 6.754   22.590  71.608 1.00 33.69 ? 476 CYS   A O    1 
ATOM   1724 C  CB   . CYS   A 1 212 ? 5.194   19.808  72.400 1.00 46.97 ? 476 CYS   A CB   1 
ATOM   1725 S  SG   . CYS   A 1 212 ? 3.833   20.611  71.480 1.00 58.40 ? 476 CYS   A SG   1 
ATOM   1726 N  N    . SER   A 1 213 ? 7.606   21.908  73.547 1.00 41.46 ? 477 SER   A N    1 
ATOM   1727 C  CA   . SER   A 1 213 ? 8.022   23.275  73.928 1.00 41.64 ? 477 SER   A CA   1 
ATOM   1728 C  C    . SER   A 1 213 ? 9.158   23.763  73.060 1.00 39.78 ? 477 SER   A C    1 
ATOM   1729 O  O    . SER   A 1 213 ? 9.223   24.938  72.685 1.00 37.17 ? 477 SER   A O    1 
ATOM   1730 C  CB   . SER   A 1 213 ? 8.421   23.330  75.410 1.00 45.21 ? 477 SER   A CB   1 
ATOM   1731 O  OG   . SER   A 1 213 ? 9.814   23.197  75.572 1.00 49.36 ? 477 SER   A OG   1 
ATOM   1732 N  N    . GLN   A 1 214 ? 10.067  22.857  72.764 1.00 34.42 ? 478 GLN   A N    1 
ATOM   1733 C  CA   . GLN   A 1 214 ? 11.145  23.182  71.850 1.00 31.75 ? 478 GLN   A CA   1 
ATOM   1734 C  C    . GLN   A 1 214 ? 10.627  23.595  70.483 1.00 26.79 ? 478 GLN   A C    1 
ATOM   1735 O  O    . GLN   A 1 214 ? 11.117  24.574  69.921 1.00 30.54 ? 478 GLN   A O    1 
ATOM   1736 C  CB   . GLN   A 1 214 ? 12.105  21.995  71.642 1.00 36.25 ? 478 GLN   A CB   1 
ATOM   1737 C  CG   . GLN   A 1 214 ? 13.058  21.697  72.760 1.00 40.58 ? 478 GLN   A CG   1 
ATOM   1738 C  CD   . GLN   A 1 214 ? 14.006  20.576  72.377 1.00 40.09 ? 478 GLN   A CD   1 
ATOM   1739 O  OE1  . GLN   A 1 214 ? 13.896  19.459  72.879 1.00 47.72 ? 478 GLN   A OE1  1 
ATOM   1740 N  NE2  . GLN   A 1 214 ? 14.930  20.862  71.473 1.00 41.26 ? 478 GLN   A NE2  1 
ATOM   1741 N  N    . HIS   A 1 215 ? 9.650   22.839  69.971 1.00 26.52 ? 479 HIS   A N    1 
ATOM   1742 C  CA   . HIS   A 1 215 ? 9.034   23.114  68.671 1.00 25.30 ? 479 HIS   A CA   1 
ATOM   1743 C  C    . HIS   A 1 215 ? 8.403   24.467  68.697 1.00 22.93 ? 479 HIS   A C    1 
ATOM   1744 O  O    . HIS   A 1 215 ? 8.541   25.278  67.758 1.00 27.63 ? 479 HIS   A O    1 
ATOM   1745 C  CB   . HIS   A 1 215 ? 7.969   22.049  68.330 1.00 23.91 ? 479 HIS   A CB   1 
ATOM   1746 C  CG   . HIS   A 1 215 ? 6.891   22.539  67.396 1.00 25.34 ? 479 HIS   A CG   1 
ATOM   1747 N  ND1  . HIS   A 1 215 ? 7.128   22.742  66.051 1.00 27.28 ? 479 HIS   A ND1  1 
ATOM   1748 C  CD2  . HIS   A 1 215 ? 5.590   22.835  67.606 1.00 29.03 ? 479 HIS   A CD2  1 
ATOM   1749 C  CE1  . HIS   A 1 215 ? 6.002   23.128  65.472 1.00 27.82 ? 479 HIS   A CE1  1 
ATOM   1750 N  NE2  . HIS   A 1 215 ? 5.051   23.223  66.388 1.00 29.40 ? 479 HIS   A NE2  1 
ATOM   1751 N  N    . VAL   A 1 216 ? 7.677   24.751  69.779 1.00 24.18 ? 480 VAL   A N    1 
ATOM   1752 C  CA   . VAL   A 1 216 ? 7.012   26.051  69.890 1.00 28.64 ? 480 VAL   A CA   1 
ATOM   1753 C  C    . VAL   A 1 216 ? 8.003   27.220  69.847 1.00 28.48 ? 480 VAL   A C    1 
ATOM   1754 O  O    . VAL   A 1 216 ? 7.752   28.223  69.167 1.00 28.17 ? 480 VAL   A O    1 
ATOM   1755 C  CB   . VAL   A 1 216 ? 6.178   26.099  71.152 1.00 27.66 ? 480 VAL   A CB   1 
ATOM   1756 C  CG1  . VAL   A 1 216 ? 5.678   27.512  71.403 1.00 29.86 ? 480 VAL   A CG1  1 
ATOM   1757 C  CG2  . VAL   A 1 216 ? 4.972   25.164  70.998 1.00 33.56 ? 480 VAL   A CG2  1 
ATOM   1758 N  N    . GLU   A 1 217 ? 9.122   27.101  70.560 1.00 26.51 ? 481 GLU   A N    1 
ATOM   1759 C  CA   . GLU   A 1 217 ? 10.150  28.134  70.511 1.00 28.34 ? 481 GLU   A CA   1 
ATOM   1760 C  C    . GLU   A 1 217 ? 10.689  28.316  69.085 1.00 25.30 ? 481 GLU   A C    1 
ATOM   1761 O  O    . GLU   A 1 217 ? 10.796  29.451  68.602 1.00 29.16 ? 481 GLU   A O    1 
ATOM   1762 C  CB   . GLU   A 1 217 ? 11.312  27.806  71.465 1.00 31.86 ? 481 GLU   A CB   1 
ATOM   1763 C  CG   . GLU   A 1 217 ? 11.071  28.154  72.923 1.00 48.23 ? 481 GLU   A CG   1 
ATOM   1764 C  CD   . GLU   A 1 217 ? 12.353  28.637  73.627 1.00 63.57 ? 481 GLU   A CD   1 
ATOM   1765 O  OE1  . GLU   A 1 217 ? 13.350  28.925  72.926 1.00 65.85 ? 481 GLU   A OE1  1 
ATOM   1766 O  OE2  . GLU   A 1 217 ? 12.369  28.729  74.878 1.00 70.28 ? 481 GLU   A OE2  1 
ATOM   1767 N  N    . ARG   A 1 218 ? 11.006  27.213  68.396 1.00 24.16 ? 482 ARG   A N    1 
ATOM   1768 C  CA   . ARG   A 1 218 ? 11.641  27.326  67.083 1.00 27.74 ? 482 ARG   A CA   1 
ATOM   1769 C  C    . ARG   A 1 218 ? 10.658  27.813  66.044 1.00 22.75 ? 482 ARG   A C    1 
ATOM   1770 O  O    . ARG   A 1 218 ? 11.025  28.584  65.176 1.00 25.47 ? 482 ARG   A O    1 
ATOM   1771 C  CB   . ARG   A 1 218 ? 12.271  25.999  66.627 1.00 30.02 ? 482 ARG   A CB   1 
ATOM   1772 C  CG   . ARG   A 1 218 ? 13.207  25.359  67.644 1.00 42.12 ? 482 ARG   A CG   1 
ATOM   1773 C  CD   . ARG   A 1 218 ? 14.304  26.313  68.088 1.00 48.13 ? 482 ARG   A CD   1 
ATOM   1774 N  NE   . ARG   A 1 218 ? 14.970  26.930  66.945 1.00 50.61 ? 482 ARG   A NE   1 
ATOM   1775 C  CZ   . ARG   A 1 218 ? 16.002  27.761  67.046 1.00 56.01 ? 482 ARG   A CZ   1 
ATOM   1776 N  NH1  . ARG   A 1 218 ? 16.550  28.282  65.953 1.00 57.96 ? 482 ARG   A NH1  1 
ATOM   1777 N  NH2  . ARG   A 1 218 ? 16.480  28.074  68.243 1.00 52.22 ? 482 ARG   A NH2  1 
ATOM   1778 N  N    . LEU   A 1 219 ? 9.411   27.373  66.127 1.00 21.57 ? 483 LEU   A N    1 
ATOM   1779 C  CA   . LEU   A 1 219 ? 8.394   27.864  65.225 1.00 22.89 ? 483 LEU   A CA   1 
ATOM   1780 C  C    . LEU   A 1 219 ? 8.303   29.407  65.298 1.00 24.00 ? 483 LEU   A C    1 
ATOM   1781 O  O    . LEU   A 1 219 ? 8.180   30.081  64.276 1.00 23.26 ? 483 LEU   A O    1 
ATOM   1782 C  CB   . LEU   A 1 219 ? 7.036   27.195  65.574 1.00 23.55 ? 483 LEU   A CB   1 
ATOM   1783 C  CG   . LEU   A 1 219 ? 5.852   27.664  64.750 1.00 27.43 ? 483 LEU   A CG   1 
ATOM   1784 C  CD1  . LEU   A 1 219 ? 6.117   27.413  63.287 1.00 27.43 ? 483 LEU   A CD1  1 
ATOM   1785 C  CD2  . LEU   A 1 219 ? 4.592   26.854  65.215 1.00 27.89 ? 483 LEU   A CD2  1 
ATOM   1786 N  N    . GLN   A 1 220 ? 8.333   29.962  66.506 1.00 22.38 ? 484 GLN   A N    1 
ATOM   1787 C  CA   . GLN   A 1 220 ? 8.220   31.416  66.625 1.00 27.35 ? 484 GLN   A CA   1 
ATOM   1788 C  C    . GLN   A 1 220 ? 9.380   32.153  65.958 1.00 26.05 ? 484 GLN   A C    1 
ATOM   1789 O  O    . GLN   A 1 220 ? 9.189   33.224  65.387 1.00 26.96 ? 484 GLN   A O    1 
ATOM   1790 C  CB   . GLN   A 1 220 ? 8.157   31.852  68.074 1.00 34.64 ? 484 GLN   A CB   1 
ATOM   1791 C  CG   . GLN   A 1 220 ? 6.934   31.417  68.788 1.00 42.49 ? 484 GLN   A CG   1 
ATOM   1792 C  CD   . GLN   A 1 220 ? 6.853   32.087  70.141 1.00 56.58 ? 484 GLN   A CD   1 
ATOM   1793 O  OE1  . GLN   A 1 220 ? 7.745   32.862  70.517 1.00 56.58 ? 484 GLN   A OE1  1 
ATOM   1794 N  NE2  . GLN   A 1 220 ? 5.793   31.791  70.885 1.00 62.10 ? 484 GLN   A NE2  1 
ATOM   1795 N  N    . ILE   A 1 221 ? 10.574  31.572  66.052 1.00 24.95 ? 485 ILE   A N    1 
ATOM   1796 C  CA   . ILE   A 1 221 ? 11.761  32.160  65.436 1.00 22.72 ? 485 ILE   A CA   1 
ATOM   1797 C  C    . ILE   A 1 221 ? 11.594  32.100  63.918 1.00 22.69 ? 485 ILE   A C    1 
ATOM   1798 O  O    . ILE   A 1 221 ? 11.791  33.108  63.253 1.00 22.19 ? 485 ILE   A O    1 
ATOM   1799 C  CB   . ILE   A 1 221 ? 13.023  31.487  65.894 1.00 26.51 ? 485 ILE   A CB   1 
ATOM   1800 C  CG1  . ILE   A 1 221 ? 13.289  31.891  67.345 1.00 29.61 ? 485 ILE   A CG1  1 
ATOM   1801 C  CG2  . ILE   A 1 221 ? 14.166  31.963  65.034 1.00 25.46 ? 485 ILE   A CG2  1 
ATOM   1802 C  CD1  . ILE   A 1 221 ? 14.334  30.993  68.047 1.00 36.14 ? 485 ILE   A CD1  1 
ATOM   1803 N  N    . PHE   A 1 222 ? 11.187  30.952  63.376 1.00 22.05 ? 486 PHE   A N    1 
ATOM   1804 C  CA   . PHE   A 1 222 ? 11.002  30.867  61.919 1.00 22.62 ? 486 PHE   A CA   1 
ATOM   1805 C  C    . PHE   A 1 222 ? 9.966   31.864  61.424 1.00 21.37 ? 486 PHE   A C    1 
ATOM   1806 O  O    . PHE   A 1 222 ? 10.148  32.495  60.375 1.00 23.41 ? 486 PHE   A O    1 
ATOM   1807 C  CB   . PHE   A 1 222 ? 10.602  29.468  61.500 1.00 20.69 ? 486 PHE   A CB   1 
ATOM   1808 C  CG   . PHE   A 1 222 ? 11.719  28.475  61.509 1.00 21.07 ? 486 PHE   A CG   1 
ATOM   1809 C  CD1  . PHE   A 1 222 ? 12.939  28.721  60.888 1.00 25.19 ? 486 PHE   A CD1  1 
ATOM   1810 C  CD2  . PHE   A 1 222 ? 11.524  27.245  62.099 1.00 21.52 ? 486 PHE   A CD2  1 
ATOM   1811 C  CE1  . PHE   A 1 222 ? 13.943  27.734  60.923 1.00 25.86 ? 486 PHE   A CE1  1 
ATOM   1812 C  CE2  . PHE   A 1 222 ? 12.469  26.294  62.113 1.00 24.22 ? 486 PHE   A CE2  1 
ATOM   1813 C  CZ   . PHE   A 1 222 ? 13.697  26.517  61.533 1.00 26.86 ? 486 PHE   A CZ   1 
ATOM   1814 N  N    . GLN   A 1 223 ? 8.839   31.981  62.135 1.00 21.79 ? 487 GLN   A N    1 
ATOM   1815 C  CA   . GLN   A 1 223 ? 7.811   32.927  61.774 1.00 22.75 ? 487 GLN   A CA   1 
ATOM   1816 C  C    . GLN   A 1 223 ? 8.255   34.386  61.818 1.00 22.67 ? 487 GLN   A C    1 
ATOM   1817 O  O    . GLN   A 1 223 ? 7.773   35.226  61.081 1.00 27.63 ? 487 GLN   A O    1 
ATOM   1818 C  CB   . GLN   A 1 223 ? 6.632   32.746  62.714 1.00 25.71 ? 487 GLN   A CB   1 
ATOM   1819 C  CG   . GLN   A 1 223 ? 5.731   31.584  62.342 1.00 37.51 ? 487 GLN   A CG   1 
ATOM   1820 C  CD   . GLN   A 1 223 ? 4.743   31.975  61.256 1.00 51.91 ? 487 GLN   A CD   1 
ATOM   1821 O  OE1  . GLN   A 1 223 ? 5.055   31.937  60.059 1.00 52.37 ? 487 GLN   A OE1  1 
ATOM   1822 N  NE2  . GLN   A 1 223 ? 3.546   32.377  61.674 1.00 61.81 ? 487 GLN   A NE2  1 
ATOM   1823 N  N    . HIS   A 1 224 ? 9.187   34.680  62.718 1.00 24.63 ? 488 HIS   A N    1 
ATOM   1824 C  CA   . HIS   A 1 224 ? 9.734   36.004  62.803 1.00 23.95 ? 488 HIS   A CA   1 
ATOM   1825 C  C    . HIS   A 1 224 ? 10.607  36.324  61.599 1.00 23.87 ? 488 HIS   A C    1 
ATOM   1826 O  O    . HIS   A 1 224 ? 10.558  37.426  61.043 1.00 24.32 ? 488 HIS   A O    1 
ATOM   1827 C  CB   . HIS   A 1 224 ? 10.565  36.106  64.074 1.00 27.81 ? 488 HIS   A CB   1 
ATOM   1828 C  CG   . HIS   A 1 224 ? 11.053  37.479  64.338 1.00 29.93 ? 488 HIS   A CG   1 
ATOM   1829 N  ND1  . HIS   A 1 224 ? 12.380  37.844  64.314 1.00 30.26 ? 488 HIS   A ND1  1 
ATOM   1830 C  CD2  . HIS   A 1 224 ? 10.353  38.619  64.596 1.00 27.32 ? 488 HIS   A CD2  1 
ATOM   1831 C  CE1  . HIS   A 1 224 ? 12.489  39.136  64.596 1.00 29.71 ? 488 HIS   A CE1  1 
ATOM   1832 N  NE2  . HIS   A 1 224 ? 11.266  39.620  64.768 1.00 35.34 ? 488 HIS   A NE2  1 
ATOM   1833 N  N    . LEU   A 1 225 ? 11.444  35.355  61.248 1.00 22.73 ? 489 LEU   A N    1 
ATOM   1834 C  CA   . LEU   A 1 225 ? 12.412  35.550  60.167 1.00 24.22 ? 489 LEU   A CA   1 
ATOM   1835 C  C    . LEU   A 1 225 ? 11.699  35.585  58.828 1.00 25.41 ? 489 LEU   A C    1 
ATOM   1836 O  O    . LEU   A 1 225 ? 12.052  36.387  57.949 1.00 27.33 ? 489 LEU   A O    1 
ATOM   1837 C  CB   . LEU   A 1 225 ? 13.459  34.433  60.174 1.00 22.10 ? 489 LEU   A CB   1 
ATOM   1838 C  CG   . LEU   A 1 225 ? 14.292  34.472  61.467 1.00 24.12 ? 489 LEU   A CG   1 
ATOM   1839 C  CD1  . LEU   A 1 225 ? 15.227  33.246  61.524 1.00 23.70 ? 489 LEU   A CD1  1 
ATOM   1840 C  CD2  . LEU   A 1 225 ? 15.135  35.753  61.582 1.00 30.51 ? 489 LEU   A CD2  1 
ATOM   1841 N  N    . HIS   A 1 226 ? 10.701  34.717  58.676 1.00 23.62 ? 490 HIS   A N    1 
ATOM   1842 C  CA   . HIS   A 1 226 ? 10.002  34.534  57.415 1.00 25.61 ? 490 HIS   A CA   1 
ATOM   1843 C  C    . HIS   A 1 226 ? 8.532   34.233  57.660 1.00 24.05 ? 490 HIS   A C    1 
ATOM   1844 O  O    . HIS   A 1 226 ? 8.104   33.096  57.596 1.00 24.23 ? 490 HIS   A O    1 
ATOM   1845 C  CB   . HIS   A 1 226 ? 10.681  33.423  56.606 1.00 21.42 ? 490 HIS   A CB   1 
ATOM   1846 C  CG   . HIS   A 1 226 ? 12.067  33.774  56.193 1.00 27.24 ? 490 HIS   A CG   1 
ATOM   1847 N  ND1  . HIS   A 1 226 ? 12.331  34.653  55.162 1.00 34.32 ? 490 HIS   A ND1  1 
ATOM   1848 C  CD2  . HIS   A 1 226 ? 13.263  33.365  56.665 1.00 27.81 ? 490 HIS   A CD2  1 
ATOM   1849 C  CE1  . HIS   A 1 226 ? 13.643  34.792  55.039 1.00 31.09 ? 490 HIS   A CE1  1 
ATOM   1850 N  NE2  . HIS   A 1 226 ? 14.236  34.006  55.923 1.00 30.69 ? 490 HIS   A NE2  1 
ATOM   1851 N  N    . PRO   A 1 227 ? 7.752   35.252  57.955 1.00 24.00 ? 491 PRO   A N    1 
ATOM   1852 C  CA   . PRO   A 1 227 ? 6.337   34.987  58.194 1.00 23.45 ? 491 PRO   A CA   1 
ATOM   1853 C  C    . PRO   A 1 227 ? 5.699   34.385  56.915 1.00 31.58 ? 491 PRO   A C    1 
ATOM   1854 O  O    . PRO   A 1 227 ? 5.961   34.872  55.798 1.00 31.92 ? 491 PRO   A O    1 
ATOM   1855 C  CB   . PRO   A 1 227 ? 5.752   36.376  58.535 1.00 32.86 ? 491 PRO   A CB   1 
ATOM   1856 C  CG   . PRO   A 1 227 ? 6.787   37.346  58.153 1.00 32.97 ? 491 PRO   A CG   1 
ATOM   1857 C  CD   . PRO   A 1 227 ? 8.112   36.682  58.071 1.00 28.01 ? 491 PRO   A CD   1 
ATOM   1858 N  N    . ILE   A 1 228 ? 4.955   33.298  57.058 1.00 31.23 ? 492 ILE   A N    1 
ATOM   1859 C  CA   . ILE   A 1 228 ? 4.480   32.615  55.848 1.00 28.72 ? 492 ILE   A CA   1 
ATOM   1860 C  C    . ILE   A 1 228 ? 3.347   33.335  55.152 1.00 42.12 ? 492 ILE   A C    1 
ATOM   1861 O  O    . ILE   A 1 228 ? 2.450   33.758  55.830 1.00 42.30 ? 492 ILE   A O    1 
ATOM   1862 C  CB   . ILE   A 1 228 ? 4.107   31.262  56.204 1.00 33.89 ? 492 ILE   A CB   1 
ATOM   1863 C  CG1  . ILE   A 1 228 ? 3.112   31.336  57.382 1.00 35.94 ? 492 ILE   A CG1  1 
ATOM   1864 C  CG2  . ILE   A 1 228 ? 5.381   30.440  56.465 1.00 33.20 ? 492 ILE   A CG2  1 
ATOM   1865 C  CD1  . ILE   A 1 228 ? 1.685   31.462  56.889 1.00 40.50 ? 492 ILE   A CD1  1 
ATOM   1866 N  N    . ALA   B 1 1   ? -22.287 -0.840  31.627 1.00 43.88 ? 265 ALA   B N    1 
ATOM   1867 C  CA   . ALA   B 1 1   ? -22.345 -0.799  33.085 1.00 40.44 ? 265 ALA   B CA   1 
ATOM   1868 C  C    . ALA   B 1 1   ? -22.455 0.628   33.630 1.00 43.35 ? 265 ALA   B C    1 
ATOM   1869 O  O    . ALA   B 1 1   ? -21.753 1.547   33.208 1.00 43.93 ? 265 ALA   B O    1 
ATOM   1870 C  CB   . ALA   B 1 1   ? -21.125 -1.506  33.693 1.00 35.59 ? 265 ALA   B CB   1 
ATOM   1871 N  N    . SER   B 1 2   ? -23.376 0.792   34.572 1.00 46.70 ? 266 SER   B N    1 
ATOM   1872 C  CA   . SER   B 1 2   ? -23.476 2.002   35.368 1.00 47.87 ? 266 SER   B CA   1 
ATOM   1873 C  C    . SER   B 1 2   ? -22.250 2.252   36.202 1.00 44.20 ? 266 SER   B C    1 
ATOM   1874 O  O    . SER   B 1 2   ? -21.504 1.331   36.534 1.00 43.46 ? 266 SER   B O    1 
ATOM   1875 C  CB   . SER   B 1 2   ? -24.670 1.909   36.304 1.00 55.54 ? 266 SER   B CB   1 
ATOM   1876 O  OG   . SER   B 1 2   ? -25.845 1.685   35.558 1.00 72.49 ? 266 SER   B OG   1 
ATOM   1877 N  N    . LEU   B 1 3   ? -22.039 3.507   36.568 1.00 47.72 ? 267 LEU   B N    1 
ATOM   1878 C  CA   . LEU   B 1 3   ? -20.921 3.824   37.448 1.00 40.67 ? 267 LEU   B CA   1 
ATOM   1879 C  C    . LEU   B 1 3   ? -21.015 3.000   38.731 1.00 42.49 ? 267 LEU   B C    1 
ATOM   1880 O  O    . LEU   B 1 3   ? -20.032 2.451   39.239 1.00 38.98 ? 267 LEU   B O    1 
ATOM   1881 C  CB   . LEU   B 1 3   ? -20.921 5.307   37.780 1.00 41.32 ? 267 LEU   B CB   1 
ATOM   1882 C  CG   . LEU   B 1 3   ? -19.914 5.705   38.849 1.00 44.32 ? 267 LEU   B CG   1 
ATOM   1883 C  CD1  . LEU   B 1 3   ? -18.521 5.233   38.456 1.00 45.18 ? 267 LEU   B CD1  1 
ATOM   1884 C  CD2  . LEU   B 1 3   ? -19.945 7.197   39.014 1.00 48.22 ? 267 LEU   B CD2  1 
ATOM   1885 N  N    . THR   B 1 4   ? -22.226 2.929   39.264 1.00 45.48 ? 268 THR   B N    1 
ATOM   1886 C  CA   . THR   B 1 4   ? -22.473 2.156   40.459 1.00 41.83 ? 268 THR   B CA   1 
ATOM   1887 C  C    . THR   B 1 4   ? -22.138 0.691   40.226 1.00 38.59 ? 268 THR   B C    1 
ATOM   1888 O  O    . THR   B 1 4   ? -21.604 0.046   41.096 1.00 36.55 ? 268 THR   B O    1 
ATOM   1889 C  CB   . THR   B 1 4   ? -23.953 2.282   40.924 1.00 42.82 ? 268 THR   B CB   1 
ATOM   1890 O  OG1  . THR   B 1 4   ? -24.206 3.628   41.344 1.00 53.82 ? 268 THR   B OG1  1 
ATOM   1891 C  CG2  . THR   B 1 4   ? -24.208 1.344   42.081 1.00 49.81 ? 268 THR   B CG2  1 
ATOM   1892 N  N    . GLU   B 1 5   ? -22.451 0.146   39.056 1.00 39.20 ? 269 GLU   B N    1 
ATOM   1893 C  CA   . GLU   B 1 5   ? -22.149 -1.264  38.823 1.00 35.82 ? 269 GLU   B CA   1 
ATOM   1894 C  C    . GLU   B 1 5   ? -20.653 -1.548  38.743 1.00 33.65 ? 269 GLU   B C    1 
ATOM   1895 O  O    . GLU   B 1 5   ? -20.210 -2.595  39.204 1.00 34.66 ? 269 GLU   B O    1 
ATOM   1896 C  CB   . GLU   B 1 5   ? -22.836 -1.751  37.547 1.00 41.76 ? 269 GLU   B CB   1 
ATOM   1897 C  CG   . GLU   B 1 5   ? -24.345 -1.754  37.652 1.00 49.72 ? 269 GLU   B CG   1 
ATOM   1898 C  CD   . GLU   B 1 5   ? -25.023 -2.125  36.354 1.00 58.06 ? 269 GLU   B CD   1 
ATOM   1899 O  OE1  . GLU   B 1 5   ? -25.896 -3.022  36.364 1.00 68.38 ? 269 GLU   B OE1  1 
ATOM   1900 O  OE2  . GLU   B 1 5   ? -24.717 -1.505  35.326 1.00 51.93 ? 269 GLU   B OE2  1 
ATOM   1901 N  N    . ILE   B 1 6   ? -19.907 -0.636  38.104 1.00 30.85 ? 270 ILE   B N    1 
ATOM   1902 C  CA   . ILE   B 1 6   ? -18.440 -0.694  38.050 1.00 28.79 ? 270 ILE   B CA   1 
ATOM   1903 C  C    . ILE   B 1 6   ? -17.880 -0.666  39.443 1.00 31.33 ? 270 ILE   B C    1 
ATOM   1904 O  O    . ILE   B 1 6   ? -17.111 -1.541  39.824 1.00 30.10 ? 270 ILE   B O    1 
ATOM   1905 C  CB   . ILE   B 1 6   ? -17.893 0.454   37.222 1.00 31.12 ? 270 ILE   B CB   1 
ATOM   1906 C  CG1  . ILE   B 1 6   ? -18.516 0.386   35.818 1.00 29.61 ? 270 ILE   B CG1  1 
ATOM   1907 C  CG2  . ILE   B 1 6   ? -16.348 0.414   37.211 1.00 31.24 ? 270 ILE   B CG2  1 
ATOM   1908 C  CD1  . ILE   B 1 6   ? -18.156 1.527   34.955 1.00 31.91 ? 270 ILE   B CD1  1 
ATOM   1909 N  N    . GLU   B 1 7   ? -18.292 0.325   40.223 1.00 35.03 ? 271 GLU   B N    1 
ATOM   1910 C  CA   . GLU   B 1 7   ? -17.811 0.450   41.591 1.00 34.42 ? 271 GLU   B CA   1 
ATOM   1911 C  C    . GLU   B 1 7   ? -18.178 -0.769  42.413 1.00 36.22 ? 271 GLU   B C    1 
ATOM   1912 O  O    . GLU   B 1 7   ? -17.332 -1.265  43.144 1.00 31.85 ? 271 GLU   B O    1 
ATOM   1913 C  CB   . GLU   B 1 7   ? -18.341 1.727   42.245 1.00 44.63 ? 271 GLU   B CB   1 
ATOM   1914 C  CG   . GLU   B 1 7   ? -17.791 2.980   41.578 1.00 55.24 ? 271 GLU   B CG   1 
ATOM   1915 C  CD   . GLU   B 1 7   ? -17.633 4.150   42.536 1.00 72.11 ? 271 GLU   B CD   1 
ATOM   1916 O  OE1  . GLU   B 1 7   ? -18.568 4.971   42.636 1.00 72.36 ? 271 GLU   B OE1  1 
ATOM   1917 O  OE2  . GLU   B 1 7   ? -16.561 4.248   43.182 1.00 82.52 ? 271 GLU   B OE2  1 
ATOM   1918 N  N    . HIS   B 1 8   ? -19.393 -1.312  42.269 1.00 34.52 ? 272 HIS   B N    1 
ATOM   1919 C  CA   . HIS   B 1 8   ? -19.706 -2.537  43.006 1.00 39.13 ? 272 HIS   B CA   1 
ATOM   1920 C  C    . HIS   B 1 8   ? -18.829 -3.736  42.586 1.00 35.80 ? 272 HIS   B C    1 
ATOM   1921 O  O    . HIS   B 1 8   ? -18.478 -4.582  43.412 1.00 38.37 ? 272 HIS   B O    1 
ATOM   1922 C  CB   . HIS   B 1 8   ? -21.186 -2.894  42.859 1.00 43.15 ? 272 HIS   B CB   1 
ATOM   1923 C  CG   . HIS   B 1 8   ? -22.085 -2.141  43.794 1.00 52.92 ? 272 HIS   B CG   1 
ATOM   1924 N  ND1  . HIS   B 1 8   ? -22.276 -0.780  43.708 1.00 56.65 ? 272 HIS   B ND1  1 
ATOM   1925 C  CD2  . HIS   B 1 8   ? -22.852 -2.559  44.831 1.00 62.23 ? 272 HIS   B CD2  1 
ATOM   1926 C  CE1  . HIS   B 1 8   ? -23.122 -0.390  44.645 1.00 61.75 ? 272 HIS   B CE1  1 
ATOM   1927 N  NE2  . HIS   B 1 8   ? -23.480 -1.449  45.347 1.00 63.47 ? 272 HIS   B NE2  1 
ATOM   1928 N  N    . LEU   B 1 9   ? -18.463 -3.816  41.311 1.00 33.64 ? 273 LEU   B N    1 
ATOM   1929 C  CA   . LEU   B 1 9   ? -17.624 -4.903  40.851 1.00 29.39 ? 273 LEU   B CA   1 
ATOM   1930 C  C    . LEU   B 1 9   ? -16.226 -4.794  41.484 1.00 28.54 ? 273 LEU   B C    1 
ATOM   1931 O  O    . LEU   B 1 9   ? -15.683 -5.786  41.974 1.00 30.39 ? 273 LEU   B O    1 
ATOM   1932 C  CB   . LEU   B 1 9   ? -17.502 -4.913  39.325 1.00 26.03 ? 273 LEU   B CB   1 
ATOM   1933 C  CG   . LEU   B 1 9   ? -16.687 -6.072  38.732 1.00 29.89 ? 273 LEU   B CG   1 
ATOM   1934 C  CD1  . LEU   B 1 9   ? -17.181 -7.413  39.317 1.00 32.58 ? 273 LEU   B CD1  1 
ATOM   1935 C  CD2  . LEU   B 1 9   ? -16.718 -6.090  37.202 1.00 30.85 ? 273 LEU   B CD2  1 
ATOM   1936 N  N    . VAL   B 1 10  ? -15.672 -3.581  41.489 1.00 28.15 ? 274 VAL   B N    1 
ATOM   1937 C  CA   . VAL   B 1 10  ? -14.402 -3.355  42.157 1.00 28.28 ? 274 VAL   B CA   1 
ATOM   1938 C  C    . VAL   B 1 10  ? -14.492 -3.836  43.601 1.00 27.82 ? 274 VAL   B C    1 
ATOM   1939 O  O    . VAL   B 1 10  ? -13.628 -4.594  44.078 1.00 26.15 ? 274 VAL   B O    1 
ATOM   1940 C  CB   . VAL   B 1 10  ? -13.975 -1.910  42.133 1.00 28.72 ? 274 VAL   B CB   1 
ATOM   1941 C  CG1  . VAL   B 1 10  ? -12.752 -1.775  43.008 1.00 28.69 ? 274 VAL   B CG1  1 
ATOM   1942 C  CG2  . VAL   B 1 10  ? -13.672 -1.465  40.705 1.00 28.29 ? 274 VAL   B CG2  1 
ATOM   1943 N  N    . GLN   B 1 11  ? -15.545 -3.438  44.293 1.00 29.25 ? 275 GLN   B N    1 
ATOM   1944 C  CA   . GLN   B 1 11  ? -15.664 -3.799  45.691 1.00 31.79 ? 275 GLN   B CA   1 
ATOM   1945 C  C    . GLN   B 1 11  ? -15.815 -5.315  45.876 1.00 28.97 ? 275 GLN   B C    1 
ATOM   1946 O  O    . GLN   B 1 11  ? -15.296 -5.891  46.818 1.00 32.06 ? 275 GLN   B O    1 
ATOM   1947 C  CB   . GLN   B 1 11  ? -16.838 -3.045  46.323 1.00 34.66 ? 275 GLN   B CB   1 
ATOM   1948 C  CG   . GLN   B 1 11  ? -16.554 -1.568  46.484 1.00 44.71 ? 275 GLN   B CG   1 
ATOM   1949 C  CD   . GLN   B 1 11  ? -17.836 -0.742  46.633 1.00 59.21 ? 275 GLN   B CD   1 
ATOM   1950 O  OE1  . GLN   B 1 11  ? -18.862 -1.239  47.113 1.00 56.95 ? 275 GLN   B OE1  1 
ATOM   1951 N  NE2  . GLN   B 1 11  ? -17.781 0.522   46.209 1.00 68.30 ? 275 GLN   B NE2  1 
ATOM   1952 N  N    . SER   B 1 12  ? -16.534 -5.958  44.967 1.00 32.13 ? 276 SER   B N    1 
ATOM   1953 C  CA   . SER   B 1 12  ? -16.779 -7.386  45.077 1.00 29.67 ? 276 SER   B CA   1 
ATOM   1954 C  C    . SER   B 1 12  ? -15.487 -8.198  44.885 1.00 26.19 ? 276 SER   B C    1 
ATOM   1955 O  O    . SER   B 1 12  ? -15.256 -9.161  45.612 1.00 32.66 ? 276 SER   B O    1 
ATOM   1956 C  CB   . SER   B 1 12  ? -17.828 -7.815  44.052 1.00 37.93 ? 276 SER   B CB   1 
ATOM   1957 O  OG   . SER   B 1 12  ? -17.980 -9.212  44.062 1.00 45.73 ? 276 SER   B OG   1 
ATOM   1958 N  N    . VAL   B 1 13  ? -14.690 -7.817  43.898 1.00 30.36 ? 277 VAL   B N    1 
ATOM   1959 C  CA   . VAL   B 1 13  ? -13.424 -8.482  43.621 1.00 27.81 ? 277 VAL   B CA   1 
ATOM   1960 C  C    . VAL   B 1 13  ? -12.482 -8.315  44.797 1.00 29.69 ? 277 VAL   B C    1 
ATOM   1961 O  O    . VAL   B 1 13  ? -11.801 -9.271  45.217 1.00 25.22 ? 277 VAL   B O    1 
ATOM   1962 C  CB   . VAL   B 1 13  ? -12.794 -7.941  42.323 1.00 27.71 ? 277 VAL   B CB   1 
ATOM   1963 C  CG1  . VAL   B 1 13  ? -11.364 -8.477  42.132 1.00 28.63 ? 277 VAL   B CG1  1 
ATOM   1964 C  CG2  . VAL   B 1 13  ? -13.692 -8.301  41.159 1.00 29.14 ? 277 VAL   B CG2  1 
ATOM   1965 N  N    . CYS   B 1 14  ? -12.431 -7.113  45.348 1.00 29.25 ? 278 CYS   B N    1 
ATOM   1966 C  CA   . CYS   B 1 14  ? -11.501 -6.863  46.465 1.00 27.95 ? 278 CYS   B CA   1 
ATOM   1967 C  C    . CYS   B 1 14  ? -11.907 -7.641  47.703 1.00 27.44 ? 278 CYS   B C    1 
ATOM   1968 O  O    . CYS   B 1 14  ? -11.042 -8.165  48.427 1.00 28.73 ? 278 CYS   B O    1 
ATOM   1969 C  CB   . CYS   B 1 14  ? -11.425 -5.359  46.778 1.00 29.49 ? 278 CYS   B CB   1 
ATOM   1970 S  SG   . CYS   B 1 14  ? -10.636 -4.389  45.421 1.00 32.81 ? 278 CYS   B SG   1 
ATOM   1971 N  N    . LYS   B 1 15  ? -13.209 -7.744  47.950 1.00 26.67 ? 279 LYS   B N    1 
ATOM   1972 C  CA   . LYS   B 1 15  ? -13.705 -8.523  49.059 1.00 30.96 ? 279 LYS   B CA   1 
ATOM   1973 C  C    . LYS   B 1 15  ? -13.330 -9.987  48.871 1.00 32.34 ? 279 LYS   B C    1 
ATOM   1974 O  O    . LYS   B 1 15  ? -12.924 -10.655 49.824 1.00 30.61 ? 279 LYS   B O    1 
ATOM   1975 C  CB   . LYS   B 1 15  ? -15.219 -8.382  49.202 1.00 36.07 ? 279 LYS   B CB   1 
ATOM   1976 C  CG   . LYS   B 1 15  ? -15.752 -9.085  50.455 1.00 44.73 ? 279 LYS   B CG   1 
ATOM   1977 C  CD   . LYS   B 1 15  ? -17.020 -8.428  50.968 1.00 52.55 ? 279 LYS   B CD   1 
ATOM   1978 C  CE   . LYS   B 1 15  ? -17.171 -8.641  52.476 1.00 62.78 ? 279 LYS   B CE   1 
ATOM   1979 N  NZ   . LYS   B 1 15  ? -16.145 -7.876  53.261 1.00 66.41 ? 279 LYS   B NZ   1 
ATOM   1980 N  N    . SER   B 1 16  ? -13.511 -10.490 47.658 1.00 28.51 ? 280 SER   B N    1 
ATOM   1981 C  CA   . SER   B 1 16  ? -13.289 -11.912 47.401 1.00 31.13 ? 280 SER   B CA   1 
ATOM   1982 C  C    . SER   B 1 16  ? -11.811 -12.191 47.676 1.00 27.53 ? 280 SER   B C    1 
ATOM   1983 O  O    . SER   B 1 16  ? -11.437 -13.212 48.245 1.00 28.61 ? 280 SER   B O    1 
ATOM   1984 C  CB   . SER   B 1 16  ? -13.651 -12.245 45.957 1.00 28.21 ? 280 SER   B CB   1 
ATOM   1985 O  OG   . SER   B 1 16  ? -15.060 -12.031 45.742 1.00 37.81 ? 280 SER   B OG   1 
ATOM   1986 N  N    . TYR   B 1 17  ? -10.978 -11.263 47.249 1.00 26.90 ? 281 TYR   B N    1 
ATOM   1987 C  CA   . TYR   B 1 17  ? -9.550  -11.344 47.484 1.00 24.32 ? 281 TYR   B CA   1 
ATOM   1988 C  C    . TYR   B 1 17  ? -9.215  -11.319 48.997 1.00 25.92 ? 281 TYR   B C    1 
ATOM   1989 O  O    . TYR   B 1 17  ? -8.490  -12.195 49.502 1.00 29.61 ? 281 TYR   B O    1 
ATOM   1990 C  CB   . TYR   B 1 17  ? -8.832  -10.221 46.734 1.00 25.37 ? 281 TYR   B CB   1 
ATOM   1991 C  CG   . TYR   B 1 17  ? -7.384  -10.225 47.088 1.00 25.67 ? 281 TYR   B CG   1 
ATOM   1992 C  CD1  . TYR   B 1 17  ? -6.540  -11.174 46.555 1.00 28.81 ? 281 TYR   B CD1  1 
ATOM   1993 C  CD2  . TYR   B 1 17  ? -6.889  -9.322  47.995 1.00 31.16 ? 281 TYR   B CD2  1 
ATOM   1994 C  CE1  . TYR   B 1 17  ? -5.196  -11.216 46.920 1.00 34.00 ? 281 TYR   B CE1  1 
ATOM   1995 C  CE2  . TYR   B 1 17  ? -5.586  -9.347  48.348 1.00 32.25 ? 281 TYR   B CE2  1 
ATOM   1996 C  CZ   . TYR   B 1 17  ? -4.752  -10.297 47.810 1.00 34.98 ? 281 TYR   B CZ   1 
ATOM   1997 O  OH   . TYR   B 1 17  ? -3.436  -10.319 48.178 1.00 50.51 ? 281 TYR   B OH   1 
ATOM   1998 N  N    . ARG   B 1 18  ? -9.736  -10.332 49.733 1.00 25.86 ? 282 ARG   B N    1 
ATOM   1999 C  CA   . ARG   B 1 18  ? -9.548  -10.325 51.181 1.00 28.69 ? 282 ARG   B CA   1 
ATOM   2000 C  C    . ARG   B 1 18  ? -9.948  -11.626 51.866 1.00 27.88 ? 282 ARG   B C    1 
ATOM   2001 O  O    . ARG   B 1 18  ? -9.297  -12.052 52.817 1.00 33.38 ? 282 ARG   B O    1 
ATOM   2002 C  CB   . ARG   B 1 18  ? -10.322 -9.177  51.824 1.00 32.69 ? 282 ARG   B CB   1 
ATOM   2003 C  CG   . ARG   B 1 18  ? -9.820  -7.813  51.375 1.00 36.12 ? 282 ARG   B CG   1 
ATOM   2004 C  CD   . ARG   B 1 18  ? -10.249 -6.725  52.348 1.00 42.10 ? 282 ARG   B CD   1 
ATOM   2005 N  NE   . ARG   B 1 18  ? -11.692 -6.537  52.326 1.00 47.16 ? 282 ARG   B NE   1 
ATOM   2006 C  CZ   . ARG   B 1 18  ? -12.332 -5.835  51.395 1.00 43.34 ? 282 ARG   B CZ   1 
ATOM   2007 N  NH1  . ARG   B 1 18  ? -13.647 -5.726  51.444 1.00 46.19 ? 282 ARG   B NH1  1 
ATOM   2008 N  NH2  . ARG   B 1 18  ? -11.649 -5.269  50.409 1.00 41.41 ? 282 ARG   B NH2  1 
ATOM   2009 N  N    . GLU   B 1 19  ? -11.023 -12.246 51.379 1.00 31.93 ? 283 GLU   B N    1 
ATOM   2010 C  CA   . GLU   B 1 19  ? -11.607 -13.426 52.006 1.00 30.32 ? 283 GLU   B CA   1 
ATOM   2011 C  C    . GLU   B 1 19  ? -10.732 -14.668 51.773 1.00 28.75 ? 283 GLU   B C    1 
ATOM   2012 O  O    . GLU   B 1 19  ? -10.906 -15.669 52.460 1.00 32.59 ? 283 GLU   B O    1 
ATOM   2013 C  CB   . GLU   B 1 19  ? -13.033 -13.660 51.473 1.00 33.24 ? 283 GLU   B CB   1 
ATOM   2014 C  CG   . GLU   B 1 19  ? -14.086 -12.708 52.065 1.00 31.37 ? 283 GLU   B CG   1 
ATOM   2015 C  CD   . GLU   B 1 19  ? -15.399 -12.759 51.345 1.00 42.77 ? 283 GLU   B CD   1 
ATOM   2016 O  OE1  . GLU   B 1 19  ? -15.465 -13.285 50.209 1.00 43.29 ? 283 GLU   B OE1  1 
ATOM   2017 O  OE2  . GLU   B 1 19  ? -16.372 -12.229 51.912 1.00 45.78 ? 283 GLU   B OE2  1 
ATOM   2018 N  N    . THR   B 1 20  ? -9.804  -14.572 50.820 1.00 26.16 ? 284 THR   B N    1 
ATOM   2019 C  CA   . THR   B 1 20  ? -8.995  -15.728 50.410 1.00 26.70 ? 284 THR   B CA   1 
ATOM   2020 C  C    . THR   B 1 20  ? -7.483  -15.454 50.387 1.00 29.05 ? 284 THR   B C    1 
ATOM   2021 O  O    . THR   B 1 20  ? -6.741  -16.223 49.775 1.00 28.50 ? 284 THR   B O    1 
ATOM   2022 C  CB   . THR   B 1 20  ? -9.428  -16.216 49.016 1.00 22.21 ? 284 THR   B CB   1 
ATOM   2023 O  OG1  . THR   B 1 20  ? -9.250  -15.164 48.073 1.00 24.57 ? 284 THR   B OG1  1 
ATOM   2024 C  CG2  . THR   B 1 20  ? -10.939 -16.604 49.014 1.00 24.18 ? 284 THR   B CG2  1 
ATOM   2025 N  N    . CYS   B 1 21  ? -6.997  -14.377 50.977 1.00 34.77 ? 285 CYS   B N    1 
ATOM   2026 C  CA   . CYS   B 1 21  ? -5.568  -14.018 50.819 1.00 30.91 ? 285 CYS   B CA   1 
ATOM   2027 C  C    . CYS   B 1 21  ? -4.469  -14.800 51.579 1.00 37.99 ? 285 CYS   B C    1 
ATOM   2028 O  O    . CYS   B 1 21  ? -3.318  -14.664 51.233 1.00 41.07 ? 285 CYS   B O    1 
ATOM   2029 C  CB   . CYS   B 1 21  ? -5.357  -12.490 51.035 1.00 43.29 ? 285 CYS   B CB   1 
ATOM   2030 S  SG   . CYS   B 1 21  ? -5.586  -11.879 52.671 1.00 48.08 ? 285 CYS   B SG   1 
ATOM   2031 N  N    . GLN   B 1 22  ? -4.802  -15.569 52.590 1.00 37.28 ? 286 GLN   B N    1 
ATOM   2032 C  CA   . GLN   B 1 22  ? -3.826  -16.397 53.336 1.00 35.87 ? 286 GLN   B CA   1 
ATOM   2033 C  C    . GLN   B 1 22  ? -3.139  -15.664 54.483 1.00 40.43 ? 286 GLN   B C    1 
ATOM   2034 O  O    . GLN   B 1 22  ? -3.265  -16.080 55.626 1.00 43.86 ? 286 GLN   B O    1 
ATOM   2035 C  CB   . GLN   B 1 22  ? -2.769  -17.043 52.415 1.00 42.14 ? 286 GLN   B CB   1 
ATOM   2036 C  CG   . GLN   B 1 22  ? -3.191  -18.366 51.784 1.00 45.13 ? 286 GLN   B CG   1 
ATOM   2037 C  CD   . GLN   B 1 22  ? -2.047  -19.093 51.081 1.00 47.09 ? 286 GLN   B CD   1 
ATOM   2038 O  OE1  . GLN   B 1 22  ? -1.623  -18.705 49.997 1.00 48.18 ? 286 GLN   B OE1  1 
ATOM   2039 N  NE2  . GLN   B 1 22  ? -1.555  -20.155 51.698 1.00 41.06 ? 286 GLN   B NE2  1 
ATOM   2040 N  N    . LEU   B 1 23  ? -2.399  -14.609 54.191 1.00 30.95 ? 287 LEU   B N    1 
ATOM   2041 C  CA   . LEU   B 1 23  ? -1.760  -13.805 55.205 1.00 29.42 ? 287 LEU   B CA   1 
ATOM   2042 C  C    . LEU   B 1 23  ? -2.010  -12.339 54.874 1.00 30.63 ? 287 LEU   B C    1 
ATOM   2043 O  O    . LEU   B 1 23  ? -2.238  -12.017 53.737 1.00 38.04 ? 287 LEU   B O    1 
ATOM   2044 C  CB   . LEU   B 1 23  ? -0.273  -14.090 55.244 1.00 27.64 ? 287 LEU   B CB   1 
ATOM   2045 C  CG   . LEU   B 1 23  ? 0.162   -15.496 55.644 1.00 34.87 ? 287 LEU   B CG   1 
ATOM   2046 C  CD1  . LEU   B 1 23  ? 1.626   -15.704 55.314 1.00 34.43 ? 287 LEU   B CD1  1 
ATOM   2047 C  CD2  . LEU   B 1 23  ? -0.092  -15.717 57.121 1.00 41.76 ? 287 LEU   B CD2  1 
ATOM   2048 N  N    . ARG   B 1 24  ? -1.967  -11.470 55.869 1.00 29.88 ? 288 ARG   B N    1 
ATOM   2049 C  CA   . ARG   B 1 24  ? -2.177  -10.040 55.660 1.00 32.79 ? 288 ARG   B CA   1 
ATOM   2050 C  C    . ARG   B 1 24  ? -0.909  -9.360  55.209 1.00 28.94 ? 288 ARG   B C    1 
ATOM   2051 O  O    . ARG   B 1 24  ? 0.169   -9.700  55.681 1.00 30.51 ? 288 ARG   B O    1 
ATOM   2052 C  CB   . ARG   B 1 24  ? -2.680  -9.385  56.954 1.00 39.76 ? 288 ARG   B CB   1 
ATOM   2053 C  CG   . ARG   B 1 24  ? -4.156  -9.627  57.222 1.00 50.94 ? 288 ARG   B CG   1 
ATOM   2054 C  CD   . ARG   B 1 24  ? -4.501  -9.617  58.708 1.00 60.93 ? 288 ARG   B CD   1 
ATOM   2055 N  NE   . ARG   B 1 24  ? -3.775  -8.604  59.471 1.00 72.07 ? 288 ARG   B NE   1 
ATOM   2056 C  CZ   . ARG   B 1 24  ? -3.825  -8.493  60.798 1.00 78.79 ? 288 ARG   B CZ   1 
ATOM   2057 N  NH1  . ARG   B 1 24  ? -4.568  -9.334  61.509 1.00 80.95 ? 288 ARG   B NH1  1 
ATOM   2058 N  NH2  . ARG   B 1 24  ? -3.130  -7.546  61.415 1.00 79.42 ? 288 ARG   B NH2  1 
ATOM   2059 N  N    . LEU   B 1 25  ? -1.030  -8.364  54.338 1.00 31.71 ? 289 LEU   B N    1 
ATOM   2060 C  CA   . LEU   B 1 25  ? 0.148   -7.692  53.819 1.00 29.32 ? 289 LEU   B CA   1 
ATOM   2061 C  C    . LEU   B 1 25  ? 0.911   -7.027  54.956 1.00 29.99 ? 289 LEU   B C    1 
ATOM   2062 O  O    . LEU   B 1 25  ? 2.145   -7.099  55.001 1.00 30.13 ? 289 LEU   B O    1 
ATOM   2063 C  CB   . LEU   B 1 25  ? -0.231  -6.666  52.764 1.00 30.37 ? 289 LEU   B CB   1 
ATOM   2064 C  CG   . LEU   B 1 25  ? 0.946   -5.872  52.200 1.00 30.11 ? 289 LEU   B CG   1 
ATOM   2065 C  CD1  . LEU   B 1 25  ? 1.943   -6.816  51.573 1.00 30.13 ? 289 LEU   B CD1  1 
ATOM   2066 C  CD2  . LEU   B 1 25  ? 0.422   -4.814  51.211 1.00 33.10 ? 289 LEU   B CD2  1 
ATOM   2067 N  N    . GLU   B 1 26  ? 0.209   -6.368  55.862 1.00 30.87 ? 290 GLU   B N    1 
ATOM   2068 C  CA   . GLU   B 1 26  ? 0.871   -5.730  56.995 1.00 35.41 ? 290 GLU   B CA   1 
ATOM   2069 C  C    . GLU   B 1 26  ? 1.772   -6.704  57.731 1.00 36.19 ? 290 GLU   B C    1 
ATOM   2070 O  O    . GLU   B 1 26  ? 2.890   -6.366  58.102 1.00 37.66 ? 290 GLU   B O    1 
ATOM   2071 C  CB   . GLU   B 1 26  ? -0.134  -5.176  58.002 1.00 44.87 ? 290 GLU   B CB   1 
ATOM   2072 C  CG   . GLU   B 1 26  ? -0.706  -3.843  57.696 1.00 57.37 ? 290 GLU   B CG   1 
ATOM   2073 C  CD   . GLU   B 1 26  ? -1.178  -3.159  58.967 1.00 66.12 ? 290 GLU   B CD   1 
ATOM   2074 O  OE1  . GLU   B 1 26  ? -0.510  -3.361  60.009 1.00 65.98 ? 290 GLU   B OE1  1 
ATOM   2075 O  OE2  . GLU   B 1 26  ? -2.201  -2.435  58.930 1.00 74.16 ? 290 GLU   B OE2  1 
ATOM   2076 N  N    . ASP   B 1 27  ? 1.257   -7.901  57.977 1.00 34.06 ? 291 ASP   B N    1 
ATOM   2077 C  CA   . ASP   B 1 27  ? 1.990   -8.873  58.771 1.00 33.90 ? 291 ASP   B CA   1 
ATOM   2078 C  C    . ASP   B 1 27  ? 3.217   -9.341  58.028 1.00 34.10 ? 291 ASP   B C    1 
ATOM   2079 O  O    . ASP   B 1 27  ? 4.283   -9.475  58.608 1.00 33.76 ? 291 ASP   B O    1 
ATOM   2080 C  CB   . ASP   B 1 27  ? 1.120   -10.076 59.106 1.00 36.52 ? 291 ASP   B CB   1 
ATOM   2081 C  CG   . ASP   B 1 27  ? 0.217   -9.830  60.287 1.00 52.85 ? 291 ASP   B CG   1 
ATOM   2082 O  OD1  . ASP   B 1 27  ? 0.653   -9.171  61.255 1.00 58.17 ? 291 ASP   B OD1  1 
ATOM   2083 O  OD2  . ASP   B 1 27  ? -0.934  -10.300 60.243 1.00 57.64 ? 291 ASP   B OD2  1 
ATOM   2084 N  N    . LEU   B 1 28  ? 3.046   -9.607  56.740 1.00 27.28 ? 292 LEU   B N    1 
ATOM   2085 C  CA   . LEU   B 1 28  ? 4.166   -9.989  55.905 1.00 26.85 ? 292 LEU   B CA   1 
ATOM   2086 C  C    . LEU   B 1 28  ? 5.264   -8.921  55.964 1.00 27.82 ? 292 LEU   B C    1 
ATOM   2087 O  O    . LEU   B 1 28  ? 6.446   -9.257  56.077 1.00 28.70 ? 292 LEU   B O    1 
ATOM   2088 C  CB   . LEU   B 1 28  ? 3.709   -10.220 54.466 1.00 25.40 ? 292 LEU   B CB   1 
ATOM   2089 C  CG   . LEU   B 1 28  ? 3.063   -11.587 54.266 1.00 25.48 ? 292 LEU   B CG   1 
ATOM   2090 C  CD1  . LEU   B 1 28  ? 2.330   -11.655 52.901 1.00 27.34 ? 292 LEU   B CD1  1 
ATOM   2091 C  CD2  . LEU   B 1 28  ? 4.080   -12.705 54.376 1.00 25.36 ? 292 LEU   B CD2  1 
ATOM   2092 N  N    . LEU   B 1 29  ? 4.873   -7.647  55.883 1.00 31.35 ? 293 LEU   B N    1 
ATOM   2093 C  CA   . LEU   B 1 29  ? 5.859   -6.565  55.836 1.00 26.33 ? 293 LEU   B CA   1 
ATOM   2094 C  C    . LEU   B 1 29  ? 6.568   -6.414  57.168 1.00 31.56 ? 293 LEU   B C    1 
ATOM   2095 O  O    . LEU   B 1 29  ? 7.788   -6.212  57.221 1.00 31.26 ? 293 LEU   B O    1 
ATOM   2096 C  CB   . LEU   B 1 29  ? 5.190   -5.241  55.452 1.00 26.73 ? 293 LEU   B CB   1 
ATOM   2097 C  CG   . LEU   B 1 29  ? 4.715   -5.229  54.002 1.00 28.71 ? 293 LEU   B CG   1 
ATOM   2098 C  CD1  . LEU   B 1 29  ? 3.979   -3.908  53.695 1.00 29.46 ? 293 LEU   B CD1  1 
ATOM   2099 C  CD2  . LEU   B 1 29  ? 5.869   -5.403  53.066 1.00 32.21 ? 293 LEU   B CD2  1 
ATOM   2100 N  N    . ARG   B 1 30  ? 5.809   -6.526  58.251 1.00 31.93 ? 294 ARG   B N    1 
ATOM   2101 C  CA   . ARG   B 1 30  ? 6.388   -6.392  59.580 1.00 34.33 ? 294 ARG   B CA   1 
ATOM   2102 C  C    . ARG   B 1 30  ? 7.365   -7.527  59.879 1.00 38.03 ? 294 ARG   B C    1 
ATOM   2103 O  O    . ARG   B 1 30  ? 8.348   -7.327  60.593 1.00 36.34 ? 294 ARG   B O    1 
ATOM   2104 C  CB   . ARG   B 1 30  ? 5.302   -6.369  60.643 1.00 38.01 ? 294 ARG   B CB   1 
ATOM   2105 C  CG   . ARG   B 1 30  ? 4.495   -5.069  60.693 1.00 34.51 ? 294 ARG   B CG   1 
ATOM   2106 C  CD   . ARG   B 1 30  ? 3.481   -5.194  61.806 1.00 37.69 ? 294 ARG   B CD   1 
ATOM   2107 N  NE   . ARG   B 1 30  ? 2.620   -4.023  61.953 1.00 40.02 ? 294 ARG   B NE   1 
ATOM   2108 C  CZ   . ARG   B 1 30  ? 2.863   -2.990  62.753 1.00 43.89 ? 294 ARG   B CZ   1 
ATOM   2109 N  NH1  . ARG   B 1 30  ? 3.972   -2.938  63.489 1.00 48.22 ? 294 ARG   B NH1  1 
ATOM   2110 N  NH2  . ARG   B 1 30  ? 1.996   -1.992  62.817 1.00 46.59 ? 294 ARG   B NH2  1 
ATOM   2111 N  N    . GLN   B 1 31  ? 7.082   -8.708  59.338 1.00 33.22 ? 295 GLN   B N    1 
ATOM   2112 C  CA   . GLN   B 1 31  ? 7.922   -9.887  59.593 1.00 32.37 ? 295 GLN   B CA   1 
ATOM   2113 C  C    . GLN   B 1 31  ? 9.237   -9.880  58.810 1.00 33.46 ? 295 GLN   B C    1 
ATOM   2114 O  O    . GLN   B 1 31  ? 10.021  -10.818 58.937 1.00 31.84 ? 295 GLN   B O    1 
ATOM   2115 C  CB   . GLN   B 1 31  ? 7.151   -11.170 59.274 1.00 33.81 ? 295 GLN   B CB   1 
ATOM   2116 C  CG   . GLN   B 1 31  ? 6.049   -11.480 60.250 1.00 42.24 ? 295 GLN   B CG   1 
ATOM   2117 C  CD   . GLN   B 1 31  ? 6.363   -12.661 61.136 1.00 54.78 ? 295 GLN   B CD   1 
ATOM   2118 O  OE1  . GLN   B 1 31  ? 7.302   -13.421 60.888 1.00 56.07 ? 295 GLN   B OE1  1 
ATOM   2119 N  NE2  . GLN   B 1 31  ? 5.586   -12.813 62.196 1.00 64.23 ? 295 GLN   B NE2  1 
ATOM   2120 N  N    . ARG   B 1 32  ? 9.481   -8.828  58.026 1.00 32.22 ? 296 ARG   B N    1 
ATOM   2121 C  CA   . ARG   B 1 32  ? 10.638  -8.769  57.142 1.00 29.53 ? 296 ARG   B CA   1 
ATOM   2122 C  C    . ARG   B 1 32  ? 11.926  -8.840  57.949 1.00 32.38 ? 296 ARG   B C    1 
ATOM   2123 O  O    . ARG   B 1 32  ? 12.914  -9.325  57.432 1.00 30.85 ? 296 ARG   B O    1 
ATOM   2124 C  CB   . ARG   B 1 32  ? 10.619  -7.508  56.270 1.00 27.21 ? 296 ARG   B CB   1 
ATOM   2125 C  CG   . ARG   B 1 32  ? 9.669   -7.633  55.066 1.00 26.51 ? 296 ARG   B CG   1 
ATOM   2126 C  CD   . ARG   B 1 32  ? 9.696   -6.384  54.145 1.00 32.03 ? 296 ARG   B CD   1 
ATOM   2127 N  NE   . ARG   B 1 32  ? 9.061   -6.684  52.852 1.00 32.60 ? 296 ARG   B NE   1 
ATOM   2128 C  CZ   . ARG   B 1 32  ? 9.073   -5.861  51.804 1.00 32.95 ? 296 ARG   B CZ   1 
ATOM   2129 N  NH1  . ARG   B 1 32  ? 9.694   -4.691  51.901 1.00 32.77 ? 296 ARG   B NH1  1 
ATOM   2130 N  NH2  . ARG   B 1 32  ? 8.493   -6.208  50.659 1.00 29.62 ? 296 ARG   B NH2  1 
ATOM   2131 N  N    . SER   B 1 33  ? 11.892  -8.431  59.222 1.00 34.73 ? 297 SER   B N    1 
ATOM   2132 C  CA   . SER   B 1 33  ? 13.098  -8.494  60.062 1.00 37.06 ? 297 SER   B CA   1 
ATOM   2133 C  C    . SER   B 1 33  ? 13.377  -9.885  60.667 1.00 33.58 ? 297 SER   B C    1 
ATOM   2134 O  O    . SER   B 1 33  ? 14.440  -10.109 61.272 1.00 36.18 ? 297 SER   B O    1 
ATOM   2135 C  CB   . SER   B 1 33  ? 13.019  -7.458  61.191 1.00 41.02 ? 297 SER   B CB   1 
ATOM   2136 O  OG   . SER   B 1 33  ? 11.904  -7.726  62.031 1.00 45.68 ? 297 SER   B OG   1 
ATOM   2137 N  N    . ASN   B 1 34  ? 12.422  -10.800 60.513 1.00 31.66 ? 298 ASN   B N    1 
ATOM   2138 C  CA   . ASN   B 1 34  ? 12.550  -12.199 60.925 1.00 33.22 ? 298 ASN   B CA   1 
ATOM   2139 C  C    . ASN   B 1 34  ? 13.176  -13.035 59.825 1.00 31.17 ? 298 ASN   B C    1 
ATOM   2140 O  O    . ASN   B 1 34  ? 12.473  -13.509 58.967 1.00 32.15 ? 298 ASN   B O    1 
ATOM   2141 C  CB   . ASN   B 1 34  ? 11.175  -12.762 61.289 1.00 39.75 ? 298 ASN   B CB   1 
ATOM   2142 C  CG   . ASN   B 1 34  ? 11.253  -13.952 62.236 1.00 48.78 ? 298 ASN   B CG   1 
ATOM   2143 O  OD1  . ASN   B 1 34  ? 12.334  -14.381 62.620 1.00 50.05 ? 298 ASN   B OD1  1 
ATOM   2144 N  ND2  . ASN   B 1 34  ? 10.094  -14.473 62.635 1.00 48.46 ? 298 ASN   B ND2  1 
ATOM   2145 N  N    . ILE   B 1 35  ? 14.503  -13.209 59.866 1.00 28.66 ? 299 ILE   B N    1 
ATOM   2146 C  CA   . ILE   B 1 35  ? 15.241  -13.852 58.778 1.00 28.37 ? 299 ILE   B CA   1 
ATOM   2147 C  C    . ILE   B 1 35  ? 15.932  -15.099 59.293 1.00 24.96 ? 299 ILE   B C    1 
ATOM   2148 O  O    . ILE   B 1 35  ? 16.455  -15.097 60.414 1.00 27.41 ? 299 ILE   B O    1 
ATOM   2149 C  CB   . ILE   B 1 35  ? 16.251  -12.850 58.185 1.00 29.95 ? 299 ILE   B CB   1 
ATOM   2150 C  CG1  . ILE   B 1 35  ? 15.497  -11.646 57.609 1.00 33.94 ? 299 ILE   B CG1  1 
ATOM   2151 C  CG2  . ILE   B 1 35  ? 17.154  -13.526 57.185 1.00 30.36 ? 299 ILE   B CG2  1 
ATOM   2152 C  CD1  . ILE   B 1 35  ? 16.333  -10.410 57.445 1.00 34.84 ? 299 ILE   B CD1  1 
ATOM   2153 N  N    . PHE   B 1 36  ? 15.931  -16.161 58.496 1.00 26.55 ? 300 PHE   B N    1 
ATOM   2154 C  CA   . PHE   B 1 36  ? 16.609  -17.389 58.896 1.00 26.56 ? 300 PHE   B CA   1 
ATOM   2155 C  C    . PHE   B 1 36  ? 18.065  -17.164 59.146 1.00 30.54 ? 300 PHE   B C    1 
ATOM   2156 O  O    . PHE   B 1 36  ? 18.757  -16.553 58.337 1.00 31.66 ? 300 PHE   B O    1 
ATOM   2157 C  CB   . PHE   B 1 36  ? 16.482  -18.456 57.833 1.00 26.10 ? 300 PHE   B CB   1 
ATOM   2158 C  CG   . PHE   B 1 36  ? 15.083  -19.050 57.727 1.00 24.42 ? 300 PHE   B CG   1 
ATOM   2159 C  CD1  . PHE   B 1 36  ? 14.581  -19.850 58.758 1.00 24.67 ? 300 PHE   B CD1  1 
ATOM   2160 C  CD2  . PHE   B 1 36  ? 14.301  -18.823 56.599 1.00 25.35 ? 300 PHE   B CD2  1 
ATOM   2161 C  CE1  . PHE   B 1 36  ? 13.299  -20.436 58.644 1.00 23.44 ? 300 PHE   B CE1  1 
ATOM   2162 C  CE2  . PHE   B 1 36  ? 13.038  -19.384 56.457 1.00 22.71 ? 300 PHE   B CE2  1 
ATOM   2163 C  CZ   . PHE   B 1 36  ? 12.501  -20.188 57.482 1.00 23.56 ? 300 PHE   B CZ   1 
ATOM   2164 N  N    . SER   B 1 37  ? 18.521  -17.704 60.254 1.00 26.28 ? 301 SER   B N    1 
ATOM   2165 C  CA   . SER   B 1 37  ? 19.930  -17.604 60.626 1.00 27.90 ? 301 SER   B CA   1 
ATOM   2166 C  C    . SER   B 1 37  ? 20.777  -18.487 59.706 1.00 29.76 ? 301 SER   B C    1 
ATOM   2167 O  O    . SER   B 1 37  ? 20.237  -19.354 59.029 1.00 30.25 ? 301 SER   B O    1 
ATOM   2168 C  CB   . SER   B 1 37  ? 20.086  -18.034 62.063 1.00 35.53 ? 301 SER   B CB   1 
ATOM   2169 O  OG   . SER   B 1 37  ? 19.913  -19.436 62.172 1.00 35.78 ? 301 SER   B OG   1 
ATOM   2170 N  N    . ARG   B 1 38  ? 22.102  -18.287 59.697 1.00 33.45 ? 302 ARG   B N    1 
ATOM   2171 C  CA   . ARG   B 1 38  ? 22.981  -19.115 58.855 1.00 34.57 ? 302 ARG   B CA   1 
ATOM   2172 C  C    . ARG   B 1 38  ? 22.838  -20.601 59.211 1.00 34.13 ? 302 ARG   B C    1 
ATOM   2173 O  O    . ARG   B 1 38  ? 22.849  -21.465 58.330 1.00 35.55 ? 302 ARG   B O    1 
ATOM   2174 C  CB   . ARG   B 1 38  ? 24.461  -18.675 58.978 1.00 38.35 ? 302 ARG   B CB   1 
ATOM   2175 C  CG   . ARG   B 1 38  ? 25.388  -19.401 57.979 1.00 51.69 ? 302 ARG   B CG   1 
ATOM   2176 C  CD   . ARG   B 1 38  ? 24.843  -19.218 56.544 1.00 64.18 ? 302 ARG   B CD   1 
ATOM   2177 N  NE   . ARG   B 1 38  ? 25.336  -20.145 55.509 1.00 70.62 ? 302 ARG   B NE   1 
ATOM   2178 C  CZ   . ARG   B 1 38  ? 24.655  -21.203 55.063 1.00 68.90 ? 302 ARG   B CZ   1 
ATOM   2179 N  NH1  . ARG   B 1 38  ? 23.484  -21.497 55.596 1.00 70.34 ? 302 ARG   B NH1  1 
ATOM   2180 N  NH2  . ARG   B 1 38  ? 25.144  -21.984 54.103 1.00 66.30 ? 302 ARG   B NH2  1 
ATOM   2181 N  N    . GLU   B 1 39  ? 22.652  -20.885 60.497 1.00 30.88 ? 303 GLU   B N    1 
ATOM   2182 C  CA   . GLU   B 1 39  ? 22.494  -22.256 60.927 1.00 34.55 ? 303 GLU   B CA   1 
ATOM   2183 C  C    . GLU   B 1 39  ? 21.163  -22.834 60.434 1.00 28.74 ? 303 GLU   B C    1 
ATOM   2184 O  O    . GLU   B 1 39  ? 21.090  -24.005 60.066 1.00 30.20 ? 303 GLU   B O    1 
ATOM   2185 C  CB   . GLU   B 1 39  ? 22.551  -22.363 62.429 1.00 43.15 ? 303 GLU   B CB   1 
ATOM   2186 C  CG   . GLU   B 1 39  ? 22.483  -23.788 62.884 1.00 59.11 ? 303 GLU   B CG   1 
ATOM   2187 C  CD   . GLU   B 1 39  ? 21.398  -24.017 63.905 1.00 74.66 ? 303 GLU   B CD   1 
ATOM   2188 O  OE1  . GLU   B 1 39  ? 20.942  -25.178 64.029 1.00 81.00 ? 303 GLU   B OE1  1 
ATOM   2189 O  OE2  . GLU   B 1 39  ? 21.007  -23.039 64.582 1.00 79.05 ? 303 GLU   B OE2  1 
ATOM   2190 N  N    . GLU   B 1 40  ? 20.112  -22.025 60.449 1.00 31.96 ? 304 GLU   B N    1 
ATOM   2191 C  CA   . GLU   B 1 40  ? 18.827  -22.508 59.944 1.00 26.02 ? 304 GLU   B CA   1 
ATOM   2192 C  C    . GLU   B 1 40  ? 18.903  -22.772 58.449 1.00 26.37 ? 304 GLU   B C    1 
ATOM   2193 O  O    . GLU   B 1 40  ? 18.302  -23.716 57.950 1.00 25.85 ? 304 GLU   B O    1 
ATOM   2194 C  CB   . GLU   B 1 40  ? 17.706  -21.504 60.238 1.00 26.47 ? 304 GLU   B CB   1 
ATOM   2195 C  CG   . GLU   B 1 40  ? 17.310  -21.554 61.692 1.00 35.06 ? 304 GLU   B CG   1 
ATOM   2196 C  CD   . GLU   B 1 40  ? 16.451  -20.389 62.122 1.00 44.34 ? 304 GLU   B CD   1 
ATOM   2197 O  OE1  . GLU   B 1 40  ? 15.481  -20.630 62.868 1.00 51.45 ? 304 GLU   B OE1  1 
ATOM   2198 O  OE2  . GLU   B 1 40  ? 16.753  -19.243 61.730 1.00 37.95 ? 304 GLU   B OE2  1 
ATOM   2199 N  N    . VAL   B 1 41  ? 19.617  -21.913 57.726 1.00 25.60 ? 305 VAL   B N    1 
ATOM   2200 C  CA   . VAL   B 1 41  ? 19.713  -22.053 56.292 1.00 26.42 ? 305 VAL   B CA   1 
ATOM   2201 C  C    . VAL   B 1 41  ? 20.450  -23.350 56.000 1.00 25.51 ? 305 VAL   B C    1 
ATOM   2202 O  O    . VAL   B 1 41  ? 20.063  -24.092 55.079 1.00 25.56 ? 305 VAL   B O    1 
ATOM   2203 C  CB   . VAL   B 1 41  ? 20.421  -20.864 55.646 1.00 24.73 ? 305 VAL   B CB   1 
ATOM   2204 C  CG1  . VAL   B 1 41  ? 20.731  -21.168 54.163 1.00 24.87 ? 305 VAL   B CG1  1 
ATOM   2205 C  CG2  . VAL   B 1 41  ? 19.581  -19.619 55.758 1.00 25.82 ? 305 VAL   B CG2  1 
ATOM   2206 N  N    . THR   B 1 42  ? 21.517  -23.623 56.762 1.00 28.25 ? 306 THR   B N    1 
ATOM   2207 C  CA   . THR   B 1 42  ? 22.288  -24.849 56.530 1.00 27.30 ? 306 THR   B CA   1 
ATOM   2208 C  C    . THR   B 1 42  ? 21.409  -26.054 56.815 1.00 30.34 ? 306 THR   B C    1 
ATOM   2209 O  O    . THR   B 1 42  ? 21.457  -27.035 56.075 1.00 26.42 ? 306 THR   B O    1 
ATOM   2210 C  CB   . THR   B 1 42  ? 23.560  -24.905 57.363 1.00 32.21 ? 306 THR   B CB   1 
ATOM   2211 O  OG1  . THR   B 1 42  ? 24.392  -23.834 56.940 1.00 34.07 ? 306 THR   B OG1  1 
ATOM   2212 C  CG2  . THR   B 1 42  ? 24.269  -26.242 57.111 1.00 32.85 ? 306 THR   B CG2  1 
ATOM   2213 N  N    . GLY   B 1 43  ? 20.551  -25.943 57.832 1.00 23.92 ? 307 GLY   B N    1 
ATOM   2214 C  CA   . GLY   B 1 43  ? 19.648  -27.039 58.154 1.00 25.84 ? 307 GLY   B CA   1 
ATOM   2215 C  C    . GLY   B 1 43  ? 18.749  -27.353 56.956 1.00 26.23 ? 307 GLY   B C    1 
ATOM   2216 O  O    . GLY   B 1 43  ? 18.546  -28.516 56.612 1.00 25.88 ? 307 GLY   B O    1 
ATOM   2217 N  N    . TYR   B 1 44  ? 18.156  -26.316 56.338 1.00 23.11 ? 308 TYR   B N    1 
ATOM   2218 C  CA   . TYR   B 1 44  ? 17.308  -26.562 55.162 1.00 25.04 ? 308 TYR   B CA   1 
ATOM   2219 C  C    . TYR   B 1 44  ? 18.128  -27.137 54.009 1.00 20.78 ? 308 TYR   B C    1 
ATOM   2220 O  O    . TYR   B 1 44  ? 17.640  -28.027 53.297 1.00 23.15 ? 308 TYR   B O    1 
ATOM   2221 C  CB   . TYR   B 1 44  ? 16.588  -25.282 54.686 1.00 21.27 ? 308 TYR   B CB   1 
ATOM   2222 C  CG   . TYR   B 1 44  ? 15.307  -24.967 55.412 1.00 20.81 ? 308 TYR   B CG   1 
ATOM   2223 C  CD1  . TYR   B 1 44  ? 14.141  -25.634 55.106 1.00 23.37 ? 308 TYR   B CD1  1 
ATOM   2224 C  CD2  . TYR   B 1 44  ? 15.256  -23.960 56.361 1.00 20.18 ? 308 TYR   B CD2  1 
ATOM   2225 C  CE1  . TYR   B 1 44  ? 12.970  -25.362 55.728 1.00 24.90 ? 308 TYR   B CE1  1 
ATOM   2226 C  CE2  . TYR   B 1 44  ? 14.047  -23.638 57.037 1.00 20.89 ? 308 TYR   B CE2  1 
ATOM   2227 C  CZ   . TYR   B 1 44  ? 12.888  -24.360 56.677 1.00 24.40 ? 308 TYR   B CZ   1 
ATOM   2228 O  OH   . TYR   B 1 44  ? 11.709  -24.067 57.296 1.00 27.03 ? 308 TYR   B OH   1 
ATOM   2229 N  N    . GLN   B 1 45  ? 19.378  -26.716 53.850 1.00 23.94 ? 309 GLN   B N    1 
ATOM   2230 C  CA   . GLN   B 1 45  ? 20.188  -27.188 52.729 1.00 22.66 ? 309 GLN   B CA   1 
ATOM   2231 C  C    . GLN   B 1 45  ? 20.539  -28.670 52.901 1.00 24.56 ? 309 GLN   B C    1 
ATOM   2232 O  O    . GLN   B 1 45  ? 20.779  -29.384 51.927 1.00 27.22 ? 309 GLN   B O    1 
ATOM   2233 C  CB   . GLN   B 1 45  ? 21.465  -26.337 52.612 1.00 24.87 ? 309 GLN   B CB   1 
ATOM   2234 C  CG   . GLN   B 1 45  ? 21.153  -24.945 52.108 1.00 23.33 ? 309 GLN   B CG   1 
ATOM   2235 C  CD   . GLN   B 1 45  ? 22.349  -24.016 52.023 1.00 23.97 ? 309 GLN   B CD   1 
ATOM   2236 O  OE1  . GLN   B 1 45  ? 23.339  -24.161 52.779 1.00 29.02 ? 309 GLN   B OE1  1 
ATOM   2237 N  NE2  . GLN   B 1 45  ? 22.263  -23.039 51.125 1.00 27.01 ? 309 GLN   B NE2  1 
ATOM   2238 N  N    A ARG   B 1 46  ? 20.544  -29.118 54.152 0.47 21.88 ? 310 ARG   B N    1 
ATOM   2239 N  N    B ARG   B 1 46  ? 20.546  -29.127 54.148 0.53 21.72 ? 310 ARG   B N    1 
ATOM   2240 C  CA   A ARG   B 1 46  ? 20.910  -30.494 54.502 0.47 23.71 ? 310 ARG   B CA   1 
ATOM   2241 C  CA   B ARG   B 1 46  ? 20.907  -30.511 54.475 0.53 23.71 ? 310 ARG   B CA   1 
ATOM   2242 C  C    A ARG   B 1 46  ? 19.742  -31.480 54.464 0.47 22.02 ? 310 ARG   B C    1 
ATOM   2243 C  C    B ARG   B 1 46  ? 19.744  -31.491 54.421 0.53 21.72 ? 310 ARG   B C    1 
ATOM   2244 O  O    A ARG   B 1 46  ? 19.953  -32.688 54.625 0.47 23.66 ? 310 ARG   B O    1 
ATOM   2245 O  O    B ARG   B 1 46  ? 19.959  -32.706 54.545 0.53 23.59 ? 310 ARG   B O    1 
ATOM   2246 C  CB   A ARG   B 1 46  ? 21.554  -30.538 55.890 0.47 27.47 ? 310 ARG   B CB   1 
ATOM   2247 C  CB   B ARG   B 1 46  ? 21.535  -30.584 55.862 0.53 27.09 ? 310 ARG   B CB   1 
ATOM   2248 C  CG   A ARG   B 1 46  ? 23.085  -30.379 55.874 0.47 29.59 ? 310 ARG   B CG   1 
ATOM   2249 C  CG   B ARG   B 1 46  ? 22.839  -29.797 55.991 0.53 27.09 ? 310 ARG   B CG   1 
ATOM   2250 C  CD   A ARG   B 1 46  ? 23.650  -31.290 54.791 0.47 34.44 ? 310 ARG   B CD   1 
ATOM   2251 C  CD   B ARG   B 1 46  ? 23.332  -29.780 57.425 0.53 34.78 ? 310 ARG   B CD   1 
ATOM   2252 N  NE   A ARG   B 1 46  ? 25.002  -31.811 55.007 0.47 42.09 ? 310 ARG   B NE   1 
ATOM   2253 N  NE   B ARG   B 1 46  ? 24.396  -30.743 57.631 0.53 43.02 ? 310 ARG   B NE   1 
ATOM   2254 C  CZ   A ARG   B 1 46  ? 25.360  -33.035 54.625 0.47 41.69 ? 310 ARG   B CZ   1 
ATOM   2255 C  CZ   B ARG   B 1 46  ? 24.203  -31.975 58.084 0.53 46.43 ? 310 ARG   B CZ   1 
ATOM   2256 N  NH1  A ARG   B 1 46  ? 24.459  -33.817 54.059 0.47 43.81 ? 310 ARG   B NH1  1 
ATOM   2257 N  NH1  B ARG   B 1 46  ? 22.976  -32.388 58.378 0.53 45.46 ? 310 ARG   B NH1  1 
ATOM   2258 N  NH2  A ARG   B 1 46  ? 26.579  -33.489 54.821 0.47 46.71 ? 310 ARG   B NH2  1 
ATOM   2259 N  NH2  B ARG   B 1 46  ? 25.236  -32.792 58.243 0.53 44.83 ? 310 ARG   B NH2  1 
ATOM   2260 N  N    . LYS   B 1 47  ? 18.522  -30.965 54.277 1.00 23.30 ? 311 LYS   B N    1 
ATOM   2261 C  CA   . LYS   B 1 47  ? 17.351  -31.808 54.133 1.00 19.63 ? 311 LYS   B CA   1 
ATOM   2262 C  C    . LYS   B 1 47  ? 17.444  -32.550 52.805 1.00 20.97 ? 311 LYS   B C    1 
ATOM   2263 O  O    . LYS   B 1 47  ? 18.086  -32.068 51.860 1.00 23.70 ? 311 LYS   B O    1 
ATOM   2264 C  CB   . LYS   B 1 47  ? 16.058  -30.983 54.171 1.00 20.25 ? 311 LYS   B CB   1 
ATOM   2265 C  CG   . LYS   B 1 47  ? 15.810  -30.384 55.546 1.00 23.56 ? 311 LYS   B CG   1 
ATOM   2266 C  CD   . LYS   B 1 47  ? 14.498  -29.566 55.567 1.00 24.65 ? 311 LYS   B CD   1 
ATOM   2267 C  CE   . LYS   B 1 47  ? 14.255  -28.959 56.963 1.00 28.85 ? 311 LYS   B CE   1 
ATOM   2268 N  NZ   . LYS   B 1 47  ? 14.042  -29.999 58.021 1.00 32.19 ? 311 LYS   B NZ   1 
ATOM   2269 N  N    . SER   B 1 48  ? 16.799  -33.728 52.733 1.00 20.34 ? 312 SER   B N    1 
ATOM   2270 C  CA   . SER   B 1 48  ? 16.775  -34.454 51.479 1.00 20.46 ? 312 SER   B CA   1 
ATOM   2271 C  C    . SER   B 1 48  ? 15.784  -33.788 50.534 1.00 22.09 ? 312 SER   B C    1 
ATOM   2272 O  O    . SER   B 1 48  ? 14.875  -33.047 50.993 1.00 23.63 ? 312 SER   B O    1 
ATOM   2273 C  CB   . SER   B 1 48  ? 16.338  -35.895 51.698 1.00 20.44 ? 312 SER   B CB   1 
ATOM   2274 O  OG   . SER   B 1 48  ? 15.054  -35.887 52.278 1.00 27.41 ? 312 SER   B OG   1 
ATOM   2275 N  N    . MET   B 1 49  ? 15.954  -34.026 49.232 1.00 23.90 ? 313 MET   B N    1 
ATOM   2276 C  CA   . MET   B 1 49  ? 14.980  -33.529 48.225 1.00 23.14 ? 313 MET   B CA   1 
ATOM   2277 C  C    . MET   B 1 49  ? 13.595  -34.014 48.563 1.00 22.90 ? 313 MET   B C    1 
ATOM   2278 O  O    . MET   B 1 49  ? 12.585  -33.276 48.429 1.00 23.43 ? 313 MET   B O    1 
ATOM   2279 C  CB   . MET   B 1 49  ? 15.356  -34.014 46.809 1.00 23.85 ? 313 MET   B CB   1 
ATOM   2280 C  CG   . MET   B 1 49  ? 14.421  -33.484 45.750 1.00 22.50 ? 313 MET   B CG   1 
ATOM   2281 S  SD   . MET   B 1 49  ? 14.619  -34.390 44.201 1.00 39.64 ? 313 MET   B SD   1 
ATOM   2282 C  CE   . MET   B 1 49  ? 15.813  -33.418 43.283 1.00 45.39 ? 313 MET   B CE   1 
ATOM   2283 N  N    . TRP   B 1 50  ? 13.495  -35.258 48.996 1.00 23.18 ? 314 TRP   B N    1 
ATOM   2284 C  CA   . TRP   B 1 50  ? 12.209  -35.851 49.324 1.00 23.72 ? 314 TRP   B CA   1 
ATOM   2285 C  C    . TRP   B 1 50  ? 11.484  -35.092 50.424 1.00 21.11 ? 314 TRP   B C    1 
ATOM   2286 O  O    . TRP   B 1 50  ? 10.305  -34.842 50.332 1.00 23.41 ? 314 TRP   B O    1 
ATOM   2287 C  CB   . TRP   B 1 50  ? 12.438  -37.304 49.736 1.00 31.02 ? 314 TRP   B CB   1 
ATOM   2288 C  CG   . TRP   B 1 50  ? 11.291  -38.180 49.944 1.00 49.11 ? 314 TRP   B CG   1 
ATOM   2289 C  CD1  . TRP   B 1 50  ? 9.973   -37.877 49.827 1.00 60.23 ? 314 TRP   B CD1  1 
ATOM   2290 C  CD2  . TRP   B 1 50  ? 11.361  -39.555 50.317 1.00 61.76 ? 314 TRP   B CD2  1 
ATOM   2291 N  NE1  . TRP   B 1 50  ? 9.210   -38.984 50.109 1.00 61.52 ? 314 TRP   B NE1  1 
ATOM   2292 C  CE2  . TRP   B 1 50  ? 10.043  -40.029 50.412 1.00 69.09 ? 314 TRP   B CE2  1 
ATOM   2293 C  CE3  . TRP   B 1 50  ? 12.415  -40.433 50.576 1.00 58.35 ? 314 TRP   B CE3  1 
ATOM   2294 C  CZ2  . TRP   B 1 50  ? 9.751   -41.343 50.755 1.00 70.00 ? 314 TRP   B CZ2  1 
ATOM   2295 C  CZ3  . TRP   B 1 50  ? 12.124  -41.734 50.915 1.00 59.13 ? 314 TRP   B CZ3  1 
ATOM   2296 C  CH2  . TRP   B 1 50  ? 10.802  -42.178 51.003 1.00 64.53 ? 314 TRP   B CH2  1 
ATOM   2297 N  N    . GLU   B 1 51  ? 12.224  -34.733 51.463 1.00 21.49 ? 315 GLU   B N    1 
ATOM   2298 C  CA   . GLU   B 1 51  ? 11.610  -34.012 52.565 1.00 21.77 ? 315 GLU   B CA   1 
ATOM   2299 C  C    . GLU   B 1 51  ? 11.171  -32.627 52.133 1.00 22.10 ? 315 GLU   B C    1 
ATOM   2300 O  O    . GLU   B 1 51  ? 10.050  -32.188 52.484 1.00 20.96 ? 315 GLU   B O    1 
ATOM   2301 C  CB   . GLU   B 1 51  ? 12.569  -33.901 53.757 1.00 20.71 ? 315 GLU   B CB   1 
ATOM   2302 C  CG   . GLU   B 1 51  ? 11.888  -33.074 54.861 1.00 25.50 ? 315 GLU   B CG   1 
ATOM   2303 C  CD   . GLU   B 1 51  ? 12.692  -32.853 56.100 1.00 33.84 ? 315 GLU   B CD   1 
ATOM   2304 O  OE1  . GLU   B 1 51  ? 13.674  -33.573 56.333 1.00 30.90 ? 315 GLU   B OE1  1 
ATOM   2305 O  OE2  . GLU   B 1 51  ? 12.305  -31.953 56.870 1.00 32.74 ? 315 GLU   B OE2  1 
ATOM   2306 N  N    . MET   B 1 52  ? 12.039  -31.918 51.400 1.00 20.13 ? 316 MET   B N    1 
ATOM   2307 C  CA   . MET   B 1 52  ? 11.672  -30.578 50.904 1.00 18.44 ? 316 MET   B CA   1 
ATOM   2308 C  C    . MET   B 1 52  ? 10.467  -30.656 49.951 1.00 20.69 ? 316 MET   B C    1 
ATOM   2309 O  O    . MET   B 1 52  ? 9.579   -29.793 50.004 1.00 21.56 ? 316 MET   B O    1 
ATOM   2310 C  CB   . MET   B 1 52  ? 12.857  -29.881 50.207 1.00 22.67 ? 316 MET   B CB   1 
ATOM   2311 C  CG   . MET   B 1 52  ? 13.905  -29.382 51.224 1.00 22.06 ? 316 MET   B CG   1 
ATOM   2312 S  SD   . MET   B 1 52  ? 13.217  -28.107 52.316 1.00 27.43 ? 316 MET   B SD   1 
ATOM   2313 C  CE   . MET   B 1 52  ? 12.965  -26.672 51.239 1.00 22.96 ? 316 MET   B CE   1 
ATOM   2314 N  N    . TRP   B 1 53  ? 10.425  -31.684 49.092 1.00 19.58 ? 317 TRP   B N    1 
ATOM   2315 C  CA   . TRP   B 1 53  ? 9.272   -31.842 48.186 1.00 19.16 ? 317 TRP   B CA   1 
ATOM   2316 C  C    . TRP   B 1 53  ? 8.017   -32.066 48.997 1.00 19.96 ? 317 TRP   B C    1 
ATOM   2317 O  O    . TRP   B 1 53  ? 6.975   -31.454 48.684 1.00 21.85 ? 317 TRP   B O    1 
ATOM   2318 C  CB   . TRP   B 1 53  ? 9.577   -32.979 47.195 1.00 19.15 ? 317 TRP   B CB   1 
ATOM   2319 C  CG   . TRP   B 1 53  ? 8.376   -33.660 46.577 1.00 21.30 ? 317 TRP   B CG   1 
ATOM   2320 C  CD1  . TRP   B 1 53  ? 8.090   -35.000 46.648 1.00 20.88 ? 317 TRP   B CD1  1 
ATOM   2321 C  CD2  . TRP   B 1 53  ? 7.325   -33.061 45.788 1.00 21.10 ? 317 TRP   B CD2  1 
ATOM   2322 N  NE1  . TRP   B 1 53  ? 6.935   -35.261 45.949 1.00 23.40 ? 317 TRP   B NE1  1 
ATOM   2323 C  CE2  . TRP   B 1 53  ? 6.458   -34.106 45.395 1.00 21.96 ? 317 TRP   B CE2  1 
ATOM   2324 C  CE3  . TRP   B 1 53  ? 7.061   -31.765 45.347 1.00 22.56 ? 317 TRP   B CE3  1 
ATOM   2325 C  CZ2  . TRP   B 1 53  ? 5.294   -33.883 44.629 1.00 22.28 ? 317 TRP   B CZ2  1 
ATOM   2326 C  CZ3  . TRP   B 1 53  ? 5.897   -31.532 44.560 1.00 22.54 ? 317 TRP   B CZ3  1 
ATOM   2327 C  CH2  . TRP   B 1 53  ? 5.024   -32.595 44.230 1.00 22.73 ? 317 TRP   B CH2  1 
ATOM   2328 N  N    . GLU   B 1 54  ? 8.053   -32.890 50.040 1.00 17.97 ? 318 GLU   B N    1 
ATOM   2329 C  CA   . GLU   B 1 54  ? 6.809   -33.100 50.811 1.00 19.15 ? 318 GLU   B CA   1 
ATOM   2330 C  C    . GLU   B 1 54  ? 6.333   -31.782 51.421 1.00 20.13 ? 318 GLU   B C    1 
ATOM   2331 O  O    . GLU   B 1 54  ? 5.119   -31.462 51.438 1.00 21.80 ? 318 GLU   B O    1 
ATOM   2332 C  CB   . GLU   B 1 54  ? 7.039   -34.149 51.916 1.00 26.15 ? 318 GLU   B CB   1 
ATOM   2333 C  CG   . GLU   B 1 54  ? 7.279   -35.536 51.397 1.00 27.21 ? 318 GLU   B CG   1 
ATOM   2334 C  CD   . GLU   B 1 54  ? 7.254   -36.576 52.528 1.00 43.64 ? 318 GLU   B CD   1 
ATOM   2335 O  OE1  . GLU   B 1 54  ? 7.094   -37.773 52.240 1.00 43.90 ? 318 GLU   B OE1  1 
ATOM   2336 O  OE2  . GLU   B 1 54  ? 7.385   -36.193 53.709 1.00 50.37 ? 318 GLU   B OE2  1 
ATOM   2337 N  N    . ARG   B 1 55  ? 7.271   -31.009 51.925 1.00 20.00 ? 319 ARG   B N    1 
ATOM   2338 C  CA   . ARG   B 1 55  ? 6.931   -29.717 52.533 1.00 19.64 ? 319 ARG   B CA   1 
ATOM   2339 C  C    . ARG   B 1 55  ? 6.339   -28.779 51.503 1.00 23.11 ? 319 ARG   B C    1 
ATOM   2340 O  O    . ARG   B 1 55  ? 5.288   -28.123 51.728 1.00 22.80 ? 319 ARG   B O    1 
ATOM   2341 C  CB   . ARG   B 1 55  ? 8.189   -29.066 53.147 1.00 22.53 ? 319 ARG   B CB   1 
ATOM   2342 C  CG   . ARG   B 1 55  ? 8.651   -29.740 54.387 1.00 25.77 ? 319 ARG   B CG   1 
ATOM   2343 C  CD   . ARG   B 1 55  ? 9.899   -29.015 54.942 1.00 26.96 ? 319 ARG   B CD   1 
ATOM   2344 N  NE   . ARG   B 1 55  ? 10.350  -29.684 56.158 1.00 32.69 ? 319 ARG   B NE   1 
ATOM   2345 C  CZ   . ARG   B 1 55  ? 10.312  -29.175 57.383 1.00 34.56 ? 319 ARG   B CZ   1 
ATOM   2346 N  NH1  . ARG   B 1 55  ? 9.882   -27.933 57.609 1.00 35.94 ? 319 ARG   B NH1  1 
ATOM   2347 N  NH2  . ARG   B 1 55  ? 10.731  -29.919 58.394 1.00 37.43 ? 319 ARG   B NH2  1 
ATOM   2348 N  N    . CYS   B 1 56  ? 7.007   -28.689 50.363 1.00 19.64 ? 320 CYS   B N    1 
ATOM   2349 C  CA   . CYS   B 1 56  ? 6.653   -27.659 49.411 1.00 24.76 ? 320 CYS   B CA   1 
ATOM   2350 C  C    . CYS   B 1 56  ? 5.385   -28.081 48.646 1.00 20.91 ? 320 CYS   B C    1 
ATOM   2351 O  O    . CYS   B 1 56  ? 4.601   -27.193 48.202 1.00 22.58 ? 320 CYS   B O    1 
ATOM   2352 C  CB   . CYS   B 1 56  ? 7.801   -27.353 48.470 1.00 21.15 ? 320 CYS   B CB   1 
ATOM   2353 S  SG   . CYS   B 1 56  ? 9.205   -26.594 49.353 1.00 24.13 ? 320 CYS   B SG   1 
ATOM   2354 N  N    . ALA   B 1 57  ? 5.134   -29.384 48.506 1.00 17.57 ? 321 ALA   B N    1 
ATOM   2355 C  CA   . ALA   B 1 57  ? 3.883   -29.852 47.894 1.00 19.47 ? 321 ALA   B CA   1 
ATOM   2356 C  C    . ALA   B 1 57  ? 2.720   -29.428 48.773 1.00 22.23 ? 321 ALA   B C    1 
ATOM   2357 O  O    . ALA   B 1 57  ? 1.647   -29.050 48.271 1.00 22.76 ? 321 ALA   B O    1 
ATOM   2358 C  CB   . ALA   B 1 57  ? 3.877   -31.378 47.709 1.00 20.14 ? 321 ALA   B CB   1 
ATOM   2359 N  N    . HIS   B 1 58  ? 2.910   -29.472 50.085 1.00 19.14 ? 322 HIS   B N    1 
ATOM   2360 C  CA   . HIS   B 1 58  ? 1.869   -28.991 51.003 1.00 21.67 ? 322 HIS   B CA   1 
ATOM   2361 C  C    . HIS   B 1 58  ? 1.596   -27.489 50.761 1.00 20.83 ? 322 HIS   B C    1 
ATOM   2362 O  O    . HIS   B 1 58  ? 0.431   -27.035 50.661 1.00 20.87 ? 322 HIS   B O    1 
ATOM   2363 C  CB   . HIS   B 1 58  ? 2.283   -29.197 52.454 1.00 26.85 ? 322 HIS   B CB   1 
ATOM   2364 C  CG   . HIS   B 1 58  ? 1.428   -28.458 53.429 1.00 33.44 ? 322 HIS   B CG   1 
ATOM   2365 N  ND1  . HIS   B 1 58  ? 0.188   -28.911 53.808 1.00 36.38 ? 322 HIS   B ND1  1 
ATOM   2366 C  CD2  . HIS   B 1 58  ? 1.616   -27.286 54.085 1.00 39.75 ? 322 HIS   B CD2  1 
ATOM   2367 C  CE1  . HIS   B 1 58  ? -0.360  -28.056 54.651 1.00 41.31 ? 322 HIS   B CE1  1 
ATOM   2368 N  NE2  . HIS   B 1 58  ? 0.487   -27.057 54.833 1.00 43.10 ? 322 HIS   B NE2  1 
ATOM   2369 N  N    . HIS   B 1 59  ? 2.658   -26.693 50.682 1.00 18.73 ? 323 HIS   B N    1 
ATOM   2370 C  CA   . HIS   B 1 59  ? 2.477   -25.252 50.496 1.00 17.28 ? 323 HIS   B CA   1 
ATOM   2371 C  C    . HIS   B 1 59  ? 1.807   -24.930 49.202 1.00 21.97 ? 323 HIS   B C    1 
ATOM   2372 O  O    . HIS   B 1 59  ? 0.926   -24.026 49.167 1.00 20.93 ? 323 HIS   B O    1 
ATOM   2373 C  CB   . HIS   B 1 59  ? 3.817   -24.531 50.567 1.00 19.95 ? 323 HIS   B CB   1 
ATOM   2374 C  CG   . HIS   B 1 59  ? 4.504   -24.733 51.873 1.00 21.27 ? 323 HIS   B CG   1 
ATOM   2375 N  ND1  . HIS   B 1 59  ? 3.862   -24.573 53.082 1.00 27.52 ? 323 HIS   B ND1  1 
ATOM   2376 C  CD2  . HIS   B 1 59  ? 5.794   -25.077 52.168 1.00 20.41 ? 323 HIS   B CD2  1 
ATOM   2377 C  CE1  . HIS   B 1 59  ? 4.717   -24.824 54.060 1.00 28.28 ? 323 HIS   B CE1  1 
ATOM   2378 N  NE2  . HIS   B 1 59  ? 5.890   -25.126 53.529 1.00 23.24 ? 323 HIS   B NE2  1 
ATOM   2379 N  N    . LEU   B 1 60  ? 2.195   -25.660 48.157 1.00 20.95 ? 324 LEU   B N    1 
ATOM   2380 C  CA   . LEU   B 1 60  ? 1.643   -25.445 46.810 1.00 19.43 ? 324 LEU   B CA   1 
ATOM   2381 C  C    . LEU   B 1 60  ? 0.162   -25.779 46.826 1.00 19.24 ? 324 LEU   B C    1 
ATOM   2382 O  O    . LEU   B 1 60  ? -0.703  -24.986 46.343 1.00 21.36 ? 324 LEU   B O    1 
ATOM   2383 C  CB   . LEU   B 1 60  ? 2.357   -26.345 45.809 1.00 22.09 ? 324 LEU   B CB   1 
ATOM   2384 C  CG   . LEU   B 1 60  ? 1.775   -26.453 44.409 1.00 27.43 ? 324 LEU   B CG   1 
ATOM   2385 C  CD1  . LEU   B 1 60  ? 1.981   -25.137 43.789 1.00 29.39 ? 324 LEU   B CD1  1 
ATOM   2386 C  CD2  . LEU   B 1 60  ? 2.457   -27.584 43.623 1.00 30.79 ? 324 LEU   B CD2  1 
ATOM   2387 N  N    . THR   B 1 61  ? -0.178  -26.934 47.386 1.00 20.08 ? 325 THR   B N    1 
ATOM   2388 C  CA   . THR   B 1 61  ? -1.548  -27.353 47.381 1.00 20.41 ? 325 THR   B CA   1 
ATOM   2389 C  C    . THR   B 1 61  ? -2.457  -26.405 48.146 1.00 20.73 ? 325 THR   B C    1 
ATOM   2390 O  O    . THR   B 1 61  ? -3.588  -26.084 47.688 1.00 21.13 ? 325 THR   B O    1 
ATOM   2391 C  CB   . THR   B 1 61  ? -1.620  -28.804 47.958 1.00 21.16 ? 325 THR   B CB   1 
ATOM   2392 O  OG1  . THR   B 1 61  ? -1.171  -29.658 46.900 1.00 32.08 ? 325 THR   B OG1  1 
ATOM   2393 C  CG2  . THR   B 1 61  ? -3.061  -29.095 48.327 1.00 41.25 ? 325 THR   B CG2  1 
ATOM   2394 N  N    . GLU   B 1 62  ? -1.972  -25.933 49.289 1.00 18.97 ? 326 GLU   B N    1 
ATOM   2395 C  CA   . GLU   B 1 62  ? -2.696  -24.967 50.092 1.00 18.30 ? 326 GLU   B CA   1 
ATOM   2396 C  C    . GLU   B 1 62  ? -2.911  -23.664 49.347 1.00 19.80 ? 326 GLU   B C    1 
ATOM   2397 O  O    . GLU   B 1 62  ? -4.047  -23.130 49.370 1.00 20.51 ? 326 GLU   B O    1 
ATOM   2398 C  CB   . GLU   B 1 62  ? -1.933  -24.734 51.410 1.00 23.49 ? 326 GLU   B CB   1 
ATOM   2399 C  CG   . GLU   B 1 62  ? -2.615  -23.725 52.311 1.00 27.31 ? 326 GLU   B CG   1 
ATOM   2400 C  CD   . GLU   B 1 62  ? -1.981  -23.616 53.682 1.00 44.71 ? 326 GLU   B CD   1 
ATOM   2401 O  OE1  . GLU   B 1 62  ? -0.762  -23.869 53.810 1.00 45.27 ? 326 GLU   B OE1  1 
ATOM   2402 O  OE2  . GLU   B 1 62  ? -2.706  -23.271 54.633 1.00 52.56 ? 326 GLU   B OE2  1 
ATOM   2403 N  N    . ALA   B 1 63  ? -1.874  -23.171 48.653 1.00 20.20 ? 327 ALA   B N    1 
ATOM   2404 C  CA   . ALA   B 1 63  ? -2.009  -21.885 47.928 1.00 17.37 ? 327 ALA   B CA   1 
ATOM   2405 C  C    . ALA   B 1 63  ? -3.048  -22.030 46.800 1.00 19.52 ? 327 ALA   B C    1 
ATOM   2406 O  O    . ALA   B 1 63  ? -3.873  -21.111 46.584 1.00 19.55 ? 327 ALA   B O    1 
ATOM   2407 C  CB   . ALA   B 1 63  ? -0.668  -21.449 47.361 1.00 21.01 ? 327 ALA   B CB   1 
ATOM   2408 N  N    . ILE   B 1 64  ? -2.997  -23.160 46.113 1.00 20.54 ? 328 ILE   B N    1 
ATOM   2409 C  CA   . ILE   B 1 64  ? -3.950  -23.409 45.008 1.00 18.39 ? 328 ILE   B CA   1 
ATOM   2410 C  C    . ILE   B 1 64  ? -5.358  -23.471 45.561 1.00 20.15 ? 328 ILE   B C    1 
ATOM   2411 O  O    . ILE   B 1 64  ? -6.296  -22.937 44.931 1.00 19.92 ? 328 ILE   B O    1 
ATOM   2412 C  CB   . ILE   B 1 64  ? -3.607  -24.688 44.219 1.00 17.34 ? 328 ILE   B CB   1 
ATOM   2413 C  CG1  . ILE   B 1 64  ? -2.374  -24.457 43.328 1.00 20.54 ? 328 ILE   B CG1  1 
ATOM   2414 C  CG2  . ILE   B 1 64  ? -4.811  -25.157 43.358 1.00 23.27 ? 328 ILE   B CG2  1 
ATOM   2415 C  CD1  . ILE   B 1 64  ? -1.880  -25.759 42.757 1.00 29.30 ? 328 ILE   B CD1  1 
ATOM   2416 N  N    . GLN   B 1 65  ? -5.543  -24.082 46.733 1.00 17.90 ? 329 GLN   B N    1 
ATOM   2417 C  CA   . GLN   B 1 65  ? -6.913  -24.182 47.309 1.00 20.09 ? 329 GLN   B CA   1 
ATOM   2418 C  C    . GLN   B 1 65  ? -7.507  -22.780 47.495 1.00 20.06 ? 329 GLN   B C    1 
ATOM   2419 O  O    . GLN   B 1 65  ? -8.720  -22.554 47.262 1.00 20.16 ? 329 GLN   B O    1 
ATOM   2420 C  CB   . GLN   B 1 65  ? -6.862  -24.899 48.663 1.00 21.71 ? 329 GLN   B CB   1 
ATOM   2421 C  CG   . GLN   B 1 65  ? -6.881  -26.401 48.564 1.00 39.48 ? 329 GLN   B CG   1 
ATOM   2422 C  CD   . GLN   B 1 65  ? -6.480  -27.068 49.872 1.00 53.14 ? 329 GLN   B CD   1 
ATOM   2423 O  OE1  . GLN   B 1 65  ? -6.201  -26.396 50.868 1.00 57.50 ? 329 GLN   B OE1  1 
ATOM   2424 N  NE2  . GLN   B 1 65  ? -6.440  -28.398 49.870 1.00 55.71 ? 329 GLN   B NE2  1 
ATOM   2425 N  N    . TYR   B 1 66  ? -6.699  -21.851 47.985 1.00 19.19 ? 330 TYR   B N    1 
ATOM   2426 C  CA   . TYR   B 1 66  ? -7.198  -20.500 48.231 1.00 20.64 ? 330 TYR   B CA   1 
ATOM   2427 C  C    . TYR   B 1 66  ? -7.526  -19.790 46.911 1.00 20.65 ? 330 TYR   B C    1 
ATOM   2428 O  O    . TYR   B 1 66  ? -8.480  -19.000 46.830 1.00 20.53 ? 330 TYR   B O    1 
ATOM   2429 C  CB   . TYR   B 1 66  ? -6.179  -19.638 49.019 1.00 22.55 ? 330 TYR   B CB   1 
ATOM   2430 C  CG   . TYR   B 1 66  ? -6.210  -19.876 50.505 1.00 23.53 ? 330 TYR   B CG   1 
ATOM   2431 C  CD1  . TYR   B 1 66  ? -5.583  -20.975 51.054 1.00 30.26 ? 330 TYR   B CD1  1 
ATOM   2432 C  CD2  . TYR   B 1 66  ? -6.902  -19.034 51.356 1.00 28.63 ? 330 TYR   B CD2  1 
ATOM   2433 C  CE1  . TYR   B 1 66  ? -5.612  -21.201 52.402 1.00 33.71 ? 330 TYR   B CE1  1 
ATOM   2434 C  CE2  . TYR   B 1 66  ? -6.923  -19.246 52.714 1.00 32.22 ? 330 TYR   B CE2  1 
ATOM   2435 C  CZ   . TYR   B 1 66  ? -6.279  -20.346 53.229 1.00 37.17 ? 330 TYR   B CZ   1 
ATOM   2436 O  OH   . TYR   B 1 66  ? -6.293  -20.602 54.583 1.00 41.85 ? 330 TYR   B OH   1 
ATOM   2437 N  N    . VAL   B 1 67  ? -6.730  -20.019 45.891 1.00 20.26 ? 331 VAL   B N    1 
ATOM   2438 C  CA   . VAL   B 1 67  ? -6.966  -19.382 44.588 1.00 19.37 ? 331 VAL   B CA   1 
ATOM   2439 C  C    . VAL   B 1 67  ? -8.241  -19.949 43.974 1.00 20.27 ? 331 VAL   B C    1 
ATOM   2440 O  O    . VAL   B 1 67  ? -8.990  -19.223 43.358 1.00 20.20 ? 331 VAL   B O    1 
ATOM   2441 C  CB   . VAL   B 1 67  ? -5.773  -19.583 43.638 1.00 20.67 ? 331 VAL   B CB   1 
ATOM   2442 C  CG1  . VAL   B 1 67  ? -6.162  -19.233 42.202 1.00 22.88 ? 331 VAL   B CG1  1 
ATOM   2443 C  CG2  . VAL   B 1 67  ? -4.526  -18.732 44.100 1.00 21.51 ? 331 VAL   B CG2  1 
ATOM   2444 N  N    . VAL   B 1 68  ? -8.477  -21.266 44.084 1.00 18.49 ? 332 VAL   B N    1 
ATOM   2445 C  CA   . VAL   B 1 68  ? -9.744  -21.813 43.592 1.00 17.97 ? 332 VAL   B CA   1 
ATOM   2446 C  C    . VAL   B 1 68  ? -10.911 -21.169 44.296 1.00 21.60 ? 332 VAL   B C    1 
ATOM   2447 O  O    . VAL   B 1 68  ? -11.954 -20.869 43.648 1.00 19.18 ? 332 VAL   B O    1 
ATOM   2448 C  CB   . VAL   B 1 68  ? -9.761  -23.349 43.752 1.00 17.82 ? 332 VAL   B CB   1 
ATOM   2449 C  CG1  . VAL   B 1 68  ? -11.158 -23.934 43.479 1.00 21.93 ? 332 VAL   B CG1  1 
ATOM   2450 C  CG2  . VAL   B 1 68  ? -8.773  -23.953 42.786 1.00 20.70 ? 332 VAL   B CG2  1 
ATOM   2451 N  N    . GLU   B 1 69  ? -10.805 -20.979 45.605 1.00 19.16 ? 333 GLU   B N    1 
ATOM   2452 C  CA   . GLU   B 1 69  ? -11.900 -20.363 46.343 1.00 19.36 ? 333 GLU   B CA   1 
ATOM   2453 C  C    . GLU   B 1 69  ? -12.106 -18.899 45.948 1.00 22.90 ? 333 GLU   B C    1 
ATOM   2454 O  O    . GLU   B 1 69  ? -13.261 -18.454 45.859 1.00 24.06 ? 333 GLU   B O    1 
ATOM   2455 C  CB   . GLU   B 1 69  ? -11.693 -20.492 47.854 1.00 21.97 ? 333 GLU   B CB   1 
ATOM   2456 C  CG   . GLU   B 1 69  ? -12.847 -19.908 48.698 1.00 23.48 ? 333 GLU   B CG   1 
ATOM   2457 C  CD   . GLU   B 1 69  ? -14.178 -20.677 48.526 1.00 28.75 ? 333 GLU   B CD   1 
ATOM   2458 O  OE1  . GLU   B 1 69  ? -15.228 -20.044 48.767 1.00 28.36 ? 333 GLU   B OE1  1 
ATOM   2459 O  OE2  . GLU   B 1 69  ? -14.148 -21.878 48.146 1.00 24.40 ? 333 GLU   B OE2  1 
ATOM   2460 N  N    . PHE   B 1 70  ? -11.013 -18.170 45.707 1.00 19.43 ? 334 PHE   B N    1 
ATOM   2461 C  CA   . PHE   B 1 70  ? -11.086 -16.802 45.157 1.00 20.60 ? 334 PHE   B CA   1 
ATOM   2462 C  C    . PHE   B 1 70  ? -11.912 -16.791 43.881 1.00 21.91 ? 334 PHE   B C    1 
ATOM   2463 O  O    . PHE   B 1 70  ? -12.806 -15.953 43.736 1.00 21.70 ? 334 PHE   B O    1 
ATOM   2464 C  CB   . PHE   B 1 70  ? -9.658  -16.281 44.876 1.00 22.21 ? 334 PHE   B CB   1 
ATOM   2465 C  CG   . PHE   B 1 70  ? -9.607  -14.995 44.063 1.00 20.61 ? 334 PHE   B CG   1 
ATOM   2466 C  CD1  . PHE   B 1 70  ? -10.049 -13.817 44.618 1.00 22.41 ? 334 PHE   B CD1  1 
ATOM   2467 C  CD2  . PHE   B 1 70  ? -9.024  -14.997 42.789 1.00 20.49 ? 334 PHE   B CD2  1 
ATOM   2468 C  CE1  . PHE   B 1 70  ? -9.989  -12.615 43.906 1.00 26.58 ? 334 PHE   B CE1  1 
ATOM   2469 C  CE2  . PHE   B 1 70  ? -8.902  -13.763 42.066 1.00 24.40 ? 334 PHE   B CE2  1 
ATOM   2470 C  CZ   . PHE   B 1 70  ? -9.409  -12.588 42.636 1.00 30.22 ? 334 PHE   B CZ   1 
ATOM   2471 N  N    . ALA   B 1 71  ? -11.588 -17.683 42.947 1.00 21.09 ? 335 ALA   B N    1 
ATOM   2472 C  CA   . ALA   B 1 71  ? -12.297 -17.757 41.670 1.00 23.18 ? 335 ALA   B CA   1 
ATOM   2473 C  C    . ALA   B 1 71  ? -13.797 -17.989 41.882 1.00 25.86 ? 335 ALA   B C    1 
ATOM   2474 O  O    . ALA   B 1 71  ? -14.624 -17.311 41.270 1.00 23.92 ? 335 ALA   B O    1 
ATOM   2475 C  CB   . ALA   B 1 71  ? -11.693 -18.889 40.771 1.00 24.62 ? 335 ALA   B CB   1 
ATOM   2476 N  N    . LYS   B 1 72  ? -14.159 -18.920 42.763 1.00 21.59 ? 336 LYS   B N    1 
ATOM   2477 C  CA   . LYS   B 1 72  ? -15.559 -19.265 42.934 1.00 19.73 ? 336 LYS   B CA   1 
ATOM   2478 C  C    . LYS   B 1 72  ? -16.323 -18.104 43.532 1.00 28.03 ? 336 LYS   B C    1 
ATOM   2479 O  O    . LYS   B 1 72  ? -17.536 -18.003 43.320 1.00 27.60 ? 336 LYS   B O    1 
ATOM   2480 C  CB   . LYS   B 1 72  ? -15.713 -20.494 43.779 1.00 25.04 ? 336 LYS   B CB   1 
ATOM   2481 C  CG   . LYS   B 1 72  ? -15.148 -21.713 43.072 1.00 24.65 ? 336 LYS   B CG   1 
ATOM   2482 C  CD   . LYS   B 1 72  ? -15.165 -22.852 43.985 1.00 25.31 ? 336 LYS   B CD   1 
ATOM   2483 C  CE   . LYS   B 1 72  ? -14.811 -24.139 43.235 1.00 28.21 ? 336 LYS   B CE   1 
ATOM   2484 N  NZ   . LYS   B 1 72  ? -14.616 -25.201 44.253 1.00 29.02 ? 336 LYS   B NZ   1 
ATOM   2485 N  N    . ARG   B 1 73  ? -15.638 -17.216 44.234 1.00 23.75 ? 337 ARG   B N    1 
ATOM   2486 C  CA   . ARG   B 1 73  ? -16.312 -16.079 44.834 1.00 25.77 ? 337 ARG   B CA   1 
ATOM   2487 C  C    . ARG   B 1 73  ? -16.349 -14.878 43.895 1.00 28.41 ? 337 ARG   B C    1 
ATOM   2488 O  O    . ARG   B 1 73  ? -17.047 -13.896 44.174 1.00 33.41 ? 337 ARG   B O    1 
ATOM   2489 C  CB   . ARG   B 1 73  ? -15.652 -15.670 46.158 1.00 28.36 ? 337 ARG   B CB   1 
ATOM   2490 C  CG   . ARG   B 1 73  ? -15.845 -16.706 47.255 1.00 30.12 ? 337 ARG   B CG   1 
ATOM   2491 C  CD   . ARG   B 1 73  ? -15.002 -16.456 48.514 1.00 32.60 ? 337 ARG   B CD   1 
ATOM   2492 N  NE   . ARG   B 1 73  ? -15.424 -17.426 49.523 1.00 36.61 ? 337 ARG   B NE   1 
ATOM   2493 C  CZ   . ARG   B 1 73  ? -16.260 -17.146 50.520 1.00 50.60 ? 337 ARG   B CZ   1 
ATOM   2494 N  NH1  . ARG   B 1 73  ? -16.696 -15.905 50.694 1.00 51.47 ? 337 ARG   B NH1  1 
ATOM   2495 N  NH2  . ARG   B 1 73  ? -16.633 -18.098 51.368 1.00 57.20 ? 337 ARG   B NH2  1 
ATOM   2496 N  N    . LEU   B 1 74  ? -15.579 -14.951 42.820 1.00 32.74 ? 338 LEU   B N    1 
ATOM   2497 C  CA   . LEU   B 1 74  ? -15.350 -13.825 41.929 1.00 38.33 ? 338 LEU   B CA   1 
ATOM   2498 C  C    . LEU   B 1 74  ? -16.641 -13.572 41.207 1.00 35.35 ? 338 LEU   B C    1 
ATOM   2499 O  O    . LEU   B 1 74  ? -17.216 -14.496 40.649 1.00 34.01 ? 338 LEU   B O    1 
ATOM   2500 C  CB   . LEU   B 1 74  ? -14.231 -14.149 40.951 1.00 42.73 ? 338 LEU   B CB   1 
ATOM   2501 C  CG   . LEU   B 1 74  ? -13.455 -13.050 40.252 1.00 41.12 ? 338 LEU   B CG   1 
ATOM   2502 C  CD1  . LEU   B 1 74  ? -12.990 -12.034 41.268 1.00 39.97 ? 338 LEU   B CD1  1 
ATOM   2503 C  CD2  . LEU   B 1 74  ? -12.285 -13.649 39.487 1.00 40.51 ? 338 LEU   B CD2  1 
ATOM   2504 N  N    . SER   B 1 75  ? -17.118 -12.324 41.229 1.00 41.48 ? 339 SER   B N    1 
ATOM   2505 C  CA   . SER   B 1 75  ? -18.434 -11.997 40.644 1.00 43.67 ? 339 SER   B CA   1 
ATOM   2506 C  C    . SER   B 1 75  ? -18.461 -12.312 39.155 1.00 42.61 ? 339 SER   B C    1 
ATOM   2507 O  O    . SER   B 1 75  ? -17.673 -11.746 38.393 1.00 47.29 ? 339 SER   B O    1 
ATOM   2508 C  CB   . SER   B 1 75  ? -18.769 -10.525 40.885 1.00 41.57 ? 339 SER   B CB   1 
ATOM   2509 O  OG   . SER   B 1 75  ? -19.900 -10.105 40.131 1.00 47.69 ? 339 SER   B OG   1 
ATOM   2510 N  N    . GLY   B 1 76  ? -19.328 -13.236 38.739 1.00 29.27 ? 340 GLY   B N    1 
ATOM   2511 C  CA   . GLY   B 1 76  ? -19.367 -13.657 37.344 1.00 32.89 ? 340 GLY   B CA   1 
ATOM   2512 C  C    . GLY   B 1 76  ? -18.718 -14.974 36.939 1.00 30.50 ? 340 GLY   B C    1 
ATOM   2513 O  O    . GLY   B 1 76  ? -19.064 -15.549 35.895 1.00 29.76 ? 340 GLY   B O    1 
ATOM   2514 N  N    . PHE   B 1 77  ? -17.778 -15.477 37.739 1.00 28.23 ? 341 PHE   B N    1 
ATOM   2515 C  CA   . PHE   B 1 77  ? -17.106 -16.733 37.398 1.00 26.00 ? 341 PHE   B CA   1 
ATOM   2516 C  C    . PHE   B 1 77  ? -18.120 -17.882 37.375 1.00 25.32 ? 341 PHE   B C    1 
ATOM   2517 O  O    . PHE   B 1 77  ? -18.036 -18.785 36.532 1.00 26.51 ? 341 PHE   B O    1 
ATOM   2518 C  CB   . PHE   B 1 77  ? -15.984 -17.004 38.391 1.00 25.37 ? 341 PHE   B CB   1 
ATOM   2519 C  CG   . PHE   B 1 77  ? -15.183 -18.226 38.097 1.00 25.75 ? 341 PHE   B CG   1 
ATOM   2520 C  CD1  . PHE   B 1 77  ? -14.122 -18.178 37.173 1.00 25.04 ? 341 PHE   B CD1  1 
ATOM   2521 C  CD2  . PHE   B 1 77  ? -15.434 -19.410 38.777 1.00 23.65 ? 341 PHE   B CD2  1 
ATOM   2522 C  CE1  . PHE   B 1 77  ? -13.354 -19.297 36.918 1.00 26.79 ? 341 PHE   B CE1  1 
ATOM   2523 C  CE2  . PHE   B 1 77  ? -14.642 -20.537 38.540 1.00 26.57 ? 341 PHE   B CE2  1 
ATOM   2524 C  CZ   . PHE   B 1 77  ? -13.596 -20.469 37.603 1.00 22.94 ? 341 PHE   B CZ   1 
ATOM   2525 N  N    . MET   B 1 78  ? -19.061 -17.836 38.305 1.00 29.60 ? 342 MET   B N    1 
ATOM   2526 C  CA   . MET   B 1 78  ? -20.015 -18.923 38.423 1.00 34.26 ? 342 MET   B CA   1 
ATOM   2527 C  C    . MET   B 1 78  ? -21.041 -18.872 37.298 1.00 38.11 ? 342 MET   B C    1 
ATOM   2528 O  O    . MET   B 1 78  ? -21.854 -19.777 37.181 1.00 36.48 ? 342 MET   B O    1 
ATOM   2529 C  CB   . MET   B 1 78  ? -20.707 -18.894 39.791 1.00 32.50 ? 342 MET   B CB   1 
ATOM   2530 C  CG   . MET   B 1 78  ? -19.830 -19.199 40.959 1.00 35.83 ? 342 MET   B CG   1 
ATOM   2531 S  SD   . MET   B 1 78  ? -18.847 -20.689 40.631 1.00 36.67 ? 342 MET   B SD   1 
ATOM   2532 C  CE   . MET   B 1 78  ? -19.076 -21.662 42.145 1.00 46.84 ? 342 MET   B CE   1 
ATOM   2533 N  N    . GLU   B 1 79  ? -20.996 -17.842 36.449 1.00 35.10 ? 343 GLU   B N    1 
ATOM   2534 C  CA   . GLU   B 1 79  ? -21.911 -17.783 35.301 1.00 35.77 ? 343 GLU   B CA   1 
ATOM   2535 C  C    . GLU   B 1 79  ? -21.354 -18.577 34.144 1.00 31.81 ? 343 GLU   B C    1 
ATOM   2536 O  O    . GLU   B 1 79  ? -22.061 -18.895 33.206 1.00 37.04 ? 343 GLU   B O    1 
ATOM   2537 C  CB   . GLU   B 1 79  ? -22.161 -16.343 34.892 1.00 46.54 ? 343 GLU   B CB   1 
ATOM   2538 C  CG   . GLU   B 1 79  ? -22.684 -15.522 36.040 1.00 62.38 ? 343 GLU   B CG   1 
ATOM   2539 C  CD   . GLU   B 1 79  ? -24.138 -15.221 35.891 1.00 82.67 ? 343 GLU   B CD   1 
ATOM   2540 O  OE1  . GLU   B 1 79  ? -24.450 -14.083 35.468 1.00 90.74 ? 343 GLU   B OE1  1 
ATOM   2541 O  OE2  . GLU   B 1 79  ? -24.977 -16.100 36.214 1.00 89.48 ? 343 GLU   B OE2  1 
ATOM   2542 N  N    . LEU   B 1 80  ? -20.069 -18.933 34.222 1.00 25.33 ? 344 LEU   B N    1 
ATOM   2543 C  CA   . LEU   B 1 80  ? -19.505 -19.751 33.170 1.00 26.51 ? 344 LEU   B CA   1 
ATOM   2544 C  C    . LEU   B 1 80  ? -19.912 -21.195 33.401 1.00 26.90 ? 344 LEU   B C    1 
ATOM   2545 O  O    . LEU   B 1 80  ? -20.148 -21.621 34.542 1.00 32.34 ? 344 LEU   B O    1 
ATOM   2546 C  CB   . LEU   B 1 80  ? -17.964 -19.631 33.144 1.00 25.33 ? 344 LEU   B CB   1 
ATOM   2547 C  CG   . LEU   B 1 80  ? -17.423 -18.180 33.188 1.00 27.29 ? 344 LEU   B CG   1 
ATOM   2548 C  CD1  . LEU   B 1 80  ? -15.890 -18.162 33.225 1.00 28.03 ? 344 LEU   B CD1  1 
ATOM   2549 C  CD2  . LEU   B 1 80  ? -17.905 -17.325 32.050 1.00 31.54 ? 344 LEU   B CD2  1 
ATOM   2550 N  N    . CYS   B 1 81  ? -19.925 -21.973 32.325 1.00 28.48 ? 345 CYS   B N    1 
ATOM   2551 C  CA   . CYS   B 1 81  ? -20.212 -23.377 32.443 1.00 30.04 ? 345 CYS   B CA   1 
ATOM   2552 C  C    . CYS   B 1 81  ? -19.058 -24.079 33.147 1.00 26.25 ? 345 CYS   B C    1 
ATOM   2553 O  O    . CYS   B 1 81  ? -17.922 -23.561 33.231 1.00 29.08 ? 345 CYS   B O    1 
ATOM   2554 C  CB   . CYS   B 1 81  ? -20.487 -23.991 31.070 1.00 36.46 ? 345 CYS   B CB   1 
ATOM   2555 S  SG   . CYS   B 1 81  ? -19.014 -24.071 30.023 1.00 36.76 ? 345 CYS   B SG   1 
ATOM   2556 N  N    . GLN   B 1 82  ? -19.344 -25.235 33.734 1.00 25.72 ? 346 GLN   B N    1 
ATOM   2557 C  CA   . GLN   B 1 82  ? -18.285 -25.894 34.497 1.00 29.37 ? 346 GLN   B CA   1 
ATOM   2558 C  C    . GLN   B 1 82  ? -17.040 -26.170 33.665 1.00 25.06 ? 346 GLN   B C    1 
ATOM   2559 O  O    . GLN   B 1 82  ? -15.926 -26.035 34.171 1.00 25.43 ? 346 GLN   B O    1 
ATOM   2560 C  CB   . GLN   B 1 82  ? -18.797 -27.214 35.083 1.00 28.91 ? 346 GLN   B CB   1 
ATOM   2561 C  CG   . GLN   B 1 82  ? -17.858 -27.769 36.107 1.00 35.61 ? 346 GLN   B CG   1 
ATOM   2562 C  CD   . GLN   B 1 82  ? -18.459 -28.974 36.764 1.00 34.77 ? 346 GLN   B CD   1 
ATOM   2563 O  OE1  . GLN   B 1 82  ? -18.787 -28.944 37.948 1.00 36.79 ? 346 GLN   B OE1  1 
ATOM   2564 N  NE2  . GLN   B 1 82  ? -18.623 -30.034 35.997 1.00 33.65 ? 346 GLN   B NE2  1 
ATOM   2565 N  N    . ASN   B 1 83  ? -17.217 -26.572 32.406 1.00 30.57 ? 347 ASN   B N    1 
ATOM   2566 C  CA   . ASN   B 1 83  ? -16.045 -26.782 31.546 1.00 29.00 ? 347 ASN   B CA   1 
ATOM   2567 C  C    . ASN   B 1 83  ? -15.106 -25.592 31.546 1.00 28.17 ? 347 ASN   B C    1 
ATOM   2568 O  O    . ASN   B 1 83  ? -13.872 -25.742 31.715 1.00 27.56 ? 347 ASN   B O    1 
ATOM   2569 C  CB   . ASN   B 1 83  ? -16.444 -27.056 30.083 1.00 29.74 ? 347 ASN   B CB   1 
ATOM   2570 C  CG   . ASN   B 1 83  ? -15.214 -27.135 29.145 1.00 39.83 ? 347 ASN   B CG   1 
ATOM   2571 O  OD1  . ASN   B 1 83  ? -14.796 -26.140 28.523 1.00 40.16 ? 347 ASN   B OD1  1 
ATOM   2572 N  ND2  . ASN   B 1 83  ? -14.613 -28.314 29.073 1.00 42.46 ? 347 ASN   B ND2  1 
ATOM   2573 N  N    . ASP   B 1 84  ? -15.676 -24.415 31.323 1.00 27.22 ? 348 ASP   B N    1 
ATOM   2574 C  CA   . ASP   B 1 84  ? -14.864 -23.219 31.164 1.00 28.36 ? 348 ASP   B CA   1 
ATOM   2575 C  C    . ASP   B 1 84  ? -14.262 -22.801 32.491 1.00 22.72 ? 348 ASP   B C    1 
ATOM   2576 O  O    . ASP   B 1 84  ? -13.119 -22.309 32.521 1.00 22.75 ? 348 ASP   B O    1 
ATOM   2577 C  CB   . ASP   B 1 84  ? -15.678 -22.071 30.554 1.00 23.22 ? 348 ASP   B CB   1 
ATOM   2578 C  CG   . ASP   B 1 84  ? -15.991 -22.295 29.088 1.00 29.73 ? 348 ASP   B CG   1 
ATOM   2579 O  OD1  . ASP   B 1 84  ? -15.523 -23.305 28.546 1.00 33.39 ? 348 ASP   B OD1  1 
ATOM   2580 O  OD2  . ASP   B 1 84  ? -16.707 -21.466 28.491 1.00 30.24 ? 348 ASP   B OD2  1 
ATOM   2581 N  N    . GLN   B 1 85  ? -14.975 -23.026 33.595 1.00 21.32 ? 349 GLN   B N    1 
ATOM   2582 C  CA   . GLN   B 1 85  ? -14.365 -22.787 34.921 1.00 20.72 ? 349 GLN   B CA   1 
ATOM   2583 C  C    . GLN   B 1 85  ? -13.096 -23.604 35.075 1.00 21.16 ? 349 GLN   B C    1 
ATOM   2584 O  O    . GLN   B 1 85  ? -12.033 -23.122 35.547 1.00 21.78 ? 349 GLN   B O    1 
ATOM   2585 C  CB   . GLN   B 1 85  ? -15.329 -23.148 36.036 1.00 22.21 ? 349 GLN   B CB   1 
ATOM   2586 C  CG   . GLN   B 1 85  ? -16.571 -22.251 36.122 1.00 22.03 ? 349 GLN   B CG   1 
ATOM   2587 C  CD   . GLN   B 1 85  ? -17.513 -22.767 37.171 1.00 30.27 ? 349 GLN   B CD   1 
ATOM   2588 O  OE1  . GLN   B 1 85  ? -17.094 -23.379 38.147 1.00 29.12 ? 349 GLN   B OE1  1 
ATOM   2589 N  NE2  . GLN   B 1 85  ? -18.810 -22.543 36.969 1.00 31.12 ? 349 GLN   B NE2  1 
ATOM   2590 N  N    . ILE   B 1 86  ? -13.199 -24.865 34.683 1.00 20.92 ? 350 ILE   B N    1 
ATOM   2591 C  CA   . ILE   B 1 86  ? -12.074 -25.762 34.833 1.00 21.17 ? 350 ILE   B CA   1 
ATOM   2592 C  C    . ILE   B 1 86  ? -10.924 -25.352 33.910 1.00 21.37 ? 350 ILE   B C    1 
ATOM   2593 O  O    . ILE   B 1 86  ? -9.744  -25.329 34.319 1.00 21.32 ? 350 ILE   B O    1 
ATOM   2594 C  CB   . ILE   B 1 86  ? -12.526 -27.208 34.594 1.00 23.07 ? 350 ILE   B CB   1 
ATOM   2595 C  CG1  . ILE   B 1 86  ? -13.317 -27.663 35.812 1.00 25.31 ? 350 ILE   B CG1  1 
ATOM   2596 C  CG2  . ILE   B 1 86  ? -11.318 -28.113 34.311 1.00 24.12 ? 350 ILE   B CG2  1 
ATOM   2597 C  CD1  . ILE   B 1 86  ? -14.129 -28.892 35.551 1.00 28.11 ? 350 ILE   B CD1  1 
ATOM   2598 N  N    . VAL   B 1 87  ? -11.277 -25.014 32.667 1.00 21.70 ? 351 VAL   B N    1 
ATOM   2599 C  CA   . VAL   B 1 87  ? -10.232 -24.544 31.740 1.00 22.84 ? 351 VAL   B CA   1 
ATOM   2600 C  C    . VAL   B 1 87  ? -9.494  -23.345 32.295 1.00 22.77 ? 351 VAL   B C    1 
ATOM   2601 O  O    . VAL   B 1 87  ? -8.225  -23.305 32.301 1.00 23.07 ? 351 VAL   B O    1 
ATOM   2602 C  CB   . VAL   B 1 87  ? -10.837 -24.193 30.376 1.00 24.60 ? 351 VAL   B CB   1 
ATOM   2603 C  CG1  . VAL   B 1 87  ? -9.783  -23.478 29.501 1.00 23.62 ? 351 VAL   B CG1  1 
ATOM   2604 C  CG2  . VAL   B 1 87  ? -11.340 -25.464 29.677 1.00 29.64 ? 351 VAL   B CG2  1 
ATOM   2605 N  N    . LEU   B 1 88  ? -10.253 -22.371 32.776 1.00 20.06 ? 352 LEU   B N    1 
ATOM   2606 C  CA   . LEU   B 1 88  ? -9.604  -21.145 33.288 1.00 19.92 ? 352 LEU   B CA   1 
ATOM   2607 C  C    . LEU   B 1 88  ? -8.753  -21.423 34.498 1.00 22.62 ? 352 LEU   B C    1 
ATOM   2608 O  O    . LEU   B 1 88  ? -7.671  -20.839 34.643 1.00 21.64 ? 352 LEU   B O    1 
ATOM   2609 C  CB   . LEU   B 1 88  ? -10.689 -20.090 33.627 1.00 19.28 ? 352 LEU   B CB   1 
ATOM   2610 C  CG   . LEU   B 1 88  ? -11.436 -19.547 32.429 1.00 20.80 ? 352 LEU   B CG   1 
ATOM   2611 C  CD1  . LEU   B 1 88  ? -12.444 -18.531 32.893 1.00 23.49 ? 352 LEU   B CD1  1 
ATOM   2612 C  CD2  . LEU   B 1 88  ? -10.483 -18.931 31.391 1.00 23.63 ? 352 LEU   B CD2  1 
ATOM   2613 N  N    . LEU   B 1 89  ? -9.208  -22.283 35.411 1.00 21.35 ? 353 LEU   B N    1 
ATOM   2614 C  CA   . LEU   B 1 89  ? -8.369  -22.516 36.593 1.00 20.74 ? 353 LEU   B CA   1 
ATOM   2615 C  C    . LEU   B 1 89  ? -7.179  -23.409 36.292 1.00 24.39 ? 353 LEU   B C    1 
ATOM   2616 O  O    . LEU   B 1 89  ? -6.071  -23.237 36.854 1.00 24.66 ? 353 LEU   B O    1 
ATOM   2617 C  CB   . LEU   B 1 89  ? -9.217  -23.124 37.716 1.00 24.33 ? 353 LEU   B CB   1 
ATOM   2618 C  CG   . LEU   B 1 89  ? -10.067 -22.122 38.488 1.00 27.36 ? 353 LEU   B CG   1 
ATOM   2619 C  CD1  . LEU   B 1 89  ? -11.042 -22.818 39.330 1.00 28.00 ? 353 LEU   B CD1  1 
ATOM   2620 C  CD2  . LEU   B 1 89  ? -9.153  -21.291 39.365 1.00 31.46 ? 353 LEU   B CD2  1 
ATOM   2621 N  N    . LYS   B 1 90  ? -7.334  -24.358 35.387 1.00 23.25 ? 354 LYS   B N    1 
ATOM   2622 C  CA   . LYS   B 1 90  ? -6.179  -25.193 35.067 1.00 27.49 ? 354 LYS   B CA   1 
ATOM   2623 C  C    . LYS   B 1 90  ? -5.049  -24.368 34.484 1.00 26.00 ? 354 LYS   B C    1 
ATOM   2624 O  O    . LYS   B 1 90  ? -3.862  -24.621 34.811 1.00 28.05 ? 354 LYS   B O    1 
ATOM   2625 C  CB   . LYS   B 1 90  ? -6.579  -26.326 34.133 1.00 28.75 ? 354 LYS   B CB   1 
ATOM   2626 C  CG   . LYS   B 1 90  ? -7.151  -27.513 34.924 1.00 37.82 ? 354 LYS   B CG   1 
ATOM   2627 C  CD   . LYS   B 1 90  ? -7.796  -28.579 34.032 1.00 45.88 ? 354 LYS   B CD   1 
ATOM   2628 C  CE   . LYS   B 1 90  ? -6.810  -29.155 33.022 1.00 56.77 ? 354 LYS   B CE   1 
ATOM   2629 N  NZ   . LYS   B 1 90  ? -7.488  -29.942 31.932 1.00 60.17 ? 354 LYS   B NZ   1 
ATOM   2630 N  N    . ALA   B 1 91  ? -5.423  -23.422 33.620 1.00 24.50 ? 355 ALA   B N    1 
ATOM   2631 C  CA   . ALA   B 1 91  ? -4.482  -22.528 32.931 1.00 24.76 ? 355 ALA   B CA   1 
ATOM   2632 C  C    . ALA   B 1 91  ? -3.938  -21.417 33.826 1.00 30.92 ? 355 ALA   B C    1 
ATOM   2633 O  O    . ALA   B 1 91  ? -2.798  -20.976 33.629 1.00 29.77 ? 355 ALA   B O    1 
ATOM   2634 C  CB   . ALA   B 1 91  ? -5.159  -21.912 31.701 1.00 27.69 ? 355 ALA   B CB   1 
ATOM   2635 N  N    . GLY   B 1 92  ? -4.732  -20.987 34.810 1.00 26.10 ? 356 GLY   B N    1 
ATOM   2636 C  CA   . GLY   B 1 92  ? -4.465  -19.725 35.485 1.00 24.64 ? 356 GLY   B CA   1 
ATOM   2637 C  C    . GLY   B 1 92  ? -4.204  -19.764 36.988 1.00 24.37 ? 356 GLY   B C    1 
ATOM   2638 O  O    . GLY   B 1 92  ? -3.626  -18.796 37.522 1.00 24.45 ? 356 GLY   B O    1 
ATOM   2639 N  N    . ALA   B 1 93  ? -4.597  -20.841 37.667 1.00 23.50 ? 357 ALA   B N    1 
ATOM   2640 C  CA   . ALA   B 1 93  ? -4.518  -20.868 39.125 1.00 23.34 ? 357 ALA   B CA   1 
ATOM   2641 C  C    . ALA   B 1 93  ? -3.050  -20.678 39.561 1.00 21.13 ? 357 ALA   B C    1 
ATOM   2642 O  O    . ALA   B 1 93  ? -2.760  -19.936 40.522 1.00 19.94 ? 357 ALA   B O    1 
ATOM   2643 C  CB   . ALA   B 1 93  ? -5.070  -22.159 39.665 1.00 24.30 ? 357 ALA   B CB   1 
ATOM   2644 N  N    . MET   B 1 94  ? -2.124  -21.366 38.899 1.00 24.49 ? 358 MET   B N    1 
ATOM   2645 C  CA   . MET   B 1 94  ? -0.720  -21.305 39.329 1.00 22.43 ? 358 MET   B CA   1 
ATOM   2646 C  C    . MET   B 1 94  ? -0.144  -19.922 39.036 1.00 22.73 ? 358 MET   B C    1 
ATOM   2647 O  O    . MET   B 1 94  ? 0.693   -19.404 39.768 1.00 23.52 ? 358 MET   B O    1 
ATOM   2648 C  CB   . MET   B 1 94  ? 0.089   -22.415 38.633 1.00 25.03 ? 358 MET   B CB   1 
ATOM   2649 C  CG   . MET   B 1 94  ? 1.489   -22.555 39.159 1.00 28.28 ? 358 MET   B CG   1 
ATOM   2650 S  SD   . MET   B 1 94  ? 1.410   -23.071 40.883 1.00 29.01 ? 358 MET   B SD   1 
ATOM   2651 C  CE   . MET   B 1 94  ? 3.043   -22.569 41.371 1.00 30.49 ? 358 MET   B CE   1 
ATOM   2652 N  N    . GLU   B 1 95  ? -0.611  -19.295 37.965 1.00 24.70 ? 359 GLU   B N    1 
ATOM   2653 C  CA   . GLU   B 1 95  ? -0.218  -17.943 37.655 1.00 24.46 ? 359 GLU   B CA   1 
ATOM   2654 C  C    . GLU   B 1 95  ? -0.631  -17.009 38.794 1.00 23.67 ? 359 GLU   B C    1 
ATOM   2655 O  O    . GLU   B 1 95  ? 0.126   -16.150 39.199 1.00 23.58 ? 359 GLU   B O    1 
ATOM   2656 C  CB   . GLU   B 1 95  ? -0.818  -17.522 36.300 1.00 31.34 ? 359 GLU   B CB   1 
ATOM   2657 C  CG   . GLU   B 1 95  ? -0.351  -18.411 35.116 1.00 41.31 ? 359 GLU   B CG   1 
ATOM   2658 C  CD   . GLU   B 1 95  ? -0.798  -17.898 33.740 1.00 52.92 ? 359 GLU   B CD   1 
ATOM   2659 O  OE1  . GLU   B 1 95  ? -1.634  -16.985 33.668 1.00 53.50 ? 359 GLU   B OE1  1 
ATOM   2660 O  OE2  . GLU   B 1 95  ? -0.298  -18.409 32.717 1.00 56.83 ? 359 GLU   B OE2  1 
ATOM   2661 N  N    . VAL   B 1 96  ? -1.828  -17.189 39.318 1.00 19.82 ? 360 VAL   B N    1 
ATOM   2662 C  CA   . VAL   B 1 96  ? -2.286  -16.364 40.419 1.00 19.26 ? 360 VAL   B CA   1 
ATOM   2663 C  C    . VAL   B 1 96  ? -1.445  -16.646 41.668 1.00 22.72 ? 360 VAL   B C    1 
ATOM   2664 O  O    . VAL   B 1 96  ? -1.121  -15.731 42.406 1.00 22.22 ? 360 VAL   B O    1 
ATOM   2665 C  CB   . VAL   B 1 96  ? -3.796  -16.537 40.678 1.00 19.11 ? 360 VAL   B CB   1 
ATOM   2666 C  CG1  . VAL   B 1 96  ? -4.215  -15.795 41.924 1.00 19.88 ? 360 VAL   B CG1  1 
ATOM   2667 C  CG2  . VAL   B 1 96  ? -4.543  -15.954 39.512 1.00 22.21 ? 360 VAL   B CG2  1 
ATOM   2668 N  N    . VAL   B 1 97  ? -1.147  -17.914 41.936 1.00 20.27 ? 361 VAL   B N    1 
ATOM   2669 C  CA   . VAL   B 1 97  ? -0.275  -18.214 43.117 1.00 18.68 ? 361 VAL   B CA   1 
ATOM   2670 C  C    . VAL   B 1 97  ? 1.037   -17.449 43.032 1.00 21.08 ? 361 VAL   B C    1 
ATOM   2671 O  O    . VAL   B 1 97  ? 1.485   -16.849 44.028 1.00 21.60 ? 361 VAL   B O    1 
ATOM   2672 C  CB   . VAL   B 1 97  ? -0.022  -19.734 43.243 1.00 20.14 ? 361 VAL   B CB   1 
ATOM   2673 C  CG1  . VAL   B 1 97  ? 1.161   -20.032 44.271 1.00 21.74 ? 361 VAL   B CG1  1 
ATOM   2674 C  CG2  . VAL   B 1 97  ? -1.308  -20.446 43.630 1.00 19.63 ? 361 VAL   B CG2  1 
ATOM   2675 N  N    . LEU   B 1 98  ? 1.636   -17.461 41.848 1.00 19.45 ? 362 LEU   B N    1 
ATOM   2676 C  CA   . LEU   B 1 98  ? 2.950   -16.819 41.670 1.00 21.01 ? 362 LEU   B CA   1 
ATOM   2677 C  C    . LEU   B 1 98  ? 2.861   -15.258 41.787 1.00 20.97 ? 362 LEU   B C    1 
ATOM   2678 O  O    . LEU   B 1 98  ? 3.771   -14.611 42.279 1.00 26.70 ? 362 LEU   B O    1 
ATOM   2679 C  CB   . LEU   B 1 98  ? 3.512   -17.233 40.335 1.00 19.28 ? 362 LEU   B CB   1 
ATOM   2680 C  CG   . LEU   B 1 98  ? 3.953   -18.699 40.256 1.00 23.75 ? 362 LEU   B CG   1 
ATOM   2681 C  CD1  . LEU   B 1 98  ? 4.121   -19.086 38.818 1.00 26.96 ? 362 LEU   B CD1  1 
ATOM   2682 C  CD2  . LEU   B 1 98  ? 5.294   -18.956 41.000 1.00 22.83 ? 362 LEU   B CD2  1 
ATOM   2683 N  N    . VAL   B 1 99  ? 1.764   -14.672 41.322 1.00 24.03 ? 363 VAL   B N    1 
ATOM   2684 C  CA   . VAL   B 1 99  ? 1.573   -13.249 41.472 1.00 21.32 ? 363 VAL   B CA   1 
ATOM   2685 C  C    . VAL   B 1 99  ? 1.353   -12.956 42.924 1.00 22.78 ? 363 VAL   B C    1 
ATOM   2686 O  O    . VAL   B 1 99  ? 1.907   -12.001 43.427 1.00 24.24 ? 363 VAL   B O    1 
ATOM   2687 C  CB   . VAL   B 1 99  ? 0.389   -12.720 40.591 1.00 22.96 ? 363 VAL   B CB   1 
ATOM   2688 C  CG1  . VAL   B 1 99  ? 0.095   -11.230 40.887 1.00 23.51 ? 363 VAL   B CG1  1 
ATOM   2689 C  CG2  . VAL   B 1 99  ? 0.781   -12.908 39.096 1.00 24.03 ? 363 VAL   B CG2  1 
ATOM   2690 N  N    . ARG   B 1 100 ? 0.534   -13.749 43.617 1.00 22.25 ? 364 ARG   B N    1 
ATOM   2691 C  CA   . ARG   B 1 100 ? 0.272   -13.496 45.025 1.00 21.93 ? 364 ARG   B CA   1 
ATOM   2692 C  C    . ARG   B 1 100 ? 1.556   -13.537 45.862 1.00 24.12 ? 364 ARG   B C    1 
ATOM   2693 O  O    . ARG   B 1 100 ? 1.655   -12.842 46.898 1.00 23.59 ? 364 ARG   B O    1 
ATOM   2694 C  CB   . ARG   B 1 100 ? -0.716  -14.516 45.574 1.00 21.21 ? 364 ARG   B CB   1 
ATOM   2695 C  CG   . ARG   B 1 100 ? -2.186  -14.237 45.174 1.00 20.66 ? 364 ARG   B CG   1 
ATOM   2696 C  CD   . ARG   B 1 100 ? -3.082  -15.376 45.745 1.00 21.74 ? 364 ARG   B CD   1 
ATOM   2697 N  NE   . ARG   B 1 100 ? -4.499  -15.018 45.668 1.00 21.46 ? 364 ARG   B NE   1 
ATOM   2698 C  CZ   . ARG   B 1 100 ? -5.422  -15.390 46.554 1.00 23.86 ? 364 ARG   B CZ   1 
ATOM   2699 N  NH1  . ARG   B 1 100 ? -5.063  -16.234 47.540 1.00 25.81 ? 364 ARG   B NH1  1 
ATOM   2700 N  NH2  . ARG   B 1 100 ? -6.692  -14.956 46.425 1.00 25.12 ? 364 ARG   B NH2  1 
ATOM   2701 N  N    . MET   B 1 101 ? 2.491   -14.370 45.435 1.00 23.59 ? 365 MET   B N    1 
ATOM   2702 C  CA   . MET   B 1 101 ? 3.746   -14.566 46.165 1.00 21.21 ? 365 MET   B CA   1 
ATOM   2703 C  C    . MET   B 1 101 ? 4.527   -13.262 46.330 1.00 24.92 ? 365 MET   B C    1 
ATOM   2704 O  O    . MET   B 1 101 ? 5.301   -13.134 47.282 1.00 27.39 ? 365 MET   B O    1 
ATOM   2705 C  CB   . MET   B 1 101 ? 4.594   -15.620 45.486 1.00 27.26 ? 365 MET   B CB   1 
ATOM   2706 C  CG   . MET   B 1 101 ? 5.846   -15.851 46.240 1.00 29.34 ? 365 MET   B CG   1 
ATOM   2707 S  SD   . MET   B 1 101 ? 6.652   -17.235 45.458 1.00 33.49 ? 365 MET   B SD   1 
ATOM   2708 C  CE   . MET   B 1 101 ? 5.369   -18.478 45.720 1.00 36.20 ? 365 MET   B CE   1 
ATOM   2709 N  N    . CYS   B 1 102 ? 4.316   -12.275 45.458 1.00 22.55 ? 366 CYS   B N    1 
ATOM   2710 C  CA   . CYS   B 1 102 ? 5.168   -11.099 45.522 1.00 25.75 ? 366 CYS   B CA   1 
ATOM   2711 C  C    . CYS   B 1 102 ? 4.920   -10.315 46.815 1.00 25.81 ? 366 CYS   B C    1 
ATOM   2712 O  O    . CYS   B 1 102 ? 5.800   -9.548  47.255 1.00 25.47 ? 366 CYS   B O    1 
ATOM   2713 C  CB   . CYS   B 1 102 ? 4.983   -10.182 44.285 1.00 25.92 ? 366 CYS   B CB   1 
ATOM   2714 S  SG   . CYS   B 1 102 ? 3.493   -9.229  44.190 1.00 27.83 ? 366 CYS   B SG   1 
ATOM   2715 N  N    . ARG   B 1 103 ? 3.763   -10.537 47.434 1.00 24.22 ? 367 ARG   B N    1 
ATOM   2716 C  CA   . ARG   B 1 103 ? 3.429   -9.902  48.704 1.00 23.91 ? 367 ARG   B CA   1 
ATOM   2717 C  C    . ARG   B 1 103 ? 4.412   -10.322 49.787 1.00 26.08 ? 367 ARG   B C    1 
ATOM   2718 O  O    . ARG   B 1 103 ? 4.710   -9.563  50.735 1.00 29.00 ? 367 ARG   B O    1 
ATOM   2719 C  CB   . ARG   B 1 103 ? 2.008   -10.289 49.100 1.00 23.14 ? 367 ARG   B CB   1 
ATOM   2720 C  CG   . ARG   B 1 103 ? 0.965   -9.685  48.213 1.00 24.76 ? 367 ARG   B CG   1 
ATOM   2721 C  CD   . ARG   B 1 103 ? -0.372  -10.390 48.451 1.00 24.83 ? 367 ARG   B CD   1 
ATOM   2722 N  NE   . ARG   B 1 103 ? -1.088  -9.909  49.620 1.00 27.80 ? 367 ARG   B NE   1 
ATOM   2723 C  CZ   . ARG   B 1 103 ? -1.266  -10.600 50.740 1.00 23.23 ? 367 ARG   B CZ   1 
ATOM   2724 N  NH1  . ARG   B 1 103 ? -0.759  -11.835 50.860 1.00 26.10 ? 367 ARG   B NH1  1 
ATOM   2725 N  NH2  . ARG   B 1 103 ? -2.014  -10.054 51.700 1.00 28.14 ? 367 ARG   B NH2  1 
ATOM   2726 N  N    . ALA   B 1 104 ? 4.883   -11.540 49.643 1.00 21.78 ? 368 ALA   B N    1 
ATOM   2727 C  CA   . ALA   B 1 104 ? 5.729   -12.201 50.634 1.00 22.51 ? 368 ALA   B CA   1 
ATOM   2728 C  C    . ALA   B 1 104 ? 7.198   -12.122 50.268 1.00 23.48 ? 368 ALA   B C    1 
ATOM   2729 O  O    . ALA   B 1 104 ? 8.053   -12.803 50.872 1.00 24.57 ? 368 ALA   B O    1 
ATOM   2730 C  CB   . ALA   B 1 104 ? 5.288   -13.666 50.787 1.00 23.98 ? 368 ALA   B CB   1 
ATOM   2731 N  N    . TYR   B 1 105 ? 7.502   -11.287 49.279 1.00 23.01 ? 369 TYR   B N    1 
ATOM   2732 C  CA   . TYR   B 1 105 ? 8.859   -11.125 48.763 1.00 22.04 ? 369 TYR   B CA   1 
ATOM   2733 C  C    . TYR   B 1 105 ? 9.383   -9.757  49.195 1.00 22.95 ? 369 TYR   B C    1 
ATOM   2734 O  O    . TYR   B 1 105 ? 8.716   -8.740  49.053 1.00 25.19 ? 369 TYR   B O    1 
ATOM   2735 C  CB   . TYR   B 1 105 ? 8.888   -11.262 47.230 1.00 22.65 ? 369 TYR   B CB   1 
ATOM   2736 C  CG   . TYR   B 1 105 ? 10.260  -11.036 46.637 1.00 21.40 ? 369 TYR   B CG   1 
ATOM   2737 C  CD1  . TYR   B 1 105 ? 11.200  -12.048 46.646 1.00 22.81 ? 369 TYR   B CD1  1 
ATOM   2738 C  CD2  . TYR   B 1 105 ? 10.626  -9.794  46.099 1.00 25.00 ? 369 TYR   B CD2  1 
ATOM   2739 C  CE1  . TYR   B 1 105 ? 12.453  -11.861 46.121 1.00 22.70 ? 369 TYR   B CE1  1 
ATOM   2740 C  CE2  . TYR   B 1 105 ? 11.913  -9.584  45.575 1.00 29.26 ? 369 TYR   B CE2  1 
ATOM   2741 C  CZ   . TYR   B 1 105 ? 12.815  -10.630 45.576 1.00 24.43 ? 369 TYR   B CZ   1 
ATOM   2742 O  OH   . TYR   B 1 105 ? 14.103  -10.479 45.092 1.00 29.80 ? 369 TYR   B OH   1 
ATOM   2743 N  N    . ASN   B 1 106 ? 10.595  -9.775  49.735 1.00 23.24 ? 370 ASN   B N    1 
ATOM   2744 C  CA   . ASN   B 1 106 ? 11.300  -8.561  50.145 1.00 25.79 ? 370 ASN   B CA   1 
ATOM   2745 C  C    . ASN   B 1 106 ? 12.386  -8.299  49.142 1.00 24.73 ? 370 ASN   B C    1 
ATOM   2746 O  O    . ASN   B 1 106 ? 13.409  -8.969  49.145 1.00 23.41 ? 370 ASN   B O    1 
ATOM   2747 C  CB   . ASN   B 1 106 ? 11.911  -8.728  51.542 1.00 24.71 ? 370 ASN   B CB   1 
ATOM   2748 C  CG   . ASN   B 1 106 ? 12.567  -7.444  52.038 1.00 25.10 ? 370 ASN   B CG   1 
ATOM   2749 O  OD1  . ASN   B 1 106 ? 12.577  -6.450  51.326 1.00 28.99 ? 370 ASN   B OD1  1 
ATOM   2750 N  ND2  . ASN   B 1 106 ? 13.090  -7.464  53.258 1.00 32.04 ? 370 ASN   B ND2  1 
ATOM   2751 N  N    . ALA   B 1 107 ? 12.205  -7.329  48.267 1.00 26.09 ? 371 ALA   B N    1 
ATOM   2752 C  CA   . ALA   B 1 107 ? 13.252  -7.034  47.300 1.00 27.86 ? 371 ALA   B CA   1 
ATOM   2753 C  C    . ALA   B 1 107 ? 14.548  -6.436  47.896 1.00 30.22 ? 371 ALA   B C    1 
ATOM   2754 O  O    . ALA   B 1 107 ? 15.572  -6.490  47.236 1.00 32.53 ? 371 ALA   B O    1 
ATOM   2755 C  CB   . ALA   B 1 107 ? 12.686  -6.091  46.208 1.00 29.50 ? 371 ALA   B CB   1 
ATOM   2756 N  N    . ASP   B 1 108 ? 14.492  -5.864  49.104 1.00 29.63 ? 372 ASP   B N    1 
ATOM   2757 C  CA   . ASP   B 1 108 ? 15.663  -5.251  49.743 1.00 33.11 ? 372 ASP   B CA   1 
ATOM   2758 C  C    . ASP   B 1 108 ? 16.807  -6.247  49.935 1.00 31.53 ? 372 ASP   B C    1 
ATOM   2759 O  O    . ASP   B 1 108 ? 17.988  -5.901  49.747 1.00 37.08 ? 372 ASP   B O    1 
ATOM   2760 C  CB   . ASP   B 1 108 ? 15.292  -4.648  51.110 1.00 36.05 ? 372 ASP   B CB   1 
ATOM   2761 C  CG   . ASP   B 1 108 ? 14.145  -3.637  51.039 1.00 53.83 ? 372 ASP   B CG   1 
ATOM   2762 O  OD1  . ASP   B 1 108 ? 13.929  -3.019  49.975 1.00 60.01 ? 372 ASP   B OD1  1 
ATOM   2763 O  OD2  . ASP   B 1 108 ? 13.454  -3.463  52.066 1.00 57.70 ? 372 ASP   B OD2  1 
ATOM   2764 N  N    . ASN   B 1 109 ? 16.488  -7.479  50.349 1.00 28.37 ? 373 ASN   B N    1 
ATOM   2765 C  CA   . ASN   B 1 109 ? 17.528  -8.464  50.631 1.00 28.71 ? 373 ASN   B CA   1 
ATOM   2766 C  C    . ASN   B 1 109 ? 17.273  -9.743  49.816 1.00 27.34 ? 373 ASN   B C    1 
ATOM   2767 O  O    . ASN   B 1 109 ? 17.964  -10.729 49.986 1.00 29.37 ? 373 ASN   B O    1 
ATOM   2768 C  CB   . ASN   B 1 109 ? 17.607  -8.773  52.143 1.00 29.38 ? 373 ASN   B CB   1 
ATOM   2769 C  CG   . ASN   B 1 109 ? 16.286  -9.231  52.723 1.00 29.06 ? 373 ASN   B CG   1 
ATOM   2770 O  OD1  . ASN   B 1 109 ? 15.318  -9.455  51.994 1.00 30.35 ? 373 ASN   B OD1  1 
ATOM   2771 N  ND2  . ASN   B 1 109 ? 16.247  -9.399  54.047 1.00 31.74 ? 373 ASN   B ND2  1 
ATOM   2772 N  N    . ARG   B 1 110 ? 16.304  -9.671  48.910 1.00 28.23 ? 374 ARG   B N    1 
ATOM   2773 C  CA   . ARG   B 1 110 ? 15.943  -10.782 48.008 1.00 28.46 ? 374 ARG   B CA   1 
ATOM   2774 C  C    . ARG   B 1 110 ? 15.579  -12.071 48.787 1.00 25.39 ? 374 ARG   B C    1 
ATOM   2775 O  O    . ARG   B 1 110 ? 16.099  -13.172 48.530 1.00 30.53 ? 374 ARG   B O    1 
ATOM   2776 C  CB   . ARG   B 1 110 ? 17.087  -11.028 47.017 1.00 27.97 ? 374 ARG   B CB   1 
ATOM   2777 C  CG   . ARG   B 1 110 ? 17.504  -9.751  46.237 1.00 33.01 ? 374 ARG   B CG   1 
ATOM   2778 C  CD   . ARG   B 1 110 ? 18.321  -10.090 44.976 1.00 47.18 ? 374 ARG   B CD   1 
ATOM   2779 N  NE   . ARG   B 1 110 ? 17.533  -10.909 44.049 1.00 65.81 ? 374 ARG   B NE   1 
ATOM   2780 C  CZ   . ARG   B 1 110 ? 17.099  -10.514 42.849 1.00 73.37 ? 374 ARG   B CZ   1 
ATOM   2781 N  NH1  . ARG   B 1 110 ? 16.360  -11.336 42.095 1.00 69.11 ? 374 ARG   B NH1  1 
ATOM   2782 N  NH2  . ARG   B 1 110 ? 17.410  -9.304  42.396 1.00 79.45 ? 374 ARG   B NH2  1 
ATOM   2783 N  N    . THR   B 1 111 ? 14.650  -11.914 49.716 1.00 25.14 ? 375 THR   B N    1 
ATOM   2784 C  CA   . THR   B 1 111 ? 14.176  -13.033 50.502 1.00 24.09 ? 375 THR   B CA   1 
ATOM   2785 C  C    . THR   B 1 111 ? 12.672  -13.212 50.340 1.00 23.29 ? 375 THR   B C    1 
ATOM   2786 O  O    . THR   B 1 111 ? 11.935  -12.288 49.941 1.00 22.94 ? 375 THR   B O    1 
ATOM   2787 C  CB   . THR   B 1 111 ? 14.466  -12.851 52.013 1.00 27.29 ? 375 THR   B CB   1 
ATOM   2788 O  OG1  . THR   B 1 111 ? 13.861  -11.620 52.457 1.00 28.38 ? 375 THR   B OG1  1 
ATOM   2789 C  CG2  . THR   B 1 111 ? 15.971  -12.823 52.283 1.00 28.54 ? 375 THR   B CG2  1 
ATOM   2790 N  N    . VAL   B 1 112 ? 12.206  -14.425 50.628 1.00 21.42 ? 376 VAL   B N    1 
ATOM   2791 C  CA   . VAL   B 1 112 ? 10.780  -14.714 50.567 1.00 22.58 ? 376 VAL   B CA   1 
ATOM   2792 C  C    . VAL   B 1 112 ? 10.356  -15.322 51.897 1.00 23.61 ? 376 VAL   B C    1 
ATOM   2793 O  O    . VAL   B 1 112 ? 11.127  -16.023 52.519 1.00 22.56 ? 376 VAL   B O    1 
ATOM   2794 C  CB   . VAL   B 1 112 ? 10.460  -15.634 49.410 1.00 20.58 ? 376 VAL   B CB   1 
ATOM   2795 C  CG1  . VAL   B 1 112 ? 10.889  -17.040 49.719 1.00 24.35 ? 376 VAL   B CG1  1 
ATOM   2796 C  CG2  . VAL   B 1 112 ? 8.922   -15.591 49.053 1.00 20.27 ? 376 VAL   B CG2  1 
ATOM   2797 N  N    . PHE   B 1 113 ? 9.142   -15.022 52.325 1.00 21.10 ? 377 PHE   B N    1 
ATOM   2798 C  CA   . PHE   B 1 113 ? 8.624   -15.574 53.584 1.00 22.54 ? 377 PHE   B CA   1 
ATOM   2799 C  C    . PHE   B 1 113 ? 8.326   -17.051 53.342 1.00 25.02 ? 377 PHE   B C    1 
ATOM   2800 O  O    . PHE   B 1 113 ? 7.558   -17.386 52.445 1.00 25.77 ? 377 PHE   B O    1 
ATOM   2801 C  CB   . PHE   B 1 113 ? 7.359   -14.820 54.027 1.00 21.82 ? 377 PHE   B CB   1 
ATOM   2802 C  CG   . PHE   B 1 113 ? 6.874   -15.169 55.410 1.00 23.66 ? 377 PHE   B CG   1 
ATOM   2803 C  CD1  . PHE   B 1 113 ? 7.561   -14.781 56.533 1.00 27.03 ? 377 PHE   B CD1  1 
ATOM   2804 C  CD2  . PHE   B 1 113 ? 5.666   -15.823 55.567 1.00 33.09 ? 377 PHE   B CD2  1 
ATOM   2805 C  CE1  . PHE   B 1 113 ? 7.084   -15.086 57.791 1.00 27.56 ? 377 PHE   B CE1  1 
ATOM   2806 C  CE2  . PHE   B 1 113 ? 5.179   -16.115 56.835 1.00 32.29 ? 377 PHE   B CE2  1 
ATOM   2807 C  CZ   . PHE   B 1 113 ? 5.884   -15.751 57.933 1.00 32.99 ? 377 PHE   B CZ   1 
ATOM   2808 N  N    . PHE   B 1 114 ? 8.919   -17.922 54.147 1.00 20.09 ? 378 PHE   B N    1 
ATOM   2809 C  CA   . PHE   B 1 114 ? 8.726   -19.368 53.985 1.00 23.12 ? 378 PHE   B CA   1 
ATOM   2810 C  C    . PHE   B 1 114 ? 8.796   -20.041 55.359 1.00 19.46 ? 378 PHE   B C    1 
ATOM   2811 O  O    . PHE   B 1 114 ? 9.800   -19.928 56.055 1.00 22.93 ? 378 PHE   B O    1 
ATOM   2812 C  CB   . PHE   B 1 114 ? 9.801   -19.916 53.048 1.00 20.28 ? 378 PHE   B CB   1 
ATOM   2813 C  CG   . PHE   B 1 114 ? 9.743   -21.423 52.838 1.00 19.29 ? 378 PHE   B CG   1 
ATOM   2814 C  CD1  . PHE   B 1 114 ? 8.891   -21.945 51.900 1.00 23.86 ? 378 PHE   B CD1  1 
ATOM   2815 C  CD2  . PHE   B 1 114 ? 10.605  -22.284 53.521 1.00 19.28 ? 378 PHE   B CD2  1 
ATOM   2816 C  CE1  . PHE   B 1 114 ? 8.830   -23.303 51.662 1.00 21.64 ? 378 PHE   B CE1  1 
ATOM   2817 C  CE2  . PHE   B 1 114 ? 10.554  -23.683 53.260 1.00 22.13 ? 378 PHE   B CE2  1 
ATOM   2818 C  CZ   . PHE   B 1 114 ? 9.667   -24.166 52.332 1.00 22.86 ? 378 PHE   B CZ   1 
ATOM   2819 N  N    . GLU   B 1 115 ? 7.739   -20.755 55.732 1.00 20.95 ? 379 GLU   B N    1 
ATOM   2820 C  CA   . GLU   B 1 115 ? 7.741   -21.478 57.000 1.00 21.95 ? 379 GLU   B CA   1 
ATOM   2821 C  C    . GLU   B 1 115 ? 8.167   -20.594 58.175 1.00 26.80 ? 379 GLU   B C    1 
ATOM   2822 O  O    . GLU   B 1 115 ? 8.962   -21.001 59.043 1.00 25.74 ? 379 GLU   B O    1 
ATOM   2823 C  CB   . GLU   B 1 115 ? 8.598   -22.773 56.879 1.00 19.35 ? 379 GLU   B CB   1 
ATOM   2824 C  CG   . GLU   B 1 115 ? 8.028   -23.709 55.815 1.00 20.08 ? 379 GLU   B CG   1 
ATOM   2825 C  CD   . GLU   B 1 115 ? 8.629   -25.118 55.763 1.00 23.64 ? 379 GLU   B CD   1 
ATOM   2826 O  OE1  . GLU   B 1 115 ? 9.720   -25.356 56.334 1.00 24.77 ? 379 GLU   B OE1  1 
ATOM   2827 O  OE2  . GLU   B 1 115 ? 7.995   -26.005 55.161 1.00 22.22 ? 379 GLU   B OE2  1 
ATOM   2828 N  N    . GLY   B 1 116 ? 7.609   -19.374 58.216 1.00 25.15 ? 380 GLY   B N    1 
ATOM   2829 C  CA   . GLY   B 1 116 ? 7.737   -18.552 59.415 1.00 26.06 ? 380 GLY   B CA   1 
ATOM   2830 C  C    . GLY   B 1 116 ? 8.807   -17.479 59.452 1.00 24.94 ? 380 GLY   B C    1 
ATOM   2831 O  O    . GLY   B 1 116 ? 8.773   -16.613 60.332 1.00 25.96 ? 380 GLY   B O    1 
ATOM   2832 N  N    . LYS   B 1 117 ? 9.758   -17.544 58.518 1.00 23.60 ? 381 LYS   B N    1 
ATOM   2833 C  CA   . LYS   B 1 117 ? 10.801  -16.540 58.430 1.00 25.72 ? 381 LYS   B CA   1 
ATOM   2834 C  C    . LYS   B 1 117 ? 11.129  -16.252 56.970 1.00 23.05 ? 381 LYS   B C    1 
ATOM   2835 O  O    . LYS   B 1 117 ? 10.736  -16.970 56.066 1.00 22.58 ? 381 LYS   B O    1 
ATOM   2836 C  CB   . LYS   B 1 117 ? 12.062  -16.990 59.185 1.00 26.44 ? 381 LYS   B CB   1 
ATOM   2837 C  CG   . LYS   B 1 117 ? 11.813  -17.377 60.635 1.00 27.95 ? 381 LYS   B CG   1 
ATOM   2838 C  CD   . LYS   B 1 117 ? 13.171  -17.619 61.312 1.00 31.71 ? 381 LYS   B CD   1 
ATOM   2839 C  CE   . LYS   B 1 117 ? 13.042  -18.157 62.742 1.00 34.60 ? 381 LYS   B CE   1 
ATOM   2840 N  NZ   . LYS   B 1 117 ? 14.423  -18.071 63.353 1.00 37.27 ? 381 LYS   B NZ   1 
ATOM   2841 N  N    . TYR   B 1 118 ? 11.864  -15.179 56.745 1.00 21.79 ? 382 TYR   B N    1 
ATOM   2842 C  CA   . TYR   B 1 118 ? 12.365  -14.874 55.405 1.00 22.21 ? 382 TYR   B CA   1 
ATOM   2843 C  C    . TYR   B 1 118 ? 13.640  -15.573 55.066 1.00 23.08 ? 382 TYR   B C    1 
ATOM   2844 O  O    . TYR   B 1 118 ? 14.566  -15.648 55.874 1.00 25.54 ? 382 TYR   B O    1 
ATOM   2845 C  CB   . TYR   B 1 118 ? 12.567  -13.345 55.252 1.00 23.62 ? 382 TYR   B CB   1 
ATOM   2846 C  CG   . TYR   B 1 118 ? 11.239  -12.644 55.017 1.00 26.33 ? 382 TYR   B CG   1 
ATOM   2847 C  CD1  . TYR   B 1 118 ? 10.377  -12.333 56.081 1.00 22.58 ? 382 TYR   B CD1  1 
ATOM   2848 C  CD2  . TYR   B 1 118 ? 10.843  -12.288 53.713 1.00 21.23 ? 382 TYR   B CD2  1 
ATOM   2849 C  CE1  . TYR   B 1 118 ? 9.144   -11.725 55.853 1.00 27.34 ? 382 TYR   B CE1  1 
ATOM   2850 C  CE2  . TYR   B 1 118 ? 9.619   -11.699 53.481 1.00 23.19 ? 382 TYR   B CE2  1 
ATOM   2851 C  CZ   . TYR   B 1 118 ? 8.766   -11.421 54.534 1.00 22.95 ? 382 TYR   B CZ   1 
ATOM   2852 O  OH   . TYR   B 1 118 ? 7.588   -10.809 54.274 1.00 25.86 ? 382 TYR   B OH   1 
ATOM   2853 N  N    . GLY   B 1 119 ? 13.726  -16.068 53.849 1.00 21.92 ? 383 GLY   B N    1 
ATOM   2854 C  CA   . GLY   B 1 119 ? 14.926  -16.744 53.401 1.00 26.26 ? 383 GLY   B CA   1 
ATOM   2855 C  C    . GLY   B 1 119 ? 15.244  -16.452 51.945 1.00 25.46 ? 383 GLY   B C    1 
ATOM   2856 O  O    . GLY   B 1 119 ? 14.342  -16.203 51.166 1.00 23.45 ? 383 GLY   B O    1 
ATOM   2857 N  N    . GLY   B 1 120 ? 16.520  -16.486 51.586 1.00 24.51 ? 384 GLY   B N    1 
ATOM   2858 C  CA   . GLY   B 1 120 ? 16.900  -16.293 50.196 1.00 24.94 ? 384 GLY   B CA   1 
ATOM   2859 C  C    . GLY   B 1 120 ? 16.800  -17.560 49.357 1.00 25.53 ? 384 GLY   B C    1 
ATOM   2860 O  O    . GLY   B 1 120 ? 16.435  -18.624 49.860 1.00 25.17 ? 384 GLY   B O    1 
ATOM   2861 N  N    . MET   B 1 121 ? 17.134  -17.459 48.075 1.00 24.78 ? 385 MET   B N    1 
ATOM   2862 C  CA   . MET   B 1 121 ? 16.924  -18.604 47.216 1.00 23.33 ? 385 MET   B CA   1 
ATOM   2863 C  C    . MET   B 1 121 ? 17.811  -19.813 47.614 1.00 22.99 ? 385 MET   B C    1 
ATOM   2864 O  O    . MET   B 1 121 ? 17.435  -20.976 47.367 1.00 23.96 ? 385 MET   B O    1 
ATOM   2865 C  CB   . MET   B 1 121 ? 17.118  -18.189 45.756 1.00 27.26 ? 385 MET   B CB   1 
ATOM   2866 C  CG   . MET   B 1 121 ? 18.498  -17.747 45.407 1.00 32.94 ? 385 MET   B CG   1 
ATOM   2867 S  SD   . MET   B 1 121 ? 18.513  -17.359 43.639 1.00 39.32 ? 385 MET   B SD   1 
ATOM   2868 C  CE   . MET   B 1 121 ? 20.135  -16.670 43.490 1.00 34.39 ? 385 MET   B CE   1 
ATOM   2869 N  N    . GLU   B 1 122 ? 18.948  -19.562 48.268 1.00 21.59 ? 386 GLU   B N    1 
ATOM   2870 C  CA   . GLU   B 1 122 ? 19.816  -20.646 48.666 1.00 24.98 ? 386 GLU   B CA   1 
ATOM   2871 C  C    . GLU   B 1 122 ? 19.151  -21.560 49.692 1.00 26.89 ? 386 GLU   B C    1 
ATOM   2872 O  O    . GLU   B 1 122 ? 19.630  -22.681 49.890 1.00 25.77 ? 386 GLU   B O    1 
ATOM   2873 C  CB   . GLU   B 1 122 ? 21.144  -20.098 49.219 1.00 26.96 ? 386 GLU   B CB   1 
ATOM   2874 C  CG   . GLU   B 1 122 ? 21.050  -19.517 50.594 1.00 30.24 ? 386 GLU   B CG   1 
ATOM   2875 C  CD   . GLU   B 1 122 ? 20.711  -18.030 50.646 1.00 35.60 ? 386 GLU   B CD   1 
ATOM   2876 O  OE1  . GLU   B 1 122 ? 20.897  -17.475 51.758 1.00 37.28 ? 386 GLU   B OE1  1 
ATOM   2877 O  OE2  . GLU   B 1 122 ? 20.242  -17.418 49.630 1.00 34.59 ? 386 GLU   B OE2  1 
ATOM   2878 N  N    . LEU   B 1 123 ? 18.053  -21.122 50.315 1.00 24.92 ? 387 LEU   B N    1 
ATOM   2879 C  CA   . LEU   B 1 123 ? 17.350  -21.975 51.296 1.00 21.35 ? 387 LEU   B CA   1 
ATOM   2880 C  C    . LEU   B 1 123 ? 16.792  -23.233 50.619 1.00 25.02 ? 387 LEU   B C    1 
ATOM   2881 O  O    . LEU   B 1 123 ? 16.537  -24.236 51.277 1.00 27.03 ? 387 LEU   B O    1 
ATOM   2882 C  CB   . LEU   B 1 123 ? 16.171  -21.224 51.957 1.00 25.34 ? 387 LEU   B CB   1 
ATOM   2883 C  CG   . LEU   B 1 123 ? 15.667  -21.739 53.310 1.00 30.81 ? 387 LEU   B CG   1 
ATOM   2884 C  CD1  . LEU   B 1 123 ? 16.215  -20.895 54.408 1.00 33.54 ? 387 LEU   B CD1  1 
ATOM   2885 C  CD2  . LEU   B 1 123 ? 14.152  -21.629 53.379 1.00 35.22 ? 387 LEU   B CD2  1 
ATOM   2886 N  N    . PHE   B 1 124 ? 16.542  -23.160 49.309 1.00 21.02 ? 388 PHE   B N    1 
ATOM   2887 C  CA   . PHE   B 1 124 ? 15.826  -24.224 48.611 1.00 20.56 ? 388 PHE   B CA   1 
ATOM   2888 C  C    . PHE   B 1 124 ? 16.673  -25.134 47.776 1.00 22.12 ? 388 PHE   B C    1 
ATOM   2889 O  O    . PHE   B 1 124 ? 16.165  -25.896 46.969 1.00 22.82 ? 388 PHE   B O    1 
ATOM   2890 C  CB   . PHE   B 1 124 ? 14.733  -23.572 47.730 1.00 21.14 ? 388 PHE   B CB   1 
ATOM   2891 C  CG   . PHE   B 1 124 ? 13.846  -22.663 48.486 1.00 23.12 ? 388 PHE   B CG   1 
ATOM   2892 C  CD1  . PHE   B 1 124 ? 12.879  -23.201 49.323 1.00 19.40 ? 388 PHE   B CD1  1 
ATOM   2893 C  CD2  . PHE   B 1 124 ? 14.012  -21.272 48.412 1.00 21.49 ? 388 PHE   B CD2  1 
ATOM   2894 C  CE1  . PHE   B 1 124 ? 12.040  -22.367 50.058 1.00 20.07 ? 388 PHE   B CE1  1 
ATOM   2895 C  CE2  . PHE   B 1 124 ? 13.163  -20.410 49.159 1.00 22.87 ? 388 PHE   B CE2  1 
ATOM   2896 C  CZ   . PHE   B 1 124 ? 12.187  -20.970 49.983 1.00 19.67 ? 388 PHE   B CZ   1 
ATOM   2897 N  N    . ARG   B 1 125 ? 17.997  -25.109 47.991 1.00 21.37 ? 389 ARG   B N    1 
ATOM   2898 C  CA   . ARG   B 1 125 ? 18.900  -25.884 47.134 1.00 22.26 ? 389 ARG   B CA   1 
ATOM   2899 C  C    . ARG   B 1 125 ? 18.624  -27.392 47.166 1.00 21.25 ? 389 ARG   B C    1 
ATOM   2900 O  O    . ARG   B 1 125 ? 18.861  -28.084 46.168 1.00 24.25 ? 389 ARG   B O    1 
ATOM   2901 C  CB   . ARG   B 1 125 ? 20.354  -25.634 47.507 1.00 23.58 ? 389 ARG   B CB   1 
ATOM   2902 C  CG   . ARG   B 1 125 ? 20.802  -24.271 47.095 1.00 23.33 ? 389 ARG   B CG   1 
ATOM   2903 C  CD   . ARG   B 1 125 ? 22.236  -24.094 47.369 1.00 24.65 ? 389 ARG   B CD   1 
ATOM   2904 N  NE   . ARG   B 1 125 ? 22.613  -22.711 47.061 1.00 26.41 ? 389 ARG   B NE   1 
ATOM   2905 C  CZ   . ARG   B 1 125 ? 23.814  -22.211 47.341 1.00 25.55 ? 389 ARG   B CZ   1 
ATOM   2906 N  NH1  . ARG   B 1 125 ? 24.133  -20.952 47.074 1.00 26.28 ? 389 ARG   B NH1  1 
ATOM   2907 N  NH2  . ARG   B 1 125 ? 24.738  -22.996 47.885 1.00 27.26 ? 389 ARG   B NH2  1 
ATOM   2908 N  N    . ALA   B 1 126 ? 18.107  -27.925 48.285 1.00 20.26 ? 390 ALA   B N    1 
ATOM   2909 C  CA   . ALA   B 1 126 ? 17.881  -29.378 48.342 1.00 23.13 ? 390 ALA   B CA   1 
ATOM   2910 C  C    . ALA   B 1 126 ? 16.785  -29.871 47.373 1.00 23.59 ? 390 ALA   B C    1 
ATOM   2911 O  O    . ALA   B 1 126 ? 16.745  -31.070 47.071 1.00 24.32 ? 390 ALA   B O    1 
ATOM   2912 C  CB   . ALA   B 1 126 ? 17.523  -29.810 49.762 1.00 27.78 ? 390 ALA   B CB   1 
ATOM   2913 N  N    . LEU   B 1 127 ? 15.943  -28.959 46.876 1.00 24.50 ? 391 LEU   B N    1 
ATOM   2914 C  CA   . LEU   B 1 127 ? 14.934  -29.338 45.893 1.00 22.67 ? 391 LEU   B CA   1 
ATOM   2915 C  C    . LEU   B 1 127 ? 15.564  -29.703 44.571 1.00 24.57 ? 391 LEU   B C    1 
ATOM   2916 O  O    . LEU   B 1 127 ? 14.963  -30.411 43.788 1.00 23.81 ? 391 LEU   B O    1 
ATOM   2917 C  CB   . LEU   B 1 127 ? 13.914  -28.204 45.656 1.00 24.02 ? 391 LEU   B CB   1 
ATOM   2918 C  CG   . LEU   B 1 127 ? 13.001  -27.906 46.817 1.00 24.88 ? 391 LEU   B CG   1 
ATOM   2919 C  CD1  . LEU   B 1 127 ? 12.255  -26.610 46.510 1.00 25.86 ? 391 LEU   B CD1  1 
ATOM   2920 C  CD2  . LEU   B 1 127 ? 12.002  -29.092 46.982 1.00 22.79 ? 391 LEU   B CD2  1 
ATOM   2921 N  N    . GLY   B 1 128 ? 16.804  -29.250 44.323 1.00 22.18 ? 392 GLY   B N    1 
ATOM   2922 C  CA   . GLY   B 1 128 ? 17.425  -29.603 43.071 1.00 25.58 ? 392 GLY   B CA   1 
ATOM   2923 C  C    . GLY   B 1 128 ? 16.908  -28.977 41.816 1.00 27.94 ? 392 GLY   B C    1 
ATOM   2924 O  O    . GLY   B 1 128 ? 16.981  -29.578 40.727 1.00 31.64 ? 392 GLY   B O    1 
ATOM   2925 N  N    . CYS   B 1 129 ? 16.374  -27.777 41.947 1.00 27.44 ? 393 CYS   B N    1 
ATOM   2926 C  CA   . CYS   B 1 129 ? 15.844  -27.052 40.782 1.00 27.01 ? 393 CYS   B CA   1 
ATOM   2927 C  C    . CYS   B 1 129 ? 16.162  -25.573 40.946 1.00 23.92 ? 393 CYS   B C    1 
ATOM   2928 O  O    . CYS   B 1 129 ? 15.274  -24.725 40.971 1.00 24.86 ? 393 CYS   B O    1 
ATOM   2929 C  CB   . CYS   B 1 129 ? 14.328  -27.293 40.598 1.00 28.75 ? 393 CYS   B CB   1 
ATOM   2930 S  SG   . CYS   B 1 129 ? 13.282  -27.091 42.083 1.00 27.26 ? 393 CYS   B SG   1 
ATOM   2931 N  N    . SER   B 1 130 ? 17.464  -25.287 41.079 1.00 32.53 ? 394 SER   B N    1 
ATOM   2932 C  CA   . SER   B 1 130 ? 17.952  -23.929 41.290 1.00 33.10 ? 394 SER   B CA   1 
ATOM   2933 C  C    . SER   B 1 130 ? 17.491  -22.939 40.262 1.00 24.15 ? 394 SER   B C    1 
ATOM   2934 O  O    . SER   B 1 130 ? 17.179  -21.777 40.589 1.00 29.85 ? 394 SER   B O    1 
ATOM   2935 C  CB   . SER   B 1 130 ? 19.479  -23.901 41.234 1.00 44.26 ? 394 SER   B CB   1 
ATOM   2936 O  OG   . SER   B 1 130 ? 19.880  -23.992 39.877 1.00 56.22 ? 394 SER   B OG   1 
ATOM   2937 N  N    . GLU   B 1 131 ? 17.536  -23.372 39.007 1.00 25.41 ? 395 GLU   B N    1 
ATOM   2938 C  CA   . GLU   B 1 131 ? 17.171  -22.477 37.924 1.00 31.46 ? 395 GLU   B CA   1 
ATOM   2939 C  C    . GLU   B 1 131 ? 15.716  -22.012 38.139 1.00 30.15 ? 395 GLU   B C    1 
ATOM   2940 O  O    . GLU   B 1 131 ? 15.404  -20.812 38.043 1.00 28.58 ? 395 GLU   B O    1 
ATOM   2941 C  CB   . GLU   B 1 131 ? 17.327  -23.159 36.559 1.00 42.98 ? 395 GLU   B CB   1 
ATOM   2942 C  CG   . GLU   B 1 131 ? 16.978  -22.256 35.370 1.00 57.81 ? 395 GLU   B CG   1 
ATOM   2943 C  CD   . GLU   B 1 131 ? 17.677  -22.648 34.059 1.00 71.88 ? 395 GLU   B CD   1 
ATOM   2944 O  OE1  . GLU   B 1 131 ? 17.919  -23.859 33.833 1.00 76.03 ? 395 GLU   B OE1  1 
ATOM   2945 O  OE2  . GLU   B 1 131 ? 17.976  -21.732 33.249 1.00 74.44 ? 395 GLU   B OE2  1 
ATOM   2946 N  N    . LEU   B 1 132 ? 14.829  -22.959 38.436 1.00 28.20 ? 396 LEU   B N    1 
ATOM   2947 C  CA   . LEU   B 1 132 ? 13.409  -22.610 38.634 1.00 25.08 ? 396 LEU   B CA   1 
ATOM   2948 C  C    . LEU   B 1 132 ? 13.229  -21.672 39.850 1.00 22.78 ? 396 LEU   B C    1 
ATOM   2949 O  O    . LEU   B 1 132 ? 12.457  -20.702 39.811 1.00 23.13 ? 396 LEU   B O    1 
ATOM   2950 C  CB   . LEU   B 1 132 ? 12.539  -23.879 38.813 1.00 26.63 ? 396 LEU   B CB   1 
ATOM   2951 C  CG   . LEU   B 1 132 ? 11.077  -23.728 39.260 1.00 28.89 ? 396 LEU   B CG   1 
ATOM   2952 C  CD1  . LEU   B 1 132 ? 10.297  -22.831 38.330 1.00 27.26 ? 396 LEU   B CD1  1 
ATOM   2953 C  CD2  . LEU   B 1 132 ? 10.471  -25.133 39.313 1.00 26.63 ? 396 LEU   B CD2  1 
ATOM   2954 N  N    . ILE   B 1 133 ? 13.924  -21.985 40.936 1.00 21.64 ? 397 ILE   B N    1 
ATOM   2955 C  CA   . ILE   B 1 133 ? 13.839  -21.193 42.137 1.00 20.79 ? 397 ILE   B CA   1 
ATOM   2956 C  C    . ILE   B 1 133 ? 14.291  -19.757 41.822 1.00 23.66 ? 397 ILE   B C    1 
ATOM   2957 O  O    . ILE   B 1 133 ? 13.623  -18.772 42.210 1.00 20.59 ? 397 ILE   B O    1 
ATOM   2958 C  CB   . ILE   B 1 133 ? 14.662  -21.789 43.299 1.00 25.18 ? 397 ILE   B CB   1 
ATOM   2959 C  CG1  . ILE   B 1 133 ? 14.122  -23.173 43.719 1.00 26.45 ? 397 ILE   B CG1  1 
ATOM   2960 C  CG2  . ILE   B 1 133 ? 14.639  -20.823 44.500 1.00 24.26 ? 397 ILE   B CG2  1 
ATOM   2961 C  CD1  . ILE   B 1 133 ? 12.668  -23.131 44.214 1.00 25.04 ? 397 ILE   B CD1  1 
ATOM   2962 N  N    . SER   B 1 134 ? 15.444  -19.622 41.172 1.00 22.81 ? 398 SER   B N    1 
ATOM   2963 C  CA   . SER   B 1 134 ? 15.906  -18.254 40.836 1.00 21.23 ? 398 SER   B CA   1 
ATOM   2964 C  C    . SER   B 1 134 ? 14.828  -17.556 39.932 1.00 29.15 ? 398 SER   B C    1 
ATOM   2965 O  O    . SER   B 1 134 ? 14.568  -16.362 40.104 1.00 26.19 ? 398 SER   B O    1 
ATOM   2966 C  CB   . SER   B 1 134 ? 17.313  -18.281 40.186 1.00 32.10 ? 398 SER   B CB   1 
ATOM   2967 O  OG   . SER   B 1 134 ? 17.236  -18.663 38.834 1.00 50.19 ? 398 SER   B OG   1 
ATOM   2968 N  N    . SER   B 1 135 ? 14.162  -18.305 39.034 1.00 26.69 ? 399 SER   B N    1 
ATOM   2969 C  CA   . SER   B 1 135 ? 13.097  -17.742 38.184 1.00 24.84 ? 399 SER   B CA   1 
ATOM   2970 C  C    . SER   B 1 135 ? 11.905  -17.209 38.977 1.00 23.12 ? 399 SER   B C    1 
ATOM   2971 O  O    . SER   B 1 135 ? 11.373  -16.147 38.656 1.00 25.68 ? 399 SER   B O    1 
ATOM   2972 C  CB   . SER   B 1 135 ? 12.583  -18.781 37.179 1.00 31.81 ? 399 SER   B CB   1 
ATOM   2973 O  OG   . SER   B 1 135 ? 13.574  -19.078 36.207 1.00 38.44 ? 399 SER   B OG   1 
ATOM   2974 N  N    . ILE   B 1 136 ? 11.511  -17.929 40.015 1.00 21.82 ? 400 ILE   B N    1 
ATOM   2975 C  CA   . ILE   B 1 136 ? 10.425  -17.503 40.892 1.00 19.05 ? 400 ILE   B CA   1 
ATOM   2976 C  C    . ILE   B 1 136 ? 10.834  -16.215 41.608 1.00 22.33 ? 400 ILE   B C    1 
ATOM   2977 O  O    . ILE   B 1 136 ? 10.089  -15.271 41.664 1.00 24.74 ? 400 ILE   B O    1 
ATOM   2978 C  CB   . ILE   B 1 136 ? 10.063  -18.610 41.898 1.00 21.44 ? 400 ILE   B CB   1 
ATOM   2979 C  CG1  . ILE   B 1 136 ? 9.483   -19.849 41.213 1.00 24.26 ? 400 ILE   B CG1  1 
ATOM   2980 C  CG2  . ILE   B 1 136 ? 9.136   -18.082 42.967 1.00 23.43 ? 400 ILE   B CG2  1 
ATOM   2981 C  CD1  . ILE   B 1 136 ? 9.486   -21.023 42.156 1.00 27.42 ? 400 ILE   B CD1  1 
ATOM   2982 N  N    . PHE   B 1 137 ? 12.068  -16.177 42.128 1.00 22.67 ? 401 PHE   B N    1 
ATOM   2983 C  CA   . PHE   B 1 137 ? 12.570  -14.965 42.793 1.00 22.01 ? 401 PHE   B CA   1 
ATOM   2984 C  C    . PHE   B 1 137 ? 12.618  -13.777 41.842 1.00 22.47 ? 401 PHE   B C    1 
ATOM   2985 O  O    . PHE   B 1 137 ? 12.258  -12.651 42.231 1.00 25.16 ? 401 PHE   B O    1 
ATOM   2986 C  CB   . PHE   B 1 137 ? 13.953  -15.222 43.408 1.00 22.03 ? 401 PHE   B CB   1 
ATOM   2987 C  CG   . PHE   B 1 137 ? 13.872  -15.832 44.765 1.00 23.08 ? 401 PHE   B CG   1 
ATOM   2988 C  CD1  . PHE   B 1 137 ? 13.322  -17.111 44.942 1.00 21.54 ? 401 PHE   B CD1  1 
ATOM   2989 C  CD2  . PHE   B 1 137 ? 14.295  -15.124 45.880 1.00 26.37 ? 401 PHE   B CD2  1 
ATOM   2990 C  CE1  . PHE   B 1 137 ? 13.240  -17.680 46.205 1.00 23.78 ? 401 PHE   B CE1  1 
ATOM   2991 C  CE2  . PHE   B 1 137 ? 14.200  -15.683 47.143 1.00 27.81 ? 401 PHE   B CE2  1 
ATOM   2992 C  CZ   . PHE   B 1 137 ? 13.671  -16.963 47.311 1.00 25.67 ? 401 PHE   B CZ   1 
ATOM   2993 N  N    . ASP   B 1 138 ? 13.089  -13.998 40.614 1.00 24.31 ? 402 ASP   B N    1 
ATOM   2994 C  CA   . ASP   B 1 138 ? 13.162  -12.925 39.641 1.00 27.08 ? 402 ASP   B CA   1 
ATOM   2995 C  C    . ASP   B 1 138 ? 11.775  -12.396 39.281 1.00 27.19 ? 402 ASP   B C    1 
ATOM   2996 O  O    . ASP   B 1 138 ? 11.630  -11.188 39.045 1.00 26.47 ? 402 ASP   B O    1 
ATOM   2997 C  CB   . ASP   B 1 138 ? 13.874  -13.380 38.370 1.00 28.96 ? 402 ASP   B CB   1 
ATOM   2998 C  CG   . ASP   B 1 138 ? 15.351  -13.654 38.597 1.00 45.15 ? 402 ASP   B CG   1 
ATOM   2999 O  OD1  . ASP   B 1 138 ? 15.930  -13.249 39.643 1.00 51.57 ? 402 ASP   B OD1  1 
ATOM   3000 O  OD2  . ASP   B 1 138 ? 15.929  -14.281 37.706 1.00 43.59 ? 402 ASP   B OD2  1 
ATOM   3001 N  N    . PHE   B 1 139 ? 10.793  -13.283 39.208 1.00 26.86 ? 403 PHE   B N    1 
ATOM   3002 C  CA   . PHE   B 1 139 ? 9.432   -12.859 38.865 1.00 25.17 ? 403 PHE   B CA   1 
ATOM   3003 C  C    . PHE   B 1 139 ? 8.882   -11.975 39.973 1.00 26.74 ? 403 PHE   B C    1 
ATOM   3004 O  O    . PHE   B 1 139 ? 8.336   -10.872 39.723 1.00 26.76 ? 403 PHE   B O    1 
ATOM   3005 C  CB   . PHE   B 1 139 ? 8.510   -14.047 38.660 1.00 23.08 ? 403 PHE   B CB   1 
ATOM   3006 C  CG   . PHE   B 1 139 ? 7.126   -13.641 38.242 1.00 22.58 ? 403 PHE   B CG   1 
ATOM   3007 C  CD1  . PHE   B 1 139 ? 6.946   -13.023 37.023 1.00 27.61 ? 403 PHE   B CD1  1 
ATOM   3008 C  CD2  . PHE   B 1 139 ? 6.048   -13.857 39.054 1.00 26.58 ? 403 PHE   B CD2  1 
ATOM   3009 C  CE1  . PHE   B 1 139 ? 5.706   -12.601 36.625 1.00 26.63 ? 403 PHE   B CE1  1 
ATOM   3010 C  CE2  . PHE   B 1 139 ? 4.792   -13.456 38.649 1.00 29.57 ? 403 PHE   B CE2  1 
ATOM   3011 C  CZ   . PHE   B 1 139 ? 4.634   -12.826 37.435 1.00 29.13 ? 403 PHE   B CZ   1 
ATOM   3012 N  N    . SER   B 1 140 ? 9.050   -12.440 41.209 1.00 23.37 ? 404 SER   B N    1 
ATOM   3013 C  CA   . SER   B 1 140 ? 8.586   -11.672 42.362 1.00 22.15 ? 404 SER   B CA   1 
ATOM   3014 C  C    . SER   B 1 140 ? 9.283   -10.339 42.386 1.00 21.58 ? 404 SER   B C    1 
ATOM   3015 O  O    . SER   B 1 140 ? 8.683   -9.316  42.691 1.00 23.82 ? 404 SER   B O    1 
ATOM   3016 C  CB   . SER   B 1 140 ? 8.859   -12.404 43.651 1.00 26.13 ? 404 SER   B CB   1 
ATOM   3017 O  OG   . SER   B 1 140 ? 8.110   -13.599 43.655 1.00 36.33 ? 404 SER   B OG   1 
ATOM   3018 N  N    . HIS   B 1 141 ? 10.585  -10.346 42.133 1.00 23.65 ? 405 HIS   B N    1 
ATOM   3019 C  CA   . HIS   B 1 141 ? 11.324  -9.117  42.178 1.00 23.93 ? 405 HIS   B CA   1 
ATOM   3020 C  C    . HIS   B 1 141 ? 10.743  -8.120  41.182 1.00 26.99 ? 405 HIS   B C    1 
ATOM   3021 O  O    . HIS   B 1 141 ? 10.599  -6.937  41.499 1.00 27.01 ? 405 HIS   B O    1 
ATOM   3022 C  CB   . HIS   B 1 141 ? 12.808  -9.376  41.903 1.00 26.61 ? 405 HIS   B CB   1 
ATOM   3023 C  CG   . HIS   B 1 141 ? 13.693  -8.245  42.313 1.00 30.47 ? 405 HIS   B CG   1 
ATOM   3024 N  ND1  . HIS   B 1 141 ? 14.267  -8.167  43.564 1.00 30.03 ? 405 HIS   B ND1  1 
ATOM   3025 C  CD2  . HIS   B 1 141 ? 14.119  -7.153  41.633 1.00 36.54 ? 405 HIS   B CD2  1 
ATOM   3026 C  CE1  . HIS   B 1 141 ? 14.998  -7.068  43.640 1.00 33.92 ? 405 HIS   B CE1  1 
ATOM   3027 N  NE2  . HIS   B 1 141 ? 14.927  -6.438  42.481 1.00 35.98 ? 405 HIS   B NE2  1 
ATOM   3028 N  N    . SER   B 1 142 ? 10.364  -8.599  39.995 1.00 27.93 ? 406 SER   B N    1 
ATOM   3029 C  CA   . SER   B 1 142 ? 9.846   -7.701  38.971 1.00 24.21 ? 406 SER   B CA   1 
ATOM   3030 C  C    . SER   B 1 142 ? 8.532   -7.072  39.406 1.00 27.92 ? 406 SER   B C    1 
ATOM   3031 O  O    . SER   B 1 142 ? 8.282   -5.907  39.120 1.00 29.57 ? 406 SER   B O    1 
ATOM   3032 C  CB   . SER   B 1 142 ? 9.657   -8.428  37.645 1.00 29.67 ? 406 SER   B CB   1 
ATOM   3033 O  OG   . SER   B 1 142 ? 8.560   -9.325  37.716 1.00 38.72 ? 406 SER   B OG   1 
ATOM   3034 N  N    . LEU   B 1 143 ? 7.689   -7.842  40.085 1.00 27.52 ? 407 LEU   B N    1 
ATOM   3035 C  CA   . LEU   B 1 143 ? 6.430   -7.332  40.595 1.00 27.63 ? 407 LEU   B CA   1 
ATOM   3036 C  C    . LEU   B 1 143 ? 6.599   -6.387  41.771 1.00 31.98 ? 407 LEU   B C    1 
ATOM   3037 O  O    . LEU   B 1 143 ? 5.764   -5.528  42.008 1.00 29.37 ? 407 LEU   B O    1 
ATOM   3038 C  CB   . LEU   B 1 143 ? 5.512   -8.501  40.996 1.00 28.63 ? 407 LEU   B CB   1 
ATOM   3039 C  CG   . LEU   B 1 143 ? 4.944   -9.339  39.864 1.00 29.71 ? 407 LEU   B CG   1 
ATOM   3040 C  CD1  . LEU   B 1 143 ? 3.980   -10.429 40.429 1.00 27.92 ? 407 LEU   B CD1  1 
ATOM   3041 C  CD2  . LEU   B 1 143 ? 4.207   -8.506  38.841 1.00 32.57 ? 407 LEU   B CD2  1 
ATOM   3042 N  N    . SER   B 1 144 ? 7.697   -6.532  42.499 1.00 27.63 ? 408 SER   B N    1 
ATOM   3043 C  CA   . SER   B 1 144 ? 7.874   -5.799  43.745 1.00 30.61 ? 408 SER   B CA   1 
ATOM   3044 C  C    . SER   B 1 144 ? 8.001   -4.307  43.455 1.00 32.90 ? 408 SER   B C    1 
ATOM   3045 O  O    . SER   B 1 144 ? 7.701   -3.462  44.306 1.00 30.80 ? 408 SER   B O    1 
ATOM   3046 C  CB   . SER   B 1 144 ? 9.096   -6.357  44.504 1.00 34.73 ? 408 SER   B CB   1 
ATOM   3047 O  OG   . SER   B 1 144 ? 10.308  -6.004  43.848 1.00 36.66 ? 408 SER   B OG   1 
ATOM   3048 N  N    . ALA   B 1 145 ? 8.435   -3.991  42.238 1.00 31.48 ? 409 ALA   B N    1 
ATOM   3049 C  CA   . ALA   B 1 145 ? 8.664   -2.622  41.820 1.00 37.08 ? 409 ALA   B CA   1 
ATOM   3050 C  C    . ALA   B 1 145 ? 7.386   -1.816  41.833 1.00 32.91 ? 409 ALA   B C    1 
ATOM   3051 O  O    . ALA   B 1 145 ? 7.412   -0.602  41.979 1.00 35.13 ? 409 ALA   B O    1 
ATOM   3052 C  CB   . ALA   B 1 145 ? 9.277   -2.598  40.420 1.00 40.29 ? 409 ALA   B CB   1 
ATOM   3053 N  N    . LEU   B 1 146 ? 6.261   -2.510  41.660 1.00 32.43 ? 410 LEU   B N    1 
ATOM   3054 C  CA   . LEU   B 1 146 ? 4.988   -1.847  41.480 1.00 29.10 ? 410 LEU   B CA   1 
ATOM   3055 C  C    . LEU   B 1 146 ? 4.390   -1.309  42.765 1.00 31.26 ? 410 LEU   B C    1 
ATOM   3056 O  O    . LEU   B 1 146 ? 3.527   -0.407  42.707 1.00 30.58 ? 410 LEU   B O    1 
ATOM   3057 C  CB   . LEU   B 1 146 ? 3.973   -2.798  40.848 1.00 33.73 ? 410 LEU   B CB   1 
ATOM   3058 C  CG   . LEU   B 1 146 ? 4.266   -3.401  39.471 1.00 44.43 ? 410 LEU   B CG   1 
ATOM   3059 C  CD1  . LEU   B 1 146 ? 2.925   -3.693  38.783 1.00 45.30 ? 410 LEU   B CD1  1 
ATOM   3060 C  CD2  . LEU   B 1 146 ? 5.113   -2.499  38.649 1.00 46.93 ? 410 LEU   B CD2  1 
ATOM   3061 N  N    . HIS   B 1 147 ? 4.833   -1.845  43.902 1.00 31.90 ? 411 HIS   B N    1 
ATOM   3062 C  CA   . HIS   B 1 147 ? 4.152   -1.610  45.173 1.00 28.50 ? 411 HIS   B CA   1 
ATOM   3063 C  C    . HIS   B 1 147 ? 2.624   -1.775  45.006 1.00 25.69 ? 411 HIS   B C    1 
ATOM   3064 O  O    . HIS   B 1 147 ? 1.841   -0.896  45.346 1.00 27.64 ? 411 HIS   B O    1 
ATOM   3065 C  CB   . HIS   B 1 147 ? 4.497   -0.203  45.716 1.00 29.64 ? 411 HIS   B CB   1 
ATOM   3066 C  CG   . HIS   B 1 147 ? 5.936   -0.026  46.124 1.00 39.92 ? 411 HIS   B CG   1 
ATOM   3067 N  ND1  . HIS   B 1 147 ? 6.989   -0.604  45.451 1.00 41.14 ? 411 HIS   B ND1  1 
ATOM   3068 C  CD2  . HIS   B 1 147 ? 6.490   0.713   47.117 1.00 43.58 ? 411 HIS   B CD2  1 
ATOM   3069 C  CE1  . HIS   B 1 147 ? 8.129   -0.251  46.022 1.00 43.28 ? 411 HIS   B CE1  1 
ATOM   3070 N  NE2  . HIS   B 1 147 ? 7.851   0.539   47.041 1.00 41.00 ? 411 HIS   B NE2  1 
ATOM   3071 N  N    . PHE   B 1 148 ? 2.188   -2.924  44.492 1.00 27.22 ? 412 PHE   B N    1 
ATOM   3072 C  CA   . PHE   B 1 148 ? 0.741   -3.193  44.380 1.00 26.43 ? 412 PHE   B CA   1 
ATOM   3073 C  C    . PHE   B 1 148 ? 0.028   -2.902  45.693 1.00 26.45 ? 412 PHE   B C    1 
ATOM   3074 O  O    . PHE   B 1 148 ? 0.480   -3.349  46.767 1.00 29.87 ? 412 PHE   B O    1 
ATOM   3075 C  CB   . PHE   B 1 148 ? 0.483   -4.670  44.073 1.00 27.63 ? 412 PHE   B CB   1 
ATOM   3076 C  CG   . PHE   B 1 148 ? 0.603   -5.074  42.636 1.00 30.67 ? 412 PHE   B CG   1 
ATOM   3077 C  CD1  . PHE   B 1 148 ? -0.003  -4.340  41.621 1.00 39.00 ? 412 PHE   B CD1  1 
ATOM   3078 C  CD2  . PHE   B 1 148 ? 1.266   -6.259  42.309 1.00 31.16 ? 412 PHE   B CD2  1 
ATOM   3079 C  CE1  . PHE   B 1 148 ? 0.080   -4.773  40.310 1.00 43.59 ? 412 PHE   B CE1  1 
ATOM   3080 C  CE2  . PHE   B 1 148 ? 1.345   -6.699  41.010 1.00 36.47 ? 412 PHE   B CE2  1 
ATOM   3081 C  CZ   . PHE   B 1 148 ? 0.753   -5.961  40.007 1.00 39.54 ? 412 PHE   B CZ   1 
ATOM   3082 N  N    . SER   B 1 149 ? -1.081  -2.182  45.631 1.00 23.78 ? 413 SER   B N    1 
ATOM   3083 C  CA   . SER   B 1 149 ? -1.975  -2.159  46.765 1.00 26.87 ? 413 SER   B CA   1 
ATOM   3084 C  C    . SER   B 1 149 ? -2.725  -3.487  46.817 1.00 26.02 ? 413 SER   B C    1 
ATOM   3085 O  O    . SER   B 1 149 ? -2.741  -4.247  45.836 1.00 26.57 ? 413 SER   B O    1 
ATOM   3086 C  CB   . SER   B 1 149 ? -2.939  -0.983  46.654 1.00 29.39 ? 413 SER   B CB   1 
ATOM   3087 O  OG   . SER   B 1 149 ? -3.894  -1.175  45.612 1.00 28.11 ? 413 SER   B OG   1 
ATOM   3088 N  N    . GLU   B 1 150 ? -3.386  -3.770  47.929 1.00 27.14 ? 414 GLU   B N    1 
ATOM   3089 C  CA   . GLU   B 1 150 ? -4.158  -5.019  47.965 1.00 25.71 ? 414 GLU   B CA   1 
ATOM   3090 C  C    . GLU   B 1 150 ? -5.316  -5.005  46.973 1.00 23.80 ? 414 GLU   B C    1 
ATOM   3091 O  O    . GLU   B 1 150 ? -5.686  -6.053  46.415 1.00 26.02 ? 414 GLU   B O    1 
ATOM   3092 C  CB   . GLU   B 1 150 ? -4.672  -5.289  49.370 1.00 29.64 ? 414 GLU   B CB   1 
ATOM   3093 C  CG   . GLU   B 1 150 ? -3.562  -5.620  50.349 1.00 31.51 ? 414 GLU   B CG   1 
ATOM   3094 C  CD   . GLU   B 1 150 ? -2.966  -7.005  50.112 1.00 34.50 ? 414 GLU   B CD   1 
ATOM   3095 O  OE1  . GLU   B 1 150 ? -3.532  -8.001  50.630 1.00 31.38 ? 414 GLU   B OE1  1 
ATOM   3096 O  OE2  . GLU   B 1 150 ? -1.937  -7.094  49.394 1.00 31.42 ? 414 GLU   B OE2  1 
ATOM   3097 N  N    . ASP   B 1 151 ? -5.906  -3.840  46.765 1.00 26.45 ? 415 ASP   B N    1 
ATOM   3098 C  CA   . ASP   B 1 151 ? -7.004  -3.731  45.813 1.00 24.69 ? 415 ASP   B CA   1 
ATOM   3099 C  C    . ASP   B 1 151 ? -6.460  -3.970  44.412 1.00 24.51 ? 415 ASP   B C    1 
ATOM   3100 O  O    . ASP   B 1 151 ? -7.108  -4.614  43.595 1.00 26.40 ? 415 ASP   B O    1 
ATOM   3101 C  CB   . ASP   B 1 151 ? -7.671  -2.349  45.869 1.00 27.24 ? 415 ASP   B CB   1 
ATOM   3102 C  CG   . ASP   B 1 151 ? -8.537  -2.144  47.095 1.00 36.87 ? 415 ASP   B CG   1 
ATOM   3103 O  OD1  . ASP   B 1 151 ? -8.838  -3.125  47.808 1.00 34.06 ? 415 ASP   B OD1  1 
ATOM   3104 O  OD2  . ASP   B 1 151 ? -8.927  -0.972  47.330 1.00 41.33 ? 415 ASP   B OD2  1 
ATOM   3105 N  N    . GLU   B 1 152 ? -5.282  -3.421  44.120 1.00 24.54 ? 416 GLU   B N    1 
ATOM   3106 C  CA   . GLU   B 1 152 ? -4.676  -3.622  42.796 1.00 23.96 ? 416 GLU   B CA   1 
ATOM   3107 C  C    . GLU   B 1 152 ? -4.344  -5.076  42.495 1.00 24.20 ? 416 GLU   B C    1 
ATOM   3108 O  O    . GLU   B 1 152 ? -4.624  -5.577  41.402 1.00 24.30 ? 416 GLU   B O    1 
ATOM   3109 C  CB   . GLU   B 1 152 ? -3.407  -2.776  42.650 1.00 23.52 ? 416 GLU   B CB   1 
ATOM   3110 C  CG   . GLU   B 1 152 ? -3.705  -1.279  42.474 1.00 26.23 ? 416 GLU   B CG   1 
ATOM   3111 C  CD   . GLU   B 1 152 ? -2.490  -0.395  42.681 1.00 25.19 ? 416 GLU   B CD   1 
ATOM   3112 O  OE1  . GLU   B 1 152 ? -1.403  -0.929  42.987 1.00 27.79 ? 416 GLU   B OE1  1 
ATOM   3113 O  OE2  . GLU   B 1 152 ? -2.624  0.833   42.499 1.00 28.15 ? 416 GLU   B OE2  1 
ATOM   3114 N  N    . ILE   B 1 153 ? -3.766  -5.770  43.465 1.00 22.87 ? 417 ILE   B N    1 
ATOM   3115 C  CA   . ILE   B 1 153 ? -3.421  -7.155  43.215 1.00 23.86 ? 417 ILE   B CA   1 
ATOM   3116 C  C    . ILE   B 1 153 ? -4.735  -8.017  43.087 1.00 22.16 ? 417 ILE   B C    1 
ATOM   3117 O  O    . ILE   B 1 153 ? -4.757  -8.979  42.320 1.00 22.62 ? 417 ILE   B O    1 
ATOM   3118 C  CB   . ILE   B 1 153 ? -2.416  -7.639  44.276 1.00 26.70 ? 417 ILE   B CB   1 
ATOM   3119 C  CG1  . ILE   B 1 153 ? -1.580  -8.775  43.711 1.00 31.16 ? 417 ILE   B CG1  1 
ATOM   3120 C  CG2  . ILE   B 1 153 ? -3.132  -8.026  45.551 1.00 25.98 ? 417 ILE   B CG2  1 
ATOM   3121 C  CD1  . ILE   B 1 153 ? -0.659  -9.418  44.724 1.00 28.33 ? 417 ILE   B CD1  1 
ATOM   3122 N  N    . ALA   B 1 154 ? -5.816  -7.625  43.756 1.00 24.64 ? 418 ALA   B N    1 
ATOM   3123 C  CA   . ALA   B 1 154 ? -7.101  -8.331  43.651 1.00 20.21 ? 418 ALA   B CA   1 
ATOM   3124 C  C    . ALA   B 1 154 ? -7.623  -8.232  42.224 1.00 21.21 ? 418 ALA   B C    1 
ATOM   3125 O  O    . ALA   B 1 154 ? -8.054  -9.241  41.615 1.00 23.61 ? 418 ALA   B O    1 
ATOM   3126 C  CB   . ALA   B 1 154 ? -8.128  -7.757  44.647 1.00 22.62 ? 418 ALA   B CB   1 
ATOM   3127 N  N    . LEU   B 1 155 ? -7.593  -7.011  41.682 1.00 21.66 ? 419 LEU   B N    1 
ATOM   3128 C  CA   . LEU   B 1 155 ? -8.145  -6.793  40.336 1.00 21.14 ? 419 LEU   B CA   1 
ATOM   3129 C  C    . LEU   B 1 155 ? -7.211  -7.409  39.304 1.00 23.23 ? 419 LEU   B C    1 
ATOM   3130 O  O    . LEU   B 1 155 ? -7.667  -7.992  38.318 1.00 23.67 ? 419 LEU   B O    1 
ATOM   3131 C  CB   . LEU   B 1 155 ? -8.332  -5.302  40.044 1.00 23.40 ? 419 LEU   B CB   1 
ATOM   3132 C  CG   . LEU   B 1 155 ? -9.317  -4.695  41.015 1.00 26.43 ? 419 LEU   B CG   1 
ATOM   3133 C  CD1  . LEU   B 1 155 ? -8.994  -3.172  41.259 1.00 27.27 ? 419 LEU   B CD1  1 
ATOM   3134 C  CD2  . LEU   B 1 155 ? -10.706 -4.859  40.405 1.00 31.08 ? 419 LEU   B CD2  1 
ATOM   3135 N  N    . TYR   B 1 156 ? -5.891  -7.290  39.521 1.00 21.82 ? 420 TYR   B N    1 
ATOM   3136 C  CA   . TYR   B 1 156 ? -4.961  -7.841  38.558 1.00 19.58 ? 420 TYR   B CA   1 
ATOM   3137 C  C    . TYR   B 1 156 ? -5.065  -9.382  38.515 1.00 22.58 ? 420 TYR   B C    1 
ATOM   3138 O  O    . TYR   B 1 156 ? -5.106  -9.948  37.435 1.00 22.11 ? 420 TYR   B O    1 
ATOM   3139 C  CB   . TYR   B 1 156 ? -3.526  -7.399  38.898 1.00 22.66 ? 420 TYR   B CB   1 
ATOM   3140 C  CG   . TYR   B 1 156 ? -2.523  -7.932  37.955 1.00 25.56 ? 420 TYR   B CG   1 
ATOM   3141 C  CD1  . TYR   B 1 156 ? -2.442  -7.462  36.663 1.00 31.15 ? 420 TYR   B CD1  1 
ATOM   3142 C  CD2  . TYR   B 1 156 ? -1.650  -8.893  38.369 1.00 25.65 ? 420 TYR   B CD2  1 
ATOM   3143 C  CE1  . TYR   B 1 156 ? -1.447  -7.976  35.785 1.00 34.89 ? 420 TYR   B CE1  1 
ATOM   3144 C  CE2  . TYR   B 1 156 ? -0.683  -9.429  37.509 1.00 35.99 ? 420 TYR   B CE2  1 
ATOM   3145 C  CZ   . TYR   B 1 156 ? -0.604  -8.961  36.225 1.00 40.07 ? 420 TYR   B CZ   1 
ATOM   3146 O  OH   . TYR   B 1 156 ? 0.362   -9.479  35.395 1.00 44.40 ? 420 TYR   B OH   1 
ATOM   3147 N  N    . THR   B 1 157 ? -5.135  -10.046 39.673 1.00 20.17 ? 421 THR   B N    1 
ATOM   3148 C  CA   . THR   B 1 157 ? -5.209  -11.497 39.657 1.00 19.05 ? 421 THR   B CA   1 
ATOM   3149 C  C    . THR   B 1 157 ? -6.556  -11.974 39.133 1.00 18.57 ? 421 THR   B C    1 
ATOM   3150 O  O    . THR   B 1 157 ? -6.603  -13.081 38.537 1.00 21.77 ? 421 THR   B O    1 
ATOM   3151 C  CB   . THR   B 1 157 ? -4.930  -12.132 41.035 1.00 19.58 ? 421 THR   B CB   1 
ATOM   3152 O  OG1  . THR   B 1 157 ? -5.769  -11.526 42.033 1.00 23.70 ? 421 THR   B OG1  1 
ATOM   3153 C  CG2  . THR   B 1 157 ? -3.445  -11.982 41.400 1.00 21.36 ? 421 THR   B CG2  1 
ATOM   3154 N  N    . ALA   B 1 158 ? -7.614  -11.172 39.294 1.00 19.57 ? 422 ALA   B N    1 
ATOM   3155 C  CA   . ALA   B 1 158 ? -8.887  -11.550 38.692 1.00 18.95 ? 422 ALA   B CA   1 
ATOM   3156 C  C    . ALA   B 1 158 ? -8.724  -11.596 37.147 1.00 20.64 ? 422 ALA   B C    1 
ATOM   3157 O  O    . ALA   B 1 158 ? -9.218  -12.527 36.494 1.00 23.44 ? 422 ALA   B O    1 
ATOM   3158 C  CB   . ALA   B 1 158 ? -9.996  -10.563 39.096 1.00 21.94 ? 422 ALA   B CB   1 
ATOM   3159 N  N    . LEU   B 1 159 ? -7.990  -10.635 36.579 1.00 22.04 ? 423 LEU   B N    1 
ATOM   3160 C  CA   . LEU   B 1 159 ? -7.750  -10.644 35.132 1.00 21.91 ? 423 LEU   B CA   1 
ATOM   3161 C  C    . LEU   B 1 159 ? -6.785  -11.736 34.683 1.00 27.39 ? 423 LEU   B C    1 
ATOM   3162 O  O    . LEU   B 1 159 ? -6.889  -12.200 33.543 1.00 26.27 ? 423 LEU   B O    1 
ATOM   3163 C  CB   . LEU   B 1 159 ? -7.258  -9.249  34.669 1.00 20.30 ? 423 LEU   B CB   1 
ATOM   3164 C  CG   . LEU   B 1 159 ? -8.371  -8.202  34.606 1.00 26.16 ? 423 LEU   B CG   1 
ATOM   3165 C  CD1  . LEU   B 1 159 ? -7.876  -6.750  34.586 1.00 27.00 ? 423 LEU   B CD1  1 
ATOM   3166 C  CD2  . LEU   B 1 159 ? -9.227  -8.473  33.347 1.00 29.19 ? 423 LEU   B CD2  1 
ATOM   3167 N  N    . VAL   B 1 160 ? -5.835  -12.136 35.538 1.00 22.63 ? 424 VAL   B N    1 
ATOM   3168 C  CA   . VAL   B 1 160 ? -4.974  -13.260 35.229 1.00 24.63 ? 424 VAL   B CA   1 
ATOM   3169 C  C    . VAL   B 1 160 ? -5.841  -14.501 34.992 1.00 25.61 ? 424 VAL   B C    1 
ATOM   3170 O  O    . VAL   B 1 160 ? -5.617  -15.285 34.050 1.00 23.89 ? 424 VAL   B O    1 
ATOM   3171 C  CB   . VAL   B 1 160 ? -3.959  -13.513 36.352 1.00 22.19 ? 424 VAL   B CB   1 
ATOM   3172 C  CG1  . VAL   B 1 160 ? -3.191  -14.812 36.073 1.00 28.51 ? 424 VAL   B CG1  1 
ATOM   3173 C  CG2  . VAL   B 1 160 ? -2.992  -12.394 36.477 1.00 23.47 ? 424 VAL   B CG2  1 
ATOM   3174 N  N    . LEU   B 1 161 ? -6.839  -14.660 35.857 1.00 22.96 ? 425 LEU   B N    1 
ATOM   3175 C  CA   . LEU   B 1 161 ? -7.702  -15.838 35.773 1.00 23.77 ? 425 LEU   B CA   1 
ATOM   3176 C  C    . LEU   B 1 161 ? -8.704  -15.763 34.639 1.00 23.95 ? 425 LEU   B C    1 
ATOM   3177 O  O    . LEU   B 1 161 ? -8.906  -16.766 33.959 1.00 24.13 ? 425 LEU   B O    1 
ATOM   3178 C  CB   . LEU   B 1 161 ? -8.453  -16.052 37.082 1.00 22.98 ? 425 LEU   B CB   1 
ATOM   3179 C  CG   . LEU   B 1 161 ? -7.687  -16.653 38.215 1.00 27.94 ? 425 LEU   B CG   1 
ATOM   3180 C  CD1  . LEU   B 1 161 ? -8.632  -16.746 39.402 1.00 34.20 ? 425 LEU   B CD1  1 
ATOM   3181 C  CD2  . LEU   B 1 161 ? -7.239  -18.041 37.822 1.00 29.01 ? 425 LEU   B CD2  1 
ATOM   3182 N  N    . ILE   B 1 162 ? -9.358  -14.617 34.442 1.00 22.28 ? 426 ILE   B N    1 
ATOM   3183 C  CA   . ILE   B 1 162 ? -10.456 -14.518 33.447 1.00 25.91 ? 426 ILE   B CA   1 
ATOM   3184 C  C    . ILE   B 1 162 ? -9.837  -14.022 32.149 1.00 27.71 ? 426 ILE   B C    1 
ATOM   3185 O  O    . ILE   B 1 162 ? -9.820  -12.829 31.862 1.00 27.23 ? 426 ILE   B O    1 
ATOM   3186 C  CB   . ILE   B 1 162 ? -11.598 -13.602 33.909 1.00 21.62 ? 426 ILE   B CB   1 
ATOM   3187 C  CG1  . ILE   B 1 162 ? -12.050 -13.970 35.309 1.00 24.33 ? 426 ILE   B CG1  1 
ATOM   3188 C  CG2  . ILE   B 1 162 ? -12.812 -13.624 32.892 1.00 24.14 ? 426 ILE   B CG2  1 
ATOM   3189 C  CD1  . ILE   B 1 162 ? -12.454 -15.452 35.493 1.00 27.64 ? 426 ILE   B CD1  1 
ATOM   3190 N  N    . ASN   B 1 163 ? -9.300  -14.971 31.398 1.00 28.79 ? 427 ASN   B N    1 
ATOM   3191 C  CA   . ASN   B 1 163 ? -8.529  -14.728 30.184 1.00 26.76 ? 427 ASN   B CA   1 
ATOM   3192 C  C    . ASN   B 1 163 ? -9.212  -15.473 29.033 1.00 26.22 ? 427 ASN   B C    1 
ATOM   3193 O  O    . ASN   B 1 163 ? -9.244  -16.710 28.983 1.00 24.99 ? 427 ASN   B O    1 
ATOM   3194 C  CB   . ASN   B 1 163 ? -7.083  -15.197 30.396 1.00 26.81 ? 427 ASN   B CB   1 
ATOM   3195 C  CG   . ASN   B 1 163 ? -6.198  -15.038 29.164 1.00 30.76 ? 427 ASN   B CG   1 
ATOM   3196 O  OD1  . ASN   B 1 163 ? -6.662  -14.885 28.053 1.00 33.16 ? 427 ASN   B OD1  1 
ATOM   3197 N  ND2  . ASN   B 1 163 ? -4.874  -15.095 29.385 1.00 32.66 ? 427 ASN   B ND2  1 
ATOM   3198 N  N    . ALA   B 1 164 ? -9.763  -14.721 28.101 1.00 25.17 ? 428 ALA   B N    1 
ATOM   3199 C  CA   . ALA   B 1 164 ? -10.547 -15.327 27.056 1.00 26.59 ? 428 ALA   B CA   1 
ATOM   3200 C  C    . ALA   B 1 164 ? -9.685  -15.984 25.986 1.00 27.31 ? 428 ALA   B C    1 
ATOM   3201 O  O    . ALA   B 1 164 ? -10.218 -16.587 25.062 1.00 31.82 ? 428 ALA   B O    1 
ATOM   3202 C  CB   . ALA   B 1 164 ? -11.490 -14.287 26.418 1.00 31.57 ? 428 ALA   B CB   1 
ATOM   3203 N  N    . HIS   B 1 165 ? -8.364  -15.904 26.115 1.00 28.68 ? 429 HIS   B N    1 
ATOM   3204 C  CA   . HIS   B 1 165 ? -7.518  -16.536 25.117 1.00 32.22 ? 429 HIS   B CA   1 
ATOM   3205 C  C    . HIS   B 1 165 ? -7.138  -17.965 25.479 1.00 32.96 ? 429 HIS   B C    1 
ATOM   3206 O  O    . HIS   B 1 165 ? -6.430  -18.603 24.696 1.00 34.60 ? 429 HIS   B O    1 
ATOM   3207 C  CB   . HIS   B 1 165 ? -6.256  -15.701 24.891 1.00 40.29 ? 429 HIS   B CB   1 
ATOM   3208 C  CG   . HIS   B 1 165 ? -6.533  -14.370 24.263 1.00 49.47 ? 429 HIS   B CG   1 
ATOM   3209 N  ND1  . HIS   B 1 165 ? -5.646  -13.317 24.310 1.00 53.15 ? 429 HIS   B ND1  1 
ATOM   3210 C  CD2  . HIS   B 1 165 ? -7.626  -13.910 23.608 1.00 60.38 ? 429 HIS   B CD2  1 
ATOM   3211 C  CE1  . HIS   B 1 165 ? -6.168  -12.273 23.694 1.00 54.48 ? 429 HIS   B CE1  1 
ATOM   3212 N  NE2  . HIS   B 1 165 ? -7.369  -12.607 23.259 1.00 64.24 ? 429 HIS   B NE2  1 
ATOM   3213 N  N    . ARG   B 1 166 ? -7.583  -18.483 26.633 1.00 27.91 ? 430 ARG   B N    1 
ATOM   3214 C  CA   . ARG   B 1 166 ? -7.231  -19.865 26.966 1.00 28.32 ? 430 ARG   B CA   1 
ATOM   3215 C  C    . ARG   B 1 166 ? -7.828  -20.816 25.950 1.00 28.80 ? 430 ARG   B C    1 
ATOM   3216 O  O    . ARG   B 1 166 ? -9.056  -20.747 25.655 1.00 26.91 ? 430 ARG   B O    1 
ATOM   3217 C  CB   . ARG   B 1 166 ? -7.705  -20.253 28.375 1.00 26.06 ? 430 ARG   B CB   1 
ATOM   3218 C  CG   . ARG   B 1 166 ? -7.269  -19.299 29.498 1.00 23.18 ? 430 ARG   B CG   1 
ATOM   3219 C  CD   . ARG   B 1 166 ? -5.766  -19.134 29.603 1.00 27.72 ? 430 ARG   B CD   1 
ATOM   3220 N  NE   . ARG   B 1 166 ? -5.467  -18.592 30.918 1.00 27.66 ? 430 ARG   B NE   1 
ATOM   3221 C  CZ   . ARG   B 1 166 ? -4.241  -18.275 31.334 1.00 30.71 ? 430 ARG   B CZ   1 
ATOM   3222 N  NH1  . ARG   B 1 166 ? -3.217  -18.415 30.508 1.00 32.74 ? 430 ARG   B NH1  1 
ATOM   3223 N  NH2  . ARG   B 1 166 ? -4.042  -17.810 32.551 1.00 27.72 ? 430 ARG   B NH2  1 
ATOM   3224 N  N    . PRO   B 1 167 ? -7.003  -21.721 25.426 1.00 29.63 ? 431 PRO   B N    1 
ATOM   3225 C  CA   . PRO   B 1 167 ? -7.552  -22.735 24.525 1.00 36.06 ? 431 PRO   B CA   1 
ATOM   3226 C  C    . PRO   B 1 167 ? -8.545  -23.654 25.236 1.00 32.00 ? 431 PRO   B C    1 
ATOM   3227 O  O    . PRO   B 1 167 ? -8.356  -24.028 26.397 1.00 31.76 ? 431 PRO   B O    1 
ATOM   3228 C  CB   . PRO   B 1 167 ? -6.317  -23.516 24.073 1.00 37.72 ? 431 PRO   B CB   1 
ATOM   3229 C  CG   . PRO   B 1 167 ? -5.154  -22.630 24.361 1.00 37.49 ? 431 PRO   B CG   1 
ATOM   3230 C  CD   . PRO   B 1 167 ? -5.541  -21.804 25.543 1.00 32.12 ? 431 PRO   B CD   1 
ATOM   3231 N  N    . GLY   B 1 168 ? -9.614  -23.996 24.553 1.00 30.91 ? 432 GLY   B N    1 
ATOM   3232 C  CA   . GLY   B 1 168 ? -10.525 -25.006 25.074 1.00 35.26 ? 432 GLY   B CA   1 
ATOM   3233 C  C    . GLY   B 1 168 ? -11.828 -24.483 25.656 1.00 34.12 ? 432 GLY   B C    1 
ATOM   3234 O  O    . GLY   B 1 168 ? -12.660 -25.261 26.118 1.00 34.88 ? 432 GLY   B O    1 
ATOM   3235 N  N    . LEU   B 1 169 ? -12.032 -23.167 25.621 1.00 30.65 ? 433 LEU   B N    1 
ATOM   3236 C  CA   . LEU   B 1 169 ? -13.265 -22.584 26.116 1.00 26.79 ? 433 LEU   B CA   1 
ATOM   3237 C  C    . LEU   B 1 169 ? -14.443 -22.916 25.214 1.00 32.25 ? 433 LEU   B C    1 
ATOM   3238 O  O    . LEU   B 1 169 ? -14.328 -22.880 23.982 1.00 34.92 ? 433 LEU   B O    1 
ATOM   3239 C  CB   . LEU   B 1 169 ? -13.092 -21.062 26.249 1.00 26.94 ? 433 LEU   B CB   1 
ATOM   3240 C  CG   . LEU   B 1 169 ? -12.020 -20.650 27.261 1.00 28.60 ? 433 LEU   B CG   1 
ATOM   3241 C  CD1  . LEU   B 1 169 ? -11.807 -19.142 27.239 1.00 24.86 ? 433 LEU   B CD1  1 
ATOM   3242 C  CD2  . LEU   B 1 169 ? -12.458 -21.080 28.648 1.00 29.50 ? 433 LEU   B CD2  1 
ATOM   3243 N  N    . GLN   B 1 170 ? -15.576 -23.244 25.828 1.00 29.54 ? 434 GLN   B N    1 
ATOM   3244 C  CA   . GLN   B 1 170 ? -16.789 -23.546 25.082 1.00 31.95 ? 434 GLN   B CA   1 
ATOM   3245 C  C    . GLN   B 1 170 ? -17.644 -22.306 24.813 1.00 32.18 ? 434 GLN   B C    1 
ATOM   3246 O  O    . GLN   B 1 170 ? -18.307 -22.239 23.797 1.00 36.38 ? 434 GLN   B O    1 
ATOM   3247 C  CB   . GLN   B 1 170 ? -17.591 -24.586 25.835 1.00 31.04 ? 434 GLN   B CB   1 
ATOM   3248 C  CG   . GLN   B 1 170 ? -16.915 -25.946 25.787 1.00 40.25 ? 434 GLN   B CG   1 
ATOM   3249 C  CD   . GLN   B 1 170 ? -17.678 -27.007 26.570 1.00 46.92 ? 434 GLN   B CD   1 
ATOM   3250 O  OE1  . GLN   B 1 170 ? -18.735 -26.734 27.159 1.00 46.93 ? 434 GLN   B OE1  1 
ATOM   3251 N  NE2  . GLN   B 1 170 ? -17.132 -28.212 26.600 1.00 49.84 ? 434 GLN   B NE2  1 
ATOM   3252 N  N    . GLU   B 1 171 ? -17.591 -21.320 25.709 1.00 29.68 ? 435 GLU   B N    1 
ATOM   3253 C  CA   . GLU   B 1 171 ? -18.341 -20.093 25.571 1.00 31.44 ? 435 GLU   B CA   1 
ATOM   3254 C  C    . GLU   B 1 171 ? -17.356 -18.927 25.562 1.00 30.01 ? 435 GLU   B C    1 
ATOM   3255 O  O    . GLU   B 1 171 ? -17.306 -18.172 26.504 1.00 29.58 ? 435 GLU   B O    1 
ATOM   3256 C  CB   . GLU   B 1 171 ? -19.349 -19.959 26.705 1.00 34.00 ? 435 GLU   B CB   1 
ATOM   3257 C  CG   . GLU   B 1 171 ? -20.344 -21.140 26.737 1.00 40.69 ? 435 GLU   B CG   1 
ATOM   3258 C  CD   . GLU   B 1 171 ? -21.445 -20.993 27.779 1.00 50.52 ? 435 GLU   B CD   1 
ATOM   3259 O  OE1  . GLU   B 1 171 ? -22.618 -21.172 27.409 1.00 58.23 ? 435 GLU   B OE1  1 
ATOM   3260 O  OE2  . GLU   B 1 171 ? -21.161 -20.716 28.956 1.00 53.36 ? 435 GLU   B OE2  1 
ATOM   3261 N  N    . LYS   B 1 172 ? -16.578 -18.797 24.493 1.00 31.33 ? 436 LYS   B N    1 
ATOM   3262 C  CA   . LYS   B 1 172 ? -15.494 -17.802 24.481 1.00 31.19 ? 436 LYS   B CA   1 
ATOM   3263 C  C    . LYS   B 1 172 ? -16.028 -16.397 24.662 1.00 29.55 ? 436 LYS   B C    1 
ATOM   3264 O  O    . LYS   B 1 172 ? -15.452 -15.616 25.402 1.00 27.66 ? 436 LYS   B O    1 
ATOM   3265 C  CB   . LYS   B 1 172 ? -14.690 -17.891 23.191 1.00 35.75 ? 436 LYS   B CB   1 
ATOM   3266 C  CG   . LYS   B 1 172 ? -13.456 -16.985 23.192 1.00 39.91 ? 436 LYS   B CG   1 
ATOM   3267 C  CD   . LYS   B 1 172 ? -12.733 -17.033 21.864 1.00 42.53 ? 436 LYS   B CD   1 
ATOM   3268 C  CE   . LYS   B 1 172 ? -11.613 -16.016 21.795 1.00 47.87 ? 436 LYS   B CE   1 
ATOM   3269 N  NZ   . LYS   B 1 172 ? -10.786 -16.249 20.587 1.00 53.31 ? 436 LYS   B NZ   1 
ATOM   3270 N  N    . ARG   B 1 173 ? -17.140 -16.059 24.004 1.00 29.60 ? 437 ARG   B N    1 
ATOM   3271 C  CA   . ARG   B 1 173 ? -17.628 -14.687 24.097 1.00 29.95 ? 437 ARG   B CA   1 
ATOM   3272 C  C    . ARG   B 1 173 ? -18.118 -14.370 25.512 1.00 27.80 ? 437 ARG   B C    1 
ATOM   3273 O  O    . ARG   B 1 173 ? -17.977 -13.217 25.950 1.00 27.95 ? 437 ARG   B O    1 
ATOM   3274 C  CB   . ARG   B 1 173 ? -18.738 -14.429 23.068 1.00 32.45 ? 437 ARG   B CB   1 
ATOM   3275 C  CG   . ARG   B 1 173 ? -19.252 -13.012 23.018 1.00 34.65 ? 437 ARG   B CG   1 
ATOM   3276 C  CD   . ARG   B 1 173 ? -18.138 -11.997 22.641 1.00 32.81 ? 437 ARG   B CD   1 
ATOM   3277 N  NE   . ARG   B 1 173 ? -18.708 -10.683 22.340 1.00 35.68 ? 437 ARG   B NE   1 
ATOM   3278 C  CZ   . ARG   B 1 173 ? -17.986 -9.622  21.973 1.00 36.98 ? 437 ARG   B CZ   1 
ATOM   3279 N  NH1  . ARG   B 1 173 ? -16.671 -9.727  21.851 1.00 33.21 ? 437 ARG   B NH1  1 
ATOM   3280 N  NH2  . ARG   B 1 173 ? -18.588 -8.474  21.713 1.00 35.17 ? 437 ARG   B NH2  1 
ATOM   3281 N  N    . LYS   B 1 174 ? -18.700 -15.349 26.220 1.00 27.59 ? 438 LYS   B N    1 
ATOM   3282 C  CA   . LYS   B 1 174 ? -19.083 -15.083 27.617 1.00 28.41 ? 438 LYS   B CA   1 
ATOM   3283 C  C    . LYS   B 1 174 ? -17.817 -14.755 28.420 1.00 28.61 ? 438 LYS   B C    1 
ATOM   3284 O  O    . LYS   B 1 174 ? -17.857 -13.880 29.286 1.00 27.77 ? 438 LYS   B O    1 
ATOM   3285 C  CB   . LYS   B 1 174 ? -19.840 -16.253 28.290 1.00 28.07 ? 438 LYS   B CB   1 
ATOM   3286 C  CG   . LYS   B 1 174 ? -21.283 -16.339 27.890 1.00 45.22 ? 438 LYS   B CG   1 
ATOM   3287 C  CD   . LYS   B 1 174 ? -22.012 -15.020 28.156 1.00 56.63 ? 438 LYS   B CD   1 
ATOM   3288 C  CE   . LYS   B 1 174 ? -23.021 -14.665 27.045 1.00 59.77 ? 438 LYS   B CE   1 
ATOM   3289 N  NZ   . LYS   B 1 174 ? -22.403 -14.415 25.704 1.00 57.85 ? 438 LYS   B NZ   1 
ATOM   3290 N  N    . VAL   B 1 175 ? -16.705 -15.460 28.179 1.00 25.00 ? 439 VAL   B N    1 
ATOM   3291 C  CA   . VAL   B 1 175 ? -15.463 -15.194 28.940 1.00 23.58 ? 439 VAL   B CA   1 
ATOM   3292 C  C    . VAL   B 1 175 ? -14.941 -13.803 28.561 1.00 21.37 ? 439 VAL   B C    1 
ATOM   3293 O  O    . VAL   B 1 175 ? -14.538 -13.033 29.444 1.00 26.46 ? 439 VAL   B O    1 
ATOM   3294 C  CB   . VAL   B 1 175 ? -14.397 -16.279 28.696 1.00 22.00 ? 439 VAL   B CB   1 
ATOM   3295 C  CG1  . VAL   B 1 175 ? -13.146 -15.943 29.451 1.00 25.02 ? 439 VAL   B CG1  1 
ATOM   3296 C  CG2  . VAL   B 1 175 ? -14.953 -17.686 29.125 1.00 25.60 ? 439 VAL   B CG2  1 
ATOM   3297 N  N    . GLU   B 1 176 ? -15.044 -13.439 27.277 1.00 24.20 ? 440 GLU   B N    1 
ATOM   3298 C  CA   . GLU   B 1 176 ? -14.652 -12.099 26.831 1.00 21.57 ? 440 GLU   B CA   1 
ATOM   3299 C  C    . GLU   B 1 176 ? -15.436 -10.985 27.515 1.00 25.88 ? 440 GLU   B C    1 
ATOM   3300 O  O    . GLU   B 1 176 ? -14.881 -9.941  27.870 1.00 25.98 ? 440 GLU   B O    1 
ATOM   3301 C  CB   . GLU   B 1 176 ? -14.799 -11.961 25.331 1.00 24.33 ? 440 GLU   B CB   1 
ATOM   3302 C  CG   . GLU   B 1 176 ? -13.843 -12.794 24.515 1.00 28.50 ? 440 GLU   B CG   1 
ATOM   3303 C  CD   . GLU   B 1 176 ? -14.194 -12.749 23.026 1.00 46.26 ? 440 GLU   B CD   1 
ATOM   3304 O  OE1  . GLU   B 1 176 ? -14.516 -11.657 22.505 1.00 45.62 ? 440 GLU   B OE1  1 
ATOM   3305 O  OE2  . GLU   B 1 176 ? -14.161 -13.814 22.370 1.00 55.79 ? 440 GLU   B OE2  1 
ATOM   3306 N  N    . GLN   B 1 177 ? -16.722 -11.214 27.714 1.00 26.91 ? 441 GLN   B N    1 
ATOM   3307 C  CA   . GLN   B 1 177 ? -17.568 -10.230 28.366 1.00 25.49 ? 441 GLN   B CA   1 
ATOM   3308 C  C    . GLN   B 1 177 ? -17.146 -10.109 29.842 1.00 25.69 ? 441 GLN   B C    1 
ATOM   3309 O  O    . GLN   B 1 177 ? -17.017 -9.005  30.369 1.00 26.89 ? 441 GLN   B O    1 
ATOM   3310 C  CB   . GLN   B 1 177 ? -19.051 -10.610 28.211 1.00 28.16 ? 441 GLN   B CB   1 
ATOM   3311 C  CG   . GLN   B 1 177 ? -19.507 -10.693 26.752 1.00 38.81 ? 441 GLN   B CG   1 
ATOM   3312 C  CD   . GLN   B 1 177 ? -20.492 -9.644  26.387 1.00 56.64 ? 441 GLN   B CD   1 
ATOM   3313 O  OE1  . GLN   B 1 177 ? -20.304 -8.467  26.713 1.00 61.95 ? 441 GLN   B OE1  1 
ATOM   3314 N  NE2  . GLN   B 1 177 ? -21.573 -10.051 25.706 1.00 53.34 ? 441 GLN   B NE2  1 
ATOM   3315 N  N    . LEU   B 1 178 ? -16.877 -11.217 30.529 1.00 25.95 ? 442 LEU   B N    1 
ATOM   3316 C  CA   . LEU   B 1 178 ? -16.479 -11.107 31.945 1.00 25.65 ? 442 LEU   B CA   1 
ATOM   3317 C  C    . LEU   B 1 178 ? -15.110 -10.454 32.063 1.00 23.68 ? 442 LEU   B C    1 
ATOM   3318 O  O    . LEU   B 1 178 ? -14.850 -9.650  32.951 1.00 25.79 ? 442 LEU   B O    1 
ATOM   3319 C  CB   . LEU   B 1 178 ? -16.449 -12.478 32.630 1.00 25.30 ? 442 LEU   B CB   1 
ATOM   3320 C  CG   . LEU   B 1 178 ? -15.985 -12.511 34.106 1.00 28.73 ? 442 LEU   B CG   1 
ATOM   3321 C  CD1  . LEU   B 1 178 ? -16.712 -11.501 35.038 1.00 34.52 ? 442 LEU   B CD1  1 
ATOM   3322 C  CD2  . LEU   B 1 178 ? -16.064 -13.922 34.679 1.00 36.40 ? 442 LEU   B CD2  1 
ATOM   3323 N  N    . GLN   B 1 179 ? -14.218 -10.862 31.187 1.00 20.79 ? 443 GLN   B N    1 
ATOM   3324 C  CA   . GLN   B 1 179 ? -12.902 -10.261 31.140 1.00 23.65 ? 443 GLN   B CA   1 
ATOM   3325 C  C    . GLN   B 1 179 ? -13.020 -8.745  30.970 1.00 26.23 ? 443 GLN   B C    1 
ATOM   3326 O  O    . GLN   B 1 179 ? -12.372 -7.970  31.678 1.00 22.74 ? 443 GLN   B O    1 
ATOM   3327 C  CB   . GLN   B 1 179 ? -12.116 -10.879 29.990 1.00 22.32 ? 443 GLN   B CB   1 
ATOM   3328 C  CG   . GLN   B 1 179 ? -10.712 -10.307 29.825 1.00 23.31 ? 443 GLN   B CG   1 
ATOM   3329 C  CD   . GLN   B 1 179 ? -10.042 -10.882 28.601 1.00 32.67 ? 443 GLN   B CD   1 
ATOM   3330 O  OE1  . GLN   B 1 179 ? -9.110  -11.682 28.704 1.00 39.37 ? 443 GLN   B OE1  1 
ATOM   3331 N  NE2  . GLN   B 1 179 ? -10.471 -10.432 27.431 1.00 35.63 ? 443 GLN   B NE2  1 
ATOM   3332 N  N    . TYR   B 1 180 ? -13.836 -8.302  30.011 1.00 24.73 ? 444 TYR   B N    1 
ATOM   3333 C  CA   . TYR   B 1 180 ? -14.010 -6.871  29.802 1.00 24.50 ? 444 TYR   B CA   1 
ATOM   3334 C  C    . TYR   B 1 180 ? -14.568 -6.166  31.068 1.00 24.34 ? 444 TYR   B C    1 
ATOM   3335 O  O    . TYR   B 1 180 ? -14.116 -5.069  31.436 1.00 23.75 ? 444 TYR   B O    1 
ATOM   3336 C  CB   . TYR   B 1 180 ? -14.934 -6.598  28.589 1.00 25.25 ? 444 TYR   B CB   1 
ATOM   3337 C  CG   . TYR   B 1 180 ? -15.226 -5.116  28.502 1.00 24.91 ? 444 TYR   B CG   1 
ATOM   3338 C  CD1  . TYR   B 1 180 ? -14.264 -4.242  28.044 1.00 24.72 ? 444 TYR   B CD1  1 
ATOM   3339 C  CD2  . TYR   B 1 180 ? -16.446 -4.590  28.920 1.00 26.57 ? 444 TYR   B CD2  1 
ATOM   3340 C  CE1  . TYR   B 1 180 ? -14.485 -2.903  27.994 1.00 25.74 ? 444 TYR   B CE1  1 
ATOM   3341 C  CE2  . TYR   B 1 180 ? -16.677 -3.230  28.867 1.00 27.53 ? 444 TYR   B CE2  1 
ATOM   3342 C  CZ   . TYR   B 1 180 ? -15.679 -2.394  28.407 1.00 26.01 ? 444 TYR   B CZ   1 
ATOM   3343 O  OH   . TYR   B 1 180 ? -15.852 -1.052  28.359 1.00 27.32 ? 444 TYR   B OH   1 
ATOM   3344 N  N    . ASN   B 1 181 ? -15.565 -6.762  31.716 1.00 25.66 ? 445 ASN   B N    1 
ATOM   3345 C  CA   . ASN   B 1 181 ? -16.118 -6.133  32.924 1.00 24.75 ? 445 ASN   B CA   1 
ATOM   3346 C  C    . ASN   B 1 181 ? -14.995 -5.891  33.938 1.00 27.16 ? 445 ASN   B C    1 
ATOM   3347 O  O    . ASN   B 1 181 ? -14.975 -4.843  34.590 1.00 25.03 ? 445 ASN   B O    1 
ATOM   3348 C  CB   . ASN   B 1 181 ? -17.181 -6.990  33.560 1.00 25.68 ? 445 ASN   B CB   1 
ATOM   3349 C  CG   . ASN   B 1 181 ? -18.400 -7.122  32.706 1.00 29.11 ? 445 ASN   B CG   1 
ATOM   3350 O  OD1  . ASN   B 1 181 ? -18.634 -6.339  31.801 1.00 35.21 ? 445 ASN   B OD1  1 
ATOM   3351 N  ND2  . ASN   B 1 181 ? -19.180 -8.148  32.987 1.00 34.69 ? 445 ASN   B ND2  1 
ATOM   3352 N  N    . LEU   B 1 182 ? -14.117 -6.885  34.098 1.00 23.44 ? 446 LEU   B N    1 
ATOM   3353 C  CA   . LEU   B 1 182 ? -12.971 -6.765  35.004 1.00 20.99 ? 446 LEU   B CA   1 
ATOM   3354 C  C    . LEU   B 1 182 ? -11.963 -5.743  34.498 1.00 22.62 ? 446 LEU   B C    1 
ATOM   3355 O  O    . LEU   B 1 182 ? -11.344 -5.012  35.318 1.00 26.94 ? 446 LEU   B O    1 
ATOM   3356 C  CB   . LEU   B 1 182 ? -12.295 -8.128  35.182 1.00 22.47 ? 446 LEU   B CB   1 
ATOM   3357 C  CG   . LEU   B 1 182 ? -13.167 -9.057  36.012 1.00 24.99 ? 446 LEU   B CG   1 
ATOM   3358 C  CD1  . LEU   B 1 182 ? -12.642 -10.506 35.887 1.00 24.91 ? 446 LEU   B CD1  1 
ATOM   3359 C  CD2  . LEU   B 1 182 ? -13.277 -8.634  37.467 1.00 25.01 ? 446 LEU   B CD2  1 
ATOM   3360 N  N    . GLU   B 1 183 ? -11.742 -5.667  33.175 1.00 22.66 ? 447 GLU   B N    1 
ATOM   3361 C  CA   . GLU   B 1 183 ? -10.842 -4.634  32.595 1.00 23.96 ? 447 GLU   B CA   1 
ATOM   3362 C  C    . GLU   B 1 183 ? -11.376 -3.242  32.904 1.00 21.97 ? 447 GLU   B C    1 
ATOM   3363 O  O    . GLU   B 1 183 ? -10.629 -2.338  33.291 1.00 23.83 ? 447 GLU   B O    1 
ATOM   3364 C  CB   . GLU   B 1 183 ? -10.708 -4.778  31.066 1.00 26.59 ? 447 GLU   B CB   1 
ATOM   3365 C  CG   . GLU   B 1 183 ? -9.903  -6.024  30.604 1.00 27.21 ? 447 GLU   B CG   1 
ATOM   3366 C  CD   . GLU   B 1 183 ? -9.830  -6.208  29.074 1.00 39.18 ? 447 GLU   B CD   1 
ATOM   3367 O  OE1  . GLU   B 1 183 ? -10.557 -5.497  28.342 1.00 40.45 ? 447 GLU   B OE1  1 
ATOM   3368 O  OE2  . GLU   B 1 183 ? -9.026  -7.074  28.606 1.00 41.09 ? 447 GLU   B OE2  1 
ATOM   3369 N  N    . LEU   B 1 184 ? -12.702 -3.082  32.761 1.00 22.56 ? 448 LEU   B N    1 
ATOM   3370 C  CA   . LEU   B 1 184 ? -13.311 -1.788  33.042 1.00 23.04 ? 448 LEU   B CA   1 
ATOM   3371 C  C    . LEU   B 1 184 ? -13.173 -1.443  34.533 1.00 25.04 ? 448 LEU   B C    1 
ATOM   3372 O  O    . LEU   B 1 184 ? -12.936 -0.311  34.901 1.00 25.24 ? 448 LEU   B O    1 
ATOM   3373 C  CB   . LEU   B 1 184 ? -14.798 -1.791  32.626 1.00 22.53 ? 448 LEU   B CB   1 
ATOM   3374 C  CG   . LEU   B 1 184 ? -15.674 -0.541  32.868 1.00 25.06 ? 448 LEU   B CG   1 
ATOM   3375 C  CD1  . LEU   B 1 184 ? -14.981 0.704   32.278 1.00 29.10 ? 448 LEU   B CD1  1 
ATOM   3376 C  CD2  . LEU   B 1 184 ? -17.080 -0.728  32.265 1.00 27.05 ? 448 LEU   B CD2  1 
ATOM   3377 N  N    . ALA   B 1 185 ? -13.391 -2.414  35.393 1.00 26.20 ? 449 ALA   B N    1 
ATOM   3378 C  CA   . ALA   B 1 185 ? -13.227 -2.232  36.828 1.00 23.76 ? 449 ALA   B CA   1 
ATOM   3379 C  C    . ALA   B 1 185 ? -11.813 -1.809  37.192 1.00 25.14 ? 449 ALA   B C    1 
ATOM   3380 O  O    . ALA   B 1 185 ? -11.619 -0.898  37.972 1.00 27.30 ? 449 ALA   B O    1 
ATOM   3381 C  CB   . ALA   B 1 185 ? -13.564 -3.542  37.549 1.00 24.10 ? 449 ALA   B CB   1 
ATOM   3382 N  N    . PHE   B 1 186 ? -10.835 -2.513  36.645 1.00 22.19 ? 450 PHE   B N    1 
ATOM   3383 C  CA   . PHE   B 1 186 ? -9.412  -2.239  36.952 1.00 23.68 ? 450 PHE   B CA   1 
ATOM   3384 C  C    . PHE   B 1 186 ? -9.053  -0.847  36.456 1.00 25.16 ? 450 PHE   B C    1 
ATOM   3385 O  O    . PHE   B 1 186 ? -8.468  -0.011  37.178 1.00 25.77 ? 450 PHE   B O    1 
ATOM   3386 C  CB   . PHE   B 1 186 ? -8.561  -3.328  36.279 1.00 23.28 ? 450 PHE   B CB   1 
ATOM   3387 C  CG   . PHE   B 1 186 ? -7.102  -3.376  36.693 1.00 24.54 ? 450 PHE   B CG   1 
ATOM   3388 C  CD1  . PHE   B 1 186 ? -6.672  -3.003  37.943 1.00 25.56 ? 450 PHE   B CD1  1 
ATOM   3389 C  CD2  . PHE   B 1 186 ? -6.190  -3.842  35.791 1.00 25.82 ? 450 PHE   B CD2  1 
ATOM   3390 C  CE1  . PHE   B 1 186 ? -5.313  -3.126  38.274 1.00 22.76 ? 450 PHE   B CE1  1 
ATOM   3391 C  CE2  . PHE   B 1 186 ? -4.824  -3.933  36.090 1.00 28.74 ? 450 PHE   B CE2  1 
ATOM   3392 C  CZ   . PHE   B 1 186 ? -4.405  -3.594  37.345 1.00 26.25 ? 450 PHE   B CZ   1 
ATOM   3393 N  N    . HIS   B 1 187 ? -9.404  -0.574  35.198 1.00 26.08 ? 451 HIS   B N    1 
ATOM   3394 C  CA   . HIS   B 1 187 ? -9.180  0.732   34.609 1.00 24.25 ? 451 HIS   B CA   1 
ATOM   3395 C  C    . HIS   B 1 187 ? -9.795  1.870   35.446 1.00 26.87 ? 451 HIS   B C    1 
ATOM   3396 O  O    . HIS   B 1 187 ? -9.168  2.891   35.739 1.00 26.30 ? 451 HIS   B O    1 
ATOM   3397 C  CB   . HIS   B 1 187 ? -9.749  0.727   33.196 1.00 24.93 ? 451 HIS   B CB   1 
ATOM   3398 C  CG   . HIS   B 1 187 ? -9.770  2.069   32.550 1.00 32.52 ? 451 HIS   B CG   1 
ATOM   3399 N  ND1  . HIS   B 1 187 ? -8.665  2.657   31.987 1.00 27.59 ? 451 HIS   B ND1  1 
ATOM   3400 C  CD2  . HIS   B 1 187 ? -10.783 2.958   32.387 1.00 32.77 ? 451 HIS   B CD2  1 
ATOM   3401 C  CE1  . HIS   B 1 187 ? -8.991  3.833   31.476 1.00 29.78 ? 451 HIS   B CE1  1 
ATOM   3402 N  NE2  . HIS   B 1 187 ? -10.276 4.036   31.713 1.00 37.58 ? 451 HIS   B NE2  1 
ATOM   3403 N  N    . HIS   B 1 188 ? -11.066 1.702   35.795 1.00 26.61 ? 452 HIS   B N    1 
ATOM   3404 C  CA   . HIS   B 1 188 ? -11.714 2.667   36.644 1.00 28.31 ? 452 HIS   B CA   1 
ATOM   3405 C  C    . HIS   B 1 188 ? -10.956 2.937   37.935 1.00 24.81 ? 452 HIS   B C    1 
ATOM   3406 O  O    . HIS   B 1 188 ? -10.742 4.079   38.314 1.00 27.98 ? 452 HIS   B O    1 
ATOM   3407 C  CB   . HIS   B 1 188 ? -13.125 2.191   36.977 1.00 25.76 ? 452 HIS   B CB   1 
ATOM   3408 C  CG   . HIS   B 1 188 ? -13.933 3.223   37.701 1.00 29.47 ? 452 HIS   B CG   1 
ATOM   3409 N  ND1  . HIS   B 1 188 ? -14.380 4.379   37.093 1.00 35.54 ? 452 HIS   B ND1  1 
ATOM   3410 C  CD2  . HIS   B 1 188 ? -14.293 3.312   38.999 1.00 32.15 ? 452 HIS   B CD2  1 
ATOM   3411 C  CE1  . HIS   B 1 188 ? -15.041 5.103   37.979 1.00 40.15 ? 452 HIS   B CE1  1 
ATOM   3412 N  NE2  . HIS   B 1 188 ? -15.009 4.480   39.143 1.00 34.72 ? 452 HIS   B NE2  1 
ATOM   3413 N  N    . HIS   B 1 189 ? -10.589 1.857   38.611 1.00 24.06 ? 453 HIS   B N    1 
ATOM   3414 C  CA   . HIS   B 1 189 ? -9.944  1.956   39.906 1.00 24.18 ? 453 HIS   B CA   1 
ATOM   3415 C  C    . HIS   B 1 189 ? -8.613  2.675   39.758 1.00 26.04 ? 453 HIS   B C    1 
ATOM   3416 O  O    . HIS   B 1 189 ? -8.263  3.533   40.565 1.00 24.32 ? 453 HIS   B O    1 
ATOM   3417 C  CB   . HIS   B 1 189 ? -9.768  0.562   40.506 1.00 24.74 ? 453 HIS   B CB   1 
ATOM   3418 C  CG   . HIS   B 1 189 ? -9.132  0.572   41.862 1.00 27.82 ? 453 HIS   B CG   1 
ATOM   3419 N  ND1  . HIS   B 1 189 ? -9.814  0.975   42.991 1.00 38.23 ? 453 HIS   B ND1  1 
ATOM   3420 C  CD2  . HIS   B 1 189 ? -7.876  0.283   42.264 1.00 35.08 ? 453 HIS   B CD2  1 
ATOM   3421 C  CE1  . HIS   B 1 189 ? -9.007  0.909   44.033 1.00 31.40 ? 453 HIS   B CE1  1 
ATOM   3422 N  NE2  . HIS   B 1 189 ? -7.827  0.490   43.621 1.00 35.57 ? 453 HIS   B NE2  1 
ATOM   3423 N  N    . LEU   B 1 190 ? -7.870  2.335   38.711 1.00 25.74 ? 454 LEU   B N    1 
ATOM   3424 C  CA   . LEU   B 1 190 ? -6.541  2.974   38.522 1.00 25.21 ? 454 LEU   B CA   1 
ATOM   3425 C  C    . LEU   B 1 190 ? -6.699  4.450   38.189 1.00 28.37 ? 454 LEU   B C    1 
ATOM   3426 O  O    . LEU   B 1 190 ? -5.877  5.270   38.599 1.00 27.39 ? 454 LEU   B O    1 
ATOM   3427 C  CB   . LEU   B 1 190 ? -5.742  2.287   37.414 1.00 21.59 ? 454 LEU   B CB   1 
ATOM   3428 C  CG   . LEU   B 1 190 ? -5.419  0.802   37.624 1.00 25.66 ? 454 LEU   B CG   1 
ATOM   3429 C  CD1  . LEU   B 1 190 ? -4.663  0.233   36.418 1.00 25.21 ? 454 LEU   B CD1  1 
ATOM   3430 C  CD2  . LEU   B 1 190 ? -4.593  0.678   38.853 1.00 25.43 ? 454 LEU   B CD2  1 
ATOM   3431 N  N    . CYS   B 1 191 ? -7.752  4.814   37.442 1.00 27.69 ? 455 CYS   B N    1 
ATOM   3432 C  CA   . CYS   B 1 191 ? -7.967  6.218   37.151 1.00 30.95 ? 455 CYS   B CA   1 
ATOM   3433 C  C    . CYS   B 1 191 ? -8.345  6.986   38.402 1.00 31.20 ? 455 CYS   B C    1 
ATOM   3434 O  O    . CYS   B 1 191 ? -7.828  8.084   38.621 1.00 36.95 ? 455 CYS   B O    1 
ATOM   3435 C  CB   . CYS   B 1 191 ? -9.056  6.398   36.097 1.00 36.71 ? 455 CYS   B CB   1 
ATOM   3436 S  SG   . CYS   B 1 191 ? -8.589  5.848   34.430 1.00 40.17 ? 455 CYS   B SG   1 
ATOM   3437 N  N    . LYS   B 1 192 ? -9.257  6.440   39.208 1.00 31.98 ? 456 LYS   B N    1 
ATOM   3438 C  CA   . LYS   B 1 192 ? -9.678  7.157   40.414 1.00 34.51 ? 456 LYS   B CA   1 
ATOM   3439 C  C    . LYS   B 1 192 ? -8.520  7.299   41.384 1.00 38.74 ? 456 LYS   B C    1 
ATOM   3440 O  O    . LYS   B 1 192 ? -8.409  8.310   42.079 1.00 39.93 ? 456 LYS   B O    1 
ATOM   3441 C  CB   . LYS   B 1 192 ? -10.845 6.463   41.120 1.00 34.65 ? 456 LYS   B CB   1 
ATOM   3442 C  CG   . LYS   B 1 192 ? -12.216 6.733   40.494 1.00 45.33 ? 456 LYS   B CG   1 
ATOM   3443 C  CD   . LYS   B 1 192 ? -12.322 8.141   39.930 1.00 55.38 ? 456 LYS   B CD   1 
ATOM   3444 C  CE   . LYS   B 1 192 ? -13.728 8.448   39.430 1.00 67.00 ? 456 LYS   B CE   1 
ATOM   3445 N  NZ   . LYS   B 1 192 ? -14.746 8.486   40.532 1.00 72.59 ? 456 LYS   B NZ   1 
ATOM   3446 N  N    . THR   B 1 193 ? -7.647  6.300   41.441 1.00 33.08 ? 457 THR   B N    1 
ATOM   3447 C  CA   . THR   B 1 193 ? -6.543  6.366   42.389 1.00 32.46 ? 457 THR   B CA   1 
ATOM   3448 C  C    . THR   B 1 193 ? -5.250  6.921   41.774 1.00 34.52 ? 457 THR   B C    1 
ATOM   3449 O  O    . THR   B 1 193 ? -4.192  6.887   42.408 1.00 36.26 ? 457 THR   B O    1 
ATOM   3450 C  CB   . THR   B 1 193 ? -6.258  4.973   42.988 1.00 31.87 ? 457 THR   B CB   1 
ATOM   3451 O  OG1  . THR   B 1 193 ? -5.909  4.083   41.925 1.00 31.88 ? 457 THR   B OG1  1 
ATOM   3452 C  CG2  . THR   B 1 193 ? -7.481  4.442   43.711 1.00 32.68 ? 457 THR   B CG2  1 
ATOM   3453 N  N    . HIS   B 1 194 ? -5.337  7.446   40.547 1.00 33.76 ? 458 HIS   B N    1 
ATOM   3454 C  CA   . HIS   B 1 194 ? -4.180  7.978   39.830 1.00 33.90 ? 458 HIS   B CA   1 
ATOM   3455 C  C    . HIS   B 1 194 ? -3.000  7.013   39.771 1.00 31.99 ? 458 HIS   B C    1 
ATOM   3456 O  O    . HIS   B 1 194 ? -1.869  7.397   40.006 1.00 34.16 ? 458 HIS   B O    1 
ATOM   3457 C  CB   . HIS   B 1 194 ? -3.730  9.288   40.473 1.00 36.26 ? 458 HIS   B CB   1 
ATOM   3458 C  CG   . HIS   B 1 194 ? -4.831  10.278  40.612 1.00 45.35 ? 458 HIS   B CG   1 
ATOM   3459 N  ND1  . HIS   B 1 194 ? -5.427  10.878  39.528 1.00 50.95 ? 458 HIS   B ND1  1 
ATOM   3460 C  CD2  . HIS   B 1 194 ? -5.481  10.745  41.707 1.00 50.60 ? 458 HIS   B CD2  1 
ATOM   3461 C  CE1  . HIS   B 1 194 ? -6.374  11.700  39.945 1.00 55.47 ? 458 HIS   B CE1  1 
ATOM   3462 N  NE2  . HIS   B 1 194 ? -6.430  11.625  41.265 1.00 54.65 ? 458 HIS   B NE2  1 
ATOM   3463 N  N    . ARG   B 1 195 ? -3.283  5.753   39.448 1.00 29.97 ? 459 ARG   B N    1 
ATOM   3464 C  CA   . ARG   B 1 195 ? -2.259  4.715   39.400 1.00 28.40 ? 459 ARG   B CA   1 
ATOM   3465 C  C    . ARG   B 1 195 ? -2.164  4.033   38.043 1.00 26.37 ? 459 ARG   B C    1 
ATOM   3466 O  O    . ARG   B 1 195 ? -1.727  2.867   37.937 1.00 26.65 ? 459 ARG   B O    1 
ATOM   3467 C  CB   . ARG   B 1 195 ? -2.524  3.693   40.486 1.00 28.65 ? 459 ARG   B CB   1 
ATOM   3468 C  CG   . ARG   B 1 195 ? -2.252  4.230   41.867 1.00 29.07 ? 459 ARG   B CG   1 
ATOM   3469 C  CD   . ARG   B 1 195 ? -0.773  4.074   42.176 1.00 29.04 ? 459 ARG   B CD   1 
ATOM   3470 N  NE   . ARG   B 1 195 ? -0.495  2.643   42.446 1.00 30.09 ? 459 ARG   B NE   1 
ATOM   3471 C  CZ   . ARG   B 1 195 ? 0.709   2.136   42.689 1.00 30.91 ? 459 ARG   B CZ   1 
ATOM   3472 N  NH1  . ARG   B 1 195 ? 1.783   2.924   42.679 1.00 36.84 ? 459 ARG   B NH1  1 
ATOM   3473 N  NH2  . ARG   B 1 195 ? 0.845   0.831   42.943 1.00 29.35 ? 459 ARG   B NH2  1 
ATOM   3474 N  N    . GLN   B 1 196 ? -2.560  4.757   36.999 1.00 30.31 ? 460 GLN   B N    1 
ATOM   3475 C  CA   . GLN   B 1 196 ? -2.489  4.239   35.647 1.00 31.64 ? 460 GLN   B CA   1 
ATOM   3476 C  C    . GLN   B 1 196 ? -1.068  3.867   35.258 1.00 35.92 ? 460 GLN   B C    1 
ATOM   3477 O  O    . GLN   B 1 196 ? -0.841  2.979   34.426 1.00 34.77 ? 460 GLN   B O    1 
ATOM   3478 C  CB   . GLN   B 1 196 ? -3.036  5.264   34.669 1.00 37.04 ? 460 GLN   B CB   1 
ATOM   3479 C  CG   . GLN   B 1 196 ? -4.442  5.734   35.004 1.00 45.95 ? 460 GLN   B CG   1 
ATOM   3480 C  CD   . GLN   B 1 196 ? -4.471  7.139   35.604 1.00 49.61 ? 460 GLN   B CD   1 
ATOM   3481 O  OE1  . GLN   B 1 196 ? -3.710  7.465   36.527 1.00 43.92 ? 460 GLN   B OE1  1 
ATOM   3482 N  NE2  . GLN   B 1 196 ? -5.359  7.978   35.079 1.00 54.53 ? 460 GLN   B NE2  1 
ATOM   3483 N  N    . SER   B 1 197 ? -0.102  4.561   35.851 1.00 33.56 ? 461 SER   B N    1 
ATOM   3484 C  CA   . SER   B 1 197 ? 1.293   4.303   35.542 1.00 34.31 ? 461 SER   B CA   1 
ATOM   3485 C  C    . SER   B 1 197 ? 1.685   2.835   35.748 1.00 34.56 ? 461 SER   B C    1 
ATOM   3486 O  O    . SER   B 1 197 ? 2.606   2.370   35.091 1.00 41.98 ? 461 SER   B O    1 
ATOM   3487 C  CB   . SER   B 1 197 ? 2.187   5.199   36.401 1.00 37.26 ? 461 SER   B CB   1 
ATOM   3488 O  OG   . SER   B 1 197 ? 2.038   4.877   37.772 1.00 40.39 ? 461 SER   B OG   1 
ATOM   3489 N  N    . ILE   B 1 198 ? 1.005   2.104   36.632 1.00 31.50 ? 462 ILE   B N    1 
ATOM   3490 C  CA   . ILE   B 1 198 ? 1.471   0.742   36.912 1.00 32.01 ? 462 ILE   B CA   1 
ATOM   3491 C  C    . ILE   B 1 198 ? 1.325   -0.141  35.678 1.00 33.65 ? 462 ILE   B C    1 
ATOM   3492 O  O    . ILE   B 1 198 ? 2.016   -1.140  35.553 1.00 36.15 ? 462 ILE   B O    1 
ATOM   3493 C  CB   . ILE   B 1 198 ? 0.758   0.080   38.142 1.00 32.37 ? 462 ILE   B CB   1 
ATOM   3494 C  CG1  . ILE   B 1 198 ? -0.718  -0.286  37.852 1.00 27.68 ? 462 ILE   B CG1  1 
ATOM   3495 C  CG2  . ILE   B 1 198 ? 0.864   0.960   39.376 1.00 38.01 ? 462 ILE   B CG2  1 
ATOM   3496 C  CD1  . ILE   B 1 198 ? -1.403  -0.968  39.032 1.00 33.47 ? 462 ILE   B CD1  1 
ATOM   3497 N  N    . LEU   B 1 199 ? 0.439   0.218   34.763 1.00 33.95 ? 463 LEU   B N    1 
ATOM   3498 C  CA   . LEU   B 1 199 ? 0.151   -0.669  33.640 1.00 37.95 ? 463 LEU   B CA   1 
ATOM   3499 C  C    . LEU   B 1 199 ? 1.359   -0.891  32.742 1.00 44.69 ? 463 LEU   B C    1 
ATOM   3500 O  O    . LEU   B 1 199 ? 1.551   -1.992  32.216 1.00 46.95 ? 463 LEU   B O    1 
ATOM   3501 C  CB   . LEU   B 1 199 ? -1.023  -0.129  32.816 1.00 37.88 ? 463 LEU   B CB   1 
ATOM   3502 C  CG   . LEU   B 1 199 ? -2.425  -0.024  33.442 1.00 37.24 ? 463 LEU   B CG   1 
ATOM   3503 C  CD1  . LEU   B 1 199 ? -3.352  0.760   32.516 1.00 40.49 ? 463 LEU   B CD1  1 
ATOM   3504 C  CD2  . LEU   B 1 199 ? -3.015  -1.400  33.778 1.00 39.49 ? 463 LEU   B CD2  1 
ATOM   3505 N  N    . ALA   B 1 200 ? 2.177   0.138   32.549 1.00 44.67 ? 464 ALA   B N    1 
ATOM   3506 C  CA   . ALA   B 1 200 ? 3.334   -0.011  31.693 1.00 49.46 ? 464 ALA   B CA   1 
ATOM   3507 C  C    . ALA   B 1 200 ? 4.255   -1.020  32.342 1.00 54.13 ? 464 ALA   B C    1 
ATOM   3508 O  O    . ALA   B 1 200 ? 4.833   -1.875  31.672 1.00 58.42 ? 464 ALA   B O    1 
ATOM   3509 C  CB   . ALA   B 1 200 ? 4.031   1.307   31.487 1.00 50.47 ? 464 ALA   B CB   1 
ATOM   3510 N  N    . LYS   B 1 201 ? 4.326   -0.938  33.668 1.00 52.74 ? 465 LYS   B N    1 
ATOM   3511 C  CA   . LYS   B 1 201 ? 5.274   -1.699  34.472 1.00 50.96 ? 465 LYS   B CA   1 
ATOM   3512 C  C    . LYS   B 1 201 ? 4.891   -3.168  34.674 1.00 47.12 ? 465 LYS   B C    1 
ATOM   3513 O  O    . LYS   B 1 201 ? 5.722   -3.959  35.093 1.00 50.59 ? 465 LYS   B O    1 
ATOM   3514 C  CB   . LYS   B 1 201 ? 5.446   -1.019  35.833 1.00 49.12 ? 465 LYS   B CB   1 
ATOM   3515 C  CG   . LYS   B 1 201 ? 5.869   0.438   35.739 1.00 50.20 ? 465 LYS   B CG   1 
ATOM   3516 C  CD   . LYS   B 1 201 ? 5.786   1.139   37.088 1.00 49.17 ? 465 LYS   B CD   1 
ATOM   3517 C  CE   . LYS   B 1 201 ? 6.295   2.574   37.028 1.00 54.96 ? 465 LYS   B CE   1 
ATOM   3518 N  NZ   . LYS   B 1 201 ? 5.557   3.424   36.043 1.00 60.59 ? 465 LYS   B NZ   1 
ATOM   3519 N  N    . LEU   B 1 202 ? 3.658   -3.535  34.387 1.00 53.81 ? 466 LEU   B N    1 
ATOM   3520 C  CA   . LEU   B 1 202 ? 3.206   -4.915  34.532 1.00 54.16 ? 466 LEU   B CA   1 
ATOM   3521 C  C    . LEU   B 1 202 ? 4.113   -5.789  33.691 1.00 67.31 ? 466 LEU   B C    1 
ATOM   3522 O  O    . LEU   B 1 202 ? 4.777   -5.314  32.772 1.00 72.13 ? 466 LEU   B O    1 
ATOM   3523 C  CB   . LEU   B 1 202 ? 1.740   -5.071  34.131 1.00 46.79 ? 466 LEU   B CB   1 
ATOM   3524 C  CG   . LEU   B 1 202 ? 0.709   -4.510  35.093 1.00 41.31 ? 466 LEU   B CG   1 
ATOM   3525 C  CD1  . LEU   B 1 202 ? -0.653  -4.555  34.445 1.00 45.69 ? 466 LEU   B CD1  1 
ATOM   3526 C  CD2  . LEU   B 1 202 ? 0.731   -5.296  36.391 1.00 41.73 ? 466 LEU   B CD2  1 
ATOM   3527 N  N    . PRO   B 1 203 ? 4.169   -7.078  34.007 1.00 70.52 ? 467 PRO   B N    1 
ATOM   3528 C  CA   . PRO   B 1 203 ? 5.134   -7.862  33.251 1.00 71.16 ? 467 PRO   B CA   1 
ATOM   3529 C  C    . PRO   B 1 203 ? 4.510   -8.525  32.049 1.00 71.36 ? 467 PRO   B C    1 
ATOM   3530 O  O    . PRO   B 1 203 ? 3.300   -8.700  32.004 1.00 73.06 ? 467 PRO   B O    1 
ATOM   3531 C  CB   . PRO   B 1 203 ? 5.583   -8.916  34.276 1.00 71.19 ? 467 PRO   B CB   1 
ATOM   3532 C  CG   . PRO   B 1 203 ? 4.403   -9.114  35.137 1.00 71.56 ? 467 PRO   B CG   1 
ATOM   3533 C  CD   . PRO   B 1 203 ? 3.688   -7.789  35.204 1.00 71.51 ? 467 PRO   B CD   1 
ATOM   3534 N  N    . PRO   B 1 204 ? 5.352   -8.876  31.054 1.00 70.67 ? 468 PRO   B N    1 
ATOM   3535 C  CA   . PRO   B 1 204 ? 4.806   -9.631  29.924 1.00 73.83 ? 468 PRO   B CA   1 
ATOM   3536 C  C    . PRO   B 1 204 ? 4.155   -10.908 30.359 1.00 75.04 ? 468 PRO   B C    1 
ATOM   3537 O  O    . PRO   B 1 204 ? 4.745   -11.638 31.143 1.00 76.24 ? 468 PRO   B O    1 
ATOM   3538 C  CB   . PRO   B 1 204 ? 6.059   -10.018 29.156 1.00 75.69 ? 468 PRO   B CB   1 
ATOM   3539 C  CG   . PRO   B 1 204 ? 7.016   -8.950  29.440 1.00 70.92 ? 468 PRO   B CG   1 
ATOM   3540 C  CD   . PRO   B 1 204 ? 6.793   -8.593  30.855 1.00 68.62 ? 468 PRO   B CD   1 
ATOM   3541 N  N    . LYS   B 1 205 ? 2.983   -11.209 29.846 1.00 76.16 ? 469 LYS   B N    1 
ATOM   3542 C  CA   . LYS   B 1 205 ? 2.275   -12.393 30.301 1.00 81.15 ? 469 LYS   B CA   1 
ATOM   3543 C  C    . LYS   B 1 205 ? 3.059   -13.656 30.035 1.00 88.34 ? 469 LYS   B C    1 
ATOM   3544 O  O    . LYS   B 1 205 ? 2.644   -14.737 30.433 1.00 95.12 ? 469 LYS   B O    1 
ATOM   3545 C  CB   . LYS   B 1 205 ? 0.934   -12.502 29.599 1.00 80.83 ? 469 LYS   B CB   1 
ATOM   3546 C  CG   . LYS   B 1 205 ? -0.192  -11.794 30.325 1.00 77.14 ? 469 LYS   B CG   1 
ATOM   3547 C  CD   . LYS   B 1 205 ? -1.526  -12.057 29.659 1.00 78.27 ? 469 LYS   B CD   1 
ATOM   3548 C  CE   . LYS   B 1 205 ? -1.863  -13.529 29.667 1.00 81.25 ? 469 LYS   B CE   1 
ATOM   3549 N  NZ   . LYS   B 1 205 ? -1.978  -14.080 28.290 1.00 81.88 ? 469 LYS   B NZ   1 
ATOM   3550 N  N    . GLY   B 1 206 ? 4.199   -13.532 29.373 1.00 85.38 ? 470 GLY   B N    1 
ATOM   3551 C  CA   . GLY   B 1 206 ? 4.939   -14.706 28.990 1.00 86.91 ? 470 GLY   B CA   1 
ATOM   3552 C  C    . GLY   B 1 206 ? 6.047   -15.021 29.915 1.00 86.49 ? 470 GLY   B C    1 
ATOM   3553 O  O    . GLY   B 1 206 ? 6.506   -16.149 29.944 1.00 88.48 ? 470 GLY   B O    1 
ATOM   3554 N  N    . LYS   B 1 207 ? 6.512   -14.038 30.657 1.00 78.47 ? 471 LYS   B N    1 
ATOM   3555 C  CA   . LYS   B 1 207 ? 7.499   -14.351 31.661 1.00 77.26 ? 471 LYS   B CA   1 
ATOM   3556 C  C    . LYS   B 1 207 ? 6.732   -15.201 32.644 1.00 67.85 ? 471 LYS   B C    1 
ATOM   3557 O  O    . LYS   B 1 207 ? 7.299   -16.002 33.358 1.00 65.65 ? 471 LYS   B O    1 
ATOM   3558 C  CB   . LYS   B 1 207 ? 8.041   -13.110 32.337 1.00 82.28 ? 471 LYS   B CB   1 
ATOM   3559 C  CG   . LYS   B 1 207 ? 8.614   -12.081 31.385 1.00 88.24 ? 471 LYS   B CG   1 
ATOM   3560 C  CD   . LYS   B 1 207 ? 10.063  -12.399 31.047 1.00 87.35 ? 471 LYS   B CD   1 
ATOM   3561 C  CE   . LYS   B 1 207 ? 10.853  -12.776 32.289 1.00 82.28 ? 471 LYS   B CE   1 
ATOM   3562 N  NZ   . LYS   B 1 207 ? 12.268  -13.112 31.970 1.00 79.76 ? 471 LYS   B NZ   1 
ATOM   3563 N  N    . LEU   B 1 208 ? 5.421   -15.069 32.624 1.00 60.02 ? 472 LEU   B N    1 
ATOM   3564 C  CA   . LEU   B 1 208 ? 4.680   -15.796 33.636 1.00 56.53 ? 472 LEU   B CA   1 
ATOM   3565 C  C    . LEU   B 1 208 ? 4.223   -17.148 33.092 1.00 60.73 ? 472 LEU   B C    1 
ATOM   3566 O  O    . LEU   B 1 208 ? 4.142   -18.127 33.828 1.00 57.80 ? 472 LEU   B O    1 
ATOM   3567 C  CB   . LEU   B 1 208 ? 3.491   -14.963 34.089 1.00 54.94 ? 472 LEU   B CB   1 
ATOM   3568 C  CG   . LEU   B 1 208 ? 2.392   -15.530 34.972 1.00 50.45 ? 472 LEU   B CG   1 
ATOM   3569 C  CD1  . LEU   B 1 208 ? 2.979   -16.062 36.255 1.00 48.46 ? 472 LEU   B CD1  1 
ATOM   3570 C  CD2  . LEU   B 1 208 ? 1.383   -14.421 35.253 1.00 52.64 ? 472 LEU   B CD2  1 
ATOM   3571 N  N    . ARG   B 1 209 ? 3.926   -17.193 31.796 1.00 64.16 ? 473 ARG   B N    1 
ATOM   3572 C  CA   . ARG   B 1 209 ? 3.585   -18.447 31.133 1.00 64.74 ? 473 ARG   B CA   1 
ATOM   3573 C  C    . ARG   B 1 209 ? 4.833   -19.347 31.029 1.00 60.42 ? 473 ARG   B C    1 
ATOM   3574 O  O    . ARG   B 1 209 ? 4.729   -20.575 31.047 1.00 61.24 ? 473 ARG   B O    1 
ATOM   3575 C  CB   . ARG   B 1 209 ? 2.968   -18.168 29.752 1.00 71.38 ? 473 ARG   B CB   1 
ATOM   3576 C  CG   . ARG   B 1 209 ? 2.323   -19.375 29.062 1.00 74.17 ? 473 ARG   B CG   1 
ATOM   3577 C  CD   . ARG   B 1 209 ? 1.658   -18.978 27.737 1.00 80.04 ? 473 ARG   B CD   1 
ATOM   3578 N  NE   . ARG   B 1 209 ? 1.709   -20.043 26.734 1.00 84.65 ? 473 ARG   B NE   1 
ATOM   3579 C  CZ   . ARG   B 1 209 ? 0.723   -20.904 26.498 1.00 87.75 ? 473 ARG   B CZ   1 
ATOM   3580 N  NH1  . ARG   B 1 209 ? -0.406  -20.825 27.195 1.00 89.01 ? 473 ARG   B NH1  1 
ATOM   3581 N  NH2  . ARG   B 1 209 ? 0.862   -21.840 25.560 1.00 87.94 ? 473 ARG   B NH2  1 
ATOM   3582 N  N    . SER   B 1 210 ? 6.012   -18.737 30.950 1.00 49.09 ? 474 SER   B N    1 
ATOM   3583 C  CA   . SER   B 1 210 ? 7.264   -19.485 30.940 1.00 45.72 ? 474 SER   B CA   1 
ATOM   3584 C  C    . SER   B 1 210 ? 7.737   -20.016 32.309 1.00 49.38 ? 474 SER   B C    1 
ATOM   3585 O  O    . SER   B 1 210 ? 8.426   -21.055 32.410 1.00 44.09 ? 474 SER   B O    1 
ATOM   3586 C  CB   . SER   B 1 210 ? 8.370   -18.632 30.382 1.00 47.91 ? 474 SER   B CB   1 
ATOM   3587 O  OG   . SER   B 1 210 ? 9.590   -19.234 30.757 1.00 49.75 ? 474 SER   B OG   1 
ATOM   3588 N  N    . LEU   B 1 211 ? 7.413   -19.268 33.356 1.00 42.52 ? 475 LEU   B N    1 
ATOM   3589 C  CA   . LEU   B 1 211 ? 7.677   -19.706 34.707 1.00 35.99 ? 475 LEU   B CA   1 
ATOM   3590 C  C    . LEU   B 1 211 ? 6.767   -20.883 35.027 1.00 35.49 ? 475 LEU   B C    1 
ATOM   3591 O  O    . LEU   B 1 211 ? 7.196   -21.886 35.595 1.00 38.52 ? 475 LEU   B O    1 
ATOM   3592 C  CB   . LEU   B 1 211 ? 7.464   -18.539 35.667 1.00 39.39 ? 475 LEU   B CB   1 
ATOM   3593 C  CG   . LEU   B 1 211 ? 7.550   -18.757 37.153 1.00 33.01 ? 475 LEU   B CG   1 
ATOM   3594 C  CD1  . LEU   B 1 211 ? 8.864   -19.386 37.559 1.00 38.36 ? 475 LEU   B CD1  1 
ATOM   3595 C  CD2  . LEU   B 1 211 ? 7.362   -17.424 37.810 1.00 29.03 ? 475 LEU   B CD2  1 
ATOM   3596 N  N    . CYS   B 1 212 ? 5.511   -20.790 34.616 1.00 37.63 ? 476 CYS   B N    1 
ATOM   3597 C  CA   . CYS   B 1 212 ? 4.567   -21.880 34.833 1.00 38.53 ? 476 CYS   B CA   1 
ATOM   3598 C  C    . CYS   B 1 212 ? 4.996   -23.151 34.132 1.00 38.39 ? 476 CYS   B C    1 
ATOM   3599 O  O    . CYS   B 1 212 ? 4.851   -24.234 34.691 1.00 36.51 ? 476 CYS   B O    1 
ATOM   3600 C  CB   . CYS   B 1 212 ? 3.188   -21.472 34.358 1.00 44.67 ? 476 CYS   B CB   1 
ATOM   3601 S  SG   . CYS   B 1 212 ? 2.649   -20.078 35.253 1.00 46.54 ? 476 CYS   B SG   1 
ATOM   3602 N  N    . SER   B 1 213 ? 5.505   -23.005 32.911 1.00 36.32 ? 477 SER   B N    1 
ATOM   3603 C  CA   . SER   B 1 213 ? 6.058   -24.108 32.136 1.00 40.49 ? 477 SER   B CA   1 
ATOM   3604 C  C    . SER   B 1 213 ? 7.151   -24.835 32.898 1.00 35.52 ? 477 SER   B C    1 
ATOM   3605 O  O    . SER   B 1 213 ? 7.176   -26.062 32.917 1.00 33.04 ? 477 SER   B O    1 
ATOM   3606 C  CB   . SER   B 1 213 ? 6.633   -23.605 30.810 1.00 47.41 ? 477 SER   B CB   1 
ATOM   3607 O  OG   . SER   B 1 213 ? 5.663   -22.895 30.064 1.00 59.81 ? 477 SER   B OG   1 
ATOM   3608 N  N    . GLN   B 1 214 ? 8.065   -24.065 33.500 1.00 33.21 ? 478 GLN   B N    1 
ATOM   3609 C  CA   . GLN   B 1 214 ? 9.156   -24.644 34.280 1.00 33.39 ? 478 GLN   B CA   1 
ATOM   3610 C  C    . GLN   B 1 214 ? 8.585   -25.431 35.468 1.00 29.66 ? 478 GLN   B C    1 
ATOM   3611 O  O    . GLN   B 1 214 ? 9.034   -26.540 35.787 1.00 30.12 ? 478 GLN   B O    1 
ATOM   3612 C  CB   . GLN   B 1 214 ? 10.095  -23.555 34.795 1.00 35.12 ? 478 GLN   B CB   1 
ATOM   3613 C  CG   . GLN   B 1 214 ? 11.037  -22.933 33.787 1.00 44.83 ? 478 GLN   B CG   1 
ATOM   3614 C  CD   . GLN   B 1 214 ? 12.106  -22.090 34.481 1.00 46.25 ? 478 GLN   B CD   1 
ATOM   3615 O  OE1  . GLN   B 1 214 ? 13.039  -22.620 35.104 1.00 49.77 ? 478 GLN   B OE1  1 
ATOM   3616 N  NE2  . GLN   B 1 214 ? 11.954  -20.780 34.408 1.00 47.06 ? 478 GLN   B NE2  1 
ATOM   3617 N  N    . HIS   B 1 215 ? 7.594   -24.824 36.121 1.00 29.78 ? 479 HIS   B N    1 
ATOM   3618 C  CA   . HIS   B 1 215 ? 6.955   -25.420 37.284 1.00 26.58 ? 479 HIS   B CA   1 
ATOM   3619 C  C    . HIS   B 1 215 ? 6.280   -26.723 36.868 1.00 30.95 ? 479 HIS   B C    1 
ATOM   3620 O  O    . HIS   B 1 215 ? 6.394   -27.726 37.558 1.00 28.20 ? 479 HIS   B O    1 
ATOM   3621 C  CB   . HIS   B 1 215 ? 5.936   -24.436 37.901 1.00 25.33 ? 479 HIS   B CB   1 
ATOM   3622 C  CG   . HIS   B 1 215 ? 4.853   -25.114 38.667 1.00 26.53 ? 479 HIS   B CG   1 
ATOM   3623 N  ND1  . HIS   B 1 215 ? 5.040   -25.612 39.931 1.00 30.36 ? 479 HIS   B ND1  1 
ATOM   3624 C  CD2  . HIS   B 1 215 ? 3.550   -25.359 38.349 1.00 27.26 ? 479 HIS   B CD2  1 
ATOM   3625 C  CE1  . HIS   B 1 215 ? 3.915   -26.156 40.359 1.00 30.13 ? 479 HIS   B CE1  1 
ATOM   3626 N  NE2  . HIS   B 1 215 ? 2.998   -26.021 39.407 1.00 28.38 ? 479 HIS   B NE2  1 
ATOM   3627 N  N    . VAL   B 1 216 ? 5.610   -26.725 35.716 1.00 26.65 ? 480 VAL   B N    1 
ATOM   3628 C  CA   . VAL   B 1 216 ? 4.871   -27.912 35.364 1.00 29.89 ? 480 VAL   B CA   1 
ATOM   3629 C  C    . VAL   B 1 216 ? 5.837   -29.050 35.096 1.00 32.92 ? 480 VAL   B C    1 
ATOM   3630 O  O    . VAL   B 1 216 ? 5.539   -30.184 35.486 1.00 30.27 ? 480 VAL   B O    1 
ATOM   3631 C  CB   . VAL   B 1 216 ? 3.947   -27.711 34.169 1.00 32.97 ? 480 VAL   B CB   1 
ATOM   3632 C  CG1  . VAL   B 1 216 ? 3.497   -29.046 33.704 1.00 40.33 ? 480 VAL   B CG1  1 
ATOM   3633 C  CG2  . VAL   B 1 216 ? 2.743   -26.855 34.583 1.00 33.86 ? 480 VAL   B CG2  1 
ATOM   3634 N  N    . GLU   B 1 217 ? 6.976   -28.756 34.447 1.00 32.18 ? 481 GLU   B N    1 
ATOM   3635 C  CA   . GLU   B 1 217 ? 7.982   -29.783 34.184 1.00 37.02 ? 481 GLU   B CA   1 
ATOM   3636 C  C    . GLU   B 1 217 ? 8.554   -30.301 35.507 1.00 30.10 ? 481 GLU   B C    1 
ATOM   3637 O  O    . GLU   B 1 217 ? 8.702   -31.510 35.694 1.00 30.26 ? 481 GLU   B O    1 
ATOM   3638 C  CB   . GLU   B 1 217 ? 9.137   -29.258 33.310 1.00 48.56 ? 481 GLU   B CB   1 
ATOM   3639 C  CG   . GLU   B 1 217 ? 8.794   -28.845 31.878 1.00 65.17 ? 481 GLU   B CG   1 
ATOM   3640 C  CD   . GLU   B 1 217 ? 10.004  -28.258 31.124 1.00 75.37 ? 481 GLU   B CD   1 
ATOM   3641 O  OE1  . GLU   B 1 217 ? 10.802  -27.499 31.737 1.00 75.53 ? 481 GLU   B OE1  1 
ATOM   3642 O  OE2  . GLU   B 1 217 ? 10.155  -28.557 29.917 1.00 79.29 ? 481 GLU   B OE2  1 
ATOM   3643 N  N    . ARG   B 1 218 ? 8.896   -29.398 36.417 1.00 27.09 ? 482 ARG   B N    1 
ATOM   3644 C  CA   . ARG   B 1 218 ? 9.541   -29.840 37.638 1.00 28.15 ? 482 ARG   B CA   1 
ATOM   3645 C  C    . ARG   B 1 218 ? 8.584   -30.618 38.540 1.00 27.47 ? 482 ARG   B C    1 
ATOM   3646 O  O    . ARG   B 1 218 ? 8.970   -31.591 39.196 1.00 23.54 ? 482 ARG   B O    1 
ATOM   3647 C  CB   . ARG   B 1 218 ? 10.128  -28.683 38.414 1.00 28.89 ? 482 ARG   B CB   1 
ATOM   3648 C  CG   . ARG   B 1 218 ? 10.940  -29.205 39.578 1.00 35.66 ? 482 ARG   B CG   1 
ATOM   3649 C  CD   . ARG   B 1 218 ? 12.078  -30.105 39.076 1.00 46.25 ? 482 ARG   B CD   1 
ATOM   3650 N  NE   . ARG   B 1 218 ? 12.831  -30.656 40.193 1.00 50.00 ? 482 ARG   B NE   1 
ATOM   3651 C  CZ   . ARG   B 1 218 ? 13.972  -31.324 40.071 1.00 46.56 ? 482 ARG   B CZ   1 
ATOM   3652 N  NH1  . ARG   B 1 218 ? 14.481  -31.524 38.865 1.00 39.25 ? 482 ARG   B NH1  1 
ATOM   3653 N  NH2  . ARG   B 1 218 ? 14.582  -31.793 41.153 1.00 36.12 ? 482 ARG   B NH2  1 
ATOM   3654 N  N    . LEU   B 1 219 ? 7.329   -30.193 38.557 1.00 23.96 ? 483 LEU   B N    1 
ATOM   3655 C  CA   . LEU   B 1 219 ? 6.314   -30.870 39.335 1.00 23.22 ? 483 LEU   B CA   1 
ATOM   3656 C  C    . LEU   B 1 219 ? 6.189   -32.345 38.893 1.00 23.60 ? 483 LEU   B C    1 
ATOM   3657 O  O    . LEU   B 1 219 ? 6.053   -33.244 39.732 1.00 26.36 ? 483 LEU   B O    1 
ATOM   3658 C  CB   . LEU   B 1 219 ? 4.981   -30.117 39.192 1.00 25.06 ? 483 LEU   B CB   1 
ATOM   3659 C  CG   . LEU   B 1 219 ? 3.799   -30.764 39.907 1.00 27.65 ? 483 LEU   B CG   1 
ATOM   3660 C  CD1  . LEU   B 1 219 ? 4.046   -30.651 41.392 1.00 27.36 ? 483 LEU   B CD1  1 
ATOM   3661 C  CD2  . LEU   B 1 219 ? 2.483   -30.053 39.510 1.00 32.28 ? 483 LEU   B CD2  1 
ATOM   3662 N  N    . GLN   B 1 220 ? 6.228   -32.612 37.596 1.00 24.46 ? 484 GLN   B N    1 
ATOM   3663 C  CA   . GLN   B 1 220 ? 6.043   -33.985 37.144 1.00 25.23 ? 484 GLN   B CA   1 
ATOM   3664 C  C    . GLN   B 1 220 ? 7.243   -34.845 37.511 1.00 24.67 ? 484 GLN   B C    1 
ATOM   3665 O  O    . GLN   B 1 220 ? 7.062   -36.048 37.748 1.00 26.90 ? 484 GLN   B O    1 
ATOM   3666 C  CB   . GLN   B 1 220 ? 5.726   -34.064 35.644 1.00 38.10 ? 484 GLN   B CB   1 
ATOM   3667 C  CG   . GLN   B 1 220 ? 6.721   -33.506 34.662 1.00 46.91 ? 484 GLN   B CG   1 
ATOM   3668 C  CD   . GLN   B 1 220 ? 6.287   -33.753 33.211 1.00 55.63 ? 484 GLN   B CD   1 
ATOM   3669 O  OE1  . GLN   B 1 220 ? 5.132   -34.118 32.946 1.00 57.37 ? 484 GLN   B OE1  1 
ATOM   3670 N  NE2  . GLN   B 1 220 ? 7.217   -33.558 32.269 1.00 59.84 ? 484 GLN   B NE2  1 
ATOM   3671 N  N    . ILE   B 1 221 ? 8.423   -34.232 37.577 1.00 24.32 ? 485 ILE   B N    1 
ATOM   3672 C  CA   . ILE   B 1 221 ? 9.639   -34.943 38.038 1.00 24.14 ? 485 ILE   B CA   1 
ATOM   3673 C  C    . ILE   B 1 221 ? 9.508   -35.300 39.518 1.00 23.62 ? 485 ILE   B C    1 
ATOM   3674 O  O    . ILE   B 1 221 ? 9.721   -36.452 39.880 1.00 23.61 ? 485 ILE   B O    1 
ATOM   3675 C  CB   . ILE   B 1 221 ? 10.884  -34.128 37.785 1.00 24.25 ? 485 ILE   B CB   1 
ATOM   3676 C  CG1  . ILE   B 1 221 ? 11.153  -34.093 36.283 1.00 29.26 ? 485 ILE   B CG1  1 
ATOM   3677 C  CG2  . ILE   B 1 221 ? 12.124  -34.783 38.507 1.00 25.55 ? 485 ILE   B CG2  1 
ATOM   3678 C  CD1  . ILE   B 1 221 ? 12.336  -33.130 35.918 1.00 28.25 ? 485 ILE   B CD1  1 
ATOM   3679 N  N    . PHE   B 1 222 ? 9.100   -34.350 40.358 1.00 22.80 ? 486 PHE   B N    1 
ATOM   3680 C  CA   . PHE   B 1 222 ? 8.898   -34.682 41.772 1.00 22.49 ? 486 PHE   B CA   1 
ATOM   3681 C  C    . PHE   B 1 222 ? 7.883   -35.775 41.990 1.00 22.85 ? 486 PHE   B C    1 
ATOM   3682 O  O    . PHE   B 1 222 ? 8.095   -36.681 42.799 1.00 23.58 ? 486 PHE   B O    1 
ATOM   3683 C  CB   . PHE   B 1 222 ? 8.491   -33.449 42.596 1.00 22.68 ? 486 PHE   B CB   1 
ATOM   3684 C  CG   . PHE   B 1 222 ? 9.607   -32.461 42.817 1.00 22.12 ? 486 PHE   B CG   1 
ATOM   3685 C  CD1  . PHE   B 1 222 ? 10.873  -32.864 43.240 1.00 22.89 ? 486 PHE   B CD1  1 
ATOM   3686 C  CD2  . PHE   B 1 222 ? 9.402   -31.118 42.616 1.00 21.82 ? 486 PHE   B CD2  1 
ATOM   3687 C  CE1  . PHE   B 1 222 ? 11.890  -31.909 43.448 1.00 23.97 ? 486 PHE   B CE1  1 
ATOM   3688 C  CE2  . PHE   B 1 222 ? 10.372  -30.190 42.831 1.00 21.85 ? 486 PHE   B CE2  1 
ATOM   3689 C  CZ   . PHE   B 1 222 ? 11.648  -30.576 43.248 1.00 22.45 ? 486 PHE   B CZ   1 
ATOM   3690 N  N    . GLN   B 1 223 ? 6.733   -35.675 41.296 1.00 23.17 ? 487 GLN   B N    1 
ATOM   3691 C  CA   . GLN   B 1 223 ? 5.729   -36.699 41.394 1.00 23.80 ? 487 GLN   B CA   1 
ATOM   3692 C  C    . GLN   B 1 223 ? 6.189   -38.055 40.914 1.00 26.75 ? 487 GLN   B C    1 
ATOM   3693 O  O    . GLN   B 1 223 ? 5.694   -39.063 41.382 1.00 29.70 ? 487 GLN   B O    1 
ATOM   3694 C  CB   . GLN   B 1 223 ? 4.510   -36.244 40.609 1.00 24.35 ? 487 GLN   B CB   1 
ATOM   3695 C  CG   . GLN   B 1 223 ? 3.637   -35.318 41.431 1.00 31.80 ? 487 GLN   B CG   1 
ATOM   3696 C  CD   . GLN   B 1 223 ? 2.871   -36.123 42.504 1.00 42.64 ? 487 GLN   B CD   1 
ATOM   3697 O  OE1  . GLN   B 1 223 ? 3.125   -36.002 43.696 1.00 52.46 ? 487 GLN   B OE1  1 
ATOM   3698 N  NE2  . GLN   B 1 223 ? 1.953   -36.987 42.054 1.00 53.88 ? 487 GLN   B NE2  1 
ATOM   3699 N  N    . HIS   B 1 224 ? 7.130   -38.074 39.985 1.00 24.46 ? 488 HIS   B N    1 
ATOM   3700 C  CA   . HIS   B 1 224 ? 7.689   -39.333 39.543 1.00 25.26 ? 488 HIS   B CA   1 
ATOM   3701 C  C    . HIS   B 1 224 ? 8.589   -39.927 40.631 1.00 28.04 ? 488 HIS   B C    1 
ATOM   3702 O  O    . HIS   B 1 224 ? 8.537   -41.126 40.937 1.00 26.50 ? 488 HIS   B O    1 
ATOM   3703 C  CB   . HIS   B 1 224 ? 8.466   -39.103 38.258 1.00 26.38 ? 488 HIS   B CB   1 
ATOM   3704 C  CG   . HIS   B 1 224 ? 9.116   -40.331 37.733 1.00 26.53 ? 488 HIS   B CG   1 
ATOM   3705 N  ND1  . HIS   B 1 224 ? 8.397   -41.359 37.166 1.00 31.15 ? 488 HIS   B ND1  1 
ATOM   3706 C  CD2  . HIS   B 1 224 ? 10.417  -40.712 37.703 1.00 28.47 ? 488 HIS   B CD2  1 
ATOM   3707 C  CE1  . HIS   B 1 224 ? 9.226   -42.314 36.790 1.00 35.39 ? 488 HIS   B CE1  1 
ATOM   3708 N  NE2  . HIS   B 1 224 ? 10.456  -41.949 37.120 1.00 36.25 ? 488 HIS   B NE2  1 
ATOM   3709 N  N    . LEU   B 1 225 ? 9.409   -39.074 41.227 1.00 24.29 ? 489 LEU   B N    1 
ATOM   3710 C  CA   . LEU   B 1 225 ? 10.394  -39.570 42.177 1.00 24.46 ? 489 LEU   B CA   1 
ATOM   3711 C  C    . LEU   B 1 225 ? 9.691   -39.941 43.472 1.00 27.31 ? 489 LEU   B C    1 
ATOM   3712 O  O    . LEU   B 1 225 ? 10.047  -40.965 44.053 1.00 32.59 ? 489 LEU   B O    1 
ATOM   3713 C  CB   . LEU   B 1 225 ? 11.483  -38.537 42.391 1.00 24.43 ? 489 LEU   B CB   1 
ATOM   3714 C  CG   . LEU   B 1 225 ? 12.235  -38.209 41.118 1.00 24.34 ? 489 LEU   B CG   1 
ATOM   3715 C  CD1  . LEU   B 1 225 ? 13.121  -37.028 41.469 1.00 29.37 ? 489 LEU   B CD1  1 
ATOM   3716 C  CD2  . LEU   B 1 225 ? 13.071  -39.398 40.682 1.00 28.94 ? 489 LEU   B CD2  1 
ATOM   3717 N  N    . HIS   B 1 226 ? 8.674   -39.156 43.886 1.00 24.18 ? 490 HIS   B N    1 
ATOM   3718 C  CA   . HIS   B 1 226 ? 7.973   -39.408 45.137 1.00 28.03 ? 490 HIS   B CA   1 
ATOM   3719 C  C    . HIS   B 1 226 ? 6.518   -39.062 45.011 1.00 30.78 ? 490 HIS   B C    1 
ATOM   3720 O  O    . HIS   B 1 226 ? 6.067   -37.972 45.378 1.00 28.07 ? 490 HIS   B O    1 
ATOM   3721 C  CB   . HIS   B 1 226 ? 8.621   -38.612 46.272 1.00 30.08 ? 490 HIS   B CB   1 
ATOM   3722 C  CG   . HIS   B 1 226 ? 10.029  -39.017 46.527 1.00 40.90 ? 490 HIS   B CG   1 
ATOM   3723 N  ND1  . HIS   B 1 226 ? 10.360  -40.229 47.095 1.00 50.82 ? 490 HIS   B ND1  1 
ATOM   3724 C  CD2  . HIS   B 1 226 ? 11.204  -38.398 46.247 1.00 36.75 ? 490 HIS   B CD2  1 
ATOM   3725 C  CE1  . HIS   B 1 226 ? 11.677  -40.335 47.173 1.00 44.32 ? 490 HIS   B CE1  1 
ATOM   3726 N  NE2  . HIS   B 1 226 ? 12.211  -39.235 46.665 1.00 40.21 ? 490 HIS   B NE2  1 
ATOM   3727 N  N    . PRO   B 1 227 ? 5.735   -39.994 44.481 1.00 31.59 ? 491 PRO   B N    1 
ATOM   3728 C  CA   . PRO   B 1 227 ? 4.315   -39.699 44.324 1.00 32.73 ? 491 PRO   B CA   1 
ATOM   3729 C  C    . PRO   B 1 227 ? 3.687   -39.386 45.693 1.00 33.64 ? 491 PRO   B C    1 
ATOM   3730 O  O    . PRO   B 1 227 ? 4.003   -40.091 46.673 1.00 39.37 ? 491 PRO   B O    1 
ATOM   3731 C  CB   . PRO   B 1 227 ? 3.746   -41.002 43.728 1.00 37.22 ? 491 PRO   B CB   1 
ATOM   3732 C  CG   . PRO   B 1 227 ? 4.896   -41.802 43.322 1.00 30.15 ? 491 PRO   B CG   1 
ATOM   3733 C  CD   . PRO   B 1 227 ? 6.113   -41.363 44.063 1.00 32.50 ? 491 PRO   B CD   1 
ATOM   3734 N  N    . ILE   B 1 228 ? 2.892   -38.335 45.780 1.00 30.50 ? 492 ILE   B N    1 
ATOM   3735 C  CA   . ILE   B 1 228 ? 2.327   -37.930 47.078 1.00 29.60 ? 492 ILE   B CA   1 
ATOM   3736 C  C    . ILE   B 1 228 ? 1.082   -38.740 47.447 1.00 38.40 ? 492 ILE   B C    1 
ATOM   3737 O  O    . ILE   B 1 228 ? 0.443   -39.297 46.565 1.00 43.92 ? 492 ILE   B O    1 
ATOM   3738 C  CB   . ILE   B 1 228 ? 2.058   -36.462 47.075 1.00 38.11 ? 492 ILE   B CB   1 
ATOM   3739 C  CG1  . ILE   B 1 228 ? 3.364   -35.675 46.937 1.00 34.35 ? 492 ILE   B CG1  1 
ATOM   3740 C  CG2  . ILE   B 1 228 ? 1.288   -36.060 48.326 1.00 41.63 ? 492 ILE   B CG2  1 
ATOM   3741 C  CD1  . ILE   B 1 228 ? 4.106   -35.459 48.226 1.00 40.98 ? 492 ILE   B CD1  1 
HETATM 3742 C  C16  . A1BW2 C 2 .   ? 7.886   20.385  60.632 1.00 18.62 ? 601 A1BW2 A C16  1 
HETATM 3743 C  C17  . A1BW2 C 2 .   ? 8.503   21.395  61.335 1.00 23.21 ? 601 A1BW2 A C17  1 
HETATM 3744 C  C15  . A1BW2 C 2 .   ? 7.547   19.193  61.263 1.00 20.37 ? 601 A1BW2 A C15  1 
HETATM 3745 C  C18  . A1BW2 C 2 .   ? 8.819   21.293  62.676 1.00 24.36 ? 601 A1BW2 A C18  1 
HETATM 3746 C  C21  . A1BW2 C 2 .   ? 7.848   19.111  62.596 1.00 21.91 ? 601 A1BW2 A C21  1 
HETATM 3747 C  C19  . A1BW2 C 2 .   ? 8.465   20.109  63.303 1.00 29.23 ? 601 A1BW2 A C19  1 
HETATM 3748 C  C14  . A1BW2 C 2 .   ? 7.018   18.112  60.478 1.00 22.87 ? 601 A1BW2 A C14  1 
HETATM 3749 C  C10  . A1BW2 C 2 .   ? 7.621   17.583  59.356 1.00 20.63 ? 601 A1BW2 A C10  1 
HETATM 3750 C  C12  . A1BW2 C 2 .   ? 5.863   16.238  59.400 1.00 23.34 ? 601 A1BW2 A C12  1 
HETATM 3751 C  C8   . A1BW2 C 2 .   ? 8.877   18.144  58.845 1.00 25.15 ? 601 A1BW2 A C8   1 
HETATM 3752 C  C33  . A1BW2 C 2 .   ? 5.003   15.162  59.051 1.00 29.53 ? 601 A1BW2 A C33  1 
HETATM 3753 C  C5   . A1BW2 C 2 .   ? 12.230  17.710  60.136 1.00 35.27 ? 601 A1BW2 A C5   1 
HETATM 3754 C  C4   . A1BW2 C 2 .   ? 11.334  17.240  61.255 1.00 36.98 ? 601 A1BW2 A C4   1 
HETATM 3755 C  C6   . A1BW2 C 2 .   ? 11.280  18.330  59.151 1.00 29.77 ? 601 A1BW2 A C6   1 
HETATM 3756 C  C2   . A1BW2 C 2 .   ? 10.066  16.821  60.549 1.00 27.83 ? 601 A1BW2 A C2   1 
HETATM 3757 C  C1   . A1BW2 C 2 .   ? 10.288  15.507  59.877 1.00 31.45 ? 601 A1BW2 A C1   1 
HETATM 3758 C  C38  . A1BW2 C 2 .   ? 5.571   11.063  56.748 1.00 45.50 ? 601 A1BW2 A C38  1 
HETATM 3759 C  C39  . A1BW2 C 2 .   ? 6.821   12.110  58.611 1.00 42.34 ? 601 A1BW2 A C39  1 
HETATM 3760 C  C36  . A1BW2 C 2 .   ? 4.889   13.251  57.544 1.00 40.87 ? 601 A1BW2 A C36  1 
HETATM 3761 C  C23  . A1BW2 C 2 .   ? 9.584   22.444  63.350 1.00 20.78 ? 601 A1BW2 A C23  1 
HETATM 3762 C  C37  . A1BW2 C 2 .   ? 6.095   12.355  57.312 1.00 43.29 ? 601 A1BW2 A C37  1 
HETATM 3763 C  C25  . A1BW2 C 2 .   ? 9.210   23.819  62.902 1.00 27.39 ? 601 A1BW2 A C25  1 
HETATM 3764 C  C29  . A1BW2 C 2 .   ? 11.065  22.208  63.036 1.00 27.58 ? 601 A1BW2 A C29  1 
HETATM 3765 N  N11  . A1BW2 C 2 .   ? 6.982   16.537  58.740 1.00 23.50 ? 601 A1BW2 A N11  1 
HETATM 3766 N  N7   . A1BW2 C 2 .   ? 9.987   17.838  59.561 1.00 28.11 ? 601 A1BW2 A N7   1 
HETATM 3767 N  N35  . A1BW2 C 2 .   ? 5.329   14.588  57.852 1.00 33.44 ? 601 A1BW2 A N35  1 
HETATM 3768 O  O9   . A1BW2 C 2 .   ? 8.937   18.873  57.872 1.00 24.39 ? 601 A1BW2 A O9   1 
HETATM 3769 O  O34  . A1BW2 C 2 .   ? 4.107   14.759  59.789 1.00 28.69 ? 601 A1BW2 A O34  1 
HETATM 3770 O  O24  . A1BW2 C 2 .   ? 9.548   22.432  64.747 1.00 22.84 ? 601 A1BW2 A O24  1 
HETATM 3771 O  O40  . A1BW2 C 2 .   ? 7.020   12.919  56.384 1.00 40.80 ? 601 A1BW2 A O40  1 
HETATM 3772 F  F26  . A1BW2 C 2 .   ? 7.841   23.937  62.938 1.00 25.36 ? 601 A1BW2 A F26  1 
HETATM 3773 F  F27  . A1BW2 C 2 .   ? 9.642   24.147  61.679 1.00 26.15 ? 601 A1BW2 A F27  1 
HETATM 3774 F  F28  . A1BW2 C 2 .   ? 9.675   24.761  63.736 1.00 29.22 ? 601 A1BW2 A F28  1 
HETATM 3775 F  F30  . A1BW2 C 2 .   ? 11.290  22.152  61.717 1.00 27.63 ? 601 A1BW2 A F30  1 
HETATM 3776 F  F31  . A1BW2 C 2 .   ? 11.485  21.074  63.615 1.00 29.37 ? 601 A1BW2 A F31  1 
HETATM 3777 F  F32  . A1BW2 C 2 .   ? 11.756  23.184  63.620 1.00 28.71 ? 601 A1BW2 A F32  1 
HETATM 3778 S  S13  . A1BW2 C 2 .   ? 5.558   17.215  60.766 1.00 23.95 ? 601 A1BW2 A S13  1 
HETATM 3779 CL CL22 . A1BW2 C 2 .   ? 7.481   17.621  63.415 1.00 26.41 ? 601 A1BW2 A CL22 1 
HETATM 3780 CL CL20 . A1BW2 C 2 .   ? 8.822   19.815  64.974 1.00 44.75 ? 601 A1BW2 A CL20 1 
HETATM 3781 H  H50  . A1BW2 C 2 .   ? 7.656   20.523  59.582 1.00 22.35 ? 601 A1BW2 A H50  1 
HETATM 3782 H  H51  . A1BW2 C 2 .   ? 8.762   22.307  60.809 1.00 27.85 ? 601 A1BW2 A H51  1 
HETATM 3783 H  H46  . A1BW2 C 2 .   ? 12.953  18.445  60.498 1.00 42.32 ? 601 A1BW2 A H46  1 
HETATM 3784 H  H47  . A1BW2 C 2 .   ? 12.765  16.869  59.686 1.00 42.32 ? 601 A1BW2 A H47  1 
HETATM 3785 H  H45  . A1BW2 C 2 .   ? 11.137  18.049  61.963 1.00 44.38 ? 601 A1BW2 A H45  1 
HETATM 3786 H  H44  . A1BW2 C 2 .   ? 11.782  16.397  61.787 1.00 44.38 ? 601 A1BW2 A H44  1 
HETATM 3787 H  H48  . A1BW2 C 2 .   ? 11.282  19.422  59.209 1.00 35.72 ? 601 A1BW2 A H48  1 
HETATM 3788 H  H49  . A1BW2 C 2 .   ? 11.478  18.003  58.127 1.00 35.72 ? 601 A1BW2 A H49  1 
HETATM 3789 H  H3   . A1BW2 C 2 .   ? 9.187   16.834  61.202 1.00 33.40 ? 601 A1BW2 A H3   1 
HETATM 3790 H  H41  . A1BW2 C 2 .   ? 11.155  15.562  59.213 1.00 37.73 ? 601 A1BW2 A H41  1 
HETATM 3791 H  H42  . A1BW2 C 2 .   ? 9.412   15.231  59.284 1.00 37.73 ? 601 A1BW2 A H42  1 
HETATM 3792 H  H43  . A1BW2 C 2 .   ? 10.467  14.726  60.620 1.00 37.73 ? 601 A1BW2 A H43  1 
HETATM 3793 H  H56  . A1BW2 C 2 .   ? 5.094   11.237  55.780 1.00 54.60 ? 601 A1BW2 A H56  1 
HETATM 3794 H  H58  . A1BW2 C 2 .   ? 4.835   10.624  57.426 1.00 54.60 ? 601 A1BW2 A H58  1 
HETATM 3795 H  H57  . A1BW2 C 2 .   ? 6.388   10.349  56.611 1.00 54.60 ? 601 A1BW2 A H57  1 
HETATM 3796 H  H60  . A1BW2 C 2 .   ? 7.574   11.327  58.483 1.00 50.81 ? 601 A1BW2 A H60  1 
HETATM 3797 H  H61  . A1BW2 C 2 .   ? 6.118   11.793  59.385 1.00 50.81 ? 601 A1BW2 A H61  1 
HETATM 3798 H  H59  . A1BW2 C 2 .   ? 7.321   13.023  58.945 1.00 50.81 ? 601 A1BW2 A H59  1 
HETATM 3799 H  H54  . A1BW2 C 2 .   ? 4.280   12.889  58.377 1.00 49.05 ? 601 A1BW2 A H54  1 
HETATM 3800 H  H55  . A1BW2 C 2 .   ? 4.267   13.303  56.646 1.00 49.05 ? 601 A1BW2 A H55  1 
HETATM 3801 H  H53  . A1BW2 C 2 .   ? 5.986   15.052  57.234 1.00 40.13 ? 601 A1BW2 A H53  1 
HETATM 3802 H  H52  . A1BW2 C 2 .   ? 8.635   22.213  64.998 1.00 27.40 ? 601 A1BW2 A H52  1 
HETATM 3803 H  H62  . A1BW2 C 2 .   ? 7.301   13.772  56.758 1.00 48.97 ? 601 A1BW2 A H62  1 
HETATM 3804 C  C16  . A1BW2 D 2 .   ? 5.863   -24.800 45.780 1.00 18.47 ? 601 A1BW2 B C16  1 
HETATM 3805 C  C17  . A1BW2 D 2 .   ? 6.502   -25.585 44.841 1.00 22.91 ? 601 A1BW2 B C17  1 
HETATM 3806 C  C15  . A1BW2 D 2 .   ? 5.514   -23.500 45.468 1.00 19.89 ? 601 A1BW2 B C15  1 
HETATM 3807 C  C18  . A1BW2 D 2 .   ? 6.814   -25.147 43.565 1.00 23.12 ? 601 A1BW2 B C18  1 
HETATM 3808 C  C21  . A1BW2 D 2 .   ? 5.816   -23.076 44.196 1.00 19.32 ? 601 A1BW2 B C21  1 
HETATM 3809 C  C19  . A1BW2 D 2 .   ? 6.432   -23.860 43.255 1.00 28.74 ? 601 A1BW2 B C19  1 
HETATM 3810 C  C14  . A1BW2 D 2 .   ? 4.972   -22.668 46.541 1.00 20.14 ? 601 A1BW2 B C14  1 
HETATM 3811 C  C10  . A1BW2 D 2 .   ? 5.563   -22.424 47.763 1.00 20.34 ? 601 A1BW2 B C10  1 
HETATM 3812 C  C12  . A1BW2 D 2 .   ? 3.808   -21.162 48.073 1.00 25.68 ? 601 A1BW2 B C12  1 
HETATM 3813 C  C8   . A1BW2 D 2 .   ? 6.841   -23.065 48.125 1.00 22.10 ? 601 A1BW2 B C8   1 
HETATM 3814 C  C33  . A1BW2 D 2 .   ? 2.891   -20.218 48.664 1.00 27.38 ? 601 A1BW2 B C33  1 
HETATM 3815 C  C5   . A1BW2 D 2 .   ? 10.166  -22.725 46.774 1.00 34.93 ? 601 A1BW2 B C5   1 
HETATM 3816 C  C4   . A1BW2 D 2 .   ? 9.325   -21.761 45.955 1.00 36.01 ? 601 A1BW2 B C4   1 
HETATM 3817 C  C6   . A1BW2 D 2 .   ? 9.171   -23.378 47.686 1.00 30.07 ? 601 A1BW2 B C6   1 
HETATM 3818 C  C2   . A1BW2 D 2 .   ? 8.108   -21.406 46.805 1.00 26.33 ? 601 A1BW2 B C2   1 
HETATM 3819 C  C1   . A1BW2 D 2 .   ? 8.412   -20.234 47.696 1.00 31.92 ? 601 A1BW2 B C1   1 
HETATM 3820 C  C38  . A1BW2 D 2 .   ? 3.136   -16.772 51.841 1.00 52.26 ? 601 A1BW2 B C38  1 
HETATM 3821 C  C39  . A1BW2 D 2 .   ? 4.367   -17.311 49.761 1.00 54.75 ? 601 A1BW2 B C39  1 
HETATM 3822 C  C36  . A1BW2 D 2 .   ? 2.611   -18.796 50.609 1.00 42.37 ? 601 A1BW2 B C36  1 
HETATM 3823 C  C23  . A1BW2 D 2 .   ? 7.547   -26.061 42.622 1.00 19.96 ? 601 A1BW2 B C23  1 
HETATM 3824 C  C37  . A1BW2 D 2 .   ? 3.733   -17.869 51.009 1.00 51.40 ? 601 A1BW2 B C37  1 
HETATM 3825 C  C25  . A1BW2 D 2 .   ? 7.162   -27.508 42.670 1.00 25.89 ? 601 A1BW2 B C25  1 
HETATM 3826 C  C29  . A1BW2 D 2 .   ? 9.016   -25.938 42.975 1.00 25.51 ? 601 A1BW2 B C29  1 
HETATM 3827 N  N11  . A1BW2 D 2 .   ? 4.933   -21.585 48.638 1.00 21.79 ? 601 A1BW2 B N11  1 
HETATM 3828 N  N7   . A1BW2 D 2 .   ? 7.959   -22.577 47.571 1.00 23.59 ? 601 A1BW2 B N7   1 
HETATM 3829 N  N35  . A1BW2 D 2 .   ? 3.170   -19.963 49.980 1.00 35.26 ? 601 A1BW2 B N35  1 
HETATM 3830 O  O9   . A1BW2 D 2 .   ? 6.858   -24.032 48.856 1.00 24.64 ? 601 A1BW2 B O9   1 
HETATM 3831 O  O34  . A1BW2 D 2 .   ? 2.000   -19.639 48.037 1.00 26.38 ? 601 A1BW2 B O34  1 
HETATM 3832 O  O24  . A1BW2 D 2 .   ? 7.509   -25.650 41.281 1.00 25.53 ? 601 A1BW2 B O24  1 
HETATM 3833 O  O40  . A1BW2 D 2 .   ? 4.753   -18.547 51.751 1.00 54.47 ? 601 A1BW2 B O40  1 
HETATM 3834 F  F26  . A1BW2 D 2 .   ? 5.788   -27.620 42.560 1.00 23.21 ? 601 A1BW2 B F26  1 
HETATM 3835 F  F27  . A1BW2 D 2 .   ? 7.555   -28.115 43.777 1.00 26.13 ? 601 A1BW2 B F27  1 
HETATM 3836 F  F28  . A1BW2 D 2 .   ? 7.615   -28.307 41.683 1.00 27.91 ? 601 A1BW2 B F28  1 
HETATM 3837 F  F30  . A1BW2 D 2 .   ? 9.224   -26.282 44.232 1.00 27.40 ? 601 A1BW2 B F30  1 
HETATM 3838 F  F31  . A1BW2 D 2 .   ? 9.512   -24.694 42.819 1.00 31.92 ? 601 A1BW2 B F31  1 
HETATM 3839 F  F32  . A1BW2 D 2 .   ? 9.684   -26.788 42.210 1.00 27.12 ? 601 A1BW2 B F32  1 
HETATM 3840 S  S13  . A1BW2 D 2 .   ? 3.500   -21.755 46.498 1.00 24.11 ? 601 A1BW2 B S13  1 
HETATM 3841 CL CL22 . A1BW2 D 2 .   ? 5.440   -21.436 43.761 1.00 26.02 ? 601 A1BW2 B CL22 1 
HETATM 3842 CL CL20 . A1BW2 D 2 .   ? 6.755   -23.136 41.721 1.00 56.09 ? 601 A1BW2 B CL20 1 
HETATM 3843 H  H50  . A1BW2 D 2 .   ? 5.646   -25.199 46.764 1.00 22.16 ? 601 A1BW2 B H50  1 
HETATM 3844 H  H51  . A1BW2 D 2 .   ? 6.769   -26.599 45.115 1.00 27.49 ? 601 A1BW2 B H51  1 
HETATM 3845 H  H46  . A1BW2 D 2 .   ? 10.651  -23.464 46.131 1.00 41.92 ? 601 A1BW2 B H46  1 
HETATM 3846 H  H47  . A1BW2 D 2 .   ? 10.928  -22.190 47.346 1.00 41.92 ? 601 A1BW2 B H47  1 
HETATM 3847 H  H45  . A1BW2 D 2 .   ? 9.011   -22.230 45.019 1.00 43.21 ? 601 A1BW2 B H45  1 
HETATM 3848 H  H44  . A1BW2 D 2 .   ? 9.899   -20.861 45.719 1.00 43.21 ? 601 A1BW2 B H44  1 
HETATM 3849 H  H48  . A1BW2 D 2 .   ? 8.948   -24.402 47.377 1.00 36.08 ? 601 A1BW2 B H48  1 
HETATM 3850 H  H49  . A1BW2 D 2 .   ? 9.505   -23.364 48.727 1.00 36.08 ? 601 A1BW2 B H49  1 
HETATM 3851 H  H3   . A1BW2 D 2 .   ? 7.213   -21.245 46.196 1.00 31.59 ? 601 A1BW2 B H3   1 
HETATM 3852 H  H41  . A1BW2 D 2 .   ? 9.289   -20.445 48.314 1.00 38.30 ? 601 A1BW2 B H41  1 
HETATM 3853 H  H42  . A1BW2 D 2 .   ? 7.564   -20.027 48.353 1.00 38.30 ? 601 A1BW2 B H42  1 
HETATM 3854 H  H43  . A1BW2 D 2 .   ? 8.614   -19.344 47.096 1.00 38.30 ? 601 A1BW2 B H43  1 
HETATM 3855 H  H56  . A1BW2 D 2 .   ? 3.897   -16.028 52.091 1.00 62.71 ? 601 A1BW2 B H56  1 
HETATM 3856 H  H58  . A1BW2 D 2 .   ? 2.728   -17.178 52.770 1.00 62.71 ? 601 A1BW2 B H58  1 
HETATM 3857 H  H57  . A1BW2 D 2 .   ? 2.330   -16.276 51.294 1.00 62.71 ? 601 A1BW2 B H57  1 
HETATM 3858 H  H60  . A1BW2 D 2 .   ? 3.601   -16.914 49.090 1.00 65.70 ? 601 A1BW2 B H60  1 
HETATM 3859 H  H61  . A1BW2 D 2 .   ? 5.060   -16.504 50.015 1.00 65.70 ? 601 A1BW2 B H61  1 
HETATM 3860 H  H59  . A1BW2 D 2 .   ? 4.921   -18.092 49.234 1.00 65.70 ? 601 A1BW2 B H59  1 
HETATM 3861 H  H54  . A1BW2 D 2 .   ? 2.047   -19.124 51.486 1.00 50.84 ? 601 A1BW2 B H54  1 
HETATM 3862 H  H55  . A1BW2 D 2 .   ? 1.934   -18.314 49.900 1.00 50.84 ? 601 A1BW2 B H55  1 
HETATM 3863 H  H53  . A1BW2 D 2 .   ? 3.856   -20.524 50.473 1.00 42.31 ? 601 A1BW2 B H53  1 
HETATM 3864 H  H52  . A1BW2 D 2 .   ? 6.600   -25.354 41.108 1.00 30.63 ? 601 A1BW2 B H52  1 
HETATM 3865 H  H62  . A1BW2 D 2 .   ? 5.070   -19.272 51.186 1.00 65.36 ? 601 A1BW2 B H62  1 
HETATM 3866 O  O    . HOH   E 3 .   ? -16.628 27.259  67.560 1.00 33.20 ? 701 HOH   A O    1 
HETATM 3867 O  O    . HOH   E 3 .   ? 8.934   7.783   47.035 1.00 48.26 ? 702 HOH   A O    1 
HETATM 3868 O  O    . HOH   E 3 .   ? 22.680  25.522  53.534 1.00 29.98 ? 703 HOH   A O    1 
HETATM 3869 O  O    . HOH   E 3 .   ? 8.910   3.132   58.370 1.00 40.61 ? 704 HOH   A O    1 
HETATM 3870 O  O    . HOH   E 3 .   ? 12.937  14.882  47.760 1.00 31.53 ? 705 HOH   A O    1 
HETATM 3871 O  O    . HOH   E 3 .   ? 2.385   8.509   60.321 1.00 32.14 ? 706 HOH   A O    1 
HETATM 3872 O  O    . HOH   E 3 .   ? 20.788  22.556  47.138 1.00 35.35 ? 707 HOH   A O    1 
HETATM 3873 O  O    . HOH   E 3 .   ? 20.350  9.301   53.388 1.00 42.52 ? 708 HOH   A O    1 
HETATM 3874 O  O    . HOH   E 3 .   ? -5.518  11.294  78.325 1.00 28.63 ? 709 HOH   A O    1 
HETATM 3875 O  O    . HOH   E 3 .   ? 17.965  27.336  48.894 1.00 29.48 ? 710 HOH   A O    1 
HETATM 3876 O  O    . HOH   E 3 .   ? 23.292  22.936  56.132 1.00 29.78 ? 711 HOH   A O    1 
HETATM 3877 O  O    . HOH   E 3 .   ? 9.285   3.323   64.189 1.00 38.26 ? 712 HOH   A O    1 
HETATM 3878 O  O    . HOH   E 3 .   ? 16.909  33.915  56.009 1.00 29.63 ? 713 HOH   A O    1 
HETATM 3879 O  O    . HOH   E 3 .   ? 18.965  20.942  55.271 1.00 29.23 ? 714 HOH   A O    1 
HETATM 3880 O  O    . HOH   E 3 .   ? -15.148 21.590  61.009 1.00 39.17 ? 715 HOH   A O    1 
HETATM 3881 O  O    . HOH   E 3 .   ? -17.016 14.646  62.222 1.00 28.47 ? 716 HOH   A O    1 
HETATM 3882 O  O    . HOH   E 3 .   ? -8.436  21.095  83.022 1.00 46.09 ? 717 HOH   A O    1 
HETATM 3883 O  O    . HOH   E 3 .   ? -4.791  9.185   79.675 1.00 35.93 ? 718 HOH   A O    1 
HETATM 3884 O  O    . HOH   E 3 .   ? -7.960  11.591  55.294 1.00 38.14 ? 719 HOH   A O    1 
HETATM 3885 O  O    . HOH   E 3 .   ? 15.182  3.480   55.838 1.00 26.66 ? 720 HOH   A O    1 
HETATM 3886 O  O    . HOH   E 3 .   ? 18.669  21.814  61.828 1.00 29.55 ? 721 HOH   A O    1 
HETATM 3887 O  O    . HOH   E 3 .   ? 21.104  27.329  57.286 1.00 28.96 ? 722 HOH   A O    1 
HETATM 3888 O  O    . HOH   E 3 .   ? 18.387  7.538   70.490 1.00 46.71 ? 723 HOH   A O    1 
HETATM 3889 O  O    . HOH   E 3 .   ? 20.296  16.959  64.811 1.00 33.14 ? 724 HOH   A O    1 
HETATM 3890 O  O    . HOH   E 3 .   ? 0.278   14.575  76.274 1.00 35.90 ? 725 HOH   A O    1 
HETATM 3891 O  O    . HOH   E 3 .   ? 20.333  11.198  55.271 1.00 32.54 ? 726 HOH   A O    1 
HETATM 3892 O  O    . HOH   E 3 .   ? 3.489   12.816  61.627 1.00 38.42 ? 727 HOH   A O    1 
HETATM 3893 O  O    . HOH   E 3 .   ? 15.789  23.253  70.418 1.00 39.65 ? 728 HOH   A O    1 
HETATM 3894 O  O    . HOH   E 3 .   ? 11.625  38.068  55.810 1.00 36.37 ? 729 HOH   A O    1 
HETATM 3895 O  O    . HOH   E 3 .   ? 6.249   1.759   67.387 1.00 30.45 ? 730 HOH   A O    1 
HETATM 3896 O  O    . HOH   E 3 .   ? 13.312  13.527  72.561 1.00 40.45 ? 731 HOH   A O    1 
HETATM 3897 O  O    . HOH   E 3 .   ? -5.052  17.685  74.307 1.00 22.80 ? 732 HOH   A O    1 
HETATM 3898 O  O    . HOH   E 3 .   ? -2.311  14.232  76.789 1.00 28.64 ? 733 HOH   A O    1 
HETATM 3899 O  O    . HOH   E 3 .   ? 19.723  10.076  61.917 1.00 25.64 ? 734 HOH   A O    1 
HETATM 3900 O  O    . HOH   E 3 .   ? 7.148   35.058  65.857 1.00 29.53 ? 735 HOH   A O    1 
HETATM 3901 O  O    . HOH   E 3 .   ? -8.603  19.543  58.907 1.00 24.72 ? 736 HOH   A O    1 
HETATM 3902 O  O    . HOH   E 3 .   ? 8.382   20.319  49.362 1.00 42.62 ? 737 HOH   A O    1 
HETATM 3903 O  O    . HOH   E 3 .   ? 23.903  12.240  61.151 1.00 31.84 ? 738 HOH   A O    1 
HETATM 3904 O  O    . HOH   E 3 .   ? 2.346   23.974  66.092 1.00 43.86 ? 739 HOH   A O    1 
HETATM 3905 O  O    . HOH   E 3 .   ? 2.905   16.226  56.201 1.00 25.14 ? 740 HOH   A O    1 
HETATM 3906 O  O    . HOH   E 3 .   ? -15.065 8.052   61.805 1.00 39.97 ? 741 HOH   A O    1 
HETATM 3907 O  O    . HOH   E 3 .   ? -11.177 19.264  59.699 1.00 27.17 ? 742 HOH   A O    1 
HETATM 3908 O  O    . HOH   E 3 .   ? 20.519  2.061   55.612 1.00 44.28 ? 743 HOH   A O    1 
HETATM 3909 O  O    . HOH   E 3 .   ? -4.279  9.991   65.362 1.00 23.88 ? 744 HOH   A O    1 
HETATM 3910 O  O    . HOH   E 3 .   ? 18.717  16.967  47.073 1.00 41.20 ? 745 HOH   A O    1 
HETATM 3911 O  O    . HOH   E 3 .   ? -17.660 27.029  73.058 1.00 41.28 ? 746 HOH   A O    1 
HETATM 3912 O  O    . HOH   E 3 .   ? 5.199   27.155  52.625 1.00 34.57 ? 747 HOH   A O    1 
HETATM 3913 O  O    . HOH   E 3 .   ? -5.627  9.702   55.384 1.00 29.79 ? 748 HOH   A O    1 
HETATM 3914 O  O    . HOH   E 3 .   ? -1.026  13.721  60.632 1.00 28.07 ? 749 HOH   A O    1 
HETATM 3915 O  O    . HOH   E 3 .   ? -1.908  1.804   57.499 1.00 35.17 ? 750 HOH   A O    1 
HETATM 3916 O  O    . HOH   E 3 .   ? 26.784  20.270  57.192 1.00 45.08 ? 751 HOH   A O    1 
HETATM 3917 O  O    . HOH   E 3 .   ? 14.975  19.661  46.023 1.00 52.71 ? 752 HOH   A O    1 
HETATM 3918 O  O    . HOH   E 3 .   ? -0.617  8.835   60.876 1.00 33.18 ? 753 HOH   A O    1 
HETATM 3919 O  O    . HOH   E 3 .   ? 7.243   14.316  53.678 1.00 34.28 ? 754 HOH   A O    1 
HETATM 3920 O  O    . HOH   E 3 .   ? -4.714  24.628  74.991 1.00 28.80 ? 755 HOH   A O    1 
HETATM 3921 O  O    . HOH   E 3 .   ? -15.029 15.053  56.513 1.00 29.49 ? 756 HOH   A O    1 
HETATM 3922 O  O    . HOH   E 3 .   ? -4.424  23.967  77.504 1.00 34.20 ? 757 HOH   A O    1 
HETATM 3923 O  O    . HOH   E 3 .   ? 21.695  23.924  64.427 1.00 37.00 ? 758 HOH   A O    1 
HETATM 3924 O  O    . HOH   E 3 .   ? 11.464  1.217   63.082 1.00 39.87 ? 759 HOH   A O    1 
HETATM 3925 O  O    . HOH   E 3 .   ? 21.679  4.441   67.792 1.00 37.76 ? 760 HOH   A O    1 
HETATM 3926 O  O    . HOH   E 3 .   ? -21.065 3.143   83.159 1.00 53.40 ? 761 HOH   A O    1 
HETATM 3927 O  O    . HOH   E 3 .   ? 22.893  16.764  61.985 1.00 30.46 ? 762 HOH   A O    1 
HETATM 3928 O  O    . HOH   E 3 .   ? -18.525 8.887   72.781 1.00 48.17 ? 763 HOH   A O    1 
HETATM 3929 O  O    . HOH   E 3 .   ? -18.710 1.490   60.270 1.00 45.65 ? 764 HOH   A O    1 
HETATM 3930 O  O    . HOH   E 3 .   ? -15.465 6.335   63.382 1.00 45.18 ? 765 HOH   A O    1 
HETATM 3931 O  O    . HOH   E 3 .   ? 21.929  8.980   65.823 1.00 35.23 ? 766 HOH   A O    1 
HETATM 3932 O  O    . HOH   E 3 .   ? 19.584  9.993   64.754 1.00 30.82 ? 767 HOH   A O    1 
HETATM 3933 O  O    . HOH   E 3 .   ? -3.475  4.844   80.203 1.00 56.97 ? 768 HOH   A O    1 
HETATM 3934 O  O    . HOH   E 3 .   ? 8.521   33.559  52.480 1.00 47.92 ? 769 HOH   A O    1 
HETATM 3935 O  O    . HOH   E 3 .   ? -17.478 20.408  84.356 1.00 42.69 ? 770 HOH   A O    1 
HETATM 3936 O  O    . HOH   E 3 .   ? 17.971  31.570  54.903 1.00 24.60 ? 771 HOH   A O    1 
HETATM 3937 O  O    . HOH   E 3 .   ? 25.113  7.460   48.025 1.00 40.74 ? 772 HOH   A O    1 
HETATM 3938 O  O    . HOH   E 3 .   ? 1.204   32.207  59.624 1.00 54.54 ? 773 HOH   A O    1 
HETATM 3939 O  O    . HOH   E 3 .   ? -6.124  27.093  74.760 1.00 40.65 ? 774 HOH   A O    1 
HETATM 3940 O  O    . HOH   E 3 .   ? -19.793 10.642  68.462 1.00 44.05 ? 775 HOH   A O    1 
HETATM 3941 O  O    . HOH   E 3 .   ? -2.612  11.984  78.254 1.00 45.83 ? 776 HOH   A O    1 
HETATM 3942 O  O    . HOH   E 3 .   ? 21.108  20.519  62.630 1.00 28.22 ? 777 HOH   A O    1 
HETATM 3943 O  O    . HOH   E 3 .   ? 15.564  37.462  54.733 1.00 41.30 ? 778 HOH   A O    1 
HETATM 3944 O  O    . HOH   E 3 .   ? -1.313  10.219  76.964 1.00 56.53 ? 779 HOH   A O    1 
HETATM 3945 O  O    . HOH   E 3 .   ? -0.393  32.981  53.105 1.00 35.21 ? 780 HOH   A O    1 
HETATM 3946 O  O    . HOH   E 3 .   ? 5.397   29.378  51.505 1.00 39.05 ? 781 HOH   A O    1 
HETATM 3947 O  O    . HOH   E 3 .   ? 21.069  7.402   55.585 1.00 42.50 ? 782 HOH   A O    1 
HETATM 3948 O  O    . HOH   F 3 .   ? 22.172  -34.138 54.396 1.00 36.34 ? 701 HOH   B O    1 
HETATM 3949 O  O    . HOH   F 3 .   ? 14.763  -37.463 53.980 1.00 43.77 ? 702 HOH   B O    1 
HETATM 3950 O  O    . HOH   F 3 .   ? -16.775 4.232   45.632 1.00 59.20 ? 703 HOH   B O    1 
HETATM 3951 O  O    . HOH   F 3 .   ? -19.379 -7.502  28.840 1.00 39.58 ? 704 HOH   B O    1 
HETATM 3952 O  O    . HOH   F 3 .   ? -16.928 -12.879 48.203 1.00 35.90 ? 705 HOH   B O    1 
HETATM 3953 O  O    . HOH   F 3 .   ? -16.067 -10.634 43.230 1.00 35.91 ? 706 HOH   B O    1 
HETATM 3954 O  O    . HOH   F 3 .   ? -4.983  1.778   42.930 1.00 37.39 ? 707 HOH   B O    1 
HETATM 3955 O  O    . HOH   F 3 .   ? 1.520   -17.351 46.901 1.00 36.01 ? 708 HOH   B O    1 
HETATM 3956 O  O    . HOH   F 3 .   ? 21.352  -28.589 49.517 1.00 30.69 ? 709 HOH   B O    1 
HETATM 3957 O  O    . HOH   F 3 .   ? 0.890   -13.660 49.254 1.00 33.10 ? 710 HOH   B O    1 
HETATM 3958 O  O    . HOH   F 3 .   ? -5.632  0.747   45.247 1.00 33.51 ? 711 HOH   B O    1 
HETATM 3959 O  O    . HOH   F 3 .   ? 15.617  -34.913 55.202 1.00 32.32 ? 712 HOH   B O    1 
HETATM 3960 O  O    . HOH   F 3 .   ? 20.714  -31.922 51.226 1.00 25.65 ? 713 HOH   B O    1 
HETATM 3961 O  O    . HOH   F 3 .   ? -14.597 -4.412  48.890 1.00 39.15 ? 714 HOH   B O    1 
HETATM 3962 O  O    . HOH   F 3 .   ? -0.849  -16.717 30.754 1.00 50.09 ? 715 HOH   B O    1 
HETATM 3963 O  O    . HOH   F 3 .   ? 18.879  -32.688 47.041 1.00 25.45 ? 716 HOH   B O    1 
HETATM 3964 O  O    . HOH   F 3 .   ? -12.552 -8.983  26.556 1.00 30.05 ? 717 HOH   B O    1 
HETATM 3965 O  O    . HOH   F 3 .   ? -10.195 -19.012 23.882 1.00 43.22 ? 718 HOH   B O    1 
HETATM 3966 O  O    . HOH   F 3 .   ? -7.465  -11.177 31.107 1.00 28.12 ? 719 HOH   B O    1 
HETATM 3967 O  O    . HOH   F 3 .   ? -17.154 -25.873 44.923 1.00 33.00 ? 720 HOH   B O    1 
HETATM 3968 O  O    . HOH   F 3 .   ? 17.831  -14.703 47.112 1.00 26.69 ? 721 HOH   B O    1 
HETATM 3969 O  O    . HOH   F 3 .   ? 5.032   -37.656 36.942 1.00 27.08 ? 722 HOH   B O    1 
HETATM 3970 O  O    . HOH   F 3 .   ? -8.576  -7.564  25.972 1.00 29.60 ? 723 HOH   B O    1 
HETATM 3971 O  O    . HOH   F 3 .   ? -24.570 4.671   38.858 1.00 49.21 ? 724 HOH   B O    1 
HETATM 3972 O  O    . HOH   F 3 .   ? -7.012  -18.601 33.239 1.00 23.34 ? 725 HOH   B O    1 
HETATM 3973 O  O    . HOH   F 3 .   ? 3.071   -33.270 51.498 1.00 36.39 ? 726 HOH   B O    1 
HETATM 3974 O  O    . HOH   F 3 .   ? 13.444  -9.936  54.817 1.00 31.26 ? 727 HOH   B O    1 
HETATM 3975 O  O    . HOH   F 3 .   ? 5.355   -21.196 51.370 1.00 43.48 ? 728 HOH   B O    1 
HETATM 3976 O  O    . HOH   F 3 .   ? 16.971  -26.911 50.822 1.00 22.40 ? 729 HOH   B O    1 
HETATM 3977 O  O    . HOH   F 3 .   ? -2.693  -23.776 37.154 1.00 35.47 ? 730 HOH   B O    1 
HETATM 3978 O  O    . HOH   F 3 .   ? 7.248   -8.959  52.261 1.00 30.15 ? 731 HOH   B O    1 
HETATM 3979 O  O    . HOH   F 3 .   ? 7.183   -7.002  47.563 1.00 40.42 ? 732 HOH   B O    1 
HETATM 3980 O  O    . HOH   F 3 .   ? -10.649 -24.526 47.442 1.00 26.94 ? 733 HOH   B O    1 
HETATM 3981 O  O    . HOH   F 3 .   ? -9.868  -29.175 30.741 1.00 51.55 ? 734 HOH   B O    1 
HETATM 3982 O  O    . HOH   F 3 .   ? -13.128 -23.141 50.396 1.00 43.53 ? 735 HOH   B O    1 
HETATM 3983 O  O    . HOH   F 3 .   ? 0.329   -26.848 39.419 1.00 49.48 ? 736 HOH   B O    1 
HETATM 3984 O  O    . HOH   F 3 .   ? 0.736   -21.960 51.049 1.00 26.36 ? 737 HOH   B O    1 
HETATM 3985 O  O    . HOH   F 3 .   ? 16.649  -26.064 44.158 1.00 27.45 ? 738 HOH   B O    1 
HETATM 3986 O  O    . HOH   F 3 .   ? -19.936 -1.963  30.560 1.00 34.10 ? 739 HOH   B O    1 
HETATM 3987 O  O    . HOH   F 3 .   ? -4.226  -29.853 50.852 1.00 40.27 ? 740 HOH   B O    1 
HETATM 3988 O  O    . HOH   F 3 .   ? 0.026   -6.059  47.643 1.00 35.16 ? 741 HOH   B O    1 
HETATM 3989 O  O    . HOH   F 3 .   ? -6.279  -13.539 43.956 1.00 27.13 ? 742 HOH   B O    1 
HETATM 3990 O  O    . HOH   F 3 .   ? 18.374  -35.099 48.213 1.00 25.76 ? 743 HOH   B O    1 
HETATM 3991 O  O    . HOH   F 3 .   ? -13.163 -24.121 46.711 1.00 27.45 ? 744 HOH   B O    1 
HETATM 3992 O  O    . HOH   F 3 .   ? -16.070 -20.680 22.423 1.00 52.71 ? 745 HOH   B O    1 
HETATM 3993 O  O    . HOH   F 3 .   ? 11.821  -3.600  43.667 1.00 42.33 ? 746 HOH   B O    1 
HETATM 3994 O  O    . HOH   F 3 .   ? -6.702  -25.047 30.635 1.00 27.99 ? 747 HOH   B O    1 
HETATM 3995 O  O    . HOH   F 3 .   ? -6.280  -23.577 28.303 1.00 35.86 ? 748 HOH   B O    1 
HETATM 3996 O  O    . HOH   F 3 .   ? -20.184 -32.204 37.001 1.00 44.60 ? 749 HOH   B O    1 
HETATM 3997 O  O    . HOH   F 3 .   ? 11.680  -27.144 34.883 1.00 48.16 ? 750 HOH   B O    1 
HETATM 3998 O  O    . HOH   F 3 .   ? 4.648   1.955   41.523 1.00 48.13 ? 751 HOH   B O    1 
HETATM 3999 O  O    . HOH   F 3 .   ? 4.169   -5.001  44.391 1.00 30.31 ? 752 HOH   B O    1 
HETATM 4000 O  O    . HOH   F 3 .   ? 5.615   -40.634 36.988 1.00 33.13 ? 753 HOH   B O    1 
HETATM 4001 O  O    . HOH   F 3 .   ? -2.602  -13.703 48.603 1.00 38.92 ? 754 HOH   B O    1 
HETATM 4002 O  O    . HOH   F 3 .   ? -19.079 -18.965 45.569 1.00 26.68 ? 755 HOH   B O    1 
HETATM 4003 O  O    . HOH   F 3 .   ? -3.009  -18.478 47.430 1.00 26.24 ? 756 HOH   B O    1 
HETATM 4004 O  O    . HOH   F 3 .   ? -17.029 -20.943 50.910 1.00 32.76 ? 757 HOH   B O    1 
HETATM 4005 O  O    . HOH   F 3 .   ? 17.533  -13.827 44.389 1.00 32.61 ? 758 HOH   B O    1 
HETATM 4006 O  O    . HOH   F 3 .   ? -17.533 -3.386  34.810 1.00 35.16 ? 759 HOH   B O    1 
HETATM 4007 O  O    . HOH   F 3 .   ? -3.168  -1.970  50.300 1.00 40.38 ? 760 HOH   B O    1 
HETATM 4008 O  O    . HOH   F 3 .   ? 20.831  -21.130 45.261 1.00 30.24 ? 761 HOH   B O    1 
HETATM 4009 O  O    . HOH   F 3 .   ? 19.699  -27.303 41.182 1.00 31.28 ? 762 HOH   B O    1 
HETATM 4010 O  O    . HOH   F 3 .   ? 21.876  -16.800 47.162 1.00 35.33 ? 763 HOH   B O    1 
HETATM 4011 O  O    . HOH   F 3 .   ? 15.676  -37.264 48.213 1.00 43.63 ? 764 HOH   B O    1 
HETATM 4012 O  O    . HOH   F 3 .   ? 19.093  -24.568 43.632 1.00 28.16 ? 765 HOH   B O    1 
HETATM 4013 O  O    . HOH   F 3 .   ? -5.750  -1.617  48.959 1.00 38.27 ? 766 HOH   B O    1 
HETATM 4014 O  O    . HOH   F 3 .   ? -0.377  -16.110 48.704 1.00 49.37 ? 767 HOH   B O    1 
HETATM 4015 O  O    . HOH   F 3 .   ? -15.164 1.534   44.217 1.00 50.23 ? 768 HOH   B O    1 
HETATM 4016 O  O    . HOH   F 3 .   ? -7.958  -27.412 29.948 1.00 42.55 ? 769 HOH   B O    1 
HETATM 4017 O  O    . HOH   F 3 .   ? -12.299 -9.604  23.781 1.00 36.43 ? 770 HOH   B O    1 
HETATM 4018 O  O    . HOH   F 3 .   ? -12.841 2.349   42.631 1.00 51.67 ? 771 HOH   B O    1 
HETATM 4019 O  O    . HOH   F 3 .   ? -19.207 -9.429  36.466 1.00 34.04 ? 772 HOH   B O    1 
HETATM 4020 O  O    . HOH   F 3 .   ? 0.290   -32.470 49.648 1.00 46.51 ? 773 HOH   B O    1 
HETATM 4021 O  O    . HOH   F 3 .   ? 21.072  -26.273 43.461 1.00 49.19 ? 774 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   . ALA A 1   ? 0.3057 0.4742 0.5571 0.0422  0.0572  0.2028  265 ALA A N   
2    C CA  . ALA A 1   ? 0.3646 0.5120 0.5816 0.0348  0.0383  0.1791  265 ALA A CA  
3    C C   . ALA A 1   ? 0.3275 0.4769 0.5331 0.0172  0.0091  0.1720  265 ALA A C   
4    O O   . ALA A 1   ? 0.3227 0.4548 0.5031 0.0121  0.0083  0.1576  265 ALA A O   
5    C CB  . ALA A 1   ? 0.2899 0.4028 0.4679 0.0373  0.0569  0.1569  265 ALA A CB  
6    N N   . SER A 2   ? 0.2955 0.4670 0.5206 0.0062  -0.0122 0.1863  266 SER A N   
7    C CA  . SER A 2   ? 0.3152 0.4842 0.5311 -0.0136 -0.0328 0.1847  266 SER A CA  
8    C C   . SER A 2   ? 0.3118 0.4481 0.4908 -0.0218 -0.0456 0.1633  266 SER A C   
9    O O   . SER A 2   ? 0.3099 0.4349 0.4760 -0.0145 -0.0442 0.1529  266 SER A O   
10   C CB  . SER A 2   ? 0.3232 0.5280 0.5680 -0.0304 -0.0495 0.2105  266 SER A CB  
11   O OG  . SER A 2   ? 0.3368 0.5479 0.5773 -0.0391 -0.0650 0.2138  266 SER A OG  
12   N N   . LEU A 3   ? 0.3235 0.4421 0.4863 -0.0364 -0.0545 0.1589  267 LEU A N   
13   C CA  . LEU A 3   ? 0.2914 0.3730 0.4205 -0.0428 -0.0598 0.1422  267 LEU A CA  
14   C C   . LEU A 3   ? 0.2901 0.3707 0.4093 -0.0568 -0.0732 0.1425  267 LEU A C   
15   O O   . LEU A 3   ? 0.3260 0.3853 0.4246 -0.0513 -0.0716 0.1290  267 LEU A O   
16   C CB  . LEU A 3   ? 0.2756 0.3305 0.3884 -0.0555 -0.0600 0.1404  267 LEU A CB  
17   C CG  . LEU A 3   ? 0.3545 0.3605 0.4302 -0.0633 -0.0580 0.1263  267 LEU A CG  
18   C CD1 . LEU A 3   ? 0.3277 0.3228 0.3971 -0.0413 -0.0477 0.1162  267 LEU A CD1 
19   C CD2 . LEU A 3   ? 0.3985 0.3694 0.4575 -0.0736 -0.0503 0.1268  267 LEU A CD2 
20   N N   . THR A 4   ? 0.3571 0.4660 0.4923 -0.0759 -0.0869 0.1611  268 THR A N   
21   C CA  . THR A 4   ? 0.3719 0.4857 0.4949 -0.0944 -0.1028 0.1655  268 THR A CA  
22   C C   . THR A 4   ? 0.3129 0.4439 0.4516 -0.0729 -0.0978 0.1677  268 THR A C   
23   O O   . THR A 4   ? 0.3296 0.4442 0.4442 -0.0787 -0.1039 0.1588  268 THR A O   
24   C CB  . THR A 4   ? 0.3450 0.5001 0.4874 -0.1241 -0.1223 0.1932  268 THR A CB  
25   O OG1 . THR A 4   ? 0.4611 0.5868 0.5751 -0.1506 -0.1265 0.1864  268 THR A OG1 
26   C CG2 . THR A 4   ? 0.4238 0.5911 0.5525 -0.1465 -0.1411 0.2019  268 THR A CG2 
27   N N   . GLU A 5   ? 0.2975 0.4556 0.4725 -0.0487 -0.0829 0.1788  269 GLU A N   
28   C CA  . GLU A 5   ? 0.2516 0.4152 0.4369 -0.0270 -0.0709 0.1791  269 GLU A CA  
29   C C   . GLU A 5   ? 0.2827 0.4056 0.4326 -0.0172 -0.0630 0.1502  269 GLU A C   
30   O O   . GLU A 5   ? 0.2768 0.3944 0.4184 -0.0128 -0.0637 0.1461  269 GLU A O   
31   C CB  . GLU A 5   ? 0.2570 0.4428 0.4788 -0.0048 -0.0479 0.1945  269 GLU A CB  
32   C CG  . GLU A 5   ? 0.3341 0.5723 0.6038 -0.0094 -0.0537 0.2332  269 GLU A CG  
33   C CD  . GLU A 5   ? 0.4203 0.6783 0.7292 0.0120  -0.0259 0.2527  269 GLU A CD  
34   O OE1 . GLU A 5   ? 0.4028 0.6296 0.6941 0.0256  -0.0026 0.2333  269 GLU A OE1 
35   O OE2 . GLU A 5   ? 0.3706 0.6633 0.7125 0.0099  -0.0225 0.2832  269 GLU A OE2 
36   N N   . ILE A 6   ? 0.2512 0.3502 0.3831 -0.0151 -0.0568 0.1341  270 ILE A N   
37   C CA  . ILE A 6   ? 0.2467 0.3180 0.3528 -0.0066 -0.0501 0.1140  270 ILE A CA  
38   C C   . ILE A 6   ? 0.3332 0.3783 0.4119 -0.0189 -0.0606 0.1044  270 ILE A C   
39   O O   . ILE A 6   ? 0.2868 0.3176 0.3504 -0.0128 -0.0575 0.0937  270 ILE A O   
40   C CB  . ILE A 6   ? 0.2806 0.3440 0.3812 -0.0012 -0.0410 0.1078  270 ILE A CB  
41   C CG1 . ILE A 6   ? 0.3309 0.4093 0.4432 0.0084  -0.0259 0.1116  270 ILE A CG1 
42   C CG2 . ILE A 6   ? 0.3275 0.3704 0.4069 0.0038  -0.0381 0.0949  270 ILE A CG2 
43   C CD1 . ILE A 6   ? 0.3244 0.3955 0.4246 0.0167  -0.0139 0.1019  270 ILE A CD1 
44   N N   . GLU A 7   ? 0.3510 0.3850 0.4184 -0.0385 -0.0703 0.1075  271 GLU A N   
45   C CA  . GLU A 7   ? 0.3328 0.3306 0.3630 -0.0557 -0.0754 0.0971  271 GLU A CA  
46   C C   . GLU A 7   ? 0.3754 0.3862 0.4016 -0.0635 -0.0865 0.1015  271 GLU A C   
47   O O   . GLU A 7   ? 0.3692 0.3526 0.3682 -0.0639 -0.0834 0.0886  271 GLU A O   
48   C CB  . GLU A 7   ? 0.3380 0.3160 0.3484 -0.0830 -0.0819 0.0998  271 GLU A CB  
49   C CG  . GLU A 7   ? 0.4029 0.3573 0.4116 -0.0742 -0.0673 0.0954  271 GLU A CG  
50   C CD  . GLU A 7   ? 0.4290 0.3593 0.4171 -0.1022 -0.0704 0.0982  271 GLU A CD  
51   O OE1 . GLU A 7   ? 0.4437 0.3985 0.4349 -0.1290 -0.0885 0.1104  271 GLU A OE1 
52   O OE2 . GLU A 7   ? 0.4656 0.3528 0.4351 -0.0984 -0.0532 0.0911  271 GLU A OE2 
53   N N   . HIS A 8   ? 0.3387 0.3936 0.3946 -0.0691 -0.0981 0.1232  272 HIS A N   
54   C CA  . HIS A 8   ? 0.3408 0.4161 0.3996 -0.0748 -0.1089 0.1346  272 HIS A CA  
55   C C   . HIS A 8   ? 0.3709 0.4424 0.4366 -0.0470 -0.0944 0.1259  272 HIS A C   
56   O O   . HIS A 8   ? 0.3723 0.4374 0.4226 -0.0499 -0.0987 0.1237  272 HIS A O   
57   C CB  . HIS A 8   ? 0.3075 0.4397 0.4085 -0.0820 -0.1210 0.1686  272 HIS A CB  
58   C CG  . HIS A 8   ? 0.4559 0.5968 0.5434 -0.1199 -0.1415 0.1802  272 HIS A CG  
59   N ND1 . HIS A 8   ? 0.5691 0.6578 0.6020 -0.1461 -0.1443 0.1578  272 HIS A ND1 
60   C CD2 . HIS A 8   ? 0.5067 0.7010 0.6266 -0.1386 -0.1579 0.2136  272 HIS A CD2 
61   C CE1 . HIS A 8   ? 0.6245 0.7281 0.6487 -0.1835 -0.1625 0.1730  272 HIS A CE1 
62   N NE2 . HIS A 8   ? 0.6197 0.7930 0.6987 -0.1806 -0.1739 0.2084  272 HIS A NE2 
63   N N   . LEU A 9   ? 0.2911 0.3628 0.3736 -0.0237 -0.0769 0.1198  273 LEU A N   
64   C CA  . LEU A 9   ? 0.3248 0.3889 0.4069 -0.0038 -0.0622 0.1103  273 LEU A CA  
65   C C   . LEU A 9   ? 0.2924 0.3221 0.3404 -0.0052 -0.0608 0.0888  273 LEU A C   
66   O O   . LEU A 9   ? 0.3245 0.3470 0.3624 -0.0013 -0.0591 0.0840  273 LEU A O   
67   C CB  . LEU A 9   ? 0.2684 0.3363 0.3649 0.0123  -0.0435 0.1080  273 LEU A CB  
68   C CG  . LEU A 9   ? 0.3243 0.3792 0.4113 0.0255  -0.0270 0.0971  273 LEU A CG  
69   C CD1 . LEU A 9   ? 0.2839 0.3467 0.3831 0.0331  -0.0222 0.1092  273 LEU A CD1 
70   C CD2 . LEU A 9   ? 0.3656 0.4173 0.4531 0.0322  -0.0080 0.0929  273 LEU A CD2 
71   N N   . VAL A 10  ? 0.3061 0.3144 0.3385 -0.0098 -0.0593 0.0788  274 VAL A N   
72   C CA  . VAL A 10  ? 0.3278 0.3029 0.3323 -0.0091 -0.0534 0.0639  274 VAL A CA  
73   C C   . VAL A 10  ? 0.3578 0.3148 0.3355 -0.0249 -0.0619 0.0612  274 VAL A C   
74   O O   . VAL A 10  ? 0.3642 0.3087 0.3286 -0.0194 -0.0569 0.0531  274 VAL A O   
75   C CB  . VAL A 10  ? 0.3674 0.3189 0.3619 -0.0104 -0.0461 0.0601  274 VAL A CB  
76   C CG1 . VAL A 10  ? 0.3732 0.2871 0.3415 -0.0075 -0.0340 0.0495  274 VAL A CG1 
77   C CG2 . VAL A 10  ? 0.3175 0.2899 0.3349 0.0032  -0.0393 0.0647  274 VAL A CG2 
78   N N   . GLN A 11  ? 0.3599 0.3176 0.3275 -0.0481 -0.0755 0.0693  275 GLN A N   
79   C CA  . GLN A 11  ? 0.3653 0.3063 0.2990 -0.0719 -0.0861 0.0684  275 GLN A CA  
80   C C   . GLN A 11  ? 0.3652 0.3344 0.3132 -0.0647 -0.0927 0.0781  275 GLN A C   
81   O O   . GLN A 11  ? 0.4076 0.3551 0.3252 -0.0731 -0.0935 0.0705  275 GLN A O   
82   C CB  . GLN A 11  ? 0.3971 0.3452 0.3183 -0.1058 -0.1040 0.0807  275 GLN A CB  
83   C CG  . GLN A 11  ? 0.6014 0.5037 0.4922 -0.1190 -0.0939 0.0680  275 GLN A CG  
84   C CD  . GLN A 11  ? 0.7399 0.6574 0.6270 -0.1522 -0.1114 0.0822  275 GLN A CD  
85   O OE1 . GLN A 11  ? 0.7401 0.6983 0.6357 -0.1742 -0.1341 0.1022  275 GLN A OE1 
86   N NE2 . GLN A 11  ? 0.8112 0.7000 0.6886 -0.1562 -0.1008 0.0756  275 GLN A NE2 
87   N N   . SER A 12  ? 0.3403 0.3538 0.3326 -0.0498 -0.0946 0.0963  276 SER A N   
88   C CA  . SER A 12  ? 0.3007 0.3371 0.3072 -0.0425 -0.0972 0.1099  276 SER A CA  
89   C C   . SER A 12  ? 0.3380 0.3500 0.3340 -0.0223 -0.0802 0.0909  276 SER A C   
90   O O   . SER A 12  ? 0.3740 0.3803 0.3562 -0.0239 -0.0821 0.0909  276 SER A O   
91   C CB  . SER A 12  ? 0.4497 0.5331 0.5072 -0.0285 -0.0953 0.1379  276 SER A CB  
92   O OG  . SER A 12  ? 0.5393 0.6189 0.6157 -0.0065 -0.0755 0.1300  276 SER A OG  
93   N N   . VAL A 13  ? 0.3380 0.3382 0.3389 -0.0069 -0.0652 0.0767  277 VAL A N   
94   C CA  . VAL A 13  ? 0.3224 0.3076 0.3155 0.0073  -0.0510 0.0625  277 VAL A CA  
95   C C   . VAL A 13  ? 0.3320 0.2862 0.2914 -0.0004 -0.0512 0.0488  277 VAL A C   
96   O O   . VAL A 13  ? 0.3537 0.2997 0.3029 0.0042  -0.0464 0.0436  277 VAL A O   
97   C CB  . VAL A 13  ? 0.3421 0.3288 0.3452 0.0183  -0.0385 0.0550  277 VAL A CB  
98   C CG1 . VAL A 13  ? 0.3531 0.3280 0.3437 0.0251  -0.0276 0.0421  277 VAL A CG1 
99   C CG2 . VAL A 13  ? 0.3386 0.3458 0.3666 0.0258  -0.0313 0.0661  277 VAL A CG2 
100  N N   . CYS A 14  ? 0.3330 0.2649 0.2728 -0.0122 -0.0530 0.0432  278 CYS A N   
101  C CA  . CYS A 14  ? 0.3534 0.2450 0.2561 -0.0196 -0.0457 0.0305  278 CYS A CA  
102  C C   . CYS A 14  ? 0.4037 0.2865 0.2785 -0.0377 -0.0563 0.0323  278 CYS A C   
103  O O   . CYS A 14  ? 0.4476 0.3065 0.2990 -0.0363 -0.0476 0.0227  278 CYS A O   
104  C CB  . CYS A 14  ? 0.3760 0.2355 0.2590 -0.0295 -0.0391 0.0254  278 CYS A CB  
105  S SG  . CYS A 14  ? 0.4508 0.3184 0.3645 -0.0048 -0.0222 0.0266  278 CYS A SG  
106  N N   . LYS A 15  ? 0.4038 0.3101 0.2821 -0.0563 -0.0758 0.0479  279 LYS A N   
107  C CA  . LYS A 15  ? 0.4275 0.3382 0.2829 -0.0776 -0.0907 0.0572  279 LYS A CA  
108  C C   . LYS A 15  ? 0.3736 0.3038 0.2486 -0.0584 -0.0875 0.0632  279 LYS A C   
109  O O   . LYS A 15  ? 0.4379 0.3500 0.2830 -0.0670 -0.0879 0.0589  279 LYS A O   
110  C CB  . LYS A 15  ? 0.4051 0.3552 0.2746 -0.1003 -0.1144 0.0823  279 LYS A CB  
111  C CG  . LYS A 15  ? 0.4663 0.4378 0.3190 -0.1262 -0.1355 0.1023  279 LYS A CG  
112  C CD  . LYS A 15  ? 0.5564 0.5800 0.4318 -0.1507 -0.1608 0.1349  279 LYS A CD  
113  C CE  . LYS A 15  ? 0.6499 0.7223 0.5383 -0.1661 -0.1813 0.1687  279 LYS A CE  
114  N NZ  . LYS A 15  ? 0.7579 0.8868 0.6923 -0.1803 -0.1912 0.1989  279 LYS A NZ  
115  N N   . SER A 16  ? 0.3524 0.3122 0.2721 -0.0339 -0.0806 0.0717  280 SER A N   
116  C CA  . SER A 16  ? 0.3252 0.2963 0.2620 -0.0154 -0.0718 0.0773  280 SER A CA  
117  C C   . SER A 16  ? 0.3353 0.2722 0.2453 -0.0093 -0.0582 0.0548  280 SER A C   
118  O O   . SER A 16  ? 0.3843 0.3155 0.2817 -0.0096 -0.0575 0.0560  280 SER A O   
119  C CB  . SER A 16  ? 0.3608 0.3526 0.3379 0.0068  -0.0585 0.0847  280 SER A CB  
120  O OG  . SER A 16  ? 0.4127 0.4406 0.4214 0.0046  -0.0676 0.1118  280 SER A OG  
121  N N   . TYR A 17  ? 0.3473 0.2653 0.2512 -0.0043 -0.0477 0.0381  281 TYR A N   
122  C CA  . TYR A 17  ? 0.3510 0.2440 0.2375 0.0025  -0.0333 0.0224  281 TYR A CA  
123  C C   . TYR A 17  ? 0.3941 0.2533 0.2378 -0.0134 -0.0338 0.0157  281 TYR A C   
124  O O   . TYR A 17  ? 0.3877 0.2359 0.2180 -0.0104 -0.0271 0.0110  281 TYR A O   
125  C CB  . TYR A 17  ? 0.3342 0.2227 0.2304 0.0113  -0.0220 0.0151  281 TYR A CB  
126  C CG  . TYR A 17  ? 0.4136 0.2851 0.2996 0.0191  -0.0063 0.0067  281 TYR A CG  
127  C CD1 . TYR A 17  ? 0.4568 0.3431 0.3538 0.0270  -0.0011 0.0058  281 TYR A CD1 
128  C CD2 . TYR A 17  ? 0.4773 0.3144 0.3406 0.0172  0.0063  0.0010  281 TYR A CD2 
129  C CE1 . TYR A 17  ? 0.5414 0.4197 0.4339 0.0329  0.0123  0.0021  281 TYR A CE1 
130  C CE2 . TYR A 17  ? 0.5549 0.3805 0.4159 0.0277  0.0246  -0.0017 281 TYR A CE2 
131  C CZ  . TYR A 17  ? 0.5789 0.4303 0.4572 0.0350  0.0251  0.0001  281 TYR A CZ  
132  O OH  . TYR A 17  ? 0.6681 0.5160 0.5488 0.0437  0.0416  0.0012  281 TYR A OH  
133  N N   . ARG A 18  ? 0.4257 0.2639 0.2422 -0.0333 -0.0398 0.0142  282 ARG A N   
134  C CA  . ARG A 18  ? 0.5021 0.2975 0.2648 -0.0547 -0.0366 0.0053  282 ARG A CA  
135  C C   . ARG A 18  ? 0.5283 0.3391 0.2795 -0.0663 -0.0514 0.0156  282 ARG A C   
136  O O   . ARG A 18  ? 0.5740 0.3550 0.2896 -0.0728 -0.0431 0.0070  282 ARG A O   
137  C CB  . ARG A 18  ? 0.5477 0.3151 0.2740 -0.0835 -0.0421 0.0029  282 ARG A CB  
138  C CG  . ARG A 18  ? 0.6879 0.4231 0.4117 -0.0754 -0.0217 -0.0075 282 ARG A CG  
139  C CD  . ARG A 18  ? 0.7551 0.4448 0.4242 -0.1114 -0.0226 -0.0135 282 ARG A CD  
140  N NE  . ARG A 18  ? 0.9194 0.6487 0.5929 -0.1385 -0.0550 0.0027  282 ARG A NE  
141  C CZ  . ARG A 18  ? 1.1286 0.8692 0.7731 -0.1693 -0.0766 0.0121  282 ARG A CZ  
142  N NH1 . ARG A 18  ? 1.2007 0.9895 0.8609 -0.1921 -0.1064 0.0347  282 ARG A NH1 
143  N NH2 . ARG A 18  ? 1.1780 0.8862 0.7797 -0.1784 -0.0688 0.0027  282 ARG A NH2 
144  N N   . GLU A 19  ? 0.4526 0.3106 0.2363 -0.0672 -0.0709 0.0374  283 GLU A N   
145  C CA  . GLU A 19  ? 0.4464 0.3279 0.2288 -0.0756 -0.0851 0.0560  283 GLU A CA  
146  C C   . GLU A 19  ? 0.4371 0.3185 0.2336 -0.0516 -0.0708 0.0527  283 GLU A C   
147  O O   . GLU A 19  ? 0.4418 0.3320 0.2293 -0.0579 -0.0781 0.0655  283 GLU A O   
148  C CB  . GLU A 19  ? 0.4322 0.3698 0.2580 -0.0768 -0.1042 0.0880  283 GLU A CB  
149  C CG  . GLU A 19  ? 0.4957 0.4439 0.3032 -0.1115 -0.1260 0.0995  283 GLU A CG  
150  C CD  . GLU A 19  ? 0.5859 0.5948 0.4496 -0.1060 -0.1398 0.1328  283 GLU A CD  
151  O OE1 . GLU A 19  ? 0.5116 0.5426 0.4256 -0.0720 -0.1259 0.1411  283 GLU A OE1 
152  O OE2 . GLU A 19  ? 0.5991 0.6323 0.4544 -0.1382 -0.1628 0.1518  283 GLU A OE2 
153  N N   . THR A 20  ? 0.4037 0.2771 0.2202 -0.0276 -0.0516 0.0379  284 THR A N   
154  C CA  . THR A 20  ? 0.3752 0.2526 0.2071 -0.0088 -0.0390 0.0368  284 THR A CA  
155  C C   . THR A 20  ? 0.4038 0.2548 0.2237 -0.0001 -0.0200 0.0155  284 THR A C   
156  O O   . THR A 20  ? 0.3937 0.2502 0.2287 0.0130  -0.0087 0.0123  284 THR A O   
157  C CB  . THR A 20  ? 0.3407 0.2456 0.2163 0.0097  -0.0334 0.0473  284 THR A CB  
158  O OG1 . THR A 20  ? 0.3431 0.2496 0.2324 0.0151  -0.0281 0.0373  284 THR A OG1 
159  C CG2 . THR A 20  ? 0.3414 0.2787 0.2406 0.0071  -0.0470 0.0758  284 THR A CG2 
160  N N   . CYS A 21  ? 0.3120 0.2807 0.2944 -0.0351 -0.0208 0.0116  285 CYS A N   
161  C CA  . CYS A 21  ? 0.3329 0.2939 0.3066 -0.0301 -0.0198 0.0100  285 CYS A CA  
162  C C   . CYS A 21  ? 0.3731 0.3378 0.3463 -0.0276 -0.0223 0.0096  285 CYS A C   
163  O O   . CYS A 21  ? 0.3724 0.3325 0.3407 -0.0233 -0.0217 0.0081  285 CYS A O   
164  C CB  . CYS A 21  ? 0.4204 0.3695 0.3836 -0.0312 -0.0179 0.0079  285 CYS A CB  
165  S SG  . CYS A 21  ? 0.4667 0.4149 0.4258 -0.0364 -0.0198 0.0056  285 CYS A SG  
166  N N   . GLN A 22  ? 0.3286 0.3015 0.3068 -0.0303 -0.0250 0.0111  286 GLN A N   
167  C CA  . GLN A 22  ? 0.3375 0.3151 0.3164 -0.0286 -0.0269 0.0117  286 GLN A CA  
168  C C   . GLN A 22  ? 0.3995 0.3728 0.3692 -0.0294 -0.0270 0.0090  286 GLN A C   
169  O O   . GLN A 22  ? 0.4130 0.3907 0.3815 -0.0324 -0.0290 0.0096  286 GLN A O   
170  C CB  . GLN A 22  ? 0.4208 0.3993 0.4032 -0.0232 -0.0258 0.0118  286 GLN A CB  
171  C CG  . GLN A 22  ? 0.4463 0.4317 0.4333 -0.0224 -0.0274 0.0136  286 GLN A CG  
172  C CD  . GLN A 22  ? 0.5047 0.4917 0.4970 -0.0179 -0.0264 0.0134  286 GLN A CD  
173  O OE1 . GLN A 22  ? 0.5359 0.5197 0.5286 -0.0151 -0.0250 0.0120  286 GLN A OE1 
174  N NE2 . GLN A 22  ? 0.4278 0.4197 0.4239 -0.0174 -0.0271 0.0148  286 GLN A NE2 
175  N N   . LEU A 23  ? 0.3655 0.3303 0.3286 -0.0265 -0.0248 0.0060  287 LEU A N   
176  C CA  . LEU A 23  ? 0.3194 0.2788 0.2740 -0.0272 -0.0241 0.0027  287 LEU A CA  
177  C C   . LEU A 23  ? 0.3288 0.2778 0.2773 -0.0281 -0.0223 0.0005  287 LEU A C   
178  O O   . LEU A 23  ? 0.3744 0.3189 0.3235 -0.0258 -0.0210 0.0015  287 LEU A O   
179  C CB  . LEU A 23  ? 0.3394 0.2982 0.2930 -0.0221 -0.0230 0.0009  287 LEU A CB  
180  C CG  . LEU A 23  ? 0.4471 0.4150 0.4059 -0.0216 -0.0239 0.0026  287 LEU A CG  
181  C CD1 . LEU A 23  ? 0.4507 0.4173 0.4090 -0.0169 -0.0222 -0.0001 287 LEU A CD1 
182  C CD2 . LEU A 23  ? 0.4705 0.4424 0.4261 -0.0267 -0.0253 0.0033  287 LEU A CD2 
183  N N   . ARG A 24  ? 0.3354 0.2799 0.2775 -0.0318 -0.0220 -0.0024 288 ARG A N   
184  C CA  . ARG A 24  ? 0.3246 0.2576 0.2606 -0.0329 -0.0199 -0.0048 288 ARG A CA  
185  C C   . ARG A 24  ? 0.3543 0.2785 0.2855 -0.0268 -0.0178 -0.0069 288 ARG A C   
186  O O   . ARG A 24  ? 0.3432 0.2698 0.2740 -0.0239 -0.0178 -0.0087 288 ARG A O   
187  C CB  . ARG A 24  ? 0.4303 0.3613 0.3614 -0.0391 -0.0203 -0.0079 288 ARG A CB  
188  C CG  . ARG A 24  ? 0.5412 0.4818 0.4777 -0.0452 -0.0233 -0.0059 288 ARG A CG  
189  C CD  . ARG A 24  ? 0.7186 0.6568 0.6501 -0.0519 -0.0241 -0.0095 288 ARG A CD  
190  N NE  . ARG A 24  ? 0.8599 0.7896 0.7823 -0.0512 -0.0221 -0.0144 288 ARG A NE  
191  C CZ  . ARG A 24  ? 0.9460 0.8784 0.8629 -0.0542 -0.0234 -0.0175 288 ARG A CZ  
192  N NH1 . ARG A 24  ? 0.9619 0.9055 0.8809 -0.0581 -0.0274 -0.0155 288 ARG A NH1 
193  N NH2 . ARG A 24  ? 0.9490 0.8729 0.8581 -0.0532 -0.0206 -0.0226 288 ARG A NH2 
194  N N   . LEU A 25  ? 0.3778 0.2920 0.3059 -0.0250 -0.0161 -0.0064 289 LEU A N   
195  C CA  . LEU A 25  ? 0.3504 0.2560 0.2745 -0.0184 -0.0149 -0.0077 289 LEU A CA  
196  C C   . LEU A 25  ? 0.3888 0.2890 0.3082 -0.0186 -0.0137 -0.0123 289 LEU A C   
197  O O   . LEU A 25  ? 0.3833 0.2827 0.3027 -0.0130 -0.0134 -0.0143 289 LEU A O   
198  C CB  . LEU A 25  ? 0.3831 0.2776 0.3028 -0.0170 -0.0133 -0.0057 289 LEU A CB  
199  C CG  . LEU A 25  ? 0.4149 0.3000 0.3302 -0.0096 -0.0130 -0.0063 289 LEU A CG  
200  C CD1 . LEU A 25  ? 0.4246 0.3180 0.3447 -0.0037 -0.0152 -0.0051 289 LEU A CD1 
201  C CD2 . LEU A 25  ? 0.5189 0.3905 0.4275 -0.0097 -0.0110 -0.0039 289 LEU A CD2 
202  N N   . GLU A 26  ? 0.4073 0.3036 0.3229 -0.0248 -0.0128 -0.0146 290 GLU A N   
203  C CA  . GLU A 26  ? 0.4167 0.3074 0.3274 -0.0250 -0.0112 -0.0198 290 GLU A CA  
204  C C   . GLU A 26  ? 0.3931 0.2937 0.3058 -0.0234 -0.0117 -0.0217 290 GLU A C   
205  O O   . GLU A 26  ? 0.4169 0.3134 0.3272 -0.0203 -0.0096 -0.0258 290 GLU A O   
206  C CB  . GLU A 26  ? 0.4202 0.3066 0.3265 -0.0328 -0.0105 -0.0228 290 GLU A CB  
207  C CG  . GLU A 26  ? 0.6227 0.5161 0.5324 -0.0398 -0.0125 -0.0202 290 GLU A CG  
208  C CD  . GLU A 26  ? 0.6536 0.5416 0.5653 -0.0395 -0.0115 -0.0164 290 GLU A CD  
209  O OE1 . GLU A 26  ? 0.7376 0.6132 0.6450 -0.0414 -0.0090 -0.0176 290 GLU A OE1 
210  O OE2 . GLU A 26  ? 0.5948 0.4903 0.5118 -0.0374 -0.0128 -0.0122 290 GLU A OE2 
211  N N   . ASP A 27  ? 0.3610 0.2740 0.2782 -0.0258 -0.0140 -0.0188 291 ASP A N   
212  C CA  . ASP A 27  ? 0.3735 0.2956 0.2923 -0.0250 -0.0142 -0.0198 291 ASP A CA  
213  C C   . ASP A 27  ? 0.3645 0.2881 0.2882 -0.0174 -0.0134 -0.0194 291 ASP A C   
214  O O   . ASP A 27  ? 0.3920 0.3166 0.3153 -0.0149 -0.0115 -0.0227 291 ASP A O   
215  C CB  . ASP A 27  ? 0.4407 0.3748 0.3634 -0.0290 -0.0170 -0.0159 291 ASP A CB  
216  C CG  . ASP A 27  ? 0.6740 0.6088 0.5929 -0.0366 -0.0188 -0.0163 291 ASP A CG  
217  O OD1 . ASP A 27  ? 0.7512 0.6793 0.6630 -0.0396 -0.0174 -0.0210 291 ASP A OD1 
218  O OD2 . ASP A 27  ? 0.8196 0.7620 0.7432 -0.0396 -0.0218 -0.0124 291 ASP A OD2 
219  N N   . LEU A 28  ? 0.3197 0.2437 0.2478 -0.0141 -0.0148 -0.0158 292 LEU A N   
220  C CA  . LEU A 28  ? 0.3500 0.2759 0.2831 -0.0071 -0.0150 -0.0156 292 LEU A CA  
221  C C   . LEU A 28  ? 0.3737 0.2902 0.3038 -0.0020 -0.0132 -0.0194 292 LEU A C   
222  O O   . LEU A 28  ? 0.3757 0.2959 0.3101 0.0027  -0.0125 -0.0216 292 LEU A O   
223  C CB  . LEU A 28  ? 0.3552 0.2817 0.2915 -0.0049 -0.0169 -0.0116 292 LEU A CB  
224  C CG  . LEU A 28  ? 0.3502 0.2870 0.2924 -0.0081 -0.0185 -0.0080 292 LEU A CG  
225  C CD1 . LEU A 28  ? 0.3997 0.3348 0.3434 -0.0064 -0.0195 -0.0050 292 LEU A CD1 
226  C CD2 . LEU A 28  ? 0.3851 0.3318 0.3339 -0.0061 -0.0189 -0.0082 292 LEU A CD2 
227  N N   . LEU A 29  ? 0.3626 0.2672 0.2864 -0.0029 -0.0122 -0.0202 293 LEU A N   
228  C CA  . LEU A 29  ? 0.3557 0.2498 0.2770 0.0025  -0.0107 -0.0232 293 LEU A CA  
229  C C   . LEU A 29  ? 0.3635 0.2580 0.2839 0.0019  -0.0078 -0.0288 293 LEU A C   
230  O O   . LEU A 29  ? 0.3543 0.2475 0.2779 0.0080  -0.0066 -0.0318 293 LEU A O   
231  C CB  . LEU A 29  ? 0.3325 0.2122 0.2470 0.0013  -0.0099 -0.0223 293 LEU A CB  
232  C CG  . LEU A 29  ? 0.3610 0.2381 0.2750 0.0030  -0.0118 -0.0169 293 LEU A CG  
233  C CD1 . LEU A 29  ? 0.3825 0.2449 0.2894 0.0011  -0.0102 -0.0156 293 LEU A CD1 
234  C CD2 . LEU A 29  ? 0.4133 0.2922 0.3308 0.0114  -0.0139 -0.0157 293 LEU A CD2 
235  N N   . ARG A 30  ? 0.3466 0.2438 0.2632 -0.0053 -0.0068 -0.0305 294 ARG A N   
236  C CA  . ARG A 30  ? 0.3458 0.2431 0.2598 -0.0065 -0.0036 -0.0363 294 ARG A CA  
237  C C   . ARG A 30  ? 0.3719 0.2812 0.2917 -0.0042 -0.0027 -0.0371 294 ARG A C   
238  O O   . ARG A 30  ? 0.4114 0.3206 0.3307 -0.0030 0.0007  -0.0421 294 ARG A O   
239  C CB  . ARG A 30  ? 0.3659 0.2628 0.2727 -0.0153 -0.0032 -0.0380 294 ARG A CB  
240  C CG  . ARG A 30  ? 0.4375 0.3203 0.3388 -0.0172 -0.0024 -0.0398 294 ARG A CG  
241  C CD  . ARG A 30  ? 0.5002 0.3819 0.3949 -0.0262 -0.0024 -0.0424 294 ARG A CD  
242  N NE  . ARG A 30  ? 0.5810 0.4723 0.4775 -0.0314 -0.0061 -0.0377 294 ARG A NE  
243  C CZ  . ARG A 30  ? 0.5834 0.4758 0.4758 -0.0393 -0.0075 -0.0389 294 ARG A CZ  
244  N NH1 . ARG A 30  ? 0.5034 0.3873 0.3891 -0.0429 -0.0053 -0.0450 294 ARG A NH1 
245  N NH2 . ARG A 30  ? 0.6334 0.5355 0.5291 -0.0433 -0.0112 -0.0343 294 ARG A NH2 
246  N N   . GLN A 31  ? 0.3539 0.2728 0.2796 -0.0036 -0.0053 -0.0324 295 GLN A N   
247  C CA  . GLN A 31  ? 0.3000 0.2299 0.2320 -0.0019 -0.0044 -0.0327 295 GLN A CA  
248  C C   . GLN A 31  ? 0.3539 0.2849 0.2941 0.0061  -0.0042 -0.0339 295 GLN A C   
249  O O   . GLN A 31  ? 0.3458 0.2860 0.2927 0.0076  -0.0030 -0.0348 295 GLN A O   
250  C CB  . GLN A 31  ? 0.3478 0.2872 0.2831 -0.0053 -0.0072 -0.0272 295 GLN A CB  
251  C CG  . GLN A 31  ? 0.3986 0.3408 0.3275 -0.0131 -0.0077 -0.0259 295 GLN A CG  
252  C CD  . GLN A 31  ? 0.5275 0.4749 0.4531 -0.0159 -0.0046 -0.0286 295 GLN A CD  
253  O OE1 . GLN A 31  ? 0.5504 0.4986 0.4784 -0.0123 -0.0010 -0.0325 295 GLN A OE1 
254  N NE2 . GLN A 31  ? 0.6095 0.5607 0.5295 -0.0222 -0.0059 -0.0266 295 GLN A NE2 
255  N N   . ARG A 32  ? 0.3835 0.3055 0.3234 0.0111  -0.0056 -0.0339 296 ARG A N   
256  C CA  . ARG A 32  ? 0.3485 0.2722 0.2965 0.0192  -0.0069 -0.0345 296 ARG A CA  
257  C C   . ARG A 32  ? 0.3472 0.2756 0.3014 0.0225  -0.0034 -0.0399 296 ARG A C   
258  O O   . ARG A 32  ? 0.4155 0.3514 0.3792 0.0273  -0.0044 -0.0404 296 ARG A O   
259  C CB  . ARG A 32  ? 0.3934 0.3046 0.3379 0.0240  -0.0088 -0.0336 296 ARG A CB  
260  C CG  . ARG A 32  ? 0.4043 0.3139 0.3463 0.0231  -0.0125 -0.0279 296 ARG A CG  
261  C CD  . ARG A 32  ? 0.5008 0.3971 0.4374 0.0271  -0.0140 -0.0260 296 ARG A CD  
262  N NE  . ARG A 32  ? 0.6461 0.5435 0.5812 0.0266  -0.0171 -0.0208 296 ARG A NE  
263  C CZ  . ARG A 32  ? 0.7122 0.6058 0.6467 0.0325  -0.0202 -0.0183 296 ARG A CZ  
264  N NH1 . ARG A 32  ? 0.6847 0.5796 0.6168 0.0311  -0.0223 -0.0142 296 ARG A NH1 
265  N NH2 . ARG A 32  ? 0.7096 0.5981 0.6456 0.0398  -0.0213 -0.0201 296 ARG A NH2 
266  N N   . SER A 33  ? 0.3658 0.2901 0.3152 0.0200  0.0010  -0.0446 297 SER A N   
267  C CA  . SER A 33  ? 0.4165 0.3454 0.3722 0.0232  0.0053  -0.0502 297 SER A CA  
268  C C   . SER A 33  ? 0.4462 0.3877 0.4046 0.0185  0.0080  -0.0505 297 SER A C   
269  O O   . SER A 33  ? 0.4553 0.4027 0.4200 0.0205  0.0121  -0.0548 297 SER A O   
270  C CB  . SER A 33  ? 0.4377 0.3566 0.3874 0.0229  0.0096  -0.0560 297 SER A CB  
271  O OG  . SER A 33  ? 0.5057 0.4221 0.4444 0.0145  0.0113  -0.0564 297 SER A OG  
272  N N   . ASN A 34  ? 0.4088 0.3541 0.3628 0.0125  0.0058  -0.0455 298 ASN A N   
273  C CA  . ASN A 34  ? 0.3916 0.3477 0.3471 0.0078  0.0078  -0.0442 298 ASN A CA  
274  C C   . ASN A 34  ? 0.3628 0.3282 0.3301 0.0110  0.0055  -0.0414 298 ASN A C   
275  O O   . ASN A 34  ? 0.3609 0.3282 0.3288 0.0095  0.0014  -0.0362 298 ASN A O   
276  C CB  . ASN A 34  ? 0.4051 0.3603 0.3507 0.0002  0.0060  -0.0402 298 ASN A CB  
277  C CG  . ASN A 34  ? 0.4423 0.4060 0.3859 -0.0052 0.0085  -0.0388 298 ASN A CG  
278  O OD1 . ASN A 34  ? 0.4759 0.4456 0.4245 -0.0041 0.0126  -0.0414 298 ASN A OD1 
279  N ND2 . ASN A 34  ? 0.4299 0.3941 0.3662 -0.0112 0.0059  -0.0345 298 ASN A ND2 
280  N N   . ILE A 35  ? 0.3759 0.3471 0.3535 0.0156  0.0082  -0.0453 299 ILE A N   
281  C CA  . ILE A 35  ? 0.3531 0.3328 0.3433 0.0194  0.0058  -0.0441 299 ILE A CA  
282  C C   . ILE A 35  ? 0.3262 0.3169 0.3230 0.0162  0.0102  -0.0449 299 ILE A C   
283  O O   . ILE A 35  ? 0.3557 0.3479 0.3510 0.0143  0.0161  -0.0488 299 ILE A O   
284  C CB  . ILE A 35  ? 0.3529 0.3312 0.3516 0.0279  0.0044  -0.0480 299 ILE A CB  
285  C CG1 . ILE A 35  ? 0.3974 0.3640 0.3888 0.0310  -0.0003 -0.0458 299 ILE A CG1 
286  C CG2 . ILE A 35  ? 0.3325 0.3217 0.3454 0.0313  0.0024  -0.0482 299 ILE A CG2 
287  C CD1 . ILE A 35  ? 0.4167 0.3766 0.4107 0.0383  0.0000  -0.0500 299 ILE A CD1 
288  N N   . PHE A 36  ? 0.3211 0.3188 0.3248 0.0152  0.0078  -0.0413 300 PHE A N   
289  C CA  . PHE A 36  ? 0.3195 0.3270 0.3307 0.0121  0.0123  -0.0418 300 PHE A CA  
290  C C   . PHE A 36  ? 0.3150 0.3282 0.3374 0.0164  0.0164  -0.0483 300 PHE A C   
291  O O   . PHE A 36  ? 0.3326 0.3467 0.3640 0.0231  0.0132  -0.0511 300 PHE A O   
292  C CB  . PHE A 36  ? 0.2777 0.2913 0.2969 0.0113  0.0089  -0.0377 300 PHE A CB  
293  C CG  . PHE A 36  ? 0.3011 0.3115 0.3117 0.0062  0.0063  -0.0313 300 PHE A CG  
294  C CD1 . PHE A 36  ? 0.2599 0.2711 0.2636 -0.0001 0.0098  -0.0283 300 PHE A CD1 
295  C CD2 . PHE A 36  ? 0.2998 0.3067 0.3095 0.0078  0.0005  -0.0281 300 PHE A CD2 
296  C CE1 . PHE A 36  ? 0.2872 0.2961 0.2842 -0.0043 0.0068  -0.0221 300 PHE A CE1 
297  C CE2 . PHE A 36  ? 0.3151 0.3198 0.3185 0.0033  -0.0017 -0.0224 300 PHE A CE2 
298  C CZ  . PHE A 36  ? 0.2677 0.2737 0.2656 -0.0025 0.0011  -0.0194 300 PHE A CZ  
299  N N   . SER A 37  ? 0.3166 0.3337 0.3382 0.0125  0.0235  -0.0505 301 SER A N   
300  C CA  . SER A 37  ? 0.3258 0.3502 0.3597 0.0157  0.0289  -0.0569 301 SER A CA  
301  C C   . SER A 37  ? 0.3485 0.3836 0.3990 0.0171  0.0279  -0.0571 301 SER A C   
302  O O   . SER A 37  ? 0.3631 0.4002 0.4145 0.0142  0.0247  -0.0522 301 SER A O   
303  C CB  . SER A 37  ? 0.3907 0.4165 0.4183 0.0101  0.0376  -0.0591 301 SER A CB  
304  O OG  . SER A 37  ? 0.3908 0.4215 0.4171 0.0036  0.0397  -0.0542 301 SER A OG  
305  N N   . ARG A 38  ? 0.3320 0.3744 0.3968 0.0214  0.0309  -0.0632 302 ARG A N   
306  C CA  . ARG A 38  ? 0.3420 0.3959 0.4242 0.0223  0.0306  -0.0646 302 ARG A CA  
307  C C   . ARG A 38  ? 0.3442 0.4028 0.4261 0.0143  0.0355  -0.0610 302 ARG A C   
308  O O   . ARG A 38  ? 0.3724 0.4357 0.4621 0.0130  0.0326  -0.0585 302 ARG A O   
309  C CB  . ARG A 38  ? 0.3999 0.4617 0.4976 0.0275  0.0345  -0.0723 302 ARG A CB  
310  C CG  . ARG A 38  ? 0.5581 0.6325 0.6762 0.0296  0.0326  -0.0749 302 ARG A CG  
311  C CD  . ARG A 38  ? 0.7477 0.8293 0.8821 0.0371  0.0336  -0.0826 302 ARG A CD  
312  N NE  . ARG A 38  ? 0.8500 0.9234 0.9799 0.0451  0.0268  -0.0831 302 ARG A NE  
313  C CZ  . ARG A 38  ? 0.8677 0.9357 0.9947 0.0492  0.0298  -0.0869 302 ARG A CZ  
314  N NH1 . ARG A 38  ? 0.8625 0.9332 0.9906 0.0462  0.0398  -0.0912 302 ARG A NH1 
315  N NH2 . ARG A 38  ? 0.8720 0.9314 0.9947 0.0563  0.0233  -0.0864 302 ARG A NH2 
316  N N   . GLU A 39  ? 0.3367 0.3931 0.4085 0.0088  0.0429  -0.0606 303 GLU A N   
317  C CA  . GLU A 39  ? 0.3810 0.4404 0.4506 0.0013  0.0476  -0.0562 303 GLU A CA  
318  C C   . GLU A 39  ? 0.3405 0.3941 0.4005 -0.0020 0.0415  -0.0481 303 GLU A C   
319  O O   . GLU A 39  ? 0.3438 0.4012 0.4093 -0.0057 0.0420  -0.0443 303 GLU A O   
320  C CB  . GLU A 39  ? 0.4895 0.5468 0.5473 -0.0038 0.0564  -0.0572 303 GLU A CB  
321  C CG  . GLU A 39  ? 0.7335 0.7941 0.7896 -0.0114 0.0618  -0.0523 303 GLU A CG  
322  C CD  . GLU A 39  ? 0.9372 0.9931 0.9752 -0.0176 0.0686  -0.0504 303 GLU A CD  
323  O OE1 . GLU A 39  ? 0.9996 1.0490 1.0249 -0.0165 0.0683  -0.0527 303 GLU A OE1 
324  O OE2 . GLU A 39  ? 1.0104 1.0686 1.0463 -0.0237 0.0741  -0.0466 303 GLU A OE2 
325  N N   . GLU A 40  ? 0.3347 0.3793 0.3815 -0.0007 0.0362  -0.0456 304 GLU A N   
326  C CA  . GLU A 40  ? 0.3393 0.3789 0.3780 -0.0035 0.0307  -0.0383 304 GLU A CA  
327  C C   . GLU A 40  ? 0.3257 0.3683 0.3760 0.0000  0.0245  -0.0376 304 GLU A C   
328  O O   . GLU A 40  ? 0.3214 0.3642 0.3725 -0.0030 0.0224  -0.0326 304 GLU A O   
329  C CB  . GLU A 40  ? 0.3342 0.3643 0.3574 -0.0033 0.0270  -0.0366 304 GLU A CB  
330  C CG  . GLU A 40  ? 0.4212 0.4479 0.4308 -0.0077 0.0326  -0.0373 304 GLU A CG  
331  C CD  . GLU A 40  ? 0.5142 0.5317 0.5097 -0.0076 0.0290  -0.0369 304 GLU A CD  
332  O OE1 . GLU A 40  ? 0.6302 0.6442 0.6131 -0.0128 0.0281  -0.0322 304 GLU A OE1 
333  O OE2 . GLU A 40  ? 0.4029 0.4167 0.4003 -0.0024 0.0269  -0.0410 304 GLU A OE2 
334  N N   . VAL A 41  ? 0.2872 0.3319 0.3464 0.0064  0.0215  -0.0426 305 VAL A N   
335  C CA  . VAL A 41  ? 0.2809 0.3291 0.3508 0.0099  0.0154  -0.0428 305 VAL A CA  
336  C C   . VAL A 41  ? 0.2784 0.3359 0.3623 0.0068  0.0185  -0.0433 305 VAL A C   
337  O O   . VAL A 41  ? 0.2652 0.3235 0.3527 0.0051  0.0155  -0.0402 305 VAL A O   
338  C CB  . VAL A 41  ? 0.2993 0.3488 0.3762 0.0177  0.0116  -0.0482 305 VAL A CB  
339  C CG1 . VAL A 41  ? 0.2969 0.3525 0.3864 0.0207  0.0061  -0.0494 305 VAL A CG1 
340  C CG2 . VAL A 41  ? 0.2956 0.3343 0.3589 0.0208  0.0077  -0.0468 305 VAL A CG2 
341  N N   . THR A 42  ? 0.2923 0.3565 0.3845 0.0058  0.0252  -0.0475 306 THR A N   
342  C CA  . THR A 42  ? 0.3368 0.4097 0.4427 0.0021  0.0293  -0.0483 306 THR A CA  
343  C C   . THR A 42  ? 0.3407 0.4094 0.4387 -0.0049 0.0313  -0.0409 306 THR A C   
344  O O   . THR A 42  ? 0.2926 0.3644 0.3996 -0.0072 0.0306  -0.0392 306 THR A O   
345  C CB  . THR A 42  ? 0.3370 0.4173 0.4517 0.0011  0.0377  -0.0536 306 THR A CB  
346  O OG1 . THR A 42  ? 0.3189 0.4040 0.4438 0.0084  0.0351  -0.0605 306 THR A OG1 
347  C CG2 . THR A 42  ? 0.3049 0.3936 0.4339 -0.0038 0.0424  -0.0538 306 THR A CG2 
348  N N   . GLY A 43  ? 0.2977 0.3592 0.3791 -0.0079 0.0334  -0.0367 307 GLY A N   
349  C CA  . GLY A 43  ? 0.3204 0.3772 0.3928 -0.0138 0.0344  -0.0290 307 GLY A CA  
350  C C   . GLY A 43  ? 0.3200 0.3739 0.3939 -0.0129 0.0273  -0.0249 307 GLY A C   
351  O O   . GLY A 43  ? 0.2941 0.3489 0.3732 -0.0163 0.0281  -0.0212 307 GLY A O   
352  N N   . TYR A 44  ? 0.2711 0.3212 0.3409 -0.0081 0.0206  -0.0259 308 TYR A N   
353  C CA  . TYR A 44  ? 0.2470 0.2945 0.3183 -0.0070 0.0143  -0.0229 308 TYR A CA  
354  C C   . TYR A 44  ? 0.2301 0.2844 0.3183 -0.0056 0.0130  -0.0265 308 TYR A C   
355  O O   . TYR A 44  ? 0.2426 0.2960 0.3347 -0.0073 0.0109  -0.0236 308 TYR A O   
356  C CB  . TYR A 44  ? 0.2296 0.2716 0.2928 -0.0024 0.0084  -0.0237 308 TYR A CB  
357  C CG  . TYR A 44  ? 0.2514 0.2857 0.2989 -0.0047 0.0074  -0.0186 308 TYR A CG  
358  C CD1 . TYR A 44  ? 0.2561 0.2873 0.3004 -0.0073 0.0047  -0.0127 308 TYR A CD1 
359  C CD2 . TYR A 44  ? 0.2546 0.2852 0.2916 -0.0044 0.0090  -0.0202 308 TYR A CD2 
360  C CE1 . TYR A 44  ? 0.2849 0.3105 0.3167 -0.0094 0.0032  -0.0084 308 TYR A CE1 
361  C CE2 . TYR A 44  ? 0.2557 0.2799 0.2790 -0.0070 0.0075  -0.0160 308 TYR A CE2 
362  C CZ  . TYR A 44  ? 0.2355 0.2579 0.2568 -0.0095 0.0045  -0.0102 308 TYR A CZ  
363  O OH  . TYR A 44  ? 0.2935 0.3108 0.3025 -0.0121 0.0027  -0.0065 308 TYR A OH  
364  N N   . GLN A 45  ? 0.2816 0.3425 0.3798 -0.0023 0.0138  -0.0331 309 GLN A N   
365  C CA  . GLN A 45  ? 0.2748 0.3433 0.3895 -0.0009 0.0120  -0.0375 309 GLN A CA  
366  C C   . GLN A 45  ? 0.2893 0.3617 0.4133 -0.0070 0.0177  -0.0360 309 GLN A C   
367  O O   . GLN A 45  ? 0.2843 0.3605 0.4201 -0.0078 0.0160  -0.0377 309 GLN A O   
368  C CB  . GLN A 45  ? 0.2568 0.3326 0.3812 0.0041  0.0115  -0.0450 309 GLN A CB  
369  C CG  . GLN A 45  ? 0.2340 0.3055 0.3514 0.0108  0.0044  -0.0463 309 GLN A CG  
370  C CD  . GLN A 45  ? 0.2919 0.3696 0.4181 0.0165  0.0036  -0.0530 309 GLN A CD  
371  O OE1 . GLN A 45  ? 0.3024 0.3864 0.4368 0.0154  0.0096  -0.0564 309 GLN A OE1 
372  N NE2 . GLN A 45  ? 0.2422 0.3178 0.3664 0.0229  -0.0037 -0.0546 309 GLN A NE2 
373  N N   . ARG A 46  ? 0.2387 0.3096 0.3569 -0.0115 0.0246  -0.0328 310 ARG A N   
374  C CA  . ARG A 46  ? 0.2676 0.3405 0.3926 -0.0176 0.0308  -0.0302 310 ARG A CA  
375  C C   . ARG A 46  ? 0.2495 0.3148 0.3673 -0.0214 0.0298  -0.0220 310 ARG A C   
376  O O   . ARG A 46  ? 0.2619 0.3275 0.3859 -0.0263 0.0343  -0.0191 310 ARG A O   
377  C CB  . ARG A 46  ? 0.2698 0.3448 0.3917 -0.0212 0.0396  -0.0303 310 ARG A CB  
378  C CG  . ARG A 46  ? 0.3508 0.4354 0.4853 -0.0188 0.0431  -0.0387 310 ARG A CG  
379  C CD  . ARG A 46  ? 0.5619 0.6485 0.6943 -0.0239 0.0535  -0.0383 310 ARG A CD  
380  N NE  . ARG A 46  ? 0.7218 0.8030 0.8369 -0.0235 0.0558  -0.0369 310 ARG A NE  
381  C CZ  . ARG A 46  ? 0.8181 0.8912 0.9155 -0.0277 0.0574  -0.0297 310 ARG A CZ  
382  N NH1 . ARG A 46  ? 0.8779 0.9466 0.9724 -0.0320 0.0570  -0.0223 310 ARG A NH1 
383  N NH2 . ARG A 46  ? 0.7943 0.8634 0.8770 -0.0273 0.0593  -0.0300 310 ARG A NH2 
384  N N   . LYS A 47  ? 0.2384 0.2969 0.3441 -0.0192 0.0241  -0.0182 311 LYS A N   
385  C CA  . LYS A 47  ? 0.2061 0.2580 0.3063 -0.0221 0.0227  -0.0106 311 LYS A CA  
386  C C   . LYS A 47  ? 0.2134 0.2666 0.3266 -0.0219 0.0203  -0.0119 311 LYS A C   
387  O O   . LYS A 47  ? 0.2899 0.3482 0.4128 -0.0185 0.0172  -0.0186 311 LYS A O   
388  C CB  . LYS A 47  ? 0.2571 0.3025 0.3431 -0.0197 0.0173  -0.0069 311 LYS A CB  
389  C CG  . LYS A 47  ? 0.2789 0.3217 0.3502 -0.0208 0.0195  -0.0052 311 LYS A CG  
390  C CD  . LYS A 47  ? 0.2767 0.3134 0.3360 -0.0192 0.0138  -0.0016 311 LYS A CD  
391  C CE  . LYS A 47  ? 0.3288 0.3624 0.3727 -0.0205 0.0152  -0.0002 311 LYS A CE  
392  N NZ  . LYS A 47  ? 0.3576 0.3903 0.3953 -0.0259 0.0200  0.0051  311 LYS A NZ  
393  N N   . SER A 48  ? 0.2191 0.2678 0.3330 -0.0254 0.0214  -0.0058 312 SER A N   
394  C CA  . SER A 48  ? 0.2270 0.2756 0.3525 -0.0252 0.0190  -0.0073 312 SER A CA  
395  C C   . SER A 48  ? 0.2264 0.2720 0.3475 -0.0208 0.0118  -0.0080 312 SER A C   
396  O O   . SER A 48  ? 0.2513 0.2928 0.3597 -0.0190 0.0090  -0.0046 312 SER A O   
397  C CB  . SER A 48  ? 0.2062 0.2499 0.3346 -0.0299 0.0226  -0.0004 312 SER A CB  
398  O OG  . SER A 48  ? 0.2422 0.2788 0.3578 -0.0296 0.0200  0.0075  312 SER A OG  
399  N N   . MET A 49  ? 0.2624 0.3100 0.3942 -0.0194 0.0092  -0.0127 313 MET A N   
400  C CA  . MET A 49  ? 0.1976 0.2420 0.3260 -0.0160 0.0035  -0.0133 313 MET A CA  
401  C C   . MET A 49  ? 0.2108 0.2479 0.3320 -0.0173 0.0033  -0.0053 313 MET A C   
402  O O   . MET A 49  ? 0.2327 0.2666 0.3450 -0.0148 -0.0005 -0.0035 313 MET A O   
403  C CB  . MET A 49  ? 0.2656 0.3123 0.4067 -0.0158 0.0019  -0.0189 313 MET A CB  
404  C CG  . MET A 49  ? 0.3777 0.4233 0.5144 -0.0113 -0.0042 -0.0224 313 MET A CG  
405  S SD  . MET A 49  ? 0.5133 0.5569 0.6609 -0.0128 -0.0045 -0.0247 313 MET A SD  
406  C CE  . MET A 49  ? 0.2371 0.2727 0.3763 -0.0147 -0.0021 -0.0138 313 MET A CE  
407  N N   . TRP A 50  ? 0.2020 0.2366 0.3280 -0.0213 0.0073  -0.0003 314 TRP A N   
408  C CA  . TRP A 50  ? 0.2639 0.2920 0.3850 -0.0223 0.0067  0.0078  314 TRP A CA  
409  C C   . TRP A 50  ? 0.2562 0.2823 0.3623 -0.0217 0.0051  0.0128  314 TRP A C   
410  O O   . TRP A 50  ? 0.2306 0.2537 0.3310 -0.0198 0.0013  0.0157  314 TRP A O   
411  C CB  . TRP A 50  ? 0.2414 0.2668 0.3695 -0.0268 0.0118  0.0127  314 TRP A CB  
412  C CG  . TRP A 50  ? 0.2498 0.2685 0.3762 -0.0278 0.0114  0.0212  314 TRP A CG  
413  C CD1 . TRP A 50  ? 0.3052 0.3208 0.4256 -0.0252 0.0071  0.0252  314 TRP A CD1 
414  C CD2 . TRP A 50  ? 0.2713 0.2856 0.4035 -0.0315 0.0157  0.0271  314 TRP A CD2 
415  N NE1 . TRP A 50  ? 0.3363 0.3462 0.4588 -0.0268 0.0079  0.0334  314 TRP A NE1 
416  C CE2 . TRP A 50  ? 0.3383 0.3467 0.4675 -0.0305 0.0132  0.0349  314 TRP A CE2 
417  C CE3 . TRP A 50  ? 0.3317 0.3464 0.4715 -0.0357 0.0217  0.0268  314 TRP A CE3 
418  C CZ2 . TRP A 50  ? 0.3643 0.3665 0.4974 -0.0331 0.0161  0.0429  314 TRP A CZ2 
419  C CZ3 . TRP A 50  ? 0.3187 0.3267 0.4619 -0.0389 0.0252  0.0345  314 TRP A CZ3 
420  C CH2 . TRP A 50  ? 0.3160 0.3174 0.4554 -0.0373 0.0221  0.0428  314 TRP A CH2 
421  N N   . GLU A 51  ? 0.2237 0.2519 0.3238 -0.0235 0.0082  0.0132  315 GLU A N   
422  C CA  . GLU A 51  ? 0.2358 0.2624 0.3214 -0.0234 0.0069  0.0168  315 GLU A CA  
423  C C   . GLU A 51  ? 0.2513 0.2783 0.3308 -0.0193 0.0022  0.0126  315 GLU A C   
424  O O   . GLU A 51  ? 0.2197 0.2437 0.2897 -0.0188 -0.0008 0.0163  315 GLU A O   
425  C CB  . GLU A 51  ? 0.2590 0.2878 0.3394 -0.0262 0.0120  0.0166  315 GLU A CB  
426  C CG  . GLU A 51  ? 0.3897 0.4172 0.4548 -0.0256 0.0103  0.0178  315 GLU A CG  
427  C CD  . GLU A 51  ? 0.5174 0.5464 0.5751 -0.0285 0.0156  0.0177  315 GLU A CD  
428  O OE1 . GLU A 51  ? 0.3992 0.4307 0.4639 -0.0312 0.0212  0.0170  315 GLU A OE1 
429  O OE2 . GLU A 51  ? 0.5690 0.5967 0.6141 -0.0284 0.0145  0.0180  315 GLU A OE2 
430  N N   . MET A 52  ? 0.2186 0.2492 0.3029 -0.0165 0.0014  0.0051  316 MET A N   
431  C CA  . MET A 52  ? 0.2094 0.2394 0.2876 -0.0125 -0.0028 0.0016  316 MET A CA  
432  C C   . MET A 52  ? 0.2451 0.2718 0.3235 -0.0109 -0.0067 0.0033  316 MET A C   
433  O O   . MET A 52  ? 0.2250 0.2489 0.2947 -0.0094 -0.0095 0.0044  316 MET A O   
434  C CB  . MET A 52  ? 0.2699 0.3047 0.3543 -0.0094 -0.0033 -0.0063 316 MET A CB  
435  C CG  . MET A 52  ? 0.2902 0.3279 0.3717 -0.0096 -0.0001 -0.0086 316 MET A CG  
436  S SD  . MET A 52  ? 0.3314 0.3644 0.3965 -0.0085 -0.0013 -0.0068 316 MET A SD  
437  C CE  . MET A 52  ? 0.3483 0.3796 0.4112 -0.0027 -0.0069 -0.0113 316 MET A CE  
438  N N   . TRP A 53  ? 0.2270 0.2537 0.3156 -0.0115 -0.0063 0.0033  317 TRP A N   
439  C CA  . TRP A 53  ? 0.1986 0.2223 0.2883 -0.0102 -0.0091 0.0046  317 TRP A CA  
440  C C   . TRP A 53  ? 0.2281 0.2483 0.3115 -0.0117 -0.0097 0.0122  317 TRP A C   
441  O O   . TRP A 53  ? 0.2376 0.2560 0.3166 -0.0102 -0.0124 0.0129  317 TRP A O   
442  C CB  . TRP A 53  ? 0.1887 0.2128 0.2913 -0.0108 -0.0079 0.0026  317 TRP A CB  
443  C CG  . TRP A 53  ? 0.2231 0.2434 0.3292 -0.0107 -0.0088 0.0060  317 TRP A CG  
444  C CD1 . TRP A 53  ? 0.2367 0.2546 0.3511 -0.0129 -0.0065 0.0103  317 TRP A CD1 
445  C CD2 . TRP A 53  ? 0.2478 0.2663 0.3509 -0.0082 -0.0115 0.0048  317 TRP A CD2 
446  N NE1 . TRP A 53  ? 0.2381 0.2531 0.3552 -0.0115 -0.0080 0.0118  317 TRP A NE1 
447  C CE2 . TRP A 53  ? 0.2198 0.2355 0.3302 -0.0088 -0.0107 0.0083  317 TRP A CE2 
448  C CE3 . TRP A 53  ? 0.2664 0.2849 0.3613 -0.0054 -0.0142 0.0014  317 TRP A CE3 
449  C CZ2 . TRP A 53  ? 0.2438 0.2577 0.3543 -0.0069 -0.0122 0.0079  317 TRP A CZ2 
450  C CZ3 . TRP A 53  ? 0.2592 0.2754 0.3529 -0.0040 -0.0155 0.0017  317 TRP A CZ3 
451  C CH2 . TRP A 53  ? 0.2400 0.2543 0.3420 -0.0047 -0.0143 0.0044  317 TRP A CH2 
452  N N   . GLU A 54  ? 0.2002 0.2199 0.2832 -0.0149 -0.0073 0.0178  318 GLU A N   
453  C CA  . GLU A 54  ? 0.2312 0.2482 0.3080 -0.0162 -0.0090 0.0253  318 GLU A CA  
454  C C   . GLU A 54  ? 0.2268 0.2437 0.2912 -0.0155 -0.0114 0.0246  318 GLU A C   
455  O O   . GLU A 54  ? 0.2404 0.2560 0.3013 -0.0151 -0.0144 0.0276  318 GLU A O   
456  C CB  . GLU A 54  ? 0.2653 0.2813 0.3409 -0.0197 -0.0063 0.0318  318 GLU A CB  
457  C CG  . GLU A 54  ? 0.3497 0.3639 0.4372 -0.0209 -0.0038 0.0341  318 GLU A CG  
458  C CD  . GLU A 54  ? 0.5030 0.5154 0.5874 -0.0246 -0.0006 0.0411  318 GLU A CD  
459  O OE1 . GLU A 54  ? 0.5485 0.5573 0.6393 -0.0255 0.0001  0.0466  318 GLU A OE1 
460  O OE2 . GLU A 54  ? 0.5997 0.6136 0.6749 -0.0266 0.0014  0.0410  318 GLU A OE2 
461  N N   . ARG A 55  ? 0.2201 0.2386 0.2792 -0.0155 -0.0099 0.0206  319 ARG A N   
462  C CA  . ARG A 55  ? 0.2208 0.2383 0.2683 -0.0150 -0.0116 0.0195  319 ARG A CA  
463  C C   . ARG A 55  ? 0.2384 0.2544 0.2851 -0.0119 -0.0147 0.0162  319 ARG A C   
464  O O   . ARG A 55  ? 0.2504 0.2644 0.2902 -0.0122 -0.0171 0.0182  319 ARG A O   
465  C CB  . ARG A 55  ? 0.2610 0.2802 0.3045 -0.0150 -0.0088 0.0150  319 ARG A CB  
466  C CG  . ARG A 55  ? 0.2673 0.2872 0.3065 -0.0188 -0.0052 0.0186  319 ARG A CG  
467  C CD  . ARG A 55  ? 0.3169 0.3389 0.3535 -0.0184 -0.0016 0.0130  319 ARG A CD  
468  N NE  . ARG A 55  ? 0.4363 0.4588 0.4674 -0.0224 0.0025  0.0161  319 ARG A NE  
469  C CZ  . ARG A 55  ? 0.4616 0.4829 0.4806 -0.0241 0.0037  0.0161  319 ARG A CZ  
470  N NH1 . ARG A 55  ? 0.4286 0.4480 0.4409 -0.0220 0.0013  0.0125  319 ARG A NH1 
471  N NH2 . ARG A 55  ? 0.4681 0.4897 0.4816 -0.0280 0.0079  0.0193  319 ARG A NH2 
472  N N   . CYS A 56  ? 0.2208 0.2378 0.2742 -0.0092 -0.0147 0.0113  320 CYS A N   
473  C CA  . CYS A 56  ? 0.2420 0.2572 0.2930 -0.0062 -0.0172 0.0078  320 CYS A CA  
474  C C   . CYS A 56  ? 0.2269 0.2406 0.2813 -0.0062 -0.0186 0.0105  320 CYS A C   
475  O O   . CYS A 56  ? 0.2683 0.2797 0.3175 -0.0051 -0.0203 0.0101  320 CYS A O   
476  C CB  . CYS A 56  ? 0.2662 0.2834 0.3222 -0.0033 -0.0172 0.0016  320 CYS A CB  
477  S SG  . CYS A 56  ? 0.2731 0.2922 0.3249 -0.0022 -0.0158 -0.0022 320 CYS A SG  
478  N N   . ALA A 57  ? 0.2063 0.2211 0.2696 -0.0075 -0.0176 0.0135  321 ALA A N   
479  C CA  . ALA A 57  ? 0.2345 0.2482 0.3024 -0.0075 -0.0186 0.0165  321 ALA A CA  
480  C C   . ALA A 57  ? 0.2630 0.2760 0.3240 -0.0090 -0.0205 0.0212  321 ALA A C   
481  O O   . ALA A 57  ? 0.2609 0.2733 0.3218 -0.0083 -0.0218 0.0215  321 ALA A O   
482  C CB  . ALA A 57  ? 0.2315 0.2457 0.3104 -0.0086 -0.0170 0.0195  321 ALA A CB  
483  N N   . HIS A 58  ? 0.2435 0.2571 0.2987 -0.0113 -0.0205 0.0245  322 HIS A N   
484  C CA  . HIS A 58  ? 0.2572 0.2706 0.3050 -0.0132 -0.0228 0.0283  322 HIS A CA  
485  C C   . HIS A 58  ? 0.2368 0.2484 0.2767 -0.0123 -0.0238 0.0244  322 HIS A C   
486  O O   . HIS A 58  ? 0.2382 0.2496 0.2768 -0.0130 -0.0256 0.0259  322 HIS A O   
487  C CB  . HIS A 58  ? 0.3032 0.3172 0.3439 -0.0160 -0.0224 0.0315  322 HIS A CB  
488  C CG  . HIS A 58  ? 0.4618 0.4757 0.4927 -0.0182 -0.0250 0.0336  322 HIS A CG  
489  N ND1 . HIS A 58  ? 0.4823 0.4979 0.5143 -0.0197 -0.0281 0.0392  322 HIS A ND1 
490  C CD2 . HIS A 58  ? 0.5537 0.5661 0.5742 -0.0191 -0.0251 0.0304  322 HIS A CD2 
491  C CE1 . HIS A 58  ? 0.5130 0.5286 0.5354 -0.0219 -0.0303 0.0392  322 HIS A CE1 
492  N NE2 . HIS A 58  ? 0.5644 0.5776 0.5796 -0.0217 -0.0282 0.0338  322 HIS A NE2 
493  N N   . HIS A 59  ? 0.2433 0.2534 0.2783 -0.0109 -0.0225 0.0195  323 HIS A N   
494  C CA  . HIS A 59  ? 0.2302 0.2370 0.2572 -0.0099 -0.0233 0.0163  323 HIS A CA  
495  C C   . HIS A 59  ? 0.2419 0.2472 0.2720 -0.0080 -0.0238 0.0148  323 HIS A C   
496  O O   . HIS A 59  ? 0.2667 0.2694 0.2917 -0.0085 -0.0245 0.0148  323 HIS A O   
497  C CB  . HIS A 59  ? 0.2528 0.2583 0.2755 -0.0079 -0.0220 0.0115  323 HIS A CB  
498  C CG  . HIS A 59  ? 0.2921 0.2989 0.3111 -0.0100 -0.0205 0.0123  323 HIS A CG  
499  N ND1 . HIS A 59  ? 0.3793 0.3858 0.3917 -0.0134 -0.0211 0.0156  323 HIS A ND1 
500  C CD2 . HIS A 59  ? 0.2599 0.2688 0.2811 -0.0092 -0.0181 0.0098  323 HIS A CD2 
501  C CE1 . HIS A 59  ? 0.3571 0.3649 0.3665 -0.0148 -0.0188 0.0153  323 HIS A CE1 
502  N NE2 . HIS A 59  ? 0.2836 0.2929 0.2987 -0.0123 -0.0167 0.0117  323 HIS A NE2 
503  N N   . LEU A 60  ? 0.2255 0.2322 0.2637 -0.0060 -0.0229 0.0132  324 LEU A N   
504  C CA  . LEU A 60  ? 0.2002 0.2055 0.2409 -0.0043 -0.0228 0.0112  324 LEU A CA  
505  C C   . LEU A 60  ? 0.2216 0.2280 0.2661 -0.0061 -0.0231 0.0150  324 LEU A C   
506  O O   . LEU A 60  ? 0.2568 0.2612 0.2978 -0.0062 -0.0230 0.0143  324 LEU A O   
507  C CB  . LEU A 60  ? 0.2494 0.2564 0.2986 -0.0025 -0.0219 0.0084  324 LEU A CB  
508  C CG  . LEU A 60  ? 0.3523 0.3578 0.4032 -0.0008 -0.0213 0.0056  324 LEU A CG  
509  C CD1 . LEU A 60  ? 0.3735 0.3751 0.4134 0.0007  -0.0220 0.0031  324 LEU A CD1 
510  C CD2 . LEU A 60  ? 0.4347 0.4419 0.4935 0.0007  -0.0206 0.0018  324 LEU A CD2 
511  N N   . THR A 61  ? 0.2371 0.2466 0.2892 -0.0074 -0.0235 0.0191  325 THR A N   
512  C CA  . THR A 61  ? 0.2222 0.2337 0.2802 -0.0085 -0.0242 0.0226  325 THR A CA  
513  C C   . THR A 61  ? 0.2332 0.2447 0.2840 -0.0109 -0.0260 0.0246  325 THR A C   
514  O O   . THR A 61  ? 0.2547 0.2670 0.3081 -0.0115 -0.0260 0.0250  325 THR A O   
515  C CB  . THR A 61  ? 0.3151 0.3293 0.3830 -0.0089 -0.0247 0.0273  325 THR A CB  
516  O OG1 . THR A 61  ? 0.3910 0.4057 0.4545 -0.0107 -0.0258 0.0305  325 THR A OG1 
517  C CG2 . THR A 61  ? 0.2551 0.2687 0.3316 -0.0069 -0.0225 0.0249  325 THR A CG2 
518  N N   . GLU A 62  ? 0.2327 0.2433 0.2746 -0.0126 -0.0271 0.0250  326 GLU A N   
519  C CA  . GLU A 62  ? 0.2223 0.2323 0.2566 -0.0153 -0.0288 0.0259  326 GLU A CA  
520  C C   . GLU A 62  ? 0.2296 0.2353 0.2588 -0.0146 -0.0273 0.0220  326 GLU A C   
521  O O   . GLU A 62  ? 0.2489 0.2548 0.2779 -0.0166 -0.0278 0.0225  326 GLU A O   
522  C CB  . GLU A 62  ? 0.2666 0.2756 0.2918 -0.0170 -0.0294 0.0260  326 GLU A CB  
523  C CG  . GLU A 62  ? 0.3643 0.3718 0.3805 -0.0201 -0.0310 0.0257  326 GLU A CG  
524  C CD  . GLU A 62  ? 0.6304 0.6398 0.6407 -0.0229 -0.0326 0.0281  326 GLU A CD  
525  O OE1 . GLU A 62  ? 0.7546 0.7655 0.7669 -0.0221 -0.0319 0.0300  326 GLU A OE1 
526  O OE2 . GLU A 62  ? 0.6995 0.7085 0.7028 -0.0260 -0.0344 0.0279  326 GLU A OE2 
527  N N   . ALA A 63  ? 0.2123 0.2141 0.2372 -0.0120 -0.0257 0.0181  327 ALA A N   
528  C CA  . ALA A 63  ? 0.2440 0.2407 0.2627 -0.0110 -0.0244 0.0151  327 ALA A CA  
529  C C   . ALA A 63  ? 0.2496 0.2471 0.2742 -0.0109 -0.0230 0.0153  327 ALA A C   
530  O O   . ALA A 63  ? 0.2651 0.2598 0.2858 -0.0124 -0.0219 0.0149  327 ALA A O   
531  C CB  . ALA A 63  ? 0.2488 0.2419 0.2628 -0.0074 -0.0237 0.0113  327 ALA A CB  
532  N N   . ILE A 64  ? 0.2551 0.2563 0.2894 -0.0094 -0.0224 0.0156  328 ILE A N   
533  C CA  . ILE A 64  ? 0.2156 0.2178 0.2562 -0.0090 -0.0203 0.0151  328 ILE A CA  
534  C C   . ILE A 64  ? 0.2476 0.2536 0.2936 -0.0121 -0.0208 0.0183  328 ILE A C   
535  O O   . ILE A 64  ? 0.2459 0.2514 0.2930 -0.0131 -0.0186 0.0175  328 ILE A O   
536  C CB  . ILE A 64  ? 0.1951 0.2001 0.2457 -0.0068 -0.0194 0.0143  328 ILE A CB  
537  C CG1 . ILE A 64  ? 0.2503 0.2520 0.2957 -0.0040 -0.0188 0.0099  328 ILE A CG1 
538  C CG2 . ILE A 64  ? 0.2592 0.2666 0.3193 -0.0069 -0.0171 0.0144  328 ILE A CG2 
539  C CD1 . ILE A 64  ? 0.3202 0.3178 0.3592 -0.0029 -0.0167 0.0065  328 ILE A CD1 
540  N N   . GLN A 65  ? 0.2133 0.2232 0.2624 -0.0138 -0.0238 0.0220  329 GLN A N   
541  C CA  . GLN A 65  ? 0.2183 0.2330 0.2731 -0.0168 -0.0256 0.0252  329 GLN A CA  
542  C C   . GLN A 65  ? 0.2152 0.2270 0.2625 -0.0197 -0.0249 0.0235  329 GLN A C   
543  O O   . GLN A 65  ? 0.2344 0.2495 0.2880 -0.0216 -0.0241 0.0240  329 GLN A O   
544  C CB  . GLN A 65  ? 0.2568 0.2751 0.3119 -0.0181 -0.0296 0.0293  329 GLN A CB  
545  C CG  . GLN A 65  ? 0.4771 0.5013 0.5377 -0.0208 -0.0332 0.0331  329 GLN A CG  
546  C CD  . GLN A 65  ? 0.6149 0.6416 0.6752 -0.0211 -0.0367 0.0375  329 GLN A CD  
547  O OE1 . GLN A 65  ? 0.5737 0.5975 0.6308 -0.0193 -0.0355 0.0373  329 GLN A OE1 
548  N NE2 . GLN A 65  ? 0.6627 0.6949 0.7263 -0.0232 -0.0410 0.0416  329 GLN A NE2 
549  N N   . TYR A 66  ? 0.2312 0.2371 0.2661 -0.0201 -0.0249 0.0216  330 TYR A N   
550  C CA  . TYR A 66  ? 0.2325 0.2342 0.2600 -0.0229 -0.0239 0.0201  330 TYR A CA  
551  C C   . TYR A 66  ? 0.2545 0.2522 0.2812 -0.0219 -0.0197 0.0178  330 TYR A C   
552  O O   . TYR A 66  ? 0.2616 0.2584 0.2883 -0.0249 -0.0179 0.0176  330 TYR A O   
553  C CB  . TYR A 66  ? 0.2981 0.2937 0.3131 -0.0230 -0.0247 0.0184  330 TYR A CB  
554  C CG  . TYR A 66  ? 0.2876 0.2866 0.3009 -0.0257 -0.0282 0.0201  330 TYR A CG  
555  C CD1 . TYR A 66  ? 0.3291 0.3314 0.3440 -0.0242 -0.0300 0.0218  330 TYR A CD1 
556  C CD2 . TYR A 66  ? 0.2807 0.2793 0.2903 -0.0301 -0.0296 0.0199  330 TYR A CD2 
557  C CE1 . TYR A 66  ? 0.3962 0.4013 0.4078 -0.0269 -0.0329 0.0236  330 TYR A CE1 
558  C CE2 . TYR A 66  ? 0.3470 0.3487 0.3536 -0.0328 -0.0330 0.0211  330 TYR A CE2 
559  C CZ  . TYR A 66  ? 0.4027 0.4074 0.4095 -0.0311 -0.0346 0.0231  330 TYR A CZ  
560  O OH  . TYR A 66  ? 0.4441 0.4517 0.4464 -0.0340 -0.0377 0.0245  330 TYR A OH  
561  N N   . VAL A 67  ? 0.2702 0.2653 0.2955 -0.0181 -0.0179 0.0161  331 VAL A N   
562  C CA  . VAL A 67  ? 0.2574 0.2481 0.2797 -0.0170 -0.0139 0.0139  331 VAL A CA  
563  C C   . VAL A 67  ? 0.2307 0.2271 0.2647 -0.0185 -0.0114 0.0145  331 VAL A C   
564  O O   . VAL A 67  ? 0.2300 0.2239 0.2622 -0.0203 -0.0076 0.0136  331 VAL A O   
565  C CB  . VAL A 67  ? 0.2327 0.2204 0.2510 -0.0126 -0.0134 0.0115  331 VAL A CB  
566  C CG1 . VAL A 67  ? 0.2637 0.2479 0.2791 -0.0116 -0.0094 0.0093  331 VAL A CG1 
567  C CG2 . VAL A 67  ? 0.2429 0.2242 0.2493 -0.0111 -0.0153 0.0105  331 VAL A CG2 
568  N N   . VAL A 68  ? 0.2413 0.2452 0.2878 -0.0176 -0.0131 0.0162  332 VAL A N   
569  C CA  . VAL A 68  ? 0.1984 0.2086 0.2584 -0.0185 -0.0109 0.0167  332 VAL A CA  
570  C C   . VAL A 68  ? 0.2361 0.2494 0.2992 -0.0228 -0.0112 0.0182  332 VAL A C   
571  O O   . VAL A 68  ? 0.2242 0.2394 0.2930 -0.0245 -0.0074 0.0172  332 VAL A O   
572  C CB  . VAL A 68  ? 0.1951 0.2116 0.2678 -0.0163 -0.0134 0.0189  332 VAL A CB  
573  C CG1 . VAL A 68  ? 0.2495 0.2733 0.3379 -0.0170 -0.0120 0.0200  332 VAL A CG1 
574  C CG2 . VAL A 68  ? 0.2332 0.2466 0.3049 -0.0126 -0.0118 0.0164  332 VAL A CG2 
575  N N   . GLU A 69  ? 0.2316 0.2457 0.2910 -0.0251 -0.0156 0.0202  333 GLU A N   
576  C CA  . GLU A 69  ? 0.2027 0.2203 0.2651 -0.0298 -0.0166 0.0210  333 GLU A CA  
577  C C   . GLU A 69  ? 0.1982 0.2080 0.2506 -0.0324 -0.0122 0.0185  333 GLU A C   
578  O O   . GLU A 69  ? 0.2476 0.2600 0.3057 -0.0360 -0.0097 0.0180  333 GLU A O   
579  C CB  . GLU A 69  ? 0.2325 0.2522 0.2916 -0.0318 -0.0224 0.0232  333 GLU A CB  
580  C CG  . GLU A 69  ? 0.2265 0.2505 0.2889 -0.0372 -0.0243 0.0234  333 GLU A CG  
581  C CD  . GLU A 69  ? 0.2631 0.2981 0.3430 -0.0379 -0.0256 0.0254  333 GLU A CD  
582  O OE1 . GLU A 69  ? 0.2862 0.3257 0.3755 -0.0341 -0.0265 0.0274  333 GLU A OE1 
583  O OE2 . GLU A 69  ? 0.2638 0.3028 0.3488 -0.0424 -0.0256 0.0246  333 GLU A OE2 
584  N N   . PHE A 70  ? 0.2291 0.2292 0.2672 -0.0305 -0.0111 0.0169  334 PHE A N   
585  C CA  . PHE A 70  ? 0.2401 0.2312 0.2677 -0.0323 -0.0068 0.0152  334 PHE A CA  
586  C C   . PHE A 70  ? 0.2552 0.2472 0.2879 -0.0325 -0.0009 0.0142  334 PHE A C   
587  O O   . PHE A 70  ? 0.2871 0.2772 0.3196 -0.0365 0.0030  0.0138  334 PHE A O   
588  C CB  . PHE A 70  ? 0.2278 0.2093 0.2410 -0.0286 -0.0069 0.0141  334 PHE A CB  
589  C CG  . PHE A 70  ? 0.2799 0.2511 0.2816 -0.0290 -0.0025 0.0131  334 PHE A CG  
590  C CD1 . PHE A 70  ? 0.2690 0.2344 0.2651 -0.0333 -0.0011 0.0133  334 PHE A CD1 
591  C CD2 . PHE A 70  ? 0.2986 0.2654 0.2942 -0.0251 0.0000  0.0120  334 PHE A CD2 
592  C CE1 . PHE A 70  ? 0.3251 0.2795 0.3097 -0.0337 0.0033  0.0131  334 PHE A CE1 
593  C CE2 . PHE A 70  ? 0.3202 0.2765 0.3031 -0.0253 0.0038  0.0118  334 PHE A CE2 
594  C CZ  . PHE A 70  ? 0.3041 0.2537 0.2814 -0.0295 0.0056  0.0127  334 PHE A CZ  
595  N N   . ALA A 71  ? 0.2327 0.2273 0.2700 -0.0285 0.0001  0.0135  335 ALA A N   
596  C CA  . ALA A 71  ? 0.2426 0.2380 0.2843 -0.0283 0.0061  0.0118  335 ALA A CA  
597  C C   . ALA A 71  ? 0.2347 0.2392 0.2920 -0.0321 0.0079  0.0123  335 ALA A C   
598  O O   . ALA A 71  ? 0.2649 0.2683 0.3230 -0.0350 0.0137  0.0112  335 ALA A O   
599  C CB  . ALA A 71  ? 0.2885 0.2860 0.3340 -0.0235 0.0063  0.0103  335 ALA A CB  
600  N N   . LYS A 72  ? 0.2214 0.2350 0.2912 -0.0321 0.0029  0.0143  336 LYS A N   
601  C CA  . LYS A 72  ? 0.2422 0.2661 0.3292 -0.0350 0.0036  0.0149  336 LYS A CA  
602  C C   . LYS A 72  ? 0.2990 0.3225 0.3845 -0.0410 0.0045  0.0148  336 LYS A C   
603  O O   . LYS A 72  ? 0.2671 0.2983 0.3662 -0.0441 0.0071  0.0143  336 LYS A O   
604  C CB  . LYS A 72  ? 0.2356 0.2687 0.3350 -0.0334 -0.0030 0.0178  336 LYS A CB  
605  C CG  . LYS A 72  ? 0.2136 0.2489 0.3205 -0.0281 -0.0026 0.0178  336 LYS A CG  
606  C CD  . LYS A 72  ? 0.2529 0.2949 0.3687 -0.0264 -0.0096 0.0217  336 LYS A CD  
607  C CE  . LYS A 72  ? 0.2983 0.3414 0.4225 -0.0215 -0.0088 0.0218  336 LYS A CE  
608  N NZ  . LYS A 72  ? 0.3293 0.3768 0.4593 -0.0198 -0.0156 0.0264  336 LYS A NZ  
609  N N   . ARG A 73  ? 0.2703 0.2854 0.3408 -0.0427 0.0025  0.0150  337 ARG A N   
610  C CA  . ARG A 73  ? 0.2804 0.2933 0.3482 -0.0487 0.0035  0.0145  337 ARG A CA  
611  C C   . ARG A 73  ? 0.3149 0.3177 0.3725 -0.0504 0.0111  0.0129  337 ARG A C   
612  O O   . ARG A 73  ? 0.4034 0.4042 0.4610 -0.0559 0.0144  0.0122  337 ARG A O   
613  C CB  . ARG A 73  ? 0.2636 0.2720 0.3209 -0.0499 -0.0023 0.0152  337 ARG A CB  
614  C CG  . ARG A 73  ? 0.3119 0.3305 0.3786 -0.0494 -0.0096 0.0171  337 ARG A CG  
615  C CD  . ARG A 73  ? 0.3383 0.3539 0.3953 -0.0510 -0.0150 0.0173  337 ARG A CD  
616  N NE  . ARG A 73  ? 0.5041 0.5318 0.5736 -0.0531 -0.0207 0.0190  337 ARG A NE  
617  C CZ  . ARG A 73  ? 0.6357 0.6660 0.7021 -0.0556 -0.0268 0.0196  337 ARG A CZ  
618  N NH1 . ARG A 73  ? 0.6662 0.6874 0.7171 -0.0562 -0.0277 0.0182  337 ARG A NH1 
619  N NH2 . ARG A 73  ? 0.4969 0.5393 0.5761 -0.0574 -0.0321 0.0214  337 ARG A NH2 
620  N N   . LEU A 74  ? 0.3409 0.4439 0.4829 -0.0289 -0.0170 0.0127  338 LEU A N   
621  C CA  . LEU A 74  ? 0.3743 0.4624 0.5169 -0.0377 -0.0018 0.0187  338 LEU A CA  
622  C C   . LEU A 74  ? 0.3498 0.4508 0.5209 -0.0423 0.0103  0.0175  338 LEU A C   
623  O O   . LEU A 74  ? 0.3476 0.4601 0.5230 -0.0356 0.0119  0.0188  338 LEU A O   
624  C CB  . LEU A 74  ? 0.4177 0.4869 0.5283 -0.0328 0.0035  0.0296  338 LEU A CB  
625  C CG  . LEU A 74  ? 0.5118 0.5620 0.6103 -0.0368 0.0152  0.0373  338 LEU A CG  
626  C CD1 . LEU A 74  ? 0.5222 0.5622 0.6192 -0.0408 0.0113  0.0349  338 LEU A CD1 
627  C CD2 . LEU A 74  ? 0.5442 0.5849 0.6139 -0.0297 0.0156  0.0442  338 LEU A CD2 
628  N N   . SER A 75  ? 0.3388 0.4370 0.5314 -0.0539 0.0208  0.0145  339 SER A N   
629  C CA  . SER A 75  ? 0.3291 0.4385 0.5526 -0.0604 0.0366  0.0132  339 SER A CA  
630  C C   . SER A 75  ? 0.4191 0.5187 0.6226 -0.0536 0.0504  0.0255  339 SER A C   
631  O O   . SER A 75  ? 0.4964 0.5714 0.6680 -0.0514 0.0583  0.0364  339 SER A O   
632  C CB  . SER A 75  ? 0.3450 0.4412 0.5865 -0.0747 0.0516  0.0116  339 SER A CB  
633  O OG  . SER A 75  ? 0.4370 0.5440 0.7128 -0.0828 0.0703  0.0097  339 SER A OG  
634  N N   . GLY A 76  ? 0.2626 0.3824 0.4834 -0.0485 0.0521  0.0228  340 GLY A N   
635  C CA  . GLY A 76  ? 0.2675 0.3788 0.4723 -0.0425 0.0670  0.0320  340 GLY A CA  
636  C C   . GLY A 76  ? 0.3043 0.4120 0.4805 -0.0297 0.0576  0.0351  340 GLY A C   
637  O O   . GLY A 76  ? 0.3040 0.4107 0.4741 -0.0237 0.0675  0.0385  340 GLY A O   
638  N N   . PHE A 77  ? 0.2841 0.3883 0.4435 -0.0258 0.0401  0.0334  341 PHE A N   
639  C CA  . PHE A 77  ? 0.2292 0.3257 0.3622 -0.0155 0.0338  0.0362  341 PHE A CA  
640  C C   . PHE A 77  ? 0.2338 0.3475 0.3823 -0.0055 0.0308  0.0327  341 PHE A C   
641  O O   . PHE A 77  ? 0.2257 0.3310 0.3589 0.0020  0.0367  0.0359  341 PHE A O   
642  C CB  . PHE A 77  ? 0.2209 0.3081 0.3338 -0.0145 0.0192  0.0357  341 PHE A CB  
643  C CG  . PHE A 77  ? 0.2394 0.3147 0.3263 -0.0067 0.0161  0.0383  341 PHE A CG  
644  C CD1 . PHE A 77  ? 0.2483 0.3065 0.3104 -0.0082 0.0215  0.0420  341 PHE A CD1 
645  C CD2 . PHE A 77  ? 0.2417 0.3222 0.3285 0.0024  0.0077  0.0364  341 PHE A CD2 
646  C CE1 . PHE A 77  ? 0.2337 0.2811 0.2762 -0.0035 0.0195  0.0416  341 PHE A CE1 
647  C CE2 . PHE A 77  ? 0.2823 0.3474 0.3462 0.0085  0.0082  0.0390  341 PHE A CE2 
648  C CZ  . PHE A 77  ? 0.2269 0.2757 0.2710 0.0038  0.0145  0.0405  341 PHE A CZ  
649  N N   . MET A 78  ? 0.2503 0.3882 0.4288 -0.0043 0.0209  0.0251  342 MET A N   
650  C CA  . MET A 78  ? 0.2767 0.4338 0.4707 0.0086  0.0158  0.0219  342 MET A CA  
651  C C   . MET A 78  ? 0.2895 0.4581 0.5067 0.0093  0.0324  0.0220  342 MET A C   
652  O O   . MET A 78  ? 0.3333 0.5152 0.5615 0.0221  0.0315  0.0208  342 MET A O   
653  C CB  . MET A 78  ? 0.3076 0.4911 0.5263 0.0114  -0.0021 0.0120  342 MET A CB  
654  C CG  . MET A 78  ? 0.3373 0.5090 0.5291 0.0148  -0.0174 0.0123  342 MET A CG  
655  S SD  . MET A 78  ? 0.3833 0.5281 0.5318 0.0294  -0.0173 0.0229  342 MET A SD  
656  C CE  . MET A 78  ? 0.4515 0.6113 0.5967 0.0465  -0.0387 0.0186  342 MET A CE  
657  N N   . GLU A 79  ? 0.2855 0.4468 0.5078 -0.0025 0.0493  0.0244  343 GLU A N   
658  C CA  . GLU A 79  ? 0.3452 0.5126 0.5837 -0.0013 0.0693  0.0259  343 GLU A CA  
659  C C   . GLU A 79  ? 0.2935 0.4373 0.4954 0.0075  0.0784  0.0329  343 GLU A C   
660  O O   . GLU A 79  ? 0.3674 0.5164 0.5783 0.0141  0.0919  0.0331  343 GLU A O   
661  C CB  . GLU A 79  ? 0.5000 0.6629 0.7519 -0.0159 0.0877  0.0275  343 GLU A CB  
662  C CG  . GLU A 79  ? 0.6443 0.8334 0.9439 -0.0269 0.0843  0.0172  343 GLU A CG  
663  C CD  . GLU A 79  ? 0.7772 0.9498 1.0803 -0.0427 0.1021  0.0207  343 GLU A CD  
664  O OE1 . GLU A 79  ? 0.8088 0.9548 1.0822 -0.0427 0.1206  0.0320  343 GLU A OE1 
665  O OE2 . GLU A 79  ? 0.8205 1.0048 1.1540 -0.0543 0.0976  0.0118  343 GLU A OE2 
666  N N   . LEU A 80  ? 0.2624 0.3813 0.4250 0.0072  0.0714  0.0370  344 LEU A N   
667  C CA  . LEU A 80  ? 0.2688 0.3663 0.3987 0.0137  0.0785  0.0401  344 LEU A CA  
668  C C   . LEU A 80  ? 0.3126 0.4135 0.4445 0.0270  0.0731  0.0381  344 LEU A C   
669  O O   . LEU A 80  ? 0.2828 0.3946 0.4249 0.0323  0.0582  0.0364  344 LEU A O   
670  C CB  . LEU A 80  ? 0.2521 0.3268 0.3461 0.0092  0.0714  0.0425  344 LEU A CB  
671  C CG  . LEU A 80  ? 0.3199 0.3883 0.4072 -0.0008 0.0744  0.0461  344 LEU A CG  
672  C CD1 . LEU A 80  ? 0.3181 0.3691 0.3735 -0.0026 0.0646  0.0472  344 LEU A CD1 
673  C CD2 . LEU A 80  ? 0.3952 0.4571 0.4774 -0.0019 0.0947  0.0500  344 LEU A CD2 
674  N N   . CYS A 81  ? 0.3256 0.4127 0.4418 0.0338  0.0852  0.0385  345 CYS A N   
675  C CA  . CYS A 81  ? 0.3347 0.4178 0.4486 0.0477  0.0828  0.0376  345 CYS A CA  
676  C C   . CYS A 81  ? 0.3634 0.4273 0.4516 0.0482  0.0705  0.0387  345 CYS A C   
677  O O   . CYS A 81  ? 0.3161 0.3670 0.3841 0.0378  0.0666  0.0387  345 CYS A O   
678  C CB  . CYS A 81  ? 0.3744 0.4429 0.4757 0.0540  0.1005  0.0363  345 CYS A CB  
679  S SG  . CYS A 81  ? 0.4284 0.4623 0.4825 0.0458  0.1051  0.0338  345 CYS A SG  
680  N N   . GLN A 82  ? 0.3560 0.4179 0.4453 0.0615  0.0654  0.0401  346 GLN A N   
681  C CA  . GLN A 82  ? 0.3345 0.3780 0.4016 0.0622  0.0563  0.0424  346 GLN A CA  
682  C C   . GLN A 82  ? 0.3393 0.3543 0.3779 0.0531  0.0638  0.0399  346 GLN A C   
683  O O   . GLN A 82  ? 0.3086 0.3146 0.3338 0.0449  0.0570  0.0397  346 GLN A O   
684  C CB  . GLN A 82  ? 0.4279 0.4670 0.4946 0.0810  0.0540  0.0463  346 GLN A CB  
685  C CG  . GLN A 82  ? 0.7034 0.7736 0.7950 0.0905  0.0397  0.0468  346 GLN A CG  
686  C CD  . GLN A 82  ? 0.8786 0.9464 0.9571 0.0895  0.0248  0.0489  346 GLN A CD  
687  O OE1 . GLN A 82  ? 0.9559 0.9954 1.0064 0.0878  0.0276  0.0525  346 GLN A OE1 
688  N NE2 . GLN A 82  ? 0.8880 0.9854 0.9877 0.0901  0.0100  0.0453  346 GLN A NE2 
689  N N   . ASN A 83  ? 0.3692 0.3721 0.4000 0.0543  0.0776  0.0363  347 ASN A N   
690  C CA  . ASN A 83  ? 0.3877 0.3664 0.3928 0.0453  0.0829  0.0302  347 ASN A CA  
691  C C   . ASN A 83  ? 0.3323 0.3174 0.3299 0.0314  0.0754  0.0283  347 ASN A C   
692  O O   . ASN A 83  ? 0.3636 0.3374 0.3470 0.0234  0.0707  0.0243  347 ASN A O   
693  C CB  . ASN A 83  ? 0.4420 0.4092 0.4385 0.0486  0.0982  0.0244  347 ASN A CB  
694  C CG  . ASN A 83  ? 0.5829 0.5308 0.5541 0.0381  0.1010  0.0145  347 ASN A CG  
695  O OD1 . ASN A 83  ? 0.5737 0.5280 0.5350 0.0307  0.0995  0.0113  347 ASN A OD1 
696  N ND2 . ASN A 83  ? 0.6542 0.5783 0.6147 0.0379  0.1050  0.0090  347 ASN A ND2 
697  N N   . ASP A 84  ? 0.3315 0.3341 0.3402 0.0291  0.0760  0.0309  348 ASP A N   
698  C CA  . ASP A 84  ? 0.3283 0.3340 0.3275 0.0192  0.0715  0.0309  348 ASP A CA  
699  C C   . ASP A 84  ? 0.3264 0.3392 0.3322 0.0142  0.0575  0.0340  348 ASP A C   
700  O O   . ASP A 84  ? 0.3038 0.3118 0.2962 0.0074  0.0515  0.0322  348 ASP A O   
701  C CB  . ASP A 84  ? 0.2866 0.3032 0.2942 0.0190  0.0809  0.0343  348 ASP A CB  
702  C CG  . ASP A 84  ? 0.3815 0.3864 0.3701 0.0222  0.0951  0.0304  348 ASP A CG  
703  O OD1 . ASP A 84  ? 0.4042 0.3937 0.3764 0.0245  0.0968  0.0234  348 ASP A OD1 
704  O OD2 . ASP A 84  ? 0.4202 0.4297 0.4100 0.0223  0.1062  0.0340  348 ASP A OD2 
705  N N   . GLN A 85  ? 0.2529 0.2777 0.2784 0.0189  0.0516  0.0374  349 GLN A N   
706  C CA  . GLN A 85  ? 0.2697 0.2979 0.2970 0.0159  0.0389  0.0390  349 GLN A CA  
707  C C   . GLN A 85  ? 0.2306 0.2409 0.2391 0.0140  0.0369  0.0369  349 GLN A C   
708  O O   . GLN A 85  ? 0.2805 0.2900 0.2834 0.0072  0.0302  0.0363  349 GLN A O   
709  C CB  . GLN A 85  ? 0.2724 0.3147 0.3182 0.0245  0.0320  0.0410  349 GLN A CB  
710  C CG  . GLN A 85  ? 0.2582 0.3239 0.3320 0.0246  0.0333  0.0402  349 GLN A CG  
711  C CD  . GLN A 85  ? 0.3314 0.4157 0.4249 0.0350  0.0234  0.0392  349 GLN A CD  
712  O OE1 . GLN A 85  ? 0.3040 0.3829 0.3859 0.0408  0.0135  0.0405  349 GLN A OE1 
713  N NE2 . GLN A 85  ? 0.3163 0.4235 0.4393 0.0390  0.0265  0.0366  349 GLN A NE2 
714  N N   . ILE A 86  ? 0.2641 0.2599 0.2655 0.0202  0.0442  0.0357  350 ILE A N   
715  C CA  . ILE A 86  ? 0.2931 0.2688 0.2800 0.0171  0.0465  0.0327  350 ILE A CA  
716  C C   . ILE A 86  ? 0.2831 0.2551 0.2599 0.0055  0.0471  0.0244  350 ILE A C   
717  O O   . ILE A 86  ? 0.3155 0.2849 0.2891 -0.0014 0.0430  0.0215  350 ILE A O   
718  C CB  . ILE A 86  ? 0.3180 0.2745 0.2996 0.0266  0.0571  0.0333  350 ILE A CB  
719  C CG1 . ILE A 86  ? 0.3512 0.3130 0.3391 0.0403  0.0524  0.0421  350 ILE A CG1 
720  C CG2 . ILE A 86  ? 0.3332 0.2653 0.3020 0.0194  0.0643  0.0278  350 ILE A CG2 
721  C CD1 . ILE A 86  ? 0.3383 0.2834 0.3221 0.0550  0.0624  0.0455  350 ILE A CD1 
722  N N   . VAL A 87  ? 0.3106 0.2845 0.2826 0.0049  0.0519  0.0204  351 VAL A N   
723  C CA  . VAL A 87  ? 0.3132 0.2865 0.2724 -0.0029 0.0498  0.0117  351 VAL A CA  
724  C C   . VAL A 87  ? 0.2975 0.2843 0.2585 -0.0075 0.0387  0.0147  351 VAL A C   
725  O O   . VAL A 87  ? 0.3119 0.2995 0.2690 -0.0137 0.0328  0.0081  351 VAL A O   
726  C CB  . VAL A 87  ? 0.3559 0.3286 0.3046 0.0001  0.0569  0.0086  351 VAL A CB  
727  C CG1 . VAL A 87  ? 0.3386 0.3149 0.2699 -0.0046 0.0511  0.0011  351 VAL A CG1 
728  C CG2 . VAL A 87  ? 0.3956 0.3514 0.3405 0.0044  0.0688  0.0028  351 VAL A CG2 
729  N N   . LEU A 88  ? 0.2761 0.2739 0.2458 -0.0047 0.0364  0.0235  352 LEU A N   
730  C CA  . LEU A 88  ? 0.2622 0.2687 0.2323 -0.0082 0.0279  0.0265  352 LEU A CA  
731  C C   . LEU A 88  ? 0.2701 0.2770 0.2461 -0.0113 0.0207  0.0261  352 LEU A C   
732  O O   . LEU A 88  ? 0.2723 0.2831 0.2448 -0.0148 0.0144  0.0235  352 LEU A O   
733  C CB  . LEU A 88  ? 0.2679 0.2828 0.2488 -0.0063 0.0298  0.0347  352 LEU A CB  
734  C CG  . LEU A 88  ? 0.2705 0.2840 0.2443 -0.0037 0.0402  0.0366  352 LEU A CG  
735  C CD1 . LEU A 88  ? 0.2772 0.2989 0.2688 -0.0045 0.0447  0.0437  352 LEU A CD1 
736  C CD2 . LEU A 88  ? 0.3052 0.3136 0.2546 -0.0033 0.0390  0.0346  352 LEU A CD2 
737  N N   . LEU A 89  ? 0.2711 0.2744 0.2549 -0.0084 0.0218  0.0288  353 LEU A N   
738  C CA  . LEU A 89  ? 0.2765 0.2774 0.2617 -0.0103 0.0174  0.0291  353 LEU A CA  
739  C C   . LEU A 89  ? 0.2904 0.2815 0.2705 -0.0160 0.0212  0.0215  353 LEU A C   
740  O O   . LEU A 89  ? 0.3077 0.3011 0.2903 -0.0204 0.0182  0.0193  353 LEU A O   
741  C CB  . LEU A 89  ? 0.3344 0.3328 0.3236 -0.0029 0.0173  0.0347  353 LEU A CB  
742  C CG  . LEU A 89  ? 0.3090 0.3219 0.3085 -0.0012 0.0094  0.0382  353 LEU A CG  
743  C CD1 . LEU A 89  ? 0.3052 0.3205 0.3090 0.0084  0.0070  0.0413  353 LEU A CD1 
744  C CD2 . LEU A 89  ? 0.3191 0.3345 0.3176 -0.0055 0.0028  0.0378  353 LEU A CD2 
745  N N   . LYS A 90  ? 0.3054 0.2853 0.2810 -0.0162 0.0294  0.0164  354 LYS A N   
746  C CA  . LYS A 90  ? 0.3414 0.3115 0.3167 -0.0239 0.0348  0.0066  354 LYS A CA  
747  C C   . LYS A 90  ? 0.4095 0.3951 0.3864 -0.0308 0.0261  -0.0025 354 LYS A C   
748  O O   . LYS A 90  ? 0.3773 0.3662 0.3622 -0.0379 0.0253  -0.0096 354 LYS A O   
749  C CB  . LYS A 90  ? 0.4130 0.3662 0.3828 -0.0230 0.0457  0.0012  354 LYS A CB  
750  C CG  . LYS A 90  ? 0.6603 0.5979 0.6331 -0.0321 0.0550  -0.0094 354 LYS A CG  
751  C CD  . LYS A 90  ? 0.7853 0.6973 0.7520 -0.0280 0.0695  -0.0100 354 LYS A CD  
752  C CE  . LYS A 90  ? 0.8116 0.7247 0.7717 -0.0280 0.0701  -0.0196 354 LYS A CE  
753  N NZ  . LYS A 90  ? 0.8499 0.7350 0.8053 -0.0265 0.0860  -0.0246 354 LYS A NZ  
754  N N   . ALA A 91  ? 0.3679 0.3634 0.3374 -0.0272 0.0204  -0.0015 355 ALA A N   
755  C CA  . ALA A 91  ? 0.3657 0.3752 0.3306 -0.0290 0.0111  -0.0089 355 ALA A CA  
756  C C   . ALA A 91  ? 0.3911 0.4134 0.3616 -0.0275 0.0021  -0.0028 355 ALA A C   
757  O O   . ALA A 91  ? 0.3888 0.4240 0.3616 -0.0290 -0.0060 -0.0101 355 ALA A O   
758  C CB  . ALA A 91  ? 0.3563 0.3664 0.3052 -0.0233 0.0113  -0.0079 355 ALA A CB  
759  N N   . GLY A 92  ? 0.3124 0.3321 0.2862 -0.0238 0.0031  0.0092  356 GLY A N   
760  C CA  . GLY A 92  ? 0.3337 0.3614 0.3103 -0.0213 -0.0036 0.0154  356 GLY A CA  
761  C C   . GLY A 92  ? 0.2924 0.3191 0.2790 -0.0224 -0.0042 0.0191  356 GLY A C   
762  O O   . GLY A 92  ? 0.2802 0.3127 0.2693 -0.0208 -0.0094 0.0218  356 GLY A O   
763  N N   . ALA A 93  ? 0.2970 0.3145 0.2863 -0.0235 0.0018  0.0198  357 ALA A N   
764  C CA  . ALA A 93  ? 0.2839 0.2988 0.2764 -0.0220 0.0014  0.0243  357 ALA A CA  
765  C C   . ALA A 93  ? 0.2727 0.2927 0.2712 -0.0256 0.0006  0.0197  357 ALA A C   
766  O O   . ALA A 93  ? 0.2781 0.3012 0.2782 -0.0234 -0.0030 0.0227  357 ALA A O   
767  C CB  . ALA A 93  ? 0.3363 0.3385 0.3250 -0.0190 0.0082  0.0273  357 ALA A CB  
768  N N   . MET A 94  ? 0.3082 0.3296 0.3122 -0.0316 0.0046  0.0110  358 MET A N   
769  C CA  . MET A 94  ? 0.2572 0.2880 0.2733 -0.0357 0.0047  0.0047  358 MET A CA  
770  C C   . MET A 94  ? 0.2934 0.3412 0.3124 -0.0316 -0.0067 0.0042  358 MET A C   
771  O O   . MET A 94  ? 0.2746 0.3300 0.3016 -0.0300 -0.0085 0.0041  358 MET A O   
772  C CB  . MET A 94  ? 0.3386 0.3710 0.3657 -0.0448 0.0110  -0.0078 358 MET A CB  
773  C CG  . MET A 94  ? 0.3310 0.3718 0.3759 -0.0506 0.0157  -0.0146 358 MET A CG  
774  S SD  . MET A 94  ? 0.3820 0.4034 0.4207 -0.0483 0.0291  -0.0039 358 MET A SD  
775  C CE  . MET A 94  ? 0.3394 0.3827 0.4007 -0.0511 0.0282  -0.0112 358 MET A CE  
776  N N   . GLU A 95  ? 0.2922 0.3447 0.3030 -0.0283 -0.0133 0.0043  359 GLU A N   
777  C CA  . GLU A 95  ? 0.2828 0.3464 0.2907 -0.0213 -0.0226 0.0065  359 GLU A CA  
778  C C   . GLU A 95  ? 0.2771 0.3333 0.2827 -0.0167 -0.0224 0.0168  359 GLU A C   
779  O O   . GLU A 95  ? 0.2961 0.3585 0.3058 -0.0121 -0.0264 0.0178  359 GLU A O   
780  C CB  . GLU A 95  ? 0.3383 0.4029 0.3313 -0.0170 -0.0268 0.0067  359 GLU A CB  
781  C CG  . GLU A 95  ? 0.4705 0.5409 0.4647 -0.0226 -0.0271 -0.0070 359 GLU A CG  
782  C CD  . GLU A 95  ? 0.5538 0.6240 0.5279 -0.0171 -0.0307 -0.0083 359 GLU A CD  
783  O OE1 . GLU A 95  ? 0.4028 0.4656 0.3618 -0.0096 -0.0299 0.0032  359 GLU A OE1 
784  O OE2 . GLU A 95  ? 0.6272 0.7034 0.6002 -0.0207 -0.0330 -0.0217 359 GLU A OE2 
785  N N   . VAL A 96  ? 0.2143 0.2579 0.2151 -0.0175 -0.0179 0.0231  360 VAL A N   
786  C CA  . VAL A 96  ? 0.2067 0.2445 0.2077 -0.0149 -0.0183 0.0290  360 VAL A CA  
787  C C   . VAL A 96  ? 0.2265 0.2644 0.2335 -0.0156 -0.0166 0.0264  360 VAL A C   
788  O O   . VAL A 96  ? 0.2436 0.2802 0.2516 -0.0122 -0.0184 0.0281  360 VAL A O   
789  C CB  . VAL A 96  ? 0.2085 0.2381 0.2072 -0.0158 -0.0157 0.0332  360 VAL A CB  
790  C CG1 . VAL A 96  ? 0.2358 0.2609 0.2373 -0.0147 -0.0174 0.0352  360 VAL A CG1 
791  C CG2 . VAL A 96  ? 0.2737 0.3028 0.2679 -0.0148 -0.0145 0.0366  360 VAL A CG2 
792  N N   . VAL A 97  ? 0.2444 0.2803 0.2536 -0.0195 -0.0108 0.0227  361 VAL A N   
793  C CA  . VAL A 97  ? 0.2307 0.2644 0.2431 -0.0198 -0.0056 0.0210  361 VAL A CA  
794  C C   . VAL A 97  ? 0.2399 0.2876 0.2644 -0.0183 -0.0085 0.0167  361 VAL A C   
795  O O   . VAL A 97  ? 0.2552 0.3018 0.2807 -0.0146 -0.0077 0.0177  361 VAL A O   
796  C CB  . VAL A 97  ? 0.2420 0.2687 0.2551 -0.0245 0.0048  0.0184  361 VAL A CB  
797  C CG1 . VAL A 97  ? 0.2396 0.2652 0.2583 -0.0255 0.0137  0.0161  361 VAL A CG1 
798  C CG2 . VAL A 97  ? 0.2645 0.2759 0.2629 -0.0213 0.0073  0.0245  361 VAL A CG2 
799  N N   . LEU A 98  ? 0.2368 0.2984 0.2698 -0.0199 -0.0126 0.0111  362 LEU A N   
800  C CA  . LEU A 98  ? 0.2493 0.3293 0.2964 -0.0163 -0.0174 0.0056  362 LEU A CA  
801  C C   . LEU A 98  ? 0.2501 0.3294 0.2903 -0.0061 -0.0245 0.0123  362 LEU A C   
802  O O   . LEU A 98  ? 0.3262 0.4146 0.3762 -0.0004 -0.0257 0.0107  362 LEU A O   
803  C CB  . LEU A 98  ? 0.2379 0.3354 0.2941 -0.0192 -0.0230 -0.0041 362 LEU A CB  
804  C CG  . LEU A 98  ? 0.2576 0.3566 0.3276 -0.0310 -0.0136 -0.0142 362 LEU A CG  
805  C CD1 . LEU A 98  ? 0.2856 0.3981 0.3606 -0.0351 -0.0203 -0.0258 362 LEU A CD1 
806  C CD2 . LEU A 98  ? 0.2824 0.3935 0.3757 -0.0345 -0.0065 -0.0209 362 LEU A CD2 
807  N N   . VAL A 99  ? 0.2534 0.3213 0.2785 -0.0034 -0.0273 0.0197  363 VAL A N   
808  C CA  . VAL A 99  ? 0.2624 0.3226 0.2801 0.0051  -0.0301 0.0271  363 VAL A CA  
809  C C   . VAL A 99  ? 0.2877 0.3353 0.3061 0.0046  -0.0251 0.0289  363 VAL A C   
810  O O   . VAL A 99  ? 0.2643 0.3096 0.2844 0.0115  -0.0254 0.0305  363 VAL A O   
811  C CB  . VAL A 99  ? 0.2767 0.3261 0.2799 0.0064  -0.0305 0.0344  363 VAL A CB  
812  C CG1 . VAL A 99  ? 0.2839 0.3176 0.2802 0.0126  -0.0283 0.0429  363 VAL A CG1 
813  C CG2 . VAL A 99  ? 0.3020 0.3635 0.2989 0.0108  -0.0366 0.0321  363 VAL A CG2 
814  N N   . ARG A 100 ? 0.3009 0.3395 0.3158 -0.0020 -0.0210 0.0284  364 ARG A N   
815  C CA  . ARG A 100 ? 0.2677 0.2952 0.2794 -0.0020 -0.0180 0.0278  364 ARG A CA  
816  C C   . ARG A 100 ? 0.2983 0.3303 0.3162 0.0012  -0.0140 0.0238  364 ARG A C   
817  O O   . ARG A 100 ? 0.2798 0.3032 0.2947 0.0048  -0.0122 0.0229  364 ARG A O   
818  C CB  . ARG A 100 ? 0.2335 0.2553 0.2387 -0.0068 -0.0160 0.0271  364 ARG A CB  
819  C CG  . ARG A 100 ? 0.2518 0.2689 0.2544 -0.0089 -0.0192 0.0298  364 ARG A CG  
820  C CD  . ARG A 100 ? 0.2719 0.2872 0.2692 -0.0105 -0.0189 0.0290  364 ARG A CD  
821  N NE  . ARG A 100 ? 0.2525 0.2671 0.2526 -0.0119 -0.0227 0.0291  364 ARG A NE  
822  C CZ  . ARG A 100 ? 0.2830 0.2971 0.2803 -0.0105 -0.0265 0.0258  364 ARG A CZ  
823  N NH1 . ARG A 100 ? 0.3232 0.3335 0.3082 -0.0060 -0.0261 0.0244  364 ARG A NH1 
824  N NH2 . ARG A 100 ? 0.2930 0.3113 0.3000 -0.0131 -0.0302 0.0237  364 ARG A NH2 
825  N N   . MET A 101 ? 0.2722 0.3181 0.3006 -0.0008 -0.0115 0.0199  365 MET A N   
826  C CA  . MET A 101 ? 0.2652 0.3183 0.3044 0.0009  -0.0050 0.0152  365 MET A CA  
827  C C   . MET A 101 ? 0.2755 0.3341 0.3220 0.0105  -0.0080 0.0152  365 MET A C   
828  O O   . MET A 101 ? 0.2495 0.3084 0.3014 0.0139  -0.0013 0.0124  365 MET A O   
829  C CB  . MET A 101 ? 0.3173 0.3866 0.3727 -0.0052 -0.0014 0.0091  365 MET A CB  
830  C CG  . MET A 101 ? 0.2941 0.3761 0.3682 -0.0044 0.0064  0.0030  365 MET A CG  
831  S SD  . MET A 101 ? 0.3634 0.4611 0.4601 -0.0162 0.0145  -0.0067 365 MET A SD  
832  C CE  . MET A 101 ? 0.3219 0.3911 0.3938 -0.0228 0.0228  -0.0001 365 MET A CE  
833  N N   . CYS A 102 ? 0.2622 0.3233 0.3071 0.0166  -0.0164 0.0192  366 CYS A N   
834  C CA  . CYS A 102 ? 0.2636 0.3274 0.3136 0.0288  -0.0184 0.0207  366 CYS A CA  
835  C C   . CYS A 102 ? 0.2811 0.3227 0.3216 0.0314  -0.0125 0.0223  366 CYS A C   
836  O O   . CYS A 102 ? 0.2803 0.3222 0.3267 0.0410  -0.0101 0.0216  366 CYS A O   
837  C CB  . CYS A 102 ? 0.2887 0.3541 0.3322 0.0373  -0.0271 0.0269  366 CYS A CB  
838  S SG  . CYS A 102 ? 0.3582 0.3931 0.3802 0.0365  -0.0253 0.0371  366 CYS A SG  
839  N N   . ARG A 103 ? 0.2575 0.2814 0.2846 0.0237  -0.0106 0.0229  367 ARG A N   
840  C CA  . ARG A 103 ? 0.3059 0.3107 0.3244 0.0250  -0.0062 0.0203  367 ARG A CA  
841  C C   . ARG A 103 ? 0.3076 0.3152 0.3282 0.0274  0.0016  0.0145  367 ARG A C   
842  O O   . ARG A 103 ? 0.3022 0.2967 0.3173 0.0322  0.0062  0.0110  367 ARG A O   
843  C CB  . ARG A 103 ? 0.2740 0.2663 0.2808 0.0163  -0.0082 0.0190  367 ARG A CB  
844  C CG  . ARG A 103 ? 0.3080 0.2955 0.3146 0.0130  -0.0124 0.0242  367 ARG A CG  
845  C CD  . ARG A 103 ? 0.3258 0.3107 0.3278 0.0043  -0.0152 0.0216  367 ARG A CD  
846  N NE  . ARG A 103 ? 0.3284 0.3006 0.3263 0.0018  -0.0157 0.0143  367 ARG A NE  
847  C CZ  . ARG A 103 ? 0.3081 0.2799 0.2965 0.0013  -0.0175 0.0072  367 ARG A CZ  
848  N NH1 . ARG A 103 ? 0.3030 0.2827 0.2842 0.0033  -0.0159 0.0086  367 ARG A NH1 
849  N NH2 . ARG A 103 ? 0.3491 0.3113 0.3342 -0.0012 -0.0206 -0.0021 367 ARG A NH2 
850  N N   . ALA A 104 ? 0.2574 0.2798 0.2851 0.0233  0.0053  0.0127  368 ALA A N   
851  C CA  . ALA A 104 ? 0.2578 0.2818 0.2868 0.0238  0.0167  0.0082  368 ALA A CA  
852  C C   . ALA A 104 ? 0.2255 0.2718 0.2801 0.0287  0.0210  0.0052  368 ALA A C   
853  O O   . ALA A 104 ? 0.2451 0.2972 0.3081 0.0285  0.0331  0.0011  368 ALA A O   
854  C CB  . ALA A 104 ? 0.2270 0.2485 0.2469 0.0155  0.0216  0.0087  368 ALA A CB  
855  N N   . TYR A 105 ? 0.2505 0.2202 0.2547 -0.0041 -0.0342 0.0281  369 TYR A N   
856  C CA  . TYR A 105 ? 0.2548 0.2290 0.2679 0.0015  -0.0360 0.0326  369 TYR A CA  
857  C C   . TYR A 105 ? 0.3098 0.2754 0.3298 0.0049  -0.0298 0.0379  369 TYR A C   
858  O O   . TYR A 105 ? 0.3125 0.2724 0.3302 0.0049  -0.0266 0.0416  369 TYR A O   
859  C CB  . TYR A 105 ? 0.2752 0.2608 0.2860 0.0035  -0.0430 0.0365  369 TYR A CB  
860  C CG  . TYR A 105 ? 0.2511 0.2457 0.2713 0.0086  -0.0467 0.0418  369 TYR A CG  
861  C CD1 . TYR A 105 ? 0.2655 0.2675 0.2928 0.0087  -0.0499 0.0383  369 TYR A CD1 
862  C CD2 . TYR A 105 ? 0.2614 0.2579 0.2849 0.0134  -0.0465 0.0512  369 TYR A CD2 
863  C CE1 . TYR A 105 ? 0.2759 0.2884 0.3135 0.0127  -0.0539 0.0433  369 TYR A CE1 
864  C CE2 . TYR A 105 ? 0.2642 0.2720 0.2973 0.0182  -0.0505 0.0575  369 TYR A CE2 
865  C CZ  . TYR A 105 ? 0.2798 0.2962 0.3201 0.0175  -0.0547 0.0532  369 TYR A CZ  
866  O OH  . TYR A 105 ? 0.3581 0.3877 0.4094 0.0217  -0.0592 0.0600  369 TYR A OH  
867  N N   . ASN A 106 ? 0.2642 0.2292 0.2946 0.0084  -0.0274 0.0394  370 ASN A N   
868  C CA  . ASN A 106 ? 0.2802 0.2365 0.3200 0.0124  -0.0196 0.0453  370 ASN A CA  
869  C C   . ASN A 106 ? 0.2889 0.2571 0.3393 0.0193  -0.0241 0.0552  370 ASN A C   
870  O O   . ASN A 106 ? 0.2990 0.2751 0.3575 0.0214  -0.0274 0.0552  370 ASN A O   
871  C CB  . ASN A 106 ? 0.3177 0.2632 0.3617 0.0112  -0.0115 0.0399  370 ASN A CB  
872  C CG  . ASN A 106 ? 0.3411 0.2754 0.3960 0.0153  -0.0011 0.0455  370 ASN A CG  
873  O OD1 . ASN A 106 ? 0.3913 0.3261 0.4511 0.0191  0.0002  0.0541  370 ASN A OD1 
874  N ND2 . ASN A 106 ? 0.3778 0.3019 0.4369 0.0148  0.0072  0.0413  370 ASN A ND2 
875  N N   . ALA A 107 ? 0.3197 0.2909 0.3705 0.0228  -0.0246 0.0641  371 ALA A N   
876  C CA  . ALA A 107 ? 0.3350 0.3217 0.3946 0.0293  -0.0304 0.0747  371 ALA A CA  
877  C C   . ALA A 107 ? 0.3392 0.3240 0.4165 0.0353  -0.0241 0.0823  371 ALA A C   
878  O O   . ALA A 107 ? 0.3464 0.3468 0.4337 0.0401  -0.0298 0.0903  371 ALA A O   
879  C CB  . ALA A 107 ? 0.3453 0.3366 0.4003 0.0323  -0.0317 0.0839  371 ALA A CB  
880  N N   . ASP A 108 ? 0.3050 0.2717 0.3868 0.0348  -0.0120 0.0800  372 ASP A N   
881  C CA  . ASP A 108 ? 0.3530 0.3154 0.4528 0.0409  -0.0035 0.0878  372 ASP A CA  
882  C C   . ASP A 108 ? 0.3465 0.3168 0.4553 0.0418  -0.0072 0.0854  372 ASP A C   
883  O O   . ASP A 108 ? 0.4005 0.3781 0.5266 0.0484  -0.0058 0.0957  372 ASP A O   
884  C CB  . ASP A 108 ? 0.4582 0.3973 0.5590 0.0386  0.0118  0.0832  372 ASP A CB  
885  C CG  . ASP A 108 ? 0.6352 0.5653 0.7320 0.0382  0.0177  0.0866  372 ASP A CG  
886  O OD1 . ASP A 108 ? 0.6875 0.6287 0.7877 0.0436  0.0138  0.0985  372 ASP A OD1 
887  O OD2 . ASP A 108 ? 0.7408 0.6537 0.8313 0.0322  0.0266  0.0775  372 ASP A OD2 
888  N N   . ASN A 109 ? 0.3125 0.2821 0.4116 0.0358  -0.0113 0.0732  373 ASN A N   
889  C CA  . ASN A 109 ? 0.3244 0.3013 0.4323 0.0363  -0.0143 0.0704  373 ASN A CA  
890  C C   . ASN A 109 ? 0.2823 0.2733 0.3819 0.0320  -0.0265 0.0636  373 ASN A C   
891  O O   . ASN A 109 ? 0.3291 0.3255 0.4353 0.0313  -0.0287 0.0596  373 ASN A O   
892  C CB  . ASN A 109 ? 0.3654 0.3252 0.4733 0.0343  -0.0036 0.0627  373 ASN A CB  
893  C CG  . ASN A 109 ? 0.3419 0.2922 0.4312 0.0268  -0.0026 0.0510  373 ASN A CG  
894  O OD1 . ASN A 109 ? 0.3325 0.2888 0.4101 0.0233  -0.0100 0.0485  373 ASN A OD1 
895  N ND2 . ASN A 109 ? 0.4050 0.3413 0.4911 0.0244  0.0067  0.0442  373 ASN A ND2 
896  N N   . ARG A 110 ? 0.2750 0.2718 0.3621 0.0294  -0.0331 0.0631  374 ARG A N   
897  C CA  . ARG A 110 ? 0.2519 0.2615 0.3316 0.0252  -0.0433 0.0566  374 ARG A CA  
898  C C   . ARG A 110 ? 0.3010 0.3041 0.3762 0.0204  -0.0410 0.0457  374 ARG A C   
899  O O   . ARG A 110 ? 0.3134 0.3249 0.3939 0.0190  -0.0450 0.0414  374 ARG A O   
900  C CB  . ARG A 110 ? 0.3049 0.3344 0.3967 0.0279  -0.0518 0.0617  374 ARG A CB  
901  C CG  . ARG A 110 ? 0.4009 0.4399 0.4966 0.0333  -0.0545 0.0746  374 ARG A CG  
902  C CD  . ARG A 110 ? 0.6087 0.6725 0.7115 0.0342  -0.0661 0.0788  374 ARG A CD  
903  N NE  . ARG A 110 ? 0.7428 0.8154 0.8307 0.0280  -0.0746 0.0701  374 ARG A NE  
904  C CZ  . ARG A 110 ? 0.7589 0.8421 0.8353 0.0279  -0.0809 0.0739  374 ARG A CZ  
905  N NH1 . ARG A 110 ? 0.6898 0.7788 0.7526 0.0218  -0.0869 0.0646  374 ARG A NH1 
906  N NH2 . ARG A 110 ? 0.7850 0.8728 0.8638 0.0343  -0.0802 0.0875  374 ARG A NH2 
907  N N   . THR A 111 ? 0.2564 0.2450 0.3218 0.0176  -0.0344 0.0413  375 THR A N   
908  C CA  . THR A 111 ? 0.2550 0.2392 0.3142 0.0134  -0.0323 0.0326  375 THR A CA  
909  C C   . THR A 111 ? 0.2812 0.2626 0.3251 0.0084  -0.0336 0.0285  375 THR A C   
910  O O   . THR A 111 ? 0.2787 0.2574 0.3165 0.0080  -0.0338 0.0315  375 THR A O   
911  C CB  . THR A 111 ? 0.2916 0.2628 0.3533 0.0138  -0.0226 0.0302  375 THR A CB  
912  O OG1 . THR A 111 ? 0.3181 0.2771 0.3742 0.0129  -0.0162 0.0312  375 THR A OG1 
913  C CG2 . THR A 111 ? 0.2799 0.2530 0.3586 0.0190  -0.0199 0.0347  375 THR A CG2 
914  N N   . VAL A 112 ? 0.2510 0.2344 0.2906 0.0052  -0.0342 0.0225  376 VAL A N   
915  C CA  . VAL A 112 ? 0.2501 0.2328 0.2775 0.0007  -0.0351 0.0194  376 VAL A CA  
916  C C   . VAL A 112 ? 0.3187 0.2963 0.3419 -0.0019 -0.0299 0.0151  376 VAL A C   
917  O O   . VAL A 112 ? 0.2599 0.2378 0.2895 -0.0002 -0.0271 0.0136  376 VAL A O   
918  C CB  . VAL A 112 ? 0.2338 0.2269 0.2601 -0.0005 -0.0409 0.0180  376 VAL A CB  
919  C CG1 . VAL A 112 ? 0.2704 0.2678 0.3038 -0.0006 -0.0399 0.0143  376 VAL A CG1 
920  C CG2 . VAL A 112 ? 0.2651 0.2572 0.2799 -0.0043 -0.0414 0.0170  376 VAL A CG2 
921  N N   . PHE A 113 ? 0.2690 0.2429 0.2819 -0.0060 -0.0285 0.0134  377 PHE A N   
922  C CA  . PHE A 113 ? 0.2702 0.2427 0.2773 -0.0091 -0.0249 0.0097  377 PHE A CA  
923  C C   . PHE A 113 ? 0.2878 0.2699 0.2962 -0.0091 -0.0269 0.0096  377 PHE A C   
924  O O   . PHE A 113 ? 0.3049 0.2924 0.3113 -0.0103 -0.0304 0.0108  377 PHE A O   
925  C CB  . PHE A 113 ? 0.2939 0.2626 0.2908 -0.0145 -0.0240 0.0080  377 PHE A CB  
926  C CG  . PHE A 113 ? 0.3093 0.2777 0.2989 -0.0186 -0.0205 0.0038  377 PHE A CG  
927  C CD1 . PHE A 113 ? 0.3174 0.2776 0.3061 -0.0187 -0.0144 0.0004  377 PHE A CD1 
928  C CD2 . PHE A 113 ? 0.4466 0.4237 0.4297 -0.0225 -0.0230 0.0037  377 PHE A CD2 
929  C CE1 . PHE A 113 ? 0.3261 0.2869 0.3055 -0.0233 -0.0113 -0.0042 377 PHE A CE1 
930  C CE2 . PHE A 113 ? 0.3861 0.3657 0.3615 -0.0266 -0.0206 0.0005  377 PHE A CE2 
931  C CZ  . PHE A 113 ? 0.3464 0.3180 0.3189 -0.0271 -0.0150 -0.0039 377 PHE A CZ  
932  N N   . PHE A 114 ? 0.2699 0.2533 0.2820 -0.0074 -0.0233 0.0086  378 PHE A N   
933  C CA  . PHE A 114 ? 0.2441 0.2357 0.2608 -0.0063 -0.0230 0.0095  378 PHE A CA  
934  C C   . PHE A 114 ? 0.2784 0.2705 0.2929 -0.0058 -0.0177 0.0093  378 PHE A C   
935  O O   . PHE A 114 ? 0.2491 0.2358 0.2665 -0.0035 -0.0137 0.0082  378 PHE A O   
936  C CB  . PHE A 114 ? 0.2604 0.2546 0.2900 -0.0028 -0.0243 0.0095  378 PHE A CB  
937  C CG  . PHE A 114 ? 0.2614 0.2624 0.2986 -0.0018 -0.0220 0.0096  378 PHE A CG  
938  C CD1 . PHE A 114 ? 0.3137 0.3195 0.3499 -0.0037 -0.0236 0.0098  378 PHE A CD1 
939  C CD2 . PHE A 114 ? 0.2452 0.2465 0.2908 0.0011  -0.0168 0.0099  378 PHE A CD2 
940  C CE1 . PHE A 114 ? 0.2767 0.2874 0.3217 -0.0027 -0.0194 0.0101  378 PHE A CE1 
941  C CE2 . PHE A 114 ? 0.3049 0.3117 0.3597 0.0025  -0.0128 0.0107  378 PHE A CE2 
942  C CZ  . PHE A 114 ? 0.2725 0.2838 0.3272 0.0004  -0.0138 0.0108  378 PHE A CZ  
943  N N   . GLU A 115 ? 0.2635 0.2629 0.2729 -0.0076 -0.0172 0.0112  379 GLU A N   
944  C CA  . GLU A 115 ? 0.2665 0.2695 0.2730 -0.0065 -0.0123 0.0124  379 GLU A CA  
945  C C   . GLU A 115 ? 0.3051 0.3002 0.3030 -0.0083 -0.0093 0.0085  379 GLU A C   
946  O O   . GLU A 115 ? 0.3064 0.2993 0.3057 -0.0054 -0.0039 0.0083  379 GLU A O   
947  C CB  . GLU A 115 ? 0.2793 0.2850 0.2988 -0.0011 -0.0077 0.0149  379 GLU A CB  
948  C CG  . GLU A 115 ? 0.2693 0.2825 0.2970 -0.0003 -0.0084 0.0180  379 GLU A CG  
949  C CD  . GLU A 115 ? 0.2887 0.3056 0.3305 0.0044  -0.0020 0.0209  379 GLU A CD  
950  O OE1 . GLU A 115 ? 0.3070 0.3203 0.3541 0.0076  0.0022  0.0203  379 GLU A OE1 
951  O OE2 . GLU A 115 ? 0.2990 0.3217 0.3472 0.0049  0.0000  0.0240  379 GLU A OE2 
952  N N   . GLY A 116 ? 0.2903 0.2805 0.2796 -0.0131 -0.0118 0.0052  380 GLY A N   
953  C CA  . GLY A 116 ? 0.2869 0.2699 0.2660 -0.0167 -0.0079 0.0002  380 GLY A CA  
954  C C   . GLY A 116 ? 0.3404 0.3091 0.3234 -0.0154 -0.0041 -0.0029 380 GLY A C   
955  O O   . GLY A 116 ? 0.3306 0.2911 0.3053 -0.0195 0.0003  -0.0081 380 GLY A O   
956  N N   . LYS A 117 ? 0.2907 0.2573 0.2871 -0.0099 -0.0048 0.0003  381 LYS A N   
957  C CA  . LYS A 117 ? 0.2963 0.2516 0.2995 -0.0076 -0.0012 -0.0002 381 LYS A CA  
958  C C   . LYS A 117 ? 0.3212 0.2792 0.3351 -0.0044 -0.0068 0.0040  381 LYS A C   
959  O O   . LYS A 117 ? 0.2871 0.2544 0.3034 -0.0040 -0.0125 0.0060  381 LYS A O   
960  C CB  . LYS A 117 ? 0.3146 0.2651 0.3250 -0.0029 0.0057  0.0000  381 LYS A CB  
961  C CG  . LYS A 117 ? 0.3662 0.3148 0.3651 -0.0051 0.0120  -0.0038 381 LYS A CG  
962  C CD  . LYS A 117 ? 0.3672 0.3079 0.3742 0.0000  0.0205  -0.0034 381 LYS A CD  
963  C CE  . LYS A 117 ? 0.4408 0.3806 0.4345 -0.0018 0.0272  -0.0069 381 LYS A CE  
964  N NZ  . LYS A 117 ? 0.5442 0.4724 0.5436 0.0023  0.0375  -0.0075 381 LYS A NZ  
965  N N   . TYR A 118 ? 0.3134 0.2635 0.3340 -0.0021 -0.0044 0.0057  382 TYR A N   
966  C CA  . TYR A 118 ? 0.2514 0.2063 0.2821 0.0014  -0.0100 0.0108  382 TYR A CA  
967  C C   . TYR A 118 ? 0.2802 0.2407 0.3256 0.0066  -0.0107 0.0136  382 TYR A C   
968  O O   . TYR A 118 ? 0.3084 0.2635 0.3606 0.0093  -0.0043 0.0136  382 TYR A O   
969  C CB  . TYR A 118 ? 0.2574 0.2035 0.2903 0.0023  -0.0068 0.0135  382 TYR A CB  
970  C CG  . TYR A 118 ? 0.2779 0.2218 0.3005 -0.0023 -0.0085 0.0124  382 TYR A CG  
971  C CD1 . TYR A 118 ? 0.3099 0.2465 0.3213 -0.0083 -0.0039 0.0063  382 TYR A CD1 
972  C CD2 . TYR A 118 ? 0.2689 0.2188 0.2927 -0.0011 -0.0147 0.0171  382 TYR A CD2 
973  C CE1 . TYR A 118 ? 0.3094 0.2447 0.3134 -0.0130 -0.0054 0.0052  382 TYR A CE1 
974  C CE2 . TYR A 118 ? 0.3232 0.2707 0.3388 -0.0049 -0.0156 0.0167  382 TYR A CE2 
975  C CZ  . TYR A 118 ? 0.3199 0.2600 0.3265 -0.0110 -0.0109 0.0107  382 TYR A CZ  
976  O OH  . TYR A 118 ? 0.3711 0.3096 0.3716 -0.0153 -0.0115 0.0101  382 TYR A OH  
977  N N   . GLY A 119 ? 0.2705 0.2421 0.3213 0.0073  -0.0181 0.0152  383 GLY A N   
978  C CA  . GLY A 119 ? 0.2746 0.2532 0.3411 0.0110  -0.0196 0.0170  383 GLY A CA  
979  C C   . GLY A 119 ? 0.2712 0.2601 0.3433 0.0117  -0.0279 0.0200  383 GLY A C   
980  O O   . GLY A 119 ? 0.2889 0.2808 0.3516 0.0091  -0.0326 0.0198  383 GLY A O   
981  N N   . GLY A 120 ? 0.2993 0.2952 0.3871 0.0149  -0.0297 0.0230  384 GLY A N   
982  C CA  . GLY A 120 ? 0.2510 0.2599 0.3436 0.0150  -0.0385 0.0256  384 GLY A CA  
983  C C   . GLY A 120 ? 0.2759 0.2952 0.3713 0.0116  -0.0433 0.0200  384 GLY A C   
984  O O   . GLY A 120 ? 0.2801 0.2960 0.3748 0.0099  -0.0392 0.0151  384 GLY A O   
985  N N   . MET A 121 ? 0.2636 0.2962 0.3628 0.0106  -0.0515 0.0207  385 MET A N   
986  C CA  . MET A 121 ? 0.2431 0.2840 0.3425 0.0059  -0.0552 0.0135  385 MET A CA  
987  C C   . MET A 121 ? 0.2577 0.3004 0.3733 0.0057  -0.0514 0.0094  385 MET A C   
988  O O   . MET A 121 ? 0.2140 0.2589 0.3310 0.0019  -0.0502 0.0026  385 MET A O   
989  C CB  . MET A 121 ? 0.2780 0.3341 0.3769 0.0039  -0.0649 0.0139  385 MET A CB  
990  C CG  . MET A 121 ? 0.2969 0.3651 0.4113 0.0068  -0.0696 0.0195  385 MET A CG  
991  S SD  . MET A 121 ? 0.4674 0.5558 0.5756 0.0034  -0.0819 0.0197  385 MET A SD  
992  C CE  . MET A 121 ? 0.4338 0.5396 0.5634 0.0072  -0.0876 0.0280  385 MET A CE  
993  N N   . GLU A 122 ? 0.2472 0.2895 0.3769 0.0099  -0.0487 0.0139  386 GLU A N   
994  C CA  . GLU A 122 ? 0.2472 0.2908 0.3936 0.0101  -0.0441 0.0106  386 GLU A CA  
995  C C   . GLU A 122 ? 0.2457 0.2773 0.3870 0.0104  -0.0347 0.0076  386 GLU A C   
996  O O   . GLU A 122 ? 0.2340 0.2669 0.3882 0.0102  -0.0302 0.0044  386 GLU A O   
997  C CB  . GLU A 122 ? 0.2572 0.3022 0.4206 0.0151  -0.0421 0.0170  386 GLU A CB  
998  C CG  . GLU A 122 ? 0.2857 0.3151 0.4441 0.0199  -0.0332 0.0220  386 GLU A CG  
999  C CD  . GLU A 122 ? 0.4013 0.4269 0.5486 0.0217  -0.0352 0.0280  386 GLU A CD  
1000 O OE1 . GLU A 122 ? 0.4592 0.4718 0.6041 0.0251  -0.0272 0.0314  386 GLU A OE1 
1001 O OE2 . GLU A 122 ? 0.4264 0.4613 0.5678 0.0198  -0.0437 0.0292  386 GLU A OE2 
1002 N N   . LEU A 123 ? 0.2563 0.2778 0.3801 0.0107  -0.0317 0.0089  387 LEU A N   
1003 C CA  . LEU A 123 ? 0.2497 0.2633 0.3678 0.0109  -0.0238 0.0072  387 LEU A CA  
1004 C C   . LEU A 123 ? 0.2478 0.2670 0.3693 0.0075  -0.0235 0.0021  387 LEU A C   
1005 O O   . LEU A 123 ? 0.2710 0.2875 0.3972 0.0086  -0.0159 0.0015  387 LEU A O   
1006 C CB  . LEU A 123 ? 0.2513 0.2566 0.3496 0.0102  -0.0227 0.0088  387 LEU A CB  
1007 C CG  . LEU A 123 ? 0.2968 0.2952 0.3900 0.0116  -0.0144 0.0091  387 LEU A CG  
1008 C CD1 . LEU A 123 ? 0.3047 0.2949 0.3994 0.0149  -0.0087 0.0114  387 LEU A CD1 
1009 C CD2 . LEU A 123 ? 0.3745 0.3701 0.4488 0.0085  -0.0154 0.0090  387 LEU A CD2 
1010 N N   . PHE A 124 ? 0.2348 0.2615 0.3539 0.0035  -0.0306 -0.0012 388 PHE A N   
1011 C CA  . PHE A 124 ? 0.2572 0.2866 0.3752 -0.0006 -0.0292 -0.0066 388 PHE A CA  
1012 C C   . PHE A 124 ? 0.2481 0.2854 0.3834 -0.0037 -0.0292 -0.0130 388 PHE A C   
1013 O O   . PHE A 124 ? 0.2135 0.2534 0.3490 -0.0082 -0.0282 -0.0190 388 PHE A O   
1014 C CB  . PHE A 124 ? 0.2417 0.2724 0.3430 -0.0037 -0.0353 -0.0071 388 PHE A CB  
1015 C CG  . PHE A 124 ? 0.2284 0.2513 0.3147 -0.0016 -0.0346 -0.0019 388 PHE A CG  
1016 C CD1 . PHE A 124 ? 0.2174 0.2349 0.2980 -0.0011 -0.0283 -0.0004 388 PHE A CD1 
1017 C CD2 . PHE A 124 ? 0.2457 0.2678 0.3256 -0.0002 -0.0396 0.0020  388 PHE A CD2 
1018 C CE1 . PHE A 124 ? 0.2276 0.2395 0.2949 -0.0004 -0.0280 0.0034  388 PHE A CE1 
1019 C CE2 . PHE A 124 ? 0.2539 0.2680 0.3214 0.0008  -0.0379 0.0057  388 PHE A CE2 
1020 C CZ  . PHE A 124 ? 0.2310 0.2404 0.2918 0.0000  -0.0325 0.0055  388 PHE A CZ  
1021 N N   . ARG A 125 ? 0.2231 0.2641 0.3746 -0.0018 -0.0294 -0.0122 389 ARG A N   
1022 C CA  . ARG A 125 ? 0.2121 0.2628 0.3814 -0.0060 -0.0309 -0.0191 389 ARG A CA  
1023 C C   . ARG A 125 ? 0.2132 0.2608 0.3927 -0.0083 -0.0213 -0.0248 389 ARG A C   
1024 O O   . ARG A 125 ? 0.2210 0.2754 0.4099 -0.0142 -0.0222 -0.0331 389 ARG A O   
1025 C CB  . ARG A 125 ? 0.1972 0.2531 0.3849 -0.0032 -0.0320 -0.0162 389 ARG A CB  
1026 C CG  . ARG A 125 ? 0.2129 0.2763 0.3962 -0.0020 -0.0421 -0.0110 389 ARG A CG  
1027 C CD  . ARG A 125 ? 0.2078 0.2794 0.4129 0.0002  -0.0437 -0.0079 389 ARG A CD  
1028 N NE  . ARG A 125 ? 0.2512 0.3297 0.4531 0.0029  -0.0517 -0.0003 389 ARG A NE  
1029 C CZ  . ARG A 125 ? 0.2346 0.3181 0.4529 0.0071  -0.0521 0.0064  389 ARG A CZ  
1030 N NH1 . ARG A 125 ? 0.2241 0.3144 0.4404 0.0100  -0.0585 0.0147  389 ARG A NH1 
1031 N NH2 . ARG A 125 ? 0.2231 0.3054 0.4620 0.0085  -0.0454 0.0055  389 ARG A NH2 
1032 N N   . ALA A 126 ? 0.2080 0.2461 0.3862 -0.0036 -0.0116 -0.0200 390 ALA A N   
1033 C CA  . ALA A 126 ? 0.2324 0.2677 0.4228 -0.0042 -0.0007 -0.0229 390 ALA A CA  
1034 C C   . ALA A 126 ? 0.2339 0.2688 0.4165 -0.0092 0.0006  -0.0282 390 ALA A C   
1035 O O   . ALA A 126 ? 0.2450 0.2790 0.4413 -0.0116 0.0094  -0.0330 390 ALA A O   
1036 C CB  . ALA A 126 ? 0.2992 0.3266 0.4884 0.0027  0.0090  -0.0145 390 ALA A CB  
1037 N N   . LEU A 127 ? 0.2190 0.2543 0.3815 -0.0109 -0.0070 -0.0274 391 LEU A N   
1038 C CA  . LEU A 127 ? 0.2326 0.2674 0.3876 -0.0158 -0.0056 -0.0327 391 LEU A CA  
1039 C C   . LEU A 127 ? 0.2744 0.3161 0.4379 -0.0234 -0.0084 -0.0441 391 LEU A C   
1040 O O   . LEU A 127 ? 0.2803 0.3200 0.4439 -0.0280 -0.0030 -0.0506 391 LEU A O   
1041 C CB  . LEU A 127 ? 0.2124 0.2460 0.3445 -0.0156 -0.0129 -0.0288 391 LEU A CB  
1042 C CG  . LEU A 127 ? 0.2389 0.2662 0.3604 -0.0105 -0.0091 -0.0195 391 LEU A CG  
1043 C CD1 . LEU A 127 ? 0.2599 0.2867 0.3619 -0.0110 -0.0172 -0.0165 391 LEU A CD1 
1044 C CD2 . LEU A 127 ? 0.2279 0.2517 0.3526 -0.0104 0.0015  -0.0183 391 LEU A CD2 
1045 N N   . GLY A 128 ? 0.2221 0.2726 0.3940 -0.0251 -0.0164 -0.0470 392 GLY A N   
1046 C CA  . GLY A 128 ? 0.2974 0.3571 0.4780 -0.0336 -0.0196 -0.0590 392 GLY A CA  
1047 C C   . GLY A 128 ? 0.2815 0.3467 0.4436 -0.0397 -0.0278 -0.0649 392 GLY A C   
1048 O O   . GLY A 128 ? 0.3254 0.3946 0.4908 -0.0478 -0.0266 -0.0766 392 GLY A O   
1049 N N   . CYS A 129 ? 0.2820 0.3472 0.4249 -0.0361 -0.0356 -0.0572 393 CYS A N   
1050 C CA  . CYS A 129 ? 0.3020 0.3734 0.4263 -0.0406 -0.0439 -0.0607 393 CYS A CA  
1051 C C   . CYS A 129 ? 0.3098 0.3887 0.4245 -0.0364 -0.0558 -0.0517 393 CYS A C   
1052 O O   . CYS A 129 ? 0.2997 0.3743 0.3975 -0.0331 -0.0582 -0.0450 393 CYS A O   
1053 C CB  . CYS A 129 ? 0.3412 0.4017 0.4500 -0.0405 -0.0373 -0.0600 393 CYS A CB  
1054 S SG  . CYS A 129 ? 0.3527 0.4001 0.4569 -0.0314 -0.0305 -0.0467 393 CYS A SG  
1055 N N   . SER A 130 ? 0.3919 0.4821 0.5202 -0.0364 -0.0621 -0.0511 394 SER A N   
1056 C CA  . SER A 130 ? 0.4132 0.5116 0.5377 -0.0316 -0.0719 -0.0413 394 SER A CA  
1057 C C   . SER A 130 ? 0.2451 0.3508 0.3491 -0.0327 -0.0807 -0.0389 394 SER A C   
1058 O O   . SER A 130 ? 0.2751 0.3769 0.3695 -0.0265 -0.0829 -0.0281 394 SER A O   
1059 C CB  . SER A 130 ? 0.5722 0.6859 0.7172 -0.0333 -0.0777 -0.0427 394 SER A CB  
1060 O OG  . SER A 130 ? 0.7421 0.8642 0.8870 -0.0278 -0.0858 -0.0315 394 SER A OG  
1061 N N   . GLU A 131 ? 0.2907 0.4065 0.3880 -0.0406 -0.0852 -0.0487 395 GLU A N   
1062 C CA  . GLU A 131 ? 0.3618 0.4849 0.4379 -0.0420 -0.0926 -0.0471 395 GLU A CA  
1063 C C   . GLU A 131 ? 0.3662 0.4736 0.4248 -0.0377 -0.0870 -0.0412 395 GLU A C   
1064 O O   . GLU A 131 ? 0.3370 0.4456 0.3830 -0.0332 -0.0916 -0.0318 395 GLU A O   
1065 C CB  . GLU A 131 ? 0.4712 0.6038 0.5409 -0.0524 -0.0948 -0.0615 395 GLU A CB  
1066 C CG  . GLU A 131 ? 0.6810 0.8385 0.7562 -0.0580 -0.1071 -0.0656 395 GLU A CG  
1067 C CD  . GLU A 131 ? 0.8359 1.0022 0.8994 -0.0693 -0.1091 -0.0811 395 GLU A CD  
1068 O OE1 . GLU A 131 ? 0.9020 1.0640 0.9765 -0.0770 -0.1019 -0.0951 395 GLU A OE1 
1069 O OE2 . GLU A 131 ? 0.8505 1.0275 0.8938 -0.0707 -0.1169 -0.0795 395 GLU A OE2 
1070 N N   . LEU A 132 ? 0.3248 0.4179 0.3834 -0.0394 -0.0765 -0.0467 396 LEU A N   
1071 C CA  . LEU A 132 ? 0.2813 0.3605 0.3263 -0.0358 -0.0708 -0.0411 396 LEU A CA  
1072 C C   . LEU A 132 ? 0.2837 0.3558 0.3294 -0.0276 -0.0706 -0.0285 396 LEU A C   
1073 O O   . LEU A 132 ? 0.2915 0.3599 0.3239 -0.0245 -0.0723 -0.0214 396 LEU A O   
1074 C CB  . LEU A 132 ? 0.3264 0.3933 0.3760 -0.0382 -0.0586 -0.0473 396 LEU A CB  
1075 C CG  . LEU A 132 ? 0.3743 0.4286 0.4128 -0.0347 -0.0525 -0.0409 396 LEU A CG  
1076 C CD1 . LEU A 132 ? 0.3731 0.4291 0.3918 -0.0353 -0.0572 -0.0387 396 LEU A CD1 
1077 C CD2 . LEU A 132 ? 0.3210 0.3665 0.3664 -0.0373 -0.0402 -0.0466 396 LEU A CD2 
1078 N N   . ILE A 133 ? 0.2367 0.3061 0.2982 -0.0246 -0.0676 -0.0264 397 ILE A N   
1079 C CA  . ILE A 133 ? 0.2337 0.2957 0.2955 -0.0180 -0.0663 -0.0165 397 ILE A CA  
1080 C C   . ILE A 133 ? 0.2618 0.3312 0.3185 -0.0147 -0.0744 -0.0085 397 ILE A C   
1081 O O   . ILE A 133 ? 0.2665 0.3285 0.3134 -0.0110 -0.0735 -0.0013 397 ILE A O   
1082 C CB  . ILE A 133 ? 0.2870 0.3461 0.3662 -0.0153 -0.0617 -0.0157 397 ILE A CB  
1083 C CG1 . ILE A 133 ? 0.2811 0.3329 0.3666 -0.0172 -0.0522 -0.0212 397 ILE A CG1 
1084 C CG2 . ILE A 133 ? 0.2889 0.3402 0.3664 -0.0093 -0.0602 -0.0066 397 ILE A CG2 
1085 C CD1 . ILE A 133 ? 0.2866 0.3283 0.3596 -0.0162 -0.0467 -0.0184 397 ILE A CD1 
1086 N N   . SER A 134 ? 0.2653 0.3498 0.3298 -0.0159 -0.0820 -0.0091 398 SER A N   
1087 C CA  . SER A 134 ? 0.2611 0.3541 0.3220 -0.0117 -0.0890 0.0007  398 SER A CA  
1088 C C   . SER A 134 ? 0.3229 0.4173 0.3632 -0.0128 -0.0920 0.0022  398 SER A C   
1089 O O   . SER A 134 ? 0.2986 0.3919 0.3329 -0.0077 -0.0933 0.0124  398 SER A O   
1090 C CB  . SER A 134 ? 0.3475 0.4598 0.4232 -0.0124 -0.0970 0.0014  398 SER A CB  
1091 O OG  . SER A 134 ? 0.5179 0.6462 0.5840 -0.0171 -0.1055 -0.0021 398 SER A OG  
1092 N N   . SER A 135 ? 0.2861 0.3806 0.3160 -0.0189 -0.0912 -0.0072 399 SER A N   
1093 C CA  . SER A 135 ? 0.2726 0.3667 0.2827 -0.0195 -0.0926 -0.0054 399 SER A CA  
1094 C C   . SER A 135 ? 0.2945 0.3715 0.2979 -0.0152 -0.0855 0.0011  399 SER A C   
1095 O O   . SER A 135 ? 0.3466 0.4227 0.3388 -0.0122 -0.0867 0.0085  399 SER A O   
1096 C CB  . SER A 135 ? 0.3315 0.4269 0.3324 -0.0270 -0.0910 -0.0174 399 SER A CB  
1097 O OG  . SER A 135 ? 0.4589 0.5721 0.4615 -0.0325 -0.0986 -0.0245 399 SER A OG  
1098 N N   . ILE A 136 ? 0.2595 0.3242 0.2704 -0.0151 -0.0782 -0.0013 400 ILE A N   
1099 C CA  . ILE A 136 ? 0.2940 0.3447 0.2998 -0.0123 -0.0721 0.0038  400 ILE A CA  
1100 C C   . ILE A 136 ? 0.2906 0.3393 0.2991 -0.0066 -0.0734 0.0138  400 ILE A C   
1101 O O   . ILE A 136 ? 0.2889 0.3312 0.2892 -0.0044 -0.0716 0.0198  400 ILE A O   
1102 C CB  . ILE A 136 ? 0.2635 0.3054 0.2775 -0.0134 -0.0649 -0.0004 400 ILE A CB  
1103 C CG1 . ILE A 136 ? 0.2790 0.3205 0.2910 -0.0183 -0.0609 -0.0085 400 ILE A CG1 
1104 C CG2 . ILE A 136 ? 0.2730 0.3038 0.2836 -0.0109 -0.0601 0.0051  400 ILE A CG2 
1105 C CD1 . ILE A 136 ? 0.3100 0.3456 0.3337 -0.0185 -0.0533 -0.0113 400 ILE A CD1 
1106 N N   . PHE A 137 ? 0.2479 0.3008 0.2699 -0.0044 -0.0749 0.0153  401 PHE A N   
1107 C CA  . PHE A 137 ? 0.2811 0.3312 0.3086 0.0011  -0.0742 0.0246  401 PHE A CA  
1108 C C   . PHE A 137 ? 0.2683 0.3270 0.2891 0.0039  -0.0793 0.0325  401 PHE A C   
1109 O O   . PHE A 137 ? 0.2955 0.3475 0.3145 0.0080  -0.0762 0.0406  401 PHE A O   
1110 C CB  . PHE A 137 ? 0.2511 0.3058 0.2960 0.0033  -0.0745 0.0252  401 PHE A CB  
1111 C CG  . PHE A 137 ? 0.2303 0.2722 0.2814 0.0036  -0.0668 0.0222  401 PHE A CG  
1112 C CD1 . PHE A 137 ? 0.2599 0.2982 0.3099 -0.0003 -0.0635 0.0142  401 PHE A CD1 
1113 C CD2 . PHE A 137 ? 0.2535 0.2866 0.3105 0.0078  -0.0616 0.0279  401 PHE A CD2 
1114 C CE1 . PHE A 137 ? 0.2708 0.2991 0.3248 0.0004  -0.0563 0.0127  401 PHE A CE1 
1115 C CE2 . PHE A 137 ? 0.2557 0.2778 0.3158 0.0077  -0.0544 0.0247  401 PHE A CE2 
1116 C CZ  . PHE A 137 ? 0.2849 0.3056 0.3428 0.0041  -0.0523 0.0175  401 PHE A CZ  
1117 N N   . ASP A 138 ? 0.2577 0.3323 0.2754 0.0016  -0.0869 0.0304  402 ASP A N   
1118 C CA  . ASP A 138 ? 0.3296 0.4157 0.3406 0.0051  -0.0924 0.0397  402 ASP A CA  
1119 C C   . ASP A 138 ? 0.3509 0.4284 0.3457 0.0054  -0.0890 0.0423  402 ASP A C   
1120 O O   . ASP A 138 ? 0.3629 0.4410 0.3546 0.0106  -0.0885 0.0530  402 ASP A O   
1121 C CB  . ASP A 138 ? 0.4071 0.5142 0.4167 0.0014  -0.1019 0.0357  402 ASP A CB  
1122 C CG  . ASP A 138 ? 0.7116 0.8308 0.7402 0.0022  -0.1062 0.0366  402 ASP A CG  
1123 O OD1 . ASP A 138 ? 0.7700 0.8830 0.8117 0.0078  -0.1022 0.0445  402 ASP A OD1 
1124 O OD2 . ASP A 138 ? 0.7920 0.9265 0.8231 -0.0031 -0.1129 0.0290  402 ASP A OD2 
1125 N N   . PHE A 139 ? 0.3454 0.4148 0.3315 0.0003  -0.0858 0.0331  403 PHE A N   
1126 C CA  . PHE A 139 ? 0.3139 0.3747 0.2862 0.0001  -0.0818 0.0349  403 PHE A CA  
1127 C C   . PHE A 139 ? 0.3389 0.3853 0.3155 0.0038  -0.0752 0.0414  403 PHE A C   
1128 O O   . PHE A 139 ? 0.3874 0.4299 0.3578 0.0068  -0.0729 0.0491  403 PHE A O   
1129 C CB  . PHE A 139 ? 0.3247 0.3798 0.2901 -0.0058 -0.0785 0.0245  403 PHE A CB  
1130 C CG  . PHE A 139 ? 0.3055 0.3526 0.2579 -0.0059 -0.0742 0.0270  403 PHE A CG  
1131 C CD1 . PHE A 139 ? 0.3837 0.4383 0.3229 -0.0050 -0.0772 0.0306  403 PHE A CD1 
1132 C CD2 . PHE A 139 ? 0.3754 0.4090 0.3291 -0.0067 -0.0674 0.0266  403 PHE A CD2 
1133 C CE1 . PHE A 139 ? 0.4124 0.4592 0.3406 -0.0046 -0.0724 0.0334  403 PHE A CE1 
1134 C CE2 . PHE A 139 ? 0.3433 0.3704 0.2871 -0.0068 -0.0633 0.0295  403 PHE A CE2 
1135 C CZ  . PHE A 139 ? 0.3764 0.4092 0.3079 -0.0055 -0.0654 0.0331  403 PHE A CZ  
1136 N N   . SER A 140 ? 0.2984 0.3366 0.2853 0.0030  -0.0714 0.0380  404 SER A N   
1137 C CA  . SER A 140 ? 0.2603 0.2848 0.2504 0.0049  -0.0647 0.0419  404 SER A CA  
1138 C C   . SER A 140 ? 0.2858 0.3117 0.2819 0.0109  -0.0642 0.0525  404 SER A C   
1139 O O   . SER A 140 ? 0.3233 0.3396 0.3183 0.0128  -0.0587 0.0579  404 SER A O   
1140 C CB  . SER A 140 ? 0.3098 0.3274 0.3084 0.0030  -0.0610 0.0362  404 SER A CB  
1141 O OG  . SER A 140 ? 0.4344 0.4492 0.4277 -0.0016 -0.0594 0.0291  404 SER A OG  
1142 N N   . HIS A 141 ? 0.3188 0.3568 0.3234 0.0138  -0.0691 0.0558  405 HIS A N   
1143 C CA  . HIS A 141 ? 0.2693 0.3098 0.2826 0.0204  -0.0677 0.0677  405 HIS A CA  
1144 C C   . HIS A 141 ? 0.3134 0.3583 0.3169 0.0235  -0.0686 0.0764  405 HIS A C   
1145 O O   . HIS A 141 ? 0.3455 0.3835 0.3530 0.0283  -0.0625 0.0860  405 HIS A O   
1146 C CB  . HIS A 141 ? 0.2833 0.3394 0.3087 0.0230  -0.0738 0.0708  405 HIS A CB  
1147 C CG  . HIS A 141 ? 0.3337 0.3895 0.3736 0.0302  -0.0696 0.0830  405 HIS A CG  
1148 N ND1 . HIS A 141 ? 0.3321 0.3760 0.3848 0.0314  -0.0622 0.0820  405 HIS A ND1 
1149 C CD2 . HIS A 141 ? 0.4123 0.4780 0.4564 0.0368  -0.0706 0.0969  405 HIS A CD2 
1150 C CE1 . HIS A 141 ? 0.3880 0.4333 0.4530 0.0384  -0.0582 0.0945  405 HIS A CE1 
1151 N NE2 . HIS A 141 ? 0.4314 0.4905 0.4926 0.0421  -0.0632 0.1045  405 HIS A NE2 
1152 N N   . SER A 142 ? 0.3075 0.3630 0.2983 0.0206  -0.0750 0.0729  406 SER A N   
1153 C CA  . SER A 142 ? 0.3163 0.3775 0.2963 0.0241  -0.0760 0.0819  406 SER A CA  
1154 C C   . SER A 142 ? 0.3551 0.3986 0.3299 0.0239  -0.0672 0.0831  406 SER A C   
1155 O O   . SER A 142 ? 0.3929 0.4346 0.3674 0.0292  -0.0631 0.0943  406 SER A O   
1156 C CB  . SER A 142 ? 0.3932 0.4688 0.3588 0.0202  -0.0839 0.0763  406 SER A CB  
1157 O OG  . SER A 142 ? 0.5450 0.6109 0.5006 0.0140  -0.0813 0.0653  406 SER A OG  
1158 N N   . LEU A 143 ? 0.3496 0.3811 0.3220 0.0180  -0.0638 0.0726  407 LEU A N   
1159 C CA  . LEU A 143 ? 0.3097 0.3259 0.2794 0.0168  -0.0559 0.0733  407 LEU A CA  
1160 C C   . LEU A 143 ? 0.3902 0.3945 0.3719 0.0193  -0.0484 0.0778  407 LEU A C   
1161 O O   . LEU A 143 ? 0.3955 0.3897 0.3773 0.0202  -0.0415 0.0823  407 LEU A O   
1162 C CB  . LEU A 143 ? 0.3199 0.3289 0.2852 0.0100  -0.0547 0.0621  407 LEU A CB  
1163 C CG  . LEU A 143 ? 0.3643 0.3803 0.3175 0.0069  -0.0585 0.0572  407 LEU A CG  
1164 C CD1 . LEU A 143 ? 0.3694 0.3774 0.3220 0.0013  -0.0551 0.0490  407 LEU A CD1 
1165 C CD2 . LEU A 143 ? 0.4136 0.4312 0.3564 0.0098  -0.0574 0.0648  407 LEU A CD2 
1166 N N   . SER A 144 ? 0.4047 0.4091 0.3971 0.0199  -0.0486 0.0757  408 SER A N   
1167 C CA  . SER A 144 ? 0.4604 0.4525 0.4644 0.0217  -0.0402 0.0785  408 SER A CA  
1168 C C   . SER A 144 ? 0.4262 0.4171 0.4359 0.0286  -0.0347 0.0921  408 SER A C   
1169 O O   . SER A 144 ? 0.4127 0.3890 0.4289 0.0287  -0.0248 0.0937  408 SER A O   
1170 C CB  . SER A 144 ? 0.4529 0.4478 0.4678 0.0227  -0.0414 0.0762  408 SER A CB  
1171 O OG  . SER A 144 ? 0.4702 0.4788 0.4921 0.0292  -0.0456 0.0862  408 SER A OG  
1172 N N   . ALA A 145 ? 0.3817 0.3882 0.3889 0.0341  -0.0406 0.1017  409 ALA A N   
1173 C CA  . ALA A 145 ? 0.4341 0.4434 0.4467 0.0422  -0.0360 0.1173  409 ALA A CA  
1174 C C   . ALA A 145 ? 0.4410 0.4382 0.4490 0.0420  -0.0279 0.1204  409 ALA A C   
1175 O O   . ALA A 145 ? 0.4551 0.4481 0.4716 0.0484  -0.0198 0.1327  409 ALA A O   
1176 C CB  . ALA A 145 ? 0.4680 0.5000 0.4748 0.0467  -0.0459 0.1257  409 ALA A CB  
1177 N N   . LEU A 146 ? 0.3923 0.3842 0.3885 0.0353  -0.0295 0.1104  410 LEU A N   
1178 C CA  . LEU A 146 ? 0.3844 0.3666 0.3764 0.0348  -0.0225 0.1135  410 LEU A CA  
1179 C C   . LEU A 146 ? 0.4421 0.4050 0.4436 0.0305  -0.0121 0.1083  410 LEU A C   
1180 O O   . LEU A 146 ? 0.4277 0.3812 0.4314 0.0308  -0.0039 0.1126  410 LEU A O   
1181 C CB  . LEU A 146 ? 0.4575 0.4431 0.4339 0.0298  -0.0279 0.1064  410 LEU A CB  
1182 C CG  . LEU A 146 ? 0.5628 0.5646 0.5265 0.0337  -0.0350 0.1124  410 LEU A CG  
1183 C CD1 . LEU A 146 ? 0.6229 0.6402 0.5893 0.0366  -0.0432 0.1142  410 LEU A CD1 
1184 C CD2 . LEU A 146 ? 0.6259 0.6284 0.5760 0.0274  -0.0390 0.1023  410 LEU A CD2 
1185 N N   . HIS A 147 ? 0.4054 0.3632 0.4122 0.0259  -0.0121 0.0987  411 HIS A N   
1186 C CA  . HIS A 147 ? 0.3580 0.2992 0.3712 0.0199  -0.0034 0.0909  411 HIS A CA  
1187 C C   . HIS A 147 ? 0.3711 0.3072 0.3773 0.0136  -0.0021 0.0856  411 HIS A C   
1188 O O   . HIS A 147 ? 0.3954 0.3197 0.4079 0.0117  0.0072  0.0867  411 HIS A O   
1189 C CB  . HIS A 147 ? 0.3856 0.3159 0.4134 0.0245  0.0088  0.0991  411 HIS A CB  
1190 C CG  . HIS A 147 ? 0.4916 0.4260 0.5291 0.0304  0.0090  0.1042  411 HIS A CG  
1191 N ND1 . HIS A 147 ? 0.5940 0.5422 0.6349 0.0397  0.0054  0.1182  411 HIS A ND1 
1192 C CD2 . HIS A 147 ? 0.5691 0.4977 0.6132 0.0281  0.0115  0.0974  411 HIS A CD2 
1193 C CE1 . HIS A 147 ? 0.5796 0.5302 0.6310 0.0430  0.0060  0.1203  411 HIS A CE1 
1194 N NE2 . HIS A 147 ? 0.5742 0.5119 0.6276 0.0363  0.0103  0.1077  411 HIS A NE2 
1195 N N   . PHE A 148 ? 0.3477 0.2927 0.3424 0.0105  -0.0108 0.0807  412 PHE A N   
1196 C CA  . PHE A 148 ? 0.3301 0.2721 0.3192 0.0047  -0.0100 0.0764  412 PHE A CA  
1197 C C   . PHE A 148 ? 0.3931 0.3234 0.3889 -0.0028 -0.0035 0.0688  412 PHE A C   
1198 O O   . PHE A 148 ? 0.3963 0.3241 0.3945 -0.0070 -0.0038 0.0607  412 PHE A O   
1199 C CB  . PHE A 148 ? 0.3769 0.3280 0.3563 0.0008  -0.0186 0.0692  412 PHE A CB  
1200 C CG  . PHE A 148 ? 0.4482 0.4097 0.4176 0.0048  -0.0240 0.0737  412 PHE A CG  
1201 C CD1 . PHE A 148 ? 0.5128 0.4741 0.4777 0.0084  -0.0211 0.0819  412 PHE A CD1 
1202 C CD2 . PHE A 148 ? 0.5131 0.4842 0.4770 0.0042  -0.0316 0.0686  412 PHE A CD2 
1203 C CE1 . PHE A 148 ? 0.5412 0.5124 0.4944 0.0111  -0.0260 0.0846  412 PHE A CE1 
1204 C CE2 . PHE A 148 ? 0.5631 0.5435 0.5170 0.0062  -0.0361 0.0704  412 PHE A CE2 
1205 C CZ  . PHE A 148 ? 0.5563 0.5368 0.5036 0.0096  -0.0335 0.0781  412 PHE A CZ  
1206 N N   . SER A 149 ? 0.3530 0.2770 0.3512 -0.0054 0.0023  0.0706  413 SER A N   
1207 C CA  . SER A 149 ? 0.3354 0.2528 0.3374 -0.0151 0.0056  0.0611  413 SER A CA  
1208 C C   . SER A 149 ? 0.3642 0.2910 0.3584 -0.0205 -0.0024 0.0546  413 SER A C   
1209 O O   . SER A 149 ? 0.3741 0.3095 0.3606 -0.0170 -0.0082 0.0579  413 SER A O   
1210 C CB  . SER A 149 ? 0.3542 0.2626 0.3636 -0.0169 0.0146  0.0647  413 SER A CB  
1211 O OG  . SER A 149 ? 0.3675 0.2815 0.3715 -0.0147 0.0123  0.0708  413 SER A OG  
1212 N N   . GLU A 150 ? 0.3437 0.2691 0.3402 -0.0295 -0.0018 0.0456  414 GLU A N   
1213 C CA  . GLU A 150 ? 0.3390 0.2746 0.3303 -0.0345 -0.0085 0.0414  414 GLU A CA  
1214 C C   . GLU A 150 ? 0.3355 0.2740 0.3259 -0.0333 -0.0082 0.0477  414 GLU A C   
1215 O O   . GLU A 150 ? 0.3751 0.3223 0.3600 -0.0323 -0.0132 0.0489  414 GLU A O   
1216 C CB  . GLU A 150 ? 0.3821 0.3181 0.3762 -0.0445 -0.0080 0.0320  414 GLU A CB  
1217 C CG  . GLU A 150 ? 0.3602 0.2949 0.3526 -0.0464 -0.0087 0.0246  414 GLU A CG  
1218 C CD  . GLU A 150 ? 0.3595 0.3042 0.3455 -0.0426 -0.0160 0.0248  414 GLU A CD  
1219 O OE1 . GLU A 150 ? 0.4361 0.3905 0.4194 -0.0474 -0.0203 0.0212  414 GLU A OE1 
1220 O OE2 . GLU A 150 ? 0.3917 0.3355 0.3766 -0.0352 -0.0170 0.0287  414 GLU A OE2 
1221 N N   . ASP A 151 ? 0.3540 0.2847 0.3507 -0.0334 -0.0011 0.0520  415 ASP A N   
1222 C CA  . ASP A 151 ? 0.3135 0.2462 0.3098 -0.0320 0.0003  0.0586  415 ASP A CA  
1223 C C   . ASP A 151 ? 0.3269 0.2630 0.3137 -0.0229 -0.0020 0.0664  415 ASP A C   
1224 O O   . ASP A 151 ? 0.3395 0.2814 0.3208 -0.0220 -0.0042 0.0687  415 ASP A O   
1225 C CB  . ASP A 151 ? 0.3688 0.2914 0.3753 -0.0336 0.0096  0.0619  415 ASP A CB  
1226 C CG  . ASP A 151 ? 0.4279 0.3494 0.4436 -0.0450 0.0116  0.0532  415 ASP A CG  
1227 O OD1 . ASP A 151 ? 0.4573 0.3878 0.4706 -0.0514 0.0051  0.0461  415 ASP A OD1 
1228 O OD2 . ASP A 151 ? 0.4804 0.3924 0.5064 -0.0477 0.0200  0.0536  415 ASP A OD2 
1229 N N   . GLU A 152 ? 0.3398 0.2736 0.3248 -0.0162 -0.0014 0.0703  416 GLU A N   
1230 C CA  . GLU A 152 ? 0.3515 0.2915 0.3262 -0.0086 -0.0051 0.0765  416 GLU A CA  
1231 C C   . GLU A 152 ? 0.3177 0.2673 0.2844 -0.0099 -0.0131 0.0707  416 GLU A C   
1232 O O   . GLU A 152 ? 0.3308 0.2855 0.2887 -0.0073 -0.0151 0.0731  416 GLU A O   
1233 C CB  . GLU A 152 ? 0.3475 0.2860 0.3239 -0.0015 -0.0036 0.0825  416 GLU A CB  
1234 C CG  . GLU A 152 ? 0.3598 0.2894 0.3440 0.0024  0.0062  0.0918  416 GLU A CG  
1235 C CD  . GLU A 152 ? 0.4234 0.3490 0.4157 0.0078  0.0104  0.0970  416 GLU A CD  
1236 O OE1 . GLU A 152 ? 0.3865 0.3161 0.3786 0.0084  0.0055  0.0933  416 GLU A OE1 
1237 O OE2 . GLU A 152 ? 0.4077 0.3258 0.4082 0.0118  0.0197  0.1056  416 GLU A OE2 
1238 N N   . ILE A 153 ? 0.3020 0.2535 0.2714 -0.0135 -0.0168 0.0631  417 ILE A N   
1239 C CA  . ILE A 153 ? 0.3295 0.2892 0.2939 -0.0150 -0.0228 0.0578  417 ILE A CA  
1240 C C   . ILE A 153 ? 0.3575 0.3204 0.3206 -0.0187 -0.0221 0.0571  417 ILE A C   
1241 O O   . ILE A 153 ? 0.3467 0.3147 0.3036 -0.0172 -0.0241 0.0569  417 ILE A O   
1242 C CB  . ILE A 153 ? 0.3616 0.3218 0.3306 -0.0184 -0.0250 0.0507  417 ILE A CB  
1243 C CG1 . ILE A 153 ? 0.4431 0.4020 0.4131 -0.0133 -0.0259 0.0523  417 ILE A CG1 
1244 C CG2 . ILE A 153 ? 0.4426 0.4108 0.4094 -0.0210 -0.0291 0.0457  417 ILE A CG2 
1245 C CD1 . ILE A 153 ? 0.5246 0.4842 0.4981 -0.0150 -0.0279 0.0460  417 ILE A CD1 
1246 N N   . ALA A 154 ? 0.3102 0.2702 0.2802 -0.0238 -0.0188 0.0570  418 ALA A N   
1247 C CA  . ALA A 154 ? 0.2643 0.2285 0.2360 -0.0271 -0.0177 0.0581  418 ALA A CA  
1248 C C   . ALA A 154 ? 0.3143 0.2772 0.2796 -0.0224 -0.0148 0.0643  418 ALA A C   
1249 O O   . ALA A 154 ? 0.3208 0.2882 0.2826 -0.0221 -0.0148 0.0644  418 ALA A O   
1250 C CB  . ALA A 154 ? 0.3153 0.2774 0.2967 -0.0335 -0.0146 0.0576  418 ALA A CB  
1251 N N   . LEU A 155 ? 0.2929 0.2494 0.2570 -0.0187 -0.0108 0.0699  419 LEU A N   
1252 C CA  . LEU A 155 ? 0.2816 0.2367 0.2385 -0.0142 -0.0071 0.0765  419 LEU A CA  
1253 C C   . LEU A 155 ? 0.3507 0.3107 0.2945 -0.0097 -0.0108 0.0755  419 LEU A C   
1254 O O   . LEU A 155 ? 0.3499 0.3114 0.2862 -0.0087 -0.0090 0.0764  419 LEU A O   
1255 C CB  . LEU A 155 ? 0.3195 0.2674 0.2789 -0.0106 -0.0013 0.0839  419 LEU A CB  
1256 C CG  . LEU A 155 ? 0.3541 0.2965 0.3272 -0.0159 0.0037  0.0842  419 LEU A CG  
1257 C CD1 . LEU A 155 ? 0.3721 0.3059 0.3513 -0.0128 0.0099  0.0895  419 LEU A CD1 
1258 C CD2 . LEU A 155 ? 0.3536 0.2968 0.3288 -0.0175 0.0078  0.0879  419 LEU A CD2 
1259 N N   . TYR A 156 ? 0.3275 0.2899 0.2693 -0.0074 -0.0155 0.0734  420 TYR A N   
1260 C CA  . TYR A 156 ? 0.3220 0.2909 0.2527 -0.0043 -0.0200 0.0716  420 TYR A CA  
1261 C C   . TYR A 156 ? 0.3218 0.2949 0.2511 -0.0081 -0.0221 0.0640  420 TYR A C   
1262 O O   . TYR A 156 ? 0.3260 0.3020 0.2457 -0.0073 -0.0216 0.0625  420 TYR A O   
1263 C CB  . TYR A 156 ? 0.3029 0.2748 0.2349 -0.0013 -0.0246 0.0716  420 TYR A CB  
1264 C CG  . TYR A 156 ? 0.3616 0.3427 0.2833 0.0014  -0.0301 0.0700  420 TYR A CG  
1265 C CD1 . TYR A 156 ? 0.4100 0.3951 0.3201 0.0058  -0.0298 0.0760  420 TYR A CD1 
1266 C CD2 . TYR A 156 ? 0.4194 0.4059 0.3431 -0.0009 -0.0355 0.0625  420 TYR A CD2 
1267 C CE1 . TYR A 156 ? 0.4541 0.4499 0.3538 0.0070  -0.0358 0.0735  420 TYR A CE1 
1268 C CE2 . TYR A 156 ? 0.4132 0.4094 0.3287 0.0004  -0.0408 0.0599  420 TYR A CE2 
1269 C CZ  . TYR A 156 ? 0.4583 0.4595 0.3616 0.0039  -0.0413 0.0650  420 TYR A CZ  
1270 O OH  . TYR A 156 ? 0.4446 0.4574 0.3391 0.0039  -0.0474 0.0615  420 TYR A OH  
1271 N N   . THR A 157 ? 0.2957 0.2694 0.2347 -0.0123 -0.0234 0.0593  421 THR A N   
1272 C CA  . THR A 157 ? 0.2845 0.2626 0.2241 -0.0150 -0.0239 0.0537  421 THR A CA  
1273 C C   . THR A 157 ? 0.3322 0.3090 0.2720 -0.0164 -0.0181 0.0562  421 THR A C   
1274 O O   . THR A 157 ? 0.3153 0.2941 0.2527 -0.0170 -0.0161 0.0530  421 THR A O   
1275 C CB  . THR A 157 ? 0.2917 0.2725 0.2410 -0.0184 -0.0264 0.0495  421 THR A CB  
1276 O OG1 . THR A 157 ? 0.3195 0.2979 0.2761 -0.0214 -0.0247 0.0520  421 THR A OG1 
1277 C CG2 . THR A 157 ? 0.3120 0.2937 0.2612 -0.0165 -0.0313 0.0465  421 THR A CG2 
1278 N N   . ALA A 158 ? 0.3034 0.2763 0.2474 -0.0170 -0.0143 0.0619  422 ALA A N   
1279 C CA  . ALA A 158 ? 0.2916 0.2632 0.2364 -0.0176 -0.0078 0.0656  422 ALA A CA  
1280 C C   . ALA A 158 ? 0.3372 0.3063 0.2682 -0.0141 -0.0046 0.0659  422 ALA A C   
1281 O O   . ALA A 158 ? 0.3302 0.2991 0.2593 -0.0148 0.0003  0.0645  422 ALA A O   
1282 C CB  . ALA A 158 ? 0.3587 0.3269 0.3115 -0.0190 -0.0043 0.0718  422 ALA A CB  
1283 N N   . LEU A 159 ? 0.3380 0.3061 0.2592 -0.0105 -0.0069 0.0676  423 LEU A N   
1284 C CA  . LEU A 159 ? 0.3363 0.3043 0.2417 -0.0075 -0.0050 0.0677  423 LEU A CA  
1285 C C   . LEU A 159 ? 0.3558 0.3290 0.2542 -0.0091 -0.0085 0.0587  423 LEU A C   
1286 O O   . LEU A 159 ? 0.3895 0.3627 0.2755 -0.0091 -0.0053 0.0557  423 LEU A O   
1287 C CB  . LEU A 159 ? 0.3563 0.3246 0.2542 -0.0026 -0.0071 0.0739  423 LEU A CB  
1288 C CG  . LEU A 159 ? 0.3563 0.3178 0.2587 -0.0005 -0.0003 0.0831  423 LEU A CG  
1289 C CD1 . LEU A 159 ? 0.4037 0.3649 0.3055 0.0045  -0.0015 0.0905  423 LEU A CD1 
1290 C CD2 . LEU A 159 ? 0.4182 0.3763 0.3101 0.0010  0.0073  0.0860  423 LEU A CD2 
1291 N N   . VAL A 160 ? 0.3209 0.2983 0.2267 -0.0108 -0.0146 0.0539  424 VAL A N   
1292 C CA  . VAL A 160 ? 0.3248 0.3070 0.2272 -0.0129 -0.0170 0.0449  424 VAL A CA  
1293 C C   . VAL A 160 ? 0.3300 0.3088 0.2359 -0.0158 -0.0091 0.0417  424 VAL A C   
1294 O O   . VAL A 160 ? 0.3158 0.2948 0.2140 -0.0175 -0.0061 0.0351  424 VAL A O   
1295 C CB  . VAL A 160 ? 0.3365 0.3232 0.2486 -0.0139 -0.0236 0.0410  424 VAL A CB  
1296 C CG1 . VAL A 160 ? 0.3698 0.3600 0.2832 -0.0169 -0.0237 0.0317  424 VAL A CG1 
1297 C CG2 . VAL A 160 ? 0.3042 0.2946 0.2133 -0.0106 -0.0303 0.0440  424 VAL A CG2 
1298 N N   . LEU A 161 ? 0.3088 0.2850 0.2271 -0.0166 -0.0053 0.0465  425 LEU A N   
1299 C CA  . LEU A 161 ? 0.2842 0.2586 0.2098 -0.0185 0.0030  0.0460  425 LEU A CA  
1300 C C   . LEU A 161 ? 0.3656 0.3338 0.2838 -0.0176 0.0118  0.0494  425 LEU A C   
1301 O O   . LEU A 161 ? 0.3644 0.3295 0.2805 -0.0187 0.0196  0.0455  425 LEU A O   
1302 C CB  . LEU A 161 ? 0.3229 0.3002 0.2654 -0.0198 0.0033  0.0514  425 LEU A CB  
1303 C CG  . LEU A 161 ? 0.3517 0.3348 0.3024 -0.0210 -0.0028 0.0481  425 LEU A CG  
1304 C CD1 . LEU A 161 ? 0.3804 0.3683 0.3445 -0.0227 -0.0033 0.0538  425 LEU A CD1 
1305 C CD2 . LEU A 161 ? 0.3455 0.3298 0.2985 -0.0217 0.0007  0.0420  425 LEU A CD2 
1306 N N   . ILE A 162 ? 0.2939 0.3230 0.2690 -0.0002 -0.0400 0.0360  426 ILE A N   
1307 C CA  . ILE A 162 ? 0.3199 0.3507 0.2932 0.0058  -0.0310 0.0411  426 ILE A CA  
1308 C C   . ILE A 162 ? 0.3399 0.3610 0.2925 0.0077  -0.0289 0.0394  426 ILE A C   
1309 O O   . ILE A 162 ? 0.3464 0.3696 0.2978 0.0073  -0.0285 0.0439  426 ILE A O   
1310 C CB  . ILE A 162 ? 0.2763 0.3205 0.2702 0.0049  -0.0289 0.0488  426 ILE A CB  
1311 C CG1 . ILE A 162 ? 0.2837 0.3363 0.2947 0.0019  -0.0356 0.0491  426 ILE A CG1 
1312 C CG2 . ILE A 162 ? 0.3465 0.3928 0.3433 0.0114  -0.0163 0.0549  426 ILE A CG2 
1313 C CD1 . ILE A 162 ? 0.3527 0.4043 0.3649 0.0077  -0.0342 0.0489  426 ILE A CD1 
1314 N N   . ASN A 163 ? 0.3273 0.3358 0.2619 0.0097  -0.0283 0.0328  427 ASN A N   
1315 C CA  . ASN A 163 ? 0.3800 0.3763 0.2900 0.0106  -0.0304 0.0284  427 ASN A CA  
1316 C C   . ASN A 163 ? 0.4046 0.3872 0.2955 0.0172  -0.0193 0.0266  427 ASN A C   
1317 O O   . ASN A 163 ? 0.3877 0.3627 0.2762 0.0177  -0.0173 0.0210  427 ASN A O   
1318 C CB  . ASN A 163 ? 0.4311 0.4237 0.3393 0.0046  -0.0421 0.0194  427 ASN A CB  
1319 C CG  . ASN A 163 ? 0.4490 0.4300 0.3331 0.0045  -0.0486 0.0131  427 ASN A CG  
1320 O OD1 . ASN A 163 ? 0.4843 0.4543 0.3452 0.0098  -0.0430 0.0139  427 ASN A OD1 
1321 N ND2 . ASN A 163 ? 0.4732 0.4560 0.3631 -0.0014 -0.0607 0.0067  427 ASN A ND2 
1322 N N   . ALA A 164 ? 0.3840 0.3611 0.2608 0.0226  -0.0102 0.0319  428 ALA A N   
1323 C CA  . ALA A 164 ? 0.4271 0.3903 0.2871 0.0302  0.0047  0.0318  428 ALA A CA  
1324 C C   . ALA A 164 ? 0.5053 0.4459 0.3304 0.0304  0.0016  0.0210  428 ALA A C   
1325 O O   . ALA A 164 ? 0.5267 0.4504 0.3317 0.0365  0.0143  0.0188  428 ALA A O   
1326 C CB  . ALA A 164 ? 0.4622 0.4249 0.3184 0.0360  0.0185  0.0415  428 ALA A CB  
1327 N N   . HIS A 165 ? 0.4713 0.4114 0.2908 0.0235  -0.0152 0.0137  429 HIS A N   
1328 C CA  . HIS A 165 ? 0.5312 0.4516 0.3205 0.0216  -0.0221 0.0019  429 HIS A CA  
1329 C C   . HIS A 165 ? 0.5257 0.4407 0.3229 0.0170  -0.0242 -0.0079 429 HIS A C   
1330 O O   . HIS A 165 ? 0.5873 0.4840 0.3613 0.0146  -0.0283 -0.0189 429 HIS A O   
1331 C CB  . HIS A 165 ? 0.5672 0.4900 0.3476 0.0170  -0.0404 -0.0008 429 HIS A CB  
1332 C CG  . HIS A 165 ? 0.6383 0.5621 0.4066 0.0221  -0.0381 0.0094  429 HIS A CG  
1333 N ND1 . HIS A 165 ? 0.7479 0.6510 0.4762 0.0286  -0.0324 0.0099  429 HIS A ND1 
1334 C CD2 . HIS A 165 ? 0.6872 0.6276 0.4768 0.0220  -0.0388 0.0197  429 HIS A CD2 
1335 C CE1 . HIS A 165 ? 0.7858 0.6929 0.5114 0.0325  -0.0295 0.0210  429 HIS A CE1 
1336 N NE2 . HIS A 165 ? 0.7558 0.6857 0.5198 0.0283  -0.0333 0.0269  429 HIS A NE2 
1337 N N   . ARG A 166 ? 0.4493 0.3772 0.2762 0.0158  -0.0210 -0.0041 430 ARG A N   
1338 C CA  . ARG A 166 ? 0.4318 0.3525 0.2655 0.0122  -0.0209 -0.0116 430 ARG A CA  
1339 C C   . ARG A 166 ? 0.4851 0.3837 0.2972 0.0180  -0.0077 -0.0162 430 ARG A C   
1340 O O   . ARG A 166 ? 0.5106 0.4072 0.3195 0.0268  0.0064  -0.0091 430 ARG A O   
1341 C CB  . ARG A 166 ? 0.3859 0.3211 0.2492 0.0123  -0.0181 -0.0048 430 ARG A CB  
1342 C CG  . ARG A 166 ? 0.3918 0.3468 0.2760 0.0078  -0.0275 0.0007  430 ARG A CG  
1343 C CD  . ARG A 166 ? 0.4057 0.3616 0.2940 -0.0010 -0.0400 -0.0069 430 ARG A CD  
1344 N NE  . ARG A 166 ? 0.3755 0.3467 0.2865 -0.0048 -0.0450 -0.0022 430 ARG A NE  
1345 C CZ  . ARG A 166 ? 0.4253 0.4015 0.3474 -0.0114 -0.0541 -0.0061 430 ARG A CZ  
1346 N NH1 . ARG A 166 ? 0.4455 0.4156 0.3613 -0.0158 -0.0619 -0.0149 430 ARG A NH1 
1347 N NH2 . ARG A 166 ? 0.3803 0.3672 0.3207 -0.0138 -0.0555 -0.0016 430 ARG A NH2 
1348 N N   . PRO A 167 ? 0.5557 0.4368 0.3549 0.0127  -0.0112 -0.0284 431 PRO A N   
1349 C CA  . PRO A 167 ? 0.5859 0.4419 0.3625 0.0180  0.0025  -0.0340 431 PRO A CA  
1350 C C   . PRO A 167 ? 0.5167 0.3737 0.3114 0.0252  0.0171  -0.0268 431 PRO A C   
1351 O O   . PRO A 167 ? 0.5217 0.3914 0.3416 0.0226  0.0136  -0.0228 431 PRO A O   
1352 C CB  . PRO A 167 ? 0.6022 0.4412 0.3671 0.0081  -0.0072 -0.0497 431 PRO A CB  
1353 C CG  . PRO A 167 ? 0.6388 0.4938 0.4113 -0.0004 -0.0274 -0.0519 431 PRO A CG  
1354 C CD  . PRO A 167 ? 0.5186 0.4006 0.3217 0.0017  -0.0276 -0.0385 431 PRO A CD  
1355 N N   . GLY A 168 ? 0.5629 0.4049 0.3433 0.0350  0.0339  -0.0248 432 GLY A N   
1356 C CA  . GLY A 168 ? 0.5760 0.4171 0.3731 0.0436  0.0478  -0.0178 432 GLY A CA  
1357 C C   . GLY A 168 ? 0.5350 0.3992 0.3575 0.0526  0.0543  -0.0025 432 GLY A C   
1358 O O   . GLY A 168 ? 0.5248 0.3914 0.3645 0.0606  0.0633  0.0045  432 GLY A O   
1359 N N   . LEU A 169 ? 0.5205 0.4019 0.3476 0.0511  0.0491  0.0031  433 LEU A N   
1360 C CA  . LEU A 169 ? 0.4723 0.3759 0.3268 0.0583  0.0556  0.0169  433 LEU A CA  
1361 C C   . LEU A 169 ? 0.4749 0.3669 0.3238 0.0703  0.0769  0.0209  433 LEU A C   
1362 O O   . LEU A 169 ? 0.5538 0.4237 0.3706 0.0721  0.0860  0.0149  433 LEU A O   
1363 C CB  . LEU A 169 ? 0.4136 0.3342 0.2729 0.0538  0.0479  0.0215  433 LEU A CB  
1364 C CG  . LEU A 169 ? 0.4312 0.3665 0.3023 0.0433  0.0287  0.0197  433 LEU A CG  
1365 C CD1 . LEU A 169 ? 0.4268 0.3736 0.2983 0.0399  0.0233  0.0239  433 LEU A CD1 
1366 C CD2 . LEU A 169 ? 0.4123 0.3647 0.3140 0.0437  0.0243  0.0260  433 LEU A CD2 
1367 N N   . GLN A 170 ? 0.4961 0.4027 0.3760 0.0790  0.0850  0.0315  434 GLN A N   
1368 C CA  . GLN A 170 ? 0.5082 0.4075 0.3912 0.0917  0.1076  0.0373  434 GLN A CA  
1369 C C   . GLN A 170 ? 0.5386 0.4553 0.4384 0.0948  0.1160  0.0472  434 GLN A C   
1370 O O   . GLN A 170 ? 0.5930 0.4985 0.4862 0.1039  0.1375  0.0504  434 GLN A O   
1371 C CB  . GLN A 170 ? 0.5363 0.4423 0.4475 0.1012  0.1126  0.0444  434 GLN A CB  
1372 C CG  . GLN A 170 ? 0.6355 0.5162 0.5258 0.1005  0.1119  0.0353  434 GLN A CG  
1373 C CD  . GLN A 170 ? 0.7575 0.6432 0.6732 0.1104  0.1147  0.0435  434 GLN A CD  
1374 O OE1 . GLN A 170 ? 0.8152 0.7271 0.7667 0.1170  0.1131  0.0559  434 GLN A OE1 
1375 N NE2 . GLN A 170 ? 0.7827 0.6429 0.6804 0.1112  0.1181  0.0367  434 GLN A NE2 
1376 N N   . GLU A 171 ? 0.4558 0.3982 0.3781 0.0874  0.1012  0.0521  435 GLU A N   
1377 C CA  . GLU A 171 ? 0.4770 0.4373 0.4204 0.0885  0.1083  0.0618  435 GLU A CA  
1378 C C   . GLU A 171 ? 0.4621 0.4235 0.3882 0.0780  0.0960  0.0586  435 GLU A C   
1379 O O   . GLU A 171 ? 0.4378 0.4214 0.3883 0.0714  0.0836  0.0630  435 GLU A O   
1380 C CB  . GLU A 171 ? 0.5402 0.5328 0.5352 0.0904  0.1030  0.0724  435 GLU A CB  
1381 C CG  . GLU A 171 ? 0.5529 0.5482 0.5719 0.1035  0.1176  0.0789  435 GLU A CG  
1382 C CD  . GLU A 171 ? 0.6044 0.6326 0.6741 0.1050  0.1065  0.0886  435 GLU A CD  
1383 O OE1 . GLU A 171 ? 0.6194 0.6618 0.6970 0.0959  0.0846  0.0874  435 GLU A OE1 
1384 O OE2 . GLU A 171 ? 0.6833 0.7227 0.7851 0.1159  0.1198  0.0974  435 GLU A OE2 
1385 N N   . LYS A 172 ? 0.4841 0.4197 0.3665 0.0768  0.0988  0.0506  436 LYS A N   
1386 C CA  . LYS A 172 ? 0.5250 0.4597 0.3882 0.0677  0.0840  0.0469  436 LYS A CA  
1387 C C   . LYS A 172 ? 0.5065 0.4571 0.3880 0.0671  0.0890  0.0576  436 LYS A C   
1388 O O   . LYS A 172 ? 0.4306 0.3943 0.3211 0.0592  0.0742  0.0588  436 LYS A O   
1389 C CB  . LYS A 172 ? 0.6273 0.5305 0.4388 0.0680  0.0855  0.0369  436 LYS A CB  
1390 C CG  . LYS A 172 ? 0.6219 0.5240 0.4135 0.0598  0.0678  0.0332  436 LYS A CG  
1391 C CD  . LYS A 172 ? 0.6656 0.5366 0.4045 0.0613  0.0685  0.0243  436 LYS A CD  
1392 C CE  . LYS A 172 ? 0.6768 0.5489 0.3987 0.0548  0.0492  0.0224  436 LYS A CE  
1393 N NZ  . LYS A 172 ? 0.7695 0.6119 0.4401 0.0547  0.0430  0.0111  436 LYS A NZ  
1394 N N   . ARG A 173 ? 0.5445 0.4928 0.4333 0.0756  0.1114  0.0656  437 ARG A N   
1395 C CA  . ARG A 173 ? 0.5770 0.5375 0.4841 0.0752  0.1206  0.0762  437 ARG A CA  
1396 C C   . ARG A 173 ? 0.4750 0.4678 0.4296 0.0678  0.1063  0.0813  437 ARG A C   
1397 O O   . ARG A 173 ? 0.4628 0.4639 0.4243 0.0615  0.1009  0.0851  437 ARG A O   
1398 C CB  . ARG A 173 ? 0.6653 0.6210 0.5829 0.0860  0.1498  0.0844  437 ARG A CB  
1399 C CG  . ARG A 173 ? 0.7961 0.7459 0.7061 0.0870  0.1657  0.0929  437 ARG A CG  
1400 C CD  . ARG A 173 ? 0.8964 0.8630 0.8523 0.0926  0.1889  0.1050  437 ARG A CD  
1401 N NE  . ARG A 173 ? 0.9765 0.9480 0.9415 0.0885  0.1963  0.1139  437 ARG A NE  
1402 C CZ  . ARG A 173 ? 1.0493 0.9971 0.9851 0.0943  0.2202  0.1196  437 ARG A CZ  
1403 N NH1 . ARG A 173 ? 1.1280 1.0456 1.0227 0.1045  0.2389  0.1165  437 ARG A NH1 
1404 N NH2 . ARG A 173 ? 1.0233 0.9751 0.9690 0.0901  0.2267  0.1283  437 ARG A NH2 
1405 N N   . LYS A 174 ? 0.3989 0.4076 0.3845 0.0692  0.1009  0.0815  438 LYS A N   
1406 C CA  . LYS A 174 ? 0.3833 0.4207 0.4111 0.0626  0.0857  0.0852  438 LYS A CA  
1407 C C   . LYS A 174 ? 0.3568 0.3948 0.3715 0.0519  0.0638  0.0789  438 LYS A C   
1408 O O   . LYS A 174 ? 0.3796 0.4333 0.4157 0.0446  0.0554  0.0822  438 LYS A O   
1409 C CB  . LYS A 174 ? 0.3678 0.4160 0.4197 0.0677  0.0816  0.0858  438 LYS A CB  
1410 C CG  . LYS A 174 ? 0.4956 0.5742 0.5960 0.0645  0.0711  0.0923  438 LYS A CG  
1411 C CD  . LYS A 174 ? 0.5823 0.6723 0.7135 0.0752  0.0782  0.0982  438 LYS A CD  
1412 C CE  . LYS A 174 ? 0.6380 0.7607 0.8220 0.0723  0.0677  0.1055  438 LYS A CE  
1413 N NZ  . LYS A 174 ? 0.6355 0.7727 0.8555 0.0840  0.0741  0.1130  438 LYS A NZ  
1414 N N   . VAL A 175 ? 0.3288 0.3494 0.3104 0.0507  0.0555  0.0696  439 VAL A N   
1415 C CA  . VAL A 175 ? 0.3039 0.3258 0.2773 0.0414  0.0363  0.0638  439 VAL A CA  
1416 C C   . VAL A 175 ? 0.3584 0.3753 0.3167 0.0378  0.0365  0.0657  439 VAL A C   
1417 O O   . VAL A 175 ? 0.3546 0.3811 0.3234 0.0305  0.0251  0.0663  439 VAL A O   
1418 C CB  . VAL A 175 ? 0.3650 0.3707 0.3126 0.0405  0.0284  0.0535  439 VAL A CB  
1419 C CG1 . VAL A 175 ? 0.3386 0.3487 0.2858 0.0312  0.0108  0.0488  439 VAL A CG1 
1420 C CG2 . VAL A 175 ? 0.3896 0.3965 0.3499 0.0460  0.0313  0.0533  439 VAL A CG2 
1421 N N   . GLU A 176 ? 0.3709 0.3704 0.3022 0.0437  0.0502  0.0669  440 GLU A N   
1422 C CA  . GLU A 176 ? 0.3991 0.3905 0.3115 0.0424  0.0519  0.0705  440 GLU A CA  
1423 C C   . GLU A 176 ? 0.3957 0.4048 0.3415 0.0389  0.0561  0.0801  440 GLU A C   
1424 O O   . GLU A 176 ? 0.3839 0.3937 0.3270 0.0341  0.0490  0.0821  440 GLU A O   
1425 C CB  . GLU A 176 ? 0.4567 0.4240 0.3326 0.0509  0.0692  0.0717  440 GLU A CB  
1426 C CG  . GLU A 176 ? 0.5593 0.5043 0.3940 0.0523  0.0620  0.0604  440 GLU A CG  
1427 C CD  . GLU A 176 ? 0.7530 0.6698 0.5452 0.0607  0.0789  0.0605  440 GLU A CD  
1428 O OE1 . GLU A 176 ? 0.7676 0.6829 0.5672 0.0670  0.1008  0.0696  440 GLU A OE1 
1429 O OE2 . GLU A 176 ? 0.8538 0.7492 0.6050 0.0608  0.0704  0.0510  440 GLU A OE2 
1430 N N   . GLN A 177 ? 0.3905 0.4135 0.3694 0.0415  0.0679  0.0862  441 GLN A N   
1431 C CA  . GLN A 177 ? 0.4205 0.4610 0.4360 0.0370  0.0727  0.0947  441 GLN A CA  
1432 C C   . GLN A 177 ? 0.3933 0.4497 0.4301 0.0271  0.0522  0.0914  441 GLN A C   
1433 O O   . GLN A 177 ? 0.3736 0.4345 0.4214 0.0208  0.0500  0.0949  441 GLN A O   
1434 C CB  . GLN A 177 ? 0.4608 0.5160 0.5137 0.0417  0.0881  0.1014  441 GLN A CB  
1435 C CG  . GLN A 177 ? 0.7798 0.8187 0.8167 0.0514  0.1147  0.1072  441 GLN A CG  
1436 C CD  . GLN A 177 ? 1.0145 1.0368 1.0265 0.0508  0.1253  0.1126  441 GLN A CD  
1437 O OE1 . GLN A 177 ? 1.0273 1.0605 1.0629 0.0440  0.1243  0.1180  441 GLN A OE1 
1438 N NE2 . GLN A 177 ? 1.1328 1.1264 1.0944 0.0581  0.1349  0.1108  441 GLN A NE2 
1439 N N   . LEU A 178 ? 0.2987 0.3611 0.3400 0.0260  0.0386  0.0848  442 LEU A N   
1440 C CA  . LEU A 178 ? 0.2746 0.3477 0.3298 0.0173  0.0202  0.0809  442 LEU A CA  
1441 C C   . LEU A 178 ? 0.3210 0.3824 0.3515 0.0127  0.0117  0.0770  442 LEU A C   
1442 O O   . LEU A 178 ? 0.2962 0.3629 0.3382 0.0056  0.0044  0.0775  442 LEU A O   
1443 C CB  . LEU A 178 ? 0.2609 0.3369 0.3174 0.0186  0.0097  0.0753  442 LEU A CB  
1444 C CG  . LEU A 178 ? 0.3255 0.4100 0.3938 0.0106  -0.0074 0.0716  442 LEU A CG  
1445 C CD1 . LEU A 178 ? 0.3681 0.4678 0.4670 0.0041  -0.0092 0.0762  442 LEU A CD1 
1446 C CD2 . LEU A 178 ? 0.4028 0.4904 0.4753 0.0138  -0.0148 0.0690  442 LEU A CD2 
1447 N N   . GLN A 179 ? 0.3235 0.3686 0.3210 0.0168  0.0116  0.0726  443 GLN A N   
1448 C CA  . GLN A 179 ? 0.3009 0.3369 0.2781 0.0136  0.0022  0.0694  443 GLN A CA  
1449 C C   . GLN A 179 ? 0.3329 0.3663 0.3096 0.0130  0.0086  0.0771  443 GLN A C   
1450 O O   . GLN A 179 ? 0.3311 0.3652 0.3104 0.0084  0.0004  0.0772  443 GLN A O   
1451 C CB  . GLN A 179 ? 0.3432 0.3627 0.2867 0.0181  0.0006  0.0633  443 GLN A CB  
1452 C CG  . GLN A 179 ? 0.3472 0.3598 0.2734 0.0153  -0.0118 0.0599  443 GLN A CG  
1453 C CD  . GLN A 179 ? 0.4590 0.4563 0.3535 0.0186  -0.0161 0.0527  443 GLN A CD  
1454 O OE1 . GLN A 179 ? 0.4242 0.4151 0.3104 0.0212  -0.0117 0.0479  443 GLN A OE1 
1455 N NE2 . GLN A 179 ? 0.5414 0.5318 0.4181 0.0185  -0.0256 0.0519  443 GLN A NE2 
1456 N N   . TYR A 180 ? 0.3268 0.3544 0.2981 0.0187  0.0252  0.0841  444 TYR A N   
1457 C CA  . TYR A 180 ? 0.3119 0.3326 0.2788 0.0195  0.0354  0.0931  444 TYR A CA  
1458 C C   . TYR A 180 ? 0.3585 0.3942 0.3617 0.0111  0.0329  0.0965  444 TYR A C   
1459 O O   . TYR A 180 ? 0.3493 0.3800 0.3499 0.0082  0.0307  0.0998  444 TYR A O   
1460 C CB  . TYR A 180 ? 0.3658 0.3781 0.3253 0.0271  0.0575  0.1000  444 TYR A CB  
1461 C CG  . TYR A 180 ? 0.3939 0.3974 0.3514 0.0291  0.0750  0.1113  444 TYR A CG  
1462 C CD1 . TYR A 180 ? 0.4007 0.4188 0.3993 0.0232  0.0835  0.1180  444 TYR A CD1 
1463 C CD2 . TYR A 180 ? 0.4469 0.4257 0.3608 0.0373  0.0850  0.1154  444 TYR A CD2 
1464 C CE1 . TYR A 180 ? 0.4455 0.4535 0.4436 0.0250  0.1027  0.1289  444 TYR A CE1 
1465 C CE2 . TYR A 180 ? 0.4960 0.4629 0.4043 0.0404  0.1042  0.1270  444 TYR A CE2 
1466 C CZ  . TYR A 180 ? 0.4934 0.4751 0.4454 0.0341  0.1142  0.1340  444 TYR A CZ  
1467 O OH  . TYR A 180 ? 0.4748 0.4424 0.4212 0.0371  0.1357  0.1460  444 TYR A OH  
1468 N N   . ASN A 181 ? 0.3094 0.3624 0.3464 0.0071  0.0324  0.0954  445 ASN A N   
1469 C CA  . ASN A 181 ? 0.2899 0.3560 0.3606 -0.0020 0.0286  0.0970  445 ASN A CA  
1470 C C   . ASN A 181 ? 0.3008 0.3669 0.3686 -0.0086 0.0107  0.0899  445 ASN A C   
1471 O O   . ASN A 181 ? 0.3051 0.3695 0.3819 -0.0145 0.0096  0.0918  445 ASN A O   
1472 C CB  . ASN A 181 ? 0.2455 0.3312 0.3535 -0.0044 0.0296  0.0974  445 ASN A CB  
1473 C CG  . ASN A 181 ? 0.3066 0.3952 0.4305 0.0002  0.0505  0.1062  445 ASN A CG  
1474 O OD1 . ASN A 181 ? 0.3344 0.4106 0.4470 0.0023  0.0656  0.1132  445 ASN A OD1 
1475 N ND2 . ASN A 181 ? 0.4081 0.5124 0.5588 0.0024  0.0525  0.1068  445 ASN A ND2 
1476 N N   . LEU A 182 ? 0.2478 0.3132 0.3025 -0.0074 -0.0011 0.0821  446 LEU A N   
1477 C CA  . LEU A 182 ? 0.2529 0.3157 0.3030 -0.0126 -0.0147 0.0757  446 LEU A CA  
1478 C C   . LEU A 182 ? 0.2854 0.3358 0.3164 -0.0110 -0.0150 0.0777  446 LEU A C   
1479 O O   . LEU A 182 ? 0.2961 0.3445 0.3321 -0.0158 -0.0210 0.0760  446 LEU A O   
1480 C CB  . LEU A 182 ? 0.2479 0.3099 0.2867 -0.0110 -0.0241 0.0678  446 LEU A CB  
1481 C CG  . LEU A 182 ? 0.3312 0.4043 0.3881 -0.0127 -0.0283 0.0657  446 LEU A CG  
1482 C CD1 . LEU A 182 ? 0.3025 0.3710 0.3442 -0.0083 -0.0324 0.0601  446 LEU A CD1 
1483 C CD2 . LEU A 182 ? 0.3863 0.4628 0.4565 -0.0212 -0.0377 0.0626  446 LEU A CD2 
1484 N N   . GLU A 183 ? 0.3116 0.3522 0.3189 -0.0036 -0.0094 0.0809  447 GLU A N   
1485 C CA  . GLU A 183 ? 0.3521 0.3815 0.3408 -0.0009 -0.0121 0.0839  447 GLU A CA  
1486 C C   . GLU A 183 ? 0.3190 0.3457 0.3200 -0.0032 -0.0033 0.0926  447 GLU A C   
1487 O O   . GLU A 183 ? 0.3166 0.3391 0.3195 -0.0051 -0.0080 0.0937  447 GLU A O   
1488 C CB  . GLU A 183 ? 0.3868 0.4038 0.3427 0.0077  -0.0096 0.0854  447 GLU A CB  
1489 C CG  . GLU A 183 ? 0.3943 0.4105 0.3362 0.0090  -0.0200 0.0755  447 GLU A CG  
1490 C CD  . GLU A 183 ? 0.4847 0.4862 0.3916 0.0165  -0.0179 0.0753  447 GLU A CD  
1491 O OE1 . GLU A 183 ? 0.5374 0.5288 0.4290 0.0217  -0.0060 0.0834  447 GLU A OE1 
1492 O OE2 . GLU A 183 ? 0.4977 0.4960 0.3912 0.0167  -0.0276 0.0667  447 GLU A OE2 
1493 N N   . LEU A 184 ? 0.3144 0.3432 0.3265 -0.0031 0.0108  0.0988  448 LEU A N   
1494 C CA  . LEU A 184 ? 0.2967 0.3221 0.3237 -0.0064 0.0216  0.1071  448 LEU A CA  
1495 C C   . LEU A 184 ? 0.2869 0.3201 0.3408 -0.0167 0.0135  0.1022  448 LEU A C   
1496 O O   . LEU A 184 ? 0.3346 0.3596 0.3914 -0.0193 0.0152  0.1057  448 LEU A O   
1497 C CB  . LEU A 184 ? 0.3461 0.3757 0.3880 -0.0057 0.0391  0.1135  448 LEU A CB  
1498 C CG  . LEU A 184 ? 0.4157 0.4417 0.4772 -0.0099 0.0539  0.1226  448 LEU A CG  
1499 C CD1 . LEU A 184 ? 0.5047 0.5106 0.5410 -0.0054 0.0575  0.1300  448 LEU A CD1 
1500 C CD2 . LEU A 184 ? 0.4751 0.5032 0.5458 -0.0064 0.0734  0.1293  448 LEU A CD2 
1501 N N   . ALA A 185 ? 0.3014 0.3477 0.3714 -0.0219 0.0047  0.0942  449 ALA A N   
1502 C CA  . ALA A 185 ? 0.2386 0.2896 0.3281 -0.0316 -0.0043 0.0880  449 ALA A CA  
1503 C C   . ALA A 185 ? 0.2585 0.2991 0.3332 -0.0314 -0.0125 0.0842  449 ALA A C   
1504 O O   . ALA A 185 ? 0.2745 0.3089 0.3582 -0.0370 -0.0124 0.0838  449 ALA A O   
1505 C CB  . ALA A 185 ? 0.2643 0.3283 0.3648 -0.0347 -0.0139 0.0806  449 ALA A CB  
1506 N N   . PHE A 186 ? 0.2732 0.3119 0.3279 -0.0253 -0.0193 0.0808  450 PHE A N   
1507 C CA  . PHE A 186 ? 0.2814 0.3130 0.3270 -0.0241 -0.0263 0.0778  450 PHE A CA  
1508 C C   . PHE A 186 ? 0.2966 0.3176 0.3382 -0.0210 -0.0207 0.0859  450 PHE A C   
1509 O O   . PHE A 186 ? 0.2743 0.2890 0.3238 -0.0241 -0.0213 0.0853  450 PHE A O   
1510 C CB  . PHE A 186 ? 0.2751 0.3074 0.3027 -0.0180 -0.0335 0.0739  450 PHE A CB  
1511 C CG  . PHE A 186 ? 0.3014 0.3304 0.3267 -0.0176 -0.0413 0.0696  450 PHE A CG  
1512 C CD1 . PHE A 186 ? 0.2973 0.3244 0.3346 -0.0234 -0.0430 0.0648  450 PHE A CD1 
1513 C CD2 . PHE A 186 ? 0.3893 0.4170 0.4006 -0.0114 -0.0473 0.0693  450 PHE A CD2 
1514 C CE1 . PHE A 186 ? 0.2967 0.3210 0.3348 -0.0222 -0.0477 0.0610  450 PHE A CE1 
1515 C CE2 . PHE A 186 ? 0.4009 0.4285 0.4165 -0.0110 -0.0546 0.0653  450 PHE A CE2 
1516 C CZ  . PHE A 186 ? 0.3528 0.3790 0.3833 -0.0162 -0.0534 0.0616  450 PHE A CZ  
1517 N N   . HIS A 187 ? 0.2715 0.2878 0.2988 -0.0140 -0.0141 0.0942  451 HIS A N   
1518 C CA  . HIS A 187 ? 0.3020 0.3056 0.3208 -0.0089 -0.0093 0.1036  451 HIS A CA  
1519 C C   . HIS A 187 ? 0.2869 0.2849 0.3242 -0.0150 0.0018  0.1086  451 HIS A C   
1520 O O   . HIS A 187 ? 0.3415 0.3293 0.3803 -0.0140 0.0035  0.1128  451 HIS A O   
1521 C CB  . HIS A 187 ? 0.3184 0.3142 0.3106 0.0008  -0.0046 0.1116  451 HIS A CB  
1522 C CG  . HIS A 187 ? 0.3766 0.3735 0.3477 0.0070  -0.0177 0.1067  451 HIS A CG  
1523 N ND1 . HIS A 187 ? 0.4670 0.4598 0.4292 0.0123  -0.0286 0.1081  451 HIS A ND1 
1524 C CD2 . HIS A 187 ? 0.3963 0.3981 0.3562 0.0082  -0.0220 0.1002  451 HIS A CD2 
1525 C CE1 . HIS A 187 ? 0.4664 0.4628 0.4141 0.0153  -0.0401 0.1018  451 HIS A CE1 
1526 N NE2 . HIS A 187 ? 0.4367 0.4372 0.3814 0.0127  -0.0358 0.0965  451 HIS A NE2 
1527 N N   . HIS A 188 ? 0.2780 0.2834 0.3326 -0.0217 0.0092  0.1078  452 HIS A N   
1528 C CA  . HIS A 188 ? 0.2987 0.3003 0.3764 -0.0303 0.0187  0.1105  452 HIS A CA  
1529 C C   . HIS A 188 ? 0.2737 0.2722 0.3624 -0.0376 0.0107  0.1025  452 HIS A C   
1530 O O   . HIS A 188 ? 0.3319 0.3175 0.4273 -0.0406 0.0171  0.1058  452 HIS A O   
1531 C CB  . HIS A 188 ? 0.3059 0.3209 0.4067 -0.0372 0.0240  0.1089  452 HIS A CB  
1532 C CG  . HIS A 188 ? 0.3339 0.3477 0.4638 -0.0484 0.0311  0.1094  452 HIS A CG  
1533 N ND1 . HIS A 188 ? 0.2998 0.3026 0.4362 -0.0485 0.0482  0.1199  452 HIS A ND1 
1534 C CD2 . HIS A 188 ? 0.3498 0.3696 0.5023 -0.0604 0.0231  0.1001  452 HIS A CD2 
1535 C CE1 . HIS A 188 ? 0.3500 0.3537 0.5158 -0.0610 0.0509  0.1167  452 HIS A CE1 
1536 N NE2 . HIS A 188 ? 0.3218 0.3355 0.4965 -0.0685 0.0345  0.1042  452 HIS A NE2 
1537 N N   . HIS A 189 ? 0.2810 0.2886 0.3694 -0.0403 -0.0016 0.0920  453 HIS A N   
1538 C CA  . HIS A 189 ? 0.2923 0.2947 0.3870 -0.0471 -0.0078 0.0835  453 HIS A CA  
1539 C C   . HIS A 189 ? 0.2998 0.2897 0.3840 -0.0410 -0.0081 0.0855  453 HIS A C   
1540 O O   . HIS A 189 ? 0.3088 0.2867 0.4000 -0.0455 -0.0048 0.0836  453 HIS A O   
1541 C CB  . HIS A 189 ? 0.3224 0.3345 0.4155 -0.0502 -0.0192 0.0731  453 HIS A CB  
1542 C CG  . HIS A 189 ? 0.3411 0.3455 0.4388 -0.0588 -0.0239 0.0638  453 HIS A CG  
1543 N ND1 . HIS A 189 ? 0.4508 0.4519 0.5642 -0.0694 -0.0225 0.0608  453 HIS A ND1 
1544 C CD2 . HIS A 189 ? 0.3655 0.3619 0.4532 -0.0586 -0.0285 0.0568  453 HIS A CD2 
1545 C CE1 . HIS A 189 ? 0.4508 0.4408 0.5592 -0.0752 -0.0273 0.0516  453 HIS A CE1 
1546 N NE2 . HIS A 189 ? 0.3705 0.3571 0.4630 -0.0684 -0.0299 0.0494  453 HIS A NE2 
1547 N N   . LEU A 190 ? 0.2825 0.2753 0.3516 -0.0311 -0.0125 0.0887  454 LEU A N   
1548 C CA  . LEU A 190 ? 0.2721 0.2562 0.3358 -0.0238 -0.0136 0.0927  454 LEU A CA  
1549 C C   . LEU A 190 ? 0.3195 0.2891 0.3853 -0.0211 -0.0030 0.1034  454 LEU A C   
1550 O O   . LEU A 190 ? 0.3421 0.3011 0.4139 -0.0201 -0.0007 0.1043  454 LEU A O   
1551 C CB  . LEU A 190 ? 0.3053 0.2963 0.3536 -0.0141 -0.0219 0.0949  454 LEU A CB  
1552 C CG  . LEU A 190 ? 0.2905 0.2924 0.3372 -0.0159 -0.0315 0.0847  454 LEU A CG  
1553 C CD1 . LEU A 190 ? 0.3268 0.3338 0.3587 -0.0072 -0.0399 0.0866  454 LEU A CD1 
1554 C CD2 . LEU A 190 ? 0.2835 0.2829 0.3412 -0.0196 -0.0337 0.0770  454 LEU A CD2 
1555 N N   . CYS A 191 ? 0.3361 0.3033 0.3970 -0.0193 0.0054  0.1123  455 CYS A N   
1556 C CA  . CYS A 191 ? 0.3461 0.2965 0.4075 -0.0163 0.0176  0.1238  455 CYS A CA  
1557 C C   . CYS A 191 ? 0.3802 0.3217 0.4627 -0.0280 0.0256  0.1194  455 CYS A C   
1558 O O   . CYS A 191 ? 0.4214 0.3466 0.5074 -0.0265 0.0322  0.1240  455 CYS A O   
1559 C CB  . CYS A 191 ? 0.4882 0.4358 0.5377 -0.0119 0.0273  0.1343  455 CYS A CB  
1560 S SG  . CYS A 191 ? 0.7034 0.6537 0.7199 0.0028  0.0179  0.1397  455 CYS A SG  
1561 N N   . LYS A 192 ? 0.3826 0.3342 0.4791 -0.0396 0.0240  0.1102  456 LYS A N   
1562 C CA  . LYS A 192 ? 0.4111 0.3550 0.5267 -0.0526 0.0281  0.1034  456 LYS A CA  
1563 C C   . LYS A 192 ? 0.3834 0.3155 0.4973 -0.0538 0.0243  0.0960  456 LYS A C   
1564 O O   . LYS A 192 ? 0.4029 0.3178 0.5256 -0.0598 0.0322  0.0949  456 LYS A O   
1565 C CB  . LYS A 192 ? 0.3867 0.3468 0.5161 -0.0635 0.0215  0.0938  456 LYS A CB  
1566 C CG  . LYS A 192 ? 0.4381 0.3918 0.5887 -0.0781 0.0245  0.0873  456 LYS A CG  
1567 C CD  . LYS A 192 ? 0.4971 0.4706 0.6659 -0.0868 0.0184  0.0820  456 LYS A CD  
1568 C CE  . LYS A 192 ? 0.6289 0.5978 0.8176 -0.1028 0.0146  0.0717  456 LYS A CE  
1569 N NZ  . LYS A 192 ? 0.7417 0.6882 0.9370 -0.1071 0.0284  0.0757  456 LYS A NZ  
1570 N N   . THR A 193 ? 0.3774 0.3171 0.4807 -0.0480 0.0140  0.0911  457 THR A N   
1571 C CA  . THR A 193 ? 0.3852 0.3145 0.4877 -0.0491 0.0120  0.0832  457 THR A CA  
1572 C C   . THR A 193 ? 0.3989 0.3209 0.4975 -0.0364 0.0146  0.0914  457 THR A C   
1573 O O   . THR A 193 ? 0.4229 0.3389 0.5227 -0.0346 0.0140  0.0862  457 THR A O   
1574 C CB  . THR A 193 ? 0.3852 0.3257 0.4818 -0.0521 0.0008  0.0715  457 THR A CB  
1575 O OG1 . THR A 193 ? 0.3725 0.3290 0.4610 -0.0431 -0.0063 0.0751  457 THR A OG1 
1576 C CG2 . THR A 193 ? 0.4109 0.3575 0.5128 -0.0643 -0.0037 0.0633  457 THR A CG2 
1577 N N   . HIS A 194 ? 0.4072 0.3291 0.5009 -0.0270 0.0178  0.1047  458 HIS A N   
1578 C CA  . HIS A 194 ? 0.3528 0.2699 0.4431 -0.0133 0.0171  0.1142  458 HIS A CA  
1579 C C   . HIS A 194 ? 0.3502 0.2814 0.4394 -0.0074 0.0050  0.1093  458 HIS A C   
1580 O O   . HIS A 194 ? 0.4427 0.3694 0.5401 -0.0010 0.0051  0.1104  458 HIS A O   
1581 C CB  . HIS A 194 ? 0.4594 0.3550 0.5598 -0.0130 0.0282  0.1163  458 HIS A CB  
1582 C CG  . HIS A 194 ? 0.5119 0.3912 0.6164 -0.0207 0.0413  0.1198  458 HIS A CG  
1583 N ND1 . HIS A 194 ? 0.6040 0.4755 0.7028 -0.0141 0.0491  0.1346  458 HIS A ND1 
1584 C CD2 . HIS A 194 ? 0.6079 0.4769 0.7215 -0.0352 0.0477  0.1103  458 HIS A CD2 
1585 C CE1 . HIS A 194 ? 0.6784 0.5356 0.7862 -0.0244 0.0618  0.1343  458 HIS A CE1 
1586 N NE2 . HIS A 194 ? 0.6750 0.5315 0.7930 -0.0378 0.0600  0.1191  458 HIS A NE2 
1587 N N   . ARG A 195 ? 0.3132 0.2609 0.3945 -0.0090 -0.0044 0.1045  459 ARG A N   
1588 C CA  . ARG A 195 ? 0.3094 0.2703 0.3912 -0.0053 -0.0153 0.0986  459 ARG A CA  
1589 C C   . ARG A 195 ? 0.3609 0.3345 0.4296 0.0020  -0.0259 0.1029  459 ARG A C   
1590 O O   . ARG A 195 ? 0.3572 0.3429 0.4257 0.0020  -0.0351 0.0961  459 ARG A O   
1591 C CB  . ARG A 195 ? 0.3503 0.3155 0.4342 -0.0155 -0.0168 0.0851  459 ARG A CB  
1592 C CG  . ARG A 195 ? 0.3694 0.3197 0.4610 -0.0223 -0.0085 0.0786  459 ARG A CG  
1593 C CD  . ARG A 195 ? 0.3770 0.3246 0.4774 -0.0174 -0.0074 0.0759  459 ARG A CD  
1594 N NE  . ARG A 195 ? 0.3565 0.3155 0.4545 -0.0193 -0.0141 0.0675  459 ARG A NE  
1595 C CZ  . ARG A 195 ? 0.3468 0.3095 0.4552 -0.0145 -0.0146 0.0656  459 ARG A CZ  
1596 N NH1 . ARG A 195 ? 0.4592 0.4169 0.5827 -0.0069 -0.0097 0.0714  459 ARG A NH1 
1597 N NH2 . ARG A 195 ? 0.3435 0.3141 0.4494 -0.0172 -0.0186 0.0580  459 ARG A NH2 
1598 N N   . GLN A 196 ? 0.3965 0.3650 0.4524 0.0082  -0.0238 0.1141  460 GLN A N   
1599 C CA  . GLN A 196 ? 0.4488 0.4246 0.4852 0.0155  -0.0333 0.1180  460 GLN A CA  
1600 C C   . GLN A 196 ? 0.4425 0.4278 0.4826 0.0228  -0.0478 0.1167  460 GLN A C   
1601 O O   . GLN A 196 ? 0.4742 0.4693 0.5035 0.0244  -0.0589 0.1126  460 GLN A O   
1602 C CB  . GLN A 196 ? 0.5441 0.5072 0.5622 0.0236  -0.0276 0.1322  460 GLN A CB  
1603 C CG  . GLN A 196 ? 0.6192 0.5720 0.6384 0.0170  -0.0111 0.1359  460 GLN A CG  
1604 C CD  . GLN A 196 ? 0.6305 0.5676 0.6628 0.0166  0.0001  0.1425  460 GLN A CD  
1605 O OE1 . GLN A 196 ? 0.6005 0.5367 0.6513 0.0120  0.0005  0.1359  460 GLN A OE1 
1606 N NE2 . GLN A 196 ? 0.6182 0.5398 0.6389 0.0219  0.0110  0.1557  460 GLN A NE2 
1607 N N   . SER A 197 ? 0.4408 0.4229 0.4985 0.0269  -0.0471 0.1197  461 SER A N   
1608 C CA  . SER A 197 ? 0.5217 0.5140 0.5887 0.0354  -0.0610 0.1211  461 SER A CA  
1609 C C   . SER A 197 ? 0.5170 0.5248 0.5955 0.0296  -0.0690 0.1082  461 SER A C   
1610 O O   . SER A 197 ? 0.5365 0.5560 0.6230 0.0348  -0.0827 0.1077  461 SER A O   
1611 C CB  . SER A 197 ? 0.5696 0.5555 0.6585 0.0413  -0.0557 0.1273  461 SER A CB  
1612 O OG  . SER A 197 ? 0.6494 0.6357 0.7585 0.0329  -0.0472 0.1168  461 SER A OG  
1613 N N   . ILE A 198 ? 0.4963 0.5040 0.5766 0.0189  -0.0613 0.0981  462 ILE A N   
1614 C CA  . ILE A 198 ? 0.5070 0.5265 0.5958 0.0140  -0.0673 0.0870  462 ILE A CA  
1615 C C   . ILE A 198 ? 0.5112 0.5392 0.5820 0.0150  -0.0794 0.0845  462 ILE A C   
1616 O O   . ILE A 198 ? 0.5448 0.5823 0.6224 0.0122  -0.0864 0.0764  462 ILE A O   
1617 C CB  . ILE A 198 ? 0.5114 0.5263 0.6021 0.0035  -0.0569 0.0773  462 ILE A CB  
1618 C CG1 . ILE A 198 ? 0.4365 0.4497 0.5074 -0.0015 -0.0550 0.0761  462 ILE A CG1 
1619 C CG2 . ILE A 198 ? 0.5835 0.5855 0.6859 0.0015  -0.0446 0.0781  462 ILE A CG2 
1620 C CD1 . ILE A 198 ? 0.4920 0.5065 0.5618 -0.0100 -0.0523 0.0658  462 ILE A CD1 
1621 N N   . LEU A 199 ? 0.4703 0.4924 0.5171 0.0183  -0.0799 0.0910  463 LEU A N   
1622 C CA  . LEU A 199 ? 0.4614 0.4873 0.4869 0.0190  -0.0888 0.0876  463 LEU A CA  
1623 C C   . LEU A 199 ? 0.4926 0.5272 0.5214 0.0249  -0.1065 0.0869  463 LEU A C   
1624 O O   . LEU A 199 ? 0.5195 0.5613 0.5463 0.0216  -0.1153 0.0781  463 LEU A O   
1625 C CB  . LEU A 199 ? 0.4491 0.4641 0.4467 0.0229  -0.0834 0.0959  463 LEU A CB  
1626 C CG  . LEU A 199 ? 0.4781 0.4872 0.4754 0.0165  -0.0673 0.0964  463 LEU A CG  
1627 C CD1 . LEU A 199 ? 0.5936 0.5901 0.5708 0.0222  -0.0590 0.1082  463 LEU A CD1 
1628 C CD2 . LEU A 199 ? 0.4121 0.4270 0.4052 0.0103  -0.0665 0.0870  463 LEU A CD2 
1629 N N   . ALA A 200 ? 0.4943 0.5283 0.5306 0.0334  -0.1122 0.0963  464 ALA A N   
1630 C CA  . ALA A 200 ? 0.4976 0.5411 0.5373 0.0400  -0.1322 0.0970  464 ALA A CA  
1631 C C   . ALA A 200 ? 0.4723 0.5319 0.5489 0.0351  -0.1375 0.0877  464 ALA A C   
1632 O O   . ALA A 200 ? 0.5016 0.5732 0.5894 0.0380  -0.1554 0.0856  464 ALA A O   
1633 C CB  . ALA A 200 ? 0.5178 0.5558 0.5552 0.0521  -0.1373 0.1114  464 ALA A CB  
1634 N N   . LYS A 201 ? 0.4147 0.4737 0.5100 0.0276  -0.1220 0.0823  465 LYS A N   
1635 C CA  . LYS A 201 ? 0.4276 0.4980 0.5562 0.0226  -0.1215 0.0739  465 LYS A CA  
1636 C C   . LYS A 201 ? 0.4637 0.5350 0.5872 0.0125  -0.1176 0.0617  465 LYS A C   
1637 O O   . LYS A 201 ? 0.6229 0.7009 0.7717 0.0078  -0.1145 0.0548  465 LYS A O   
1638 C CB  . LYS A 201 ? 0.4800 0.5453 0.6319 0.0227  -0.1057 0.0767  465 LYS A CB  
1639 C CG  . LYS A 201 ? 0.5844 0.6503 0.7495 0.0338  -0.1098 0.0887  465 LYS A CG  
1640 C CD  . LYS A 201 ? 0.6305 0.6829 0.8045 0.0346  -0.0913 0.0931  465 LYS A CD  
1641 C CE  . LYS A 201 ? 0.6732 0.7266 0.8739 0.0290  -0.0789 0.0849  465 LYS A CE  
1642 N NZ  . LYS A 201 ? 0.7227 0.7631 0.9367 0.0332  -0.0638 0.0908  465 LYS A NZ  
1643 N N   . LEU A 202 ? 0.9351 0.5729 0.3407 0.1372  0.0762  -0.0205 466 LEU A N   
1644 C CA  . LEU A 202 ? 0.9050 0.5249 0.3008 0.1363  0.0781  -0.0232 466 LEU A CA  
1645 C C   . LEU A 202 ? 0.9778 0.5951 0.3610 0.1284  0.0780  -0.0291 466 LEU A C   
1646 O O   . LEU A 202 ? 0.9829 0.6109 0.3630 0.1258  0.0767  -0.0308 466 LEU A O   
1647 C CB  . LEU A 202 ? 0.9062 0.5183 0.3004 0.1438  0.0795  -0.0215 466 LEU A CB  
1648 C CG  . LEU A 202 ? 0.8472 0.4599 0.2530 0.1520  0.0795  -0.0161 466 LEU A CG  
1649 C CD1 . LEU A 202 ? 0.8927 0.5020 0.2977 0.1595  0.0807  -0.0145 466 LEU A CD1 
1650 C CD2 . LEU A 202 ? 0.9218 0.5207 0.3267 0.1522  0.0801  -0.0153 466 LEU A CD2 
1651 N N   . PRO A 203 ? 1.0715 0.6745 0.4469 0.1243  0.0795  -0.0321 467 PRO A N   
1652 C CA  . PRO A 203 ? 1.0979 0.6992 0.4625 0.1162  0.0796  -0.0381 467 PRO A CA  
1653 C C   . PRO A 203 ? 1.0968 0.6941 0.4505 0.1157  0.0804  -0.0419 467 PRO A C   
1654 O O   . PRO A 203 ? 1.0739 0.6640 0.4263 0.1216  0.0820  -0.0404 467 PRO A O   
1655 C CB  . PRO A 203 ? 1.1299 0.7154 0.4899 0.1127  0.0816  -0.0396 467 PRO A CB  
1656 C CG  . PRO A 203 ? 1.1472 0.7218 0.5105 0.1199  0.0827  -0.0350 467 PRO A CG  
1657 C CD  . PRO A 203 ? 1.0867 0.6752 0.4628 0.1264  0.0811  -0.0301 467 PRO A CD  
1658 N N   . PRO A 204 ? 1.1373 0.7390 0.4826 0.1087  0.0796  -0.0473 468 PRO A N   
1659 C CA  . PRO A 204 ? 1.1648 0.7633 0.4990 0.1074  0.0806  -0.0519 468 PRO A CA  
1660 C C   . PRO A 204 ? 1.2427 0.8216 0.5710 0.1106  0.0841  -0.0527 468 PRO A C   
1661 O O   . PRO A 204 ? 1.2715 0.8368 0.5962 0.1083  0.0856  -0.0537 468 PRO A O   
1662 C CB  . PRO A 204 ? 1.1260 0.7268 0.4516 0.0985  0.0795  -0.0582 468 PRO A CB  
1663 C CG  . PRO A 204 ? 1.0848 0.6967 0.4183 0.0961  0.0769  -0.0560 468 PRO A CG  
1664 C CD  . PRO A 204 ? 1.0988 0.7066 0.4435 0.1015  0.0779  -0.0500 468 PRO A CD  
1665 N N   . LYS A 205 ? 1.2604 0.8374 0.5873 0.1161  0.0855  -0.0519 469 LYS A N   
1666 C CA  . LYS A 205 ? 1.2961 0.8539 0.6166 0.1202  0.0888  -0.0523 469 LYS A CA  
1667 C C   . LYS A 205 ? 1.3167 0.8704 0.6255 0.1176  0.0911  -0.0587 469 LYS A C   
1668 O O   . LYS A 205 ? 1.3666 0.9330 0.6742 0.1166  0.0906  -0.0608 469 LYS A O   
1669 C CB  . LYS A 205 ? 1.3026 0.8583 0.6309 0.1296  0.0893  -0.0462 469 LYS A CB  
1670 C CG  . LYS A 205 ? 1.3295 0.8635 0.6513 0.1348  0.0922  -0.0454 469 LYS A CG  
1671 C CD  . LYS A 205 ? 1.3467 0.8668 0.6662 0.1331  0.0922  -0.0438 469 LYS A CD  
1672 C CE  . LYS A 205 ? 1.3415 0.8426 0.6577 0.1407  0.0938  -0.0397 469 LYS A CE  
1673 N NZ  . LYS A 205 ? 1.3337 0.8419 0.6616 0.1487  0.0921  -0.0335 469 LYS A NZ  
1674 N N   . GLY A 206 ? 1.3131 0.8484 0.6123 0.1162  0.0940  -0.0620 470 GLY A N   
1675 C CA  . GLY A 206 ? 1.3204 0.8416 0.6200 0.1167  0.0943  -0.0589 470 GLY A CA  
1676 C C   . GLY A 206 ? 1.3226 0.8418 0.6168 0.1079  0.0942  -0.0636 470 GLY A C   
1677 O O   . GLY A 206 ? 1.3043 0.8070 0.5931 0.1064  0.0960  -0.0635 470 GLY A O   
1678 N N   . LYS A 207 ? 1.3644 0.8998 0.6591 0.1021  0.0921  -0.0675 471 LYS A N   
1679 C CA  . LYS A 207 ? 1.3540 0.8879 0.6419 0.0934  0.0921  -0.0736 471 LYS A CA  
1680 C C   . LYS A 207 ? 1.2736 0.7979 0.5636 0.0912  0.0925  -0.0711 471 LYS A C   
1681 O O   . LYS A 207 ? 1.2508 0.7635 0.5329 0.0855  0.0945  -0.0754 471 LYS A O   
1682 C CB  . LYS A 207 ? 1.3671 0.9217 0.6570 0.0884  0.0885  -0.0763 471 LYS A CB  
1683 C CG  . LYS A 207 ? 1.3734 0.9267 0.6529 0.0800  0.0888  -0.0848 471 LYS A CG  
1684 C CD  . LYS A 207 ? 1.3424 0.9111 0.6247 0.0745  0.0849  -0.0862 471 LYS A CD  
1685 C CE  . LYS A 207 ? 1.3298 0.8909 0.6042 0.0664  0.0858  -0.0933 471 LYS A CE  
1686 N NZ  . LYS A 207 ? 1.3074 0.8686 0.5877 0.0634  0.0849  -0.0914 471 LYS A NZ  
1687 N N   . LEU A 208 ? 1.1820 0.7108 0.4827 0.0958  0.0911  -0.0643 472 LEU A N   
1688 C CA  . LEU A 208 ? 1.1592 0.6807 0.4626 0.0939  0.0916  -0.0617 472 LEU A CA  
1689 C C   . LEU A 208 ? 1.1724 0.6700 0.4677 0.0967  0.0948  -0.0597 472 LEU A C   
1690 O O   . LEU A 208 ? 1.1918 0.6773 0.4821 0.0922  0.0966  -0.0606 472 LEU A O   
1691 C CB  . LEU A 208 ? 1.1171 0.6524 0.4345 0.0975  0.0890  -0.0557 472 LEU A CB  
1692 C CG  . LEU A 208 ? 1.1486 0.6855 0.4702 0.0920  0.0889  -0.0556 472 LEU A CG  
1693 C CD1 . LEU A 208 ? 1.1452 0.6840 0.4600 0.0831  0.0892  -0.0626 472 LEU A CD1 
1694 C CD2 . LEU A 208 ? 1.1462 0.7002 0.4820 0.0946  0.0864  -0.0511 472 LEU A CD2 
1695 N N   . ARG A 209 ? 1.2415 0.7312 0.5342 0.1038  0.0958  -0.0576 473 ARG A N   
1696 C CA  . ARG A 209 ? 1.2683 0.7333 0.5503 0.1068  0.0988  -0.0561 473 ARG A CA  
1697 C C   . ARG A 209 ? 1.2498 0.7031 0.5215 0.1096  0.1015  -0.0595 473 ARG A C   
1698 O O   . ARG A 209 ? 1.3301 0.7833 0.6042 0.1172  0.1014  -0.0565 473 ARG A O   
1699 C CB  . ARG A 209 ? 1.2916 0.7523 0.5797 0.1147  0.0977  -0.0484 473 ARG A CB  
1700 C CG  . ARG A 209 ? 1.2318 0.7128 0.5338 0.1198  0.0948  -0.0452 473 ARG A CG  
1701 C CD  . ARG A 209 ? 1.2584 0.7359 0.5670 0.1273  0.0937  -0.0382 473 ARG A CD  
1702 N NE  . ARG A 209 ? 1.3548 0.8182 0.6573 0.1356  0.0949  -0.0359 473 ARG A NE  
1703 C CZ  . ARG A 209 ? 1.4361 0.9046 0.7467 0.1440  0.0936  -0.0313 473 ARG A CZ  
1704 N NH1 . ARG A 209 ? 1.4329 0.9202 0.7580 0.1449  0.0911  -0.0286 473 ARG A NH1 
1705 N NH2 . ARG A 209 ? 1.4651 0.9197 0.7690 0.1515  0.0950  -0.0297 473 ARG A NH2 
1706 N N   . SER A 210 ? 1.0938 0.5360 0.3539 0.1040  0.1044  -0.0658 474 SER A N   
1707 C CA  . SER A 210 ? 1.0633 0.5027 0.3184 0.0946  0.1054  -0.0708 474 SER A CA  
1708 C C   . SER A 210 ? 1.1591 0.5850 0.4114 0.0918  0.1064  -0.0674 474 SER A C   
1709 O O   . SER A 210 ? 1.0838 0.4923 0.3250 0.0869  0.1097  -0.0704 474 SER A O   
1710 C CB  . SER A 210 ? 1.0589 0.5219 0.3220 0.0891  0.1024  -0.0742 474 SER A CB  
1711 O OG  . SER A 210 ? 1.1117 0.5709 0.3709 0.0807  0.1033  -0.0782 474 SER A OG  
1712 N N   . LEU A 211 ? 0.5736 0.5531 0.4557 0.0241  0.0015  0.0346  475 LEU A N   
1713 C CA  . LEU A 211 ? 0.5293 0.5244 0.4510 0.0249  -0.0031 0.0316  475 LEU A CA  
1714 C C   . LEU A 211 ? 0.4592 0.4544 0.3905 0.0245  0.0061  0.0188  475 LEU A C   
1715 O O   . LEU A 211 ? 0.4105 0.4113 0.3551 0.0229  -0.0018 0.0118  475 LEU A O   
1716 C CB  . LEU A 211 ? 0.4516 0.4524 0.3983 0.0277  0.0036  0.0406  475 LEU A CB  
1717 C CG  . LEU A 211 ? 0.4061 0.4159 0.3853 0.0276  0.0025  0.0368  475 LEU A CG  
1718 C CD1 . LEU A 211 ? 0.4788 0.4963 0.4670 0.0274  -0.0117 0.0364  475 LEU A CD1 
1719 C CD2 . LEU A 211 ? 0.3281 0.3353 0.3222 0.0292  0.0099  0.0451  475 LEU A CD2 
1720 N N   . CYS A 212 ? 0.4789 0.4678 0.4055 0.0263  0.0237  0.0175  476 CYS A N   
1721 C CA  . CYS A 212 ? 0.4856 0.4763 0.4286 0.0274  0.0334  0.0087  476 CYS A CA  
1722 C C   . CYS A 212 ? 0.4981 0.4787 0.4208 0.0264  0.0279  -0.0024 476 CYS A C   
1723 O O   . CYS A 212 ? 0.4506 0.4363 0.3933 0.0263  0.0250  -0.0088 476 CYS A O   
1724 C CB  . CYS A 212 ? 0.6170 0.6041 0.5637 0.0303  0.0553  0.0118  476 CYS A CB  
1725 S SG  . CYS A 212 ? 0.7435 0.7420 0.7334 0.0324  0.0663  0.0079  476 CYS A SG  
1726 N N   . SER A 213 ? 0.5767 0.5405 0.4579 0.0242  0.0243  -0.0042 477 SER A N   
1727 C CA  . SER A 213 ? 0.5921 0.5406 0.4497 0.0211  0.0189  -0.0163 477 SER A CA  
1728 C C   . SER A 213 ? 0.5600 0.5190 0.4325 0.0160  -0.0040 -0.0179 477 SER A C   
1729 O O   . SER A 213 ? 0.5288 0.4814 0.4021 0.0138  -0.0072 -0.0277 477 SER A O   
1730 C CB  . SER A 213 ? 0.6650 0.5871 0.4657 0.0176  0.0203  -0.0186 477 SER A CB  
1731 O OG  . SER A 213 ? 0.7232 0.6460 0.5064 0.0106  -0.0048 -0.0132 477 SER A OG  
1732 N N   . GLN A 214 ? 0.4820 0.4562 0.3694 0.0146  -0.0178 -0.0074 478 GLN A N   
1733 C CA  . GLN A 214 ? 0.4349 0.4231 0.3483 0.0115  -0.0336 -0.0064 478 GLN A CA  
1734 C C   . GLN A 214 ? 0.3581 0.3555 0.3042 0.0141  -0.0262 -0.0108 478 GLN A C   
1735 O O   . GLN A 214 ? 0.4021 0.4006 0.3578 0.0110  -0.0335 -0.0161 478 GLN A O   
1736 C CB  . GLN A 214 ? 0.4811 0.4842 0.4120 0.0123  -0.0436 0.0074  478 GLN A CB  
1737 C CG  . GLN A 214 ? 0.5444 0.5442 0.4531 0.0081  -0.0602 0.0159  478 GLN A CG  
1738 C CD  . GLN A 214 ? 0.5225 0.5397 0.4611 0.0113  -0.0680 0.0314  478 GLN A CD  
1739 O OE1 . GLN A 214 ? 0.6215 0.6376 0.5543 0.0150  -0.0652 0.0422  478 GLN A OE1 
1740 N NE2 . GLN A 214 ? 0.5212 0.5532 0.4935 0.0106  -0.0754 0.0333  478 GLN A NE2 
1741 N N   . HIS A 215 ? 0.3476 0.3505 0.3096 0.0186  -0.0135 -0.0074 479 HIS A N   
1742 C CA  . HIS A 215 ? 0.3206 0.3308 0.3100 0.0196  -0.0091 -0.0096 479 HIS A CA  
1743 C C   . HIS A 215 ? 0.2936 0.2959 0.2816 0.0202  -0.0046 -0.0184 479 HIS A C   
1744 O O   . HIS A 215 ? 0.3471 0.3521 0.3505 0.0189  -0.0094 -0.0213 479 HIS A O   
1745 C CB  . HIS A 215 ? 0.2968 0.3116 0.3002 0.0217  0.0014  -0.0041 479 HIS A CB  
1746 C CG  . HIS A 215 ? 0.3060 0.3249 0.3319 0.0217  0.0058  -0.0061 479 HIS A CG  
1747 N ND1 . HIS A 215 ? 0.3241 0.3474 0.3652 0.0188  -0.0021 -0.0063 479 HIS A ND1 
1748 C CD2 . HIS A 215 ? 0.3490 0.3683 0.3859 0.0242  0.0166  -0.0062 479 HIS A CD2 
1749 C CE1 . HIS A 215 ? 0.3238 0.3503 0.3828 0.0185  0.0003  -0.0056 479 HIS A CE1 
1750 N NE2 . HIS A 215 ? 0.3430 0.3692 0.4047 0.0223  0.0117  -0.0051 479 HIS A NE2 
1751 N N   . VAL A 216 ? 0.3201 0.3100 0.2887 0.0228  0.0068  -0.0223 480 VAL A N   
1752 C CA  . VAL A 216 ? 0.3806 0.3590 0.3485 0.0253  0.0154  -0.0308 480 VAL A CA  
1753 C C   . VAL A 216 ? 0.3857 0.3542 0.3421 0.0205  0.0031  -0.0387 480 VAL A C   
1754 O O   . VAL A 216 ? 0.3769 0.3435 0.3498 0.0215  0.0038  -0.0426 480 VAL A O   
1755 C CB  . VAL A 216 ? 0.3818 0.3436 0.3255 0.0294  0.0339  -0.0341 480 VAL A CB  
1756 C CG1 . VAL A 216 ? 0.4176 0.3611 0.3558 0.0327  0.0450  -0.0444 480 VAL A CG1 
1757 C CG2 . VAL A 216 ? 0.4442 0.4183 0.4126 0.0341  0.0487  -0.0252 480 VAL A CG2 
1758 N N   . GLU A 217 ? 0.3714 0.3340 0.3021 0.0145  -0.0096 -0.0396 481 GLU A N   
1759 C CA  . GLU A 217 ? 0.3993 0.3544 0.3232 0.0074  -0.0242 -0.0457 481 GLU A CA  
1760 C C   . GLU A 217 ? 0.3428 0.3156 0.3029 0.0061  -0.0325 -0.0411 481 GLU A C   
1761 O O   . GLU A 217 ? 0.3913 0.3575 0.3593 0.0040  -0.0345 -0.0464 481 GLU A O   
1762 C CB  . GLU A 217 ? 0.4544 0.4050 0.3511 -0.0006 -0.0411 -0.0435 481 GLU A CB  
1763 C CG  . GLU A 217 ? 0.6883 0.6100 0.5343 -0.0039 -0.0379 -0.0519 481 GLU A CG  
1764 C CD  . GLU A 217 ? 0.8951 0.8055 0.7146 -0.0168 -0.0621 -0.0542 481 GLU A CD  
1765 O OE1 . GLU A 217 ? 0.9091 0.8355 0.7575 -0.0223 -0.0788 -0.0503 481 GLU A OE1 
1766 O OE2 . GLU A 217 ? 1.0055 0.8902 0.7747 -0.0224 -0.0649 -0.0593 481 GLU A OE2 
1767 N N   . ARG A 218 ? 0.3156 0.3072 0.2953 0.0075  -0.0352 -0.0312 482 ARG A N   
1768 C CA  . ARG A 218 ? 0.3480 0.3517 0.3543 0.0057  -0.0406 -0.0269 482 ARG A CA  
1769 C C   . ARG A 218 ? 0.2798 0.2829 0.3017 0.0089  -0.0327 -0.0281 482 ARG A C   
1770 O O   . ARG A 218 ? 0.3103 0.3134 0.3440 0.0064  -0.0365 -0.0282 482 ARG A O   
1771 C CB  . ARG A 218 ? 0.3678 0.3859 0.3871 0.0069  -0.0423 -0.0169 482 ARG A CB  
1772 C CG  . ARG A 218 ? 0.5229 0.5446 0.5329 0.0050  -0.0516 -0.0114 482 ARG A CG  
1773 C CD  . ARG A 218 ? 0.6002 0.6205 0.6081 -0.0027 -0.0667 -0.0131 482 ARG A CD  
1774 N NE  . ARG A 218 ? 0.6204 0.6481 0.6545 -0.0052 -0.0683 -0.0117 482 ARG A NE  
1775 C CZ  . ARG A 218 ? 0.6852 0.7149 0.7282 -0.0130 -0.0809 -0.0113 482 ARG A CZ  
1776 N NH1 . ARG A 218 ? 0.6993 0.7354 0.7673 -0.0149 -0.0788 -0.0088 482 ARG A NH1 
1777 N NH2 . ARG A 218 ? 0.6453 0.6688 0.6703 -0.0201 -0.0959 -0.0130 482 ARG A NH2 
1778 N N   . LEU A 219 ? 0.2642 0.2675 0.2881 0.0139  -0.0226 -0.0273 483 LEU A N   
1779 C CA  . LEU A 219 ? 0.2744 0.2787 0.3166 0.0163  -0.0183 -0.0261 483 LEU A CA  
1780 C C   . LEU A 219 ? 0.2923 0.2843 0.3351 0.0169  -0.0178 -0.0324 483 LEU A C   
1781 O O   . LEU A 219 ? 0.2776 0.2702 0.3358 0.0163  -0.0212 -0.0297 483 LEU A O   
1782 C CB  . LEU A 219 ? 0.2792 0.2871 0.3286 0.0211  -0.0075 -0.0231 483 LEU A CB  
1783 C CG  . LEU A 219 ? 0.3183 0.3305 0.3935 0.0235  -0.0052 -0.0189 483 LEU A CG  
1784 C CD1 . LEU A 219 ? 0.3132 0.3314 0.3976 0.0182  -0.0167 -0.0132 483 LEU A CD1 
1785 C CD2 . LEU A 219 ? 0.3174 0.3367 0.4057 0.0270  0.0055  -0.0139 483 LEU A CD2 
1786 N N   . GLN A 220 ? 0.2835 0.2608 0.3063 0.0177  -0.0130 -0.0406 484 GLN A N   
1787 C CA  . GLN A 220 ? 0.3527 0.3126 0.3737 0.0182  -0.0104 -0.0479 484 GLN A CA  
1788 C C   . GLN A 220 ? 0.3354 0.2939 0.3604 0.0108  -0.0236 -0.0483 484 GLN A C   
1789 O O   . GLN A 220 ? 0.3457 0.2960 0.3826 0.0115  -0.0229 -0.0491 484 GLN A O   
1790 C CB  . GLN A 220 ? 0.4633 0.4003 0.4523 0.0184  -0.0025 -0.0588 484 GLN A CB  
1791 C CG  . GLN A 220 ? 0.5653 0.4984 0.5505 0.0266  0.0163  -0.0589 484 GLN A CG  
1792 C CD  . GLN A 220 ? 0.7673 0.6690 0.7137 0.0268  0.0277  -0.0715 484 GLN A CD  
1793 O OE1 . GLN A 220 ? 0.7819 0.6645 0.7033 0.0191  0.0178  -0.0806 484 GLN A OE1 
1794 N NE2 . GLN A 220 ? 0.8422 0.7359 0.7815 0.0346  0.0491  -0.0722 484 GLN A NE2 
1795 N N   . ILE A 221 ? 0.3208 0.2878 0.3393 0.0042  -0.0346 -0.0461 485 ILE A N   
1796 C CA  . ILE A 221 ? 0.2887 0.2579 0.3169 -0.0033 -0.0456 -0.0443 485 ILE A CA  
1797 C C   . ILE A 221 ? 0.2773 0.2569 0.3281 -0.0015 -0.0439 -0.0357 485 ILE A C   
1798 O O   . ILE A 221 ? 0.2702 0.2430 0.3301 -0.0040 -0.0456 -0.0351 485 ILE A O   
1799 C CB  . ILE A 221 ? 0.3346 0.3138 0.3589 -0.0096 -0.0567 -0.0410 485 ILE A CB  
1800 C CG1 . ILE A 221 ? 0.3890 0.3515 0.3845 -0.0151 -0.0635 -0.0498 485 ILE A CG1 
1801 C CG2 . ILE A 221 ? 0.3118 0.2984 0.3571 -0.0162 -0.0644 -0.0357 485 ILE A CG2 
1802 C CD1 . ILE A 221 ? 0.4699 0.4437 0.4595 -0.0205 -0.0770 -0.0437 485 ILE A CD1 
1803 N N   . PHE A 222 ? 0.2633 0.2553 0.3192 0.0020  -0.0405 -0.0293 486 PHE A N   
1804 C CA  . PHE A 222 ? 0.2652 0.2613 0.3329 0.0018  -0.0401 -0.0219 486 PHE A CA  
1805 C C   . PHE A 222 ? 0.2493 0.2372 0.3254 0.0047  -0.0387 -0.0209 486 PHE A C   
1806 O O   . PHE A 222 ? 0.2745 0.2585 0.3566 0.0020  -0.0417 -0.0158 486 PHE A O   
1807 C CB  . PHE A 222 ? 0.2383 0.2431 0.3048 0.0036  -0.0372 -0.0170 486 PHE A CB  
1808 C CG  . PHE A 222 ? 0.2415 0.2534 0.3058 0.0018  -0.0370 -0.0144 486 PHE A CG  
1809 C CD1 . PHE A 222 ? 0.2910 0.3043 0.3619 -0.0020 -0.0377 -0.0109 486 PHE A CD1 
1810 C CD2 . PHE A 222 ? 0.2470 0.2641 0.3065 0.0045  -0.0342 -0.0135 486 PHE A CD2 
1811 C CE1 . PHE A 222 ? 0.2951 0.3163 0.3711 -0.0017 -0.0350 -0.0065 486 PHE A CE1 
1812 C CE2 . PHE A 222 ? 0.2787 0.3014 0.3401 0.0045  -0.0328 -0.0094 486 PHE A CE2 
1813 C CZ  . PHE A 222 ? 0.3078 0.3334 0.3792 0.0021  -0.0329 -0.0057 486 PHE A CZ  
1814 N N   . GLN A 223 ? 0.2548 0.2400 0.3333 0.0106  -0.0330 -0.0239 487 GLN A N   
1815 C CA  . GLN A 223 ? 0.2638 0.2427 0.3579 0.0153  -0.0306 -0.0210 487 GLN A CA  
1816 C C   . GLN A 223 ? 0.2680 0.2306 0.3629 0.0142  -0.0309 -0.0251 487 GLN A C   
1817 O O   . GLN A 223 ? 0.3276 0.2849 0.4373 0.0164  -0.0322 -0.0191 487 GLN A O   
1818 C CB  . GLN A 223 ? 0.2993 0.2783 0.3993 0.0231  -0.0198 -0.0235 487 GLN A CB  
1819 C CG  . GLN A 223 ? 0.4393 0.4343 0.5517 0.0243  -0.0201 -0.0153 487 GLN A CG  
1820 C CD  . GLN A 223 ? 0.6109 0.6116 0.7498 0.0258  -0.0261 -0.0039 487 GLN A CD  
1821 O OE1 . GLN A 223 ? 0.6171 0.6190 0.7538 0.0197  -0.0379 0.0027  487 GLN A OE1 
1822 N NE2 . GLN A 223 ? 0.7272 0.7302 0.8913 0.0338  -0.0175 -0.0004 487 GLN A NE2 
1823 N N   . HIS A 224 ? 0.3013 0.2545 0.3798 0.0099  -0.0313 -0.0347 488 HIS A N   
1824 C CA  . HIS A 224 ? 0.2991 0.2344 0.3764 0.0061  -0.0331 -0.0396 488 HIS A CA  
1825 C C   . HIS A 224 ? 0.2935 0.2331 0.3805 -0.0006 -0.0410 -0.0314 488 HIS A C   
1826 O O   . HIS A 224 ? 0.3002 0.2275 0.3965 -0.0011 -0.0412 -0.0285 488 HIS A O   
1827 C CB  . HIS A 224 ? 0.3594 0.2835 0.4138 0.0000  -0.0357 -0.0513 488 HIS A CB  
1828 C CG  . HIS A 224 ? 0.3958 0.2961 0.4452 -0.0058 -0.0378 -0.0588 488 HIS A CG  
1829 N ND1 . HIS A 224 ? 0.4009 0.2998 0.4490 -0.0178 -0.0497 -0.0598 488 HIS A ND1 
1830 C CD2 . HIS A 224 ? 0.3713 0.2468 0.4202 -0.0011 -0.0286 -0.0651 488 HIS A CD2 
1831 C CE1 . HIS A 224 ? 0.4045 0.2770 0.4476 -0.0221 -0.0494 -0.0676 488 HIS A CE1 
1832 N NE2 . HIS A 224 ? 0.4815 0.3379 0.5235 -0.0113 -0.0357 -0.0715 488 HIS A NE2 
1833 N N   . LEU A 225 ? 0.2747 0.2296 0.3592 -0.0052 -0.0453 -0.0272 489 LEU A N   
1834 C CA  . LEU A 225 ? 0.2900 0.2482 0.3821 -0.0116 -0.0484 -0.0193 489 LEU A CA  
1835 C C   . LEU A 225 ? 0.3041 0.2616 0.3999 -0.0090 -0.0472 -0.0090 489 LEU A C   
1836 O O   . LEU A 225 ? 0.3296 0.2790 0.4298 -0.0126 -0.0480 -0.0025 489 LEU A O   
1837 C CB  . LEU A 225 ? 0.2582 0.2320 0.3495 -0.0153 -0.0495 -0.0168 489 LEU A CB  
1838 C CG  . LEU A 225 ? 0.2842 0.2594 0.3730 -0.0202 -0.0558 -0.0239 489 LEU A CG  
1839 C CD1 . LEU A 225 ? 0.2707 0.2643 0.3655 -0.0215 -0.0570 -0.0184 489 LEU A CD1 
1840 C CD2 . LEU A 225 ? 0.3660 0.3304 0.4628 -0.0291 -0.0618 -0.0259 489 LEU A CD2 
1841 N N   . HIS A 226 ? 0.2797 0.2447 0.3730 -0.0039 -0.0466 -0.0066 490 HIS A N   
1842 C CA  . HIS A 226 ? 0.3054 0.2699 0.3979 -0.0038 -0.0499 0.0039  490 HIS A CA  
1843 C C   . HIS A 226 ? 0.2807 0.2505 0.3827 0.0025  -0.0516 0.0058  490 HIS A C   
1844 O O   . HIS A 226 ? 0.2814 0.2603 0.3790 0.0022  -0.0526 0.0068  490 HIS A O   
1845 C CB  . HIS A 226 ? 0.2558 0.2245 0.3334 -0.0088 -0.0485 0.0074  490 HIS A CB  
1846 C CG  . HIS A 226 ? 0.3315 0.2964 0.4072 -0.0142 -0.0440 0.0091  490 HIS A CG  
1847 N ND1 . HIS A 226 ? 0.4259 0.3790 0.4989 -0.0181 -0.0439 0.0171  490 HIS A ND1 
1848 C CD2 . HIS A 226 ? 0.3347 0.3072 0.4146 -0.0163 -0.0392 0.0058  490 HIS A CD2 
1849 C CE1 . HIS A 226 ? 0.3835 0.3373 0.4606 -0.0226 -0.0372 0.0180  490 HIS A CE1 
1850 N NE2 . HIS A 226 ? 0.3718 0.3387 0.4557 -0.0216 -0.0349 0.0117  490 HIS A NE2 
1851 N N   . PRO A 227 ? 0.2765 0.2402 0.3951 0.0082  -0.0508 0.0069  491 PRO A N   
1852 C CA  . PRO A 227 ? 0.2609 0.2326 0.3976 0.0150  -0.0504 0.0111  491 PRO A CA  
1853 C C   . PRO A 227 ? 0.3610 0.3398 0.4990 0.0105  -0.0629 0.0245  491 PRO A C   
1854 O O   . PRO A 227 ? 0.3707 0.3411 0.5010 0.0056  -0.0712 0.0332  491 PRO A O   
1855 C CB  . PRO A 227 ? 0.3768 0.3372 0.5344 0.0227  -0.0454 0.0122  491 PRO A CB  
1856 C CG  . PRO A 227 ? 0.3865 0.3317 0.5344 0.0178  -0.0472 0.0109  491 PRO A CG  
1857 C CD  . PRO A 227 ? 0.3304 0.2786 0.4553 0.0088  -0.0487 0.0054  491 PRO A CD  
1858 N N   . ILE A 228 ? 0.3509 0.3421 0.4935 0.0103  -0.0648 0.0260  492 ILE A N   
1859 C CA  . ILE A 228 ? 0.3206 0.3142 0.4563 0.0025  -0.0793 0.0367  492 ILE A CA  
1860 C C   . ILE A 228 ? 0.4811 0.4773 0.6421 0.0037  -0.0923 0.0523  492 ILE A C   
1861 O O   . ILE A 228 ? 0.4687 0.4742 0.6641 0.0125  -0.0877 0.0553  492 ILE A O   
1862 C CB  . ILE A 228 ? 0.3837 0.3872 0.5169 0.0001  -0.0783 0.0335  492 ILE A CB  
1863 C CG1 . ILE A 228 ? 0.3943 0.4109 0.5603 0.0095  -0.0693 0.0327  492 ILE A CG1 
1864 C CG2 . ILE A 228 ? 0.3864 0.3846 0.4904 -0.0031 -0.0696 0.0224  492 ILE A CG2 
1865 C CD1 . ILE A 228 ? 0.4367 0.4648 0.6372 0.0098  -0.0807 0.0477  492 ILE A CD1 
1866 N N   . ALA B 1   ? 0.3892 0.5981 0.6799 0.0135  0.0010  0.1896  265 ALA B N   
1867 C CA  . ALA B 1   ? 0.3492 0.5523 0.6350 0.0281  0.0242  0.1850  265 ALA B CA  
1868 C C   . ALA B 1   ? 0.3913 0.5806 0.6751 0.0549  0.0399  0.1832  265 ALA B C   
1869 O O   . ALA B 1   ? 0.4133 0.5756 0.6802 0.0585  0.0332  0.1746  265 ALA B O   
1870 C CB  . ALA B 1   ? 0.3118 0.4838 0.5565 0.0202  0.0256  0.1642  265 ALA B CB  
1871 N N   . SER B 2   ? 0.4214 0.6298 0.7232 0.0750  0.0602  0.1936  266 SER B N   
1872 C CA  . SER B 2   ? 0.4480 0.6347 0.7361 0.1068  0.0771  0.1877  266 SER B CA  
1873 C C   . SER B 2   ? 0.4363 0.5704 0.6727 0.1123  0.0795  0.1617  266 SER B C   
1874 O O   . SER B 2   ? 0.4374 0.5614 0.6525 0.0962  0.0770  0.1511  266 SER B O   
1875 C CB  . SER B 2   ? 0.5254 0.7476 0.8373 0.1307  0.1020  0.2051  266 SER B CB  
1876 O OG  . SER B 2   ? 0.7038 0.9793 1.0712 0.1242  0.0978  0.2337  266 SER B OG  
1877 N N   . LEU B 3   ? 0.5002 0.5971 0.7158 0.1356  0.0819  0.1517  267 LEU B N   
1878 C CA  . LEU B 3   ? 0.4458 0.4876 0.6118 0.1417  0.0799  0.1279  267 LEU B CA  
1879 C C   . LEU B 3   ? 0.4751 0.5199 0.6194 0.1514  0.0989  0.1221  267 LEU B C   
1880 O O   . LEU B 3   ? 0.4494 0.4691 0.5626 0.1393  0.0944  0.1070  267 LEU B O   
1881 C CB  . LEU B 3   ? 0.4755 0.4727 0.6217 0.1698  0.0777  0.1195  267 LEU B CB  
1882 C CG  . LEU B 3   ? 0.5526 0.4867 0.6446 0.1799  0.0726  0.0951  267 LEU B CG  
1883 C CD1 . LEU B 3   ? 0.5724 0.4900 0.6540 0.1458  0.0525  0.0870  267 LEU B CD1 
1884 C CD2 . LEU B 3   ? 0.6254 0.5084 0.6985 0.2057  0.0630  0.0873  267 LEU B CD2 
1885 N N   . THR B 4   ? 0.4951 0.5745 0.6583 0.1748  0.1213  0.1373  268 THR B N   
1886 C CA  . THR B 4   ? 0.4499 0.5419 0.5977 0.1865  0.1425  0.1386  268 THR B CA  
1887 C C   . THR B 4   ? 0.3956 0.5129 0.5576 0.1514  0.1356  0.1440  268 THR B C   
1888 O O   . THR B 4   ? 0.3845 0.4871 0.5171 0.1495  0.1415  0.1343  268 THR B O   
1889 C CB  . THR B 4   ? 0.4361 0.5769 0.6141 0.2177  0.1699  0.1634  268 THR B CB  
1890 O OG1 . THR B 4   ? 0.5949 0.7029 0.7470 0.2583  0.1785  0.1543  268 THR B OG1 
1891 C CG2 . THR B 4   ? 0.5204 0.6841 0.6882 0.2262  0.1926  0.1713  268 THR B CG2 
1892 N N   . GLU B 5   ? 0.3781 0.5295 0.5817 0.1245  0.1210  0.1589  269 GLU B N   
1893 C CA  . GLU B 5   ? 0.3274 0.4944 0.5391 0.0935  0.1108  0.1621  269 GLU B CA  
1894 C C   . GLU B 5   ? 0.3283 0.4511 0.4990 0.0763  0.0954  0.1373  269 GLU B C   
1895 O O   . GLU B 5   ? 0.3464 0.4666 0.5038 0.0633  0.0951  0.1331  269 GLU B O   
1896 C CB  . GLU B 5   ? 0.3743 0.5796 0.6329 0.0709  0.0937  0.1818  269 GLU B CB  
1897 C CG  . GLU B 5   ? 0.4399 0.6993 0.7498 0.0818  0.1065  0.2129  269 GLU B CG  
1898 C CD  . GLU B 5   ? 0.5196 0.8116 0.8749 0.0588  0.0839  0.2322  269 GLU B CD  
1899 O OE1 . GLU B 5   ? 0.6226 0.9562 1.0192 0.0455  0.0809  0.2576  269 GLU B OE1 
1900 O OE2 . GLU B 5   ? 0.4486 0.7251 0.7994 0.0540  0.0676  0.2244  269 GLU B OE2 
1901 N N   . ILE B 6   ? 0.3078 0.4004 0.4638 0.0755  0.0820  0.1250  270 ILE B N   
1902 C CA  . ILE B 6   ? 0.3059 0.3603 0.4276 0.0626  0.0685  0.1058  270 ILE B CA  
1903 C C   . ILE B 6   ? 0.3620 0.3835 0.4450 0.0758  0.0785  0.0906  270 ILE B C   
1904 O O   . ILE B 6   ? 0.3559 0.3678 0.4198 0.0629  0.0756  0.0823  270 ILE B O   
1905 C CB  . ILE B 6   ? 0.3428 0.3763 0.4633 0.0624  0.0542  0.1027  270 ILE B CB  
1906 C CG1 . ILE B 6   ? 0.3003 0.3684 0.4562 0.0508  0.0444  0.1189  270 ILE B CG1 
1907 C CG2 . ILE B 6   ? 0.3646 0.3655 0.4566 0.0489  0.0408  0.0888  270 ILE B CG2 
1908 C CD1 . ILE B 6   ? 0.3324 0.3875 0.4925 0.0518  0.0321  0.1215  270 ILE B CD1 
1909 N N   . GLU B 7   ? 0.4203 0.4224 0.4883 0.1040  0.0898  0.0868  271 GLU B N   
1910 C CA  . GLU B 7   ? 0.4404 0.4048 0.4628 0.1212  0.0975  0.0708  271 GLU B CA  
1911 C C   . GLU B 7   ? 0.4551 0.4456 0.4754 0.1207  0.1145  0.0773  271 GLU B C   
1912 O O   . GLU B 7   ? 0.4189 0.3846 0.4064 0.1155  0.1120  0.0645  271 GLU B O   
1913 C CB  . GLU B 7   ? 0.5862 0.5224 0.5872 0.1577  0.1063  0.0652  271 GLU B CB  
1914 C CG  . GLU B 7   ? 0.7347 0.6321 0.7321 0.1567  0.0844  0.0574  271 GLU B CG  
1915 C CD  . GLU B 7   ? 0.9846 0.8204 0.9347 0.1884  0.0810  0.0397  271 GLU B CD  
1916 O OE1 . GLU B 7   ? 0.9880 0.8219 0.9396 0.2187  0.0913  0.0435  271 GLU B OE1 
1917 O OE2 . GLU B 7   ? 1.1462 0.9329 1.0561 0.1838  0.0659  0.0220  271 GLU B OE2 
1918 N N   . HIS B 8   ? 0.4035 0.4459 0.4624 0.1229  0.1294  0.0999  272 HIS B N   
1919 C CA  . HIS B 8   ? 0.4516 0.5210 0.5143 0.1178  0.1428  0.1110  272 HIS B CA  
1920 C C   . HIS B 8   ? 0.4106 0.4763 0.4733 0.0835  0.1250  0.1058  272 HIS B C   
1921 O O   . HIS B 8   ? 0.4512 0.5119 0.4948 0.0796  0.1301  0.1035  272 HIS B O   
1922 C CB  . HIS B 8   ? 0.4650 0.5954 0.5790 0.1229  0.1584  0.1425  272 HIS B CB  
1923 C CG  . HIS B 8   ? 0.5870 0.7300 0.6938 0.1640  0.1865  0.1521  272 HIS B CG  
1924 N ND1 . HIS B 8   ? 0.6463 0.7667 0.7395 0.1920  0.1895  0.1431  272 HIS B ND1 
1925 C CD2 . HIS B 8   ? 0.6927 0.8692 0.8026 0.1848  0.2136  0.1714  272 HIS B CD2 
1926 C CE1 . HIS B 8   ? 0.7084 0.8451 0.7925 0.2312  0.2177  0.1540  272 HIS B CE1 
1927 N NE2 . HIS B 8   ? 0.7144 0.8883 0.8088 0.2281  0.2343  0.1724  272 HIS B NE2 
1928 N N   . LEU B 9   ? 0.3768 0.4437 0.4575 0.0614  0.1043  0.1041  273 LEU B N   
1929 C CA  . LEU B 9   ? 0.3270 0.3875 0.4022 0.0350  0.0878  0.0979  273 LEU B CA  
1930 C C   . LEU B 9   ? 0.3454 0.3626 0.3762 0.0357  0.0832  0.0762  273 LEU B C   
1931 O O   . LEU B 9   ? 0.3763 0.3867 0.3917 0.0257  0.0816  0.0719  273 LEU B O   
1932 C CB  . LEU B 9   ? 0.2749 0.3438 0.3702 0.0178  0.0679  0.1001  273 LEU B CB  
1933 C CG  . LEU B 9   ? 0.3298 0.3911 0.4149 -0.0042 0.0507  0.0933  273 LEU B CG  
1934 C CD1 . LEU B 9   ? 0.3563 0.4316 0.4501 -0.0141 0.0527  0.1029  273 LEU B CD1 
1935 C CD2 . LEU B 9   ? 0.3342 0.4050 0.4331 -0.0156 0.0322  0.0967  273 LEU B CD2 
1936 N N   . VAL B 10  ? 0.3565 0.3439 0.3690 0.0468  0.0788  0.0645  274 VAL B N   
1937 C CA  . VAL B 10  ? 0.3847 0.3306 0.3591 0.0471  0.0710  0.0471  274 VAL B CA  
1938 C C   . VAL B 10  ? 0.3922 0.3272 0.3376 0.0596  0.0851  0.0426  274 VAL B C   
1939 O O   . VAL B 10  ? 0.3825 0.3035 0.3075 0.0493  0.0799  0.0351  274 VAL B O   
1940 C CB  . VAL B 10  ? 0.4064 0.3178 0.3670 0.0584  0.0617  0.0384  274 VAL B CB  
1941 C CG1 . VAL B 10  ? 0.4334 0.3013 0.3554 0.0578  0.0511  0.0228  274 VAL B CG1 
1942 C CG2 . VAL B 10  ? 0.3883 0.3108 0.3758 0.0440  0.0469  0.0453  274 VAL B CG2 
1943 N N   . GLN B 11  ? 0.4079 0.3522 0.3511 0.0837  0.1040  0.0491  275 GLN B N   
1944 C CA  . GLN B 11  ? 0.4541 0.3893 0.3645 0.1007  0.1199  0.0466  275 GLN B CA  
1945 C C   . GLN B 11  ? 0.4027 0.3692 0.3290 0.0829  0.1256  0.0597  275 GLN B C   
1946 O O   . GLN B 11  ? 0.4571 0.4078 0.3533 0.0839  0.1285  0.0540  275 GLN B O   
1947 C CB  . GLN B 11  ? 0.4888 0.4341 0.3940 0.1357  0.1426  0.0545  275 GLN B CB  
1948 C CG  . GLN B 11  ? 0.6434 0.5398 0.5157 0.1585  0.1346  0.0365  275 GLN B CG  
1949 C CD  . GLN B 11  ? 0.8188 0.7321 0.6987 0.1930  0.1550  0.0469  275 GLN B CD  
1950 O OE1 . GLN B 11  ? 0.7707 0.7277 0.6654 0.2087  0.1809  0.0663  275 GLN B OE1 
1951 N NE2 . GLN B 11  ? 0.9471 0.8279 0.8201 0.2053  0.1430  0.0368  275 GLN B NE2 
1952 N N   . SER B 12  ? 0.4132 0.4211 0.3864 0.0661  0.1241  0.0780  276 SER B N   
1953 C CA  . SER B 12  ? 0.3671 0.4011 0.3592 0.0478  0.1246  0.0927  276 SER B CA  
1954 C C   . SER B 12  ? 0.3386 0.3455 0.3110 0.0264  0.1056  0.0776  276 SER B C   
1955 O O   . SER B 12  ? 0.4251 0.4302 0.3858 0.0207  0.1081  0.0805  276 SER B O   
1956 C CB  . SER B 12  ? 0.4395 0.5163 0.4855 0.0332  0.1198  0.1149  276 SER B CB  
1957 O OG  . SER B 12  ? 0.5269 0.6199 0.5907 0.0118  0.1125  0.1283  276 SER B OG  
1958 N N   . VAL B 13  ? 0.3975 0.3874 0.3684 0.0164  0.0879  0.0647  277 VAL B N   
1959 C CA  . VAL B 13  ? 0.3780 0.3467 0.3319 0.0007  0.0717  0.0523  277 VAL B CA  
1960 C C   . VAL B 13  ? 0.4259 0.3622 0.3399 0.0092  0.0740  0.0389  277 VAL B C   
1961 O O   . VAL B 13  ? 0.3774 0.3042 0.2769 0.0001  0.0692  0.0355  277 VAL B O   
1962 C CB  . VAL B 13  ? 0.3757 0.3397 0.3373 -0.0067 0.0561  0.0459  277 VAL B CB  
1963 C CG1 . VAL B 13  ? 0.4003 0.3453 0.3424 -0.0167 0.0430  0.0350  277 VAL B CG1 
1964 C CG2 . VAL B 13  ? 0.3732 0.3659 0.3680 -0.0160 0.0503  0.0583  277 VAL B CG2 
1965 N N   . CYS B 14  ? 0.4342 0.3493 0.3278 0.0271  0.0785  0.0309  278 CYS B N   
1966 C CA  . CYS B 14  ? 0.4449 0.3216 0.2956 0.0352  0.0750  0.0166  278 CYS B CA  
1967 C C   . CYS B 14  ? 0.4439 0.3244 0.2743 0.0443  0.0905  0.0215  278 CYS B C   
1968 O O   . CYS B 14  ? 0.4765 0.3357 0.2794 0.0402  0.0845  0.0140  278 CYS B O   
1969 C CB  . CYS B 14  ? 0.4827 0.3267 0.3111 0.0539  0.0714  0.0058  278 CYS B CB  
1970 S SG  . CYS B 14  ? 0.5202 0.3551 0.3714 0.0399  0.0486  0.0031  278 CYS B SG  
1971 N N   . LYS B 15  ? 0.4187 0.3297 0.2649 0.0565  0.1107  0.0373  279 LYS B N   
1972 C CA  . LYS B 15  ? 0.4725 0.3973 0.3064 0.0652  0.1282  0.0491  279 LYS B CA  
1973 C C   . LYS B 15  ? 0.4805 0.4175 0.3309 0.0393  0.1192  0.0570  279 LYS B C   
1974 O O   . LYS B 15  ? 0.4707 0.3967 0.2956 0.0401  0.1221  0.0570  279 LYS B O   
1975 C CB  . LYS B 15  ? 0.5144 0.4815 0.3746 0.0818  0.1521  0.0720  279 LYS B CB  
1976 C CG  . LYS B 15  ? 0.6223 0.6086 0.4687 0.0951  0.1740  0.0892  279 LYS B CG  
1977 C CD  . LYS B 15  ? 0.7097 0.7265 0.5603 0.1278  0.2026  0.1067  279 LYS B CD  
1978 C CE  . LYS B 15  ? 0.8540 0.8692 0.6621 0.1540  0.2236  0.1128  279 LYS B CE  
1979 N NZ  . LYS B 15  ? 0.9456 0.8962 0.6816 0.1730  0.2141  0.0800  279 LYS B NZ  
1980 N N   . SER B 16  ? 0.4122 0.3690 0.3019 0.0185  0.1073  0.0638  280 SER B N   
1981 C CA  . SER B 16  ? 0.4383 0.4020 0.3425 -0.0038 0.0961  0.0712  280 SER B CA  
1982 C C   . SER B 16  ? 0.4160 0.3439 0.2862 -0.0089 0.0827  0.0522  280 SER B C   
1983 O O   . SER B 16  ? 0.4354 0.3567 0.2951 -0.0163 0.0799  0.0551  280 SER B O   
1984 C CB  . SER B 16  ? 0.3833 0.3635 0.3249 -0.0212 0.0809  0.0767  280 SER B CB  
1985 O OG  . SER B 16  ? 0.4804 0.4973 0.4589 -0.0182 0.0912  0.0981  280 SER B OG  
1986 N N   . TYR B 17  ? 0.4193 0.3262 0.2764 -0.0054 0.0734  0.0356  281 TYR B N   
1987 C CA  . TYR B 17  ? 0.4050 0.2828 0.2361 -0.0095 0.0601  0.0212  281 TYR B CA  
1988 C C   . TYR B 17  ? 0.4460 0.3009 0.2378 0.0022  0.0662  0.0165  281 TYR B C   
1989 O O   . TYR B 17  ? 0.5012 0.3453 0.2785 -0.0048 0.0601  0.0151  281 TYR B O   
1990 C CB  . TYR B 17  ? 0.4220 0.2876 0.2545 -0.0087 0.0486  0.0109  281 TYR B CB  
1991 C CG  . TYR B 17  ? 0.4412 0.2818 0.2525 -0.0128 0.0345  0.0013  281 TYR B CG  
1992 C CD1 . TYR B 17  ? 0.4768 0.3227 0.2953 -0.0245 0.0248  0.0020  281 TYR B CD1 
1993 C CD2 . TYR B 17  ? 0.5304 0.3405 0.3130 -0.0035 0.0295  -0.0077 281 TYR B CD2 
1994 C CE1 . TYR B 17  ? 0.5530 0.3819 0.3572 -0.0275 0.0126  -0.0030 281 TYR B CE1 
1995 C CE2 . TYR B 17  ? 0.5560 0.3453 0.3239 -0.0095 0.0135  -0.0132 281 TYR B CE2 
1996 C CZ  . TYR B 17  ? 0.5814 0.3841 0.3636 -0.0218 0.0064  -0.0092 281 TYR B CZ  
1997 O OH  . TYR B 17  ? 0.7865 0.5738 0.5590 -0.0271 -0.0091 -0.0112 281 TYR B OH  
1998 N N   . ARG B 18  ? 0.4556 0.3007 0.2262 0.0223  0.0776  0.0137  282 ARG B N   
1999 C CA  . ARG B 18  ? 0.5142 0.3361 0.2398 0.0377  0.0841  0.0093  282 ARG B CA  
2000 C C   . ARG B 18  ? 0.4971 0.3387 0.2235 0.0340  0.0960  0.0250  282 ARG B C   
2001 O O   . ARG B 18  ? 0.5846 0.4056 0.2779 0.0361  0.0928  0.0209  282 ARG B O   
2002 C CB  . ARG B 18  ? 0.5771 0.3883 0.2767 0.0662  0.0983  0.0059  282 ARG B CB  
2003 C CG  . ARG B 18  ? 0.6344 0.4134 0.3245 0.0712  0.0820  -0.0107 282 ARG B CG  
2004 C CD  . ARG B 18  ? 0.7370 0.4835 0.3793 0.1039  0.0894  -0.0209 282 ARG B CD  
2005 N NE  . ARG B 18  ? 0.7845 0.5652 0.4420 0.1243  0.1166  -0.0068 282 ARG B NE  
2006 C CZ  . ARG B 18  ? 0.7197 0.5168 0.4101 0.1263  0.1190  -0.0027 282 ARG B CZ  
2007 N NH1 . ARG B 18  ? 0.7382 0.5712 0.4455 0.1457  0.1443  0.0134  282 ARG B NH1 
2008 N NH2 . ARG B 18  ? 0.6939 0.4759 0.4036 0.1090  0.0965  -0.0114 282 ARG B NH2 
2009 N N   . GLU B 19  ? 0.5220 0.4030 0.2882 0.0271  0.1073  0.0450  283 GLU B N   
2010 C CA  . GLU B 19  ? 0.4906 0.3952 0.2663 0.0223  0.1184  0.0667  283 GLU B CA  
2011 C C   . GLU B 19  ? 0.4727 0.3660 0.2537 -0.0007 0.0997  0.0652  283 GLU B C   
2012 O O   . GLU B 19  ? 0.5191 0.4202 0.2991 -0.0056 0.1041  0.0804  283 GLU B O   
2013 C CB  . GLU B 19  ? 0.4958 0.4467 0.3204 0.0188  0.1309  0.0923  283 GLU B CB  
2014 C CG  . GLU B 19  ? 0.4672 0.4390 0.2859 0.0476  0.1571  0.1027  283 GLU B CG  
2015 C CD  . GLU B 19  ? 0.5770 0.5968 0.4514 0.0430  0.1660  0.1280  283 GLU B CD  
2016 O OE1 . GLU B 19  ? 0.5672 0.5963 0.4813 0.0175  0.1474  0.1316  283 GLU B OE1 
2017 O OE2 . GLU B 19  ? 0.6050 0.6527 0.4816 0.0675  0.1910  0.1445  283 GLU B OE2 
2018 N N   . THR B 20  ? 0.4439 0.3201 0.2301 -0.0122 0.0801  0.0487  284 THR B N   
2019 C CA  . THR B 20  ? 0.4521 0.3184 0.2440 -0.0296 0.0626  0.0466  284 THR B CA  
2020 C C   . THR B 20  ? 0.4994 0.3371 0.2673 -0.0294 0.0478  0.0276  284 THR B C   
2021 O O   . THR B 20  ? 0.4919 0.3239 0.2669 -0.0397 0.0337  0.0242  284 THR B O   
2022 C CB  . THR B 20  ? 0.3778 0.2592 0.2069 -0.0440 0.0518  0.0513  284 THR B CB  
2023 O OG1 . THR B 20  ? 0.4051 0.2875 0.2409 -0.0399 0.0484  0.0399  284 THR B OG1 
2024 C CG2 . THR B 20  ? 0.3814 0.2942 0.2433 -0.0489 0.0614  0.0754  284 THR B CG2 
2025 N N   . CYS B 21  ? 0.4418 0.3517 0.5278 -0.0280 0.0832  0.0002  285 CYS B N   
2026 C CA  . CYS B 21  ? 0.4074 0.2980 0.4688 -0.0151 0.0655  0.0015  285 CYS B CA  
2027 C C   . CYS B 21  ? 0.5292 0.3856 0.5286 -0.0166 0.0620  0.0032  285 CYS B C   
2028 O O   . CYS B 21  ? 0.5774 0.4224 0.5607 -0.0066 0.0458  0.0045  285 CYS B O   
2029 C CB  . CYS B 21  ? 0.5512 0.4530 0.6407 -0.0015 0.0662  -0.0082 285 CYS B CB  
2030 S SG  . CYS B 21  ? 0.6152 0.5168 0.6948 -0.0012 0.0921  -0.0276 285 CYS B SG  
2031 N N   . GLN B 22  ? 0.5356 0.3784 0.5026 -0.0301 0.0756  0.0042  286 GLN B N   
2032 C CA  . GLN B 22  ? 0.5492 0.3557 0.4580 -0.0343 0.0668  0.0109  286 GLN B CA  
2033 C C   . GLN B 22  ? 0.6207 0.4185 0.4969 -0.0321 0.0745  0.0033  286 GLN B C   
2034 O O   . GLN B 22  ? 0.6814 0.4666 0.5185 -0.0474 0.0846  0.0064  286 GLN B O   
2035 C CB  . GLN B 22  ? 0.6377 0.4261 0.5375 -0.0225 0.0402  0.0160  286 GLN B CB  
2036 C CG  . GLN B 22  ? 0.6835 0.4541 0.5771 -0.0319 0.0291  0.0251  286 GLN B CG  
2037 C CD  . GLN B 22  ? 0.7190 0.4696 0.6004 -0.0191 0.0040  0.0241  286 GLN B CD  
2038 O OE1 . GLN B 22  ? 0.7181 0.4893 0.6232 -0.0078 -0.0047 0.0174  286 GLN B OE1 
2039 N NE2 . GLN B 22  ? 0.6672 0.3796 0.5132 -0.0223 -0.0082 0.0304  286 GLN B NE2 
2040 N N   . LEU B 23  ? 0.4939 0.2984 0.3837 -0.0159 0.0677  -0.0053 287 LEU B N   
2041 C CA  . LEU B 23  ? 0.4840 0.2832 0.3507 -0.0124 0.0731  -0.0157 287 LEU B CA  
2042 C C   . LEU B 23  ? 0.4758 0.2984 0.3897 -0.0009 0.0789  -0.0299 287 LEU B C   
2043 O O   . LEU B 23  ? 0.5510 0.3878 0.5066 0.0069  0.0688  -0.0258 287 LEU B O   
2044 C CB  . LEU B 23  ? 0.4804 0.2562 0.3137 -0.0038 0.0504  -0.0097 287 LEU B CB  
2045 C CG  . LEU B 23  ? 0.5967 0.3424 0.3859 -0.0116 0.0380  0.0040  287 LEU B CG  
2046 C CD1 . LEU B 23  ? 0.6004 0.3321 0.3758 0.0026  0.0130  0.0066  287 LEU B CD1 
2047 C CD2 . LEU B 23  ? 0.7033 0.4363 0.4471 -0.0297 0.0514  0.0058  287 LEU B CD2 
2048 N N   . ARG B 24  ? 0.4682 0.2929 0.3743 -0.0006 0.0921  -0.0462 288 ARG B N   
2049 C CA  . ARG B 24  ? 0.4843 0.3242 0.4371 0.0114  0.0949  -0.0620 288 ARG B CA  
2050 C C   . ARG B 24  ? 0.4404 0.2681 0.3912 0.0221  0.0722  -0.0584 288 ARG B C   
2051 O O   . ARG B 24  ? 0.4814 0.2910 0.3867 0.0203  0.0629  -0.0543 288 ARG B O   
2052 C CB  . ARG B 24  ? 0.5722 0.4199 0.5184 0.0071  0.1196  -0.0868 288 ARG B CB  
2053 C CG  . ARG B 24  ? 0.6955 0.5712 0.6688 -0.0015 0.1454  -0.0965 288 ARG B CG  
2054 C CD  . ARG B 24  ? 0.8312 0.7159 0.7679 -0.0156 0.1731  -0.1167 288 ARG B CD  
2055 N NE  . ARG B 24  ? 0.9814 0.8558 0.9012 -0.0090 0.1738  -0.1380 288 ARG B NE  
2056 C CZ  . ARG B 24  ? 1.0787 0.9587 0.9564 -0.0220 0.1949  -0.1580 288 ARG B CZ  
2057 N NH1 . ARG B 24  ? 1.1100 1.0082 0.9576 -0.0441 0.2177  -0.1568 288 ARG B NH1 
2058 N NH2 . ARG B 24  ? 1.0951 0.9640 0.9586 -0.0160 0.1927  -0.1786 288 ARG B NH2 
2059 N N   . LEU B 25  ? 0.4550 0.2936 0.4563 0.0316  0.0620  -0.0589 289 LEU B N   
2060 C CA  . LEU B 25  ? 0.4272 0.2583 0.4287 0.0374  0.0398  -0.0525 289 LEU B CA  
2061 C C   . LEU B 25  ? 0.4509 0.2656 0.4230 0.0380  0.0421  -0.0678 289 LEU B C   
2062 O O   . LEU B 25  ? 0.4662 0.2708 0.4079 0.0375  0.0271  -0.0611 289 LEU B O   
2063 C CB  . LEU B 25  ? 0.4165 0.2602 0.4771 0.0432  0.0270  -0.0476 289 LEU B CB  
2064 C CG  . LEU B 25  ? 0.4141 0.2531 0.4767 0.0443  0.0035  -0.0383 289 LEU B CG  
2065 C CD1 . LEU B 25  ? 0.4237 0.2684 0.4528 0.0401  -0.0085 -0.0227 289 LEU B CD1 
2066 C CD2 . LEU B 25  ? 0.4291 0.2773 0.5512 0.0463  -0.0116 -0.0299 289 LEU B CD2 
2067 N N   . GLU B 26  ? 0.4583 0.2735 0.4410 0.0387  0.0605  -0.0903 290 GLU B N   
2068 C CA  . GLU B 26  ? 0.5312 0.3314 0.4829 0.0373  0.0637  -0.1086 290 GLU B CA  
2069 C C   . GLU B 26  ? 0.5684 0.3552 0.4516 0.0277  0.0613  -0.1002 290 GLU B C   
2070 O O   . GLU B 26  ? 0.6004 0.3740 0.4566 0.0272  0.0477  -0.1010 290 GLU B O   
2071 C CB  . GLU B 26  ? 0.6442 0.4523 0.6083 0.0371  0.0900  -0.1392 290 GLU B CB  
2072 C CG  . GLU B 26  ? 0.7792 0.5913 0.8091 0.0498  0.0884  -0.1576 290 GLU B CG  
2073 C CD  . GLU B 26  ? 0.8898 0.7048 0.9177 0.0505  0.1118  -0.1966 290 GLU B CD  
2074 O OE1 . GLU B 26  ? 0.9118 0.7167 0.8786 0.0401  0.1182  -0.2058 290 GLU B OE1 
2075 O OE2 . GLU B 26  ? 0.9669 0.7962 1.0546 0.0611  0.1229  -0.2191 290 GLU B OE2 
2076 N N   . ASP B 27  ? 0.5491 0.3386 0.4063 0.0190  0.0726  -0.0916 291 ASP B N   
2077 C CA  . ASP B 27  ? 0.5739 0.3468 0.3674 0.0086  0.0680  -0.0818 291 ASP B CA  
2078 C C   . ASP B 27  ? 0.5822 0.3457 0.3676 0.0154  0.0405  -0.0625 291 ASP B C   
2079 O O   . ASP B 27  ? 0.5951 0.3450 0.3427 0.0134  0.0274  -0.0596 291 ASP B O   
2080 C CB  . ASP B 27  ? 0.6137 0.3885 0.3853 -0.0046 0.0826  -0.0730 291 ASP B CB  
2081 C CG  . ASP B 27  ? 0.8224 0.6088 0.5769 -0.0182 0.1113  -0.0928 291 ASP B CG  
2082 O OD1 . ASP B 27  ? 0.9008 0.6828 0.6267 -0.0221 0.1160  -0.1098 291 ASP B OD1 
2083 O OD2 . ASP B 27  ? 0.8723 0.6757 0.6420 -0.0263 0.1298  -0.0927 291 ASP B OD2 
2084 N N   . LEU B 28  ? 0.4799 0.2545 0.3022 0.0226  0.0320  -0.0508 292 LEU B N   
2085 C CA  . LEU B 28  ? 0.4743 0.2496 0.2962 0.0295  0.0088  -0.0376 292 LEU B CA  
2086 C C   . LEU B 28  ? 0.4852 0.2621 0.3098 0.0335  -0.0047 -0.0426 292 LEU B C   
2087 O O   . LEU B 28  ? 0.5052 0.2784 0.3069 0.0355  -0.0210 -0.0370 292 LEU B O   
2088 C CB  . LEU B 28  ? 0.4362 0.2298 0.2991 0.0340  0.0043  -0.0285 292 LEU B CB  
2089 C CG  . LEU B 28  ? 0.4422 0.2306 0.2953 0.0300  0.0086  -0.0203 292 LEU B CG  
2090 C CD1 . LEU B 28  ? 0.4445 0.2538 0.3407 0.0316  0.0074  -0.0147 292 LEU B CD1 
2091 C CD2 . LEU B 28  ? 0.4570 0.2299 0.2766 0.0328  -0.0077 -0.0126 292 LEU B CD2 
2092 N N   . LEU B 29  ? 0.5174 0.2996 0.3740 0.0346  0.0001  -0.0531 293 LEU B N   
2093 C CA  . LEU B 29  ? 0.4515 0.2334 0.3157 0.0357  -0.0150 -0.0561 293 LEU B CA  
2094 C C   . LEU B 29  ? 0.5383 0.3030 0.3578 0.0310  -0.0156 -0.0672 293 LEU B C   
2095 O O   . LEU B 29  ? 0.5390 0.3037 0.3450 0.0303  -0.0333 -0.0631 293 LEU B O   
2096 C CB  . LEU B 29  ? 0.4396 0.2240 0.3522 0.0378  -0.0133 -0.0642 293 LEU B CB  
2097 C CG  . LEU B 29  ? 0.4436 0.2467 0.4004 0.0397  -0.0208 -0.0483 293 LEU B CG  
2098 C CD1 . LEU B 29  ? 0.4365 0.2373 0.4454 0.0421  -0.0233 -0.0542 293 LEU B CD1 
2099 C CD2 . LEU B 29  ? 0.4837 0.3025 0.4374 0.0368  -0.0410 -0.0312 293 LEU B CD2 
2100 N N   . ARG B 30  ? 0.5544 0.3087 0.3500 0.0257  0.0039  -0.0814 294 ARG B N   
2101 C CA  . ARG B 30  ? 0.6060 0.3456 0.3527 0.0176  0.0042  -0.0927 294 ARG B CA  
2102 C C   . ARG B 30  ? 0.6702 0.4023 0.3724 0.0143  -0.0117 -0.0753 294 ARG B C   
2103 O O   . ARG B 30  ? 0.6623 0.3858 0.3328 0.0099  -0.0249 -0.0772 294 ARG B O   
2104 C CB  . ARG B 30  ? 0.6599 0.3973 0.3870 0.0092  0.0311  -0.1121 294 ARG B CB  
2105 C CG  . ARG B 30  ? 0.5994 0.3422 0.3695 0.0142  0.0456  -0.1388 294 ARG B CG  
2106 C CD  . ARG B 30  ? 0.6452 0.3947 0.3923 0.0047  0.0753  -0.1613 294 ARG B CD  
2107 N NE  . ARG B 30  ? 0.6567 0.4143 0.4496 0.0120  0.0917  -0.1932 294 ARG B NE  
2108 C CZ  . ARG B 30  ? 0.7106 0.4598 0.4972 0.0114  0.0946  -0.2229 294 ARG B CZ  
2109 N NH1 . ARG B 30  ? 0.7886 0.5220 0.5217 0.0017  0.0817  -0.2232 294 ARG B NH1 
2110 N NH2 . ARG B 30  ? 0.7256 0.4819 0.5629 0.0213  0.1088  -0.2543 294 ARG B NH2 
2111 N N   . GLN B 31  ? 0.6083 0.3425 0.3112 0.0168  -0.0126 -0.0591 295 GLN B N   
2112 C CA  . GLN B 31  ? 0.6131 0.3361 0.2808 0.0163  -0.0304 -0.0430 295 GLN B CA  
2113 C C   . GLN B 31  ? 0.6167 0.3513 0.3033 0.0273  -0.0552 -0.0353 295 GLN B C   
2114 O O   . GLN B 31  ? 0.6046 0.3327 0.2727 0.0310  -0.0729 -0.0246 295 GLN B O   
2115 C CB  . GLN B 31  ? 0.6340 0.3512 0.2995 0.0151  -0.0249 -0.0304 295 GLN B CB  
2116 C CG  . GLN B 31  ? 0.7542 0.4618 0.3888 -0.0010 -0.0033 -0.0334 295 GLN B CG  
2117 C CD  . GLN B 31  ? 0.9390 0.6225 0.5200 -0.0128 -0.0148 -0.0169 295 GLN B CD  
2118 O OE1 . GLN B 31  ? 0.9614 0.6325 0.5365 -0.0049 -0.0405 -0.0029 295 GLN B OE1 
2119 N NE2 . GLN B 31  ? 1.0733 0.7515 0.6157 -0.0328 0.0031  -0.0189 295 GLN B NE2 
2120 N N   . ARG B 32  ? 0.5820 0.3352 0.3069 0.0317  -0.0575 -0.0407 296 ARG B N   
2121 C CA  . ARG B 32  ? 0.5332 0.3080 0.2807 0.0388  -0.0772 -0.0340 296 ARG B CA  
2122 C C   . ARG B 32  ? 0.5804 0.3508 0.2992 0.0377  -0.0962 -0.0332 296 ARG B C   
2123 O O   . ARG B 32  ? 0.5512 0.3395 0.2814 0.0453  -0.1131 -0.0271 296 ARG B O   
2124 C CB  . ARG B 32  ? 0.4838 0.2776 0.2725 0.0371  -0.0772 -0.0366 296 ARG B CB  
2125 C CG  . ARG B 32  ? 0.4581 0.2662 0.2831 0.0399  -0.0681 -0.0311 296 ARG B CG  
2126 C CD  . ARG B 32  ? 0.5087 0.3343 0.3740 0.0353  -0.0737 -0.0280 296 ARG B CD  
2127 N NE  . ARG B 32  ? 0.4991 0.3449 0.3947 0.0362  -0.0713 -0.0184 296 ARG B NE  
2128 C CZ  . ARG B 32  ? 0.4858 0.3514 0.4147 0.0296  -0.0796 -0.0091 296 ARG B CZ  
2129 N NH1 . ARG B 32  ? 0.4803 0.3455 0.4191 0.0220  -0.0912 -0.0077 296 ARG B NH1 
2130 N NH2 . ARG B 32  ? 0.4298 0.3151 0.3804 0.0282  -0.0785 0.0002  296 ARG B NH2 
2131 N N   . SER B 33  ? 0.6293 0.3789 0.3113 0.0280  -0.0934 -0.0407 297 SER B N   
2132 C CA  . SER B 33  ? 0.6706 0.4154 0.3222 0.0247  -0.1141 -0.0387 297 SER B CA  
2133 C C   . SER B 33  ? 0.6435 0.3720 0.2605 0.0265  -0.1269 -0.0258 297 SER B C   
2134 O O   . SER B 33  ? 0.6840 0.4100 0.2807 0.0259  -0.1494 -0.0205 297 SER B O   
2135 C CB  . SER B 33  ? 0.7354 0.4651 0.3579 0.0113  -0.1086 -0.0534 297 SER B CB  
2136 O OG  . SER B 33  ? 0.8120 0.5225 0.4013 0.0025  -0.0879 -0.0600 297 SER B OG  
2137 N N   . ASN B 34  ? 0.4713 0.3912 0.3403 0.0268  -0.0554 -0.1413 298 ASN B N   
2138 C CA  . ASN B 34  ? 0.4898 0.4200 0.3523 0.0225  -0.0451 -0.1330 298 ASN B CA  
2139 C C   . ASN B 34  ? 0.4498 0.3989 0.3357 0.0205  -0.0513 -0.1182 298 ASN B C   
2140 O O   . ASN B 34  ? 0.4486 0.4130 0.3600 0.0253  -0.0441 -0.1190 298 ASN B O   
2141 C CB  . ASN B 34  ? 0.5678 0.5048 0.4375 0.0266  -0.0210 -0.1446 298 ASN B CB  
2142 C CG  . ASN B 34  ? 0.6936 0.6241 0.5358 0.0201  -0.0067 -0.1390 298 ASN B CG  
2143 O OD1 . ASN B 34  ? 0.7213 0.6420 0.5385 0.0148  -0.0188 -0.1264 298 ASN B OD1 
2144 N ND2 . ASN B 34  ? 0.6869 0.6203 0.5339 0.0205  0.0191  -0.1497 298 ASN B ND2 
2145 N N   . ILE B 35  ? 0.4207 0.3683 0.2999 0.0136  -0.0650 -0.1067 299 ILE B N   
2146 C CA  . ILE B 35  ? 0.4035 0.3677 0.3068 0.0112  -0.0700 -0.0943 299 ILE B CA  
2147 C C   . ILE B 35  ? 0.3604 0.3309 0.2570 0.0076  -0.0712 -0.0848 299 ILE B C   
2148 O O   . ILE B 35  ? 0.4049 0.3611 0.2754 0.0049  -0.0793 -0.0853 299 ILE B O   
2149 C CB  . ILE B 35  ? 0.4228 0.3808 0.3343 0.0059  -0.0838 -0.0916 299 ILE B CB  
2150 C CG1 . ILE B 35  ? 0.4777 0.4221 0.3898 0.0108  -0.0838 -0.1001 299 ILE B CG1 
2151 C CG2 . ILE B 35  ? 0.4153 0.3882 0.3499 0.0014  -0.0853 -0.0801 299 ILE B CG2 
2152 C CD1 . ILE B 35  ? 0.4963 0.4233 0.4043 0.0043  -0.0953 -0.1008 299 ILE B CD1 
2153 N N   . PHE B 36  ? 0.3683 0.3558 0.2848 0.0086  -0.0653 -0.0767 300 PHE B N   
2154 C CA  . PHE B 36  ? 0.3686 0.3603 0.2803 0.0067  -0.0681 -0.0675 300 PHE B CA  
2155 C C   . PHE B 36  ? 0.4183 0.4088 0.3334 0.0023  -0.0874 -0.0633 300 PHE B C   
2156 O O   . PHE B 36  ? 0.4214 0.4204 0.3611 -0.0014 -0.0932 -0.0625 300 PHE B O   
2157 C CB  . PHE B 36  ? 0.3482 0.3585 0.2851 0.0086  -0.0601 -0.0602 300 PHE B CB  
2158 C CG  . PHE B 36  ? 0.3253 0.3391 0.2635 0.0125  -0.0422 -0.0649 300 PHE B CG  
2159 C CD1 . PHE B 36  ? 0.3395 0.3431 0.2545 0.0115  -0.0313 -0.0656 300 PHE B CD1 
2160 C CD2 . PHE B 36  ? 0.3257 0.3498 0.2876 0.0169  -0.0369 -0.0694 300 PHE B CD2 
2161 C CE1 . PHE B 36  ? 0.3191 0.3283 0.2433 0.0128  -0.0117 -0.0718 300 PHE B CE1 
2162 C CE2 . PHE B 36  ? 0.2862 0.3172 0.2593 0.0205  -0.0229 -0.0765 300 PHE B CE2 
2163 C CZ  . PHE B 36  ? 0.3033 0.3296 0.2621 0.0176  -0.0083 -0.0786 300 PHE B CZ  
2164 N N   . SER B 37  ? 0.3768 0.3545 0.2670 0.0025  -0.0970 -0.0614 301 SER B N   
2165 C CA  . SER B 37  ? 0.3952 0.3723 0.2927 0.0000  -0.1204 -0.0600 301 SER B CA  
2166 C C   . SER B 37  ? 0.3974 0.3987 0.3346 -0.0002 -0.1230 -0.0524 301 SER B C   
2167 O O   . SER B 37  ? 0.3972 0.4090 0.3431 0.0024  -0.1082 -0.0467 301 SER B O   
2168 C CB  . SER B 37  ? 0.5160 0.4657 0.3683 0.0028  -0.1329 -0.0605 301 SER B CB  
2169 O OG  . SER B 37  ? 0.5237 0.4708 0.3648 0.0067  -0.1273 -0.0521 301 SER B OG  
2170 N N   . ARG B 38  ? 0.4321 0.4425 0.3964 -0.0033 -0.1415 -0.0539 302 ARG B N   
2171 C CA  . ARG B 38  ? 0.4239 0.4585 0.4311 -0.0034 -0.1424 -0.0492 302 ARG B CA  
2172 C C   . ARG B 38  ? 0.4244 0.4555 0.4170 0.0045  -0.1440 -0.0418 302 ARG B C   
2173 O O   . ARG B 38  ? 0.4291 0.4765 0.4449 0.0063  -0.1328 -0.0363 302 ARG B O   
2174 C CB  . ARG B 38  ? 0.4554 0.5015 0.5005 -0.0081 -0.1631 -0.0558 302 ARG B CB  
2175 C CG  . ARG B 38  ? 0.5969 0.6713 0.6956 -0.0094 -0.1588 -0.0540 302 ARG B CG  
2176 C CD  . ARG B 38  ? 0.7483 0.8317 0.8587 -0.0144 -0.1300 -0.0497 302 ARG B CD  
2177 N NE  . ARG B 38  ? 0.8113 0.9150 0.9570 -0.0139 -0.1180 -0.0461 302 ARG B NE  
2178 C CZ  . ARG B 38  ? 0.7933 0.8978 0.9267 -0.0072 -0.1064 -0.0385 302 ARG B CZ  
2179 N NH1 . ARG B 38  ? 0.8307 0.9193 0.9225 -0.0013 -0.1046 -0.0343 302 ARG B NH1 
2180 N NH2 . ARG B 38  ? 0.7447 0.8655 0.9090 -0.0068 -0.0954 -0.0364 302 ARG B NH2 
2181 N N   . GLU B 39  ? 0.4070 0.4111 0.3550 0.0091  -0.1566 -0.0418 303 GLU B N   
2182 C CA  . GLU B 39  ? 0.4658 0.4568 0.3902 0.0159  -0.1581 -0.0342 303 GLU B CA  
2183 C C   . GLU B 39  ? 0.3967 0.3876 0.3078 0.0154  -0.1288 -0.0291 303 GLU B C   
2184 O O   . GLU B 39  ? 0.4115 0.4069 0.3290 0.0188  -0.1227 -0.0223 303 GLU B O   
2185 C CB  . GLU B 39  ? 0.6069 0.5584 0.4744 0.0201  -0.1767 -0.0351 303 GLU B CB  
2186 C CG  . GLU B 39  ? 0.8264 0.7562 0.6635 0.0270  -0.1798 -0.0263 303 GLU B CG  
2187 C CD  . GLU B 39  ? 1.0617 0.9483 0.8269 0.0261  -0.1657 -0.0238 303 GLU B CD  
2188 O OE1 . GLU B 39  ? 1.1560 1.0254 0.8962 0.0282  -0.1545 -0.0157 303 GLU B OE1 
2189 O OE2 . GLU B 39  ? 1.1339 1.0020 0.8675 0.0227  -0.1640 -0.0307 303 GLU B OE2 
2190 N N   . GLU B 40  ? 0.4443 0.4301 0.3400 0.0118  -0.1122 -0.0340 304 GLU B N   
2191 C CA  . GLU B 40  ? 0.3684 0.3582 0.2620 0.0115  -0.0863 -0.0327 304 GLU B CA  
2192 C C   . GLU B 40  ? 0.3478 0.3670 0.2872 0.0116  -0.0783 -0.0300 304 GLU B C   
2193 O O   . GLU B 40  ? 0.3374 0.3622 0.2826 0.0132  -0.0650 -0.0264 304 GLU B O   
2194 C CB  . GLU B 40  ? 0.3826 0.3637 0.2592 0.0091  -0.0722 -0.0419 304 GLU B CB  
2195 C CG  . GLU B 40  ? 0.5210 0.4676 0.3436 0.0085  -0.0701 -0.0445 304 GLU B CG  
2196 C CD  . GLU B 40  ? 0.6469 0.5838 0.4541 0.0066  -0.0593 -0.0561 304 GLU B CD  
2197 O OE1 . GLU B 40  ? 0.7544 0.6711 0.5294 0.0050  -0.0400 -0.0606 304 GLU B OE1 
2198 O OE2 . GLU B 40  ? 0.5560 0.5031 0.3829 0.0063  -0.0687 -0.0615 304 GLU B OE2 
2199 N N   . VAL B 41  ? 0.3233 0.3574 0.2920 0.0091  -0.0851 -0.0325 305 VAL B N   
2200 C CA  . VAL B 41  ? 0.3160 0.3696 0.3183 0.0084  -0.0758 -0.0304 305 VAL B CA  
2201 C C   . VAL B 41  ? 0.2950 0.3590 0.3153 0.0114  -0.0789 -0.0237 305 VAL B C   
2202 O O   . VAL B 41  ? 0.2886 0.3614 0.3211 0.0133  -0.0667 -0.0204 305 VAL B O   
2203 C CB  . VAL B 41  ? 0.2856 0.3452 0.3089 0.0030  -0.0796 -0.0341 305 VAL B CB  
2204 C CG1 . VAL B 41  ? 0.2737 0.3466 0.3247 0.0016  -0.0687 -0.0308 305 VAL B CG1 
2205 C CG2 . VAL B 41  ? 0.3096 0.3564 0.3151 0.0017  -0.0761 -0.0406 305 VAL B CG2 
2206 N N   . THR B 42  ? 0.3295 0.3914 0.3525 0.0128  -0.0973 -0.0229 306 THR B N   
2207 C CA  . THR B 42  ? 0.3076 0.3787 0.3512 0.0176  -0.1032 -0.0181 306 THR B CA  
2208 C C   . THR B 42  ? 0.3599 0.4171 0.3757 0.0221  -0.0946 -0.0118 306 THR B C   
2209 O O   . THR B 42  ? 0.3011 0.3680 0.3345 0.0250  -0.0873 -0.0077 306 THR B O   
2210 C CB  . THR B 42  ? 0.3668 0.4363 0.4206 0.0206  -0.1296 -0.0208 306 THR B CB  
2211 O OG1 . THR B 42  ? 0.3727 0.4592 0.4626 0.0142  -0.1338 -0.0283 306 THR B OG1 
2212 C CG2 . THR B 42  ? 0.3644 0.4424 0.4413 0.0280  -0.1365 -0.0171 306 THR B CG2 
2213 N N   . GLY B 43  ? 0.3012 0.3341 0.2734 0.0215  -0.0920 -0.0119 307 GLY B N   
2214 C CA  . GLY B 43  ? 0.3404 0.3564 0.2849 0.0229  -0.0791 -0.0069 307 GLY B CA  
2215 C C   . GLY B 43  ? 0.3314 0.3655 0.2996 0.0212  -0.0579 -0.0075 307 GLY B C   
2216 O O   . GLY B 43  ? 0.3258 0.3596 0.2978 0.0232  -0.0510 -0.0028 307 GLY B O   
2217 N N   . TYR B 44  ? 0.2836 0.3296 0.2649 0.0183  -0.0493 -0.0142 308 TYR B N   
2218 C CA  . TYR B 44  ? 0.2966 0.3561 0.2986 0.0186  -0.0345 -0.0164 308 TYR B CA  
2219 C C   . TYR B 44  ? 0.2282 0.3027 0.2586 0.0211  -0.0370 -0.0120 308 TYR B C   
2220 O O   . TYR B 44  ? 0.2540 0.3325 0.2932 0.0229  -0.0279 -0.0107 308 TYR B O   
2221 C CB  . TYR B 44  ? 0.2454 0.3094 0.2533 0.0175  -0.0301 -0.0250 308 TYR B CB  
2222 C CG  . TYR B 44  ? 0.2481 0.3028 0.2398 0.0163  -0.0194 -0.0330 308 TYR B CG  
2223 C CD1 . TYR B 44  ? 0.2761 0.3347 0.2772 0.0167  -0.0052 -0.0377 308 TYR B CD1 
2224 C CD2 . TYR B 44  ? 0.2508 0.2938 0.2222 0.0144  -0.0227 -0.0380 308 TYR B CD2 
2225 C CE1 . TYR B 44  ? 0.2989 0.3526 0.2945 0.0148  0.0078  -0.0479 308 TYR B CE1 
2226 C CE2 . TYR B 44  ? 0.2666 0.3013 0.2257 0.0131  -0.0090 -0.0478 308 TYR B CE2 
2227 C CZ  . TYR B 44  ? 0.3034 0.3454 0.2783 0.0132  0.0075  -0.0533 308 TYR B CZ  
2228 O OH  . TYR B 44  ? 0.3390 0.3765 0.3113 0.0112  0.0237  -0.0656 308 TYR B OH  
2229 N N   . GLN B 45  ? 0.2603 0.3426 0.3068 0.0206  -0.0479 -0.0110 309 GLN B N   
2230 C CA  . GLN B 45  ? 0.2297 0.3260 0.3054 0.0219  -0.0456 -0.0090 309 GLN B CA  
2231 C C   . GLN B 45  ? 0.2524 0.3484 0.3324 0.0271  -0.0482 -0.0036 309 GLN B C   
2232 O O   . GLN B 45  ? 0.2770 0.3815 0.3758 0.0293  -0.0413 -0.0024 309 GLN B O   
2233 C CB  . GLN B 45  ? 0.2470 0.3527 0.3452 0.0182  -0.0537 -0.0118 309 GLN B CB  
2234 C CG  . GLN B 45  ? 0.2301 0.3322 0.3241 0.0125  -0.0480 -0.0162 309 GLN B CG  
2235 C CD  . GLN B 45  ? 0.2286 0.3372 0.3449 0.0059  -0.0528 -0.0201 309 GLN B CD  
2236 O OE1 . GLN B 45  ? 0.2840 0.4006 0.4178 0.0059  -0.0667 -0.0218 309 GLN B OE1 
2237 N NE2 . GLN B 45  ? 0.2696 0.3719 0.3848 0.0002  -0.0427 -0.0223 309 GLN B NE2 
2238 N N   A ARG B 46  ? 0.2311 0.3121 0.2880 0.0293  -0.0583 -0.0006 310 ARG B N   
2239 N N   B ARG B 46  ? 0.2291 0.3101 0.2861 0.0293  -0.0583 -0.0006 310 ARG B N   
2240 C CA  A ARG B 46  ? 0.2587 0.3307 0.3115 0.0352  -0.0645 0.0052  310 ARG B CA  
2241 C CA  B ARG B 46  ? 0.2584 0.3307 0.3117 0.0352  -0.0642 0.0052  310 ARG B CA  
2242 C C   A ARG B 46  ? 0.2485 0.3073 0.2811 0.0346  -0.0497 0.0086  310 ARG B C   
2243 C C   B ARG B 46  ? 0.2441 0.3035 0.2777 0.0347  -0.0495 0.0086  310 ARG B C   
2244 O O   A ARG B 46  ? 0.2746 0.3225 0.3018 0.0390  -0.0526 0.0139  310 ARG B O   
2245 O O   B ARG B 46  ? 0.2726 0.3217 0.3019 0.0391  -0.0521 0.0138  310 ARG B O   
2246 C CB  A ARG B 46  ? 0.3207 0.3732 0.3499 0.0387  -0.0857 0.0071  310 ARG B CB  
2247 C CB  B ARG B 46  ? 0.3158 0.3684 0.3452 0.0388  -0.0852 0.0073  310 ARG B CB  
2248 C CG  A ARG B 46  ? 0.3308 0.3983 0.3953 0.0435  -0.1068 0.0036  310 ARG B CG  
2249 C CG  B ARG B 46  ? 0.3017 0.3684 0.3592 0.0401  -0.1045 0.0020  310 ARG B CG  
2250 C CD  A ARG B 46  ? 0.3727 0.4592 0.4768 0.0479  -0.1011 0.0039  310 ARG B CD  
2251 C CD  B ARG B 46  ? 0.4176 0.4593 0.4447 0.0447  -0.1297 0.0025  310 ARG B CD  
2252 N NE  A ARG B 46  ? 0.4565 0.5506 0.5921 0.0565  -0.1224 0.0009  310 ARG B NE  
2253 N NE  B ARG B 46  ? 0.5171 0.5567 0.5610 0.0549  -0.1511 0.0035  310 ARG B NE  
2254 C CZ  A ARG B 46  ? 0.4457 0.5411 0.5974 0.0645  -0.1236 0.0029  310 ARG B CZ  
2255 C CZ  B ARG B 46  ? 0.5791 0.5921 0.5930 0.0619  -0.1559 0.0109  310 ARG B CZ  
2256 N NH1 A ARG B 46  ? 0.4806 0.5683 0.6157 0.0636  -0.1049 0.0086  310 ARG B NH1 
2257 N NH1 B ARG B 46  ? 0.5909 0.5784 0.5581 0.0574  -0.1373 0.0177  310 ARG B NH1 
2258 N NH2 A ARG B 46  ? 0.4951 0.5987 0.6811 0.0740  -0.1445 -0.0021 310 ARG B NH2 
2259 N NH2 B ARG B 46  ? 0.5533 0.5640 0.5860 0.0732  -0.1790 0.0105  310 ARG B NH2 
2260 N N   . LYS B 47  ? 0.2675 0.3263 0.2916 0.0294  -0.0349 0.0043  311 LYS B N   
2261 C CA  . LYS B 47  ? 0.2261 0.2774 0.2423 0.0272  -0.0192 0.0041  311 LYS B CA  
2262 C C   . LYS B 47  ? 0.2292 0.2945 0.2730 0.0304  -0.0148 0.0042  311 LYS B C   
2263 O O   . LYS B 47  ? 0.2513 0.3322 0.3172 0.0325  -0.0181 0.0024  311 LYS B O   
2264 C CB  . LYS B 47  ? 0.2345 0.2879 0.2472 0.0221  -0.0065 -0.0045 311 LYS B CB  
2265 C CG  . LYS B 47  ? 0.2934 0.3283 0.2737 0.0183  -0.0060 -0.0058 311 LYS B CG  
2266 C CD  . LYS B 47  ? 0.3043 0.3439 0.2883 0.0141  0.0083  -0.0171 311 LYS B CD  
2267 C CE  . LYS B 47  ? 0.3766 0.3948 0.3249 0.0100  0.0120  -0.0197 311 LYS B CE  
2268 N NZ  . LYS B 47  ? 0.4417 0.4292 0.3521 0.0056  0.0223  -0.0142 311 LYS B NZ  
2269 N N   . SER B 48  ? 0.2258 0.2818 0.2653 0.0298  -0.0056 0.0059  312 SER B N   
2270 C CA  . SER B 48  ? 0.2165 0.2823 0.2784 0.0329  -0.0015 0.0048  312 SER B CA  
2271 C C   . SER B 48  ? 0.2291 0.3062 0.3042 0.0311  0.0056  -0.0045 312 SER B C   
2272 O O   . SER B 48  ? 0.2504 0.3272 0.3201 0.0272  0.0100  -0.0106 312 SER B O   
2273 C CB  . SER B 48  ? 0.2243 0.2744 0.2779 0.0322  0.0053  0.0083  312 SER B CB  
2274 O OG  . SER B 48  ? 0.3197 0.3604 0.3613 0.0245  0.0185  0.0038  312 SER B OG  
2275 N N   . MET B 49  ? 0.2681 0.3285 0.3114 0.0159  -0.0312 -0.0336 313 MET B N   
2276 C CA  . MET B 49  ? 0.2616 0.3165 0.3012 0.0131  -0.0263 -0.0356 313 MET B CA  
2277 C C   . MET B 49  ? 0.2658 0.3036 0.3006 0.0120  -0.0271 -0.0333 313 MET B C   
2278 O O   . MET B 49  ? 0.2763 0.3081 0.3058 0.0068  -0.0237 -0.0324 313 MET B O   
2279 C CB  . MET B 49  ? 0.2665 0.3300 0.3096 0.0215  -0.0244 -0.0407 313 MET B CB  
2280 C CG  . MET B 49  ? 0.2522 0.3132 0.2896 0.0208  -0.0202 -0.0427 313 MET B CG  
2281 S SD  . MET B 49  ? 0.4670 0.5367 0.5023 0.0371  -0.0215 -0.0524 313 MET B SD  
2282 C CE  . MET B 49  ? 0.5279 0.6308 0.5660 0.0413  -0.0114 -0.0458 313 MET B CE  
2283 N N   . TRP B 50  ? 0.2698 0.3004 0.3105 0.0169  -0.0321 -0.0305 314 TRP B N   
2284 C CA  . TRP B 50  ? 0.2798 0.2966 0.3248 0.0156  -0.0336 -0.0241 314 TRP B CA  
2285 C C   . TRP B 50  ? 0.2495 0.2674 0.2851 0.0108  -0.0289 -0.0152 314 TRP B C   
2286 O O   . TRP B 50  ? 0.2808 0.2929 0.3158 0.0073  -0.0258 -0.0120 314 TRP B O   
2287 C CB  . TRP B 50  ? 0.3695 0.3796 0.4294 0.0215  -0.0411 -0.0194 314 TRP B CB  
2288 C CG  . TRP B 50  ? 0.5981 0.5984 0.6696 0.0192  -0.0427 -0.0058 314 TRP B CG  
2289 C CD1 . TRP B 50  ? 0.7380 0.7252 0.8253 0.0173  -0.0471 -0.0046 314 TRP B CD1 
2290 C CD2 . TRP B 50  ? 0.7563 0.7628 0.8276 0.0194  -0.0399 0.0115  314 TRP B CD2 
2291 N NE1 . TRP B 50  ? 0.7502 0.7353 0.8517 0.0146  -0.0465 0.0150  314 TRP B NE1 
2292 C CE2 . TRP B 50  ? 0.8455 0.8441 0.9354 0.0169  -0.0409 0.0260  314 TRP B CE2 
2293 C CE3 . TRP B 50  ? 0.7130 0.7331 0.7709 0.0228  -0.0374 0.0165  314 TRP B CE3 
2294 C CZ2 . TRP B 50  ? 0.8525 0.8598 0.9475 0.0186  -0.0367 0.0488  314 TRP B CZ2 
2295 C CZ3 . TRP B 50  ? 0.7204 0.7481 0.7783 0.0261  -0.0346 0.0356  314 TRP B CZ3 
2296 C CH2 . TRP B 50  ? 0.7842 0.8072 0.8603 0.0243  -0.0329 0.0531  314 TRP B CH2 
2297 N N   . GLU B 51  ? 0.2538 0.2815 0.2812 0.0123  -0.0291 -0.0130 315 GLU B N   
2298 C CA  . GLU B 51  ? 0.2603 0.2920 0.2749 0.0127  -0.0261 -0.0077 315 GLU B CA  
2299 C C   . GLU B 51  ? 0.2677 0.2977 0.2744 0.0075  -0.0232 -0.0158 315 GLU B C   
2300 O O   . GLU B 51  ? 0.2561 0.2841 0.2560 0.0076  -0.0192 -0.0119 315 GLU B O   
2301 C CB  . GLU B 51  ? 0.2459 0.2891 0.2518 0.0185  -0.0302 -0.0073 315 GLU B CB  
2302 C CG  . GLU B 51  ? 0.3103 0.3598 0.2986 0.0232  -0.0284 -0.0054 315 GLU B CG  
2303 C CD  . GLU B 51  ? 0.4161 0.4782 0.3915 0.0321  -0.0347 -0.0079 315 GLU B CD  
2304 O OE1 . GLU B 51  ? 0.3753 0.4423 0.3563 0.0349  -0.0392 -0.0057 315 GLU B OE1 
2305 O OE2 . GLU B 51  ? 0.4059 0.4734 0.3645 0.0383  -0.0360 -0.0131 315 GLU B OE2 
2306 N N   . MET B 52  ? 0.2406 0.2733 0.2507 0.0037  -0.0249 -0.0250 316 MET B N   
2307 C CA  . MET B 52  ? 0.2206 0.2511 0.2288 -0.0018 -0.0229 -0.0304 316 MET B CA  
2308 C C   . MET B 52  ? 0.2515 0.2738 0.2607 -0.0043 -0.0176 -0.0283 316 MET B C   
2309 O O   . MET B 52  ? 0.2658 0.2838 0.2697 -0.0066 -0.0151 -0.0288 316 MET B O   
2310 C CB  . MET B 52  ? 0.2679 0.3062 0.2873 -0.0059 -0.0251 -0.0349 316 MET B CB  
2311 C CG  . MET B 52  ? 0.2571 0.3022 0.2790 -0.0052 -0.0335 -0.0389 316 MET B CG  
2312 S SD  . MET B 52  ? 0.3310 0.3693 0.3418 -0.0042 -0.0395 -0.0463 316 MET B SD  
2313 C CE  . MET B 52  ? 0.2714 0.3041 0.2970 -0.0138 -0.0387 -0.0480 316 MET B CE  
2314 N N   . TRP B 53  ? 0.2359 0.2558 0.2524 -0.0025 -0.0175 -0.0276 317 TRP B N   
2315 C CA  . TRP B 53  ? 0.2324 0.2444 0.2512 -0.0036 -0.0156 -0.0276 317 TRP B CA  
2316 C C   . TRP B 53  ? 0.2445 0.2505 0.2632 -0.0043 -0.0142 -0.0194 317 TRP B C   
2317 O O   . TRP B 53  ? 0.2703 0.2727 0.2872 -0.0070 -0.0110 -0.0188 317 TRP B O   
2318 C CB  . TRP B 53  ? 0.2300 0.2405 0.2571 0.0017  -0.0200 -0.0322 317 TRP B CB  
2319 C CG  . TRP B 53  ? 0.2584 0.2578 0.2931 0.0028  -0.0238 -0.0331 317 TRP B CG  
2320 C CD1 . TRP B 53  ? 0.2512 0.2412 0.3007 0.0061  -0.0319 -0.0319 317 TRP B CD1 
2321 C CD2 . TRP B 53  ? 0.2578 0.2538 0.2902 0.0005  -0.0221 -0.0352 317 TRP B CD2 
2322 N NE1 . TRP B 53  ? 0.2832 0.2640 0.3418 0.0056  -0.0366 -0.0343 317 TRP B NE1 
2323 C CE2 . TRP B 53  ? 0.2676 0.2527 0.3140 0.0027  -0.0304 -0.0368 317 TRP B CE2 
2324 C CE3 . TRP B 53  ? 0.2778 0.2785 0.3008 -0.0030 -0.0159 -0.0358 317 TRP B CE3 
2325 C CZ2 . TRP B 53  ? 0.2723 0.2522 0.3218 0.0016  -0.0327 -0.0395 317 TRP B CZ2 
2326 C CZ3 . TRP B 53  ? 0.2790 0.2748 0.3027 -0.0035 -0.0166 -0.0374 317 TRP B CZ3 
2327 C CH2 . TRP B 53  ? 0.2805 0.2667 0.3166 -0.0011 -0.0249 -0.0397 317 TRP B CH2 
2328 N N   . GLU B 54  ? 0.2177 0.2254 0.2395 -0.0011 -0.0155 -0.0108 318 GLU B N   
2329 C CA  . GLU B 54  ? 0.2316 0.2397 0.2564 -0.0004 -0.0119 0.0021  318 GLU B CA  
2330 C C   . GLU B 54  ? 0.2475 0.2613 0.2558 0.0007  -0.0065 0.0006  318 GLU B C   
2331 O O   . GLU B 54  ? 0.2684 0.2821 0.2776 0.0002  -0.0021 0.0061  318 GLU B O   
2332 C CB  . GLU B 54  ? 0.3161 0.3301 0.3474 0.0047  -0.0129 0.0160  318 GLU B CB  
2333 C CG  . GLU B 54  ? 0.3251 0.3304 0.3785 0.0043  -0.0202 0.0189  318 GLU B CG  
2334 C CD  . GLU B 54  ? 0.5270 0.5382 0.5927 0.0086  -0.0206 0.0386  318 GLU B CD  
2335 O OE1 . GLU B 54  ? 0.5247 0.5267 0.6165 0.0077  -0.0276 0.0456  318 GLU B OE1 
2336 O OE2 . GLU B 54  ? 0.6125 0.6384 0.6631 0.0140  -0.0149 0.0473  318 GLU B OE2 
2337 N N   . ARG B 55  ? 0.2486 0.2673 0.2441 0.0030  -0.0086 -0.0077 319 ARG B N   
2338 C CA  . ARG B 55  ? 0.2478 0.2695 0.2288 0.0061  -0.0075 -0.0134 319 ARG B CA  
2339 C C   . ARG B 55  ? 0.2936 0.3069 0.2775 -0.0002 -0.0058 -0.0196 319 ARG B C   
2340 O O   . ARG B 55  ? 0.2916 0.3047 0.2698 0.0021  -0.0023 -0.0187 319 ARG B O   
2341 C CB  . ARG B 55  ? 0.2857 0.3115 0.2588 0.0090  -0.0148 -0.0242 319 ARG B CB  
2342 C CG  . ARG B 55  ? 0.3259 0.3629 0.2905 0.0184  -0.0169 -0.0190 319 ARG B CG  
2343 C CD  . ARG B 55  ? 0.3417 0.3820 0.3007 0.0213  -0.0274 -0.0325 319 ARG B CD  
2344 N NE  . ARG B 55  ? 0.4136 0.4668 0.3617 0.0326  -0.0302 -0.0277 319 ARG B NE  
2345 C CZ  . ARG B 55  ? 0.4403 0.5039 0.3688 0.0462  -0.0351 -0.0333 319 ARG B CZ  
2346 N NH1 . ARG B 55  ? 0.4622 0.5226 0.3808 0.0506  -0.0396 -0.0469 319 ARG B NH1 
2347 N NH2 . ARG B 55  ? 0.4752 0.5532 0.3936 0.0574  -0.0366 -0.0259 319 ARG B NH2 
2348 N N   . CYS B 56  ? 0.2482 0.2572 0.2407 -0.0066 -0.0078 -0.0249 320 CYS B N   
2349 C CA  . CYS B 56  ? 0.3139 0.3180 0.3090 -0.0116 -0.0065 -0.0291 320 CYS B CA  
2350 C C   . CYS B 56  ? 0.2652 0.2649 0.2643 -0.0128 -0.0025 -0.0242 320 CYS B C   
2351 O O   . CYS B 56  ? 0.2879 0.2840 0.2859 -0.0147 -0.0003 -0.0253 320 CYS B O   
2352 C CB  . CYS B 56  ? 0.2642 0.2714 0.2680 -0.0158 -0.0085 -0.0324 320 CYS B CB  
2353 S SG  . CYS B 56  ? 0.2991 0.3112 0.3065 -0.0164 -0.0161 -0.0380 320 CYS B SG  
2354 N N   . ALA B 57  ? 0.2207 0.2197 0.2272 -0.0116 -0.0033 -0.0190 321 ALA B N   
2355 C CA  . ALA B 57  ? 0.2433 0.2375 0.2590 -0.0128 -0.0028 -0.0148 321 ALA B CA  
2356 C C   . ALA B 57  ? 0.2780 0.2752 0.2914 -0.0113 0.0023  -0.0066 321 ALA B C   
2357 O O   . ALA B 57  ? 0.2842 0.2791 0.3016 -0.0130 0.0041  -0.0052 321 ALA B O   
2358 C CB  . ALA B 57  ? 0.2479 0.2386 0.2787 -0.0117 -0.0084 -0.0111 321 ALA B CB  
2359 N N   . HIS B 58  ? 0.2386 0.2437 0.2448 -0.0061 0.0047  -0.0011 322 HIS B N   
2360 C CA  . HIS B 58  ? 0.2699 0.2836 0.2699 -0.0002 0.0109  0.0066  322 HIS B CA  
2361 C C   . HIS B 58  ? 0.2644 0.2741 0.2529 0.0004  0.0115  -0.0045 322 HIS B C   
2362 O O   . HIS B 58  ? 0.2639 0.2752 0.2540 0.0018  0.0157  -0.0010 322 HIS B O   
2363 C CB  . HIS B 58  ? 0.3349 0.3618 0.3233 0.0095  0.0128  0.0125  322 HIS B CB  
2364 C CG  . HIS B 58  ? 0.4188 0.4586 0.3933 0.0206  0.0189  0.0160  322 HIS B CG  
2365 N ND1 . HIS B 58  ? 0.4484 0.5014 0.4324 0.0248  0.0271  0.0344  322 HIS B ND1 
2366 C CD2 . HIS B 58  ? 0.5046 0.5474 0.4584 0.0300  0.0170  0.0030  322 HIS B CD2 
2367 C CE1 . HIS B 58  ? 0.5124 0.5787 0.4784 0.0379  0.0321  0.0331  322 HIS B CE1 
2368 N NE2 . HIS B 58  ? 0.5441 0.6028 0.4906 0.0418  0.0248  0.0121  322 HIS B NE2 
2369 N N   . HIS B 59  ? 0.2421 0.2469 0.2229 -0.0007 0.0065  -0.0170 323 HIS B N   
2370 C CA  . HIS B 59  ? 0.2272 0.2260 0.2031 -0.0006 0.0045  -0.0266 323 HIS B CA  
2371 C C   . HIS B 59  ? 0.2859 0.2778 0.2711 -0.0074 0.0065  -0.0252 323 HIS B C   
2372 O O   . HIS B 59  ? 0.2742 0.2636 0.2575 -0.0051 0.0081  -0.0268 323 HIS B O   
2373 C CB  . HIS B 59  ? 0.2626 0.2571 0.2383 -0.0027 -0.0035 -0.0375 323 HIS B CB  
2374 C CG  . HIS B 59  ? 0.2806 0.2821 0.2455 0.0057  -0.0080 -0.0417 323 HIS B CG  
2375 N ND1 . HIS B 59  ? 0.3621 0.3721 0.3113 0.0190  -0.0069 -0.0426 323 HIS B ND1 
2376 C CD2 . HIS B 59  ? 0.2682 0.2724 0.2350 0.0048  -0.0140 -0.0450 323 HIS B CD2 
2377 C CE1 . HIS B 59  ? 0.3725 0.3898 0.3123 0.0264  -0.0124 -0.0469 323 HIS B CE1 
2378 N NE2 . HIS B 59  ? 0.3063 0.3190 0.2577 0.0170  -0.0173 -0.0486 323 HIS B NE2 
2379 N N   . LEU B 60  ? 0.2705 0.2609 0.2646 -0.0134 0.0058  -0.0230 324 LEU B N   
2380 C CA  . LEU B 60  ? 0.2503 0.2371 0.2508 -0.0174 0.0065  -0.0224 324 LEU B CA  
2381 C C   . LEU B 60  ? 0.2462 0.2336 0.2512 -0.0159 0.0093  -0.0163 324 LEU B C   
2382 O O   . LEU B 60  ? 0.2735 0.2586 0.2794 -0.0161 0.0108  -0.0162 324 LEU B O   
2383 C CB  . LEU B 60  ? 0.2818 0.2704 0.2873 -0.0191 0.0039  -0.0234 324 LEU B CB  
2384 C CG  . LEU B 60  ? 0.3482 0.3366 0.3573 -0.0190 0.0029  -0.0240 324 LEU B CG  
2385 C CD1 . LEU B 60  ? 0.3733 0.3632 0.3801 -0.0206 0.0053  -0.0235 324 LEU B CD1 
2386 C CD2 . LEU B 60  ? 0.3889 0.3805 0.4003 -0.0157 -0.0017 -0.0280 324 LEU B CD2 
2387 N N   . THR B 61  ? 0.2533 0.2447 0.2652 -0.0144 0.0096  -0.0089 325 THR B N   
2388 C CA  . THR B 61  ? 0.2524 0.2466 0.2766 -0.0142 0.0115  0.0003  325 THR B CA  
2389 C C   . THR B 61  ? 0.2564 0.2571 0.2740 -0.0088 0.0180  0.0040  325 THR B C   
2390 O O   . THR B 61  ? 0.2586 0.2602 0.2839 -0.0093 0.0196  0.0073  325 THR B O   
2391 C CB  . THR B 61  ? 0.2552 0.2539 0.2950 -0.0141 0.0100  0.0115  325 THR B CB  
2392 O OG1 . THR B 61  ? 0.3930 0.3828 0.4432 -0.0178 0.0011  0.0051  325 THR B OG1 
2393 C CG2 . THR B 61  ? 0.5010 0.5081 0.5583 -0.0134 0.0137  0.0266  325 THR B CG2 
2394 N N   . GLU B 62  ? 0.2373 0.2435 0.2401 -0.0019 0.0207  0.0019  326 GLU B N   
2395 C CA  . GLU B 62  ? 0.2299 0.2433 0.2221 0.0076  0.0254  0.0012  326 GLU B CA  
2396 C C   . GLU B 62  ? 0.2536 0.2559 0.2428 0.0058  0.0227  -0.0095 326 GLU B C   
2397 O O   . GLU B 62  ? 0.2607 0.2670 0.2515 0.0104  0.0266  -0.0066 326 GLU B O   
2398 C CB  . GLU B 62  ? 0.2992 0.3200 0.2734 0.0182  0.0250  -0.0038 326 GLU B CB  
2399 C CG  . GLU B 62  ? 0.3497 0.3792 0.3089 0.0329  0.0278  -0.0086 326 GLU B CG  
2400 C CD  . GLU B 62  ? 0.5731 0.6138 0.5120 0.0477  0.0259  -0.0144 326 GLU B CD  
2401 O OE1 . GLU B 62  ? 0.5832 0.6181 0.5189 0.0440  0.0191  -0.0209 326 GLU B OE1 
2402 O OE2 . GLU B 62  ? 0.6714 0.7290 0.5967 0.0648  0.0310  -0.0126 326 GLU B OE2 
2403 N N   . ALA B 63  ? 0.2629 0.2535 0.2512 -0.0007 0.0166  -0.0190 327 ALA B N   
2404 C CA  . ALA B 63  ? 0.2296 0.2103 0.2199 -0.0028 0.0137  -0.0253 327 ALA B CA  
2405 C C   . ALA B 63  ? 0.2537 0.2343 0.2536 -0.0070 0.0164  -0.0186 327 ALA B C   
2406 O O   . ALA B 63  ? 0.2546 0.2325 0.2558 -0.0043 0.0171  -0.0193 327 ALA B O   
2407 C CB  . ALA B 63  ? 0.2770 0.2501 0.2710 -0.0096 0.0079  -0.0307 327 ALA B CB  
2408 N N   . ILE B 64  ? 0.2634 0.2465 0.2705 -0.0119 0.0158  -0.0137 328 ILE B N   
2409 C CA  . ILE B 64  ? 0.2329 0.2163 0.2497 -0.0144 0.0149  -0.0099 328 ILE B CA  
2410 C C   . ILE B 64  ? 0.2504 0.2406 0.2746 -0.0106 0.0189  -0.0025 328 ILE B C   
2411 O O   . ILE B 64  ? 0.2458 0.2358 0.2752 -0.0102 0.0188  -0.0012 328 ILE B O   
2412 C CB  . ILE B 64  ? 0.2169 0.2008 0.2410 -0.0177 0.0098  -0.0100 328 ILE B CB  
2413 C CG1 . ILE B 64  ? 0.2605 0.2427 0.2771 -0.0189 0.0073  -0.0160 328 ILE B CG1 
2414 C CG2 . ILE B 64  ? 0.2872 0.2722 0.3245 -0.0182 0.0055  -0.0076 328 ILE B CG2 
2415 C CD1 . ILE B 64  ? 0.3697 0.3533 0.3900 -0.0182 0.0016  -0.0193 328 ILE B CD1 
2416 N N   . GLN B 65  ? 0.2183 0.2177 0.2441 -0.0066 0.0230  0.0044  329 GLN B N   
2417 C CA  . GLN B 65  ? 0.2382 0.2507 0.2745 -0.0015 0.0290  0.0161  329 GLN B CA  
2418 C C   . GLN B 65  ? 0.2412 0.2539 0.2672 0.0061  0.0324  0.0109  329 GLN B C   
2419 O O   . GLN B 65  ? 0.2367 0.2561 0.2734 0.0082  0.0351  0.0173  329 GLN B O   
2420 C CB  . GLN B 65  ? 0.2536 0.2811 0.2901 0.0048  0.0351  0.0273  329 GLN B CB  
2421 C CG  . GLN B 65  ? 0.4700 0.5008 0.5291 -0.0018 0.0323  0.0397  329 GLN B CG  
2422 C CD  . GLN B 65  ? 0.6391 0.6840 0.6958 0.0044  0.0380  0.0516  329 GLN B CD  
2423 O OE1 . GLN B 65  ? 0.6987 0.7527 0.7331 0.0156  0.0438  0.0486  329 GLN B OE1 
2424 N NE2 . GLN B 65  ? 0.6631 0.7099 0.7436 -0.0014 0.0347  0.0645  329 GLN B NE2 
2425 N N   . TYR B 66  ? 0.2383 0.2441 0.2466 0.0111  0.0310  -0.0007 330 TYR B N   
2426 C CA  . TYR B 66  ? 0.2602 0.2632 0.2609 0.0199  0.0312  -0.0083 330 TYR B CA  
2427 C C   . TYR B 66  ? 0.2614 0.2525 0.2705 0.0129  0.0273  -0.0103 330 TYR B C   
2428 O O   . TYR B 66  ? 0.2588 0.2509 0.2704 0.0188  0.0287  -0.0103 330 TYR B O   
2429 C CB  . TYR B 66  ? 0.2924 0.2871 0.2773 0.0267  0.0257  -0.0231 330 TYR B CB  
2430 C CG  . TYR B 66  ? 0.3044 0.3148 0.2747 0.0417  0.0296  -0.0238 330 TYR B CG  
2431 C CD1 . TYR B 66  ? 0.3876 0.4074 0.3549 0.0405  0.0319  -0.0171 330 TYR B CD1 
2432 C CD2 . TYR B 66  ? 0.3703 0.3887 0.3289 0.0595  0.0311  -0.0305 330 TYR B CD2 
2433 C CE1 . TYR B 66  ? 0.4301 0.4681 0.3825 0.0562  0.0361  -0.0153 330 TYR B CE1 
2434 C CE2 . TYR B 66  ? 0.4151 0.4528 0.3563 0.0773  0.0350  -0.0311 330 TYR B CE2 
2435 C CZ  . TYR B 66  ? 0.4752 0.5238 0.4132 0.0754  0.0381  -0.0221 330 TYR B CZ  
2436 O OH  . TYR B 66  ? 0.5330 0.6049 0.4524 0.0948  0.0429  -0.0197 330 TYR B OH  
2437 N N   . VAL B 67  ? 0.2583 0.2406 0.2710 0.0027  0.0226  -0.0114 331 VAL B N   
2438 C CA  . VAL B 67  ? 0.2472 0.2226 0.2660 -0.0018 0.0195  -0.0107 331 VAL B CA  
2439 C C   . VAL B 67  ? 0.2524 0.2358 0.2818 -0.0023 0.0208  -0.0031 331 VAL B C   
2440 O O   . VAL B 67  ? 0.2506 0.2326 0.2843 -0.0007 0.0201  -0.0017 331 VAL B O   
2441 C CB  . VAL B 67  ? 0.2653 0.2361 0.2838 -0.0094 0.0157  -0.0114 331 VAL B CB  
2442 C CG1 . VAL B 67  ? 0.2916 0.2628 0.3150 -0.0114 0.0140  -0.0069 331 VAL B CG1 
2443 C CG2 . VAL B 67  ? 0.2797 0.2420 0.2956 -0.0104 0.0126  -0.0172 331 VAL B CG2 
2444 N N   . VAL B 68  ? 0.2245 0.2159 0.2622 -0.0050 0.0209  0.0022  332 VAL B N   
2445 C CA  . VAL B 68  ? 0.2096 0.2087 0.2645 -0.0058 0.0193  0.0095  332 VAL B CA  
2446 C C   . VAL B 68  ? 0.2508 0.2594 0.3106 0.0015  0.0258  0.0155  332 VAL B C   
2447 O O   . VAL B 68  ? 0.2155 0.2273 0.2862 0.0022  0.0241  0.0189  332 VAL B O   
2448 C CB  . VAL B 68  ? 0.2006 0.2052 0.2711 -0.0102 0.0160  0.0154  332 VAL B CB  
2449 C CG1 . VAL B 68  ? 0.2408 0.2546 0.3380 -0.0116 0.0127  0.0251  332 VAL B CG1 
2450 C CG2 . VAL B 68  ? 0.2416 0.2373 0.3077 -0.0147 0.0075  0.0068  332 VAL B CG2 
2451 N N   . GLU B 69  ? 0.2204 0.2360 0.2717 0.0092  0.0329  0.0169  333 GLU B N   
2452 C CA  . GLU B 69  ? 0.2178 0.2468 0.2709 0.0205  0.0401  0.0220  333 GLU B CA  
2453 C C   . GLU B 69  ? 0.2693 0.2871 0.3138 0.0257  0.0378  0.0120  333 GLU B C   
2454 O O   . GLU B 69  ? 0.2783 0.3045 0.3315 0.0316  0.0406  0.0168  333 GLU B O   
2455 C CB  . GLU B 69  ? 0.2500 0.2930 0.2916 0.0320  0.0479  0.0246  333 GLU B CB  
2456 C CG  . GLU B 69  ? 0.2627 0.3260 0.3036 0.0485  0.0569  0.0305  333 GLU B CG  
2457 C CD  . GLU B 69  ? 0.3125 0.3973 0.3827 0.0463  0.0626  0.0517  333 GLU B CD  
2458 O OE1 . GLU B 69  ? 0.3015 0.4007 0.3754 0.0575  0.0685  0.0560  333 GLU B OE1 
2459 O OE2 . GLU B 69  ? 0.2496 0.3362 0.3412 0.0338  0.0596  0.0631  333 GLU B OE2 
2460 N N   . PHE B 70  ? 0.2355 0.2355 0.2674 0.0232  0.0322  0.0002  334 PHE B N   
2461 C CA  . PHE B 70  ? 0.2551 0.2415 0.2860 0.0255  0.0276  -0.0066 334 PHE B CA  
2462 C C   . PHE B 70  ? 0.2671 0.2546 0.3106 0.0203  0.0258  0.0008  334 PHE B C   
2463 O O   . PHE B 70  ? 0.2628 0.2506 0.3111 0.0267  0.0261  0.0015  334 PHE B O   
2464 C CB  . PHE B 70  ? 0.2831 0.2522 0.3085 0.0193  0.0208  -0.0146 334 PHE B CB  
2465 C CG  . PHE B 70  ? 0.2652 0.2202 0.2978 0.0180  0.0150  -0.0159 334 PHE B CG  
2466 C CD1 . PHE B 70  ? 0.2902 0.2372 0.3239 0.0284  0.0118  -0.0235 334 PHE B CD1 
2467 C CD2 . PHE B 70  ? 0.2630 0.2141 0.3015 0.0081  0.0125  -0.0089 334 PHE B CD2 
2468 C CE1 . PHE B 70  ? 0.3440 0.2762 0.3895 0.0269  0.0052  -0.0228 334 PHE B CE1 
2469 C CE2 . PHE B 70  ? 0.3127 0.2531 0.3614 0.0071  0.0078  -0.0054 334 PHE B CE2 
2470 C CZ  . PHE B 70  ? 0.3881 0.3176 0.4425 0.0154  0.0037  -0.0118 334 PHE B CZ  
2471 N N   . ALA B 71  ? 0.2551 0.2433 0.3030 0.0105  0.0227  0.0048  335 ALA B N   
2472 C CA  . ALA B 71  ? 0.2776 0.2684 0.3349 0.0076  0.0184  0.0095  335 ALA B CA  
2473 C C   . ALA B 71  ? 0.3021 0.3062 0.3744 0.0119  0.0207  0.0164  335 ALA B C   
2474 O O   . ALA B 71  ? 0.2751 0.2803 0.3534 0.0151  0.0189  0.0187  335 ALA B O   
2475 C CB  . ALA B 71  ? 0.2953 0.2872 0.3529 0.0004  0.0126  0.0091  335 ALA B CB  
2476 N N   . LYS B 72  ? 0.2408 0.2574 0.3223 0.0124  0.0249  0.0222  336 LYS B N   
2477 C CA  . LYS B 72  ? 0.2044 0.2380 0.3074 0.0153  0.0273  0.0331  336 LYS B CA  
2478 C C   . LYS B 72  ? 0.3087 0.3484 0.4080 0.0275  0.0344  0.0337  336 LYS B C   
2479 O O   . LYS B 72  ? 0.2933 0.3455 0.4099 0.0308  0.0352  0.0416  336 LYS B O   
2480 C CB  . LYS B 72  ? 0.2616 0.3098 0.3799 0.0133  0.0312  0.0440  336 LYS B CB  
2481 C CG  . LYS B 72  ? 0.2558 0.2968 0.3840 0.0020  0.0209  0.0424  336 LYS B CG  
2482 C CD  . LYS B 72  ? 0.2545 0.3074 0.3998 -0.0002 0.0244  0.0547  336 LYS B CD  
2483 C CE  . LYS B 72  ? 0.2880 0.3326 0.4510 -0.0104 0.0108  0.0526  336 LYS B CE  
2484 N NZ  . LYS B 72  ? 0.2897 0.3438 0.4692 -0.0127 0.0148  0.0661  336 LYS B NZ  
2485 N N   . ARG B 73  ? 0.2643 0.2950 0.3433 0.0352  0.0375  0.0241  337 ARG B N   
2486 C CA  . ARG B 73  ? 0.2901 0.3245 0.3645 0.0499  0.0417  0.0207  337 ARG B CA  
2487 C C   . ARG B 73  ? 0.3299 0.3464 0.4031 0.0497  0.0346  0.0140  337 ARG B C   
2488 O O   . ARG B 73  ? 0.3929 0.4101 0.4666 0.0618  0.0358  0.0110  337 ARG B O   
2489 C CB  . ARG B 73  ? 0.3297 0.3636 0.3843 0.0621  0.0454  0.0108  337 ARG B CB  
2490 C CG  . ARG B 73  ? 0.3434 0.4021 0.3987 0.0677  0.0551  0.0214  337 ARG B CG  
2491 C CD  . ARG B 73  ? 0.3826 0.4420 0.4141 0.0804  0.0569  0.0103  337 ARG B CD  
2492 N NE  . ARG B 73  ? 0.4222 0.5123 0.4566 0.0884  0.0684  0.0262  337 ARG B NE  
2493 C CZ  . ARG B 73  ? 0.5920 0.7093 0.6213 0.1097  0.0785  0.0315  337 ARG B CZ  
2494 N NH1 . ARG B 73  ? 0.6080 0.7215 0.6260 0.1260  0.0766  0.0175  337 ARG B NH1 
2495 N NH2 . ARG B 73  ? 0.6626 0.8122 0.6986 0.1164  0.0905  0.0517  337 ARG B NH2 
2496 N N   . LEU B 74  ? 0.3221 0.4757 0.4460 0.0486  0.0188  -0.0124 338 LEU B N   
2497 C CA  . LEU B 74  ? 0.3984 0.5322 0.5257 0.0565  0.0097  -0.0134 338 LEU B CA  
2498 C C   . LEU B 74  ? 0.3504 0.4974 0.4953 0.0607  0.0034  -0.0125 338 LEU B C   
2499 O O   . LEU B 74  ? 0.3302 0.4858 0.4764 0.0527  0.0023  -0.0053 338 LEU B O   
2500 C CB  . LEU B 74  ? 0.4685 0.5761 0.5791 0.0490  0.0056  -0.0047 338 LEU B CB  
2501 C CG  . LEU B 74  ? 0.4570 0.5411 0.5643 0.0531  -0.0020 -0.0030 338 LEU B CG  
2502 C CD1 . LEU B 74  ? 0.4430 0.5221 0.5535 0.0612  -0.0010 -0.0121 338 LEU B CD1 
2503 C CD2 . LEU B 74  ? 0.4609 0.5283 0.5501 0.0442  -0.0023 0.0054  338 LEU B CD2 
2504 N N   . SER B 75  ? 0.4229 0.5709 0.5823 0.0738  -0.0023 -0.0201 339 SER B N   
2505 C CA  . SER B 75  ? 0.4388 0.6022 0.6182 0.0799  -0.0091 -0.0208 339 SER B CA  
2506 C C   . SER B 75  ? 0.4324 0.5798 0.6068 0.0726  -0.0184 -0.0089 339 SER B C   
2507 O O   . SER B 75  ? 0.5037 0.6246 0.6683 0.0724  -0.0257 -0.0042 339 SER B O   
2508 C CB  . SER B 75  ? 0.4080 0.5690 0.6027 0.0967  -0.0163 -0.0321 339 SER B CB  
2509 O OG  . SER B 75  ? 0.4761 0.6459 0.6898 0.1034  -0.0259 -0.0318 339 SER B OG  
2510 N N   . GLY B 76  ? 0.2559 0.4202 0.4362 0.0658  -0.0186 -0.0034 340 GLY B N   
2511 C CA  . GLY B 76  ? 0.3087 0.4590 0.4819 0.0588  -0.0278 0.0068  340 GLY B CA  
2512 C C   . GLY B 76  ? 0.2883 0.4290 0.4416 0.0454  -0.0255 0.0145  340 GLY B C   
2513 O O   . GLY B 76  ? 0.2813 0.4182 0.4313 0.0398  -0.0329 0.0211  340 GLY B O   
2514 N N   . PHE B 77  ? 0.2655 0.4016 0.4054 0.0408  -0.0166 0.0130  341 PHE B N   
2515 C CA  . PHE B 77  ? 0.2469 0.3723 0.3685 0.0299  -0.0159 0.0186  341 PHE B CA  
2516 C C   . PHE B 77  ? 0.2300 0.3724 0.3594 0.0216  -0.0179 0.0225  341 PHE B C   
2517 O O   . PHE B 77  ? 0.2519 0.3840 0.3712 0.0145  -0.0245 0.0275  341 PHE B O   
2518 C CB  . PHE B 77  ? 0.2453 0.3643 0.3542 0.0275  -0.0069 0.0157  341 PHE B CB  
2519 C CG  . PHE B 77  ? 0.2604 0.3667 0.3513 0.0185  -0.0073 0.0197  341 PHE B CG  
2520 C CD1 . PHE B 77  ? 0.2637 0.3496 0.3382 0.0186  -0.0107 0.0218  341 PHE B CD1 
2521 C CD2 . PHE B 77  ? 0.2309 0.3464 0.3211 0.0100  -0.0048 0.0215  341 PHE B CD2 
2522 C CE1 . PHE B 77  ? 0.2946 0.3701 0.3531 0.0128  -0.0115 0.0230  341 PHE B CE1 
2523 C CE2 . PHE B 77  ? 0.2783 0.3789 0.3523 0.0031  -0.0074 0.0239  341 PHE B CE2 
2524 C CZ  . PHE B 77  ? 0.2441 0.3248 0.3025 0.0058  -0.0107 0.0233  341 PHE B CZ  
2525 N N   . MET B 78  ? 0.2694 0.4386 0.4167 0.0225  -0.0128 0.0200  342 MET B N   
2526 C CA  . MET B 78  ? 0.3188 0.5075 0.4755 0.0125  -0.0146 0.0256  342 MET B CA  
2527 C C   . MET B 78  ? 0.3619 0.5550 0.5310 0.0129  -0.0257 0.0292  342 MET B C   
2528 O O   . MET B 78  ? 0.3340 0.5406 0.5116 0.0036  -0.0301 0.0350  342 MET B O   
2529 C CB  . MET B 78  ? 0.2801 0.5023 0.4523 0.0124  -0.0046 0.0230  342 MET B CB  
2530 C CG  . MET B 78  ? 0.3271 0.5479 0.4863 0.0090  0.0053  0.0212  342 MET B CG  
2531 S SD  . MET B 78  ? 0.3546 0.5480 0.4908 -0.0054 0.0003  0.0294  342 MET B SD  
2532 C CE  . MET B 78  ? 0.4749 0.6923 0.6125 -0.0179 0.0081  0.0349  342 MET B CE  
2533 N N   . GLU B 79  ? 0.3276 0.5085 0.4976 0.0226  -0.0317 0.0270  343 GLU B N   
2534 C CA  . GLU B 79  ? 0.3323 0.5148 0.5119 0.0230  -0.0438 0.0310  343 GLU B CA  
2535 C C   . GLU B 79  ? 0.2973 0.4556 0.4559 0.0158  -0.0525 0.0364  343 GLU B C   
2536 O O   . GLU B 79  ? 0.3621 0.5207 0.5245 0.0131  -0.0633 0.0404  343 GLU B O   
2537 C CB  . GLU B 79  ? 0.4662 0.6459 0.6562 0.0361  -0.0485 0.0273  343 GLU B CB  
2538 C CG  . GLU B 79  ? 0.6522 0.8554 0.8626 0.0461  -0.0410 0.0188  343 GLU B CG  
2539 C CD  . GLU B 79  ? 0.8910 1.1210 1.1290 0.0514  -0.0467 0.0176  343 GLU B CD  
2540 O OE1 . GLU B 79  ? 0.9912 1.2165 1.2399 0.0634  -0.0544 0.0137  343 GLU B OE1 
2541 O OE2 . GLU B 79  ? 0.9644 1.2208 1.2146 0.0435  -0.0444 0.0208  343 GLU B OE2 
2542 N N   . LEU B 80  ? 0.2292 0.3678 0.3654 0.0133  -0.0480 0.0356  344 LEU B N   
2543 C CA  . LEU B 80  ? 0.2576 0.3762 0.3732 0.0082  -0.0558 0.0384  344 LEU B CA  
2544 C C   . LEU B 80  ? 0.2610 0.3839 0.3771 -0.0026 -0.0596 0.0408  344 LEU B C   
2545 O O   . LEU B 80  ? 0.3220 0.4592 0.4476 -0.0078 -0.0529 0.0414  344 LEU B O   
2546 C CB  . LEU B 80  ? 0.2568 0.3558 0.3498 0.0103  -0.0501 0.0362  344 LEU B CB  
2547 C CG  . LEU B 80  ? 0.2830 0.3772 0.3767 0.0189  -0.0459 0.0351  344 LEU B CG  
2548 C CD1 . LEU B 80  ? 0.3043 0.3828 0.3778 0.0189  -0.0401 0.0341  344 LEU B CD1 
2549 C CD2 . LEU B 80  ? 0.3370 0.4276 0.4339 0.0234  -0.0556 0.0390  344 LEU B CD2 
2550 N N   . CYS B 81  ? 0.2894 0.3989 0.3937 -0.0063 -0.0712 0.0424  345 CYS B N   
2551 C CA  . CYS B 81  ? 0.3103 0.4176 0.4134 -0.0168 -0.0784 0.0445  345 CYS B CA  
2552 C C   . CYS B 81  ? 0.2719 0.3663 0.3593 -0.0197 -0.0725 0.0418  345 CYS B C   
2553 O O   . CYS B 81  ? 0.3157 0.4000 0.3893 -0.0131 -0.0645 0.0377  345 CYS B O   
2554 C CB  . CYS B 81  ? 0.3995 0.4932 0.4924 -0.0183 -0.0942 0.0447  345 CYS B CB  
2555 S SG  . CYS B 81  ? 0.4232 0.4907 0.4828 -0.0110 -0.0960 0.0383  345 CYS B SG  
2556 N N   . GLN B 82  ? 0.2634 0.3591 0.3546 -0.0303 -0.0770 0.0452  346 GLN B N   
2557 C CA  . GLN B 82  ? 0.3182 0.4015 0.3962 -0.0331 -0.0726 0.0433  346 GLN B CA  
2558 C C   . GLN B 82  ? 0.2802 0.3383 0.3335 -0.0263 -0.0764 0.0360  346 GLN B C   
2559 O O   . GLN B 82  ? 0.2909 0.3418 0.3334 -0.0225 -0.0679 0.0324  346 GLN B O   
2560 C CB  . GLN B 82  ? 0.3100 0.3941 0.3944 -0.0470 -0.0814 0.0497  346 GLN B CB  
2561 C CG  . GLN B 82  ? 0.4009 0.4764 0.4758 -0.0507 -0.0763 0.0495  346 GLN B CG  
2562 C CD  . GLN B 82  ? 0.3865 0.4647 0.4697 -0.0664 -0.0856 0.0588  346 GLN B CD  
2563 O OE1 . GLN B 82  ? 0.4018 0.5001 0.4959 -0.0741 -0.0772 0.0658  346 GLN B OE1 
2564 N NE2 . GLN B 82  ? 0.3805 0.4392 0.4586 -0.0716 -0.1038 0.0592  346 GLN B NE2 
2565 N N   . ASN B 83  ? 0.3568 0.4034 0.4012 -0.0244 -0.0892 0.0335  347 ASN B N   
2566 C CA  . ASN B 83  ? 0.3512 0.3793 0.3715 -0.0162 -0.0918 0.0254  347 ASN B CA  
2567 C C   . ASN B 83  ? 0.3418 0.3736 0.3551 -0.0074 -0.0779 0.0234  347 ASN B C   
2568 O O   . ASN B 83  ? 0.3415 0.3647 0.3408 -0.0033 -0.0726 0.0185  347 ASN B O   
2569 C CB  . ASN B 83  ? 0.3662 0.3867 0.3770 -0.0132 -0.1058 0.0224  347 ASN B CB  
2570 C CG  . ASN B 83  ? 0.5068 0.5150 0.4917 -0.0031 -0.1063 0.0133  347 ASN B CG  
2571 O OD1 . ASN B 83  ? 0.5114 0.5257 0.4886 0.0036  -0.0993 0.0135  347 ASN B OD1 
2572 N ND2 . ASN B 83  ? 0.5496 0.5420 0.5218 -0.0022 -0.1149 0.0056  347 ASN B ND2 
2573 N N   . ASP B 84  ? 0.3223 0.3662 0.3458 -0.0046 -0.0735 0.0275  348 ASP B N   
2574 C CA  . ASP B 84  ? 0.3383 0.3836 0.3558 0.0026  -0.0638 0.0274  348 ASP B CA  
2575 C C   . ASP B 84  ? 0.2636 0.3127 0.2870 0.0026  -0.0511 0.0270  348 ASP B C   
2576 O O   . ASP B 84  ? 0.2690 0.3133 0.2820 0.0069  -0.0441 0.0252  348 ASP B O   
2577 C CB  . ASP B 84  ? 0.2669 0.3208 0.2946 0.0056  -0.0658 0.0322  348 ASP B CB  
2578 C CG  . ASP B 84  ? 0.3549 0.4037 0.3711 0.0070  -0.0778 0.0326  348 ASP B CG  
2579 O OD1 . ASP B 84  ? 0.4101 0.4491 0.4096 0.0069  -0.0839 0.0276  348 ASP B OD1 
2580 O OD2 . ASP B 84  ? 0.3570 0.4112 0.3807 0.0090  -0.0821 0.0373  348 ASP B OD2 
2581 N N   . GLN B 85  ? 0.2371 0.2964 0.2765 -0.0028 -0.0483 0.0291  349 GLN B N   
2582 C CA  . GLN B 85  ? 0.2275 0.2903 0.2695 -0.0031 -0.0370 0.0279  349 GLN B CA  
2583 C C   . GLN B 85  ? 0.2438 0.2916 0.2685 -0.0036 -0.0365 0.0240  349 GLN B C   
2584 O O   . GLN B 85  ? 0.2548 0.2993 0.2733 0.0001  -0.0282 0.0216  349 GLN B O   
2585 C CB  . GLN B 85  ? 0.2355 0.3142 0.2943 -0.0101 -0.0349 0.0311  349 GLN B CB  
2586 C CG  . GLN B 85  ? 0.2194 0.3186 0.2989 -0.0078 -0.0334 0.0332  349 GLN B CG  
2587 C CD  . GLN B 85  ? 0.3114 0.4317 0.4068 -0.0157 -0.0310 0.0370  349 GLN B CD  
2588 O OE1 . GLN B 85  ? 0.2981 0.4191 0.3892 -0.0216 -0.0264 0.0381  349 GLN B OE1 
2589 N NE2 . GLN B 85  ? 0.3095 0.4491 0.4238 -0.0166 -0.0344 0.0400  349 GLN B NE2 
2590 N N   . ILE B 86  ? 0.2462 0.2846 0.2642 -0.0079 -0.0469 0.0230  350 ILE B N   
2591 C CA  . ILE B 86  ? 0.2591 0.2827 0.2624 -0.0072 -0.0489 0.0181  350 ILE B CA  
2592 C C   . ILE B 86  ? 0.2690 0.2866 0.2563 0.0020  -0.0465 0.0125  350 ILE B C   
2593 O O   . ILE B 86  ? 0.2724 0.2859 0.2519 0.0053  -0.0404 0.0091  350 ILE B O   
2594 C CB  . ILE B 86  ? 0.2878 0.3001 0.2886 -0.0134 -0.0638 0.0176  350 ILE B CB  
2595 C CG1 . ILE B 86  ? 0.3086 0.3290 0.3241 -0.0248 -0.0639 0.0252  350 ILE B CG1 
2596 C CG2 . ILE B 86  ? 0.3130 0.3072 0.2963 -0.0085 -0.0697 0.0093  350 ILE B CG2 
2597 C CD1 . ILE B 86  ? 0.3454 0.3581 0.3645 -0.0339 -0.0803 0.0286  350 ILE B CD1 
2598 N N   . VAL B 87  ? 0.2742 0.2934 0.2569 0.0057  -0.0514 0.0125  351 VAL B N   
2599 C CA  . VAL B 87  ? 0.2939 0.3127 0.2611 0.0133  -0.0483 0.0092  351 VAL B CA  
2600 C C   . VAL B 87  ? 0.2896 0.3150 0.2606 0.0150  -0.0357 0.0126  351 VAL B C   
2601 O O   . VAL B 87  ? 0.2970 0.3217 0.2580 0.0187  -0.0303 0.0095  351 VAL B O   
2602 C CB  . VAL B 87  ? 0.3168 0.3390 0.2788 0.0156  -0.0551 0.0110  351 VAL B CB  
2603 C CG1 . VAL B 87  ? 0.3076 0.3351 0.2548 0.0216  -0.0497 0.0110  351 VAL B CG1 
2604 C CG2 . VAL B 87  ? 0.3862 0.3993 0.3405 0.0153  -0.0695 0.0053  351 VAL B CG2 
2605 N N   . LEU B 88  ? 0.2480 0.2803 0.2340 0.0129  -0.0319 0.0184  352 LEU B N   
2606 C CA  . LEU B 88  ? 0.2436 0.2793 0.2339 0.0149  -0.0225 0.0211  352 LEU B CA  
2607 C C   . LEU B 88  ? 0.2787 0.3117 0.2690 0.0140  -0.0155 0.0178  352 LEU B C   
2608 O O   . LEU B 88  ? 0.2679 0.3003 0.2538 0.0161  -0.0097 0.0179  352 LEU B O   
2609 C CB  . LEU B 88  ? 0.2274 0.2699 0.2352 0.0147  -0.0220 0.0255  352 LEU B CB  
2610 C CG  . LEU B 88  ? 0.2456 0.2902 0.2546 0.0162  -0.0294 0.0301  352 LEU B CG  
2611 C CD1 . LEU B 88  ? 0.2710 0.3221 0.2995 0.0178  -0.0297 0.0326  352 LEU B CD1 
2612 C CD2 . LEU B 88  ? 0.2869 0.3290 0.2819 0.0183  -0.0296 0.0339  352 LEU B CD2 
2613 N N   . LEU B 89  ? 0.2613 0.2932 0.2567 0.0098  -0.0166 0.0160  353 LEU B N   
2614 C CA  . LEU B 89  ? 0.2549 0.2839 0.2491 0.0086  -0.0106 0.0137  353 LEU B CA  
2615 C C   . LEU B 89  ? 0.3090 0.3290 0.2889 0.0109  -0.0129 0.0087  353 LEU B C   
2616 O O   . LEU B 89  ? 0.3141 0.3323 0.2905 0.0127  -0.0074 0.0067  353 LEU B O   
2617 C CB  . LEU B 89  ? 0.2960 0.3289 0.2995 0.0022  -0.0110 0.0152  353 LEU B CB  
2618 C CG  . LEU B 89  ? 0.3249 0.3714 0.3432 0.0021  -0.0048 0.0174  353 LEU B CG  
2619 C CD1 . LEU B 89  ? 0.3269 0.3832 0.3540 -0.0051 -0.0057 0.0202  353 LEU B CD1 
2620 C CD2 . LEU B 89  ? 0.3774 0.4231 0.3947 0.0054  0.0036  0.0150  353 LEU B CD2 
2621 N N   . LYS B 90  ? 0.2990 0.3135 0.2707 0.0120  -0.0220 0.0056  354 LYS B N   
2622 C CA  . LYS B 90  ? 0.3595 0.3668 0.3181 0.0168  -0.0249 -0.0016 354 LYS B CA  
2623 C C   . LYS B 90  ? 0.3403 0.3556 0.2921 0.0227  -0.0175 -0.0024 354 LYS B C   
2624 O O   . LYS B 90  ? 0.3680 0.3828 0.3151 0.0260  -0.0144 -0.0067 354 LYS B O   
2625 C CB  . LYS B 90  ? 0.3809 0.3802 0.3312 0.0186  -0.0377 -0.0068 354 LYS B CB  
2626 C CG  . LYS B 90  ? 0.4983 0.4855 0.4533 0.0120  -0.0473 -0.0068 354 LYS B CG  
2627 C CD  . LYS B 90  ? 0.6056 0.5824 0.5553 0.0121  -0.0631 -0.0109 354 LYS B CD  
2628 C CE  . LYS B 90  ? 0.7510 0.7220 0.6842 0.0234  -0.0689 -0.0229 354 LYS B CE  
2629 N NZ  . LYS B 90  ? 0.7992 0.7616 0.7253 0.0256  -0.0842 -0.0284 354 LYS B NZ  
2630 N N   . ALA B 91  ? 0.3184 0.3418 0.2706 0.0233  -0.0158 0.0026  355 ALA B N   
2631 C CA  . ALA B 91  ? 0.3203 0.3538 0.2666 0.0264  -0.0098 0.0053  355 ALA B CA  
2632 C C   . ALA B 91  ? 0.3943 0.4302 0.3501 0.0237  -0.0014 0.0107  355 ALA B C   
2633 O O   . ALA B 91  ? 0.3787 0.4217 0.3305 0.0251  0.0036  0.0121  355 ALA B O   
2634 C CB  . ALA B 91  ? 0.3566 0.3962 0.2994 0.0265  -0.0132 0.0108  355 ALA B CB  
2635 N N   . GLY B 92  ? 0.3306 0.3621 0.2989 0.0202  -0.0003 0.0132  356 GLY B N   
2636 C CA  . GLY B 92  ? 0.3087 0.3412 0.2862 0.0187  0.0051  0.0178  356 GLY B CA  
2637 C C   . GLY B 92  ? 0.3045 0.3329 0.2883 0.0173  0.0093  0.0147  356 GLY B C   
2638 O O   . GLY B 92  ? 0.3041 0.3321 0.2928 0.0171  0.0130  0.0167  356 GLY B O   
2639 N N   . ALA B 93  ? 0.2949 0.3198 0.2782 0.0158  0.0077  0.0106  357 ALA B N   
2640 C CA  . ALA B 93  ? 0.2919 0.3148 0.2800 0.0136  0.0114  0.0088  357 ALA B CA  
2641 C C   . ALA B 93  ? 0.2662 0.2865 0.2501 0.0149  0.0151  0.0070  357 ALA B C   
2642 O O   . ALA B 93  ? 0.2497 0.2694 0.2386 0.0144  0.0189  0.0069  357 ALA B O   
2643 C CB  . ALA B 93  ? 0.3056 0.3257 0.2922 0.0097  0.0075  0.0071  357 ALA B CB  
2644 N N   . MET B 94  ? 0.3119 0.3316 0.2870 0.0172  0.0134  0.0047  358 MET B N   
2645 C CA  . MET B 94  ? 0.2864 0.3064 0.2594 0.0186  0.0164  0.0027  358 MET B CA  
2646 C C   . MET B 94  ? 0.2867 0.3126 0.2644 0.0183  0.0204  0.0080  358 MET B C   
2647 O O   . MET B 94  ? 0.2958 0.3209 0.2770 0.0172  0.0230  0.0084  358 MET B O   
2648 C CB  . MET B 94  ? 0.3220 0.3432 0.2858 0.0231  0.0131  -0.0027 358 MET B CB  
2649 C CG  . MET B 94  ? 0.3628 0.3856 0.3261 0.0252  0.0152  -0.0057 358 MET B CG  
2650 S SD  . MET B 94  ? 0.3755 0.3857 0.3412 0.0213  0.0135  -0.0074 358 MET B SD  
2651 C CE  . MET B 94  ? 0.3916 0.4068 0.3601 0.0230  0.0173  -0.0083 358 MET B CE  
2652 N N   . GLU B 95  ? 0.3098 0.3407 0.2879 0.0182  0.0194  0.0130  359 GLU B N   
2653 C CA  . GLU B 95  ? 0.3040 0.3382 0.2873 0.0161  0.0206  0.0204  359 GLU B CA  
2654 C C   . GLU B 95  ? 0.2933 0.3190 0.2869 0.0148  0.0205  0.0205  359 GLU B C   
2655 O O   . GLU B 95  ? 0.2912 0.3150 0.2896 0.0130  0.0208  0.0232  359 GLU B O   
2656 C CB  . GLU B 95  ? 0.3901 0.4298 0.3710 0.0157  0.0177  0.0267  359 GLU B CB  
2657 C CG  . GLU B 95  ? 0.5169 0.5676 0.4852 0.0183  0.0177  0.0250  359 GLU B CG  
2658 C CD  . GLU B 95  ? 0.6630 0.7212 0.6265 0.0172  0.0149  0.0325  359 GLU B CD  
2659 O OE1 . GLU B 95  ? 0.6699 0.7224 0.6405 0.0146  0.0114  0.0388  359 GLU B OE1 
2660 O OE2 . GLU B 95  ? 0.7121 0.7829 0.6642 0.0196  0.0155  0.0317  359 GLU B OE2 
2661 N N   . VAL B 96  ? 0.2445 0.2666 0.2418 0.0159  0.0195  0.0170  360 VAL B N   
2662 C CA  . VAL B 96  ? 0.2361 0.2536 0.2423 0.0168  0.0198  0.0145  360 VAL B CA  
2663 C C   . VAL B 96  ? 0.2816 0.2959 0.2857 0.0162  0.0228  0.0098  360 VAL B C   
2664 O O   . VAL B 96  ? 0.2751 0.2848 0.2842 0.0169  0.0223  0.0085  360 VAL B O   
2665 C CB  . VAL B 96  ? 0.2313 0.2519 0.2428 0.0186  0.0190  0.0117  360 VAL B CB  
2666 C CG1 . VAL B 96  ? 0.2385 0.2586 0.2581 0.0215  0.0203  0.0065  360 VAL B CG1 
2667 C CG2 . VAL B 96  ? 0.2686 0.2907 0.2844 0.0197  0.0145  0.0168  360 VAL B CG2 
2668 N N   . VAL B 97  ? 0.2528 0.2681 0.2494 0.0152  0.0242  0.0069  361 VAL B N   
2669 C CA  . VAL B 97  ? 0.2348 0.2463 0.2286 0.0143  0.0258  0.0032  361 VAL B CA  
2670 C C   . VAL B 97  ? 0.2649 0.2752 0.2608 0.0139  0.0257  0.0053  361 VAL B C   
2671 O O   . VAL B 97  ? 0.2722 0.2777 0.2708 0.0136  0.0256  0.0032  361 VAL B O   
2672 C CB  . VAL B 97  ? 0.2563 0.2668 0.2420 0.0133  0.0247  0.0008  361 VAL B CB  
2673 C CG1 . VAL B 97  ? 0.2792 0.2853 0.2617 0.0126  0.0248  -0.0020 361 VAL B CG1 
2674 C CG2 . VAL B 97  ? 0.2498 0.2612 0.2349 0.0110  0.0236  0.0004  361 VAL B CG2 
2675 N N   . LEU B 98  ? 0.2428 0.2590 0.2374 0.0136  0.0255  0.0098  362 LEU B N   
2676 C CA  . LEU B 98  ? 0.2603 0.2801 0.2580 0.0116  0.0256  0.0138  362 LEU B CA  
2677 C C   . LEU B 98  ? 0.2586 0.2727 0.2655 0.0090  0.0224  0.0191  362 LEU B C   
2678 O O   . LEU B 98  ? 0.3305 0.3420 0.3422 0.0064  0.0206  0.0208  362 LEU B O   
2679 C CB  . LEU B 98  ? 0.2355 0.2682 0.2290 0.0120  0.0269  0.0175  362 LEU B CB  
2680 C CG  . LEU B 98  ? 0.2933 0.3302 0.2790 0.0161  0.0277  0.0106  362 LEU B CG  
2681 C CD1 . LEU B 98  ? 0.3314 0.3818 0.3111 0.0187  0.0284  0.0119  362 LEU B CD1 
2682 C CD2 . LEU B 98  ? 0.2802 0.3193 0.2680 0.0165  0.0283  0.0077  362 LEU B CD2 
2683 N N   . VAL B 99  ? 0.2974 0.3085 0.3073 0.0099  0.0199  0.0214  363 VAL B N   
2684 C CA  . VAL B 99  ? 0.2629 0.2652 0.2820 0.0089  0.0142  0.0249  363 VAL B CA  
2685 C C   . VAL B 99  ? 0.2835 0.2765 0.3056 0.0123  0.0132  0.0159  363 VAL B C   
2686 O O   . VAL B 99  ? 0.3029 0.2874 0.3308 0.0111  0.0082  0.0163  363 VAL B O   
2687 C CB  . VAL B 99  ? 0.2828 0.2840 0.3054 0.0103  0.0103  0.0290  363 VAL B CB  
2688 C CG1 . VAL B 99  ? 0.2905 0.2787 0.3240 0.0111  0.0016  0.0306  363 VAL B CG1 
2689 C CG2 . VAL B 99  ? 0.2946 0.3065 0.3121 0.0061  0.0107  0.0391  363 VAL B CG2 
2690 N N   . ARG B 100 ? 0.2774 0.2728 0.2953 0.0160  0.0173  0.0080  364 ARG B N   
2691 C CA  . ARG B 100 ? 0.2745 0.2654 0.2931 0.0195  0.0173  -0.0009 364 ARG B CA  
2692 C C   . ARG B 100 ? 0.3048 0.2912 0.3204 0.0171  0.0169  -0.0026 364 ARG B C   
2693 O O   . ARG B 100 ? 0.2999 0.2791 0.3173 0.0196  0.0138  -0.0089 364 ARG B O   
2694 C CB  . ARG B 100 ? 0.2645 0.2636 0.2780 0.0213  0.0225  -0.0061 364 ARG B CB  
2695 C CG  . ARG B 100 ? 0.2534 0.2583 0.2732 0.0251  0.0222  -0.0071 364 ARG B CG  
2696 C CD  . ARG B 100 ? 0.2647 0.2810 0.2802 0.0243  0.0274  -0.0101 364 ARG B CD  
2697 N NE  . ARG B 100 ? 0.2553 0.2810 0.2792 0.0285  0.0275  -0.0126 364 ARG B NE  
2698 C CZ  . ARG B 100 ? 0.2808 0.3203 0.3057 0.0297  0.0317  -0.0172 364 ARG B CZ  
2699 N NH1 . ARG B 100 ? 0.3072 0.3505 0.3229 0.0254  0.0356  -0.0181 364 ARG B NH1 
2700 N NH2 . ARG B 100 ? 0.2893 0.3405 0.3246 0.0346  0.0316  -0.0199 364 ARG B NH2 
2701 N N   . MET B 101 ? 0.2980 0.2891 0.3090 0.0133  0.0193  0.0015  365 MET B N   
2702 C CA  . MET B 101 ? 0.2692 0.2583 0.2784 0.0112  0.0187  0.0001  365 MET B CA  
2703 C C   . MET B 101 ? 0.3160 0.2974 0.3335 0.0089  0.0124  0.0029  365 MET B C   
2704 O O   . MET B 101 ? 0.3491 0.3255 0.3663 0.0081  0.0099  -0.0007 365 MET B O   
2705 C CB  . MET B 101 ? 0.3442 0.3420 0.3495 0.0093  0.0215  0.0035  365 MET B CB  
2706 C CG  . MET B 101 ? 0.3710 0.3678 0.3760 0.0078  0.0201  0.0018  365 MET B CG  
2707 S SD  . MET B 101 ? 0.4210 0.4296 0.4219 0.0089  0.0227  0.0025  365 MET B SD  
2708 C CE  . MET B 101 ? 0.4603 0.4641 0.4512 0.0116  0.0239  -0.0026 365 MET B CE  
2709 N N   . CYS B 102 ? 0.2842 0.2632 0.3094 0.0071  0.0081  0.0096  366 CYS B N   
2710 C CA  . CYS B 102 ? 0.3245 0.2954 0.3586 0.0027  -0.0001 0.0147  366 CYS B CA  
2711 C C   . CYS B 102 ? 0.3297 0.2853 0.3656 0.0071  -0.0066 0.0048  366 CYS B C   
2712 O O   . CYS B 102 ? 0.3265 0.2729 0.3682 0.0036  -0.0144 0.0061  366 CYS B O   
2713 C CB  . CYS B 102 ? 0.3242 0.2945 0.3660 -0.0016 -0.0054 0.0263  366 CYS B CB  
2714 S SG  . CYS B 102 ? 0.3512 0.3083 0.3978 0.0044  -0.0123 0.0229  366 CYS B SG  
2715 N N   . ARG B 103 ? 0.3114 0.2663 0.3424 0.0146  -0.0036 -0.0053 367 ARG B N   
2716 C CA  . ARG B 103 ? 0.3111 0.2560 0.3414 0.0210  -0.0083 -0.0174 367 ARG B CA  
2717 C C   . ARG B 103 ? 0.3412 0.2847 0.3648 0.0192  -0.0079 -0.0218 367 ARG B C   
2718 O O   . ARG B 103 ? 0.3818 0.3141 0.4060 0.0220  -0.0154 -0.0294 367 ARG B O   
2719 C CB  . ARG B 103 ? 0.3001 0.2531 0.3259 0.0288  -0.0024 -0.0263 367 ARG B CB  
2720 C CG  . ARG B 103 ? 0.3180 0.2707 0.3522 0.0325  -0.0052 -0.0243 367 ARG B CG  
2721 C CD  . ARG B 103 ? 0.3152 0.2826 0.3457 0.0380  0.0030  -0.0305 367 ARG B CD  
2722 N NE  . ARG B 103 ? 0.3521 0.3217 0.3823 0.0475  0.0022  -0.0445 367 ARG B NE  
2723 C CZ  . ARG B 103 ? 0.2938 0.2748 0.3141 0.0491  0.0092  -0.0518 367 ARG B CZ  
2724 N NH1 . ARG B 103 ? 0.3312 0.3187 0.3418 0.0413  0.0160  -0.0457 367 ARG B NH1 
2725 N NH2 . ARG B 103 ? 0.3540 0.3411 0.3743 0.0590  0.0088  -0.0652 367 ARG B NH2 
2726 N N   . ALA B 104 ? 0.2854 0.2396 0.3027 0.0153  -0.0004 -0.0178 368 ALA B N   
2727 C CA  . ALA B 104 ? 0.2970 0.2515 0.3067 0.0138  0.0005  -0.0214 368 ALA B CA  
2728 C C   . ALA B 104 ? 0.3071 0.2616 0.3235 0.0072  -0.0033 -0.0138 368 ALA B C   
2729 O O   . ALA B 104 ? 0.3216 0.2782 0.3337 0.0055  -0.0029 -0.0150 368 ALA B O   
2730 C CB  . ALA B 104 ? 0.3156 0.2808 0.3149 0.0141  0.0089  -0.0223 368 ALA B CB  
2731 N N   . TYR B 105 ? 0.2979 0.2513 0.3253 0.0031  -0.0076 -0.0050 369 TYR B N   
2732 C CA  . TYR B 105 ? 0.2807 0.2398 0.3168 -0.0045 -0.0106 0.0047  369 TYR B CA  
2733 C C   . TYR B 105 ? 0.2939 0.2382 0.3397 -0.0082 -0.0231 0.0060  369 TYR B C   
2734 O O   . TYR B 105 ? 0.3249 0.2569 0.3753 -0.0067 -0.0301 0.0057  369 TYR B O   
2735 C CB  . TYR B 105 ? 0.2821 0.2554 0.3230 -0.0085 -0.0062 0.0162  369 TYR B CB  
2736 C CG  . TYR B 105 ? 0.2590 0.2444 0.3099 -0.0168 -0.0082 0.0272  369 TYR B CG  
2737 C CD1 . TYR B 105 ? 0.2720 0.2729 0.3218 -0.0168 -0.0029 0.0268  369 TYR B CD1 
2738 C CD2 . TYR B 105 ? 0.3016 0.2838 0.3643 -0.0249 -0.0166 0.0386  369 TYR B CD2 
2739 C CE1 . TYR B 105 ? 0.2616 0.2789 0.3221 -0.0237 -0.0038 0.0363  369 TYR B CE1 
2740 C CE2 . TYR B 105 ? 0.3467 0.3448 0.4201 -0.0342 -0.0181 0.0506  369 TYR B CE2 
2741 C CZ  . TYR B 105 ? 0.2793 0.2972 0.3517 -0.0332 -0.0107 0.0490  369 TYR B CZ  
2742 O OH  . TYR B 105 ? 0.3364 0.3753 0.4206 -0.0415 -0.0111 0.0599  369 TYR B OH  
2743 N N   . ASN B 106 ? 0.2961 0.2411 0.3457 -0.0126 -0.0272 0.0072  370 ASN B N   
2744 C CA  . ASN B 106 ? 0.3297 0.2606 0.3897 -0.0180 -0.0409 0.0097  370 ASN B CA  
2745 C C   . ASN B 106 ? 0.3069 0.2517 0.3809 -0.0293 -0.0427 0.0260  370 ASN B C   
2746 O O   . ASN B 106 ? 0.2840 0.2445 0.3609 -0.0327 -0.0388 0.0293  370 ASN B O   
2747 C CB  . ASN B 106 ? 0.3204 0.2433 0.3753 -0.0158 -0.0456 -0.0003 370 ASN B CB  
2748 C CG  . ASN B 106 ? 0.3277 0.2329 0.3929 -0.0207 -0.0621 0.0005  370 ASN B CG  
2749 O OD1 . ASN B 106 ? 0.3753 0.2737 0.4524 -0.0266 -0.0705 0.0097  370 ASN B OD1 
2750 N ND2 . ASN B 106 ? 0.4203 0.3166 0.4806 -0.0188 -0.0682 -0.0088 370 ASN B ND2 
2751 N N   . ALA B 107 ? 0.3223 0.2633 0.4058 -0.0355 -0.0491 0.0371  371 ALA B N   
2752 C CA  . ALA B 107 ? 0.3344 0.2928 0.4312 -0.0481 -0.0507 0.0549  371 ALA B CA  
2753 C C   . ALA B 107 ? 0.3610 0.3165 0.4707 -0.0573 -0.0621 0.0600  371 ALA B C   
2754 O O   . ALA B 107 ? 0.3791 0.3571 0.4998 -0.0674 -0.0604 0.0738  371 ALA B O   
2755 C CB  . ALA B 107 ? 0.3546 0.3087 0.4576 -0.0541 -0.0565 0.0679  371 ALA B CB  
2756 N N   . ASP B 108 ? 0.3624 0.2924 0.4709 -0.0538 -0.0739 0.0490  372 ASP B N   
2757 C CA  . ASP B 108 ? 0.4047 0.3283 0.5252 -0.0624 -0.0872 0.0527  372 ASP B CA  
2758 C C   . ASP B 108 ? 0.3756 0.3238 0.4986 -0.0646 -0.0789 0.0541  372 ASP B C   
2759 O O   . ASP B 108 ? 0.4364 0.3968 0.5755 -0.0763 -0.0851 0.0663  372 ASP B O   
2760 C CB  . ASP B 108 ? 0.4544 0.3466 0.5685 -0.0548 -0.1003 0.0361  372 ASP B CB  
2761 C CG  . ASP B 108 ? 0.6886 0.5554 0.8012 -0.0495 -0.1103 0.0312  372 ASP B CG  
2762 O OD1 . ASP B 108 ? 0.7637 0.6308 0.8857 -0.0567 -0.1143 0.0452  372 ASP B OD1 
2763 O OD2 . ASP B 108 ? 0.7476 0.5953 0.8493 -0.0376 -0.1147 0.0129  372 ASP B OD2 
2764 N N   . ASN B 109 ? 0.3379 0.2935 0.4465 -0.0537 -0.0664 0.0419  373 ASN B N   
2765 C CA  . ASN B 109 ? 0.3350 0.3103 0.4456 -0.0537 -0.0607 0.0409  373 ASN B CA  
2766 C C   . ASN B 109 ? 0.3121 0.3112 0.4155 -0.0475 -0.0442 0.0405  373 ASN B C   
2767 O O   . ASN B 109 ? 0.3325 0.3474 0.4359 -0.0444 -0.0389 0.0374  373 ASN B O   
2768 C CB  . ASN B 109 ? 0.3528 0.3106 0.4529 -0.0468 -0.0661 0.0258  373 ASN B CB  
2769 C CG  . ASN B 109 ? 0.3605 0.3037 0.4401 -0.0351 -0.0603 0.0117  373 ASN B CG  
2770 O OD1 . ASN B 109 ? 0.3774 0.3244 0.4513 -0.0313 -0.0517 0.0123  373 ASN B OD1 
2771 N ND2 . ASN B 109 ? 0.4030 0.3319 0.4712 -0.0297 -0.0651 -0.0008 373 ASN B ND2 
2772 N N   . ARG B 110 ? 0.3246 0.3251 0.4229 -0.0458 -0.0380 0.0437  374 ARG B N   
2773 C CA  . ARG B 110 ? 0.3232 0.3439 0.4142 -0.0400 -0.0241 0.0432  374 ARG B CA  
2774 C C   . ARG B 110 ? 0.2909 0.3068 0.3670 -0.0290 -0.0183 0.0288  374 ARG B C   
2775 O O   . ARG B 110 ? 0.3503 0.3840 0.4256 -0.0250 -0.0118 0.0267  374 ARG B O   
2776 C CB  . ARG B 110 ? 0.3016 0.3556 0.4054 -0.0461 -0.0192 0.0548  374 ARG B CB  
2777 C CG  . ARG B 110 ? 0.3579 0.4195 0.4769 -0.0600 -0.0257 0.0726  374 ARG B CG  
2778 C CD  . ARG B 110 ? 0.5209 0.6230 0.6489 -0.0651 -0.0168 0.0848  374 ARG B CD  
2779 N NE  . ARG B 110 ? 0.7573 0.8709 0.8721 -0.0567 -0.0050 0.0810  374 ARG B NE  
2780 C CZ  . ARG B 110 ? 0.8496 0.9750 0.9631 -0.0616 -0.0016 0.0923  374 ARG B CZ  
2781 N NH1 . ARG B 110 ? 0.7973 0.9309 0.8975 -0.0527 0.0081  0.0866  374 ARG B NH1 
2782 N NH2 . ARG B 110 ? 0.9217 1.0500 1.0470 -0.0759 -0.0092 0.1099  374 ARG B NH2 
2783 N N   . THR B 111 ? 0.2992 0.2920 0.3640 -0.0241 -0.0213 0.0191  375 THR B N   
2784 C CA  . THR B 111 ? 0.2926 0.2801 0.3426 -0.0160 -0.0170 0.0079  375 THR B CA  
2785 C C   . THR B 111 ? 0.2889 0.2687 0.3271 -0.0106 -0.0116 0.0033  375 THR B C   
2786 O O   . THR B 111 ? 0.2861 0.2588 0.3268 -0.0116 -0.0134 0.0057  375 THR B O   
2787 C CB  . THR B 111 ? 0.3403 0.3115 0.3851 -0.0151 -0.0251 -0.0003 375 THR B CB  
2788 O OG1 . THR B 111 ? 0.3602 0.3133 0.4046 -0.0156 -0.0323 -0.0032 375 THR B OG1 
2789 C CG2 . THR B 111 ? 0.3495 0.3287 0.4063 -0.0201 -0.0313 0.0035  375 THR B CG2 
2790 N N   . VAL B 112 ? 0.2688 0.2501 0.2951 -0.0052 -0.0060 -0.0028 376 VAL B N   
2791 C CA  . VAL B 112 ? 0.2885 0.2650 0.3044 -0.0010 -0.0010 -0.0068 376 VAL B CA  
2792 C C   . VAL B 112 ? 0.3089 0.2767 0.3116 0.0021  -0.0016 -0.0152 376 VAL B C   
2793 O O   . VAL B 112 ? 0.2966 0.2646 0.2961 0.0018  -0.0040 -0.0168 376 VAL B O   
2794 C CB  . VAL B 112 ? 0.2595 0.2485 0.2740 0.0009  0.0059  -0.0035 376 VAL B CB  
2795 C CG1 . VAL B 112 ? 0.3081 0.3008 0.3162 0.0037  0.0068  -0.0071 376 VAL B CG1 
2796 C CG2 . VAL B 112 ? 0.2587 0.2443 0.2671 0.0035  0.0099  -0.0049 376 VAL B CG2 
2797 N N   . PHE B 113 ? 0.2813 0.2435 0.2768 0.0050  0.0001  -0.0200 377 PHE B N   
2798 C CA  . PHE B 113 ? 0.3055 0.2640 0.2870 0.0070  0.0007  -0.0267 377 PHE B CA  
2799 C C   . PHE B 113 ? 0.3372 0.3020 0.3116 0.0064  0.0051  -0.0240 377 PHE B C   
2800 O O   . PHE B 113 ? 0.3444 0.3146 0.3202 0.0071  0.0098  -0.0213 377 PHE B O   
2801 C CB  . PHE B 113 ? 0.2985 0.2549 0.2758 0.0111  0.0023  -0.0331 377 PHE B CB  
2802 C CG  . PHE B 113 ? 0.3264 0.2835 0.2892 0.0129  0.0031  -0.0402 377 PHE B CG  
2803 C CD1 . PHE B 113 ? 0.3734 0.3233 0.3304 0.0134  -0.0031 -0.0458 377 PHE B CD1 
2804 C CD2 . PHE B 113 ? 0.4452 0.4119 0.4000 0.0138  0.0098  -0.0406 377 PHE B CD2 
2805 C CE1 . PHE B 113 ? 0.3842 0.3376 0.3256 0.0149  -0.0019 -0.0520 377 PHE B CE1 
2806 C CE2 . PHE B 113 ? 0.4381 0.4101 0.3788 0.0143  0.0113  -0.0456 377 PHE B CE2 
2807 C CZ  . PHE B 113 ? 0.4515 0.4174 0.3847 0.0152  0.0059  -0.0514 377 PHE B CZ  
2808 N N   . PHE B 114 ? 0.2781 0.2404 0.2450 0.0050  0.0020  -0.0247 378 PHE B N   
2809 C CA  . PHE B 114 ? 0.3178 0.2822 0.2785 0.0041  0.0027  -0.0219 378 PHE B CA  
2810 C C   . PHE B 114 ? 0.2776 0.2367 0.2250 0.0015  -0.0015 -0.0231 378 PHE B C   
2811 O O   . PHE B 114 ? 0.3234 0.2777 0.2701 0.0010  -0.0073 -0.0247 378 PHE B O   
2812 C CB  . PHE B 114 ? 0.2776 0.2455 0.2475 0.0054  0.0005  -0.0194 378 PHE B CB  
2813 C CG  . PHE B 114 ? 0.2673 0.2338 0.2320 0.0062  -0.0021 -0.0183 378 PHE B CG  
2814 C CD1 . PHE B 114 ? 0.3242 0.2938 0.2884 0.0072  0.0011  -0.0168 378 PHE B CD1 
2815 C CD2 . PHE B 114 ? 0.2701 0.2309 0.2315 0.0062  -0.0096 -0.0190 378 PHE B CD2 
2816 C CE1 . PHE B 114 ? 0.2989 0.2644 0.2590 0.0082  -0.0037 -0.0166 378 PHE B CE1 
2817 C CE2 . PHE B 114 ? 0.3089 0.2652 0.2666 0.0076  -0.0148 -0.0184 378 PHE B CE2 
2818 C CZ  . PHE B 114 ? 0.3178 0.2759 0.2749 0.0086  -0.0121 -0.0175 378 PHE B CZ  
2819 N N   . GLU B 115 ? 0.2993 0.2604 0.2363 -0.0010 0.0008  -0.0212 379 GLU B N   
2820 C CA  . GLU B 115 ? 0.3177 0.2757 0.2407 -0.0052 -0.0035 -0.0197 379 GLU B CA  
2821 C C   . GLU B 115 ? 0.3819 0.3381 0.2984 -0.0045 -0.0055 -0.0251 379 GLU B C   
2822 O O   . GLU B 115 ? 0.3729 0.3230 0.2821 -0.0067 -0.0125 -0.0246 379 GLU B O   
2823 C CB  . GLU B 115 ? 0.2875 0.2373 0.2103 -0.0069 -0.0119 -0.0155 379 GLU B CB  
2824 C CG  . GLU B 115 ? 0.2955 0.2456 0.2220 -0.0070 -0.0116 -0.0118 379 GLU B CG  
2825 C CD  . GLU B 115 ? 0.3445 0.2844 0.2694 -0.0077 -0.0221 -0.0088 379 GLU B CD  
2826 O OE1 . GLU B 115 ? 0.3611 0.2945 0.2855 -0.0067 -0.0296 -0.0099 379 GLU B OE1 
2827 O OE2 . GLU B 115 ? 0.3275 0.2647 0.2520 -0.0090 -0.0244 -0.0057 379 GLU B OE2 
2828 N N   . GLY B 116 ? 0.3588 0.3193 0.2777 -0.0007 -0.0009 -0.0311 380 GLY B N   
2829 C CA  . GLY B 116 ? 0.3737 0.3330 0.2836 0.0012  -0.0032 -0.0385 380 GLY B CA  
2830 C C   . GLY B 116 ? 0.3598 0.3094 0.2784 0.0042  -0.0097 -0.0437 380 GLY B C   
2831 O O   . GLY B 116 ? 0.3757 0.3228 0.2879 0.0073  -0.0125 -0.0519 380 GLY B O   
2832 N N   . LYS B 117 ? 0.3393 0.2849 0.2724 0.0032  -0.0126 -0.0392 381 LYS B N   
2833 C CA  . LYS B 117 ? 0.3647 0.3035 0.3091 0.0038  -0.0192 -0.0415 381 LYS B CA  
2834 C C   . LYS B 117 ? 0.3235 0.2661 0.2861 0.0033  -0.0171 -0.0357 381 LYS B C   
2835 O O   . LYS B 117 ? 0.3145 0.2640 0.2796 0.0032  -0.0113 -0.0311 381 LYS B O   
2836 C CB  . LYS B 117 ? 0.3763 0.3099 0.3184 0.0012  -0.0277 -0.0408 381 LYS B CB  
2837 C CG  . LYS B 117 ? 0.4031 0.3338 0.3249 0.0006  -0.0306 -0.0448 381 LYS B CG  
2838 C CD  . LYS B 117 ? 0.4530 0.3768 0.3749 -0.0017 -0.0412 -0.0442 381 LYS B CD  
2839 C CE  . LYS B 117 ? 0.4979 0.4190 0.3978 -0.0035 -0.0453 -0.0462 381 LYS B CE  
2840 N NZ  . LYS B 117 ? 0.5335 0.4464 0.4363 -0.0050 -0.0573 -0.0470 381 LYS B NZ  
2841 N N   . TYR B 118 ? 0.3050 0.2433 0.2798 0.0023  -0.0227 -0.0357 382 TYR B N   
2842 C CA  . TYR B 118 ? 0.3023 0.2474 0.2942 -0.0001 -0.0214 -0.0281 382 TYR B CA  
2843 C C   . TYR B 118 ? 0.3076 0.2610 0.3081 -0.0026 -0.0234 -0.0230 382 TYR B C   
2844 O O   . TYR B 118 ? 0.3399 0.2897 0.3407 -0.0040 -0.0304 -0.0247 382 TYR B O   
2845 C CB  . TYR B 118 ? 0.3191 0.2564 0.3221 -0.0019 -0.0281 -0.0279 382 TYR B CB  
2846 C CG  . TYR B 118 ? 0.3558 0.2885 0.3561 0.0020  -0.0253 -0.0316 382 TYR B CG  
2847 C CD1 . TYR B 118 ? 0.3150 0.2403 0.3026 0.0077  -0.0264 -0.0425 382 TYR B CD1 
2848 C CD2 . TYR B 118 ? 0.2862 0.2240 0.2965 0.0007  -0.0218 -0.0245 382 TYR B CD2 
2849 C CE1 . TYR B 118 ? 0.3759 0.2999 0.3628 0.0130  -0.0239 -0.0470 382 TYR B CE1 
2850 C CE2 . TYR B 118 ? 0.3128 0.2466 0.3217 0.0051  -0.0202 -0.0279 382 TYR B CE2 
2851 C CZ  . TYR B 118 ? 0.3154 0.2427 0.3138 0.0116  -0.0212 -0.0395 382 TYR B CZ  
2852 O OH  . TYR B 118 ? 0.3525 0.2782 0.3520 0.0171  -0.0202 -0.0437 382 TYR B OH  
2853 N N   . GLY B 119 ? 0.2862 0.2523 0.2945 -0.0024 -0.0176 -0.0175 383 GLY B N   
2854 C CA  . GLY B 119 ? 0.3337 0.3123 0.3517 -0.0026 -0.0187 -0.0141 383 GLY B CA  
2855 C C   . GLY B 119 ? 0.3132 0.3091 0.3451 -0.0041 -0.0139 -0.0070 383 GLY B C   
2856 O O   . GLY B 119 ? 0.2880 0.2852 0.3179 -0.0037 -0.0084 -0.0048 383 GLY B O   
2857 N N   . GLY B 120 ? 0.2913 0.3027 0.3371 -0.0058 -0.0159 -0.0031 384 GLY B N   
2858 C CA  . GLY B 120 ? 0.2852 0.3190 0.3433 -0.0075 -0.0104 0.0043  384 GLY B CA  
2859 C C   . GLY B 120 ? 0.2893 0.3371 0.3435 0.0002  -0.0039 0.0009  384 GLY B C   
2860 O O   . GLY B 120 ? 0.2919 0.3294 0.3350 0.0061  -0.0051 -0.0064 384 GLY B O   
2861 N N   . MET B 121 ? 0.2639 0.3004 0.3774 -0.0242 0.0090  -0.0121 385 MET B N   
2862 C CA  . MET B 121 ? 0.2429 0.2892 0.3542 -0.0218 0.0203  -0.0135 385 MET B CA  
2863 C C   . MET B 121 ? 0.2297 0.2844 0.3596 -0.0198 0.0193  -0.0166 385 MET B C   
2864 O O   . MET B 121 ? 0.2427 0.3004 0.3674 -0.0158 0.0230  -0.0201 385 MET B O   
2865 C CB  . MET B 121 ? 0.2906 0.3429 0.4022 -0.0247 0.0332  -0.0092 385 MET B CB  
2866 C CG  . MET B 121 ? 0.3502 0.4123 0.4890 -0.0292 0.0381  -0.0036 385 MET B CG  
2867 S SD  . MET B 121 ? 0.4315 0.5003 0.5622 -0.0300 0.0565  0.0031  385 MET B SD  
2868 C CE  . MET B 121 ? 0.3514 0.4338 0.5215 -0.0361 0.0616  0.0139  385 MET B CE  
2869 N N   . GLU B 122 ? 0.2034 0.2605 0.3563 -0.0225 0.0121  -0.0153 386 GLU B N   
2870 C CA  . GLU B 122 ? 0.2370 0.3020 0.4102 -0.0205 0.0100  -0.0175 386 GLU B CA  
2871 C C   . GLU B 122 ? 0.2681 0.3262 0.4274 -0.0155 0.0012  -0.0216 386 GLU B C   
2872 O O   . GLU B 122 ? 0.2477 0.3115 0.4199 -0.0129 0.0004  -0.0237 386 GLU B O   
2873 C CB  . GLU B 122 ? 0.2508 0.3190 0.4545 -0.0251 0.0010  -0.0140 386 GLU B CB  
2874 C CG  . GLU B 122 ? 0.3001 0.3529 0.4961 -0.0254 -0.0183 -0.0158 386 GLU B CG  
2875 C CD  . GLU B 122 ? 0.3758 0.4160 0.5610 -0.0290 -0.0243 -0.0137 386 GLU B CD  
2876 O OE1 . GLU B 122 ? 0.4032 0.4287 0.5847 -0.0286 -0.0422 -0.0159 386 GLU B OE1 
2877 O OE2 . GLU B 122 ? 0.3644 0.4071 0.5426 -0.0314 -0.0130 -0.0103 386 GLU B OE2 
2878 N N   . LEU B 123 ? 0.2554 0.3020 0.3897 -0.0134 -0.0043 -0.0217 387 LEU B N   
2879 C CA  . LEU B 123 ? 0.2161 0.2579 0.3372 -0.0080 -0.0104 -0.0225 387 LEU B CA  
2880 C C   . LEU B 123 ? 0.2605 0.3088 0.3814 -0.0060 -0.0026 -0.0232 387 LEU B C   
2881 O O   . LEU B 123 ? 0.2861 0.3340 0.4069 -0.0028 -0.0071 -0.0225 387 LEU B O   
2882 C CB  . LEU B 123 ? 0.2794 0.3099 0.3735 -0.0042 -0.0137 -0.0209 387 LEU B CB  
2883 C CG  . LEU B 123 ? 0.3556 0.3796 0.4353 0.0026  -0.0211 -0.0193 387 LEU B CG  
2884 C CD1 . LEU B 123 ? 0.3974 0.4083 0.4687 0.0052  -0.0338 -0.0214 387 LEU B CD1 
2885 C CD2 . LEU B 123 ? 0.4192 0.4413 0.4778 0.0075  -0.0151 -0.0151 387 LEU B CD2 
2886 N N   . PHE B 124 ? 0.2092 0.2615 0.3279 -0.0076 0.0076  -0.0241 388 PHE B N   
2887 C CA  . PHE B 124 ? 0.2049 0.2582 0.3181 -0.0054 0.0117  -0.0258 388 PHE B CA  
2888 C C   . PHE B 124 ? 0.2180 0.2772 0.3451 -0.0037 0.0174  -0.0305 388 PHE B C   
2889 O O   . PHE B 124 ? 0.2301 0.2870 0.3500 -0.0013 0.0202  -0.0338 388 PHE B O   
2890 C CB  . PHE B 124 ? 0.2198 0.2692 0.3143 -0.0064 0.0168  -0.0242 388 PHE B CB  
2891 C CG  . PHE B 124 ? 0.2510 0.2949 0.3325 -0.0062 0.0127  -0.0197 388 PHE B CG  
2892 C CD1 . PHE B 124 ? 0.2063 0.2485 0.2822 -0.0028 0.0082  -0.0159 388 PHE B CD1 
2893 C CD2 . PHE B 124 ? 0.2333 0.2737 0.3095 -0.0085 0.0137  -0.0184 388 PHE B CD2 
2894 C CE1 . PHE B 124 ? 0.2208 0.2584 0.2832 0.0000  0.0066  -0.0114 388 PHE B CE1 
2895 C CE2 . PHE B 124 ? 0.2580 0.2911 0.3200 -0.0060 0.0096  -0.0155 388 PHE B CE2 
2896 C CZ  . PHE B 124 ? 0.2204 0.2526 0.2746 -0.0008 0.0071  -0.0123 388 PHE B CZ  
2897 N N   . ARG B 125 ? 0.1992 0.2654 0.3475 -0.0041 0.0180  -0.0312 389 ARG B N   
2898 C CA  . ARG B 125 ? 0.2030 0.2766 0.3661 -0.0006 0.0263  -0.0353 389 ARG B CA  
2899 C C   . ARG B 125 ? 0.1912 0.2610 0.3550 0.0045  0.0222  -0.0403 389 ARG B C   
2900 O O   . ARG B 125 ? 0.2294 0.2994 0.3925 0.0096  0.0294  -0.0460 389 ARG B O   
2901 C CB  . ARG B 125 ? 0.2066 0.2904 0.3990 -0.0018 0.0266  -0.0331 389 ARG B CB  
2902 C CG  . ARG B 125 ? 0.2001 0.2888 0.3976 -0.0067 0.0326  -0.0277 389 ARG B CG  
2903 C CD  . ARG B 125 ? 0.2013 0.3015 0.4338 -0.0085 0.0322  -0.0239 389 ARG B CD  
2904 N NE  . ARG B 125 ? 0.2195 0.3234 0.4604 -0.0148 0.0355  -0.0165 389 ARG B NE  
2905 C CZ  . ARG B 125 ? 0.1939 0.3074 0.4694 -0.0189 0.0326  -0.0101 389 ARG B CZ  
2906 N NH1 . ARG B 125 ? 0.1989 0.3146 0.4850 -0.0256 0.0338  -0.0020 389 ARG B NH1 
2907 N NH2 . ARG B 125 ? 0.2038 0.3248 0.5073 -0.0167 0.0273  -0.0108 389 ARG B NH2 
2908 N N   . ALA B 126 ? 0.1804 0.2453 0.3443 0.0039  0.0105  -0.0380 390 ALA B N   
2909 C CA  . ALA B 126 ? 0.2164 0.2771 0.3852 0.0078  0.0050  -0.0410 390 ALA B CA  
2910 C C   . ALA B 126 ? 0.2309 0.2831 0.3824 0.0093  0.0059  -0.0443 390 ALA B C   
2911 O O   . ALA B 126 ? 0.2404 0.2870 0.3967 0.0133  0.0016  -0.0491 390 ALA B O   
2912 C CB  . ALA B 126 ? 0.2751 0.3330 0.4475 0.0066  -0.0070 -0.0349 390 ALA B CB  
2913 N N   . LEU B 127 ? 0.2495 0.2992 0.3823 0.0065  0.0096  -0.0420 391 LEU B N   
2914 C CA  . LEU B 127 ? 0.2347 0.2752 0.3514 0.0077  0.0083  -0.0450 391 LEU B CA  
2915 C C   . LEU B 127 ? 0.2621 0.2992 0.3722 0.0136  0.0159  -0.0545 391 LEU B C   
2916 O O   . LEU B 127 ? 0.2603 0.2859 0.3584 0.0168  0.0112  -0.0601 391 LEU B O   
2917 C CB  . LEU B 127 ? 0.2582 0.2971 0.3575 0.0036  0.0101  -0.0397 391 LEU B CB  
2918 C CG  . LEU B 127 ? 0.2680 0.3085 0.3688 0.0005  0.0038  -0.0303 391 LEU B CG  
2919 C CD1 . LEU B 127 ? 0.2857 0.3255 0.3711 -0.0020 0.0077  -0.0262 391 LEU B CD1 
2920 C CD2 . LEU B 127 ? 0.2415 0.2767 0.3478 0.0006  -0.0062 -0.0269 391 LEU B CD2 
2921 N N   . GLY B 128 ? 0.2258 0.2724 0.3444 0.0159  0.0273  -0.0561 392 GLY B N   
2922 C CA  . GLY B 128 ? 0.2722 0.3170 0.3828 0.0240  0.0377  -0.0641 392 GLY B CA  
2923 C C   . GLY B 128 ? 0.3138 0.3518 0.3959 0.0257  0.0451  -0.0657 392 GLY B C   
2924 O O   . GLY B 128 ? 0.3696 0.3983 0.4343 0.0344  0.0491  -0.0743 392 GLY B O   
2925 N N   . CYS B 129 ? 0.3089 0.3498 0.3838 0.0184  0.0461  -0.0579 393 CYS B N   
2926 C CA  . CYS B 129 ? 0.3148 0.3492 0.3624 0.0191  0.0522  -0.0576 393 CYS B CA  
2927 C C   . CYS B 129 ? 0.2706 0.3154 0.3230 0.0127  0.0604  -0.0479 393 CYS B C   
2928 O O   . CYS B 129 ? 0.2877 0.3284 0.3287 0.0073  0.0562  -0.0428 393 CYS B O   
2929 C CB  . CYS B 129 ? 0.3479 0.3675 0.3771 0.0168  0.0382  -0.0584 393 CYS B CB  
2930 S SG  . CYS B 129 ? 0.3227 0.3453 0.3679 0.0080  0.0248  -0.0495 393 CYS B SG  
2931 N N   . SER B 130 ? 0.3680 0.4266 0.4413 0.0134  0.0711  -0.0450 394 SER B N   
2932 C CA  . SER B 130 ? 0.3681 0.4364 0.4531 0.0067  0.0769  -0.0352 394 SER B CA  
2933 C C   . SER B 130 ? 0.2638 0.3281 0.3258 0.0053  0.0844  -0.0302 394 SER B C   
2934 O O   . SER B 130 ? 0.3355 0.3997 0.3989 -0.0021 0.0812  -0.0228 394 SER B O   
2935 C CB  . SER B 130 ? 0.4949 0.5792 0.6076 0.0089  0.0889  -0.0317 394 SER B CB  
2936 O OG  . SER B 130 ? 0.6502 0.7370 0.7489 0.0168  0.1059  -0.0320 394 SER B OG  
2937 N N   . GLU B 131 ? 0.2885 0.3483 0.3286 0.0134  0.0943  -0.0342 395 GLU B N   
2938 C CA  . GLU B 131 ? 0.3751 0.4303 0.3901 0.0132  0.1022  -0.0287 395 GLU B CA  
2939 C C   . GLU B 131 ? 0.3685 0.4106 0.3665 0.0072  0.0874  -0.0281 395 GLU B C   
2940 O O   . GLU B 131 ? 0.3499 0.3919 0.3442 0.0011  0.0879  -0.0195 395 GLU B O   
2941 C CB  . GLU B 131 ? 0.5330 0.5810 0.5189 0.0254  0.1133  -0.0350 395 GLU B CB  
2942 C CG  . GLU B 131 ? 0.7331 0.7750 0.6883 0.0264  0.1219  -0.0283 395 GLU B CG  
2943 C CD  . GLU B 131 ? 0.9197 0.9609 0.8506 0.0402  0.1408  -0.0303 395 GLU B CD  
2944 O OE1 . GLU B 131 ? 0.9770 1.0121 0.8995 0.0513  0.1413  -0.0425 395 GLU B OE1 
2945 O OE2 . GLU B 131 ? 0.9545 1.0005 0.8735 0.0408  0.1554  -0.0192 395 GLU B OE2 
2946 N N   . LEU B 132 ? 0.3498 0.3813 0.3404 0.0089  0.0738  -0.0360 396 LEU B N   
2947 C CA  . LEU B 132 ? 0.3175 0.3389 0.2966 0.0040  0.0603  -0.0341 396 LEU B CA  
2948 C C   . LEU B 132 ? 0.2794 0.3079 0.2782 -0.0037 0.0558  -0.0265 396 LEU B C   
2949 O O   . LEU B 132 ? 0.2879 0.3124 0.2786 -0.0077 0.0523  -0.0208 396 LEU B O   
2950 C CB  . LEU B 132 ? 0.3418 0.3527 0.3174 0.0067  0.0460  -0.0416 396 LEU B CB  
2951 C CG  . LEU B 132 ? 0.3726 0.3773 0.3476 0.0017  0.0315  -0.0376 396 LEU B CG  
2952 C CD1 . LEU B 132 ? 0.3623 0.3587 0.3147 0.0003  0.0303  -0.0336 396 LEU B CD1 
2953 C CD2 . LEU B 132 ? 0.3464 0.3419 0.3234 0.0044  0.0182  -0.0439 396 LEU B CD2 
2954 N N   . ILE B 133 ? 0.2541 0.2913 0.2769 -0.0048 0.0546  -0.0272 397 ILE B N   
2955 C CA  . ILE B 133 ? 0.2375 0.2780 0.2743 -0.0099 0.0490  -0.0220 397 ILE B CA  
2956 C C   . ILE B 133 ? 0.2727 0.3155 0.3106 -0.0142 0.0552  -0.0149 397 ILE B C   
2957 O O   . ILE B 133 ? 0.2370 0.2747 0.2706 -0.0175 0.0497  -0.0105 397 ILE B O   
2958 C CB  . ILE B 133 ? 0.2832 0.3307 0.3430 -0.0095 0.0456  -0.0241 397 ILE B CB  
2959 C CG1 . ILE B 133 ? 0.2999 0.3443 0.3606 -0.0060 0.0379  -0.0291 397 ILE B CG1 
2960 C CG2 . ILE B 133 ? 0.2688 0.3160 0.3370 -0.0133 0.0389  -0.0196 397 ILE B CG2 
2961 C CD1 . ILE B 133 ? 0.2872 0.3255 0.3388 -0.0070 0.0288  -0.0258 397 ILE B CD1 
2962 N N   . SER B 134 ? 0.2566 0.3073 0.3029 -0.0139 0.0668  -0.0126 398 SER B N   
2963 C CA  . SER B 134 ? 0.2338 0.2874 0.2855 -0.0191 0.0725  -0.0031 398 SER B CA  
2964 C C   . SER B 134 ? 0.3467 0.3899 0.3711 -0.0198 0.0725  0.0004  398 SER B C   
2965 O O   . SER B 134 ? 0.3101 0.3494 0.3358 -0.0248 0.0689  0.0070  398 SER B O   
2966 C CB  . SER B 134 ? 0.3614 0.4284 0.4300 -0.0181 0.0874  0.0018  398 SER B CB  
2967 O OG  . SER B 134 ? 0.5985 0.6643 0.6440 -0.0118 0.0998  0.0013  398 SER B OG  
2968 N N   . SER B 135 ? 0.3258 0.3624 0.3259 -0.0145 0.0738  -0.0045 399 SER B N   
2969 C CA  . SER B 135 ? 0.3148 0.3402 0.2889 -0.0148 0.0710  -0.0014 399 SER B CA  
2970 C C   . SER B 135 ? 0.2950 0.3137 0.2698 -0.0182 0.0576  -0.0002 399 SER B C   
2971 O O   . SER B 135 ? 0.3320 0.3451 0.2986 -0.0211 0.0558  0.0063  399 SER B O   
2972 C CB  . SER B 135 ? 0.4148 0.4311 0.3626 -0.0079 0.0704  -0.0087 399 SER B CB  
2973 O OG  . SER B 135 ? 0.5008 0.5207 0.4390 -0.0021 0.0852  -0.0090 399 SER B OG  
2974 N N   . ILE B 136 ? 0.2746 0.2945 0.2601 -0.0170 0.0493  -0.0053 400 ILE B N   
2975 C CA  . ILE B 136 ? 0.2399 0.2559 0.2279 -0.0179 0.0393  -0.0032 400 ILE B CA  
2976 C C   . ILE B 136 ? 0.2780 0.2943 0.2762 -0.0212 0.0391  0.0015  400 ILE B C   
2977 O O   . ILE B 136 ? 0.3125 0.3225 0.3049 -0.0219 0.0350  0.0056  400 ILE B O   
2978 C CB  . ILE B 136 ? 0.2657 0.2848 0.2640 -0.0152 0.0329  -0.0076 400 ILE B CB  
2979 C CG1 . ILE B 136 ? 0.3054 0.3207 0.2955 -0.0126 0.0288  -0.0118 400 ILE B CG1 
2980 C CG2 . ILE B 136 ? 0.2899 0.3079 0.2924 -0.0143 0.0264  -0.0038 400 ILE B CG2 
2981 C CD1 . ILE B 136 ? 0.3391 0.3587 0.3440 -0.0107 0.0240  -0.0149 400 ILE B CD1 
2982 N N   . PHE B 137 ? 0.2746 0.2971 0.2895 -0.0230 0.0423  0.0008  401 PHE B N   
2983 C CA  . PHE B 137 ? 0.2634 0.2832 0.2895 -0.0265 0.0388  0.0046  401 PHE B CA  
2984 C C   . PHE B 137 ? 0.2723 0.2880 0.2934 -0.0308 0.0426  0.0126  401 PHE B C   
2985 O O   . PHE B 137 ? 0.3094 0.3163 0.3303 -0.0324 0.0358  0.0158  401 PHE B O   
2986 C CB  . PHE B 137 ? 0.2537 0.2810 0.3023 -0.0285 0.0395  0.0033  401 PHE B CB  
2987 C CG  . PHE B 137 ? 0.2656 0.2919 0.3193 -0.0249 0.0308  -0.0026 401 PHE B CG  
2988 C CD1 . PHE B 137 ? 0.2470 0.2764 0.2950 -0.0204 0.0308  -0.0072 401 PHE B CD1 
2989 C CD2 . PHE B 137 ? 0.3065 0.3265 0.3689 -0.0257 0.0211  -0.0031 401 PHE B CD2 
2990 C CE1 . PHE B 137 ? 0.2742 0.3030 0.3262 -0.0169 0.0237  -0.0104 401 PHE B CE1 
2991 C CE2 . PHE B 137 ? 0.3259 0.3432 0.3876 -0.0210 0.0132  -0.0080 401 PHE B CE2 
2992 C CZ  . PHE B 137 ? 0.2987 0.3215 0.3553 -0.0167 0.0156  -0.0108 401 PHE B CZ  
2993 N N   . ASP B 138 ? 0.2956 0.3166 0.3116 -0.0318 0.0535  0.0163  402 ASP B N   
2994 C CA  . ASP B 138 ? 0.3338 0.3516 0.3436 -0.0356 0.0585  0.0261  402 ASP B CA  
2995 C C   . ASP B 138 ? 0.3462 0.3521 0.3349 -0.0345 0.0517  0.0275  402 ASP B C   
2996 O O   . ASP B 138 ? 0.3393 0.3386 0.3277 -0.0382 0.0494  0.0352  402 ASP B O   
2997 C CB  . ASP B 138 ? 0.3573 0.3830 0.3599 -0.0342 0.0736  0.0301  402 ASP B CB  
2998 C CG  . ASP B 138 ? 0.5487 0.5886 0.5782 -0.0355 0.0824  0.0325  402 ASP B CG  
2999 O OD1 . ASP B 138 ? 0.6205 0.6629 0.6761 -0.0399 0.0752  0.0332  402 ASP B OD1 
3000 O OD2 . ASP B 138 ? 0.5282 0.5760 0.5519 -0.0313 0.0962  0.0337  402 ASP B OD2 
3001 N N   . PHE B 139 ? 0.3476 0.3509 0.3220 -0.0297 0.0478  0.0211  403 PHE B N   
3002 C CA  . PHE B 139 ? 0.3346 0.3282 0.2935 -0.0284 0.0403  0.0233  403 PHE B CA  
3003 C C   . PHE B 139 ? 0.3528 0.3416 0.3217 -0.0281 0.0317  0.0241  403 PHE B C   
3004 O O   . PHE B 139 ? 0.3574 0.3378 0.3217 -0.0293 0.0277  0.0299  403 PHE B O   
3005 C CB  . PHE B 139 ? 0.3120 0.3045 0.2603 -0.0241 0.0354  0.0174  403 PHE B CB  
3006 C CG  . PHE B 139 ? 0.3124 0.2963 0.2493 -0.0231 0.0266  0.0210  403 PHE B CG  
3007 C CD1 . PHE B 139 ? 0.3850 0.3608 0.3034 -0.0246 0.0273  0.0269  403 PHE B CD1 
3008 C CD2 . PHE B 139 ? 0.3598 0.3444 0.3056 -0.0204 0.0184  0.0202  403 PHE B CD2 
3009 C CE1 . PHE B 139 ? 0.3781 0.3456 0.2880 -0.0240 0.0177  0.0309  403 PHE B CE1 
3010 C CE2 . PHE B 139 ? 0.4016 0.3800 0.3418 -0.0194 0.0103  0.0250  403 PHE B CE2 
3011 C CZ  . PHE B 139 ? 0.4048 0.3742 0.3276 -0.0215 0.0090  0.0299  403 PHE B CZ  
3012 N N   . SER B 140 ? 0.3048 0.2975 0.2858 -0.0255 0.0288  0.0182  404 SER B N   
3013 C CA  . SER B 140 ? 0.2898 0.2762 0.2757 -0.0223 0.0215  0.0174  404 SER B CA  
3014 C C   . SER B 140 ? 0.2832 0.2618 0.2752 -0.0266 0.0193  0.0215  404 SER B C   
3015 O O   . SER B 140 ? 0.3161 0.2840 0.3050 -0.0244 0.0129  0.0233  404 SER B O   
3016 C CB  . SER B 140 ? 0.3360 0.3268 0.3301 -0.0183 0.0195  0.0111  404 SER B CB  
3017 O OG  . SER B 140 ? 0.4639 0.4612 0.4553 -0.0148 0.0204  0.0093  404 SER B OG  
3018 N N   . HIS B 141 ? 0.3037 0.2875 0.3075 -0.0323 0.0238  0.0235  405 HIS B N   
3019 C CA  . HIS B 141 ? 0.3055 0.2824 0.3213 -0.0378 0.0200  0.0292  405 HIS B CA  
3020 C C   . HIS B 141 ? 0.3500 0.3192 0.3562 -0.0404 0.0203  0.0380  405 HIS B C   
3021 O O   . HIS B 141 ? 0.3533 0.3098 0.3632 -0.0415 0.0116  0.0408  405 HIS B O   
3022 C CB  . HIS B 141 ? 0.3292 0.3171 0.3647 -0.0440 0.0268  0.0331  405 HIS B CB  
3023 C CG  . HIS B 141 ? 0.3732 0.3546 0.4299 -0.0503 0.0190  0.0386  405 HIS B CG  
3024 N ND1 . HIS B 141 ? 0.3647 0.3408 0.4354 -0.0498 0.0075  0.0324  405 HIS B ND1 
3025 C CD2 . HIS B 141 ? 0.4477 0.4256 0.5149 -0.0575 0.0194  0.0504  405 HIS B CD2 
3026 C CE1 . HIS B 141 ? 0.4100 0.3786 0.5003 -0.0567 -0.0006 0.0393  405 HIS B CE1 
3027 N NE2 . HIS B 141 ? 0.4354 0.4058 0.5258 -0.0619 0.0070  0.0511  405 HIS B NE2 
3028 N N   . SER B 142 ? 0.3650 0.3393 0.3567 -0.0406 0.0285  0.0418  406 SER B N   
3029 C CA  . SER B 142 ? 0.3244 0.2908 0.3046 -0.0431 0.0284  0.0513  406 SER B CA  
3030 C C   . SER B 142 ? 0.3779 0.3323 0.3508 -0.0384 0.0176  0.0494  406 SER B C   
3031 O O   . SER B 142 ? 0.4024 0.3461 0.3751 -0.0405 0.0125  0.0564  406 SER B O   
3032 C CB  . SER B 142 ? 0.3985 0.3698 0.3589 -0.0424 0.0374  0.0542  406 SER B CB  
3033 O OG  . SER B 142 ? 0.5179 0.4883 0.4652 -0.0365 0.0329  0.0465  406 SER B OG  
3034 N N   . LEU B 143 ? 0.3732 0.3302 0.3422 -0.0314 0.0146  0.0412  407 LEU B N   
3035 C CA  . LEU B 143 ? 0.3784 0.3273 0.3439 -0.0249 0.0067  0.0401  407 LEU B CA  
3036 C C   . LEU B 143 ? 0.4343 0.3728 0.4080 -0.0213 -0.0004 0.0366  407 LEU B C   
3037 O O   . LEU B 143 ? 0.4057 0.3337 0.3765 -0.0161 -0.0066 0.0376  407 LEU B O   
3038 C CB  . LEU B 143 ? 0.3891 0.3466 0.3523 -0.0185 0.0071  0.0349  407 LEU B CB  
3039 C CG  . LEU B 143 ? 0.4046 0.3666 0.3577 -0.0201 0.0083  0.0374  407 LEU B CG  
3040 C CD1 . LEU B 143 ? 0.3777 0.3475 0.3357 -0.0144 0.0059  0.0339  407 LEU B CD1 
3041 C CD2 . LEU B 143 ? 0.4471 0.4001 0.3903 -0.0216 0.0036  0.0453  407 LEU B CD2 
3042 N N   . SER B 144 ? 0.3755 0.3152 0.3589 -0.0234 -0.0007 0.0321  408 SER B N   
3043 C CA  . SER B 144 ? 0.4164 0.3432 0.4034 -0.0182 -0.0100 0.0261  408 SER B CA  
3044 C C   . SER B 144 ? 0.4497 0.3598 0.4404 -0.0217 -0.0185 0.0315  408 SER B C   
3045 O O   . SER B 144 ? 0.4297 0.3231 0.4175 -0.0147 -0.0286 0.0265  408 SER B O   
3046 C CB  . SER B 144 ? 0.4637 0.3947 0.4612 -0.0208 -0.0109 0.0207  408 SER B CB  
3047 O OG  . SER B 144 ? 0.4820 0.4155 0.4953 -0.0318 -0.0099 0.0275  408 SER B OG  
3048 N N   . ALA B 145 ? 0.4290 0.3423 0.4248 -0.0316 -0.0143 0.0422  409 ALA B N   
3049 C CA  . ALA B 145 ? 0.5024 0.4014 0.5052 -0.0371 -0.0218 0.0505  409 ALA B CA  
3050 C C   . ALA B 145 ? 0.4578 0.3429 0.4496 -0.0295 -0.0288 0.0504  409 ALA B C   
3051 O O   . ALA B 145 ? 0.4902 0.3575 0.4871 -0.0299 -0.0395 0.0528  409 ALA B O   
3052 C CB  . ALA B 145 ? 0.5383 0.4468 0.5456 -0.0478 -0.0125 0.0643  409 ALA B CB  
3053 N N   . LEU B 146 ? 0.4532 0.3466 0.4325 -0.0225 -0.0234 0.0483  410 LEU B N   
3054 C CA  . LEU B 146 ? 0.4162 0.3007 0.3887 -0.0155 -0.0283 0.0506  410 LEU B CA  
3055 C C   . LEU B 146 ? 0.4485 0.3202 0.4189 -0.0022 -0.0356 0.0413  410 LEU B C   
3056 O O   . LEU B 146 ? 0.4448 0.3042 0.4130 0.0042  -0.0417 0.0434  410 LEU B O   
3057 C CB  . LEU B 146 ? 0.4730 0.3713 0.4374 -0.0129 -0.0219 0.0528  410 LEU B CB  
3058 C CG  . LEU B 146 ? 0.6076 0.5153 0.5653 -0.0223 -0.0155 0.0606  410 LEU B CG  
3059 C CD1 . LEU B 146 ? 0.6206 0.5305 0.5700 -0.0185 -0.0178 0.0644  410 LEU B CD1 
3060 C CD2 . LEU B 146 ? 0.6413 0.5413 0.6005 -0.0318 -0.0159 0.0705  410 LEU B CD2 
3061 N N   . HIS B 147 ? 0.4048 0.3692 0.4380 -0.0050 -0.0369 0.0033  411 HIS B N   
3062 C CA  . HIS B 147 ? 0.3786 0.3130 0.3913 0.0013  -0.0405 0.0021  411 HIS B CA  
3063 C C   . HIS B 147 ? 0.3529 0.2709 0.3524 0.0068  -0.0313 0.0098  411 HIS B C   
3064 O O   . HIS B 147 ? 0.3859 0.2851 0.3793 0.0059  -0.0279 0.0113  411 HIS B O   
3065 C CB  . HIS B 147 ? 0.3972 0.3183 0.4107 -0.0079 -0.0440 -0.0005 411 HIS B CB  
3066 C CG  . HIS B 147 ? 0.5180 0.4542 0.5445 -0.0137 -0.0545 -0.0102 411 HIS B CG  
3067 N ND1 . HIS B 147 ? 0.5147 0.4850 0.5636 -0.0164 -0.0565 -0.0152 411 HIS B ND1 
3068 C CD2 . HIS B 147 ? 0.5696 0.4938 0.5924 -0.0178 -0.0638 -0.0176 411 HIS B CD2 
3069 C CE1 . HIS B 147 ? 0.5340 0.5150 0.5956 -0.0215 -0.0670 -0.0255 411 HIS B CE1 
3070 N NE2 . HIS B 147 ? 0.5206 0.4723 0.5650 -0.0227 -0.0723 -0.0263 411 HIS B NE2 
3071 N N   . PHE B 148 ? 0.3701 0.2965 0.3676 0.0129  -0.0279 0.0129  412 PHE B N   
3072 C CA  . PHE B 148 ? 0.3672 0.2820 0.3550 0.0173  -0.0197 0.0185  412 PHE B CA  
3073 C C   . PHE B 148 ? 0.3811 0.2730 0.3510 0.0201  -0.0181 0.0139  412 PHE B C   
3074 O O   . PHE B 148 ? 0.4334 0.3152 0.3864 0.0218  -0.0243 0.0080  412 PHE B O   
3075 C CB  . PHE B 148 ? 0.3822 0.3035 0.3642 0.0234  -0.0192 0.0198  412 PHE B CB  
3076 C CG  . PHE B 148 ? 0.4090 0.3511 0.4052 0.0220  -0.0161 0.0242  412 PHE B CG  
3077 C CD1 . PHE B 148 ? 0.5106 0.4562 0.5149 0.0166  -0.0100 0.0319  412 PHE B CD1 
3078 C CD2 . PHE B 148 ? 0.4099 0.3653 0.4088 0.0267  -0.0208 0.0199  412 PHE B CD2 
3079 C CE1 . PHE B 148 ? 0.5608 0.5234 0.5718 0.0138  -0.0072 0.0359  412 PHE B CE1 
3080 C CE2 . PHE B 148 ? 0.4672 0.4420 0.4766 0.0254  -0.0167 0.0216  412 PHE B CE2 
3081 C CZ  . PHE B 148 ? 0.5034 0.4821 0.5170 0.0178  -0.0092 0.0300  412 PHE B CZ  
3082 N N   . SER B 149 ? 0.3492 0.2326 0.3217 0.0206  -0.0107 0.0151  413 SER B N   
3083 C CA  . SER B 149 ? 0.3987 0.2668 0.3554 0.0232  -0.0048 0.0083  413 SER B CA  
3084 C C   . SER B 149 ? 0.3911 0.2617 0.3358 0.0251  0.0012  0.0103  413 SER B C   
3085 O O   . SER B 149 ? 0.3912 0.2743 0.3441 0.0262  0.0007  0.0171  413 SER B O   
3086 C CB  . SER B 149 ? 0.4284 0.2904 0.3980 0.0252  0.0006  0.0054  413 SER B CB  
3087 O OG  . SER B 149 ? 0.4036 0.2760 0.3886 0.0283  0.0051  0.0115  413 SER B OG  
3088 N N   . GLU B 150 ? 0.4166 0.2746 0.3401 0.0237  0.0077  0.0040  414 GLU B N   
3089 C CA  . GLU B 150 ? 0.4028 0.2611 0.3129 0.0218  0.0142  0.0068  414 GLU B CA  
3090 C C   . GLU B 150 ? 0.3655 0.2399 0.2989 0.0237  0.0231  0.0096  414 GLU B C   
3091 O O   . GLU B 150 ? 0.3919 0.2724 0.3242 0.0226  0.0244  0.0151  414 GLU B O   
3092 C CB  . GLU B 150 ? 0.4689 0.3101 0.3473 0.0156  0.0215  -0.0005 414 GLU B CB  
3093 C CG  . GLU B 150 ? 0.5097 0.3303 0.3573 0.0132  0.0088  -0.0013 414 GLU B CG  
3094 C CD  . GLU B 150 ? 0.5547 0.3682 0.3879 0.0140  -0.0033 0.0067  414 GLU B CD  
3095 O OE1 . GLU B 150 ? 0.5303 0.3280 0.3341 0.0073  -0.0001 0.0092  414 GLU B OE1 
3096 O OE2 . GLU B 150 ? 0.5060 0.3299 0.3578 0.0206  -0.0158 0.0095  414 GLU B OE2 
3097 N N   . ASP B 151 ? 0.3904 0.2698 0.3448 0.0271  0.0271  0.0051  415 ASP B N   
3098 C CA  . ASP B 151 ? 0.3550 0.2490 0.3342 0.0306  0.0316  0.0069  415 ASP B CA  
3099 C C   . ASP B 151 ? 0.3461 0.2485 0.3366 0.0317  0.0225  0.0189  415 ASP B C   
3100 O O   . ASP B 151 ? 0.3636 0.2769 0.3625 0.0321  0.0241  0.0235  415 ASP B O   
3101 C CB  . ASP B 151 ? 0.3801 0.2738 0.3810 0.0366  0.0331  -0.0014 415 ASP B CB  
3102 C CG  . ASP B 151 ? 0.5039 0.3970 0.5000 0.0361  0.0461  -0.0173 415 ASP B CG  
3103 O OD1 . ASP B 151 ? 0.4749 0.3692 0.4499 0.0286  0.0561  -0.0202 415 ASP B OD1 
3104 O OD2 . ASP B 151 ? 0.5559 0.4461 0.5685 0.0427  0.0462  -0.0277 415 ASP B OD2 
3105 N N   . GLU B 152 ? 0.3477 0.2464 0.3385 0.0307  0.0138  0.0229  416 GLU B N   
3106 C CA  . GLU B 152 ? 0.3341 0.2432 0.3330 0.0289  0.0076  0.0325  416 GLU B CA  
3107 C C   . GLU B 152 ? 0.3375 0.2549 0.3270 0.0284  0.0073  0.0349  416 GLU B C   
3108 O O   . GLU B 152 ? 0.3331 0.2611 0.3292 0.0283  0.0071  0.0404  416 GLU B O   
3109 C CB  . GLU B 152 ? 0.3287 0.2355 0.3296 0.0244  0.0006  0.0340  416 GLU B CB  
3110 C CG  . GLU B 152 ? 0.3635 0.2585 0.3746 0.0237  -0.0026 0.0351  416 GLU B CG  
3111 C CD  . GLU B 152 ? 0.3531 0.2413 0.3628 0.0165  -0.0086 0.0346  416 GLU B CD  
3112 O OE1 . GLU B 152 ? 0.3848 0.2819 0.3891 0.0131  -0.0101 0.0319  416 GLU B OE1 
3113 O OE2 . GLU B 152 ? 0.3936 0.2672 0.4087 0.0143  -0.0134 0.0364  416 GLU B OE2 
3114 N N   . ILE B 153 ? 0.3289 0.2386 0.3012 0.0284  0.0055  0.0305  417 ILE B N   
3115 C CA  . ILE B 153 ? 0.3437 0.2561 0.3068 0.0296  0.0019  0.0318  417 ILE B CA  
3116 C C   . ILE B 153 ? 0.3244 0.2352 0.2823 0.0285  0.0088  0.0339  417 ILE B C   
3117 O O   . ILE B 153 ? 0.3284 0.2446 0.2865 0.0293  0.0065  0.0368  417 ILE B O   
3118 C CB  . ILE B 153 ? 0.3898 0.2897 0.3349 0.0309  -0.0067 0.0269  417 ILE B CB  
3119 C CG1 . ILE B 153 ? 0.4439 0.3504 0.3897 0.0353  -0.0158 0.0264  417 ILE B CG1 
3120 C CG2 . ILE B 153 ? 0.3965 0.2752 0.3154 0.0279  -0.0030 0.0247  417 ILE B CG2 
3121 C CD1 . ILE B 153 ? 0.4190 0.3101 0.3474 0.0392  -0.0289 0.0213  417 ILE B CD1 
3122 N N   . ALA B 154 ? 0.3579 0.2641 0.3144 0.0261  0.0178  0.0306  418 ALA B N   
3123 C CA  . ALA B 154 ? 0.3006 0.2103 0.2571 0.0226  0.0259  0.0306  418 ALA B CA  
3124 C C   . ALA B 154 ? 0.2998 0.2263 0.2796 0.0253  0.0244  0.0355  418 ALA B C   
3125 O O   . ALA B 154 ? 0.3292 0.2601 0.3078 0.0233  0.0242  0.0384  418 ALA B O   
3126 C CB  . ALA B 154 ? 0.3315 0.2401 0.2880 0.0191  0.0378  0.0223  418 ALA B CB  
3127 N N   . LEU B 155 ? 0.2974 0.2300 0.2958 0.0291  0.0218  0.0366  419 LEU B N   
3128 C CA  . LEU B 155 ? 0.2810 0.2249 0.2972 0.0310  0.0179  0.0422  419 LEU B CA  
3129 C C   . LEU B 155 ? 0.3083 0.2566 0.3177 0.0294  0.0117  0.0487  419 LEU B C   
3130 O O   . LEU B 155 ? 0.3101 0.2663 0.3229 0.0287  0.0098  0.0524  419 LEU B O   
3131 C CB  . LEU B 155 ? 0.3050 0.2468 0.3375 0.0346  0.0134  0.0430  419 LEU B CB  
3132 C CG  . LEU B 155 ? 0.3398 0.2806 0.3839 0.0384  0.0198  0.0325  419 LEU B CG  
3133 C CD1 . LEU B 155 ? 0.3519 0.2805 0.4037 0.0426  0.0142  0.0303  419 LEU B CD1 
3134 C CD2 . LEU B 155 ? 0.3868 0.3415 0.4525 0.0417  0.0200  0.0305  419 LEU B CD2 
3135 N N   . TYR B 156 ? 0.2940 0.2396 0.2954 0.0287  0.0086  0.0482  420 TYR B N   
3136 C CA  . TYR B 156 ? 0.2632 0.2186 0.2623 0.0273  0.0048  0.0504  420 TYR B CA  
3137 C C   . TYR B 156 ? 0.3045 0.2597 0.2939 0.0293  0.0042  0.0477  420 TYR B C   
3138 O O   . TYR B 156 ? 0.2949 0.2592 0.2858 0.0287  0.0028  0.0493  420 TYR B O   
3139 C CB  . TYR B 156 ? 0.3018 0.2591 0.3000 0.0260  0.0019  0.0471  420 TYR B CB  
3140 C CG  . TYR B 156 ? 0.3324 0.3060 0.3329 0.0243  0.0002  0.0452  420 TYR B CG  
3141 C CD1 . TYR B 156 ? 0.3982 0.3829 0.4025 0.0176  0.0017  0.0505  420 TYR B CD1 
3142 C CD2 . TYR B 156 ? 0.3334 0.3104 0.3310 0.0293  -0.0038 0.0371  420 TYR B CD2 
3143 C CE1 . TYR B 156 ? 0.4385 0.4427 0.4446 0.0144  0.0030  0.0456  420 TYR B CE1 
3144 C CE2 . TYR B 156 ? 0.4554 0.4520 0.4599 0.0295  -0.0048 0.0309  420 TYR B CE2 
3145 C CZ  . TYR B 156 ? 0.5003 0.5126 0.5094 0.0214  0.0005  0.0345  420 TYR B CZ  
3146 O OH  . TYR B 156 ? 0.5452 0.5807 0.5612 0.0202  0.0023  0.0256  420 TYR B OH  
3147 N N   . THR B 157 ? 0.2828 0.2245 0.2591 0.0305  0.0044  0.0438  421 THR B N   
3148 C CA  . THR B 157 ? 0.2753 0.2096 0.2389 0.0314  0.0011  0.0423  421 THR B CA  
3149 C C   . THR B 157 ? 0.2675 0.2042 0.2339 0.0275  0.0056  0.0453  421 THR B C   
3150 O O   . THR B 157 ? 0.3105 0.2456 0.2711 0.0277  0.0017  0.0449  421 THR B O   
3151 C CB  . THR B 157 ? 0.2968 0.2089 0.2384 0.0313  -0.0026 0.0394  421 THR B CB  
3152 O OG1 . THR B 157 ? 0.3535 0.2576 0.2891 0.0258  0.0058  0.0396  421 THR B OG1 
3153 C CG2 . THR B 157 ? 0.3198 0.2311 0.2606 0.0372  -0.0120 0.0346  421 THR B CG2 
3154 N N   . ALA B 158 ? 0.2748 0.2165 0.2524 0.0247  0.0123  0.0466  422 ALA B N   
3155 C CA  . ALA B 158 ? 0.2612 0.2107 0.2481 0.0213  0.0150  0.0478  422 ALA B CA  
3156 C C   . ALA B 158 ? 0.2759 0.2371 0.2710 0.0234  0.0086  0.0518  422 ALA B C   
3157 O O   . ALA B 158 ? 0.3115 0.2747 0.3045 0.0211  0.0065  0.0520  422 ALA B O   
3158 C CB  . ALA B 158 ? 0.2904 0.2479 0.2953 0.0207  0.0217  0.0451  422 ALA B CB  
3159 N N   . LEU B 159 ? 0.2900 0.2569 0.2906 0.0256  0.0056  0.0547  423 LEU B N   
3160 C CA  . LEU B 159 ? 0.2850 0.2613 0.2863 0.0244  0.0008  0.0586  423 LEU B CA  
3161 C C   . LEU B 159 ? 0.3573 0.3363 0.3472 0.0251  -0.0008 0.0541  423 LEU B C   
3162 O O   . LEU B 159 ? 0.3418 0.3278 0.3287 0.0233  -0.0032 0.0545  423 LEU B O   
3163 C CB  . LEU B 159 ? 0.2624 0.2408 0.2682 0.0226  -0.0014 0.0639  423 LEU B CB  
3164 C CG  . LEU B 159 ? 0.3334 0.3080 0.3524 0.0239  -0.0050 0.0683  423 LEU B CG  
3165 C CD1 . LEU B 159 ? 0.3460 0.3128 0.3669 0.0224  -0.0085 0.0731  423 LEU B CD1 
3166 C CD2 . LEU B 159 ? 0.3695 0.3491 0.3903 0.0224  -0.0120 0.0730  423 LEU B CD2 
3167 N N   . VAL B 160 ? 0.3009 0.2742 0.2847 0.0286  -0.0009 0.0484  424 VAL B N   
3168 C CA  . VAL B 160 ? 0.3279 0.3028 0.3051 0.0326  -0.0048 0.0409  424 VAL B CA  
3169 C C   . VAL B 160 ? 0.3462 0.3114 0.3153 0.0323  -0.0076 0.0401  424 VAL B C   
3170 O O   . VAL B 160 ? 0.3237 0.2942 0.2900 0.0339  -0.0106 0.0354  424 VAL B O   
3171 C CB  . VAL B 160 ? 0.3013 0.2673 0.2743 0.0383  -0.0088 0.0347  424 VAL B CB  
3172 C CG1 . VAL B 160 ? 0.3833 0.3479 0.3521 0.0457  -0.0164 0.0248  424 VAL B CG1 
3173 C CG2 . VAL B 160 ? 0.3102 0.2884 0.2930 0.0375  -0.0070 0.0336  424 VAL B CG2 
3174 N N   . LEU B 161 ? 0.3186 0.2703 0.2836 0.0288  -0.0056 0.0436  425 LEU B N   
3175 C CA  . LEU B 161 ? 0.3355 0.2760 0.2917 0.0250  -0.0077 0.0432  425 LEU B CA  
3176 C C   . LEU B 161 ? 0.3300 0.2838 0.2963 0.0207  -0.0071 0.0460  425 LEU B C   
3177 O O   . LEU B 161 ? 0.3355 0.2859 0.2955 0.0196  -0.0116 0.0432  425 LEU B O   
3178 C CB  . LEU B 161 ? 0.3341 0.2580 0.2808 0.0185  -0.0036 0.0451  425 LEU B CB  
3179 C CG  . LEU B 161 ? 0.4122 0.3118 0.3376 0.0202  -0.0086 0.0432  425 LEU B CG  
3180 C CD1 . LEU B 161 ? 0.5009 0.3858 0.4128 0.0089  -0.0013 0.0460  425 LEU B CD1 
3181 C CD2 . LEU B 161 ? 0.4359 0.3189 0.3475 0.0238  -0.0199 0.0393  425 LEU B CD2 
3182 N N   . ILE B 162 ? 0.2996 0.2659 0.2810 0.0189  -0.0037 0.0507  426 ILE B N   
3183 C CA  . ILE B 162 ? 0.3384 0.3155 0.3307 0.0155  -0.0066 0.0534  426 ILE B CA  
3184 C C   . ILE B 162 ? 0.3591 0.3452 0.3488 0.0171  -0.0114 0.0561  426 ILE B C   
3185 O O   . ILE B 162 ? 0.3489 0.3401 0.3454 0.0173  -0.0125 0.0615  426 ILE B O   
3186 C CB  . ILE B 162 ? 0.2748 0.2597 0.2870 0.0142  -0.0035 0.0551  426 ILE B CB  
3187 C CG1 . ILE B 162 ? 0.3118 0.2898 0.3227 0.0099  0.0052  0.0510  426 ILE B CG1 
3188 C CG2 . ILE B 162 ? 0.2977 0.2947 0.3248 0.0119  -0.0103 0.0563  426 ILE B CG2 
3189 C CD1 . ILE B 162 ? 0.3617 0.3293 0.3591 0.0018  0.0057  0.0485  426 ILE B CD1 
3190 N N   . ASN B 163 ? 0.3769 0.3628 0.3542 0.0172  -0.0141 0.0516  427 ASN B N   
3191 C CA  . ASN B 163 ? 0.3508 0.3463 0.3198 0.0162  -0.0156 0.0511  427 ASN B CA  
3192 C C   . ASN B 163 ? 0.3457 0.3429 0.3075 0.0126  -0.0217 0.0497  427 ASN B C   
3193 O O   . ASN B 163 ? 0.3344 0.3254 0.2897 0.0138  -0.0236 0.0422  427 ASN B O   
3194 C CB  . ASN B 163 ? 0.3527 0.3505 0.3156 0.0208  -0.0122 0.0419  427 ASN B CB  
3195 C CG  . ASN B 163 ? 0.4001 0.4134 0.3552 0.0176  -0.0099 0.0376  427 ASN B CG  
3196 O OD1 . ASN B 163 ? 0.4320 0.4494 0.3784 0.0113  -0.0121 0.0413  427 ASN B OD1 
3197 N ND2 . ASN B 163 ? 0.4201 0.4432 0.3778 0.0212  -0.0055 0.0282  427 ASN B ND2 
3198 N N   . ALA B 164 ? 0.3311 0.3333 0.2919 0.0079  -0.0268 0.0571  428 ALA B N   
3199 C CA  . ALA B 164 ? 0.3512 0.3540 0.3051 0.0040  -0.0348 0.0565  428 ALA B CA  
3200 C C   . ALA B 164 ? 0.3660 0.3729 0.2988 0.0016  -0.0336 0.0488  428 ALA B C   
3201 O O   . ALA B 164 ? 0.4267 0.4328 0.3494 -0.0021 -0.0403 0.0465  428 ALA B O   
3202 C CB  . ALA B 164 ? 0.4123 0.4162 0.3712 0.0008  -0.0448 0.0669  428 ALA B CB  
3203 N N   . HIS B 165 ? 0.3829 0.3961 0.3106 0.0035  -0.0250 0.0428  429 HIS B N   
3204 C CA  . HIS B 165 ? 0.4301 0.4525 0.3415 0.0015  -0.0216 0.0314  429 HIS B CA  
3205 C C   . HIS B 165 ? 0.4402 0.4582 0.3541 0.0104  -0.0217 0.0159  429 HIS B C   
3206 O O   . HIS B 165 ? 0.4613 0.4880 0.3652 0.0113  -0.0190 0.0023  429 HIS B O   
3207 C CB  . HIS B 165 ? 0.5289 0.5660 0.4358 -0.0029 -0.0117 0.0299  429 HIS B CB  
3208 C CG  . HIS B 165 ? 0.6495 0.6851 0.5448 -0.0146 -0.0136 0.0451  429 HIS B CG  
3209 N ND1 . HIS B 165 ? 0.6947 0.7372 0.5874 -0.0218 -0.0062 0.0493  429 HIS B ND1 
3210 C CD2 . HIS B 165 ? 0.7947 0.8193 0.6801 -0.0203 -0.0247 0.0575  429 HIS B CD2 
3211 C CE1 . HIS B 165 ? 0.7201 0.7519 0.5980 -0.0321 -0.0129 0.0647  429 HIS B CE1 
3212 N NE2 . HIS B 165 ? 0.8487 0.8695 0.7226 -0.0301 -0.0252 0.0697  429 HIS B NE2 
3213 N N   . ARG B 166 ? 0.3776 0.3805 0.3024 0.0163  -0.0252 0.0170  430 ARG B N   
3214 C CA  . ARG B 166 ? 0.3877 0.3782 0.3100 0.0241  -0.0292 0.0038  430 ARG B CA  
3215 C C   . ARG B 166 ? 0.3996 0.3848 0.3097 0.0211  -0.0356 -0.0027 430 ARG B C   
3216 O O   . ARG B 166 ? 0.3775 0.3582 0.2866 0.0132  -0.0407 0.0062  430 ARG B O   
3217 C CB  . ARG B 166 ? 0.3642 0.3335 0.2923 0.0266  -0.0326 0.0087  430 ARG B CB  
3218 C CG  . ARG B 166 ? 0.3239 0.2953 0.2617 0.0288  -0.0273 0.0155  430 ARG B CG  
3219 C CD  . ARG B 166 ? 0.3764 0.3589 0.3181 0.0370  -0.0244 0.0057  430 ARG B CD  
3220 N NE  . ARG B 166 ? 0.3759 0.3514 0.3238 0.0397  -0.0232 0.0108  430 ARG B NE  
3221 C CZ  . ARG B 166 ? 0.4090 0.3935 0.3643 0.0463  -0.0220 0.0041  430 ARG B CZ  
3222 N NH1 . ARG B 166 ? 0.4262 0.4312 0.3867 0.0502  -0.0197 -0.0090 430 ARG B NH1 
3223 N NH2 . ARG B 166 ? 0.3732 0.3485 0.3314 0.0480  -0.0226 0.0089  430 ARG B NH2 
3224 N N   . PRO B 167 ? 0.4121 0.3985 0.3153 0.0277  -0.0365 -0.0199 431 PRO B N   
3225 C CA  . PRO B 167 ? 0.5008 0.4783 0.3909 0.0255  -0.0437 -0.0283 431 PRO B CA  
3226 C C   . PRO B 167 ? 0.4587 0.4081 0.3489 0.0240  -0.0538 -0.0243 431 PRO B C   
3227 O O   . PRO B 167 ? 0.4602 0.3917 0.3549 0.0291  -0.0563 -0.0232 431 PRO B O   
3228 C CB  . PRO B 167 ? 0.5206 0.5047 0.4079 0.0362  -0.0421 -0.0511 431 PRO B CB  
3229 C CG  . PRO B 167 ? 0.5061 0.5134 0.4051 0.0399  -0.0313 -0.0535 431 PRO B CG  
3230 C CD  . PRO B 167 ? 0.4372 0.4366 0.3466 0.0377  -0.0311 -0.0348 431 PRO B CD  
3231 N N   . GLY B 168 ? 0.4488 0.3935 0.3321 0.0151  -0.0600 -0.0216 432 GLY B N   
3232 C CA  . GLY B 168 ? 0.5131 0.4320 0.3948 0.0104  -0.0691 -0.0204 432 GLY B CA  
3233 C C   . GLY B 168 ? 0.4938 0.4144 0.3881 -0.0012 -0.0686 -0.0048 432 GLY B C   
3234 O O   . GLY B 168 ? 0.5096 0.4122 0.4034 -0.0092 -0.0738 -0.0035 432 GLY B O   
3235 N N   . LEU B 169 ? 0.4387 0.3809 0.3448 -0.0029 -0.0627 0.0056  433 LEU B N   
3236 C CA  . LEU B 169 ? 0.3816 0.3308 0.3055 -0.0113 -0.0625 0.0168  433 LEU B CA  
3237 C C   . LEU B 169 ? 0.4484 0.4021 0.3748 -0.0204 -0.0723 0.0163  433 LEU B C   
3238 O O   . LEU B 169 ? 0.4842 0.4440 0.3986 -0.0202 -0.0785 0.0130  433 LEU B O   
3239 C CB  . LEU B 169 ? 0.3733 0.3411 0.3093 -0.0081 -0.0565 0.0262  433 LEU B CB  
3240 C CG  . LEU B 169 ? 0.3951 0.3597 0.3317 -0.0006 -0.0473 0.0269  433 LEU B CG  
3241 C CD1 . LEU B 169 ? 0.3394 0.3198 0.2854 0.0014  -0.0428 0.0355  433 LEU B CD1 
3242 C CD2 . LEU B 169 ? 0.4093 0.3597 0.3517 -0.0038 -0.0440 0.0288  433 LEU B CD2 
3243 N N   . GLN B 170 ? 0.4097 0.3617 0.3510 -0.0300 -0.0736 0.0188  434 GLN B N   
3244 C CA  . GLN B 170 ? 0.4347 0.3945 0.3848 -0.0396 -0.0839 0.0174  434 GLN B CA  
3245 C C   . GLN B 170 ? 0.4207 0.4064 0.3957 -0.0397 -0.0875 0.0246  434 GLN B C   
3246 O O   . GLN B 170 ? 0.4701 0.4646 0.4477 -0.0427 -0.1001 0.0239  434 GLN B O   
3247 C CB  . GLN B 170 ? 0.4257 0.3727 0.3810 -0.0525 -0.0835 0.0146  434 GLN B CB  
3248 C CG  . GLN B 170 ? 0.5623 0.4770 0.4899 -0.0526 -0.0875 0.0067  434 GLN B CG  
3249 C CD  . GLN B 170 ? 0.6541 0.5483 0.5801 -0.0687 -0.0881 0.0059  434 GLN B CD  
3250 O OE1 . GLN B 170 ? 0.6421 0.5514 0.5896 -0.0816 -0.0827 0.0100  434 GLN B OE1 
3251 N NE2 . GLN B 170 ? 0.7114 0.5706 0.6119 -0.0687 -0.0947 -0.0005 434 GLN B NE2 
3252 N N   . GLU B 171 ? 0.3800 0.3756 0.3722 -0.0353 -0.0784 0.0305  435 GLU B N   
3253 C CA  . GLU B 171 ? 0.3865 0.4035 0.4047 -0.0324 -0.0832 0.0358  435 GLU B CA  
3254 C C   . GLU B 171 ? 0.3714 0.3876 0.3810 -0.0221 -0.0794 0.0429  435 GLU B C   
3255 O O   . GLU B 171 ? 0.3592 0.3805 0.3842 -0.0181 -0.0709 0.0457  435 GLU B O   
3256 C CB  . GLU B 171 ? 0.4031 0.4346 0.4540 -0.0380 -0.0755 0.0335  435 GLU B CB  
3257 C CG  . GLU B 171 ? 0.4845 0.5178 0.5439 -0.0527 -0.0778 0.0262  435 GLU B CG  
3258 C CD  . GLU B 171 ? 0.5903 0.6448 0.6846 -0.0620 -0.0681 0.0216  435 GLU B CD  
3259 O OE1 . GLU B 171 ? 0.6719 0.7472 0.7933 -0.0699 -0.0757 0.0156  435 GLU B OE1 
3260 O OE2 . GLU B 171 ? 0.6265 0.6790 0.7220 -0.0624 -0.0526 0.0225  435 GLU B OE2 
3261 N N   . LYS B 172 ? 0.4182 0.4033 0.3688 -0.0533 -0.1068 0.0532  436 LYS B N   
3262 C CA  . LYS B 172 ? 0.4174 0.4069 0.3608 -0.0445 -0.0901 0.0508  436 LYS B CA  
3263 C C   . LYS B 172 ? 0.3876 0.3936 0.3417 -0.0428 -0.0856 0.0644  436 LYS B C   
3264 O O   . LYS B 172 ? 0.3581 0.3711 0.3216 -0.0373 -0.0726 0.0672  436 LYS B O   
3265 C CB  . LYS B 172 ? 0.4892 0.4675 0.4014 -0.0432 -0.0869 0.0377  436 LYS B CB  
3266 C CG  . LYS B 172 ? 0.5418 0.5262 0.4485 -0.0375 -0.0673 0.0332  436 LYS B CG  
3267 C CD  . LYS B 172 ? 0.5887 0.5651 0.4621 -0.0402 -0.0603 0.0194  436 LYS B CD  
3268 C CE  . LYS B 172 ? 0.6550 0.6404 0.5233 -0.0390 -0.0395 0.0165  436 LYS B CE  
3269 N NZ  . LYS B 172 ? 0.7359 0.7163 0.5731 -0.0439 -0.0279 -0.0013 436 LYS B NZ  
3270 N N   . ARG B 173 ? 0.3864 0.3972 0.3409 -0.0467 -0.0989 0.0721  437 ARG B N   
3271 C CA  . ARG B 173 ? 0.3831 0.4060 0.3490 -0.0424 -0.0981 0.0833  437 ARG B CA  
3272 C C   . ARG B 173 ? 0.3369 0.3793 0.3399 -0.0398 -0.0906 0.0888  437 ARG B C   
3273 O O   . ARG B 173 ? 0.3335 0.3829 0.3455 -0.0330 -0.0823 0.0937  437 ARG B O   
3274 C CB  . ARG B 173 ? 0.4166 0.4387 0.3778 -0.0455 -0.1190 0.0894  437 ARG B CB  
3275 C CG  . ARG B 173 ? 0.4386 0.4674 0.4106 -0.0390 -0.1240 0.1000  437 ARG B CG  
3276 C CD  . ARG B 173 ? 0.4312 0.4436 0.3717 -0.0361 -0.1123 0.1022  437 ARG B CD  
3277 N NE  . ARG B 173 ? 0.4682 0.4768 0.4108 -0.0310 -0.1242 0.1134  437 ARG B NE  
3278 C CZ  . ARG B 173 ? 0.4997 0.4906 0.4149 -0.0306 -0.1188 0.1189  437 ARG B CZ  
3279 N NH1 . ARG B 173 ? 0.4641 0.4458 0.3517 -0.0359 -0.0991 0.1129  437 ARG B NH1 
3280 N NH2 . ARG B 173 ? 0.4791 0.4611 0.3963 -0.0254 -0.1343 0.1296  437 ARG B NH2 
3281 N N   . LYS B 174 ? 0.3258 0.3751 0.3474 -0.0468 -0.0931 0.0876  438 LYS B N   
3282 C CA  . LYS B 174 ? 0.3212 0.3875 0.3708 -0.0475 -0.0820 0.0914  438 LYS B CA  
3283 C C   . LYS B 174 ? 0.3305 0.3873 0.3694 -0.0415 -0.0662 0.0891  438 LYS B C   
3284 O O   . LYS B 174 ? 0.3115 0.3792 0.3644 -0.0372 -0.0554 0.0923  438 LYS B O   
3285 C CB  . LYS B 174 ? 0.3104 0.3816 0.3745 -0.0609 -0.0852 0.0914  438 LYS B CB  
3286 C CG  . LYS B 174 ? 0.5117 0.6041 0.6024 -0.0679 -0.0974 0.0938  438 LYS B CG  
3287 C CD  . LYS B 174 ? 0.6363 0.7565 0.7590 -0.0595 -0.0929 0.0968  438 LYS B CD  
3288 C CE  . LYS B 174 ? 0.6664 0.7985 0.8059 -0.0568 -0.1138 0.0980  438 LYS B CE  
3289 N NZ  . LYS B 174 ? 0.6634 0.7693 0.7655 -0.0505 -0.1275 0.0993  438 LYS B NZ  
3290 N N   . VAL B 175 ? 0.2985 0.3359 0.3156 -0.0407 -0.0657 0.0818  439 VAL B N   
3291 C CA  . VAL B 175 ? 0.2845 0.3147 0.2966 -0.0346 -0.0538 0.0781  439 VAL B CA  
3292 C C   . VAL B 175 ? 0.2561 0.2916 0.2644 -0.0270 -0.0450 0.0799  439 VAL B C   
3293 O O   . VAL B 175 ? 0.3168 0.3560 0.3328 -0.0229 -0.0351 0.0820  439 VAL B O   
3294 C CB  . VAL B 175 ? 0.2757 0.2869 0.2732 -0.0333 -0.0574 0.0667  439 VAL B CB  
3295 C CG1 . VAL B 175 ? 0.3148 0.3221 0.3139 -0.0262 -0.0482 0.0620  439 VAL B CG1 
3296 C CG2 . VAL B 175 ? 0.3255 0.3237 0.3235 -0.0423 -0.0696 0.0666  439 VAL B CG2 
3297 N N   . GLU B 176 ? 0.2976 0.3306 0.2913 -0.0269 -0.0500 0.0801  440 GLU B N   
3298 C CA  . GLU B 176 ? 0.2677 0.3000 0.2520 -0.0231 -0.0440 0.0843  440 GLU B CA  
3299 C C   . GLU B 176 ? 0.3117 0.3546 0.3169 -0.0185 -0.0437 0.0936  440 GLU B C   
3300 O O   . GLU B 176 ? 0.3139 0.3547 0.3187 -0.0142 -0.0352 0.0959  440 GLU B O   
3301 C CB  . GLU B 176 ? 0.3148 0.3371 0.2724 -0.0272 -0.0525 0.0852  440 GLU B CB  
3302 C CG  . GLU B 176 ? 0.3794 0.3915 0.3121 -0.0312 -0.0480 0.0726  440 GLU B CG  
3303 C CD  . GLU B 176 ? 0.6197 0.6190 0.5190 -0.0380 -0.0578 0.0736  440 GLU B CD  
3304 O OE1 . GLU B 176 ? 0.6186 0.6113 0.5034 -0.0398 -0.0624 0.0844  440 GLU B OE1 
3305 O OE2 . GLU B 176 ? 0.7478 0.7399 0.6321 -0.0418 -0.0628 0.0635  440 GLU B OE2 
3306 N N   . GLN B 177 ? 0.3137 0.3690 0.3396 -0.0195 -0.0528 0.0972  441 GLN B N   
3307 C CA  . GLN B 177 ? 0.2821 0.3519 0.3347 -0.0136 -0.0521 0.1019  441 GLN B CA  
3308 C C   . GLN B 177 ? 0.2790 0.3543 0.3429 -0.0122 -0.0360 0.0991  441 GLN B C   
3309 O O   . GLN B 177 ? 0.2912 0.3679 0.3624 -0.0053 -0.0293 0.1002  441 GLN B O   
3310 C CB  . GLN B 177 ? 0.3010 0.3890 0.3801 -0.0160 -0.0647 0.1032  441 GLN B CB  
3311 C CG  . GLN B 177 ? 0.4434 0.5226 0.5087 -0.0175 -0.0849 0.1064  441 GLN B CG  
3312 C CD  . GLN B 177 ? 0.6595 0.7466 0.7458 -0.0092 -0.0995 0.1113  441 GLN B CD  
3313 O OE1 . GLN B 177 ? 0.7261 0.8101 0.8175 0.0000  -0.0954 0.1137  441 GLN B OE1 
3314 N NE2 . GLN B 177 ? 0.6100 0.7059 0.7107 -0.0118 -0.1194 0.1120  441 GLN B NE2 
3315 N N   . LEU B 178 ? 0.2837 0.3573 0.3448 -0.0192 -0.0315 0.0954  442 LEU B N   
3316 C CA  . LEU B 178 ? 0.2789 0.3523 0.3433 -0.0197 -0.0189 0.0938  442 LEU B CA  
3317 C C   . LEU B 178 ? 0.2635 0.3233 0.3131 -0.0137 -0.0126 0.0917  442 LEU B C   
3318 O O   . LEU B 178 ? 0.2888 0.3487 0.3421 -0.0100 -0.0041 0.0915  442 LEU B O   
3319 C CB  . LEU B 178 ? 0.2789 0.3454 0.3368 -0.0303 -0.0196 0.0923  442 LEU B CB  
3320 C CG  . LEU B 178 ? 0.3273 0.3859 0.3784 -0.0336 -0.0100 0.0918  442 LEU B CG  
3321 C CD1 . LEU B 178 ? 0.3899 0.4654 0.4564 -0.0325 0.0030  0.0920  442 LEU B CD1 
3322 C CD2 . LEU B 178 ? 0.4332 0.4777 0.4721 -0.0465 -0.0152 0.0928  442 LEU B CD2 
3323 N N   . GLN B 179 ? 0.2358 0.2847 0.2693 -0.0138 -0.0163 0.0884  443 GLN B N   
3324 C CA  . GLN B 179 ? 0.2779 0.3187 0.3020 -0.0101 -0.0096 0.0848  443 GLN B CA  
3325 C C   . GLN B 179 ? 0.3096 0.3515 0.3354 -0.0058 -0.0059 0.0902  443 GLN B C   
3326 O O   . GLN B 179 ? 0.2660 0.3044 0.2935 -0.0031 0.0012  0.0894  443 GLN B O   
3327 C CB  . GLN B 179 ? 0.2679 0.3027 0.2774 -0.0121 -0.0119 0.0780  443 GLN B CB  
3328 C CG  . GLN B 179 ? 0.2830 0.3154 0.2873 -0.0107 -0.0025 0.0718  443 GLN B CG  
3329 C CD  . GLN B 179 ? 0.4065 0.4375 0.3972 -0.0139 -0.0009 0.0622  443 GLN B CD  
3330 O OE1 . GLN B 179 ? 0.4893 0.5210 0.4856 -0.0119 0.0008  0.0496  443 GLN B OE1 
3331 N NE2 . GLN B 179 ? 0.4513 0.4792 0.4232 -0.0187 -0.0020 0.0670  443 GLN B NE2 
3332 N N   . TYR B 180 ? 0.2910 0.3338 0.3147 -0.0052 -0.0136 0.0959  444 TYR B N   
3333 C CA  . TYR B 180 ? 0.2901 0.3273 0.3135 -0.0005 -0.0148 0.1020  444 TYR B CA  
3334 C C   . TYR B 180 ? 0.2778 0.3229 0.3239 0.0065  -0.0101 0.1016  444 TYR B C   
3335 O O   . TYR B 180 ? 0.2738 0.3100 0.3185 0.0105  -0.0059 0.1024  444 TYR B O   
3336 C CB  . TYR B 180 ? 0.3030 0.3362 0.3203 -0.0003 -0.0298 0.1088  444 TYR B CB  
3337 C CG  . TYR B 180 ? 0.3015 0.3241 0.3208 0.0062  -0.0355 0.1156  444 TYR B CG  
3338 C CD1 . TYR B 180 ? 0.3142 0.3164 0.3086 0.0021  -0.0322 0.1197  444 TYR B CD1 
3339 C CD2 . TYR B 180 ? 0.3093 0.3423 0.3577 0.0160  -0.0440 0.1165  444 TYR B CD2 
3340 C CE1 . TYR B 180 ? 0.3330 0.3191 0.3261 0.0072  -0.0396 0.1266  444 TYR B CE1 
3341 C CE2 . TYR B 180 ? 0.3249 0.3444 0.3769 0.0243  -0.0518 0.1210  444 TYR B CE2 
3342 C CZ  . TYR B 180 ? 0.3247 0.3174 0.3462 0.0196  -0.0506 0.1270  444 TYR B CZ  
3343 O OH  . TYR B 180 ? 0.3481 0.3207 0.3692 0.0266  -0.0604 0.1324  444 TYR B OH  
3344 N N   . ASN B 181 ? 0.2825 0.3439 0.3486 0.0067  -0.0100 0.0992  445 ASN B N   
3345 C CA  . ASN B 181 ? 0.2609 0.3324 0.3470 0.0119  -0.0019 0.0957  445 ASN B CA  
3346 C C   . ASN B 181 ? 0.2996 0.3596 0.3728 0.0109  0.0091  0.0923  445 ASN B C   
3347 O O   . ASN B 181 ? 0.2720 0.3287 0.3505 0.0170  0.0142  0.0899  445 ASN B O   
3348 C CB  . ASN B 181 ? 0.2594 0.3517 0.3646 0.0069  0.0016  0.0922  445 ASN B CB  
3349 C CG  . ASN B 181 ? 0.2904 0.3986 0.4171 0.0084  -0.0104 0.0938  445 ASN B CG  
3350 O OD1 . ASN B 181 ? 0.3683 0.4713 0.4981 0.0163  -0.0226 0.0974  445 ASN B OD1 
3351 N ND2 . ASN B 181 ? 0.3509 0.4763 0.4909 -0.0006 -0.0089 0.0917  445 ASN B ND2 
3352 N N   . LEU B 182 ? 0.2597 0.3130 0.3180 0.0039  0.0105  0.0908  446 LEU B N   
3353 C CA  . LEU B 182 ? 0.2362 0.2777 0.2837 0.0029  0.0163  0.0871  446 LEU B CA  
3354 C C   . LEU B 182 ? 0.2625 0.2936 0.3035 0.0059  0.0167  0.0876  446 LEU B C   
3355 O O   . LEU B 182 ? 0.3205 0.3435 0.3595 0.0075  0.0211  0.0850  446 LEU B O   
3356 C CB  . LEU B 182 ? 0.2603 0.2956 0.2977 -0.0033 0.0126  0.0845  446 LEU B CB  
3357 C CG  . LEU B 182 ? 0.2912 0.3297 0.3285 -0.0102 0.0130  0.0854  446 LEU B CG  
3358 C CD1 . LEU B 182 ? 0.2975 0.3246 0.3242 -0.0159 0.0038  0.0841  446 LEU B CD1 
3359 C CD2 . LEU B 182 ? 0.2946 0.3291 0.3266 -0.0125 0.0214  0.0837  446 LEU B CD2 
3360 N N   . GLU B 183 ? 0.2658 0.2949 0.3001 0.0044  0.0125  0.0907  447 GLU B N   
3361 C CA  . GLU B 183 ? 0.2893 0.3073 0.3138 0.0028  0.0146  0.0924  447 GLU B CA  
3362 C C   . GLU B 183 ? 0.2655 0.2750 0.2943 0.0087  0.0132  0.0968  447 GLU B C   
3363 O O   . GLU B 183 ? 0.2939 0.2922 0.3191 0.0081  0.0166  0.0960  447 GLU B O   
3364 C CB  . GLU B 183 ? 0.3289 0.3437 0.3379 -0.0030 0.0113  0.0959  447 GLU B CB  
3365 C CG  . GLU B 183 ? 0.3360 0.3576 0.3401 -0.0083 0.0144  0.0876  447 GLU B CG  
3366 C CD  . GLU B 183 ? 0.4958 0.5139 0.4792 -0.0154 0.0134  0.0887  447 GLU B CD  
3367 O OE1 . GLU B 183 ? 0.5196 0.5276 0.4897 -0.0167 0.0064  0.0984  447 GLU B OE1 
3368 O OE2 . GLU B 183 ? 0.5194 0.5432 0.4988 -0.0194 0.0186  0.0786  447 GLU B OE2 
3369 N N   . LEU B 184 ? 0.2673 0.2824 0.3074 0.0151  0.0067  0.0998  448 LEU B N   
3370 C CA  . LEU B 184 ? 0.2728 0.2800 0.3226 0.0241  0.0029  0.1011  448 LEU B CA  
3371 C C   . LEU B 184 ? 0.2947 0.3035 0.3533 0.0281  0.0127  0.0929  448 LEU B C   
3372 O O   . LEU B 184 ? 0.3023 0.2967 0.3601 0.0326  0.0127  0.0917  448 LEU B O   
3373 C CB  . LEU B 184 ? 0.2562 0.2747 0.3253 0.0320  -0.0074 0.1027  448 LEU B CB  
3374 C CG  . LEU B 184 ? 0.2831 0.2971 0.3721 0.0455  -0.0148 0.1009  448 LEU B CG  
3375 C CD1 . LEU B 184 ? 0.3522 0.3334 0.4202 0.0454  -0.0234 0.1085  448 LEU B CD1 
3376 C CD2 . LEU B 184 ? 0.2948 0.3244 0.4086 0.0529  -0.0285 0.1013  448 LEU B CD2 
3377 N N   . ALA B 185 ? 0.3027 0.3261 0.3666 0.0254  0.0201  0.0874  449 ALA B N   
3378 C CA  . ALA B 185 ? 0.2726 0.2945 0.3357 0.0260  0.0295  0.0798  449 ALA B CA  
3379 C C   . ALA B 185 ? 0.3014 0.3053 0.3486 0.0223  0.0303  0.0788  449 ALA B C   
3380 O O   . ALA B 185 ? 0.3330 0.3259 0.3782 0.0257  0.0332  0.0742  449 ALA B O   
3381 C CB  . ALA B 185 ? 0.2734 0.3077 0.3346 0.0186  0.0352  0.0771  449 ALA B CB  
3382 N N   . PHE B 186 ? 0.2673 0.2697 0.3059 0.0152  0.0276  0.0813  450 PHE B N   
3383 C CA  . PHE B 186 ? 0.2924 0.2838 0.3235 0.0107  0.0277  0.0784  450 PHE B CA  
3384 C C   . PHE B 186 ? 0.3164 0.2943 0.3455 0.0110  0.0267  0.0815  450 PHE B C   
3385 O O   . PHE B 186 ? 0.3292 0.2943 0.3557 0.0107  0.0273  0.0780  450 PHE B O   
3386 C CB  . PHE B 186 ? 0.2852 0.2837 0.3155 0.0048  0.0255  0.0774  450 PHE B CB  
3387 C CG  . PHE B 186 ? 0.3018 0.2967 0.3338 0.0008  0.0244  0.0710  450 PHE B CG  
3388 C CD1 . PHE B 186 ? 0.3191 0.3036 0.3484 0.0014  0.0223  0.0669  450 PHE B CD1 
3389 C CD2 . PHE B 186 ? 0.3133 0.3168 0.3509 -0.0037 0.0250  0.0675  450 PHE B CD2 
3390 C CE1 . PHE B 186 ? 0.2819 0.2651 0.3178 -0.0020 0.0176  0.0601  450 PHE B CE1 
3391 C CE2 . PHE B 186 ? 0.3457 0.3522 0.3941 -0.0068 0.0235  0.0588  450 PHE B CE2 
3392 C CZ  . PHE B 186 ? 0.3172 0.3137 0.3664 -0.0054 0.0181  0.0557  450 PHE B CZ  
3393 N N   . HIS B 187 ? 0.3292 0.3058 0.3559 0.0101  0.0234  0.0888  451 HIS B N   
3394 C CA  . HIS B 187 ? 0.3151 0.2725 0.3339 0.0082  0.0198  0.0946  451 HIS B CA  
3395 C C   . HIS B 187 ? 0.3510 0.2942 0.3755 0.0182  0.0169  0.0921  451 HIS B C   
3396 O O   . HIS B 187 ? 0.3522 0.2761 0.3709 0.0158  0.0157  0.0916  451 HIS B O   
3397 C CB  . HIS B 187 ? 0.3278 0.2821 0.3375 0.0061  0.0133  0.1039  451 HIS B CB  
3398 C CG  . HIS B 187 ? 0.4374 0.3646 0.4334 0.0039  0.0053  0.1127  451 HIS B CG  
3399 N ND1 . HIS B 187 ? 0.3864 0.2981 0.3640 -0.0107 0.0084  0.1173  451 HIS B ND1 
3400 C CD2 . HIS B 187 ? 0.4453 0.3559 0.4439 0.0141  -0.0074 0.1176  451 HIS B CD2 
3401 C CE1 . HIS B 187 ? 0.4289 0.3108 0.3919 -0.0114 -0.0026 0.1270  451 HIS B CE1 
3402 N NE2 . HIS B 187 ? 0.5238 0.4036 0.5005 0.0053  -0.0140 0.1270  451 HIS B NE2 
3403 N N   . HIS B 188 ? 0.3398 0.2934 0.3780 0.0292  0.0158  0.0889  452 HIS B N   
3404 C CA  . HIS B 188 ? 0.3608 0.3059 0.4089 0.0406  0.0154  0.0819  452 HIS B CA  
3405 C C   . HIS B 188 ? 0.3215 0.2586 0.3625 0.0383  0.0226  0.0730  452 HIS B C   
3406 O O   . HIS B 188 ? 0.3697 0.2858 0.4077 0.0419  0.0197  0.0696  452 HIS B O   
3407 C CB  . HIS B 188 ? 0.3137 0.2817 0.3833 0.0505  0.0181  0.0756  452 HIS B CB  
3408 C CG  . HIS B 188 ? 0.3565 0.3203 0.4427 0.0645  0.0186  0.0649  452 HIS B CG  
3409 N ND1 . HIS B 188 ? 0.4367 0.3820 0.5317 0.0755  0.0048  0.0670  452 HIS B ND1 
3410 C CD2 . HIS B 188 ? 0.3856 0.3577 0.4781 0.0689  0.0309  0.0508  452 HIS B CD2 
3411 C CE1 . HIS B 188 ? 0.4889 0.4349 0.6018 0.0888  0.0085  0.0526  452 HIS B CE1 
3412 N NE2 . HIS B 188 ? 0.4149 0.3786 0.5257 0.0843  0.0263  0.0419  452 HIS B NE2 
3413 N N   . HIS B 189 ? 0.3090 0.2597 0.3454 0.0321  0.0297  0.0692  453 HIS B N   
3414 C CA  . HIS B 189 ? 0.3171 0.2588 0.3428 0.0293  0.0337  0.0609  453 HIS B CA  
3415 C C   . HIS B 189 ? 0.3494 0.2725 0.3674 0.0224  0.0282  0.0628  453 HIS B C   
3416 O O   . HIS B 189 ? 0.3358 0.2411 0.3472 0.0233  0.0272  0.0566  453 HIS B O   
3417 C CB  . HIS B 189 ? 0.3225 0.2767 0.3408 0.0226  0.0372  0.0594  453 HIS B CB  
3418 C CG  . HIS B 189 ? 0.3717 0.3124 0.3729 0.0184  0.0378  0.0521  453 HIS B CG  
3419 N ND1 . HIS B 189 ? 0.5086 0.4438 0.5003 0.0216  0.0456  0.0430  453 HIS B ND1 
3420 C CD2 . HIS B 189 ? 0.4701 0.4009 0.4618 0.0114  0.0305  0.0513  453 HIS B CD2 
3421 C CE1 . HIS B 189 ? 0.4346 0.3532 0.4051 0.0154  0.0423  0.0385  453 HIS B CE1 
3422 N NE2 . HIS B 189 ? 0.4879 0.4036 0.4601 0.0099  0.0314  0.0437  453 HIS B NE2 
3423 N N   . LEU B 190 ? 0.3436 0.2716 0.3627 0.0141  0.0256  0.0702  454 LEU B N   
3424 C CA  . LEU B 190 ? 0.3420 0.2580 0.3580 0.0040  0.0229  0.0708  454 LEU B CA  
3425 C C   . LEU B 190 ? 0.3920 0.2830 0.4029 0.0048  0.0186  0.0749  454 LEU B C   
3426 O O   . LEU B 190 ? 0.3865 0.2605 0.3935 -0.0014 0.0158  0.0722  454 LEU B O   
3427 C CB  . LEU B 190 ? 0.2900 0.2207 0.3098 -0.0063 0.0249  0.0751  454 LEU B CB  
3428 C CG  . LEU B 190 ? 0.3321 0.2838 0.3591 -0.0066 0.0260  0.0700  454 LEU B CG  
3429 C CD1 . LEU B 190 ? 0.3193 0.2862 0.3524 -0.0153 0.0297  0.0707  454 LEU B CD1 
3430 C CD2 . LEU B 190 ? 0.3298 0.2774 0.3590 -0.0076 0.0215  0.0616  454 LEU B CD2 
3431 N N   . CYS B 191 ? 0.3851 0.2709 0.3963 0.0122  0.0150  0.0813  455 CYS B N   
3432 C CA  . CYS B 191 ? 0.4385 0.2941 0.4435 0.0146  0.0064  0.0854  455 CYS B CA  
3433 C C   . CYS B 191 ? 0.4451 0.2865 0.4538 0.0261  0.0052  0.0737  455 CYS B C   
3434 O O   . CYS B 191 ? 0.5299 0.3431 0.5308 0.0228  -0.0007 0.0729  455 CYS B O   
3435 C CB  . CYS B 191 ? 0.5127 0.3635 0.5185 0.0220  -0.0020 0.0943  455 CYS B CB  
3436 S SG  . CYS B 191 ? 0.5608 0.4154 0.5500 0.0055  -0.0027 0.1091  455 CYS B SG  
3437 N N   . LYS B 192 ? 0.4457 0.3050 0.4645 0.0381  0.0116  0.0638  456 LYS B N   
3438 C CA  . LYS B 192 ? 0.4813 0.3287 0.5012 0.0487  0.0137  0.0495  456 LYS B CA  
3439 C C   . LYS B 192 ? 0.5441 0.3790 0.5487 0.0389  0.0152  0.0435  456 LYS B C   
3440 O O   . LYS B 192 ? 0.5694 0.3799 0.5676 0.0427  0.0119  0.0347  456 LYS B O   
3441 C CB  . LYS B 192 ? 0.4706 0.3437 0.5023 0.0590  0.0246  0.0387  456 LYS B CB  
3442 C CG  . LYS B 192 ? 0.5946 0.4774 0.6502 0.0741  0.0211  0.0376  456 LYS B CG  
3443 C CD  . LYS B 192 ? 0.7315 0.5821 0.7907 0.0831  0.0055  0.0398  456 LYS B CD  
3444 C CE  . LYS B 192 ? 0.8661 0.7254 0.9541 0.1014  -0.0023 0.0359  456 LYS B CE  
3445 N NZ  . LYS B 192 ? 0.9220 0.8028 1.0333 0.1160  0.0108  0.0136  456 LYS B NZ  
3446 N N   . THR B 193 ? 0.4320 0.3360 0.4888 0.0055  0.0183  0.0752  457 THR B N   
3447 C CA  . THR B 193 ? 0.4226 0.3161 0.4946 0.0104  0.0206  0.0608  457 THR B CA  
3448 C C   . THR B 193 ? 0.4428 0.3293 0.5396 0.0119  0.0268  0.0723  457 THR B C   
3449 O O   . THR B 193 ? 0.4612 0.3432 0.5732 0.0157  0.0280  0.0590  457 THR B O   
3450 C CB  . THR B 193 ? 0.4337 0.3167 0.4606 0.0079  0.0240  0.0466  457 THR B CB  
3451 O OG1 . THR B 193 ? 0.4480 0.3239 0.4393 0.0022  0.0305  0.0578  457 THR B OG1 
3452 C CG2 . THR B 193 ? 0.4493 0.3374 0.4549 0.0034  0.0224  0.0356  457 THR B CG2 
3453 N N   . HIS B 194 ? 0.4313 0.3188 0.5328 0.0094  0.0309  0.0968  458 HIS B N   
3454 C CA  . HIS B 194 ? 0.4277 0.3093 0.5510 0.0079  0.0419  0.1121  458 HIS B CA  
3455 C C   . HIS B 194 ? 0.4105 0.2910 0.5141 0.0063  0.0516  0.1037  458 HIS B C   
3456 O O   . HIS B 194 ? 0.4258 0.3070 0.5649 0.0068  0.0575  0.0983  458 HIS B O   
3457 C CB  . HIS B 194 ? 0.4380 0.3152 0.6247 0.0109  0.0395  0.1072  458 HIS B CB  
3458 C CG  . HIS B 194 ? 0.5454 0.4213 0.7562 0.0158  0.0290  0.1124  458 HIS B CG  
3459 N ND1 . HIS B 194 ? 0.6190 0.4903 0.8266 0.0168  0.0296  0.1407  458 HIS B ND1 
3460 C CD2 . HIS B 194 ? 0.6023 0.4820 0.8381 0.0226  0.0170  0.0918  458 HIS B CD2 
3461 C CE1 . HIS B 194 ? 0.6671 0.5387 0.9016 0.0247  0.0173  0.1373  458 HIS B CE1 
3462 N NE2 . HIS B 194 ? 0.6486 0.5267 0.9013 0.0277  0.0105  0.1067  458 HIS B NE2 
3463 N N   . ARG B 195 ? 0.4029 0.2826 0.4531 0.0046  0.0525  0.1007  459 ARG B N   
3464 C CA  . ARG B 195 ? 0.3920 0.2681 0.4190 0.0062  0.0599  0.0906  459 ARG B CA  
3465 C C   . ARG B 195 ? 0.3797 0.2568 0.3653 0.0029  0.0703  0.1050  459 ARG B C   
3466 O O   . ARG B 195 ? 0.3969 0.2683 0.3476 0.0049  0.0736  0.0942  459 ARG B O   
3467 C CB  . ARG B 195 ? 0.4078 0.2742 0.4064 0.0098  0.0511  0.0683  459 ARG B CB  
3468 C CG  . ARG B 195 ? 0.4015 0.2683 0.4346 0.0168  0.0422  0.0501  459 ARG B CG  
3469 C CD  . ARG B 195 ? 0.3940 0.2626 0.4467 0.0248  0.0444  0.0376  459 ARG B CD  
3470 N NE  . ARG B 195 ? 0.4285 0.2830 0.4318 0.0310  0.0430  0.0263  459 ARG B NE  
3471 C CZ  . ARG B 195 ? 0.4378 0.2923 0.4444 0.0416  0.0427  0.0133  459 ARG B CZ  
3472 N NH1 . ARG B 195 ? 0.4884 0.3617 0.5495 0.0448  0.0448  0.0080  459 ARG B NH1 
3473 N NH2 . ARG B 195 ? 0.4406 0.2758 0.3987 0.0493  0.0400  0.0047  459 ARG B NH2 
3474 N N   . GLN B 196 ? 0.4274 0.3101 0.4141 -0.0002 0.0748  0.1290  460 GLN B N   
3475 C CA  . GLN B 196 ? 0.4573 0.3434 0.4016 -0.0015 0.0844  0.1434  460 GLN B CA  
3476 C C   . GLN B 196 ? 0.5098 0.3996 0.4556 0.0002  0.1020  0.1411  460 GLN B C   
3477 O O   . GLN B 196 ? 0.5087 0.4005 0.4117 0.0016  0.1096  0.1404  460 GLN B O   
3478 C CB  . GLN B 196 ? 0.5236 0.4134 0.4703 -0.0019 0.0861  0.1725  460 GLN B CB  
3479 C CG  . GLN B 196 ? 0.6341 0.5253 0.5867 -0.0006 0.0675  0.1740  460 GLN B CG  
3480 C CD  . GLN B 196 ? 0.6628 0.5490 0.6730 0.0017  0.0644  0.1818  460 GLN B CD  
3481 O OE1 . GLN B 196 ? 0.5786 0.4606 0.6297 0.0008  0.0676  0.1686  460 GLN B OE1 
3482 N NE2 . GLN B 196 ? 0.7240 0.6102 0.7379 0.0063  0.0562  0.2016  460 GLN B NE2 
3483 N N   . SER B 197 ? 0.4608 0.3543 0.4598 0.0005  0.1083  0.1372  461 SER B N   
3484 C CA  . SER B 197 ? 0.4621 0.3663 0.4753 0.0019  0.1256  0.1324  461 SER B CA  
3485 C C   . SER B 197 ? 0.4785 0.3802 0.4545 0.0098  0.1229  0.1089  461 SER B C   
3486 O O   . SER B 197 ? 0.5714 0.4837 0.5400 0.0130  0.1383  0.1069  461 SER B O   
3487 C CB  . SER B 197 ? 0.4735 0.3847 0.5575 0.0006  0.1273  0.1234  461 SER B CB  
3488 O OG  . SER B 197 ? 0.5118 0.4172 0.6056 0.0074  0.1078  0.0971  461 SER B OG  
3489 N N   . ILE B 198 ? 0.4527 0.3390 0.4050 0.0133  0.1052  0.0918  462 ILE B N   
3490 C CA  . ILE B 198 ? 0.4735 0.3497 0.3932 0.0221  0.1026  0.0707  462 ILE B CA  
3491 C C   . ILE B 198 ? 0.5123 0.3864 0.3799 0.0217  0.1115  0.0751  462 ILE B C   
3492 O O   . ILE B 198 ? 0.5525 0.4218 0.3993 0.0304  0.1153  0.0601  462 ILE B O   
3493 C CB  . ILE B 198 ? 0.4924 0.3463 0.3914 0.0250  0.0844  0.0544  462 ILE B CB  
3494 C CG1 . ILE B 198 ? 0.4502 0.2925 0.3089 0.0152  0.0777  0.0612  462 ILE B CG1 
3495 C CG2 . ILE B 198 ? 0.5470 0.4050 0.4922 0.0277  0.0747  0.0473  462 ILE B CG2 
3496 C CD1 . ILE B 198 ? 0.5376 0.3581 0.3759 0.0150  0.0655  0.0471  462 ILE B CD1 
3497 N N   . LEU B 199 ? 0.5220 0.4000 0.3678 0.0139  0.1130  0.0938  463 LEU B N   
3498 C CA  . LEU B 199 ? 0.5916 0.4678 0.3825 0.0142  0.1171  0.0938  463 LEU B CA  
3499 C C   . LEU B 199 ? 0.6738 0.5646 0.4597 0.0210  0.1378  0.0942  463 LEU B C   
3500 O O   . LEU B 199 ? 0.7179 0.6031 0.4630 0.0270  0.1405  0.0800  463 LEU B O   
3501 C CB  . LEU B 199 ? 0.5956 0.4781 0.3656 0.0072  0.1119  0.1135  463 LEU B CB  
3502 C CG  . LEU B 199 ? 0.5901 0.4652 0.3597 0.0004  0.0921  0.1114  463 LEU B CG  
3503 C CD1 . LEU B 199 ? 0.6300 0.5187 0.3898 -0.0019 0.0874  0.1334  463 LEU B CD1 
3504 C CD2 . LEU B 199 ? 0.6369 0.4942 0.3695 -0.0030 0.0817  0.0886  463 LEU B CD2 
3505 N N   . ALA B 200 ? 0.6527 0.5625 0.4819 0.0197  0.1538  0.1090  464 ALA B N   
3506 C CA  . ALA B 200 ? 0.7066 0.6361 0.5364 0.0245  0.1778  0.1099  464 ALA B CA  
3507 C C   . ALA B 200 ? 0.7636 0.6913 0.6018 0.0363  0.1758  0.0797  464 ALA B C   
3508 O O   . ALA B 200 ? 0.8250 0.7590 0.6356 0.0453  0.1868  0.0679  464 ALA B O   
3509 C CB  . ALA B 200 ? 0.6954 0.6439 0.5781 0.0174  0.1971  0.1312  464 ALA B CB  
3510 N N   . LYS B 201 ? 0.7380 0.6556 0.6104 0.0387  0.1597  0.0664  465 LYS B N   
3511 C CA  . LYS B 201 ? 0.7106 0.6266 0.5991 0.0531  0.1543  0.0396  465 LYS B CA  
3512 C C   . LYS B 201 ? 0.6908 0.5760 0.5235 0.0632  0.1408  0.0208  465 LYS B C   
3513 O O   . LYS B 201 ? 0.7356 0.6161 0.5706 0.0790  0.1377  -0.0003 465 LYS B O   
3514 C CB  . LYS B 201 ? 0.6701 0.5861 0.6101 0.0537  0.1399  0.0326  465 LYS B CB  
3515 C CG  . LYS B 201 ? 0.6542 0.5958 0.6573 0.0427  0.1519  0.0476  465 LYS B CG  
3516 C CD  . LYS B 201 ? 0.6273 0.5653 0.6754 0.0426  0.1338  0.0385  465 LYS B CD  
3517 C CE  . LYS B 201 ? 0.6700 0.6301 0.7880 0.0309  0.1454  0.0495  465 LYS B CE  
3518 N NZ  . LYS B 201 ? 0.7459 0.7018 0.8545 0.0159  0.1589  0.0823  465 LYS B NZ  
3519 N N   . LEU B 202 ? 0.7986 0.6622 0.5838 0.0544  0.1326  0.0275  466 LEU B N   
3520 C CA  . LEU B 202 ? 0.8312 0.6607 0.5658 0.0599  0.1213  0.0101  466 LEU B CA  
3521 C C   . LEU B 202 ? 1.0040 0.8357 0.7176 0.0745  0.1322  -0.0065 466 LEU B C   
3522 O O   . LEU B 202 ? 1.0497 0.9135 0.7774 0.0771  0.1513  -0.0014 466 LEU B O   
3523 C CB  . LEU B 202 ? 0.7562 0.5719 0.4498 0.0454  0.1140  0.0184  466 LEU B CB  
3524 C CG  . LEU B 202 ? 0.6854 0.4924 0.3919 0.0332  0.1003  0.0274  466 LEU B CG  
3525 C CD1 . LEU B 202 ? 0.7523 0.5575 0.4264 0.0195  0.0945  0.0342  466 LEU B CD1 
3526 C CD2 . LEU B 202 ? 0.7027 0.4777 0.4052 0.0385  0.0880  0.0127  466 LEU B CD2 
3527 N N   . PRO B 203 ? 1.0680 0.8637 0.7478 0.0847  0.1214  -0.0263 467 PRO B N   
3528 C CA  . PRO B 203 ? 1.0867 0.8766 0.7403 0.1005  0.1287  -0.0460 467 PRO B CA  
3529 C C   . PRO B 203 ? 1.1043 0.8949 0.7120 0.0919  0.1353  -0.0450 467 PRO B C   
3530 O O   . PRO B 203 ? 1.1424 0.9122 0.7212 0.0770  0.1241  -0.0404 467 PRO B O   
3531 C CB  . PRO B 203 ? 1.1119 0.8515 0.7413 0.1120  0.1114  -0.0635 467 PRO B CB  
3532 C CG  . PRO B 203 ? 1.1123 0.8424 0.7644 0.1060  0.0985  -0.0532 467 PRO B CG  
3533 C CD  . PRO B 203 ? 1.0977 0.8539 0.7655 0.0839  0.1026  -0.0313 467 PRO B CD  
3534 N N   . PRO B 204 ? 1.0886 0.9062 0.6902 0.1018  0.1534  -0.0514 468 PRO B N   
3535 C CA  . PRO B 204 ? 1.1451 0.9642 0.6958 0.0983  0.1587  -0.0557 468 PRO B CA  
3536 C C   . PRO B 204 ? 1.1858 0.9630 0.7024 0.0994  0.1400  -0.0791 468 PRO B C   
3537 O O   . PRO B 204 ? 1.2039 0.9681 0.7249 0.1158  0.1386  -0.0996 468 PRO B O   
3538 C CB  . PRO B 204 ? 1.1534 1.0107 0.7117 0.1131  0.1839  -0.0617 468 PRO B CB  
3539 C CG  . PRO B 204 ? 1.0750 0.9369 0.6826 0.1290  0.1854  -0.0738 468 PRO B CG  
3540 C CD  . PRO B 204 ? 1.0381 0.8883 0.6808 0.1180  0.1697  -0.0585 468 PRO B CD  
3541 N N   . LYS B 205 ? 1.2123 0.9736 0.7077 0.0812  0.1244  -0.0756 469 LYS B N   
3542 C CA  . LYS B 205 ? 1.2942 1.0212 0.7680 0.0779  0.1087  -0.0967 469 LYS B CA  
3543 C C   . LYS B 205 ? 1.3852 1.1221 0.8494 0.0940  0.1156  -0.1188 469 LYS B C   
3544 O O   . LYS B 205 ? 1.4637 1.2362 0.9142 0.0944  0.1249  -0.1203 469 LYS B O   
3545 C CB  . LYS B 205 ? 1.2962 1.0247 0.7504 0.0573  0.0966  -0.0943 469 LYS B CB  
3546 C CG  . LYS B 205 ? 1.2525 0.9630 0.7157 0.0396  0.0862  -0.0801 469 LYS B CG  
3547 C CD  . LYS B 205 ? 1.2724 0.9830 0.7183 0.0209  0.0728  -0.0863 469 LYS B CD  
3548 C CE  . LYS B 205 ? 1.3292 0.9970 0.7611 0.0158  0.0633  -0.1100 469 LYS B CE  
3549 N NZ  . LYS B 205 ? 1.3483 0.9740 0.7889 0.0030  0.0579  -0.1049 469 LYS B NZ  
3550 N N   . GLY B 206 ? 1.3552 1.0619 0.8270 0.1082  0.1108  -0.1351 470 GLY B N   
3551 C CA  . GLY B 206 ? 1.3730 1.0878 0.8414 0.1255  0.1169  -0.1583 470 GLY B CA  
3552 C C   . GLY B 206 ? 1.3638 1.0640 0.8585 0.1466  0.1162  -0.1659 470 GLY B C   
3553 O O   . GLY B 206 ? 1.3998 1.0709 0.8912 0.1572  0.1075  -0.1841 470 GLY B O   
3554 N N   . LYS B 207 ? 1.3143 0.8926 0.7746 -0.0093 -0.0347 0.0364  471 LYS B N   
3555 C CA  . LYS B 207 ? 1.2756 0.8855 0.7743 -0.0194 -0.0073 0.0237  471 LYS B CA  
3556 C C   . LYS B 207 ? 1.1217 0.7770 0.6791 -0.0116 -0.0164 0.0094  471 LYS B C   
3557 O O   . LYS B 207 ? 1.0744 0.7612 0.6586 -0.0177 -0.0012 -0.0029 471 LYS B O   
3558 C CB  . LYS B 207 ? 1.3411 0.9346 0.8505 -0.0258 0.0091  0.0298  471 LYS B CB  
3559 C CG  . LYS B 207 ? 1.4488 0.9984 0.9054 -0.0366 0.0265  0.0443  471 LYS B CG  
3560 C CD  . LYS B 207 ? 1.4334 0.9950 0.8906 -0.0529 0.0593  0.0359  471 LYS B CD  
3561 C CE  . LYS B 207 ? 1.3384 0.9316 0.8564 -0.0588 0.0723  0.0231  471 LYS B CE  
3562 N NZ  . LYS B 207 ? 1.2988 0.9043 0.8273 -0.0744 0.1018  0.0151  471 LYS B NZ  
3563 N N   . LEU B 208 ? 1.0153 0.6721 0.5931 0.0022  -0.0411 0.0122  472 LEU B N   
3564 C CA  . LEU B 208 ? 0.9404 0.6357 0.5716 0.0104  -0.0485 0.0008  472 LEU B CA  
3565 C C   . LEU B 208 ? 0.9894 0.7003 0.6178 0.0134  -0.0623 -0.0051 472 LEU B C   
3566 O O   . LEU B 208 ? 0.9286 0.6741 0.5934 0.0142  -0.0581 -0.0161 472 LEU B O   
3567 C CB  . LEU B 208 ? 0.9117 0.6015 0.5742 0.0236  -0.0651 0.0055  472 LEU B CB  
3568 C CG  . LEU B 208 ? 0.8257 0.5473 0.5439 0.0349  -0.0746 -0.0030 472 LEU B CG  
3569 C CD1 . LEU B 208 ? 0.7800 0.5343 0.5270 0.0296  -0.0522 -0.0155 472 LEU B CD1 
3570 C CD2 . LEU B 208 ? 0.8492 0.5565 0.5944 0.0469  -0.0865 0.0030  472 LEU B CD2 
3571 N N   . ARG B 209 ? 1.0576 0.7400 0.6403 0.0151  -0.0794 0.0023  473 ARG B N   
3572 C CA  . ARG B 209 ? 1.0653 0.7567 0.6376 0.0167  -0.0935 -0.0051 473 ARG B CA  
3573 C C   . ARG B 209 ? 1.0120 0.7156 0.5679 0.0040  -0.0678 -0.0150 473 ARG B C   
3574 O O   . ARG B 209 ? 1.0093 0.7359 0.5816 0.0041  -0.0706 -0.0263 473 ARG B O   
3575 C CB  . ARG B 209 ? 1.1806 0.8323 0.6994 0.0219  -0.1211 0.0050  473 ARG B CB  
3576 C CG  . ARG B 209 ? 1.2160 0.8740 0.7282 0.0260  -0.1450 -0.0042 473 ARG B CG  
3577 C CD  . ARG B 209 ? 1.3239 0.9384 0.7788 0.0323  -0.1780 0.0063  473 ARG B CD  
3578 N NE  . ARG B 209 ? 1.4004 1.0049 0.8111 0.0294  -0.1895 -0.0033 473 ARG B NE  
3579 C CZ  . ARG B 209 ? 1.4275 1.0447 0.8620 0.0370  -0.2210 -0.0132 473 ARG B CZ  
3580 N NH1 . ARG B 209 ? 1.4112 1.0533 0.9177 0.0479  -0.2424 -0.0135 473 ARG B NH1 
3581 N NH2 . ARG B 209 ? 1.4494 1.0536 0.8381 0.0334  -0.2302 -0.0239 473 ARG B NH2 
3582 N N   . SER B 210 ? 0.8819 0.5708 0.4124 -0.0069 -0.0421 -0.0110 474 SER B N   
3583 C CA  . SER B 210 ? 0.8361 0.5386 0.3625 -0.0187 -0.0154 -0.0205 474 SER B CA  
3584 C C   . SER B 210 ? 0.8484 0.5936 0.4343 -0.0211 -0.0015 -0.0313 474 SER B C   
3585 O O   . SER B 210 ? 0.7702 0.5364 0.3687 -0.0267 0.0113  -0.0417 474 SER B O   
3586 C CB  . SER B 210 ? 0.8872 0.5597 0.3735 -0.0301 0.0087  -0.0126 474 SER B CB  
3587 O OG  . SER B 210 ? 0.8960 0.5911 0.4032 -0.0408 0.0358  -0.0231 474 SER B OG  
3588 N N   . LEU B 211 ? 0.7471 0.5018 0.3667 -0.0169 -0.0037 -0.0286 475 LEU B N   
3589 C CA  . LEU B 211 ? 0.6364 0.4265 0.3046 -0.0172 0.0048  -0.0375 475 LEU B CA  
3590 C C   . LEU B 211 ? 0.6116 0.4276 0.3093 -0.0086 -0.0090 -0.0438 475 LEU B C   
3591 O O   . LEU B 211 ? 0.6326 0.4754 0.3553 -0.0112 -0.0010 -0.0518 475 LEU B O   
3592 C CB  . LEU B 211 ? 0.6740 0.4610 0.3617 -0.0142 0.0056  -0.0341 475 LEU B CB  
3593 C CG  . LEU B 211 ? 0.5698 0.3858 0.2985 -0.0126 0.0114  -0.0422 475 LEU B CG  
3594 C CD1 . LEU B 211 ? 0.6283 0.4629 0.3664 -0.0230 0.0272  -0.0498 475 LEU B CD1 
3595 C CD2 . LEU B 211 ? 0.5222 0.3241 0.2568 -0.0103 0.0126  -0.0396 475 LEU B CD2 
3596 N N   . CYS B 212 ? 0.6417 0.4488 0.3393 0.0014  -0.0308 -0.0396 476 CYS B N   
3597 C CA  . CYS B 212 ? 0.6342 0.4644 0.3653 0.0090  -0.0445 -0.0454 476 CYS B CA  
3598 C C   . CYS B 212 ? 0.6343 0.4711 0.3533 0.0040  -0.0434 -0.0535 476 CYS B C   
3599 O O   . CYS B 212 ? 0.5896 0.4534 0.3441 0.0053  -0.0418 -0.0606 476 CYS B O   
3600 C CB  . CYS B 212 ? 0.7148 0.5317 0.4508 0.0201  -0.0706 -0.0398 476 CYS B CB  
3601 S SG  . CYS B 212 ? 0.7326 0.5437 0.4920 0.0272  -0.0692 -0.0327 476 CYS B SG  
3602 N N   . SER B 213 ? 0.6344 0.4438 0.3017 -0.0016 -0.0430 -0.0521 477 SER B N   
3603 C CA  . SER B 213 ? 0.6938 0.5035 0.3412 -0.0074 -0.0377 -0.0616 477 SER B CA  
3604 C C   . SER B 213 ? 0.6119 0.4488 0.2888 -0.0146 -0.0138 -0.0694 477 SER B C   
3605 O O   . SER B 213 ? 0.5675 0.4227 0.2651 -0.0147 -0.0137 -0.0790 477 SER B O   
3606 C CB  . SER B 213 ? 0.8171 0.5878 0.3964 -0.0136 -0.0326 -0.0577 477 SER B CB  
3607 O OG  . SER B 213 ? 0.9950 0.7361 0.5413 -0.0064 -0.0579 -0.0485 477 SER B OG  
3608 N N   . GLN B 214 ? 0.5811 0.4192 0.2616 -0.0207 0.0048  -0.0655 478 GLN B N   
3609 C CA  . GLN B 214 ? 0.5646 0.4279 0.2763 -0.0272 0.0239  -0.0721 478 GLN B CA  
3610 C C   . GLN B 214 ? 0.4903 0.3853 0.2514 -0.0204 0.0164  -0.0748 478 GLN B C   
3611 O O   . GLN B 214 ? 0.4806 0.3966 0.2673 -0.0221 0.0225  -0.0815 478 GLN B O   
3612 C CB  . GLN B 214 ? 0.5881 0.4464 0.3000 -0.0343 0.0395  -0.0677 478 GLN B CB  
3613 C CG  . GLN B 214 ? 0.7328 0.5642 0.4064 -0.0443 0.0568  -0.0654 478 GLN B CG  
3614 C CD  . GLN B 214 ? 0.7435 0.5782 0.4356 -0.0527 0.0732  -0.0642 478 GLN B CD  
3615 O OE1 . GLN B 214 ? 0.7687 0.6270 0.4954 -0.0578 0.0841  -0.0716 478 GLN B OE1 
3616 N NE2 . GLN B 214 ? 0.7680 0.5790 0.4411 -0.0537 0.0726  -0.0553 478 GLN B NE2 
3617 N N   . HIS B 215 ? 0.4870 0.3832 0.2614 -0.0125 0.0048  -0.0688 479 HIS B N   
3618 C CA  . HIS B 215 ? 0.4239 0.3455 0.2405 -0.0059 0.0013  -0.0695 479 HIS B CA  
3619 C C   . HIS B 215 ? 0.4695 0.4023 0.3042 -0.0020 -0.0087 -0.0745 479 HIS B C   
3620 O O   . HIS B 215 ? 0.4168 0.3716 0.2830 -0.0015 -0.0039 -0.0773 479 HIS B O   
3621 C CB  . HIS B 215 ? 0.4068 0.3231 0.2324 0.0022  -0.0063 -0.0632 479 HIS B CB  
3622 C CG  . HIS B 215 ? 0.4025 0.3381 0.2674 0.0107  -0.0117 -0.0633 479 HIS B CG  
3623 N ND1 . HIS B 215 ? 0.4361 0.3917 0.3260 0.0114  -0.0008 -0.0638 479 HIS B ND1 
3624 C CD2 . HIS B 215 ? 0.4047 0.3413 0.2899 0.0188  -0.0265 -0.0625 479 HIS B CD2 
3625 C CE1 . HIS B 215 ? 0.4184 0.3858 0.3408 0.0190  -0.0046 -0.0625 479 HIS B CE1 
3626 N NE2 . HIS B 215 ? 0.3984 0.3564 0.3233 0.0234  -0.0205 -0.0625 479 HIS B NE2 
3627 N N   . VAL B 216 ? 0.4279 0.3435 0.2414 0.0004  -0.0240 -0.0756 480 VAL B N   
3628 C CA  . VAL B 216 ? 0.4582 0.3840 0.2937 0.0042  -0.0366 -0.0821 480 VAL B CA  
3629 C C   . VAL B 216 ? 0.4933 0.4279 0.3297 -0.0026 -0.0248 -0.0913 480 VAL B C   
3630 O O   . VAL B 216 ? 0.4407 0.3947 0.3146 -0.0005 -0.0263 -0.0958 480 VAL B O   
3631 C CB  . VAL B 216 ? 0.5123 0.4163 0.3239 0.0084  -0.0604 -0.0831 480 VAL B CB  
3632 C CG1 . VAL B 216 ? 0.5962 0.5092 0.4271 0.0094  -0.0718 -0.0936 480 VAL B CG1 
3633 C CG2 . VAL B 216 ? 0.5170 0.4195 0.3502 0.0177  -0.0752 -0.0750 480 VAL B CG2 
3634 N N   . GLU B 217 ? 0.5011 0.4209 0.3006 -0.0105 -0.0113 -0.0939 481 GLU B N   
3635 C CA  . GLU B 217 ? 0.5580 0.4859 0.3628 -0.0167 0.0031  -0.1037 481 GLU B CA  
3636 C C   . GLU B 217 ? 0.4453 0.4019 0.2966 -0.0171 0.0145  -0.1019 481 GLU B C   
3637 O O   . GLU B 217 ? 0.4320 0.4045 0.3134 -0.0167 0.0166  -0.1079 481 GLU B O   
3638 C CB  . GLU B 217 ? 0.7258 0.6324 0.4870 -0.0256 0.0205  -0.1062 481 GLU B CB  
3639 C CG  . GLU B 217 ? 0.9676 0.8393 0.6693 -0.0264 0.0127  -0.1076 481 GLU B CG  
3640 C CD  . GLU B 217 ? 1.1186 0.9676 0.7773 -0.0361 0.0368  -0.1079 481 GLU B CD  
3641 O OE1 . GLU B 217 ? 1.1150 0.9693 0.7856 -0.0410 0.0527  -0.1015 481 GLU B OE1 
3642 O OE2 . GLU B 217 ? 1.1918 1.0162 0.8046 -0.0391 0.0406  -0.1151 481 GLU B OE2 
3643 N N   . ARG B 218 ? 0.4045 0.3651 0.2597 -0.0178 0.0205  -0.0939 482 ARG B N   
3644 C CA  . ARG B 218 ? 0.3987 0.3820 0.2887 -0.0183 0.0285  -0.0921 482 ARG B CA  
3645 C C   . ARG B 218 ? 0.3729 0.3734 0.2976 -0.0107 0.0204  -0.0883 482 ARG B C   
3646 O O   . ARG B 218 ? 0.3076 0.3250 0.2619 -0.0103 0.0245  -0.0883 482 ARG B O   
3647 C CB  . ARG B 218 ? 0.4111 0.3922 0.2942 -0.0211 0.0344  -0.0865 482 ARG B CB  
3648 C CG  . ARG B 218 ? 0.4798 0.4815 0.3935 -0.0222 0.0393  -0.0858 482 ARG B CG  
3649 C CD  . ARG B 218 ? 0.6060 0.6157 0.5357 -0.0280 0.0488  -0.0935 482 ARG B CD  
3650 N NE  . ARG B 218 ? 0.6361 0.6650 0.5986 -0.0277 0.0490  -0.0916 482 ARG B NE  
3651 C CZ  . ARG B 218 ? 0.5807 0.6201 0.5684 -0.0321 0.0562  -0.0972 482 ARG B CZ  
3652 N NH1 . ARG B 218 ? 0.4924 0.5244 0.4743 -0.0375 0.0682  -0.1062 482 ARG B NH1 
3653 N NH2 . ARG B 218 ? 0.4332 0.4886 0.4506 -0.0305 0.0514  -0.0937 482 ARG B NH2 
3654 N N   . LEU B 219 ? 0.3307 0.3256 0.2542 -0.0044 0.0096  -0.0842 483 LEU B N   
3655 C CA  . LEU B 219 ? 0.3047 0.3140 0.2637 0.0025  0.0052  -0.0803 483 LEU B CA  
3656 C C   . LEU B 219 ? 0.2975 0.3164 0.2827 0.0022  0.0022  -0.0868 483 LEU B C   
3657 O O   . LEU B 219 ? 0.3160 0.3504 0.3351 0.0045  0.0064  -0.0831 483 LEU B O   
3658 C CB  . LEU B 219 ? 0.3308 0.3315 0.2897 0.0090  -0.0060 -0.0769 483 LEU B CB  
3659 C CG  . LEU B 219 ? 0.3445 0.3594 0.3466 0.0159  -0.0080 -0.0732 483 LEU B CG  
3660 C CD1 . LEU B 219 ? 0.3347 0.3591 0.3456 0.0174  0.0070  -0.0655 483 LEU B CD1 
3661 C CD2 . LEU B 219 ? 0.4033 0.4099 0.4132 0.0225  -0.0215 -0.0721 483 LEU B CD2 
3662 N N   . GLN B 220 ? 0.3181 0.3254 0.2858 -0.0005 -0.0047 -0.0964 484 GLN B N   
3663 C CA  . GLN B 220 ? 0.3173 0.3313 0.3102 -0.0006 -0.0087 -0.1052 484 GLN B CA  
3664 C C   . GLN B 220 ? 0.3007 0.3263 0.3103 -0.0047 0.0057  -0.1078 484 GLN B C   
3665 O O   . GLN B 220 ? 0.3129 0.3500 0.3592 -0.0032 0.0054  -0.1100 484 GLN B O   
3666 C CB  . GLN B 220 ? 0.4963 0.4911 0.4601 -0.0022 -0.0216 -0.1170 484 GLN B CB  
3667 C CG  . GLN B 220 ? 0.6319 0.6064 0.5441 -0.0084 -0.0138 -0.1228 484 GLN B CG  
3668 C CD  . GLN B 220 ? 0.7614 0.7132 0.6390 -0.0091 -0.0280 -0.1349 484 GLN B CD  
3669 O OE1 . GLN B 220 ? 0.7786 0.7297 0.6713 -0.0043 -0.0491 -0.1382 484 GLN B OE1 
3670 N NE2 . GLN B 220 ? 0.8370 0.7689 0.6679 -0.0153 -0.0164 -0.1420 484 GLN B NE2 
3671 N N   . ILE B 221 ? 0.3044 0.3269 0.2927 -0.0096 0.0172  -0.1070 485 ILE B N   
3672 C CA  . ILE B 221 ? 0.2901 0.3255 0.3015 -0.0127 0.0293  -0.1085 485 ILE B CA  
3673 C C   . ILE B 221 ? 0.2673 0.3194 0.3107 -0.0082 0.0289  -0.0963 485 ILE B C   
3674 O O   . ILE B 221 ? 0.2522 0.3155 0.3293 -0.0068 0.0306  -0.0959 485 ILE B O   
3675 C CB  . ILE B 221 ? 0.3012 0.3304 0.2899 -0.0193 0.0409  -0.1107 485 ILE B CB  
3676 C CG1 . ILE B 221 ? 0.3815 0.3920 0.3384 -0.0243 0.0466  -0.1231 485 ILE B CG1 
3677 C CG2 . ILE B 221 ? 0.3002 0.3464 0.3242 -0.0213 0.0498  -0.1104 485 ILE B CG2 
3678 C CD1 . ILE B 221 ? 0.3801 0.3806 0.3125 -0.0320 0.0624  -0.1243 485 ILE B CD1 
3679 N N   . PHE B 222 ? 0.2615 0.3125 0.2924 -0.0056 0.0269  -0.0864 486 PHE B N   
3680 C CA  . PHE B 222 ? 0.2472 0.3091 0.2984 -0.0010 0.0280  -0.0746 486 PHE B CA  
3681 C C   . PHE B 222 ? 0.2386 0.3073 0.3223 0.0038  0.0260  -0.0710 486 PHE B C   
3682 O O   . PHE B 222 ? 0.2367 0.3141 0.3452 0.0058  0.0292  -0.0636 486 PHE B O   
3683 C CB  . PHE B 222 ? 0.2592 0.3152 0.2875 0.0014  0.0281  -0.0669 486 PHE B CB  
3684 C CG  . PHE B 222 ? 0.2613 0.3127 0.2662 -0.0034 0.0302  -0.0683 486 PHE B CG  
3685 C CD1 . PHE B 222 ? 0.2645 0.3241 0.2810 -0.0067 0.0315  -0.0686 486 PHE B CD1 
3686 C CD2 . PHE B 222 ? 0.2713 0.3098 0.2479 -0.0046 0.0297  -0.0694 486 PHE B CD2 
3687 C CE1 . PHE B 222 ? 0.2842 0.3405 0.2862 -0.0119 0.0320  -0.0710 486 PHE B CE1 
3688 C CE2 . PHE B 222 ? 0.2790 0.3124 0.2388 -0.0097 0.0317  -0.0711 486 PHE B CE2 
3689 C CZ  . PHE B 222 ? 0.2788 0.3217 0.2524 -0.0139 0.0327  -0.0725 486 PHE B CZ  
3690 N N   . GLN B 223 ? 0.2437 0.3072 0.3296 0.0058  0.0195  -0.0752 487 GLN B N   
3691 C CA  . GLN B 223 ? 0.2366 0.3067 0.3609 0.0092  0.0172  -0.0737 487 GLN B CA  
3692 C C   . GLN B 223 ? 0.2634 0.3385 0.4147 0.0069  0.0170  -0.0810 487 GLN B C   
3693 O O   . GLN B 223 ? 0.2857 0.3679 0.4748 0.0092  0.0190  -0.0759 487 GLN B O   
3694 C CB  . GLN B 223 ? 0.2458 0.3093 0.3700 0.0114  0.0060  -0.0792 487 GLN B CB  
3695 C CG  . GLN B 223 ? 0.3406 0.4037 0.4641 0.0164  0.0091  -0.0693 487 GLN B CG  
3696 C CD  . GLN B 223 ? 0.4604 0.5342 0.6256 0.0203  0.0190  -0.0590 487 GLN B CD  
3697 O OE1 . GLN B 223 ? 0.5864 0.6618 0.7450 0.0220  0.0319  -0.0478 487 GLN B OE1 
3698 N NE2 . GLN B 223 ? 0.5869 0.6660 0.7943 0.0212  0.0128  -0.0631 487 GLN B NE2 
3699 N N   . HIS B 224 ? 0.2420 0.3118 0.3754 0.0023  0.0168  -0.0929 488 HIS B N   
3700 C CA  . HIS B 224 ? 0.2421 0.3156 0.4019 0.0003  0.0192  -0.1018 488 HIS B CA  
3701 C C   . HIS B 224 ? 0.2658 0.3502 0.4493 0.0015  0.0273  -0.0911 488 HIS B C   
3702 O O   . HIS B 224 ? 0.2315 0.3219 0.4535 0.0034  0.0286  -0.0885 488 HIS B O   
3703 C CB  . HIS B 224 ? 0.2699 0.3322 0.4003 -0.0049 0.0209  -0.1181 488 HIS B CB  
3704 C CG  . HIS B 224 ? 0.2627 0.3268 0.4184 -0.0068 0.0262  -0.1303 488 HIS B CG  
3705 N ND1 . HIS B 224 ? 0.3140 0.3755 0.4938 -0.0060 0.0192  -0.1406 488 HIS B ND1 
3706 C CD2 . HIS B 224 ? 0.2824 0.3506 0.4488 -0.0094 0.0379  -0.1349 488 HIS B CD2 
3707 C CE1 . HIS B 224 ? 0.3607 0.4229 0.5609 -0.0078 0.0274  -0.1517 488 HIS B CE1 
3708 N NE2 . HIS B 224 ? 0.3719 0.4390 0.5665 -0.0095 0.0394  -0.1479 488 HIS B NE2 
3709 N N   . LEU B 225 ? 0.2255 0.3109 0.3866 0.0005  0.0308  -0.0844 489 LEU B N   
3710 C CA  . LEU B 225 ? 0.2183 0.3123 0.3987 0.0017  0.0336  -0.0754 489 LEU B CA  
3711 C C   . LEU B 225 ? 0.2493 0.3460 0.4422 0.0072  0.0329  -0.0575 489 LEU B C   
3712 O O   . LEU B 225 ? 0.3050 0.4063 0.5269 0.0097  0.0333  -0.0496 489 LEU B O   
3713 C CB  . LEU B 225 ? 0.2262 0.3200 0.3821 -0.0016 0.0348  -0.0757 489 LEU B CB  
3714 C CG  . LEU B 225 ? 0.2304 0.3195 0.3751 -0.0078 0.0408  -0.0920 489 LEU B CG  
3715 C CD1 . LEU B 225 ? 0.3013 0.3897 0.4249 -0.0116 0.0423  -0.0900 489 LEU B CD1 
3716 C CD2 . LEU B 225 ? 0.2740 0.3696 0.4559 -0.0087 0.0462  -0.1008 489 LEU B CD2 
3717 N N   . HIS B 226 ? 0.2180 0.3101 0.3905 0.0094  0.0334  -0.0510 490 HIS B N   
3718 C CA  . HIS B 226 ? 0.2650 0.3566 0.4435 0.0143  0.0379  -0.0340 490 HIS B CA  
3719 C C   . HIS B 226 ? 0.2996 0.3885 0.4813 0.0164  0.0409  -0.0336 490 HIS B C   
3720 O O   . HIS B 226 ? 0.2758 0.3596 0.4310 0.0179  0.0432  -0.0310 490 HIS B O   
3721 C CB  . HIS B 226 ? 0.3033 0.3910 0.4486 0.0157  0.0378  -0.0239 490 HIS B CB  
3722 C CG  . HIS B 226 ? 0.4369 0.5288 0.5883 0.0144  0.0316  -0.0228 490 HIS B CG  
3723 N ND1 . HIS B 226 ? 0.5525 0.6468 0.7315 0.0175  0.0303  -0.0122 490 HIS B ND1 
3724 C CD2 . HIS B 226 ? 0.3873 0.4815 0.5275 0.0105  0.0261  -0.0312 490 HIS B CD2 
3725 C CE1 . HIS B 226 ? 0.4664 0.5653 0.6522 0.0164  0.0222  -0.0143 490 HIS B CE1 
3726 N NE2 . HIS B 226 ? 0.4212 0.5211 0.5857 0.0117  0.0204  -0.0263 490 HIS B NE2 
3727 N N   . PRO B 227 ? 0.2962 0.3883 0.5157 0.0166  0.0404  -0.0373 491 PRO B N   
3728 C CA  . PRO B 227 ? 0.3062 0.3978 0.5397 0.0186  0.0412  -0.0379 491 PRO B CA  
3729 C C   . PRO B 227 ? 0.3199 0.4092 0.5491 0.0230  0.0552  -0.0208 491 PRO B C   
3730 O O   . PRO B 227 ? 0.3912 0.4792 0.6256 0.0245  0.0641  -0.0068 491 PRO B O   
3731 C CB  . PRO B 227 ? 0.3449 0.4410 0.6284 0.0175  0.0380  -0.0437 491 PRO B CB  
3732 C CG  . PRO B 227 ? 0.2535 0.3505 0.5414 0.0148  0.0349  -0.0499 491 PRO B CG  
3733 C CD  . PRO B 227 ? 0.2941 0.3903 0.5506 0.0152  0.0387  -0.0415 491 PRO B CD  
3734 N N   . ILE B 228 ? 0.2855 0.3717 0.5018 0.0252  0.0576  -0.0217 492 ILE B N   
3735 C CA  . ILE B 228 ? 0.2790 0.3603 0.4854 0.0295  0.0746  -0.0077 492 ILE B CA  
3736 C C   . ILE B 228 ? 0.3727 0.4578 0.6284 0.0317  0.0881  0.0004  492 ILE B C   
3737 O O   . ILE B 228 ? 0.4257 0.5182 0.7251 0.0302  0.0799  -0.0081 492 ILE B O   
3738 C CB  . ILE B 228 ? 0.3991 0.4745 0.5746 0.0314  0.0742  -0.0127 492 ILE B CB  
3739 C CG1 . ILE B 228 ? 0.3689 0.4390 0.4973 0.0284  0.0647  -0.0180 492 ILE B CG1 
3740 C CG2 . ILE B 228 ? 0.4479 0.5168 0.6172 0.0362  0.0948  -0.0014 492 ILE B CG2 
3741 C CD1 . ILE B 228 ? 0.4671 0.5298 0.5601 0.0295  0.0722  -0.0079 492 ILE B CD1 
# 
