data_9BPX
# 
_entry.id   9BPX 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.402 
_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   9BPX         pdb_00009bpx 10.2210/pdb9bpx/pdb 
WWPDB D_1000283926 ?            ?                   
# 
_pdbx_audit_revision_history.ordinal             1 
_pdbx_audit_revision_history.data_content_type   'Structure model' 
_pdbx_audit_revision_history.major_revision      1 
_pdbx_audit_revision_history.minor_revision      0 
_pdbx_audit_revision_history.revision_date       2025-02-12 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        9BPX 
_pdbx_database_status.recvd_initial_deposition_date   2024-05-08 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           N 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              sfanning@luc.edu 
_pdbx_contact_author.name_first         Sean 
_pdbx_contact_author.name_last          Fanning 
_pdbx_contact_author.name_mi            W 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-9428-0060 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Young, K.Y.'   1 ? 
'Fanning, S.W.' 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                   ? 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'Breast Cancer Res' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            ? 
_citation.journal_id_ISSN           1465-542X 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            27 
_citation.language                  ? 
_citation.page_first                10 
_citation.page_last                 10 
_citation.title                     
'Targeting unique ligand binding domain structural features downregulates DKK1 in Y537S ESR1 mutant breast cancer cells.' 
_citation.year                      2025 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1186/s13058-024-01945-z 
_citation.pdbx_database_id_PubMed   39825366 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Young, K.S.'    1  ? 
primary 'Hancock, G.R.'  2  ? 
primary 'Fink, E.C.'     3  ? 
primary 'Zigrossi, A.'   4  ? 
primary 'Flowers, B.'    5  ? 
primary 'Cooper, D.A.'   6  ? 
primary 'Nguyen, V.T.'   7  ? 
primary 'Martinez, M.C.' 8  ? 
primary 'Mon, K.S.'      9  ? 
primary 'Bosland, M.'    10 ? 
primary 'Zak, D.R.'      11 ? 
primary 'Runde, A.P.'    12 ? 
primary 'Sharifi, M.N.'  13 ? 
primary 'Kastrati, I.'   14 ? 
primary 'Minh, D.D.L.'   15 ? 
primary 'Kregel, S.'     16 ? 
primary 'Fanning, S.W.'  17 ? 
# 
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 'Estrogen receptor' 30015.990 2   ? ? ? ? 
2 non-polymer syn HISTIDINE 156.162   1   ? ? ? ? 
3 non-polymer syn 
;[(1'R)-1'-(4-{[(3R)-1-(3-fluoropropyl)pyrrolidin-3-yl]methoxy}phenyl)-6'-hydroxy-1',4'-dihydro-2'H-spiro[cyclopropane-1,3'-isoquinolin]-2'-yl](phenyl)methanone
;
514.630   1   ? ? ? ? 
4 non-polymer syn 
;[(1'R)-1'-(4-{[(3S)-1-(3-fluoropropyl)-2,3-dihydro-1H-pyrrol-3-yl]methoxy}phenyl)-6'-hydroxy-1',4'-dihydro-2'H-spiro[cyclopropane-1,3'-isoquinolin]-2'-yl](phenyl)methanone
;
512.614   1   ? ? ? ? 
5 water       nat water 18.015    186 ? ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'ER,ER-alpha,Estradiol receptor,Nuclear receptor subfamily 3 group A member 1' 
# 
_entity_poly.entity_id                      1 
_entity_poly.type                           'polypeptide(L)' 
_entity_poly.nstd_linkage                   no 
_entity_poly.nstd_monomer                   no 
_entity_poly.pdbx_seq_one_letter_code       
;HHHHHHENLYFQSLALSLTADQMVSALLDAEPPILYSEYDPTRPFSEASMMGLLTNLADRELVHMINWAKRVPGFVDLTL
HDQVHLLESAWLEILMIGLVWRSMEHPGKLLFAPNLLLDRNQGKSVEGMVEIFDMLLATSSRFRMMNLQGEEFVCLKSII
LLNSGVYTFLSSTLKSLEEKDHIHRVLDKITDTLIHLMAKAGLTLQQQHQRLAQLLLILSHIRHMSNKGMEHLYSMKSKN
VVPLSDLLLEMLDAHRLHAPTS
;
_entity_poly.pdbx_seq_one_letter_code_can   
;HHHHHHENLYFQSLALSLTADQMVSALLDAEPPILYSEYDPTRPFSEASMMGLLTNLADRELVHMINWAKRVPGFVDLTL
HDQVHLLESAWLEILMIGLVWRSMEHPGKLLFAPNLLLDRNQGKSVEGMVEIFDMLLATSSRFRMMNLQGEEFVCLKSII
LLNSGVYTFLSSTLKSLEEKDHIHRVLDKITDTLIHLMAKAGLTLQQQHQRLAQLLLILSHIRHMSNKGMEHLYSMKSKN
VVPLSDLLLEMLDAHRLHAPTS
;
_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 HISTIDINE HIS   
3 
;[(1'R)-1'-(4-{[(3R)-1-(3-fluoropropyl)pyrrolidin-3-yl]methoxy}phenyl)-6'-hydroxy-1',4'-dihydro-2'H-spiro[cyclopropane-1,3'-isoquinolin]-2'-yl](phenyl)methanone
;
TZI   
4 
;[(1'R)-1'-(4-{[(3S)-1-(3-fluoropropyl)-2,3-dihydro-1H-pyrrol-3-yl]methoxy}phenyl)-6'-hydroxy-1',4'-dihydro-2'H-spiro[cyclopropane-1,3'-isoquinolin]-2'-yl](phenyl)methanone
;
A1BV9 
5 water HOH   
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   HIS n 
1 2   HIS n 
1 3   HIS n 
1 4   HIS n 
1 5   HIS n 
1 6   HIS n 
1 7   GLU n 
1 8   ASN n 
1 9   LEU n 
1 10  TYR n 
1 11  PHE n 
1 12  GLN n 
1 13  SER n 
1 14  LEU n 
1 15  ALA n 
1 16  LEU n 
1 17  SER n 
1 18  LEU n 
1 19  THR n 
1 20  ALA n 
1 21  ASP n 
1 22  GLN n 
1 23  MET n 
1 24  VAL n 
1 25  SER n 
1 26  ALA n 
1 27  LEU n 
1 28  LEU n 
1 29  ASP n 
1 30  ALA n 
1 31  GLU n 
1 32  PRO n 
1 33  PRO n 
1 34  ILE n 
1 35  LEU n 
1 36  TYR n 
1 37  SER n 
1 38  GLU n 
1 39  TYR n 
1 40  ASP n 
1 41  PRO n 
1 42  THR n 
1 43  ARG n 
1 44  PRO n 
1 45  PHE n 
1 46  SER n 
1 47  GLU n 
1 48  ALA n 
1 49  SER n 
1 50  MET n 
1 51  MET n 
1 52  GLY n 
1 53  LEU n 
1 54  LEU n 
1 55  THR n 
1 56  ASN n 
1 57  LEU n 
1 58  ALA n 
1 59  ASP n 
1 60  ARG n 
1 61  GLU n 
1 62  LEU n 
1 63  VAL n 
1 64  HIS n 
1 65  MET n 
1 66  ILE n 
1 67  ASN n 
1 68  TRP n 
1 69  ALA n 
1 70  LYS n 
1 71  ARG n 
1 72  VAL n 
1 73  PRO n 
1 74  GLY n 
1 75  PHE n 
1 76  VAL n 
1 77  ASP n 
1 78  LEU n 
1 79  THR n 
1 80  LEU n 
1 81  HIS n 
1 82  ASP n 
1 83  GLN n 
1 84  VAL n 
1 85  HIS n 
1 86  LEU n 
1 87  LEU n 
1 88  GLU n 
1 89  SER n 
1 90  ALA n 
1 91  TRP n 
1 92  LEU n 
1 93  GLU n 
1 94  ILE n 
1 95  LEU n 
1 96  MET n 
1 97  ILE n 
1 98  GLY n 
1 99  LEU n 
1 100 VAL n 
1 101 TRP n 
1 102 ARG n 
1 103 SER n 
1 104 MET n 
1 105 GLU n 
1 106 HIS n 
1 107 PRO n 
1 108 GLY n 
1 109 LYS n 
1 110 LEU n 
1 111 LEU n 
1 112 PHE n 
1 113 ALA n 
1 114 PRO n 
1 115 ASN n 
1 116 LEU n 
1 117 LEU n 
1 118 LEU n 
1 119 ASP n 
1 120 ARG n 
1 121 ASN n 
1 122 GLN n 
1 123 GLY n 
1 124 LYS n 
1 125 SER n 
1 126 VAL n 
1 127 GLU n 
1 128 GLY n 
1 129 MET n 
1 130 VAL n 
1 131 GLU n 
1 132 ILE n 
1 133 PHE n 
1 134 ASP n 
1 135 MET n 
1 136 LEU n 
1 137 LEU n 
1 138 ALA n 
1 139 THR n 
1 140 SER n 
1 141 SER n 
1 142 ARG n 
1 143 PHE n 
1 144 ARG n 
1 145 MET n 
1 146 MET n 
1 147 ASN n 
1 148 LEU n 
1 149 GLN n 
1 150 GLY n 
1 151 GLU n 
1 152 GLU n 
1 153 PHE n 
1 154 VAL n 
1 155 CYS n 
1 156 LEU n 
1 157 LYS n 
1 158 SER n 
1 159 ILE n 
1 160 ILE n 
1 161 LEU n 
1 162 LEU n 
1 163 ASN n 
1 164 SER n 
1 165 GLY n 
1 166 VAL n 
1 167 TYR n 
1 168 THR n 
1 169 PHE n 
1 170 LEU n 
1 171 SER n 
1 172 SER n 
1 173 THR n 
1 174 LEU n 
1 175 LYS n 
1 176 SER n 
1 177 LEU n 
1 178 GLU n 
1 179 GLU n 
1 180 LYS n 
1 181 ASP n 
1 182 HIS n 
1 183 ILE n 
1 184 HIS n 
1 185 ARG n 
1 186 VAL n 
1 187 LEU n 
1 188 ASP n 
1 189 LYS n 
1 190 ILE n 
1 191 THR n 
1 192 ASP n 
1 193 THR n 
1 194 LEU n 
1 195 ILE n 
1 196 HIS n 
1 197 LEU n 
1 198 MET n 
1 199 ALA n 
1 200 LYS n 
1 201 ALA n 
1 202 GLY n 
1 203 LEU n 
1 204 THR n 
1 205 LEU n 
1 206 GLN n 
1 207 GLN n 
1 208 GLN n 
1 209 HIS n 
1 210 GLN n 
1 211 ARG n 
1 212 LEU n 
1 213 ALA n 
1 214 GLN n 
1 215 LEU n 
1 216 LEU n 
1 217 LEU n 
1 218 ILE n 
1 219 LEU n 
1 220 SER n 
1 221 HIS n 
1 222 ILE n 
1 223 ARG n 
1 224 HIS n 
1 225 MET n 
1 226 SER n 
1 227 ASN n 
1 228 LYS n 
1 229 GLY n 
1 230 MET n 
1 231 GLU n 
1 232 HIS n 
1 233 LEU n 
1 234 TYR n 
1 235 SER n 
1 236 MET n 
1 237 LYS n 
1 238 SER n 
1 239 LYS n 
1 240 ASN n 
1 241 VAL n 
1 242 VAL n 
1 243 PRO n 
1 244 LEU n 
1 245 SER n 
1 246 ASP n 
1 247 LEU n 
1 248 LEU n 
1 249 LEU n 
1 250 GLU n 
1 251 MET n 
1 252 LEU n 
1 253 ASP n 
1 254 ALA n 
1 255 HIS n 
1 256 ARG n 
1 257 LEU n 
1 258 HIS n 
1 259 ALA n 
1 260 PRO n 
1 261 THR n 
1 262 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                   262 
_entity_src_gen.gene_src_common_name               human 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 'ESR1, ESR, NR3A1' 
_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 
A1BV9 non-polymer         . 
;[(1'R)-1'-(4-{[(3S)-1-(3-fluoropropyl)-2,3-dihydro-1H-pyrrol-3-yl]methoxy}phenyl)-6'-hydroxy-1',4'-dihydro-2'H-spiro[cyclopropane-1,3'-isoquinolin]-2'-yl](phenyl)methanone
;
? 'C32 H33 F N2 O3' 512.614 
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 
TZI   non-polymer         . 
;[(1'R)-1'-(4-{[(3R)-1-(3-fluoropropyl)pyrrolidin-3-yl]methoxy}phenyl)-6'-hydroxy-1',4'-dihydro-2'H-spiro[cyclopropane-1,3'-isoquinolin]-2'-yl](phenyl)methanone
;
? 'C32 H35 F N2 O3' 514.630 
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   HIS 1   293 ?   ?   ?   A . n 
A 1 2   HIS 2   294 ?   ?   ?   A . n 
A 1 3   HIS 3   295 ?   ?   ?   A . n 
A 1 4   HIS 4   296 ?   ?   ?   A . n 
A 1 5   HIS 5   297 ?   ?   ?   A . n 
A 1 6   HIS 6   298 ?   ?   ?   A . n 
A 1 7   GLU 7   299 ?   ?   ?   A . n 
A 1 8   ASN 8   300 ?   ?   ?   A . n 
A 1 9   LEU 9   301 ?   ?   ?   A . n 
A 1 10  TYR 10  302 ?   ?   ?   A . n 
A 1 11  PHE 11  303 ?   ?   ?   A . n 
A 1 12  GLN 12  304 ?   ?   ?   A . n 
A 1 13  SER 13  305 ?   ?   ?   A . n 
A 1 14  LEU 14  306 306 LEU LEU A . n 
A 1 15  ALA 15  307 307 ALA ALA A . n 
A 1 16  LEU 16  308 308 LEU LEU A . n 
A 1 17  SER 17  309 309 SER SER A . n 
A 1 18  LEU 18  310 310 LEU LEU A . n 
A 1 19  THR 19  311 311 THR THR A . n 
A 1 20  ALA 20  312 312 ALA ALA A . n 
A 1 21  ASP 21  313 313 ASP ASP A . n 
A 1 22  GLN 22  314 314 GLN GLN A . n 
A 1 23  MET 23  315 315 MET MET A . n 
A 1 24  VAL 24  316 316 VAL VAL A . n 
A 1 25  SER 25  317 317 SER SER A . n 
A 1 26  ALA 26  318 318 ALA ALA A . n 
A 1 27  LEU 27  319 319 LEU LEU A . n 
A 1 28  LEU 28  320 320 LEU LEU A . n 
A 1 29  ASP 29  321 321 ASP ASP A . n 
A 1 30  ALA 30  322 322 ALA ALA A . n 
A 1 31  GLU 31  323 323 GLU GLU A . n 
A 1 32  PRO 32  324 324 PRO PRO A . n 
A 1 33  PRO 33  325 325 PRO PRO A . n 
A 1 34  ILE 34  326 326 ILE ILE A . n 
A 1 35  LEU 35  327 327 LEU LEU A . n 
A 1 36  TYR 36  328 328 TYR TYR A . n 
A 1 37  SER 37  329 329 SER SER A . n 
A 1 38  GLU 38  330 330 GLU GLU A . n 
A 1 39  TYR 39  331 331 TYR TYR A . n 
A 1 40  ASP 40  332 332 ASP ASP A . n 
A 1 41  PRO 41  333 333 PRO PRO A . n 
A 1 42  THR 42  334 334 THR THR A . n 
A 1 43  ARG 43  335 335 ARG ARG A . n 
A 1 44  PRO 44  336 336 PRO PRO A . n 
A 1 45  PHE 45  337 337 PHE PHE A . n 
A 1 46  SER 46  338 338 SER SER A . n 
A 1 47  GLU 47  339 339 GLU GLU A . n 
A 1 48  ALA 48  340 340 ALA ALA A . n 
A 1 49  SER 49  341 341 SER SER A . n 
A 1 50  MET 50  342 342 MET MET A . n 
A 1 51  MET 51  343 343 MET MET A . n 
A 1 52  GLY 52  344 344 GLY GLY A . n 
A 1 53  LEU 53  345 345 LEU LEU A . n 
A 1 54  LEU 54  346 346 LEU LEU A . n 
A 1 55  THR 55  347 347 THR THR A . n 
A 1 56  ASN 56  348 348 ASN ASN A . n 
A 1 57  LEU 57  349 349 LEU LEU A . n 
A 1 58  ALA 58  350 350 ALA ALA A . n 
A 1 59  ASP 59  351 351 ASP ASP A . n 
A 1 60  ARG 60  352 352 ARG ARG A . n 
A 1 61  GLU 61  353 353 GLU GLU A . n 
A 1 62  LEU 62  354 354 LEU LEU A . n 
A 1 63  VAL 63  355 355 VAL VAL A . n 
A 1 64  HIS 64  356 356 HIS HIS A . n 
A 1 65  MET 65  357 357 MET MET A . n 
A 1 66  ILE 66  358 358 ILE ILE A . n 
A 1 67  ASN 67  359 359 ASN ASN A . n 
A 1 68  TRP 68  360 360 TRP TRP A . n 
A 1 69  ALA 69  361 361 ALA ALA A . n 
A 1 70  LYS 70  362 362 LYS LYS A . n 
A 1 71  ARG 71  363 363 ARG ARG A . n 
A 1 72  VAL 72  364 364 VAL VAL A . n 
A 1 73  PRO 73  365 365 PRO PRO A . n 
A 1 74  GLY 74  366 366 GLY GLY A . n 
A 1 75  PHE 75  367 367 PHE PHE A . n 
A 1 76  VAL 76  368 368 VAL VAL A . n 
A 1 77  ASP 77  369 369 ASP ASP A . n 
A 1 78  LEU 78  370 370 LEU LEU A . n 
A 1 79  THR 79  371 371 THR THR A . n 
A 1 80  LEU 80  372 372 LEU LEU A . n 
A 1 81  HIS 81  373 373 HIS HIS A . n 
A 1 82  ASP 82  374 374 ASP ASP A . n 
A 1 83  GLN 83  375 375 GLN GLN A . n 
A 1 84  VAL 84  376 376 VAL VAL A . n 
A 1 85  HIS 85  377 377 HIS HIS A . n 
A 1 86  LEU 86  378 378 LEU LEU A . n 
A 1 87  LEU 87  379 379 LEU LEU A . n 
A 1 88  GLU 88  380 380 GLU GLU A . n 
A 1 89  SER 89  381 381 SER SER A . n 
A 1 90  ALA 90  382 382 ALA ALA A . n 
A 1 91  TRP 91  383 383 TRP TRP A . n 
A 1 92  LEU 92  384 384 LEU LEU A . n 
A 1 93  GLU 93  385 385 GLU GLU A . n 
A 1 94  ILE 94  386 386 ILE ILE A . n 
A 1 95  LEU 95  387 387 LEU LEU A . n 
A 1 96  MET 96  388 388 MET MET A . n 
A 1 97  ILE 97  389 389 ILE ILE A . n 
A 1 98  GLY 98  390 390 GLY GLY A . n 
A 1 99  LEU 99  391 391 LEU LEU A . n 
A 1 100 VAL 100 392 392 VAL VAL A . n 
A 1 101 TRP 101 393 393 TRP TRP A . n 
A 1 102 ARG 102 394 394 ARG ARG A . n 
A 1 103 SER 103 395 395 SER SER A . n 
A 1 104 MET 104 396 396 MET MET A . n 
A 1 105 GLU 105 397 397 GLU GLU A . n 
A 1 106 HIS 106 398 398 HIS HIS A . n 
A 1 107 PRO 107 399 399 PRO PRO A . n 
A 1 108 GLY 108 400 400 GLY GLY A . n 
A 1 109 LYS 109 401 401 LYS LYS A . n 
A 1 110 LEU 110 402 402 LEU LEU A . n 
A 1 111 LEU 111 403 403 LEU LEU A . n 
A 1 112 PHE 112 404 404 PHE PHE A . n 
A 1 113 ALA 113 405 405 ALA ALA A . n 
A 1 114 PRO 114 406 406 PRO PRO A . n 
A 1 115 ASN 115 407 407 ASN ASN A . n 
A 1 116 LEU 116 408 408 LEU LEU A . n 
A 1 117 LEU 117 409 409 LEU LEU A . n 
A 1 118 LEU 118 410 410 LEU LEU A . n 
A 1 119 ASP 119 411 411 ASP ASP A . n 
A 1 120 ARG 120 412 412 ARG ARG A . n 
A 1 121 ASN 121 413 413 ASN ASN A . n 
A 1 122 GLN 122 414 414 GLN GLN A . n 
A 1 123 GLY 123 415 415 GLY GLY A . n 
A 1 124 LYS 124 416 416 LYS LYS A . n 
A 1 125 SER 125 417 417 SER SER A . n 
A 1 126 VAL 126 418 418 VAL VAL A . n 
A 1 127 GLU 127 419 419 GLU GLU A . n 
A 1 128 GLY 128 420 420 GLY GLY A . n 
A 1 129 MET 129 421 421 MET MET A . n 
A 1 130 VAL 130 422 422 VAL VAL A . n 
A 1 131 GLU 131 423 423 GLU GLU A . n 
A 1 132 ILE 132 424 424 ILE ILE A . n 
A 1 133 PHE 133 425 425 PHE PHE A . n 
A 1 134 ASP 134 426 426 ASP ASP A . n 
A 1 135 MET 135 427 427 MET MET A . n 
A 1 136 LEU 136 428 428 LEU LEU A . n 
A 1 137 LEU 137 429 429 LEU LEU A . n 
A 1 138 ALA 138 430 430 ALA ALA A . n 
A 1 139 THR 139 431 431 THR THR A . n 
A 1 140 SER 140 432 432 SER SER A . n 
A 1 141 SER 141 433 433 SER SER A . n 
A 1 142 ARG 142 434 434 ARG ARG A . n 
A 1 143 PHE 143 435 435 PHE PHE A . n 
A 1 144 ARG 144 436 436 ARG ARG A . n 
A 1 145 MET 145 437 437 MET MET A . n 
A 1 146 MET 146 438 438 MET MET A . n 
A 1 147 ASN 147 439 439 ASN ASN A . n 
A 1 148 LEU 148 440 440 LEU LEU A . n 
A 1 149 GLN 149 441 441 GLN GLN A . n 
A 1 150 GLY 150 442 442 GLY GLY A . n 
A 1 151 GLU 151 443 443 GLU GLU A . n 
A 1 152 GLU 152 444 444 GLU GLU A . n 
A 1 153 PHE 153 445 445 PHE PHE A . n 
A 1 154 VAL 154 446 446 VAL VAL A . n 
A 1 155 CYS 155 447 447 CYS CYS A . n 
A 1 156 LEU 156 448 448 LEU LEU A . n 
A 1 157 LYS 157 449 449 LYS LYS A . n 
A 1 158 SER 158 450 450 SER SER A . n 
A 1 159 ILE 159 451 451 ILE ILE A . n 
A 1 160 ILE 160 452 452 ILE ILE A . n 
A 1 161 LEU 161 453 453 LEU LEU A . n 
A 1 162 LEU 162 454 454 LEU LEU A . n 
A 1 163 ASN 163 455 455 ASN ASN A . n 
A 1 164 SER 164 456 456 SER SER A . n 
A 1 165 GLY 165 457 457 GLY GLY A . n 
A 1 166 VAL 166 458 458 VAL VAL A . n 
A 1 167 TYR 167 459 459 TYR TYR A . n 
A 1 168 THR 168 460 460 THR THR A . n 
A 1 169 PHE 169 461 461 PHE PHE A . n 
A 1 170 LEU 170 462 ?   ?   ?   A . n 
A 1 171 SER 171 463 ?   ?   ?   A . n 
A 1 172 SER 172 464 464 SER SER A . n 
A 1 173 THR 173 465 465 THR THR A . n 
A 1 174 LEU 174 466 466 LEU LEU A . n 
A 1 175 LYS 175 467 467 LYS LYS A . n 
A 1 176 SER 176 468 468 SER SER A . n 
A 1 177 LEU 177 469 469 LEU LEU A . n 
A 1 178 GLU 178 470 470 GLU GLU A . n 
A 1 179 GLU 179 471 471 GLU GLU A . n 
A 1 180 LYS 180 472 472 LYS LYS A . n 
A 1 181 ASP 181 473 473 ASP ASP A . n 
A 1 182 HIS 182 474 474 HIS HIS A . n 
A 1 183 ILE 183 475 475 ILE ILE A . n 
A 1 184 HIS 184 476 476 HIS HIS A . n 
A 1 185 ARG 185 477 477 ARG ARG A . n 
A 1 186 VAL 186 478 478 VAL VAL A . n 
A 1 187 LEU 187 479 479 LEU LEU A . n 
A 1 188 ASP 188 480 480 ASP ASP A . n 
A 1 189 LYS 189 481 481 LYS LYS A . n 
A 1 190 ILE 190 482 482 ILE ILE A . n 
A 1 191 THR 191 483 483 THR THR A . n 
A 1 192 ASP 192 484 484 ASP ASP A . n 
A 1 193 THR 193 485 485 THR THR A . n 
A 1 194 LEU 194 486 486 LEU LEU A . n 
A 1 195 ILE 195 487 487 ILE ILE A . n 
A 1 196 HIS 196 488 488 HIS HIS A . n 
A 1 197 LEU 197 489 489 LEU LEU A . n 
A 1 198 MET 198 490 490 MET MET A . n 
A 1 199 ALA 199 491 491 ALA ALA A . n 
A 1 200 LYS 200 492 492 LYS LYS A . n 
A 1 201 ALA 201 493 493 ALA ALA A . n 
A 1 202 GLY 202 494 494 GLY GLY A . n 
A 1 203 LEU 203 495 495 LEU LEU A . n 
A 1 204 THR 204 496 496 THR THR A . n 
A 1 205 LEU 205 497 497 LEU LEU A . n 
A 1 206 GLN 206 498 498 GLN GLN A . n 
A 1 207 GLN 207 499 499 GLN GLN A . n 
A 1 208 GLN 208 500 500 GLN GLN A . n 
A 1 209 HIS 209 501 501 HIS HIS A . n 
A 1 210 GLN 210 502 502 GLN GLN A . n 
A 1 211 ARG 211 503 503 ARG ARG A . n 
A 1 212 LEU 212 504 504 LEU LEU A . n 
A 1 213 ALA 213 505 505 ALA ALA A . n 
A 1 214 GLN 214 506 506 GLN GLN A . n 
A 1 215 LEU 215 507 507 LEU LEU A . n 
A 1 216 LEU 216 508 508 LEU LEU A . n 
A 1 217 LEU 217 509 509 LEU LEU A . n 
A 1 218 ILE 218 510 510 ILE ILE A . n 
A 1 219 LEU 219 511 511 LEU LEU A . n 
A 1 220 SER 220 512 512 SER SER A . n 
A 1 221 HIS 221 513 513 HIS HIS A . n 
A 1 222 ILE 222 514 514 ILE ILE A . n 
A 1 223 ARG 223 515 515 ARG ARG A . n 
A 1 224 HIS 224 516 516 HIS HIS A . n 
A 1 225 MET 225 517 517 MET MET A . n 
A 1 226 SER 226 518 518 SER SER A . n 
A 1 227 ASN 227 519 519 ASN ASN A . n 
A 1 228 LYS 228 520 520 LYS LYS A . n 
A 1 229 GLY 229 521 521 GLY GLY A . n 
A 1 230 MET 230 522 522 MET MET A . n 
A 1 231 GLU 231 523 523 GLU GLU A . n 
A 1 232 HIS 232 524 524 HIS HIS A . n 
A 1 233 LEU 233 525 525 LEU LEU A . n 
A 1 234 TYR 234 526 526 TYR TYR A . n 
A 1 235 SER 235 527 527 SER SER A . n 
A 1 236 MET 236 528 528 MET MET A . n 
A 1 237 LYS 237 529 ?   ?   ?   A . n 
A 1 238 SER 238 530 ?   ?   ?   A . n 
A 1 239 LYS 239 531 ?   ?   ?   A . n 
A 1 240 ASN 240 532 ?   ?   ?   A . n 
A 1 241 VAL 241 533 ?   ?   ?   A . n 
A 1 242 VAL 242 534 ?   ?   ?   A . n 
A 1 243 PRO 243 535 ?   ?   ?   A . n 
A 1 244 LEU 244 536 536 LEU LEU A . n 
A 1 245 SER 245 537 537 SER SER A . n 
A 1 246 ASP 246 538 538 ASP ASP A . n 
A 1 247 LEU 247 539 539 LEU LEU A . n 
A 1 248 LEU 248 540 540 LEU LEU A . n 
A 1 249 LEU 249 541 541 LEU LEU A . n 
A 1 250 GLU 250 542 542 GLU GLU A . n 
A 1 251 MET 251 543 543 MET MET A . n 
A 1 252 LEU 252 544 544 LEU LEU A . n 
A 1 253 ASP 253 545 545 ASP ASP A . n 
A 1 254 ALA 254 546 546 ALA ALA A . n 
A 1 255 HIS 255 547 547 HIS HIS A . n 
A 1 256 ARG 256 548 548 ARG ARG A . n 
A 1 257 LEU 257 549 549 LEU LEU A . n 
A 1 258 HIS 258 550 ?   ?   ?   A . n 
A 1 259 ALA 259 551 ?   ?   ?   A . n 
A 1 260 PRO 260 552 ?   ?   ?   A . n 
A 1 261 THR 261 553 ?   ?   ?   A . n 
A 1 262 SER 262 554 ?   ?   ?   A . n 
B 1 1   HIS 1   293 ?   ?   ?   B . n 
B 1 2   HIS 2   294 ?   ?   ?   B . n 
B 1 3   HIS 3   295 ?   ?   ?   B . n 
B 1 4   HIS 4   296 ?   ?   ?   B . n 
B 1 5   HIS 5   297 ?   ?   ?   B . n 
B 1 6   HIS 6   298 ?   ?   ?   B . n 
B 1 7   GLU 7   299 ?   ?   ?   B . n 
B 1 8   ASN 8   300 ?   ?   ?   B . n 
B 1 9   LEU 9   301 ?   ?   ?   B . n 
B 1 10  TYR 10  302 ?   ?   ?   B . n 
B 1 11  PHE 11  303 ?   ?   ?   B . n 
B 1 12  GLN 12  304 ?   ?   ?   B . n 
B 1 13  SER 13  305 ?   ?   ?   B . n 
B 1 14  LEU 14  306 306 LEU LEU B . n 
B 1 15  ALA 15  307 307 ALA ALA B . n 
B 1 16  LEU 16  308 308 LEU LEU B . n 
B 1 17  SER 17  309 309 SER SER B . n 
B 1 18  LEU 18  310 310 LEU LEU B . n 
B 1 19  THR 19  311 311 THR THR B . n 
B 1 20  ALA 20  312 312 ALA ALA B . n 
B 1 21  ASP 21  313 313 ASP ASP B . n 
B 1 22  GLN 22  314 314 GLN GLN B . n 
B 1 23  MET 23  315 315 MET MET B . n 
B 1 24  VAL 24  316 316 VAL VAL B . n 
B 1 25  SER 25  317 317 SER SER B . n 
B 1 26  ALA 26  318 318 ALA ALA B . n 
B 1 27  LEU 27  319 319 LEU LEU B . n 
B 1 28  LEU 28  320 320 LEU LEU B . n 
B 1 29  ASP 29  321 321 ASP ASP B . n 
B 1 30  ALA 30  322 322 ALA ALA B . n 
B 1 31  GLU 31  323 323 GLU GLU B . n 
B 1 32  PRO 32  324 324 PRO PRO B . n 
B 1 33  PRO 33  325 325 PRO PRO B . n 
B 1 34  ILE 34  326 326 ILE ILE B . n 
B 1 35  LEU 35  327 327 LEU LEU B . n 
B 1 36  TYR 36  328 328 TYR TYR B . n 
B 1 37  SER 37  329 329 SER SER B . n 
B 1 38  GLU 38  330 330 GLU GLU B . n 
B 1 39  TYR 39  331 331 TYR TYR B . n 
B 1 40  ASP 40  332 332 ASP ASP B . n 
B 1 41  PRO 41  333 333 PRO PRO B . n 
B 1 42  THR 42  334 334 THR THR B . n 
B 1 43  ARG 43  335 335 ARG ARG B . n 
B 1 44  PRO 44  336 336 PRO PRO B . n 
B 1 45  PHE 45  337 337 PHE PHE B . n 
B 1 46  SER 46  338 338 SER SER B . n 
B 1 47  GLU 47  339 339 GLU GLU B . n 
B 1 48  ALA 48  340 340 ALA ALA B . n 
B 1 49  SER 49  341 341 SER SER B . n 
B 1 50  MET 50  342 342 MET MET B . n 
B 1 51  MET 51  343 343 MET MET B . n 
B 1 52  GLY 52  344 344 GLY GLY B . n 
B 1 53  LEU 53  345 345 LEU LEU B . n 
B 1 54  LEU 54  346 346 LEU LEU B . n 
B 1 55  THR 55  347 347 THR THR B . n 
B 1 56  ASN 56  348 348 ASN ASN B . n 
B 1 57  LEU 57  349 349 LEU LEU B . n 
B 1 58  ALA 58  350 350 ALA ALA B . n 
B 1 59  ASP 59  351 351 ASP ASP B . n 
B 1 60  ARG 60  352 352 ARG ARG B . n 
B 1 61  GLU 61  353 353 GLU GLU B . n 
B 1 62  LEU 62  354 354 LEU LEU B . n 
B 1 63  VAL 63  355 355 VAL VAL B . n 
B 1 64  HIS 64  356 356 HIS HIS B . n 
B 1 65  MET 65  357 357 MET MET B . n 
B 1 66  ILE 66  358 358 ILE ILE B . n 
B 1 67  ASN 67  359 359 ASN ASN B . n 
B 1 68  TRP 68  360 360 TRP TRP B . n 
B 1 69  ALA 69  361 361 ALA ALA B . n 
B 1 70  LYS 70  362 362 LYS LYS B . n 
B 1 71  ARG 71  363 363 ARG ARG B . n 
B 1 72  VAL 72  364 364 VAL VAL B . n 
B 1 73  PRO 73  365 365 PRO PRO B . n 
B 1 74  GLY 74  366 366 GLY GLY B . n 
B 1 75  PHE 75  367 367 PHE PHE B . n 
B 1 76  VAL 76  368 368 VAL VAL B . n 
B 1 77  ASP 77  369 369 ASP ASP B . n 
B 1 78  LEU 78  370 370 LEU LEU B . n 
B 1 79  THR 79  371 371 THR THR B . n 
B 1 80  LEU 80  372 372 LEU LEU B . n 
B 1 81  HIS 81  373 373 HIS HIS B . n 
B 1 82  ASP 82  374 374 ASP ASP B . n 
B 1 83  GLN 83  375 375 GLN GLN B . n 
B 1 84  VAL 84  376 376 VAL VAL B . n 
B 1 85  HIS 85  377 377 HIS HIS B . n 
B 1 86  LEU 86  378 378 LEU LEU B . n 
B 1 87  LEU 87  379 379 LEU LEU B . n 
B 1 88  GLU 88  380 380 GLU GLU B . n 
B 1 89  SER 89  381 381 SER SER B . n 
B 1 90  ALA 90  382 382 ALA ALA B . n 
B 1 91  TRP 91  383 383 TRP TRP B . n 
B 1 92  LEU 92  384 384 LEU LEU B . n 
B 1 93  GLU 93  385 385 GLU GLU B . n 
B 1 94  ILE 94  386 386 ILE ILE B . n 
B 1 95  LEU 95  387 387 LEU LEU B . n 
B 1 96  MET 96  388 388 MET MET B . n 
B 1 97  ILE 97  389 389 ILE ILE B . n 
B 1 98  GLY 98  390 390 GLY GLY B . n 
B 1 99  LEU 99  391 391 LEU LEU B . n 
B 1 100 VAL 100 392 392 VAL VAL B . n 
B 1 101 TRP 101 393 393 TRP TRP B . n 
B 1 102 ARG 102 394 394 ARG ARG B . n 
B 1 103 SER 103 395 395 SER SER B . n 
B 1 104 MET 104 396 396 MET MET B . n 
B 1 105 GLU 105 397 397 GLU GLU B . n 
B 1 106 HIS 106 398 398 HIS HIS B . n 
B 1 107 PRO 107 399 399 PRO PRO B . n 
B 1 108 GLY 108 400 400 GLY GLY B . n 
B 1 109 LYS 109 401 401 LYS LYS B . n 
B 1 110 LEU 110 402 402 LEU LEU B . n 
B 1 111 LEU 111 403 403 LEU LEU B . n 
B 1 112 PHE 112 404 404 PHE PHE B . n 
B 1 113 ALA 113 405 405 ALA ALA B . n 
B 1 114 PRO 114 406 406 PRO PRO B . n 
B 1 115 ASN 115 407 407 ASN ASN B . n 
B 1 116 LEU 116 408 408 LEU LEU B . n 
B 1 117 LEU 117 409 409 LEU LEU B . n 
B 1 118 LEU 118 410 410 LEU LEU B . n 
B 1 119 ASP 119 411 411 ASP ASP B . n 
B 1 120 ARG 120 412 412 ARG ARG B . n 
B 1 121 ASN 121 413 413 ASN ASN B . n 
B 1 122 GLN 122 414 414 GLN GLN B . n 
B 1 123 GLY 123 415 415 GLY GLY B . n 
B 1 124 LYS 124 416 416 LYS LYS B . n 
B 1 125 SER 125 417 417 SER SER B . n 
B 1 126 VAL 126 418 418 VAL VAL B . n 
B 1 127 GLU 127 419 419 GLU GLU B . n 
B 1 128 GLY 128 420 420 GLY GLY B . n 
B 1 129 MET 129 421 421 MET MET B . n 
B 1 130 VAL 130 422 422 VAL VAL B . n 
B 1 131 GLU 131 423 423 GLU GLU B . n 
B 1 132 ILE 132 424 424 ILE ILE B . n 
B 1 133 PHE 133 425 425 PHE PHE B . n 
B 1 134 ASP 134 426 426 ASP ASP B . n 
B 1 135 MET 135 427 427 MET MET B . n 
B 1 136 LEU 136 428 428 LEU LEU B . n 
B 1 137 LEU 137 429 429 LEU LEU B . n 
B 1 138 ALA 138 430 430 ALA ALA B . n 
B 1 139 THR 139 431 431 THR THR B . n 
B 1 140 SER 140 432 432 SER SER B . n 
B 1 141 SER 141 433 433 SER SER B . n 
B 1 142 ARG 142 434 434 ARG ARG B . n 
B 1 143 PHE 143 435 435 PHE PHE B . n 
B 1 144 ARG 144 436 436 ARG ARG B . n 
B 1 145 MET 145 437 437 MET MET B . n 
B 1 146 MET 146 438 438 MET MET B . n 
B 1 147 ASN 147 439 439 ASN ASN B . n 
B 1 148 LEU 148 440 440 LEU LEU B . n 
B 1 149 GLN 149 441 441 GLN GLN B . n 
B 1 150 GLY 150 442 442 GLY GLY B . n 
B 1 151 GLU 151 443 443 GLU GLU B . n 
B 1 152 GLU 152 444 444 GLU GLU B . n 
B 1 153 PHE 153 445 445 PHE PHE B . n 
B 1 154 VAL 154 446 446 VAL VAL B . n 
B 1 155 CYS 155 447 447 CYS CYS B . n 
B 1 156 LEU 156 448 448 LEU LEU B . n 
B 1 157 LYS 157 449 449 LYS LYS B . n 
B 1 158 SER 158 450 450 SER SER B . n 
B 1 159 ILE 159 451 451 ILE ILE B . n 
B 1 160 ILE 160 452 452 ILE ILE B . n 
B 1 161 LEU 161 453 453 LEU LEU B . n 
B 1 162 LEU 162 454 454 LEU LEU B . n 
B 1 163 ASN 163 455 455 ASN ASN B . n 
B 1 164 SER 164 456 456 SER SER B . n 
B 1 165 GLY 165 457 457 GLY GLY B . n 
B 1 166 VAL 166 458 458 VAL VAL B . n 
B 1 167 TYR 167 459 459 TYR TYR B . n 
B 1 168 THR 168 460 ?   ?   ?   B . n 
B 1 169 PHE 169 461 ?   ?   ?   B . n 
B 1 170 LEU 170 462 ?   ?   ?   B . n 
B 1 171 SER 171 463 ?   ?   ?   B . n 
B 1 172 SER 172 464 ?   ?   ?   B . n 
B 1 173 THR 173 465 ?   ?   ?   B . n 
B 1 174 LEU 174 466 ?   ?   ?   B . n 
B 1 175 LYS 175 467 ?   ?   ?   B . n 
B 1 176 SER 176 468 ?   ?   ?   B . n 
B 1 177 LEU 177 469 469 LEU LEU B . n 
B 1 178 GLU 178 470 470 GLU GLU B . n 
B 1 179 GLU 179 471 471 GLU GLU B . n 
B 1 180 LYS 180 472 472 LYS LYS B . n 
B 1 181 ASP 181 473 473 ASP ASP B . n 
B 1 182 HIS 182 474 474 HIS HIS B . n 
B 1 183 ILE 183 475 475 ILE ILE B . n 
B 1 184 HIS 184 476 476 HIS HIS B . n 
B 1 185 ARG 185 477 477 ARG ARG B . n 
B 1 186 VAL 186 478 478 VAL VAL B . n 
B 1 187 LEU 187 479 479 LEU LEU B . n 
B 1 188 ASP 188 480 480 ASP ASP B . n 
B 1 189 LYS 189 481 481 LYS LYS B . n 
B 1 190 ILE 190 482 482 ILE ILE B . n 
B 1 191 THR 191 483 483 THR THR B . n 
B 1 192 ASP 192 484 484 ASP ASP B . n 
B 1 193 THR 193 485 485 THR THR B . n 
B 1 194 LEU 194 486 486 LEU LEU B . n 
B 1 195 ILE 195 487 487 ILE ILE B . n 
B 1 196 HIS 196 488 488 HIS HIS B . n 
B 1 197 LEU 197 489 489 LEU LEU B . n 
B 1 198 MET 198 490 490 MET MET B . n 
B 1 199 ALA 199 491 491 ALA ALA B . n 
B 1 200 LYS 200 492 492 LYS LYS B . n 
B 1 201 ALA 201 493 493 ALA ALA B . n 
B 1 202 GLY 202 494 494 GLY GLY B . n 
B 1 203 LEU 203 495 495 LEU LEU B . n 
B 1 204 THR 204 496 496 THR THR B . n 
B 1 205 LEU 205 497 497 LEU LEU B . n 
B 1 206 GLN 206 498 498 GLN GLN B . n 
B 1 207 GLN 207 499 499 GLN GLN B . n 
B 1 208 GLN 208 500 500 GLN GLN B . n 
B 1 209 HIS 209 501 501 HIS HIS B . n 
B 1 210 GLN 210 502 502 GLN GLN B . n 
B 1 211 ARG 211 503 503 ARG ARG B . n 
B 1 212 LEU 212 504 504 LEU LEU B . n 
B 1 213 ALA 213 505 505 ALA ALA B . n 
B 1 214 GLN 214 506 506 GLN GLN B . n 
B 1 215 LEU 215 507 507 LEU LEU B . n 
B 1 216 LEU 216 508 508 LEU LEU B . n 
B 1 217 LEU 217 509 509 LEU LEU B . n 
B 1 218 ILE 218 510 510 ILE ILE B . n 
B 1 219 LEU 219 511 511 LEU LEU B . n 
B 1 220 SER 220 512 512 SER SER B . n 
B 1 221 HIS 221 513 513 HIS HIS B . n 
B 1 222 ILE 222 514 514 ILE ILE B . n 
B 1 223 ARG 223 515 515 ARG ARG B . n 
B 1 224 HIS 224 516 516 HIS HIS B . n 
B 1 225 MET 225 517 517 MET MET B . n 
B 1 226 SER 226 518 518 SER SER B . n 
B 1 227 ASN 227 519 519 ASN ASN B . n 
B 1 228 LYS 228 520 520 LYS LYS B . n 
B 1 229 GLY 229 521 521 GLY GLY B . n 
B 1 230 MET 230 522 522 MET MET B . n 
B 1 231 GLU 231 523 523 GLU GLU B . n 
B 1 232 HIS 232 524 524 HIS HIS B . n 
B 1 233 LEU 233 525 525 LEU LEU B . n 
B 1 234 TYR 234 526 526 TYR TYR B . n 
B 1 235 SER 235 527 527 SER SER B . n 
B 1 236 MET 236 528 ?   ?   ?   B . n 
B 1 237 LYS 237 529 ?   ?   ?   B . n 
B 1 238 SER 238 530 ?   ?   ?   B . n 
B 1 239 LYS 239 531 ?   ?   ?   B . n 
B 1 240 ASN 240 532 ?   ?   ?   B . n 
B 1 241 VAL 241 533 533 VAL VAL B . n 
B 1 242 VAL 242 534 534 VAL VAL B . n 
B 1 243 PRO 243 535 535 PRO PRO B . n 
B 1 244 LEU 244 536 536 LEU LEU B . n 
B 1 245 SER 245 537 537 SER SER B . n 
B 1 246 ASP 246 538 538 ASP ASP B . n 
B 1 247 LEU 247 539 539 LEU LEU B . n 
B 1 248 LEU 248 540 540 LEU LEU B . n 
B 1 249 LEU 249 541 541 LEU LEU B . n 
B 1 250 GLU 250 542 542 GLU GLU B . n 
B 1 251 MET 251 543 543 MET MET B . n 
B 1 252 LEU 252 544 544 LEU LEU B . n 
B 1 253 ASP 253 545 545 ASP ASP B . n 
B 1 254 ALA 254 546 546 ALA ALA B . n 
B 1 255 HIS 255 547 ?   ?   ?   B . n 
B 1 256 ARG 256 548 ?   ?   ?   B . n 
B 1 257 LEU 257 549 ?   ?   ?   B . n 
B 1 258 HIS 258 550 ?   ?   ?   B . n 
B 1 259 ALA 259 551 ?   ?   ?   B . n 
B 1 260 PRO 260 552 ?   ?   ?   B . n 
B 1 261 THR 261 553 ?   ?   ?   B . n 
B 1 262 SER 262 554 ?   ?   ?   B . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        TZI 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   TZI 
_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 HIS   1   601 550 HIS   HIS A . 
D 3 TZI   1   602 601 TZI   LIG A . 
E 4 A1BV9 1   601 601 A1BV9 LIG B . 
F 5 HOH   1   701 60  HOH   HOH A . 
F 5 HOH   2   702 166 HOH   HOH A . 
F 5 HOH   3   703 131 HOH   HOH A . 
F 5 HOH   4   704 97  HOH   HOH A . 
F 5 HOH   5   705 78  HOH   HOH A . 
F 5 HOH   6   706 42  HOH   HOH A . 
F 5 HOH   7   707 158 HOH   HOH A . 
F 5 HOH   8   708 127 HOH   HOH A . 
F 5 HOH   9   709 65  HOH   HOH A . 
F 5 HOH   10  710 142 HOH   HOH A . 
F 5 HOH   11  711 151 HOH   HOH A . 
F 5 HOH   12  712 35  HOH   HOH A . 
F 5 HOH   13  713 34  HOH   HOH A . 
F 5 HOH   14  714 39  HOH   HOH A . 
F 5 HOH   15  715 51  HOH   HOH A . 
F 5 HOH   16  716 155 HOH   HOH A . 
F 5 HOH   17  717 63  HOH   HOH A . 
F 5 HOH   18  718 194 HOH   HOH A . 
F 5 HOH   19  719 2   HOH   HOH A . 
F 5 HOH   20  720 7   HOH   HOH A . 
F 5 HOH   21  721 53  HOH   HOH A . 
F 5 HOH   22  722 33  HOH   HOH A . 
F 5 HOH   23  723 13  HOH   HOH A . 
F 5 HOH   24  724 8   HOH   HOH A . 
F 5 HOH   25  725 21  HOH   HOH A . 
F 5 HOH   26  726 10  HOH   HOH A . 
F 5 HOH   27  727 47  HOH   HOH A . 
F 5 HOH   28  728 3   HOH   HOH A . 
F 5 HOH   29  729 37  HOH   HOH A . 
F 5 HOH   30  730 107 HOH   HOH A . 
F 5 HOH   31  731 5   HOH   HOH A . 
F 5 HOH   32  732 117 HOH   HOH A . 
F 5 HOH   33  733 58  HOH   HOH A . 
F 5 HOH   34  734 43  HOH   HOH A . 
F 5 HOH   35  735 11  HOH   HOH A . 
F 5 HOH   36  736 105 HOH   HOH A . 
F 5 HOH   37  737 163 HOH   HOH A . 
F 5 HOH   38  738 62  HOH   HOH A . 
F 5 HOH   39  739 38  HOH   HOH A . 
F 5 HOH   40  740 79  HOH   HOH A . 
F 5 HOH   41  741 17  HOH   HOH A . 
F 5 HOH   42  742 81  HOH   HOH A . 
F 5 HOH   43  743 49  HOH   HOH A . 
F 5 HOH   44  744 137 HOH   HOH A . 
F 5 HOH   45  745 162 HOH   HOH A . 
F 5 HOH   46  746 141 HOH   HOH A . 
F 5 HOH   47  747 6   HOH   HOH A . 
F 5 HOH   48  748 171 HOH   HOH A . 
F 5 HOH   49  749 100 HOH   HOH A . 
F 5 HOH   50  750 88  HOH   HOH A . 
F 5 HOH   51  751 121 HOH   HOH A . 
F 5 HOH   52  752 115 HOH   HOH A . 
F 5 HOH   53  753 41  HOH   HOH A . 
F 5 HOH   54  754 113 HOH   HOH A . 
F 5 HOH   55  755 16  HOH   HOH A . 
F 5 HOH   56  756 109 HOH   HOH A . 
F 5 HOH   57  757 69  HOH   HOH A . 
F 5 HOH   58  758 106 HOH   HOH A . 
F 5 HOH   59  759 139 HOH   HOH A . 
F 5 HOH   60  760 82  HOH   HOH A . 
F 5 HOH   61  761 168 HOH   HOH A . 
F 5 HOH   62  762 111 HOH   HOH A . 
F 5 HOH   63  763 196 HOH   HOH A . 
F 5 HOH   64  764 114 HOH   HOH A . 
F 5 HOH   65  765 56  HOH   HOH A . 
F 5 HOH   66  766 27  HOH   HOH A . 
F 5 HOH   67  767 95  HOH   HOH A . 
F 5 HOH   68  768 180 HOH   HOH A . 
F 5 HOH   69  769 70  HOH   HOH A . 
F 5 HOH   70  770 54  HOH   HOH A . 
F 5 HOH   71  771 71  HOH   HOH A . 
F 5 HOH   72  772 61  HOH   HOH A . 
F 5 HOH   73  773 116 HOH   HOH A . 
F 5 HOH   74  774 104 HOH   HOH A . 
F 5 HOH   75  775 198 HOH   HOH A . 
F 5 HOH   76  776 144 HOH   HOH A . 
F 5 HOH   77  777 175 HOH   HOH A . 
F 5 HOH   78  778 73  HOH   HOH A . 
F 5 HOH   79  779 189 HOH   HOH A . 
F 5 HOH   80  780 128 HOH   HOH A . 
F 5 HOH   81  781 67  HOH   HOH A . 
F 5 HOH   82  782 140 HOH   HOH A . 
F 5 HOH   83  783 87  HOH   HOH A . 
F 5 HOH   84  784 93  HOH   HOH A . 
F 5 HOH   85  785 178 HOH   HOH A . 
F 5 HOH   86  786 186 HOH   HOH A . 
F 5 HOH   87  787 188 HOH   HOH A . 
F 5 HOH   88  788 138 HOH   HOH A . 
F 5 HOH   89  789 147 HOH   HOH A . 
F 5 HOH   90  790 126 HOH   HOH A . 
F 5 HOH   91  791 174 HOH   HOH A . 
F 5 HOH   92  792 154 HOH   HOH A . 
F 5 HOH   93  793 119 HOH   HOH A . 
F 5 HOH   94  794 200 HOH   HOH A . 
F 5 HOH   95  795 136 HOH   HOH A . 
F 5 HOH   96  796 181 HOH   HOH A . 
F 5 HOH   97  797 83  HOH   HOH A . 
F 5 HOH   98  798 57  HOH   HOH A . 
F 5 HOH   99  799 191 HOH   HOH A . 
F 5 HOH   100 800 32  HOH   HOH A . 
F 5 HOH   101 801 152 HOH   HOH A . 
F 5 HOH   102 802 134 HOH   HOH A . 
F 5 HOH   103 803 72  HOH   HOH A . 
F 5 HOH   104 804 164 HOH   HOH A . 
F 5 HOH   105 805 179 HOH   HOH A . 
F 5 HOH   106 806 195 HOH   HOH A . 
G 5 HOH   1   701 110 HOH   HOH B . 
G 5 HOH   2   702 84  HOH   HOH B . 
G 5 HOH   3   703 193 HOH   HOH B . 
G 5 HOH   4   704 55  HOH   HOH B . 
G 5 HOH   5   705 44  HOH   HOH B . 
G 5 HOH   6   706 125 HOH   HOH B . 
G 5 HOH   7   707 24  HOH   HOH B . 
G 5 HOH   8   708 50  HOH   HOH B . 
G 5 HOH   9   709 102 HOH   HOH B . 
G 5 HOH   10  710 112 HOH   HOH B . 
G 5 HOH   11  711 18  HOH   HOH B . 
G 5 HOH   12  712 26  HOH   HOH B . 
G 5 HOH   13  713 75  HOH   HOH B . 
G 5 HOH   14  714 19  HOH   HOH B . 
G 5 HOH   15  715 20  HOH   HOH B . 
G 5 HOH   16  716 22  HOH   HOH B . 
G 5 HOH   17  717 52  HOH   HOH B . 
G 5 HOH   18  718 159 HOH   HOH B . 
G 5 HOH   19  719 4   HOH   HOH B . 
G 5 HOH   20  720 129 HOH   HOH B . 
G 5 HOH   21  721 31  HOH   HOH B . 
G 5 HOH   22  722 29  HOH   HOH B . 
G 5 HOH   23  723 64  HOH   HOH B . 
G 5 HOH   24  724 14  HOH   HOH B . 
G 5 HOH   25  725 30  HOH   HOH B . 
G 5 HOH   26  726 66  HOH   HOH B . 
G 5 HOH   27  727 12  HOH   HOH B . 
G 5 HOH   28  728 169 HOH   HOH B . 
G 5 HOH   29  729 48  HOH   HOH B . 
G 5 HOH   30  730 46  HOH   HOH B . 
G 5 HOH   31  731 36  HOH   HOH B . 
G 5 HOH   32  732 9   HOH   HOH B . 
G 5 HOH   33  733 40  HOH   HOH B . 
G 5 HOH   34  734 108 HOH   HOH B . 
G 5 HOH   35  735 15  HOH   HOH B . 
G 5 HOH   36  736 146 HOH   HOH B . 
G 5 HOH   37  737 1   HOH   HOH B . 
G 5 HOH   38  738 74  HOH   HOH B . 
G 5 HOH   39  739 122 HOH   HOH B . 
G 5 HOH   40  740 103 HOH   HOH B . 
G 5 HOH   41  741 149 HOH   HOH B . 
G 5 HOH   42  742 133 HOH   HOH B . 
G 5 HOH   43  743 77  HOH   HOH B . 
G 5 HOH   44  744 28  HOH   HOH B . 
G 5 HOH   45  745 143 HOH   HOH B . 
G 5 HOH   46  746 165 HOH   HOH B . 
G 5 HOH   47  747 94  HOH   HOH B . 
G 5 HOH   48  748 167 HOH   HOH B . 
G 5 HOH   49  749 173 HOH   HOH B . 
G 5 HOH   50  750 68  HOH   HOH B . 
G 5 HOH   51  751 80  HOH   HOH B . 
G 5 HOH   52  752 45  HOH   HOH B . 
G 5 HOH   53  753 23  HOH   HOH B . 
G 5 HOH   54  754 170 HOH   HOH B . 
G 5 HOH   55  755 89  HOH   HOH B . 
G 5 HOH   56  756 59  HOH   HOH B . 
G 5 HOH   57  757 99  HOH   HOH B . 
G 5 HOH   58  758 172 HOH   HOH B . 
G 5 HOH   59  759 91  HOH   HOH B . 
G 5 HOH   60  760 92  HOH   HOH B . 
G 5 HOH   61  761 148 HOH   HOH B . 
G 5 HOH   62  762 177 HOH   HOH B . 
G 5 HOH   63  763 123 HOH   HOH B . 
G 5 HOH   64  764 184 HOH   HOH B . 
G 5 HOH   65  765 85  HOH   HOH B . 
G 5 HOH   66  766 201 HOH   HOH B . 
G 5 HOH   67  767 76  HOH   HOH B . 
G 5 HOH   68  768 197 HOH   HOH B . 
G 5 HOH   69  769 118 HOH   HOH B . 
G 5 HOH   70  770 183 HOH   HOH B . 
G 5 HOH   71  771 124 HOH   HOH B . 
G 5 HOH   72  772 130 HOH   HOH B . 
G 5 HOH   73  773 150 HOH   HOH B . 
G 5 HOH   74  774 160 HOH   HOH B . 
G 5 HOH   75  775 199 HOH   HOH B . 
G 5 HOH   76  776 86  HOH   HOH B . 
G 5 HOH   77  777 176 HOH   HOH B . 
G 5 HOH   78  778 145 HOH   HOH B . 
G 5 HOH   79  779 90  HOH   HOH B . 
G 5 HOH   80  780 190 HOH   HOH B . 
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1  1 Y 1 A LEU 306 ? CG  ? A LEU 14  CG  
2  1 Y 1 A LEU 306 ? CD1 ? A LEU 14  CD1 
3  1 Y 1 A LEU 306 ? CD2 ? A LEU 14  CD2 
4  1 Y 1 A ARG 335 ? CG  ? A ARG 43  CG  
5  1 Y 1 A ARG 335 ? CD  ? A ARG 43  CD  
6  1 Y 1 A ARG 335 ? NE  ? A ARG 43  NE  
7  1 Y 1 A ARG 335 ? CZ  ? A ARG 43  CZ  
8  1 Y 1 A ARG 335 ? NH1 ? A ARG 43  NH1 
9  1 Y 1 A ARG 335 ? NH2 ? A ARG 43  NH2 
10 1 Y 1 A GLU 339 ? CG  ? A GLU 47  CG  
11 1 Y 1 A GLU 339 ? CD  ? A GLU 47  CD  
12 1 Y 1 A GLU 339 ? OE1 ? A GLU 47  OE1 
13 1 Y 1 A GLU 339 ? OE2 ? A GLU 47  OE2 
14 1 Y 1 A MET 437 ? CG  ? A MET 145 CG  
15 1 Y 1 A MET 437 ? SD  ? A MET 145 SD  
16 1 Y 1 A MET 437 ? CE  ? A MET 145 CE  
17 1 Y 1 A THR 460 ? CG2 ? A THR 168 CG2 
18 1 Y 1 A ARG 477 ? CZ  ? A ARG 185 CZ  
19 1 Y 1 A ARG 477 ? NH1 ? A ARG 185 NH1 
20 1 Y 1 A ARG 477 ? NH2 ? A ARG 185 NH2 
21 1 Y 1 A ASP 538 ? CG  ? A ASP 246 CG  
22 1 Y 1 A ASP 538 ? OD1 ? A ASP 246 OD1 
23 1 Y 1 A ASP 538 ? OD2 ? A ASP 246 OD2 
24 1 Y 1 A ARG 548 ? CG  ? A ARG 256 CG  
25 1 Y 1 A ARG 548 ? CD  ? A ARG 256 CD  
26 1 Y 1 A ARG 548 ? NE  ? A ARG 256 NE  
27 1 Y 1 A ARG 548 ? CZ  ? A ARG 256 CZ  
28 1 Y 1 A ARG 548 ? NH1 ? A ARG 256 NH1 
29 1 Y 1 A ARG 548 ? NH2 ? A ARG 256 NH2 
30 1 Y 1 B ARG 335 ? CG  ? B ARG 43  CG  
31 1 Y 1 B ARG 335 ? CD  ? B ARG 43  CD  
32 1 Y 1 B ARG 335 ? NE  ? B ARG 43  NE  
33 1 Y 1 B ARG 335 ? CZ  ? B ARG 43  CZ  
34 1 Y 1 B ARG 335 ? NH1 ? B ARG 43  NH1 
35 1 Y 1 B ARG 335 ? NH2 ? B ARG 43  NH2 
36 1 Y 1 B GLU 339 ? CG  ? B GLU 47  CG  
37 1 Y 1 B GLU 339 ? CD  ? B GLU 47  CD  
38 1 Y 1 B GLU 339 ? OE1 ? B GLU 47  OE1 
39 1 Y 1 B GLU 339 ? OE2 ? B GLU 47  OE2 
40 1 Y 1 B GLU 397 ? CG  ? B GLU 105 CG  
41 1 Y 1 B GLU 397 ? CD  ? B GLU 105 CD  
42 1 Y 1 B GLU 397 ? OE1 ? B GLU 105 OE1 
43 1 Y 1 B GLU 397 ? OE2 ? B GLU 105 OE2 
44 1 Y 1 B LYS 401 ? CG  ? B LYS 109 CG  
45 1 Y 1 B LYS 401 ? CD  ? B LYS 109 CD  
46 1 Y 1 B LYS 401 ? CE  ? B LYS 109 CE  
47 1 Y 1 B LYS 401 ? NZ  ? B LYS 109 NZ  
48 1 Y 1 B LYS 416 ? NZ  ? B LYS 124 NZ  
49 1 Y 1 B GLU 419 ? CG  ? B GLU 127 CG  
50 1 Y 1 B GLU 419 ? CD  ? B GLU 127 CD  
51 1 Y 1 B GLU 419 ? OE1 ? B GLU 127 OE1 
52 1 Y 1 B GLU 419 ? OE2 ? B GLU 127 OE2 
53 1 Y 1 B GLU 423 ? CG  ? B GLU 131 CG  
54 1 Y 1 B GLU 423 ? CD  ? B GLU 131 CD  
55 1 Y 1 B GLU 423 ? OE1 ? B GLU 131 OE1 
56 1 Y 1 B GLU 423 ? OE2 ? B GLU 131 OE2 
57 1 Y 1 B MET 437 ? CG  ? B MET 145 CG  
58 1 Y 1 B MET 437 ? SD  ? B MET 145 SD  
59 1 Y 1 B MET 437 ? CE  ? B MET 145 CE  
60 1 Y 1 B LEU 469 ? CG  ? B LEU 177 CG  
61 1 Y 1 B LEU 469 ? CD1 ? B LEU 177 CD1 
62 1 Y 1 B LEU 469 ? CD2 ? B LEU 177 CD2 
63 1 Y 1 B GLU 470 ? CG  ? B GLU 178 CG  
64 1 Y 1 B GLU 470 ? CD  ? B GLU 178 CD  
65 1 Y 1 B GLU 470 ? OE1 ? B GLU 178 OE1 
66 1 Y 1 B GLU 470 ? OE2 ? B GLU 178 OE2 
67 1 Y 1 B GLU 471 ? CG  ? B GLU 179 CG  
68 1 Y 1 B GLU 471 ? CD  ? B GLU 179 CD  
69 1 Y 1 B GLU 471 ? OE1 ? B GLU 179 OE1 
70 1 Y 1 B GLU 471 ? OE2 ? B GLU 179 OE2 
71 1 Y 1 B ASP 545 ? CG  ? B ASP 253 CG  
72 1 Y 1 B ASP 545 ? OD1 ? B ASP 253 OD1 
73 1 Y 1 B ASP 545 ? OD2 ? B ASP 253 OD2 
74 1 N 1 A HIS 601 ? OXT ? C HIS 1   OXT 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement       ? ? ? ? ? ? ? ? ? ? ? PHENIX   ? ? ? '(1.20.1_4487: ???)' 1 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? HKL-3000 ? ? ? .                    2 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? HKL-3000 ? ? ? .                    3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHASER   ? ? ? .                    4 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   103.52 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9BPX 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     101.731 
_cell.length_a_esd                 ? 
_cell.length_b                     58.294 
_cell.length_b_esd                 ? 
_cell.length_c                     87.011 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        8 
_cell.reciprocal_angle_alpha       ? 
_cell.reciprocal_angle_beta        ? 
_cell.reciprocal_angle_gamma       ? 
_cell.reciprocal_angle_alpha_esd   ? 
_cell.reciprocal_angle_beta_esd    ? 
_cell.reciprocal_angle_gamma_esd   ? 
_cell.reciprocal_length_a          ? 
_cell.reciprocal_length_b          ? 
_cell.reciprocal_length_c          ? 
_cell.reciprocal_length_a_esd      ? 
_cell.reciprocal_length_b_esd      ? 
_cell.reciprocal_length_c_esd      ? 
_cell.pdbx_unique_axis             ? 
_cell.pdbx_esd_method              ? 
# 
_symmetry.entry_id                         9BPX 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                5 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'C 1 2 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                   9BPX 
_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             2.09 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          41.13 
_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, HANGING 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    'PEG 3,350, MgCl2' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            298 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS 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         2024-03-15 
_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   1.00 
_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                        'NSLS-II BEAMLINE 17-ID-1' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        1.00 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   17-ID-1 
_diffrn_source.pdbx_synchrotron_site       NSLS-II 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       9BPX 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              2.2 
_reflns.d_resolution_low                               50 
_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                                     24826 
_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                           98.1 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                3.7 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          1894.37 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               ? 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                ? 
_reflns.pdbx_Rpim_I_all                                0.068 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.999 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              ? 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
_reflns_shell.d_res_high                                    2.2 
_reflns_shell.d_res_low                                     2.24 
_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                             1248 
_reflns_shell.percent_possible_obs                          ? 
_reflns_shell.Rmerge_F_all                                  ? 
_reflns_shell.Rmerge_F_obs                                  ? 
_reflns_shell.meanI_over_sigI_gt                            ? 
_reflns_shell.meanI_over_uI_all                             ? 
_reflns_shell.meanI_over_uI_gt                              ? 
_reflns_shell.number_measured_gt                            ? 
_reflns_shell.number_unique_gt                              ? 
_reflns_shell.percent_possible_gt                           ? 
_reflns_shell.Rmerge_F_gt                                   ? 
_reflns_shell.Rmerge_I_gt                                   ? 
_reflns_shell.pdbx_redundancy                               ? 
_reflns_shell.pdbx_chi_squared                              ? 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     ? 
_reflns_shell.pdbx_Rrim_I_all                               ? 
_reflns_shell.pdbx_Rpim_I_all                               ? 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.655 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          ? 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  ? 
_reflns_shell.pdbx_Rsym_value                               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal             ? 
_reflns_shell.pdbx_percent_possible_spherical               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous   ? 
_reflns_shell.pdbx_percent_possible_spherical_anomalous     ? 
_reflns_shell.pdbx_redundancy_anomalous                     ? 
_reflns_shell.pdbx_CC_half_anomalous                        ? 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous             ? 
_reflns_shell.pdbx_percent_possible_anomalous               ? 
# 
_refine.aniso_B[1][1]                            ? 
_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                                 9BPX 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            2.20 
_refine.ls_d_res_low                             45.63 
_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                     23841 
_refine.ls_number_reflns_R_free                  1137 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    94.02 
_refine.ls_percent_reflns_R_free                 4.77 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1875 
_refine.ls_R_factor_R_free                       0.2211 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1858 
_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                          1.36 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               'FREE R-VALUE' 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       ML 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             1.10 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.90 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 21.98 
_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                            0.22 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       2.20 
_refine_hist.d_res_low                        45.63 
_refine_hist.number_atoms_solvent             186 
_refine_hist.number_atoms_total               3883 
_refine_hist.number_reflns_all                ? 
_refine_hist.number_reflns_obs                ? 
_refine_hist.number_reflns_R_free             ? 
_refine_hist.number_reflns_R_work             ? 
_refine_hist.R_factor_all                     ? 
_refine_hist.R_factor_obs                     ? 
_refine_hist.R_factor_R_free                  ? 
_refine_hist.R_factor_R_work                  ? 
_refine_hist.pdbx_number_residues_total       ? 
_refine_hist.pdbx_B_iso_mean_ligand           ? 
_refine_hist.pdbx_B_iso_mean_solvent          ? 
_refine_hist.pdbx_number_atoms_protein        3611 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         86 
_refine_hist.pdbx_number_atoms_lipid          ? 
_refine_hist.pdbx_number_atoms_carb           ? 
_refine_hist.pdbx_pseudo_atom_details         ? 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.criterion 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.number 
_refine_ls_restr.rejects 
_refine_ls_restr.type 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' ? 0.002  ? 3833 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 0.511  ? 5198 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 11.480 ? 517  ? f_dihedral_angle_d ? ? 
'X-RAY DIFFRACTION' ? 0.032  ? 610  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.004  ? 639  ? f_plane_restr      ? ? 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_obs 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.redundancy_reflns_all 
_refine_ls_shell.redundancy_reflns_obs 
_refine_ls_shell.wR_factor_all 
_refine_ls_shell.wR_factor_obs 
_refine_ls_shell.wR_factor_R_free 
_refine_ls_shell.wR_factor_R_work 
_refine_ls_shell.pdbx_R_complete 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.pdbx_phase_error 
_refine_ls_shell.pdbx_fsc_work 
_refine_ls_shell.pdbx_fsc_free 
_refine_ls_shell.R_factor_R_free 
'X-RAY DIFFRACTION' 2.20 2.30  . . 112 2247 75.00 . . . . 0.2330 . . . . . . . . . . . 0.2793 
'X-RAY DIFFRACTION' 2.30 2.42  . . 132 2743 91.00 . . . . 0.2150 . . . . . . . . . . . 0.3038 
'X-RAY DIFFRACTION' 2.42 2.57  . . 156 2844 95.00 . . . . 0.2027 . . . . . . . . . . . 0.2448 
'X-RAY DIFFRACTION' 2.57 2.77  . . 149 2964 99.00 . . . . 0.2082 . . . . . . . . . . . 0.2667 
'X-RAY DIFFRACTION' 2.77 3.05  . . 164 2946 99.00 . . . . 0.1923 . . . . . . . . . . . 0.2247 
'X-RAY DIFFRACTION' 3.05 3.49  . . 128 2977 98.00 . . . . 0.1818 . . . . . . . . . . . 0.2100 
'X-RAY DIFFRACTION' 3.49 4.40  . . 132 2999 98.00 . . . . 0.1597 . . . . . . . . . . . 0.1993 
'X-RAY DIFFRACTION' 4.40 45.63 . . 164 2984 97.00 . . . . 0.1812 . . . . . . . . . . . 0.1922 
# 
_struct.entry_id                     9BPX 
_struct.title                        
;Estrogen Receptor Alpha Ligand Binding Domain Y537S Mutant in Complex with (1'-(4-((1-butylpyrrolidin-3-yl)methoxy)phenyl)-6'-hydroxy-1',4'-dihydro-2'<i>H</i>-spiro[cyclopropane-1,3'-isoquinolin]-2'-yl)(phenyl)methanone
;
_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        9BPX 
_struct_keywords.text            'Estrogen, Alpha Helical Bundle, Breast Cancer, TRANSCRIPTION' 
_struct_keywords.pdbx_keywords   TRANSCRIPTION 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 1 ? 
C N N 2 ? 
D N N 3 ? 
E N N 4 ? 
F N N 5 ? 
G N N 5 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    ESR1_HUMAN 
_struct_ref.pdbx_db_accession          P03372 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;SLALSLTADQMVSALLDAEPPILYSEYDPTRPFSEASMMGLLTNLADRELVHMINWAKRVPGFVDLTLHDQVHLLECAWL
EILMIGLVWRSMEHPGKLLFAPNLLLDRNQGKCVEGMVEIFDMLLATSSRFRMMNLQGEEFVCLKSIILLNSGVYTFLSS
TLKSLEEKDHIHRVLDKITDTLIHLMAKAGLTLQQQHQRLAQLLLILSHIRHMSNKGMEHLYSMKCKNVVPLYDLLLEML
DAHRLHAPTS
;
_struct_ref.pdbx_align_begin           305 
# 
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 9BPX A 13 ? 262 ? P03372 305 ? 554 ? 305 554 
2 1 9BPX B 13 ? 262 ? P03372 305 ? 554 ? 305 554 
# 
loop_
_struct_ref_seq_dif.align_id 
_struct_ref_seq_dif.pdbx_pdb_id_code 
_struct_ref_seq_dif.mon_id 
_struct_ref_seq_dif.pdbx_pdb_strand_id 
_struct_ref_seq_dif.seq_num 
_struct_ref_seq_dif.pdbx_pdb_ins_code 
_struct_ref_seq_dif.pdbx_seq_db_name 
_struct_ref_seq_dif.pdbx_seq_db_accession_code 
_struct_ref_seq_dif.db_mon_id 
_struct_ref_seq_dif.pdbx_seq_db_seq_num 
_struct_ref_seq_dif.details 
_struct_ref_seq_dif.pdbx_auth_seq_num 
_struct_ref_seq_dif.pdbx_ordinal 
1 9BPX HIS A 1   ? UNP P03372 ?   ?   'expression tag'      293 1  
1 9BPX HIS A 2   ? UNP P03372 ?   ?   'expression tag'      294 2  
1 9BPX HIS A 3   ? UNP P03372 ?   ?   'expression tag'      295 3  
1 9BPX HIS A 4   ? UNP P03372 ?   ?   'expression tag'      296 4  
1 9BPX HIS A 5   ? UNP P03372 ?   ?   'expression tag'      297 5  
1 9BPX HIS A 6   ? UNP P03372 ?   ?   'expression tag'      298 6  
1 9BPX GLU A 7   ? UNP P03372 ?   ?   'expression tag'      299 7  
1 9BPX ASN A 8   ? UNP P03372 ?   ?   'expression tag'      300 8  
1 9BPX LEU A 9   ? UNP P03372 ?   ?   'expression tag'      301 9  
1 9BPX TYR A 10  ? UNP P03372 ?   ?   'expression tag'      302 10 
1 9BPX PHE A 11  ? UNP P03372 ?   ?   'expression tag'      303 11 
1 9BPX GLN A 12  ? UNP P03372 ?   ?   'expression tag'      304 12 
1 9BPX SER A 89  ? UNP P03372 CYS 381 'engineered mutation' 381 13 
1 9BPX SER A 125 ? UNP P03372 CYS 417 'engineered mutation' 417 14 
1 9BPX SER A 238 ? UNP P03372 CYS 530 'engineered mutation' 530 15 
1 9BPX SER A 245 ? UNP P03372 TYR 537 'engineered mutation' 537 16 
2 9BPX HIS B 1   ? UNP P03372 ?   ?   'expression tag'      293 17 
2 9BPX HIS B 2   ? UNP P03372 ?   ?   'expression tag'      294 18 
2 9BPX HIS B 3   ? UNP P03372 ?   ?   'expression tag'      295 19 
2 9BPX HIS B 4   ? UNP P03372 ?   ?   'expression tag'      296 20 
2 9BPX HIS B 5   ? UNP P03372 ?   ?   'expression tag'      297 21 
2 9BPX HIS B 6   ? UNP P03372 ?   ?   'expression tag'      298 22 
2 9BPX GLU B 7   ? UNP P03372 ?   ?   'expression tag'      299 23 
2 9BPX ASN B 8   ? UNP P03372 ?   ?   'expression tag'      300 24 
2 9BPX LEU B 9   ? UNP P03372 ?   ?   'expression tag'      301 25 
2 9BPX TYR B 10  ? UNP P03372 ?   ?   'expression tag'      302 26 
2 9BPX PHE B 11  ? UNP P03372 ?   ?   'expression tag'      303 27 
2 9BPX GLN B 12  ? UNP P03372 ?   ?   'expression tag'      304 28 
2 9BPX SER B 89  ? UNP P03372 CYS 381 'engineered mutation' 381 29 
2 9BPX SER B 125 ? UNP P03372 CYS 417 'engineered mutation' 417 30 
2 9BPX SER B 238 ? UNP P03372 CYS 530 'engineered mutation' 530 31 
2 9BPX SER B 245 ? UNP P03372 TYR 537 'engineered mutation' 537 32 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_and_software_defined_assembly 
_pdbx_struct_assembly.method_details       PISA 
_pdbx_struct_assembly.oligomeric_details   dimeric 
_pdbx_struct_assembly.oligomeric_count     2 
# 
loop_
_pdbx_struct_assembly_prop.biol_id 
_pdbx_struct_assembly_prop.type 
_pdbx_struct_assembly_prop.value 
_pdbx_struct_assembly_prop.details 
1 'ABSA (A^2)' 2850  ? 
1 MORE         -8    ? 
1 'SSA (A^2)'  19800 ? 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F,G 
# 
_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 LEU A 14  ? LEU A 18  ? LEU A 306 LEU A 310 5 ? 5  
HELX_P HELX_P2  AA2 THR A 19  ? ALA A 30  ? THR A 311 ALA A 322 1 ? 12 
HELX_P HELX_P3  AA3 SER A 49  ? ARG A 71  ? SER A 341 ARG A 363 1 ? 23 
HELX_P HELX_P4  AA4 THR A 79  ? SER A 103 ? THR A 371 SER A 395 1 ? 25 
HELX_P HELX_P5  AA5 MET A 104 ? HIS A 106 ? MET A 396 HIS A 398 5 ? 3  
HELX_P HELX_P6  AA6 ARG A 120 ? LYS A 124 ? ARG A 412 LYS A 416 1 ? 5  
HELX_P HELX_P7  AA7 GLY A 128 ? ASN A 147 ? GLY A 420 ASN A 439 1 ? 20 
HELX_P HELX_P8  AA8 GLN A 149 ? SER A 164 ? GLN A 441 SER A 456 1 ? 16 
HELX_P HELX_P9  AA9 THR A 173 ? ALA A 201 ? THR A 465 ALA A 493 1 ? 29 
HELX_P HELX_P10 AB1 THR A 204 ? SER A 235 ? THR A 496 SER A 527 1 ? 32 
HELX_P HELX_P11 AB2 SER A 245 ? ASP A 253 ? SER A 537 ASP A 545 1 ? 9  
HELX_P HELX_P12 AB3 LEU B 14  ? LEU B 18  ? LEU B 306 LEU B 310 5 ? 5  
HELX_P HELX_P13 AB4 THR B 19  ? ALA B 30  ? THR B 311 ALA B 322 1 ? 12 
HELX_P HELX_P14 AB5 SER B 49  ? ARG B 71  ? SER B 341 ARG B 363 1 ? 23 
HELX_P HELX_P15 AB6 THR B 79  ? SER B 103 ? THR B 371 SER B 395 1 ? 25 
HELX_P HELX_P16 AB7 ARG B 120 ? LYS B 124 ? ARG B 412 LYS B 416 1 ? 5  
HELX_P HELX_P17 AB8 GLY B 128 ? ASN B 147 ? GLY B 420 ASN B 439 1 ? 20 
HELX_P HELX_P18 AB9 GLN B 149 ? SER B 164 ? GLN B 441 SER B 456 1 ? 16 
HELX_P HELX_P19 AC1 GLU B 178 ? ALA B 201 ? GLU B 470 ALA B 493 1 ? 24 
HELX_P HELX_P20 AC2 THR B 204 ? TYR B 234 ? THR B 496 TYR B 526 1 ? 31 
HELX_P HELX_P21 AC3 PRO B 243 ? ASP B 253 ? PRO B 535 ASP B 545 1 ? 11 
# 
_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 ? 2 ? 
AA2 ? 2 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA2 1 2 ? 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 LYS A 109 ? ALA A 113 ? LYS A 401 ALA A 405 
AA1 2 LEU A 116 ? ASP A 119 ? LEU A 408 ASP A 411 
AA2 1 LYS B 109 ? ALA B 113 ? LYS B 401 ALA B 405 
AA2 2 LEU B 116 ? ASP B 119 ? LEU B 408 ASP B 411 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 N LEU A 110 ? N LEU A 402 O LEU A 118 ? O LEU A 410 
AA2 1 2 N LEU B 110 ? N LEU B 402 O LEU B 118 ? O LEU B 410 
# 
_pdbx_entry_details.entry_id                   9BPX 
_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_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 -3.3868  -16.1815 23.7159 0.2837 ? 0.1104  ? -0.0201 ? 0.1833 ? -0.0226 ? 0.2540 ? 5.5688 ? 
3.7576  ? -1.6082 ? 5.8774 ? -2.6756 ? 3.1099 ? 0.1035  ? 0.1867  ? 0.5449  ? -0.1357 ? 0.1707  ? 0.6655  ? -0.1332 ? -0.2174 ? 
-0.3206 ? 
2  'X-RAY DIFFRACTION' ? refined 0.3715   -22.9104 17.6258 0.1939 ? 0.0605  ? 0.0005  ? 0.2309 ? -0.0232 ? 0.2221 ? 3.4289 ? 
1.1316  ? -1.9894 ? 0.4955 ? -1.0431 ? 4.3317 ? -0.0355 ? 0.4964  ? 0.0028  ? -0.0465 ? -0.0087 ? 0.0373  ? 0.0016  ? -0.2853 ? 
0.0404  ? 
3  'X-RAY DIFFRACTION' ? refined -2.6670  -28.2828 37.1851 0.2804 ? 0.0431  ? 0.0319  ? 0.2612 ? 0.0349  ? 0.2440 ? 7.5929 ? 
-0.0327 ? 1.0008  ? 1.5275 ? 0.9427  ? 7.1805 ? 0.0526  ? -0.5605 ? -0.5393 ? 0.4932  ? 0.0814  ? 0.2052  ? 0.4744  ? -0.3001 ? 
-0.0660 ? 
4  'X-RAY DIFFRACTION' ? refined 9.5746   -22.7108 26.2047 0.1557 ? 0.0510  ? -0.0218 ? 0.1853 ? 0.0128  ? 0.2286 ? 2.2438 ? 
0.7592  ? -0.7742 ? 2.1700 ? -1.9462 ? 5.3230 ? -0.0194 ? -0.0049 ? -0.1027 ? -0.0363 ? -0.0349 ? -0.0333 ? 0.1747  ? 0.3183  ? 
0.0772  ? 
5  'X-RAY DIFFRACTION' ? refined 17.0373  -12.8915 15.2337 0.2914 ? 0.0001  ? -0.0002 ? 0.2160 ? 0.1064  ? 0.2811 ? 2.9037 ? 
1.1950  ? 1.1337  ? 4.1526 ? 3.2644  ? 2.2218 ? -0.0228 ? 0.3644  ? 0.3100  ? -0.2755 ? -0.0020 ? -0.1435 ? -0.5329 ? 0.1726  ? 
0.0537  ? 
6  'X-RAY DIFFRACTION' ? refined 13.7659  -25.4634 26.4970 0.2359 ? 0.0766  ? 0.0031  ? 0.1796 ? 0.0186  ? 0.2175 ? 7.6265 ? 
3.4642  ? 0.3063  ? 5.7412 ? 0.2994  ? 2.0256 ? -0.0682 ? -0.0704 ? -0.3991 ? -0.1395 ? -0.0697 ? -0.3278 ? 0.1128  ? 0.0554  ? 
0.1514  ? 
7  'X-RAY DIFFRACTION' ? refined -5.1230  -25.5501 8.2564  0.6188 ? -0.1661 ? -0.0413 ? 0.9444 ? -0.1898 ? 0.4342 ? 6.7977 ? 
-5.9540 ? 5.7441  ? 2.1501 ? -7.7597 ? 2.1716 ? 0.2293  ? 0.1031  ? -0.5760 ? 0.6377  ? -0.0173 ? 1.0139  ? 0.7411  ? -0.7876 ? 
-0.3322 ? 
8  'X-RAY DIFFRACTION' ? refined -13.0003 -12.5400 4.7115  0.5177 ? 0.2385  ? 0.3982  ? 1.5712 ? -0.4048 ? 1.5353 ? 2.0004 ? 
1.9997  ? -8.8167 ? 2.0000 ? 0.0668  ? 2.0002 ? 0.0345  ? -0.3746 ? 0.9017  ? 0.5554  ? 0.0291  ? 1.8800  ? -0.1721 ? 0.2977  ? 
-0.0983 ? 
9  'X-RAY DIFFRACTION' ? refined 38.3707  -32.1886 26.5943 0.1397 ? 0.0332  ? 0.0073  ? 0.3689 ? 0.0009  ? 0.3794 ? 4.8745 ? 
-0.0034 ? 2.0672  ? 7.7701 ? 1.6481  ? 4.8875 ? -0.1629 ? -0.0194 ? 0.5886  ? 0.2514  ? 0.0161  ? -0.4304 ? 0.0705  ? 0.4208  ? 
0.1519  ? 
10 'X-RAY DIFFRACTION' ? refined 31.5506  -56.7861 7.9844  0.8111 ? -0.0742 ? 0.0439  ? 0.6938 ? -0.2525 ? 0.9367 ? 1.1056 ? 
0.6299  ? -1.9047 ? 7.8541 ? -1.3075 ? 9.2015 ? 0.3289  ? 0.3140  ? -0.4679 ? -0.0190 ? 1.2046  ? -0.5996 ? 1.0579  ? 0.5046  ? 
-1.4935 ? 
11 'X-RAY DIFFRACTION' ? refined 31.6002  -41.3876 28.0777 0.2045 ? 0.0730  ? -0.0053 ? 0.2247 ? 0.0577  ? 0.2022 ? 3.7237 ? 
-0.7467 ? -0.1719 ? 7.1208 ? 2.1120  ? 5.1467 ? -0.0896 ? -0.1421 ? -0.3459 ? 0.5422  ? 0.3114  ? -0.3916 ? 0.2259  ? 0.4242  ? 
-0.1632 ? 
12 'X-RAY DIFFRACTION' ? refined 27.8956  -37.8807 21.5956 0.1718 ? 0.0801  ? -0.0103 ? 0.1880 ? 0.0188  ? 0.2126 ? 3.4062 ? 
-0.8980 ? 0.7669  ? 4.5924 ? 0.1985  ? 2.8378 ? 0.1911  ? 0.2996  ? 0.1120  ? -0.0776 ? 0.0097  ? -0.1476 ? 0.1683  ? 0.0712  ? 
-0.1320 ? 
13 'X-RAY DIFFRACTION' ? refined 22.7366  -45.9616 6.0234  0.6412 ? 0.1717  ? -0.0721 ? 0.9063 ? -0.2668 ? 0.4471 ? 6.4552 ? 
-3.4855 ? 0.9359  ? 3.1223 ? -1.2065 ? 1.2535 ? 0.4980  ? 1.0954  ? -0.4270 ? -0.9415 ? -0.5318 ? 0.7348  ? 1.1899  ? -0.6328 ? 
-0.0047 ? 
14 'X-RAY DIFFRACTION' ? refined 25.2642  -30.1369 19.0669 0.1693 ? 0.1127  ? 0.0134  ? 0.2463 ? 0.0283  ? 0.2387 ? 3.2821 ? 
0.2939  ? 1.5146  ? 5.6020 ? 1.7928  ? 5.1620 ? 0.1693  ? 0.3029  ? 0.0575  ? -0.1714 ? -0.0077 ? -0.1321 ? -0.1418 ? -0.0198 ? 
-0.1127 ? 
15 'X-RAY DIFFRACTION' ? refined 24.7580  -23.3076 24.4258 0.1009 ? 0.0504  ? 0.0081  ? 0.2226 ? -0.0023 ? 0.2086 ? 3.4163 ? 
0.7718  ? 0.3361  ? 6.2259 ? -0.8700 ? 2.8569 ? -0.0671 ? -0.0316 ? 0.2036  ? 0.1182  ? -0.0395 ? -0.2477 ? -0.2167 ? 0.1881  ? 
0.1112  ? 
16 'X-RAY DIFFRACTION' ? refined 23.8812  -48.8899 32.3275 0.5553 ? 0.0986  ? -0.0698 ? 0.4783 ? -0.1142 ? 0.4327 ? 2.2492 ? 
-2.7806 ? -0.8970 ? 6.6271 ? -3.9167 ? 9.7697 ? 0.6614  ? 1.3184  ? -0.7907 ? -1.2428 ? -0.3580 ? 0.6832  ? 0.5011  ? -0.6687 ? 
-0.4004 ? 
# 
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 306 through 341 )
;
2  'X-RAY DIFFRACTION' 2  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 342 through 394 )
;
3  'X-RAY DIFFRACTION' 3  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 395 through 420 )
;
4  'X-RAY DIFFRACTION' 4  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 421 through 465 )
;
5  'X-RAY DIFFRACTION' 5  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 466 through 496 )
;
6  'X-RAY DIFFRACTION' 6  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 497 through 526 )
;
7  'X-RAY DIFFRACTION' 7  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 527 through 549 )
;
8  'X-RAY DIFFRACTION' 8  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 550 through 550 )
;
9  'X-RAY DIFFRACTION' 9  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'B' and (resid 306 through 331 )
;
10 'X-RAY DIFFRACTION' 10 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'B' and (resid 332 through 341 )
;
11 'X-RAY DIFFRACTION' 11 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'B' and (resid 342 through 371 )
;
12 'X-RAY DIFFRACTION' 12 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'B' and (resid 372 through 407 )
;
13 'X-RAY DIFFRACTION' 13 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'B' and (resid 408 through 420 )
;
14 'X-RAY DIFFRACTION' 14 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'B' and (resid 421 through 469 )
;
15 'X-RAY DIFFRACTION' 15 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'B' and (resid 470 through 525 )
;
16 'X-RAY DIFFRACTION' 16 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'B' and (resid 526 through 546 )
;
# 
loop_
_pdbx_distant_solvent_atoms.id 
_pdbx_distant_solvent_atoms.PDB_model_num 
_pdbx_distant_solvent_atoms.auth_atom_id 
_pdbx_distant_solvent_atoms.label_alt_id 
_pdbx_distant_solvent_atoms.auth_asym_id 
_pdbx_distant_solvent_atoms.auth_comp_id 
_pdbx_distant_solvent_atoms.auth_seq_id 
_pdbx_distant_solvent_atoms.PDB_ins_code 
_pdbx_distant_solvent_atoms.neighbor_macromolecule_distance 
_pdbx_distant_solvent_atoms.neighbor_ligand_distance 
1 1 O ? A HOH 806 ? 6.44 . 
2 1 O ? B HOH 780 ? 7.48 . 
# 
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 HIS 293 ? A HIS 1   
2  1 Y 1 A HIS 294 ? A HIS 2   
3  1 Y 1 A HIS 295 ? A HIS 3   
4  1 Y 1 A HIS 296 ? A HIS 4   
5  1 Y 1 A HIS 297 ? A HIS 5   
6  1 Y 1 A HIS 298 ? A HIS 6   
7  1 Y 1 A GLU 299 ? A GLU 7   
8  1 Y 1 A ASN 300 ? A ASN 8   
9  1 Y 1 A LEU 301 ? A LEU 9   
10 1 Y 1 A TYR 302 ? A TYR 10  
11 1 Y 1 A PHE 303 ? A PHE 11  
12 1 Y 1 A GLN 304 ? A GLN 12  
13 1 Y 1 A SER 305 ? A SER 13  
14 1 Y 1 A LEU 462 ? A LEU 170 
15 1 Y 1 A SER 463 ? A SER 171 
16 1 Y 1 A LYS 529 ? A LYS 237 
17 1 Y 1 A SER 530 ? A SER 238 
18 1 Y 1 A LYS 531 ? A LYS 239 
19 1 Y 1 A ASN 532 ? A ASN 240 
20 1 Y 1 A VAL 533 ? A VAL 241 
21 1 Y 1 A VAL 534 ? A VAL 242 
22 1 Y 1 A PRO 535 ? A PRO 243 
23 1 Y 1 A HIS 550 ? A HIS 258 
24 1 Y 1 A ALA 551 ? A ALA 259 
25 1 Y 1 A PRO 552 ? A PRO 260 
26 1 Y 1 A THR 553 ? A THR 261 
27 1 Y 1 A SER 554 ? A SER 262 
28 1 Y 1 B HIS 293 ? B HIS 1   
29 1 Y 1 B HIS 294 ? B HIS 2   
30 1 Y 1 B HIS 295 ? B HIS 3   
31 1 Y 1 B HIS 296 ? B HIS 4   
32 1 Y 1 B HIS 297 ? B HIS 5   
33 1 Y 1 B HIS 298 ? B HIS 6   
34 1 Y 1 B GLU 299 ? B GLU 7   
35 1 Y 1 B ASN 300 ? B ASN 8   
36 1 Y 1 B LEU 301 ? B LEU 9   
37 1 Y 1 B TYR 302 ? B TYR 10  
38 1 Y 1 B PHE 303 ? B PHE 11  
39 1 Y 1 B GLN 304 ? B GLN 12  
40 1 Y 1 B SER 305 ? B SER 13  
41 1 Y 1 B THR 460 ? B THR 168 
42 1 Y 1 B PHE 461 ? B PHE 169 
43 1 Y 1 B LEU 462 ? B LEU 170 
44 1 Y 1 B SER 463 ? B SER 171 
45 1 Y 1 B SER 464 ? B SER 172 
46 1 Y 1 B THR 465 ? B THR 173 
47 1 Y 1 B LEU 466 ? B LEU 174 
48 1 Y 1 B LYS 467 ? B LYS 175 
49 1 Y 1 B SER 468 ? B SER 176 
50 1 Y 1 B MET 528 ? B MET 236 
51 1 Y 1 B LYS 529 ? B LYS 237 
52 1 Y 1 B SER 530 ? B SER 238 
53 1 Y 1 B LYS 531 ? B LYS 239 
54 1 Y 1 B ASN 532 ? B ASN 240 
55 1 Y 1 B HIS 547 ? B HIS 255 
56 1 Y 1 B ARG 548 ? B ARG 256 
57 1 Y 1 B LEU 549 ? B LEU 257 
58 1 Y 1 B HIS 550 ? B HIS 258 
59 1 Y 1 B ALA 551 ? B ALA 259 
60 1 Y 1 B PRO 552 ? B PRO 260 
61 1 Y 1 B THR 553 ? B THR 261 
62 1 Y 1 B SER 554 ? B SER 262 
# 
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 
A1BV9 N1   N N N 1   
A1BV9 C4   C Y N 2   
A1BV9 C5   C Y N 3   
A1BV9 C6   C Y N 4   
A1BV9 C7   C N N 5   
A1BV9 C8   C N N 6   
A1BV9 C10  C N N 7   
A1BV9 C13  C Y N 8   
A1BV9 C15  C Y N 9   
A1BV9 C17  C N N 10  
A1BV9 C20  C Y N 11  
A1BV9 C21  C Y N 12  
A1BV9 C22  C Y N 13  
A1BV9 C24  C Y N 14  
A1BV9 C26  C N S 15  
A1BV9 C28  C N N 16  
A1BV9 C1   C Y N 17  
A1BV9 C11  C Y N 18  
A1BV9 C12  C Y N 19  
A1BV9 C14  C Y N 20  
A1BV9 C16  C Y N 21  
A1BV9 C18  C N N 22  
A1BV9 C19  C Y N 23  
A1BV9 C2   C Y N 24  
A1BV9 C23  C Y N 25  
A1BV9 C25  C N N 26  
A1BV9 C27  C N N 27  
A1BV9 C29  C N N 28  
A1BV9 C3   C Y N 29  
A1BV9 C30  C N N 30  
A1BV9 C31  C N N 31  
A1BV9 C32  C N N 32  
A1BV9 C9   C N R 33  
A1BV9 F1   F N N 34  
A1BV9 N2   N N N 35  
A1BV9 O1   O N N 36  
A1BV9 O2   O N N 37  
A1BV9 O3   O N N 38  
A1BV9 H1   H N N 39  
A1BV9 H2   H N N 40  
A1BV9 H3   H N N 41  
A1BV9 H4   H N N 42  
A1BV9 H5   H N N 43  
A1BV9 H6   H N N 44  
A1BV9 H7   H N N 45  
A1BV9 H8   H N N 46  
A1BV9 H9   H N N 47  
A1BV9 H10  H N N 48  
A1BV9 H11  H N N 49  
A1BV9 H12  H N N 50  
A1BV9 H13  H N N 51  
A1BV9 H14  H N N 52  
A1BV9 H15  H N N 53  
A1BV9 H16  H N N 54  
A1BV9 H17  H N N 55  
A1BV9 H18  H N N 56  
A1BV9 H19  H N N 57  
A1BV9 H20  H N N 58  
A1BV9 H21  H N N 59  
A1BV9 H22  H N N 60  
A1BV9 H23  H N N 61  
A1BV9 H24  H N N 62  
A1BV9 H25  H N N 63  
A1BV9 H26  H N N 64  
A1BV9 H27  H N N 65  
A1BV9 H28  H N N 66  
A1BV9 H29  H N N 67  
A1BV9 H30  H N N 68  
A1BV9 H31  H N N 69  
A1BV9 H32  H N N 70  
A1BV9 H33  H N N 71  
ALA   N    N N N 72  
ALA   CA   C N S 73  
ALA   C    C N N 74  
ALA   O    O N N 75  
ALA   CB   C N N 76  
ALA   OXT  O N N 77  
ALA   H    H N N 78  
ALA   H2   H N N 79  
ALA   HA   H N N 80  
ALA   HB1  H N N 81  
ALA   HB2  H N N 82  
ALA   HB3  H N N 83  
ALA   HXT  H N N 84  
ARG   N    N N N 85  
ARG   CA   C N S 86  
ARG   C    C N N 87  
ARG   O    O N N 88  
ARG   CB   C N N 89  
ARG   CG   C N N 90  
ARG   CD   C N N 91  
ARG   NE   N N N 92  
ARG   CZ   C N N 93  
ARG   NH1  N N N 94  
ARG   NH2  N N N 95  
ARG   OXT  O N N 96  
ARG   H    H N N 97  
ARG   H2   H N N 98  
ARG   HA   H N N 99  
ARG   HB2  H N N 100 
ARG   HB3  H N N 101 
ARG   HG2  H N N 102 
ARG   HG3  H N N 103 
ARG   HD2  H N N 104 
ARG   HD3  H N N 105 
ARG   HE   H N N 106 
ARG   HH11 H N N 107 
ARG   HH12 H N N 108 
ARG   HH21 H N N 109 
ARG   HH22 H N N 110 
ARG   HXT  H N N 111 
ASN   N    N N N 112 
ASN   CA   C N S 113 
ASN   C    C N N 114 
ASN   O    O N N 115 
ASN   CB   C N N 116 
ASN   CG   C N N 117 
ASN   OD1  O N N 118 
ASN   ND2  N N N 119 
ASN   OXT  O N N 120 
ASN   H    H N N 121 
ASN   H2   H N N 122 
ASN   HA   H N N 123 
ASN   HB2  H N N 124 
ASN   HB3  H N N 125 
ASN   HD21 H N N 126 
ASN   HD22 H N N 127 
ASN   HXT  H N N 128 
ASP   N    N N N 129 
ASP   CA   C N S 130 
ASP   C    C N N 131 
ASP   O    O N N 132 
ASP   CB   C N N 133 
ASP   CG   C N N 134 
ASP   OD1  O N N 135 
ASP   OD2  O N N 136 
ASP   OXT  O N N 137 
ASP   H    H N N 138 
ASP   H2   H N N 139 
ASP   HA   H N N 140 
ASP   HB2  H N N 141 
ASP   HB3  H N N 142 
ASP   HD2  H N N 143 
ASP   HXT  H N N 144 
CYS   N    N N N 145 
CYS   CA   C N R 146 
CYS   C    C N N 147 
CYS   O    O N N 148 
CYS   CB   C N N 149 
CYS   SG   S N N 150 
CYS   OXT  O N N 151 
CYS   H    H N N 152 
CYS   H2   H N N 153 
CYS   HA   H N N 154 
CYS   HB2  H N N 155 
CYS   HB3  H N N 156 
CYS   HG   H N N 157 
CYS   HXT  H N N 158 
GLN   N    N N N 159 
GLN   CA   C N S 160 
GLN   C    C N N 161 
GLN   O    O N N 162 
GLN   CB   C N N 163 
GLN   CG   C N N 164 
GLN   CD   C N N 165 
GLN   OE1  O N N 166 
GLN   NE2  N N N 167 
GLN   OXT  O N N 168 
GLN   H    H N N 169 
GLN   H2   H N N 170 
GLN   HA   H N N 171 
GLN   HB2  H N N 172 
GLN   HB3  H N N 173 
GLN   HG2  H N N 174 
GLN   HG3  H N N 175 
GLN   HE21 H N N 176 
GLN   HE22 H N N 177 
GLN   HXT  H N N 178 
GLU   N    N N N 179 
GLU   CA   C N S 180 
GLU   C    C N N 181 
GLU   O    O N N 182 
GLU   CB   C N N 183 
GLU   CG   C N N 184 
GLU   CD   C N N 185 
GLU   OE1  O N N 186 
GLU   OE2  O N N 187 
GLU   OXT  O N N 188 
GLU   H    H N N 189 
GLU   H2   H N N 190 
GLU   HA   H N N 191 
GLU   HB2  H N N 192 
GLU   HB3  H N N 193 
GLU   HG2  H N N 194 
GLU   HG3  H N N 195 
GLU   HE2  H N N 196 
GLU   HXT  H N N 197 
GLY   N    N N N 198 
GLY   CA   C N N 199 
GLY   C    C N N 200 
GLY   O    O N N 201 
GLY   OXT  O N N 202 
GLY   H    H N N 203 
GLY   H2   H N N 204 
GLY   HA2  H N N 205 
GLY   HA3  H N N 206 
GLY   HXT  H N N 207 
HIS   N    N N N 208 
HIS   CA   C N S 209 
HIS   C    C N N 210 
HIS   O    O N N 211 
HIS   CB   C N N 212 
HIS   CG   C Y N 213 
HIS   ND1  N Y N 214 
HIS   CD2  C Y N 215 
HIS   CE1  C Y N 216 
HIS   NE2  N Y N 217 
HIS   OXT  O N N 218 
HIS   H    H N N 219 
HIS   H2   H N N 220 
HIS   HA   H N N 221 
HIS   HB2  H N N 222 
HIS   HB3  H N N 223 
HIS   HD1  H N N 224 
HIS   HD2  H N N 225 
HIS   HE1  H N N 226 
HIS   HE2  H N N 227 
HIS   HXT  H N N 228 
HOH   O    O N N 229 
HOH   H1   H N N 230 
HOH   H2   H N N 231 
ILE   N    N N N 232 
ILE   CA   C N S 233 
ILE   C    C N N 234 
ILE   O    O N N 235 
ILE   CB   C N S 236 
ILE   CG1  C N N 237 
ILE   CG2  C N N 238 
ILE   CD1  C N N 239 
ILE   OXT  O N N 240 
ILE   H    H N N 241 
ILE   H2   H N N 242 
ILE   HA   H N N 243 
ILE   HB   H N N 244 
ILE   HG12 H N N 245 
ILE   HG13 H N N 246 
ILE   HG21 H N N 247 
ILE   HG22 H N N 248 
ILE   HG23 H N N 249 
ILE   HD11 H N N 250 
ILE   HD12 H N N 251 
ILE   HD13 H N N 252 
ILE   HXT  H N N 253 
LEU   N    N N N 254 
LEU   CA   C N S 255 
LEU   C    C N N 256 
LEU   O    O N N 257 
LEU   CB   C N N 258 
LEU   CG   C N N 259 
LEU   CD1  C N N 260 
LEU   CD2  C N N 261 
LEU   OXT  O N N 262 
LEU   H    H N N 263 
LEU   H2   H N N 264 
LEU   HA   H N N 265 
LEU   HB2  H N N 266 
LEU   HB3  H N N 267 
LEU   HG   H N N 268 
LEU   HD11 H N N 269 
LEU   HD12 H N N 270 
LEU   HD13 H N N 271 
LEU   HD21 H N N 272 
LEU   HD22 H N N 273 
LEU   HD23 H N N 274 
LEU   HXT  H N N 275 
LYS   N    N N N 276 
LYS   CA   C N S 277 
LYS   C    C N N 278 
LYS   O    O N N 279 
LYS   CB   C N N 280 
LYS   CG   C N N 281 
LYS   CD   C N N 282 
LYS   CE   C N N 283 
LYS   NZ   N N N 284 
LYS   OXT  O N N 285 
LYS   H    H N N 286 
LYS   H2   H N N 287 
LYS   HA   H N N 288 
LYS   HB2  H N N 289 
LYS   HB3  H N N 290 
LYS   HG2  H N N 291 
LYS   HG3  H N N 292 
LYS   HD2  H N N 293 
LYS   HD3  H N N 294 
LYS   HE2  H N N 295 
LYS   HE3  H N N 296 
LYS   HZ1  H N N 297 
LYS   HZ2  H N N 298 
LYS   HZ3  H N N 299 
LYS   HXT  H N N 300 
MET   N    N N N 301 
MET   CA   C N S 302 
MET   C    C N N 303 
MET   O    O N N 304 
MET   CB   C N N 305 
MET   CG   C N N 306 
MET   SD   S N N 307 
MET   CE   C N N 308 
MET   OXT  O N N 309 
MET   H    H N N 310 
MET   H2   H N N 311 
MET   HA   H N N 312 
MET   HB2  H N N 313 
MET   HB3  H N N 314 
MET   HG2  H N N 315 
MET   HG3  H N N 316 
MET   HE1  H N N 317 
MET   HE2  H N N 318 
MET   HE3  H N N 319 
MET   HXT  H N N 320 
PHE   N    N N N 321 
PHE   CA   C N S 322 
PHE   C    C N N 323 
PHE   O    O N N 324 
PHE   CB   C N N 325 
PHE   CG   C Y N 326 
PHE   CD1  C Y N 327 
PHE   CD2  C Y N 328 
PHE   CE1  C Y N 329 
PHE   CE2  C Y N 330 
PHE   CZ   C Y N 331 
PHE   OXT  O N N 332 
PHE   H    H N N 333 
PHE   H2   H N N 334 
PHE   HA   H N N 335 
PHE   HB2  H N N 336 
PHE   HB3  H N N 337 
PHE   HD1  H N N 338 
PHE   HD2  H N N 339 
PHE   HE1  H N N 340 
PHE   HE2  H N N 341 
PHE   HZ   H N N 342 
PHE   HXT  H N N 343 
PRO   N    N N N 344 
PRO   CA   C N S 345 
PRO   C    C N N 346 
PRO   O    O N N 347 
PRO   CB   C N N 348 
PRO   CG   C N N 349 
PRO   CD   C N N 350 
PRO   OXT  O N N 351 
PRO   H    H N N 352 
PRO   HA   H N N 353 
PRO   HB2  H N N 354 
PRO   HB3  H N N 355 
PRO   HG2  H N N 356 
PRO   HG3  H N N 357 
PRO   HD2  H N N 358 
PRO   HD3  H N N 359 
PRO   HXT  H N N 360 
SER   N    N N N 361 
SER   CA   C N S 362 
SER   C    C N N 363 
SER   O    O N N 364 
SER   CB   C N N 365 
SER   OG   O N N 366 
SER   OXT  O N N 367 
SER   H    H N N 368 
SER   H2   H N N 369 
SER   HA   H N N 370 
SER   HB2  H N N 371 
SER   HB3  H N N 372 
SER   HG   H N N 373 
SER   HXT  H N N 374 
THR   N    N N N 375 
THR   CA   C N S 376 
THR   C    C N N 377 
THR   O    O N N 378 
THR   CB   C N R 379 
THR   OG1  O N N 380 
THR   CG2  C N N 381 
THR   OXT  O N N 382 
THR   H    H N N 383 
THR   H2   H N N 384 
THR   HA   H N N 385 
THR   HB   H N N 386 
THR   HG1  H N N 387 
THR   HG21 H N N 388 
THR   HG22 H N N 389 
THR   HG23 H N N 390 
THR   HXT  H N N 391 
TRP   N    N N N 392 
TRP   CA   C N S 393 
TRP   C    C N N 394 
TRP   O    O N N 395 
TRP   CB   C N N 396 
TRP   CG   C Y N 397 
TRP   CD1  C Y N 398 
TRP   CD2  C Y N 399 
TRP   NE1  N Y N 400 
TRP   CE2  C Y N 401 
TRP   CE3  C Y N 402 
TRP   CZ2  C Y N 403 
TRP   CZ3  C Y N 404 
TRP   CH2  C Y N 405 
TRP   OXT  O N N 406 
TRP   H    H N N 407 
TRP   H2   H N N 408 
TRP   HA   H N N 409 
TRP   HB2  H N N 410 
TRP   HB3  H N N 411 
TRP   HD1  H N N 412 
TRP   HE1  H N N 413 
TRP   HE3  H N N 414 
TRP   HZ2  H N N 415 
TRP   HZ3  H N N 416 
TRP   HH2  H N N 417 
TRP   HXT  H N N 418 
TYR   N    N N N 419 
TYR   CA   C N S 420 
TYR   C    C N N 421 
TYR   O    O N N 422 
TYR   CB   C N N 423 
TYR   CG   C Y N 424 
TYR   CD1  C Y N 425 
TYR   CD2  C Y N 426 
TYR   CE1  C Y N 427 
TYR   CE2  C Y N 428 
TYR   CZ   C Y N 429 
TYR   OH   O N N 430 
TYR   OXT  O N N 431 
TYR   H    H N N 432 
TYR   H2   H N N 433 
TYR   HA   H N N 434 
TYR   HB2  H N N 435 
TYR   HB3  H N N 436 
TYR   HD1  H N N 437 
TYR   HD2  H N N 438 
TYR   HE1  H N N 439 
TYR   HE2  H N N 440 
TYR   HH   H N N 441 
TYR   HXT  H N N 442 
TZI   N1   N N N 443 
TZI   C4   C Y N 444 
TZI   C5   C Y N 445 
TZI   C6   C Y N 446 
TZI   C7   C N N 447 
TZI   C8   C N N 448 
TZI   C10  C N N 449 
TZI   C13  C Y N 450 
TZI   C15  C Y N 451 
TZI   C17  C N N 452 
TZI   C20  C Y N 453 
TZI   C21  C Y N 454 
TZI   C22  C Y N 455 
TZI   C24  C Y N 456 
TZI   C26  C N R 457 
TZI   C28  C N N 458 
TZI   C1   C Y N 459 
TZI   C11  C Y N 460 
TZI   C12  C Y N 461 
TZI   C14  C Y N 462 
TZI   C16  C Y N 463 
TZI   C18  C N N 464 
TZI   C19  C Y N 465 
TZI   C2   C Y N 466 
TZI   C23  C Y N 467 
TZI   C25  C N N 468 
TZI   C27  C N N 469 
TZI   C29  C N N 470 
TZI   C3   C Y N 471 
TZI   C30  C N N 472 
TZI   C31  C N N 473 
TZI   C32  C N N 474 
TZI   C9   C N R 475 
TZI   F1   F N N 476 
TZI   N2   N N N 477 
TZI   O1   O N N 478 
TZI   O2   O N N 479 
TZI   O3   O N N 480 
TZI   H1   H N N 481 
TZI   H2   H N N 482 
TZI   H3   H N N 483 
TZI   H4   H N N 484 
TZI   H5   H N N 485 
TZI   H6   H N N 486 
TZI   H7   H N N 487 
TZI   H8   H N N 488 
TZI   H9   H N N 489 
TZI   H10  H N N 490 
TZI   H11  H N N 491 
TZI   H12  H N N 492 
TZI   H13  H N N 493 
TZI   H14  H N N 494 
TZI   H15  H N N 495 
TZI   H16  H N N 496 
TZI   H17  H N N 497 
TZI   H18  H N N 498 
TZI   H19  H N N 499 
TZI   H20  H N N 500 
TZI   H21  H N N 501 
TZI   H22  H N N 502 
TZI   H23  H N N 503 
TZI   H24  H N N 504 
TZI   H25  H N N 505 
TZI   H26  H N N 506 
TZI   H27  H N N 507 
TZI   H28  H N N 508 
TZI   H29  H N N 509 
TZI   H30  H N N 510 
TZI   H31  H N N 511 
TZI   H32  H N N 512 
TZI   H33  H N N 513 
TZI   H34  H N N 514 
TZI   H36  H N N 515 
VAL   N    N N N 516 
VAL   CA   C N S 517 
VAL   C    C N N 518 
VAL   O    O N N 519 
VAL   CB   C N N 520 
VAL   CG1  C N N 521 
VAL   CG2  C N N 522 
VAL   OXT  O N N 523 
VAL   H    H N N 524 
VAL   H2   H N N 525 
VAL   HA   H N N 526 
VAL   HB   H N N 527 
VAL   HG11 H N N 528 
VAL   HG12 H N N 529 
VAL   HG13 H N N 530 
VAL   HG21 H N N 531 
VAL   HG22 H N N 532 
VAL   HG23 H N N 533 
VAL   HXT  H N N 534 
# 
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 
A1BV9 C15 C14  doub Y N 1   
A1BV9 C15 C16  sing Y N 2   
A1BV9 C14 C13  sing Y N 3   
A1BV9 C16 C11  doub Y N 4   
A1BV9 C13 C12  doub Y N 5   
A1BV9 C11 C12  sing Y N 6   
A1BV9 C11 C10  sing N N 7   
A1BV9 O1  C10  doub N N 8   
A1BV9 C10 N1   sing N N 9   
A1BV9 N1  C8   sing N N 10  
A1BV9 N1  C9   sing N N 11  
A1BV9 C18 C8   sing N N 12  
A1BV9 C18 C17  sing N N 13  
A1BV9 C8  C7   sing N N 14  
A1BV9 C8  C17  sing N N 15  
A1BV9 C7  C5   sing N N 16  
A1BV9 C9  C6   sing N N 17  
A1BV9 C9  C19  sing N N 18  
A1BV9 C5  C6   doub Y N 19  
A1BV9 C5  C4   sing Y N 20  
A1BV9 C6  C1   sing Y N 21  
A1BV9 C4  C3   doub Y N 22  
A1BV9 C1  C2   doub Y N 23  
A1BV9 C3  C2   sing Y N 24  
A1BV9 C3  O2   sing N N 25  
A1BV9 C19 C24  doub Y N 26  
A1BV9 C19 C20  sing Y N 27  
A1BV9 C24 C23  sing Y N 28  
A1BV9 C20 C21  doub Y N 29  
A1BV9 C23 C22  doub Y N 30  
A1BV9 C21 C22  sing Y N 31  
A1BV9 C22 O3   sing N N 32  
A1BV9 O3  C25  sing N N 33  
A1BV9 C25 C26  sing N N 34  
A1BV9 C26 C27  sing N N 35  
A1BV9 C26 C29  sing N N 36  
A1BV9 C27 C28  doub N N 37  
A1BV9 C29 N2   sing N N 38  
A1BV9 C28 N2   sing N N 39  
A1BV9 N2  C30  sing N N 40  
A1BV9 C30 C31  sing N N 41  
A1BV9 F1  C32  sing N N 42  
A1BV9 C32 C31  sing N N 43  
A1BV9 C4  H1   sing N N 44  
A1BV9 C7  H2   sing N N 45  
A1BV9 C7  H3   sing N N 46  
A1BV9 C13 H4   sing N N 47  
A1BV9 C15 H5   sing N N 48  
A1BV9 C17 H6   sing N N 49  
A1BV9 C17 H7   sing N N 50  
A1BV9 C20 H8   sing N N 51  
A1BV9 C21 H9   sing N N 52  
A1BV9 C24 H10  sing N N 53  
A1BV9 C26 H11  sing N N 54  
A1BV9 C28 H12  sing N N 55  
A1BV9 C1  H13  sing N N 56  
A1BV9 C12 H14  sing N N 57  
A1BV9 C14 H15  sing N N 58  
A1BV9 C16 H16  sing N N 59  
A1BV9 C18 H17  sing N N 60  
A1BV9 C18 H18  sing N N 61  
A1BV9 C2  H19  sing N N 62  
A1BV9 C23 H20  sing N N 63  
A1BV9 C25 H21  sing N N 64  
A1BV9 C25 H22  sing N N 65  
A1BV9 C27 H23  sing N N 66  
A1BV9 C29 H24  sing N N 67  
A1BV9 C29 H25  sing N N 68  
A1BV9 C30 H26  sing N N 69  
A1BV9 C30 H27  sing N N 70  
A1BV9 C31 H28  sing N N 71  
A1BV9 C31 H29  sing N N 72  
A1BV9 C32 H30  sing N N 73  
A1BV9 C32 H31  sing N N 74  
A1BV9 C9  H32  sing N N 75  
A1BV9 O2  H33  sing N N 76  
ALA   N   CA   sing N N 77  
ALA   N   H    sing N N 78  
ALA   N   H2   sing N N 79  
ALA   CA  C    sing N N 80  
ALA   CA  CB   sing N N 81  
ALA   CA  HA   sing N N 82  
ALA   C   O    doub N N 83  
ALA   C   OXT  sing N N 84  
ALA   CB  HB1  sing N N 85  
ALA   CB  HB2  sing N N 86  
ALA   CB  HB3  sing N N 87  
ALA   OXT HXT  sing N N 88  
ARG   N   CA   sing N N 89  
ARG   N   H    sing N N 90  
ARG   N   H2   sing N N 91  
ARG   CA  C    sing N N 92  
ARG   CA  CB   sing N N 93  
ARG   CA  HA   sing N N 94  
ARG   C   O    doub N N 95  
ARG   C   OXT  sing N N 96  
ARG   CB  CG   sing N N 97  
ARG   CB  HB2  sing N N 98  
ARG   CB  HB3  sing N N 99  
ARG   CG  CD   sing N N 100 
ARG   CG  HG2  sing N N 101 
ARG   CG  HG3  sing N N 102 
ARG   CD  NE   sing N N 103 
ARG   CD  HD2  sing N N 104 
ARG   CD  HD3  sing N N 105 
ARG   NE  CZ   sing N N 106 
ARG   NE  HE   sing N N 107 
ARG   CZ  NH1  sing N N 108 
ARG   CZ  NH2  doub N N 109 
ARG   NH1 HH11 sing N N 110 
ARG   NH1 HH12 sing N N 111 
ARG   NH2 HH21 sing N N 112 
ARG   NH2 HH22 sing N N 113 
ARG   OXT HXT  sing N N 114 
ASN   N   CA   sing N N 115 
ASN   N   H    sing N N 116 
ASN   N   H2   sing N N 117 
ASN   CA  C    sing N N 118 
ASN   CA  CB   sing N N 119 
ASN   CA  HA   sing N N 120 
ASN   C   O    doub N N 121 
ASN   C   OXT  sing N N 122 
ASN   CB  CG   sing N N 123 
ASN   CB  HB2  sing N N 124 
ASN   CB  HB3  sing N N 125 
ASN   CG  OD1  doub N N 126 
ASN   CG  ND2  sing N N 127 
ASN   ND2 HD21 sing N N 128 
ASN   ND2 HD22 sing N N 129 
ASN   OXT HXT  sing N N 130 
ASP   N   CA   sing N N 131 
ASP   N   H    sing N N 132 
ASP   N   H2   sing N N 133 
ASP   CA  C    sing N N 134 
ASP   CA  CB   sing N N 135 
ASP   CA  HA   sing N N 136 
ASP   C   O    doub N N 137 
ASP   C   OXT  sing N N 138 
ASP   CB  CG   sing N N 139 
ASP   CB  HB2  sing N N 140 
ASP   CB  HB3  sing N N 141 
ASP   CG  OD1  doub N N 142 
ASP   CG  OD2  sing N N 143 
ASP   OD2 HD2  sing N N 144 
ASP   OXT HXT  sing N N 145 
CYS   N   CA   sing N N 146 
CYS   N   H    sing N N 147 
CYS   N   H2   sing N N 148 
CYS   CA  C    sing N N 149 
CYS   CA  CB   sing N N 150 
CYS   CA  HA   sing N N 151 
CYS   C   O    doub N N 152 
CYS   C   OXT  sing N N 153 
CYS   CB  SG   sing N N 154 
CYS   CB  HB2  sing N N 155 
CYS   CB  HB3  sing N N 156 
CYS   SG  HG   sing N N 157 
CYS   OXT HXT  sing N N 158 
GLN   N   CA   sing N N 159 
GLN   N   H    sing N N 160 
GLN   N   H2   sing N N 161 
GLN   CA  C    sing N N 162 
GLN   CA  CB   sing N N 163 
GLN   CA  HA   sing N N 164 
GLN   C   O    doub N N 165 
GLN   C   OXT  sing N N 166 
GLN   CB  CG   sing N N 167 
GLN   CB  HB2  sing N N 168 
GLN   CB  HB3  sing N N 169 
GLN   CG  CD   sing N N 170 
GLN   CG  HG2  sing N N 171 
GLN   CG  HG3  sing N N 172 
GLN   CD  OE1  doub N N 173 
GLN   CD  NE2  sing N N 174 
GLN   NE2 HE21 sing N N 175 
GLN   NE2 HE22 sing N N 176 
GLN   OXT HXT  sing N N 177 
GLU   N   CA   sing N N 178 
GLU   N   H    sing N N 179 
GLU   N   H2   sing N N 180 
GLU   CA  C    sing N N 181 
GLU   CA  CB   sing N N 182 
GLU   CA  HA   sing N N 183 
GLU   C   O    doub N N 184 
GLU   C   OXT  sing N N 185 
GLU   CB  CG   sing N N 186 
GLU   CB  HB2  sing N N 187 
GLU   CB  HB3  sing N N 188 
GLU   CG  CD   sing N N 189 
GLU   CG  HG2  sing N N 190 
GLU   CG  HG3  sing N N 191 
GLU   CD  OE1  doub N N 192 
GLU   CD  OE2  sing N N 193 
GLU   OE2 HE2  sing N N 194 
GLU   OXT HXT  sing N N 195 
GLY   N   CA   sing N N 196 
GLY   N   H    sing N N 197 
GLY   N   H2   sing N N 198 
GLY   CA  C    sing N N 199 
GLY   CA  HA2  sing N N 200 
GLY   CA  HA3  sing N N 201 
GLY   C   O    doub N N 202 
GLY   C   OXT  sing N N 203 
GLY   OXT HXT  sing N N 204 
HIS   N   CA   sing N N 205 
HIS   N   H    sing N N 206 
HIS   N   H2   sing N N 207 
HIS   CA  C    sing N N 208 
HIS   CA  CB   sing N N 209 
HIS   CA  HA   sing N N 210 
HIS   C   O    doub N N 211 
HIS   C   OXT  sing N N 212 
HIS   CB  CG   sing N N 213 
HIS   CB  HB2  sing N N 214 
HIS   CB  HB3  sing N N 215 
HIS   CG  ND1  sing Y N 216 
HIS   CG  CD2  doub Y N 217 
HIS   ND1 CE1  doub Y N 218 
HIS   ND1 HD1  sing N N 219 
HIS   CD2 NE2  sing Y N 220 
HIS   CD2 HD2  sing N N 221 
HIS   CE1 NE2  sing Y N 222 
HIS   CE1 HE1  sing N N 223 
HIS   NE2 HE2  sing N N 224 
HIS   OXT HXT  sing N N 225 
HOH   O   H1   sing N N 226 
HOH   O   H2   sing N N 227 
ILE   N   CA   sing N N 228 
ILE   N   H    sing N N 229 
ILE   N   H2   sing N N 230 
ILE   CA  C    sing N N 231 
ILE   CA  CB   sing N N 232 
ILE   CA  HA   sing N N 233 
ILE   C   O    doub N N 234 
ILE   C   OXT  sing N N 235 
ILE   CB  CG1  sing N N 236 
ILE   CB  CG2  sing N N 237 
ILE   CB  HB   sing N N 238 
ILE   CG1 CD1  sing N N 239 
ILE   CG1 HG12 sing N N 240 
ILE   CG1 HG13 sing N N 241 
ILE   CG2 HG21 sing N N 242 
ILE   CG2 HG22 sing N N 243 
ILE   CG2 HG23 sing N N 244 
ILE   CD1 HD11 sing N N 245 
ILE   CD1 HD12 sing N N 246 
ILE   CD1 HD13 sing N N 247 
ILE   OXT HXT  sing N N 248 
LEU   N   CA   sing N N 249 
LEU   N   H    sing N N 250 
LEU   N   H2   sing N N 251 
LEU   CA  C    sing N N 252 
LEU   CA  CB   sing N N 253 
LEU   CA  HA   sing N N 254 
LEU   C   O    doub N N 255 
LEU   C   OXT  sing N N 256 
LEU   CB  CG   sing N N 257 
LEU   CB  HB2  sing N N 258 
LEU   CB  HB3  sing N N 259 
LEU   CG  CD1  sing N N 260 
LEU   CG  CD2  sing N N 261 
LEU   CG  HG   sing N N 262 
LEU   CD1 HD11 sing N N 263 
LEU   CD1 HD12 sing N N 264 
LEU   CD1 HD13 sing N N 265 
LEU   CD2 HD21 sing N N 266 
LEU   CD2 HD22 sing N N 267 
LEU   CD2 HD23 sing N N 268 
LEU   OXT HXT  sing N N 269 
LYS   N   CA   sing N N 270 
LYS   N   H    sing N N 271 
LYS   N   H2   sing N N 272 
LYS   CA  C    sing N N 273 
LYS   CA  CB   sing N N 274 
LYS   CA  HA   sing N N 275 
LYS   C   O    doub N N 276 
LYS   C   OXT  sing N N 277 
LYS   CB  CG   sing N N 278 
LYS   CB  HB2  sing N N 279 
LYS   CB  HB3  sing N N 280 
LYS   CG  CD   sing N N 281 
LYS   CG  HG2  sing N N 282 
LYS   CG  HG3  sing N N 283 
LYS   CD  CE   sing N N 284 
LYS   CD  HD2  sing N N 285 
LYS   CD  HD3  sing N N 286 
LYS   CE  NZ   sing N N 287 
LYS   CE  HE2  sing N N 288 
LYS   CE  HE3  sing N N 289 
LYS   NZ  HZ1  sing N N 290 
LYS   NZ  HZ2  sing N N 291 
LYS   NZ  HZ3  sing N N 292 
LYS   OXT HXT  sing N N 293 
MET   N   CA   sing N N 294 
MET   N   H    sing N N 295 
MET   N   H2   sing N N 296 
MET   CA  C    sing N N 297 
MET   CA  CB   sing N N 298 
MET   CA  HA   sing N N 299 
MET   C   O    doub N N 300 
MET   C   OXT  sing N N 301 
MET   CB  CG   sing N N 302 
MET   CB  HB2  sing N N 303 
MET   CB  HB3  sing N N 304 
MET   CG  SD   sing N N 305 
MET   CG  HG2  sing N N 306 
MET   CG  HG3  sing N N 307 
MET   SD  CE   sing N N 308 
MET   CE  HE1  sing N N 309 
MET   CE  HE2  sing N N 310 
MET   CE  HE3  sing N N 311 
MET   OXT HXT  sing N N 312 
PHE   N   CA   sing N N 313 
PHE   N   H    sing N N 314 
PHE   N   H2   sing N N 315 
PHE   CA  C    sing N N 316 
PHE   CA  CB   sing N N 317 
PHE   CA  HA   sing N N 318 
PHE   C   O    doub N N 319 
PHE   C   OXT  sing N N 320 
PHE   CB  CG   sing N N 321 
PHE   CB  HB2  sing N N 322 
PHE   CB  HB3  sing N N 323 
PHE   CG  CD1  doub Y N 324 
PHE   CG  CD2  sing Y N 325 
PHE   CD1 CE1  sing Y N 326 
PHE   CD1 HD1  sing N N 327 
PHE   CD2 CE2  doub Y N 328 
PHE   CD2 HD2  sing N N 329 
PHE   CE1 CZ   doub Y N 330 
PHE   CE1 HE1  sing N N 331 
PHE   CE2 CZ   sing Y N 332 
PHE   CE2 HE2  sing N N 333 
PHE   CZ  HZ   sing N N 334 
PHE   OXT HXT  sing N N 335 
PRO   N   CA   sing N N 336 
PRO   N   CD   sing N N 337 
PRO   N   H    sing N N 338 
PRO   CA  C    sing N N 339 
PRO   CA  CB   sing N N 340 
PRO   CA  HA   sing N N 341 
PRO   C   O    doub N N 342 
PRO   C   OXT  sing N N 343 
PRO   CB  CG   sing N N 344 
PRO   CB  HB2  sing N N 345 
PRO   CB  HB3  sing N N 346 
PRO   CG  CD   sing N N 347 
PRO   CG  HG2  sing N N 348 
PRO   CG  HG3  sing N N 349 
PRO   CD  HD2  sing N N 350 
PRO   CD  HD3  sing N N 351 
PRO   OXT HXT  sing N N 352 
SER   N   CA   sing N N 353 
SER   N   H    sing N N 354 
SER   N   H2   sing N N 355 
SER   CA  C    sing N N 356 
SER   CA  CB   sing N N 357 
SER   CA  HA   sing N N 358 
SER   C   O    doub N N 359 
SER   C   OXT  sing N N 360 
SER   CB  OG   sing N N 361 
SER   CB  HB2  sing N N 362 
SER   CB  HB3  sing N N 363 
SER   OG  HG   sing N N 364 
SER   OXT HXT  sing N N 365 
THR   N   CA   sing N N 366 
THR   N   H    sing N N 367 
THR   N   H2   sing N N 368 
THR   CA  C    sing N N 369 
THR   CA  CB   sing N N 370 
THR   CA  HA   sing N N 371 
THR   C   O    doub N N 372 
THR   C   OXT  sing N N 373 
THR   CB  OG1  sing N N 374 
THR   CB  CG2  sing N N 375 
THR   CB  HB   sing N N 376 
THR   OG1 HG1  sing N N 377 
THR   CG2 HG21 sing N N 378 
THR   CG2 HG22 sing N N 379 
THR   CG2 HG23 sing N N 380 
THR   OXT HXT  sing N N 381 
TRP   N   CA   sing N N 382 
TRP   N   H    sing N N 383 
TRP   N   H2   sing N N 384 
TRP   CA  C    sing N N 385 
TRP   CA  CB   sing N N 386 
TRP   CA  HA   sing N N 387 
TRP   C   O    doub N N 388 
TRP   C   OXT  sing N N 389 
TRP   CB  CG   sing N N 390 
TRP   CB  HB2  sing N N 391 
TRP   CB  HB3  sing N N 392 
TRP   CG  CD1  doub Y N 393 
TRP   CG  CD2  sing Y N 394 
TRP   CD1 NE1  sing Y N 395 
TRP   CD1 HD1  sing N N 396 
TRP   CD2 CE2  doub Y N 397 
TRP   CD2 CE3  sing Y N 398 
TRP   NE1 CE2  sing Y N 399 
TRP   NE1 HE1  sing N N 400 
TRP   CE2 CZ2  sing Y N 401 
TRP   CE3 CZ3  doub Y N 402 
TRP   CE3 HE3  sing N N 403 
TRP   CZ2 CH2  doub Y N 404 
TRP   CZ2 HZ2  sing N N 405 
TRP   CZ3 CH2  sing Y N 406 
TRP   CZ3 HZ3  sing N N 407 
TRP   CH2 HH2  sing N N 408 
TRP   OXT HXT  sing N N 409 
TYR   N   CA   sing N N 410 
TYR   N   H    sing N N 411 
TYR   N   H2   sing N N 412 
TYR   CA  C    sing N N 413 
TYR   CA  CB   sing N N 414 
TYR   CA  HA   sing N N 415 
TYR   C   O    doub N N 416 
TYR   C   OXT  sing N N 417 
TYR   CB  CG   sing N N 418 
TYR   CB  HB2  sing N N 419 
TYR   CB  HB3  sing N N 420 
TYR   CG  CD1  doub Y N 421 
TYR   CG  CD2  sing Y N 422 
TYR   CD1 CE1  sing Y N 423 
TYR   CD1 HD1  sing N N 424 
TYR   CD2 CE2  doub Y N 425 
TYR   CD2 HD2  sing N N 426 
TYR   CE1 CZ   doub Y N 427 
TYR   CE1 HE1  sing N N 428 
TYR   CE2 CZ   sing Y N 429 
TYR   CE2 HE2  sing N N 430 
TYR   CZ  OH   sing N N 431 
TYR   OH  HH   sing N N 432 
TYR   OXT HXT  sing N N 433 
TZI   F1  C32  sing N N 434 
TZI   C32 C31  sing N N 435 
TZI   C31 C30  sing N N 436 
TZI   C30 N2   sing N N 437 
TZI   N2  C29  sing N N 438 
TZI   N2  C28  sing N N 439 
TZI   C29 C26  sing N N 440 
TZI   C28 C27  sing N N 441 
TZI   C26 C27  sing N N 442 
TZI   C26 C25  sing N N 443 
TZI   C25 O3   sing N N 444 
TZI   O3  C22  sing N N 445 
TZI   C22 C21  doub Y N 446 
TZI   C22 C23  sing Y N 447 
TZI   C21 C20  sing Y N 448 
TZI   C23 C24  doub Y N 449 
TZI   C20 C19  doub Y N 450 
TZI   C24 C19  sing Y N 451 
TZI   C19 C9   sing N N 452 
TZI   C17 C18  sing N N 453 
TZI   C17 C8   sing N N 454 
TZI   C2  C1   doub Y N 455 
TZI   C2  C3   sing Y N 456 
TZI   O2  C3   sing N N 457 
TZI   C1  C6   sing Y N 458 
TZI   C3  C4   doub Y N 459 
TZI   C6  C9   sing N N 460 
TZI   C6  C5   doub Y N 461 
TZI   C4  C5   sing Y N 462 
TZI   C9  N1   sing N N 463 
TZI   C18 C8   sing N N 464 
TZI   C5  C7   sing N N 465 
TZI   C8  C7   sing N N 466 
TZI   C8  N1   sing N N 467 
TZI   N1  C10  sing N N 468 
TZI   C10 O1   doub N N 469 
TZI   C10 C11  sing N N 470 
TZI   C12 C11  doub Y N 471 
TZI   C12 C13  sing Y N 472 
TZI   C11 C16  sing Y N 473 
TZI   C13 C14  doub Y N 474 
TZI   C16 C15  doub Y N 475 
TZI   C14 C15  sing Y N 476 
TZI   C4  H1   sing N N 477 
TZI   C7  H2   sing N N 478 
TZI   C7  H3   sing N N 479 
TZI   C13 H4   sing N N 480 
TZI   C15 H5   sing N N 481 
TZI   C17 H6   sing N N 482 
TZI   C17 H7   sing N N 483 
TZI   C20 H8   sing N N 484 
TZI   C21 H9   sing N N 485 
TZI   C24 H10  sing N N 486 
TZI   C26 H11  sing N N 487 
TZI   C28 H12  sing N N 488 
TZI   C28 H13  sing N N 489 
TZI   C1  H14  sing N N 490 
TZI   C12 H15  sing N N 491 
TZI   C14 H16  sing N N 492 
TZI   C16 H17  sing N N 493 
TZI   C18 H18  sing N N 494 
TZI   C18 H19  sing N N 495 
TZI   C2  H20  sing N N 496 
TZI   C23 H21  sing N N 497 
TZI   C25 H22  sing N N 498 
TZI   C25 H23  sing N N 499 
TZI   C27 H24  sing N N 500 
TZI   C27 H25  sing N N 501 
TZI   C29 H26  sing N N 502 
TZI   C29 H27  sing N N 503 
TZI   C30 H28  sing N N 504 
TZI   C30 H29  sing N N 505 
TZI   C31 H30  sing N N 506 
TZI   C31 H31  sing N N 507 
TZI   C32 H32  sing N N 508 
TZI   C32 H33  sing N N 509 
TZI   C9  H34  sing N N 510 
TZI   O2  H36  sing N N 511 
VAL   N   CA   sing N N 512 
VAL   N   H    sing N N 513 
VAL   N   H2   sing N N 514 
VAL   CA  C    sing N N 515 
VAL   CA  CB   sing N N 516 
VAL   CA  HA   sing N N 517 
VAL   C   O    doub N N 518 
VAL   C   OXT  sing N N 519 
VAL   CB  CG1  sing N N 520 
VAL   CB  CG2  sing N N 521 
VAL   CB  HB   sing N N 522 
VAL   CG1 HG11 sing N N 523 
VAL   CG1 HG12 sing N N 524 
VAL   CG1 HG13 sing N N 525 
VAL   CG2 HG21 sing N N 526 
VAL   CG2 HG22 sing N N 527 
VAL   CG2 HG23 sing N N 528 
VAL   OXT HXT  sing N N 529 
# 
_pdbx_audit_support.funding_organization   'National Institutes of Health/National Cancer Institute (NIH/NCI)' 
_pdbx_audit_support.country                'United States' 
_pdbx_audit_support.grant_number           5R37CA279341 
_pdbx_audit_support.ordinal                1 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'experimental model' 
_pdbx_initial_refinement_model.source_name      PDB 
_pdbx_initial_refinement_model.accession_code   8dvb 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    9BPX 
_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]   0.009830 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.002364 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.017154 
_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]   0.011820 
_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 
F 
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   . LEU   A 1 14  ? 11.093  -6.144  5.372  1.00 63.55  ? 306 LEU   A N   1 
ATOM   2    C CA  . LEU   A 1 14  ? 10.152  -5.555  6.317  1.00 55.13  ? 306 LEU   A CA  1 
ATOM   3    C C   . LEU   A 1 14  ? 10.477  -5.965  7.750  1.00 58.59  ? 306 LEU   A C   1 
ATOM   4    O O   . LEU   A 1 14  ? 10.751  -5.118  8.601  1.00 61.86  ? 306 LEU   A O   1 
ATOM   5    C CB  . LEU   A 1 14  ? 8.718   -5.962  5.968  1.00 54.12  ? 306 LEU   A CB  1 
ATOM   6    N N   . ALA   A 1 15  ? 10.446  -7.274  8.009  1.00 62.50  ? 307 ALA   A N   1 
ATOM   7    C CA  . ALA   A 1 15  ? 10.710  -7.766  9.357  1.00 42.92  ? 307 ALA   A CA  1 
ATOM   8    C C   . ALA   A 1 15  ? 12.156  -7.535  9.773  1.00 42.55  ? 307 ALA   A C   1 
ATOM   9    O O   . ALA   A 1 15  ? 12.429  -7.307  10.957 1.00 46.95  ? 307 ALA   A O   1 
ATOM   10   C CB  . ALA   A 1 15  ? 10.366  -9.251  9.451  1.00 49.20  ? 307 ALA   A CB  1 
ATOM   11   N N   . LEU   A 1 16  ? 13.091  -7.590  8.827  1.00 46.52  ? 308 LEU   A N   1 
ATOM   12   C CA  . LEU   A 1 16  ? 14.499  -7.410  9.151  1.00 46.71  ? 308 LEU   A CA  1 
ATOM   13   C C   . LEU   A 1 16  ? 14.869  -5.958  9.412  1.00 53.85  ? 308 LEU   A C   1 
ATOM   14   O O   . LEU   A 1 16  ? 15.982  -5.695  9.881  1.00 53.36  ? 308 LEU   A O   1 
ATOM   15   C CB  . LEU   A 1 16  ? 15.371  -7.960  8.023  1.00 51.39  ? 308 LEU   A CB  1 
ATOM   16   C CG  . LEU   A 1 16  ? 15.265  -9.469  7.816  1.00 51.52  ? 308 LEU   A CG  1 
ATOM   17   C CD1 . LEU   A 1 16  ? 16.071  -9.896  6.600  1.00 48.52  ? 308 LEU   A CD1 1 
ATOM   18   C CD2 . LEU   A 1 16  ? 15.713  -10.207 9.070  1.00 46.86  ? 308 LEU   A CD2 1 
ATOM   19   N N   . SER   A 1 17  ? 13.978  -5.015  9.113  1.00 50.04  ? 309 SER   A N   1 
ATOM   20   C CA  . SER   A 1 17  ? 14.232  -3.600  9.334  1.00 55.57  ? 309 SER   A CA  1 
ATOM   21   C C   . SER   A 1 17  ? 13.559  -3.069  10.591 1.00 54.52  ? 309 SER   A C   1 
ATOM   22   O O   . SER   A 1 17  ? 13.671  -1.874  10.879 1.00 56.27  ? 309 SER   A O   1 
ATOM   23   C CB  . SER   A 1 17  ? 13.776  -2.787  8.118  1.00 54.64  ? 309 SER   A CB  1 
ATOM   24   O OG  . SER   A 1 17  ? 12.390  -2.503  8.188  1.00 64.13  ? 309 SER   A OG  1 
ATOM   25   N N   . LEU   A 1 18  ? 12.864  -3.922  11.339 1.00 47.37  ? 310 LEU   A N   1 
ATOM   26   C CA  . LEU   A 1 18  ? 12.231  -3.489  12.575 1.00 39.96  ? 310 LEU   A CA  1 
ATOM   27   C C   . LEU   A 1 18  ? 13.273  -3.263  13.661 1.00 42.60  ? 310 LEU   A C   1 
ATOM   28   O O   . LEU   A 1 18  ? 14.254  -4.004  13.768 1.00 49.81  ? 310 LEU   A O   1 
ATOM   29   C CB  . LEU   A 1 18  ? 11.219  -4.529  13.055 1.00 46.09  ? 310 LEU   A CB  1 
ATOM   30   C CG  . LEU   A 1 18  ? 9.965   -4.773  12.220 1.00 52.21  ? 310 LEU   A CG  1 
ATOM   31   C CD1 . LEU   A 1 18  ? 9.171   -5.920  12.817 1.00 34.14  ? 310 LEU   A CD1 1 
ATOM   32   C CD2 . LEU   A 1 18  ? 9.117   -3.520  12.150 1.00 54.42  ? 310 LEU   A CD2 1 
ATOM   33   N N   . THR   A 1 19  ? 13.051  -2.235  14.474 1.00 37.36  ? 311 THR   A N   1 
ATOM   34   C CA  . THR   A 1 19  ? 13.861  -2.050  15.664 1.00 44.25  ? 311 THR   A CA  1 
ATOM   35   C C   . THR   A 1 19  ? 13.444  -3.054  16.736 1.00 39.89  ? 311 THR   A C   1 
ATOM   36   O O   . THR   A 1 19  ? 12.469  -3.796  16.590 1.00 33.59  ? 311 THR   A O   1 
ATOM   37   C CB  . THR   A 1 19  ? 13.729  -0.622  16.192 1.00 39.07  ? 311 THR   A CB  1 
ATOM   38   O OG1 . THR   A 1 19  ? 12.445  -0.455  16.806 1.00 42.60  ? 311 THR   A OG1 1 
ATOM   39   C CG2 . THR   A 1 19  ? 13.879  0.383   15.058 1.00 40.16  ? 311 THR   A CG2 1 
ATOM   40   N N   . ALA   A 1 20  ? 14.205  -3.074  17.832 1.00 39.25  ? 312 ALA   A N   1 
ATOM   41   C CA  . ALA   A 1 20  ? 13.882  -3.981  18.928 1.00 36.66  ? 312 ALA   A CA  1 
ATOM   42   C C   . ALA   A 1 20  ? 12.553  -3.614  19.575 1.00 42.76  ? 312 ALA   A C   1 
ATOM   43   O O   . ALA   A 1 20  ? 11.773  -4.498  19.948 1.00 45.77  ? 312 ALA   A O   1 
ATOM   44   C CB  . ALA   A 1 20  ? 15.005  -3.975  19.963 1.00 36.87  ? 312 ALA   A CB  1 
ATOM   45   N N   . ASP   A 1 21  ? 12.273  -2.316  19.713 1.00 39.70  ? 313 ASP   A N   1 
ATOM   46   C CA  . ASP   A 1 21  ? 11.014  -1.898  20.319 1.00 45.32  ? 313 ASP   A CA  1 
ATOM   47   C C   . ASP   A 1 21  ? 9.838   -2.179  19.394 1.00 35.70  ? 313 ASP   A C   1 
ATOM   48   O O   . ASP   A 1 21  ? 8.772   -2.608  19.850 1.00 36.74  ? 313 ASP   A O   1 
ATOM   49   C CB  . ASP   A 1 21  ? 11.075  -0.416  20.686 1.00 42.98  ? 313 ASP   A CB  1 
ATOM   50   C CG  . ASP   A 1 21  ? 12.172  -0.113  21.684 1.00 51.82  ? 313 ASP   A CG  1 
ATOM   51   O OD1 . ASP   A 1 21  ? 13.330  0.078   21.259 1.00 72.84  ? 313 ASP   A OD1 1 
ATOM   52   O OD2 . ASP   A 1 21  ? 11.875  -0.070  22.896 1.00 58.93  ? 313 ASP   A OD2 1 
ATOM   53   N N   . GLN   A 1 22  ? 10.013  -1.952  18.091 1.00 39.92  ? 314 GLN   A N   1 
ATOM   54   C CA  . GLN   A 1 22  ? 8.967   -2.305  17.138 1.00 41.95  ? 314 GLN   A CA  1 
ATOM   55   C C   . GLN   A 1 22  ? 8.770   -3.815  17.051 1.00 38.93  ? 314 GLN   A C   1 
ATOM   56   O O   . GLN   A 1 22  ? 7.677   -4.276  16.705 1.00 36.26  ? 314 GLN   A O   1 
ATOM   57   C CB  . GLN   A 1 22  ? 9.296   -1.733  15.759 1.00 38.09  ? 314 GLN   A CB  1 
ATOM   58   C CG  . GLN   A 1 22  ? 9.369   -0.212  15.690 1.00 36.28  ? 314 GLN   A CG  1 
ATOM   59   C CD  . GLN   A 1 22  ? 9.854   0.274   14.336 1.00 38.76  ? 314 GLN   A CD  1 
ATOM   60   O OE1 . GLN   A 1 22  ? 10.643  -0.400  13.674 1.00 53.13  ? 314 GLN   A OE1 1 
ATOM   61   N NE2 . GLN   A 1 22  ? 9.390   1.448   13.920 1.00 51.89  ? 314 GLN   A NE2 1 
ATOM   62   N N   . MET   A 1 23  ? 9.803   -4.601  17.359 1.00 36.81  ? 315 MET   A N   1 
ATOM   63   C CA  . MET   A 1 23  ? 9.644   -6.051  17.373 1.00 30.30  ? 315 MET   A CA  1 
ATOM   64   C C   . MET   A 1 23  ? 8.949   -6.527  18.646 1.00 29.28  ? 315 MET   A C   1 
ATOM   65   O O   . MET   A 1 23  ? 8.145   -7.466  18.604 1.00 35.76  ? 315 MET   A O   1 
ATOM   66   C CB  . MET   A 1 23  ? 11.011  -6.715  17.184 1.00 32.92  ? 315 MET   A CB  1 
ATOM   67   C CG  . MET   A 1 23  ? 11.045  -8.212  17.401 1.00 38.58  ? 315 MET   A CG  1 
ATOM   68   S SD  . MET   A 1 23  ? 10.384  -9.061  15.951 1.00 39.67  ? 315 MET   A SD  1 
ATOM   69   C CE  . MET   A 1 23  ? 11.517  -8.507  14.685 1.00 38.55  ? 315 MET   A CE  1 
ATOM   70   N N   . VAL   A 1 24  ? 9.238   -5.890  19.782 1.00 34.04  ? 316 VAL   A N   1 
ATOM   71   C CA  . VAL   A 1 24  ? 8.492   -6.184  21.003 1.00 30.29  ? 316 VAL   A CA  1 
ATOM   72   C C   . VAL   A 1 24  ? 7.021   -5.834  20.817 1.00 27.19  ? 316 VAL   A C   1 
ATOM   73   O O   . VAL   A 1 24  ? 6.128   -6.617  21.162 1.00 36.05  ? 316 VAL   A O   1 
ATOM   74   C CB  . VAL   A 1 24  ? 9.097   -5.432  22.200 1.00 34.06  ? 316 VAL   A CB  1 
ATOM   75   C CG1 . VAL   A 1 24  ? 8.138   -5.461  23.378 1.00 30.48  ? 316 VAL   A CG1 1 
ATOM   76   C CG2 . VAL   A 1 24  ? 10.425  -6.038  22.587 1.00 31.78  ? 316 VAL   A CG2 1 
ATOM   77   N N   . SER   A 1 25  ? 6.752   -4.654  20.252 1.00 27.05  ? 317 SER   A N   1 
ATOM   78   C CA  . SER   A 1 25  ? 5.375   -4.198  20.088 1.00 32.57  ? 317 SER   A CA  1 
ATOM   79   C C   . SER   A 1 25  ? 4.585   -5.127  19.176 1.00 33.51  ? 317 SER   A C   1 
ATOM   80   O O   . SER   A 1 25  ? 3.426   -5.449  19.461 1.00 38.93  ? 317 SER   A O   1 
ATOM   81   C CB  . SER   A 1 25  ? 5.358   -2.771  19.541 1.00 30.69  ? 317 SER   A CB  1 
ATOM   82   O OG  . SER   A 1 25  ? 5.594   -1.829  20.571 1.00 51.27  ? 317 SER   A OG  1 
ATOM   83   N N   . ALA   A 1 26  ? 5.194   -5.570  18.074 1.00 32.75  ? 318 ALA   A N   1 
ATOM   84   C CA  . ALA   A 1 26  ? 4.496   -6.469  17.161 1.00 35.25  ? 318 ALA   A CA  1 
ATOM   85   C C   . ALA   A 1 26  ? 4.238   -7.826  17.806 1.00 36.11  ? 318 ALA   A C   1 
ATOM   86   O O   . ALA   A 1 26  ? 3.199   -8.449  17.559 1.00 32.29  ? 318 ALA   A O   1 
ATOM   87   C CB  . ALA   A 1 26  ? 5.296   -6.631  15.869 1.00 29.95  ? 318 ALA   A CB  1 
ATOM   88   N N   . LEU   A 1 27  ? 5.168   -8.298  18.639 1.00 26.43  ? 319 LEU   A N   1 
ATOM   89   C CA  . LEU   A 1 27  ? 4.979   -9.589  19.293 1.00 33.20  ? 319 LEU   A CA  1 
ATOM   90   C C   . LEU   A 1 27  ? 3.958   -9.494  20.421 1.00 28.32  ? 319 LEU   A C   1 
ATOM   91   O O   . LEU   A 1 27  ? 3.137   -10.401 20.600 1.00 23.36  ? 319 LEU   A O   1 
ATOM   92   C CB  . LEU   A 1 27  ? 6.315   -10.117 19.813 1.00 23.05  ? 319 LEU   A CB  1 
ATOM   93   C CG  . LEU   A 1 27  ? 7.315   -10.553 18.740 1.00 23.04  ? 319 LEU   A CG  1 
ATOM   94   C CD1 . LEU   A 1 27  ? 8.555   -11.174 19.368 1.00 24.87  ? 319 LEU   A CD1 1 
ATOM   95   C CD2 . LEU   A 1 27  ? 6.659   -11.514 17.760 1.00 25.48  ? 319 LEU   A CD2 1 
ATOM   96   N N   . LEU   A 1 28  ? 3.996   -8.406  21.195 1.00 27.48  ? 320 LEU   A N   1 
ATOM   97   C CA  . LEU   A 1 28  ? 2.984   -8.200  22.226 1.00 29.28  ? 320 LEU   A CA  1 
ATOM   98   C C   . LEU   A 1 28  ? 1.600   -8.043  21.610 1.00 33.74  ? 320 LEU   A C   1 
ATOM   99   O O   . LEU   A 1 28  ? 0.608   -8.539  22.158 1.00 30.95  ? 320 LEU   A O   1 
ATOM   100  C CB  . LEU   A 1 28  ? 3.334   -6.976  23.072 1.00 31.83  ? 320 LEU   A CB  1 
ATOM   101  C CG  . LEU   A 1 28  ? 4.456   -7.136  24.099 1.00 32.76  ? 320 LEU   A CG  1 
ATOM   102  C CD1 . LEU   A 1 28  ? 4.698   -5.823  24.827 1.00 26.51  ? 320 LEU   A CD1 1 
ATOM   103  C CD2 . LEU   A 1 28  ? 4.128   -8.246  25.085 1.00 24.39  ? 320 LEU   A CD2 1 
ATOM   104  N N   A ASP   A 1 29  ? 1.513   -7.356  20.468 0.42 34.97  ? 321 ASP   A N   1 
ATOM   105  N N   B ASP   A 1 29  ? 1.512   -7.354  20.470 0.58 35.02  ? 321 ASP   A N   1 
ATOM   106  C CA  A ASP   A 1 29  ? 0.225   -7.178  19.806 0.42 34.91  ? 321 ASP   A CA  1 
ATOM   107  C CA  B ASP   A 1 29  ? 0.223   -7.182  19.810 0.58 34.86  ? 321 ASP   A CA  1 
ATOM   108  C C   A ASP   A 1 29  ? -0.268  -8.474  19.176 0.42 34.37  ? 321 ASP   A C   1 
ATOM   109  C C   B ASP   A 1 29  ? -0.269  -8.483  19.189 0.58 34.34  ? 321 ASP   A C   1 
ATOM   110  O O   A ASP   A 1 29  ? -1.481  -8.686  19.067 0.42 35.40  ? 321 ASP   A O   1 
ATOM   111  O O   B ASP   A 1 29  ? -1.481  -8.706  19.100 0.58 35.61  ? 321 ASP   A O   1 
ATOM   112  C CB  A ASP   A 1 29  ? 0.327   -6.078  18.748 0.42 33.75  ? 321 ASP   A CB  1 
ATOM   113  C CB  B ASP   A 1 29  ? 0.316   -6.089  18.746 0.58 33.46  ? 321 ASP   A CB  1 
ATOM   114  C CG  A ASP   A 1 29  ? -1.030  -5.628  18.241 0.42 39.30  ? 321 ASP   A CG  1 
ATOM   115  C CG  B ASP   A 1 29  ? 0.463   -4.705  19.344 0.58 34.10  ? 321 ASP   A CG  1 
ATOM   116  O OD1 A ASP   A 1 29  ? -1.877  -5.236  19.071 0.42 42.78  ? 321 ASP   A OD1 1 
ATOM   117  O OD1 B ASP   A 1 29  ? 0.234   -4.556  20.564 0.58 35.45  ? 321 ASP   A OD1 1 
ATOM   118  O OD2 A ASP   A 1 29  ? -1.248  -5.665  17.012 0.42 37.28  ? 321 ASP   A OD2 1 
ATOM   119  O OD2 B ASP   A 1 29  ? 0.809   -3.766  18.597 0.58 41.93  ? 321 ASP   A OD2 1 
ATOM   120  N N   . ALA   A 1 30  ? 0.648   -9.349  18.758 1.00 38.19  ? 322 ALA   A N   1 
ATOM   121  C CA  . ALA   A 1 30  ? 0.273   -10.627 18.169 1.00 40.73  ? 322 ALA   A CA  1 
ATOM   122  C C   . ALA   A 1 30  ? -0.168  -11.648 19.204 1.00 30.49  ? 322 ALA   A C   1 
ATOM   123  O O   . ALA   A 1 30  ? -0.637  -12.727 18.824 1.00 32.56  ? 322 ALA   A O   1 
ATOM   124  C CB  . ALA   A 1 30  ? 1.441   -11.199 17.365 1.00 32.49  ? 322 ALA   A CB  1 
ATOM   125  N N   . GLU   A 1 31  ? -0.026  -11.338 20.486 1.00 29.00  ? 323 GLU   A N   1 
ATOM   126  C CA  . GLU   A 1 31  ? -0.287  -12.318 21.530 1.00 30.85  ? 323 GLU   A CA  1 
ATOM   127  C C   . GLU   A 1 31  ? -1.739  -12.787 21.473 1.00 31.88  ? 323 GLU   A C   1 
ATOM   128  O O   . GLU   A 1 31  ? -2.657  -11.954 21.457 1.00 37.27  ? 323 GLU   A O   1 
ATOM   129  C CB  . GLU   A 1 31  ? 0.028   -11.726 22.903 1.00 24.50  ? 323 GLU   A CB  1 
ATOM   130  C CG  . GLU   A 1 31  ? -0.054  -12.723 24.052 1.00 48.11  ? 323 GLU   A CG  1 
ATOM   131  C CD  . GLU   A 1 31  ? 1.148   -13.650 24.142 1.00 29.35  ? 323 GLU   A CD  1 
ATOM   132  O OE1 . GLU   A 1 31  ? 1.313   -14.283 25.202 1.00 34.02  ? 323 GLU   A OE1 1 
ATOM   133  O OE2 . GLU   A 1 31  ? 1.936   -13.741 23.174 1.00 25.76  ? 323 GLU   A OE2 1 
ATOM   134  N N   . PRO   A 1 32  ? -1.989  -14.092 21.444 1.00 28.82  ? 324 PRO   A N   1 
ATOM   135  C CA  . PRO   A 1 32  ? -3.364  -14.588 21.372 1.00 23.59  ? 324 PRO   A CA  1 
ATOM   136  C C   . PRO   A 1 32  ? -4.063  -14.430 22.710 1.00 29.82  ? 324 PRO   A C   1 
ATOM   137  O O   . PRO   A 1 32  ? -3.408  -14.213 23.740 1.00 24.91  ? 324 PRO   A O   1 
ATOM   138  C CB  . PRO   A 1 32  ? -3.181  -16.068 21.007 1.00 25.51  ? 324 PRO   A CB  1 
ATOM   139  C CG  . PRO   A 1 32  ? -1.859  -16.426 21.592 1.00 34.82  ? 324 PRO   A CG  1 
ATOM   140  C CD  . PRO   A 1 32  ? -1.003  -15.186 21.499 1.00 31.70  ? 324 PRO   A CD  1 
ATOM   141  N N   . PRO   A 1 33  ? -5.388  -14.522 22.741 1.00 31.50  ? 325 PRO   A N   1 
ATOM   142  C CA  . PRO   A 1 33  ? -6.102  -14.402 24.014 1.00 25.12  ? 325 PRO   A CA  1 
ATOM   143  C C   . PRO   A 1 33  ? -5.965  -15.658 24.860 1.00 22.78  ? 325 PRO   A C   1 
ATOM   144  O O   . PRO   A 1 33  ? -5.635  -16.743 24.377 1.00 23.67  ? 325 PRO   A O   1 
ATOM   145  C CB  . PRO   A 1 33  ? -7.558  -14.184 23.594 1.00 25.68  ? 325 PRO   A CB  1 
ATOM   146  C CG  . PRO   A 1 33  ? -7.663  -14.758 22.230 1.00 29.13  ? 325 PRO   A CG  1 
ATOM   147  C CD  . PRO   A 1 33  ? -6.302  -14.714 21.599 1.00 28.74  ? 325 PRO   A CD  1 
ATOM   148  N N   . ILE   A 1 34  ? -6.224  -15.485 26.153 1.00 22.20  ? 326 ILE   A N   1 
ATOM   149  C CA  . ILE   A 1 34  ? -6.270  -16.603 27.087 1.00 26.21  ? 326 ILE   A CA  1 
ATOM   150  C C   . ILE   A 1 34  ? -7.656  -17.230 26.982 1.00 25.27  ? 326 ILE   A C   1 
ATOM   151  O O   . ILE   A 1 34  ? -8.660  -16.603 27.326 1.00 24.44  ? 326 ILE   A O   1 
ATOM   152  C CB  . ILE   A 1 34  ? -5.967  -16.155 28.520 1.00 31.93  ? 326 ILE   A CB  1 
ATOM   153  C CG1 . ILE   A 1 34  ? -4.535  -15.626 28.617 1.00 32.65  ? 326 ILE   A CG1 1 
ATOM   154  C CG2 . ILE   A 1 34  ? -6.179  -17.306 29.493 1.00 26.22  ? 326 ILE   A CG2 1 
ATOM   155  C CD1 . ILE   A 1 34  ? -4.247  -14.883 29.899 1.00 35.11  ? 326 ILE   A CD1 1 
ATOM   156  N N   . LEU   A 1 35  ? -7.713  -18.464 26.495 1.00 22.94  ? 327 LEU   A N   1 
ATOM   157  C CA  . LEU   A 1 35  ? -8.980  -19.140 26.279 1.00 23.84  ? 327 LEU   A CA  1 
ATOM   158  C C   . LEU   A 1 35  ? -9.430  -19.860 27.545 1.00 25.88  ? 327 LEU   A C   1 
ATOM   159  O O   . LEU   A 1 35  ? -8.635  -20.159 28.439 1.00 23.89  ? 327 LEU   A O   1 
ATOM   160  C CB  . LEU   A 1 35  ? -8.872  -20.128 25.118 1.00 26.56  ? 327 LEU   A CB  1 
ATOM   161  C CG  . LEU   A 1 35  ? -8.505  -19.517 23.765 1.00 22.65  ? 327 LEU   A CG  1 
ATOM   162  C CD1 . LEU   A 1 35  ? -8.703  -20.534 22.654 1.00 23.30  ? 327 LEU   A CD1 1 
ATOM   163  C CD2 . LEU   A 1 35  ? -9.317  -18.256 23.497 1.00 24.71  ? 327 LEU   A CD2 1 
ATOM   164  N N   . TYR   A 1 36  ? -10.727 -20.139 27.606 1.00 24.82  ? 328 TYR   A N   1 
ATOM   165  C CA  . TYR   A 1 36  ? -11.345 -20.784 28.753 1.00 27.16  ? 328 TYR   A CA  1 
ATOM   166  C C   . TYR   A 1 36  ? -11.757 -22.206 28.408 1.00 24.95  ? 328 TYR   A C   1 
ATOM   167  O O   . TYR   A 1 36  ? -12.015 -22.534 27.246 1.00 28.81  ? 328 TYR   A O   1 
ATOM   168  C CB  . TYR   A 1 36  ? -12.578 -20.011 29.225 1.00 27.97  ? 328 TYR   A CB  1 
ATOM   169  C CG  . TYR   A 1 36  ? -12.266 -18.793 30.058 1.00 37.54  ? 328 TYR   A CG  1 
ATOM   170  C CD1 . TYR   A 1 36  ? -11.724 -17.654 29.481 1.00 28.98  ? 328 TYR   A CD1 1 
ATOM   171  C CD2 . TYR   A 1 36  ? -12.514 -18.784 31.424 1.00 30.29  ? 328 TYR   A CD2 1 
ATOM   172  C CE1 . TYR   A 1 36  ? -11.441 -16.537 30.241 1.00 40.25  ? 328 TYR   A CE1 1 
ATOM   173  C CE2 . TYR   A 1 36  ? -12.237 -17.672 32.191 1.00 31.83  ? 328 TYR   A CE2 1 
ATOM   174  C CZ  . TYR   A 1 36  ? -11.699 -16.552 31.595 1.00 31.84  ? 328 TYR   A CZ  1 
ATOM   175  O OH  . TYR   A 1 36  ? -11.418 -15.443 32.358 1.00 46.75  ? 328 TYR   A OH  1 
ATOM   176  N N   . SER   A 1 37  ? -11.822 -23.047 29.435 1.00 29.87  ? 329 SER   A N   1 
ATOM   177  C CA  . SER   A 1 37  ? -12.435 -24.354 29.282 1.00 27.36  ? 329 SER   A CA  1 
ATOM   178  C C   . SER   A 1 37  ? -13.950 -24.205 29.184 1.00 28.73  ? 329 SER   A C   1 
ATOM   179  O O   . SER   A 1 37  ? -14.538 -23.225 29.648 1.00 31.96  ? 329 SER   A O   1 
ATOM   180  C CB  . SER   A 1 37  ? -12.064 -25.263 30.453 1.00 29.39  ? 329 SER   A CB  1 
ATOM   181  O OG  . SER   A 1 37  ? -12.509 -26.589 30.223 1.00 28.51  ? 329 SER   A OG  1 
ATOM   182  N N   . GLU   A 1 38  ? -14.583 -25.200 28.570 1.00 38.54  ? 330 GLU   A N   1 
ATOM   183  C CA  . GLU   A 1 38  ? -16.011 -25.125 28.297 1.00 37.84  ? 330 GLU   A CA  1 
ATOM   184  C C   . GLU   A 1 38  ? -16.822 -25.128 29.589 1.00 34.20  ? 330 GLU   A C   1 
ATOM   185  O O   . GLU   A 1 38  ? -16.556 -25.904 30.510 1.00 46.54  ? 330 GLU   A O   1 
ATOM   186  C CB  . GLU   A 1 38  ? -16.435 -26.288 27.398 1.00 50.64  ? 330 GLU   A CB  1 
ATOM   187  C CG  . GLU   A 1 38  ? -15.484 -26.553 26.230 1.00 47.33  ? 330 GLU   A CG  1 
ATOM   188  C CD  . GLU   A 1 38  ? -14.366 -27.521 26.574 1.00 58.21  ? 330 GLU   A CD  1 
ATOM   189  O OE1 . GLU   A 1 38  ? -14.583 -28.744 26.459 1.00 58.23  ? 330 GLU   A OE1 1 
ATOM   190  O OE2 . GLU   A 1 38  ? -13.270 -27.058 26.958 1.00 46.03  ? 330 GLU   A OE2 1 
ATOM   191  N N   . TYR   A 1 39  ? -17.815 -24.240 29.650 1.00 40.26  ? 331 TYR   A N   1 
ATOM   192  C CA  . TYR   A 1 39  ? -18.728 -24.154 30.789 1.00 38.72  ? 331 TYR   A CA  1 
ATOM   193  C C   . TYR   A 1 39  ? -19.994 -24.960 30.496 1.00 52.34  ? 331 TYR   A C   1 
ATOM   194  O O   . TYR   A 1 39  ? -21.090 -24.423 30.332 1.00 61.50  ? 331 TYR   A O   1 
ATOM   195  C CB  . TYR   A 1 39  ? -19.072 -22.697 31.088 1.00 46.08  ? 331 TYR   A CB  1 
ATOM   196  C CG  . TYR   A 1 39  ? -18.046 -21.929 31.890 1.00 49.25  ? 331 TYR   A CG  1 
ATOM   197  C CD1 . TYR   A 1 39  ? -18.094 -21.912 33.278 1.00 54.26  ? 331 TYR   A CD1 1 
ATOM   198  C CD2 . TYR   A 1 39  ? -17.058 -21.188 31.260 1.00 42.09  ? 331 TYR   A CD2 1 
ATOM   199  C CE1 . TYR   A 1 39  ? -17.168 -21.197 34.016 1.00 39.79  ? 331 TYR   A CE1 1 
ATOM   200  C CE2 . TYR   A 1 39  ? -16.130 -20.470 31.988 1.00 45.52  ? 331 TYR   A CE2 1 
ATOM   201  C CZ  . TYR   A 1 39  ? -16.189 -20.477 33.365 1.00 38.36  ? 331 TYR   A CZ  1 
ATOM   202  O OH  . TYR   A 1 39  ? -15.264 -19.761 34.092 1.00 43.68  ? 331 TYR   A OH  1 
ATOM   203  N N   . ASP   A 1 40  ? -19.825 -26.279 30.425 1.00 48.90  ? 332 ASP   A N   1 
ATOM   204  C CA  . ASP   A 1 40  ? -20.953 -27.158 30.155 1.00 52.76  ? 332 ASP   A CA  1 
ATOM   205  C C   . ASP   A 1 40  ? -21.438 -27.767 31.461 1.00 48.48  ? 332 ASP   A C   1 
ATOM   206  O O   . ASP   A 1 40  ? -20.757 -28.644 32.013 1.00 47.15  ? 332 ASP   A O   1 
ATOM   207  C CB  . ASP   A 1 40  ? -20.564 -28.255 29.166 1.00 57.03  ? 332 ASP   A CB  1 
ATOM   208  C CG  . ASP   A 1 40  ? -21.770 -28.981 28.598 1.00 61.52  ? 332 ASP   A CG  1 
ATOM   209  O OD1 . ASP   A 1 40  ? -22.910 -28.557 28.879 1.00 61.23  ? 332 ASP   A OD1 1 
ATOM   210  O OD2 . ASP   A 1 40  ? -21.578 -29.977 27.869 1.00 73.11  ? 332 ASP   A OD2 1 
ATOM   211  N N   . PRO   A 1 41  ? -22.586 -27.341 31.996 1.00 54.38  ? 333 PRO   A N   1 
ATOM   212  C CA  . PRO   A 1 41  ? -23.082 -27.957 33.237 1.00 59.64  ? 333 PRO   A CA  1 
ATOM   213  C C   . PRO   A 1 41  ? -23.404 -29.427 33.078 1.00 60.96  ? 333 PRO   A C   1 
ATOM   214  O O   . PRO   A 1 41  ? -23.285 -30.193 34.044 1.00 61.78  ? 333 PRO   A O   1 
ATOM   215  C CB  . PRO   A 1 41  ? -24.339 -27.134 33.557 1.00 66.50  ? 333 PRO   A CB  1 
ATOM   216  C CG  . PRO   A 1 41  ? -24.756 -26.550 32.241 1.00 64.68  ? 333 PRO   A CG  1 
ATOM   217  C CD  . PRO   A 1 41  ? -23.478 -26.276 31.508 1.00 49.62  ? 333 PRO   A CD  1 
ATOM   218  N N   . THR   A 1 42  ? -23.813 -29.844 31.882 1.00 61.01  ? 334 THR   A N   1 
ATOM   219  C CA  . THR   A 1 42  ? -24.094 -31.241 31.593 1.00 61.57  ? 334 THR   A CA  1 
ATOM   220  C C   . THR   A 1 42  ? -22.826 -32.023 31.264 1.00 64.81  ? 334 THR   A C   1 
ATOM   221  O O   . THR   A 1 42  ? -22.896 -33.151 30.759 1.00 71.73  ? 334 THR   A O   1 
ATOM   222  C CB  . THR   A 1 42  ? -25.090 -31.353 30.437 1.00 51.71  ? 334 THR   A CB  1 
ATOM   223  O OG1 . THR   A 1 42  ? -24.396 -31.153 29.201 1.00 55.96  ? 334 THR   A OG1 1 
ATOM   224  C CG2 . THR   A 1 42  ? -26.198 -30.291 30.566 1.00 54.74  ? 334 THR   A CG2 1 
ATOM   225  N N   . ARG   A 1 43  ? -21.672 -31.420 31.514 1.00 58.01  ? 335 ARG   A N   1 
ATOM   226  C CA  . ARG   A 1 43  ? -20.381 -32.081 31.412 1.00 50.61  ? 335 ARG   A CA  1 
ATOM   227  C C   . ARG   A 1 43  ? -19.466 -31.544 32.507 1.00 50.12  ? 335 ARG   A C   1 
ATOM   228  O O   . ARG   A 1 43  ? -18.450 -30.904 32.206 1.00 48.67  ? 335 ARG   A O   1 
ATOM   229  C CB  . ARG   A 1 43  ? -19.764 -31.860 30.030 1.00 51.95  ? 335 ARG   A CB  1 
ATOM   230  N N   . PRO   A 1 44  ? -19.791 -31.770 33.780 1.00 50.85  ? 336 PRO   A N   1 
ATOM   231  C CA  . PRO   A 1 44  ? -18.940 -31.258 34.858 1.00 55.70  ? 336 PRO   A CA  1 
ATOM   232  C C   . PRO   A 1 44  ? -17.570 -31.916 34.834 1.00 56.00  ? 336 PRO   A C   1 
ATOM   233  O O   . PRO   A 1 44  ? -17.370 -32.988 34.258 1.00 59.28  ? 336 PRO   A O   1 
ATOM   234  C CB  . PRO   A 1 44  ? -19.712 -31.627 36.130 1.00 55.16  ? 336 PRO   A CB  1 
ATOM   235  C CG  . PRO   A 1 44  ? -20.527 -32.809 35.734 1.00 57.13  ? 336 PRO   A CG  1 
ATOM   236  C CD  . PRO   A 1 44  ? -20.916 -32.568 34.303 1.00 50.23  ? 336 PRO   A CD  1 
ATOM   237  N N   . PHE   A 1 45  ? -16.614 -31.249 35.473 1.00 51.07  ? 337 PHE   A N   1 
ATOM   238  C CA  . PHE   A 1 45  ? -15.245 -31.740 35.459 1.00 45.79  ? 337 PHE   A CA  1 
ATOM   239  C C   . PHE   A 1 45  ? -15.133 -33.052 36.224 1.00 43.56  ? 337 PHE   A C   1 
ATOM   240  O O   . PHE   A 1 45  ? -15.722 -33.222 37.295 1.00 47.26  ? 337 PHE   A O   1 
ATOM   241  C CB  . PHE   A 1 45  ? -14.289 -30.711 36.057 1.00 43.48  ? 337 PHE   A CB  1 
ATOM   242  C CG  . PHE   A 1 45  ? -12.857 -31.167 36.076 1.00 42.06  ? 337 PHE   A CG  1 
ATOM   243  C CD1 . PHE   A 1 45  ? -12.068 -31.047 34.944 1.00 39.72  ? 337 PHE   A CD1 1 
ATOM   244  C CD2 . PHE   A 1 45  ? -12.305 -31.730 37.216 1.00 37.78  ? 337 PHE   A CD2 1 
ATOM   245  C CE1 . PHE   A 1 45  ? -10.753 -31.471 34.950 1.00 37.55  ? 337 PHE   A CE1 1 
ATOM   246  C CE2 . PHE   A 1 45  ? -10.991 -32.156 37.228 1.00 38.13  ? 337 PHE   A CE2 1 
ATOM   247  C CZ  . PHE   A 1 45  ? -10.214 -32.026 36.093 1.00 37.80  ? 337 PHE   A CZ  1 
ATOM   248  N N   . SER   A 1 46  ? -14.364 -33.978 35.662 1.00 42.92  ? 338 SER   A N   1 
ATOM   249  C CA  . SER   A 1 46  ? -14.111 -35.272 36.278 1.00 39.53  ? 338 SER   A CA  1 
ATOM   250  C C   . SER   A 1 46  ? -12.864 -35.858 35.634 1.00 41.16  ? 338 SER   A C   1 
ATOM   251  O O   . SER   A 1 46  ? -12.333 -35.319 34.660 1.00 36.52  ? 338 SER   A O   1 
ATOM   252  C CB  . SER   A 1 46  ? -15.308 -36.215 36.124 1.00 38.23  ? 338 SER   A CB  1 
ATOM   253  O OG  . SER   A 1 46  ? -15.348 -36.769 34.821 1.00 47.75  ? 338 SER   A OG  1 
ATOM   254  N N   . GLU   A 1 47  ? -12.400 -36.975 36.197 1.00 36.33  ? 339 GLU   A N   1 
ATOM   255  C CA  . GLU   A 1 47  ? -11.239 -37.650 35.629 1.00 47.75  ? 339 GLU   A CA  1 
ATOM   256  C C   . GLU   A 1 47  ? -11.536 -38.190 34.237 1.00 47.10  ? 339 GLU   A C   1 
ATOM   257  O O   . GLU   A 1 47  ? -10.648 -38.216 33.378 1.00 47.59  ? 339 GLU   A O   1 
ATOM   258  C CB  . GLU   A 1 47  ? -10.781 -38.779 36.554 1.00 39.09  ? 339 GLU   A CB  1 
ATOM   259  N N   . ALA   A 1 48  ? -12.779 -38.612 33.990 1.00 40.35  ? 340 ALA   A N   1 
ATOM   260  C CA  . ALA   A 1 48  ? -13.123 -39.171 32.686 1.00 47.15  ? 340 ALA   A CA  1 
ATOM   261  C C   . ALA   A 1 48  ? -13.179 -38.091 31.612 1.00 41.42  ? 340 ALA   A C   1 
ATOM   262  O O   . ALA   A 1 48  ? -12.684 -38.290 30.497 1.00 54.61  ? 340 ALA   A O   1 
ATOM   263  C CB  . ALA   A 1 48  ? -14.457 -39.911 32.772 1.00 38.39  ? 340 ALA   A CB  1 
ATOM   264  N N   . SER   A 1 49  ? -13.774 -36.943 31.926 1.00 46.73  ? 341 SER   A N   1 
ATOM   265  C CA  . SER   A 1 49  ? -13.956 -35.869 30.959 1.00 38.10  ? 341 SER   A CA  1 
ATOM   266  C C   . SER   A 1 49  ? -12.759 -34.930 30.871 1.00 34.21  ? 341 SER   A C   1 
ATOM   267  O O   . SER   A 1 49  ? -12.811 -33.962 30.106 1.00 36.57  ? 341 SER   A O   1 
ATOM   268  C CB  . SER   A 1 49  ? -15.210 -35.059 31.303 1.00 36.07  ? 341 SER   A CB  1 
ATOM   269  O OG  . SER   A 1 49  ? -14.963 -34.177 32.384 1.00 36.78  ? 341 SER   A OG  1 
ATOM   270  N N   . MET   A 1 50  ? -11.685 -35.194 31.618 1.00 32.97  ? 342 MET   A N   1 
ATOM   271  C CA  . MET   A 1 50  ? -10.575 -34.248 31.687 1.00 34.43  ? 342 MET   A CA  1 
ATOM   272  C C   . MET   A 1 50  ? -9.885  -34.088 30.337 1.00 32.00  ? 342 MET   A C   1 
ATOM   273  O O   . MET   A 1 50  ? -9.652  -32.963 29.878 1.00 34.01  ? 342 MET   A O   1 
ATOM   274  C CB  . MET   A 1 50  ? -9.574  -34.692 32.752 1.00 37.45  ? 342 MET   A CB  1 
ATOM   275  C CG  . MET   A 1 50  ? -8.367  -33.782 32.869 1.00 39.72  ? 342 MET   A CG  1 
ATOM   276  S SD  . MET   A 1 50  ? -7.392  -34.125 34.342 1.00 45.03  ? 342 MET   A SD  1 
ATOM   277  C CE  . MET   A 1 50  ? -6.597  -35.654 33.863 1.00 38.68  ? 342 MET   A CE  1 
ATOM   278  N N   . MET   A 1 51  ? -9.540  -35.202 29.688 1.00 31.18  ? 343 MET   A N   1 
ATOM   279  C CA  . MET   A 1 51  ? -8.820  -35.113 28.421 1.00 30.19  ? 343 MET   A CA  1 
ATOM   280  C C   . MET   A 1 51  ? -9.689  -34.540 27.310 1.00 32.23  ? 343 MET   A C   1 
ATOM   281  O O   . MET   A 1 51  ? -9.169  -33.895 26.393 1.00 39.43  ? 343 MET   A O   1 
ATOM   282  C CB  . MET   A 1 51  ? -8.276  -36.486 28.021 1.00 32.75  ? 343 MET   A CB  1 
ATOM   283  C CG  . MET   A 1 51  ? -7.403  -37.136 29.085 1.00 49.30  ? 343 MET   A CG  1 
ATOM   284  S SD  . MET   A 1 51  ? -5.935  -36.175 29.519 1.00 56.23  ? 343 MET   A SD  1 
ATOM   285  C CE  . MET   A 1 51  ? -5.351  -35.639 27.910 1.00 44.97  ? 343 MET   A CE  1 
ATOM   286  N N   . GLY   A 1 52  ? -11.002 -34.766 27.366 1.00 32.09  ? 344 GLY   A N   1 
ATOM   287  C CA  . GLY   A 1 52  ? -11.885 -34.137 26.398 1.00 33.45  ? 344 GLY   A CA  1 
ATOM   288  C C   . GLY   A 1 52  ? -11.876 -32.624 26.512 1.00 23.30  ? 344 GLY   A C   1 
ATOM   289  O O   . GLY   A 1 52  ? -11.845 -31.915 25.504 1.00 29.59  ? 344 GLY   A O   1 
ATOM   290  N N   . LEU   A 1 53  ? -11.894 -32.111 27.745 1.00 27.30  ? 345 LEU   A N   1 
ATOM   291  C CA  . LEU   A 1 53  ? -11.828 -30.667 27.949 1.00 32.44  ? 345 LEU   A CA  1 
ATOM   292  C C   . LEU   A 1 53  ? -10.486 -30.108 27.497 1.00 27.61  ? 345 LEU   A C   1 
ATOM   293  O O   . LEU   A 1 53  ? -10.431 -29.057 26.847 1.00 27.31  ? 345 LEU   A O   1 
ATOM   294  C CB  . LEU   A 1 53  ? -12.073 -30.333 29.421 1.00 28.67  ? 345 LEU   A CB  1 
ATOM   295  C CG  . LEU   A 1 53  ? -13.393 -30.802 30.035 1.00 24.79  ? 345 LEU   A CG  1 
ATOM   296  C CD1 . LEU   A 1 53  ? -13.435 -30.467 31.517 1.00 37.65  ? 345 LEU   A CD1 1 
ATOM   297  C CD2 . LEU   A 1 53  ? -14.575 -30.183 29.312 1.00 25.96  ? 345 LEU   A CD2 1 
ATOM   298  N N   . LEU   A 1 54  ? -9.393  -30.800 27.826 1.00 25.02  ? 346 LEU   A N   1 
ATOM   299  C CA  . LEU   A 1 54  ? -8.067  -30.313 27.462 1.00 23.43  ? 346 LEU   A CA  1 
ATOM   300  C C   . LEU   A 1 54  ? -7.847  -30.376 25.956 1.00 23.95  ? 346 LEU   A C   1 
ATOM   301  O O   . LEU   A 1 54  ? -7.214  -29.484 25.379 1.00 28.98  ? 346 LEU   A O   1 
ATOM   302  C CB  . LEU   A 1 54  ? -6.997  -31.118 28.199 1.00 26.69  ? 346 LEU   A CB  1 
ATOM   303  C CG  . LEU   A 1 54  ? -6.997  -30.933 29.717 1.00 32.28  ? 346 LEU   A CG  1 
ATOM   304  C CD1 . LEU   A 1 54  ? -6.059  -31.920 30.392 1.00 22.71  ? 346 LEU   A CD1 1 
ATOM   305  C CD2 . LEU   A 1 54  ? -6.626  -29.504 30.072 1.00 26.79  ? 346 LEU   A CD2 1 
ATOM   306  N N   . THR   A 1 55  ? -8.360  -31.421 25.304 1.00 26.47  ? 347 THR   A N   1 
ATOM   307  C CA  . THR   A 1 55  ? -8.238  -31.516 23.853 1.00 29.81  ? 347 THR   A CA  1 
ATOM   308  C C   . THR   A 1 55  ? -9.035  -30.416 23.163 1.00 25.72  ? 347 THR   A C   1 
ATOM   309  O O   . THR   A 1 55  ? -8.543  -29.784 22.220 1.00 27.95  ? 347 THR   A O   1 
ATOM   310  C CB  . THR   A 1 55  ? -8.700  -32.894 23.376 1.00 29.61  ? 347 THR   A CB  1 
ATOM   311  O OG1 . THR   A 1 55  ? -7.763  -33.889 23.808 1.00 45.34  ? 347 THR   A OG1 1 
ATOM   312  C CG2 . THR   A 1 55  ? -8.803  -32.933 21.858 1.00 27.00  ? 347 THR   A CG2 1 
ATOM   313  N N   . ASN   A 1 56  ? -10.262 -30.166 23.627 1.00 27.23  ? 348 ASN   A N   1 
ATOM   314  C CA  . ASN   A 1 56  ? -11.073 -29.105 23.040 1.00 34.67  ? 348 ASN   A CA  1 
ATOM   315  C C   . ASN   A 1 56  ? -10.423 -27.742 23.236 1.00 25.10  ? 348 ASN   A C   1 
ATOM   316  O O   . ASN   A 1 56  ? -10.456 -26.894 22.337 1.00 27.19  ? 348 ASN   A O   1 
ATOM   317  C CB  . ASN   A 1 56  ? -12.478 -29.124 23.643 1.00 27.26  ? 348 ASN   A CB  1 
ATOM   318  C CG  . ASN   A 1 56  ? -13.357 -28.010 23.110 1.00 30.69  ? 348 ASN   A CG  1 
ATOM   319  O OD1 . ASN   A 1 56  ? -13.400 -26.915 23.671 1.00 34.01  ? 348 ASN   A OD1 1 
ATOM   320  N ND2 . ASN   A 1 56  ? -14.063 -28.283 22.019 1.00 46.62  ? 348 ASN   A ND2 1 
ATOM   321  N N   . LEU   A 1 57  ? -9.822  -27.514 24.407 1.00 27.98  ? 349 LEU   A N   1 
ATOM   322  C CA  . LEU   A 1 57  ? -9.140  -26.249 24.658 1.00 28.55  ? 349 LEU   A CA  1 
ATOM   323  C C   . LEU   A 1 57  ? -7.926  -26.086 23.750 1.00 26.33  ? 349 LEU   A C   1 
ATOM   324  O O   . LEU   A 1 57  ? -7.687  -24.999 23.213 1.00 23.78  ? 349 LEU   A O   1 
ATOM   325  C CB  . LEU   A 1 57  ? -8.731  -26.158 26.129 1.00 24.26  ? 349 LEU   A CB  1 
ATOM   326  C CG  . LEU   A 1 57  ? -7.772  -25.033 26.522 1.00 23.66  ? 349 LEU   A CG  1 
ATOM   327  C CD1 . LEU   A 1 57  ? -8.495  -23.695 26.555 1.00 20.48  ? 349 LEU   A CD1 1 
ATOM   328  C CD2 . LEU   A 1 57  ? -7.118  -25.328 27.865 1.00 22.06  ? 349 LEU   A CD2 1 
ATOM   329  N N   . ALA   A 1 58  ? -7.151  -27.157 23.564 1.00 25.04  ? 350 ALA   A N   1 
ATOM   330  C CA  . ALA   A 1 58  ? -5.984  -27.081 22.691 1.00 26.58  ? 350 ALA   A CA  1 
ATOM   331  C C   . ALA   A 1 58  ? -6.393  -26.874 21.238 1.00 26.93  ? 350 ALA   A C   1 
ATOM   332  O O   . ALA   A 1 58  ? -5.708  -26.167 20.490 1.00 21.67  ? 350 ALA   A O   1 
ATOM   333  C CB  . ALA   A 1 58  ? -5.135  -28.343 22.835 1.00 20.34  ? 350 ALA   A CB  1 
ATOM   334  N N   . ASP   A 1 59  ? -7.507  -27.482 20.823 1.00 24.36  ? 351 ASP   A N   1 
ATOM   335  C CA  . ASP   A 1 59  ? -7.995  -27.287 19.462 1.00 24.02  ? 351 ASP   A CA  1 
ATOM   336  C C   . ASP   A 1 59  ? -8.357  -25.829 19.213 1.00 23.34  ? 351 ASP   A C   1 
ATOM   337  O O   . ASP   A 1 59  ? -8.023  -25.267 18.163 1.00 27.31  ? 351 ASP   A O   1 
ATOM   338  C CB  . ASP   A 1 59  ? -9.201  -28.190 19.203 1.00 26.41  ? 351 ASP   A CB  1 
ATOM   339  C CG  . ASP   A 1 59  ? -8.804  -29.625 18.921 1.00 29.43  ? 351 ASP   A CG  1 
ATOM   340  O OD1 . ASP   A 1 59  ? -7.597  -29.880 18.731 1.00 40.64  ? 351 ASP   A OD1 1 
ATOM   341  O OD2 . ASP   A 1 59  ? -9.698  -30.496 18.888 1.00 33.98  ? 351 ASP   A OD2 1 
ATOM   342  N N   . ARG   A 1 60  ? -9.037  -25.198 20.171 1.00 22.29  ? 352 ARG   A N   1 
ATOM   343  C CA  . ARG   A 1 60  ? -9.389  -23.792 20.021 1.00 24.11  ? 352 ARG   A CA  1 
ATOM   344  C C   . ARG   A 1 60  ? -8.155  -22.901 20.114 1.00 25.18  ? 352 ARG   A C   1 
ATOM   345  O O   . ARG   A 1 60  ? -8.069  -21.878 19.426 1.00 28.02  ? 352 ARG   A O   1 
ATOM   346  C CB  . ARG   A 1 60  ? -10.424 -23.400 21.074 1.00 24.32  ? 352 ARG   A CB  1 
ATOM   347  C CG  . ARG   A 1 60  ? -11.824 -23.902 20.771 1.00 27.15  ? 352 ARG   A CG  1 
ATOM   348  C CD  . ARG   A 1 60  ? -12.806 -23.478 21.847 1.00 26.80  ? 352 ARG   A CD  1 
ATOM   349  N NE  . ARG   A 1 60  ? -12.643 -24.247 23.075 1.00 27.00  ? 352 ARG   A NE  1 
ATOM   350  C CZ  . ARG   A 1 60  ? -12.359 -23.720 24.259 1.00 33.88  ? 352 ARG   A CZ  1 
ATOM   351  N NH1 . ARG   A 1 60  ? -12.193 -22.417 24.414 1.00 23.85  ? 352 ARG   A NH1 1 
ATOM   352  N NH2 . ARG   A 1 60  ? -12.242 -24.521 25.313 1.00 28.21  ? 352 ARG   A NH2 1 
ATOM   353  N N   . GLU   A 1 61  ? -7.191  -23.274 20.959 1.00 21.70  ? 353 GLU   A N   1 
ATOM   354  C CA  . GLU   A 1 61  ? -5.946  -22.516 21.041 1.00 26.69  ? 353 GLU   A CA  1 
ATOM   355  C C   . GLU   A 1 61  ? -5.161  -22.595 19.738 1.00 24.84  ? 353 GLU   A C   1 
ATOM   356  O O   . GLU   A 1 61  ? -4.506  -21.624 19.340 1.00 20.73  ? 353 GLU   A O   1 
ATOM   357  C CB  . GLU   A 1 61  ? -5.090  -23.028 22.197 1.00 21.59  ? 353 GLU   A CB  1 
ATOM   358  C CG  . GLU   A 1 61  ? -5.504  -22.533 23.566 1.00 21.41  ? 353 GLU   A CG  1 
ATOM   359  C CD  . GLU   A 1 61  ? -4.481  -22.890 24.624 1.00 28.41  ? 353 GLU   A CD  1 
ATOM   360  O OE1 . GLU   A 1 61  ? -4.437  -24.068 25.028 1.00 21.79  ? 353 GLU   A OE1 1 
ATOM   361  O OE2 . GLU   A 1 61  ? -3.714  -21.997 25.042 1.00 28.36  ? 353 GLU   A OE2 1 
ATOM   362  N N   . LEU   A 1 62  ? -5.207  -23.748 19.068 1.00 21.24  ? 354 LEU   A N   1 
ATOM   363  C CA  . LEU   A 1 62  ? -4.442  -23.921 17.840 1.00 27.12  ? 354 LEU   A CA  1 
ATOM   364  C C   . LEU   A 1 62  ? -4.925  -22.988 16.740 1.00 28.26  ? 354 LEU   A C   1 
ATOM   365  O O   . LEU   A 1 62  ? -4.120  -22.523 15.925 1.00 24.97  ? 354 LEU   A O   1 
ATOM   366  C CB  . LEU   A 1 62  ? -4.524  -25.373 17.375 1.00 26.46  ? 354 LEU   A CB  1 
ATOM   367  C CG  . LEU   A 1 62  ? -3.568  -25.767 16.252 1.00 33.83  ? 354 LEU   A CG  1 
ATOM   368  C CD1 . LEU   A 1 62  ? -2.129  -25.752 16.742 1.00 26.10  ? 354 LEU   A CD1 1 
ATOM   369  C CD2 . LEU   A 1 62  ? -3.945  -27.131 15.718 1.00 37.58  ? 354 LEU   A CD2 1 
ATOM   370  N N   . VAL   A 1 63  ? -6.230  -22.706 16.696 1.00 30.39  ? 355 VAL   A N   1 
ATOM   371  C CA  . VAL   A 1 63  ? -6.752  -21.748 15.725 1.00 30.76  ? 355 VAL   A CA  1 
ATOM   372  C C   . VAL   A 1 63  ? -6.146  -20.372 15.969 1.00 26.08  ? 355 VAL   A C   1 
ATOM   373  O O   . VAL   A 1 63  ? -5.726  -19.684 15.030 1.00 28.81  ? 355 VAL   A O   1 
ATOM   374  C CB  . VAL   A 1 63  ? -8.290  -21.708 15.787 1.00 26.59  ? 355 VAL   A CB  1 
ATOM   375  C CG1 . VAL   A 1 63  ? -8.828  -20.656 14.829 1.00 28.71  ? 355 VAL   A CG1 1 
ATOM   376  C CG2 . VAL   A 1 63  ? -8.875  -23.081 15.486 1.00 28.43  ? 355 VAL   A CG2 1 
ATOM   377  N N   . HIS   A 1 64  ? -6.080  -19.956 17.236 1.00 29.35  ? 356 HIS   A N   1 
ATOM   378  C CA  . HIS   A 1 64  ? -5.488  -18.666 17.569 1.00 27.73  ? 356 HIS   A CA  1 
ATOM   379  C C   . HIS   A 1 64  ? -3.978  -18.680 17.385 1.00 21.96  ? 356 HIS   A C   1 
ATOM   380  O O   . HIS   A 1 64  ? -3.379  -17.635 17.107 1.00 25.86  ? 356 HIS   A O   1 
ATOM   381  C CB  . HIS   A 1 64  ? -5.844  -18.280 19.004 1.00 25.01  ? 356 HIS   A CB  1 
ATOM   382  C CG  . HIS   A 1 64  ? -7.281  -17.903 19.187 1.00 23.78  ? 356 HIS   A CG  1 
ATOM   383  N ND1 . HIS   A 1 64  ? -7.726  -16.601 19.099 1.00 26.07  ? 356 HIS   A ND1 1 
ATOM   384  C CD2 . HIS   A 1 64  ? -8.375  -18.657 19.448 1.00 26.25  ? 356 HIS   A CD2 1 
ATOM   385  C CE1 . HIS   A 1 64  ? -9.031  -16.569 19.301 1.00 25.76  ? 356 HIS   A CE1 1 
ATOM   386  N NE2 . HIS   A 1 64  ? -9.449  -17.804 19.515 1.00 32.97  ? 356 HIS   A NE2 1 
ATOM   387  N N   . MET   A 1 65  ? -3.347  -19.847 17.541 1.00 20.65  ? 357 MET   A N   1 
ATOM   388  C CA  . MET   A 1 65  ? -1.915  -19.952 17.288 1.00 25.32  ? 357 MET   A CA  1 
ATOM   389  C C   . MET   A 1 65  ? -1.586  -19.674 15.828 1.00 24.55  ? 357 MET   A C   1 
ATOM   390  O O   . MET   A 1 65  ? -0.512  -19.142 15.525 1.00 26.14  ? 357 MET   A O   1 
ATOM   391  C CB  . MET   A 1 65  ? -1.410  -21.339 17.685 1.00 28.63  ? 357 MET   A CB  1 
ATOM   392  C CG  . MET   A 1 65  ? 0.104   -21.452 17.739 1.00 23.61  ? 357 MET   A CG  1 
ATOM   393  S SD  . MET   A 1 65  ? 0.665   -23.162 17.810 1.00 24.54  ? 357 MET   A SD  1 
ATOM   394  C CE  . MET   A 1 65  ? -0.084  -23.691 19.348 1.00 22.99  ? 357 MET   A CE  1 
ATOM   395  N N   . ILE   A 1 66  ? -2.495  -20.022 14.915 1.00 25.48  ? 358 ILE   A N   1 
ATOM   396  C CA  . ILE   A 1 66  ? -2.261  -19.776 13.494 1.00 26.51  ? 358 ILE   A CA  1 
ATOM   397  C C   . ILE   A 1 66  ? -2.193  -18.279 13.224 1.00 22.61  ? 358 ILE   A C   1 
ATOM   398  O O   . ILE   A 1 66  ? -1.275  -17.791 12.553 1.00 28.63  ? 358 ILE   A O   1 
ATOM   399  C CB  . ILE   A 1 66  ? -3.355  -20.451 12.645 1.00 36.44  ? 358 ILE   A CB  1 
ATOM   400  C CG1 . ILE   A 1 66  ? -3.258  -21.975 12.741 1.00 44.24  ? 358 ILE   A CG1 1 
ATOM   401  C CG2 . ILE   A 1 66  ? -3.251  -20.006 11.192 1.00 46.35  ? 358 ILE   A CG2 1 
ATOM   402  C CD1 . ILE   A 1 66  ? -1.849  -22.501 12.763 1.00 36.90  ? 358 ILE   A CD1 1 
ATOM   403  N N   . ASN   A 1 67  ? -3.170  -17.528 13.742 1.00 24.23  ? 359 ASN   A N   1 
ATOM   404  C CA  . ASN   A 1 67  ? -3.163  -16.078 13.573 1.00 27.06  ? 359 ASN   A CA  1 
ATOM   405  C C   . ASN   A 1 67  ? -1.937  -15.452 14.216 1.00 31.14  ? 359 ASN   A C   1 
ATOM   406  O O   . ASN   A 1 67  ? -1.333  -14.532 13.653 1.00 30.11  ? 359 ASN   A O   1 
ATOM   407  C CB  . ASN   A 1 67  ? -4.423  -15.464 14.175 1.00 36.77  ? 359 ASN   A CB  1 
ATOM   408  C CG  . ASN   A 1 67  ? -5.684  -15.992 13.552 1.00 51.09  ? 359 ASN   A CG  1 
ATOM   409  O OD1 . ASN   A 1 67  ? -5.654  -16.717 12.557 1.00 52.54  ? 359 ASN   A OD1 1 
ATOM   410  N ND2 . ASN   A 1 67  ? -6.813  -15.622 14.132 1.00 56.98  ? 359 ASN   A ND2 1 
ATOM   411  N N   . TRP   A 1 68  ? -1.574  -15.920 15.412 1.00 23.87  ? 360 TRP   A N   1 
ATOM   412  C CA  . TRP   A 1 68  ? -0.393  -15.396 16.088 1.00 27.19  ? 360 TRP   A CA  1 
ATOM   413  C C   . TRP   A 1 68  ? 0.856   -15.599 15.240 1.00 21.20  ? 360 TRP   A C   1 
ATOM   414  O O   . TRP   A 1 68  ? 1.684   -14.691 15.106 1.00 26.33  ? 360 TRP   A O   1 
ATOM   415  C CB  . TRP   A 1 68  ? -0.229  -16.067 17.450 1.00 21.56  ? 360 TRP   A CB  1 
ATOM   416  C CG  . TRP   A 1 68  ? 1.137   -15.882 18.027 1.00 24.31  ? 360 TRP   A CG  1 
ATOM   417  C CD1 . TRP   A 1 68  ? 1.613   -14.777 18.668 1.00 20.78  ? 360 TRP   A CD1 1 
ATOM   418  C CD2 . TRP   A 1 68  ? 2.215   -16.824 17.995 1.00 18.90  ? 360 TRP   A CD2 1 
ATOM   419  N NE1 . TRP   A 1 68  ? 2.918   -14.976 19.049 1.00 24.56  ? 360 TRP   A NE1 1 
ATOM   420  C CE2 . TRP   A 1 68  ? 3.312   -16.225 18.646 1.00 18.66  ? 360 TRP   A CE2 1 
ATOM   421  C CE3 . TRP   A 1 68  ? 2.358   -18.118 17.484 1.00 23.06  ? 360 TRP   A CE3 1 
ATOM   422  C CZ2 . TRP   A 1 68  ? 4.534   -16.875 18.799 1.00 22.33  ? 360 TRP   A CZ2 1 
ATOM   423  C CZ3 . TRP   A 1 68  ? 3.572   -18.760 17.637 1.00 17.31  ? 360 TRP   A CZ3 1 
ATOM   424  C CH2 . TRP   A 1 68  ? 4.644   -18.139 18.289 1.00 17.35  ? 360 TRP   A CH2 1 
ATOM   425  N N   . ALA   A 1 69  ? 1.007   -16.793 14.661 1.00 24.04  ? 361 ALA   A N   1 
ATOM   426  C CA  . ALA   A 1 69  ? 2.176   -17.082 13.837 1.00 22.88  ? 361 ALA   A CA  1 
ATOM   427  C C   . ALA   A 1 69  ? 2.250   -16.144 12.639 1.00 24.32  ? 361 ALA   A C   1 
ATOM   428  O O   . ALA   A 1 69  ? 3.313   -15.592 12.333 1.00 26.16  ? 361 ALA   A O   1 
ATOM   429  C CB  . ALA   A 1 69  ? 2.147   -18.540 13.381 1.00 25.17  ? 361 ALA   A CB  1 
ATOM   430  N N   . LYS   A 1 70  ? 1.120   -15.941 11.956 1.00 26.53  ? 362 LYS   A N   1 
ATOM   431  C CA  . LYS   A 1 70  ? 1.089   -15.047 10.803 1.00 24.40  ? 362 LYS   A CA  1 
ATOM   432  C C   . LYS   A 1 70  ? 1.440   -13.612 11.170 1.00 27.07  ? 362 LYS   A C   1 
ATOM   433  O O   . LYS   A 1 70  ? 1.793   -12.826 10.284 1.00 26.55  ? 362 LYS   A O   1 
ATOM   434  C CB  . LYS   A 1 70  ? -0.291  -15.088 10.144 1.00 31.45  ? 362 LYS   A CB  1 
ATOM   435  C CG  . LYS   A 1 70  ? -0.642  -16.425 9.509  1.00 35.77  ? 362 LYS   A CG  1 
ATOM   436  C CD  . LYS   A 1 70  ? -2.126  -16.507 9.192  1.00 42.42  ? 362 LYS   A CD  1 
ATOM   437  C CE  . LYS   A 1 70  ? -2.450  -15.780 7.899  1.00 44.37  ? 362 LYS   A CE  1 
ATOM   438  N NZ  . LYS   A 1 70  ? -2.648  -16.720 6.761  1.00 68.92  ? 362 LYS   A NZ  1 
ATOM   439  N N   . ARG   A 1 71  ? 1.349   -13.250 12.446 1.00 32.12  ? 363 ARG   A N   1 
ATOM   440  C CA  . ARG   A 1 71  ? 1.687   -11.908 12.895 1.00 33.46  ? 363 ARG   A CA  1 
ATOM   441  C C   . ARG   A 1 71  ? 3.080   -11.819 13.504 1.00 32.15  ? 363 ARG   A C   1 
ATOM   442  O O   . ARG   A 1 71  ? 3.502   -10.727 13.894 1.00 34.86  ? 363 ARG   A O   1 
ATOM   443  C CB  . ARG   A 1 71  ? 0.642   -11.411 13.898 1.00 30.96  ? 363 ARG   A CB  1 
ATOM   444  C CG  . ARG   A 1 71  ? -0.757  -11.303 13.308 1.00 40.80  ? 363 ARG   A CG  1 
ATOM   445  C CD  . ARG   A 1 71  ? -1.745  -10.693 14.300 1.00 51.91  ? 363 ARG   A CD  1 
ATOM   446  N NE  . ARG   A 1 71  ? -1.392  -9.377  14.834 1.00 61.51  ? 363 ARG   A NE  1 
ATOM   447  C CZ  . ARG   A 1 71  ? -0.887  -8.351  14.156 1.00 68.38  ? 363 ARG   A CZ  1 
ATOM   448  N NH1 . ARG   A 1 71  ? -0.740  -8.385  12.842 1.00 68.42  ? 363 ARG   A NH1 1 
ATOM   449  N NH2 . ARG   A 1 71  ? -0.550  -7.246  14.816 1.00 68.54  ? 363 ARG   A NH2 1 
ATOM   450  N N   . VAL   A 1 72  ? 3.796   -12.934 13.601 1.00 24.34  ? 364 VAL   A N   1 
ATOM   451  C CA  . VAL   A 1 72  ? 5.201   -12.912 14.000 1.00 24.40  ? 364 VAL   A CA  1 
ATOM   452  C C   . VAL   A 1 72  ? 5.993   -12.369 12.817 1.00 28.02  ? 364 VAL   A C   1 
ATOM   453  O O   . VAL   A 1 72  ? 5.911   -12.928 11.714 1.00 30.11  ? 364 VAL   A O   1 
ATOM   454  C CB  . VAL   A 1 72  ? 5.690   -14.305 14.426 1.00 23.09  ? 364 VAL   A CB  1 
ATOM   455  C CG1 . VAL   A 1 72  ? 7.207   -14.330 14.517 1.00 23.13  ? 364 VAL   A CG1 1 
ATOM   456  C CG2 . VAL   A 1 72  ? 5.062   -14.699 15.756 1.00 21.88  ? 364 VAL   A CG2 1 
ATOM   457  N N   . PRO   A 1 73  ? 6.749   -11.285 12.993 1.00 30.86  ? 365 PRO   A N   1 
ATOM   458  C CA  . PRO   A 1 73  ? 7.420   -10.650 11.850 1.00 29.29  ? 365 PRO   A CA  1 
ATOM   459  C C   . PRO   A 1 73  ? 8.315   -11.625 11.096 1.00 34.32  ? 365 PRO   A C   1 
ATOM   460  O O   . PRO   A 1 73  ? 9.142   -12.324 11.686 1.00 26.99  ? 365 PRO   A O   1 
ATOM   461  C CB  . PRO   A 1 73  ? 8.233   -9.525  12.501 1.00 35.33  ? 365 PRO   A CB  1 
ATOM   462  C CG  . PRO   A 1 73  ? 7.496   -9.209  13.756 1.00 31.52  ? 365 PRO   A CG  1 
ATOM   463  C CD  . PRO   A 1 73  ? 6.903   -10.505 14.234 1.00 25.51  ? 365 PRO   A CD  1 
ATOM   464  N N   . GLY   A 1 74  ? 8.133   -11.669 9.775  1.00 26.01  ? 366 GLY   A N   1 
ATOM   465  C CA  . GLY   A 1 74  ? 8.906   -12.535 8.914  1.00 29.04  ? 366 GLY   A CA  1 
ATOM   466  C C   . GLY   A 1 74  ? 8.289   -13.888 8.634  1.00 36.81  ? 366 GLY   A C   1 
ATOM   467  O O   . GLY   A 1 74  ? 8.747   -14.578 7.714  1.00 33.09  ? 366 GLY   A O   1 
ATOM   468  N N   . PHE   A 1 75  ? 7.261   -14.287 9.387  1.00 23.63  ? 367 PHE   A N   1 
ATOM   469  C CA  . PHE   A 1 75  ? 6.691   -15.621 9.212  1.00 25.61  ? 367 PHE   A CA  1 
ATOM   470  C C   . PHE   A 1 75  ? 5.954   -15.748 7.885  1.00 24.95  ? 367 PHE   A C   1 
ATOM   471  O O   . PHE   A 1 75  ? 6.099   -16.757 7.186  1.00 29.46  ? 367 PHE   A O   1 
ATOM   472  C CB  . PHE   A 1 75  ? 5.756   -15.950 10.374 1.00 24.87  ? 367 PHE   A CB  1 
ATOM   473  C CG  . PHE   A 1 75  ? 5.273   -17.371 10.377 1.00 23.36  ? 367 PHE   A CG  1 
ATOM   474  C CD1 . PHE   A 1 75  ? 6.103   -18.398 10.794 1.00 28.56  ? 367 PHE   A CD1 1 
ATOM   475  C CD2 . PHE   A 1 75  ? 3.989   -17.682 9.961  1.00 26.25  ? 367 PHE   A CD2 1 
ATOM   476  C CE1 . PHE   A 1 75  ? 5.663   -19.708 10.796 1.00 26.02  ? 367 PHE   A CE1 1 
ATOM   477  C CE2 . PHE   A 1 75  ? 3.541   -18.991 9.962  1.00 24.27  ? 367 PHE   A CE2 1 
ATOM   478  C CZ  . PHE   A 1 75  ? 4.380   -20.005 10.380 1.00 24.30  ? 367 PHE   A CZ  1 
ATOM   479  N N   . VAL   A 1 76  ? 5.154   -14.741 7.521  1.00 29.31  ? 368 VAL   A N   1 
ATOM   480  C CA  . VAL   A 1 76  ? 4.410   -14.797 6.263  1.00 26.70  ? 368 VAL   A CA  1 
ATOM   481  C C   . VAL   A 1 76  ? 5.279   -14.547 5.043  1.00 38.13  ? 368 VAL   A C   1 
ATOM   482  O O   . VAL   A 1 76  ? 4.795   -14.695 3.913  1.00 30.91  ? 368 VAL   A O   1 
ATOM   483  C CB  . VAL   A 1 76  ? 3.243   -13.792 6.256  1.00 33.78  ? 368 VAL   A CB  1 
ATOM   484  C CG1 . VAL   A 1 76  ? 2.270   -14.105 7.380  1.00 38.90  ? 368 VAL   A CG1 1 
ATOM   485  C CG2 . VAL   A 1 76  ? 3.766   -12.371 6.376  1.00 29.13  ? 368 VAL   A CG2 1 
ATOM   486  N N   . ASP   A 1 77  ? 6.546   -14.167 5.230  1.00 27.22  ? 369 ASP   A N   1 
ATOM   487  C CA  . ASP   A 1 77  ? 7.457   -14.073 4.096  1.00 34.66  ? 369 ASP   A CA  1 
ATOM   488  C C   . ASP   A 1 77  ? 7.846   -15.444 3.564  1.00 35.77  ? 369 ASP   A C   1 
ATOM   489  O O   . ASP   A 1 77  ? 8.329   -15.541 2.431  1.00 33.63  ? 369 ASP   A O   1 
ATOM   490  C CB  . ASP   A 1 77  ? 8.716   -13.293 4.482  1.00 41.44  ? 369 ASP   A CB  1 
ATOM   491  C CG  . ASP   A 1 77  ? 8.422   -11.853 4.843  1.00 37.00  ? 369 ASP   A CG  1 
ATOM   492  O OD1 . ASP   A 1 77  ? 7.494   -11.267 4.247  1.00 40.16  ? 369 ASP   A OD1 1 
ATOM   493  O OD2 . ASP   A 1 77  ? 9.122   -11.304 5.720  1.00 44.88  ? 369 ASP   A OD2 1 
ATOM   494  N N   . LEU   A 1 78  ? 7.646   -16.496 4.352  1.00 32.52  ? 370 LEU   A N   1 
ATOM   495  C CA  . LEU   A 1 78  ? 7.956   -17.853 3.938  1.00 32.90  ? 370 LEU   A CA  1 
ATOM   496  C C   . LEU   A 1 78  ? 6.820   -18.430 3.096  1.00 30.40  ? 370 LEU   A C   1 
ATOM   497  O O   . LEU   A 1 78  ? 5.691   -17.930 3.099  1.00 27.83  ? 370 LEU   A O   1 
ATOM   498  C CB  . LEU   A 1 78  ? 8.189   -18.742 5.158  1.00 36.01  ? 370 LEU   A CB  1 
ATOM   499  C CG  . LEU   A 1 78  ? 9.116   -18.191 6.240  1.00 27.50  ? 370 LEU   A CG  1 
ATOM   500  C CD1 . LEU   A 1 78  ? 9.012   -19.047 7.488  1.00 22.52  ? 370 LEU   A CD1 1 
ATOM   501  C CD2 . LEU   A 1 78  ? 10.547  -18.137 5.739  1.00 24.47  ? 370 LEU   A CD2 1 
ATOM   502  N N   . THR   A 1 79  ? 7.135   -19.494 2.364  1.00 30.57  ? 371 THR   A N   1 
ATOM   503  C CA  . THR   A 1 79  ? 6.102   -20.257 1.678  1.00 36.62  ? 371 THR   A CA  1 
ATOM   504  C C   . THR   A 1 79  ? 5.199   -20.926 2.705  1.00 30.93  ? 371 THR   A C   1 
ATOM   505  O O   . THR   A 1 79  ? 5.614   -21.209 3.831  1.00 27.45  ? 371 THR   A O   1 
ATOM   506  C CB  . THR   A 1 79  ? 6.729   -21.315 0.774  1.00 43.03  ? 371 THR   A CB  1 
ATOM   507  O OG1 . THR   A 1 79  ? 7.267   -22.369 1.584  1.00 33.92  ? 371 THR   A OG1 1 
ATOM   508  C CG2 . THR   A 1 79  ? 7.845   -20.707 -0.057 1.00 33.96  ? 371 THR   A CG2 1 
ATOM   509  N N   . LEU   A 1 80  ? 3.944   -21.177 2.322  1.00 29.35  ? 372 LEU   A N   1 
ATOM   510  C CA  . LEU   A 1 80  ? 3.049   -21.787 3.300  1.00 42.03  ? 372 LEU   A CA  1 
ATOM   511  C C   . LEU   A 1 80  ? 3.457   -23.215 3.624  1.00 30.36  ? 372 LEU   A C   1 
ATOM   512  O O   . LEU   A 1 80  ? 3.185   -23.694 4.730  1.00 29.45  ? 372 LEU   A O   1 
ATOM   513  C CB  . LEU   A 1 80  ? 1.592   -21.767 2.837  1.00 57.16  ? 372 LEU   A CB  1 
ATOM   514  C CG  . LEU   A 1 80  ? 0.966   -20.638 2.022  1.00 58.29  ? 372 LEU   A CG  1 
ATOM   515  C CD1 . LEU   A 1 80  ? -0.464  -21.062 1.645  1.00 49.40  ? 372 LEU   A CD1 1 
ATOM   516  C CD2 . LEU   A 1 80  ? 0.974   -19.300 2.769  1.00 54.07  ? 372 LEU   A CD2 1 
ATOM   517  N N   . HIS   A 1 81  ? 4.086   -23.915 2.675  1.00 32.43  ? 373 HIS   A N   1 
ATOM   518  C CA  . HIS   A 1 81  ? 4.605   -25.245 2.973  1.00 34.11  ? 373 HIS   A CA  1 
ATOM   519  C C   . HIS   A 1 81  ? 5.607   -25.189 4.117  1.00 27.81  ? 373 HIS   A C   1 
ATOM   520  O O   . HIS   A 1 81  ? 5.589   -26.043 5.010  1.00 29.92  ? 373 HIS   A O   1 
ATOM   521  C CB  . HIS   A 1 81  ? 5.240   -25.866 1.727  1.00 34.09  ? 373 HIS   A CB  1 
ATOM   522  C CG  . HIS   A 1 81  ? 5.999   -27.132 1.998  1.00 49.13  ? 373 HIS   A CG  1 
ATOM   523  N ND1 . HIS   A 1 81  ? 7.298   -27.138 2.461  1.00 61.25  ? 373 HIS   A ND1 1 
ATOM   524  C CD2 . HIS   A 1 81  ? 5.641   -28.433 1.871  1.00 59.63  ? 373 HIS   A CD2 1 
ATOM   525  C CE1 . HIS   A 1 81  ? 7.706   -28.386 2.609  1.00 61.82  ? 373 HIS   A CE1 1 
ATOM   526  N NE2 . HIS   A 1 81  ? 6.720   -29.191 2.258  1.00 63.62  ? 373 HIS   A NE2 1 
ATOM   527  N N   . ASP   A 1 82  ? 6.488   -24.186 4.109  1.00 30.92  ? 374 ASP   A N   1 
ATOM   528  C CA  . ASP   A 1 82  ? 7.422   -24.009 5.214  1.00 26.79  ? 374 ASP   A CA  1 
ATOM   529  C C   . ASP   A 1 82  ? 6.736   -23.440 6.448  1.00 25.55  ? 374 ASP   A C   1 
ATOM   530  O O   . ASP   A 1 82  ? 7.160   -23.727 7.573  1.00 24.09  ? 374 ASP   A O   1 
ATOM   531  C CB  . ASP   A 1 82  ? 8.582   -23.110 4.786  1.00 34.76  ? 374 ASP   A CB  1 
ATOM   532  C CG  . ASP   A 1 82  ? 9.523   -23.801 3.818  1.00 40.28  ? 374 ASP   A CG  1 
ATOM   533  O OD1 . ASP   A 1 82  ? 9.319   -25.003 3.552  1.00 39.86  ? 374 ASP   A OD1 1 
ATOM   534  O OD2 . ASP   A 1 82  ? 10.465  -23.147 3.324  1.00 37.77  ? 374 ASP   A OD2 1 
ATOM   535  N N   . GLN   A 1 83  ? 5.685   -22.636 6.264  1.00 24.71  ? 375 GLN   A N   1 
ATOM   536  C CA  . GLN   A 1 83  ? 4.889   -22.203 7.406  1.00 27.73  ? 375 GLN   A CA  1 
ATOM   537  C C   . GLN   A 1 83  ? 4.208   -23.389 8.077  1.00 23.05  ? 375 GLN   A C   1 
ATOM   538  O O   . GLN   A 1 83  ? 4.128   -23.453 9.310  1.00 22.71  ? 375 GLN   A O   1 
ATOM   539  C CB  . GLN   A 1 83  ? 3.851   -21.168 6.969  1.00 23.94  ? 375 GLN   A CB  1 
ATOM   540  C CG  . GLN   A 1 83  ? 4.428   -19.816 6.581  1.00 24.85  ? 375 GLN   A CG  1 
ATOM   541  C CD  . GLN   A 1 83  ? 3.366   -18.860 6.070  1.00 31.53  ? 375 GLN   A CD  1 
ATOM   542  O OE1 . GLN   A 1 83  ? 2.290   -18.740 6.656  1.00 31.08  ? 375 GLN   A OE1 1 
ATOM   543  N NE2 . GLN   A 1 83  ? 3.663   -18.177 4.971  1.00 32.60  ? 375 GLN   A NE2 1 
ATOM   544  N N   . VAL   A 1 84  ? 3.716   -24.341 7.281  1.00 27.40  ? 376 VAL   A N   1 
ATOM   545  C CA  . VAL   A 1 84  ? 3.075   -25.526 7.845  1.00 30.45  ? 376 VAL   A CA  1 
ATOM   546  C C   . VAL   A 1 84  ? 4.091   -26.384 8.588  1.00 28.46  ? 376 VAL   A C   1 
ATOM   547  O O   . VAL   A 1 84  ? 3.826   -26.858 9.700  1.00 26.63  ? 376 VAL   A O   1 
ATOM   548  C CB  . VAL   A 1 84  ? 2.359   -26.327 6.741  1.00 35.79  ? 376 VAL   A CB  1 
ATOM   549  C CG1 . VAL   A 1 84  ? 1.927   -27.687 7.267  1.00 31.20  ? 376 VAL   A CG1 1 
ATOM   550  C CG2 . VAL   A 1 84  ? 1.153   -25.561 6.223  1.00 27.29  ? 376 VAL   A CG2 1 
ATOM   551  N N   . HIS   A 1 85  ? 5.269   -26.597 7.993  1.00 26.59  ? 377 HIS   A N   1 
ATOM   552  C CA  . HIS   A 1 85  ? 6.278   -27.434 8.638  1.00 26.60  ? 377 HIS   A CA  1 
ATOM   553  C C   . HIS   A 1 85  ? 6.739   -26.833 9.959  1.00 24.73  ? 377 HIS   A C   1 
ATOM   554  O O   . HIS   A 1 85  ? 6.908   -27.553 10.950 1.00 27.39  ? 377 HIS   A O   1 
ATOM   555  C CB  . HIS   A 1 85  ? 7.473   -27.643 7.710  1.00 27.30  ? 377 HIS   A CB  1 
ATOM   556  C CG  . HIS   A 1 85  ? 8.574   -28.450 8.325  1.00 37.71  ? 377 HIS   A CG  1 
ATOM   557  N ND1 . HIS   A 1 85  ? 8.492   -29.817 8.490  0.51 38.52  ? 377 HIS   A ND1 1 
ATOM   558  C CD2 . HIS   A 1 85  ? 9.770   -28.081 8.841  1.00 34.29  ? 377 HIS   A CD2 1 
ATOM   559  C CE1 . HIS   A 1 85  ? 9.597   -30.255 9.067  0.69 42.96  ? 377 HIS   A CE1 1 
ATOM   560  N NE2 . HIS   A 1 85  ? 10.389  -29.222 9.290  1.00 36.46  ? 377 HIS   A NE2 1 
ATOM   561  N N   . LEU   A 1 86  ? 6.952   -25.515 9.992  1.00 27.59  ? 378 LEU   A N   1 
ATOM   562  C CA  . LEU   A 1 86  ? 7.374   -24.868 11.231 1.00 21.52  ? 378 LEU   A CA  1 
ATOM   563  C C   . LEU   A 1 86  ? 6.316   -25.009 12.315 1.00 20.65  ? 378 LEU   A C   1 
ATOM   564  O O   . LEU   A 1 86  ? 6.640   -25.267 13.480 1.00 22.33  ? 378 LEU   A O   1 
ATOM   565  C CB  . LEU   A 1 86  ? 7.684   -23.393 10.978 1.00 20.22  ? 378 LEU   A CB  1 
ATOM   566  C CG  . LEU   A 1 86  ? 9.010   -23.068 10.288 1.00 25.63  ? 378 LEU   A CG  1 
ATOM   567  C CD1 . LEU   A 1 86  ? 9.179   -21.565 10.149 1.00 20.54  ? 378 LEU   A CD1 1 
ATOM   568  C CD2 . LEU   A 1 86  ? 10.177  -23.671 11.055 1.00 20.68  ? 378 LEU   A CD2 1 
ATOM   569  N N   . LEU   A 1 87  ? 5.044   -24.846 11.953 1.00 22.37  ? 379 LEU   A N   1 
ATOM   570  C CA  . LEU   A 1 87  ? 3.982   -24.962 12.944 1.00 25.86  ? 379 LEU   A CA  1 
ATOM   571  C C   . LEU   A 1 87  ? 3.730   -26.414 13.328 1.00 19.96  ? 379 LEU   A C   1 
ATOM   572  O O   . LEU   A 1 87  ? 3.383   -26.695 14.480 1.00 24.38  ? 379 LEU   A O   1 
ATOM   573  C CB  . LEU   A 1 87  ? 2.708   -24.306 12.418 1.00 24.81  ? 379 LEU   A CB  1 
ATOM   574  C CG  . LEU   A 1 87  ? 2.582   -22.835 12.820 1.00 30.93  ? 379 LEU   A CG  1 
ATOM   575  C CD1 . LEU   A 1 87  ? 1.602   -22.110 11.923 1.00 27.85  ? 379 LEU   A CD1 1 
ATOM   576  C CD2 . LEU   A 1 87  ? 2.166   -22.716 14.277 1.00 33.43  ? 379 LEU   A CD2 1 
ATOM   577  N N   . GLU   A 1 88  ? 3.901   -27.345 12.386 1.00 23.53  ? 380 GLU   A N   1 
ATOM   578  C CA  . GLU   A 1 88  ? 3.798   -28.763 12.719 1.00 29.17  ? 380 GLU   A CA  1 
ATOM   579  C C   . GLU   A 1 88  ? 4.852   -29.162 13.743 1.00 33.98  ? 380 GLU   A C   1 
ATOM   580  O O   . GLU   A 1 88  ? 4.591   -29.984 14.629 1.00 30.63  ? 380 GLU   A O   1 
ATOM   581  C CB  . GLU   A 1 88  ? 3.942   -29.612 11.457 1.00 29.90  ? 380 GLU   A CB  1 
ATOM   582  C CG  . GLU   A 1 88  ? 2.703   -30.404 11.080 1.00 41.08  ? 380 GLU   A CG  1 
ATOM   583  C CD  . GLU   A 1 88  ? 2.945   -31.320 9.896  1.00 62.28  ? 380 GLU   A CD  1 
ATOM   584  O OE1 . GLU   A 1 88  ? 2.797   -30.860 8.744  1.00 65.64  ? 380 GLU   A OE1 1 
ATOM   585  O OE2 . GLU   A 1 88  ? 3.288   -32.499 10.118 1.00 68.67  ? 380 GLU   A OE2 1 
ATOM   586  N N   . SER   A 1 89  ? 6.050   -28.587 13.636 1.00 24.73  ? 381 SER   A N   1 
ATOM   587  C CA  . SER   A 1 89  ? 7.142   -28.947 14.530 1.00 23.94  ? 381 SER   A CA  1 
ATOM   588  C C   . SER   A 1 89  ? 7.037   -28.255 15.882 1.00 20.28  ? 381 SER   A C   1 
ATOM   589  O O   . SER   A 1 89  ? 7.552   -28.775 16.877 1.00 28.41  ? 381 SER   A O   1 
ATOM   590  C CB  . SER   A 1 89  ? 8.484   -28.603 13.881 1.00 21.71  ? 381 SER   A CB  1 
ATOM   591  O OG  . SER   A 1 89  ? 8.641   -29.265 12.638 1.00 42.50  ? 381 SER   A OG  1 
ATOM   592  N N   . ALA   A 1 90  ? 6.373   -27.101 15.946 1.00 18.91  ? 382 ALA   A N   1 
ATOM   593  C CA  . ALA   A 1 90  ? 6.436   -26.246 17.122 1.00 21.10  ? 382 ALA   A CA  1 
ATOM   594  C C   . ALA   A 1 90  ? 5.125   -26.115 17.887 1.00 20.37  ? 382 ALA   A C   1 
ATOM   595  O O   . ALA   A 1 90  ? 5.137   -25.555 18.989 1.00 19.50  ? 382 ALA   A O   1 
ATOM   596  C CB  . ALA   A 1 90  ? 6.914   -24.841 16.723 1.00 18.45  ? 382 ALA   A CB  1 
ATOM   597  N N   . TRP   A 1 91  ? 4.006   -26.614 17.349 1.00 19.21  ? 383 TRP   A N   1 
ATOM   598  C CA  . TRP   A 1 91  ? 2.706   -26.304 17.943 1.00 19.53  ? 383 TRP   A CA  1 
ATOM   599  C C   . TRP   A 1 91  ? 2.607   -26.803 19.380 1.00 19.76  ? 383 TRP   A C   1 
ATOM   600  O O   . TRP   A 1 91  ? 2.082   -26.099 20.251 1.00 20.08  ? 383 TRP   A O   1 
ATOM   601  C CB  . TRP   A 1 91  ? 1.573   -26.891 17.097 1.00 24.03  ? 383 TRP   A CB  1 
ATOM   602  C CG  . TRP   A 1 91  ? 1.481   -28.385 17.142 1.00 18.99  ? 383 TRP   A CG  1 
ATOM   603  C CD1 . TRP   A 1 91  ? 2.126   -29.268 16.330 1.00 20.10  ? 383 TRP   A CD1 1 
ATOM   604  C CD2 . TRP   A 1 91  ? 0.705   -29.171 18.054 1.00 19.90  ? 383 TRP   A CD2 1 
ATOM   605  N NE1 . TRP   A 1 91  ? 1.798   -30.556 16.676 1.00 28.50  ? 383 TRP   A NE1 1 
ATOM   606  C CE2 . TRP   A 1 91  ? 0.928   -30.524 17.733 1.00 24.29  ? 383 TRP   A CE2 1 
ATOM   607  C CE3 . TRP   A 1 91  ? -0.157  -28.862 19.111 1.00 28.41  ? 383 TRP   A CE3 1 
ATOM   608  C CZ2 . TRP   A 1 91  ? 0.319   -31.567 18.428 1.00 26.98  ? 383 TRP   A CZ2 1 
ATOM   609  C CZ3 . TRP   A 1 91  ? -0.760  -29.900 19.800 1.00 29.59  ? 383 TRP   A CZ3 1 
ATOM   610  C CH2 . TRP   A 1 91  ? -0.518  -31.235 19.456 1.00 22.49  ? 383 TRP   A CH2 1 
ATOM   611  N N   . LEU   A 1 92  ? 3.106   -28.010 19.655 1.00 17.74  ? 384 LEU   A N   1 
ATOM   612  C CA  . LEU   A 1 92  ? 3.018   -28.525 21.017 1.00 23.62  ? 384 LEU   A CA  1 
ATOM   613  C C   . LEU   A 1 92  ? 3.931   -27.747 21.955 1.00 21.39  ? 384 LEU   A C   1 
ATOM   614  O O   . LEU   A 1 92  ? 3.549   -27.450 23.092 1.00 16.98  ? 384 LEU   A O   1 
ATOM   615  C CB  . LEU   A 1 92  ? 3.350   -30.017 21.052 1.00 18.88  ? 384 LEU   A CB  1 
ATOM   616  C CG  . LEU   A 1 92  ? 3.074   -30.663 22.413 1.00 23.31  ? 384 LEU   A CG  1 
ATOM   617  C CD1 . LEU   A 1 92  ? 1.636   -30.406 22.840 1.00 18.46  ? 384 LEU   A CD1 1 
ATOM   618  C CD2 . LEU   A 1 92  ? 3.368   -32.151 22.397 1.00 20.79  ? 384 LEU   A CD2 1 
ATOM   619  N N   . GLU   A 1 93  ? 5.136   -27.400 21.492 1.00 23.53  ? 385 GLU   A N   1 
ATOM   620  C CA  . GLU   A 1 93  ? 6.030   -26.565 22.290 1.00 20.58  ? 385 GLU   A CA  1 
ATOM   621  C C   . GLU   A 1 93  ? 5.382   -25.230 22.635 1.00 20.40  ? 385 GLU   A C   1 
ATOM   622  O O   . GLU   A 1 93  ? 5.506   -24.745 23.766 1.00 18.19  ? 385 GLU   A O   1 
ATOM   623  C CB  . GLU   A 1 93  ? 7.341   -26.333 21.539 1.00 22.46  ? 385 GLU   A CB  1 
ATOM   624  C CG  . GLU   A 1 93  ? 8.344   -27.466 21.638 1.00 27.86  ? 385 GLU   A CG  1 
ATOM   625  C CD  . GLU   A 1 93  ? 9.555   -27.248 20.751 1.00 28.77  ? 385 GLU   A CD  1 
ATOM   626  O OE1 . GLU   A 1 93  ? 9.474   -27.565 19.546 1.00 35.84  ? 385 GLU   A OE1 1 
ATOM   627  O OE2 . GLU   A 1 93  ? 10.588  -26.764 21.259 1.00 29.72  ? 385 GLU   A OE2 1 
ATOM   628  N N   . ILE   A 1 94  ? 4.692   -24.618 21.670 1.00 18.96  ? 386 ILE   A N   1 
ATOM   629  C CA  . ILE   A 1 94  ? 4.061   -23.324 21.909 1.00 18.44  ? 386 ILE   A CA  1 
ATOM   630  C C   . ILE   A 1 94  ? 2.925   -23.463 22.916 1.00 18.01  ? 386 ILE   A C   1 
ATOM   631  O O   . ILE   A 1 94  ? 2.758   -22.617 23.803 1.00 18.70  ? 386 ILE   A O   1 
ATOM   632  C CB  . ILE   A 1 94  ? 3.580   -22.715 20.579 1.00 18.85  ? 386 ILE   A CB  1 
ATOM   633  C CG1 . ILE   A 1 94  ? 4.776   -22.232 19.755 1.00 24.42  ? 386 ILE   A CG1 1 
ATOM   634  C CG2 . ILE   A 1 94  ? 2.623   -21.559 20.827 1.00 15.64  ? 386 ILE   A CG2 1 
ATOM   635  C CD1 . ILE   A 1 94  ? 4.534   -22.242 18.260 1.00 35.33  ? 386 ILE   A CD1 1 
ATOM   636  N N   . LEU   A 1 95  ? 2.136   -24.535 22.806 1.00 15.25  ? 387 LEU   A N   1 
ATOM   637  C CA  . LEU   A 1 95  ? 1.081   -24.781 23.784 1.00 21.98  ? 387 LEU   A CA  1 
ATOM   638  C C   . LEU   A 1 95  ? 1.654   -24.951 25.186 1.00 24.06  ? 387 LEU   A C   1 
ATOM   639  O O   . LEU   A 1 95  ? 1.112   -24.407 26.155 1.00 19.70  ? 387 LEU   A O   1 
ATOM   640  C CB  . LEU   A 1 95  ? 0.269   -26.015 23.385 1.00 21.28  ? 387 LEU   A CB  1 
ATOM   641  C CG  . LEU   A 1 95  ? -0.759  -25.863 22.262 1.00 23.93  ? 387 LEU   A CG  1 
ATOM   642  C CD1 . LEU   A 1 95  ? -1.539  -27.157 22.076 1.00 22.05  ? 387 LEU   A CD1 1 
ATOM   643  C CD2 . LEU   A 1 95  ? -1.704  -24.704 22.545 1.00 20.12  ? 387 LEU   A CD2 1 
ATOM   644  N N   . MET   A 1 96  ? 2.757   -25.695 25.312 1.00 19.24  ? 388 MET   A N   1 
ATOM   645  C CA  . MET   A 1 96  ? 3.335   -25.943 26.629 1.00 18.19  ? 388 MET   A CA  1 
ATOM   646  C C   . MET   A 1 96  ? 3.936   -24.677 27.231 1.00 22.71  ? 388 MET   A C   1 
ATOM   647  O O   . MET   A 1 96  ? 3.750   -24.408 28.424 1.00 23.41  ? 388 MET   A O   1 
ATOM   648  C CB  . MET   A 1 96  ? 4.387   -27.050 26.547 1.00 23.00  ? 388 MET   A CB  1 
ATOM   649  C CG  . MET   A 1 96  ? 3.869   -28.370 25.999 1.00 24.10  ? 388 MET   A CG  1 
ATOM   650  S SD  . MET   A 1 96  ? 5.142   -29.646 25.967 1.00 20.96  ? 388 MET   A SD  1 
ATOM   651  C CE  . MET   A 1 96  ? 4.227   -31.065 26.552 1.00 19.51  ? 388 MET   A CE  1 
ATOM   652  N N   . ILE   A 1 97  ? 4.663   -23.891 26.431 1.00 16.66  ? 389 ILE   A N   1 
ATOM   653  C CA  . ILE   A 1 97  ? 5.274   -22.684 26.981 1.00 20.00  ? 389 ILE   A CA  1 
ATOM   654  C C   . ILE   A 1 97  ? 4.208   -21.654 27.332 1.00 19.06  ? 389 ILE   A C   1 
ATOM   655  O O   . ILE   A 1 97  ? 4.382   -20.870 28.273 1.00 23.20  ? 389 ILE   A O   1 
ATOM   656  C CB  . ILE   A 1 97  ? 6.329   -22.108 26.016 1.00 19.38  ? 389 ILE   A CB  1 
ATOM   657  C CG1 . ILE   A 1 97  ? 7.187   -21.067 26.741 1.00 17.37  ? 389 ILE   A CG1 1 
ATOM   658  C CG2 . ILE   A 1 97  ? 5.678   -21.501 24.780 1.00 16.66  ? 389 ILE   A CG2 1 
ATOM   659  C CD1 . ILE   A 1 97  ? 8.284   -20.466 25.893 1.00 18.07  ? 389 ILE   A CD1 1 
ATOM   660  N N   . GLY   A 1 98  ? 3.092   -21.636 26.600 1.00 18.27  ? 390 GLY   A N   1 
ATOM   661  C CA  . GLY   A 1 98  ? 1.973   -20.805 27.009 1.00 15.77  ? 390 GLY   A CA  1 
ATOM   662  C C   . GLY   A 1 98  ? 1.367   -21.277 28.316 1.00 23.09  ? 390 GLY   A C   1 
ATOM   663  O O   . GLY   A 1 98  ? 1.046   -20.468 29.191 1.00 19.81  ? 390 GLY   A O   1 
ATOM   664  N N   . LEU   A 1 99  ? 1.215   -22.594 28.469 1.00 20.65  ? 391 LEU   A N   1 
ATOM   665  C CA  . LEU   A 1 99  ? 0.756   -23.160 29.734 1.00 21.86  ? 391 LEU   A CA  1 
ATOM   666  C C   . LEU   A 1 99  ? 1.724   -22.834 30.865 1.00 21.35  ? 391 LEU   A C   1 
ATOM   667  O O   . LEU   A 1 99  ? 1.311   -22.421 31.955 1.00 26.45  ? 391 LEU   A O   1 
ATOM   668  C CB  . LEU   A 1 99  ? 0.587   -24.673 29.592 1.00 17.78  ? 391 LEU   A CB  1 
ATOM   669  C CG  . LEU   A 1 99  ? 0.254   -25.449 30.868 1.00 19.19  ? 391 LEU   A CG  1 
ATOM   670  C CD1 . LEU   A 1 99  ? -1.073  -24.993 31.445 1.00 19.13  ? 391 LEU   A CD1 1 
ATOM   671  C CD2 . LEU   A 1 99  ? 0.249   -26.945 30.603 1.00 16.99  ? 391 LEU   A CD2 1 
ATOM   672  N N   . VAL   A 1 100 ? 3.022   -23.020 30.621 1.00 20.20  ? 392 VAL   A N   1 
ATOM   673  C CA  . VAL   A 1 100 ? 4.026   -22.749 31.646 1.00 20.73  ? 392 VAL   A CA  1 
ATOM   674  C C   . VAL   A 1 100 ? 4.018   -21.272 32.023 1.00 18.57  ? 392 VAL   A C   1 
ATOM   675  O O   . VAL   A 1 100 ? 4.181   -20.912 33.196 1.00 25.40  ? 392 VAL   A O   1 
ATOM   676  C CB  . VAL   A 1 100 ? 5.412   -23.213 31.157 1.00 23.29  ? 392 VAL   A CB  1 
ATOM   677  C CG1 . VAL   A 1 100 ? 6.509   -22.662 32.040 1.00 25.54  ? 392 VAL   A CG1 1 
ATOM   678  C CG2 . VAL   A 1 100 ? 5.476   -24.733 31.120 1.00 20.00  ? 392 VAL   A CG2 1 
ATOM   679  N N   . TRP   A 1 101 ? 3.815   -20.394 31.038 1.00 24.47  ? 393 TRP   A N   1 
ATOM   680  C CA  . TRP   A 1 101 ? 3.729   -18.965 31.322 1.00 20.80  ? 393 TRP   A CA  1 
ATOM   681  C C   . TRP   A 1 101 ? 2.488   -18.638 32.145 1.00 22.87  ? 393 TRP   A C   1 
ATOM   682  O O   . TRP   A 1 101 ? 2.560   -17.857 33.101 1.00 25.44  ? 393 TRP   A O   1 
ATOM   683  C CB  . TRP   A 1 101 ? 3.737   -18.178 30.010 1.00 20.68  ? 393 TRP   A CB  1 
ATOM   684  C CG  . TRP   A 1 101 ? 3.470   -16.708 30.155 1.00 21.49  ? 393 TRP   A CG  1 
ATOM   685  C CD1 . TRP   A 1 101 ? 2.353   -16.036 29.751 1.00 21.72  ? 393 TRP   A CD1 1 
ATOM   686  C CD2 . TRP   A 1 101 ? 4.344   -15.724 30.726 1.00 21.26  ? 393 TRP   A CD2 1 
ATOM   687  N NE1 . TRP   A 1 101 ? 2.473   -14.698 30.042 1.00 25.15  ? 393 TRP   A NE1 1 
ATOM   688  C CE2 . TRP   A 1 101 ? 3.686   -14.481 30.640 1.00 26.48  ? 393 TRP   A CE2 1 
ATOM   689  C CE3 . TRP   A 1 101 ? 5.616   -15.775 31.304 1.00 25.93  ? 393 TRP   A CE3 1 
ATOM   690  C CZ2 . TRP   A 1 101 ? 4.256   -13.300 31.112 1.00 24.38  ? 393 TRP   A CZ2 1 
ATOM   691  C CZ3 . TRP   A 1 101 ? 6.181   -14.601 31.771 1.00 33.81  ? 393 TRP   A CZ3 1 
ATOM   692  C CH2 . TRP   A 1 101 ? 5.500   -13.381 31.674 1.00 29.24  ? 393 TRP   A CH2 1 
ATOM   693  N N   . ARG   A 1 102 ? 1.343   -19.234 31.795 1.00 22.63  ? 394 ARG   A N   1 
ATOM   694  C CA  . ARG   A 1 102 ? 0.117   -18.995 32.552 1.00 23.37  ? 394 ARG   A CA  1 
ATOM   695  C C   . ARG   A 1 102 ? 0.229   -19.494 33.986 1.00 19.49  ? 394 ARG   A C   1 
ATOM   696  O O   . ARG   A 1 102 ? -0.354  -18.898 34.899 1.00 23.36  ? 394 ARG   A O   1 
ATOM   697  C CB  . ARG   A 1 102 ? -1.070  -19.672 31.864 1.00 24.59  ? 394 ARG   A CB  1 
ATOM   698  C CG  . ARG   A 1 102 ? -1.441  -19.088 30.516 1.00 28.79  ? 394 ARG   A CG  1 
ATOM   699  C CD  . ARG   A 1 102 ? -2.845  -19.514 30.110 1.00 31.54  ? 394 ARG   A CD  1 
ATOM   700  N NE  . ARG   A 1 102 ? -2.941  -20.945 29.844 1.00 23.15  ? 394 ARG   A NE  1 
ATOM   701  C CZ  . ARG   A 1 102 ? -2.494  -21.538 28.745 1.00 18.86  ? 394 ARG   A CZ  1 
ATOM   702  N NH1 . ARG   A 1 102 ? -1.879  -20.856 27.793 1.00 18.06  ? 394 ARG   A NH1 1 
ATOM   703  N NH2 . ARG   A 1 102 ? -2.672  -22.847 28.595 1.00 15.55  ? 394 ARG   A NH2 1 
ATOM   704  N N   . SER   A 1 103 ? 0.962   -20.583 34.204 1.00 23.58  ? 395 SER   A N   1 
ATOM   705  C CA  . SER   A 1 103 ? 1.070   -21.212 35.513 1.00 22.81  ? 395 SER   A CA  1 
ATOM   706  C C   . SER   A 1 103 ? 2.195   -20.636 36.360 1.00 30.29  ? 395 SER   A C   1 
ATOM   707  O O   . SER   A 1 103 ? 2.458   -21.158 37.449 1.00 29.55  ? 395 SER   A O   1 
ATOM   708  C CB  . SER   A 1 103 ? 1.275   -22.720 35.351 1.00 17.17  ? 395 SER   A CB  1 
ATOM   709  O OG  . SER   A 1 103 ? 0.404   -23.246 34.365 1.00 20.34  ? 395 SER   A OG  1 
ATOM   710  N N   . MET   A 1 104 ? 2.858   -19.576 35.890 1.00 27.97  ? 396 MET   A N   1 
ATOM   711  C CA  . MET   A 1 104 ? 4.012   -19.036 36.604 1.00 27.05  ? 396 MET   A CA  1 
ATOM   712  C C   . MET   A 1 104 ? 3.632   -18.556 37.999 1.00 26.68  ? 396 MET   A C   1 
ATOM   713  O O   . MET   A 1 104 ? 4.405   -18.716 38.951 1.00 32.41  ? 396 MET   A O   1 
ATOM   714  C CB  . MET   A 1 104 ? 4.631   -17.896 35.795 1.00 40.09  ? 396 MET   A CB  1 
ATOM   715  C CG  . MET   A 1 104 ? 6.071   -17.580 36.151 1.00 47.37  ? 396 MET   A CG  1 
ATOM   716  S SD  . MET   A 1 104 ? 6.827   -16.471 34.948 1.00 38.90  ? 396 MET   A SD  1 
ATOM   717  C CE  . MET   A 1 104 ? 7.251   -15.077 35.986 1.00 31.44  ? 396 MET   A CE  1 
ATOM   718  N N   . GLU   A 1 105 ? 2.448   -17.969 38.141 1.00 29.90  ? 397 GLU   A N   1 
ATOM   719  C CA  . GLU   A 1 105 ? 1.999   -17.410 39.408 1.00 26.28  ? 397 GLU   A CA  1 
ATOM   720  C C   . GLU   A 1 105 ? 1.191   -18.397 40.239 1.00 29.14  ? 397 GLU   A C   1 
ATOM   721  O O   . GLU   A 1 105 ? 0.533   -17.986 41.200 1.00 31.58  ? 397 GLU   A O   1 
ATOM   722  C CB  . GLU   A 1 105 ? 1.168   -16.150 39.157 1.00 28.91  ? 397 GLU   A CB  1 
ATOM   723  C CG  . GLU   A 1 105 ? 1.993   -14.930 38.796 1.00 38.21  ? 397 GLU   A CG  1 
ATOM   724  C CD  . GLU   A 1 105 ? 2.107   -14.732 37.299 1.00 38.08  ? 397 GLU   A CD  1 
ATOM   725  O OE1 . GLU   A 1 105 ? 1.696   -15.640 36.545 1.00 47.79  ? 397 GLU   A OE1 1 
ATOM   726  O OE2 . GLU   A 1 105 ? 2.607   -13.668 36.877 1.00 66.71  ? 397 GLU   A OE2 1 
ATOM   727  N N   . HIS   A 1 106 ? 1.223   -19.683 39.897 1.00 27.56  ? 398 HIS   A N   1 
ATOM   728  C CA  . HIS   A 1 106 ? 0.430   -20.708 40.573 1.00 23.50  ? 398 HIS   A CA  1 
ATOM   729  C C   . HIS   A 1 106 ? 1.341   -21.893 40.862 1.00 22.87  ? 398 HIS   A C   1 
ATOM   730  O O   . HIS   A 1 106 ? 1.357   -22.880 40.113 1.00 24.94  ? 398 HIS   A O   1 
ATOM   731  C CB  . HIS   A 1 106 ? -0.781  -21.096 39.725 1.00 22.40  ? 398 HIS   A CB  1 
ATOM   732  C CG  . HIS   A 1 106 ? -1.577  -19.918 39.255 1.00 39.32  ? 398 HIS   A CG  1 
ATOM   733  N ND1 . HIS   A 1 106 ? -2.660  -19.426 39.950 1.00 32.46  ? 398 HIS   A ND1 1 
ATOM   734  C CD2 . HIS   A 1 106 ? -1.421  -19.111 38.179 1.00 34.88  ? 398 HIS   A CD2 1 
ATOM   735  C CE1 . HIS   A 1 106 ? -3.150  -18.378 39.312 1.00 42.95  ? 398 HIS   A CE1 1 
ATOM   736  N NE2 . HIS   A 1 106 ? -2.414  -18.164 38.236 1.00 41.23  ? 398 HIS   A NE2 1 
ATOM   737  N N   . PRO   A 1 107 ? 2.122   -21.822 41.940 1.00 26.70  ? 399 PRO   A N   1 
ATOM   738  C CA  . PRO   A 1 107 ? 3.106   -22.876 42.215 1.00 29.60  ? 399 PRO   A CA  1 
ATOM   739  C C   . PRO   A 1 107 ? 2.445   -24.229 42.433 1.00 30.04  ? 399 PRO   A C   1 
ATOM   740  O O   . PRO   A 1 107 ? 1.400   -24.337 43.080 1.00 28.54  ? 399 PRO   A O   1 
ATOM   741  C CB  . PRO   A 1 107 ? 3.803   -22.381 43.487 1.00 33.48  ? 399 PRO   A CB  1 
ATOM   742  C CG  . PRO   A 1 107 ? 3.604   -20.900 43.471 1.00 30.29  ? 399 PRO   A CG  1 
ATOM   743  C CD  . PRO   A 1 107 ? 2.232   -20.705 42.893 1.00 34.46  ? 399 PRO   A CD  1 
ATOM   744  N N   . GLY   A 1 108 ? 3.070   -25.268 41.882 1.00 31.77  ? 400 GLY   A N   1 
ATOM   745  C CA  . GLY   A 1 108 ? 2.551   -26.614 42.003 1.00 31.15  ? 400 GLY   A CA  1 
ATOM   746  C C   . GLY   A 1 108 ? 1.278   -26.884 41.237 1.00 37.97  ? 400 GLY   A C   1 
ATOM   747  O O   . GLY   A 1 108 ? 0.676   -27.946 41.420 1.00 39.66  ? 400 GLY   A O   1 
ATOM   748  N N   . LYS   A 1 109 ? 0.847   -25.960 40.380 1.00 27.64  ? 401 LYS   A N   1 
ATOM   749  C CA  . LYS   A 1 109 ? -0.394  -26.111 39.638 1.00 22.95  ? 401 LYS   A CA  1 
ATOM   750  C C   . LYS   A 1 109 ? -0.191  -25.638 38.207 1.00 25.02  ? 401 LYS   A C   1 
ATOM   751  O O   . LYS   A 1 109 ? 0.682   -24.813 37.927 1.00 26.83  ? 401 LYS   A O   1 
ATOM   752  C CB  . LYS   A 1 109 ? -1.539  -25.325 40.290 1.00 24.34  ? 401 LYS   A CB  1 
ATOM   753  C CG  . LYS   A 1 109 ? -2.045  -25.933 41.586 1.00 43.42  ? 401 LYS   A CG  1 
ATOM   754  C CD  . LYS   A 1 109 ? -2.947  -24.967 42.334 1.00 35.52  ? 401 LYS   A CD  1 
ATOM   755  C CE  . LYS   A 1 109 ? -3.787  -25.692 43.372 1.00 45.84  ? 401 LYS   A CE  1 
ATOM   756  N NZ  . LYS   A 1 109 ? -2.955  -26.170 44.508 1.00 47.83  ? 401 LYS   A NZ  1 
ATOM   757  N N   . LEU   A 1 110 ? -1.009  -26.170 37.304 1.00 21.36  ? 402 LEU   A N   1 
ATOM   758  C CA  . LEU   A 1 110 ? -0.989  -25.796 35.896 1.00 24.02  ? 402 LEU   A CA  1 
ATOM   759  C C   . LEU   A 1 110 ? -2.297  -25.096 35.554 1.00 22.88  ? 402 LEU   A C   1 
ATOM   760  O O   . LEU   A 1 110 ? -3.373  -25.690 35.681 1.00 26.21  ? 402 LEU   A O   1 
ATOM   761  C CB  . LEU   A 1 110 ? -0.785  -27.021 35.004 1.00 17.41  ? 402 LEU   A CB  1 
ATOM   762  C CG  . LEU   A 1 110 ? 0.575   -27.712 35.111 1.00 31.54  ? 402 LEU   A CG  1 
ATOM   763  C CD1 . LEU   A 1 110 ? 0.631   -28.932 34.204 1.00 19.36  ? 402 LEU   A CD1 1 
ATOM   764  C CD2 . LEU   A 1 110 ? 1.694   -26.735 34.777 1.00 19.64  ? 402 LEU   A CD2 1 
ATOM   765  N N   . LEU   A 1 111 ? -2.202  -23.837 35.125 1.00 23.91  ? 403 LEU   A N   1 
ATOM   766  C CA  . LEU   A 1 111 ? -3.375  -23.065 34.717 1.00 25.40  ? 403 LEU   A CA  1 
ATOM   767  C C   . LEU   A 1 111 ? -3.603  -23.300 33.228 1.00 23.77  ? 403 LEU   A C   1 
ATOM   768  O O   . LEU   A 1 111 ? -3.162  -22.538 32.366 1.00 23.43  ? 403 LEU   A O   1 
ATOM   769  C CB  . LEU   A 1 111 ? -3.191  -21.587 35.047 1.00 23.97  ? 403 LEU   A CB  1 
ATOM   770  C CG  . LEU   A 1 111 ? -4.419  -20.667 35.011 1.00 31.11  ? 403 LEU   A CG  1 
ATOM   771  C CD1 . LEU   A 1 111 ? -4.234  -19.512 35.970 1.00 39.09  ? 403 LEU   A CD1 1 
ATOM   772  C CD2 . LEU   A 1 111 ? -4.669  -20.119 33.618 1.00 30.46  ? 403 LEU   A CD2 1 
ATOM   773  N N   . PHE   A 1 112 ? -4.290  -24.406 32.927 1.00 22.76  ? 404 PHE   A N   1 
ATOM   774  C CA  . PHE   A 1 112 ? -4.691  -24.673 31.550 1.00 29.62  ? 404 PHE   A CA  1 
ATOM   775  C C   . PHE   A 1 112 ? -5.641  -23.595 31.051 1.00 21.54  ? 404 PHE   A C   1 
ATOM   776  O O   . PHE   A 1 112 ? -5.545  -23.146 29.902 1.00 21.49  ? 404 PHE   A O   1 
ATOM   777  C CB  . PHE   A 1 112 ? -5.344  -26.051 31.451 1.00 19.03  ? 404 PHE   A CB  1 
ATOM   778  C CG  . PHE   A 1 112 ? -4.380  -27.192 31.598 1.00 18.98  ? 404 PHE   A CG  1 
ATOM   779  C CD1 . PHE   A 1 112 ? -3.673  -27.665 30.506 1.00 19.16  ? 404 PHE   A CD1 1 
ATOM   780  C CD2 . PHE   A 1 112 ? -4.183  -27.793 32.830 1.00 20.28  ? 404 PHE   A CD2 1 
ATOM   781  C CE1 . PHE   A 1 112 ? -2.789  -28.718 30.638 1.00 19.64  ? 404 PHE   A CE1 1 
ATOM   782  C CE2 . PHE   A 1 112 ? -3.298  -28.843 32.969 1.00 20.04  ? 404 PHE   A CE2 1 
ATOM   783  C CZ  . PHE   A 1 112 ? -2.600  -29.306 31.871 1.00 20.94  ? 404 PHE   A CZ  1 
ATOM   784  N N   . ALA   A 1 113 ? -6.561  -23.168 31.905 1.00 20.30  ? 405 ALA   A N   1 
ATOM   785  C CA  . ALA   A 1 113 ? -7.469  -22.066 31.639 1.00 26.50  ? 405 ALA   A CA  1 
ATOM   786  C C   . ALA   A 1 113 ? -7.771  -21.392 32.964 1.00 29.20  ? 405 ALA   A C   1 
ATOM   787  O O   . ALA   A 1 113 ? -7.537  -21.981 34.028 1.00 22.84  ? 405 ALA   A O   1 
ATOM   788  C CB  . ALA   A 1 113 ? -8.761  -22.552 30.966 1.00 24.67  ? 405 ALA   A CB  1 
ATOM   789  N N   . PRO   A 1 114 ? -8.259  -20.148 32.947 1.00 23.04  ? 406 PRO   A N   1 
ATOM   790  C CA  . PRO   A 1 114 ? -8.644  -19.509 34.215 1.00 25.93  ? 406 PRO   A CA  1 
ATOM   791  C C   . PRO   A 1 114 ? -9.689  -20.294 34.988 1.00 37.90  ? 406 PRO   A C   1 
ATOM   792  O O   . PRO   A 1 114 ? -9.765  -20.165 36.216 1.00 28.38  ? 406 PRO   A O   1 
ATOM   793  C CB  . PRO   A 1 114 ? -9.174  -18.140 33.767 1.00 27.07  ? 406 PRO   A CB  1 
ATOM   794  C CG  . PRO   A 1 114 ? -8.445  -17.867 32.498 1.00 26.18  ? 406 PRO   A CG  1 
ATOM   795  C CD  . PRO   A 1 114 ? -8.330  -19.204 31.816 1.00 23.98  ? 406 PRO   A CD  1 
ATOM   796  N N   . ASN   A 1 115 ? -10.497 -21.107 34.306 1.00 27.83  ? 407 ASN   A N   1 
ATOM   797  C CA  . ASN   A 1 115 ? -11.464 -21.981 34.954 1.00 29.95  ? 407 ASN   A CA  1 
ATOM   798  C C   . ASN   A 1 115 ? -11.012 -23.437 34.963 1.00 36.29  ? 407 ASN   A C   1 
ATOM   799  O O   . ASN   A 1 115 ? -11.834 -24.334 35.181 1.00 28.72  ? 407 ASN   A O   1 
ATOM   800  C CB  . ASN   A 1 115 ? -12.831 -21.857 34.278 1.00 31.18  ? 407 ASN   A CB  1 
ATOM   801  C CG  . ASN   A 1 115 ? -12.822 -22.351 32.844 1.00 29.16  ? 407 ASN   A CG  1 
ATOM   802  O OD1 . ASN   A 1 115 ? -11.787 -22.349 32.179 1.00 27.76  ? 407 ASN   A OD1 1 
ATOM   803  N ND2 . ASN   A 1 115 ? -13.981 -22.783 32.362 1.00 29.85  ? 407 ASN   A ND2 1 
ATOM   804  N N   . LEU   A 1 116 ? -9.716  -23.691 34.726 1.00 27.84  ? 408 LEU   A N   1 
ATOM   805  C CA  . LEU   A 1 116 ? -9.164  -25.048 34.693 1.00 28.07  ? 408 LEU   A CA  1 
ATOM   806  C C   . LEU   A 1 116 ? -7.763  -25.004 35.306 1.00 21.44  ? 408 LEU   A C   1 
ATOM   807  O O   . LEU   A 1 116 ? -6.748  -25.068 34.609 1.00 25.71  ? 408 LEU   A O   1 
ATOM   808  C CB  . LEU   A 1 116 ? -9.143  -25.609 33.272 1.00 39.42  ? 408 LEU   A CB  1 
ATOM   809  C CG  . LEU   A 1 116 ? -9.128  -27.135 33.158 1.00 29.77  ? 408 LEU   A CG  1 
ATOM   810  C CD1 . LEU   A 1 116 ? -10.206 -27.750 34.037 1.00 38.18  ? 408 LEU   A CD1 1 
ATOM   811  C CD2 . LEU   A 1 116 ? -9.300  -27.568 31.712 1.00 27.25  ? 408 LEU   A CD2 1 
ATOM   812  N N   . LEU   A 1 117 ? -7.713  -24.893 36.630 1.00 31.76  ? 409 LEU   A N   1 
ATOM   813  C CA  . LEU   A 1 117 ? -6.464  -24.930 37.381 1.00 23.49  ? 409 LEU   A CA  1 
ATOM   814  C C   . LEU   A 1 117 ? -6.334  -26.318 37.997 1.00 24.29  ? 409 LEU   A C   1 
ATOM   815  O O   . LEU   A 1 117 ? -7.130  -26.697 38.862 1.00 28.70  ? 409 LEU   A O   1 
ATOM   816  C CB  . LEU   A 1 117 ? -6.435  -23.842 38.452 1.00 32.34  ? 409 LEU   A CB  1 
ATOM   817  C CG  . LEU   A 1 117 ? -5.157  -23.749 39.285 1.00 38.59  ? 409 LEU   A CG  1 
ATOM   818  C CD1 . LEU   A 1 117 ? -4.002  -23.254 38.431 1.00 29.40  ? 409 LEU   A CD1 1 
ATOM   819  C CD2 . LEU   A 1 117 ? -5.369  -22.843 40.488 1.00 30.12  ? 409 LEU   A CD2 1 
ATOM   820  N N   . LEU   A 1 118 ? -5.339  -27.075 37.547 1.00 21.92  ? 410 LEU   A N   1 
ATOM   821  C CA  . LEU   A 1 118 ? -5.162  -28.461 37.951 1.00 35.08  ? 410 LEU   A CA  1 
ATOM   822  C C   . LEU   A 1 118 ? -3.912  -28.607 38.807 1.00 24.48  ? 410 LEU   A C   1 
ATOM   823  O O   . LEU   A 1 118 ? -2.870  -28.015 38.509 1.00 28.02  ? 410 LEU   A O   1 
ATOM   824  C CB  . LEU   A 1 118 ? -5.066  -29.376 36.727 1.00 24.05  ? 410 LEU   A CB  1 
ATOM   825  C CG  . LEU   A 1 118 ? -6.270  -29.378 35.783 1.00 25.56  ? 410 LEU   A CG  1 
ATOM   826  C CD1 . LEU   A 1 118 ? -6.137  -30.484 34.745 1.00 33.76  ? 410 LEU   A CD1 1 
ATOM   827  C CD2 . LEU   A 1 118 ? -7.568  -29.524 36.562 1.00 28.52  ? 410 LEU   A CD2 1 
ATOM   828  N N   . ASP   A 1 119 ? -4.021  -29.396 39.871 1.00 33.31  ? 411 ASP   A N   1 
ATOM   829  C CA  . ASP   A 1 119 ? -2.881  -29.711 40.714 1.00 43.71  ? 411 ASP   A CA  1 
ATOM   830  C C   . ASP   A 1 119 ? -2.271  -31.045 40.286 1.00 44.17  ? 411 ASP   A C   1 
ATOM   831  O O   . ASP   A 1 119 ? -2.744  -31.710 39.361 1.00 32.81  ? 411 ASP   A O   1 
ATOM   832  C CB  . ASP   A 1 119 ? -3.282  -29.701 42.195 1.00 42.39  ? 411 ASP   A CB  1 
ATOM   833  C CG  . ASP   A 1 119 ? -4.372  -30.710 42.532 1.00 53.57  ? 411 ASP   A CG  1 
ATOM   834  O OD1 . ASP   A 1 119 ? -4.320  -31.863 42.053 1.00 56.28  ? 411 ASP   A OD1 1 
ATOM   835  O OD2 . ASP   A 1 119 ? -5.292  -30.343 43.294 1.00 70.30  ? 411 ASP   A OD2 1 
ATOM   836  N N   . ARG   A 1 120 ? -1.203  -31.437 40.983 1.00 39.33  ? 412 ARG   A N   1 
ATOM   837  C CA  . ARG   A 1 120 ? -0.462  -32.636 40.605 1.00 35.09  ? 412 ARG   A CA  1 
ATOM   838  C C   . ARG   A 1 120 ? -1.320  -33.888 40.732 1.00 50.11  ? 412 ARG   A C   1 
ATOM   839  O O   . ARG   A 1 120 ? -1.235  -34.796 39.895 1.00 41.34  ? 412 ARG   A O   1 
ATOM   840  C CB  . ARG   A 1 120 ? 0.790   -32.761 41.470 1.00 37.03  ? 412 ARG   A CB  1 
ATOM   841  C CG  . ARG   A 1 120 ? 1.771   -33.810 40.996 1.00 41.60  ? 412 ARG   A CG  1 
ATOM   842  C CD  . ARG   A 1 120 ? 3.142   -33.577 41.605 1.00 39.28  ? 412 ARG   A CD  1 
ATOM   843  N NE  . ARG   A 1 120 ? 4.072   -34.651 41.278 1.00 43.27  ? 412 ARG   A NE  1 
ATOM   844  C CZ  . ARG   A 1 120 ? 4.025   -35.870 41.795 1.00 44.93  ? 412 ARG   A CZ  1 
ATOM   845  N NH1 . ARG   A 1 120 ? 3.111   -36.207 42.690 1.00 61.85  ? 412 ARG   A NH1 1 
ATOM   846  N NH2 . ARG   A 1 120 ? 4.921   -36.774 41.409 1.00 50.64  ? 412 ARG   A NH2 1 
ATOM   847  N N   . ASN   A 1 121 ? -2.156  -33.955 41.771 1.00 36.12  ? 413 ASN   A N   1 
ATOM   848  C CA  . ASN   A 1 121 ? -2.917  -35.172 42.034 1.00 42.02  ? 413 ASN   A CA  1 
ATOM   849  C C   . ASN   A 1 121 ? -3.942  -35.450 40.943 1.00 40.64  ? 413 ASN   A C   1 
ATOM   850  O O   . ASN   A 1 121 ? -4.231  -36.616 40.651 1.00 43.14  ? 413 ASN   A O   1 
ATOM   851  C CB  . ASN   A 1 121 ? -3.606  -35.076 43.394 1.00 42.53  ? 413 ASN   A CB  1 
ATOM   852  C CG  . ASN   A 1 121 ? -2.656  -35.329 44.546 1.00 52.34  ? 413 ASN   A CG  1 
ATOM   853  O OD1 . ASN   A 1 121 ? -1.731  -36.133 44.437 1.00 53.23  ? 413 ASN   A OD1 1 
ATOM   854  N ND2 . ASN   A 1 121 ? -2.882  -34.645 45.659 1.00 69.01  ? 413 ASN   A ND2 1 
ATOM   855  N N   . GLN   A 1 122 ? -4.503  -34.404 40.333 1.00 48.27  ? 414 GLN   A N   1 
ATOM   856  C CA  . GLN   A 1 122 ? -5.456  -34.606 39.250 1.00 46.62  ? 414 GLN   A CA  1 
ATOM   857  C C   . GLN   A 1 122 ? -4.793  -35.148 37.991 1.00 53.17  ? 414 GLN   A C   1 
ATOM   858  O O   . GLN   A 1 122 ? -5.486  -35.702 37.131 1.00 60.23  ? 414 GLN   A O   1 
ATOM   859  C CB  . GLN   A 1 122 ? -6.189  -33.298 38.947 1.00 45.84  ? 414 GLN   A CB  1 
ATOM   860  C CG  . GLN   A 1 122 ? -7.022  -32.788 40.112 1.00 49.74  ? 414 GLN   A CG  1 
ATOM   861  C CD  . GLN   A 1 122 ? -7.524  -31.375 39.904 1.00 47.14  ? 414 GLN   A CD  1 
ATOM   862  O OE1 . GLN   A 1 122 ? -6.770  -30.410 40.030 1.00 45.25  ? 414 GLN   A OE1 1 
ATOM   863  N NE2 . GLN   A 1 122 ? -8.806  -31.244 39.584 1.00 49.82  ? 414 GLN   A NE2 1 
ATOM   864  N N   . GLY   A 1 123 ? -3.471  -35.006 37.865 1.00 45.86  ? 415 GLY   A N   1 
ATOM   865  C CA  . GLY   A 1 123 ? -2.763  -35.622 36.758 1.00 45.36  ? 415 GLY   A CA  1 
ATOM   866  C C   . GLY   A 1 123 ? -2.499  -37.101 36.935 1.00 55.67  ? 415 GLY   A C   1 
ATOM   867  O O   . GLY   A 1 123 ? -2.304  -37.807 35.940 1.00 55.20  ? 415 GLY   A O   1 
ATOM   868  N N   . LYS   A 1 124 ? -2.494  -37.587 38.179 1.00 60.10  ? 416 LYS   A N   1 
ATOM   869  C CA  . LYS   A 1 124 ? -2.272  -39.006 38.431 1.00 46.56  ? 416 LYS   A CA  1 
ATOM   870  C C   . LYS   A 1 124 ? -3.403  -39.878 37.903 1.00 56.36  ? 416 LYS   A C   1 
ATOM   871  O O   . LYS   A 1 124 ? -3.203  -41.085 37.728 1.00 56.89  ? 416 LYS   A O   1 
ATOM   872  C CB  . LYS   A 1 124 ? -2.095  -39.256 39.929 1.00 51.67  ? 416 LYS   A CB  1 
ATOM   873  C CG  . LYS   A 1 124 ? -0.718  -38.917 40.471 1.00 66.80  ? 416 LYS   A CG  1 
ATOM   874  C CD  . LYS   A 1 124 ? -0.553  -39.433 41.893 1.00 69.67  ? 416 LYS   A CD  1 
ATOM   875  C CE  . LYS   A 1 124 ? -0.145  -38.320 42.841 1.00 61.30  ? 416 LYS   A CE  1 
ATOM   876  N NZ  . LYS   A 1 124 ? 0.734   -38.811 43.939 1.00 60.56  ? 416 LYS   A NZ  1 
ATOM   877  N N   . SER   A 1 125 ? -4.582  -39.302 37.655 1.00 57.57  ? 417 SER   A N   1 
ATOM   878  C CA  . SER   A 1 125 ? -5.708  -40.097 37.172 1.00 53.62  ? 417 SER   A CA  1 
ATOM   879  C C   . SER   A 1 125 ? -5.428  -40.700 35.802 1.00 60.23  ? 417 SER   A C   1 
ATOM   880  O O   . SER   A 1 125 ? -5.892  -41.807 35.505 1.00 58.68  ? 417 SER   A O   1 
ATOM   881  C CB  . SER   A 1 125 ? -6.973  -39.240 37.131 1.00 62.70  ? 417 SER   A CB  1 
ATOM   882  O OG  . SER   A 1 125 ? -6.690  -37.937 36.652 1.00 60.33  ? 417 SER   A OG  1 
ATOM   883  N N   . VAL   A 1 126 ? -4.679  -39.995 34.957 1.00 67.88  ? 418 VAL   A N   1 
ATOM   884  C CA  . VAL   A 1 126 ? -4.268  -40.501 33.652 1.00 68.09  ? 418 VAL   A CA  1 
ATOM   885  C C   . VAL   A 1 126 ? -2.848  -41.034 33.770 1.00 57.37  ? 418 VAL   A C   1 
ATOM   886  O O   . VAL   A 1 126 ? -1.946  -40.325 34.233 1.00 60.66  ? 418 VAL   A O   1 
ATOM   887  C CB  . VAL   A 1 126 ? -4.360  -39.409 32.572 1.00 60.28  ? 418 VAL   A CB  1 
ATOM   888  C CG1 . VAL   A 1 126 ? -3.810  -39.926 31.251 1.00 59.34  ? 418 VAL   A CG1 1 
ATOM   889  C CG2 . VAL   A 1 126 ? -5.799  -38.950 32.408 1.00 55.42  ? 418 VAL   A CG2 1 
ATOM   890  N N   . GLU   A 1 127 ? -2.648  -42.282 33.355 1.00 53.47  ? 419 GLU   A N   1 
ATOM   891  C CA  . GLU   A 1 127 ? -1.346  -42.917 33.501 1.00 58.06  ? 419 GLU   A CA  1 
ATOM   892  C C   . GLU   A 1 127 ? -0.355  -42.313 32.512 1.00 68.14  ? 419 GLU   A C   1 
ATOM   893  O O   . GLU   A 1 127 ? -0.652  -42.175 31.321 1.00 54.13  ? 419 GLU   A O   1 
ATOM   894  C CB  . GLU   A 1 127 ? -1.473  -44.427 33.298 1.00 63.08  ? 419 GLU   A CB  1 
ATOM   895  C CG  . GLU   A 1 127 ? -0.236  -45.224 33.683 1.00 73.98  ? 419 GLU   A CG  1 
ATOM   896  C CD  . GLU   A 1 127 ? 0.778   -45.312 32.561 1.00 83.09  ? 419 GLU   A CD  1 
ATOM   897  O OE1 . GLU   A 1 127 ? 1.992   -45.320 32.853 1.00 89.26  ? 419 GLU   A OE1 1 
ATOM   898  O OE2 . GLU   A 1 127 ? 0.361   -45.376 31.387 1.00 90.24  ? 419 GLU   A OE2 1 
ATOM   899  N N   . GLY   A 1 128 ? 0.826   -41.949 33.011 1.00 69.75  ? 420 GLY   A N   1 
ATOM   900  C CA  . GLY   A 1 128 ? 1.824   -41.266 32.217 1.00 48.40  ? 420 GLY   A CA  1 
ATOM   901  C C   . GLY   A 1 128 ? 1.714   -39.756 32.220 1.00 50.08  ? 420 GLY   A C   1 
ATOM   902  O O   . GLY   A 1 128 ? 2.603   -39.084 31.681 1.00 46.90  ? 420 GLY   A O   1 
ATOM   903  N N   . MET   A 1 129 ? 0.659   -39.203 32.818 1.00 47.10  ? 421 MET   A N   1 
ATOM   904  C CA  . MET   A 1 129 ? 0.433   -37.763 32.787 1.00 34.19  ? 421 MET   A CA  1 
ATOM   905  C C   . MET   A 1 129 ? 1.304   -37.018 33.791 1.00 31.74  ? 421 MET   A C   1 
ATOM   906  O O   . MET   A 1 129 ? 1.817   -35.936 33.484 1.00 36.08  ? 421 MET   A O   1 
ATOM   907  C CB  . MET   A 1 129 ? -1.043  -37.470 33.051 1.00 30.86  ? 421 MET   A CB  1 
ATOM   908  C CG  . MET   A 1 129 ? -1.450  -36.035 32.801 1.00 37.90  ? 421 MET   A CG  1 
ATOM   909  S SD  . MET   A 1 129 ? -3.235  -35.814 32.780 1.00 44.22  ? 421 MET   A SD  1 
ATOM   910  C CE  . MET   A 1 129 ? -3.382  -34.355 31.754 1.00 50.61  ? 421 MET   A CE  1 
ATOM   911  N N   . VAL   A 1 130 ? 1.486   -37.578 34.989 1.00 40.57  ? 422 VAL   A N   1 
ATOM   912  C CA  . VAL   A 1 130 ? 2.166   -36.839 36.050 1.00 36.03  ? 422 VAL   A CA  1 
ATOM   913  C C   . VAL   A 1 130 ? 3.630   -36.596 35.702 1.00 29.02  ? 422 VAL   A C   1 
ATOM   914  O O   . VAL   A 1 130 ? 4.228   -35.617 36.165 1.00 31.62  ? 422 VAL   A O   1 
ATOM   915  C CB  . VAL   A 1 130 ? 2.014   -37.571 37.398 1.00 36.30  ? 422 VAL   A CB  1 
ATOM   916  C CG1 . VAL   A 1 130 ? 2.886   -38.819 37.443 1.00 36.59  ? 422 VAL   A CG1 1 
ATOM   917  C CG2 . VAL   A 1 130 ? 2.340   -36.634 38.555 1.00 42.29  ? 422 VAL   A CG2 1 
ATOM   918  N N   . GLU   A 1 131 ? 4.230   -37.460 34.881 1.00 31.87  ? 423 GLU   A N   1 
ATOM   919  C CA  . GLU   A 1 131 ? 5.615   -37.245 34.472 1.00 31.09  ? 423 GLU   A CA  1 
ATOM   920  C C   . GLU   A 1 131 ? 5.740   -35.984 33.627 1.00 31.63  ? 423 GLU   A C   1 
ATOM   921  O O   . GLU   A 1 131 ? 6.626   -35.154 33.857 1.00 31.57  ? 423 GLU   A O   1 
ATOM   922  C CB  . GLU   A 1 131 ? 6.133   -38.466 33.712 1.00 30.77  ? 423 GLU   A CB  1 
ATOM   923  C CG  . GLU   A 1 131 ? 6.423   -39.669 34.596 1.00 43.33  ? 423 GLU   A CG  1 
ATOM   924  C CD  . GLU   A 1 131 ? 5.178   -40.476 34.907 1.00 54.03  ? 423 GLU   A CD  1 
ATOM   925  O OE1 . GLU   A 1 131 ? 5.132   -41.116 35.978 1.00 65.50  ? 423 GLU   A OE1 1 
ATOM   926  O OE2 . GLU   A 1 131 ? 4.241   -40.464 34.083 1.00 51.62  ? 423 GLU   A OE2 1 
ATOM   927  N N   . ILE   A 1 132 ? 4.852   -35.822 32.645 1.00 26.09  ? 424 ILE   A N   1 
ATOM   928  C CA  . ILE   A 1 132 ? 4.822   -34.585 31.872 1.00 25.93  ? 424 ILE   A CA  1 
ATOM   929  C C   . ILE   A 1 132 ? 4.364   -33.429 32.750 1.00 25.59  ? 424 ILE   A C   1 
ATOM   930  O O   . ILE   A 1 132 ? 4.849   -32.299 32.620 1.00 26.98  ? 424 ILE   A O   1 
ATOM   931  C CB  . ILE   A 1 132 ? 3.914   -34.747 30.640 1.00 27.66  ? 424 ILE   A CB  1 
ATOM   932  C CG1 . ILE   A 1 132 ? 4.062   -36.142 30.032 1.00 40.82  ? 424 ILE   A CG1 1 
ATOM   933  C CG2 . ILE   A 1 132 ? 4.204   -33.661 29.612 1.00 27.20  ? 424 ILE   A CG2 1 
ATOM   934  C CD1 . ILE   A 1 132 ? 5.289   -36.312 29.196 1.00 49.17  ? 424 ILE   A CD1 1 
ATOM   935  N N   . PHE   A 1 133 ? 3.415   -33.697 33.650 1.00 25.66  ? 425 PHE   A N   1 
ATOM   936  C CA  . PHE   A 1 133 ? 2.924   -32.676 34.570 1.00 26.59  ? 425 PHE   A CA  1 
ATOM   937  C C   . PHE   A 1 133 ? 4.061   -32.092 35.399 1.00 23.60  ? 425 PHE   A C   1 
ATOM   938  O O   . PHE   A 1 133 ? 4.165   -30.871 35.561 1.00 20.40  ? 425 PHE   A O   1 
ATOM   939  C CB  . PHE   A 1 133 ? 1.852   -33.284 35.477 1.00 29.56  ? 425 PHE   A CB  1 
ATOM   940  C CG  . PHE   A 1 133 ? 0.838   -32.297 35.983 1.00 32.53  ? 425 PHE   A CG  1 
ATOM   941  C CD1 . PHE   A 1 133 ? 1.153   -31.425 37.011 1.00 26.25  ? 425 PHE   A CD1 1 
ATOM   942  C CD2 . PHE   A 1 133 ? -0.441  -32.265 35.451 1.00 26.83  ? 425 PHE   A CD2 1 
ATOM   943  C CE1 . PHE   A 1 133 ? 0.217   -30.525 37.487 1.00 29.71  ? 425 PHE   A CE1 1 
ATOM   944  C CE2 . PHE   A 1 133 ? -1.381  -31.368 35.924 1.00 35.76  ? 425 PHE   A CE2 1 
ATOM   945  C CZ  . PHE   A 1 133 ? -1.051  -30.496 36.943 1.00 33.20  ? 425 PHE   A CZ  1 
ATOM   946  N N   . ASP   A 1 134 ? 4.932   -32.956 35.925 1.00 27.15  ? 426 ASP   A N   1 
ATOM   947  C CA  . ASP   A 1 134 ? 6.019   -32.488 36.778 1.00 31.76  ? 426 ASP   A CA  1 
ATOM   948  C C   . ASP   A 1 134 ? 7.048   -31.693 35.986 1.00 23.79  ? 426 ASP   A C   1 
ATOM   949  O O   . ASP   A 1 134 ? 7.625   -30.729 36.504 1.00 20.99  ? 426 ASP   A O   1 
ATOM   950  C CB  . ASP   A 1 134 ? 6.680   -33.672 37.483 1.00 28.63  ? 426 ASP   A CB  1 
ATOM   951  C CG  . ASP   A 1 134 ? 5.788   -34.286 38.541 1.00 28.52  ? 426 ASP   A CG  1 
ATOM   952  O OD1 . ASP   A 1 134 ? 4.803   -33.629 38.935 1.00 33.35  ? 426 ASP   A OD1 1 
ATOM   953  O OD2 . ASP   A 1 134 ? 6.069   -35.421 38.977 1.00 33.19  ? 426 ASP   A OD2 1 
ATOM   954  N N   . MET   A 1 135 ? 7.299   -32.079 34.734 1.00 24.93  ? 427 MET   A N   1 
ATOM   955  C CA  . MET   A 1 135 ? 8.232   -31.315 33.912 1.00 27.69  ? 427 MET   A CA  1 
ATOM   956  C C   . MET   A 1 135 ? 7.690   -29.923 33.615 1.00 20.89  ? 427 MET   A C   1 
ATOM   957  O O   . MET   A 1 135 ? 8.446   -28.944 33.610 1.00 25.16  ? 427 MET   A O   1 
ATOM   958  C CB  . MET   A 1 135 ? 8.534   -32.061 32.613 1.00 26.93  ? 427 MET   A CB  1 
ATOM   959  C CG  . MET   A 1 135 ? 9.358   -33.325 32.792 1.00 31.98  ? 427 MET   A CG  1 
ATOM   960  S SD  . MET   A 1 135 ? 9.769   -34.113 31.221 1.00 39.89  ? 427 MET   A SD  1 
ATOM   961  C CE  . MET   A 1 135 ? 8.145   -34.427 30.547 1.00 28.42  ? 427 MET   A CE  1 
ATOM   962  N N   . LEU   A 1 136 ? 6.385   -29.815 33.358 1.00 18.90  ? 428 LEU   A N   1 
ATOM   963  C CA  . LEU   A 1 136 ? 5.783   -28.504 33.145 1.00 21.12  ? 428 LEU   A CA  1 
ATOM   964  C C   . LEU   A 1 136 ? 5.818   -27.674 34.422 1.00 23.46  ? 428 LEU   A C   1 
ATOM   965  O O   . LEU   A 1 136 ? 6.022   -26.456 34.373 1.00 20.76  ? 428 LEU   A O   1 
ATOM   966  C CB  . LEU   A 1 136 ? 4.348   -28.658 32.642 1.00 17.89  ? 428 LEU   A CB  1 
ATOM   967  C CG  . LEU   A 1 136 ? 4.177   -29.223 31.229 1.00 22.72  ? 428 LEU   A CG  1 
ATOM   968  C CD1 . LEU   A 1 136 ? 2.835   -29.927 31.091 1.00 19.14  ? 428 LEU   A CD1 1 
ATOM   969  C CD2 . LEU   A 1 136 ? 4.318   -28.125 30.183 1.00 17.62  ? 428 LEU   A CD2 1 
ATOM   970  N N   . LEU   A 1 137 ? 5.623   -28.320 35.575 1.00 24.49  ? 429 LEU   A N   1 
ATOM   971  C CA  . LEU   A 1 137 ? 5.699   -27.611 36.849 1.00 25.05  ? 429 LEU   A CA  1 
ATOM   972  C C   . LEU   A 1 137 ? 7.104   -27.082 37.102 1.00 24.53  ? 429 LEU   A C   1 
ATOM   973  O O   . LEU   A 1 137 ? 7.274   -25.953 37.577 1.00 28.84  ? 429 LEU   A O   1 
ATOM   974  C CB  . LEU   A 1 137 ? 5.265   -28.534 37.989 1.00 25.24  ? 429 LEU   A CB  1 
ATOM   975  C CG  . LEU   A 1 137 ? 3.774   -28.847 38.108 1.00 23.65  ? 429 LEU   A CG  1 
ATOM   976  C CD1 . LEU   A 1 137 ? 3.510   -29.743 39.311 1.00 21.35  ? 429 LEU   A CD1 1 
ATOM   977  C CD2 . LEU   A 1 137 ? 2.964   -27.566 38.201 1.00 27.82  ? 429 LEU   A CD2 1 
ATOM   978  N N   . ALA   A 1 138 ? 8.125   -27.887 36.794 1.00 23.56  ? 430 ALA   A N   1 
ATOM   979  C CA  . ALA   A 1 138 ? 9.501   -27.457 37.024 1.00 19.76  ? 430 ALA   A CA  1 
ATOM   980  C C   . ALA   A 1 138 ? 9.878   -26.296 36.113 1.00 20.49  ? 430 ALA   A C   1 
ATOM   981  O O   . ALA   A 1 138 ? 10.611  -25.390 36.525 1.00 32.37  ? 430 ALA   A O   1 
ATOM   982  C CB  . ALA   A 1 138 ? 10.459  -28.631 36.822 1.00 24.07  ? 430 ALA   A CB  1 
ATOM   983  N N   . THR   A 1 139 ? 9.389   -26.306 34.871 1.00 28.07  ? 431 THR   A N   1 
ATOM   984  C CA  . THR   A 1 139 ? 9.644   -25.187 33.971 1.00 23.69  ? 431 THR   A CA  1 
ATOM   985  C C   . THR   A 1 139 ? 8.965   -23.920 34.472 1.00 25.38  ? 431 THR   A C   1 
ATOM   986  O O   . THR   A 1 139 ? 9.535   -22.826 34.387 1.00 26.43  ? 431 THR   A O   1 
ATOM   987  C CB  . THR   A 1 139 ? 9.167   -25.525 32.560 1.00 24.93  ? 431 THR   A CB  1 
ATOM   988  O OG1 . THR   A 1 139 ? 9.593   -26.847 32.217 1.00 26.05  ? 431 THR   A OG1 1 
ATOM   989  C CG2 . THR   A 1 139 ? 9.741   -24.539 31.555 1.00 25.78  ? 431 THR   A CG2 1 
ATOM   990  N N   . SER   A 1 140 ? 7.745   -24.050 34.999 1.00 21.58  ? 432 SER   A N   1 
ATOM   991  C CA  . SER   A 1 140 ? 7.055   -22.899 35.572 1.00 25.55  ? 432 SER   A CA  1 
ATOM   992  C C   . SER   A 1 140 ? 7.807   -22.353 36.779 1.00 24.04  ? 432 SER   A C   1 
ATOM   993  O O   . SER   A 1 140 ? 7.861   -21.136 36.989 1.00 31.21  ? 432 SER   A O   1 
ATOM   994  C CB  . SER   A 1 140 ? 5.627   -23.285 35.953 1.00 27.47  ? 432 SER   A CB  1 
ATOM   995  O OG  . SER   A 1 140 ? 4.841   -22.136 36.207 1.00 38.46  ? 432 SER   A OG  1 
ATOM   996  N N   . SER   A 1 141 ? 8.397   -23.241 37.583 1.00 22.95  ? 433 SER   A N   1 
ATOM   997  C CA  . SER   A 1 141 ? 9.219   -22.795 38.703 1.00 26.83  ? 433 SER   A CA  1 
ATOM   998  C C   . SER   A 1 141 ? 10.493  -22.119 38.212 1.00 26.46  ? 433 SER   A C   1 
ATOM   999  O O   . SER   A 1 141 ? 10.967  -21.156 38.826 1.00 27.04  ? 433 SER   A O   1 
ATOM   1000 C CB  . SER   A 1 141 ? 9.557   -23.977 39.611 1.00 25.54  ? 433 SER   A CB  1 
ATOM   1001 O OG  . SER   A 1 141 ? 8.385   -24.539 40.175 1.00 48.13  ? 433 SER   A OG  1 
ATOM   1002 N N   . ARG   A 1 142 ? 11.061  -22.614 37.110 1.00 27.30  ? 434 ARG   A N   1 
ATOM   1003 C CA  . ARG   A 1 142 ? 12.256  -22.000 36.541 1.00 22.61  ? 434 ARG   A CA  1 
ATOM   1004 C C   . ARG   A 1 142 ? 11.962  -20.590 36.045 1.00 23.95  ? 434 ARG   A C   1 
ATOM   1005 O O   . ARG   A 1 142 ? 12.734  -19.657 36.296 1.00 26.37  ? 434 ARG   A O   1 
ATOM   1006 C CB  . ARG   A 1 142 ? 12.797  -22.875 35.409 1.00 31.10  ? 434 ARG   A CB  1 
ATOM   1007 C CG  . ARG   A 1 142 ? 14.000  -22.306 34.677 1.00 31.21  ? 434 ARG   A CG  1 
ATOM   1008 C CD  . ARG   A 1 142 ? 15.193  -22.100 35.594 1.00 41.78  ? 434 ARG   A CD  1 
ATOM   1009 N NE  . ARG   A 1 142 ? 16.354  -21.610 34.859 1.00 47.56  ? 434 ARG   A NE  1 
ATOM   1010 C CZ  . ARG   A 1 142 ? 17.460  -21.144 35.423 1.00 55.99  ? 434 ARG   A CZ  1 
ATOM   1011 N NH1 . ARG   A 1 142 ? 17.594  -21.086 36.738 1.00 53.39  ? 434 ARG   A NH1 1 
ATOM   1012 N NH2 . ARG   A 1 142 ? 18.457  -20.725 34.649 1.00 52.22  ? 434 ARG   A NH2 1 
ATOM   1013 N N   . PHE   A 1 143 ? 10.844  -20.416 35.334 1.00 26.46  ? 435 PHE   A N   1 
ATOM   1014 C CA  . PHE   A 1 143 ? 10.434  -19.079 34.911 1.00 23.48  ? 435 PHE   A CA  1 
ATOM   1015 C C   . PHE   A 1 143 ? 10.184  -18.178 36.112 1.00 27.00  ? 435 PHE   A C   1 
ATOM   1016 O O   . PHE   A 1 143 ? 10.554  -16.998 36.103 1.00 28.92  ? 435 PHE   A O   1 
ATOM   1017 C CB  . PHE   A 1 143 ? 9.177   -19.162 34.045 1.00 25.23  ? 435 PHE   A CB  1 
ATOM   1018 C CG  . PHE   A 1 143 ? 9.438   -19.556 32.620 1.00 35.60  ? 435 PHE   A CG  1 
ATOM   1019 C CD1 . PHE   A 1 143 ? 10.732  -19.681 32.142 1.00 39.69  ? 435 PHE   A CD1 1 
ATOM   1020 C CD2 . PHE   A 1 143 ? 8.384   -19.796 31.756 1.00 38.44  ? 435 PHE   A CD2 1 
ATOM   1021 C CE1 . PHE   A 1 143 ? 10.968  -20.042 30.828 1.00 38.38  ? 435 PHE   A CE1 1 
ATOM   1022 C CE2 . PHE   A 1 143 ? 8.612   -20.158 30.442 1.00 29.06  ? 435 PHE   A CE2 1 
ATOM   1023 C CZ  . PHE   A 1 143 ? 9.905   -20.281 29.977 1.00 29.17  ? 435 PHE   A CZ  1 
ATOM   1024 N N   . ARG   A 1 144 ? 9.554   -18.721 37.155 1.00 26.81  ? 436 ARG   A N   1 
ATOM   1025 C CA  . ARG   A 1 144 ? 9.254   -17.935 38.346 1.00 27.46  ? 436 ARG   A CA  1 
ATOM   1026 C C   . ARG   A 1 144 ? 10.531  -17.507 39.057 1.00 23.77  ? 436 ARG   A C   1 
ATOM   1027 O O   . ARG   A 1 144 ? 10.678  -16.345 39.451 1.00 28.80  ? 436 ARG   A O   1 
ATOM   1028 C CB  . ARG   A 1 144 ? 8.356   -18.745 39.280 1.00 27.72  ? 436 ARG   A CB  1 
ATOM   1029 C CG  . ARG   A 1 144 ? 7.787   -17.972 40.453 1.00 30.74  ? 436 ARG   A CG  1 
ATOM   1030 C CD  . ARG   A 1 144 ? 7.070   -18.922 41.394 1.00 30.19  ? 436 ARG   A CD  1 
ATOM   1031 N NE  . ARG   A 1 144 ? 6.243   -19.868 40.655 1.00 45.70  ? 436 ARG   A NE  1 
ATOM   1032 C CZ  . ARG   A 1 144 ? 6.303   -21.186 40.790 1.00 35.92  ? 436 ARG   A CZ  1 
ATOM   1033 N NH1 . ARG   A 1 144 ? 7.140   -21.756 41.642 1.00 36.85  ? 436 ARG   A NH1 1 
ATOM   1034 N NH2 . ARG   A 1 144 ? 5.508   -21.951 40.049 1.00 41.53  ? 436 ARG   A NH2 1 
ATOM   1035 N N   . MET   A 1 145 ? 11.473  -18.440 39.225 1.00 24.73  ? 437 MET   A N   1 
ATOM   1036 C CA  . MET   A 1 145 ? 12.741  -18.107 39.865 1.00 28.28  ? 437 MET   A CA  1 
ATOM   1037 C C   . MET   A 1 145 ? 13.536  -17.099 39.046 1.00 26.85  ? 437 MET   A C   1 
ATOM   1038 O O   . MET   A 1 145 ? 14.310  -16.315 39.607 1.00 37.33  ? 437 MET   A O   1 
ATOM   1039 C CB  . MET   A 1 145 ? 13.566  -19.375 40.089 1.00 29.63  ? 437 MET   A CB  1 
ATOM   1040 N N   . MET   A 1 146 ? 13.363  -17.104 37.725 1.00 34.18  ? 438 MET   A N   1 
ATOM   1041 C CA  . MET   A 1 146 ? 14.053  -16.161 36.857 1.00 33.77  ? 438 MET   A CA  1 
ATOM   1042 C C   . MET   A 1 146 ? 13.332  -14.829 36.724 1.00 28.83  ? 438 MET   A C   1 
ATOM   1043 O O   . MET   A 1 146 ? 13.911  -13.891 36.164 1.00 29.08  ? 438 MET   A O   1 
ATOM   1044 C CB  . MET   A 1 146 ? 14.240  -16.766 35.466 1.00 31.23  ? 438 MET   A CB  1 
ATOM   1045 C CG  . MET   A 1 146 ? 15.355  -17.778 35.373 1.00 43.24  ? 438 MET   A CG  1 
ATOM   1046 S SD  . MET   A 1 146 ? 15.540  -18.334 33.676 1.00 48.04  ? 438 MET   A SD  1 
ATOM   1047 C CE  . MET   A 1 146 ? 16.727  -17.133 33.083 1.00 42.54  ? 438 MET   A CE  1 
ATOM   1048 N N   . ASN   A 1 147 ? 12.100  -14.723 37.221 1.00 30.02  ? 439 ASN   A N   1 
ATOM   1049 C CA  . ASN   A 1 147 ? 11.263  -13.542 37.018 1.00 38.71  ? 439 ASN   A CA  1 
ATOM   1050 C C   . ASN   A 1 147 ? 11.139  -13.225 35.528 1.00 25.10  ? 439 ASN   A C   1 
ATOM   1051 O O   . ASN   A 1 147 ? 11.446  -12.122 35.068 1.00 27.53  ? 439 ASN   A O   1 
ATOM   1052 C CB  . ASN   A 1 147 ? 11.802  -12.339 37.800 1.00 28.89  ? 439 ASN   A CB  1 
ATOM   1053 C CG  . ASN   A 1 147 ? 10.803  -11.199 37.879 1.00 39.53  ? 439 ASN   A CG  1 
ATOM   1054 O OD1 . ASN   A 1 147 ? 9.599   -11.420 38.012 1.00 38.58  ? 439 ASN   A OD1 1 
ATOM   1055 N ND2 . ASN   A 1 147 ? 11.300  -9.970  37.796 1.00 57.64  ? 439 ASN   A ND2 1 
ATOM   1056 N N   . LEU   A 1 148 ? 10.697  -14.226 34.767 1.00 26.28  ? 440 LEU   A N   1 
ATOM   1057 C CA  . LEU   A 1 148 ? 10.528  -14.064 33.329 1.00 26.65  ? 440 LEU   A CA  1 
ATOM   1058 C C   . LEU   A 1 148 ? 9.518   -12.965 33.031 1.00 21.78  ? 440 LEU   A C   1 
ATOM   1059 O O   . LEU   A 1 148 ? 8.434   -12.921 33.620 1.00 28.91  ? 440 LEU   A O   1 
ATOM   1060 C CB  . LEU   A 1 148 ? 10.074  -15.379 32.692 1.00 20.64  ? 440 LEU   A CB  1 
ATOM   1061 C CG  . LEU   A 1 148 ? 9.922   -15.350 31.168 1.00 23.65  ? 440 LEU   A CG  1 
ATOM   1062 C CD1 . LEU   A 1 148 ? 11.275  -15.201 30.492 1.00 19.55  ? 440 LEU   A CD1 1 
ATOM   1063 C CD2 . LEU   A 1 148 ? 9.198   -16.585 30.657 1.00 26.41  ? 440 LEU   A CD2 1 
ATOM   1064 N N   . GLN   A 1 149 ? 9.880   -12.076 32.113 1.00 22.25  ? 441 GLN   A N   1 
ATOM   1065 C CA  . GLN   A 1 149 ? 9.034   -10.957 31.731 1.00 28.76  ? 441 GLN   A CA  1 
ATOM   1066 C C   . GLN   A 1 149 ? 8.223   -11.309 30.491 1.00 24.43  ? 441 GLN   A C   1 
ATOM   1067 O O   . GLN   A 1 149 ? 8.641   -12.120 29.661 1.00 25.00  ? 441 GLN   A O   1 
ATOM   1068 C CB  . GLN   A 1 149 ? 9.876   -9.707  31.472 1.00 28.27  ? 441 GLN   A CB  1 
ATOM   1069 C CG  . GLN   A 1 149 ? 10.641  -9.227  32.692 1.00 26.94  ? 441 GLN   A CG  1 
ATOM   1070 C CD  . GLN   A 1 149 ? 9.724   -8.764  33.805 1.00 28.41  ? 441 GLN   A CD  1 
ATOM   1071 O OE1 . GLN   A 1 149 ? 8.946   -7.826  33.633 1.00 46.96  ? 441 GLN   A OE1 1 
ATOM   1072 N NE2 . GLN   A 1 149 ? 9.803   -9.428  34.952 1.00 28.45  ? 441 GLN   A NE2 1 
ATOM   1073 N N   . GLY   A 1 150 ? 7.047   -10.687 30.376 1.00 27.20  ? 442 GLY   A N   1 
ATOM   1074 C CA  . GLY   A 1 150 ? 6.192   -10.947 29.229 1.00 25.44  ? 442 GLY   A CA  1 
ATOM   1075 C C   . GLY   A 1 150 ? 6.856   -10.598 27.912 1.00 24.17  ? 442 GLY   A C   1 
ATOM   1076 O O   . GLY   A 1 150 ? 6.661   -11.285 26.906 1.00 29.08  ? 442 GLY   A O   1 
ATOM   1077 N N   . GLU   A 1 151 ? 7.652   -9.526  27.900 1.00 27.67  ? 443 GLU   A N   1 
ATOM   1078 C CA  . GLU   A 1 151 ? 8.390   -9.164  26.695 1.00 23.82  ? 443 GLU   A CA  1 
ATOM   1079 C C   . GLU   A 1 151 ? 9.401   -10.239 26.322 1.00 25.23  ? 443 GLU   A C   1 
ATOM   1080 O O   . GLU   A 1 151 ? 9.650   -10.473 25.134 1.00 24.68  ? 443 GLU   A O   1 
ATOM   1081 C CB  . GLU   A 1 151 ? 9.092   -7.821  26.893 1.00 30.25  ? 443 GLU   A CB  1 
ATOM   1082 C CG  . GLU   A 1 151 ? 8.144   -6.643  27.008 1.00 32.17  ? 443 GLU   A CG  1 
ATOM   1083 C CD  . GLU   A 1 151 ? 7.789   -6.320  28.446 1.00 38.61  ? 443 GLU   A CD  1 
ATOM   1084 O OE1 . GLU   A 1 151 ? 8.031   -7.175  29.325 1.00 40.23  ? 443 GLU   A OE1 1 
ATOM   1085 O OE2 . GLU   A 1 151 ? 7.264   -5.214  28.697 1.00 51.93  ? 443 GLU   A OE2 1 
ATOM   1086 N N   . GLU   A 1 152 ? 9.998   -10.897 27.320 1.00 26.57  ? 444 GLU   A N   1 
ATOM   1087 C CA  . GLU   A 1 152 ? 10.894  -12.011 27.037 1.00 21.18  ? 444 GLU   A CA  1 
ATOM   1088 C C   . GLU   A 1 152 ? 10.121  -13.251 26.610 1.00 18.26  ? 444 GLU   A C   1 
ATOM   1089 O O   . GLU   A 1 152 ? 10.605  -14.022 25.774 1.00 23.66  ? 444 GLU   A O   1 
ATOM   1090 C CB  . GLU   A 1 152 ? 11.752  -12.325 28.262 1.00 24.48  ? 444 GLU   A CB  1 
ATOM   1091 C CG  . GLU   A 1 152 ? 12.747  -11.239 28.627 1.00 25.73  ? 444 GLU   A CG  1 
ATOM   1092 C CD  . GLU   A 1 152 ? 13.407  -11.492 29.969 1.00 26.01  ? 444 GLU   A CD  1 
ATOM   1093 O OE1 . GLU   A 1 152 ? 12.685  -11.840 30.928 1.00 28.00  ? 444 GLU   A OE1 1 
ATOM   1094 O OE2 . GLU   A 1 152 ? 14.644  -11.351 30.065 1.00 29.23  ? 444 GLU   A OE2 1 
ATOM   1095 N N   . PHE   A 1 153 ? 8.925   -13.455 27.168 1.00 24.16  ? 445 PHE   A N   1 
ATOM   1096 C CA  . PHE   A 1 153 ? 8.145   -14.648 26.850 1.00 24.26  ? 445 PHE   A CA  1 
ATOM   1097 C C   . PHE   A 1 153 ? 7.734   -14.667 25.384 1.00 21.46  ? 445 PHE   A C   1 
ATOM   1098 O O   . PHE   A 1 153 ? 7.835   -15.701 24.712 1.00 22.49  ? 445 PHE   A O   1 
ATOM   1099 C CB  . PHE   A 1 153 ? 6.914   -14.727 27.750 1.00 24.95  ? 445 PHE   A CB  1 
ATOM   1100 C CG  . PHE   A 1 153 ? 5.861   -15.676 27.249 1.00 22.58  ? 445 PHE   A CG  1 
ATOM   1101 C CD1 . PHE   A 1 153 ? 6.063   -17.046 27.297 1.00 20.95  ? 445 PHE   A CD1 1 
ATOM   1102 C CD2 . PHE   A 1 153 ? 4.673   -15.197 26.724 1.00 24.99  ? 445 PHE   A CD2 1 
ATOM   1103 C CE1 . PHE   A 1 153 ? 5.096   -17.921 26.833 1.00 18.56  ? 445 PHE   A CE1 1 
ATOM   1104 C CE2 . PHE   A 1 153 ? 3.701   -16.066 26.259 1.00 22.81  ? 445 PHE   A CE2 1 
ATOM   1105 C CZ  . PHE   A 1 153 ? 3.913   -17.431 26.315 1.00 23.32  ? 445 PHE   A CZ  1 
ATOM   1106 N N   . VAL   A 1 154 ? 7.262   -13.529 24.868 1.00 19.51  ? 446 VAL   A N   1 
ATOM   1107 C CA  . VAL   A 1 154 ? 6.830   -13.484 23.475 1.00 20.80  ? 446 VAL   A CA  1 
ATOM   1108 C C   . VAL   A 1 154 ? 8.015   -13.671 22.534 1.00 18.46  ? 446 VAL   A C   1 
ATOM   1109 O O   . VAL   A 1 154 ? 7.856   -14.186 21.421 1.00 22.34  ? 446 VAL   A O   1 
ATOM   1110 C CB  . VAL   A 1 154 ? 6.068   -12.176 23.188 1.00 26.53  ? 446 VAL   A CB  1 
ATOM   1111 C CG1 . VAL   A 1 154 ? 4.881   -12.041 24.129 1.00 20.08  ? 446 VAL   A CG1 1 
ATOM   1112 C CG2 . VAL   A 1 154 ? 6.987   -10.972 23.319 1.00 21.40  ? 446 VAL   A CG2 1 
ATOM   1113 N N   . CYS   A 1 155 ? 9.216   -13.273 22.960 1.00 17.45  ? 447 CYS   A N   1 
ATOM   1114 C CA  . CYS   A 1 155 ? 10.407  -13.544 22.161 1.00 21.21  ? 447 CYS   A CA  1 
ATOM   1115 C C   . CYS   A 1 155 ? 10.735  -15.031 22.156 1.00 18.07  ? 447 CYS   A C   1 
ATOM   1116 O O   . CYS   A 1 155 ? 11.047  -15.600 21.103 1.00 24.85  ? 447 CYS   A O   1 
ATOM   1117 C CB  . CYS   A 1 155 ? 11.593  -12.739 22.692 1.00 20.89  ? 447 CYS   A CB  1 
ATOM   1118 S SG  . CYS   A 1 155 ? 11.498  -10.955 22.416 1.00 26.83  ? 447 CYS   A SG  1 
ATOM   1119 N N   . LEU   A 1 156 ? 10.669  -15.676 23.324 1.00 20.88  ? 448 LEU   A N   1 
ATOM   1120 C CA  . LEU   A 1 156 ? 10.949  -17.106 23.406 1.00 22.72  ? 448 LEU   A CA  1 
ATOM   1121 C C   . LEU   A 1 156 ? 9.952   -17.911 22.584 1.00 20.71  ? 448 LEU   A C   1 
ATOM   1122 O O   . LEU   A 1 156 ? 10.325  -18.885 21.920 1.00 24.17  ? 448 LEU   A O   1 
ATOM   1123 C CB  . LEU   A 1 156 ? 10.922  -17.563 24.865 1.00 17.72  ? 448 LEU   A CB  1 
ATOM   1124 C CG  . LEU   A 1 156 ? 12.082  -17.138 25.765 1.00 22.96  ? 448 LEU   A CG  1 
ATOM   1125 C CD1 . LEU   A 1 156 ? 12.013  -17.872 27.098 1.00 29.82  ? 448 LEU   A CD1 1 
ATOM   1126 C CD2 . LEU   A 1 156 ? 13.420  -17.380 25.081 1.00 23.91  ? 448 LEU   A CD2 1 
ATOM   1127 N N   . LYS   A 1 157 ? 8.675   -17.522 22.622 1.00 18.49  ? 449 LYS   A N   1 
ATOM   1128 C CA  . LYS   A 1 157 ? 7.659   -18.227 21.847 1.00 23.75  ? 449 LYS   A CA  1 
ATOM   1129 C C   . LYS   A 1 157 ? 7.892   -18.061 20.351 1.00 24.37  ? 449 LYS   A C   1 
ATOM   1130 O O   . LYS   A 1 157 ? 7.706   -19.008 19.579 1.00 23.26  ? 449 LYS   A O   1 
ATOM   1131 C CB  . LYS   A 1 157 ? 6.268   -17.724 22.235 1.00 19.43  ? 449 LYS   A CB  1 
ATOM   1132 C CG  . LYS   A 1 157 ? 5.141   -18.686 21.913 1.00 22.09  ? 449 LYS   A CG  1 
ATOM   1133 C CD  . LYS   A 1 157 ? 3.864   -18.296 22.641 1.00 25.44  ? 449 LYS   A CD  1 
ATOM   1134 C CE  . LYS   A 1 157 ? 3.572   -16.810 22.493 1.00 24.10  ? 449 LYS   A CE  1 
ATOM   1135 N NZ  . LYS   A 1 157 ? 2.143   -16.496 22.765 1.00 25.43  ? 449 LYS   A NZ  1 
ATOM   1136 N N   . SER   A 1 158 ? 8.298   -16.862 19.925 1.00 18.01  ? 450 SER   A N   1 
ATOM   1137 C CA  . SER   A 1 158 ? 8.586   -16.638 18.513 1.00 21.74  ? 450 SER   A CA  1 
ATOM   1138 C C   . SER   A 1 158 ? 9.833   -17.391 18.069 1.00 19.00  ? 450 SER   A C   1 
ATOM   1139 O O   . SER   A 1 158 ? 9.904   -17.845 16.921 1.00 20.44  ? 450 SER   A O   1 
ATOM   1140 C CB  . SER   A 1 158 ? 8.743   -15.143 18.242 1.00 18.91  ? 450 SER   A CB  1 
ATOM   1141 O OG  . SER   A 1 158 ? 7.566   -14.444 18.602 1.00 41.65  ? 450 SER   A OG  1 
ATOM   1142 N N   . ILE   A 1 159 ? 10.820  -17.533 18.956 1.00 18.11  ? 451 ILE   A N   1 
ATOM   1143 C CA  . ILE   A 1 159 ? 12.007  -18.318 18.627 1.00 18.74  ? 451 ILE   A CA  1 
ATOM   1144 C C   . ILE   A 1 159 ? 11.630  -19.775 18.398 1.00 17.08  ? 451 ILE   A C   1 
ATOM   1145 O O   . ILE   A 1 159 ? 12.109  -20.415 17.455 1.00 25.77  ? 451 ILE   A O   1 
ATOM   1146 C CB  . ILE   A 1 159 ? 13.069  -18.174 19.732 1.00 20.98  ? 451 ILE   A CB  1 
ATOM   1147 C CG1 . ILE   A 1 159 ? 13.723  -16.795 19.668 1.00 31.37  ? 451 ILE   A CG1 1 
ATOM   1148 C CG2 . ILE   A 1 159 ? 14.127  -19.254 19.599 1.00 19.91  ? 451 ILE   A CG2 1 
ATOM   1149 C CD1 . ILE   A 1 159 ? 14.450  -16.406 20.937 1.00 20.88  ? 451 ILE   A CD1 1 
ATOM   1150 N N   . ILE   A 1 160 ? 10.763  -20.320 19.255 1.00 20.13  ? 452 ILE   A N   1 
ATOM   1151 C CA  . ILE   A 1 160 ? 10.323  -21.705 19.097 1.00 22.96  ? 452 ILE   A CA  1 
ATOM   1152 C C   . ILE   A 1 160 ? 9.648   -21.898 17.746 1.00 21.72  ? 452 ILE   A C   1 
ATOM   1153 O O   . ILE   A 1 160 ? 9.889   -22.892 17.049 1.00 24.10  ? 452 ILE   A O   1 
ATOM   1154 C CB  . ILE   A 1 160 ? 9.389   -22.103 20.255 1.00 21.54  ? 452 ILE   A CB  1 
ATOM   1155 C CG1 . ILE   A 1 160 ? 10.176  -22.230 21.562 1.00 23.52  ? 452 ILE   A CG1 1 
ATOM   1156 C CG2 . ILE   A 1 160 ? 8.661   -23.397 19.932 1.00 19.90  ? 452 ILE   A CG2 1 
ATOM   1157 C CD1 . ILE   A 1 160 ? 9.300   -22.272 22.794 1.00 23.84  ? 452 ILE   A CD1 1 
ATOM   1158 N N   . LEU   A 1 161 ? 8.799   -20.945 17.354 1.00 17.48  ? 453 LEU   A N   1 
ATOM   1159 C CA  . LEU   A 1 161 ? 8.092   -21.040 16.081 1.00 19.59  ? 453 LEU   A CA  1 
ATOM   1160 C C   . LEU   A 1 161 ? 9.062   -21.160 14.911 1.00 18.96  ? 453 LEU   A C   1 
ATOM   1161 O O   . LEU   A 1 161 ? 8.836   -21.948 13.985 1.00 21.39  ? 453 LEU   A O   1 
ATOM   1162 C CB  . LEU   A 1 161 ? 7.188   -19.820 15.901 1.00 18.55  ? 453 LEU   A CB  1 
ATOM   1163 C CG  . LEU   A 1 161 ? 6.489   -19.648 14.552 1.00 23.22  ? 453 LEU   A CG  1 
ATOM   1164 C CD1 . LEU   A 1 161 ? 5.622   -20.857 14.235 1.00 25.92  ? 453 LEU   A CD1 1 
ATOM   1165 C CD2 . LEU   A 1 161 ? 5.669   -18.367 14.535 1.00 19.03  ? 453 LEU   A CD2 1 
ATOM   1166 N N   . LEU   A 1 162 ? 10.153  -20.398 14.942 1.00 21.26  ? 454 LEU   A N   1 
ATOM   1167 C CA  . LEU   A 1 162 ? 11.073  -20.341 13.813 1.00 22.47  ? 454 LEU   A CA  1 
ATOM   1168 C C   . LEU   A 1 162 ? 12.200  -21.360 13.904 1.00 22.15  ? 454 LEU   A C   1 
ATOM   1169 O O   . LEU   A 1 162 ? 12.740  -21.764 12.868 1.00 25.91  ? 454 LEU   A O   1 
ATOM   1170 C CB  . LEU   A 1 162 ? 11.667  -18.935 13.697 1.00 19.88  ? 454 LEU   A CB  1 
ATOM   1171 C CG  . LEU   A 1 162 ? 10.650  -17.819 13.454 1.00 21.76  ? 454 LEU   A CG  1 
ATOM   1172 C CD1 . LEU   A 1 162 ? 11.253  -16.464 13.782 1.00 31.28  ? 454 LEU   A CD1 1 
ATOM   1173 C CD2 . LEU   A 1 162 ? 10.147  -17.854 12.021 1.00 20.63  ? 454 LEU   A CD2 1 
ATOM   1174 N N   . ASN   A 1 163 ? 12.565  -21.792 15.110 1.00 23.14  ? 455 ASN   A N   1 
ATOM   1175 C CA  . ASN   A 1 163 ? 13.724  -22.660 15.278 1.00 25.68  ? 455 ASN   A CA  1 
ATOM   1176 C C   . ASN   A 1 163 ? 13.380  -24.143 15.289 1.00 25.54  ? 455 ASN   A C   1 
ATOM   1177 O O   . ASN   A 1 163 ? 14.201  -24.958 14.852 1.00 25.48  ? 455 ASN   A O   1 
ATOM   1178 C CB  . ASN   A 1 163 ? 14.459  -22.318 16.577 1.00 20.74  ? 455 ASN   A CB  1 
ATOM   1179 C CG  . ASN   A 1 163 ? 15.764  -23.074 16.723 1.00 22.25  ? 455 ASN   A CG  1 
ATOM   1180 O OD1 . ASN   A 1 163 ? 16.712  -22.847 15.973 1.00 27.48  ? 455 ASN   A OD1 1 
ATOM   1181 N ND2 . ASN   A 1 163 ? 15.815  -23.991 17.685 1.00 22.76  ? 455 ASN   A ND2 1 
ATOM   1182 N N   . SER   A 1 164 ? 12.190  -24.513 15.771 1.00 21.96  ? 456 SER   A N   1 
ATOM   1183 C CA  . SER   A 1 164 ? 11.903  -25.921 16.035 1.00 33.40  ? 456 SER   A CA  1 
ATOM   1184 C C   . SER   A 1 164 ? 11.949  -26.768 14.771 1.00 28.67  ? 456 SER   A C   1 
ATOM   1185 O O   . SER   A 1 164 ? 12.360  -27.934 14.824 1.00 29.59  ? 456 SER   A O   1 
ATOM   1186 C CB  . SER   A 1 164 ? 10.544  -26.066 16.721 1.00 38.46  ? 456 SER   A CB  1 
ATOM   1187 O OG  . SER   A 1 164 ? 10.627  -25.700 18.087 1.00 31.66  ? 456 SER   A OG  1 
ATOM   1188 N N   . GLY   A 1 165 ? 11.542  -26.212 13.631 1.00 29.09  ? 457 GLY   A N   1 
ATOM   1189 C CA  . GLY   A 1 165 ? 11.522  -26.955 12.387 1.00 27.53  ? 457 GLY   A CA  1 
ATOM   1190 C C   . GLY   A 1 165 ? 12.573  -26.573 11.370 1.00 31.31  ? 457 GLY   A C   1 
ATOM   1191 O O   . GLY   A 1 165 ? 12.546  -27.098 10.251 1.00 36.84  ? 457 GLY   A O   1 
ATOM   1192 N N   . VAL   A 1 166 ? 13.513  -25.688 11.715 1.00 34.12  ? 458 VAL   A N   1 
ATOM   1193 C CA  . VAL   A 1 166 ? 14.457  -25.180 10.724 1.00 30.35  ? 458 VAL   A CA  1 
ATOM   1194 C C   . VAL   A 1 166 ? 15.555  -26.182 10.385 1.00 31.56  ? 458 VAL   A C   1 
ATOM   1195 O O   . VAL   A 1 166 ? 16.230  -26.022 9.360  1.00 41.01  ? 458 VAL   A O   1 
ATOM   1196 C CB  . VAL   A 1 166 ? 15.077  -23.855 11.204 1.00 32.92  ? 458 VAL   A CB  1 
ATOM   1197 C CG1 . VAL   A 1 166 ? 16.221  -24.116 12.173 1.00 28.72  ? 458 VAL   A CG1 1 
ATOM   1198 C CG2 . VAL   A 1 166 ? 15.543  -23.018 10.017 1.00 27.86  ? 458 VAL   A CG2 1 
ATOM   1199 N N   . TYR   A 1 167 ? 15.757  -27.211 11.205 1.00 33.10  ? 459 TYR   A N   1 
ATOM   1200 C CA  . TYR   A 1 167 ? 16.769  -28.223 10.936 1.00 39.99  ? 459 TYR   A CA  1 
ATOM   1201 C C   . TYR   A 1 167 ? 16.183  -29.496 10.339 1.00 41.93  ? 459 TYR   A C   1 
ATOM   1202 O O   . TYR   A 1 167 ? 16.884  -30.511 10.264 1.00 53.86  ? 459 TYR   A O   1 
ATOM   1203 C CB  . TYR   A 1 167 ? 17.544  -28.558 12.214 1.00 34.01  ? 459 TYR   A CB  1 
ATOM   1204 C CG  . TYR   A 1 167 ? 17.952  -27.348 13.024 1.00 44.89  ? 459 TYR   A CG  1 
ATOM   1205 C CD1 . TYR   A 1 167 ? 19.031  -26.562 12.640 1.00 57.25  ? 459 TYR   A CD1 1 
ATOM   1206 C CD2 . TYR   A 1 167 ? 17.255  -26.990 14.171 1.00 44.11  ? 459 TYR   A CD2 1 
ATOM   1207 C CE1 . TYR   A 1 167 ? 19.408  -25.456 13.379 1.00 47.19  ? 459 TYR   A CE1 1 
ATOM   1208 C CE2 . TYR   A 1 167 ? 17.624  -25.886 14.916 1.00 46.50  ? 459 TYR   A CE2 1 
ATOM   1209 C CZ  . TYR   A 1 167 ? 18.699  -25.121 14.515 1.00 53.03  ? 459 TYR   A CZ  1 
ATOM   1210 O OH  . TYR   A 1 167 ? 19.065  -24.019 15.254 1.00 40.31  ? 459 TYR   A OH  1 
ATOM   1211 N N   . THR   A 1 168 ? 14.924  -29.470 9.907  1.00 41.90  ? 460 THR   A N   1 
ATOM   1212 C CA  . THR   A 1 168 ? 14.264  -30.667 9.394  1.00 51.18  ? 460 THR   A CA  1 
ATOM   1213 C C   . THR   A 1 168 ? 13.421  -30.342 8.168  1.00 51.49  ? 460 THR   A C   1 
ATOM   1214 O O   . THR   A 1 168 ? 12.328  -30.886 7.983  1.00 57.50  ? 460 THR   A O   1 
ATOM   1215 C CB  . THR   A 1 168 ? 13.407  -31.328 10.473 1.00 46.81  ? 460 THR   A CB  1 
ATOM   1216 O OG1 . THR   A 1 168 ? 12.592  -30.338 11.113 1.00 42.33  ? 460 THR   A OG1 1 
ATOM   1217 N N   . PHE   A 1 169 ? 13.919  -29.460 7.306  1.00 60.60  ? 461 PHE   A N   1 
ATOM   1218 C CA  . PHE   A 1 169 ? 13.219  -29.132 6.066  1.00 57.47  ? 461 PHE   A CA  1 
ATOM   1219 C C   . PHE   A 1 169 ? 13.401  -30.241 5.032  1.00 57.95  ? 461 PHE   A C   1 
ATOM   1220 O O   . PHE   A 1 169 ? 14.442  -30.897 4.986  1.00 73.87  ? 461 PHE   A O   1 
ATOM   1221 C CB  . PHE   A 1 169 ? 13.712  -27.800 5.495  1.00 49.69  ? 461 PHE   A CB  1 
ATOM   1222 C CG  . PHE   A 1 169 ? 12.925  -26.605 5.961  1.00 50.31  ? 461 PHE   A CG  1 
ATOM   1223 C CD1 . PHE   A 1 169 ? 11.649  -26.752 6.480  1.00 60.57  ? 461 PHE   A CD1 1 
ATOM   1224 C CD2 . PHE   A 1 169 ? 13.463  -25.332 5.875  1.00 64.85  ? 461 PHE   A CD2 1 
ATOM   1225 C CE1 . PHE   A 1 169 ? 10.926  -25.650 6.907  1.00 48.40  ? 461 PHE   A CE1 1 
ATOM   1226 C CE2 . PHE   A 1 169 ? 12.746  -24.227 6.299  1.00 61.83  ? 461 PHE   A CE2 1 
ATOM   1227 C CZ  . PHE   A 1 169 ? 11.476  -24.387 6.817  1.00 41.08  ? 461 PHE   A CZ  1 
ATOM   1228 N N   . SER   A 1 172 ? 16.790  -28.376 0.641  1.00 56.16  ? 464 SER   A N   1 
ATOM   1229 C CA  . SER   A 1 172 ? 17.993  -28.517 -0.172 1.00 53.49  ? 464 SER   A CA  1 
ATOM   1230 C C   . SER   A 1 172 ? 17.913  -27.662 -1.433 1.00 66.74  ? 464 SER   A C   1 
ATOM   1231 O O   . SER   A 1 172 ? 18.932  -27.341 -2.042 1.00 65.60  ? 464 SER   A O   1 
ATOM   1232 C CB  . SER   A 1 172 ? 18.216  -29.984 -0.546 1.00 75.83  ? 464 SER   A CB  1 
ATOM   1233 O OG  . SER   A 1 172 ? 17.210  -30.440 -1.434 1.00 80.69  ? 464 SER   A OG  1 
ATOM   1234 N N   . THR   A 1 173 ? 16.693  -27.297 -1.818 1.00 71.96  ? 465 THR   A N   1 
ATOM   1235 C CA  . THR   A 1 173 ? 16.492  -26.481 -3.005 1.00 67.05  ? 465 THR   A CA  1 
ATOM   1236 C C   . THR   A 1 173 ? 16.983  -25.054 -2.770 1.00 56.70  ? 465 THR   A C   1 
ATOM   1237 O O   . THR   A 1 173 ? 17.201  -24.618 -1.636 1.00 49.82  ? 465 THR   A O   1 
ATOM   1238 C CB  . THR   A 1 173 ? 15.015  -26.465 -3.401 1.00 65.93  ? 465 THR   A CB  1 
ATOM   1239 O OG1 . THR   A 1 173 ? 14.328  -25.452 -2.656 1.00 55.83  ? 465 THR   A OG1 1 
ATOM   1240 C CG2 . THR   A 1 173 ? 14.372  -27.817 -3.120 1.00 75.75  ? 465 THR   A CG2 1 
ATOM   1241 N N   . LEU   A 1 174 ? 17.161  -24.324 -3.877 1.00 37.89  ? 466 LEU   A N   1 
ATOM   1242 C CA  . LEU   A 1 174 ? 17.572  -22.925 -3.790 1.00 47.49  ? 466 LEU   A CA  1 
ATOM   1243 C C   . LEU   A 1 174 ? 16.571  -22.106 -2.986 1.00 46.78  ? 466 LEU   A C   1 
ATOM   1244 O O   . LEU   A 1 174 ? 16.959  -21.235 -2.198 1.00 44.54  ? 466 LEU   A O   1 
ATOM   1245 C CB  . LEU   A 1 174 ? 17.740  -22.339 -5.191 1.00 52.31  ? 466 LEU   A CB  1 
ATOM   1246 C CG  . LEU   A 1 174 ? 18.313  -20.923 -5.273 1.00 56.38  ? 466 LEU   A CG  1 
ATOM   1247 C CD1 . LEU   A 1 174 ? 19.563  -20.788 -4.416 1.00 56.60  ? 466 LEU   A CD1 1 
ATOM   1248 C CD2 . LEU   A 1 174 ? 18.603  -20.550 -6.717 1.00 50.03  ? 466 LEU   A CD2 1 
ATOM   1249 N N   . LYS   A 1 175 ? 15.276  -22.366 -3.177 1.00 41.52  ? 467 LYS   A N   1 
ATOM   1250 C CA  . LYS   A 1 175 ? 14.258  -21.714 -2.360 1.00 38.27  ? 467 LYS   A CA  1 
ATOM   1251 C C   . LYS   A 1 175 ? 14.419  -22.071 -0.888 1.00 40.22  ? 467 LYS   A C   1 
ATOM   1252 O O   . LYS   A 1 175 ? 14.327  -21.198 -0.016 1.00 45.61  ? 467 LYS   A O   1 
ATOM   1253 C CB  . LYS   A 1 175 ? 12.865  -22.107 -2.844 1.00 35.38  ? 467 LYS   A CB  1 
ATOM   1254 C CG  . LYS   A 1 175 ? 11.765  -21.704 -1.880 1.00 54.64  ? 467 LYS   A CG  1 
ATOM   1255 C CD  . LYS   A 1 175 ? 10.863  -22.884 -1.569 1.00 63.85  ? 467 LYS   A CD  1 
ATOM   1256 C CE  . LYS   A 1 175 ? 11.223  -23.501 -0.237 1.00 51.62  ? 467 LYS   A CE  1 
ATOM   1257 N NZ  . LYS   A 1 175 ? 10.134  -24.372 0.278  1.00 53.24  ? 467 LYS   A NZ  1 
ATOM   1258 N N   . SER   A 1 176 ? 14.662  -23.350 -0.594 1.00 42.24  ? 468 SER   A N   1 
ATOM   1259 C CA  . SER   A 1 176 ? 14.824  -23.774 0.792  1.00 34.82  ? 468 SER   A CA  1 
ATOM   1260 C C   . SER   A 1 176 ? 16.031  -23.112 1.441  1.00 39.71  ? 468 SER   A C   1 
ATOM   1261 O O   . SER   A 1 176 ? 16.024  -22.861 2.652  1.00 39.33  ? 468 SER   A O   1 
ATOM   1262 C CB  . SER   A 1 176 ? 14.947  -25.296 0.866  1.00 45.00  ? 468 SER   A CB  1 
ATOM   1263 O OG  . SER   A 1 176 ? 13.720  -25.924 0.535  1.00 67.04  ? 468 SER   A OG  1 
ATOM   1264 N N   . LEU   A 1 177 ? 17.069  -22.816 0.657  1.00 36.02  ? 469 LEU   A N   1 
ATOM   1265 C CA  . LEU   A 1 177 ? 18.232  -22.130 1.208  1.00 34.45  ? 469 LEU   A CA  1 
ATOM   1266 C C   . LEU   A 1 177 ? 17.917  -20.671 1.511  1.00 33.39  ? 469 LEU   A C   1 
ATOM   1267 O O   . LEU   A 1 177 ? 18.424  -20.111 2.490  1.00 34.89  ? 469 LEU   A O   1 
ATOM   1268 C CB  . LEU   A 1 177 ? 19.412  -22.242 0.244  1.00 41.37  ? 469 LEU   A CB  1 
ATOM   1269 C CG  . LEU   A 1 177 ? 19.927  -23.664 0.006  1.00 53.40  ? 469 LEU   A CG  1 
ATOM   1270 C CD1 . LEU   A 1 177 ? 20.915  -23.698 -1.149 1.00 40.62  ? 469 LEU   A CD1 1 
ATOM   1271 C CD2 . LEU   A 1 177 ? 20.552  -24.229 1.274  1.00 43.40  ? 469 LEU   A CD2 1 
ATOM   1272 N N   . GLU   A 1 178 ? 17.082  -20.038 0.683  1.00 32.44  ? 470 GLU   A N   1 
ATOM   1273 C CA  . GLU   A 1 178 ? 16.647  -18.676 0.974  1.00 32.97  ? 470 GLU   A CA  1 
ATOM   1274 C C   . GLU   A 1 178 ? 15.756  -18.635 2.208  1.00 30.99  ? 470 GLU   A C   1 
ATOM   1275 O O   . GLU   A 1 178 ? 15.886  -17.734 3.045  1.00 38.27  ? 470 GLU   A O   1 
ATOM   1276 C CB  . GLU   A 1 178 ? 15.913  -18.086 -0.230 1.00 35.57  ? 470 GLU   A CB  1 
ATOM   1277 C CG  . GLU   A 1 178 ? 16.815  -17.695 -1.387 1.00 39.69  ? 470 GLU   A CG  1 
ATOM   1278 C CD  . GLU   A 1 178 ? 16.061  -17.583 -2.697 1.00 47.61  ? 470 GLU   A CD  1 
ATOM   1279 O OE1 . GLU   A 1 178 ? 14.826  -17.770 -2.693 1.00 62.81  ? 470 GLU   A OE1 1 
ATOM   1280 O OE2 . GLU   A 1 178 ? 16.704  -17.305 -3.731 1.00 52.24  ? 470 GLU   A OE2 1 
ATOM   1281 N N   . GLU   A 1 179 ? 14.844  -19.603 2.337  1.00 36.25  ? 471 GLU   A N   1 
ATOM   1282 C CA  . GLU   A 1 179 ? 13.945  -19.635 3.487  1.00 38.79  ? 471 GLU   A CA  1 
ATOM   1283 C C   . GLU   A 1 179 ? 14.718  -19.823 4.785  1.00 30.30  ? 471 GLU   A C   1 
ATOM   1284 O O   . GLU   A 1 179 ? 14.453  -19.143 5.783  1.00 29.13  ? 471 GLU   A O   1 
ATOM   1285 C CB  . GLU   A 1 179 ? 12.910  -20.747 3.314  1.00 28.93  ? 471 GLU   A CB  1 
ATOM   1286 C CG  . GLU   A 1 179 ? 12.023  -20.594 2.092  1.00 34.02  ? 471 GLU   A CG  1 
ATOM   1287 C CD  . GLU   A 1 179 ? 10.740  -19.852 2.399  1.00 41.84  ? 471 GLU   A CD  1 
ATOM   1288 O OE1 . GLU   A 1 179 ? 9.748   -20.506 2.782  1.00 32.96  ? 471 GLU   A OE1 1 
ATOM   1289 O OE2 . GLU   A 1 179 ? 10.725  -18.612 2.258  1.00 51.46  ? 471 GLU   A OE2 1 
ATOM   1290 N N   . LYS   A 1 180 ? 15.680  -20.750 4.790  1.00 28.90  ? 472 LYS   A N   1 
ATOM   1291 C CA  . LYS   A 1 180 ? 16.457  -21.006 5.999  1.00 39.81  ? 472 LYS   A CA  1 
ATOM   1292 C C   . LYS   A 1 180 ? 17.281  -19.787 6.394  1.00 27.43  ? 472 LYS   A C   1 
ATOM   1293 O O   . LYS   A 1 180 ? 17.371  -19.447 7.579  1.00 32.85  ? 472 LYS   A O   1 
ATOM   1294 C CB  . LYS   A 1 180 ? 17.359  -22.222 5.794  1.00 37.96  ? 472 LYS   A CB  1 
ATOM   1295 C CG  . LYS   A 1 180 ? 16.630  -23.552 5.867  1.00 45.85  ? 472 LYS   A CG  1 
ATOM   1296 C CD  . LYS   A 1 180 ? 17.609  -24.715 5.887  1.00 53.30  ? 472 LYS   A CD  1 
ATOM   1297 C CE  . LYS   A 1 180 ? 17.203  -25.793 4.897  1.00 55.42  ? 472 LYS   A CE  1 
ATOM   1298 N NZ  . LYS   A 1 180 ? 18.265  -26.824 4.731  1.00 53.12  ? 472 LYS   A NZ  1 
ATOM   1299 N N   A ASP   A 1 181 ? 17.892  -19.119 5.412  0.98 30.35  ? 473 ASP   A N   1 
ATOM   1300 C CA  A ASP   A 1 181 ? 18.642  -17.902 5.702  0.98 34.24  ? 473 ASP   A CA  1 
ATOM   1301 C C   A ASP   A 1 181 ? 17.734  -16.822 6.274  0.98 33.80  ? 473 ASP   A C   1 
ATOM   1302 O O   A ASP   A 1 181 ? 18.110  -16.121 7.219  0.98 34.43  ? 473 ASP   A O   1 
ATOM   1303 C CB  A ASP   A 1 181 ? 19.342  -17.403 4.436  0.98 34.32  ? 473 ASP   A CB  1 
ATOM   1304 C CG  A ASP   A 1 181 ? 19.960  -16.029 4.613  0.98 50.45  ? 473 ASP   A CG  1 
ATOM   1305 O OD1 A ASP   A 1 181 ? 19.266  -15.023 4.350  0.98 62.79  ? 473 ASP   A OD1 1 
ATOM   1306 O OD2 A ASP   A 1 181 ? 21.140  -15.954 5.015  0.98 49.73  ? 473 ASP   A OD2 1 
ATOM   1307 N N   . HIS   A 1 182 ? 16.528  -16.680 5.717  1.00 39.04  ? 474 HIS   A N   1 
ATOM   1308 C CA  . HIS   A 1 182 ? 15.588  -15.689 6.230  1.00 29.97  ? 474 HIS   A CA  1 
ATOM   1309 C C   . HIS   A 1 182 ? 15.145  -16.026 7.648  1.00 26.43  ? 474 HIS   A C   1 
ATOM   1310 O O   . HIS   A 1 182 ? 15.042  -15.134 8.498  1.00 34.43  ? 474 HIS   A O   1 
ATOM   1311 C CB  . HIS   A 1 182 ? 14.378  -15.587 5.304  1.00 38.78  ? 474 HIS   A CB  1 
ATOM   1312 C CG  . HIS   A 1 182 ? 13.333  -14.628 5.781  1.00 34.81  ? 474 HIS   A CG  1 
ATOM   1313 N ND1 . HIS   A 1 182 ? 13.540  -13.267 5.834  1.00 48.28  ? 474 HIS   A ND1 1 
ATOM   1314 C CD2 . HIS   A 1 182 ? 12.072  -14.834 6.228  1.00 36.55  ? 474 HIS   A CD2 1 
ATOM   1315 C CE1 . HIS   A 1 182 ? 12.451  -12.675 6.291  1.00 43.46  ? 474 HIS   A CE1 1 
ATOM   1316 N NE2 . HIS   A 1 182 ? 11.545  -13.604 6.538  1.00 39.60  ? 474 HIS   A NE2 1 
ATOM   1317 N N   . ILE   A 1 183 ? 14.874  -17.305 7.919  1.00 31.61  ? 475 ILE   A N   1 
ATOM   1318 C CA  . ILE   A 1 183 ? 14.475  -17.714 9.264  1.00 27.71  ? 475 ILE   A CA  1 
ATOM   1319 C C   . ILE   A 1 183 ? 15.575  -17.390 10.265 1.00 31.62  ? 475 ILE   A C   1 
ATOM   1320 O O   . ILE   A 1 183 ? 15.307  -16.911 11.375 1.00 28.43  ? 475 ILE   A O   1 
ATOM   1321 C CB  . ILE   A 1 183 ? 14.117  -19.212 9.281  1.00 24.80  ? 475 ILE   A CB  1 
ATOM   1322 C CG1 . ILE   A 1 183 ? 12.783  -19.456 8.574  1.00 28.51  ? 475 ILE   A CG1 1 
ATOM   1323 C CG2 . ILE   A 1 183 ? 14.061  -19.733 10.706 1.00 21.40  ? 475 ILE   A CG2 1 
ATOM   1324 C CD1 . ILE   A 1 183 ? 12.536  -20.909 8.229  1.00 27.21  ? 475 ILE   A CD1 1 
ATOM   1325 N N   . HIS   A 1 184 ? 16.831  -17.633 9.887  1.00 27.08  ? 476 HIS   A N   1 
ATOM   1326 C CA  . HIS   A 1 184 ? 17.940  -17.346 10.789 1.00 32.83  ? 476 HIS   A CA  1 
ATOM   1327 C C   . HIS   A 1 184 ? 18.200  -15.849 10.902 1.00 25.34  ? 476 HIS   A C   1 
ATOM   1328 O O   . HIS   A 1 184 ? 18.675  -15.384 11.944 1.00 26.00  ? 476 HIS   A O   1 
ATOM   1329 C CB  . HIS   A 1 184 ? 19.196  -18.079 10.322 1.00 26.74  ? 476 HIS   A CB  1 
ATOM   1330 C CG  . HIS   A 1 184 ? 19.194  -19.541 10.645 1.00 32.80  ? 476 HIS   A CG  1 
ATOM   1331 N ND1 . HIS   A 1 184 ? 19.035  -20.019 11.928 1.00 31.96  ? 476 HIS   A ND1 1 
ATOM   1332 C CD2 . HIS   A 1 184 ? 19.324  -20.630 9.851  1.00 25.35  ? 476 HIS   A CD2 1 
ATOM   1333 C CE1 . HIS   A 1 184 ? 19.072  -21.340 11.911 1.00 31.29  ? 476 HIS   A CE1 1 
ATOM   1334 N NE2 . HIS   A 1 184 ? 19.246  -21.735 10.663 1.00 39.41  ? 476 HIS   A NE2 1 
ATOM   1335 N N   . ARG   A 1 185 ? 17.905  -15.082 9.850  1.00 25.89  ? 477 ARG   A N   1 
ATOM   1336 C CA  . ARG   A 1 185 ? 18.013  -13.630 9.951  1.00 28.56  ? 477 ARG   A CA  1 
ATOM   1337 C C   . ARG   A 1 185 ? 16.966  -13.069 10.905 1.00 27.80  ? 477 ARG   A C   1 
ATOM   1338 O O   . ARG   A 1 185 ? 17.253  -12.148 11.679 1.00 29.45  ? 477 ARG   A O   1 
ATOM   1339 C CB  . ARG   A 1 185 ? 17.881  -12.987 8.569  1.00 37.65  ? 477 ARG   A CB  1 
ATOM   1340 C CG  . ARG   A 1 185 ? 19.068  -13.200 7.634  1.00 41.53  ? 477 ARG   A CG  1 
ATOM   1341 C CD  . ARG   A 1 185 ? 20.376  -13.359 8.394  1.00 51.07  ? 477 ARG   A CD  1 
ATOM   1342 N NE  . ARG   A 1 185 ? 20.942  -14.693 8.232  1.00 58.32  ? 477 ARG   A NE  1 
ATOM   1343 N N   . VAL   A 1 186 ? 15.747  -13.611 10.865 1.00 33.27  ? 478 VAL   A N   1 
ATOM   1344 C CA  . VAL   A 1 186 ? 14.706  -13.160 11.783 1.00 33.12  ? 478 VAL   A CA  1 
ATOM   1345 C C   . VAL   A 1 186 ? 15.011  -13.621 13.204 1.00 28.39  ? 478 VAL   A C   1 
ATOM   1346 O O   . VAL   A 1 186 ? 14.765  -12.893 14.173 1.00 29.46  ? 478 VAL   A O   1 
ATOM   1347 C CB  . VAL   A 1 186 ? 13.325  -13.651 11.307 1.00 38.90  ? 478 VAL   A CB  1 
ATOM   1348 C CG1 . VAL   A 1 186 ? 12.242  -13.253 12.300 1.00 25.67  ? 478 VAL   A CG1 1 
ATOM   1349 C CG2 . VAL   A 1 186 ? 13.012  -13.093 9.926  1.00 30.37  ? 478 VAL   A CG2 1 
ATOM   1350 N N   . LEU   A 1 187 ? 15.555  -14.833 13.352 1.00 26.28  ? 479 LEU   A N   1 
ATOM   1351 C CA  . LEU   A 1 187 ? 15.939  -15.314 14.676 1.00 24.88  ? 479 LEU   A CA  1 
ATOM   1352 C C   . LEU   A 1 187 ? 17.017  -14.432 15.292 1.00 24.33  ? 479 LEU   A C   1 
ATOM   1353 O O   . LEU   A 1 187 ? 16.992  -14.159 16.498 1.00 26.02  ? 479 LEU   A O   1 
ATOM   1354 C CB  . LEU   A 1 187 ? 16.420  -16.762 14.596 1.00 23.23  ? 479 LEU   A CB  1 
ATOM   1355 C CG  . LEU   A 1 187 ? 15.345  -17.848 14.554 1.00 19.45  ? 479 LEU   A CG  1 
ATOM   1356 C CD1 . LEU   A 1 187 ? 15.959  -19.185 14.177 1.00 18.29  ? 479 LEU   A CD1 1 
ATOM   1357 C CD2 . LEU   A 1 187 ? 14.627  -17.941 15.893 1.00 20.03  ? 479 LEU   A CD2 1 
ATOM   1358 N N   . ASP   A 1 188 ? 17.977  -13.982 14.479 1.00 24.13  ? 480 ASP   A N   1 
ATOM   1359 C CA  . ASP   A 1 188 ? 18.996  -13.064 14.977 1.00 22.36  ? 480 ASP   A CA  1 
ATOM   1360 C C   . ASP   A 1 188 ? 18.374  -11.764 15.466 1.00 34.32  ? 480 ASP   A C   1 
ATOM   1361 O O   . ASP   A 1 188 ? 18.826  -11.183 16.460 1.00 33.92  ? 480 ASP   A O   1 
ATOM   1362 C CB  . ASP   A 1 188 ? 20.023  -12.774 13.884 1.00 23.14  ? 480 ASP   A CB  1 
ATOM   1363 C CG  . ASP   A 1 188 ? 20.939  -13.947 13.621 1.00 36.75  ? 480 ASP   A CG  1 
ATOM   1364 O OD1 . ASP   A 1 188 ? 20.968  -14.877 14.454 1.00 30.34  ? 480 ASP   A OD1 1 
ATOM   1365 O OD2 . ASP   A 1 188 ? 21.631  -13.938 12.581 1.00 30.56  ? 480 ASP   A OD2 1 
ATOM   1366 N N   . LYS   A 1 189 ? 17.339  -11.283 14.772 1.00 31.28  ? 481 LYS   A N   1 
ATOM   1367 C CA  . LYS   A 1 189 ? 16.699  -10.038 15.179 1.00 25.27  ? 481 LYS   A CA  1 
ATOM   1368 C C   . LYS   A 1 189 ? 15.905  -10.214 16.467 1.00 26.15  ? 481 LYS   A C   1 
ATOM   1369 O O   . LYS   A 1 189 ? 15.787  -9.267  17.253 1.00 26.34  ? 481 LYS   A O   1 
ATOM   1370 C CB  . LYS   A 1 189 ? 15.797  -9.517  14.061 1.00 27.68  ? 481 LYS   A CB  1 
ATOM   1371 C CG  . LYS   A 1 189 ? 15.028  -8.256  14.427 1.00 34.67  ? 481 LYS   A CG  1 
ATOM   1372 C CD  . LYS   A 1 189 ? 15.914  -7.017  14.442 1.00 45.18  ? 481 LYS   A CD  1 
ATOM   1373 C CE  . LYS   A 1 189 ? 16.245  -6.559  13.037 1.00 50.14  ? 481 LYS   A CE  1 
ATOM   1374 N NZ  . LYS   A 1 189 ? 17.470  -5.699  12.987 1.00 52.92  ? 481 LYS   A NZ  1 
ATOM   1375 N N   . ILE   A 1 190 ? 15.355  -11.407 16.702 1.00 24.97  ? 482 ILE   A N   1 
ATOM   1376 C CA  . ILE   A 1 190 ? 14.749  -11.693 17.998 1.00 21.98  ? 482 ILE   A CA  1 
ATOM   1377 C C   . ILE   A 1 190 ? 15.818  -11.717 19.082 1.00 31.69  ? 482 ILE   A C   1 
ATOM   1378 O O   . ILE   A 1 190 ? 15.599  -11.245 20.203 1.00 28.78  ? 482 ILE   A O   1 
ATOM   1379 C CB  . ILE   A 1 190 ? 13.969  -13.017 17.945 1.00 22.85  ? 482 ILE   A CB  1 
ATOM   1380 C CG1 . ILE   A 1 190 ? 12.893  -12.965 16.862 1.00 23.26  ? 482 ILE   A CG1 1 
ATOM   1381 C CG2 . ILE   A 1 190 ? 13.340  -13.303 19.297 1.00 18.95  ? 482 ILE   A CG2 1 
ATOM   1382 C CD1 . ILE   A 1 190 ? 12.335  -14.321 16.521 1.00 31.65  ? 482 ILE   A CD1 1 
ATOM   1383 N N   . THR   A 1 191 ? 16.994  -12.261 18.764 1.00 22.45  ? 483 THR   A N   1 
ATOM   1384 C CA  . THR   A 1 191 ? 18.086  -12.265 19.729 1.00 23.32  ? 483 THR   A CA  1 
ATOM   1385 C C   . THR   A 1 191 ? 18.519  -10.845 20.069 1.00 22.05  ? 483 THR   A C   1 
ATOM   1386 O O   . THR   A 1 191 ? 18.728  -10.517 21.242 1.00 28.52  ? 483 THR   A O   1 
ATOM   1387 C CB  . THR   A 1 191 ? 19.266  -13.068 19.189 1.00 27.30  ? 483 THR   A CB  1 
ATOM   1388 O OG1 . THR   A 1 191 ? 18.857  -14.422 18.960 1.00 26.90  ? 483 THR   A OG1 1 
ATOM   1389 C CG2 . THR   A 1 191 ? 20.412  -13.050 20.185 1.00 26.53  ? 483 THR   A CG2 1 
ATOM   1390 N N   . ASP   A 1 192 ? 18.656  -9.989  19.052 1.00 23.60  ? 484 ASP   A N   1 
ATOM   1391 C CA  . ASP   A 1 192 ? 18.922  -8.576  19.304 1.00 30.28  ? 484 ASP   A CA  1 
ATOM   1392 C C   . ASP   A 1 192 ? 17.836  -7.968  20.178 1.00 29.87  ? 484 ASP   A C   1 
ATOM   1393 O O   . ASP   A 1 192 ? 18.119  -7.147  21.058 1.00 29.80  ? 484 ASP   A O   1 
ATOM   1394 C CB  . ASP   A 1 192 ? 19.023  -7.814  17.982 1.00 26.83  ? 484 ASP   A CB  1 
ATOM   1395 C CG  . ASP   A 1 192 ? 20.162  -8.299  17.110 1.00 33.38  ? 484 ASP   A CG  1 
ATOM   1396 O OD1 . ASP   A 1 192 ? 20.997  -9.091  17.594 1.00 33.85  ? 484 ASP   A OD1 1 
ATOM   1397 O OD2 . ASP   A 1 192 ? 20.213  -7.893  15.930 1.00 39.41  ? 484 ASP   A OD2 1 
ATOM   1398 N N   . THR   A 1 193 ? 16.584  -8.371  19.951 1.00 28.77  ? 485 THR   A N   1 
ATOM   1399 C CA  . THR   A 1 193 ? 15.471  -7.847  20.732 1.00 37.51  ? 485 THR   A CA  1 
ATOM   1400 C C   . THR   A 1 193 ? 15.544  -8.313  22.181 1.00 30.46  ? 485 THR   A C   1 
ATOM   1401 O O   . THR   A 1 193 ? 15.294  -7.529  23.104 1.00 37.78  ? 485 THR   A O   1 
ATOM   1402 C CB  . THR   A 1 193 ? 14.148  -8.274  20.094 1.00 33.62  ? 485 THR   A CB  1 
ATOM   1403 O OG1 . THR   A 1 193 ? 14.064  -7.743  18.765 1.00 33.41  ? 485 THR   A OG1 1 
ATOM   1404 C CG2 . THR   A 1 193 ? 12.976  -7.769  20.906 1.00 32.00  ? 485 THR   A CG2 1 
ATOM   1405 N N   . LEU   A 1 194 ? 15.889  -9.584  22.400 1.00 27.08  ? 486 LEU   A N   1 
ATOM   1406 C CA  . LEU   A 1 194 ? 16.013  -10.100 23.760 1.00 32.32  ? 486 LEU   A CA  1 
ATOM   1407 C C   . LEU   A 1 194 ? 17.112  -9.372  24.523 1.00 28.97  ? 486 LEU   A C   1 
ATOM   1408 O O   . LEU   A 1 194 ? 16.932  -8.995  25.687 1.00 31.78  ? 486 LEU   A O   1 
ATOM   1409 C CB  . LEU   A 1 194 ? 16.287  -11.604 23.727 1.00 29.02  ? 486 LEU   A CB  1 
ATOM   1410 C CG  . LEU   A 1 194 ? 15.079  -12.537 23.823 1.00 32.49  ? 486 LEU   A CG  1 
ATOM   1411 C CD1 . LEU   A 1 194 ? 15.516  -13.988 23.680 1.00 24.24  ? 486 LEU   A CD1 1 
ATOM   1412 C CD2 . LEU   A 1 194 ? 14.338  -12.324 25.134 1.00 24.33  ? 486 LEU   A CD2 1 
ATOM   1413 N N   . ILE   A 1 195 ? 18.263  -9.165  23.878 1.00 29.27  ? 487 ILE   A N   1 
ATOM   1414 C CA  . ILE   A 1 195 ? 19.370  -8.468  24.527 1.00 23.51  ? 487 ILE   A CA  1 
ATOM   1415 C C   . ILE   A 1 195 ? 18.993  -7.020  24.814 1.00 27.47  ? 487 ILE   A C   1 
ATOM   1416 O O   . ILE   A 1 195 ? 19.300  -6.482  25.886 1.00 30.39  ? 487 ILE   A O   1 
ATOM   1417 C CB  . ILE   A 1 195 ? 20.639  -8.567  23.659 1.00 32.00  ? 487 ILE   A CB  1 
ATOM   1418 C CG1 . ILE   A 1 195 ? 21.189  -9.995  23.679 1.00 34.29  ? 487 ILE   A CG1 1 
ATOM   1419 C CG2 . ILE   A 1 195 ? 21.697  -7.579  24.128 1.00 32.74  ? 487 ILE   A CG2 1 
ATOM   1420 C CD1 . ILE   A 1 195 ? 21.725  -10.423 25.029 1.00 33.94  ? 487 ILE   A CD1 1 
ATOM   1421 N N   . HIS   A 1 196 ? 18.315  -6.369  23.865 1.00 33.11  ? 488 HIS   A N   1 
ATOM   1422 C CA  . HIS   A 1 196 ? 17.894  -4.986  24.069 1.00 31.75  ? 488 HIS   A CA  1 
ATOM   1423 C C   . HIS   A 1 196 ? 16.936  -4.869  25.247 1.00 37.59  ? 488 HIS   A C   1 
ATOM   1424 O O   . HIS   A 1 196 ? 16.985  -3.890  26.001 1.00 33.72  ? 488 HIS   A O   1 
ATOM   1425 C CB  . HIS   A 1 196 ? 17.252  -4.444  22.792 1.00 30.04  ? 488 HIS   A CB  1 
ATOM   1426 C CG  . HIS   A 1 196 ? 16.568  -3.124  22.969 1.00 46.35  ? 488 HIS   A CG  1 
ATOM   1427 N ND1 . HIS   A 1 196 ? 17.216  -1.921  22.787 1.00 48.66  ? 488 HIS   A ND1 1 
ATOM   1428 C CD2 . HIS   A 1 196 ? 15.291  -2.818  23.299 1.00 44.51  ? 488 HIS   A CD2 1 
ATOM   1429 C CE1 . HIS   A 1 196 ? 16.369  -0.930  23.005 1.00 41.37  ? 488 HIS   A CE1 1 
ATOM   1430 N NE2 . HIS   A 1 196 ? 15.194  -1.448  23.316 1.00 49.59  ? 488 HIS   A NE2 1 
ATOM   1431 N N   . LEU   A 1 197 ? 16.056  -5.859  25.422 1.00 32.76  ? 489 LEU   A N   1 
ATOM   1432 C CA  . LEU   A 1 197 ? 15.169  -5.863  26.582 1.00 29.88  ? 489 LEU   A CA  1 
ATOM   1433 C C   . LEU   A 1 197 ? 15.957  -6.028  27.874 1.00 29.34  ? 489 LEU   A C   1 
ATOM   1434 O O   . LEU   A 1 197 ? 15.598  -5.449  28.906 1.00 42.48  ? 489 LEU   A O   1 
ATOM   1435 C CB  . LEU   A 1 197 ? 14.130  -6.976  26.448 1.00 28.50  ? 489 LEU   A CB  1 
ATOM   1436 C CG  . LEU   A 1 197 ? 13.024  -6.777  25.411 1.00 31.27  ? 489 LEU   A CG  1 
ATOM   1437 C CD1 . LEU   A 1 197 ? 12.346  -8.101  25.094 1.00 26.37  ? 489 LEU   A CD1 1 
ATOM   1438 C CD2 . LEU   A 1 197 ? 12.012  -5.757  25.906 1.00 31.78  ? 489 LEU   A CD2 1 
ATOM   1439 N N   . MET   A 1 198 ? 17.038  -6.809  27.834 1.00 33.97  ? 490 MET   A N   1 
ATOM   1440 C CA  . MET   A 1 198 ? 17.844  -7.036  29.028 1.00 27.01  ? 490 MET   A CA  1 
ATOM   1441 C C   . MET   A 1 198 ? 18.715  -5.828  29.351 1.00 38.54  ? 490 MET   A C   1 
ATOM   1442 O O   . MET   A 1 198 ? 18.900  -5.490  30.525 1.00 33.40  ? 490 MET   A O   1 
ATOM   1443 C CB  . MET   A 1 198 ? 18.699  -8.288  28.841 1.00 26.54  ? 490 MET   A CB  1 
ATOM   1444 C CG  . MET   A 1 198 ? 17.939  -9.581  29.082 1.00 26.87  ? 490 MET   A CG  1 
ATOM   1445 S SD  . MET   A 1 198 ? 18.852  -11.034 28.539 1.00 33.79  ? 490 MET   A SD  1 
ATOM   1446 C CE  . MET   A 1 198 ? 17.511  -12.090 27.997 1.00 25.06  ? 490 MET   A CE  1 
ATOM   1447 N N   . ALA   A 1 199 ? 19.259  -5.166  28.325 1.00 39.98  ? 491 ALA   A N   1 
ATOM   1448 C CA  . ALA   A 1 199 ? 19.999  -3.931  28.559 1.00 41.97  ? 491 ALA   A CA  1 
ATOM   1449 C C   . ALA   A 1 199 ? 19.075  -2.827  29.056 1.00 45.75  ? 491 ALA   A C   1 
ATOM   1450 O O   . ALA   A 1 199 ? 19.460  -2.020  29.910 1.00 48.48  ? 491 ALA   A O   1 
ATOM   1451 C CB  . ALA   A 1 199 ? 20.718  -3.497  27.282 1.00 34.02  ? 491 ALA   A CB  1 
ATOM   1452 N N   . LYS   A 1 200 ? 17.845  -2.783  28.536 1.00 40.82  ? 492 LYS   A N   1 
ATOM   1453 C CA  . LYS   A 1 200 ? 16.869  -1.793  28.973 1.00 37.67  ? 492 LYS   A CA  1 
ATOM   1454 C C   . LYS   A 1 200 ? 16.427  -2.011  30.414 1.00 51.82  ? 492 LYS   A C   1 
ATOM   1455 O O   . LYS   A 1 200 ? 15.884  -1.087  31.027 1.00 48.74  ? 492 LYS   A O   1 
ATOM   1456 C CB  . LYS   A 1 200 ? 15.655  -1.823  28.044 1.00 42.32  ? 492 LYS   A CB  1 
ATOM   1457 C CG  . LYS   A 1 200 ? 15.262  -0.474  27.469 1.00 58.95  ? 492 LYS   A CG  1 
ATOM   1458 C CD  . LYS   A 1 200 ? 13.918  -0.561  26.762 1.00 57.09  ? 492 LYS   A CD  1 
ATOM   1459 C CE  . LYS   A 1 200 ? 12.789  -0.040  27.639 1.00 62.70  ? 492 LYS   A CE  1 
ATOM   1460 N NZ  . LYS   A 1 200 ? 11.464  -0.190  26.973 1.00 72.69  ? 492 LYS   A NZ  1 
ATOM   1461 N N   . ALA   A 1 201 ? 16.640  -3.205  30.962 1.00 45.24  ? 493 ALA   A N   1 
ATOM   1462 C CA  . ALA   A 1 201 ? 16.262  -3.517  32.333 1.00 41.49  ? 493 ALA   A CA  1 
ATOM   1463 C C   . ALA   A 1 201 ? 17.392  -3.287  33.329 1.00 46.33  ? 493 ALA   A C   1 
ATOM   1464 O O   . ALA   A 1 201 ? 17.192  -3.499  34.530 1.00 48.43  ? 493 ALA   A O   1 
ATOM   1465 C CB  . ALA   A 1 201 ? 15.777  -4.968  32.431 1.00 32.59  ? 493 ALA   A CB  1 
ATOM   1466 N N   . GLY   A 1 202 ? 18.567  -2.864  32.866 1.00 40.27  ? 494 GLY   A N   1 
ATOM   1467 C CA  . GLY   A 1 202 ? 19.684  -2.581  33.742 1.00 39.38  ? 494 GLY   A CA  1 
ATOM   1468 C C   . GLY   A 1 202 ? 20.712  -3.684  33.862 1.00 47.85  ? 494 GLY   A C   1 
ATOM   1469 O O   . GLY   A 1 202 ? 21.712  -3.497  34.566 1.00 48.88  ? 494 GLY   A O   1 
ATOM   1470 N N   . LEU   A 1 203 ? 20.502  -4.821  33.205 1.00 37.39  ? 495 LEU   A N   1 
ATOM   1471 C CA  . LEU   A 1 203 ? 21.454  -5.921  33.284 1.00 39.58  ? 495 LEU   A CA  1 
ATOM   1472 C C   . LEU   A 1 203 ? 22.777  -5.536  32.633 1.00 39.86  ? 495 LEU   A C   1 
ATOM   1473 O O   . LEU   A 1 203 ? 22.806  -4.902  31.575 1.00 33.43  ? 495 LEU   A O   1 
ATOM   1474 C CB  . LEU   A 1 203 ? 20.885  -7.167  32.605 1.00 37.51  ? 495 LEU   A CB  1 
ATOM   1475 C CG  . LEU   A 1 203 ? 20.124  -8.180  33.462 1.00 37.06  ? 495 LEU   A CG  1 
ATOM   1476 C CD1 . LEU   A 1 203 ? 18.932  -7.539  34.155 1.00 44.88  ? 495 LEU   A CD1 1 
ATOM   1477 C CD2 . LEU   A 1 203 ? 19.682  -9.362  32.614 1.00 31.99  ? 495 LEU   A CD2 1 
ATOM   1478 N N   . THR   A 1 204 ? 23.877  -5.922  33.275 1.00 39.21  ? 496 THR   A N   1 
ATOM   1479 C CA  . THR   A 1 204 ? 25.188  -5.717  32.681 1.00 44.23  ? 496 THR   A CA  1 
ATOM   1480 C C   . THR   A 1 204 ? 25.368  -6.633  31.474 1.00 41.42  ? 496 THR   A C   1 
ATOM   1481 O O   . THR   A 1 204 ? 24.618  -7.592  31.271 1.00 38.72  ? 496 THR   A O   1 
ATOM   1482 C CB  . THR   A 1 204 ? 26.296  -5.973  33.704 1.00 54.51  ? 496 THR   A CB  1 
ATOM   1483 O OG1 . THR   A 1 204 ? 26.508  -7.384  33.842 1.00 45.72  ? 496 THR   A OG1 1 
ATOM   1484 C CG2 . THR   A 1 204 ? 25.927  -5.379  35.057 1.00 48.23  ? 496 THR   A CG2 1 
ATOM   1485 N N   . LEU   A 1 205 ? 26.386  -6.323  30.666 1.00 42.07  ? 497 LEU   A N   1 
ATOM   1486 C CA  . LEU   A 1 205 ? 26.631  -7.095  29.452 1.00 45.41  ? 497 LEU   A CA  1 
ATOM   1487 C C   . LEU   A 1 205 ? 26.867  -8.566  29.768 1.00 47.44  ? 497 LEU   A C   1 
ATOM   1488 O O   . LEU   A 1 205 ? 26.386  -9.449  29.047 1.00 44.15  ? 497 LEU   A O   1 
ATOM   1489 C CB  . LEU   A 1 205 ? 27.820  -6.512  28.692 1.00 40.70  ? 497 LEU   A CB  1 
ATOM   1490 C CG  . LEU   A 1 205 ? 27.861  -6.792  27.191 1.00 49.31  ? 497 LEU   A CG  1 
ATOM   1491 C CD1 . LEU   A 1 205 ? 26.558  -6.370  26.529 1.00 45.45  ? 497 LEU   A CD1 1 
ATOM   1492 C CD2 . LEU   A 1 205 ? 29.041  -6.075  26.567 1.00 45.73  ? 497 LEU   A CD2 1 
ATOM   1493 N N   . GLN   A 1 206 ? 27.605  -8.850  30.843 1.00 44.95  ? 498 GLN   A N   1 
ATOM   1494 C CA  . GLN   A 1 206 ? 27.785  -10.234 31.266 1.00 40.33  ? 498 GLN   A CA  1 
ATOM   1495 C C   . GLN   A 1 206 ? 26.460  -10.852 31.690 1.00 38.66  ? 498 GLN   A C   1 
ATOM   1496 O O   . GLN   A 1 206 ? 26.172  -12.009 31.363 1.00 32.58  ? 498 GLN   A O   1 
ATOM   1497 C CB  . GLN   A 1 206 ? 28.804  -10.304 32.404 1.00 36.52  ? 498 GLN   A CB  1 
ATOM   1498 C CG  . GLN   A 1 206 ? 29.173  -11.716 32.823 1.00 42.53  ? 498 GLN   A CG  1 
ATOM   1499 C CD  . GLN   A 1 206 ? 30.092  -11.743 34.028 1.00 48.55  ? 498 GLN   A CD  1 
ATOM   1500 O OE1 . GLN   A 1 206 ? 30.282  -10.731 34.702 1.00 48.07  ? 498 GLN   A OE1 1 
ATOM   1501 N NE2 . GLN   A 1 206 ? 30.672  -12.906 34.305 1.00 39.83  ? 498 GLN   A NE2 1 
ATOM   1502 N N   . GLN   A 1 207 ? 25.633  -10.089 32.411 1.00 35.89  ? 499 GLN   A N   1 
ATOM   1503 C CA  . GLN   A 1 207 ? 24.328  -10.594 32.825 1.00 33.98  ? 499 GLN   A CA  1 
ATOM   1504 C C   . GLN   A 1 207 ? 23.388  -10.766 31.639 1.00 38.12  ? 499 GLN   A C   1 
ATOM   1505 O O   . GLN   A 1 207 ? 22.520  -11.646 31.662 1.00 33.02  ? 499 GLN   A O   1 
ATOM   1506 C CB  . GLN   A 1 207 ? 23.706  -9.656  33.860 1.00 38.22  ? 499 GLN   A CB  1 
ATOM   1507 C CG  . GLN   A 1 207 ? 24.429  -9.637  35.197 1.00 36.50  ? 499 GLN   A CG  1 
ATOM   1508 C CD  . GLN   A 1 207 ? 23.812  -8.658  36.179 1.00 61.54  ? 499 GLN   A CD  1 
ATOM   1509 O OE1 . GLN   A 1 207 ? 23.560  -7.500  35.844 1.00 48.78  ? 499 GLN   A OE1 1 
ATOM   1510 N NE2 . GLN   A 1 207 ? 23.566  -9.119  37.400 1.00 54.45  ? 499 GLN   A NE2 1 
ATOM   1511 N N   . GLN   A 1 208 ? 23.540  -9.939  30.601 1.00 34.41  ? 500 GLN   A N   1 
ATOM   1512 C CA  . GLN   A 1 208 ? 22.696  -10.071 29.417 1.00 29.81  ? 500 GLN   A CA  1 
ATOM   1513 C C   . GLN   A 1 208 ? 22.978  -11.377 28.687 1.00 29.04  ? 500 GLN   A C   1 
ATOM   1514 O O   . GLN   A 1 208 ? 22.053  -12.123 28.347 1.00 33.13  ? 500 GLN   A O   1 
ATOM   1515 C CB  . GLN   A 1 208 ? 22.911  -8.879  28.484 1.00 32.15  ? 500 GLN   A CB  1 
ATOM   1516 C CG  . GLN   A 1 208 ? 22.418  -7.554  29.034 1.00 32.36  ? 500 GLN   A CG  1 
ATOM   1517 C CD  . GLN   A 1 208 ? 22.851  -6.383  28.181 1.00 39.97  ? 500 GLN   A CD  1 
ATOM   1518 O OE1 . GLN   A 1 208 ? 22.971  -6.500  26.962 1.00 39.53  ? 500 GLN   A OE1 1 
ATOM   1519 N NE2 . GLN   A 1 208 ? 23.098  -5.245  28.819 1.00 41.20  ? 500 GLN   A NE2 1 
ATOM   1520 N N   . HIS   A 1 209 ? 24.257  -11.668 28.431 1.00 31.50  ? 501 HIS   A N   1 
ATOM   1521 C CA  . HIS   A 1 209 ? 24.613  -12.919 27.770 1.00 33.36  ? 501 HIS   A CA  1 
ATOM   1522 C C   . HIS   A 1 209 ? 24.241  -14.118 28.630 1.00 32.21  ? 501 HIS   A C   1 
ATOM   1523 O O   . HIS   A 1 209 ? 23.786  -15.145 28.113 1.00 29.76  ? 501 HIS   A O   1 
ATOM   1524 C CB  . HIS   A 1 209 ? 26.107  -12.941 27.453 1.00 39.78  ? 501 HIS   A CB  1 
ATOM   1525 C CG  . HIS   A 1 209 ? 26.577  -11.762 26.659 1.00 50.12  ? 501 HIS   A CG  1 
ATOM   1526 N ND1 . HIS   A 1 209 ? 27.883  -11.324 26.682 1.00 40.79  ? 501 HIS   A ND1 1 
ATOM   1527 C CD2 . HIS   A 1 209 ? 25.917  -10.933 25.816 1.00 37.60  ? 501 HIS   A CD2 1 
ATOM   1528 C CE1 . HIS   A 1 209 ? 28.007  -10.274 25.890 1.00 35.94  ? 501 HIS   A CE1 1 
ATOM   1529 N NE2 . HIS   A 1 209 ? 26.829  -10.017 25.352 1.00 44.31  ? 501 HIS   A NE2 1 
ATOM   1530 N N   . GLN   A 1 210 ? 24.431  -14.007 29.946 1.00 29.55  ? 502 GLN   A N   1 
ATOM   1531 C CA  . GLN   A 1 210 ? 24.115  -15.123 30.829 1.00 29.39  ? 502 GLN   A CA  1 
ATOM   1532 C C   . GLN   A 1 210 ? 22.620  -15.412 30.841 1.00 31.54  ? 502 GLN   A C   1 
ATOM   1533 O O   . GLN   A 1 210 ? 22.210  -16.574 30.748 1.00 31.60  ? 502 GLN   A O   1 
ATOM   1534 C CB  . GLN   A 1 210 ? 24.631  -14.839 32.239 1.00 28.84  ? 502 GLN   A CB  1 
ATOM   1535 C CG  . GLN   A 1 210 ? 26.137  -15.016 32.379 1.00 29.95  ? 502 GLN   A CG  1 
ATOM   1536 C CD  . GLN   A 1 210 ? 26.643  -14.678 33.766 1.00 32.10  ? 502 GLN   A CD  1 
ATOM   1537 O OE1 . GLN   A 1 210 ? 25.899  -14.170 34.603 1.00 33.88  ? 502 GLN   A OE1 1 
ATOM   1538 N NE2 . GLN   A 1 210 ? 27.917  -14.959 34.015 1.00 34.13  ? 502 GLN   A NE2 1 
ATOM   1539 N N   . ARG   A 1 211 ? 21.788  -14.370 30.935 1.00 26.31  ? 503 ARG   A N   1 
ATOM   1540 C CA  . ARG   A 1 211 ? 20.343  -14.586 30.950 1.00 26.97  ? 503 ARG   A CA  1 
ATOM   1541 C C   . ARG   A 1 211 ? 19.838  -15.045 29.587 1.00 25.29  ? 503 ARG   A C   1 
ATOM   1542 O O   . ARG   A 1 211 ? 18.916  -15.866 29.506 1.00 28.13  ? 503 ARG   A O   1 
ATOM   1543 C CB  . ARG   A 1 211 ? 19.619  -13.315 31.391 1.00 25.84  ? 503 ARG   A CB  1 
ATOM   1544 C CG  . ARG   A 1 211 ? 18.115  -13.492 31.547 1.00 24.19  ? 503 ARG   A CG  1 
ATOM   1545 C CD  . ARG   A 1 211 ? 17.454  -12.232 32.077 1.00 25.95  ? 503 ARG   A CD  1 
ATOM   1546 N NE  . ARG   A 1 211 ? 16.007  -12.371 32.183 1.00 25.92  ? 503 ARG   A NE  1 
ATOM   1547 C CZ  . ARG   A 1 211 ? 15.372  -12.772 33.276 1.00 26.78  ? 503 ARG   A CZ  1 
ATOM   1548 N NH1 . ARG   A 1 211 ? 16.030  -13.103 34.375 1.00 27.83  ? 503 ARG   A NH1 1 
ATOM   1549 N NH2 . ARG   A 1 211 ? 14.044  -12.843 33.266 1.00 27.02  ? 503 ARG   A NH2 1 
ATOM   1550 N N   . LEU   A 1 212 ? 20.420  -14.520 28.506 1.00 26.06  ? 504 LEU   A N   1 
ATOM   1551 C CA  . LEU   A 1 212 ? 20.084  -15.015 27.175 1.00 24.75  ? 504 LEU   A CA  1 
ATOM   1552 C C   . LEU   A 1 212 ? 20.379  -16.504 27.060 1.00 28.50  ? 504 LEU   A C   1 
ATOM   1553 O O   . LEU   A 1 212 ? 19.575  -17.265 26.509 1.00 27.14  ? 504 LEU   A O   1 
ATOM   1554 C CB  . LEU   A 1 212 ? 20.855  -14.235 26.110 1.00 23.39  ? 504 LEU   A CB  1 
ATOM   1555 C CG  . LEU   A 1 212 ? 20.634  -14.679 24.662 1.00 24.90  ? 504 LEU   A CG  1 
ATOM   1556 C CD1 . LEU   A 1 212 ? 19.179  -14.506 24.256 1.00 22.09  ? 504 LEU   A CD1 1 
ATOM   1557 C CD2 . LEU   A 1 212 ? 21.556  -13.924 23.716 1.00 24.33  ? 504 LEU   A CD2 1 
ATOM   1558 N N   . ALA   A 1 213 ? 21.526  -16.938 27.586 1.00 24.72  ? 505 ALA   A N   1 
ATOM   1559 C CA  . ALA   A 1 213 ? 21.866  -18.355 27.556 1.00 23.08  ? 505 ALA   A CA  1 
ATOM   1560 C C   . ALA   A 1 213 ? 20.902  -19.173 28.404 1.00 27.33  ? 505 ALA   A C   1 
ATOM   1561 O O   . ALA   A 1 213 ? 20.443  -20.240 27.980 1.00 24.19  ? 505 ALA   A O   1 
ATOM   1562 C CB  . ALA   A 1 213 ? 23.303  -18.557 28.032 1.00 28.30  ? 505 ALA   A CB  1 
ATOM   1563 N N   . GLN   A 1 214 ? 20.583  -18.687 29.606 1.00 23.86  ? 506 GLN   A N   1 
ATOM   1564 C CA  . GLN   A 1 214 ? 19.683  -19.421 30.489 1.00 27.92  ? 506 GLN   A CA  1 
ATOM   1565 C C   . GLN   A 1 214 ? 18.303  -19.587 29.863 1.00 27.78  ? 506 GLN   A C   1 
ATOM   1566 O O   . GLN   A 1 214 ? 17.691  -20.656 29.967 1.00 28.53  ? 506 GLN   A O   1 
ATOM   1567 C CB  . GLN   A 1 214 ? 19.578  -18.709 31.838 1.00 31.22  ? 506 GLN   A CB  1 
ATOM   1568 C CG  . GLN   A 1 214 ? 20.881  -18.635 32.619 1.00 35.54  ? 506 GLN   A CG  1 
ATOM   1569 C CD  . GLN   A 1 214 ? 20.884  -17.514 33.646 1.00 43.59  ? 506 GLN   A CD  1 
ATOM   1570 O OE1 . GLN   A 1 214 ? 19.887  -16.811 33.819 1.00 33.22  ? 506 GLN   A OE1 1 
ATOM   1571 N NE2 . GLN   A 1 214 ? 22.012  -17.336 34.325 1.00 28.08  ? 506 GLN   A NE2 1 
ATOM   1572 N N   . LEU   A 1 215 ? 17.799  -18.542 29.201 1.00 26.06  ? 507 LEU   A N   1 
ATOM   1573 C CA  . LEU   A 1 215 ? 16.469  -18.623 28.605 1.00 31.48  ? 507 LEU   A CA  1 
ATOM   1574 C C   . LEU   A 1 215 ? 16.445  -19.581 27.420 1.00 25.20  ? 507 LEU   A C   1 
ATOM   1575 O O   . LEU   A 1 215 ? 15.476  -20.327 27.239 1.00 22.80  ? 507 LEU   A O   1 
ATOM   1576 C CB  . LEU   A 1 215 ? 15.999  -17.232 28.178 1.00 23.41  ? 507 LEU   A CB  1 
ATOM   1577 C CG  . LEU   A 1 215 ? 15.632  -16.262 29.301 1.00 25.68  ? 507 LEU   A CG  1 
ATOM   1578 C CD1 . LEU   A 1 215 ? 15.189  -14.926 28.729 1.00 21.54  ? 507 LEU   A CD1 1 
ATOM   1579 C CD2 . LEU   A 1 215 ? 14.546  -16.855 30.185 1.00 31.63  ? 507 LEU   A CD2 1 
ATOM   1580 N N   . LEU   A 1 216 ? 17.501  -19.577 26.604 1.00 23.41  ? 508 LEU   A N   1 
ATOM   1581 C CA  . LEU   A 1 216 ? 17.524  -20.441 25.429 1.00 23.41  ? 508 LEU   A CA  1 
ATOM   1582 C C   . LEU   A 1 216 ? 17.770  -21.896 25.802 1.00 27.66  ? 508 LEU   A C   1 
ATOM   1583 O O   . LEU   A 1 216 ? 17.328  -22.800 25.084 1.00 21.01  ? 508 LEU   A O   1 
ATOM   1584 C CB  . LEU   A 1 216 ? 18.585  -19.955 24.444 1.00 21.21  ? 508 LEU   A CB  1 
ATOM   1585 C CG  . LEU   A 1 216 ? 18.299  -18.584 23.833 1.00 29.72  ? 508 LEU   A CG  1 
ATOM   1586 C CD1 . LEU   A 1 216 ? 19.444  -18.156 22.942 1.00 21.51  ? 508 LEU   A CD1 1 
ATOM   1587 C CD2 . LEU   A 1 216 ? 16.992  -18.605 23.056 1.00 20.41  ? 508 LEU   A CD2 1 
ATOM   1588 N N   . LEU   A 1 217 ? 18.471  -22.143 26.911 1.00 25.90  ? 509 LEU   A N   1 
ATOM   1589 C CA  . LEU   A 1 217 ? 18.666  -23.516 27.362 1.00 22.94  ? 509 LEU   A CA  1 
ATOM   1590 C C   . LEU   A 1 217 ? 17.373  -24.114 27.899 1.00 26.03  ? 509 LEU   A C   1 
ATOM   1591 O O   . LEU   A 1 217 ? 17.209  -25.340 27.894 1.00 25.58  ? 509 LEU   A O   1 
ATOM   1592 C CB  . LEU   A 1 217 ? 19.766  -23.570 28.422 1.00 20.81  ? 509 LEU   A CB  1 
ATOM   1593 C CG  . LEU   A 1 217 ? 21.184  -23.406 27.871 1.00 30.08  ? 509 LEU   A CG  1 
ATOM   1594 C CD1 . LEU   A 1 217 ? 22.215  -23.395 28.992 1.00 30.64  ? 509 LEU   A CD1 1 
ATOM   1595 C CD2 . LEU   A 1 217 ? 21.485  -24.502 26.859 1.00 26.30  ? 509 LEU   A CD2 1 
ATOM   1596 N N   . ILE   A 1 218 ? 16.449  -23.271 28.366 1.00 25.17  ? 510 ILE   A N   1 
ATOM   1597 C CA  . ILE   A 1 218 ? 15.130  -23.751 28.765 1.00 32.03  ? 510 ILE   A CA  1 
ATOM   1598 C C   . ILE   A 1 218 ? 14.376  -24.288 27.557 1.00 27.66  ? 510 ILE   A C   1 
ATOM   1599 O O   . ILE   A 1 218 ? 13.553  -25.204 27.681 1.00 28.82  ? 510 ILE   A O   1 
ATOM   1600 C CB  . ILE   A 1 218 ? 14.352  -22.623 29.473 1.00 26.65  ? 510 ILE   A CB  1 
ATOM   1601 C CG1 . ILE   A 1 218 ? 15.042  -22.245 30.783 1.00 26.48  ? 510 ILE   A CG1 1 
ATOM   1602 C CG2 . ILE   A 1 218 ? 12.913  -23.034 29.748 1.00 29.28  ? 510 ILE   A CG2 1 
ATOM   1603 C CD1 . ILE   A 1 218 ? 14.535  -20.956 31.382 1.00 34.30  ? 510 ILE   A CD1 1 
ATOM   1604 N N   . LEU   A 1 219 ? 14.657  -23.746 26.369 1.00 22.92  ? 511 LEU   A N   1 
ATOM   1605 C CA  . LEU   A 1 219 ? 13.998  -24.226 25.159 1.00 24.00  ? 511 LEU   A CA  1 
ATOM   1606 C C   . LEU   A 1 219 ? 14.352  -25.677 24.863 1.00 24.90  ? 511 LEU   A C   1 
ATOM   1607 O O   . LEU   A 1 219 ? 13.555  -26.394 24.247 1.00 25.65  ? 511 LEU   A O   1 
ATOM   1608 C CB  . LEU   A 1 219 ? 14.368  -23.337 23.973 1.00 24.89  ? 511 LEU   A CB  1 
ATOM   1609 C CG  . LEU   A 1 219 ? 13.945  -21.870 24.060 1.00 25.91  ? 511 LEU   A CG  1 
ATOM   1610 C CD1 . LEU   A 1 219 ? 14.039  -21.220 22.691 1.00 26.40  ? 511 LEU   A CD1 1 
ATOM   1611 C CD2 . LEU   A 1 219 ? 12.541  -21.733 24.631 1.00 18.58  ? 511 LEU   A CD2 1 
ATOM   1612 N N   . SER   A 1 220 ? 15.537  -26.127 25.282 1.00 21.32  ? 512 SER   A N   1 
ATOM   1613 C CA  . SER   A 1 220 ? 15.882  -27.536 25.124 1.00 21.65  ? 512 SER   A CA  1 
ATOM   1614 C C   . SER   A 1 220 ? 14.976  -28.418 25.973 1.00 23.92  ? 512 SER   A C   1 
ATOM   1615 O O   . SER   A 1 220 ? 14.556  -29.495 25.535 1.00 22.23  ? 512 SER   A O   1 
ATOM   1616 C CB  . SER   A 1 220 ? 17.351  -27.765 25.483 1.00 25.12  ? 512 SER   A CB  1 
ATOM   1617 O OG  . SER   A 1 220 ? 18.205  -27.347 24.432 1.00 36.78  ? 512 SER   A OG  1 
ATOM   1618 N N   . HIS   A 1 221 ? 14.656  -27.972 27.190 1.00 25.26  ? 513 HIS   A N   1 
ATOM   1619 C CA  . HIS   A 1 221 ? 13.744  -28.730 28.040 1.00 24.74  ? 513 HIS   A CA  1 
ATOM   1620 C C   . HIS   A 1 221 ? 12.327  -28.714 27.487 1.00 23.58  ? 513 HIS   A C   1 
ATOM   1621 O O   . HIS   A 1 221 ? 11.608  -29.717 27.578 1.00 25.51  ? 513 HIS   A O   1 
ATOM   1622 C CB  . HIS   A 1 221 ? 13.765  -28.170 29.460 1.00 28.13  ? 513 HIS   A CB  1 
ATOM   1623 C CG  . HIS   A 1 221 ? 12.837  -28.874 30.400 1.00 49.46  ? 513 HIS   A CG  1 
ATOM   1624 N ND1 . HIS   A 1 221 ? 13.083  -30.141 30.885 1.00 48.42  ? 513 HIS   A ND1 1 
ATOM   1625 C CD2 . HIS   A 1 221 ? 11.666  -28.481 30.954 1.00 35.93  ? 513 HIS   A CD2 1 
ATOM   1626 C CE1 . HIS   A 1 221 ? 12.101  -30.500 31.692 1.00 42.58  ? 513 HIS   A CE1 1 
ATOM   1627 N NE2 . HIS   A 1 221 ? 11.228  -29.510 31.751 1.00 48.35  ? 513 HIS   A NE2 1 
ATOM   1628 N N   . ILE   A 1 222 ? 11.903  -27.582 26.922 1.00 25.30  ? 514 ILE   A N   1 
ATOM   1629 C CA  . ILE   A 1 222 ? 10.567  -27.497 26.340 1.00 23.26  ? 514 ILE   A CA  1 
ATOM   1630 C C   . ILE   A 1 222 ? 10.448  -28.443 25.152 1.00 25.84  ? 514 ILE   A C   1 
ATOM   1631 O O   . ILE   A 1 222 ? 9.416   -29.100 24.962 1.00 25.02  ? 514 ILE   A O   1 
ATOM   1632 C CB  . ILE   A 1 222 ? 10.249  -26.041 25.953 1.00 25.94  ? 514 ILE   A CB  1 
ATOM   1633 C CG1 . ILE   A 1 222 ? 10.066  -25.192 27.213 1.00 21.94  ? 514 ILE   A CG1 1 
ATOM   1634 C CG2 . ILE   A 1 222 ? 9.002   -25.971 25.088 1.00 22.85  ? 514 ILE   A CG2 1 
ATOM   1635 C CD1 . ILE   A 1 222 ? 9.927   -23.713 26.941 1.00 20.87  ? 514 ILE   A CD1 1 
ATOM   1636 N N   . ARG   A 1 223 ? 11.505  -28.536 24.341 1.00 20.89  ? 515 ARG   A N   1 
ATOM   1637 C CA  . ARG   A 1 223 ? 11.527  -29.531 23.274 1.00 23.01  ? 515 ARG   A CA  1 
ATOM   1638 C C   . ARG   A 1 223 ? 11.454  -30.941 23.844 1.00 22.29  ? 515 ARG   A C   1 
ATOM   1639 O O   . ARG   A 1 223 ? 10.733  -31.797 23.318 1.00 25.71  ? 515 ARG   A O   1 
ATOM   1640 C CB  . ARG   A 1 223 ? 12.789  -29.374 22.427 1.00 22.78  ? 515 ARG   A CB  1 
ATOM   1641 C CG  . ARG   A 1 223 ? 12.951  -30.459 21.373 1.00 28.52  ? 515 ARG   A CG  1 
ATOM   1642 C CD  . ARG   A 1 223 ? 12.139  -30.128 20.134 1.00 34.99  ? 515 ARG   A CD  1 
ATOM   1643 N NE  . ARG   A 1 223 ? 12.635  -28.908 19.513 1.00 40.62  ? 515 ARG   A NE  1 
ATOM   1644 C CZ  . ARG   A 1 223 ? 13.252  -28.862 18.341 1.00 41.23  ? 515 ARG   A CZ  1 
ATOM   1645 N NH1 . ARG   A 1 223 ? 13.388  -29.940 17.587 1.00 35.31  ? 515 ARG   A NH1 1 
ATOM   1646 N NH2 . ARG   A 1 223 ? 13.754  -27.706 17.918 1.00 40.61  ? 515 ARG   A NH2 1 
ATOM   1647 N N   . HIS   A 1 224 ? 12.202  -31.200 24.920 1.00 24.59  ? 516 HIS   A N   1 
ATOM   1648 C CA  . HIS   A 1 224 ? 12.154  -32.509 25.562 1.00 22.89  ? 516 HIS   A CA  1 
ATOM   1649 C C   . HIS   A 1 224 ? 10.754  -32.816 26.075 1.00 22.60  ? 516 HIS   A C   1 
ATOM   1650 O O   . HIS   A 1 224 ? 10.260  -33.939 25.920 1.00 24.12  ? 516 HIS   A O   1 
ATOM   1651 C CB  . HIS   A 1 224 ? 13.176  -32.569 26.698 1.00 23.49  ? 516 HIS   A CB  1 
ATOM   1652 C CG  . HIS   A 1 224 ? 13.183  -33.869 27.441 1.00 26.60  ? 516 HIS   A CG  1 
ATOM   1653 N ND1 . HIS   A 1 224 ? 14.026  -34.909 27.114 1.00 32.26  ? 516 HIS   A ND1 1 
ATOM   1654 C CD2 . HIS   A 1 224 ? 12.454  -34.296 28.499 1.00 34.14  ? 516 HIS   A CD2 1 
ATOM   1655 C CE1 . HIS   A 1 224 ? 13.814  -35.921 27.936 1.00 34.56  ? 516 HIS   A CE1 1 
ATOM   1656 N NE2 . HIS   A 1 224 ? 12.864  -35.575 28.785 1.00 32.85  ? 516 HIS   A NE2 1 
ATOM   1657 N N   . MET   A 1 225 ? 10.093  -31.826 26.681 1.00 21.15  ? 517 MET   A N   1 
ATOM   1658 C CA  . MET   A 1 225 ? 8.718   -32.022 27.127 1.00 23.34  ? 517 MET   A CA  1 
ATOM   1659 C C   . MET   A 1 225 ? 7.790   -32.272 25.946 1.00 22.13  ? 517 MET   A C   1 
ATOM   1660 O O   . MET   A 1 225 ? 6.856   -33.078 26.038 1.00 25.42  ? 517 MET   A O   1 
ATOM   1661 C CB  . MET   A 1 225 ? 8.242   -30.806 27.922 1.00 23.11  ? 517 MET   A CB  1 
ATOM   1662 C CG  . MET   A 1 225 ? 8.863   -30.668 29.297 1.00 25.23  ? 517 MET   A CG  1 
ATOM   1663 S SD  . MET   A 1 225 ? 8.094   -29.351 30.260 1.00 29.23  ? 517 MET   A SD  1 
ATOM   1664 C CE  . MET   A 1 225 ? 8.302   -27.948 29.170 1.00 20.60  ? 517 MET   A CE  1 
ATOM   1665 N N   . SER   A 1 226 ? 8.035   -31.587 24.826 1.00 27.68  ? 518 SER   A N   1 
ATOM   1666 C CA  . SER   A 1 226 ? 7.196   -31.753 23.643 1.00 25.96  ? 518 SER   A CA  1 
ATOM   1667 C C   . SER   A 1 226 ? 7.285   -33.172 23.098 1.00 24.54  ? 518 SER   A C   1 
ATOM   1668 O O   . SER   A 1 226 ? 6.263   -33.789 22.777 1.00 29.14  ? 518 SER   A O   1 
ATOM   1669 C CB  . SER   A 1 226 ? 7.603   -30.743 22.571 1.00 23.83  ? 518 SER   A CB  1 
ATOM   1670 O OG  . SER   A 1 226 ? 6.760   -30.832 21.436 1.00 37.83  ? 518 SER   A OG  1 
ATOM   1671 N N   . ASN   A 1 227 ? 8.505   -33.702 22.975 1.00 24.57  ? 519 ASN   A N   1 
ATOM   1672 C CA  . ASN   A 1 227 ? 8.670   -35.068 22.489 1.00 27.11  ? 519 ASN   A CA  1 
ATOM   1673 C C   . ASN   A 1 227 ? 7.998   -36.067 23.421 1.00 31.41  ? 519 ASN   A C   1 
ATOM   1674 O O   . ASN   A 1 227 ? 7.296   -36.976 22.964 1.00 34.25  ? 519 ASN   A O   1 
ATOM   1675 C CB  . ASN   A 1 227 ? 10.154  -35.400 22.331 1.00 28.37  ? 519 ASN   A CB  1 
ATOM   1676 C CG  . ASN   A 1 227 ? 10.838  -34.534 21.296 1.00 39.39  ? 519 ASN   A CG  1 
ATOM   1677 O OD1 . ASN   A 1 227 ? 11.940  -34.031 21.519 1.00 35.64  ? 519 ASN   A OD1 1 
ATOM   1678 N ND2 . ASN   A 1 227 ? 10.187  -34.353 20.154 1.00 31.48  ? 519 ASN   A ND2 1 
ATOM   1679 N N   . LYS   A 1 228 ? 8.201   -35.915 24.732 1.00 28.00  ? 520 LYS   A N   1 
ATOM   1680 C CA  . LYS   A 1 228 ? 7.515   -36.777 25.689 1.00 30.29  ? 520 LYS   A CA  1 
ATOM   1681 C C   . LYS   A 1 228 ? 6.008   -36.563 25.640 1.00 30.21  ? 520 LYS   A C   1 
ATOM   1682 O O   . LYS   A 1 228 ? 5.234   -37.513 25.807 1.00 34.56  ? 520 LYS   A O   1 
ATOM   1683 C CB  . LYS   A 1 228 ? 8.048   -36.525 27.098 1.00 38.16  ? 520 LYS   A CB  1 
ATOM   1684 C CG  . LYS   A 1 228 ? 9.501   -36.910 27.294 1.00 45.13  ? 520 LYS   A CG  1 
ATOM   1685 C CD  . LYS   A 1 228 ? 9.663   -38.418 27.357 1.00 45.37  ? 520 LYS   A CD  1 
ATOM   1686 C CE  . LYS   A 1 228 ? 11.057  -38.837 26.925 1.00 49.01  ? 520 LYS   A CE  1 
ATOM   1687 N NZ  . LYS   A 1 228 ? 11.088  -40.250 26.450 1.00 60.34  ? 520 LYS   A NZ  1 
ATOM   1688 N N   . GLY   A 1 229 ? 5.572   -35.322 25.411 1.00 31.85  ? 521 GLY   A N   1 
ATOM   1689 C CA  . GLY   A 1 229 ? 4.151   -35.059 25.280 1.00 28.04  ? 521 GLY   A CA  1 
ATOM   1690 C C   . GLY   A 1 229 ? 3.553   -35.648 24.019 1.00 39.42  ? 521 GLY   A C   1 
ATOM   1691 O O   . GLY   A 1 229 ? 2.385   -36.048 24.012 1.00 37.49  ? 521 GLY   A O   1 
ATOM   1692 N N   A MET   A 1 230 ? 4.336   -35.714 22.940 0.33 29.77  ? 522 MET   A N   1 
ATOM   1693 N N   B MET   A 1 230 ? 4.335   -35.705 22.939 0.67 29.81  ? 522 MET   A N   1 
ATOM   1694 C CA  A MET   A 1 230 ? 3.832   -36.301 21.702 0.33 30.61  ? 522 MET   A CA  1 
ATOM   1695 C CA  B MET   A 1 230 ? 3.842   -36.300 21.701 0.67 30.54  ? 522 MET   A CA  1 
ATOM   1696 C C   A MET   A 1 230 ? 3.663   -37.810 21.835 0.33 35.27  ? 522 MET   A C   1 
ATOM   1697 C C   B MET   A 1 230 ? 3.654   -37.804 21.852 0.67 35.37  ? 522 MET   A C   1 
ATOM   1698 O O   A MET   A 1 230 ? 2.702   -38.380 21.305 0.33 34.76  ? 522 MET   A O   1 
ATOM   1699 O O   B MET   A 1 230 ? 2.673   -38.366 21.351 0.67 34.73  ? 522 MET   A O   1 
ATOM   1700 C CB  A MET   A 1 230 ? 4.763   -35.962 20.537 0.33 31.54  ? 522 MET   A CB  1 
ATOM   1701 C CB  B MET   A 1 230 ? 4.800   -35.987 20.552 0.67 31.49  ? 522 MET   A CB  1 
ATOM   1702 C CG  A MET   A 1 230 ? 4.676   -34.514 20.080 0.33 31.32  ? 522 MET   A CG  1 
ATOM   1703 C CG  B MET   A 1 230 ? 4.127   -35.862 19.195 0.67 32.21  ? 522 MET   A CG  1 
ATOM   1704 S SD  A MET   A 1 230 ? 4.495   -34.326 18.296 0.33 37.27  ? 522 MET   A SD  1 
ATOM   1705 S SD  B MET   A 1 230 ? 2.847   -34.593 19.156 0.67 31.81  ? 522 MET   A SD  1 
ATOM   1706 C CE  A MET   A 1 230 ? 4.972   -32.612 18.086 0.33 29.67  ? 522 MET   A CE  1 
ATOM   1707 C CE  B MET   A 1 230 ? 3.816   -33.144 18.744 0.67 29.52  ? 522 MET   A CE  1 
ATOM   1708 N N   . GLU   A 1 231 ? 4.585   -38.474 22.538 1.00 34.84  ? 523 GLU   A N   1 
ATOM   1709 C CA  . GLU   A 1 231 ? 4.431   -39.905 22.784 1.00 35.53  ? 523 GLU   A CA  1 
ATOM   1710 C C   . GLU   A 1 231 ? 3.232   -40.176 23.684 1.00 36.32  ? 523 GLU   A C   1 
ATOM   1711 O O   . GLU   A 1 231 ? 2.514   -41.165 23.494 1.00 38.00  ? 523 GLU   A O   1 
ATOM   1712 C CB  . GLU   A 1 231 ? 5.701   -40.481 23.413 1.00 36.53  ? 523 GLU   A CB  1 
ATOM   1713 C CG  . GLU   A 1 231 ? 6.999   -40.067 22.739 1.00 55.74  ? 523 GLU   A CG  1 
ATOM   1714 C CD  . GLU   A 1 231 ? 8.158   -39.978 23.719 1.00 68.48  ? 523 GLU   A CD  1 
ATOM   1715 O OE1 . GLU   A 1 231 ? 8.019   -40.482 24.854 1.00 66.03  ? 523 GLU   A OE1 1 
ATOM   1716 O OE2 . GLU   A 1 231 ? 9.207   -39.403 23.355 1.00 64.58  ? 523 GLU   A OE2 1 
ATOM   1717 N N   . HIS   A 1 232 ? 3.000   -39.305 24.668 1.00 33.40  ? 524 HIS   A N   1 
ATOM   1718 C CA  . HIS   A 1 232 ? 1.860   -39.477 25.562 1.00 43.84  ? 524 HIS   A CA  1 
ATOM   1719 C C   . HIS   A 1 232 ? 0.544   -39.225 24.836 1.00 45.89  ? 524 HIS   A C   1 
ATOM   1720 O O   . HIS   A 1 232 ? -0.426  -39.970 25.020 1.00 43.15  ? 524 HIS   A O   1 
ATOM   1721 C CB  . HIS   A 1 232 ? 1.997   -38.546 26.767 1.00 32.30  ? 524 HIS   A CB  1 
ATOM   1722 C CG  . HIS   A 1 232 ? 0.866   -38.647 27.741 1.00 43.45  ? 524 HIS   A CG  1 
ATOM   1723 N ND1 . HIS   A 1 232 ? 0.020   -37.592 28.010 1.00 41.95  ? 524 HIS   A ND1 1 
ATOM   1724 C CD2 . HIS   A 1 232 ? 0.440   -39.676 28.510 1.00 43.85  ? 524 HIS   A CD2 1 
ATOM   1725 C CE1 . HIS   A 1 232 ? -0.878  -37.968 28.903 1.00 49.88  ? 524 HIS   A CE1 1 
ATOM   1726 N NE2 . HIS   A 1 232 ? -0.645  -39.228 29.223 1.00 42.84  ? 524 HIS   A NE2 1 
ATOM   1727 N N   . LEU   A 1 233 ? 0.492   -38.181 24.005 1.00 40.10  ? 525 LEU   A N   1 
ATOM   1728 C CA  . LEU   A 1 233 ? -0.733  -37.878 23.271 1.00 37.96  ? 525 LEU   A CA  1 
ATOM   1729 C C   . LEU   A 1 233 ? -1.022  -38.937 22.215 1.00 43.61  ? 525 LEU   A C   1 
ATOM   1730 O O   . LEU   A 1 233 ? -2.186  -39.279 21.974 1.00 45.84  ? 525 LEU   A O   1 
ATOM   1731 C CB  . LEU   A 1 233 ? -0.631  -36.495 22.632 1.00 39.55  ? 525 LEU   A CB  1 
ATOM   1732 C CG  . LEU   A 1 233 ? -0.775  -35.308 23.584 1.00 46.00  ? 525 LEU   A CG  1 
ATOM   1733 C CD1 . LEU   A 1 233 ? -0.732  -34.000 22.813 1.00 32.53  ? 525 LEU   A CD1 1 
ATOM   1734 C CD2 . LEU   A 1 233 ? -2.059  -35.420 24.393 1.00 41.25  ? 525 LEU   A CD2 1 
ATOM   1735 N N   . TYR   A 1 234 ? 0.022   -39.466 21.572 1.00 36.90  ? 526 TYR   A N   1 
ATOM   1736 C CA  . TYR   A 1 234 ? -0.177  -40.534 20.598 1.00 57.45  ? 526 TYR   A CA  1 
ATOM   1737 C C   . TYR   A 1 234 ? -0.641  -41.821 21.266 1.00 51.53  ? 526 TYR   A C   1 
ATOM   1738 O O   . TYR   A 1 234 ? -1.317  -42.638 20.631 1.00 76.79  ? 526 TYR   A O   1 
ATOM   1739 C CB  . TYR   A 1 234 ? 1.110   -40.781 19.812 1.00 48.40  ? 526 TYR   A CB  1 
ATOM   1740 C CG  . TYR   A 1 234 ? 0.909   -41.571 18.538 1.00 67.01  ? 526 TYR   A CG  1 
ATOM   1741 C CD1 . TYR   A 1 234 ? 0.518   -40.944 17.363 1.00 74.31  ? 526 TYR   A CD1 1 
ATOM   1742 C CD2 . TYR   A 1 234 ? 1.107   -42.946 18.513 1.00 65.34  ? 526 TYR   A CD2 1 
ATOM   1743 C CE1 . TYR   A 1 234 ? 0.332   -41.664 16.196 1.00 57.96  ? 526 TYR   A CE1 1 
ATOM   1744 C CE2 . TYR   A 1 234 ? 0.923   -43.674 17.352 1.00 71.38  ? 526 TYR   A CE2 1 
ATOM   1745 C CZ  . TYR   A 1 234 ? 0.536   -43.027 16.197 1.00 74.57  ? 526 TYR   A CZ  1 
ATOM   1746 O OH  . TYR   A 1 234 ? 0.352   -43.749 15.040 1.00 82.52  ? 526 TYR   A OH  1 
ATOM   1747 N N   . SER   A 1 235 ? -0.296  -42.017 22.540 1.00 71.76  ? 527 SER   A N   1 
ATOM   1748 C CA  . SER   A 1 235 ? -0.719  -43.206 23.270 1.00 73.27  ? 527 SER   A CA  1 
ATOM   1749 C C   . SER   A 1 235 ? -2.215  -43.222 23.557 1.00 84.63  ? 527 SER   A C   1 
ATOM   1750 O O   . SER   A 1 235 ? -2.717  -44.230 24.067 1.00 80.25  ? 527 SER   A O   1 
ATOM   1751 C CB  . SER   A 1 235 ? 0.064   -43.320 24.580 1.00 70.06  ? 527 SER   A CB  1 
ATOM   1752 O OG  . SER   A 1 235 ? -0.707  -42.870 25.680 1.00 73.48  ? 527 SER   A OG  1 
ATOM   1753 N N   . MET   A 1 236 ? -2.931  -42.146 23.248 1.00 84.85  ? 528 MET   A N   1 
ATOM   1754 C CA  . MET   A 1 236 ? -4.376  -42.104 23.433 1.00 84.86  ? 528 MET   A CA  1 
ATOM   1755 C C   . MET   A 1 236 ? -5.096  -42.289 22.100 1.00 90.66  ? 528 MET   A C   1 
ATOM   1756 O O   . MET   A 1 236 ? -4.511  -42.766 21.128 1.00 91.52  ? 528 MET   A O   1 
ATOM   1757 C CB  . MET   A 1 236 ? -4.801  -40.786 24.084 1.00 83.85  ? 528 MET   A CB  1 
ATOM   1758 C CG  . MET   A 1 236 ? -3.737  -40.155 24.966 1.00 81.21  ? 528 MET   A CG  1 
ATOM   1759 S SD  . MET   A 1 236 ? -3.783  -40.777 26.658 1.00 111.30 ? 528 MET   A SD  1 
ATOM   1760 C CE  . MET   A 1 236 ? -4.520  -39.384 27.512 1.00 85.43  ? 528 MET   A CE  1 
ATOM   1761 N N   . LEU   A 1 244 ? -2.815  -33.251 11.404 1.00 71.12  ? 536 LEU   A N   1 
ATOM   1762 C CA  . LEU   A 1 244 ? -2.677  -31.841 11.749 1.00 61.13  ? 536 LEU   A CA  1 
ATOM   1763 C C   . LEU   A 1 244 ? -2.180  -31.030 10.560 1.00 54.57  ? 536 LEU   A C   1 
ATOM   1764 O O   . LEU   A 1 244 ? -2.474  -29.841 10.442 1.00 57.32  ? 536 LEU   A O   1 
ATOM   1765 C CB  . LEU   A 1 244 ? -1.723  -31.667 12.933 1.00 56.12  ? 536 LEU   A CB  1 
ATOM   1766 C CG  . LEU   A 1 244 ? -1.908  -30.389 13.753 1.00 56.84  ? 536 LEU   A CG  1 
ATOM   1767 C CD1 . LEU   A 1 244 ? -3.365  -29.963 13.731 1.00 74.42  ? 536 LEU   A CD1 1 
ATOM   1768 C CD2 . LEU   A 1 244 ? -1.422  -30.584 15.180 1.00 56.52  ? 536 LEU   A CD2 1 
ATOM   1769 N N   . SER   A 1 245 ? -1.422  -31.690 9.681  1.00 64.22  ? 537 SER   A N   1 
ATOM   1770 C CA  . SER   A 1 245 ? -0.823  -31.002 8.541  1.00 73.05  ? 537 SER   A CA  1 
ATOM   1771 C C   . SER   A 1 245 ? -1.889  -30.389 7.644  1.00 58.69  ? 537 SER   A C   1 
ATOM   1772 O O   . SER   A 1 245 ? -1.803  -29.214 7.268  1.00 61.82  ? 537 SER   A O   1 
ATOM   1773 C CB  . SER   A 1 245 ? 0.053   -31.974 7.752  1.00 73.67  ? 537 SER   A CB  1 
ATOM   1774 O OG  . SER   A 1 245 ? 0.443   -33.074 8.557  1.00 85.37  ? 537 SER   A OG  1 
ATOM   1775 N N   . ASP   A 1 246 ? -2.905  -31.177 7.287  1.00 59.96  ? 538 ASP   A N   1 
ATOM   1776 C CA  . ASP   A 1 246 ? -3.977  -30.660 6.445  1.00 58.91  ? 538 ASP   A CA  1 
ATOM   1777 C C   . ASP   A 1 246 ? -4.729  -29.534 7.140  1.00 57.87  ? 538 ASP   A C   1 
ATOM   1778 O O   . ASP   A 1 246 ? -5.081  -28.531 6.509  1.00 62.43  ? 538 ASP   A O   1 
ATOM   1779 C CB  . ASP   A 1 246 ? -4.934  -31.789 6.060  1.00 68.62  ? 538 ASP   A CB  1 
ATOM   1780 N N   . LEU   A 1 247 ? -4.978  -29.675 8.445  1.00 59.29  ? 539 LEU   A N   1 
ATOM   1781 C CA  . LEU   A 1 247 ? -5.709  -28.635 9.160  1.00 60.41  ? 539 LEU   A CA  1 
ATOM   1782 C C   . LEU   A 1 247 ? -4.865  -27.373 9.295  1.00 55.48  ? 539 LEU   A C   1 
ATOM   1783 O O   . LEU   A 1 247 ? -5.376  -26.257 9.139  1.00 55.71  ? 539 LEU   A O   1 
ATOM   1784 C CB  . LEU   A 1 247 ? -6.133  -29.139 10.538 1.00 64.73  ? 539 LEU   A CB  1 
ATOM   1785 C CG  . LEU   A 1 247 ? -6.714  -28.046 11.434 1.00 68.76  ? 539 LEU   A CG  1 
ATOM   1786 C CD1 . LEU   A 1 247 ? -8.050  -27.583 10.866 1.00 76.15  ? 539 LEU   A CD1 1 
ATOM   1787 C CD2 . LEU   A 1 247 ? -6.862  -28.497 12.875 1.00 69.58  ? 539 LEU   A CD2 1 
ATOM   1788 N N   . LEU   A 1 248 ? -3.571  -27.531 9.594  1.00 52.74  ? 540 LEU   A N   1 
ATOM   1789 C CA  . LEU   A 1 248 ? -2.677  -26.379 9.642  1.00 52.91  ? 540 LEU   A CA  1 
ATOM   1790 C C   . LEU   A 1 248 ? -2.664  -25.648 8.310  1.00 48.82  ? 540 LEU   A C   1 
ATOM   1791 O O   . LEU   A 1 248 ? -2.701  -24.413 8.268  1.00 47.75  ? 540 LEU   A O   1 
ATOM   1792 C CB  . LEU   A 1 248 ? -1.262  -26.821 10.017 1.00 48.07  ? 540 LEU   A CB  1 
ATOM   1793 C CG  . LEU   A 1 248 ? -0.977  -27.180 11.476 1.00 48.27  ? 540 LEU   A CG  1 
ATOM   1794 C CD1 . LEU   A 1 248 ? 0.471   -27.605 11.633 1.00 45.96  ? 540 LEU   A CD1 1 
ATOM   1795 C CD2 . LEU   A 1 248 ? -1.296  -26.020 12.400 1.00 48.72  ? 540 LEU   A CD2 1 
ATOM   1796 N N   . LEU   A 1 249 ? -2.617  -26.398 7.208  1.00 49.43  ? 541 LEU   A N   1 
ATOM   1797 C CA  . LEU   A 1 249 ? -2.641  -25.784 5.887  1.00 56.24  ? 541 LEU   A CA  1 
ATOM   1798 C C   . LEU   A 1 249 ? -3.939  -25.015 5.673  1.00 56.27  ? 541 LEU   A C   1 
ATOM   1799 O O   . LEU   A 1 249 ? -3.928  -23.883 5.181  1.00 59.91  ? 541 LEU   A O   1 
ATOM   1800 C CB  . LEU   A 1 249 ? -2.463  -26.860 4.814  1.00 55.34  ? 541 LEU   A CB  1 
ATOM   1801 C CG  . LEU   A 1 249 ? -2.283  -26.427 3.357  1.00 68.89  ? 541 LEU   A CG  1 
ATOM   1802 C CD1 . LEU   A 1 249 ? -1.486  -25.134 3.259  1.00 64.54  ? 541 LEU   A CD1 1 
ATOM   1803 C CD2 . LEU   A 1 249 ? -1.626  -27.536 2.544  1.00 54.41  ? 541 LEU   A CD2 1 
ATOM   1804 N N   . GLU   A 1 250 ? -5.070  -25.607 6.069  1.00 51.85  ? 542 GLU   A N   1 
ATOM   1805 C CA  . GLU   A 1 250 ? -6.366  -25.000 5.779  1.00 52.74  ? 542 GLU   A CA  1 
ATOM   1806 C C   . GLU   A 1 250 ? -6.503  -23.629 6.432  1.00 51.74  ? 542 GLU   A C   1 
ATOM   1807 O O   . GLU   A 1 250 ? -7.033  -22.696 5.817  1.00 57.59  ? 542 GLU   A O   1 
ATOM   1808 C CB  . GLU   A 1 250 ? -7.495  -25.931 6.226  1.00 56.20  ? 542 GLU   A CB  1 
ATOM   1809 C CG  . GLU   A 1 250 ? -8.838  -25.626 5.575  1.00 66.06  ? 542 GLU   A CG  1 
ATOM   1810 C CD  . GLU   A 1 250 ? -8.754  -25.566 4.061  1.00 75.00  ? 542 GLU   A CD  1 
ATOM   1811 O OE1 . GLU   A 1 250 ? -8.608  -26.633 3.426  1.00 73.90  ? 542 GLU   A OE1 1 
ATOM   1812 O OE2 . GLU   A 1 250 ? -8.828  -24.451 3.504  1.00 73.01  ? 542 GLU   A OE2 1 
ATOM   1813 N N   . MET   A 1 251 ? -6.030  -23.481 7.672  1.00 52.16  ? 543 MET   A N   1 
ATOM   1814 C CA  . MET   A 1 251 ? -6.068  -22.165 8.302  1.00 52.44  ? 543 MET   A CA  1 
ATOM   1815 C C   . MET   A 1 251 ? -4.964  -21.250 7.795  1.00 49.00  ? 543 MET   A C   1 
ATOM   1816 O O   . MET   A 1 251 ? -5.179  -20.039 7.676  1.00 48.98  ? 543 MET   A O   1 
ATOM   1817 C CB  . MET   A 1 251 ? -5.965  -22.273 9.825  1.00 54.56  ? 543 MET   A CB  1 
ATOM   1818 C CG  . MET   A 1 251 ? -6.518  -23.538 10.444 1.00 59.45  ? 543 MET   A CG  1 
ATOM   1819 S SD  . MET   A 1 251 ? -7.047  -23.176 12.130 1.00 69.02  ? 543 MET   A SD  1 
ATOM   1820 C CE  . MET   A 1 251 ? -7.185  -24.813 12.828 1.00 65.37  ? 543 MET   A CE  1 
ATOM   1821 N N   . LEU   A 1 252 ? -3.783  -21.800 7.509  1.00 52.07  ? 544 LEU   A N   1 
ATOM   1822 C CA  . LEU   A 1 252 ? -2.692  -20.974 7.006  1.00 44.85  ? 544 LEU   A CA  1 
ATOM   1823 C C   . LEU   A 1 252 ? -2.932  -20.565 5.560  1.00 48.47  ? 544 LEU   A C   1 
ATOM   1824 O O   . LEU   A 1 252 ? -2.602  -19.441 5.164  1.00 55.63  ? 544 LEU   A O   1 
ATOM   1825 C CB  . LEU   A 1 252 ? -1.364  -21.718 7.135  1.00 44.03  ? 544 LEU   A CB  1 
ATOM   1826 C CG  . LEU   A 1 252 ? -0.726  -21.739 8.524  1.00 44.15  ? 544 LEU   A CG  1 
ATOM   1827 C CD1 . LEU   A 1 252 ? 0.349   -22.810 8.594  1.00 43.33  ? 544 LEU   A CD1 1 
ATOM   1828 C CD2 . LEU   A 1 252 ? -0.158  -20.374 8.883  1.00 46.24  ? 544 LEU   A CD2 1 
ATOM   1829 N N   . ASP   A 1 253 ? -3.502  -21.463 4.755  1.00 47.00  ? 545 ASP   A N   1 
ATOM   1830 C CA  . ASP   A 1 253 ? -3.802  -21.169 3.354  1.00 48.20  ? 545 ASP   A CA  1 
ATOM   1831 C C   . ASP   A 1 253 ? -5.159  -20.469 3.266  1.00 44.48  ? 545 ASP   A C   1 
ATOM   1832 O O   . ASP   A 1 253 ? -6.162  -21.017 2.805  1.00 47.27  ? 545 ASP   A O   1 
ATOM   1833 C CB  . ASP   A 1 253 ? -3.771  -22.444 2.522  1.00 45.77  ? 545 ASP   A CB  1 
ATOM   1834 C CG  . ASP   A 1 253 ? -3.853  -22.174 1.037  1.00 45.67  ? 545 ASP   A CG  1 
ATOM   1835 O OD1 . ASP   A 1 253 ? -3.650  -21.011 0.633  1.00 43.99  ? 545 ASP   A OD1 1 
ATOM   1836 O OD2 . ASP   A 1 253 ? -4.124  -23.126 0.276  1.00 47.65  ? 545 ASP   A OD2 1 
ATOM   1837 N N   . ALA   A 1 254 ? -5.169  -19.227 3.733  1.00 53.53  ? 546 ALA   A N   1 
ATOM   1838 C CA  . ALA   A 1 254 ? -6.374  -18.420 3.676  1.00 49.88  ? 546 ALA   A CA  1 
ATOM   1839 C C   . ALA   A 1 254 ? -6.501  -17.752 2.311  1.00 52.41  ? 546 ALA   A C   1 
ATOM   1840 O O   . ALA   A 1 254 ? -5.523  -17.583 1.576  1.00 46.59  ? 546 ALA   A O   1 
ATOM   1841 C CB  . ALA   A 1 254 ? -6.370  -17.362 4.780  1.00 45.13  ? 546 ALA   A CB  1 
ATOM   1842 N N   . HIS   A 1 255 ? -7.731  -17.381 1.972  1.00 49.36  ? 547 HIS   A N   1 
ATOM   1843 C CA  . HIS   A 1 255 ? -7.985  -16.616 0.765  1.00 57.40  ? 547 HIS   A CA  1 
ATOM   1844 C C   . HIS   A 1 255 ? -7.920  -15.123 1.085  1.00 59.09  ? 547 HIS   A C   1 
ATOM   1845 O O   . HIS   A 1 255 ? -7.661  -14.715 2.220  1.00 58.62  ? 547 HIS   A O   1 
ATOM   1846 C CB  . HIS   A 1 255 ? -9.331  -17.010 0.155  1.00 41.52  ? 547 HIS   A CB  1 
ATOM   1847 C CG  . HIS   A 1 255 ? -10.476 -16.969 1.120  1.00 43.39  ? 547 HIS   A CG  1 
ATOM   1848 N ND1 . HIS   A 1 255 ? -10.715 -15.897 1.952  1.00 48.25  ? 547 HIS   A ND1 1 
ATOM   1849 C CD2 . HIS   A 1 255 ? -11.454 -17.870 1.378  1.00 44.17  ? 547 HIS   A CD2 1 
ATOM   1850 C CE1 . HIS   A 1 255 ? -11.787 -16.140 2.684  1.00 60.07  ? 547 HIS   A CE1 1 
ATOM   1851 N NE2 . HIS   A 1 255 ? -12.256 -17.330 2.354  1.00 56.50  ? 547 HIS   A NE2 1 
ATOM   1852 N N   . ARG   A 1 256 ? -8.151  -14.294 0.071  1.00 58.52  ? 548 ARG   A N   1 
ATOM   1853 C CA  . ARG   A 1 256 ? -8.178  -12.845 0.234  1.00 49.08  ? 548 ARG   A CA  1 
ATOM   1854 C C   . ARG   A 1 256 ? -9.544  -12.278 -0.133 1.00 58.62  ? 548 ARG   A C   1 
ATOM   1855 O O   . ARG   A 1 256 ? -9.651  -11.142 -0.600 1.00 73.72  ? 548 ARG   A O   1 
ATOM   1856 C CB  . ARG   A 1 256 ? -7.078  -12.186 -0.598 1.00 43.96  ? 548 ARG   A CB  1 
ATOM   1857 N N   . LEU   A 1 257 ? -10.597 -13.060 0.082  1.00 49.25  ? 549 LEU   A N   1 
ATOM   1858 C CA  . LEU   A 1 257 ? -11.935 -12.690 -0.359 1.00 62.52  ? 549 LEU   A CA  1 
ATOM   1859 C C   . LEU   A 1 257 ? -12.588 -11.698 0.596  1.00 65.92  ? 549 LEU   A C   1 
ATOM   1860 O O   . LEU   A 1 257 ? -13.812 -11.638 0.700  1.00 76.76  ? 549 LEU   A O   1 
ATOM   1861 C CB  . LEU   A 1 257 ? -12.807 -13.938 -0.498 1.00 55.34  ? 549 LEU   A CB  1 
ATOM   1862 C CG  . LEU   A 1 257 ? -12.207 -15.013 -1.407 1.00 43.57  ? 549 LEU   A CG  1 
ATOM   1863 C CD1 . LEU   A 1 257 ? -13.136 -16.214 -1.538 1.00 51.47  ? 549 LEU   A CD1 1 
ATOM   1864 C CD2 . LEU   A 1 257 ? -11.853 -14.431 -2.766 1.00 44.10  ? 549 LEU   A CD2 1 
ATOM   1865 N N   . LEU   B 1 14  ? 34.334  -23.846 42.780 1.00 78.19  ? 306 LEU   B N   1 
ATOM   1866 C CA  . LEU   B 1 14  ? 35.761  -23.579 42.921 1.00 72.19  ? 306 LEU   B CA  1 
ATOM   1867 C C   . LEU   B 1 14  ? 36.441  -23.618 41.558 1.00 69.19  ? 306 LEU   B C   1 
ATOM   1868 O O   . LEU   B 1 14  ? 37.524  -23.060 41.373 1.00 71.88  ? 306 LEU   B O   1 
ATOM   1869 C CB  . LEU   B 1 14  ? 36.408  -24.577 43.882 1.00 69.12  ? 306 LEU   B CB  1 
ATOM   1870 C CG  . LEU   B 1 14  ? 36.352  -24.202 45.367 1.00 78.81  ? 306 LEU   B CG  1 
ATOM   1871 C CD1 . LEU   B 1 14  ? 37.038  -22.863 45.599 1.00 78.04  ? 306 LEU   B CD1 1 
ATOM   1872 C CD2 . LEU   B 1 14  ? 34.923  -24.173 45.900 1.00 85.42  ? 306 LEU   B CD2 1 
ATOM   1873 N N   . ALA   B 1 15  ? 35.799  -24.292 40.605 1.00 69.35  ? 307 ALA   B N   1 
ATOM   1874 C CA  . ALA   B 1 15  ? 36.153  -24.130 39.203 1.00 57.91  ? 307 ALA   B CA  1 
ATOM   1875 C C   . ALA   B 1 15  ? 35.644  -22.813 38.637 1.00 65.02  ? 307 ALA   B C   1 
ATOM   1876 O O   . ALA   B 1 15  ? 35.970  -22.476 37.493 1.00 61.34  ? 307 ALA   B O   1 
ATOM   1877 C CB  . ALA   B 1 15  ? 35.603  -25.295 38.379 1.00 60.34  ? 307 ALA   B CB  1 
ATOM   1878 N N   . LEU   B 1 16  ? 34.853  -22.070 39.414 1.00 60.19  ? 308 LEU   B N   1 
ATOM   1879 C CA  . LEU   B 1 16  ? 34.377  -20.741 39.056 1.00 64.35  ? 308 LEU   B CA  1 
ATOM   1880 C C   . LEU   B 1 16  ? 35.473  -19.688 39.126 1.00 71.89  ? 308 LEU   B C   1 
ATOM   1881 O O   . LEU   B 1 16  ? 35.205  -18.520 38.820 1.00 67.37  ? 308 LEU   B O   1 
ATOM   1882 C CB  . LEU   B 1 16  ? 33.224  -20.340 39.977 1.00 58.26  ? 308 LEU   B CB  1 
ATOM   1883 C CG  . LEU   B 1 16  ? 32.092  -21.356 40.149 1.00 57.73  ? 308 LEU   B CG  1 
ATOM   1884 C CD1 . LEU   B 1 16  ? 31.220  -20.984 41.337 1.00 62.95  ? 308 LEU   B CD1 1 
ATOM   1885 C CD2 . LEU   B 1 16  ? 31.260  -21.458 38.882 1.00 54.83  ? 308 LEU   B CD2 1 
ATOM   1886 N N   . SER   B 1 17  ? 36.685  -20.064 39.529 1.00 66.31  ? 309 SER   B N   1 
ATOM   1887 C CA  . SER   B 1 17  ? 37.812  -19.146 39.612 1.00 63.75  ? 309 SER   B CA  1 
ATOM   1888 C C   . SER   B 1 17  ? 38.757  -19.275 38.426 1.00 65.38  ? 309 SER   B C   1 
ATOM   1889 O O   . SER   B 1 17  ? 39.829  -18.664 38.430 1.00 68.85  ? 309 SER   B O   1 
ATOM   1890 C CB  . SER   B 1 17  ? 38.576  -19.370 40.919 1.00 68.71  ? 309 SER   B CB  1 
ATOM   1891 O OG  . SER   B 1 17  ? 37.697  -19.374 42.030 1.00 78.58  ? 309 SER   B OG  1 
ATOM   1892 N N   . LEU   B 1 18  ? 38.389  -20.061 37.420 1.00 58.61  ? 310 LEU   B N   1 
ATOM   1893 C CA  . LEU   B 1 18  ? 39.182  -20.151 36.207 1.00 62.96  ? 310 LEU   B CA  1 
ATOM   1894 C C   . LEU   B 1 18  ? 38.982  -18.901 35.358 1.00 66.39  ? 310 LEU   B C   1 
ATOM   1895 O O   . LEU   B 1 18  ? 38.055  -18.115 35.570 1.00 61.26  ? 310 LEU   B O   1 
ATOM   1896 C CB  . LEU   B 1 18  ? 38.802  -21.393 35.395 1.00 48.76  ? 310 LEU   B CB  1 
ATOM   1897 C CG  . LEU   B 1 18  ? 39.400  -22.763 35.732 1.00 57.49  ? 310 LEU   B CG  1 
ATOM   1898 C CD1 . LEU   B 1 18  ? 39.295  -23.095 37.215 1.00 62.43  ? 310 LEU   B CD1 1 
ATOM   1899 C CD2 . LEU   B 1 18  ? 38.735  -23.845 34.892 1.00 48.62  ? 310 LEU   B CD2 1 
ATOM   1900 N N   . THR   B 1 19  ? 39.872  -18.714 34.392 1.00 60.82  ? 311 THR   B N   1 
ATOM   1901 C CA  . THR   B 1 19  ? 39.646  -17.700 33.377 1.00 56.08  ? 311 THR   B CA  1 
ATOM   1902 C C   . THR   B 1 19  ? 38.976  -18.338 32.166 1.00 48.94  ? 311 THR   B C   1 
ATOM   1903 O O   . THR   B 1 19  ? 38.863  -19.561 32.058 1.00 49.25  ? 311 THR   B O   1 
ATOM   1904 C CB  . THR   B 1 19  ? 40.955  -17.023 32.970 1.00 54.80  ? 311 THR   B CB  1 
ATOM   1905 O OG1 . THR   B 1 19  ? 41.916  -18.019 32.601 1.00 58.53  ? 311 THR   B OG1 1 
ATOM   1906 C CG2 . THR   B 1 19  ? 41.509  -16.197 34.122 1.00 58.10  ? 311 THR   B CG2 1 
ATOM   1907 N N   . ALA   B 1 20  ? 38.514  -17.489 31.247 1.00 48.91  ? 312 ALA   B N   1 
ATOM   1908 C CA  . ALA   B 1 20  ? 37.911  -18.000 30.022 1.00 46.35  ? 312 ALA   B CA  1 
ATOM   1909 C C   . ALA   B 1 20  ? 38.916  -18.817 29.220 1.00 51.82  ? 312 ALA   B C   1 
ATOM   1910 O O   . ALA   B 1 20  ? 38.574  -19.869 28.667 1.00 41.54  ? 312 ALA   B O   1 
ATOM   1911 C CB  . ALA   B 1 20  ? 37.360  -16.848 29.186 1.00 48.76  ? 312 ALA   B CB  1 
ATOM   1912 N N   . ASP   B 1 21  ? 40.168  -18.357 29.159 1.00 48.91  ? 313 ASP   B N   1 
ATOM   1913 C CA  . ASP   B 1 21  ? 41.193  -19.099 28.433 1.00 53.54  ? 313 ASP   B CA  1 
ATOM   1914 C C   . ASP   B 1 21  ? 41.550  -20.395 29.151 1.00 48.82  ? 313 ASP   B C   1 
ATOM   1915 O O   . ASP   B 1 21  ? 41.755  -21.430 28.507 1.00 50.67  ? 313 ASP   B O   1 
ATOM   1916 C CB  . ASP   B 1 21  ? 42.432  -18.225 28.240 1.00 49.98  ? 313 ASP   B CB  1 
ATOM   1917 C CG  . ASP   B 1 21  ? 42.189  -17.076 27.279 1.00 70.03  ? 313 ASP   B CG  1 
ATOM   1918 O OD1 . ASP   B 1 21  ? 41.628  -17.318 26.190 1.00 69.02  ? 313 ASP   B OD1 1 
ATOM   1919 O OD2 . ASP   B 1 21  ? 42.557  -15.930 27.614 1.00 56.63  ? 313 ASP   B OD2 1 
ATOM   1920 N N   . GLN   B 1 22  ? 41.629  -20.361 30.484 1.00 47.16  ? 314 GLN   B N   1 
ATOM   1921 C CA  . GLN   B 1 22  ? 41.884  -21.585 31.237 1.00 51.82  ? 314 GLN   B CA  1 
ATOM   1922 C C   . GLN   B 1 22  ? 40.707  -22.547 31.151 1.00 44.81  ? 314 GLN   B C   1 
ATOM   1923 O O   . GLN   B 1 22  ? 40.901  -23.767 31.198 1.00 48.22  ? 314 GLN   B O   1 
ATOM   1924 C CB  . GLN   B 1 22  ? 42.199  -21.252 32.696 1.00 46.48  ? 314 GLN   B CB  1 
ATOM   1925 C CG  . GLN   B 1 22  ? 43.580  -20.650 32.913 1.00 48.71  ? 314 GLN   B CG  1 
ATOM   1926 C CD  . GLN   B 1 22  ? 43.733  -20.022 34.284 1.00 55.18  ? 314 GLN   B CD  1 
ATOM   1927 O OE1 . GLN   B 1 22  ? 42.753  -19.823 35.002 1.00 51.89  ? 314 GLN   B OE1 1 
ATOM   1928 N NE2 . GLN   B 1 22  ? 44.968  -19.698 34.654 1.00 56.45  ? 314 GLN   B NE2 1 
ATOM   1929 N N   . MET   B 1 23  ? 39.486  -22.020 31.030 1.00 49.23  ? 315 MET   B N   1 
ATOM   1930 C CA  . MET   B 1 23  ? 38.328  -22.880 30.809 1.00 45.75  ? 315 MET   B CA  1 
ATOM   1931 C C   . MET   B 1 23  ? 38.423  -23.587 29.463 1.00 37.50  ? 315 MET   B C   1 
ATOM   1932 O O   . MET   B 1 23  ? 38.146  -24.788 29.367 1.00 39.61  ? 315 MET   B O   1 
ATOM   1933 C CB  . MET   B 1 23  ? 37.042  -22.057 30.900 1.00 44.84  ? 315 MET   B CB  1 
ATOM   1934 C CG  . MET   B 1 23  ? 35.781  -22.814 30.524 1.00 56.77  ? 315 MET   B CG  1 
ATOM   1935 S SD  . MET   B 1 23  ? 35.342  -24.078 31.727 1.00 59.01  ? 315 MET   B SD  1 
ATOM   1936 C CE  . MET   B 1 23  ? 34.963  -23.071 33.159 1.00 42.80  ? 315 MET   B CE  1 
ATOM   1937 N N   . VAL   B 1 24  ? 38.820  -22.860 28.415 1.00 39.93  ? 316 VAL   B N   1 
ATOM   1938 C CA  . VAL   B 1 24  ? 39.020  -23.478 27.105 1.00 40.79  ? 316 VAL   B CA  1 
ATOM   1939 C C   . VAL   B 1 24  ? 40.109  -24.540 27.182 1.00 37.80  ? 316 VAL   B C   1 
ATOM   1940 O O   . VAL   B 1 24  ? 39.943  -25.662 26.691 1.00 38.84  ? 316 VAL   B O   1 
ATOM   1941 C CB  . VAL   B 1 24  ? 39.359  -22.409 26.051 1.00 42.62  ? 316 VAL   B CB  1 
ATOM   1942 C CG1 . VAL   B 1 24  ? 39.704  -23.067 24.726 1.00 53.24  ? 316 VAL   B CG1 1 
ATOM   1943 C CG2 . VAL   B 1 24  ? 38.206  -21.449 25.877 1.00 38.39  ? 316 VAL   B CG2 1 
ATOM   1944 N N   . SER   B 1 25  ? 41.240  -24.197 27.806 1.00 38.61  ? 317 SER   B N   1 
ATOM   1945 C CA  . SER   B 1 25  ? 42.366  -25.123 27.874 1.00 37.69  ? 317 SER   B CA  1 
ATOM   1946 C C   . SER   B 1 25  ? 41.999  -26.390 28.635 1.00 34.20  ? 317 SER   B C   1 
ATOM   1947 O O   . SER   B 1 25  ? 42.438  -27.488 28.275 1.00 39.96  ? 317 SER   B O   1 
ATOM   1948 C CB  . SER   B 1 25  ? 43.567  -24.438 28.526 1.00 38.70  ? 317 SER   B CB  1 
ATOM   1949 O OG  . SER   B 1 25  ? 44.144  -23.484 27.653 1.00 57.12  ? 317 SER   B OG  1 
ATOM   1950 N N   . ALA   B 1 26  ? 41.193  -26.258 29.691 1.00 38.36  ? 318 ALA   B N   1 
ATOM   1951 C CA  . ALA   B 1 26  ? 40.786  -27.432 30.456 1.00 39.62  ? 318 ALA   B CA  1 
ATOM   1952 C C   . ALA   B 1 26  ? 39.855  -28.324 29.644 1.00 34.36  ? 318 ALA   B C   1 
ATOM   1953 O O   . ALA   B 1 26  ? 39.961  -29.555 29.700 1.00 40.01  ? 318 ALA   B O   1 
ATOM   1954 C CB  . ALA   B 1 26  ? 40.118  -27.001 31.761 1.00 32.86  ? 318 ALA   B CB  1 
ATOM   1955 N N   . LEU   B 1 27  ? 38.942  -27.723 28.879 1.00 32.10  ? 319 LEU   B N   1 
ATOM   1956 C CA  . LEU   B 1 27  ? 38.006  -28.516 28.090 1.00 32.70  ? 319 LEU   B CA  1 
ATOM   1957 C C   . LEU   B 1 27  ? 38.696  -29.165 26.897 1.00 36.63  ? 319 LEU   B C   1 
ATOM   1958 O O   . LEU   B 1 27  ? 38.370  -30.298 26.526 1.00 36.63  ? 319 LEU   B O   1 
ATOM   1959 C CB  . LEU   B 1 27  ? 36.840  -27.645 27.629 1.00 26.48  ? 319 LEU   B CB  1 
ATOM   1960 C CG  . LEU   B 1 27  ? 35.922  -27.160 28.750 1.00 36.23  ? 319 LEU   B CG  1 
ATOM   1961 C CD1 . LEU   B 1 27  ? 34.821  -26.264 28.202 1.00 29.36  ? 319 LEU   B CD1 1 
ATOM   1962 C CD2 . LEU   B 1 27  ? 35.342  -28.345 29.505 1.00 34.91  ? 319 LEU   B CD2 1 
ATOM   1963 N N   . LEU   B 1 28  ? 39.648  -28.460 26.280 1.00 29.33  ? 320 LEU   B N   1 
ATOM   1964 C CA  . LEU   B 1 28  ? 40.391  -29.044 25.169 1.00 37.00  ? 320 LEU   B CA  1 
ATOM   1965 C C   . LEU   B 1 28  ? 41.225  -30.231 25.632 1.00 43.49  ? 320 LEU   B C   1 
ATOM   1966 O O   . LEU   B 1 28  ? 41.285  -31.262 24.952 1.00 43.44  ? 320 LEU   B O   1 
ATOM   1967 C CB  . LEU   B 1 28  ? 41.280  -27.987 24.515 1.00 32.15  ? 320 LEU   B CB  1 
ATOM   1968 C CG  . LEU   B 1 28  ? 40.580  -26.848 23.772 1.00 33.66  ? 320 LEU   B CG  1 
ATOM   1969 C CD1 . LEU   B 1 28  ? 41.604  -25.891 23.182 1.00 34.32  ? 320 LEU   B CD1 1 
ATOM   1970 C CD2 . LEU   B 1 28  ? 39.665  -27.394 22.689 1.00 29.87  ? 320 LEU   B CD2 1 
ATOM   1971 N N   . ASP   B 1 29  ? 41.871  -30.106 26.794 1.00 38.81  ? 321 ASP   B N   1 
ATOM   1972 C CA  . ASP   B 1 29  ? 42.673  -31.199 27.329 1.00 35.23  ? 321 ASP   B CA  1 
ATOM   1973 C C   . ASP   B 1 29  ? 41.819  -32.374 27.787 1.00 42.48  ? 321 ASP   B C   1 
ATOM   1974 O O   . ASP   B 1 29  ? 42.340  -33.485 27.929 1.00 43.48  ? 321 ASP   B O   1 
ATOM   1975 C CB  . ASP   B 1 29  ? 43.530  -30.699 28.493 1.00 50.01  ? 321 ASP   B CB  1 
ATOM   1976 C CG  . ASP   B 1 29  ? 44.697  -29.847 28.035 1.00 63.97  ? 321 ASP   B CG  1 
ATOM   1977 O OD1 . ASP   B 1 29  ? 45.297  -30.170 26.988 1.00 73.58  ? 321 ASP   B OD1 1 
ATOM   1978 O OD2 . ASP   B 1 29  ? 45.015  -28.854 28.722 1.00 60.38  ? 321 ASP   B OD2 1 
ATOM   1979 N N   . ALA   B 1 30  ? 40.528  -32.157 28.018 1.00 39.04  ? 322 ALA   B N   1 
ATOM   1980 C CA  . ALA   B 1 30  ? 39.630  -33.202 28.486 1.00 38.25  ? 322 ALA   B CA  1 
ATOM   1981 C C   . ALA   B 1 30  ? 38.979  -33.983 27.353 1.00 35.40  ? 322 ALA   B C   1 
ATOM   1982 O O   . ALA   B 1 30  ? 38.228  -34.925 27.627 1.00 41.09  ? 322 ALA   B O   1 
ATOM   1983 C CB  . ALA   B 1 30  ? 38.540  -32.598 29.375 1.00 36.61  ? 322 ALA   B CB  1 
ATOM   1984 N N   . GLU   B 1 31  ? 39.250  -33.623 26.103 1.00 28.78  ? 323 GLU   B N   1 
ATOM   1985 C CA  . GLU   B 1 31  ? 38.559  -34.238 24.978 1.00 33.38  ? 323 GLU   B CA  1 
ATOM   1986 C C   . GLU   B 1 31  ? 38.822  -35.740 24.943 1.00 31.64  ? 323 GLU   B C   1 
ATOM   1987 O O   . GLU   B 1 31  ? 39.977  -36.167 25.077 1.00 30.03  ? 323 GLU   B O   1 
ATOM   1988 C CB  . GLU   B 1 31  ? 39.001  -33.598 23.663 1.00 28.61  ? 323 GLU   B CB  1 
ATOM   1989 C CG  . GLU   B 1 31  ? 38.116  -32.449 23.214 1.00 26.94  ? 323 GLU   B CG  1 
ATOM   1990 C CD  . GLU   B 1 31  ? 36.663  -32.859 23.083 1.00 27.99  ? 323 GLU   B CD  1 
ATOM   1991 O OE1 . GLU   B 1 31  ? 36.291  -33.405 22.024 1.00 39.20  ? 323 GLU   B OE1 1 
ATOM   1992 O OE2 . GLU   B 1 31  ? 35.894  -32.636 24.042 1.00 37.66  ? 323 GLU   B OE2 1 
ATOM   1993 N N   . PRO   B 1 32  ? 37.794  -36.565 24.771 1.00 27.71  ? 324 PRO   B N   1 
ATOM   1994 C CA  . PRO   B 1 32  ? 38.001  -38.011 24.724 1.00 23.87  ? 324 PRO   B CA  1 
ATOM   1995 C C   . PRO   B 1 32  ? 38.639  -38.419 23.410 1.00 32.55  ? 324 PRO   B C   1 
ATOM   1996 O O   . PRO   B 1 32  ? 38.580  -37.673 22.421 1.00 35.52  ? 324 PRO   B O   1 
ATOM   1997 C CB  . PRO   B 1 32  ? 36.577  -38.571 24.852 1.00 23.47  ? 324 PRO   B CB  1 
ATOM   1998 C CG  . PRO   B 1 32  ? 35.722  -37.515 24.246 1.00 36.61  ? 324 PRO   B CG  1 
ATOM   1999 C CD  . PRO   B 1 32  ? 36.376  -36.202 24.597 1.00 30.75  ? 324 PRO   B CD  1 
ATOM   2000 N N   . PRO   B 1 33  ? 39.264  -39.591 23.358 1.00 36.86  ? 325 PRO   B N   1 
ATOM   2001 C CA  . PRO   B 1 33  ? 39.852  -40.052 22.099 1.00 37.82  ? 325 PRO   B CA  1 
ATOM   2002 C C   . PRO   B 1 33  ? 38.782  -40.506 21.121 1.00 30.26  ? 325 PRO   B C   1 
ATOM   2003 O O   . PRO   B 1 33  ? 37.629  -40.753 21.479 1.00 30.86  ? 325 PRO   B O   1 
ATOM   2004 C CB  . PRO   B 1 33  ? 40.736  -41.224 22.530 1.00 28.91  ? 325 PRO   B CB  1 
ATOM   2005 C CG  . PRO   B 1 33  ? 40.074  -41.743 23.763 1.00 31.98  ? 325 PRO   B CG  1 
ATOM   2006 C CD  . PRO   B 1 33  ? 39.492  -40.543 24.459 1.00 25.50  ? 325 PRO   B CD  1 
ATOM   2007 N N   . ILE   B 1 34  ? 39.186  -40.612 19.860 1.00 33.32  ? 326 ILE   B N   1 
ATOM   2008 C CA  . ILE   B 1 34  ? 38.320  -41.133 18.809 1.00 39.56  ? 326 ILE   B CA  1 
ATOM   2009 C C   . ILE   B 1 34  ? 38.503  -42.645 18.780 1.00 29.18  ? 326 ILE   B C   1 
ATOM   2010 O O   . ILE   B 1 34  ? 39.583  -43.145 18.454 1.00 31.31  ? 326 ILE   B O   1 
ATOM   2011 C CB  . ILE   B 1 34  ? 38.635  -40.499 17.450 1.00 39.15  ? 326 ILE   B CB  1 
ATOM   2012 C CG1 . ILE   B 1 34  ? 38.198  -39.033 17.437 1.00 33.29  ? 326 ILE   B CG1 1 
ATOM   2013 C CG2 . ILE   B 1 34  ? 37.945  -41.264 16.332 1.00 33.29  ? 326 ILE   B CG2 1 
ATOM   2014 C CD1 . ILE   B 1 34  ? 38.560  -38.298 16.167 1.00 35.28  ? 326 ILE   B CD1 1 
ATOM   2015 N N   . LEU   B 1 35  ? 37.452  -43.375 19.137 1.00 34.35  ? 327 LEU   B N   1 
ATOM   2016 C CA  . LEU   B 1 35  ? 37.515  -44.826 19.196 1.00 30.80  ? 327 LEU   B CA  1 
ATOM   2017 C C   . LEU   B 1 35  ? 37.230  -45.431 17.827 1.00 43.25  ? 327 LEU   B C   1 
ATOM   2018 O O   . LEU   B 1 35  ? 36.712  -44.775 16.921 1.00 37.03  ? 327 LEU   B O   1 
ATOM   2019 C CB  . LEU   B 1 35  ? 36.526  -45.370 20.227 1.00 31.47  ? 327 LEU   B CB  1 
ATOM   2020 C CG  . LEU   B 1 35  ? 36.696  -44.862 21.660 1.00 32.67  ? 327 LEU   B CG  1 
ATOM   2021 C CD1 . LEU   B 1 35  ? 35.871  -45.697 22.624 1.00 32.31  ? 327 LEU   B CD1 1 
ATOM   2022 C CD2 . LEU   B 1 35  ? 38.162  -44.870 22.063 1.00 30.36  ? 327 LEU   B CD2 1 
ATOM   2023 N N   . TYR   B 1 36  ? 37.578  -46.706 17.688 1.00 34.57  ? 328 TYR   B N   1 
ATOM   2024 C CA  . TYR   B 1 36  ? 37.405  -47.434 16.444 1.00 37.15  ? 328 TYR   B CA  1 
ATOM   2025 C C   . TYR   B 1 36  ? 36.289  -48.458 16.571 1.00 37.84  ? 328 TYR   B C   1 
ATOM   2026 O O   . TYR   B 1 36  ? 36.021  -48.983 17.655 1.00 37.64  ? 328 TYR   B O   1 
ATOM   2027 C CB  . TYR   B 1 36  ? 38.700  -48.136 16.032 1.00 40.30  ? 328 TYR   B CB  1 
ATOM   2028 C CG  . TYR   B 1 36  ? 39.607  -47.259 15.215 1.00 41.32  ? 328 TYR   B CG  1 
ATOM   2029 C CD1 . TYR   B 1 36  ? 40.416  -46.314 15.823 1.00 41.19  ? 328 TYR   B CD1 1 
ATOM   2030 C CD2 . TYR   B 1 36  ? 39.645  -47.367 13.832 1.00 44.09  ? 328 TYR   B CD2 1 
ATOM   2031 C CE1 . TYR   B 1 36  ? 41.241  -45.506 15.081 1.00 41.61  ? 328 TYR   B CE1 1 
ATOM   2032 C CE2 . TYR   B 1 36  ? 40.471  -46.564 13.080 1.00 49.17  ? 328 TYR   B CE2 1 
ATOM   2033 C CZ  . TYR   B 1 36  ? 41.264  -45.634 13.710 1.00 44.51  ? 328 TYR   B CZ  1 
ATOM   2034 O OH  . TYR   B 1 36  ? 42.093  -44.827 12.965 1.00 51.99  ? 328 TYR   B OH  1 
ATOM   2035 N N   . SER   B 1 37  ? 35.637  -48.730 15.445 1.00 39.48  ? 329 SER   B N   1 
ATOM   2036 C CA  . SER   B 1 37  ? 34.658  -49.803 15.396 1.00 41.10  ? 329 SER   B CA  1 
ATOM   2037 C C   . SER   B 1 37  ? 35.349  -51.140 15.618 1.00 50.24  ? 329 SER   B C   1 
ATOM   2038 O O   . SER   B 1 37  ? 36.451  -51.380 15.115 1.00 45.88  ? 329 SER   B O   1 
ATOM   2039 C CB  . SER   B 1 37  ? 33.935  -49.798 14.050 1.00 42.94  ? 329 SER   B CB  1 
ATOM   2040 O OG  . SER   B 1 37  ? 33.005  -50.863 13.964 1.00 49.17  ? 329 SER   B OG  1 
ATOM   2041 N N   . GLU   B 1 38  ? 34.699  -52.014 16.387 1.00 48.56  ? 330 GLU   B N   1 
ATOM   2042 C CA  . GLU   B 1 38  ? 35.226  -53.354 16.612 1.00 49.58  ? 330 GLU   B CA  1 
ATOM   2043 C C   . GLU   B 1 38  ? 34.849  -54.233 15.428 1.00 62.61  ? 330 GLU   B C   1 
ATOM   2044 O O   . GLU   B 1 38  ? 34.240  -55.294 15.597 1.00 75.31  ? 330 GLU   B O   1 
ATOM   2045 C CB  . GLU   B 1 38  ? 34.696  -53.928 17.929 1.00 51.50  ? 330 GLU   B CB  1 
ATOM   2046 C CG  . GLU   B 1 38  ? 35.715  -54.741 18.711 1.00 60.35  ? 330 GLU   B CG  1 
ATOM   2047 C CD  . GLU   B 1 38  ? 35.159  -55.269 20.019 1.00 56.09  ? 330 GLU   B CD  1 
ATOM   2048 O OE1 . GLU   B 1 38  ? 34.355  -56.220 19.980 1.00 73.52  ? 330 GLU   B OE1 1 
ATOM   2049 O OE2 . GLU   B 1 38  ? 35.526  -54.734 21.088 1.00 48.92  ? 330 GLU   B OE2 1 
ATOM   2050 N N   . TYR   B 1 39  ? 35.226  -53.800 14.229 1.00 59.60  ? 331 TYR   B N   1 
ATOM   2051 C CA  . TYR   B 1 39  ? 34.791  -54.403 12.980 1.00 64.27  ? 331 TYR   B CA  1 
ATOM   2052 C C   . TYR   B 1 39  ? 35.980  -55.034 12.272 1.00 79.59  ? 331 TYR   B C   1 
ATOM   2053 O O   . TYR   B 1 39  ? 37.067  -54.452 12.229 1.00 83.82  ? 331 TYR   B O   1 
ATOM   2054 C CB  . TYR   B 1 39  ? 34.132  -53.345 12.089 1.00 63.78  ? 331 TYR   B CB  1 
ATOM   2055 C CG  . TYR   B 1 39  ? 34.073  -53.667 10.613 1.00 78.04  ? 331 TYR   B CG  1 
ATOM   2056 C CD1 . TYR   B 1 39  ? 33.431  -54.809 10.149 1.00 69.00  ? 331 TYR   B CD1 1 
ATOM   2057 C CD2 . TYR   B 1 39  ? 34.664  -52.824 9.680  1.00 76.35  ? 331 TYR   B CD2 1 
ATOM   2058 C CE1 . TYR   B 1 39  ? 33.374  -55.100 8.796  1.00 89.16  ? 331 TYR   B CE1 1 
ATOM   2059 C CE2 . TYR   B 1 39  ? 34.607  -53.103 8.326  1.00 79.58  ? 331 TYR   B CE2 1 
ATOM   2060 C CZ  . TYR   B 1 39  ? 33.966  -54.243 7.889  1.00 82.60  ? 331 TYR   B CZ  1 
ATOM   2061 O OH  . TYR   B 1 39  ? 33.921  -54.515 6.540  1.00 71.28  ? 331 TYR   B OH  1 
ATOM   2062 N N   . ASP   B 1 40  ? 35.774  -56.233 11.752 1.00 86.02  ? 332 ASP   B N   1 
ATOM   2063 C CA  . ASP   B 1 40  ? 36.786  -56.943 10.985 1.00 85.95  ? 332 ASP   B CA  1 
ATOM   2064 C C   . ASP   B 1 40  ? 37.046  -56.237 9.662  1.00 89.49  ? 332 ASP   B C   1 
ATOM   2065 O O   . ASP   B 1 40  ? 36.177  -56.266 8.780  1.00 87.23  ? 332 ASP   B O   1 
ATOM   2066 C CB  . ASP   B 1 40  ? 36.334  -58.381 10.739 1.00 90.99  ? 332 ASP   B CB  1 
ATOM   2067 C CG  . ASP   B 1 40  ? 37.436  -59.395 10.986 1.00 100.07 ? 332 ASP   B CG  1 
ATOM   2068 O OD1 . ASP   B 1 40  ? 38.486  -59.316 10.312 1.00 101.04 ? 332 ASP   B OD1 1 
ATOM   2069 O OD2 . ASP   B 1 40  ? 37.247  -60.279 11.847 1.00 103.85 ? 332 ASP   B OD2 1 
ATOM   2070 N N   . PRO   B 1 41  ? 38.205  -55.601 9.469  1.00 90.15  ? 333 PRO   B N   1 
ATOM   2071 C CA  . PRO   B 1 41  ? 38.485  -54.968 8.172  1.00 85.35  ? 333 PRO   B CA  1 
ATOM   2072 C C   . PRO   B 1 41  ? 38.624  -55.968 7.037  1.00 84.59  ? 333 PRO   B C   1 
ATOM   2073 O O   . PRO   B 1 41  ? 38.680  -55.554 5.872  1.00 83.89  ? 333 PRO   B O   1 
ATOM   2074 C CB  . PRO   B 1 41  ? 39.804  -54.217 8.421  1.00 88.66  ? 333 PRO   B CB  1 
ATOM   2075 C CG  . PRO   B 1 41  ? 39.945  -54.159 9.925  1.00 90.46  ? 333 PRO   B CG  1 
ATOM   2076 C CD  . PRO   B 1 41  ? 39.326  -55.432 10.405 1.00 96.82  ? 333 PRO   B CD  1 
ATOM   2077 N N   . THR   B 1 42  ? 38.674  -57.266 7.340  1.00 85.80  ? 334 THR   B N   1 
ATOM   2078 C CA  . THR   B 1 42  ? 38.812  -58.312 6.337  1.00 96.07  ? 334 THR   B CA  1 
ATOM   2079 C C   . THR   B 1 42  ? 37.537  -59.107 6.100  1.00 89.51  ? 334 THR   B C   1 
ATOM   2080 O O   . THR   B 1 42  ? 37.344  -59.621 4.997  1.00 88.23  ? 334 THR   B O   1 
ATOM   2081 C CB  . THR   B 1 42  ? 39.933  -59.282 6.733  1.00 95.73  ? 334 THR   B CB  1 
ATOM   2082 O OG1 . THR   B 1 42  ? 39.449  -60.196 7.725  1.00 91.91  ? 334 THR   B OG1 1 
ATOM   2083 C CG2 . THR   B 1 42  ? 41.121  -58.515 7.297  1.00 93.16  ? 334 THR   B CG2 1 
ATOM   2084 N N   . ARG   B 1 43  ? 36.665  -59.226 7.104  1.00 89.25  ? 335 ARG   B N   1 
ATOM   2085 C CA  . ARG   B 1 43  ? 35.409  -59.937 6.925  1.00 93.66  ? 335 ARG   B CA  1 
ATOM   2086 C C   . ARG   B 1 43  ? 34.392  -59.048 6.209  1.00 97.01  ? 335 ARG   B C   1 
ATOM   2087 O O   . ARG   B 1 43  ? 34.468  -57.819 6.289  1.00 98.66  ? 335 ARG   B O   1 
ATOM   2088 C CB  . ARG   B 1 43  ? 34.852  -60.384 8.273  1.00 97.76  ? 335 ARG   B CB  1 
ATOM   2089 N N   . PRO   B 1 44  ? 33.433  -59.647 5.499  1.00 94.40  ? 336 PRO   B N   1 
ATOM   2090 C CA  . PRO   B 1 44  ? 32.493  -58.842 4.708  1.00 90.96  ? 336 PRO   B CA  1 
ATOM   2091 C C   . PRO   B 1 44  ? 31.626  -57.942 5.576  1.00 90.84  ? 336 PRO   B C   1 
ATOM   2092 O O   . PRO   B 1 44  ? 31.334  -58.244 6.735  1.00 93.69  ? 336 PRO   B O   1 
ATOM   2093 C CB  . PRO   B 1 44  ? 31.647  -59.896 3.982  1.00 94.48  ? 336 PRO   B CB  1 
ATOM   2094 C CG  . PRO   B 1 44  ? 31.809  -61.143 4.788  1.00 99.50  ? 336 PRO   B CG  1 
ATOM   2095 C CD  . PRO   B 1 44  ? 33.208  -61.091 5.314  1.00 104.41 ? 336 PRO   B CD  1 
ATOM   2096 N N   . PHE   B 1 45  ? 31.217  -56.820 4.990  1.00 87.51  ? 337 PHE   B N   1 
ATOM   2097 C CA  . PHE   B 1 45  ? 30.328  -55.878 5.652  1.00 86.12  ? 337 PHE   B CA  1 
ATOM   2098 C C   . PHE   B 1 45  ? 28.876  -56.302 5.468  1.00 88.28  ? 337 PHE   B C   1 
ATOM   2099 O O   . PHE   B 1 45  ? 28.518  -56.961 4.487  1.00 90.41  ? 337 PHE   B O   1 
ATOM   2100 C CB  . PHE   B 1 45  ? 30.540  -54.469 5.094  1.00 78.05  ? 337 PHE   B CB  1 
ATOM   2101 C CG  . PHE   B 1 45  ? 29.903  -53.385 5.915  1.00 73.70  ? 337 PHE   B CG  1 
ATOM   2102 C CD1 . PHE   B 1 45  ? 30.252  -53.205 7.243  1.00 73.80  ? 337 PHE   B CD1 1 
ATOM   2103 C CD2 . PHE   B 1 45  ? 28.958  -52.540 5.355  1.00 67.98  ? 337 PHE   B CD2 1 
ATOM   2104 C CE1 . PHE   B 1 45  ? 29.668  -52.206 7.998  1.00 68.40  ? 337 PHE   B CE1 1 
ATOM   2105 C CE2 . PHE   B 1 45  ? 28.371  -51.539 6.105  1.00 71.76  ? 337 PHE   B CE2 1 
ATOM   2106 C CZ  . PHE   B 1 45  ? 28.726  -51.371 7.428  1.00 72.29  ? 337 PHE   B CZ  1 
ATOM   2107 N N   . SER   B 1 46  ? 28.035  -55.918 6.426  1.00 88.22  ? 338 SER   B N   1 
ATOM   2108 C CA  . SER   B 1 46  ? 26.628  -56.287 6.381  1.00 88.75  ? 338 SER   B CA  1 
ATOM   2109 C C   . SER   B 1 46  ? 25.822  -55.304 7.215  1.00 83.85  ? 338 SER   B C   1 
ATOM   2110 O O   . SER   B 1 46  ? 26.344  -54.679 8.142  1.00 83.82  ? 338 SER   B O   1 
ATOM   2111 C CB  . SER   B 1 46  ? 26.407  -57.718 6.885  1.00 87.54  ? 338 SER   B CB  1 
ATOM   2112 O OG  . SER   B 1 46  ? 25.026  -57.999 7.028  1.00 85.28  ? 338 SER   B OG  1 
ATOM   2113 N N   . GLU   B 1 47  ? 24.537  -55.180 6.874  1.00 79.68  ? 339 GLU   B N   1 
ATOM   2114 C CA  . GLU   B 1 47  ? 23.650  -54.283 7.605  1.00 77.35  ? 339 GLU   B CA  1 
ATOM   2115 C C   . GLU   B 1 47  ? 23.067  -54.943 8.848  1.00 79.25  ? 339 GLU   B C   1 
ATOM   2116 O O   . GLU   B 1 47  ? 22.716  -54.245 9.806  1.00 69.02  ? 339 GLU   B O   1 
ATOM   2117 C CB  . GLU   B 1 47  ? 22.523  -53.800 6.692  1.00 79.85  ? 339 GLU   B CB  1 
ATOM   2118 N N   . ALA   B 1 48  ? 22.953  -56.274 8.852  1.00 84.84  ? 340 ALA   B N   1 
ATOM   2119 C CA  . ALA   B 1 48  ? 22.441  -56.967 10.029 1.00 85.45  ? 340 ALA   B CA  1 
ATOM   2120 C C   . ALA   B 1 48  ? 23.380  -56.820 11.220 1.00 90.81  ? 340 ALA   B C   1 
ATOM   2121 O O   . ALA   B 1 48  ? 22.927  -56.828 12.370 1.00 87.39  ? 340 ALA   B O   1 
ATOM   2122 C CB  . ALA   B 1 48  ? 22.212  -58.445 9.712  1.00 78.52  ? 340 ALA   B CB  1 
ATOM   2123 N N   . SER   B 1 49  ? 24.679  -56.682 10.968 1.00 84.29  ? 341 SER   B N   1 
ATOM   2124 C CA  . SER   B 1 49  ? 25.669  -56.501 12.019 1.00 77.93  ? 341 SER   B CA  1 
ATOM   2125 C C   . SER   B 1 49  ? 25.970  -55.034 12.290 1.00 73.38  ? 341 SER   B C   1 
ATOM   2126 O O   . SER   B 1 49  ? 26.929  -54.733 13.007 1.00 75.25  ? 341 SER   B O   1 
ATOM   2127 C CB  . SER   B 1 49  ? 26.962  -57.234 11.655 1.00 84.85  ? 341 SER   B CB  1 
ATOM   2128 O OG  . SER   B 1 49  ? 27.393  -56.886 10.350 1.00 85.42  ? 341 SER   B OG  1 
ATOM   2129 N N   . MET   B 1 50  ? 25.176  -54.116 11.739 1.00 71.75  ? 342 MET   B N   1 
ATOM   2130 C CA  . MET   B 1 50  ? 25.512  -52.703 11.856 1.00 62.05  ? 342 MET   B CA  1 
ATOM   2131 C C   . MET   B 1 50  ? 25.090  -52.120 13.201 1.00 49.35  ? 342 MET   B C   1 
ATOM   2132 O O   . MET   B 1 50  ? 25.742  -51.197 13.695 1.00 54.74  ? 342 MET   B O   1 
ATOM   2133 C CB  . MET   B 1 50  ? 24.895  -51.922 10.690 1.00 72.20  ? 342 MET   B CB  1 
ATOM   2134 C CG  . MET   B 1 50  ? 25.732  -50.721 10.249 1.00 68.82  ? 342 MET   B CG  1 
ATOM   2135 S SD  . MET   B 1 50  ? 24.985  -49.674 8.976  1.00 80.47  ? 342 MET   B SD  1 
ATOM   2136 C CE  . MET   B 1 50  ? 23.263  -49.666 9.461  1.00 66.07  ? 342 MET   B CE  1 
ATOM   2137 N N   . MET   B 1 51  ? 24.027  -52.642 13.817 1.00 51.54  ? 343 MET   B N   1 
ATOM   2138 C CA  . MET   B 1 51  ? 23.680  -52.199 15.166 1.00 52.64  ? 343 MET   B CA  1 
ATOM   2139 C C   . MET   B 1 51  ? 24.664  -52.738 16.191 1.00 55.97  ? 343 MET   B C   1 
ATOM   2140 O O   . MET   B 1 51  ? 25.007  -52.042 17.155 1.00 58.01  ? 343 MET   B O   1 
ATOM   2141 C CB  . MET   B 1 51  ? 22.259  -52.630 15.517 1.00 49.25  ? 343 MET   B CB  1 
ATOM   2142 C CG  . MET   B 1 51  ? 21.396  -52.687 14.302 1.00 75.46  ? 343 MET   B CG  1 
ATOM   2143 S SD  . MET   B 1 51  ? 21.183  -51.015 13.697 1.00 82.90  ? 343 MET   B SD  1 
ATOM   2144 C CE  . MET   B 1 51  ? 21.527  -51.336 11.980 1.00 72.61  ? 343 MET   B CE  1 
ATOM   2145 N N   . GLY   B 1 52  ? 25.104  -53.984 16.014 1.00 44.47  ? 344 GLY   B N   1 
ATOM   2146 C CA  . GLY   B 1 52  ? 26.098  -54.539 16.914 1.00 35.50  ? 344 GLY   B CA  1 
ATOM   2147 C C   . GLY   B 1 52  ? 27.373  -53.721 16.940 1.00 34.00  ? 344 GLY   B C   1 
ATOM   2148 O O   . GLY   B 1 52  ? 27.954  -53.493 18.003 1.00 48.94  ? 344 GLY   B O   1 
ATOM   2149 N N   . LEU   B 1 53  ? 27.818  -53.256 15.771 1.00 33.88  ? 345 LEU   B N   1 
ATOM   2150 C CA  . LEU   B 1 53  ? 29.008  -52.413 15.714 1.00 38.44  ? 345 LEU   B CA  1 
ATOM   2151 C C   . LEU   B 1 53  ? 28.754  -51.055 16.354 1.00 35.03  ? 345 LEU   B C   1 
ATOM   2152 O O   . LEU   B 1 53  ? 29.622  -50.518 17.052 1.00 30.62  ? 345 LEU   B O   1 
ATOM   2153 C CB  . LEU   B 1 53  ? 29.457  -52.241 14.264 1.00 38.83  ? 345 LEU   B CB  1 
ATOM   2154 C CG  . LEU   B 1 53  ? 30.206  -53.424 13.654 1.00 50.41  ? 345 LEU   B CG  1 
ATOM   2155 C CD1 . LEU   B 1 53  ? 30.562  -53.132 12.206 1.00 53.70  ? 345 LEU   B CD1 1 
ATOM   2156 C CD2 . LEU   B 1 53  ? 31.445  -53.748 14.473 1.00 46.94  ? 345 LEU   B CD2 1 
ATOM   2157 N N   . LEU   B 1 54  ? 27.569  -50.484 16.131 1.00 35.54  ? 346 LEU   B N   1 
ATOM   2158 C CA  . LEU   B 1 54  ? 27.268  -49.161 16.666 1.00 35.95  ? 346 LEU   B CA  1 
ATOM   2159 C C   . LEU   B 1 54  ? 26.906  -49.209 18.144 1.00 25.92  ? 346 LEU   B C   1 
ATOM   2160 O O   . LEU   B 1 54  ? 27.164  -48.242 18.869 1.00 35.41  ? 346 LEU   B O   1 
ATOM   2161 C CB  . LEU   B 1 54  ? 26.145  -48.517 15.854 1.00 32.04  ? 346 LEU   B CB  1 
ATOM   2162 C CG  . LEU   B 1 54  ? 26.548  -48.272 14.398 1.00 40.02  ? 346 LEU   B CG  1 
ATOM   2163 C CD1 . LEU   B 1 54  ? 25.360  -47.863 13.541 1.00 36.33  ? 346 LEU   B CD1 1 
ATOM   2164 C CD2 . LEU   B 1 54  ? 27.660  -47.243 14.321 1.00 35.08  ? 346 LEU   B CD2 1 
ATOM   2165 N N   . THR   B 1 55  ? 26.315  -50.312 18.608 1.00 32.00  ? 347 THR   B N   1 
ATOM   2166 C CA  . THR   B 1 55  ? 26.086  -50.479 20.039 1.00 38.86  ? 347 THR   B CA  1 
ATOM   2167 C C   . THR   B 1 55  ? 27.401  -50.720 20.772 1.00 35.31  ? 347 THR   B C   1 
ATOM   2168 O O   . THR   B 1 55  ? 27.654  -50.125 21.826 1.00 28.41  ? 347 THR   B O   1 
ATOM   2169 C CB  . THR   B 1 55  ? 25.111  -51.631 20.287 1.00 38.64  ? 347 THR   B CB  1 
ATOM   2170 O OG1 . THR   B 1 55  ? 23.806  -51.265 19.821 1.00 45.14  ? 347 THR   B OG1 1 
ATOM   2171 C CG2 . THR   B 1 55  ? 25.040  -51.969 21.770 1.00 35.29  ? 347 THR   B CG2 1 
ATOM   2172 N N   . ASN   B 1 56  ? 28.254  -51.587 20.220 1.00 27.16  ? 348 ASN   B N   1 
ATOM   2173 C CA  . ASN   B 1 56  ? 29.554  -51.845 20.831 1.00 30.13  ? 348 ASN   B CA  1 
ATOM   2174 C C   . ASN   B 1 56  ? 30.407  -50.584 20.873 1.00 26.19  ? 348 ASN   B C   1 
ATOM   2175 O O   . ASN   B 1 56  ? 31.082  -50.315 21.872 1.00 34.11  ? 348 ASN   B O   1 
ATOM   2176 C CB  . ASN   B 1 56  ? 30.279  -52.957 20.071 1.00 31.33  ? 348 ASN   B CB  1 
ATOM   2177 C CG  . ASN   B 1 56  ? 31.617  -53.313 20.690 1.00 46.69  ? 348 ASN   B CG  1 
ATOM   2178 O OD1 . ASN   B 1 56  ? 32.608  -52.606 20.504 1.00 40.06  ? 348 ASN   B OD1 1 
ATOM   2179 N ND2 . ASN   B 1 56  ? 31.652  -54.417 21.427 1.00 43.54  ? 348 ASN   B ND2 1 
ATOM   2180 N N   . LEU   B 1 57  ? 30.389  -49.798 19.794 1.00 26.58  ? 349 LEU   B N   1 
ATOM   2181 C CA  . LEU   B 1 57  ? 31.169  -48.565 19.767 1.00 28.55  ? 349 LEU   B CA  1 
ATOM   2182 C C   . LEU   B 1 57  ? 30.645  -47.558 20.781 1.00 28.07  ? 349 LEU   B C   1 
ATOM   2183 O O   . LEU   B 1 57  ? 31.429  -46.889 21.464 1.00 26.60  ? 349 LEU   B O   1 
ATOM   2184 C CB  . LEU   B 1 57  ? 31.155  -47.968 18.361 1.00 31.81  ? 349 LEU   B CB  1 
ATOM   2185 C CG  . LEU   B 1 57  ? 31.835  -46.610 18.191 1.00 31.72  ? 349 LEU   B CG  1 
ATOM   2186 C CD1 . LEU   B 1 57  ? 33.326  -46.719 18.473 1.00 23.35  ? 349 LEU   B CD1 1 
ATOM   2187 C CD2 . LEU   B 1 57  ? 31.583  -46.059 16.795 1.00 32.90  ? 349 LEU   B CD2 1 
ATOM   2188 N N   . ALA   B 1 58  ? 29.320  -47.439 20.897 1.00 26.19  ? 350 ALA   B N   1 
ATOM   2189 C CA  . ALA   B 1 58  ? 28.743  -46.499 21.851 1.00 24.80  ? 350 ALA   B CA  1 
ATOM   2190 C C   . ALA   B 1 58  ? 29.059  -46.902 23.285 1.00 27.72  ? 350 ALA   B C   1 
ATOM   2191 O O   . ALA   B 1 58  ? 29.331  -46.041 24.131 1.00 24.24  ? 350 ALA   B O   1 
ATOM   2192 C CB  . ALA   B 1 58  ? 27.233  -46.402 21.641 1.00 24.23  ? 350 ALA   B CB  1 
ATOM   2193 N N   . ASP   B 1 59  ? 29.030  -48.205 23.577 1.00 20.36  ? 351 ASP   B N   1 
ATOM   2194 C CA  . ASP   B 1 59  ? 29.336  -48.671 24.926 1.00 25.48  ? 351 ASP   B CA  1 
ATOM   2195 C C   . ASP   B 1 59  ? 30.771  -48.336 25.310 1.00 31.05  ? 351 ASP   B C   1 
ATOM   2196 O O   . ASP   B 1 59  ? 31.043  -47.951 26.454 1.00 31.12  ? 351 ASP   B O   1 
ATOM   2197 C CB  . ASP   B 1 59  ? 29.093  -50.176 25.027 1.00 25.16  ? 351 ASP   B CB  1 
ATOM   2198 C CG  . ASP   B 1 59  ? 27.626  -50.536 24.929 1.00 31.43  ? 351 ASP   B CG  1 
ATOM   2199 O OD1 . ASP   B 1 59  ? 26.794  -49.612 24.843 1.00 37.60  ? 351 ASP   B OD1 1 
ATOM   2200 O OD2 . ASP   B 1 59  ? 27.303  -51.741 24.944 1.00 31.14  ? 351 ASP   B OD2 1 
ATOM   2201 N N   . ARG   B 1 60  ? 31.702  -48.470 24.364 1.00 28.63  ? 352 ARG   B N   1 
ATOM   2202 C CA  . ARG   B 1 60  ? 33.098  -48.166 24.652 1.00 27.73  ? 352 ARG   B CA  1 
ATOM   2203 C C   . ARG   B 1 60  ? 33.337  -46.666 24.748 1.00 22.77  ? 352 ARG   B C   1 
ATOM   2204 O O   . ARG   B 1 60  ? 34.181  -46.224 25.536 1.00 26.72  ? 352 ARG   B O   1 
ATOM   2205 C CB  . ARG   B 1 60  ? 33.994  -48.789 23.583 1.00 36.28  ? 352 ARG   B CB  1 
ATOM   2206 C CG  . ARG   B 1 60  ? 34.050  -50.304 23.655 1.00 30.84  ? 352 ARG   B CG  1 
ATOM   2207 C CD  . ARG   B 1 60  ? 35.070  -50.873 22.691 1.00 31.01  ? 352 ARG   B CD  1 
ATOM   2208 N NE  . ARG   B 1 60  ? 34.548  -50.960 21.332 1.00 37.98  ? 352 ARG   B NE  1 
ATOM   2209 C CZ  . ARG   B 1 60  ? 34.999  -50.248 20.309 1.00 28.18  ? 352 ARG   B CZ  1 
ATOM   2210 N NH1 . ARG   B 1 60  ? 35.993  -49.387 20.451 1.00 36.25  ? 352 ARG   B NH1 1 
ATOM   2211 N NH2 . ARG   B 1 60  ? 34.440  -50.405 19.113 1.00 38.25  ? 352 ARG   B NH2 1 
ATOM   2212 N N   . GLU   B 1 61  ? 32.610  -45.870 23.961 1.00 31.16  ? 353 GLU   B N   1 
ATOM   2213 C CA  . GLU   B 1 61  ? 32.721  -44.420 24.075 1.00 27.17  ? 353 GLU   B CA  1 
ATOM   2214 C C   . GLU   B 1 61  ? 32.171  -43.917 25.401 1.00 31.39  ? 353 GLU   B C   1 
ATOM   2215 O O   . GLU   B 1 61  ? 32.620  -42.879 25.903 1.00 25.71  ? 353 GLU   B O   1 
ATOM   2216 C CB  . GLU   B 1 61  ? 31.987  -43.738 22.925 1.00 28.56  ? 353 GLU   B CB  1 
ATOM   2217 C CG  . GLU   B 1 61  ? 32.717  -43.756 21.602 1.00 27.26  ? 353 GLU   B CG  1 
ATOM   2218 C CD  . GLU   B 1 61  ? 32.034  -42.880 20.575 1.00 32.92  ? 353 GLU   B CD  1 
ATOM   2219 O OE1 . GLU   B 1 61  ? 30.984  -43.298 20.049 1.00 28.39  ? 353 GLU   B OE1 1 
ATOM   2220 O OE2 . GLU   B 1 61  ? 32.541  -41.772 20.301 1.00 38.49  ? 353 GLU   B OE2 1 
ATOM   2221 N N   . LEU   B 1 62  ? 31.194  -44.628 25.971 1.00 23.56  ? 354 LEU   B N   1 
ATOM   2222 C CA  . LEU   B 1 62  ? 30.594  -44.195 27.228 1.00 29.45  ? 354 LEU   B CA  1 
ATOM   2223 C C   . LEU   B 1 62  ? 31.630  -44.130 28.340 1.00 29.13  ? 354 LEU   B C   1 
ATOM   2224 O O   . LEU   B 1 62  ? 31.580  -43.237 29.193 1.00 23.48  ? 354 LEU   B O   1 
ATOM   2225 C CB  . LEU   B 1 62  ? 29.454  -45.137 27.612 1.00 30.87  ? 354 LEU   B CB  1 
ATOM   2226 C CG  . LEU   B 1 62  ? 28.395  -44.595 28.572 1.00 32.40  ? 354 LEU   B CG  1 
ATOM   2227 C CD1 . LEU   B 1 62  ? 27.804  -43.301 28.042 1.00 27.41  ? 354 LEU   B CD1 1 
ATOM   2228 C CD2 . LEU   B 1 62  ? 27.308  -45.634 28.801 1.00 40.69  ? 354 LEU   B CD2 1 
ATOM   2229 N N   . VAL   B 1 63  ? 32.584  -45.063 28.341 1.00 25.18  ? 355 VAL   B N   1 
ATOM   2230 C CA  . VAL   B 1 63  ? 33.611  -45.080 29.379 1.00 28.17  ? 355 VAL   B CA  1 
ATOM   2231 C C   . VAL   B 1 63  ? 34.469  -43.823 29.299 1.00 30.28  ? 355 VAL   B C   1 
ATOM   2232 O O   . VAL   B 1 63  ? 34.693  -43.135 30.302 1.00 27.91  ? 355 VAL   B O   1 
ATOM   2233 C CB  . VAL   B 1 63  ? 34.467  -46.353 29.261 1.00 27.03  ? 355 VAL   B CB  1 
ATOM   2234 C CG1 . VAL   B 1 63  ? 35.396  -46.470 30.452 1.00 34.06  ? 355 VAL   B CG1 1 
ATOM   2235 C CG2 . VAL   B 1 63  ? 33.576  -47.579 29.137 1.00 32.25  ? 355 VAL   B CG2 1 
ATOM   2236 N N   . HIS   B 1 64  ? 34.964  -43.508 28.100 1.00 27.31  ? 356 HIS   B N   1 
ATOM   2237 C CA  . HIS   B 1 64  ? 35.774  -42.310 27.922 1.00 29.57  ? 356 HIS   B CA  1 
ATOM   2238 C C   . HIS   B 1 64  ? 34.963  -41.038 28.125 1.00 25.71  ? 356 HIS   B C   1 
ATOM   2239 O O   . HIS   B 1 64  ? 35.539  -39.997 28.458 1.00 26.25  ? 356 HIS   B O   1 
ATOM   2240 C CB  . HIS   B 1 64  ? 36.419  -42.320 26.537 1.00 22.18  ? 356 HIS   B CB  1 
ATOM   2241 C CG  . HIS   B 1 64  ? 37.377  -43.451 26.330 1.00 24.49  ? 356 HIS   B CG  1 
ATOM   2242 N ND1 . HIS   B 1 64  ? 38.692  -43.399 26.741 1.00 27.25  ? 356 HIS   B ND1 1 
ATOM   2243 C CD2 . HIS   B 1 64  ? 37.208  -44.670 25.766 1.00 24.90  ? 356 HIS   B CD2 1 
ATOM   2244 C CE1 . HIS   B 1 64  ? 39.293  -44.534 26.431 1.00 29.26  ? 356 HIS   B CE1 1 
ATOM   2245 N NE2 . HIS   B 1 64  ? 38.414  -45.323 25.839 1.00 27.83  ? 356 HIS   B NE2 1 
ATOM   2246 N N   . MET   B 1 65  ? 33.641  -41.100 27.937 1.00 24.83  ? 357 MET   B N   1 
ATOM   2247 C CA  . MET   B 1 65  ? 32.792  -39.964 28.278 1.00 27.54  ? 357 MET   B CA  1 
ATOM   2248 C C   . MET   B 1 65  ? 32.829  -39.680 29.772 1.00 25.38  ? 357 MET   B C   1 
ATOM   2249 O O   . MET   B 1 65  ? 32.760  -38.519 30.194 1.00 24.20  ? 357 MET   B O   1 
ATOM   2250 C CB  . MET   B 1 65  ? 31.356  -40.224 27.828 1.00 23.83  ? 357 MET   B CB  1 
ATOM   2251 C CG  . MET   B 1 65  ? 30.487  -38.983 27.807 1.00 20.30  ? 357 MET   B CG  1 
ATOM   2252 S SD  . MET   B 1 65  ? 28.750  -39.391 27.581 1.00 26.57  ? 357 MET   B SD  1 
ATOM   2253 C CE  . MET   B 1 65  ? 28.769  -39.919 25.872 1.00 17.40  ? 357 MET   B CE  1 
ATOM   2254 N N   . ILE   B 1 66  ? 32.932  -40.731 30.589 1.00 29.65  ? 358 ILE   B N   1 
ATOM   2255 C CA  . ILE   B 1 66  ? 33.035  -40.548 32.034 1.00 25.33  ? 358 ILE   B CA  1 
ATOM   2256 C C   . ILE   B 1 66  ? 34.326  -39.821 32.383 1.00 31.21  ? 358 ILE   B C   1 
ATOM   2257 O O   . ILE   B 1 66  ? 34.333  -38.881 33.187 1.00 30.04  ? 358 ILE   B O   1 
ATOM   2258 C CB  . ILE   B 1 66  ? 32.941  -41.903 32.759 1.00 36.12  ? 358 ILE   B CB  1 
ATOM   2259 C CG1 . ILE   B 1 66  ? 31.795  -42.745 32.197 1.00 39.27  ? 358 ILE   B CG1 1 
ATOM   2260 C CG2 . ILE   B 1 66  ? 32.762  -41.701 34.245 1.00 38.90  ? 358 ILE   B CG2 1 
ATOM   2261 C CD1 . ILE   B 1 66  ? 30.447  -42.077 32.280 1.00 34.09  ? 358 ILE   B CD1 1 
ATOM   2262 N N   . ASN   B 1 67  ? 35.441  -40.250 31.783 1.00 33.08  ? 359 ASN   B N   1 
ATOM   2263 C CA  . ASN   B 1 67  ? 36.717  -39.585 32.020 1.00 31.01  ? 359 ASN   B CA  1 
ATOM   2264 C C   . ASN   B 1 67  ? 36.662  -38.125 31.592 1.00 31.53  ? 359 ASN   B C   1 
ATOM   2265 O O   . ASN   B 1 67  ? 37.227  -37.251 32.259 1.00 41.20  ? 359 ASN   B O   1 
ATOM   2266 C CB  . ASN   B 1 67  ? 37.837  -40.311 31.275 1.00 31.58  ? 359 ASN   B CB  1 
ATOM   2267 C CG  . ASN   B 1 67  ? 38.137  -41.675 31.855 1.00 44.63  ? 359 ASN   B CG  1 
ATOM   2268 O OD1 . ASN   B 1 67  ? 37.625  -42.040 32.914 1.00 41.30  ? 359 ASN   B OD1 1 
ATOM   2269 N ND2 . ASN   B 1 67  ? 38.971  -42.442 31.161 1.00 49.52  ? 359 ASN   B ND2 1 
ATOM   2270 N N   . TRP   B 1 68  ? 35.986  -37.845 30.476 1.00 33.14  ? 360 TRP   B N   1 
ATOM   2271 C CA  . TRP   B 1 68  ? 35.852  -36.467 30.016 1.00 27.32  ? 360 TRP   B CA  1 
ATOM   2272 C C   . TRP   B 1 68  ? 34.994  -35.648 30.971 1.00 34.07  ? 360 TRP   B C   1 
ATOM   2273 O O   . TRP   B 1 68  ? 35.314  -34.489 31.262 1.00 30.53  ? 360 TRP   B O   1 
ATOM   2274 C CB  . TRP   B 1 68  ? 35.260  -36.443 28.606 1.00 25.56  ? 360 TRP   B CB  1 
ATOM   2275 C CG  . TRP   B 1 68  ? 34.675  -35.117 28.218 1.00 29.53  ? 360 TRP   B CG  1 
ATOM   2276 C CD1 . TRP   B 1 68  ? 35.341  -34.049 27.691 1.00 29.03  ? 360 TRP   B CD1 1 
ATOM   2277 C CD2 . TRP   B 1 68  ? 33.302  -34.721 28.323 1.00 26.83  ? 360 TRP   B CD2 1 
ATOM   2278 N NE1 . TRP   B 1 68  ? 34.469  -33.012 27.463 1.00 26.18  ? 360 TRP   B NE1 1 
ATOM   2279 C CE2 . TRP   B 1 68  ? 33.211  -33.400 27.843 1.00 27.04  ? 360 TRP   B CE2 1 
ATOM   2280 C CE3 . TRP   B 1 68  ? 32.141  -35.355 28.778 1.00 27.06  ? 360 TRP   B CE3 1 
ATOM   2281 C CZ2 . TRP   B 1 68  ? 32.006  -32.701 27.804 1.00 27.58  ? 360 TRP   B CZ2 1 
ATOM   2282 C CZ3 . TRP   B 1 68  ? 30.946  -34.659 28.738 1.00 19.99  ? 360 TRP   B CZ3 1 
ATOM   2283 C CH2 . TRP   B 1 68  ? 30.888  -33.347 28.255 1.00 23.76  ? 360 TRP   B CH2 1 
ATOM   2284 N N   . ALA   B 1 69  ? 33.903  -36.233 31.471 1.00 26.98  ? 361 ALA   B N   1 
ATOM   2285 C CA  . ALA   B 1 69  ? 33.016  -35.497 32.366 1.00 27.64  ? 361 ALA   B CA  1 
ATOM   2286 C C   . ALA   B 1 69  ? 33.715  -35.151 33.675 1.00 39.18  ? 361 ALA   B C   1 
ATOM   2287 O O   . ALA   B 1 69  ? 33.501  -34.068 34.233 1.00 35.56  ? 361 ALA   B O   1 
ATOM   2288 C CB  . ALA   B 1 69  ? 31.747  -36.306 32.632 1.00 26.34  ? 361 ALA   B CB  1 
ATOM   2289 N N   . LYS   B 1 70  ? 34.560  -36.057 34.175 1.00 36.12  ? 362 LYS   B N   1 
ATOM   2290 C CA  . LYS   B 1 70  ? 35.301  -35.791 35.405 1.00 41.92  ? 362 LYS   B CA  1 
ATOM   2291 C C   . LYS   B 1 70  ? 36.189  -34.560 35.278 1.00 40.98  ? 362 LYS   B C   1 
ATOM   2292 O O   . LYS   B 1 70  ? 36.489  -33.906 36.283 1.00 45.33  ? 362 LYS   B O   1 
ATOM   2293 C CB  . LYS   B 1 70  ? 36.147  -37.006 35.785 1.00 41.80  ? 362 LYS   B CB  1 
ATOM   2294 C CG  . LYS   B 1 70  ? 35.382  -38.130 36.468 1.00 46.48  ? 362 LYS   B CG  1 
ATOM   2295 C CD  . LYS   B 1 70  ? 34.862  -37.686 37.821 1.00 51.63  ? 362 LYS   B CD  1 
ATOM   2296 C CE  . LYS   B 1 70  ? 34.967  -38.795 38.856 1.00 61.80  ? 362 LYS   B CE  1 
ATOM   2297 N NZ  . LYS   B 1 70  ? 33.857  -38.732 39.853 1.00 58.74  ? 362 LYS   B NZ  1 
ATOM   2298 N N   . ARG   B 1 71  ? 36.613  -34.228 34.061 1.00 39.80  ? 363 ARG   B N   1 
ATOM   2299 C CA  . ARG   B 1 71  ? 37.519  -33.115 33.823 1.00 40.76  ? 363 ARG   B CA  1 
ATOM   2300 C C   . ARG   B 1 71  ? 36.807  -31.849 33.367 1.00 40.73  ? 363 ARG   B C   1 
ATOM   2301 O O   . ARG   B 1 71  ? 37.467  -30.826 33.160 1.00 41.55  ? 363 ARG   B O   1 
ATOM   2302 C CB  . ARG   B 1 71  ? 38.579  -33.514 32.794 1.00 45.67  ? 363 ARG   B CB  1 
ATOM   2303 C CG  . ARG   B 1 71  ? 39.353  -34.769 33.160 1.00 42.47  ? 363 ARG   B CG  1 
ATOM   2304 C CD  . ARG   B 1 71  ? 40.387  -35.100 32.101 1.00 47.59  ? 363 ARG   B CD  1 
ATOM   2305 N NE  . ARG   B 1 71  ? 41.314  -33.996 31.887 1.00 57.44  ? 363 ARG   B NE  1 
ATOM   2306 C CZ  . ARG   B 1 71  ? 42.364  -34.045 31.080 1.00 57.82  ? 363 ARG   B CZ  1 
ATOM   2307 N NH1 . ARG   B 1 71  ? 42.654  -35.134 30.387 1.00 55.78  ? 363 ARG   B NH1 1 
ATOM   2308 N NH2 . ARG   B 1 71  ? 43.144  -32.974 30.964 1.00 45.79  ? 363 ARG   B NH2 1 
ATOM   2309 N N   . VAL   B 1 72  ? 35.490  -31.890 33.192 1.00 37.95  ? 364 VAL   B N   1 
ATOM   2310 C CA  . VAL   B 1 72  ? 34.718  -30.675 32.948 1.00 34.73  ? 364 VAL   B CA  1 
ATOM   2311 C C   . VAL   B 1 72  ? 34.741  -29.868 34.240 1.00 37.03  ? 364 VAL   B C   1 
ATOM   2312 O O   . VAL   B 1 72  ? 34.282  -30.361 35.280 1.00 41.11  ? 364 VAL   B O   1 
ATOM   2313 C CB  . VAL   B 1 72  ? 33.282  -30.991 32.501 1.00 31.12  ? 364 VAL   B CB  1 
ATOM   2314 C CG1 . VAL   B 1 72  ? 32.427  -29.732 32.530 1.00 36.23  ? 364 VAL   B CG1 1 
ATOM   2315 C CG2 . VAL   B 1 72  ? 33.282  -31.606 31.109 1.00 28.52  ? 364 VAL   B CG2 1 
ATOM   2316 N N   . PRO   B 1 73  ? 35.280  -28.650 34.229 1.00 37.08  ? 365 PRO   B N   1 
ATOM   2317 C CA  . PRO   B 1 73  ? 35.436  -27.897 35.483 1.00 35.07  ? 365 PRO   B CA  1 
ATOM   2318 C C   . PRO   B 1 73  ? 34.101  -27.689 36.184 1.00 37.34  ? 365 PRO   B C   1 
ATOM   2319 O O   . PRO   B 1 73  ? 33.125  -27.237 35.582 1.00 34.08  ? 365 PRO   B O   1 
ATOM   2320 C CB  . PRO   B 1 73  ? 36.054  -26.566 35.038 1.00 38.78  ? 365 PRO   B CB  1 
ATOM   2321 C CG  . PRO   B 1 73  ? 36.496  -26.748 33.639 1.00 43.82  ? 365 PRO   B CG  1 
ATOM   2322 C CD  . PRO   B 1 73  ? 35.896  -27.984 33.069 1.00 35.18  ? 365 PRO   B CD  1 
ATOM   2323 N N   . GLY   B 1 74  ? 34.067  -28.037 37.471 1.00 35.24  ? 366 GLY   B N   1 
ATOM   2324 C CA  . GLY   B 1 74  ? 32.869  -27.935 38.271 1.00 39.08  ? 366 GLY   B CA  1 
ATOM   2325 C C   . GLY   B 1 74  ? 32.045  -29.201 38.353 1.00 41.20  ? 366 GLY   B C   1 
ATOM   2326 O O   . GLY   B 1 74  ? 31.123  -29.269 39.176 1.00 36.80  ? 366 GLY   B O   1 
ATOM   2327 N N   . PHE   B 1 75  ? 32.348  -30.209 37.533 1.00 38.11  ? 367 PHE   B N   1 
ATOM   2328 C CA  . PHE   B 1 75  ? 31.545  -31.427 37.529 1.00 48.80  ? 367 PHE   B CA  1 
ATOM   2329 C C   . PHE   B 1 75  ? 31.771  -32.244 38.795 1.00 35.67  ? 367 PHE   B C   1 
ATOM   2330 O O   . PHE   B 1 75  ? 30.814  -32.713 39.421 1.00 35.49  ? 367 PHE   B O   1 
ATOM   2331 C CB  . PHE   B 1 75  ? 31.862  -32.259 36.287 1.00 39.73  ? 367 PHE   B CB  1 
ATOM   2332 C CG  . PHE   B 1 75  ? 30.960  -33.446 36.104 1.00 36.49  ? 367 PHE   B CG  1 
ATOM   2333 C CD1 . PHE   B 1 75  ? 29.678  -33.289 35.601 1.00 25.51  ? 367 PHE   B CD1 1 
ATOM   2334 C CD2 . PHE   B 1 75  ? 31.391  -34.720 36.438 1.00 32.42  ? 367 PHE   B CD2 1 
ATOM   2335 C CE1 . PHE   B 1 75  ? 28.845  -34.379 35.430 1.00 31.04  ? 367 PHE   B CE1 1 
ATOM   2336 C CE2 . PHE   B 1 75  ? 30.563  -35.814 36.269 1.00 42.01  ? 367 PHE   B CE2 1 
ATOM   2337 C CZ  . PHE   B 1 75  ? 29.288  -35.643 35.765 1.00 29.15  ? 367 PHE   B CZ  1 
ATOM   2338 N N   . VAL   B 1 76  ? 33.035  -32.429 39.191 1.00 46.17  ? 368 VAL   B N   1 
ATOM   2339 C CA  . VAL   B 1 76  ? 33.336  -33.223 40.378 1.00 49.84  ? 368 VAL   B CA  1 
ATOM   2340 C C   . VAL   B 1 76  ? 32.897  -32.541 41.661 1.00 44.90  ? 368 VAL   B C   1 
ATOM   2341 O O   . VAL   B 1 76  ? 32.861  -33.186 42.715 1.00 47.66  ? 368 VAL   B O   1 
ATOM   2342 C CB  . VAL   B 1 76  ? 34.840  -33.546 40.488 1.00 57.34  ? 368 VAL   B CB  1 
ATOM   2343 C CG1 . VAL   B 1 76  ? 35.232  -34.627 39.490 1.00 55.16  ? 368 VAL   B CG1 1 
ATOM   2344 C CG2 . VAL   B 1 76  ? 35.680  -32.287 40.323 1.00 39.97  ? 368 VAL   B CG2 1 
ATOM   2345 N N   . ASP   B 1 77  ? 32.573  -31.247 41.602 1.00 39.34  ? 369 ASP   B N   1 
ATOM   2346 C CA  . ASP   B 1 77  ? 32.047  -30.557 42.771 1.00 43.02  ? 369 ASP   B CA  1 
ATOM   2347 C C   . ASP   B 1 77  ? 30.658  -31.050 43.145 1.00 41.95  ? 369 ASP   B C   1 
ATOM   2348 O O   . ASP   B 1 77  ? 30.259  -30.923 44.307 1.00 45.21  ? 369 ASP   B O   1 
ATOM   2349 C CB  . ASP   B 1 77  ? 32.018  -29.049 42.521 1.00 46.39  ? 369 ASP   B CB  1 
ATOM   2350 C CG  . ASP   B 1 77  ? 33.403  -28.466 42.322 1.00 55.04  ? 369 ASP   B CG  1 
ATOM   2351 O OD1 . ASP   B 1 77  ? 34.340  -28.903 43.022 1.00 57.16  ? 369 ASP   B OD1 1 
ATOM   2352 O OD2 . ASP   B 1 77  ? 33.554  -27.571 41.464 1.00 58.74  ? 369 ASP   B OD2 1 
ATOM   2353 N N   . LEU   B 1 78  ? 29.921  -31.612 42.192 1.00 42.72  ? 370 LEU   B N   1 
ATOM   2354 C CA  . LEU   B 1 78  ? 28.606  -32.164 42.462 1.00 43.73  ? 370 LEU   B CA  1 
ATOM   2355 C C   . LEU   B 1 78  ? 28.727  -33.500 43.187 1.00 40.48  ? 370 LEU   B C   1 
ATOM   2356 O O   . LEU   B 1 78  ? 29.773  -34.155 43.176 1.00 42.54  ? 370 LEU   B O   1 
ATOM   2357 C CB  . LEU   B 1 78  ? 27.825  -32.350 41.161 1.00 43.50  ? 370 LEU   B CB  1 
ATOM   2358 C CG  . LEU   B 1 78  ? 27.768  -31.140 40.227 1.00 36.83  ? 370 LEU   B CG  1 
ATOM   2359 C CD1 . LEU   B 1 78  ? 27.359  -31.562 38.824 1.00 37.25  ? 370 LEU   B CD1 1 
ATOM   2360 C CD2 . LEU   B 1 78  ? 26.816  -30.092 40.777 1.00 40.55  ? 370 LEU   B CD2 1 
ATOM   2361 N N   . THR   B 1 79  ? 27.632  -33.902 43.826 1.00 42.19  ? 371 THR   B N   1 
ATOM   2362 C CA  . THR   B 1 79  ? 27.583  -35.213 44.450 1.00 44.36  ? 371 THR   B CA  1 
ATOM   2363 C C   . THR   B 1 79  ? 27.589  -36.304 43.383 1.00 45.93  ? 371 THR   B C   1 
ATOM   2364 O O   . THR   B 1 79  ? 27.288  -36.066 42.209 1.00 37.69  ? 371 THR   B O   1 
ATOM   2365 C CB  . THR   B 1 79  ? 26.340  -35.347 45.331 1.00 54.80  ? 371 THR   B CB  1 
ATOM   2366 O OG1 . THR   B 1 79  ? 25.197  -35.623 44.511 1.00 55.01  ? 371 THR   B OG1 1 
ATOM   2367 C CG2 . THR   B 1 79  ? 26.099  -34.064 46.112 1.00 49.83  ? 371 THR   B CG2 1 
ATOM   2368 N N   . LEU   B 1 80  ? 27.948  -37.518 43.807 1.00 43.30  ? 372 LEU   B N   1 
ATOM   2369 C CA  . LEU   B 1 80  ? 27.953  -38.648 42.883 1.00 39.75  ? 372 LEU   B CA  1 
ATOM   2370 C C   . LEU   B 1 80  ? 26.561  -38.900 42.319 1.00 43.69  ? 372 LEU   B C   1 
ATOM   2371 O O   . LEU   B 1 80  ? 26.415  -39.295 41.156 1.00 42.69  ? 372 LEU   B O   1 
ATOM   2372 C CB  . LEU   B 1 80  ? 28.482  -39.898 43.583 1.00 38.86  ? 372 LEU   B CB  1 
ATOM   2373 C CG  . LEU   B 1 80  ? 29.924  -40.280 43.252 1.00 47.14  ? 372 LEU   B CG  1 
ATOM   2374 C CD1 . LEU   B 1 80  ? 30.315  -41.562 43.966 1.00 44.38  ? 372 LEU   B CD1 1 
ATOM   2375 C CD2 . LEU   B 1 80  ? 30.109  -40.420 41.754 1.00 34.86  ? 372 LEU   B CD2 1 
ATOM   2376 N N   . HIS   B 1 81  ? 25.526  -38.673 43.132 1.00 41.29  ? 373 HIS   B N   1 
ATOM   2377 C CA  . HIS   B 1 81  ? 24.155  -38.805 42.651 1.00 53.69  ? 373 HIS   B CA  1 
ATOM   2378 C C   . HIS   B 1 81  ? 23.876  -37.838 41.508 1.00 43.19  ? 373 HIS   B C   1 
ATOM   2379 O O   . HIS   B 1 81  ? 23.241  -38.207 40.512 1.00 46.74  ? 373 HIS   B O   1 
ATOM   2380 C CB  . HIS   B 1 81  ? 23.179  -38.572 43.805 1.00 40.82  ? 373 HIS   B CB  1 
ATOM   2381 C CG  . HIS   B 1 81  ? 21.740  -38.730 43.424 1.00 53.97  ? 373 HIS   B CG  1 
ATOM   2382 N ND1 . HIS   B 1 81  ? 21.131  -39.960 43.308 1.00 62.68  ? 373 HIS   B ND1 1 
ATOM   2383 C CD2 . HIS   B 1 81  ? 20.790  -37.810 43.136 1.00 48.86  ? 373 HIS   B CD2 1 
ATOM   2384 C CE1 . HIS   B 1 81  ? 19.866  -39.792 42.964 1.00 59.82  ? 373 HIS   B CE1 1 
ATOM   2385 N NE2 . HIS   B 1 81  ? 19.634  -38.496 42.852 1.00 58.21  ? 373 HIS   B NE2 1 
ATOM   2386 N N   . ASP   B 1 82  ? 24.347  -36.596 41.629 1.00 39.85  ? 374 ASP   B N   1 
ATOM   2387 C CA  . ASP   B 1 82  ? 24.120  -35.607 40.580 1.00 39.68  ? 374 ASP   B CA  1 
ATOM   2388 C C   . ASP   B 1 82  ? 25.023  -35.847 39.377 1.00 36.19  ? 374 ASP   B C   1 
ATOM   2389 O O   . ASP   B 1 82  ? 24.605  -35.634 38.234 1.00 39.45  ? 374 ASP   B O   1 
ATOM   2390 C CB  . ASP   B 1 82  ? 24.330  -34.198 41.134 1.00 33.74  ? 374 ASP   B CB  1 
ATOM   2391 C CG  . ASP   B 1 82  ? 23.320  -33.839 42.206 1.00 47.41  ? 374 ASP   B CG  1 
ATOM   2392 O OD1 . ASP   B 1 82  ? 22.338  -34.592 42.375 1.00 48.76  ? 374 ASP   B OD1 1 
ATOM   2393 O OD2 . ASP   B 1 82  ? 23.509  -32.805 42.880 1.00 50.12  ? 374 ASP   B OD2 1 
ATOM   2394 N N   . GLN   B 1 83  ? 26.263  -36.284 39.613 1.00 37.72  ? 375 GLN   B N   1 
ATOM   2395 C CA  . GLN   B 1 83  ? 27.153  -36.611 38.503 1.00 27.51  ? 375 GLN   B CA  1 
ATOM   2396 C C   . GLN   B 1 83  ? 26.577  -37.735 37.654 1.00 34.74  ? 375 GLN   B C   1 
ATOM   2397 O O   . GLN   B 1 83  ? 26.614  -37.675 36.419 1.00 35.95  ? 375 GLN   B O   1 
ATOM   2398 C CB  . GLN   B 1 83  ? 28.533  -37.004 39.030 1.00 29.86  ? 375 GLN   B CB  1 
ATOM   2399 C CG  . GLN   B 1 83  ? 29.310  -35.875 39.677 1.00 36.24  ? 375 GLN   B CG  1 
ATOM   2400 C CD  . GLN   B 1 83  ? 30.693  -36.311 40.116 1.00 37.93  ? 375 GLN   B CD  1 
ATOM   2401 O OE1 . GLN   B 1 83  ? 31.294  -37.201 39.514 1.00 41.25  ? 375 GLN   B OE1 1 
ATOM   2402 N NE2 . GLN   B 1 83  ? 31.202  -35.692 41.174 1.00 44.99  ? 375 GLN   B NE2 1 
ATOM   2403 N N   . VAL   B 1 84  ? 26.038  -38.770 38.301 1.00 37.36  ? 376 VAL   B N   1 
ATOM   2404 C CA  . VAL   B 1 84  ? 25.466  -39.895 37.570 1.00 30.27  ? 376 VAL   B CA  1 
ATOM   2405 C C   . VAL   B 1 84  ? 24.183  -39.476 36.866 1.00 28.04  ? 376 VAL   B C   1 
ATOM   2406 O O   . VAL   B 1 84  ? 23.929  -39.870 35.720 1.00 32.43  ? 376 VAL   B O   1 
ATOM   2407 C CB  . VAL   B 1 84  ? 25.233  -41.079 38.526 1.00 32.16  ? 376 VAL   B CB  1 
ATOM   2408 C CG1 . VAL   B 1 84  ? 24.278  -42.092 37.912 1.00 30.84  ? 376 VAL   B CG1 1 
ATOM   2409 C CG2 . VAL   B 1 84  ? 26.556  -41.732 38.891 1.00 48.06  ? 376 VAL   B CG2 1 
ATOM   2410 N N   . HIS   B 1 85  ? 23.360  -38.662 37.530 1.00 37.01  ? 377 HIS   B N   1 
ATOM   2411 C CA  . HIS   B 1 85  ? 22.093  -38.246 36.937 1.00 30.48  ? 377 HIS   B CA  1 
ATOM   2412 C C   . HIS   B 1 85  ? 22.315  -37.377 35.705 1.00 30.79  ? 377 HIS   B C   1 
ATOM   2413 O O   . HIS   B 1 85  ? 21.569  -37.482 34.724 1.00 32.33  ? 377 HIS   B O   1 
ATOM   2414 C CB  . HIS   B 1 85  ? 21.249  -37.508 37.974 1.00 35.73  ? 377 HIS   B CB  1 
ATOM   2415 C CG  . HIS   B 1 85  ? 20.070  -36.794 37.392 1.00 43.95  ? 377 HIS   B CG  1 
ATOM   2416 N ND1 . HIS   B 1 85  ? 20.106  -35.464 37.037 1.00 54.33  ? 377 HIS   B ND1 1 
ATOM   2417 C CD2 . HIS   B 1 85  ? 18.822  -37.229 37.097 1.00 52.09  ? 377 HIS   B CD2 1 
ATOM   2418 C CE1 . HIS   B 1 85  ? 18.931  -35.109 36.551 1.00 45.62  ? 377 HIS   B CE1 1 
ATOM   2419 N NE2 . HIS   B 1 85  ? 18.133  -36.161 36.577 1.00 51.13  ? 377 HIS   B NE2 1 
ATOM   2420 N N   . LEU   B 1 86  ? 23.333  -36.514 35.733 1.00 28.79  ? 378 LEU   B N   1 
ATOM   2421 C CA  . LEU   B 1 86  ? 23.633  -35.700 34.559 1.00 25.95  ? 378 LEU   B CA  1 
ATOM   2422 C C   . LEU   B 1 86  ? 24.178  -36.554 33.422 1.00 32.60  ? 378 LEU   B C   1 
ATOM   2423 O O   . LEU   B 1 86  ? 23.813  -36.353 32.258 1.00 28.92  ? 378 LEU   B O   1 
ATOM   2424 C CB  . LEU   B 1 86  ? 24.623  -34.594 34.922 1.00 24.59  ? 378 LEU   B CB  1 
ATOM   2425 C CG  . LEU   B 1 86  ? 24.104  -33.480 35.831 1.00 28.58  ? 378 LEU   B CG  1 
ATOM   2426 C CD1 . LEU   B 1 86  ? 25.159  -32.400 36.000 1.00 38.06  ? 378 LEU   B CD1 1 
ATOM   2427 C CD2 . LEU   B 1 86  ? 22.816  -32.892 35.279 1.00 30.74  ? 378 LEU   B CD2 1 
ATOM   2428 N N   . LEU   B 1 87  ? 25.052  -37.512 33.740 1.00 28.66  ? 379 LEU   B N   1 
ATOM   2429 C CA  . LEU   B 1 87  ? 25.600  -38.388 32.710 1.00 28.95  ? 379 LEU   B CA  1 
ATOM   2430 C C   . LEU   B 1 87  ? 24.518  -39.274 32.106 1.00 29.12  ? 379 LEU   B C   1 
ATOM   2431 O O   . LEU   B 1 87  ? 24.481  -39.472 30.886 1.00 29.80  ? 379 LEU   B O   1 
ATOM   2432 C CB  . LEU   B 1 87  ? 26.727  -39.239 33.293 1.00 29.42  ? 379 LEU   B CB  1 
ATOM   2433 C CG  . LEU   B 1 87  ? 28.095  -38.566 33.409 1.00 43.75  ? 379 LEU   B CG  1 
ATOM   2434 C CD1 . LEU   B 1 87  ? 29.018  -39.381 34.302 1.00 32.78  ? 379 LEU   B CD1 1 
ATOM   2435 C CD2 . LEU   B 1 87  ? 28.711  -38.371 32.033 1.00 35.02  ? 379 LEU   B CD2 1 
ATOM   2436 N N   . GLU   B 1 88  ? 23.627  -39.813 32.943 1.00 29.23  ? 380 GLU   B N   1 
ATOM   2437 C CA  . GLU   B 1 88  ? 22.560  -40.670 32.436 1.00 35.87  ? 380 GLU   B CA  1 
ATOM   2438 C C   . GLU   B 1 88  ? 21.601  -39.899 31.539 1.00 27.34  ? 380 GLU   B C   1 
ATOM   2439 O O   . GLU   B 1 88  ? 21.015  -40.473 30.615 1.00 30.63  ? 380 GLU   B O   1 
ATOM   2440 C CB  . GLU   B 1 88  ? 21.806  -41.310 33.604 1.00 37.05  ? 380 GLU   B CB  1 
ATOM   2441 C CG  . GLU   B 1 88  ? 20.659  -42.221 33.192 1.00 44.43  ? 380 GLU   B CG  1 
ATOM   2442 C CD  . GLU   B 1 88  ? 20.001  -42.902 34.375 1.00 55.95  ? 380 GLU   B CD  1 
ATOM   2443 O OE1 . GLU   B 1 88  ? 20.689  -43.131 35.391 1.00 58.50  ? 380 GLU   B OE1 1 
ATOM   2444 O OE2 . GLU   B 1 88  ? 18.793  -43.210 34.288 1.00 67.14  ? 380 GLU   B OE2 1 
ATOM   2445 N N   . SER   B 1 89  ? 21.440  -38.600 31.782 1.00 28.45  ? 381 SER   B N   1 
ATOM   2446 C CA  . SER   B 1 89  ? 20.501  -37.790 31.021 1.00 25.65  ? 381 SER   B CA  1 
ATOM   2447 C C   . SER   B 1 89  ? 21.110  -37.173 29.769 1.00 22.81  ? 381 SER   B C   1 
ATOM   2448 O O   . SER   B 1 89  ? 20.363  -36.785 28.864 1.00 25.97  ? 381 SER   B O   1 
ATOM   2449 C CB  . SER   B 1 89  ? 19.933  -36.676 31.907 1.00 31.30  ? 381 SER   B CB  1 
ATOM   2450 O OG  . SER   B 1 89  ? 19.174  -35.753 31.145 1.00 53.75  ? 381 SER   B OG  1 
ATOM   2451 N N   . ALA   B 1 90  ? 22.438  -37.081 29.686 1.00 22.82  ? 382 ALA   B N   1 
ATOM   2452 C CA  . ALA   B 1 90  ? 23.094  -36.365 28.602 1.00 22.97  ? 382 ALA   B CA  1 
ATOM   2453 C C   . ALA   B 1 90  ? 23.939  -37.245 27.692 1.00 17.96  ? 382 ALA   B C   1 
ATOM   2454 O O   . ALA   B 1 90  ? 24.436  -36.748 26.676 1.00 25.03  ? 382 ALA   B O   1 
ATOM   2455 C CB  . ALA   B 1 90  ? 23.984  -35.248 29.170 1.00 21.41  ? 382 ALA   B CB  1 
ATOM   2456 N N   . TRP   B 1 91  ? 24.101  -38.532 28.011 1.00 20.60  ? 383 TRP   B N   1 
ATOM   2457 C CA  . TRP   B 1 91  ? 25.107  -39.342 27.328 1.00 24.13  ? 383 TRP   B CA  1 
ATOM   2458 C C   . TRP   B 1 91  ? 24.798  -39.502 25.843 1.00 24.67  ? 383 TRP   B C   1 
ATOM   2459 O O   . TRP   B 1 91  ? 25.713  -39.496 25.011 1.00 24.49  ? 383 TRP   B O   1 
ATOM   2460 C CB  . TRP   B 1 91  ? 25.234  -40.707 28.007 1.00 18.53  ? 383 TRP   B CB  1 
ATOM   2461 C CG  . TRP   B 1 91  ? 24.057  -41.604 27.794 1.00 29.71  ? 383 TRP   B CG  1 
ATOM   2462 C CD1 . TRP   B 1 91  ? 22.942  -41.689 28.572 1.00 20.72  ? 383 TRP   B CD1 1 
ATOM   2463 C CD2 . TRP   B 1 91  ? 23.881  -42.551 26.734 1.00 25.63  ? 383 TRP   B CD2 1 
ATOM   2464 N NE1 . TRP   B 1 91  ? 22.078  -42.625 28.060 1.00 28.06  ? 383 TRP   B NE1 1 
ATOM   2465 C CE2 . TRP   B 1 91  ? 22.632  -43.170 26.931 1.00 30.89  ? 383 TRP   B CE2 1 
ATOM   2466 C CE3 . TRP   B 1 91  ? 24.657  -42.932 25.634 1.00 24.68  ? 383 TRP   B CE3 1 
ATOM   2467 C CZ2 . TRP   B 1 91  ? 22.140  -44.150 26.072 1.00 31.23  ? 383 TRP   B CZ2 1 
ATOM   2468 C CZ3 . TRP   B 1 91  ? 24.167  -43.905 24.783 1.00 24.95  ? 383 TRP   B CZ3 1 
ATOM   2469 C CH2 . TRP   B 1 91  ? 22.921  -44.503 25.006 1.00 26.43  ? 383 TRP   B CH2 1 
ATOM   2470 N N   . LEU   B 1 92  ? 23.520  -39.643 25.485 1.00 25.78  ? 384 LEU   B N   1 
ATOM   2471 C CA  . LEU   B 1 92  ? 23.183  -39.818 24.075 1.00 24.98  ? 384 LEU   B CA  1 
ATOM   2472 C C   . LEU   B 1 92  ? 23.395  -38.527 23.295 1.00 25.25  ? 384 LEU   B C   1 
ATOM   2473 O O   . LEU   B 1 92  ? 23.849  -38.558 22.145 1.00 25.40  ? 384 LEU   B O   1 
ATOM   2474 C CB  . LEU   B 1 92  ? 21.742  -40.309 23.928 1.00 26.62  ? 384 LEU   B CB  1 
ATOM   2475 C CG  . LEU   B 1 92  ? 21.351  -40.738 22.510 1.00 33.09  ? 384 LEU   B CG  1 
ATOM   2476 C CD1 . LEU   B 1 92  ? 22.307  -41.805 21.992 1.00 25.04  ? 384 LEU   B CD1 1 
ATOM   2477 C CD2 . LEU   B 1 92  ? 19.914  -41.237 22.462 1.00 29.33  ? 384 LEU   B CD2 1 
ATOM   2478 N N   . GLU   B 1 93  ? 23.078  -37.384 23.906 1.00 21.87  ? 385 GLU   B N   1 
ATOM   2479 C CA  . GLU   B 1 93  ? 23.331  -36.100 23.259 1.00 26.17  ? 385 GLU   B CA  1 
ATOM   2480 C C   . GLU   B 1 93  ? 24.821  -35.888 23.022 1.00 29.17  ? 385 GLU   B C   1 
ATOM   2481 O O   . GLU   B 1 93  ? 25.220  -35.303 22.008 1.00 23.25  ? 385 GLU   B O   1 
ATOM   2482 C CB  . GLU   B 1 93  ? 22.764  -34.966 24.111 1.00 18.12  ? 385 GLU   B CB  1 
ATOM   2483 C CG  . GLU   B 1 93  ? 21.266  -34.773 23.990 1.00 21.63  ? 385 GLU   B CG  1 
ATOM   2484 C CD  . GLU   B 1 93  ? 20.698  -33.955 25.130 1.00 29.41  ? 385 GLU   B CD  1 
ATOM   2485 O OE1 . GLU   B 1 93  ? 20.646  -34.473 26.266 1.00 37.23  ? 385 GLU   B OE1 1 
ATOM   2486 O OE2 . GLU   B 1 93  ? 20.302  -32.797 24.894 1.00 28.95  ? 385 GLU   B OE2 1 
ATOM   2487 N N   . ILE   B 1 94  ? 25.659  -36.357 23.950 1.00 21.55  ? 386 ILE   B N   1 
ATOM   2488 C CA  . ILE   B 1 94  ? 27.100  -36.164 23.819 1.00 20.30  ? 386 ILE   B CA  1 
ATOM   2489 C C   . ILE   B 1 94  ? 27.660  -37.045 22.709 1.00 23.78  ? 386 ILE   B C   1 
ATOM   2490 O O   . ILE   B 1 94  ? 28.510  -36.610 21.923 1.00 25.85  ? 386 ILE   B O   1 
ATOM   2491 C CB  . ILE   B 1 94  ? 27.795  -36.432 25.166 1.00 21.82  ? 386 ILE   B CB  1 
ATOM   2492 C CG1 . ILE   B 1 94  ? 27.301  -35.441 26.222 1.00 19.01  ? 386 ILE   B CG1 1 
ATOM   2493 C CG2 . ILE   B 1 94  ? 29.308  -36.353 25.016 1.00 20.29  ? 386 ILE   B CG2 1 
ATOM   2494 C CD1 . ILE   B 1 94  ? 27.925  -34.072 26.109 1.00 33.52  ? 386 ILE   B CD1 1 
ATOM   2495 N N   . LEU   B 1 95  ? 27.199  -38.297 22.630 1.00 18.84  ? 387 LEU   B N   1 
ATOM   2496 C CA  . LEU   B 1 95  ? 27.603  -39.166 21.528 1.00 22.76  ? 387 LEU   B CA  1 
ATOM   2497 C C   . LEU   B 1 95  ? 27.198  -38.575 20.187 1.00 22.23  ? 387 LEU   B C   1 
ATOM   2498 O O   . LEU   B 1 95  ? 27.956  -38.642 19.213 1.00 26.50  ? 387 LEU   B O   1 
ATOM   2499 C CB  . LEU   B 1 95  ? 26.985  -40.554 21.697 1.00 21.57  ? 387 LEU   B CB  1 
ATOM   2500 C CG  . LEU   B 1 95  ? 27.551  -41.469 22.778 1.00 26.24  ? 387 LEU   B CG  1 
ATOM   2501 C CD1 . LEU   B 1 95  ? 26.914  -42.842 22.675 1.00 26.69  ? 387 LEU   B CD1 1 
ATOM   2502 C CD2 . LEU   B 1 95  ? 29.060  -41.565 22.644 1.00 29.00  ? 387 LEU   B CD2 1 
ATOM   2503 N N   . MET   B 1 96  ? 26.005  -37.984 20.124 1.00 17.78  ? 388 MET   B N   1 
ATOM   2504 C CA  . MET   B 1 96  ? 25.485  -37.465 18.864 1.00 23.58  ? 388 MET   B CA  1 
ATOM   2505 C C   . MET   B 1 96  ? 26.276  -36.248 18.400 1.00 25.00  ? 388 MET   B C   1 
ATOM   2506 O O   . MET   B 1 96  ? 26.723  -36.189 17.248 1.00 26.17  ? 388 MET   B O   1 
ATOM   2507 C CB  . MET   B 1 96  ? 24.005  -37.126 19.026 1.00 21.40  ? 388 MET   B CB  1 
ATOM   2508 C CG  . MET   B 1 96  ? 23.099  -38.350 19.051 1.00 23.22  ? 388 MET   B CG  1 
ATOM   2509 S SD  . MET   B 1 96  ? 21.355  -37.903 19.091 1.00 26.74  ? 388 MET   B SD  1 
ATOM   2510 C CE  . MET   B 1 96  ? 20.580  -39.424 18.557 1.00 24.32  ? 388 MET   B CE  1 
ATOM   2511 N N   . ILE   B 1 97  ? 26.467  -35.265 19.285 1.00 20.50  ? 389 ILE   B N   1 
ATOM   2512 C CA  . ILE   B 1 97  ? 27.186  -34.057 18.889 1.00 22.14  ? 389 ILE   B CA  1 
ATOM   2513 C C   . ILE   B 1 97  ? 28.653  -34.365 18.614 1.00 21.48  ? 389 ILE   B C   1 
ATOM   2514 O O   . ILE   B 1 97  ? 29.285  -33.709 17.777 1.00 25.87  ? 389 ILE   B O   1 
ATOM   2515 C CB  . ILE   B 1 97  ? 27.015  -32.951 19.951 1.00 23.93  ? 389 ILE   B CB  1 
ATOM   2516 C CG1 . ILE   B 1 97  ? 27.439  -31.594 19.380 1.00 27.21  ? 389 ILE   B CG1 1 
ATOM   2517 C CG2 . ILE   B 1 97  ? 27.789  -33.283 21.220 1.00 23.19  ? 389 ILE   B CG2 1 
ATOM   2518 C CD1 . ILE   B 1 97  ? 27.443  -30.470 20.394 1.00 17.83  ? 389 ILE   B CD1 1 
ATOM   2519 N N   . GLY   B 1 98  ? 29.219  -35.366 19.292 1.00 23.29  ? 390 GLY   B N   1 
ATOM   2520 C CA  . GLY   B 1 98  ? 30.559  -35.809 18.945 1.00 21.60  ? 390 GLY   B CA  1 
ATOM   2521 C C   . GLY   B 1 98  ? 30.608  -36.451 17.572 1.00 23.61  ? 390 GLY   B C   1 
ATOM   2522 O O   . GLY   B 1 98  ? 31.551  -36.232 16.807 1.00 24.71  ? 390 GLY   B O   1 
ATOM   2523 N N   . LEU   B 1 99  ? 29.590  -37.249 17.242 1.00 24.58  ? 391 LEU   B N   1 
ATOM   2524 C CA  . LEU   B 1 99  ? 29.481  -37.809 15.899 1.00 28.82  ? 391 LEU   B CA  1 
ATOM   2525 C C   . LEU   B 1 99  ? 29.318  -36.706 14.863 1.00 26.65  ? 391 LEU   B C   1 
ATOM   2526 O O   . LEU   B 1 99  ? 29.981  -36.711 13.819 1.00 33.07  ? 391 LEU   B O   1 
ATOM   2527 C CB  . LEU   B 1 99  ? 28.303  -38.780 15.835 1.00 25.83  ? 391 LEU   B CB  1 
ATOM   2528 C CG  . LEU   B 1 99  ? 27.916  -39.285 14.445 1.00 24.76  ? 391 LEU   B CG  1 
ATOM   2529 C CD1 . LEU   B 1 99  ? 29.090  -39.979 13.769 1.00 22.39  ? 391 LEU   B CD1 1 
ATOM   2530 C CD2 . LEU   B 1 99  ? 26.709  -40.200 14.532 1.00 27.51  ? 391 LEU   B CD2 1 
ATOM   2531 N N   . VAL   B 1 100 ? 28.428  -35.751 15.138 1.00 29.73  ? 392 VAL   B N   1 
ATOM   2532 C CA  . VAL   B 1 100 ? 28.198  -34.640 14.219 1.00 23.04  ? 392 VAL   B CA  1 
ATOM   2533 C C   . VAL   B 1 100 ? 29.480  -33.839 14.017 1.00 28.08  ? 392 VAL   B C   1 
ATOM   2534 O O   . VAL   B 1 100 ? 29.766  -33.363 12.912 1.00 25.94  ? 392 VAL   B O   1 
ATOM   2535 C CB  . VAL   B 1 100 ? 27.047  -33.761 14.746 1.00 24.50  ? 392 VAL   B CB  1 
ATOM   2536 C CG1 . VAL   B 1 100 ? 26.983  -32.447 14.002 1.00 23.21  ? 392 VAL   B CG1 1 
ATOM   2537 C CG2 . VAL   B 1 100 ? 25.722  -34.502 14.637 1.00 20.61  ? 392 VAL   B CG2 1 
ATOM   2538 N N   . TRP   B 1 101 ? 30.282  -33.699 15.074 1.00 31.06  ? 393 TRP   B N   1 
ATOM   2539 C CA  . TRP   B 1 101 ? 31.498  -32.898 14.986 1.00 26.34  ? 393 TRP   B CA  1 
ATOM   2540 C C   . TRP   B 1 101 ? 32.521  -33.538 14.053 1.00 26.76  ? 393 TRP   B C   1 
ATOM   2541 O O   . TRP   B 1 101 ? 33.064  -32.872 13.164 1.00 31.52  ? 393 TRP   B O   1 
ATOM   2542 C CB  . TRP   B 1 101 ? 32.091  -32.691 16.380 1.00 28.86  ? 393 TRP   B CB  1 
ATOM   2543 C CG  . TRP   B 1 101 ? 33.486  -32.146 16.368 1.00 30.74  ? 393 TRP   B CG  1 
ATOM   2544 C CD1 . TRP   B 1 101 ? 34.630  -32.815 16.691 1.00 24.98  ? 393 TRP   B CD1 1 
ATOM   2545 C CD2 . TRP   B 1 101 ? 33.886  -30.818 16.009 1.00 25.62  ? 393 TRP   B CD2 1 
ATOM   2546 N NE1 . TRP   B 1 101 ? 35.717  -31.985 16.560 1.00 38.53  ? 393 TRP   B NE1 1 
ATOM   2547 C CE2 . TRP   B 1 101 ? 35.287  -30.753 16.142 1.00 29.81  ? 393 TRP   B CE2 1 
ATOM   2548 C CE3 . TRP   B 1 101 ? 33.195  -29.677 15.590 1.00 31.46  ? 393 TRP   B CE3 1 
ATOM   2549 C CZ2 . TRP   B 1 101 ? 36.009  -29.594 15.870 1.00 34.43  ? 393 TRP   B CZ2 1 
ATOM   2550 C CZ3 . TRP   B 1 101 ? 33.914  -28.527 15.320 1.00 31.89  ? 393 TRP   B CZ3 1 
ATOM   2551 C CH2 . TRP   B 1 101 ? 35.306  -28.494 15.462 1.00 35.63  ? 393 TRP   B CH2 1 
ATOM   2552 N N   . ARG   B 1 102 ? 32.733  -34.843 14.188 1.00 28.35  ? 394 ARG   B N   1 
ATOM   2553 C CA  . ARG   B 1 102 ? 33.735  -35.560 13.361 1.00 37.70  ? 394 ARG   B CA  1 
ATOM   2554 C C   . ARG   B 1 102 ? 33.207  -35.852 11.945 1.00 32.40  ? 394 ARG   B C   1 
ATOM   2555 O O   . ARG   B 1 102 ? 34.011  -36.242 11.101 1.00 34.76  ? 394 ARG   B O   1 
ATOM   2556 C CB  . ARG   B 1 102 ? 34.186  -36.826 14.098 1.00 41.62  ? 394 ARG   B CB  1 
ATOM   2557 C CG  . ARG   B 1 102 ? 33.116  -37.865 14.380 1.00 36.01  ? 394 ARG   B CG  1 
ATOM   2558 C CD  . ARG   B 1 102 ? 33.818  -38.929 15.200 1.00 28.64  ? 394 ARG   B CD  1 
ATOM   2559 N NE  . ARG   B 1 102 ? 32.980  -40.072 15.509 1.00 32.87  ? 394 ARG   B NE  1 
ATOM   2560 C CZ  . ARG   B 1 102 ? 32.308  -40.219 16.640 1.00 26.13  ? 394 ARG   B CZ  1 
ATOM   2561 N NH1 . ARG   B 1 102 ? 32.453  -39.339 17.612 1.00 29.26  ? 394 ARG   B NH1 1 
ATOM   2562 N NH2 . ARG   B 1 102 ? 31.500  -41.250 16.795 1.00 23.75  ? 394 ARG   B NH2 1 
ATOM   2563 N N   . SER   B 1 103 ? 31.908  -35.684 11.712 1.00 33.31  ? 395 SER   B N   1 
ATOM   2564 C CA  . SER   B 1 103 ? 31.295  -35.978 10.395 1.00 33.31  ? 395 SER   B CA  1 
ATOM   2565 C C   . SER   B 1 103 ? 31.158  -34.673 9.601  1.00 38.80  ? 395 SER   B C   1 
ATOM   2566 O O   . SER   B 1 103 ? 30.632  -34.714 8.491  1.00 43.01  ? 395 SER   B O   1 
ATOM   2567 C CB  . SER   B 1 103 ? 29.985  -36.688 10.584 1.00 27.67  ? 395 SER   B CB  1 
ATOM   2568 O OG  . SER   B 1 103 ? 30.118  -37.792 11.458 1.00 26.31  ? 395 SER   B OG  1 
ATOM   2569 N N   . MET   B 1 104 ? 31.670  -33.574 10.141 1.00 41.84  ? 396 MET   B N   1 
ATOM   2570 C CA  . MET   B 1 104 ? 31.524  -32.236 9.513  1.00 49.22  ? 396 MET   B CA  1 
ATOM   2571 C C   . MET   B 1 104 ? 32.202  -32.200 8.138  1.00 49.13  ? 396 MET   B C   1 
ATOM   2572 O O   . MET   B 1 104 ? 31.549  -31.766 7.192  1.00 44.80  ? 396 MET   B O   1 
ATOM   2573 C CB  . MET   B 1 104 ? 32.119  -31.151 10.419 1.00 44.78  ? 396 MET   B CB  1 
ATOM   2574 C CG  . MET   B 1 104 ? 31.108  -30.427 11.270 1.00 30.01  ? 396 MET   B CG  1 
ATOM   2575 S SD  . MET   B 1 104 ? 31.912  -29.151 12.260 1.00 47.01  ? 396 MET   B SD  1 
ATOM   2576 C CE  . MET   B 1 104 ? 31.932  -27.793 11.094 1.00 37.25  ? 396 MET   B CE  1 
ATOM   2577 N N   . GLU   B 1 105 ? 33.446  -32.668 8.041  1.00 30.00  ? 397 GLU   B N   1 
ATOM   2578 C CA  . GLU   B 1 105 ? 34.205  -32.592 6.767  1.00 30.00  ? 397 GLU   B CA  1 
ATOM   2579 C C   . GLU   B 1 105 ? 33.821  -33.739 5.841  1.00 30.00  ? 397 GLU   B C   1 
ATOM   2580 O O   . GLU   B 1 105 ? 34.538  -33.950 4.867  1.00 30.00  ? 397 GLU   B O   1 
ATOM   2581 C CB  . GLU   B 1 105 ? 35.707  -32.676 7.022  1.00 30.00  ? 397 GLU   B CB  1 
ATOM   2582 N N   . HIS   B 1 106 ? 32.748  -34.445 6.154  1.00 41.55  ? 398 HIS   B N   1 
ATOM   2583 C CA  . HIS   B 1 106 ? 32.296  -35.585 5.325  1.00 43.60  ? 398 HIS   B CA  1 
ATOM   2584 C C   . HIS   B 1 106 ? 30.830  -35.351 4.975  1.00 45.30  ? 398 HIS   B C   1 
ATOM   2585 O O   . HIS   B 1 106 ? 29.943  -36.108 5.388  1.00 52.40  ? 398 HIS   B O   1 
ATOM   2586 C CB  . HIS   B 1 106 ? 32.575  -36.900 6.052  1.00 48.14  ? 398 HIS   B CB  1 
ATOM   2587 C CG  . HIS   B 1 106 ? 33.997  -37.038 6.464  1.00 50.36  ? 398 HIS   B CG  1 
ATOM   2588 N ND1 . HIS   B 1 106 ? 34.923  -37.723 5.711  1.00 47.25  ? 398 HIS   B ND1 1 
ATOM   2589 C CD2 . HIS   B 1 106 ? 34.655  -36.568 7.525  1.00 54.00  ? 398 HIS   B CD2 1 
ATOM   2590 C CE1 . HIS   B 1 106 ? 36.097  -37.668 6.315  1.00 57.63  ? 398 HIS   B CE1 1 
ATOM   2591 N NE2 . HIS   B 1 106 ? 35.958  -36.972 7.418  1.00 47.56  ? 398 HIS   B NE2 1 
ATOM   2592 N N   . PRO   B 1 107 ? 30.541  -34.313 4.173  1.00 46.24  ? 399 PRO   B N   1 
ATOM   2593 C CA  . PRO   B 1 107 ? 29.165  -33.976 3.844  1.00 51.36  ? 399 PRO   B CA  1 
ATOM   2594 C C   . PRO   B 1 107 ? 28.384  -35.176 3.298  1.00 48.97  ? 399 PRO   B C   1 
ATOM   2595 O O   . PRO   B 1 107 ? 28.931  -35.907 2.511  1.00 45.91  ? 399 PRO   B O   1 
ATOM   2596 C CB  . PRO   B 1 107 ? 29.369  -32.854 2.824  1.00 50.38  ? 399 PRO   B CB  1 
ATOM   2597 C CG  . PRO   B 1 107 ? 30.668  -32.223 3.228  1.00 47.14  ? 399 PRO   B CG  1 
ATOM   2598 C CD  . PRO   B 1 107 ? 31.519  -33.425 3.547  1.00 50.52  ? 399 PRO   B CD  1 
ATOM   2599 N N   . GLY   B 1 108 ? 27.138  -35.345 3.749  1.00 45.37  ? 400 GLY   B N   1 
ATOM   2600 C CA  . GLY   B 1 108 ? 26.332  -36.476 3.342  1.00 46.19  ? 400 GLY   B CA  1 
ATOM   2601 C C   . GLY   B 1 108 ? 26.715  -37.793 3.973  1.00 44.15  ? 400 GLY   B C   1 
ATOM   2602 O O   . GLY   B 1 108 ? 26.160  -38.830 3.589  1.00 41.61  ? 400 GLY   B O   1 
ATOM   2603 N N   . LYS   B 1 109 ? 27.639  -37.790 4.930  1.00 45.43  ? 401 LYS   B N   1 
ATOM   2604 C CA  . LYS   B 1 109 ? 28.101  -39.016 5.560  1.00 42.41  ? 401 LYS   B CA  1 
ATOM   2605 C C   . LYS   B 1 109 ? 28.266  -38.789 7.056  1.00 38.38  ? 401 LYS   B C   1 
ATOM   2606 O O   . LYS   B 1 109 ? 28.405  -37.657 7.525  1.00 34.95  ? 401 LYS   B O   1 
ATOM   2607 C CB  . LYS   B 1 109 ? 29.422  -39.499 4.948  1.00 42.48  ? 401 LYS   B CB  1 
ATOM   2608 N N   . LEU   B 1 110 ? 28.247  -39.892 7.802  1.00 33.66  ? 402 LEU   B N   1 
ATOM   2609 C CA  . LEU   B 1 110 ? 28.438  -39.881 9.247  1.00 34.97  ? 402 LEU   B CA  1 
ATOM   2610 C C   . LEU   B 1 110 ? 29.662  -40.722 9.577  1.00 38.42  ? 402 LEU   B C   1 
ATOM   2611 O O   . LEU   B 1 110 ? 29.692  -41.922 9.282  1.00 32.77  ? 402 LEU   B O   1 
ATOM   2612 C CB  . LEU   B 1 110 ? 27.201  -40.417 9.971  1.00 27.93  ? 402 LEU   B CB  1 
ATOM   2613 C CG  . LEU   B 1 110 ? 25.942  -39.550 9.913  1.00 36.80  ? 402 LEU   B CG  1 
ATOM   2614 C CD1 . LEU   B 1 110 ? 24.831  -40.163 10.753 1.00 35.41  ? 402 LEU   B CD1 1 
ATOM   2615 C CD2 . LEU   B 1 110 ? 26.241  -38.129 10.370 1.00 26.65  ? 402 LEU   B CD2 1 
ATOM   2616 N N   . LEU   B 1 111 ? 30.668  -40.093 10.184 1.00 36.38  ? 403 LEU   B N   1 
ATOM   2617 C CA  . LEU   B 1 111 ? 31.913  -40.775 10.540 1.00 31.60  ? 403 LEU   B CA  1 
ATOM   2618 C C   . LEU   B 1 111 ? 31.795  -41.278 11.976 1.00 33.58  ? 403 LEU   B C   1 
ATOM   2619 O O   . LEU   B 1 111 ? 32.251  -40.649 12.934 1.00 28.41  ? 403 LEU   B O   1 
ATOM   2620 C CB  . LEU   B 1 111 ? 33.105  -39.842 10.360 1.00 32.47  ? 403 LEU   B CB  1 
ATOM   2621 C CG  . LEU   B 1 111 ? 34.502  -40.451 10.503 1.00 40.80  ? 403 LEU   B CG  1 
ATOM   2622 C CD1 . LEU   B 1 111 ? 34.954  -41.084 9.196  1.00 34.91  ? 403 LEU   B CD1 1 
ATOM   2623 C CD2 . LEU   B 1 111 ? 35.498  -39.398 10.964 1.00 39.85  ? 403 LEU   B CD2 1 
ATOM   2624 N N   . PHE   B 1 112 ? 31.151  -42.440 12.119 1.00 34.48  ? 404 PHE   B N   1 
ATOM   2625 C CA  . PHE   B 1 112 ? 31.031  -43.061 13.435 1.00 27.53  ? 404 PHE   B CA  1 
ATOM   2626 C C   . PHE   B 1 112 ? 32.402  -43.420 13.990 1.00 30.46  ? 404 PHE   B C   1 
ATOM   2627 O O   . PHE   B 1 112 ? 32.662  -43.256 15.189 1.00 37.47  ? 404 PHE   B O   1 
ATOM   2628 C CB  . PHE   B 1 112 ? 30.148  -44.306 13.351 1.00 25.29  ? 404 PHE   B CB  1 
ATOM   2629 C CG  . PHE   B 1 112 ? 28.713  -44.017 13.014 1.00 32.32  ? 404 PHE   B CG  1 
ATOM   2630 C CD1 . PHE   B 1 112 ? 28.300  -43.941 11.695 1.00 29.61  ? 404 PHE   B CD1 1 
ATOM   2631 C CD2 . PHE   B 1 112 ? 27.775  -43.825 14.015 1.00 35.96  ? 404 PHE   B CD2 1 
ATOM   2632 C CE1 . PHE   B 1 112 ? 26.980  -43.680 11.379 1.00 36.07  ? 404 PHE   B CE1 1 
ATOM   2633 C CE2 . PHE   B 1 112 ? 26.452  -43.567 13.706 1.00 28.89  ? 404 PHE   B CE2 1 
ATOM   2634 C CZ  . PHE   B 1 112 ? 26.055  -43.492 12.387 1.00 30.15  ? 404 PHE   B CZ  1 
ATOM   2635 N N   . ALA   B 1 113 ? 33.288  -43.906 13.130 1.00 34.55  ? 405 ALA   B N   1 
ATOM   2636 C CA  . ALA   B 1 113 ? 34.662  -44.233 13.475 1.00 30.68  ? 405 ALA   B CA  1 
ATOM   2637 C C   . ALA   B 1 113 ? 35.504  -44.059 12.223 1.00 31.17  ? 405 ALA   B C   1 
ATOM   2638 O O   . ALA   B 1 113 ? 34.966  -44.059 11.110 1.00 41.16  ? 405 ALA   B O   1 
ATOM   2639 C CB  . ALA   B 1 113 ? 34.779  -45.665 14.017 1.00 28.70  ? 405 ALA   B CB  1 
ATOM   2640 N N   . PRO   B 1 114 ? 36.823  -43.888 12.366 1.00 34.85  ? 406 PRO   B N   1 
ATOM   2641 C CA  . PRO   B 1 114 ? 37.666  -43.744 11.167 1.00 35.56  ? 406 PRO   B CA  1 
ATOM   2642 C C   . PRO   B 1 114 ? 37.546  -44.907 10.198 1.00 37.79  ? 406 PRO   B C   1 
ATOM   2643 O O   . PRO   B 1 114 ? 37.787  -44.729 8.996  1.00 40.41  ? 406 PRO   B O   1 
ATOM   2644 C CB  . PRO   B 1 114 ? 39.079  -43.638 11.756 1.00 36.59  ? 406 PRO   B CB  1 
ATOM   2645 C CG  . PRO   B 1 114 ? 38.852  -43.025 13.095 1.00 33.78  ? 406 PRO   B CG  1 
ATOM   2646 C CD  . PRO   B 1 114 ? 37.612  -43.717 13.598 1.00 34.20  ? 406 PRO   B CD  1 
ATOM   2647 N N   . ASN   B 1 115 ? 37.178  -46.092 10.680 1.00 38.42  ? 407 ASN   B N   1 
ATOM   2648 C CA  . ASN   B 1 115 ? 36.954  -47.252 9.829  1.00 39.35  ? 407 ASN   B CA  1 
ATOM   2649 C C   . ASN   B 1 115 ? 35.475  -47.530 9.597  1.00 38.26  ? 407 ASN   B C   1 
ATOM   2650 O O   . ASN   B 1 115 ? 35.131  -48.581 9.047  1.00 55.94  ? 407 ASN   B O   1 
ATOM   2651 C CB  . ASN   B 1 115 ? 37.630  -48.486 10.431 1.00 41.61  ? 407 ASN   B CB  1 
ATOM   2652 C CG  . ASN   B 1 115 ? 37.074  -48.851 11.796 1.00 44.43  ? 407 ASN   B CG  1 
ATOM   2653 O OD1 . ASN   B 1 115 ? 36.411  -48.045 12.447 1.00 37.01  ? 407 ASN   B OD1 1 
ATOM   2654 N ND2 . ASN   B 1 115 ? 37.344  -50.075 12.236 1.00 54.12  ? 407 ASN   B ND2 1 
ATOM   2655 N N   . LEU   B 1 116 ? 34.586  -46.608 10.001 1.00 44.14  ? 408 LEU   B N   1 
ATOM   2656 C CA  . LEU   B 1 116 ? 33.138  -46.814 9.906  1.00 37.26  ? 408 LEU   B CA  1 
ATOM   2657 C C   . LEU   B 1 116 ? 32.494  -45.503 9.446  1.00 37.18  ? 408 LEU   B C   1 
ATOM   2658 O O   . LEU   B 1 116 ? 31.931  -44.744 10.238 1.00 35.81  ? 408 LEU   B O   1 
ATOM   2659 C CB  . LEU   B 1 116 ? 32.561  -47.295 11.237 1.00 36.32  ? 408 LEU   B CB  1 
ATOM   2660 C CG  . LEU   B 1 116 ? 31.194  -47.978 11.187 1.00 40.13  ? 408 LEU   B CG  1 
ATOM   2661 C CD1 . LEU   B 1 116 ? 31.221  -49.172 10.245 1.00 41.16  ? 408 LEU   B CD1 1 
ATOM   2662 C CD2 . LEU   B 1 116 ? 30.749  -48.398 12.578 1.00 41.96  ? 408 LEU   B CD2 1 
ATOM   2663 N N   . LEU   B 1 117 ? 32.577  -45.244 8.143  1.00 40.72  ? 409 LEU   B N   1 
ATOM   2664 C CA  . LEU   B 1 117 ? 31.970  -44.077 7.516  1.00 39.93  ? 409 LEU   B CA  1 
ATOM   2665 C C   . LEU   B 1 117 ? 30.758  -44.539 6.717  1.00 44.36  ? 409 LEU   B C   1 
ATOM   2666 O O   . LEU   B 1 117 ? 30.882  -45.400 5.840  1.00 44.40  ? 409 LEU   B O   1 
ATOM   2667 C CB  . LEU   B 1 117 ? 32.974  -43.358 6.614  1.00 40.21  ? 409 LEU   B CB  1 
ATOM   2668 C CG  . LEU   B 1 117 ? 32.481  -42.126 5.852  1.00 47.66  ? 409 LEU   B CG  1 
ATOM   2669 C CD1 . LEU   B 1 117 ? 32.134  -41.003 6.814  1.00 45.49  ? 409 LEU   B CD1 1 
ATOM   2670 C CD2 . LEU   B 1 117 ? 33.524  -41.673 4.842  1.00 47.92  ? 409 LEU   B CD2 1 
ATOM   2671 N N   . LEU   B 1 118 ? 29.592  -43.970 7.020  1.00 43.23  ? 410 LEU   B N   1 
ATOM   2672 C CA  . LEU   B 1 118 ? 28.337  -44.405 6.425  1.00 44.12  ? 410 LEU   B CA  1 
ATOM   2673 C C   . LEU   B 1 118 ? 27.630  -43.228 5.769  1.00 50.02  ? 410 LEU   B C   1 
ATOM   2674 O O   . LEU   B 1 118 ? 27.753  -42.084 6.214  1.00 52.33  ? 410 LEU   B O   1 
ATOM   2675 C CB  . LEU   B 1 118 ? 27.396  -45.031 7.468  1.00 43.70  ? 410 LEU   B CB  1 
ATOM   2676 C CG  . LEU   B 1 118 ? 27.733  -46.395 8.078  1.00 50.45  ? 410 LEU   B CG  1 
ATOM   2677 C CD1 . LEU   B 1 118 ? 28.063  -47.417 6.999  1.00 48.14  ? 410 LEU   B CD1 1 
ATOM   2678 C CD2 . LEU   B 1 118 ? 28.855  -46.290 9.098  1.00 46.91  ? 410 LEU   B CD2 1 
ATOM   2679 N N   . ASP   B 1 119 ? 26.876  -43.522 4.714  1.00 53.60  ? 411 ASP   B N   1 
ATOM   2680 C CA  . ASP   B 1 119 ? 25.991  -42.558 4.079  1.00 49.01  ? 411 ASP   B CA  1 
ATOM   2681 C C   . ASP   B 1 119 ? 24.537  -42.922 4.373  1.00 49.96  ? 411 ASP   B C   1 
ATOM   2682 O O   . ASP   B 1 119 ? 24.248  -43.871 5.107  1.00 52.62  ? 411 ASP   B O   1 
ATOM   2683 C CB  . ASP   B 1 119 ? 26.288  -42.460 2.575  1.00 60.39  ? 411 ASP   B CB  1 
ATOM   2684 C CG  . ASP   B 1 119 ? 25.985  -43.745 1.805  1.00 63.86  ? 411 ASP   B CG  1 
ATOM   2685 O OD1 . ASP   B 1 119 ? 25.023  -44.470 2.135  1.00 78.18  ? 411 ASP   B OD1 1 
ATOM   2686 O OD2 . ASP   B 1 119 ? 26.734  -44.032 0.847  1.00 72.32  ? 411 ASP   B OD2 1 
ATOM   2687 N N   . ARG   B 1 120 ? 23.618  -42.150 3.785  1.00 58.84  ? 412 ARG   B N   1 
ATOM   2688 C CA  . ARG   B 1 120 ? 22.193  -42.363 4.028  1.00 53.87  ? 412 ARG   B CA  1 
ATOM   2689 C C   . ARG   B 1 120 ? 21.764  -43.782 3.685  1.00 59.07  ? 412 ARG   B C   1 
ATOM   2690 O O   . ARG   B 1 120 ? 20.967  -44.391 4.408  1.00 55.66  ? 412 ARG   B O   1 
ATOM   2691 C CB  . ARG   B 1 120 ? 21.363  -41.371 3.214  1.00 68.59  ? 412 ARG   B CB  1 
ATOM   2692 C CG  . ARG   B 1 120 ? 21.402  -39.940 3.697  1.00 62.03  ? 412 ARG   B CG  1 
ATOM   2693 C CD  . ARG   B 1 120 ? 20.342  -39.126 2.977  1.00 63.77  ? 412 ARG   B CD  1 
ATOM   2694 N NE  . ARG   B 1 120 ? 19.002  -39.460 3.446  1.00 55.63  ? 412 ARG   B NE  1 
ATOM   2695 C CZ  . ARG   B 1 120 ? 18.082  -40.070 2.710  1.00 67.46  ? 412 ARG   B CZ  1 
ATOM   2696 N NH1 . ARG   B 1 120 ? 18.329  -40.445 1.464  1.00 61.35  ? 412 ARG   B NH1 1 
ATOM   2697 N NH2 . ARG   B 1 120 ? 16.886  -40.314 3.237  1.00 58.23  ? 412 ARG   B NH2 1 
ATOM   2698 N N   . ASN   B 1 121 ? 22.286  -44.326 2.584  1.00 60.05  ? 413 ASN   B N   1 
ATOM   2699 C CA  . ASN   B 1 121 ? 21.744  -45.567 2.043  1.00 65.37  ? 413 ASN   B CA  1 
ATOM   2700 C C   . ASN   B 1 121 ? 22.038  -46.764 2.939  1.00 64.61  ? 413 ASN   B C   1 
ATOM   2701 O O   . ASN   B 1 121 ? 21.249  -47.716 2.970  1.00 78.60  ? 413 ASN   B O   1 
ATOM   2702 C CB  . ASN   B 1 121 ? 22.285  -45.792 0.633  1.00 74.30  ? 413 ASN   B CB  1 
ATOM   2703 C CG  . ASN   B 1 121 ? 21.779  -44.755 -0.351 1.00 94.05  ? 413 ASN   B CG  1 
ATOM   2704 O OD1 . ASN   B 1 121 ? 20.582  -44.473 -0.413 1.00 93.72  ? 413 ASN   B OD1 1 
ATOM   2705 N ND2 . ASN   B 1 121 ? 22.692  -44.171 -1.119 1.00 90.34  ? 413 ASN   B ND2 1 
ATOM   2706 N N   . GLN   B 1 122 ? 23.154  -46.745 3.671  1.00 60.83  ? 414 GLN   B N   1 
ATOM   2707 C CA  . GLN   B 1 122 ? 23.381  -47.791 4.661  1.00 69.73  ? 414 GLN   B CA  1 
ATOM   2708 C C   . GLN   B 1 122 ? 22.417  -47.684 5.834  1.00 65.63  ? 414 GLN   B C   1 
ATOM   2709 O O   . GLN   B 1 122 ? 22.189  -48.679 6.529  1.00 70.31  ? 414 GLN   B O   1 
ATOM   2710 C CB  . GLN   B 1 122 ? 24.824  -47.750 5.166  1.00 67.50  ? 414 GLN   B CB  1 
ATOM   2711 C CG  . GLN   B 1 122 ? 25.813  -48.501 4.285  1.00 59.70  ? 414 GLN   B CG  1 
ATOM   2712 C CD  . GLN   B 1 122 ? 26.875  -47.598 3.688  1.00 69.76  ? 414 GLN   B CD  1 
ATOM   2713 O OE1 . GLN   B 1 122 ? 26.584  -46.491 3.240  1.00 73.89  ? 414 GLN   B OE1 1 
ATOM   2714 N NE2 . GLN   B 1 122 ? 28.118  -48.070 3.679  1.00 59.02  ? 414 GLN   B NE2 1 
ATOM   2715 N N   . GLY   B 1 123 ? 21.843  -46.500 6.063  1.00 74.61  ? 415 GLY   B N   1 
ATOM   2716 C CA  . GLY   B 1 123 ? 20.864  -46.336 7.121  1.00 59.99  ? 415 GLY   B CA  1 
ATOM   2717 C C   . GLY   B 1 123 ? 19.448  -46.700 6.731  1.00 67.38  ? 415 GLY   B C   1 
ATOM   2718 O O   . GLY   B 1 123 ? 18.637  -47.012 7.609  1.00 75.00  ? 415 GLY   B O   1 
ATOM   2719 N N   . LYS   B 1 124 ? 19.131  -46.663 5.433  1.00 78.78  ? 416 LYS   B N   1 
ATOM   2720 C CA  . LYS   B 1 124 ? 17.781  -46.987 4.985  1.00 70.11  ? 416 LYS   B CA  1 
ATOM   2721 C C   . LYS   B 1 124 ? 17.437  -48.457 5.180  1.00 74.95  ? 416 LYS   B C   1 
ATOM   2722 O O   . LYS   B 1 124 ? 16.252  -48.808 5.172  1.00 74.55  ? 416 LYS   B O   1 
ATOM   2723 C CB  . LYS   B 1 124 ? 17.602  -46.618 3.512  1.00 67.95  ? 416 LYS   B CB  1 
ATOM   2724 C CG  . LYS   B 1 124 ? 18.091  -45.226 3.152  1.00 67.94  ? 416 LYS   B CG  1 
ATOM   2725 C CD  . LYS   B 1 124 ? 17.603  -44.791 1.772  1.00 66.80  ? 416 LYS   B CD  1 
ATOM   2726 C CE  . LYS   B 1 124 ? 16.333  -45.519 1.353  1.00 72.31  ? 416 LYS   B CE  1 
ATOM   2727 N N   . SER   B 1 125 ? 18.439  -49.320 5.355  1.00 87.66  ? 417 SER   B N   1 
ATOM   2728 C CA  . SER   B 1 125 ? 18.193  -50.746 5.530  1.00 92.97  ? 417 SER   B CA  1 
ATOM   2729 C C   . SER   B 1 125 ? 17.475  -51.073 6.832  1.00 97.56  ? 417 SER   B C   1 
ATOM   2730 O O   . SER   B 1 125 ? 17.130  -52.240 7.049  1.00 102.17 ? 417 SER   B O   1 
ATOM   2731 C CB  . SER   B 1 125 ? 19.517  -51.512 5.472  1.00 89.00  ? 417 SER   B CB  1 
ATOM   2732 O OG  . SER   B 1 125 ? 19.987  -51.811 6.776  1.00 84.46  ? 417 SER   B OG  1 
ATOM   2733 N N   . VAL   B 1 126 ? 17.244  -50.088 7.696  1.00 92.43  ? 418 VAL   B N   1 
ATOM   2734 C CA  . VAL   B 1 126 ? 16.710  -50.316 9.033  1.00 85.36  ? 418 VAL   B CA  1 
ATOM   2735 C C   . VAL   B 1 126 ? 15.551  -49.359 9.269  1.00 88.62  ? 418 VAL   B C   1 
ATOM   2736 O O   . VAL   B 1 126 ? 15.656  -48.163 8.973  1.00 84.97  ? 418 VAL   B O   1 
ATOM   2737 C CB  . VAL   B 1 126 ? 17.795  -50.133 10.110 1.00 83.53  ? 418 VAL   B CB  1 
ATOM   2738 C CG1 . VAL   B 1 126 ? 17.221  -50.379 11.496 1.00 83.82  ? 418 VAL   B CG1 1 
ATOM   2739 C CG2 . VAL   B 1 126 ? 18.955  -51.066 9.834  1.00 88.83  ? 418 VAL   B CG2 1 
ATOM   2740 N N   . GLU   B 1 127 ? 14.451  -49.886 9.803  1.00 94.12  ? 419 GLU   B N   1 
ATOM   2741 C CA  . GLU   B 1 127 ? 13.262  -49.080 10.054 1.00 91.44  ? 419 GLU   B CA  1 
ATOM   2742 C C   . GLU   B 1 127 ? 13.544  -48.050 11.141 1.00 80.89  ? 419 GLU   B C   1 
ATOM   2743 O O   . GLU   B 1 127 ? 13.911  -48.405 12.265 1.00 74.33  ? 419 GLU   B O   1 
ATOM   2744 C CB  . GLU   B 1 127 ? 12.094  -49.978 10.454 1.00 76.80  ? 419 GLU   B CB  1 
ATOM   2745 N N   . GLY   B 1 128 ? 13.374  -46.771 10.802 1.00 71.08  ? 420 GLY   B N   1 
ATOM   2746 C CA  . GLY   B 1 128 ? 13.531  -45.691 11.751 1.00 70.25  ? 420 GLY   B CA  1 
ATOM   2747 C C   . GLY   B 1 128 ? 14.911  -45.073 11.813 1.00 62.10  ? 420 GLY   B C   1 
ATOM   2748 O O   . GLY   B 1 128 ? 15.076  -44.035 12.467 1.00 56.94  ? 420 GLY   B O   1 
ATOM   2749 N N   . MET   B 1 129 ? 15.907  -45.667 11.156 1.00 54.63  ? 421 MET   B N   1 
ATOM   2750 C CA  . MET   B 1 129 ? 17.262  -45.131 11.234 1.00 60.97  ? 421 MET   B CA  1 
ATOM   2751 C C   . MET   B 1 129 ? 17.455  -43.918 10.333 1.00 48.99  ? 421 MET   B C   1 
ATOM   2752 O O   . MET   B 1 129 ? 18.103  -42.945 10.733 1.00 46.69  ? 421 MET   B O   1 
ATOM   2753 C CB  . MET   B 1 129 ? 18.279  -46.219 10.887 1.00 51.54  ? 421 MET   B CB  1 
ATOM   2754 C CG  . MET   B 1 129 ? 19.664  -45.688 10.554 1.00 56.35  ? 421 MET   B CG  1 
ATOM   2755 S SD  . MET   B 1 129 ? 20.919  -46.976 10.602 1.00 69.34  ? 421 MET   B SD  1 
ATOM   2756 C CE  . MET   B 1 129 ? 20.274  -47.990 11.928 1.00 54.98  ? 421 MET   B CE  1 
ATOM   2757 N N   . VAL   B 1 130 ? 16.898  -43.954 9.121  1.00 45.31  ? 422 VAL   B N   1 
ATOM   2758 C CA  . VAL   B 1 130 ? 17.164  -42.894 8.152  1.00 45.10  ? 422 VAL   B CA  1 
ATOM   2759 C C   . VAL   B 1 130 ? 16.624  -41.552 8.634  1.00 37.26  ? 422 VAL   B C   1 
ATOM   2760 O O   . VAL   B 1 130 ? 17.140  -40.495 8.249  1.00 46.60  ? 422 VAL   B O   1 
ATOM   2761 C CB  . VAL   B 1 130 ? 16.592  -43.283 6.772  1.00 52.74  ? 422 VAL   B CB  1 
ATOM   2762 C CG1 . VAL   B 1 130 ? 15.118  -42.919 6.666  1.00 47.57  ? 422 VAL   B CG1 1 
ATOM   2763 C CG2 . VAL   B 1 130 ? 17.395  -42.623 5.664  1.00 57.15  ? 422 VAL   B CG2 1 
ATOM   2764 N N   . GLU   B 1 131 ? 15.599  -41.563 9.488  1.00 47.12  ? 423 GLU   B N   1 
ATOM   2765 C CA  . GLU   B 1 131 ? 15.068  -40.310 10.016 1.00 36.42  ? 423 GLU   B CA  1 
ATOM   2766 C C   . GLU   B 1 131 ? 16.070  -39.644 10.949 1.00 34.31  ? 423 GLU   B C   1 
ATOM   2767 O O   . GLU   B 1 131 ? 16.330  -38.440 10.843 1.00 36.20  ? 423 GLU   B O   1 
ATOM   2768 C CB  . GLU   B 1 131 ? 13.741  -40.560 10.734 1.00 36.85  ? 423 GLU   B CB  1 
ATOM   2769 N N   . ILE   B 1 132 ? 16.649  -40.415 11.872 1.00 30.78  ? 424 ILE   B N   1 
ATOM   2770 C CA  . ILE   B 1 132 ? 17.671  -39.861 12.751 1.00 30.10  ? 424 ILE   B CA  1 
ATOM   2771 C C   . ILE   B 1 132 ? 18.962  -39.623 11.981 1.00 27.72  ? 424 ILE   B C   1 
ATOM   2772 O O   . ILE   B 1 132 ? 19.691  -38.662 12.256 1.00 30.87  ? 424 ILE   B O   1 
ATOM   2773 C CB  . ILE   B 1 132 ? 17.879  -40.784 13.966 1.00 34.99  ? 424 ILE   B CB  1 
ATOM   2774 C CG1 . ILE   B 1 132 ? 16.636  -40.759 14.855 1.00 38.14  ? 424 ILE   B CG1 1 
ATOM   2775 C CG2 . ILE   B 1 132 ? 19.097  -40.361 14.772 1.00 27.20  ? 424 ILE   B CG2 1 
ATOM   2776 C CD1 . ILE   B 1 132 ? 16.524  -41.949 15.769 1.00 40.07  ? 424 ILE   B CD1 1 
ATOM   2777 N N   . PHE   B 1 133 ? 19.255  -40.474 10.993 1.00 29.35  ? 425 PHE   B N   1 
ATOM   2778 C CA  . PHE   B 1 133 ? 20.420  -40.256 10.141 1.00 31.33  ? 425 PHE   B CA  1 
ATOM   2779 C C   . PHE   B 1 133 ? 20.356  -38.895 9.461  1.00 33.57  ? 425 PHE   B C   1 
ATOM   2780 O O   . PHE   B 1 133 ? 21.361  -38.178 9.394  1.00 33.45  ? 425 PHE   B O   1 
ATOM   2781 C CB  . PHE   B 1 133 ? 20.519  -41.372 9.101  1.00 31.96  ? 425 PHE   B CB  1 
ATOM   2782 C CG  . PHE   B 1 133 ? 21.918  -41.645 8.632  1.00 33.36  ? 425 PHE   B CG  1 
ATOM   2783 C CD1 . PHE   B 1 133 ? 22.544  -40.793 7.737  1.00 33.65  ? 425 PHE   B CD1 1 
ATOM   2784 C CD2 . PHE   B 1 133 ? 22.607  -42.759 9.082  1.00 33.06  ? 425 PHE   B CD2 1 
ATOM   2785 C CE1 . PHE   B 1 133 ? 23.832  -41.045 7.303  1.00 34.12  ? 425 PHE   B CE1 1 
ATOM   2786 C CE2 . PHE   B 1 133 ? 23.895  -43.017 8.651  1.00 34.10  ? 425 PHE   B CE2 1 
ATOM   2787 C CZ  . PHE   B 1 133 ? 24.508  -42.158 7.761  1.00 34.65  ? 425 PHE   B CZ  1 
ATOM   2788 N N   . ASP   B 1 134 ? 19.176  -38.516 8.964  1.00 34.83  ? 426 ASP   B N   1 
ATOM   2789 C CA  . ASP   B 1 134 ? 19.032  -37.230 8.289  1.00 30.99  ? 426 ASP   B CA  1 
ATOM   2790 C C   . ASP   B 1 134 ? 19.145  -36.066 9.268  1.00 35.38  ? 426 ASP   B C   1 
ATOM   2791 O O   . ASP   B 1 134 ? 19.751  -35.038 8.944  1.00 33.11  ? 426 ASP   B O   1 
ATOM   2792 C CB  . ASP   B 1 134 ? 17.703  -37.172 7.538  1.00 33.23  ? 426 ASP   B CB  1 
ATOM   2793 C CG  . ASP   B 1 134 ? 17.726  -37.976 6.252  1.00 44.48  ? 426 ASP   B CG  1 
ATOM   2794 O OD1 . ASP   B 1 134 ? 18.830  -38.251 5.737  1.00 44.21  ? 426 ASP   B OD1 1 
ATOM   2795 O OD2 . ASP   B 1 134 ? 16.635  -38.333 5.757  1.00 43.97  ? 426 ASP   B OD2 1 
ATOM   2796 N N   . MET   B 1 135 ? 18.559  -36.194 10.464 1.00 30.71  ? 427 MET   B N   1 
ATOM   2797 C CA  . MET   B 1 135 ? 18.696  -35.127 11.451 1.00 34.84  ? 427 MET   B CA  1 
ATOM   2798 C C   . MET   B 1 135 ? 20.151  -34.940 11.863 1.00 31.69  ? 427 MET   B C   1 
ATOM   2799 O O   . MET   B 1 135 ? 20.600  -33.810 12.096 1.00 35.20  ? 427 MET   B O   1 
ATOM   2800 C CB  . MET   B 1 135 ? 17.826  -35.402 12.680 1.00 29.59  ? 427 MET   B CB  1 
ATOM   2801 C CG  . MET   B 1 135 ? 16.405  -34.865 12.574 1.00 39.73  ? 427 MET   B CG  1 
ATOM   2802 S SD  . MET   B 1 135 ? 15.229  -35.509 13.787 1.00 49.32  ? 427 MET   B SD  1 
ATOM   2803 C CE  . MET   B 1 135 ? 15.688  -37.225 13.903 1.00 29.80  ? 427 MET   B CE  1 
ATOM   2804 N N   . LEU   B 1 136 ? 20.904  -36.036 11.959 1.00 28.04  ? 428 LEU   B N   1 
ATOM   2805 C CA  . LEU   B 1 136 ? 22.322  -35.922 12.280 1.00 33.66  ? 428 LEU   B CA  1 
ATOM   2806 C C   . LEU   B 1 136 ? 23.090  -35.271 11.139 1.00 27.42  ? 428 LEU   B C   1 
ATOM   2807 O O   . LEU   B 1 136 ? 24.027  -34.500 11.375 1.00 28.16  ? 428 LEU   B O   1 
ATOM   2808 C CB  . LEU   B 1 136 ? 22.903  -37.298 12.602 1.00 28.70  ? 428 LEU   B CB  1 
ATOM   2809 C CG  . LEU   B 1 136 ? 22.494  -37.891 13.951 1.00 22.76  ? 428 LEU   B CG  1 
ATOM   2810 C CD1 . LEU   B 1 136 ? 22.713  -39.394 13.967 1.00 23.93  ? 428 LEU   B CD1 1 
ATOM   2811 C CD2 . LEU   B 1 136 ? 23.260  -37.225 15.082 1.00 21.26  ? 428 LEU   B CD2 1 
ATOM   2812 N N   . LEU   B 1 137 ? 22.703  -35.564 9.895  1.00 28.45  ? 429 LEU   B N   1 
ATOM   2813 C CA  . LEU   B 1 137 ? 23.350  -34.931 8.751  1.00 28.15  ? 429 LEU   B CA  1 
ATOM   2814 C C   . LEU   B 1 137 ? 23.018  -33.446 8.681  1.00 28.18  ? 429 LEU   B C   1 
ATOM   2815 O O   . LEU   B 1 137 ? 23.871  -32.631 8.312  1.00 30.28  ? 429 LEU   B O   1 
ATOM   2816 C CB  . LEU   B 1 137 ? 22.939  -35.634 7.459  1.00 30.59  ? 429 LEU   B CB  1 
ATOM   2817 C CG  . LEU   B 1 137 ? 23.561  -37.008 7.204  1.00 31.54  ? 429 LEU   B CG  1 
ATOM   2818 C CD1 . LEU   B 1 137 ? 22.953  -37.639 5.968  1.00 35.19  ? 429 LEU   B CD1 1 
ATOM   2819 C CD2 . LEU   B 1 137 ? 25.071  -36.896 7.061  1.00 32.16  ? 429 LEU   B CD2 1 
ATOM   2820 N N   . ALA   B 1 138 ? 21.782  -33.077 9.029  1.00 35.51  ? 430 ALA   B N   1 
ATOM   2821 C CA  . ALA   B 1 138 ? 21.410  -31.667 9.031  1.00 33.93  ? 430 ALA   B CA  1 
ATOM   2822 C C   . ALA   B 1 138 ? 22.164  -30.890 10.101 1.00 32.85  ? 430 ALA   B C   1 
ATOM   2823 O O   . ALA   B 1 138 ? 22.489  -29.715 9.899  1.00 34.25  ? 430 ALA   B O   1 
ATOM   2824 C CB  . ALA   B 1 138 ? 19.901  -31.519 9.228  1.00 28.50  ? 430 ALA   B CB  1 
ATOM   2825 N N   . THR   B 1 139 ? 22.452  -31.526 11.240 1.00 26.94  ? 431 THR   B N   1 
ATOM   2826 C CA  . THR   B 1 139 ? 23.243  -30.865 12.274 1.00 30.32  ? 431 THR   B CA  1 
ATOM   2827 C C   . THR   B 1 139 ? 24.677  -30.645 11.811 1.00 34.13  ? 431 THR   B C   1 
ATOM   2828 O O   . THR   B 1 139 ? 25.265  -29.590 12.072 1.00 26.87  ? 431 THR   B O   1 
ATOM   2829 C CB  . THR   B 1 139 ? 23.223  -31.688 13.561 1.00 30.48  ? 431 THR   B CB  1 
ATOM   2830 O OG1 . THR   B 1 139 ? 21.894  -32.164 13.806 1.00 37.42  ? 431 THR   B OG1 1 
ATOM   2831 C CG2 . THR   B 1 139 ? 23.682  -30.841 14.740 1.00 25.25  ? 431 THR   B CG2 1 
ATOM   2832 N N   . SER   B 1 140 ? 25.256  -31.633 11.125 1.00 31.14  ? 432 SER   B N   1 
ATOM   2833 C CA  . SER   B 1 140 ? 26.611  -31.479 10.608 1.00 30.76  ? 432 SER   B CA  1 
ATOM   2834 C C   . SER   B 1 140 ? 26.669  -30.385 9.551  1.00 31.88  ? 432 SER   B C   1 
ATOM   2835 O O   . SER   B 1 140 ? 27.632  -29.611 9.500  1.00 38.59  ? 432 SER   B O   1 
ATOM   2836 C CB  . SER   B 1 140 ? 27.108  -32.809 10.043 1.00 33.60  ? 432 SER   B CB  1 
ATOM   2837 O OG  . SER   B 1 140 ? 28.511  -32.794 9.858  1.00 58.55  ? 432 SER   B OG  1 
ATOM   2838 N N   . SER   B 1 141 ? 25.642  -30.301 8.703  1.00 36.69  ? 433 SER   B N   1 
ATOM   2839 C CA  . SER   B 1 141 ? 25.580  -29.226 7.719  1.00 37.48  ? 433 SER   B CA  1 
ATOM   2840 C C   . SER   B 1 141 ? 25.424  -27.871 8.396  1.00 41.40  ? 433 SER   B C   1 
ATOM   2841 O O   . SER   B 1 141 ? 26.004  -26.874 7.950  1.00 40.59  ? 433 SER   B O   1 
ATOM   2842 C CB  . SER   B 1 141 ? 24.431  -29.475 6.742  1.00 39.68  ? 433 SER   B CB  1 
ATOM   2843 O OG  . SER   B 1 141 ? 24.237  -28.362 5.887  1.00 58.05  ? 433 SER   B OG  1 
ATOM   2844 N N   . ARG   B 1 142 ? 24.642  -27.816 9.478  1.00 35.12  ? 434 ARG   B N   1 
ATOM   2845 C CA  . ARG   B 1 142 ? 24.493  -26.569 10.221 1.00 30.34  ? 434 ARG   B CA  1 
ATOM   2846 C C   . ARG   B 1 142 ? 25.805  -26.159 10.878 1.00 34.36  ? 434 ARG   B C   1 
ATOM   2847 O O   . ARG   B 1 142 ? 26.169  -24.977 10.862 1.00 32.96  ? 434 ARG   B O   1 
ATOM   2848 C CB  . ARG   B 1 142 ? 23.385  -26.710 11.264 1.00 37.80  ? 434 ARG   B CB  1 
ATOM   2849 C CG  . ARG   B 1 142 ? 23.223  -25.496 12.163 1.00 28.94  ? 434 ARG   B CG  1 
ATOM   2850 C CD  . ARG   B 1 142 ? 22.686  -24.303 11.390 1.00 45.52  ? 434 ARG   B CD  1 
ATOM   2851 N NE  . ARG   B 1 142 ? 22.491  -23.143 12.251 1.00 31.84  ? 434 ARG   B NE  1 
ATOM   2852 C CZ  . ARG   B 1 142 ? 22.587  -21.885 11.846 1.00 31.89  ? 434 ARG   B CZ  1 
ATOM   2853 N NH1 . ARG   B 1 142 ? 22.870  -21.582 10.589 1.00 41.54  ? 434 ARG   B NH1 1 
ATOM   2854 N NH2 . ARG   B 1 142 ? 22.392  -20.904 12.723 1.00 38.75  ? 434 ARG   B NH2 1 
ATOM   2855 N N   . PHE   B 1 143 ? 26.525  -27.121 11.464 1.00 30.10  ? 435 PHE   B N   1 
ATOM   2856 C CA  . PHE   B 1 143 ? 27.859  -26.835 11.984 1.00 38.95  ? 435 PHE   B CA  1 
ATOM   2857 C C   . PHE   B 1 143 ? 28.777  -26.330 10.878 1.00 34.80  ? 435 PHE   B C   1 
ATOM   2858 O O   . PHE   B 1 143 ? 29.551  -25.387 11.081 1.00 32.73  ? 435 PHE   B O   1 
ATOM   2859 C CB  . PHE   B 1 143 ? 28.456  -28.087 12.630 1.00 37.76  ? 435 PHE   B CB  1 
ATOM   2860 C CG  . PHE   B 1 143 ? 27.980  -28.342 14.035 1.00 38.97  ? 435 PHE   B CG  1 
ATOM   2861 C CD1 . PHE   B 1 143 ? 27.054  -27.508 14.639 1.00 32.03  ? 435 PHE   B CD1 1 
ATOM   2862 C CD2 . PHE   B 1 143 ? 28.470  -29.421 14.753 1.00 35.11  ? 435 PHE   B CD2 1 
ATOM   2863 C CE1 . PHE   B 1 143 ? 26.624  -27.750 15.932 1.00 34.46  ? 435 PHE   B CE1 1 
ATOM   2864 C CE2 . PHE   B 1 143 ? 28.044  -29.668 16.043 1.00 28.03  ? 435 PHE   B CE2 1 
ATOM   2865 C CZ  . PHE   B 1 143 ? 27.119  -28.831 16.633 1.00 23.89  ? 435 PHE   B CZ  1 
ATOM   2866 N N   . ARG   B 1 144 ? 28.699  -26.949 9.697  1.00 36.67  ? 436 ARG   B N   1 
ATOM   2867 C CA  . ARG   B 1 144 ? 29.528  -26.542 8.567  1.00 39.22  ? 436 ARG   B CA  1 
ATOM   2868 C C   . ARG   B 1 144 ? 29.172  -25.154 8.052  1.00 41.23  ? 436 ARG   B C   1 
ATOM   2869 O O   . ARG   B 1 144 ? 30.054  -24.434 7.571  1.00 47.13  ? 436 ARG   B O   1 
ATOM   2870 C CB  . ARG   B 1 144 ? 29.416  -27.585 7.457  1.00 44.37  ? 436 ARG   B CB  1 
ATOM   2871 C CG  . ARG   B 1 144 ? 30.738  -27.960 6.824  1.00 58.49  ? 436 ARG   B CG  1 
ATOM   2872 C CD  . ARG   B 1 144 ? 30.589  -29.197 5.957  1.00 56.56  ? 436 ARG   B CD  1 
ATOM   2873 N NE  . ARG   B 1 144 ? 29.240  -29.383 5.439  1.00 47.99  ? 436 ARG   B NE  1 
ATOM   2874 C CZ  . ARG   B 1 144 ? 28.475  -30.426 5.731  1.00 56.66  ? 436 ARG   B CZ  1 
ATOM   2875 N NH1 . ARG   B 1 144 ? 28.892  -31.388 6.535  1.00 41.32  ? 436 ARG   B NH1 1 
ATOM   2876 N NH2 . ARG   B 1 144 ? 27.262  -30.510 5.200  1.00 59.59  ? 436 ARG   B NH2 1 
ATOM   2877 N N   . MET   B 1 145 ? 27.901  -24.757 8.140  1.00 44.71  ? 437 MET   B N   1 
ATOM   2878 C CA  . MET   B 1 145 ? 27.515  -23.429 7.674  1.00 44.06  ? 437 MET   B CA  1 
ATOM   2879 C C   . MET   B 1 145 ? 27.992  -22.340 8.628  1.00 45.71  ? 437 MET   B C   1 
ATOM   2880 O O   . MET   B 1 145 ? 28.458  -21.284 8.185  1.00 43.67  ? 437 MET   B O   1 
ATOM   2881 C CB  . MET   B 1 145 ? 25.999  -23.356 7.493  1.00 46.15  ? 437 MET   B CB  1 
ATOM   2882 N N   . MET   B 1 146 ? 27.883  -22.573 9.935  1.00 46.44  ? 438 MET   B N   1 
ATOM   2883 C CA  . MET   B 1 146 ? 28.359  -21.611 10.921 1.00 41.01  ? 438 MET   B CA  1 
ATOM   2884 C C   . MET   B 1 146 ? 29.868  -21.651 11.110 1.00 39.47  ? 438 MET   B C   1 
ATOM   2885 O O   . MET   B 1 146 ? 30.407  -20.782 11.805 1.00 37.23  ? 438 MET   B O   1 
ATOM   2886 C CB  . MET   B 1 146 ? 27.683  -21.855 12.270 1.00 44.72  ? 438 MET   B CB  1 
ATOM   2887 C CG  . MET   B 1 146 ? 26.194  -21.576 12.294 1.00 48.84  ? 438 MET   B CG  1 
ATOM   2888 S SD  . MET   B 1 146 ? 25.461  -22.124 13.845 1.00 50.00  ? 438 MET   B SD  1 
ATOM   2889 C CE  . MET   B 1 146 ? 26.271  -21.014 14.994 1.00 33.75  ? 438 MET   B CE  1 
ATOM   2890 N N   . ASN   B 1 147 ? 30.551  -22.627 10.516 1.00 49.31  ? 439 ASN   B N   1 
ATOM   2891 C CA  . ASN   B 1 147 ? 31.984  -22.840 10.707 1.00 42.68  ? 439 ASN   B CA  1 
ATOM   2892 C C   . ASN   B 1 147 ? 32.312  -22.955 12.197 1.00 43.14  ? 439 ASN   B C   1 
ATOM   2893 O O   . ASN   B 1 147 ? 33.050  -22.153 12.773 1.00 38.43  ? 439 ASN   B O   1 
ATOM   2894 C CB  . ASN   B 1 147 ? 32.800  -21.732 10.035 1.00 45.39  ? 439 ASN   B CB  1 
ATOM   2895 C CG  . ASN   B 1 147 ? 34.286  -22.032 10.020 1.00 60.59  ? 439 ASN   B CG  1 
ATOM   2896 O OD1 . ASN   B 1 147 ? 34.716  -23.068 9.511  1.00 55.68  ? 439 ASN   B OD1 1 
ATOM   2897 N ND2 . ASN   B 1 147 ? 35.079  -21.121 10.569 1.00 69.75  ? 439 ASN   B ND2 1 
ATOM   2898 N N   . LEU   B 1 148 ? 31.725  -23.979 12.815 1.00 46.20  ? 440 LEU   B N   1 
ATOM   2899 C CA  . LEU   B 1 148 ? 31.911  -24.210 14.240 1.00 37.02  ? 440 LEU   B CA  1 
ATOM   2900 C C   . LEU   B 1 148 ? 33.374  -24.498 14.551 1.00 33.19  ? 440 LEU   B C   1 
ATOM   2901 O O   . LEU   B 1 148 ? 34.016  -25.313 13.882 1.00 36.76  ? 440 LEU   B O   1 
ATOM   2902 C CB  . LEU   B 1 148 ? 31.034  -25.374 14.700 1.00 35.44  ? 440 LEU   B CB  1 
ATOM   2903 C CG  . LEU   B 1 148 ? 31.075  -25.700 16.193 1.00 42.00  ? 440 LEU   B CG  1 
ATOM   2904 C CD1 . LEU   B 1 148 ? 30.430  -24.589 16.994 1.00 28.49  ? 440 LEU   B CD1 1 
ATOM   2905 C CD2 . LEU   B 1 148 ? 30.397  -27.028 16.476 1.00 37.55  ? 440 LEU   B CD2 1 
ATOM   2906 N N   . GLN   B 1 149 ? 33.898  -23.824 15.567 1.00 35.11  ? 441 GLN   B N   1 
ATOM   2907 C CA  . GLN   B 1 149 ? 35.274  -24.023 15.991 1.00 36.96  ? 441 GLN   B CA  1 
ATOM   2908 C C   . GLN   B 1 149 ? 35.346  -25.075 17.094 1.00 34.24  ? 441 GLN   B C   1 
ATOM   2909 O O   . GLN   B 1 149 ? 34.372  -25.336 17.804 1.00 28.67  ? 441 GLN   B O   1 
ATOM   2910 C CB  . GLN   B 1 149 ? 35.887  -22.708 16.474 1.00 36.36  ? 441 GLN   B CB  1 
ATOM   2911 C CG  . GLN   B 1 149 ? 35.962  -21.636 15.400 1.00 38.62  ? 441 GLN   B CG  1 
ATOM   2912 C CD  . GLN   B 1 149 ? 36.816  -22.058 14.222 1.00 41.65  ? 441 GLN   B CD  1 
ATOM   2913 O OE1 . GLN   B 1 149 ? 38.034  -22.194 14.340 1.00 45.64  ? 441 GLN   B OE1 1 
ATOM   2914 N NE2 . GLN   B 1 149 ? 36.180  -22.275 13.078 1.00 41.96  ? 441 GLN   B NE2 1 
ATOM   2915 N N   . GLY   B 1 150 ? 36.527  -25.683 17.226 1.00 38.99  ? 442 GLY   B N   1 
ATOM   2916 C CA  . GLY   B 1 150 ? 36.709  -26.710 18.239 1.00 37.38  ? 442 GLY   B CA  1 
ATOM   2917 C C   . GLY   B 1 150 ? 36.533  -26.179 19.649 1.00 35.83  ? 442 GLY   B C   1 
ATOM   2918 O O   . GLY   B 1 150 ? 35.993  -26.866 20.519 1.00 38.62  ? 442 GLY   B O   1 
ATOM   2919 N N   . GLU   B 1 151 ? 36.986  -24.946 19.892 1.00 32.11  ? 443 GLU   B N   1 
ATOM   2920 C CA  . GLU   B 1 151 ? 36.794  -24.332 21.201 1.00 34.60  ? 443 GLU   B CA  1 
ATOM   2921 C C   . GLU   B 1 151 ? 35.320  -24.098 21.497 1.00 31.89  ? 443 GLU   B C   1 
ATOM   2922 O O   . GLU   B 1 151 ? 34.904  -24.141 22.660 1.00 37.50  ? 443 GLU   B O   1 
ATOM   2923 C CB  . GLU   B 1 151 ? 37.568  -23.016 21.282 1.00 39.93  ? 443 GLU   B CB  1 
ATOM   2924 C CG  . GLU   B 1 151 ? 39.070  -23.159 21.095 1.00 37.54  ? 443 GLU   B CG  1 
ATOM   2925 C CD  . GLU   B 1 151 ? 39.497  -23.019 19.646 1.00 41.88  ? 443 GLU   B CD  1 
ATOM   2926 O OE1 . GLU   B 1 151 ? 38.613  -22.936 18.767 1.00 40.57  ? 443 GLU   B OE1 1 
ATOM   2927 O OE2 . GLU   B 1 151 ? 40.718  -22.989 19.388 1.00 52.28  ? 443 GLU   B OE2 1 
ATOM   2928 N N   . GLU   B 1 152 ? 34.516  -23.845 20.463 1.00 37.48  ? 444 GLU   B N   1 
ATOM   2929 C CA  . GLU   B 1 152 ? 33.079  -23.700 20.660 1.00 31.91  ? 444 GLU   B CA  1 
ATOM   2930 C C   . GLU   B 1 152 ? 32.411  -25.054 20.868 1.00 36.34  ? 444 GLU   B C   1 
ATOM   2931 O O   . GLU   B 1 152 ? 31.453  -25.165 21.641 1.00 29.68  ? 444 GLU   B O   1 
ATOM   2932 C CB  . GLU   B 1 152 ? 32.454  -22.981 19.466 1.00 29.27  ? 444 GLU   B CB  1 
ATOM   2933 C CG  . GLU   B 1 152 ? 33.000  -21.588 19.211 1.00 33.11  ? 444 GLU   B CG  1 
ATOM   2934 C CD  . GLU   B 1 152 ? 32.449  -20.981 17.937 1.00 33.17  ? 444 GLU   B CD  1 
ATOM   2935 O OE1 . GLU   B 1 152 ? 32.562  -21.628 16.874 1.00 33.65  ? 444 GLU   B OE1 1 
ATOM   2936 O OE2 . GLU   B 1 152 ? 31.901  -19.861 17.996 1.00 33.50  ? 444 GLU   B OE2 1 
ATOM   2937 N N   . PHE   B 1 153 ? 32.909  -26.091 20.189 1.00 33.37  ? 445 PHE   B N   1 
ATOM   2938 C CA  . PHE   B 1 153 ? 32.300  -27.413 20.295 1.00 29.82  ? 445 PHE   B CA  1 
ATOM   2939 C C   . PHE   B 1 153 ? 32.454  -27.986 21.699 1.00 30.51  ? 445 PHE   B C   1 
ATOM   2940 O O   . PHE   B 1 153 ? 31.500  -28.546 22.253 1.00 24.04  ? 445 PHE   B O   1 
ATOM   2941 C CB  . PHE   B 1 153 ? 32.913  -28.354 19.258 1.00 31.68  ? 445 PHE   B CB  1 
ATOM   2942 C CG  . PHE   B 1 153 ? 32.781  -29.812 19.603 1.00 26.25  ? 445 PHE   B CG  1 
ATOM   2943 C CD1 . PHE   B 1 153 ? 31.573  -30.469 19.440 1.00 38.10  ? 445 PHE   B CD1 1 
ATOM   2944 C CD2 . PHE   B 1 153 ? 33.869  -30.527 20.079 1.00 31.41  ? 445 PHE   B CD2 1 
ATOM   2945 C CE1 . PHE   B 1 153 ? 31.449  -31.810 19.754 1.00 26.82  ? 445 PHE   B CE1 1 
ATOM   2946 C CE2 . PHE   B 1 153 ? 33.750  -31.868 20.395 1.00 26.12  ? 445 PHE   B CE2 1 
ATOM   2947 C CZ  . PHE   B 1 153 ? 32.539  -32.510 20.231 1.00 28.41  ? 445 PHE   B CZ  1 
ATOM   2948 N N   . VAL   B 1 154 ? 33.645  -27.860 22.290 1.00 26.28  ? 446 VAL   B N   1 
ATOM   2949 C CA  . VAL   B 1 154 ? 33.854  -28.393 23.632 1.00 24.23  ? 446 VAL   B CA  1 
ATOM   2950 C C   . VAL   B 1 154 ? 33.028  -27.622 24.654 1.00 30.21  ? 446 VAL   B C   1 
ATOM   2951 O O   . VAL   B 1 154 ? 32.608  -28.185 25.673 1.00 29.28  ? 446 VAL   B O   1 
ATOM   2952 C CB  . VAL   B 1 154 ? 35.353  -28.388 23.987 1.00 26.33  ? 446 VAL   B CB  1 
ATOM   2953 C CG1 . VAL   B 1 154 ? 36.124  -29.274 23.022 1.00 26.93  ? 446 VAL   B CG1 1 
ATOM   2954 C CG2 . VAL   B 1 154 ? 35.906  -26.973 23.970 1.00 34.06  ? 446 VAL   B CG2 1 
ATOM   2955 N N   . CYS   B 1 155 ? 32.771  -26.335 24.406 1.00 24.84  ? 447 CYS   B N   1 
ATOM   2956 C CA  . CYS   B 1 155 ? 31.878  -25.586 25.282 1.00 25.49  ? 447 CYS   B CA  1 
ATOM   2957 C C   . CYS   B 1 155 ? 30.442  -26.079 25.148 1.00 25.09  ? 447 CYS   B C   1 
ATOM   2958 O O   . CYS   B 1 155 ? 29.712  -26.160 26.143 1.00 27.98  ? 447 CYS   B O   1 
ATOM   2959 C CB  . CYS   B 1 155 ? 31.967  -24.091 24.974 1.00 28.69  ? 447 CYS   B CB  1 
ATOM   2960 S SG  . CYS   B 1 155 ? 33.453  -23.266 25.608 1.00 33.46  ? 447 CYS   B SG  1 
ATOM   2961 N N   . LEU   B 1 156 ? 30.023  -26.423 23.927 1.00 26.86  ? 448 LEU   B N   1 
ATOM   2962 C CA  . LEU   B 1 156 ? 28.673  -26.936 23.718 1.00 26.30  ? 448 LEU   B CA  1 
ATOM   2963 C C   . LEU   B 1 156 ? 28.480  -28.286 24.398 1.00 26.18  ? 448 LEU   B C   1 
ATOM   2964 O O   . LEU   B 1 156 ? 27.424  -28.544 24.988 1.00 27.05  ? 448 LEU   B O   1 
ATOM   2965 C CB  . LEU   B 1 156 ? 28.379  -27.047 22.221 1.00 25.04  ? 448 LEU   B CB  1 
ATOM   2966 C CG  . LEU   B 1 156 ? 28.147  -25.743 21.455 1.00 34.21  ? 448 LEU   B CG  1 
ATOM   2967 C CD1 . LEU   B 1 156 ? 27.418  -26.012 20.146 1.00 32.55  ? 448 LEU   B CD1 1 
ATOM   2968 C CD2 . LEU   B 1 156 ? 27.375  -24.749 22.307 1.00 32.65  ? 448 LEU   B CD2 1 
ATOM   2969 N N   . LYS   B 1 157 ? 29.484  -29.164 24.319 1.00 22.36  ? 449 LYS   B N   1 
ATOM   2970 C CA  . LYS   B 1 157 ? 29.392  -30.460 24.984 1.00 25.60  ? 449 LYS   B CA  1 
ATOM   2971 C C   . LYS   B 1 157 ? 29.266  -30.299 26.493 1.00 29.84  ? 449 LYS   B C   1 
ATOM   2972 O O   . LYS   B 1 157 ? 28.491  -31.014 27.140 1.00 24.53  ? 449 LYS   B O   1 
ATOM   2973 C CB  . LYS   B 1 157 ? 30.613  -31.313 24.643 1.00 30.87  ? 449 LYS   B CB  1 
ATOM   2974 C CG  . LYS   B 1 157 ? 30.428  -32.232 23.451 1.00 31.41  ? 449 LYS   B CG  1 
ATOM   2975 C CD  . LYS   B 1 157 ? 31.299  -33.471 23.578 1.00 33.25  ? 449 LYS   B CD  1 
ATOM   2976 C CE  . LYS   B 1 157 ? 32.753  -33.098 23.818 1.00 29.97  ? 449 LYS   B CE  1 
ATOM   2977 N NZ  . LYS   B 1 157 ? 33.682  -34.212 23.478 1.00 34.52  ? 449 LYS   B NZ  1 
ATOM   2978 N N   . SER   B 1 158 ? 30.024  -29.365 27.071 1.00 22.76  ? 450 SER   B N   1 
ATOM   2979 C CA  . SER   B 1 158 ? 29.955  -29.136 28.510 1.00 24.77  ? 450 SER   B CA  1 
ATOM   2980 C C   . SER   B 1 158 ? 28.595  -28.585 28.916 1.00 25.62  ? 450 SER   B C   1 
ATOM   2981 O O   . SER   B 1 158 ? 28.070  -28.935 29.980 1.00 22.97  ? 450 SER   B O   1 
ATOM   2982 C CB  . SER   B 1 158 ? 31.068  -28.183 28.941 1.00 25.83  ? 450 SER   B CB  1 
ATOM   2983 O OG  . SER   B 1 158 ? 32.334  -28.681 28.550 1.00 48.15  ? 450 SER   B OG  1 
ATOM   2984 N N   . ILE   B 1 159 ? 28.013  -27.717 28.086 1.00 21.54  ? 451 ILE   B N   1 
ATOM   2985 C CA  . ILE   B 1 159 ? 26.679  -27.200 28.373 1.00 25.09  ? 451 ILE   B CA  1 
ATOM   2986 C C   . ILE   B 1 159 ? 25.659  -28.331 28.350 1.00 20.09  ? 451 ILE   B C   1 
ATOM   2987 O O   . ILE   B 1 159 ? 24.784  -28.414 29.219 1.00 28.18  ? 451 ILE   B O   1 
ATOM   2988 C CB  . ILE   B 1 159 ? 26.311  -26.082 27.381 1.00 21.47  ? 451 ILE   B CB  1 
ATOM   2989 C CG1 . ILE   B 1 159 ? 27.193  -24.855 27.609 1.00 26.38  ? 451 ILE   B CG1 1 
ATOM   2990 C CG2 . ILE   B 1 159 ? 24.849  -25.703 27.525 1.00 19.76  ? 451 ILE   B CG2 1 
ATOM   2991 C CD1 . ILE   B 1 159 ? 27.165  -23.861 26.468 1.00 22.34  ? 451 ILE   B CD1 1 
ATOM   2992 N N   . ILE   B 1 160 ? 25.767  -29.226 27.366 1.00 23.24  ? 452 ILE   B N   1 
ATOM   2993 C CA  . ILE   B 1 160 ? 24.845  -30.357 27.272 1.00 24.12  ? 452 ILE   B CA  1 
ATOM   2994 C C   . ILE   B 1 160 ? 24.931  -31.219 28.525 1.00 27.09  ? 452 ILE   B C   1 
ATOM   2995 O O   . ILE   B 1 160 ? 23.910  -31.620 29.097 1.00 26.76  ? 452 ILE   B O   1 
ATOM   2996 C CB  . ILE   B 1 160 ? 25.136  -31.180 26.005 1.00 24.35  ? 452 ILE   B CB  1 
ATOM   2997 C CG1 . ILE   B 1 160 ? 24.685  -30.422 24.756 1.00 25.51  ? 452 ILE   B CG1 1 
ATOM   2998 C CG2 . ILE   B 1 160 ? 24.461  -32.537 26.088 1.00 24.03  ? 452 ILE   B CG2 1 
ATOM   2999 C CD1 . ILE   B 1 160 ? 25.205  -31.020 23.468 1.00 23.42  ? 452 ILE   B CD1 1 
ATOM   3000 N N   . LEU   B 1 161 ? 26.157  -31.517 28.967 1.00 20.11  ? 453 LEU   B N   1 
ATOM   3001 C CA  . LEU   B 1 161 ? 26.347  -32.327 30.167 1.00 21.72  ? 453 LEU   B CA  1 
ATOM   3002 C C   . LEU   B 1 161 ? 25.667  -31.700 31.377 1.00 25.99  ? 453 LEU   B C   1 
ATOM   3003 O O   . LEU   B 1 161 ? 25.018  -32.398 32.165 1.00 26.97  ? 453 LEU   B O   1 
ATOM   3004 C CB  . LEU   B 1 161 ? 27.840  -32.513 30.439 1.00 22.36  ? 453 LEU   B CB  1 
ATOM   3005 C CG  . LEU   B 1 161 ? 28.219  -33.240 31.731 1.00 25.43  ? 453 LEU   B CG  1 
ATOM   3006 C CD1 . LEU   B 1 161 ? 27.702  -34.673 31.716 1.00 25.39  ? 453 LEU   B CD1 1 
ATOM   3007 C CD2 . LEU   B 1 161 ? 29.724  -33.204 31.953 1.00 27.69  ? 453 LEU   B CD2 1 
ATOM   3008 N N   . LEU   B 1 162 ? 25.798  -30.385 31.538 1.00 23.90  ? 454 LEU   B N   1 
ATOM   3009 C CA  . LEU   B 1 162 ? 25.297  -29.716 32.729 1.00 30.05  ? 454 LEU   B CA  1 
ATOM   3010 C C   . LEU   B 1 162 ? 23.834  -29.313 32.626 1.00 26.23  ? 454 LEU   B C   1 
ATOM   3011 O O   . LEU   B 1 162 ? 23.188  -29.133 33.661 1.00 30.24  ? 454 LEU   B O   1 
ATOM   3012 C CB  . LEU   B 1 162 ? 26.144  -28.476 33.027 1.00 26.84  ? 454 LEU   B CB  1 
ATOM   3013 C CG  . LEU   B 1 162 ? 27.592  -28.764 33.425 1.00 29.60  ? 454 LEU   B CG  1 
ATOM   3014 C CD1 . LEU   B 1 162 ? 28.442  -27.522 33.253 1.00 31.11  ? 454 LEU   B CD1 1 
ATOM   3015 C CD2 . LEU   B 1 162 ? 27.658  -29.268 34.857 1.00 29.64  ? 454 LEU   B CD2 1 
ATOM   3016 N N   . ASN   B 1 163 ? 23.290  -29.184 31.416 1.00 26.28  ? 455 ASN   B N   1 
ATOM   3017 C CA  . ASN   B 1 163 ? 21.943  -28.658 31.240 1.00 31.85  ? 455 ASN   B CA  1 
ATOM   3018 C C   . ASN   B 1 163 ? 20.878  -29.728 31.046 1.00 25.27  ? 455 ASN   B C   1 
ATOM   3019 O O   . ASN   B 1 163 ? 19.707  -29.472 31.348 1.00 37.26  ? 455 ASN   B O   1 
ATOM   3020 C CB  . ASN   B 1 163 ? 21.905  -27.704 30.039 1.00 22.66  ? 455 ASN   B CB  1 
ATOM   3021 C CG  . ASN   B 1 163 ? 20.564  -27.031 29.875 1.00 29.03  ? 455 ASN   B CG  1 
ATOM   3022 O OD1 . ASN   B 1 163 ? 20.046  -26.423 30.809 1.00 28.92  ? 455 ASN   B OD1 1 
ATOM   3023 N ND2 . ASN   B 1 163 ? 19.984  -27.148 28.685 1.00 30.37  ? 455 ASN   B ND2 1 
ATOM   3024 N N   . SER   B 1 164 ? 21.244  -30.917 30.567 1.00 32.03  ? 456 SER   B N   1 
ATOM   3025 C CA  . SER   B 1 164 ? 20.237  -31.874 30.122 1.00 38.06  ? 456 SER   B CA  1 
ATOM   3026 C C   . SER   B 1 164 ? 19.490  -32.553 31.264 1.00 37.85  ? 456 SER   B C   1 
ATOM   3027 O O   . SER   B 1 164 ? 18.557  -33.317 30.993 1.00 40.79  ? 456 SER   B O   1 
ATOM   3028 C CB  . SER   B 1 164 ? 20.883  -32.925 29.220 1.00 36.36  ? 456 SER   B CB  1 
ATOM   3029 O OG  . SER   B 1 164 ? 21.200  -32.368 27.955 1.00 32.18  ? 456 SER   B OG  1 
ATOM   3030 N N   . GLY   B 1 165 ? 19.848  -32.287 32.518 1.00 34.71  ? 457 GLY   B N   1 
ATOM   3031 C CA  . GLY   B 1 165 ? 19.177  -32.946 33.622 1.00 40.37  ? 457 GLY   B CA  1 
ATOM   3032 C C   . GLY   B 1 165 ? 18.696  -32.042 34.740 1.00 41.56  ? 457 GLY   B C   1 
ATOM   3033 O O   . GLY   B 1 165 ? 18.040  -32.514 35.672 1.00 46.25  ? 457 GLY   B O   1 
ATOM   3034 N N   . VAL   B 1 166 ? 18.993  -30.742 34.663 1.00 45.36  ? 458 VAL   B N   1 
ATOM   3035 C CA  . VAL   B 1 166 ? 18.695  -29.848 35.783 1.00 57.68  ? 458 VAL   B CA  1 
ATOM   3036 C C   . VAL   B 1 166 ? 17.197  -29.743 36.046 1.00 52.93  ? 458 VAL   B C   1 
ATOM   3037 O O   . VAL   B 1 166 ? 16.776  -29.520 37.187 1.00 61.21  ? 458 VAL   B O   1 
ATOM   3038 C CB  . VAL   B 1 166 ? 19.323  -28.461 35.546 1.00 60.27  ? 458 VAL   B CB  1 
ATOM   3039 C CG1 . VAL   B 1 166 ? 20.824  -28.571 35.554 1.00 53.89  ? 458 VAL   B CG1 1 
ATOM   3040 C CG2 . VAL   B 1 166 ? 18.858  -27.886 34.219 1.00 47.77  ? 458 VAL   B CG2 1 
ATOM   3041 N N   A TYR   B 1 167 ? 16.374  -29.889 35.013 0.46 56.17  ? 459 TYR   B N   1 
ATOM   3042 N N   B TYR   B 1 167 ? 16.378  -29.912 35.016 0.54 56.20  ? 459 TYR   B N   1 
ATOM   3043 C CA  A TYR   B 1 167 ? 14.929  -29.788 35.189 0.46 56.90  ? 459 TYR   B CA  1 
ATOM   3044 C CA  B TYR   B 1 167 ? 14.931  -29.800 35.154 0.54 56.95  ? 459 TYR   B CA  1 
ATOM   3045 C C   A TYR   B 1 167 ? 14.297  -31.168 35.348 0.46 50.98  ? 459 TYR   B C   1 
ATOM   3046 C C   B TYR   B 1 167 ? 14.246  -31.127 34.844 0.54 50.96  ? 459 TYR   B C   1 
ATOM   3047 O O   A TYR   B 1 167 ? 13.146  -31.290 35.771 0.46 59.99  ? 459 TYR   B O   1 
ATOM   3048 O O   B TYR   B 1 167 ? 13.234  -31.471 35.456 0.54 61.31  ? 459 TYR   B O   1 
ATOM   3049 C CB  A TYR   B 1 167 ? 14.288  -29.050 34.011 0.46 50.03  ? 459 TYR   B CB  1 
ATOM   3050 C CB  B TYR   B 1 167 ? 14.378  -28.695 34.242 0.54 50.60  ? 459 TYR   B CB  1 
ATOM   3051 C CG  A TYR   B 1 167 ? 15.145  -27.956 33.411 0.46 48.35  ? 459 TYR   B CG  1 
ATOM   3052 C CG  B TYR   B 1 167 ? 15.253  -28.319 33.058 0.54 47.14  ? 459 TYR   B CG  1 
ATOM   3053 C CD1 A TYR   B 1 167 ? 15.254  -26.714 34.025 0.46 50.84  ? 459 TYR   B CD1 1 
ATOM   3054 C CD1 B TYR   B 1 167 ? 15.799  -29.290 32.221 0.54 53.50  ? 459 TYR   B CD1 1 
ATOM   3055 C CD2 A TYR   B 1 167 ? 15.830  -28.159 32.220 0.46 49.82  ? 459 TYR   B CD2 1 
ATOM   3056 C CD2 B TYR   B 1 167 ? 15.521  -26.987 32.771 0.54 46.18  ? 459 TYR   B CD2 1 
ATOM   3057 C CE1 A TYR   B 1 167 ? 16.031  -25.709 33.474 0.46 39.45  ? 459 TYR   B CE1 1 
ATOM   3058 C CE1 B TYR   B 1 167 ? 16.596  -28.944 31.146 0.54 40.31  ? 459 TYR   B CE1 1 
ATOM   3059 C CE2 A TYR   B 1 167 ? 16.605  -27.160 31.659 0.46 46.46  ? 459 TYR   B CE2 1 
ATOM   3060 C CE2 B TYR   B 1 167 ? 16.312  -26.632 31.694 0.54 47.61  ? 459 TYR   B CE2 1 
ATOM   3061 C CZ  A TYR   B 1 167 ? 16.704  -25.937 32.291 0.46 45.69  ? 459 TYR   B CZ  1 
ATOM   3062 C CZ  B TYR   B 1 167 ? 16.845  -27.614 30.886 0.54 35.43  ? 459 TYR   B CZ  1 
ATOM   3063 O OH  A TYR   B 1 167 ? 17.479  -24.943 31.739 0.46 35.02  ? 459 TYR   B OH  1 
ATOM   3064 O OH  B TYR   B 1 167 ? 17.630  -27.262 29.813 0.54 39.15  ? 459 TYR   B OH  1 
ATOM   3065 N N   . LEU   B 1 177 ? 18.869  -28.017 46.258 1.00 79.32  ? 469 LEU   B N   1 
ATOM   3066 C CA  . LEU   B 1 177 ? 18.653  -26.733 45.601 1.00 80.68  ? 469 LEU   B CA  1 
ATOM   3067 C C   . LEU   B 1 177 ? 19.981  -26.058 45.276 1.00 71.28  ? 469 LEU   B C   1 
ATOM   3068 O O   . LEU   B 1 177 ? 20.175  -25.553 44.170 1.00 70.29  ? 469 LEU   B O   1 
ATOM   3069 C CB  . LEU   B 1 177 ? 17.797  -25.818 46.479 1.00 73.27  ? 469 LEU   B CB  1 
ATOM   3070 N N   . GLU   B 1 178 ? 20.894  -26.054 46.251 1.00 72.51  ? 470 GLU   B N   1 
ATOM   3071 C CA  . GLU   B 1 178 ? 22.216  -25.480 46.030 1.00 67.72  ? 470 GLU   B CA  1 
ATOM   3072 C C   . GLU   B 1 178 ? 23.001  -26.241 44.971 1.00 67.62  ? 470 GLU   B C   1 
ATOM   3073 O O   . GLU   B 1 178 ? 23.931  -25.679 44.381 1.00 72.46  ? 470 GLU   B O   1 
ATOM   3074 C CB  . GLU   B 1 178 ? 23.002  -25.448 47.342 1.00 70.96  ? 470 GLU   B CB  1 
ATOM   3075 N N   . GLU   B 1 179 ? 22.652  -27.505 44.723 1.00 71.24  ? 471 GLU   B N   1 
ATOM   3076 C CA  . GLU   B 1 179 ? 23.289  -28.250 43.642 1.00 58.56  ? 471 GLU   B CA  1 
ATOM   3077 C C   . GLU   B 1 179 ? 22.936  -27.654 42.286 1.00 55.03  ? 471 GLU   B C   1 
ATOM   3078 O O   . GLU   B 1 179 ? 23.803  -27.526 41.413 1.00 52.79  ? 471 GLU   B O   1 
ATOM   3079 C CB  . GLU   B 1 179 ? 22.881  -29.721 43.708 1.00 51.47  ? 471 GLU   B CB  1 
ATOM   3080 N N   . LYS   B 1 180 ? 21.668  -27.286 42.089 1.00 64.24  ? 472 LYS   B N   1 
ATOM   3081 C CA  . LYS   B 1 180 ? 21.276  -26.625 40.849 1.00 55.07  ? 472 LYS   B CA  1 
ATOM   3082 C C   . LYS   B 1 180 ? 21.938  -25.259 40.723 1.00 45.45  ? 472 LYS   B C   1 
ATOM   3083 O O   . LYS   B 1 180 ? 22.296  -24.836 39.617 1.00 47.80  ? 472 LYS   B O   1 
ATOM   3084 C CB  . LYS   B 1 180 ? 19.755  -26.488 40.780 1.00 61.70  ? 472 LYS   B CB  1 
ATOM   3085 C CG  . LYS   B 1 180 ? 19.008  -27.811 40.710 1.00 66.30  ? 472 LYS   B CG  1 
ATOM   3086 C CD  . LYS   B 1 180 ? 17.590  -27.619 40.192 1.00 65.42  ? 472 LYS   B CD  1 
ATOM   3087 C CE  . LYS   B 1 180 ? 16.919  -26.413 40.834 1.00 63.89  ? 472 LYS   B CE  1 
ATOM   3088 N NZ  . LYS   B 1 180 ? 15.880  -26.811 41.824 1.00 66.97  ? 472 LYS   B NZ  1 
ATOM   3089 N N   . ASP   B 1 181 ? 22.109  -24.557 41.846 1.00 52.34  ? 473 ASP   B N   1 
ATOM   3090 C CA  . ASP   B 1 181 ? 22.764  -23.253 41.813 1.00 56.40  ? 473 ASP   B CA  1 
ATOM   3091 C C   . ASP   B 1 181 ? 24.195  -23.370 41.307 1.00 49.12  ? 473 ASP   B C   1 
ATOM   3092 O O   . ASP   B 1 181 ? 24.640  -22.557 40.489 1.00 49.86  ? 473 ASP   B O   1 
ATOM   3093 C CB  . ASP   B 1 181 ? 22.736  -22.617 43.202 1.00 56.83  ? 473 ASP   B CB  1 
ATOM   3094 C CG  . ASP   B 1 181 ? 21.567  -21.671 43.386 1.00 73.20  ? 473 ASP   B CG  1 
ATOM   3095 O OD1 . ASP   B 1 181 ? 21.224  -20.955 42.421 1.00 74.17  ? 473 ASP   B OD1 1 
ATOM   3096 O OD2 . ASP   B 1 181 ? 20.991  -21.645 44.493 1.00 75.21  ? 473 ASP   B OD2 1 
ATOM   3097 N N   . HIS   B 1 182 ? 24.929  -24.380 41.779 1.00 54.08  ? 474 HIS   B N   1 
ATOM   3098 C CA  . HIS   B 1 182 ? 26.299  -24.575 41.317 1.00 43.91  ? 474 HIS   B CA  1 
ATOM   3099 C C   . HIS   B 1 182 ? 26.338  -24.924 39.835 1.00 42.88  ? 474 HIS   B C   1 
ATOM   3100 O O   . HIS   B 1 182 ? 27.234  -24.479 39.108 1.00 40.89  ? 474 HIS   B O   1 
ATOM   3101 C CB  . HIS   B 1 182 ? 26.982  -25.664 42.142 1.00 42.91  ? 474 HIS   B CB  1 
ATOM   3102 C CG  . HIS   B 1 182 ? 28.371  -25.980 41.686 1.00 46.82  ? 474 HIS   B CG  1 
ATOM   3103 N ND1 . HIS   B 1 182 ? 29.455  -25.186 41.994 1.00 49.66  ? 474 HIS   B ND1 1 
ATOM   3104 C CD2 . HIS   B 1 182 ? 28.852  -26.999 40.936 1.00 41.59  ? 474 HIS   B CD2 1 
ATOM   3105 C CE1 . HIS   B 1 182 ? 30.544  -25.706 41.457 1.00 55.25  ? 474 HIS   B CE1 1 
ATOM   3106 N NE2 . HIS   B 1 182 ? 30.206  -26.806 40.809 1.00 49.09  ? 474 HIS   B NE2 1 
ATOM   3107 N N   . ILE   B 1 183 ? 25.376  -25.724 39.369 1.00 34.04  ? 475 ILE   B N   1 
ATOM   3108 C CA  . ILE   B 1 183 ? 25.320  -26.068 37.951 1.00 31.78  ? 475 ILE   B CA  1 
ATOM   3109 C C   . ILE   B 1 183 ? 25.070  -24.823 37.112 1.00 38.36  ? 475 ILE   B C   1 
ATOM   3110 O O   . ILE   B 1 183 ? 25.665  -24.645 36.042 1.00 32.71  ? 475 ILE   B O   1 
ATOM   3111 C CB  . ILE   B 1 183 ? 24.244  -27.141 37.703 1.00 31.97  ? 475 ILE   B CB  1 
ATOM   3112 C CG1 . ILE   B 1 183 ? 24.604  -28.440 38.423 1.00 45.19  ? 475 ILE   B CG1 1 
ATOM   3113 C CG2 . ILE   B 1 183 ? 24.091  -27.397 36.219 1.00 31.77  ? 475 ILE   B CG2 1 
ATOM   3114 C CD1 . ILE   B 1 183 ? 23.508  -29.484 38.389 1.00 30.39  ? 475 ILE   B CD1 1 
ATOM   3115 N N   . HIS   B 1 184 ? 24.193  -23.936 37.588 1.00 39.12  ? 476 HIS   B N   1 
ATOM   3116 C CA  . HIS   B 1 184 ? 23.896  -22.720 36.839 1.00 43.04  ? 476 HIS   B CA  1 
ATOM   3117 C C   . HIS   B 1 184 ? 25.077  -21.758 36.834 1.00 32.21  ? 476 HIS   B C   1 
ATOM   3118 O O   . HIS   B 1 184 ? 25.286  -21.045 35.846 1.00 35.28  ? 476 HIS   B O   1 
ATOM   3119 C CB  . HIS   B 1 184 ? 22.654  -22.041 37.415 1.00 39.25  ? 476 HIS   B CB  1 
ATOM   3120 C CG  . HIS   B 1 184 ? 21.374  -22.737 37.071 1.00 47.76  ? 476 HIS   B CG  1 
ATOM   3121 N ND1 . HIS   B 1 184 ? 20.989  -22.987 35.771 1.00 49.04  ? 476 HIS   B ND1 1 
ATOM   3122 C CD2 . HIS   B 1 184 ? 20.391  -23.237 37.857 1.00 51.52  ? 476 HIS   B CD2 1 
ATOM   3123 C CE1 . HIS   B 1 184 ? 19.825  -23.612 35.771 1.00 52.48  ? 476 HIS   B CE1 1 
ATOM   3124 N NE2 . HIS   B 1 184 ? 19.440  -23.774 37.024 1.00 51.81  ? 476 HIS   B NE2 1 
ATOM   3125 N N   . ARG   B 1 185 ? 25.858  -21.721 37.917 1.00 33.99  ? 477 ARG   B N   1 
ATOM   3126 C CA  . ARG   B 1 185 ? 27.037  -20.859 37.942 1.00 33.13  ? 477 ARG   B CA  1 
ATOM   3127 C C   . ARG   B 1 185 ? 28.095  -21.344 36.959 1.00 37.93  ? 477 ARG   B C   1 
ATOM   3128 O O   . ARG   B 1 185 ? 28.722  -20.534 36.267 1.00 43.14  ? 477 ARG   B O   1 
ATOM   3129 C CB  . ARG   B 1 185 ? 27.609  -20.787 39.357 1.00 36.53  ? 477 ARG   B CB  1 
ATOM   3130 C CG  . ARG   B 1 185 ? 26.672  -20.158 40.373 1.00 43.96  ? 477 ARG   B CG  1 
ATOM   3131 C CD  . ARG   B 1 185 ? 27.426  -19.692 41.607 1.00 47.40  ? 477 ARG   B CD  1 
ATOM   3132 N NE  . ARG   B 1 185 ? 27.364  -20.674 42.684 1.00 73.94  ? 477 ARG   B NE  1 
ATOM   3133 C CZ  . ARG   B 1 185 ? 26.321  -20.843 43.485 1.00 73.78  ? 477 ARG   B CZ  1 
ATOM   3134 N NH1 . ARG   B 1 185 ? 25.229  -20.105 43.363 1.00 67.81  ? 477 ARG   B NH1 1 
ATOM   3135 N NH2 . ARG   B 1 185 ? 26.374  -21.775 44.432 1.00 62.92  ? 477 ARG   B NH2 1 
ATOM   3136 N N   . VAL   B 1 186 ? 28.308  -22.659 36.886 1.00 32.39  ? 478 VAL   B N   1 
ATOM   3137 C CA  . VAL   B 1 186 ? 29.249  -23.200 35.910 1.00 31.64  ? 478 VAL   B CA  1 
ATOM   3138 C C   . VAL   B 1 186 ? 28.714  -23.006 34.498 1.00 29.20  ? 478 VAL   B C   1 
ATOM   3139 O O   . VAL   B 1 186 ? 29.469  -22.681 33.573 1.00 34.14  ? 478 VAL   B O   1 
ATOM   3140 C CB  . VAL   B 1 186 ? 29.541  -24.682 36.210 1.00 36.20  ? 478 VAL   B CB  1 
ATOM   3141 C CG1 . VAL   B 1 186 ? 30.487  -25.258 35.167 1.00 30.33  ? 478 VAL   B CG1 1 
ATOM   3142 C CG2 . VAL   B 1 186 ? 30.121  -24.836 37.609 1.00 32.46  ? 478 VAL   B CG2 1 
ATOM   3143 N N   . LEU   B 1 187 ? 27.405  -23.198 34.309 1.00 29.62  ? 479 LEU   B N   1 
ATOM   3144 C CA  . LEU   B 1 187 ? 26.791  -22.906 33.018 1.00 29.62  ? 479 LEU   B CA  1 
ATOM   3145 C C   . LEU   B 1 187 ? 26.967  -21.440 32.649 1.00 28.55  ? 479 LEU   B C   1 
ATOM   3146 O O   . LEU   B 1 187 ? 27.212  -21.109 31.483 1.00 30.29  ? 479 LEU   B O   1 
ATOM   3147 C CB  . LEU   B 1 187 ? 25.307  -23.277 33.046 1.00 26.96  ? 479 LEU   B CB  1 
ATOM   3148 C CG  . LEU   B 1 187 ? 24.941  -24.730 32.736 1.00 33.89  ? 479 LEU   B CG  1 
ATOM   3149 C CD1 . LEU   B 1 187 ? 23.448  -24.962 32.921 1.00 25.95  ? 479 LEU   B CD1 1 
ATOM   3150 C CD2 . LEU   B 1 187 ? 25.374  -25.104 31.326 1.00 22.31  ? 479 LEU   B CD2 1 
ATOM   3151 N N   . ASP   B 1 188 ? 26.849  -20.546 33.634 1.00 29.44  ? 480 ASP   B N   1 
ATOM   3152 C CA  . ASP   B 1 188 ? 27.073  -19.127 33.379 1.00 36.10  ? 480 ASP   B CA  1 
ATOM   3153 C C   . ASP   B 1 188 ? 28.519  -18.863 32.976 1.00 33.41  ? 480 ASP   B C   1 
ATOM   3154 O O   . ASP   B 1 188 ? 28.789  -18.005 32.128 1.00 30.50  ? 480 ASP   B O   1 
ATOM   3155 C CB  . ASP   B 1 188 ? 26.703  -18.308 34.617 1.00 30.17  ? 480 ASP   B CB  1 
ATOM   3156 C CG  . ASP   B 1 188 ? 25.204  -18.130 34.772 1.00 29.44  ? 480 ASP   B CG  1 
ATOM   3157 O OD1 . ASP   B 1 188 ? 24.462  -18.461 33.822 1.00 28.32  ? 480 ASP   B OD1 1 
ATOM   3158 O OD2 . ASP   B 1 188 ? 24.767  -17.665 35.845 1.00 37.43  ? 480 ASP   B OD2 1 
ATOM   3159 N N   . LYS   B 1 189 ? 29.464  -19.596 33.569 1.00 33.92  ? 481 LYS   B N   1 
ATOM   3160 C CA  . LYS   B 1 189 ? 30.869  -19.382 33.241 1.00 35.21  ? 481 LYS   B CA  1 
ATOM   3161 C C   . LYS   B 1 189 ? 31.199  -19.893 31.844 1.00 32.87  ? 481 LYS   B C   1 
ATOM   3162 O O   . LYS   B 1 189 ? 32.012  -19.289 31.134 1.00 34.35  ? 481 LYS   B O   1 
ATOM   3163 C CB  . LYS   B 1 189 ? 31.762  -20.051 34.283 1.00 32.91  ? 481 LYS   B CB  1 
ATOM   3164 C CG  . LYS   B 1 189 ? 33.193  -19.560 34.247 1.00 37.90  ? 481 LYS   B CG  1 
ATOM   3165 C CD  . LYS   B 1 189 ? 33.813  -19.567 35.624 1.00 44.15  ? 481 LYS   B CD  1 
ATOM   3166 C CE  . LYS   B 1 189 ? 35.007  -18.637 35.673 1.00 62.13  ? 481 LYS   B CE  1 
ATOM   3167 N NZ  . LYS   B 1 189 ? 34.611  -17.220 35.900 1.00 62.25  ? 481 LYS   B NZ  1 
ATOM   3168 N N   . ILE   B 1 190 ? 30.587  -21.006 31.434 1.00 28.18  ? 482 ILE   B N   1 
ATOM   3169 C CA  . ILE   B 1 190 ? 30.789  -21.495 30.075 1.00 36.73  ? 482 ILE   B CA  1 
ATOM   3170 C C   . ILE   B 1 190 ? 30.206  -20.513 29.067 1.00 33.59  ? 482 ILE   B C   1 
ATOM   3171 O O   . ILE   B 1 190 ? 30.762  -20.311 27.980 1.00 33.24  ? 482 ILE   B O   1 
ATOM   3172 C CB  . ILE   B 1 190 ? 30.186  -22.902 29.916 1.00 38.44  ? 482 ILE   B CB  1 
ATOM   3173 C CG1 . ILE   B 1 190 ? 30.850  -23.877 30.889 1.00 32.86  ? 482 ILE   B CG1 1 
ATOM   3174 C CG2 . ILE   B 1 190 ? 30.357  -23.398 28.491 1.00 23.75  ? 482 ILE   B CG2 1 
ATOM   3175 C CD1 . ILE   B 1 190 ? 30.140  -25.206 30.995 1.00 32.44  ? 482 ILE   B CD1 1 
ATOM   3176 N N   . THR   B 1 191 ? 29.079  -19.883 29.411 1.00 27.43  ? 483 THR   B N   1 
ATOM   3177 C CA  . THR   B 1 191 ? 28.543  -18.817 28.572 1.00 32.35  ? 483 THR   B CA  1 
ATOM   3178 C C   . THR   B 1 191 ? 29.531  -17.663 28.458 1.00 30.45  ? 483 THR   B C   1 
ATOM   3179 O O   . THR   B 1 191 ? 29.739  -17.120 27.366 1.00 35.42  ? 483 THR   B O   1 
ATOM   3180 C CB  . THR   B 1 191 ? 27.210  -18.320 29.131 1.00 33.15  ? 483 THR   B CB  1 
ATOM   3181 O OG1 . THR   B 1 191 ? 26.275  -19.405 29.191 1.00 33.14  ? 483 THR   B OG1 1 
ATOM   3182 C CG2 . THR   B 1 191 ? 26.645  -17.208 28.256 1.00 32.85  ? 483 THR   B CG2 1 
ATOM   3183 N N   . ASP   B 1 192 ? 30.150  -17.274 29.577 1.00 27.48  ? 484 ASP   B N   1 
ATOM   3184 C CA  . ASP   B 1 192 ? 31.172  -16.233 29.531 1.00 30.53  ? 484 ASP   B CA  1 
ATOM   3185 C C   . ASP   B 1 192 ? 32.369  -16.685 28.709 1.00 35.77  ? 484 ASP   B C   1 
ATOM   3186 O O   . ASP   B 1 192 ? 32.999  -15.876 28.017 1.00 32.42  ? 484 ASP   B O   1 
ATOM   3187 C CB  . ASP   B 1 192 ? 31.615  -15.856 30.946 1.00 32.48  ? 484 ASP   B CB  1 
ATOM   3188 C CG  . ASP   B 1 192 ? 30.491  -15.268 31.772 1.00 41.15  ? 484 ASP   B CG  1 
ATOM   3189 O OD1 . ASP   B 1 192 ? 29.402  -15.031 31.217 1.00 39.98  ? 484 ASP   B OD1 1 
ATOM   3190 O OD2 . ASP   B 1 192 ? 30.692  -15.029 32.978 1.00 46.87  ? 484 ASP   B OD2 1 
ATOM   3191 N N   . THR   B 1 193 ? 32.694  -17.978 28.770 1.00 31.61  ? 485 THR   B N   1 
ATOM   3192 C CA  . THR   B 1 193 ? 33.798  -18.503 27.974 1.00 31.76  ? 485 THR   B CA  1 
ATOM   3193 C C   . THR   B 1 193 ? 33.475  -18.454 26.486 1.00 35.79  ? 485 THR   B C   1 
ATOM   3194 O O   . THR   B 1 193 ? 34.324  -18.065 25.675 1.00 32.26  ? 485 THR   B O   1 
ATOM   3195 C CB  . THR   B 1 193 ? 34.121  -19.933 28.408 1.00 30.45  ? 485 THR   B CB  1 
ATOM   3196 O OG1 . THR   B 1 193 ? 34.468  -19.946 29.798 1.00 32.54  ? 485 THR   B OG1 1 
ATOM   3197 C CG2 . THR   B 1 193 ? 35.278  -20.484 27.599 1.00 37.87  ? 485 THR   B CG2 1 
ATOM   3198 N N   . LEU   B 1 194 ? 32.251  -18.837 26.112 1.00 30.92  ? 486 LEU   B N   1 
ATOM   3199 C CA  . LEU   B 1 194 ? 31.860  -18.799 24.706 1.00 33.14  ? 486 LEU   B CA  1 
ATOM   3200 C C   . LEU   B 1 194 ? 31.882  -17.376 24.164 1.00 30.72  ? 486 LEU   B C   1 
ATOM   3201 O O   . LEU   B 1 194 ? 32.382  -17.133 23.060 1.00 31.40  ? 486 LEU   B O   1 
ATOM   3202 C CB  . LEU   B 1 194 ? 30.473  -19.417 24.530 1.00 27.63  ? 486 LEU   B CB  1 
ATOM   3203 C CG  . LEU   B 1 194 ? 30.434  -20.896 24.148 1.00 35.23  ? 486 LEU   B CG  1 
ATOM   3204 C CD1 . LEU   B 1 194 ? 29.010  -21.429 24.205 1.00 34.65  ? 486 LEU   B CD1 1 
ATOM   3205 C CD2 . LEU   B 1 194 ? 31.038  -21.111 22.767 1.00 34.04  ? 486 LEU   B CD2 1 
ATOM   3206 N N   . ILE   B 1 195 ? 31.344  -16.422 24.928 1.00 30.76  ? 487 ILE   B N   1 
ATOM   3207 C CA  . ILE   B 1 195 ? 31.352  -15.027 24.496 1.00 31.00  ? 487 ILE   B CA  1 
ATOM   3208 C C   . ILE   B 1 195 ? 32.784  -14.519 24.370 1.00 31.84  ? 487 ILE   B C   1 
ATOM   3209 O O   . ILE   B 1 195 ? 33.118  -13.780 23.435 1.00 30.98  ? 487 ILE   B O   1 
ATOM   3210 C CB  . ILE   B 1 195 ? 30.520  -14.168 25.467 1.00 31.89  ? 487 ILE   B CB  1 
ATOM   3211 C CG1 . ILE   B 1 195 ? 29.025  -14.431 25.265 1.00 38.38  ? 487 ILE   B CG1 1 
ATOM   3212 C CG2 . ILE   B 1 195 ? 30.831  -12.688 25.290 1.00 28.49  ? 487 ILE   B CG2 1 
ATOM   3213 C CD1 . ILE   B 1 195 ? 28.447  -13.768 24.031 1.00 28.12  ? 487 ILE   B CD1 1 
ATOM   3214 N N   . HIS   B 1 196 ? 33.655  -14.918 25.300 1.00 33.25  ? 488 HIS   B N   1 
ATOM   3215 C CA  . HIS   B 1 196 ? 35.058  -14.525 25.220 1.00 35.41  ? 488 HIS   B CA  1 
ATOM   3216 C C   . HIS   B 1 196 ? 35.730  -15.125 23.991 1.00 37.48  ? 488 HIS   B C   1 
ATOM   3217 O O   . HIS   B 1 196 ? 36.602  -14.495 23.381 1.00 42.09  ? 488 HIS   B O   1 
ATOM   3218 C CB  . HIS   B 1 196 ? 35.790  -14.943 26.495 1.00 39.01  ? 488 HIS   B CB  1 
ATOM   3219 C CG  . HIS   B 1 196 ? 37.270  -14.718 26.448 1.00 50.45  ? 488 HIS   B CG  1 
ATOM   3220 N ND1 . HIS   B 1 196 ? 38.149  -15.655 25.949 1.00 54.75  ? 488 HIS   B ND1 1 
ATOM   3221 C CD2 . HIS   B 1 196 ? 38.025  -13.665 26.841 1.00 55.34  ? 488 HIS   B CD2 1 
ATOM   3222 C CE1 . HIS   B 1 196 ? 39.382  -15.189 26.036 1.00 50.56  ? 488 HIS   B CE1 1 
ATOM   3223 N NE2 . HIS   B 1 196 ? 39.334  -13.983 26.573 1.00 59.96  ? 488 HIS   B NE2 1 
ATOM   3224 N N   . LEU   B 1 197 ? 35.333  -16.342 23.610 1.00 44.45  ? 489 LEU   B N   1 
ATOM   3225 C CA  . LEU   B 1 197 ? 35.911  -16.977 22.430 1.00 36.02  ? 489 LEU   B CA  1 
ATOM   3226 C C   . LEU   B 1 197 ? 35.567  -16.208 21.161 1.00 38.39  ? 489 LEU   B C   1 
ATOM   3227 O O   . LEU   B 1 197 ? 36.421  -16.026 20.285 1.00 35.94  ? 489 LEU   B O   1 
ATOM   3228 C CB  . LEU   B 1 197 ? 35.429  -18.423 22.324 1.00 39.35  ? 489 LEU   B CB  1 
ATOM   3229 C CG  . LEU   B 1 197 ? 36.121  -19.443 23.229 1.00 39.59  ? 489 LEU   B CG  1 
ATOM   3230 C CD1 . LEU   B 1 197 ? 35.373  -20.765 23.213 1.00 31.27  ? 489 LEU   B CD1 1 
ATOM   3231 C CD2 . LEU   B 1 197 ? 37.563  -19.636 22.795 1.00 41.39  ? 489 LEU   B CD2 1 
ATOM   3232 N N   . MET   B 1 198 ? 34.320  -15.749 21.040 1.00 31.01  ? 490 MET   B N   1 
ATOM   3233 C CA  . MET   B 1 198 ? 33.928  -15.015 19.842 1.00 33.55  ? 490 MET   B CA  1 
ATOM   3234 C C   . MET   B 1 198 ? 34.479  -13.596 19.853 1.00 37.11  ? 490 MET   B C   1 
ATOM   3235 O O   . MET   B 1 198 ? 34.776  -13.040 18.789 1.00 40.27  ? 490 MET   B O   1 
ATOM   3236 C CB  . MET   B 1 198 ? 32.405  -14.999 19.710 1.00 34.92  ? 490 MET   B CB  1 
ATOM   3237 C CG  . MET   B 1 198 ? 31.753  -16.312 20.103 1.00 30.22  ? 490 MET   B CG  1 
ATOM   3238 S SD  . MET   B 1 198 ? 30.014  -16.155 20.542 1.00 35.33  ? 490 MET   B SD  1 
ATOM   3239 C CE  . MET   B 1 198 ? 29.430  -17.799 20.141 1.00 28.50  ? 490 MET   B CE  1 
ATOM   3240 N N   . ALA   B 1 199 ? 34.618  -12.996 21.037 1.00 40.31  ? 491 ALA   B N   1 
ATOM   3241 C CA  . ALA   B 1 199 ? 35.248  -11.684 21.128 1.00 40.42  ? 491 ALA   B CA  1 
ATOM   3242 C C   . ALA   B 1 199 ? 36.704  -11.749 20.688 1.00 38.86  ? 491 ALA   B C   1 
ATOM   3243 O O   . ALA   B 1 199 ? 37.180  -10.874 19.956 1.00 44.76  ? 491 ALA   B O   1 
ATOM   3244 C CB  . ALA   B 1 199 ? 35.140  -11.144 22.553 1.00 38.28  ? 491 ALA   B CB  1 
ATOM   3245 N N   . LYS   B 1 200 ? 37.427  -12.786 21.121 1.00 50.13  ? 492 LYS   B N   1 
ATOM   3246 C CA  . LYS   B 1 200 ? 38.801  -12.971 20.669 1.00 51.80  ? 492 LYS   B CA  1 
ATOM   3247 C C   . LYS   B 1 200 ? 38.865  -13.269 19.177 1.00 42.41  ? 492 LYS   B C   1 
ATOM   3248 O O   . LYS   B 1 200 ? 39.891  -13.009 18.538 1.00 50.22  ? 492 LYS   B O   1 
ATOM   3249 C CB  . LYS   B 1 200 ? 39.472  -14.090 21.466 1.00 45.49  ? 492 LYS   B CB  1 
ATOM   3250 C CG  . LYS   B 1 200 ? 39.779  -13.724 22.907 1.00 53.00  ? 492 LYS   B CG  1 
ATOM   3251 C CD  . LYS   B 1 200 ? 40.711  -12.526 22.986 1.00 58.40  ? 492 LYS   B CD  1 
ATOM   3252 C CE  . LYS   B 1 200 ? 41.395  -12.445 24.341 1.00 68.97  ? 492 LYS   B CE  1 
ATOM   3253 N NZ  . LYS   B 1 200 ? 42.421  -13.510 24.513 1.00 69.59  ? 492 LYS   B NZ  1 
ATOM   3254 N N   . ALA   B 1 201 ? 37.790  -13.813 18.607 1.00 44.64  ? 493 ALA   B N   1 
ATOM   3255 C CA  . ALA   B 1 201 ? 37.739  -14.033 17.169 1.00 41.79  ? 493 ALA   B CA  1 
ATOM   3256 C C   . ALA   B 1 201 ? 37.483  -12.750 16.390 1.00 54.61  ? 493 ALA   B C   1 
ATOM   3257 O O   . ALA   B 1 201 ? 37.561  -12.768 15.157 1.00 54.58  ? 493 ALA   B O   1 
ATOM   3258 C CB  . ALA   B 1 201 ? 36.664  -15.068 16.831 1.00 37.51  ? 493 ALA   B CB  1 
ATOM   3259 N N   . GLY   B 1 202 ? 37.185  -11.646 17.072 1.00 47.57  ? 494 GLY   B N   1 
ATOM   3260 C CA  . GLY   B 1 202 ? 36.922  -10.381 16.421 1.00 46.85  ? 494 GLY   B CA  1 
ATOM   3261 C C   . GLY   B 1 202 ? 35.461  -10.078 16.175 1.00 48.96  ? 494 GLY   B C   1 
ATOM   3262 O O   . GLY   B 1 202 ? 35.156  -9.039  15.576 1.00 55.32  ? 494 GLY   B O   1 
ATOM   3263 N N   . LEU   B 1 203 ? 34.553  -10.946 16.612 1.00 42.38  ? 495 LEU   B N   1 
ATOM   3264 C CA  . LEU   B 1 203 ? 33.132  -10.709 16.408 1.00 45.29  ? 495 LEU   B CA  1 
ATOM   3265 C C   . LEU   B 1 203 ? 32.675  -9.487  17.193 1.00 45.41  ? 495 LEU   B C   1 
ATOM   3266 O O   . LEU   B 1 203 ? 33.086  -9.275  18.338 1.00 37.80  ? 495 LEU   B O   1 
ATOM   3267 C CB  . LEU   B 1 203 ? 32.319  -11.935 16.831 1.00 33.55  ? 495 LEU   B CB  1 
ATOM   3268 C CG  . LEU   B 1 203 ? 32.096  -13.057 15.812 1.00 47.69  ? 495 LEU   B CG  1 
ATOM   3269 C CD1 . LEU   B 1 203 ? 33.403  -13.739 15.429 1.00 40.57  ? 495 LEU   B CD1 1 
ATOM   3270 C CD2 . LEU   B 1 203 ? 31.095  -14.072 16.346 1.00 36.25  ? 495 LEU   B CD2 1 
ATOM   3271 N N   . THR   B 1 204 ? 31.824  -8.678  16.568 1.00 45.35  ? 496 THR   B N   1 
ATOM   3272 C CA  . THR   B 1 204 ? 31.228  -7.547  17.257 1.00 39.51  ? 496 THR   B CA  1 
ATOM   3273 C C   . THR   B 1 204 ? 30.287  -8.039  18.355 1.00 35.92  ? 496 THR   B C   1 
ATOM   3274 O O   . THR   B 1 204 ? 29.920  -9.216  18.418 1.00 35.39  ? 496 THR   B O   1 
ATOM   3275 C CB  . THR   B 1 204 ? 30.471  -6.653  16.276 1.00 41.76  ? 496 THR   B CB  1 
ATOM   3276 O OG1 . THR   B 1 204 ? 29.246  -7.293  15.895 1.00 46.28  ? 496 THR   B OG1 1 
ATOM   3277 C CG2 . THR   B 1 204 ? 31.312  -6.393  15.034 1.00 42.95  ? 496 THR   B CG2 1 
ATOM   3278 N N   . LEU   B 1 205 ? 29.893  -7.112  19.232 1.00 37.39  ? 497 LEU   B N   1 
ATOM   3279 C CA  . LEU   B 1 205 ? 29.003  -7.468  20.332 1.00 34.84  ? 497 LEU   B CA  1 
ATOM   3280 C C   . LEU   B 1 205 ? 27.684  -8.027  19.817 1.00 35.39  ? 497 LEU   B C   1 
ATOM   3281 O O   . LEU   B 1 205 ? 27.138  -8.980  20.388 1.00 36.02  ? 497 LEU   B O   1 
ATOM   3282 C CB  . LEU   B 1 205 ? 28.760  -6.253  21.225 1.00 40.55  ? 497 LEU   B CB  1 
ATOM   3283 C CG  . LEU   B 1 205 ? 29.760  -6.077  22.367 1.00 55.20  ? 497 LEU   B CG  1 
ATOM   3284 C CD1 . LEU   B 1 205 ? 29.429  -4.838  23.185 1.00 47.63  ? 497 LEU   B CD1 1 
ATOM   3285 C CD2 . LEU   B 1 205 ? 29.793  -7.322  23.243 1.00 39.05  ? 497 LEU   B CD2 1 
ATOM   3286 N N   . GLN   B 1 206 ? 27.157  -7.451  18.734 1.00 34.22  ? 498 GLN   B N   1 
ATOM   3287 C CA  . GLN   B 1 206 ? 25.940  -7.987  18.135 1.00 44.20  ? 498 GLN   B CA  1 
ATOM   3288 C C   . GLN   B 1 206 ? 26.186  -9.366  17.537 1.00 33.68  ? 498 GLN   B C   1 
ATOM   3289 O O   . GLN   B 1 206 ? 25.359  -10.272 17.692 1.00 31.74  ? 498 GLN   B O   1 
ATOM   3290 C CB  . GLN   B 1 206 ? 25.408  -7.029  17.070 1.00 38.97  ? 498 GLN   B CB  1 
ATOM   3291 C CG  . GLN   B 1 206 ? 24.176  -7.543  16.345 1.00 39.07  ? 498 GLN   B CG  1 
ATOM   3292 C CD  . GLN   B 1 206 ? 23.629  -6.547  15.343 1.00 41.71  ? 498 GLN   B CD  1 
ATOM   3293 O OE1 . GLN   B 1 206 ? 24.378  -5.955  14.567 1.00 43.99  ? 498 GLN   B OE1 1 
ATOM   3294 N NE2 . GLN   B 1 206 ? 22.315  -6.358  15.354 1.00 37.82  ? 498 GLN   B NE2 1 
ATOM   3295 N N   . GLN   B 1 207 ? 27.319  -9.544  16.852 1.00 31.96  ? 499 GLN   B N   1 
ATOM   3296 C CA  . GLN   B 1 207 ? 27.647  -10.850 16.295 1.00 30.64  ? 499 GLN   B CA  1 
ATOM   3297 C C   . GLN   B 1 207 ? 27.866  -11.886 17.387 1.00 28.84  ? 499 GLN   B C   1 
ATOM   3298 O O   . GLN   B 1 207 ? 27.622  -13.078 17.169 1.00 29.03  ? 499 GLN   B O   1 
ATOM   3299 C CB  . GLN   B 1 207 ? 28.890  -10.748 15.412 1.00 34.35  ? 499 GLN   B CB  1 
ATOM   3300 C CG  . GLN   B 1 207 ? 28.666  -10.027 14.099 1.00 35.17  ? 499 GLN   B CG  1 
ATOM   3301 C CD  . GLN   B 1 207 ? 29.964  -9.730  13.381 1.00 37.83  ? 499 GLN   B CD  1 
ATOM   3302 O OE1 . GLN   B 1 207 ? 31.014  -9.590  14.008 1.00 42.62  ? 499 GLN   B OE1 1 
ATOM   3303 N NE2 . GLN   B 1 207 ? 29.901  -9.634  12.059 1.00 40.72  ? 499 GLN   B NE2 1 
ATOM   3304 N N   . GLN   B 1 208 ? 28.323  -11.454 18.565 1.00 28.47  ? 500 GLN   B N   1 
ATOM   3305 C CA  . GLN   B 1 208 ? 28.583  -12.388 19.655 1.00 30.77  ? 500 GLN   B CA  1 
ATOM   3306 C C   . GLN   B 1 208 ? 27.289  -13.001 20.177 1.00 25.91  ? 500 GLN   B C   1 
ATOM   3307 O O   . GLN   B 1 208 ? 27.127  -14.226 20.182 1.00 28.90  ? 500 GLN   B O   1 
ATOM   3308 C CB  . GLN   B 1 208 ? 29.340  -11.684 20.783 1.00 28.42  ? 500 GLN   B CB  1 
ATOM   3309 C CG  . GLN   B 1 208 ? 30.809  -11.436 20.491 1.00 31.38  ? 500 GLN   B CG  1 
ATOM   3310 C CD  . GLN   B 1 208 ? 31.445  -10.488 21.487 1.00 39.55  ? 500 GLN   B CD  1 
ATOM   3311 O OE1 . GLN   B 1 208 ? 31.248  -10.616 22.696 1.00 35.49  ? 500 GLN   B OE1 1 
ATOM   3312 N NE2 . GLN   B 1 208 ? 32.215  -9.530  20.985 1.00 35.37  ? 500 GLN   B NE2 1 
ATOM   3313 N N   . HIS   B 1 209 ? 26.352  -12.162 20.627 1.00 26.25  ? 501 HIS   B N   1 
ATOM   3314 C CA  . HIS   B 1 209 ? 25.113  -12.698 21.174 1.00 28.39  ? 501 HIS   B CA  1 
ATOM   3315 C C   . HIS   B 1 209 ? 24.235  -13.329 20.101 1.00 28.25  ? 501 HIS   B C   1 
ATOM   3316 O O   . HIS   B 1 209 ? 23.401  -14.181 20.426 1.00 27.49  ? 501 HIS   B O   1 
ATOM   3317 C CB  . HIS   B 1 209 ? 24.345  -11.616 21.947 1.00 34.38  ? 501 HIS   B CB  1 
ATOM   3318 C CG  . HIS   B 1 209 ? 23.827  -10.490 21.103 1.00 34.14  ? 501 HIS   B CG  1 
ATOM   3319 N ND1 . HIS   B 1 209 ? 24.131  -9.171  21.365 1.00 42.18  ? 501 HIS   B ND1 1 
ATOM   3320 C CD2 . HIS   B 1 209 ? 22.994  -10.477 20.035 1.00 33.69  ? 501 HIS   B CD2 1 
ATOM   3321 C CE1 . HIS   B 1 209 ? 23.526  -8.397  20.481 1.00 41.21  ? 501 HIS   B CE1 1 
ATOM   3322 N NE2 . HIS   B 1 209 ? 22.831  -9.164  19.662 1.00 36.99  ? 501 HIS   B NE2 1 
ATOM   3323 N N   . GLN   B 1 210 ? 24.409  -12.946 18.835 1.00 28.57  ? 502 GLN   B N   1 
ATOM   3324 C CA  . GLN   B 1 210 ? 23.695  -13.632 17.763 1.00 29.54  ? 502 GLN   B CA  1 
ATOM   3325 C C   . GLN   B 1 210 ? 24.233  -15.043 17.561 1.00 31.35  ? 502 GLN   B C   1 
ATOM   3326 O O   . GLN   B 1 210 ? 23.456  -15.993 17.410 1.00 28.03  ? 502 GLN   B O   1 
ATOM   3327 C CB  . GLN   B 1 210 ? 23.790  -12.832 16.464 1.00 26.22  ? 502 GLN   B CB  1 
ATOM   3328 C CG  . GLN   B 1 210 ? 22.746  -11.737 16.325 1.00 27.55  ? 502 GLN   B CG  1 
ATOM   3329 C CD  . GLN   B 1 210 ? 22.923  -10.931 15.054 1.00 35.68  ? 502 GLN   B CD  1 
ATOM   3330 O OE1 . GLN   B 1 210 ? 23.666  -11.326 14.155 1.00 32.48  ? 502 GLN   B OE1 1 
ATOM   3331 N NE2 . GLN   B 1 210 ? 22.229  -9.802  14.965 1.00 36.78  ? 502 GLN   B NE2 1 
ATOM   3332 N N   . ARG   B 1 211 ? 25.559  -15.198 17.561 1.00 25.02  ? 503 ARG   B N   1 
ATOM   3333 C CA  . ARG   B 1 211 ? 26.148  -16.518 17.363 1.00 29.16  ? 503 ARG   B CA  1 
ATOM   3334 C C   . ARG   B 1 211 ? 25.925  -17.411 18.577 1.00 27.67  ? 503 ARG   B C   1 
ATOM   3335 O O   . ARG   B 1 211 ? 25.682  -18.615 18.431 1.00 24.80  ? 503 ARG   B O   1 
ATOM   3336 C CB  . ARG   B 1 211 ? 27.639  -16.390 17.061 1.00 25.14  ? 503 ARG   B CB  1 
ATOM   3337 C CG  . ARG   B 1 211 ? 28.320  -17.716 16.766 1.00 26.71  ? 503 ARG   B CG  1 
ATOM   3338 C CD  . ARG   B 1 211 ? 29.744  -17.506 16.284 1.00 26.05  ? 503 ARG   B CD  1 
ATOM   3339 N NE  . ARG   B 1 211 ? 30.427  -18.769 16.036 1.00 33.76  ? 503 ARG   B NE  1 
ATOM   3340 C CZ  . ARG   B 1 211 ? 30.393  -19.426 14.885 1.00 41.64  ? 503 ARG   B CZ  1 
ATOM   3341 N NH1 . ARG   B 1 211 ? 29.708  -18.969 13.850 1.00 36.70  ? 503 ARG   B NH1 1 
ATOM   3342 N NH2 . ARG   B 1 211 ? 31.062  -20.570 14.771 1.00 41.99  ? 503 ARG   B NH2 1 
ATOM   3343 N N   . LEU   B 1 212 ? 26.019  -16.844 19.783 1.00 21.40  ? 504 LEU   B N   1 
ATOM   3344 C CA  . LEU   B 1 212 ? 25.718  -17.615 20.986 1.00 28.38  ? 504 LEU   B CA  1 
ATOM   3345 C C   . LEU   B 1 212 ? 24.301  -18.168 20.937 1.00 24.22  ? 504 LEU   B C   1 
ATOM   3346 O O   . LEU   B 1 212 ? 24.072  -19.339 21.258 1.00 26.97  ? 504 LEU   B O   1 
ATOM   3347 C CB  . LEU   B 1 212 ? 25.913  -16.751 22.233 1.00 20.02  ? 504 LEU   B CB  1 
ATOM   3348 C CG  . LEU   B 1 212 ? 25.437  -17.363 23.553 1.00 21.69  ? 504 LEU   B CG  1 
ATOM   3349 C CD1 . LEU   B 1 212 ? 26.392  -18.451 24.030 1.00 18.98  ? 504 LEU   B CD1 1 
ATOM   3350 C CD2 . LEU   B 1 212 ? 25.261  -16.290 24.618 1.00 24.13  ? 504 LEU   B CD2 1 
ATOM   3351 N N   . ALA   B 1 213 ? 23.337  -17.341 20.525 1.00 24.15  ? 505 ALA   B N   1 
ATOM   3352 C CA  . ALA   B 1 213 ? 21.962  -17.811 20.399 1.00 19.05  ? 505 ALA   B CA  1 
ATOM   3353 C C   . ALA   B 1 213 ? 21.849  -18.913 19.354 1.00 20.98  ? 505 ALA   B C   1 
ATOM   3354 O O   . ALA   B 1 213 ? 21.158  -19.915 19.572 1.00 23.50  ? 505 ALA   B O   1 
ATOM   3355 C CB  . ALA   B 1 213 ? 21.039  -16.644 20.052 1.00 21.88  ? 505 ALA   B CB  1 
ATOM   3356 N N   . GLN   B 1 214 ? 22.522  -18.745 18.213 1.00 23.63  ? 506 GLN   B N   1 
ATOM   3357 C CA  . GLN   B 1 214 ? 22.492  -19.775 17.179 1.00 19.26  ? 506 GLN   B CA  1 
ATOM   3358 C C   . GLN   B 1 214 ? 23.062  -21.090 17.694 1.00 28.05  ? 506 GLN   B C   1 
ATOM   3359 O O   . GLN   B 1 214 ? 22.548  -22.167 17.372 1.00 26.01  ? 506 GLN   B O   1 
ATOM   3360 C CB  . GLN   B 1 214 ? 23.269  -19.308 15.949 1.00 23.41  ? 506 GLN   B CB  1 
ATOM   3361 C CG  . GLN   B 1 214 ? 22.611  -18.183 15.177 1.00 27.45  ? 506 GLN   B CG  1 
ATOM   3362 C CD  . GLN   B 1 214 ? 23.619  -17.333 14.430 1.00 35.36  ? 506 GLN   B CD  1 
ATOM   3363 O OE1 . GLN   B 1 214 ? 24.781  -17.714 14.282 1.00 32.05  ? 506 GLN   B OE1 1 
ATOM   3364 N NE2 . GLN   B 1 214 ? 23.179  -16.176 13.953 1.00 34.30  ? 506 GLN   B NE2 1 
ATOM   3365 N N   . LEU   B 1 215 ? 24.124  -21.020 18.499 1.00 24.39  ? 507 LEU   B N   1 
ATOM   3366 C CA  . LEU   B 1 215 ? 24.738  -22.233 19.030 1.00 22.07  ? 507 LEU   B CA  1 
ATOM   3367 C C   . LEU   B 1 215 ? 23.813  -22.929 20.020 1.00 25.09  ? 507 LEU   B C   1 
ATOM   3368 O O   . LEU   B 1 215 ? 23.619  -24.149 19.954 1.00 25.27  ? 507 LEU   B O   1 
ATOM   3369 C CB  . LEU   B 1 215 ? 26.075  -21.896 19.690 1.00 25.29  ? 507 LEU   B CB  1 
ATOM   3370 C CG  . LEU   B 1 215 ? 27.263  -21.703 18.749 1.00 27.29  ? 507 LEU   B CG  1 
ATOM   3371 C CD1 . LEU   B 1 215 ? 28.537  -21.431 19.534 1.00 26.38  ? 507 LEU   B CD1 1 
ATOM   3372 C CD2 . LEU   B 1 215 ? 27.422  -22.925 17.867 1.00 31.09  ? 507 LEU   B CD2 1 
ATOM   3373 N N   . LEU   B 1 216 ? 23.232  -22.167 20.947 1.00 21.57  ? 508 LEU   B N   1 
ATOM   3374 C CA  . LEU   B 1 216 ? 22.380  -22.769 21.965 1.00 25.48  ? 508 LEU   B CA  1 
ATOM   3375 C C   . LEU   B 1 216 ? 21.067  -23.271 21.381 1.00 23.64  ? 508 LEU   B C   1 
ATOM   3376 O O   . LEU   B 1 216 ? 20.475  -24.214 21.918 1.00 22.61  ? 508 LEU   B O   1 
ATOM   3377 C CB  . LEU   B 1 216 ? 22.122  -21.764 23.085 1.00 18.28  ? 508 LEU   B CB  1 
ATOM   3378 C CG  . LEU   B 1 216 ? 23.393  -21.230 23.747 1.00 25.41  ? 508 LEU   B CG  1 
ATOM   3379 C CD1 . LEU   B 1 216 ? 23.043  -20.420 24.964 1.00 20.15  ? 508 LEU   B CD1 1 
ATOM   3380 C CD2 . LEU   B 1 216 ? 24.332  -22.367 24.120 1.00 22.79  ? 508 LEU   B CD2 1 
ATOM   3381 N N   . LEU   B 1 217 ? 20.595  -22.665 20.289 1.00 19.85  ? 509 LEU   B N   1 
ATOM   3382 C CA  . LEU   B 1 217 ? 19.389  -23.163 19.640 1.00 22.69  ? 509 LEU   B CA  1 
ATOM   3383 C C   . LEU   B 1 217 ? 19.629  -24.487 18.928 1.00 28.31  ? 509 LEU   B C   1 
ATOM   3384 O O   . LEU   B 1 217 ? 18.678  -25.251 18.729 1.00 29.10  ? 509 LEU   B O   1 
ATOM   3385 C CB  . LEU   B 1 217 ? 18.849  -22.126 18.656 1.00 19.66  ? 509 LEU   B CB  1 
ATOM   3386 C CG  . LEU   B 1 217 ? 18.102  -20.961 19.306 1.00 24.40  ? 509 LEU   B CG  1 
ATOM   3387 C CD1 . LEU   B 1 217 ? 17.611  -19.974 18.255 1.00 30.65  ? 509 LEU   B CD1 1 
ATOM   3388 C CD2 . LEU   B 1 217 ? 16.949  -21.478 20.155 1.00 19.11  ? 509 LEU   B CD2 1 
ATOM   3389 N N   . ILE   B 1 218 ? 20.874  -24.769 18.537 1.00 28.35  ? 510 ILE   B N   1 
ATOM   3390 C CA  . ILE   B 1 218 ? 21.208  -26.079 17.988 1.00 34.90  ? 510 ILE   B CA  1 
ATOM   3391 C C   . ILE   B 1 218 ? 21.034  -27.157 19.048 1.00 29.47  ? 510 ILE   B C   1 
ATOM   3392 O O   . ILE   B 1 218 ? 20.671  -28.298 18.735 1.00 25.50  ? 510 ILE   B O   1 
ATOM   3393 C CB  . ILE   B 1 218 ? 22.641  -26.062 17.418 1.00 34.19  ? 510 ILE   B CB  1 
ATOM   3394 C CG1 . ILE   B 1 218 ? 22.701  -25.213 16.148 1.00 38.20  ? 510 ILE   B CG1 1 
ATOM   3395 C CG2 . ILE   B 1 218 ? 23.136  -27.470 17.123 1.00 37.01  ? 510 ILE   B CG2 1 
ATOM   3396 C CD1 . ILE   B 1 218 ? 24.109  -24.906 15.696 1.00 37.35  ? 510 ILE   B CD1 1 
ATOM   3397 N N   . LEU   B 1 219 ? 21.262  -26.810 20.319 1.00 25.50  ? 511 LEU   B N   1 
ATOM   3398 C CA  . LEU   B 1 219 ? 21.134  -27.792 21.391 1.00 26.34  ? 511 LEU   B CA  1 
ATOM   3399 C C   . LEU   B 1 219 ? 19.711  -28.321 21.507 1.00 27.10  ? 511 LEU   B C   1 
ATOM   3400 O O   . LEU   B 1 219 ? 19.510  -29.469 21.920 1.00 25.78  ? 511 LEU   B O   1 
ATOM   3401 C CB  . LEU   B 1 219 ? 21.584  -27.181 22.717 1.00 25.93  ? 511 LEU   B CB  1 
ATOM   3402 C CG  . LEU   B 1 219 ? 23.063  -26.799 22.812 1.00 31.42  ? 511 LEU   B CG  1 
ATOM   3403 C CD1 . LEU   B 1 219 ? 23.468  -26.613 24.264 1.00 36.09  ? 511 LEU   B CD1 1 
ATOM   3404 C CD2 . LEU   B 1 219 ? 23.942  -27.839 22.131 1.00 21.62  ? 511 LEU   B CD2 1 
ATOM   3405 N N   A SER   B 1 220 ? 18.715  -27.504 21.157 0.75 26.36  ? 512 SER   B N   1 
ATOM   3406 N N   B SER   B 1 220 ? 18.713  -27.509 21.149 0.25 26.47  ? 512 SER   B N   1 
ATOM   3407 C CA  A SER   B 1 220 ? 17.336  -27.980 21.168 0.75 32.66  ? 512 SER   B CA  1 
ATOM   3408 C CA  B SER   B 1 220 ? 17.335  -27.987 21.179 0.25 29.50  ? 512 SER   B CA  1 
ATOM   3409 C C   A SER   B 1 220 ? 17.129  -29.071 20.127 0.75 34.44  ? 512 SER   B C   1 
ATOM   3410 C C   B SER   B 1 220 ? 17.084  -29.037 20.104 0.25 32.32  ? 512 SER   B C   1 
ATOM   3411 O O   A SER   B 1 220 ? 16.380  -30.028 20.359 0.75 27.95  ? 512 SER   B O   1 
ATOM   3412 O O   B SER   B 1 220 ? 16.253  -29.932 20.296 0.25 28.04  ? 512 SER   B O   1 
ATOM   3413 C CB  A SER   B 1 220 ? 16.375  -26.816 20.926 0.75 29.26  ? 512 SER   B CB  1 
ATOM   3414 C CB  B SER   B 1 220 ? 16.365  -26.815 21.021 0.25 27.29  ? 512 SER   B CB  1 
ATOM   3415 O OG  A SER   B 1 220 ? 16.069  -26.149 22.136 0.75 28.59  ? 512 SER   B OG  1 
ATOM   3416 O OG  B SER   B 1 220 ? 16.566  -26.143 19.790 0.25 30.56  ? 512 SER   B OG  1 
ATOM   3417 N N   . HIS   B 1 221 ? 17.787  -28.945 18.973 1.00 25.06  ? 513 HIS   B N   1 
ATOM   3418 C CA  . HIS   B 1 221 ? 17.686  -29.979 17.950 1.00 22.85  ? 513 HIS   B CA  1 
ATOM   3419 C C   . HIS   B 1 221 ? 18.428  -31.244 18.366 1.00 25.19  ? 513 HIS   B C   1 
ATOM   3420 O O   . HIS   B 1 221 ? 17.996  -32.353 18.033 1.00 20.44  ? 513 HIS   B O   1 
ATOM   3421 C CB  . HIS   B 1 221 ? 18.229  -29.452 16.621 1.00 29.88  ? 513 HIS   B CB  1 
ATOM   3422 C CG  . HIS   B 1 221 ? 18.167  -30.446 15.503 1.00 32.85  ? 513 HIS   B CG  1 
ATOM   3423 N ND1 . HIS   B 1 221 ? 16.993  -30.771 14.860 1.00 38.83  ? 513 HIS   B ND1 1 
ATOM   3424 C CD2 . HIS   B 1 221 ? 19.137  -31.183 14.912 1.00 24.22  ? 513 HIS   B CD2 1 
ATOM   3425 C CE1 . HIS   B 1 221 ? 17.242  -31.667 13.921 1.00 29.79  ? 513 HIS   B CE1 1 
ATOM   3426 N NE2 . HIS   B 1 221 ? 18.535  -31.934 13.933 1.00 31.36  ? 513 HIS   B NE2 1 
ATOM   3427 N N   . ILE   B 1 222 ? 19.535  -31.098 19.097 1.00 21.29  ? 514 ILE   B N   1 
ATOM   3428 C CA  . ILE   B 1 222 ? 20.268  -32.267 19.573 1.00 25.86  ? 514 ILE   B CA  1 
ATOM   3429 C C   . ILE   B 1 222 ? 19.459  -33.008 20.631 1.00 21.11  ? 514 ILE   B C   1 
ATOM   3430 O O   . ILE   B 1 222 ? 19.443  -34.244 20.667 1.00 21.01  ? 514 ILE   B O   1 
ATOM   3431 C CB  . ILE   B 1 222 ? 21.656  -31.846 20.091 1.00 27.72  ? 514 ILE   B CB  1 
ATOM   3432 C CG1 . ILE   B 1 222 ? 22.516  -31.344 18.929 1.00 23.73  ? 514 ILE   B CG1 1 
ATOM   3433 C CG2 . ILE   B 1 222 ? 22.346  -33.005 20.797 1.00 24.83  ? 514 ILE   B CG2 1 
ATOM   3434 C CD1 . ILE   B 1 222 ? 23.767  -30.618 19.359 1.00 26.15  ? 514 ILE   B CD1 1 
ATOM   3435 N N   . ARG   B 1 223 ? 18.768  -32.267 21.503 1.00 23.44  ? 515 ARG   B N   1 
ATOM   3436 C CA  . ARG   B 1 223 ? 17.830  -32.899 22.427 1.00 20.88  ? 515 ARG   B CA  1 
ATOM   3437 C C   . ARG   B 1 223 ? 16.734  -33.639 21.672 1.00 25.34  ? 515 ARG   B C   1 
ATOM   3438 O O   . ARG   B 1 223 ? 16.348  -34.751 22.051 1.00 23.85  ? 515 ARG   B O   1 
ATOM   3439 C CB  . ARG   B 1 223 ? 17.214  -31.852 23.354 1.00 22.56  ? 515 ARG   B CB  1 
ATOM   3440 C CG  . ARG   B 1 223 ? 16.292  -32.439 24.411 1.00 21.84  ? 515 ARG   B CG  1 
ATOM   3441 C CD  . ARG   B 1 223 ? 17.093  -33.156 25.481 1.00 30.05  ? 515 ARG   B CD  1 
ATOM   3442 N NE  . ARG   B 1 223 ? 17.870  -32.201 26.259 1.00 38.06  ? 515 ARG   B NE  1 
ATOM   3443 C CZ  . ARG   B 1 223 ? 17.467  -31.667 27.404 1.00 44.83  ? 515 ARG   B CZ  1 
ATOM   3444 N NH1 . ARG   B 1 223 ? 16.333  -32.034 27.977 1.00 32.62  ? 515 ARG   B NH1 1 
ATOM   3445 N NH2 . ARG   B 1 223 ? 18.213  -30.730 27.980 1.00 37.57  ? 515 ARG   B NH2 1 
ATOM   3446 N N   . HIS   B 1 224 ? 16.219  -33.029 20.600 1.00 23.59  ? 516 HIS   B N   1 
ATOM   3447 C CA  . HIS   B 1 224 ? 15.196  -33.676 19.784 1.00 19.89  ? 516 HIS   B CA  1 
ATOM   3448 C C   . HIS   B 1 224 ? 15.707  -34.983 19.194 1.00 25.26  ? 516 HIS   B C   1 
ATOM   3449 O O   . HIS   B 1 224 ? 14.993  -35.993 19.186 1.00 26.46  ? 516 HIS   B O   1 
ATOM   3450 C CB  . HIS   B 1 224 ? 14.745  -32.724 18.676 1.00 26.73  ? 516 HIS   B CB  1 
ATOM   3451 C CG  . HIS   B 1 224 ? 13.655  -33.271 17.807 1.00 28.62  ? 516 HIS   B CG  1 
ATOM   3452 N ND1 . HIS   B 1 224 ? 12.334  -33.302 18.200 1.00 37.17  ? 516 HIS   B ND1 1 
ATOM   3453 C CD2 . HIS   B 1 224 ? 13.689  -33.801 16.562 1.00 32.26  ? 516 HIS   B CD2 1 
ATOM   3454 C CE1 . HIS   B 1 224 ? 11.602  -33.829 17.235 1.00 32.88  ? 516 HIS   B CE1 1 
ATOM   3455 N NE2 . HIS   B 1 224 ? 12.401  -34.142 16.230 1.00 34.92  ? 516 HIS   B NE2 1 
ATOM   3456 N N   . MET   B 1 225 ? 16.948  -34.984 18.700 1.00 23.83  ? 517 MET   B N   1 
ATOM   3457 C CA  . MET   B 1 225 ? 17.528  -36.203 18.149 1.00 25.99  ? 517 MET   B CA  1 
ATOM   3458 C C   . MET   B 1 225 ? 17.716  -37.260 19.228 1.00 25.50  ? 517 MET   B C   1 
ATOM   3459 O O   . MET   B 1 225 ? 17.508  -38.454 18.983 1.00 28.01  ? 517 MET   B O   1 
ATOM   3460 C CB  . MET   B 1 225 ? 18.862  -35.884 17.477 1.00 24.78  ? 517 MET   B CB  1 
ATOM   3461 C CG  . MET   B 1 225 ? 18.739  -35.071 16.204 1.00 25.69  ? 517 MET   B CG  1 
ATOM   3462 S SD  . MET   B 1 225 ? 20.282  -35.043 15.278 1.00 32.49  ? 517 MET   B SD  1 
ATOM   3463 C CE  . MET   B 1 225 ? 21.338  -34.145 16.411 1.00 27.21  ? 517 MET   B CE  1 
ATOM   3464 N N   . SER   B 1 226 ? 18.112  -36.838 20.431 1.00 24.43  ? 518 SER   B N   1 
ATOM   3465 C CA  . SER   B 1 226 ? 18.297  -37.785 21.526 1.00 25.33  ? 518 SER   B CA  1 
ATOM   3466 C C   . SER   B 1 226 ? 16.978  -38.428 21.931 1.00 26.63  ? 518 SER   B C   1 
ATOM   3467 O O   . SER   B 1 226 ? 16.927  -39.633 22.204 1.00 27.80  ? 518 SER   B O   1 
ATOM   3468 C CB  . SER   B 1 226 ? 18.939  -37.084 22.721 1.00 23.11  ? 518 SER   B CB  1 
ATOM   3469 O OG  . SER   B 1 226 ? 19.190  -37.998 23.774 1.00 53.75  ? 518 SER   B OG  1 
ATOM   3470 N N   . ASN   B 1 227 ? 15.901  -37.640 21.986 1.00 27.74  ? 519 ASN   B N   1 
ATOM   3471 C CA  . ASN   B 1 227 ? 14.592  -38.197 22.309 1.00 28.37  ? 519 ASN   B CA  1 
ATOM   3472 C C   . ASN   B 1 227 ? 14.156  -39.204 21.253 1.00 29.15  ? 519 ASN   B C   1 
ATOM   3473 O O   . ASN   B 1 227 ? 13.701  -40.306 21.578 1.00 31.70  ? 519 ASN   B O   1 
ATOM   3474 C CB  . ASN   B 1 227 ? 13.559  -37.077 22.444 1.00 30.58  ? 519 ASN   B CB  1 
ATOM   3475 C CG  . ASN   B 1 227 ? 13.843  -36.158 23.615 1.00 38.41  ? 519 ASN   B CG  1 
ATOM   3476 O OD1 . ASN   B 1 227 ? 14.303  -36.598 24.669 1.00 37.42  ? 519 ASN   B OD1 1 
ATOM   3477 N ND2 . ASN   B 1 227 ? 13.560  -34.872 23.440 1.00 32.48  ? 519 ASN   B ND2 1 
ATOM   3478 N N   . LYS   B 1 228 ? 14.291  -38.838 19.975 1.00 28.52  ? 520 LYS   B N   1 
ATOM   3479 C CA  . LYS   B 1 228 ? 13.978  -39.778 18.904 1.00 33.24  ? 520 LYS   B CA  1 
ATOM   3480 C C   . LYS   B 1 228 ? 14.955  -40.945 18.887 1.00 32.34  ? 520 LYS   B C   1 
ATOM   3481 O O   . LYS   B 1 228 ? 14.576  -42.061 18.516 1.00 37.32  ? 520 LYS   B O   1 
ATOM   3482 C CB  . LYS   B 1 228 ? 13.980  -39.062 17.554 1.00 31.40  ? 520 LYS   B CB  1 
ATOM   3483 C CG  . LYS   B 1 228 ? 13.017  -37.888 17.472 1.00 33.83  ? 520 LYS   B CG  1 
ATOM   3484 C CD  . LYS   B 1 228 ? 11.707  -38.286 16.814 1.00 41.14  ? 520 LYS   B CD  1 
ATOM   3485 C CE  . LYS   B 1 228 ? 10.616  -37.265 17.100 1.00 45.51  ? 520 LYS   B CE  1 
ATOM   3486 N NZ  . LYS   B 1 228 ? 9.254   -37.849 16.960 1.00 52.10  ? 520 LYS   B NZ  1 
ATOM   3487 N N   . GLY   B 1 229 ? 16.208  -40.708 19.284 1.00 31.80  ? 521 GLY   B N   1 
ATOM   3488 C CA  . GLY   B 1 229 ? 17.158  -41.804 19.387 1.00 32.14  ? 521 GLY   B CA  1 
ATOM   3489 C C   . GLY   B 1 229 ? 16.756  -42.813 20.445 1.00 33.21  ? 521 GLY   B C   1 
ATOM   3490 O O   . GLY   B 1 229 ? 16.710  -44.018 20.188 1.00 43.14  ? 521 GLY   B O   1 
ATOM   3491 N N   . MET   B 1 230 ? 16.457  -42.329 21.654 1.00 32.88  ? 522 MET   B N   1 
ATOM   3492 C CA  . MET   B 1 230 ? 15.949  -43.204 22.706 1.00 38.55  ? 522 MET   B CA  1 
ATOM   3493 C C   . MET   B 1 230 ? 14.694  -43.931 22.246 1.00 48.52  ? 522 MET   B C   1 
ATOM   3494 O O   . MET   B 1 230 ? 14.537  -45.136 22.474 1.00 50.95  ? 522 MET   B O   1 
ATOM   3495 C CB  . MET   B 1 230 ? 15.656  -42.388 23.964 1.00 30.15  ? 522 MET   B CB  1 
ATOM   3496 C CG  . MET   B 1 230 ? 16.880  -41.793 24.619 1.00 33.41  ? 522 MET   B CG  1 
ATOM   3497 S SD  . MET   B 1 230 ? 17.950  -43.031 25.362 1.00 44.68  ? 522 MET   B SD  1 
ATOM   3498 C CE  . MET   B 1 230 ? 18.657  -42.070 26.695 1.00 32.66  ? 522 MET   B CE  1 
ATOM   3499 N N   . GLU   B 1 231 ? 13.786  -43.204 21.592 1.00 45.17  ? 523 GLU   B N   1 
ATOM   3500 C CA  . GLU   B 1 231 ? 12.579  -43.813 21.048 1.00 39.59  ? 523 GLU   B CA  1 
ATOM   3501 C C   . GLU   B 1 231 ? 12.910  -44.856 19.986 1.00 49.88  ? 523 GLU   B C   1 
ATOM   3502 O O   . GLU   B 1 231 ? 12.143  -45.804 19.786 1.00 59.11  ? 523 GLU   B O   1 
ATOM   3503 C CB  . GLU   B 1 231 ? 11.671  -42.715 20.486 1.00 41.28  ? 523 GLU   B CB  1 
ATOM   3504 C CG  . GLU   B 1 231 ? 10.574  -43.180 19.544 1.00 58.41  ? 523 GLU   B CG  1 
ATOM   3505 C CD  . GLU   B 1 231 ? 9.751   -42.024 19.008 1.00 61.90  ? 523 GLU   B CD  1 
ATOM   3506 O OE1 . GLU   B 1 231 ? 9.308   -42.097 17.842 1.00 82.55  ? 523 GLU   B OE1 1 
ATOM   3507 O OE2 . GLU   B 1 231 ? 9.549   -41.042 19.752 1.00 55.66  ? 523 GLU   B OE2 1 
ATOM   3508 N N   . HIS   B 1 232 ? 14.051  -44.712 19.313 1.00 49.20  ? 524 HIS   B N   1 
ATOM   3509 C CA  . HIS   B 1 232 ? 14.477  -45.663 18.293 1.00 57.44  ? 524 HIS   B CA  1 
ATOM   3510 C C   . HIS   B 1 232 ? 15.304  -46.802 18.882 1.00 62.87  ? 524 HIS   B C   1 
ATOM   3511 O O   . HIS   B 1 232 ? 14.970  -47.974 18.688 1.00 64.59  ? 524 HIS   B O   1 
ATOM   3512 C CB  . HIS   B 1 232 ? 15.275  -44.940 17.204 1.00 49.46  ? 524 HIS   B CB  1 
ATOM   3513 C CG  . HIS   B 1 232 ? 15.754  -45.837 16.105 1.00 57.25  ? 524 HIS   B CG  1 
ATOM   3514 N ND1 . HIS   B 1 232 ? 17.068  -46.236 15.989 1.00 50.27  ? 524 HIS   B ND1 1 
ATOM   3515 C CD2 . HIS   B 1 232 ? 15.095  -46.407 15.069 1.00 58.52  ? 524 HIS   B CD2 1 
ATOM   3516 C CE1 . HIS   B 1 232 ? 17.198  -47.015 14.930 1.00 66.79  ? 524 HIS   B CE1 1 
ATOM   3517 N NE2 . HIS   B 1 232 ? 16.015  -47.135 14.354 1.00 65.95  ? 524 HIS   B NE2 1 
ATOM   3518 N N   . LEU   B 1 233 ? 16.375  -46.470 19.611 1.00 62.20  ? 525 LEU   B N   1 
ATOM   3519 C CA  . LEU   B 1 233 ? 17.257  -47.499 20.155 1.00 67.90  ? 525 LEU   B CA  1 
ATOM   3520 C C   . LEU   B 1 233 ? 16.517  -48.432 21.105 1.00 75.88  ? 525 LEU   B C   1 
ATOM   3521 O O   . LEU   B 1 233 ? 16.786  -49.638 21.135 1.00 78.99  ? 525 LEU   B O   1 
ATOM   3522 C CB  . LEU   B 1 233 ? 18.445  -46.852 20.867 1.00 52.94  ? 525 LEU   B CB  1 
ATOM   3523 C CG  . LEU   B 1 233 ? 19.265  -45.821 20.093 1.00 51.11  ? 525 LEU   B CG  1 
ATOM   3524 C CD1 . LEU   B 1 233 ? 20.364  -45.255 20.974 1.00 46.92  ? 525 LEU   B CD1 1 
ATOM   3525 C CD2 . LEU   B 1 233 ? 19.854  -46.440 18.841 1.00 55.03  ? 525 LEU   B CD2 1 
ATOM   3526 N N   . TYR   B 1 234 ? 15.581  -47.898 21.886 1.00 89.43  ? 526 TYR   B N   1 
ATOM   3527 C CA  . TYR   B 1 234 ? 14.874  -48.693 22.879 1.00 89.83  ? 526 TYR   B CA  1 
ATOM   3528 C C   . TYR   B 1 234 ? 13.497  -49.138 22.404 1.00 98.07  ? 526 TYR   B C   1 
ATOM   3529 O O   . TYR   B 1 234 ? 12.738  -49.719 23.187 1.00 112.41 ? 526 TYR   B O   1 
ATOM   3530 C CB  . TYR   B 1 234 ? 14.783  -47.928 24.200 1.00 84.84  ? 526 TYR   B CB  1 
ATOM   3531 C CG  . TYR   B 1 234 ? 16.114  -47.873 24.923 1.00 76.39  ? 526 TYR   B CG  1 
ATOM   3532 C CD1 . TYR   B 1 234 ? 17.187  -47.161 24.398 1.00 80.19  ? 526 TYR   B CD1 1 
ATOM   3533 C CD2 . TYR   B 1 234 ? 16.309  -48.565 26.111 1.00 91.91  ? 526 TYR   B CD2 1 
ATOM   3534 C CE1 . TYR   B 1 234 ? 18.407  -47.119 25.047 1.00 73.90  ? 526 TYR   B CE1 1 
ATOM   3535 C CE2 . TYR   B 1 234 ? 17.527  -48.530 26.767 1.00 91.30  ? 526 TYR   B CE2 1 
ATOM   3536 C CZ  . TYR   B 1 234 ? 18.572  -47.807 26.231 1.00 84.28  ? 526 TYR   B CZ  1 
ATOM   3537 O OH  . TYR   B 1 234 ? 19.785  -47.770 26.882 1.00 74.86  ? 526 TYR   B OH  1 
ATOM   3538 N N   . SER   B 1 235 ? 13.157  -48.875 21.142 1.00 103.94 ? 527 SER   B N   1 
ATOM   3539 C CA  . SER   B 1 235 ? 12.114  -49.635 20.467 1.00 113.22 ? 527 SER   B CA  1 
ATOM   3540 C C   . SER   B 1 235 ? 12.655  -50.924 19.868 1.00 118.32 ? 527 SER   B C   1 
ATOM   3541 O O   . SER   B 1 235 ? 11.865  -51.783 19.462 1.00 124.90 ? 527 SER   B O   1 
ATOM   3542 C CB  . SER   B 1 235 ? 11.460  -48.796 19.368 1.00 118.82 ? 527 SER   B CB  1 
ATOM   3543 O OG  . SER   B 1 235 ? 10.540  -49.568 18.615 1.00 128.67 ? 527 SER   B OG  1 
ATOM   3544 N N   . VAL   B 1 241 ? 18.810  -54.936 31.587 1.00 74.61  ? 533 VAL   B N   1 
ATOM   3545 C CA  . VAL   B 1 241 ? 18.529  -55.438 32.926 1.00 67.87  ? 533 VAL   B CA  1 
ATOM   3546 C C   . VAL   B 1 241 ? 19.228  -54.570 33.963 1.00 63.84  ? 533 VAL   B C   1 
ATOM   3547 O O   . VAL   B 1 241 ? 18.580  -53.959 34.813 1.00 78.70  ? 533 VAL   B O   1 
ATOM   3548 C CB  . VAL   B 1 241 ? 18.956  -56.908 33.071 1.00 79.84  ? 533 VAL   B CB  1 
ATOM   3549 C CG1 . VAL   B 1 241 ? 18.356  -57.510 34.334 1.00 75.71  ? 533 VAL   B CG1 1 
ATOM   3550 C CG2 . VAL   B 1 241 ? 18.547  -57.702 31.840 1.00 70.46  ? 533 VAL   B CG2 1 
ATOM   3551 N N   . VAL   B 1 242 ? 20.554  -54.522 33.890 1.00 54.46  ? 534 VAL   B N   1 
ATOM   3552 C CA  . VAL   B 1 242 ? 21.350  -53.676 34.775 1.00 57.52  ? 534 VAL   B CA  1 
ATOM   3553 C C   . VAL   B 1 242 ? 21.096  -52.220 34.402 1.00 56.63  ? 534 VAL   B C   1 
ATOM   3554 O O   . VAL   B 1 242 ? 21.282  -51.840 33.237 1.00 49.47  ? 534 VAL   B O   1 
ATOM   3555 C CB  . VAL   B 1 242 ? 22.844  -54.022 34.688 1.00 62.83  ? 534 VAL   B CB  1 
ATOM   3556 C CG1 . VAL   B 1 242 ? 23.608  -53.383 35.839 1.00 56.94  ? 534 VAL   B CG1 1 
ATOM   3557 C CG2 . VAL   B 1 242 ? 23.041  -55.530 34.682 1.00 55.46  ? 534 VAL   B CG2 1 
ATOM   3558 N N   . PRO   B 1 243 ? 20.672  -51.378 35.342 1.00 50.69  ? 535 PRO   B N   1 
ATOM   3559 C CA  . PRO   B 1 243 ? 20.391  -49.980 34.999 1.00 51.71  ? 535 PRO   B CA  1 
ATOM   3560 C C   . PRO   B 1 243 ? 21.664  -49.227 34.650 1.00 47.56  ? 535 PRO   B C   1 
ATOM   3561 O O   . PRO   B 1 243 ? 22.755  -49.542 35.133 1.00 41.45  ? 535 PRO   B O   1 
ATOM   3562 C CB  . PRO   B 1 243 ? 19.742  -49.418 36.269 1.00 51.37  ? 535 PRO   B CB  1 
ATOM   3563 C CG  . PRO   B 1 243 ? 20.174  -50.322 37.369 1.00 57.82  ? 535 PRO   B CG  1 
ATOM   3564 C CD  . PRO   B 1 243 ? 20.485  -51.664 36.775 1.00 41.72  ? 535 PRO   B CD  1 
ATOM   3565 N N   . LEU   B 1 244 ? 21.507  -48.216 33.790 1.00 47.19  ? 536 LEU   B N   1 
ATOM   3566 C CA  . LEU   B 1 244 ? 22.656  -47.447 33.321 1.00 44.29  ? 536 LEU   B CA  1 
ATOM   3567 C C   . LEU   B 1 244 ? 23.377  -46.752 34.469 1.00 41.05  ? 536 LEU   B C   1 
ATOM   3568 O O   . LEU   B 1 244 ? 24.601  -46.584 34.420 1.00 39.74  ? 536 LEU   B O   1 
ATOM   3569 C CB  . LEU   B 1 244 ? 22.206  -46.424 32.278 1.00 43.48  ? 536 LEU   B CB  1 
ATOM   3570 C CG  . LEU   B 1 244 ? 23.294  -45.581 31.611 1.00 42.62  ? 536 LEU   B CG  1 
ATOM   3571 C CD1 . LEU   B 1 244 ? 24.262  -46.460 30.832 1.00 40.91  ? 536 LEU   B CD1 1 
ATOM   3572 C CD2 . LEU   B 1 244 ? 22.671  -44.531 30.708 1.00 41.49  ? 536 LEU   B CD2 1 
ATOM   3573 N N   . SER   B 1 245 ? 22.641  -46.350 35.509 1.00 45.92  ? 537 SER   B N   1 
ATOM   3574 C CA  . SER   B 1 245 ? 23.261  -45.669 36.641 1.00 45.12  ? 537 SER   B CA  1 
ATOM   3575 C C   . SER   B 1 245 ? 24.282  -46.561 37.337 1.00 34.65  ? 537 SER   B C   1 
ATOM   3576 O O   . SER   B 1 245 ? 25.360  -46.097 37.724 1.00 35.39  ? 537 SER   B O   1 
ATOM   3577 C CB  . SER   B 1 245 ? 22.186  -45.210 37.626 1.00 38.04  ? 537 SER   B CB  1 
ATOM   3578 O OG  . SER   B 1 245 ? 21.442  -46.314 38.110 1.00 42.72  ? 537 SER   B OG  1 
ATOM   3579 N N   . ASP   B 1 246 ? 23.958  -47.846 37.513 1.00 32.06  ? 538 ASP   B N   1 
ATOM   3580 C CA  . ASP   B 1 246 ? 24.924  -48.778 38.088 1.00 38.22  ? 538 ASP   B CA  1 
ATOM   3581 C C   . ASP   B 1 246 ? 26.171  -48.884 37.220 1.00 35.25  ? 538 ASP   B C   1 
ATOM   3582 O O   . ASP   B 1 246 ? 27.294  -48.950 37.735 1.00 29.62  ? 538 ASP   B O   1 
ATOM   3583 C CB  . ASP   B 1 246 ? 24.286  -50.155 38.271 1.00 31.68  ? 538 ASP   B CB  1 
ATOM   3584 C CG  . ASP   B 1 246 ? 23.372  -50.220 39.475 1.00 37.73  ? 538 ASP   B CG  1 
ATOM   3585 O OD1 . ASP   B 1 246 ? 23.269  -49.209 40.198 1.00 30.17  ? 538 ASP   B OD1 1 
ATOM   3586 O OD2 . ASP   B 1 246 ? 22.756  -51.282 39.699 1.00 51.53  ? 538 ASP   B OD2 1 
ATOM   3587 N N   . LEU   B 1 247 ? 25.994  -48.902 35.898 1.00 32.90  ? 539 LEU   B N   1 
ATOM   3588 C CA  . LEU   B 1 247 ? 27.141  -48.989 35.003 1.00 36.84  ? 539 LEU   B CA  1 
ATOM   3589 C C   . LEU   B 1 247 ? 27.953  -47.700 35.021 1.00 35.41  ? 539 LEU   B C   1 
ATOM   3590 O O   . LEU   B 1 247 ? 29.188  -47.737 34.954 1.00 36.55  ? 539 LEU   B O   1 
ATOM   3591 C CB  . LEU   B 1 247 ? 26.672  -49.315 33.586 1.00 35.75  ? 539 LEU   B CB  1 
ATOM   3592 C CG  . LEU   B 1 247 ? 27.588  -50.205 32.746 1.00 55.30  ? 539 LEU   B CG  1 
ATOM   3593 C CD1 . LEU   B 1 247 ? 28.202  -51.304 33.599 1.00 53.55  ? 539 LEU   B CD1 1 
ATOM   3594 C CD2 . LEU   B 1 247 ? 26.814  -50.801 31.584 1.00 58.84  ? 539 LEU   B CD2 1 
ATOM   3595 N N   . LEU   B 1 248 ? 27.279  -46.550 35.110 1.00 35.62  ? 540 LEU   B N   1 
ATOM   3596 C CA  . LEU   B 1 248 ? 27.995  -45.281 35.196 1.00 33.27  ? 540 LEU   B CA  1 
ATOM   3597 C C   . LEU   B 1 248 ? 28.772  -45.177 36.502 1.00 34.79  ? 540 LEU   B C   1 
ATOM   3598 O O   . LEU   B 1 248 ? 29.904  -44.678 36.519 1.00 39.13  ? 540 LEU   B O   1 
ATOM   3599 C CB  . LEU   B 1 248 ? 27.016  -44.114 35.059 1.00 31.24  ? 540 LEU   B CB  1 
ATOM   3600 C CG  . LEU   B 1 248 ? 26.296  -43.960 33.717 1.00 33.79  ? 540 LEU   B CG  1 
ATOM   3601 C CD1 . LEU   B 1 248 ? 25.310  -42.802 33.764 1.00 36.79  ? 540 LEU   B CD1 1 
ATOM   3602 C CD2 . LEU   B 1 248 ? 27.288  -43.782 32.578 1.00 32.62  ? 540 LEU   B CD2 1 
ATOM   3603 N N   . LEU   B 1 249 ? 28.179  -45.641 37.605 1.00 34.35  ? 541 LEU   B N   1 
ATOM   3604 C CA  . LEU   B 1 249 ? 28.872  -45.636 38.890 1.00 28.37  ? 541 LEU   B CA  1 
ATOM   3605 C C   . LEU   B 1 249 ? 30.133  -46.489 38.832 1.00 41.05  ? 541 LEU   B C   1 
ATOM   3606 O O   . LEU   B 1 249 ? 31.196  -46.083 39.316 1.00 49.52  ? 541 LEU   B O   1 
ATOM   3607 C CB  . LEU   B 1 249 ? 27.934  -46.139 39.989 1.00 42.29  ? 541 LEU   B CB  1 
ATOM   3608 C CG  . LEU   B 1 249 ? 27.109  -45.110 40.764 1.00 36.30  ? 541 LEU   B CG  1 
ATOM   3609 C CD1 . LEU   B 1 249 ? 26.232  -45.807 41.793 1.00 25.39  ? 541 LEU   B CD1 1 
ATOM   3610 C CD2 . LEU   B 1 249 ? 28.010  -44.084 41.432 1.00 30.52  ? 541 LEU   B CD2 1 
ATOM   3611 N N   . GLU   B 1 250 ? 30.030  -47.680 38.239 1.00 39.59  ? 542 GLU   B N   1 
ATOM   3612 C CA  . GLU   B 1 250 ? 31.186  -48.564 38.138 1.00 40.70  ? 542 GLU   B CA  1 
ATOM   3613 C C   . GLU   B 1 250 ? 32.283  -47.945 37.280 1.00 39.74  ? 542 GLU   B C   1 
ATOM   3614 O O   . GLU   B 1 250 ? 33.474  -48.099 37.577 1.00 45.71  ? 542 GLU   B O   1 
ATOM   3615 C CB  . GLU   B 1 250 ? 30.757  -49.916 37.572 1.00 36.35  ? 542 GLU   B CB  1 
ATOM   3616 C CG  . GLU   B 1 250 ? 31.837  -50.978 37.611 1.00 49.49  ? 542 GLU   B CG  1 
ATOM   3617 C CD  . GLU   B 1 250 ? 31.419  -52.252 36.907 1.00 54.09  ? 542 GLU   B CD  1 
ATOM   3618 O OE1 . GLU   B 1 250 ? 30.202  -52.527 36.845 1.00 60.74  ? 542 GLU   B OE1 1 
ATOM   3619 O OE2 . GLU   B 1 250 ? 32.308  -52.975 36.413 1.00 54.39  ? 542 GLU   B OE2 1 
ATOM   3620 N N   . MET   B 1 251 ? 31.901  -47.236 36.214 1.00 40.24  ? 543 MET   B N   1 
ATOM   3621 C CA  . MET   B 1 251 ? 32.889  -46.592 35.354 1.00 38.70  ? 543 MET   B CA  1 
ATOM   3622 C C   . MET   B 1 251 ? 33.636  -45.484 36.085 1.00 42.18  ? 543 MET   B C   1 
ATOM   3623 O O   . MET   B 1 251 ? 34.786  -45.182 35.745 1.00 37.94  ? 543 MET   B O   1 
ATOM   3624 C CB  . MET   B 1 251 ? 32.209  -46.032 34.104 1.00 38.74  ? 543 MET   B CB  1 
ATOM   3625 C CG  . MET   B 1 251 ? 31.796  -47.085 33.089 1.00 34.61  ? 543 MET   B CG  1 
ATOM   3626 S SD  . MET   B 1 251 ? 30.880  -46.374 31.709 1.00 48.58  ? 543 MET   B SD  1 
ATOM   3627 C CE  . MET   B 1 251 ? 29.923  -47.788 31.170 1.00 40.56  ? 543 MET   B CE  1 
ATOM   3628 N N   . LEU   B 1 252 ? 33.002  -44.870 37.087 1.00 42.83  ? 544 LEU   B N   1 
ATOM   3629 C CA  . LEU   B 1 252 ? 33.621  -43.802 37.862 1.00 40.05  ? 544 LEU   B CA  1 
ATOM   3630 C C   . LEU   B 1 252 ? 34.700  -44.307 38.813 1.00 45.40  ? 544 LEU   B C   1 
ATOM   3631 O O   . LEU   B 1 252 ? 35.497  -43.498 39.300 1.00 43.81  ? 544 LEU   B O   1 
ATOM   3632 C CB  . LEU   B 1 252 ? 32.542  -43.050 38.644 1.00 33.25  ? 544 LEU   B CB  1 
ATOM   3633 C CG  . LEU   B 1 252 ? 31.660  -42.112 37.817 1.00 39.91  ? 544 LEU   B CG  1 
ATOM   3634 C CD1 . LEU   B 1 252 ? 30.315  -41.898 38.484 1.00 47.26  ? 544 LEU   B CD1 1 
ATOM   3635 C CD2 . LEU   B 1 252 ? 32.355  -40.785 37.623 1.00 41.82  ? 544 LEU   B CD2 1 
ATOM   3636 N N   . ASP   B 1 253 ? 34.754  -45.613 39.078 1.00 36.58  ? 545 ASP   B N   1 
ATOM   3637 C CA  . ASP   B 1 253 ? 35.747  -46.168 39.989 1.00 47.99  ? 545 ASP   B CA  1 
ATOM   3638 C C   . ASP   B 1 253 ? 37.122  -46.326 39.354 1.00 41.03  ? 545 ASP   B C   1 
ATOM   3639 O O   . ASP   B 1 253 ? 38.086  -46.620 40.070 1.00 41.41  ? 545 ASP   B O   1 
ATOM   3640 C CB  . ASP   B 1 253 ? 35.272  -47.524 40.518 1.00 35.95  ? 545 ASP   B CB  1 
ATOM   3641 N N   . ALA   B 1 254 ? 37.239  -46.145 38.042 1.00 36.16  ? 546 ALA   B N   1 
ATOM   3642 C CA  . ALA   B 1 254 ? 38.524  -46.274 37.367 1.00 47.19  ? 546 ALA   B CA  1 
ATOM   3643 C C   . ALA   B 1 254 ? 39.198  -44.915 37.213 1.00 60.27  ? 546 ALA   B C   1 
ATOM   3644 O O   . ALA   B 1 254 ? 39.811  -44.405 38.151 1.00 69.32  ? 546 ALA   B O   1 
ATOM   3645 C CB  . ALA   B 1 254 ? 38.347  -46.937 36.010 1.00 40.96  ? 546 ALA   B CB  1 
HETATM 3646 N N   . HIS   C 2 .   ? -11.160 -11.900 3.551  1.00 92.27  ? 601 HIS   A N   1 
HETATM 3647 C CA  . HIS   C 2 .   ? -12.447 -11.351 3.961  1.00 95.11  ? 601 HIS   A CA  1 
HETATM 3648 C C   . HIS   C 2 .   ? -12.404 -9.827  4.013  1.00 96.75  ? 601 HIS   A C   1 
HETATM 3649 O O   . HIS   C 2 .   ? -11.784 -9.243  4.901  1.00 100.19 ? 601 HIS   A O   1 
HETATM 3650 C CB  . HIS   C 2 .   ? -12.862 -11.915 5.321  1.00 96.35  ? 601 HIS   A CB  1 
HETATM 3651 C CG  . HIS   C 2 .   ? -13.454 -13.288 5.250  1.00 95.75  ? 601 HIS   A CG  1 
HETATM 3652 N ND1 . HIS   C 2 .   ? -14.003 -13.802 4.095  1.00 95.21  ? 601 HIS   A ND1 1 
HETATM 3653 C CD2 . HIS   C 2 .   ? -13.583 -14.253 6.190  1.00 95.83  ? 601 HIS   A CD2 1 
HETATM 3654 C CE1 . HIS   C 2 .   ? -14.445 -15.025 4.327  1.00 94.94  ? 601 HIS   A CE1 1 
HETATM 3655 N NE2 . HIS   C 2 .   ? -14.202 -15.323 5.591  1.00 95.20  ? 601 HIS   A NE2 1 
HETATM 3656 N N1  . TZI   D 3 .   ? -1.992  -31.037 27.580 1.00 24.03  ? 602 TZI   A N1  1 
HETATM 3657 C C4  . TZI   D 3 .   ? -1.631  -26.781 27.076 1.00 24.13  ? 602 TZI   A C4  1 
HETATM 3658 C C5  . TZI   D 3 .   ? -1.784  -28.310 27.112 1.00 22.96  ? 602 TZI   A C5  1 
HETATM 3659 C C6  . TZI   D 3 .   ? -2.925  -28.904 26.795 1.00 15.83  ? 602 TZI   A C6  1 
HETATM 3660 C C7  . TZI   D 3 .   ? -0.503  -29.037 27.544 1.00 18.44  ? 602 TZI   A C7  1 
HETATM 3661 C C8  . TZI   D 3 .   ? -0.592  -30.571 27.436 1.00 24.47  ? 602 TZI   A C8  1 
HETATM 3662 C C10 . TZI   D 3 .   ? -2.351  -32.139 28.526 1.00 27.85  ? 602 TZI   A C10 1 
HETATM 3663 C C13 . TZI   D 3 .   ? 0.216   -34.712 30.047 1.00 33.66  ? 602 TZI   A C13 1 
HETATM 3664 C C15 . TZI   D 3 .   ? 0.225   -32.613 31.384 1.00 24.17  ? 602 TZI   A C15 1 
HETATM 3665 C C17 . TZI   D 3 .   ? 0.352   -30.691 26.192 1.00 22.32  ? 602 TZI   A C17 1 
HETATM 3666 C C20 . TZI   D 3 .   ? -2.529  -30.341 24.403 1.00 29.02  ? 602 TZI   A C20 1 
HETATM 3667 C C21 . TZI   D 3 .   ? -2.644  -30.859 22.957 1.00 35.66  ? 602 TZI   A C21 1 
HETATM 3668 C C22 . TZI   D 3 .   ? -3.414  -31.911 22.695 1.00 36.74  ? 602 TZI   A C22 1 
HETATM 3669 C C24 . TZI   D 3 .   ? -4.084  -32.170 25.075 1.00 28.03  ? 602 TZI   A C24 1 
HETATM 3670 C C26 . TZI   D 3 .   ? -4.682  -33.514 19.532 1.00 47.44  ? 602 TZI   A C26 1 
HETATM 3671 C C28 . TZI   D 3 .   ? -4.538  -31.637 18.182 1.00 43.92  ? 602 TZI   A C28 1 
HETATM 3672 C C1  . TZI   D 3 .   ? -4.126  -28.039 26.380 1.00 19.21  ? 602 TZI   A C1  1 
HETATM 3673 C C11 . TZI   D 3 .   ? -1.267  -32.841 29.412 1.00 27.90  ? 602 TZI   A C11 1 
HETATM 3674 C C12 . TZI   D 3 .   ? -0.850  -34.073 29.145 1.00 22.82  ? 602 TZI   A C12 1 
HETATM 3675 C C14 . TZI   D 3 .   ? 0.704   -34.036 31.079 1.00 30.38  ? 602 TZI   A C14 1 
HETATM 3676 C C16 . TZI   D 3 .   ? -0.694  -32.060 30.607 1.00 26.92  ? 602 TZI   A C16 1 
HETATM 3677 C C18 . TZI   D 3 .   ? 0.785   -31.314 27.469 1.00 27.06  ? 602 TZI   A C18 1 
HETATM 3678 C C19 . TZI   D 3 .   ? -3.188  -30.954 25.381 1.00 25.16  ? 602 TZI   A C19 1 
HETATM 3679 C C2  . TZI   D 3 .   ? -4.005  -26.717 26.345 1.00 18.83  ? 602 TZI   A C2  1 
HETATM 3680 C C23 . TZI   D 3 .   ? -4.186  -32.618 23.825 1.00 36.62  ? 602 TZI   A C23 1 
HETATM 3681 C C25 . TZI   D 3 .   ? -4.622  -33.234 21.119 1.00 45.84  ? 602 TZI   A C25 1 
HETATM 3682 C C27 . TZI   D 3 .   ? -3.739  -32.688 18.903 1.00 40.41  ? 602 TZI   A C27 1 
HETATM 3683 C C29 . TZI   D 3 .   ? -6.069  -33.174 19.011 1.00 41.03  ? 602 TZI   A C29 1 
HETATM 3684 C C3  . TZI   D 3 .   ? -2.673  -26.042 26.715 1.00 21.07  ? 602 TZI   A C3  1 
HETATM 3685 C C30 . TZI   D 3 .   ? -6.029  -32.610 16.958 1.00 51.62  ? 602 TZI   A C30 1 
HETATM 3686 C C31 . TZI   D 3 .   ? -7.210  -31.908 16.238 1.00 56.23  ? 602 TZI   A C31 1 
HETATM 3687 C C32 . TZI   D 3 .   ? -6.716  -30.587 15.609 1.00 60.90  ? 602 TZI   A C32 1 
HETATM 3688 C C9  . TZI   D 3 .   ? -3.080  -30.428 26.830 1.00 18.97  ? 602 TZI   A C9  1 
HETATM 3689 F F1  . TZI   D 3 .   ? -7.142  -29.521 16.360 1.00 61.26  ? 602 TZI   A F1  1 
HETATM 3690 N N2  . TZI   D 3 .   ? -5.873  -32.145 18.076 1.00 51.63  ? 602 TZI   A N2  1 
HETATM 3691 O O1  . TZI   D 3 .   ? -3.485  -32.476 28.617 1.00 39.97  ? 602 TZI   A O1  1 
HETATM 3692 O O2  . TZI   D 3 .   ? -2.557  -24.642 26.673 1.00 24.27  ? 602 TZI   A O2  1 
HETATM 3693 O O3  . TZI   D 3 .   ? -3.514  -32.382 21.361 1.00 40.34  ? 602 TZI   A O3  1 
HETATM 3694 N N1  . A1BV9 E 4 .   ? 23.939  -44.320 16.779 1.00 30.34  ? 601 A1BV9 B N1  1 
HETATM 3695 C C4  . A1BV9 E 4 .   ? 27.362  -41.953 17.883 1.00 22.04  ? 601 A1BV9 B C4  1 
HETATM 3696 C C5  . A1BV9 E 4 .   ? 26.129  -42.837 17.634 1.00 25.38  ? 601 A1BV9 B C5  1 
HETATM 3697 C C6  . A1BV9 E 4 .   ? 26.167  -44.150 17.806 1.00 24.73  ? 601 A1BV9 B C6  1 
HETATM 3698 C C7  . A1BV9 E 4 .   ? 24.892  -42.048 17.180 1.00 28.82  ? 601 A1BV9 B C7  1 
HETATM 3699 C C8  . A1BV9 E 4 .   ? 23.615  -42.901 17.056 1.00 25.55  ? 601 A1BV9 B C8  1 
HETATM 3700 C C10 . A1BV9 E 4 .   ? 23.273  -45.071 15.666 1.00 35.21  ? 601 A1BV9 B C10 1 
HETATM 3701 C C13 . A1BV9 E 4 .   ? 19.897  -44.117 13.863 1.00 30.77  ? 601 A1BV9 B C13 1 
HETATM 3702 C C15 . A1BV9 E 4 .   ? 21.756  -42.765 12.924 1.00 38.16  ? 601 A1BV9 B C15 1 
HETATM 3703 C C17 . A1BV9 E 4 .   ? 22.893  -42.288 18.305 1.00 26.69  ? 601 A1BV9 B C17 1 
HETATM 3704 C C20 . A1BV9 E 4 .   ? 24.460  -44.770 19.994 1.00 28.06  ? 601 A1BV9 B C20 1 
HETATM 3705 C C21 . A1BV9 E 4 .   ? 23.943  -45.288 21.352 1.00 33.67  ? 601 A1BV9 B C21 1 
HETATM 3706 C C22 . A1BV9 E 4 .   ? 23.467  -46.527 21.450 1.00 30.86  ? 601 A1BV9 B C22 1 
HETATM 3707 C C24 . A1BV9 E 4 .   ? 23.864  -46.989 19.035 1.00 32.32  ? 601 A1BV9 B C24 1 
HETATM 3708 C C26 . A1BV9 E 4 .   ? 23.008  -48.572 24.598 1.00 38.26  ? 601 A1BV9 B C26 1 
HETATM 3709 C C28 . A1BV9 E 4 .   ? 23.503  -50.364 25.991 1.00 51.46  ? 601 A1BV9 B C28 1 
HETATM 3710 C C1  . A1BV9 E 4 .   ? 27.478  -44.805 18.266 1.00 22.19  ? 601 A1BV9 B C1  1 
HETATM 3711 C C11 . A1BV9 E 4 .   ? 22.199  -44.412 14.731 1.00 33.40  ? 601 A1BV9 B C11 1 
HETATM 3712 C C12 . A1BV9 E 4 .   ? 20.925  -44.779 14.795 1.00 33.87  ? 601 A1BV9 B C12 1 
HETATM 3713 C C14 . A1BV9 E 4 .   ? 20.283  -43.188 12.999 1.00 36.03  ? 601 A1BV9 B C14 1 
HETATM 3714 C C16 . A1BV9 E 4 .   ? 22.646  -43.335 13.726 1.00 27.78  ? 601 A1BV9 B C16 1 
HETATM 3715 C C18 . A1BV9 E 4 .   ? 22.285  -42.084 16.965 1.00 30.73  ? 601 A1BV9 B C18 1 
HETATM 3716 C C19 . A1BV9 E 4 .   ? 24.413  -45.553 18.920 1.00 25.92  ? 601 A1BV9 B C19 1 
HETATM 3717 C C2  . A1BV9 E 4 .   ? 28.549  -44.051 18.484 1.00 21.78  ? 601 A1BV9 B C2  1 
HETATM 3718 C C23 . A1BV9 E 4 .   ? 23.419  -47.439 20.209 1.00 37.22  ? 601 A1BV9 B C23 1 
HETATM 3719 C C25 . A1BV9 E 4 .   ? 23.483  -48.273 23.084 1.00 42.81  ? 601 A1BV9 B C25 1 
HETATM 3720 C C27 . A1BV9 E 4 .   ? 22.760  -49.945 24.750 1.00 37.76  ? 601 A1BV9 B C27 1 
HETATM 3721 C C29 . A1BV9 E 4 .   ? 24.105  -48.149 25.563 1.00 34.92  ? 601 A1BV9 B C29 1 
HETATM 3722 C C3  . A1BV9 E 4 .   ? 28.491  -42.526 18.282 1.00 28.06  ? 601 A1BV9 B C3  1 
HETATM 3723 C C30 . A1BV9 E 4 .   ? 24.267  -48.995 27.547 1.00 56.08  ? 601 A1BV9 B C30 1 
HETATM 3724 C C31 . A1BV9 E 4 .   ? 24.836  -50.132 28.444 1.00 58.55  ? 601 A1BV9 B C31 1 
HETATM 3725 C C32 . A1BV9 E 4 .   ? 26.293  -50.484 28.054 1.00 61.07  ? 601 A1BV9 B C32 1 
HETATM 3726 C C9  . A1BV9 E 4 .   ? 24.939  -45.035 17.559 1.00 25.05  ? 601 A1BV9 B C9  1 
HETATM 3727 F F1  . A1BV9 E 4 .   ? 27.042  -49.342 27.938 1.00 65.08  ? 601 A1BV9 B F1  1 
HETATM 3728 N N2  . A1BV9 E 4 .   ? 24.364  -49.277 26.360 1.00 50.84  ? 601 A1BV9 B N2  1 
HETATM 3729 O O1  . A1BV9 E 4 .   ? 23.574  -46.203 15.483 1.00 43.72  ? 601 A1BV9 B O1  1 
HETATM 3730 O O2  . A1BV9 E 4 .   ? 29.636  -41.744 18.519 1.00 27.66  ? 601 A1BV9 B O2  1 
HETATM 3731 O O3  . A1BV9 E 4 .   ? 22.991  -46.997 22.705 1.00 39.99  ? 601 A1BV9 B O3  1 
HETATM 3732 O O   . HOH   F 5 .   ? 1.608   -7.703  15.276 1.00 43.76  ? 701 HOH   A O   1 
HETATM 3733 O O   . HOH   F 5 .   ? -3.275  -18.782 1.150  1.00 51.93  ? 702 HOH   A O   1 
HETATM 3734 O O   . HOH   F 5 .   ? -6.775  -18.749 12.520 1.00 44.24  ? 703 HOH   A O   1 
HETATM 3735 O O   . HOH   F 5 .   ? 12.210  -40.116 24.396 1.00 40.45  ? 704 HOH   A O   1 
HETATM 3736 O O   . HOH   F 5 .   ? 6.685   -31.363 8.701  1.00 45.88  ? 705 HOH   A O   1 
HETATM 3737 O O   . HOH   F 5 .   ? -10.041 -37.823 31.078 1.00 40.95  ? 706 HOH   A O   1 
HETATM 3738 O O   . HOH   F 5 .   ? 16.020  -28.237 7.350  1.00 51.80  ? 707 HOH   A O   1 
HETATM 3739 O O   . HOH   F 5 .   ? -8.894  -22.020 3.665  1.00 53.30  ? 708 HOH   A O   1 
HETATM 3740 O O   . HOH   F 5 .   ? 19.461  -8.201  13.622 1.00 36.65  ? 709 HOH   A O   1 
HETATM 3741 O O   . HOH   F 5 .   ? -20.607 -30.725 25.733 1.00 52.84  ? 710 HOH   A O   1 
HETATM 3742 O O   . HOH   F 5 .   ? 4.176   -46.420 32.525 1.00 46.53  ? 711 HOH   A O   1 
HETATM 3743 O O   . HOH   F 5 .   ? -12.231 -37.307 28.262 1.00 31.01  ? 712 HOH   A O   1 
HETATM 3744 O O   . HOH   F 5 .   ? 5.156   -24.411 39.818 1.00 23.52  ? 713 HOH   A O   1 
HETATM 3745 O O   . HOH   F 5 .   ? 20.753  -15.207 16.934 1.00 27.09  ? 714 HOH   A O   1 
HETATM 3746 O O   . HOH   F 5 .   ? 13.871  -29.116 12.903 1.00 41.50  ? 715 HOH   A O   1 
HETATM 3747 O O   . HOH   F 5 .   ? 21.793  -1.848  30.857 1.00 50.32  ? 716 HOH   A O   1 
HETATM 3748 O O   . HOH   F 5 .   ? -2.713  -20.046 23.728 1.00 35.05  ? 717 HOH   A O   1 
HETATM 3749 O O   . HOH   F 5 .   ? -7.327  -31.855 43.822 1.00 47.12  ? 718 HOH   A O   1 
HETATM 3750 O O   . HOH   F 5 .   ? -6.117  -20.722 28.768 1.00 15.75  ? 719 HOH   A O   1 
HETATM 3751 O O   . HOH   F 5 .   ? -1.168  -22.352 25.536 1.00 19.09  ? 720 HOH   A O   1 
HETATM 3752 O O   . HOH   F 5 .   ? 16.590  -17.599 -6.336 1.00 42.41  ? 721 HOH   A O   1 
HETATM 3753 O O   . HOH   F 5 .   ? -5.086  -20.162 26.327 1.00 23.28  ? 722 HOH   A O   1 
HETATM 3754 O O   . HOH   F 5 .   ? 4.528   -12.486 9.522  1.00 25.34  ? 723 HOH   A O   1 
HETATM 3755 O O   . HOH   F 5 .   ? 3.107   -23.620 38.106 1.00 23.08  ? 724 HOH   A O   1 
HETATM 3756 O O   . HOH   F 5 .   ? 18.217  -24.624 23.408 1.00 25.30  ? 725 HOH   A O   1 
HETATM 3757 O O   . HOH   F 5 .   ? 3.399   -13.135 20.869 1.00 21.45  ? 726 HOH   A O   1 
HETATM 3758 O O   . HOH   F 5 .   ? 12.974  -25.663 21.514 1.00 34.64  ? 727 HOH   A O   1 
HETATM 3759 O O   . HOH   F 5 .   ? 9.387   -24.767 14.158 1.00 17.78  ? 728 HOH   A O   1 
HETATM 3760 O O   . HOH   F 5 .   ? 21.651  -11.783 11.024 1.00 37.50  ? 729 HOH   A O   1 
HETATM 3761 O O   . HOH   F 5 .   ? -0.342  -17.778 5.937  1.00 46.38  ? 730 HOH   A O   1 
HETATM 3762 O O   . HOH   F 5 .   ? -11.869 -18.927 19.744 1.00 20.29  ? 731 HOH   A O   1 
HETATM 3763 O O   . HOH   F 5 .   ? -2.831  -13.164 17.326 1.00 31.89  ? 732 HOH   A O   1 
HETATM 3764 O O   . HOH   F 5 .   ? 17.312  -16.467 18.131 1.00 25.75  ? 733 HOH   A O   1 
HETATM 3765 O O   . HOH   F 5 .   ? -14.554 -26.769 32.111 1.00 31.62  ? 734 HOH   A O   1 
HETATM 3766 O O   . HOH   F 5 .   ? 6.225   -28.958 19.269 1.00 23.42  ? 735 HOH   A O   1 
HETATM 3767 O O   . HOH   F 5 .   ? 4.771   -28.676 5.094  1.00 43.20  ? 736 HOH   A O   1 
HETATM 3768 O O   . HOH   F 5 .   ? -8.697  -39.982 34.243 1.00 51.59  ? 737 HOH   A O   1 
HETATM 3769 O O   . HOH   F 5 .   ? 23.176  -4.713  24.854 1.00 39.98  ? 738 HOH   A O   1 
HETATM 3770 O O   . HOH   F 5 .   ? 22.040  -15.853 10.614 1.00 32.58  ? 739 HOH   A O   1 
HETATM 3771 O O   . HOH   F 5 .   ? 18.233  -22.201 32.294 1.00 33.06  ? 740 HOH   A O   1 
HETATM 3772 O O   . HOH   F 5 .   ? 0.987   -18.008 20.669 1.00 22.20  ? 741 HOH   A O   1 
HETATM 3773 O O   . HOH   F 5 .   ? 15.810  -12.189 4.505  1.00 47.05  ? 742 HOH   A O   1 
HETATM 3774 O O   . HOH   F 5 .   ? 0.355   -40.186 35.897 1.00 42.08  ? 743 HOH   A O   1 
HETATM 3775 O O   . HOH   F 5 .   ? 11.320  -26.351 2.007  1.00 50.91  ? 744 HOH   A O   1 
HETATM 3776 O O   . HOH   F 5 .   ? 17.068  -14.402 2.636  1.00 43.02  ? 745 HOH   A O   1 
HETATM 3777 O O   . HOH   F 5 .   ? 9.295   -13.976 40.254 1.00 43.11  ? 746 HOH   A O   1 
HETATM 3778 O O   . HOH   F 5 .   ? 0.461   -20.917 23.714 1.00 22.59  ? 747 HOH   A O   1 
HETATM 3779 O O   . HOH   F 5 .   ? 11.482  -25.844 -2.524 1.00 55.97  ? 748 HOH   A O   1 
HETATM 3780 O O   . HOH   F 5 .   ? -4.164  -14.913 17.712 1.00 34.20  ? 749 HOH   A O   1 
HETATM 3781 O O   . HOH   F 5 .   ? -5.150  -18.816 22.408 1.00 32.86  ? 750 HOH   A O   1 
HETATM 3782 O O   . HOH   F 5 .   ? 18.492  -5.017  15.616 1.00 41.70  ? 751 HOH   A O   1 
HETATM 3783 O O   . HOH   F 5 .   ? 18.874  -24.815 9.457  1.00 53.43  ? 752 HOH   A O   1 
HETATM 3784 O O   . HOH   F 5 .   ? 19.210  -10.018 11.318 1.00 40.58  ? 753 HOH   A O   1 
HETATM 3785 O O   . HOH   F 5 .   ? 2.892   -2.675  16.847 1.00 51.62  ? 754 HOH   A O   1 
HETATM 3786 O O   . HOH   F 5 .   ? 0.959   -18.355 24.709 1.00 24.58  ? 755 HOH   A O   1 
HETATM 3787 O O   . HOH   F 5 .   ? -14.846 -33.730 27.979 1.00 37.17  ? 756 HOH   A O   1 
HETATM 3788 O O   . HOH   F 5 .   ? -3.013  -19.574 20.862 1.00 23.31  ? 757 HOH   A O   1 
HETATM 3789 O O   . HOH   F 5 .   ? 6.124   -11.515 34.888 1.00 40.98  ? 758 HOH   A O   1 
HETATM 3790 O O   . HOH   F 5 .   ? -1.575  -32.223 44.489 1.00 52.04  ? 759 HOH   A O   1 
HETATM 3791 O O   . HOH   F 5 .   ? 13.362  -24.653 19.266 1.00 35.18  ? 760 HOH   A O   1 
HETATM 3792 O O   . HOH   F 5 .   ? -4.819  -16.601 37.368 1.00 45.69  ? 761 HOH   A O   1 
HETATM 3793 O O   . HOH   F 5 .   ? 5.336   -2.772  15.581 1.00 43.66  ? 762 HOH   A O   1 
HETATM 3794 O O   . HOH   F 5 .   ? -17.079 -30.685 38.386 1.00 56.13  ? 763 HOH   A O   1 
HETATM 3795 O O   . HOH   F 5 .   ? 27.668  -8.614  36.328 1.00 51.08  ? 764 HOH   A O   1 
HETATM 3796 O O   . HOH   F 5 .   ? -10.800 -21.026 18.422 1.00 34.04  ? 765 HOH   A O   1 
HETATM 3797 O O   . HOH   F 5 .   ? 21.818  -12.858 34.368 1.00 27.97  ? 766 HOH   A O   1 
HETATM 3798 O O   . HOH   F 5 .   ? 9.073   -36.141 35.398 1.00 43.50  ? 767 HOH   A O   1 
HETATM 3799 O O   . HOH   F 5 .   ? 19.804  -17.608 13.726 1.00 46.85  ? 768 HOH   A O   1 
HETATM 3800 O O   . HOH   F 5 .   ? 5.743   -9.157  32.689 1.00 37.51  ? 769 HOH   A O   1 
HETATM 3801 O O   . HOH   F 5 .   ? 23.162  -14.760 35.898 1.00 43.63  ? 770 HOH   A O   1 
HETATM 3802 O O   . HOH   F 5 .   ? 29.520  -6.875  32.252 1.00 39.42  ? 771 HOH   A O   1 
HETATM 3803 O O   . HOH   F 5 .   ? -3.091  -18.178 25.400 1.00 35.47  ? 772 HOH   A O   1 
HETATM 3804 O O   . HOH   F 5 .   ? -10.203 -24.379 38.407 1.00 37.40  ? 773 HOH   A O   1 
HETATM 3805 O O   . HOH   F 5 .   ? 7.397   -9.321  37.311 1.00 38.80  ? 774 HOH   A O   1 
HETATM 3806 O O   . HOH   F 5 .   ? 16.880  -1.469  17.640 1.00 50.97  ? 775 HOH   A O   1 
HETATM 3807 O O   . HOH   F 5 .   ? 2.193   -15.894 2.651  1.00 47.62  ? 776 HOH   A O   1 
HETATM 3808 O O   . HOH   F 5 .   ? 5.167   -40.062 30.083 1.00 50.54  ? 777 HOH   A O   1 
HETATM 3809 O O   . HOH   F 5 .   ? 19.140  -13.452 34.944 1.00 38.52  ? 778 HOH   A O   1 
HETATM 3810 O O   . HOH   F 5 .   ? -2.851  -12.471 26.357 1.00 46.45  ? 779 HOH   A O   1 
HETATM 3811 O O   . HOH   F 5 .   ? -12.723 -6.589  3.335  1.00 55.97  ? 780 HOH   A O   1 
HETATM 3812 O O   . HOH   F 5 .   ? -6.307  -14.056 17.620 1.00 43.43  ? 781 HOH   A O   1 
HETATM 3813 O O   . HOH   F 5 .   ? 6.464   -26.966 41.247 1.00 42.71  ? 782 HOH   A O   1 
HETATM 3814 O O   . HOH   F 5 .   ? -0.905  -17.796 27.135 1.00 36.11  ? 783 HOH   A O   1 
HETATM 3815 O O   . HOH   F 5 .   ? -14.475 -26.168 34.387 1.00 38.73  ? 784 HOH   A O   1 
HETATM 3816 O O   . HOH   F 5 .   ? 0.561   -14.953 32.803 1.00 42.29  ? 785 HOH   A O   1 
HETATM 3817 O O   . HOH   F 5 .   ? -1.662  -15.507 35.723 1.00 46.06  ? 786 HOH   A O   1 
HETATM 3818 O O   . HOH   F 5 .   ? 23.266  -20.589 30.781 1.00 43.30  ? 787 HOH   A O   1 
HETATM 3819 O O   . HOH   F 5 .   ? 8.600   -28.237 40.254 1.00 40.55  ? 788 HOH   A O   1 
HETATM 3820 O O   . HOH   F 5 .   ? 18.758  -14.571 -2.408 1.00 48.67  ? 789 HOH   A O   1 
HETATM 3821 O O   . HOH   F 5 .   ? -12.044 -5.552  5.284  1.00 51.14  ? 790 HOH   A O   1 
HETATM 3822 O O   . HOH   F 5 .   ? -2.098  -16.533 2.897  1.00 51.02  ? 791 HOH   A O   1 
HETATM 3823 O O   . HOH   F 5 .   ? -7.895  -19.111 10.138 1.00 51.24  ? 792 HOH   A O   1 
HETATM 3824 O O   . HOH   F 5 .   ? 11.042  -18.507 42.994 1.00 36.17  ? 793 HOH   A O   1 
HETATM 3825 O O   . HOH   F 5 .   ? 17.841  -14.016 37.593 1.00 47.66  ? 794 HOH   A O   1 
HETATM 3826 O O   . HOH   F 5 .   ? -0.143  -15.874 3.994  1.00 45.72  ? 795 HOH   A O   1 
HETATM 3827 O O   . HOH   F 5 .   ? -1.610  -15.722 32.937 1.00 37.63  ? 796 HOH   A O   1 
HETATM 3828 O O   . HOH   F 5 .   ? 3.368   -9.926  31.731 1.00 36.43  ? 797 HOH   A O   1 
HETATM 3829 O O   . HOH   F 5 .   ? 21.295  -3.729  22.824 1.00 35.39  ? 798 HOH   A O   1 
HETATM 3830 O O   . HOH   F 5 .   ? -2.550  -14.743 0.609  1.00 47.29  ? 799 HOH   A O   1 
HETATM 3831 O O   . HOH   F 5 .   ? -12.034 -25.603 16.751 1.00 38.96  ? 800 HOH   A O   1 
HETATM 3832 O O   . HOH   F 5 .   ? 4.728   -4.125  13.534 1.00 52.71  ? 801 HOH   A O   1 
HETATM 3833 O O   . HOH   F 5 .   ? -0.538  -13.633 4.295  1.00 42.65  ? 802 HOH   A O   1 
HETATM 3834 O O   . HOH   F 5 .   ? -0.379  -20.243 21.019 1.00 24.45  ? 803 HOH   A O   1 
HETATM 3835 O O   . HOH   F 5 .   ? -6.672  -16.494 35.663 1.00 36.18  ? 804 HOH   A O   1 
HETATM 3836 O O   . HOH   F 5 .   ? -0.889  -10.795 30.139 1.00 49.19  ? 805 HOH   A O   1 
HETATM 3837 O O   . HOH   F 5 .   ? -3.819  -10.655 29.671 1.00 53.56  ? 806 HOH   A O   1 
HETATM 3838 O O   . HOH   G 5 .   ? 30.838  -16.102 34.935 1.00 46.48  ? 701 HOH   B O   1 
HETATM 3839 O O   . HOH   G 5 .   ? 25.806  -8.717  22.825 1.00 42.96  ? 702 HOH   B O   1 
HETATM 3840 O O   . HOH   G 5 .   ? 28.436  -53.571 24.218 1.00 39.45  ? 703 HOH   B O   1 
HETATM 3841 O O   . HOH   G 5 .   ? 15.205  -29.525 15.600 1.00 36.24  ? 704 HOH   B O   1 
HETATM 3842 O O   . HOH   G 5 .   ? 35.515  -32.009 37.217 1.00 39.23  ? 705 HOH   B O   1 
HETATM 3843 O O   . HOH   G 5 .   ? 37.453  -53.591 5.478  1.00 53.32  ? 706 HOH   B O   1 
HETATM 3844 O O   . HOH   G 5 .   ? 25.465  -31.706 43.780 1.00 41.55  ? 707 HOH   B O   1 
HETATM 3845 O O   . HOH   G 5 .   ? 32.391  -51.672 17.218 1.00 39.66  ? 708 HOH   B O   1 
HETATM 3846 O O   . HOH   G 5 .   ? 28.032  -35.211 7.751  1.00 32.45  ? 709 HOH   B O   1 
HETATM 3847 O O   . HOH   G 5 .   ? 20.199  -45.968 34.934 1.00 49.31  ? 710 HOH   B O   1 
HETATM 3848 O O   . HOH   G 5 .   ? 35.724  -31.088 26.073 1.00 27.09  ? 711 HOH   B O   1 
HETATM 3849 O O   . HOH   G 5 .   ? 34.748  -54.499 23.517 1.00 40.63  ? 712 HOH   B O   1 
HETATM 3850 O O   . HOH   G 5 .   ? 25.593  -21.882 29.350 1.00 28.91  ? 713 HOH   B O   1 
HETATM 3851 O O   . HOH   G 5 .   ? 30.865  -37.675 21.974 1.00 25.13  ? 714 HOH   B O   1 
HETATM 3852 O O   . HOH   G 5 .   ? 24.419  -18.557 31.235 1.00 29.10  ? 715 HOH   B O   1 
HETATM 3853 O O   . HOH   G 5 .   ? 21.579  -22.231 14.824 1.00 33.71  ? 716 HOH   B O   1 
HETATM 3854 O O   . HOH   G 5 .   ? 16.518  -37.787 25.655 1.00 35.19  ? 717 HOH   B O   1 
HETATM 3855 O O   . HOH   G 5 .   ? 32.810  -36.946 42.954 1.00 49.91  ? 718 HOH   B O   1 
HETATM 3856 O O   . HOH   G 5 .   ? 34.608  -42.709 16.994 1.00 29.90  ? 719 HOH   B O   1 
HETATM 3857 O O   . HOH   G 5 .   ? 30.928  -46.323 3.263  1.00 47.51  ? 720 HOH   B O   1 
HETATM 3858 O O   . HOH   G 5 .   ? 33.032  -35.890 21.406 1.00 31.73  ? 721 HOH   B O   1 
HETATM 3859 O O   . HOH   G 5 .   ? 32.981  -36.079 25.388 1.00 25.95  ? 722 HOH   B O   1 
HETATM 3860 O O   . HOH   G 5 .   ? 13.262  -43.005 14.278 1.00 42.84  ? 723 HOH   B O   1 
HETATM 3861 O O   . HOH   G 5 .   ? 30.676  -39.532 19.819 1.00 24.25  ? 724 HOH   B O   1 
HETATM 3862 O O   . HOH   G 5 .   ? 33.646  -40.444 24.871 1.00 25.18  ? 725 HOH   B O   1 
HETATM 3863 O O   . HOH   G 5 .   ? 41.343  -30.815 31.862 1.00 48.57  ? 726 HOH   B O   1 
HETATM 3864 O O   . HOH   G 5 .   ? 20.890  -37.780 26.072 1.00 22.15  ? 727 HOH   B O   1 
HETATM 3865 O O   . HOH   G 5 .   ? 27.371  -6.133  14.061 1.00 46.00  ? 728 HOH   B O   1 
HETATM 3866 O O   . HOH   G 5 .   ? 39.874  -41.414 28.454 1.00 39.24  ? 729 HOH   B O   1 
HETATM 3867 O O   . HOH   G 5 .   ? 19.682  -43.358 29.503 1.00 33.05  ? 730 HOH   B O   1 
HETATM 3868 O O   . HOH   G 5 .   ? 29.464  -17.946 37.332 1.00 35.71  ? 731 HOH   B O   1 
HETATM 3869 O O   . HOH   G 5 .   ? 38.530  -48.174 25.328 1.00 21.97  ? 732 HOH   B O   1 
HETATM 3870 O O   . HOH   G 5 .   ? 35.939  -48.304 26.532 1.00 21.42  ? 733 HOH   B O   1 
HETATM 3871 O O   . HOH   G 5 .   ? 42.173  -41.970 17.882 1.00 42.07  ? 734 HOH   B O   1 
HETATM 3872 O O   . HOH   G 5 .   ? 22.298  -33.899 31.712 1.00 33.07  ? 735 HOH   B O   1 
HETATM 3873 O O   . HOH   G 5 .   ? 22.610  -35.355 45.951 1.00 50.57  ? 736 HOH   B O   1 
HETATM 3874 O O   . HOH   G 5 .   ? 38.196  -49.186 22.446 1.00 13.19  ? 737 HOH   B O   1 
HETATM 3875 O O   . HOH   G 5 .   ? 18.457  -44.869 31.836 1.00 46.63  ? 738 HOH   B O   1 
HETATM 3876 O O   . HOH   G 5 .   ? 21.004  -4.370  13.550 1.00 50.67  ? 739 HOH   B O   1 
HETATM 3877 O O   . HOH   G 5 .   ? 10.623  -34.465 13.816 1.00 48.25  ? 740 HOH   B O   1 
HETATM 3878 O O   . HOH   G 5 .   ? 17.950  -35.390 27.659 1.00 46.23  ? 741 HOH   B O   1 
HETATM 3879 O O   . HOH   G 5 .   ? 27.524  -4.465  18.272 1.00 41.79  ? 742 HOH   B O   1 
HETATM 3880 O O   . HOH   G 5 .   ? 27.176  -14.285 14.399 1.00 34.85  ? 743 HOH   B O   1 
HETATM 3881 O O   . HOH   G 5 .   ? 34.899  -39.608 20.715 1.00 37.37  ? 744 HOH   B O   1 
HETATM 3882 O O   . HOH   G 5 .   ? 20.751  -29.262 26.604 1.00 42.84  ? 745 HOH   B O   1 
HETATM 3883 O O   . HOH   G 5 .   ? 19.838  -35.630 4.500  1.00 38.22  ? 746 HOH   B O   1 
HETATM 3884 O O   . HOH   G 5 .   ? 21.378  -40.598 39.970 1.00 51.65  ? 747 HOH   B O   1 
HETATM 3885 O O   . HOH   G 5 .   ? 41.973  -11.082 17.318 1.00 53.34  ? 748 HOH   B O   1 
HETATM 3886 O O   . HOH   G 5 .   ? 40.721  -45.778 9.115  1.00 52.33  ? 749 HOH   B O   1 
HETATM 3887 O O   . HOH   G 5 .   ? 38.814  -51.738 17.124 1.00 32.16  ? 750 HOH   B O   1 
HETATM 3888 O O   . HOH   G 5 .   ? 37.077  -35.890 11.615 1.00 47.38  ? 751 HOH   B O   1 
HETATM 3889 O O   . HOH   G 5 .   ? 31.081  -4.250  18.799 1.00 41.52  ? 752 HOH   B O   1 
HETATM 3890 O O   . HOH   G 5 .   ? 27.599  -16.512 13.582 1.00 36.60  ? 753 HOH   B O   1 
HETATM 3891 O O   . HOH   G 5 .   ? 36.638  -6.294  16.220 1.00 48.94  ? 754 HOH   B O   1 
HETATM 3892 O O   . HOH   G 5 .   ? 8.349   -37.791 20.018 1.00 41.27  ? 755 HOH   B O   1 
HETATM 3893 O O   . HOH   G 5 .   ? 42.031  -39.342 19.124 1.00 38.77  ? 756 HOH   B O   1 
HETATM 3894 O O   . HOH   G 5 .   ? 26.321  -33.394 6.311  1.00 38.76  ? 757 HOH   B O   1 
HETATM 3895 O O   . HOH   G 5 .   ? 19.980  -27.974 8.835  1.00 52.63  ? 758 HOH   B O   1 
HETATM 3896 O O   . HOH   G 5 .   ? 22.999  -18.320 10.765 1.00 39.40  ? 759 HOH   B O   1 
HETATM 3897 O O   . HOH   G 5 .   ? 18.374  -47.550 32.953 1.00 44.79  ? 760 HOH   B O   1 
HETATM 3898 O O   . HOH   G 5 .   ? 22.061  -26.646 7.742  1.00 47.88  ? 761 HOH   B O   1 
HETATM 3899 O O   . HOH   G 5 .   ? 43.155  -44.235 38.225 1.00 36.16  ? 762 HOH   B O   1 
HETATM 3900 O O   . HOH   G 5 .   ? 34.885  -18.377 17.412 1.00 34.53  ? 763 HOH   B O   1 
HETATM 3901 O O   . HOH   G 5 .   ? 34.686  -37.303 19.648 1.00 42.67  ? 764 HOH   B O   1 
HETATM 3902 O O   . HOH   G 5 .   ? 21.456  -21.738 32.374 1.00 43.40  ? 765 HOH   B O   1 
HETATM 3903 O O   . HOH   G 5 .   ? 15.869  -37.265 30.676 1.00 51.42  ? 766 HOH   B O   1 
HETATM 3904 O O   . HOH   G 5 .   ? 19.326  -17.481 16.853 1.00 28.84  ? 767 HOH   B O   1 
HETATM 3905 O O   . HOH   G 5 .   ? 6.125   -39.746 19.184 1.00 46.53  ? 768 HOH   B O   1 
HETATM 3906 O O   . HOH   G 5 .   ? 21.428  -23.734 7.833  1.00 36.05  ? 769 HOH   B O   1 
HETATM 3907 O O   . HOH   G 5 .   ? 24.873  -5.697  22.914 1.00 43.98  ? 770 HOH   B O   1 
HETATM 3908 O O   . HOH   G 5 .   ? 37.265  -19.294 18.332 1.00 38.47  ? 771 HOH   B O   1 
HETATM 3909 O O   . HOH   G 5 .   ? 34.343  -18.305 13.308 1.00 42.69  ? 772 HOH   B O   1 
HETATM 3910 O O   . HOH   G 5 .   ? 43.455  -34.694 23.668 1.00 48.06  ? 773 HOH   B O   1 
HETATM 3911 O O   . HOH   G 5 .   ? 42.441  -36.547 21.833 1.00 58.00  ? 774 HOH   B O   1 
HETATM 3912 O O   . HOH   G 5 .   ? 16.697  -39.779 31.534 1.00 52.75  ? 775 HOH   B O   1 
HETATM 3913 O O   . HOH   G 5 .   ? 31.955  -38.348 24.726 1.00 25.26  ? 776 HOH   B O   1 
HETATM 3914 O O   . HOH   G 5 .   ? 41.750  -39.309 28.091 1.00 54.35  ? 777 HOH   B O   1 
HETATM 3915 O O   . HOH   G 5 .   ? 39.761  -18.508 17.274 1.00 51.85  ? 778 HOH   B O   1 
HETATM 3916 O O   . HOH   G 5 .   ? 11.171  -38.917 12.292 1.00 43.69  ? 779 HOH   B O   1 
HETATM 3917 O O   . HOH   G 5 .   ? 43.405  -8.332  13.723 1.00 55.13  ? 780 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   . LEU A 14  ? 1.0067 0.8939 0.5138 -0.1229 0.0630  0.1801  306 LEU A N   
2    C CA  . LEU A 14  ? 0.8795 0.7667 0.4484 -0.1015 0.0281  0.1953  306 LEU A CA  
3    C C   . LEU A 14  ? 0.9052 0.7888 0.5322 -0.0675 0.0399  0.1655  306 LEU A C   
4    O O   . LEU A 14  ? 0.9277 0.8106 0.6120 -0.0519 0.0344  0.1728  306 LEU A O   
5    C CB  . LEU A 14  ? 0.8760 0.7633 0.4170 -0.1136 -0.0028 0.2061  306 LEU A CB  
6    N N   . ALA A 15  ? 0.9621 0.8414 0.5711 -0.0599 0.0563  0.1326  307 ALA A N   
7    C CA  . ALA A 15  ? 0.6968 0.5763 0.3576 -0.0316 0.0641  0.1090  307 ALA A CA  
8    C C   . ALA A 15  ? 0.6765 0.5668 0.3733 -0.0235 0.0889  0.1050  307 ALA A C   
9    O O   . ALA A 15  ? 0.7134 0.6084 0.4621 -0.0071 0.0836  0.1010  307 ALA A O   
10   C CB  . ALA A 15  ? 0.7871 0.6591 0.4233 -0.0269 0.0764  0.0794  307 ALA A CB  
11   N N   . LEU A 16  ? 0.7341 0.6299 0.4035 -0.0381 0.1163  0.1071  308 LEU A N   
12   C CA  . LEU A 16  ? 0.7169 0.6292 0.4285 -0.0316 0.1409  0.1080  308 LEU A CA  
13   C C   . LEU A 16  ? 0.7940 0.7130 0.5392 -0.0366 0.1236  0.1343  308 LEU A C   
14   O O   . LEU A 16  ? 0.7678 0.7035 0.5562 -0.0332 0.1363  0.1384  308 LEU A O   
15   C CB  . LEU A 16  ? 0.7874 0.7025 0.4628 -0.0453 0.1830  0.1009  308 LEU A CB  
16   C CG  . LEU A 16  ? 0.8020 0.7038 0.4516 -0.0402 0.2125  0.0694  308 LEU A CG  
17   C CD1 . LEU A 16  ? 0.7805 0.6765 0.3864 -0.0582 0.2614  0.0595  308 LEU A CD1 
18   C CD2 . LEU A 16  ? 0.7157 0.6288 0.4360 -0.0114 0.2196  0.0575  308 LEU A CD2 
19   N N   . SER A 17  ? 0.7544 0.6612 0.4860 -0.0460 0.0954  0.1549  309 SER A N   
20   C CA  . SER A 17  ? 0.8140 0.7184 0.5792 -0.0513 0.0810  0.1797  309 SER A CA  
21   C C   . SER A 17  ? 0.7910 0.6801 0.6003 -0.0368 0.0584  0.1759  309 SER A C   
22   O O   . SER A 17  ? 0.8072 0.6848 0.6460 -0.0415 0.0487  0.1921  309 SER A O   
23   C CB  . SER A 17  ? 0.8154 0.7148 0.5461 -0.0728 0.0684  0.2115  309 SER A CB  
24   O OG  . SER A 17  ? 0.9391 0.8252 0.6723 -0.0694 0.0384  0.2241  309 SER A OG  
25   N N   . LEU A 18  ? 0.7006 0.5857 0.5134 -0.0213 0.0531  0.1537  310 LEU A N   
26   C CA  . LEU A 18  ? 0.6002 0.4690 0.4492 -0.0097 0.0382  0.1458  310 LEU A CA  
27   C C   . LEU A 18  ? 0.6211 0.4951 0.5023 -0.0106 0.0453  0.1351  310 LEU A C   
28   O O   . LEU A 18  ? 0.7033 0.6007 0.5884 -0.0105 0.0595  0.1277  310 LEU A O   
29   C CB  . LEU A 18  ? 0.6813 0.5476 0.5223 0.0045  0.0319  0.1263  310 LEU A CB  
30   C CG  . LEU A 18  ? 0.7689 0.6312 0.5837 0.0029  0.0175  0.1377  310 LEU A CG  
31   C CD1 . LEU A 18  ? 0.5413 0.4040 0.3516 0.0156  0.0143  0.1154  310 LEU A CD1 
32   C CD2 . LEU A 18  ? 0.7922 0.6394 0.6361 0.0023  -0.0005 0.1643  310 LEU A CD2 
33   N N   . THR A 19  ? 0.5538 0.4052 0.4607 -0.0138 0.0363  0.1358  311 THR A N   
34   C CA  . THR A 19  ? 0.6332 0.4866 0.5615 -0.0218 0.0380  0.1232  311 THR A CA  
35   C C   . THR A 19  ? 0.5766 0.4347 0.5041 -0.0116 0.0350  0.0995  311 THR A C   
36   O O   . THR A 19  ? 0.5020 0.3576 0.4166 0.0033  0.0327  0.0915  311 THR A O   
37   C CB  . THR A 19  ? 0.5733 0.3916 0.5196 -0.0340 0.0337  0.1262  311 THR A CB  
38   O OG1 . THR A 19  ? 0.6266 0.4139 0.5781 -0.0230 0.0305  0.1128  311 THR A OG1 
39   C CG2 . THR A 19  ? 0.5886 0.3984 0.5390 -0.0418 0.0342  0.1547  311 THR A CG2 
40   N N   . ALA A 20  ? 0.5611 0.4282 0.5019 -0.0236 0.0329  0.0911  312 ALA A N   
41   C CA  . ALA A 20  ? 0.5266 0.4006 0.4657 -0.0190 0.0280  0.0729  312 ALA A CA  
42   C C   . ALA A 20  ? 0.6192 0.4564 0.5490 -0.0140 0.0251  0.0556  312 ALA A C   
43   O O   . ALA A 20  ? 0.6587 0.4986 0.5815 -0.0009 0.0235  0.0434  312 ALA A O   
44   C CB  . ALA A 20  ? 0.5175 0.4125 0.4710 -0.0406 0.0215  0.0745  312 ALA A CB  
45   N N   . ASP A 21  ? 0.5908 0.3920 0.5254 -0.0239 0.0278  0.0549  313 ASP A N   
46   C CA  . ASP A 21  ? 0.6740 0.4372 0.6106 -0.0174 0.0331  0.0390  313 ASP A CA  
47   C C   . ASP A 21  ? 0.5495 0.3122 0.4946 0.0071  0.0315  0.0505  313 ASP A C   
48   O O   . ASP A 21  ? 0.5644 0.3191 0.5127 0.0196  0.0331  0.0388  313 ASP A O   
49   C CB  . ASP A 21  ? 0.6558 0.3746 0.6025 -0.0344 0.0426  0.0349  313 ASP A CB  
50   C CG  . ASP A 21  ? 0.7738 0.4908 0.7042 -0.0671 0.0411  0.0223  313 ASP A CG  
51   O OD1 . ASP A 21  ? 1.0310 0.7711 0.9654 -0.0811 0.0339  0.0393  313 ASP A OD1 
52   O OD2 . ASP A 21  ? 0.8775 0.5719 0.7898 -0.0820 0.0468  -0.0034 313 ASP A OD2 
53   N N   . GLN A 22  ? 0.5986 0.3723 0.5459 0.0104  0.0272  0.0756  314 GLN A N   
54   C CA  . GLN A 22  ? 0.6219 0.4022 0.5699 0.0256  0.0199  0.0915  314 GLN A CA  
55   C C   . GLN A 22  ? 0.5826 0.3903 0.5065 0.0343  0.0159  0.0805  314 GLN A C   
56   O O   . GLN A 22  ? 0.5483 0.3582 0.4713 0.0446  0.0086  0.0850  314 GLN A O   
57   C CB  . GLN A 22  ? 0.5717 0.3593 0.5162 0.0188  0.0148  0.1225  314 GLN A CB  
58   C CG  . GLN A 22  ? 0.5484 0.3064 0.5235 0.0114  0.0177  0.1398  314 GLN A CG  
59   C CD  . GLN A 22  ? 0.5785 0.3491 0.5452 0.0007  0.0116  0.1732  314 GLN A CD  
60   O OE1 . GLN A 22  ? 0.7620 0.5611 0.6955 -0.0069 0.0129  0.1749  314 GLN A OE1 
61   N NE2 . GLN A 22  ? 0.7412 0.4894 0.7408 -0.0006 0.0077  0.2012  314 GLN A NE2 
62   N N   . MET A 23  ? 0.5532 0.3820 0.4633 0.0296  0.0207  0.0690  315 MET A N   
63   C CA  . MET A 23  ? 0.4694 0.3180 0.3640 0.0388  0.0210  0.0576  315 MET A CA  
64   C C   . MET A 23  ? 0.4561 0.2982 0.3580 0.0451  0.0184  0.0384  315 MET A C   
65   O O   . MET A 23  ? 0.5391 0.3863 0.4334 0.0554  0.0152  0.0321  315 MET A O   
66   C CB  . MET A 23  ? 0.4950 0.3692 0.3867 0.0341  0.0310  0.0580  315 MET A CB  
67   C CG  . MET A 23  ? 0.5626 0.4531 0.4501 0.0440  0.0362  0.0458  315 MET A CG  
68   S SD  . MET A 23  ? 0.5897 0.4768 0.4408 0.0486  0.0424  0.0454  315 MET A SD  
69   C CE  . MET A 23  ? 0.5771 0.4721 0.4156 0.0362  0.0582  0.0611  315 MET A CE  
70   N N   . VAL A 24  ? 0.5174 0.3469 0.4292 0.0349  0.0205  0.0284  316 VAL A N   
71   C CA  . VAL A 24  ? 0.4735 0.2922 0.3853 0.0361  0.0213  0.0095  316 VAL A CA  
72   C C   . VAL A 24  ? 0.4368 0.2343 0.3618 0.0496  0.0235  0.0097  316 VAL A C   
73   O O   . VAL A 24  ? 0.5476 0.3496 0.4727 0.0596  0.0220  0.0018  316 VAL A O   
74   C CB  . VAL A 24  ? 0.5273 0.3309 0.4358 0.0140  0.0252  -0.0028 316 VAL A CB  
75   C CG1 . VAL A 24  ? 0.4914 0.2734 0.3932 0.0116  0.0324  -0.0246 316 VAL A CG1 
76   C CG2 . VAL A 24  ? 0.4890 0.3252 0.3932 -0.0005 0.0174  0.0024  316 VAL A CG2 
77   N N   . SER A 25  ? 0.4360 0.2123 0.3796 0.0502  0.0267  0.0232  317 SER A N   
78   C CA  . SER A 25  ? 0.5016 0.2606 0.4753 0.0639  0.0295  0.0314  317 SER A CA  
79   C C   . SER A 25  ? 0.5059 0.2905 0.4768 0.0754  0.0143  0.0470  317 SER A C   
80   O O   . SER A 25  ? 0.5681 0.3529 0.5583 0.0862  0.0139  0.0462  317 SER A O   
81   C CB  . SER A 25  ? 0.4761 0.2104 0.4795 0.0621  0.0343  0.0510  317 SER A CB  
82   O OG  . SER A 25  ? 0.7463 0.4429 0.7588 0.0519  0.0540  0.0312  317 SER A OG  
83   N N   . ALA A 26  ? 0.4979 0.3034 0.4430 0.0701  0.0038  0.0605  318 ALA A N   
84   C CA  . ALA A 26  ? 0.5284 0.3533 0.4576 0.0728  -0.0101 0.0721  318 ALA A CA  
85   C C   . ALA A 26  ? 0.5409 0.3763 0.4547 0.0780  -0.0091 0.0500  318 ALA A C   
86   O O   . ALA A 26  ? 0.4895 0.3329 0.4044 0.0819  -0.0191 0.0547  318 ALA A O   
87   C CB  . ALA A 26  ? 0.4686 0.3066 0.3627 0.0604  -0.0144 0.0857  318 ALA A CB  
88   N N   . LEU A 27  ? 0.4211 0.2590 0.3243 0.0760  0.0006  0.0297  319 LEU A N   
89   C CA  . LEU A 27  ? 0.5065 0.3544 0.4004 0.0805  0.0010  0.0131  319 LEU A CA  
90   C C   . LEU A 27  ? 0.4410 0.2796 0.3554 0.0863  0.0031  0.0031  319 LEU A C   
91   O O   . LEU A 27  ? 0.3759 0.2219 0.2899 0.0920  -0.0013 -0.0013 319 LEU A O   
92   C CB  . LEU A 27  ? 0.3768 0.2360 0.2631 0.0755  0.0083  0.0036  319 LEU A CB  
93   C CG  . LEU A 27  ? 0.3778 0.2486 0.2491 0.0727  0.0143  0.0103  319 LEU A CG  
94   C CD1 . LEU A 27  ? 0.3914 0.2791 0.2746 0.0712  0.0223  0.0068  319 LEU A CD1 
95   C CD2 . LEU A 27  ? 0.4167 0.2873 0.2640 0.0751  0.0131  0.0092  319 LEU A CD2 
96   N N   . LEU A 28  ? 0.4314 0.2508 0.3620 0.0828  0.0131  -0.0024 320 LEU A N   
97   C CA  . LEU A 28  ? 0.4527 0.2575 0.4021 0.0869  0.0235  -0.0144 320 LEU A CA  
98   C C   . LEU A 28  ? 0.4978 0.3036 0.4805 0.1006  0.0195  0.0026  320 LEU A C   
99   O O   . LEU A 28  ? 0.4564 0.2658 0.4539 0.1074  0.0229  -0.0028 320 LEU A O   
100  C CB  . LEU A 28  ? 0.4932 0.2681 0.4483 0.0762  0.0411  -0.0271 320 LEU A CB  
101  C CG  . LEU A 28  ? 0.5154 0.2908 0.4385 0.0554  0.0434  -0.0448 320 LEU A CG  
102  C CD1 . LEU A 28  ? 0.4492 0.1875 0.3705 0.0384  0.0617  -0.0592 320 LEU A CD1 
103  C CD2 . LEU A 28  ? 0.4101 0.1995 0.3171 0.0522  0.0422  -0.0580 320 LEU A CD2 
104  N N   A ASP A 29  ? 0.5081 0.3144 0.5063 0.1026  0.0106  0.0278  321 ASP A N   
105  N N   B ASP A 29  ? 0.5087 0.3149 0.5069 0.1026  0.0106  0.0278  321 ASP A N   
106  C CA  A ASP A 29  ? 0.4915 0.3065 0.5284 0.1120  0.0006  0.0541  321 ASP A CA  
107  C CA  B ASP A 29  ? 0.4909 0.3059 0.5278 0.1120  0.0006  0.0540  321 ASP A CA  
108  C C   A ASP A 29  ? 0.4832 0.3256 0.4973 0.1093  -0.0198 0.0608  321 ASP A C   
109  C C   B ASP A 29  ? 0.4828 0.3251 0.4968 0.1094  -0.0197 0.0604  321 ASP A C   
110  O O   A ASP A 29  ? 0.4815 0.3364 0.5273 0.1149  -0.0283 0.0762  321 ASP A O   
111  O O   B ASP A 29  ? 0.4843 0.3391 0.5298 0.1151  -0.0279 0.0753  321 ASP A O   
112  C CB  A ASP A 29  ? 0.4709 0.2820 0.5295 0.1101  -0.0074 0.0856  321 ASP A CB  
113  C CB  B ASP A 29  ? 0.4671 0.2784 0.5257 0.1101  -0.0075 0.0857  321 ASP A CB  
114  C CG  A ASP A 29  ? 0.5180 0.3389 0.6362 0.1194  -0.0173 0.1211  321 ASP A CG  
115  C CG  B ASP A 29  ? 0.4737 0.2513 0.5705 0.1144  0.0151  0.0827  321 ASP A CG  
116  O OD1 A ASP A 29  ? 0.5507 0.3668 0.7080 0.1268  -0.0002 0.1100  321 ASP A OD1 
117  O OD1 B ASP A 29  ? 0.4940 0.2519 0.6010 0.1172  0.0381  0.0555  321 ASP A OD1 
118  O OD2 A ASP A 29  ? 0.4867 0.3293 0.6007 0.1109  -0.0427 0.1547  321 ASP A OD2 
119  O OD2 B ASP A 29  ? 0.5706 0.3405 0.6820 0.1110  0.0110  0.1060  321 ASP A OD2 
120  N N   . ALA A 30  ? 0.5456 0.3962 0.5091 0.0997  -0.0256 0.0498  322 ALA A N   
121  C CA  . ALA A 30  ? 0.5821 0.4489 0.5166 0.0936  -0.0396 0.0498  322 ALA A CA  
122  C C   . ALA A 30  ? 0.4507 0.3204 0.3874 0.0995  -0.0342 0.0294  322 ALA A C   
123  O O   . ALA A 30  ? 0.4798 0.3592 0.3982 0.0942  -0.0448 0.0286  322 ALA A O   
124  C CB  . ALA A 30  ? 0.4942 0.3616 0.3785 0.0821  -0.0383 0.0423  322 ALA A CB  
125  N N   . GLU A 31  ? 0.4293 0.2891 0.3833 0.1063  -0.0179 0.0131  323 GLU A N   
126  C CA  . GLU A 31  ? 0.4529 0.3166 0.4026 0.1081  -0.0126 -0.0048 323 GLU A CA  
127  C C   . GLU A 31  ? 0.4539 0.3292 0.4282 0.1125  -0.0208 0.0051  323 GLU A C   
128  O O   . GLU A 31  ? 0.5079 0.3834 0.5250 0.1193  -0.0184 0.0202  323 GLU A O   
129  C CB  . GLU A 31  ? 0.3747 0.2245 0.3315 0.1072  0.0061  -0.0219 323 GLU A CB  
130  C CG  . GLU A 31  ? 0.6757 0.5318 0.6203 0.1036  0.0103  -0.0377 323 GLU A CG  
131  C CD  . GLU A 31  ? 0.4441 0.3103 0.3607 0.0967  0.0039  -0.0421 323 GLU A CD  
132  O OE1 . GLU A 31  ? 0.5039 0.3760 0.4127 0.0903  0.0061  -0.0502 323 GLU A OE1 
133  O OE2 . GLU A 31  ? 0.4010 0.2704 0.3073 0.0970  -0.0017 -0.0352 323 GLU A OE2 
134  N N   . PRO A 32  ? 0.4181 0.3033 0.3738 0.1086  -0.0294 -0.0005 324 PRO A N   
135  C CA  . PRO A 32  ? 0.3391 0.2384 0.3188 0.1091  -0.0397 0.0109  324 PRO A CA  
136  C C   . PRO A 32  ? 0.4067 0.3061 0.4201 0.1177  -0.0226 0.0026  324 PRO A C   
137  O O   . PRO A 32  ? 0.3524 0.2393 0.3546 0.1179  -0.0049 -0.0163 324 PRO A O   
138  C CB  . PRO A 32  ? 0.3753 0.2769 0.3171 0.0993  -0.0497 0.0018  324 PRO A CB  
139  C CG  . PRO A 32  ? 0.5049 0.3956 0.4224 0.1010  -0.0360 -0.0176 324 PRO A CG  
140  C CD  . PRO A 32  ? 0.4674 0.3507 0.3865 0.1035  -0.0281 -0.0156 324 PRO A CD  
141  N N   . PRO A 33  ? 0.4095 0.3239 0.4633 0.1214  -0.0265 0.0175  325 PRO A N   
142  C CA  . PRO A 33  ? 0.3182 0.2320 0.4043 0.1286  -0.0038 0.0080  325 PRO A CA  
143  C C   . PRO A 33  ? 0.2979 0.2147 0.3530 0.1216  -0.0022 -0.0101 325 PRO A C   
144  O O   . PRO A 33  ? 0.3179 0.2396 0.3418 0.1139  -0.0200 -0.0109 325 PRO A O   
145  C CB  . PRO A 33  ? 0.2969 0.2327 0.4459 0.1351  -0.0106 0.0367  325 PRO A CB  
146  C CG  . PRO A 33  ? 0.3411 0.2940 0.4719 0.1231  -0.0459 0.0581  325 PRO A CG  
147  C CD  . PRO A 33  ? 0.3613 0.2967 0.4341 0.1156  -0.0519 0.0463  325 PRO A CD  
148  N N   . ILE A 34  ? 0.2897 0.2003 0.3534 0.1223  0.0223  -0.0248 326 ILE A N   
149  C CA  . ILE A 34  ? 0.3458 0.2627 0.3873 0.1139  0.0244  -0.0362 326 ILE A CA  
150  C C   . ILE A 34  ? 0.3141 0.2524 0.3938 0.1167  0.0188  -0.0214 326 ILE A C   
151  O O   . ILE A 34  ? 0.2856 0.2296 0.4135 0.1245  0.0372  -0.0150 326 ILE A O   
152  C CB  . ILE A 34  ? 0.4290 0.3313 0.4530 0.1058  0.0522  -0.0571 326 ILE A CB  
153  C CG1 . ILE A 34  ? 0.4567 0.3425 0.4415 0.0972  0.0517  -0.0682 326 ILE A CG1 
154  C CG2 . ILE A 34  ? 0.3592 0.2728 0.3642 0.0945  0.0525  -0.0622 326 ILE A CG2 
155  C CD1 . ILE A 34  ? 0.5019 0.3682 0.4638 0.0822  0.0787  -0.0891 326 ILE A CD1 
156  N N   . LEU A 35  ? 0.2867 0.2355 0.3493 0.1097  -0.0043 -0.0155 327 LEU A N   
157  C CA  . LEU A 35  ? 0.2801 0.2504 0.3754 0.1073  -0.0152 0.0006  327 LEU A CA  
158  C C   . LEU A 35  ? 0.3032 0.2796 0.4006 0.1029  -0.0003 -0.0078 327 LEU A C   
159  O O   . LEU A 35  ? 0.2938 0.2586 0.3553 0.0971  0.0098  -0.0240 327 LEU A O   
160  C CB  . LEU A 35  ? 0.3226 0.2947 0.3918 0.0960  -0.0454 0.0083  327 LEU A CB  
161  C CG  . LEU A 35  ? 0.2782 0.2464 0.3362 0.0938  -0.0618 0.0188  327 LEU A CG  
162  C CD1 . LEU A 35  ? 0.2959 0.2648 0.3245 0.0749  -0.0881 0.0249  327 LEU A CD1 
163  C CD2 . LEU A 35  ? 0.2800 0.2644 0.3945 0.1030  -0.0600 0.0421  327 LEU A CD2 
164  N N   . TYR A 36  ? 0.2674 0.2661 0.4095 0.1029  -0.0009 0.0076  328 TYR A N   
165  C CA  . TYR A 36  ? 0.2910 0.2995 0.4417 0.0976  0.0150  0.0034  328 TYR A CA  
166  C C   . TYR A 36  ? 0.2611 0.2815 0.4055 0.0853  -0.0105 0.0135  328 TYR A C   
167  O O   . TYR A 36  ? 0.3066 0.3328 0.4551 0.0801  -0.0374 0.0271  328 TYR A O   
168  C CB  . TYR A 36  ? 0.2736 0.2990 0.4903 0.1072  0.0419  0.0133  328 TYR A CB  
169  C CG  . TYR A 36  ? 0.4017 0.4058 0.6190 0.1145  0.0817  -0.0060 328 TYR A CG  
170  C CD1 . TYR A 36  ? 0.2972 0.2841 0.5197 0.1246  0.0849  -0.0075 328 TYR A CD1 
171  C CD2 . TYR A 36  ? 0.3151 0.3131 0.5228 0.1074  0.1176  -0.0238 328 TYR A CD2 
172  C CE1 . TYR A 36  ? 0.4502 0.4112 0.6679 0.1265  0.1219  -0.0278 328 TYR A CE1 
173  C CE2 . TYR A 36  ? 0.3467 0.3178 0.5451 0.1078  0.1578  -0.0464 328 TYR A CE2 
174  C CZ  . TYR A 36  ? 0.3525 0.3044 0.5528 0.1153  0.1565  -0.0482 328 TYR A CZ  
175  O OH  . TYR A 36  ? 0.5586 0.4830 0.7349 0.1048  0.1844  -0.0679 328 TYR A OH  
176  N N   . SER A 37  ? 0.3276 0.3494 0.4579 0.0769  -0.0016 0.0071  329 SER A N   
177  C CA  . SER A 37  ? 0.2905 0.3230 0.4260 0.0647  -0.0202 0.0181  329 SER A CA  
178  C C   . SER A 37  ? 0.2763 0.3405 0.4747 0.0649  -0.0188 0.0390  329 SER A C   
179  O O   . SER A 37  ? 0.2985 0.3758 0.5399 0.0762  0.0069  0.0426  329 SER A O   
180  C CB  . SER A 37  ? 0.3272 0.3543 0.4352 0.0550  -0.0114 0.0107  329 SER A CB  
181  O OG  . SER A 37  ? 0.3140 0.3442 0.4250 0.0429  -0.0302 0.0207  329 SER A OG  
182  N N   . GLU A 38  ? 0.3939 0.4693 0.6011 0.0510  -0.0449 0.0535  330 GLU A N   
183  C CA  . GLU A 38  ? 0.3509 0.4631 0.6237 0.0474  -0.0519 0.0806  330 GLU A CA  
184  C C   . GLU A 38  ? 0.2843 0.4173 0.5979 0.0512  -0.0203 0.0837  330 GLU A C   
185  O O   . GLU A 38  ? 0.4544 0.5775 0.7364 0.0432  -0.0099 0.0716  330 GLU A O   
186  C CB  . GLU A 38  ? 0.5155 0.6314 0.7770 0.0236  -0.0888 0.0930  330 GLU A CB  
187  C CG  . GLU A 38  ? 0.5045 0.5885 0.7054 0.0136  -0.1128 0.0808  330 GLU A CG  
188  C CD  . GLU A 38  ? 0.6754 0.7197 0.8168 0.0104  -0.1070 0.0548  330 GLU A CD  
189  O OE1 . GLU A 38  ? 0.6845 0.7173 0.8108 -0.0080 -0.1193 0.0539  330 GLU A OE1 
190  O OE2 . GLU A 38  ? 0.5363 0.5613 0.6514 0.0254  -0.0902 0.0379  330 GLU A OE2 
191  N N   . TYR A 39  ? 0.3264 0.4889 0.7143 0.0630  -0.0028 0.1025  331 TYR A N   
192  C CA  . TYR A 39  ? 0.2833 0.4675 0.7203 0.0670  0.0344  0.1066  331 TYR A CA  
193  C C   . TYR A 39  ? 0.4230 0.6480 0.9176 0.0538  0.0139  0.1387  331 TYR A C   
194  O O   . TYR A 39  ? 0.4969 0.7599 1.0799 0.0619  0.0222  0.1674  331 TYR A O   
195  C CB  . TYR A 39  ? 0.3557 0.5442 0.8511 0.0895  0.0750  0.1074  331 TYR A CB  
196  C CG  . TYR A 39  ? 0.4274 0.5756 0.8680 0.0966  0.1106  0.0711  331 TYR A CG  
197  C CD1 . TYR A 39  ? 0.5015 0.6391 0.9211 0.0910  0.1549  0.0489  331 TYR A CD1 
198  C CD2 . TYR A 39  ? 0.3565 0.4782 0.7646 0.1046  0.1001  0.0603  331 TYR A CD2 
199  C CE1 . TYR A 39  ? 0.3497 0.4502 0.7119 0.0895  0.1849  0.0162  331 TYR A CE1 
200  C CE2 . TYR A 39  ? 0.4283 0.5143 0.7869 0.1066  0.1302  0.0288  331 TYR A CE2 
201  C CZ  . TYR A 39  ? 0.3494 0.4246 0.6834 0.0975  0.1713  0.0066  331 TYR A CZ  
202  O OH  . TYR A 39  ? 0.4479 0.4870 0.7246 0.0917  0.1985  -0.0246 331 TYR A OH  
203  N N   . ASP A 40  ? 0.3974 0.6143 0.8463 0.0324  -0.0130 0.1359  332 ASP A N   
204  C CA  . ASP A 40  ? 0.4200 0.6711 0.9134 0.0138  -0.0357 0.1642  332 ASP A CA  
205  C C   . ASP A 40  ? 0.3588 0.6206 0.8628 0.0086  -0.0063 0.1614  332 ASP A C   
206  O O   . ASP A 40  ? 0.3723 0.6065 0.8127 -0.0026 -0.0077 0.1430  332 ASP A O   
207  C CB  . ASP A 40  ? 0.4992 0.7298 0.9377 -0.0110 -0.0824 0.1629  332 ASP A CB  
208  C CG  . ASP A 40  ? 0.5287 0.7952 1.0136 -0.0362 -0.1136 0.1954  332 ASP A CG  
209  O OD1 . ASP A 40  ? 0.4801 0.7952 1.0512 -0.0311 -0.1025 0.2248  332 ASP A OD1 
210  O OD2 . ASP A 40  ? 0.6984 0.9437 1.1358 -0.0627 -0.1475 0.1916  332 ASP A OD2 
211  N N   . PRO A 41  ? 0.3927 0.6948 0.9786 0.0158  0.0223  0.1816  333 PRO A N   
212  C CA  . PRO A 41  ? 0.4537 0.7672 1.0454 0.0069  0.0526  0.1795  333 PRO A CA  
213  C C   . PRO A 41  ? 0.4732 0.7933 1.0497 -0.0204 0.0174  0.1931  333 PRO A C   
214  O O   . PRO A 41  ? 0.4979 0.8089 1.0407 -0.0322 0.0316  0.1844  333 PRO A O   
215  C CB  . PRO A 41  ? 0.4896 0.8484 1.1887 0.0217  0.0899  0.2030  333 PRO A CB  
216  C CG  . PRO A 41  ? 0.4464 0.8193 1.1919 0.0287  0.0558  0.2297  333 PRO A CG  
217  C CD  . PRO A 41  ? 0.2874 0.6275 0.9706 0.0324  0.0312  0.2102  333 PRO A CD  
218  N N   . THR A 42  ? 0.4620 0.7962 1.0597 -0.0345 -0.0287 0.2155  334 THR A N   
219  C CA  . THR A 42  ? 0.4765 0.8083 1.0547 -0.0648 -0.0637 0.2254  334 THR A CA  
220  C C   . THR A 42  ? 0.5689 0.8423 1.0515 -0.0745 -0.0851 0.1969  334 THR A C   
221  O O   . THR A 42  ? 0.6699 0.9273 1.1283 -0.1003 -0.1159 0.2001  334 THR A O   
222  C CB  . THR A 42  ? 0.3196 0.6897 0.9553 -0.0837 -0.1046 0.2611  334 THR A CB  
223  O OG1 . THR A 42  ? 0.3986 0.7415 0.9860 -0.0894 -0.1390 0.2526  334 THR A OG1 
224  C CG2 . THR A 42  ? 0.3170 0.7270 1.0360 -0.0633 -0.0804 0.2877  334 THR A CG2 
225  N N   . ARG A 43  ? 0.5104 0.7508 0.9430 -0.0549 -0.0673 0.1699  335 ARG A N   
226  C CA  . ARG A 43  ? 0.4599 0.6486 0.8144 -0.0586 -0.0780 0.1452  335 ARG A CA  
227  C C   . ARG A 43  ? 0.4701 0.6433 0.7909 -0.0413 -0.0445 0.1256  335 ARG A C   
228  O O   . ARG A 43  ? 0.4721 0.6206 0.7567 -0.0276 -0.0428 0.1076  335 ARG A O   
229  C CB  . ARG A 43  ? 0.4963 0.6594 0.8183 -0.0597 -0.1059 0.1358  335 ARG A CB  
230  N N   . PRO A 44  ? 0.4720 0.6599 0.8000 -0.0456 -0.0182 0.1295  336 PRO A N   
231  C CA  . PRO A 44  ? 0.5520 0.7262 0.8380 -0.0383 0.0114  0.1119  336 PRO A CA  
232  C C   . PRO A 44  ? 0.5890 0.7247 0.8140 -0.0420 -0.0067 0.1014  336 PRO A C   
233  O O   . PRO A 44  ? 0.6396 0.7563 0.8567 -0.0514 -0.0336 0.1070  336 PRO A O   
234  C CB  . PRO A 44  ? 0.5316 0.7308 0.8334 -0.0519 0.0384  0.1227  336 PRO A CB  
235  C CG  . PRO A 44  ? 0.5413 0.7537 0.8757 -0.0683 0.0125  0.1450  336 PRO A CG  
236  C CD  . PRO A 44  ? 0.4411 0.6582 0.8092 -0.0628 -0.0155 0.1510  336 PRO A CD  
237  N N   . PHE A 45  ? 0.5440 0.6672 0.7291 -0.0358 0.0103  0.0866  337 PHE A N   
238  C CA  . PHE A 45  ? 0.5023 0.5956 0.6418 -0.0370 -0.0059 0.0818  337 PHE A CA  
239  C C   . PHE A 45  ? 0.4777 0.5690 0.6082 -0.0553 -0.0144 0.0998  337 PHE A C   
240  O O   . PHE A 45  ? 0.5169 0.6300 0.6490 -0.0700 0.0021  0.1103  337 PHE A O   
241  C CB  . PHE A 45  ? 0.4880 0.5747 0.5892 -0.0318 0.0116  0.0668  337 PHE A CB  
242  C CG  . PHE A 45  ? 0.4893 0.5536 0.5552 -0.0332 -0.0058 0.0683  337 PHE A CG  
243  C CD1 . PHE A 45  ? 0.4682 0.5096 0.5312 -0.0180 -0.0217 0.0593  337 PHE A CD1 
244  C CD2 . PHE A 45  ? 0.4422 0.5111 0.4821 -0.0511 -0.0062 0.0827  337 PHE A CD2 
245  C CE1 . PHE A 45  ? 0.4532 0.4768 0.4967 -0.0169 -0.0335 0.0636  337 PHE A CE1 
246  C CE2 . PHE A 45  ? 0.4570 0.5116 0.4800 -0.0513 -0.0235 0.0920  337 PHE A CE2 
247  C CZ  . PHE A 45  ? 0.4584 0.4903 0.4876 -0.0323 -0.0353 0.0820  337 PHE A CZ  
248  N N   . SER A 46  ? 0.4815 0.5447 0.6046 -0.0550 -0.0373 0.1041  338 SER A N   
249  C CA  . SER A 46  ? 0.4412 0.4964 0.5645 -0.0697 -0.0470 0.1250  338 SER A CA  
250  C C   . SER A 46  ? 0.4765 0.4949 0.5926 -0.0606 -0.0623 0.1239  338 SER A C   
251  O O   . SER A 46  ? 0.4266 0.4267 0.5343 -0.0455 -0.0648 0.1050  338 SER A O   
252  C CB  . SER A 46  ? 0.4116 0.4730 0.5677 -0.0835 -0.0540 0.1378  338 SER A CB  
253  O OG  . SER A 46  ? 0.5387 0.5700 0.7055 -0.0811 -0.0721 0.1293  338 SER A OG  
254  N N   . GLU A 47  ? 0.4159 0.4240 0.5404 -0.0700 -0.0701 0.1468  339 GLU A N   
255  C CA  . GLU A 47  ? 0.5699 0.5414 0.7031 -0.0595 -0.0787 0.1495  339 GLU A CA  
256  C C   . GLU A 47  ? 0.5712 0.5034 0.7149 -0.0552 -0.0827 0.1298  339 GLU A C   
257  O O   . GLU A 47  ? 0.5896 0.4891 0.7295 -0.0420 -0.0809 0.1155  339 GLU A O   
258  C CB  . GLU A 47  ? 0.4536 0.4240 0.6075 -0.0706 -0.0856 0.1852  339 GLU A CB  
259  N N   . ALA A 48  ? 0.4813 0.4164 0.6354 -0.0697 -0.0871 0.1287  340 ALA A N   
260  C CA  . ALA A 48  ? 0.5803 0.4769 0.7342 -0.0756 -0.0937 0.1102  340 ALA A CA  
261  C C   . ALA A 48  ? 0.5148 0.4131 0.6457 -0.0676 -0.0953 0.0849  340 ALA A C   
262  O O   . ALA A 48  ? 0.7013 0.5593 0.8145 -0.0665 -0.0959 0.0649  340 ALA A O   
263  C CB  . ALA A 48  ? 0.4604 0.3653 0.6331 -0.0991 -0.1023 0.1209  340 ALA A CB  
264  N N   . SER A 49  ? 0.5672 0.5095 0.6990 -0.0631 -0.0932 0.0861  341 SER A N   
265  C CA  . SER A 49  ? 0.4594 0.4091 0.5792 -0.0562 -0.0966 0.0698  341 SER A CA  
266  C C   . SER A 49  ? 0.4194 0.3630 0.5173 -0.0353 -0.0872 0.0573  341 SER A C   
267  O O   . SER A 49  ? 0.4505 0.4000 0.5389 -0.0284 -0.0893 0.0459  341 SER A O   
268  C CB  . SER A 49  ? 0.4085 0.4071 0.5549 -0.0589 -0.0950 0.0804  341 SER A CB  
269  O OG  . SER A 49  ? 0.4085 0.4333 0.5556 -0.0460 -0.0755 0.0831  341 SER A OG  
270  N N   . MET A 50  ? 0.4070 0.4161 0.4298 -0.0996 0.0276  -0.0637 342 MET A N   
271  C CA  . MET A 50  ? 0.4238 0.4283 0.4560 -0.0760 0.0233  -0.0559 342 MET A CA  
272  C C   . MET A 50  ? 0.3992 0.3887 0.4281 -0.0689 0.0260  -0.0628 342 MET A C   
273  O O   . MET A 50  ? 0.4174 0.4241 0.4506 -0.0551 0.0197  -0.0630 342 MET A O   
274  C CB  . MET A 50  ? 0.4679 0.4486 0.5065 -0.0690 0.0269  -0.0405 342 MET A CB  
275  C CG  . MET A 50  ? 0.4941 0.4745 0.5405 -0.0494 0.0229  -0.0324 342 MET A CG  
276  S SD  . MET A 50  ? 0.5598 0.5361 0.6149 -0.0441 0.0242  -0.0109 342 MET A SD  
277  C CE  . MET A 50  ? 0.4948 0.4253 0.5496 -0.0422 0.0391  -0.0022 342 MET A CE  
278  N N   . MET A 51  ? 0.4030 0.3582 0.4233 -0.0784 0.0372  -0.0684 343 MET A N   
279  C CA  . MET A 51  ? 0.3965 0.3375 0.4129 -0.0722 0.0413  -0.0757 343 MET A CA  
280  C C   . MET A 51  ? 0.4126 0.3895 0.4226 -0.0806 0.0355  -0.0885 343 MET A C   
281  O O   . MET A 51  ? 0.5013 0.4845 0.5124 -0.0702 0.0330  -0.0905 343 MET A O   
282  C CB  . MET A 51  ? 0.4484 0.3403 0.4557 -0.0805 0.0585  -0.0803 343 MET A CB  
283  C CG  . MET A 51  ? 0.6660 0.5254 0.6818 -0.0693 0.0662  -0.0625 343 MET A CG  
284  S SD  . MET A 51  ? 0.7452 0.6136 0.7777 -0.0398 0.0586  -0.0437 343 MET A SD  
285  C CE  . MET A 51  ? 0.6044 0.4721 0.6322 -0.0327 0.0591  -0.0566 343 MET A CE  
286  N N   . GLY A 52  ? 0.4032 0.4090 0.4072 -0.0997 0.0334  -0.0951 344 GLY A N   
287  C CA  . GLY A 52  ? 0.4055 0.4591 0.4063 -0.1058 0.0269  -0.1021 344 GLY A CA  
288  C C   . GLY A 52  ? 0.2616 0.3475 0.2763 -0.0813 0.0159  -0.0909 344 GLY A C   
289  O O   . GLY A 52  ? 0.3334 0.4417 0.3490 -0.0739 0.0125  -0.0912 344 GLY A O   
290  N N   . LEU A 53  ? 0.3087 0.3955 0.3332 -0.0692 0.0121  -0.0809 345 LEU A N   
291  C CA  . LEU A 53  ? 0.3637 0.4702 0.3988 -0.0467 0.0060  -0.0720 345 LEU A CA  
292  C C   . LEU A 53  ? 0.3108 0.3900 0.3481 -0.0306 0.0064  -0.0687 345 LEU A C   
293  O O   . LEU A 53  ? 0.3006 0.3955 0.3416 -0.0170 0.0036  -0.0652 345 LEU A O   
294  C CB  . LEU A 53  ? 0.3130 0.4220 0.3546 -0.0414 0.0045  -0.0655 345 LEU A CB  
295  C CG  . LEU A 53  ? 0.2540 0.3934 0.2946 -0.0561 0.0037  -0.0671 345 LEU A CG  
296  C CD1 . LEU A 53  ? 0.4152 0.5540 0.4615 -0.0506 0.0031  -0.0613 345 LEU A CD1 
297  C CD2 . LEU A 53  ? 0.2506 0.4419 0.2937 -0.0541 0.0007  -0.0669 345 LEU A CD2 
298  N N   . LEU A 54  ? 0.2913 0.3321 0.3272 -0.0313 0.0108  -0.0678 346 LEU A N   
299  C CA  . LEU A 54  ? 0.2773 0.2973 0.3156 -0.0172 0.0112  -0.0634 346 LEU A CA  
300  C C   . LEU A 54  ? 0.2851 0.3069 0.3180 -0.0184 0.0129  -0.0703 346 LEU A C   
301  O O   . LEU A 54  ? 0.3472 0.3714 0.3826 -0.0057 0.0102  -0.0666 346 LEU A O   
302  C CB  . LEU A 54  ? 0.3290 0.3163 0.3689 -0.0166 0.0163  -0.0573 346 LEU A CB  
303  C CG  . LEU A 54  ? 0.3966 0.3877 0.4421 -0.0153 0.0138  -0.0481 346 LEU A CG  
304  C CD1 . LEU A 54  ? 0.2825 0.2493 0.3309 -0.0154 0.0197  -0.0380 346 LEU A CD1 
305  C CD2 . LEU A 54  ? 0.3220 0.3251 0.3709 -0.0035 0.0087  -0.0441 346 LEU A CD2 
306  N N   . THR A 55  ? 0.3204 0.3413 0.3441 -0.0360 0.0182  -0.0811 347 THR A N   
307  C CA  . THR A 55  ? 0.3627 0.3911 0.3789 -0.0413 0.0205  -0.0899 347 THR A CA  
308  C C   . THR A 55  ? 0.2939 0.3703 0.3132 -0.0365 0.0122  -0.0864 347 THR A C   
309  O O   . THR A 55  ? 0.3190 0.4041 0.3388 -0.0278 0.0103  -0.0843 347 THR A O   
310  C CB  . THR A 55  ? 0.3689 0.3853 0.3708 -0.0663 0.0305  -0.1052 347 THR A CB  
311  O OG1 . THR A 55  ? 0.5860 0.5510 0.5858 -0.0654 0.0421  -0.1057 347 THR A OG1 
312  C CG2 . THR A 55  ? 0.3329 0.3687 0.3243 -0.0771 0.0327  -0.1168 347 THR A CG2 
313  N N   . ASN A 56  ? 0.3006 0.4112 0.3229 -0.0406 0.0079  -0.0836 348 ASN A N   
314  C CA  . ASN A 56  ? 0.3763 0.5366 0.4045 -0.0317 0.0019  -0.0754 348 ASN A CA  
315  C C   . ASN A 56  ? 0.2548 0.4059 0.2931 -0.0052 -0.0005 -0.0625 348 ASN A C   
316  O O   . ASN A 56  ? 0.2724 0.4468 0.3140 0.0056  -0.0025 -0.0548 348 ASN A O   
317  C CB  . ASN A 56  ? 0.2683 0.4678 0.2996 -0.0386 -0.0005 -0.0727 348 ASN A CB  
318  C CG  . ASN A 56  ? 0.2902 0.5453 0.3307 -0.0245 -0.0047 -0.0596 348 ASN A CG  
319  O OD1 . ASN A 56  ? 0.3286 0.5838 0.3800 -0.0012 -0.0047 -0.0475 348 ASN A OD1 
320  N ND2 . ASN A 56  ? 0.4774 0.7811 0.5129 -0.0391 -0.0066 -0.0613 348 ASN A ND2 
321  N N   . LEU A 57  ? 0.3010 0.4191 0.3432 0.0036  0.0007  -0.0595 349 LEU A N   
322  C CA  . LEU A 57  ? 0.3111 0.4150 0.3588 0.0235  0.0007  -0.0503 349 LEU A CA  
323  C C   . LEU A 57  ? 0.2902 0.3753 0.3348 0.0276  0.0009  -0.0500 349 LEU A C   
324  O O   . LEU A 57  ? 0.2554 0.3455 0.3026 0.0409  0.0006  -0.0419 349 LEU A O   
325  C CB  . LEU A 57  ? 0.2649 0.3427 0.3141 0.0255  0.0024  -0.0496 349 LEU A CB  
326  C CG  . LEU A 57  ? 0.2648 0.3196 0.3147 0.0383  0.0043  -0.0442 349 LEU A CG  
327  C CD1 . LEU A 57  ? 0.2190 0.2868 0.2725 0.0533  0.0080  -0.0379 349 LEU A CD1 
328  C CD2 . LEU A 57  ? 0.2520 0.2855 0.3005 0.0324  0.0053  -0.0453 349 LEU A CD2 
329  N N   . ALA A 58  ? 0.2831 0.3458 0.3224 0.0171  0.0030  -0.0577 350 ALA A N   
330  C CA  . ALA A 58  ? 0.3083 0.3566 0.3450 0.0212  0.0042  -0.0578 350 ALA A CA  
331  C C   . ALA A 58  ? 0.3038 0.3821 0.3373 0.0189  0.0027  -0.0592 350 ALA A C   
332  O O   . ALA A 58  ? 0.2366 0.3160 0.2706 0.0277  0.0016  -0.0537 350 ALA A O   
333  C CB  . ALA A 58  ? 0.2407 0.2590 0.2734 0.0132  0.0100  -0.0645 350 ALA A CB  
334  N N   . ASP A 59  ? 0.2629 0.3702 0.2924 0.0049  0.0026  -0.0658 351 ASP A N   
335  C CA  . ASP A 59  ? 0.2462 0.3941 0.2723 -0.0004 0.0006  -0.0658 351 ASP A CA  
336  C C   . ASP A 59  ? 0.2248 0.4013 0.2606 0.0192  -0.0039 -0.0478 351 ASP A C   
337  O O   . ASP A 59  ? 0.2694 0.4628 0.3053 0.0248  -0.0053 -0.0413 351 ASP A O   
338  C CB  . ASP A 59  ? 0.2681 0.4488 0.2868 -0.0230 0.0014  -0.0759 351 ASP A CB  
339  C CG  . ASP A 59  ? 0.3206 0.4726 0.3249 -0.0454 0.0098  -0.0955 351 ASP A CG  
340  O OD1 . ASP A 59  ? 0.4762 0.5898 0.4781 -0.0401 0.0149  -0.0995 351 ASP A OD1 
341  O OD2 . ASP A 59  ? 0.3763 0.5434 0.3712 -0.0684 0.0130  -0.1068 351 ASP A OD2 
342  N N   . ARG A 60  ? 0.2073 0.3883 0.2513 0.0306  -0.0043 -0.0390 352 ARG A N   
343  C CA  . ARG A 60  ? 0.2211 0.4205 0.2745 0.0524  -0.0041 -0.0208 352 ARG A CA  
344  C C   . ARG A 60  ? 0.2483 0.4069 0.3017 0.0662  -0.0015 -0.0153 352 ARG A C   
345  O O   . ARG A 60  ? 0.2796 0.4483 0.3366 0.0804  -0.0002 -0.0014 352 ARG A O   
346  C CB  . ARG A 60  ? 0.2176 0.4280 0.2785 0.0612  -0.0018 -0.0149 352 ARG A CB  
347  C CG  . ARG A 60  ? 0.2333 0.5016 0.2967 0.0514  -0.0045 -0.0133 352 ARG A CG  
348  C CD  . ARG A 60  ? 0.2219 0.5026 0.2938 0.0624  -0.0012 -0.0065 352 ARG A CD  
349  N NE  . ARG A 60  ? 0.2371 0.4845 0.3041 0.0498  -0.0009 -0.0207 352 ARG A NE  
350  C CZ  . ARG A 60  ? 0.3350 0.5480 0.4044 0.0606  0.0037  -0.0206 352 ARG A CZ  
351  N NH1 . ARG A 60  ? 0.2107 0.4100 0.2853 0.0832  0.0102  -0.0099 352 ARG A NH1 
352  N NH2 . ARG A 60  ? 0.2718 0.4633 0.3369 0.0469  0.0030  -0.0315 352 ARG A NH2 
353  N N   . GLU A 61  ? 0.2199 0.3353 0.2691 0.0614  -0.0003 -0.0245 353 GLU A N   
354  C CA  . GLU A 61  ? 0.2950 0.3772 0.3421 0.0692  0.0017  -0.0205 353 GLU A CA  
355  C C   . GLU A 61  ? 0.2705 0.3591 0.3140 0.0670  -0.0004 -0.0197 353 GLU A C   
356  O O   . GLU A 61  ? 0.2218 0.3009 0.2650 0.0762  0.0009  -0.0105 353 GLU A O   
357  C CB  . GLU A 61  ? 0.2429 0.2906 0.2868 0.0621  0.0026  -0.0285 353 GLU A CB  
358  C CG  . GLU A 61  ? 0.2442 0.2796 0.2897 0.0655  0.0060  -0.0278 353 GLU A CG  
359  C CD  . GLU A 61  ? 0.3428 0.3519 0.3848 0.0577  0.0063  -0.0322 353 GLU A CD  
360  O OE1 . GLU A 61  ? 0.2588 0.2674 0.3015 0.0484  0.0045  -0.0374 353 GLU A OE1 
361  O OE2 . GLU A 61  ? 0.3498 0.3401 0.3877 0.0599  0.0094  -0.0294 353 GLU A OE2 
362  N N   . LEU A 62  ? 0.2216 0.3245 0.2610 0.0533  -0.0021 -0.0302 354 LEU A N   
363  C CA  . LEU A 62  ? 0.2954 0.4051 0.3300 0.0495  -0.0027 -0.0322 354 LEU A CA  
364  C C   . LEU A 62  ? 0.2964 0.4434 0.3338 0.0572  -0.0050 -0.0185 354 LEU A C   
365  O O   . LEU A 62  ? 0.2554 0.4025 0.2909 0.0608  -0.0055 -0.0132 354 LEU A O   
366  C CB  . LEU A 62  ? 0.2881 0.4024 0.3151 0.0313  -0.0003 -0.0490 354 LEU A CB  
367  C CG  . LEU A 62  ? 0.3840 0.4972 0.4042 0.0259  0.0023  -0.0557 354 LEU A CG  
368  C CD1 . LEU A 62  ? 0.2984 0.3734 0.3201 0.0340  0.0051  -0.0543 354 LEU A CD1 
369  C CD2 . LEU A 62  ? 0.4330 0.5520 0.4428 0.0057  0.0082  -0.0744 354 LEU A CD2 
370  N N   . VAL A 63  ? 0.3096 0.4928 0.3524 0.0606  -0.0062 -0.0105 355 VAL A N   
371  C CA  . VAL A 63  ? 0.2988 0.5228 0.3472 0.0719  -0.0074 0.0085  355 VAL A CA  
372  C C   . VAL A 63  ? 0.2481 0.4420 0.3008 0.0922  -0.0033 0.0245  355 VAL A C   
373  O O   . VAL A 63  ? 0.2790 0.4836 0.3321 0.0989  -0.0033 0.0372  355 VAL A O   
374  C CB  . VAL A 63  ? 0.2272 0.5002 0.2829 0.0743  -0.0083 0.0172  355 VAL A CB  
375  C CG1 . VAL A 63  ? 0.2355 0.5553 0.3000 0.0905  -0.0083 0.0429  355 VAL A CG1 
376  C CG2 . VAL A 63  ? 0.2431 0.5464 0.2907 0.0483  -0.0115 -0.0005 355 VAL A CG2 
377  N N   . HIS A 64  ? 0.3020 0.4569 0.3562 0.0999  0.0015  0.0233  356 HIS A N   
378  C CA  . HIS A 64  ? 0.2938 0.4123 0.3477 0.1143  0.0085  0.0345  356 HIS A CA  
379  C C   . HIS A 64  ? 0.2338 0.3215 0.2792 0.1059  0.0072  0.0280  356 HIS A C   
380  O O   . HIS A 64  ? 0.2903 0.3593 0.3331 0.1135  0.0117  0.0390  356 HIS A O   
381  C CB  . HIS A 64  ? 0.2693 0.3568 0.3240 0.1202  0.0156  0.0312  356 HIS A CB  
382  C CG  . HIS A 64  ? 0.2411 0.3570 0.3056 0.1348  0.0203  0.0426  356 HIS A CG  
383  N ND1 . HIS A 64  ? 0.2701 0.3805 0.3401 0.1572  0.0315  0.0618  356 HIS A ND1 
384  C CD2 . HIS A 64  ? 0.2586 0.4102 0.3286 0.1306  0.0166  0.0387  356 HIS A CD2 
385  C CE1 . HIS A 64  ? 0.2511 0.3960 0.3314 0.1689  0.0345  0.0706  356 HIS A CE1 
386  N NE2 . HIS A 64  ? 0.3332 0.5061 0.4133 0.1516  0.0246  0.0564  356 HIS A NE2 
387  N N   . MET A 65  ? 0.2206 0.3025 0.2614 0.0907  0.0024  0.0115  357 MET A N   
388  C CA  . MET A 65  ? 0.2883 0.3506 0.3230 0.0843  0.0013  0.0074  357 MET A CA  
389  C C   . MET A 65  ? 0.2707 0.3577 0.3043 0.0854  -0.0009 0.0154  357 MET A C   
390  O O   . MET A 65  ? 0.2971 0.3696 0.3264 0.0854  -0.0001 0.0199  357 MET A O   
391  C CB  . MET A 65  ? 0.3336 0.3882 0.3661 0.0720  -0.0006 -0.0087 357 MET A CB  
392  C CG  . MET A 65  ? 0.2778 0.3129 0.3063 0.0683  -0.0002 -0.0108 357 MET A CG  
393  S SD  . MET A 65  ? 0.2910 0.3224 0.3191 0.0595  0.0013  -0.0250 357 MET A SD  
394  C CE  . MET A 65  ? 0.2752 0.2917 0.3066 0.0570  0.0023  -0.0295 357 MET A CE  
395  N N   . ILE A 66  ? 0.2675 0.3966 0.3039 0.0842  -0.0037 0.0178  358 ILE A N   
396  C CA  . ILE A 66  ? 0.2704 0.4315 0.3054 0.0835  -0.0062 0.0262  358 ILE A CA  
397  C C   . ILE A 66  ? 0.2214 0.3777 0.2598 0.0992  -0.0028 0.0492  358 ILE A C   
398  O O   . ILE A 66  ? 0.3004 0.4524 0.3349 0.0989  -0.0029 0.0558  358 ILE A O   
399  C CB  . ILE A 66  ? 0.3777 0.5930 0.4138 0.0754  -0.0096 0.0240  358 ILE A CB  
400  C CG1 . ILE A 66  ? 0.4802 0.6921 0.5087 0.0562  -0.0095 -0.0011 358 ILE A CG1 
401  C CG2 . ILE A 66  ? 0.4894 0.7470 0.5248 0.0754  -0.0121 0.0370  358 ILE A CG2 
402  C CD1 . ILE A 66  ? 0.4008 0.5781 0.4231 0.0511  -0.0069 -0.0136 358 ILE A CD1 
403  N N   . ASN A 67  ? 0.2399 0.3952 0.2853 0.1137  0.0020  0.0624  359 ASN A N   
404  C CA  . ASN A 67  ? 0.2797 0.4205 0.3278 0.1310  0.0098  0.0854  359 ASN A CA  
405  C C   . ASN A 67  ? 0.3536 0.4373 0.3922 0.1276  0.0153  0.0808  359 ASN A C   
406  O O   . ASN A 67  ? 0.3459 0.4174 0.3809 0.1318  0.0195  0.0947  359 ASN A O   
407  C CB  . ASN A 67  ? 0.3988 0.5423 0.4561 0.1492  0.0176  0.0985  359 ASN A CB  
408  C CG  . ASN A 67  ? 0.5548 0.7643 0.6219 0.1517  0.0122  0.1063  359 ASN A CG  
409  O OD1 . ASN A 67  ? 0.5589 0.8131 0.6244 0.1385  0.0034  0.1026  359 ASN A OD1 
410  N ND2 . ASN A 67  ? 0.6230 0.8424 0.6997 0.1673  0.0186  0.1168  359 ASN A ND2 
411  N N   . TRP A 68  ? 0.2739 0.3254 0.3077 0.1185  0.0158  0.0627  360 TRP A N   
412  C CA  . TRP A 68  ? 0.3344 0.3408 0.3578 0.1106  0.0204  0.0574  360 TRP A CA  
413  C C   . TRP A 68  ? 0.2577 0.2723 0.2756 0.1001  0.0146  0.0564  360 TRP A C   
414  O O   . TRP A 68  ? 0.3328 0.3247 0.3428 0.0975  0.0194  0.0638  360 TRP A O   
415  C CB  . TRP A 68  ? 0.2710 0.2567 0.2915 0.1006  0.0197  0.0394  360 TRP A CB  
416  C CG  . TRP A 68  ? 0.3187 0.2765 0.3286 0.0868  0.0208  0.0324  360 TRP A CG  
417  C CD1 . TRP A 68  ? 0.2900 0.2106 0.2890 0.0823  0.0305  0.0343  360 TRP A CD1 
418  C CD2 . TRP A 68  ? 0.2472 0.2155 0.2556 0.0746  0.0134  0.0233  360 TRP A CD2 
419  N NE1 . TRP A 68  ? 0.3427 0.2570 0.3334 0.0654  0.0276  0.0270  360 TRP A NE1 
420  C CE2 . TRP A 68  ? 0.2554 0.2001 0.2534 0.0630  0.0170  0.0221  360 TRP A CE2 
421  C CE3 . TRP A 68  ? 0.2891 0.2838 0.3034 0.0723  0.0061  0.0162  360 TRP A CE3 
422  C CZ2 . TRP A 68  ? 0.2991 0.2540 0.2953 0.0518  0.0121  0.0174  360 TRP A CZ2 
423  C CZ3 . TRP A 68  ? 0.2164 0.2124 0.2287 0.0637  0.0036  0.0108  360 TRP A CZ3 
424  C CH2 . TRP A 68  ? 0.2247 0.2049 0.2295 0.0548  0.0058  0.0131  360 TRP A CH2 
425  N N   . ALA A 69  ? 0.2822 0.3281 0.3030 0.0931  0.0061  0.0466  361 ALA A N   
426  C CA  . ALA A 69  ? 0.2654 0.3223 0.2817 0.0846  0.0021  0.0445  361 ALA A CA  
427  C C   . ALA A 69  ? 0.2783 0.3518 0.2938 0.0900  0.0029  0.0628  361 ALA A C   
428  O O   . ALA A 69  ? 0.3074 0.3701 0.3164 0.0849  0.0039  0.0679  361 ALA A O   
429  C CB  . ALA A 69  ? 0.2846 0.3686 0.3032 0.0775  -0.0030 0.0295  361 ALA A CB  
430  N N   . LYS A 70  ? 0.2937 0.3981 0.3162 0.0999  0.0026  0.0749  362 LYS A N   
431  C CA  . LYS A 70  ? 0.2591 0.3854 0.2827 0.1071  0.0037  0.0970  362 LYS A CA  
432  C C   . LYS A 70  ? 0.3089 0.3916 0.3280 0.1149  0.0139  0.1133  362 LYS A C   
433  O O   . LYS A 70  ? 0.3006 0.3903 0.3179 0.1180  0.0160  0.1315  362 LYS A O   
434  C CB  . LYS A 70  ? 0.3289 0.5035 0.3626 0.1174  0.0021  0.1104  362 LYS A CB  
435  C CG  . LYS A 70  ? 0.3673 0.5904 0.4013 0.1043  -0.0064 0.0945  362 LYS A CG  
436  C CD  . LYS A 70  ? 0.4322 0.7044 0.4752 0.1110  -0.0077 0.1057  362 LYS A CD  
437  C CE  . LYS A 70  ? 0.4381 0.7616 0.4861 0.1186  -0.0088 0.1330  362 LYS A CE  
438  N NZ  . LYS A 70  ? 0.7290 1.1165 0.7731 0.1005  -0.0166 0.1239  362 LYS A NZ  
439  N N   . ARG A 71  ? 0.3893 0.4262 0.4050 0.1165  0.0216  0.1067  363 ARG A N   
440  C CA  . ARG A 71  ? 0.4258 0.4127 0.4330 0.1198  0.0350  0.1175  363 ARG A CA  
441  C C   . ARG A 71  ? 0.4251 0.3786 0.4179 0.0997  0.0356  0.1036  363 ARG A C   
442  O O   . ARG A 71  ? 0.4780 0.3873 0.4591 0.0957  0.0476  0.1088  363 ARG A O   
443  C CB  . ARG A 71  ? 0.4029 0.3604 0.4130 0.1335  0.0469  0.1194  363 ARG A CB  
444  C CG  . ARG A 71  ? 0.5099 0.5049 0.5355 0.1560  0.0485  0.1389  363 ARG A CG  
445  C CD  . ARG A 71  ? 0.6598 0.6239 0.6888 0.1725  0.0633  0.1428  363 ARG A CD  
446  N NE  . ARG A 71  ? 0.8064 0.7074 0.8233 0.1733  0.0823  0.1464  363 ARG A NE  
447  C CZ  . ARG A 71  ? 0.9021 0.7832 0.9128 0.1740  0.0912  0.1618  363 ARG A CZ  
448  N NH1 . ARG A 71  ? 0.8865 0.8091 0.9040 0.1778  0.0830  0.1798  363 ARG A NH1 
449  N NH2 . ARG A 71  ? 0.9292 0.7492 0.9258 0.1689  0.1095  0.1580  363 ARG A NH2 
450  N N   . VAL A 72  ? 0.3194 0.2935 0.3120 0.0865  0.0245  0.0868  364 VAL A N   
451  C CA  . VAL A 72  ? 0.3290 0.2878 0.3103 0.0680  0.0236  0.0780  364 VAL A CA  
452  C C   . VAL A 72  ? 0.3719 0.3442 0.3486 0.0641  0.0224  0.0913  364 VAL A C   
453  O O   . VAL A 72  ? 0.3821 0.3954 0.3663 0.0688  0.0147  0.0952  364 VAL A O   
454  C CB  . VAL A 72  ? 0.3037 0.2841 0.2894 0.0602  0.0142  0.0605  364 VAL A CB  
455  C CG1 . VAL A 72  ? 0.3063 0.2888 0.2837 0.0442  0.0121  0.0574  364 VAL A CG1 
456  C CG2 . VAL A 72  ? 0.2938 0.2562 0.2815 0.0607  0.0164  0.0490  364 VAL A CG2 
457  N N   . PRO A 73  ? 0.4233 0.3631 0.3862 0.0532  0.0308  0.0977  365 PRO A N   
458  C CA  . PRO A 73  ? 0.4014 0.3522 0.3594 0.0494  0.0308  0.1131  365 PRO A CA  
459  C C   . PRO A 73  ? 0.4478 0.4462 0.4099 0.0420  0.0182  0.1070  365 PRO A C   
460  O O   . PRO A 73  ? 0.3533 0.3588 0.3135 0.0307  0.0137  0.0928  365 PRO A O   
461  C CB  . PRO A 73  ? 0.5001 0.4034 0.4389 0.0315  0.0425  0.1139  365 PRO A CB  
462  C CG  . PRO A 73  ? 0.4674 0.3279 0.4023 0.0341  0.0534  0.1051  365 PRO A CG  
463  C CD  . PRO A 73  ? 0.3768 0.2661 0.3261 0.0426  0.0427  0.0912  365 PRO A CD  
464  N N   . GLY A 74  ? 0.3288 0.3625 0.2968 0.0495  0.0137  0.1191  366 GLY A N   
465  C CA  . GLY A 74  ? 0.3513 0.4299 0.3222 0.0437  0.0045  0.1132  366 GLY A CA  
466  C C   . GLY A 74  ? 0.4347 0.5473 0.4165 0.0511  -0.0020 0.0995  366 GLY A C   
467  O O   . GLY A 74  ? 0.3745 0.5248 0.3580 0.0481  -0.0067 0.0948  366 GLY A O   
468  N N   . PHE A 75  ? 0.2701 0.3698 0.2579 0.0591  -0.0010 0.0919  367 PHE A N   
469  C CA  . PHE A 75  ? 0.2836 0.4106 0.2790 0.0619  -0.0055 0.0767  367 PHE A CA  
470  C C   . PHE A 75  ? 0.2591 0.4305 0.2583 0.0659  -0.0087 0.0842  367 PHE A C   
471  O O   . PHE A 75  ? 0.3056 0.5089 0.3049 0.0603  -0.0115 0.0714  367 PHE A O   
472  C CB  . PHE A 75  ? 0.2805 0.3842 0.2803 0.0674  -0.0035 0.0682  367 PHE A CB  
473  C CG  . PHE A 75  ? 0.2533 0.3762 0.2582 0.0665  -0.0064 0.0505  367 PHE A CG  
474  C CD1 . PHE A 75  ? 0.3210 0.4387 0.3253 0.0609  -0.0061 0.0349  367 PHE A CD1 
475  C CD2 . PHE A 75  ? 0.2802 0.4274 0.2900 0.0710  -0.0079 0.0508  367 PHE A CD2 
476  C CE1 . PHE A 75  ? 0.2848 0.4117 0.2920 0.0597  -0.0053 0.0187  367 PHE A CE1 
477  C CE2 . PHE A 75  ? 0.2500 0.4111 0.2611 0.0658  -0.0087 0.0327  367 PHE A CE2 
478  C CZ  . PHE A 75  ? 0.2559 0.4021 0.2651 0.0602  -0.0064 0.0160  367 PHE A CZ  
479  N N   . VAL A 76  ? 0.3119 0.4877 0.3139 0.0752  -0.0066 0.1056  368 VAL A N   
480  C CA  . VAL A 76  ? 0.2597 0.4884 0.2663 0.0784  -0.0102 0.1171  368 VAL A CA  
481  C C   . VAL A 76  ? 0.3960 0.6552 0.3977 0.0711  -0.0129 0.1258  368 VAL A C   
482  O O   . VAL A 76  ? 0.2863 0.5979 0.2902 0.0699  -0.0165 0.1336  368 VAL A O   
483  C CB  . VAL A 76  ? 0.3464 0.5768 0.3604 0.0948  -0.0060 0.1428  368 VAL A CB  
484  C CG1 . VAL A 76  ? 0.4163 0.6258 0.4359 0.1022  -0.0033 0.1338  368 VAL A CG1 
485  C CG2 . VAL A 76  ? 0.3020 0.4932 0.3118 0.1010  0.0022  0.1644  368 VAL A CG2 
486  N N   . ASP A 77  ? 0.2688 0.5023 0.2633 0.0642  -0.0113 0.1250  369 ASP A N   
487  C CA  . ASP A 77  ? 0.3537 0.6197 0.3433 0.0556  -0.0141 0.1304  369 ASP A CA  
488  C C   . ASP A 77  ? 0.3570 0.6570 0.3452 0.0466  -0.0172 0.1064  369 ASP A C   
489  O O   . ASP A 77  ? 0.3178 0.6574 0.3025 0.0396  -0.0192 0.1086  369 ASP A O   
490  C CB  . ASP A 77  ? 0.4536 0.6861 0.4350 0.0485  -0.0111 0.1361  369 ASP A CB  
491  C CG  . ASP A 77  ? 0.4112 0.6047 0.3898 0.0544  -0.0040 0.1594  369 ASP A CG  
492  O OD1 . ASP A 77  ? 0.4445 0.6528 0.4286 0.0660  -0.0021 0.1806  369 ASP A OD1 
493  O OD2 . ASP A 77  ? 0.5287 0.6776 0.4988 0.0470  0.0012  0.1572  369 ASP A OD2 
494  N N   . LEU A 78  ? 0.3206 0.6041 0.3108 0.0464  -0.0158 0.0839  370 LEU A N   
495  C CA  . LEU A 78  ? 0.3193 0.6237 0.3070 0.0393  -0.0141 0.0598  370 LEU A CA  
496  C C   . LEU A 78  ? 0.2739 0.6200 0.2611 0.0345  -0.0152 0.0537  370 LEU A C   
497  O O   . LEU A 78  ? 0.2359 0.5938 0.2276 0.0394  -0.0182 0.0674  370 LEU A O   
498  C CB  . LEU A 78  ? 0.3706 0.6372 0.3605 0.0415  -0.0101 0.0411  370 LEU A CB  
499  C CG  . LEU A 78  ? 0.2748 0.5046 0.2654 0.0440  -0.0094 0.0474  370 LEU A CG  
500  C CD1 . LEU A 78  ? 0.2205 0.4203 0.2151 0.0473  -0.0063 0.0329  370 LEU A CD1 
501  C CD2 . LEU A 78  ? 0.2327 0.4776 0.2196 0.0390  -0.0085 0.0491  370 LEU A CD2 
502  N N   . THR A 79  ? 0.2701 0.6407 0.2509 0.0242  -0.0113 0.0328  371 THR A N   
503  C CA  . THR A 79  ? 0.3357 0.7436 0.3119 0.0134  -0.0102 0.0197  371 THR A CA  
504  C C   . THR A 79  ? 0.2722 0.6516 0.2512 0.0150  -0.0080 0.0068  371 THR A C   
505  O O   . THR A 79  ? 0.2431 0.5744 0.2257 0.0225  -0.0048 -0.0001 371 THR A O   
506  C CB  . THR A 79  ? 0.4134 0.8428 0.3788 -0.0002 -0.0023 -0.0049 371 THR A CB  
507  O OG1 . THR A 79  ? 0.3134 0.6974 0.2778 0.0027  0.0076  -0.0276 371 THR A OG1 
508  C CG2 . THR A 79  ? 0.2917 0.7434 0.2551 -0.0005 -0.0037 0.0065  371 THR A CG2 
509  N N   . LEU A 80  ? 0.2412 0.6558 0.2184 0.0066  -0.0100 0.0050  372 LEU A N   
510  C CA  . LEU A 80  ? 0.4091 0.7994 0.3886 0.0067  -0.0081 -0.0063 372 LEU A CA  
511  C C   . LEU A 80  ? 0.2746 0.6333 0.2457 -0.0027 0.0027  -0.0381 372 LEU A C   
512  O O   . LEU A 80  ? 0.2751 0.5944 0.2495 0.0017  0.0056  -0.0460 372 LEU A O   
513  C CB  . LEU A 80  ? 0.5836 1.0253 0.5630 -0.0019 -0.0124 -0.0004 372 LEU A CB  
514  C CG  . LEU A 80  ? 0.5767 1.0754 0.5626 0.0033  -0.0204 0.0309  372 LEU A CG  
515  C CD1 . LEU A 80  ? 0.4456 1.0016 0.4297 -0.0101 -0.0228 0.0294  372 LEU A CD1 
516  C CD2 . LEU A 80  ? 0.5289 0.9971 0.5284 0.0280  -0.0236 0.0611  372 LEU A CD2 
517  N N   . HIS A 81  ? 0.2992 0.6737 0.2592 -0.0150 0.0106  -0.0560 373 HIS A N   
518  C CA  . HIS A 81  ? 0.3358 0.6720 0.2881 -0.0198 0.0253  -0.0843 373 HIS A CA  
519  C C   . HIS A 81  ? 0.2700 0.5540 0.2328 -0.0003 0.0274  -0.0781 373 HIS A C   
520  O O   . HIS A 81  ? 0.3098 0.5531 0.2738 0.0028  0.0356  -0.0904 373 HIS A O   
521  C CB  . HIS A 81  ? 0.3322 0.6922 0.2708 -0.0335 0.0360  -0.1031 373 HIS A CB  
522  C CG  . HIS A 81  ? 0.5401 0.8543 0.4724 -0.0325 0.0552  -0.1286 373 HIS A CG  
523  N ND1 . HIS A 81  ? 0.7010 0.9841 0.6419 -0.0136 0.0603  -0.1229 373 HIS A ND1 
524  C CD2 . HIS A 81  ? 0.6846 0.9786 0.6026 -0.0477 0.0725  -0.1585 373 HIS A CD2 
525  C CE1 . HIS A 81  ? 0.7226 0.9692 0.6572 -0.0131 0.0802  -0.1456 373 HIS A CE1 
526  N NE2 . HIS A 81  ? 0.7500 0.9974 0.6697 -0.0341 0.0890  -0.1685 373 HIS A NE2 
527  N N   . ASP A 82  ? 0.3057 0.5933 0.2758 0.0112  0.0204  -0.0579 374 ASP A N   
528  C CA  . ASP A 82  ? 0.2634 0.5119 0.2426 0.0261  0.0208  -0.0496 374 ASP A CA  
529  C C   . ASP A 82  ? 0.2532 0.4771 0.2406 0.0332  0.0132  -0.0372 374 ASP A C   
530  O O   . ASP A 82  ? 0.2443 0.4338 0.2373 0.0411  0.0159  -0.0377 374 ASP A O   
531  C CB  . ASP A 82  ? 0.3586 0.6223 0.3400 0.0310  0.0165  -0.0334 374 ASP A CB  
532  C CG  . ASP A 82  ? 0.4246 0.7061 0.3998 0.0276  0.0266  -0.0467 374 ASP A CG  
533  O OD1 . ASP A 82  ? 0.4240 0.6983 0.3925 0.0224  0.0393  -0.0698 374 ASP A OD1 
534  O OD2 . ASP A 82  ? 0.3861 0.6872 0.3619 0.0294  0.0235  -0.0347 374 ASP A OD2 
535  N N   . GLN A 83  ? 0.2355 0.4793 0.2240 0.0314  0.0047  -0.0249 375 GLN A N   
536  C CA  . GLN A 83  ? 0.2791 0.4999 0.2745 0.0382  0.0003  -0.0163 375 GLN A CA  
537  C C   . GLN A 83  ? 0.2264 0.4284 0.2208 0.0336  0.0059  -0.0350 375 GLN A C   
538  O O   . GLN A 83  ? 0.2312 0.4006 0.2310 0.0401  0.0060  -0.0338 375 GLN A O   
539  C CB  . GLN A 83  ? 0.2205 0.4706 0.2186 0.0402  -0.0069 0.0024  375 GLN A CB  
540  C CG  . GLN A 83  ? 0.2295 0.4852 0.2294 0.0472  -0.0109 0.0257  375 GLN A CG  
541  C CD  . GLN A 83  ? 0.3025 0.5887 0.3067 0.0527  -0.0150 0.0476  375 GLN A CD  
542  O OE1 . GLN A 83  ? 0.2959 0.5794 0.3056 0.0586  -0.0154 0.0521  375 GLN A OE1 
543  N NE2 . GLN A 83  ? 0.3058 0.6244 0.3085 0.0520  -0.0173 0.0636  375 GLN A NE2 
544  N N   . VAL A 84  ? 0.2776 0.5000 0.2633 0.0201  0.0116  -0.0530 376 VAL A N   
545  C CA  . VAL A 84  ? 0.3246 0.5259 0.3063 0.0122  0.0192  -0.0722 376 VAL A CA  
546  C C   . VAL A 84  ? 0.3138 0.4702 0.2974 0.0197  0.0298  -0.0816 376 VAL A C   
547  O O   . VAL A 84  ? 0.2996 0.4248 0.2874 0.0233  0.0324  -0.0839 376 VAL A O   
548  C CB  . VAL A 84  ? 0.3861 0.6199 0.3540 -0.0091 0.0251  -0.0914 376 VAL A CB  
549  C CG1 . VAL A 84  ? 0.3411 0.5430 0.3012 -0.0201 0.0374  -0.1146 376 VAL A CG1 
550  C CG2 . VAL A 84  ? 0.2607 0.5466 0.2297 -0.0156 0.0141  -0.0781 376 VAL A CG2 
551  N N   . HIS A 85  ? 0.2909 0.4470 0.2722 0.0231  0.0367  -0.0850 377 HIS A N   
552  C CA  . HIS A 85  ? 0.3017 0.4219 0.2869 0.0336  0.0487  -0.0900 377 HIS A CA  
553  C C   . HIS A 85  ? 0.2801 0.3813 0.2781 0.0476  0.0412  -0.0712 377 HIS A C   
554  O O   . HIS A 85  ? 0.3220 0.3936 0.3251 0.0542  0.0479  -0.0726 377 HIS A O   
555  C CB  . HIS A 85  ? 0.3079 0.4394 0.2900 0.0369  0.0575  -0.0941 377 HIS A CB  
556  C CG  . HIS A 85  ? 0.4475 0.5490 0.4363 0.0520  0.0712  -0.0944 377 HIS A CG  
557  N ND1 . HIS A 85  ? 0.4704 0.5382 0.4549 0.0526  0.0905  -0.1117 377 HIS A ND1 
558  C CD2 . HIS A 85  ? 0.4002 0.5026 0.4000 0.0672  0.0694  -0.0773 377 HIS A CD2 
559  C CE1 . HIS A 85  ? 0.5291 0.5792 0.5239 0.0713  0.1005  -0.1027 377 HIS A CE1 
560  N NE2 . HIS A 85  ? 0.4353 0.5104 0.4398 0.0796  0.0870  -0.0818 377 HIS A NE2 
561  N N   . LEU A 86  ? 0.3095 0.4274 0.3113 0.0506  0.0285  -0.0533 378 LEU A N   
562  C CA  . LEU A 86  ? 0.2354 0.3370 0.2454 0.0586  0.0225  -0.0381 378 LEU A CA  
563  C C   . LEU A 86  ? 0.2300 0.3118 0.2429 0.0578  0.0201  -0.0394 378 LEU A C   
564  O O   . LEU A 86  ? 0.2560 0.3177 0.2747 0.0629  0.0216  -0.0354 378 LEU A O   
565  C CB  . LEU A 86  ? 0.2138 0.3311 0.2233 0.0581  0.0125  -0.0213 378 LEU A CB  
566  C CG  . LEU A 86  ? 0.2768 0.4120 0.2851 0.0592  0.0134  -0.0148 378 LEU A CG  
567  C CD1 . LEU A 86  ? 0.2104 0.3537 0.2162 0.0561  0.0048  0.0022  378 LEU A CD1 
568  C CD2 . LEU A 86  ? 0.2151 0.3410 0.2295 0.0663  0.0195  -0.0128 378 LEU A CD2 
569  N N   . LEU A 87  ? 0.2492 0.3422 0.2584 0.0510  0.0163  -0.0436 379 LEU A N   
570  C CA  . LEU A 87  ? 0.2972 0.3763 0.3092 0.0500  0.0140  -0.0447 379 LEU A CA  
571  C C   . LEU A 87  ? 0.2297 0.2887 0.2400 0.0458  0.0239  -0.0603 379 LEU A C   
572  O O   . LEU A 87  ? 0.2908 0.3299 0.3056 0.0477  0.0240  -0.0590 379 LEU A O   
573  C CB  . LEU A 87  ? 0.2758 0.3808 0.2861 0.0456  0.0075  -0.0410 379 LEU A CB  
574  C CG  . LEU A 87  ? 0.3519 0.4568 0.3667 0.0541  0.0005  -0.0221 379 LEU A CG  
575  C CD1 . LEU A 87  ? 0.3014 0.4404 0.3162 0.0544  -0.0037 -0.0127 379 LEU A CD1 
576  C CD2 . LEU A 87  ? 0.3906 0.4697 0.4100 0.0580  0.0001  -0.0203 379 LEU A CD2 
577  N N   . GLU A 88  ? 0.2766 0.3383 0.2793 0.0391  0.0339  -0.0754 380 GLU A N   
578  C CA  . GLU A 88  ? 0.3588 0.3916 0.3580 0.0353  0.0478  -0.0905 380 GLU A CA  
579  C C   . GLU A 88  ? 0.4257 0.4306 0.4347 0.0503  0.0539  -0.0811 380 GLU A C   
580  O O   . GLU A 88  ? 0.3913 0.3697 0.4027 0.0515  0.0609  -0.0832 380 GLU A O   
581  C CB  . GLU A 88  ? 0.3710 0.4076 0.3575 0.0248  0.0611  -0.1099 380 GLU A CB  
582  C CG  . GLU A 88  ? 0.5166 0.5545 0.4897 0.0036  0.0674  -0.1299 380 GLU A CG  
583  C CD  . GLU A 88  ? 0.7911 0.8268 0.7482 -0.0100 0.0844  -0.1529 380 GLU A CD  
584  O OE1 . GLU A 88  ? 0.8230 0.8987 0.7723 -0.0208 0.0798  -0.1571 380 GLU A OE1 
585  O OE2 . GLU A 88  ? 0.8880 0.8814 0.8398 -0.0099 0.1041  -0.1664 380 GLU A OE2 
586  N N   . SER A 89  ? 0.3031 0.3184 0.3180 0.0611  0.0514  -0.0687 381 SER A N   
587  C CA  . SER A 89  ? 0.2943 0.2959 0.3195 0.0752  0.0571  -0.0566 381 SER A CA  
588  C C   . SER A 89  ? 0.2455 0.2468 0.2783 0.0773  0.0459  -0.0414 381 SER A C   
589  O O   . SER A 89  ? 0.3492 0.3399 0.3903 0.0856  0.0506  -0.0319 381 SER A O   
590  C CB  . SER A 89  ? 0.2588 0.2797 0.2866 0.0835  0.0589  -0.0487 381 SER A CB  
591  O OG  . SER A 89  ? 0.5244 0.5461 0.5443 0.0814  0.0712  -0.0642 381 SER A OG  
592  N N   . ALA A 90  ? 0.2250 0.2385 0.2550 0.0702  0.0327  -0.0381 382 ALA A N   
593  C CA  . ALA A 90  ? 0.2512 0.2649 0.2855 0.0704  0.0240  -0.0254 382 ALA A CA  
594  C C   . ALA A 90  ? 0.2456 0.2494 0.2791 0.0650  0.0196  -0.0289 382 ALA A C   
595  O O   . ALA A 90  ? 0.2347 0.2353 0.2707 0.0642  0.0150  -0.0210 382 ALA A O   
596  C CB  . ALA A 90  ? 0.2134 0.2433 0.2442 0.0679  0.0157  -0.0165 382 ALA A CB  
597  N N   . TRP A 91  ? 0.2327 0.2352 0.2620 0.0595  0.0216  -0.0410 383 TRP A N   
598  C CA  . TRP A 91  ? 0.2369 0.2392 0.2658 0.0547  0.0164  -0.0426 383 TRP A CA  
599  C C   . TRP A 91  ? 0.2438 0.2293 0.2778 0.0553  0.0179  -0.0396 383 TRP A C   
600  O O   . TRP A 91  ? 0.2472 0.2331 0.2826 0.0544  0.0124  -0.0349 383 TRP A O   
601  C CB  . TRP A 91  ? 0.2926 0.3049 0.3155 0.0456  0.0187  -0.0557 383 TRP A CB  
602  C CG  . TRP A 91  ? 0.2363 0.2295 0.2558 0.0396  0.0298  -0.0685 383 TRP A CG  
603  C CD1 . TRP A 91  ? 0.2552 0.2390 0.2696 0.0382  0.0412  -0.0783 383 TRP A CD1 
604  C CD2 . TRP A 91  ? 0.2531 0.2302 0.2729 0.0338  0.0333  -0.0731 383 TRP A CD2 
605  N NE1 . TRP A 91  ? 0.3717 0.3291 0.3823 0.0322  0.0533  -0.0889 383 TRP A NE1 
606  C CE2 . TRP A 91  ? 0.3183 0.2722 0.3323 0.0287  0.0478  -0.0852 383 TRP A CE2 
607  C CE3 . TRP A 91  ? 0.3589 0.3378 0.3827 0.0323  0.0269  -0.0682 383 TRP A CE3 
608  C CZ2 . TRP A 91  ? 0.3610 0.2915 0.3726 0.0212  0.0559  -0.0914 383 TRP A CZ2 
609  C CZ3 . TRP A 91  ? 0.3801 0.3420 0.4024 0.0246  0.0330  -0.0743 383 TRP A CZ3 
610  C CH2 . TRP A 91  ? 0.3005 0.2375 0.3166 0.0187  0.0472  -0.0852 383 TRP A CH2 
611  N N   . LEU A 92  ? 0.2224 0.1925 0.2590 0.0576  0.0270  -0.0415 384 LEU A N   
612  C CA  . LEU A 92  ? 0.2991 0.2571 0.3415 0.0586  0.0286  -0.0354 384 LEU A CA  
613  C C   . LEU A 92  ? 0.2657 0.2336 0.3134 0.0626  0.0231  -0.0204 384 LEU A C   
614  O O   . LEU A 92  ? 0.2089 0.1779 0.2582 0.0588  0.0189  -0.0161 384 LEU A O   
615  C CB  . LEU A 92  ? 0.2454 0.1820 0.2899 0.0622  0.0425  -0.0376 384 LEU A CB  
616  C CG  . LEU A 92  ? 0.3036 0.2282 0.3540 0.0624  0.0450  -0.0299 384 LEU A CG  
617  C CD1 . LEU A 92  ? 0.2428 0.1700 0.2887 0.0504  0.0380  -0.0379 384 LEU A CD1 
618  C CD2 . LEU A 92  ? 0.2804 0.1770 0.3326 0.0677  0.0621  -0.0302 384 LEU A CD2 
619  N N   . GLU A 93  ? 0.2888 0.2675 0.3377 0.0678  0.0234  -0.0133 385 GLU A N   
620  C CA  . GLU A 93  ? 0.2457 0.2398 0.2965 0.0664  0.0181  -0.0003 385 GLU A CA  
621  C C   . GLU A 93  ? 0.2457 0.2403 0.2890 0.0572  0.0103  -0.0032 385 GLU A C   
622  O O   . GLU A 93  ? 0.2168 0.2155 0.2589 0.0506  0.0077  0.0020  385 GLU A O   
623  C CB  . GLU A 93  ? 0.2640 0.2738 0.3156 0.0711  0.0195  0.0066  385 GLU A CB  
624  C CG  . GLU A 93  ? 0.3270 0.3426 0.3887 0.0832  0.0290  0.0168  385 GLU A CG  
625  C CD  . GLU A 93  ? 0.3318 0.3666 0.3946 0.0889  0.0311  0.0225  385 GLU A CD  
626  O OE1 . GLU A 93  ? 0.4251 0.4519 0.4847 0.0930  0.0365  0.0121  385 GLU A OE1 
627  O OE2 . GLU A 93  ? 0.3339 0.3957 0.3997 0.0874  0.0276  0.0371  385 GLU A OE2 
628  N N   . ILE A 94  ? 0.2304 0.2218 0.2683 0.0568  0.0082  -0.0106 386 ILE A N   
629  C CA  . ILE A 94  ? 0.2272 0.2146 0.2589 0.0523  0.0045  -0.0111 386 ILE A CA  
630  C C   . ILE A 94  ? 0.2238 0.2037 0.2567 0.0500  0.0044  -0.0153 386 ILE A C   
631  O O   . ILE A 94  ? 0.2358 0.2102 0.2644 0.0451  0.0043  -0.0142 386 ILE A O   
632  C CB  . ILE A 94  ? 0.2323 0.2234 0.2605 0.0558  0.0034  -0.0132 386 ILE A CB  
633  C CG1 . ILE A 94  ? 0.3012 0.3004 0.3263 0.0557  0.0030  -0.0073 386 ILE A CG1 
634  C CG2 . ILE A 94  ? 0.1954 0.1792 0.2199 0.0564  0.0031  -0.0119 386 ILE A CG2 
635  C CD1 . ILE A 94  ? 0.4357 0.4469 0.4598 0.0594  0.0025  -0.0094 386 ILE A CD1 
636  N N   . LEU A 95  ? 0.1878 0.1668 0.2249 0.0516  0.0058  -0.0213 387 LEU A N   
637  C CA  . LEU A 95  ? 0.2736 0.2493 0.3122 0.0484  0.0056  -0.0246 387 LEU A CA  
638  C C   . LEU A 95  ? 0.2996 0.2743 0.3401 0.0440  0.0059  -0.0186 387 LEU A C   
639  O O   . LEU A 95  ? 0.2453 0.2195 0.2835 0.0392  0.0051  -0.0196 387 LEU A O   
640  C CB  . LEU A 95  ? 0.2643 0.2393 0.3050 0.0469  0.0082  -0.0322 387 LEU A CB  
641  C CG  . LEU A 95  ? 0.2948 0.2818 0.3325 0.0461  0.0070  -0.0392 387 LEU A CG  
642  C CD1 . LEU A 95  ? 0.2718 0.2581 0.3080 0.0380  0.0109  -0.0490 387 LEU A CD1 
643  C CD2 . LEU A 95  ? 0.2434 0.2400 0.2812 0.0492  0.0038  -0.0361 387 LEU A CD2 
644  N N   . MET A 96  ? 0.2359 0.2142 0.2810 0.0459  0.0080  -0.0110 388 MET A N   
645  C CA  . MET A 96  ? 0.2183 0.2058 0.2669 0.0417  0.0080  -0.0013 388 MET A CA  
646  C C   . MET A 96  ? 0.2746 0.2726 0.3158 0.0322  0.0050  0.0016  388 MET A C   
647  O O   . MET A 96  ? 0.2823 0.2868 0.3206 0.0229  0.0043  0.0025  388 MET A O   
648  C CB  . MET A 96  ? 0.2744 0.2678 0.3318 0.0497  0.0129  0.0103  388 MET A CB  
649  C CG  . MET A 96  ? 0.2932 0.2676 0.3549 0.0568  0.0204  0.0056  388 MET A CG  
650  S SD  . MET A 96  ? 0.2497 0.2242 0.3225 0.0708  0.0316  0.0215  388 MET A SD  
651  C CE  . MET A 96  ? 0.2387 0.1877 0.3150 0.0714  0.0408  0.0209  388 MET A CE  
652  N N   . ILE A 97  ? 0.1992 0.1988 0.2352 0.0319  0.0044  0.0022  389 ILE A N   
653  C CA  . ILE A 97  ? 0.2430 0.2484 0.2683 0.0187  0.0038  0.0033  389 ILE A CA  
654  C C   . ILE A 97  ? 0.2410 0.2264 0.2566 0.0134  0.0062  -0.0074 389 ILE A C   
655  O O   . ILE A 97  ? 0.2971 0.2821 0.3024 -0.0008 0.0089  -0.0102 389 ILE A O   
656  C CB  . ILE A 97  ? 0.2347 0.2458 0.2558 0.0181  0.0034  0.0074  389 ILE A CB  
657  C CG1 . ILE A 97  ? 0.2099 0.2317 0.2185 -0.0010 0.0039  0.0096  389 ILE A CG1 
658  C CG2 . ILE A 97  ? 0.2079 0.1996 0.2254 0.0253  0.0041  0.0005  389 ILE A CG2 
659  C CD1 . ILE A 97  ? 0.2177 0.2484 0.2207 -0.0053 0.0035  0.0144  389 ILE A CD1 
660  N N   . GLY A 98  ? 0.2350 0.2059 0.2532 0.0241  0.0070  -0.0134 390 GLY A N   
661  C CA  . GLY A 98  ? 0.2103 0.1660 0.2229 0.0239  0.0112  -0.0207 390 GLY A CA  
662  C C   . GLY A 98  ? 0.3006 0.2616 0.3150 0.0182  0.0116  -0.0239 390 GLY A C   
663  O O   . GLY A 98  ? 0.2649 0.2174 0.2705 0.0102  0.0169  -0.0297 390 GLY A O   
664  N N   . LEU A 99  ? 0.2622 0.2354 0.2869 0.0213  0.0076  -0.0206 391 LEU A N   
665  C CA  . LEU A 99  ? 0.2739 0.2556 0.3010 0.0149  0.0074  -0.0208 391 LEU A CA  
666  C C   . LEU A 99  ? 0.2648 0.2605 0.2858 0.0003  0.0078  -0.0164 391 LEU A C   
667  O O   . LEU A 99  ? 0.3306 0.3294 0.3452 -0.0102 0.0104  -0.0215 391 LEU A O   
668  C CB  . LEU A 99  ? 0.2166 0.2039 0.2549 0.0205  0.0053  -0.0157 391 LEU A CB  
669  C CG  . LEU A 99  ? 0.2297 0.2275 0.2721 0.0141  0.0051  -0.0116 391 LEU A CG  
670  C CD1 . LEU A 99  ? 0.2307 0.2268 0.2694 0.0106  0.0060  -0.0213 391 LEU A CD1 
671  C CD2 . LEU A 99  ? 0.1996 0.1942 0.2515 0.0200  0.0064  -0.0051 391 LEU A CD2 
672  N N   . VAL A 100 ? 0.2452 0.2545 0.2677 -0.0018 0.0057  -0.0066 392 VAL A N   
673  C CA  . VAL A 100 ? 0.2455 0.2799 0.2622 -0.0182 0.0053  0.0000  392 VAL A CA  
674  C C   . VAL A 100 ? 0.2283 0.2509 0.2262 -0.0348 0.0105  -0.0123 392 VAL A C   
675  O O   . VAL A 100 ? 0.3132 0.3505 0.3015 -0.0534 0.0128  -0.0152 392 VAL A O   
676  C CB  . VAL A 100 ? 0.2683 0.3249 0.2917 -0.0148 0.0027  0.0149  392 VAL A CB  
677  C CG1 . VAL A 100 ? 0.2887 0.3784 0.3033 -0.0352 0.0020  0.0216  392 VAL A CG1 
678  C CG2 . VAL A 100 ? 0.2177 0.2837 0.2585 0.0004  0.0021  0.0283  392 VAL A CG2 
679  N N   . TRP A 101 ? 0.3146 0.3094 0.3059 -0.0291 0.0143  -0.0197 393 TRP A N   
680  C CA  . TRP A 101 ? 0.2819 0.2540 0.2542 -0.0428 0.0236  -0.0317 393 TRP A CA  
681  C C   . TRP A 101 ? 0.3150 0.2712 0.2829 -0.0433 0.0307  -0.0433 393 TRP A C   
682  O O   . TRP A 101 ? 0.3549 0.3054 0.3064 -0.0623 0.0392  -0.0534 393 TRP A O   
683  C CB  . TRP A 101 ? 0.2907 0.2357 0.2595 -0.0327 0.0272  -0.0327 393 TRP A CB  
684  C CG  . TRP A 101 ? 0.3190 0.2285 0.2689 -0.0415 0.0407  -0.0437 393 TRP A CG  
685  C CD1 . TRP A 101 ? 0.3328 0.2104 0.2822 -0.0263 0.0499  -0.0483 393 TRP A CD1 
686  C CD2 . TRP A 101 ? 0.3261 0.2275 0.2543 -0.0679 0.0491  -0.0506 393 TRP A CD2 
687  N NE1 . TRP A 101 ? 0.3946 0.2375 0.3236 -0.0387 0.0655  -0.0573 393 TRP A NE1 
688  C CE2 . TRP A 101 ? 0.4126 0.2673 0.3264 -0.0667 0.0655  -0.0610 393 TRP A CE2 
689  C CE3 . TRP A 101 ? 0.3783 0.3099 0.2970 -0.0932 0.0456  -0.0484 393 TRP A CE3 
690  C CZ2 . TRP A 101 ? 0.4032 0.2319 0.2910 -0.0923 0.0800  -0.0722 393 TRP A CZ2 
691  C CZ3 . TRP A 101 ? 0.4924 0.4070 0.3852 -0.1213 0.0575  -0.0596 393 TRP A CZ3 
692  C CH2 . TRP A 101 ? 0.4585 0.3178 0.3347 -0.1218 0.0754  -0.0729 393 TRP A CH2 
693  N N   . ARG A 102 ? 0.3091 0.2605 0.2902 -0.0244 0.0284  -0.0427 394 ARG A N   
694  C CA  . ARG A 102 ? 0.3221 0.2647 0.3012 -0.0227 0.0350  -0.0520 394 ARG A CA  
695  C C   . ARG A 102 ? 0.2656 0.2327 0.2423 -0.0396 0.0332  -0.0535 394 ARG A C   
696  O O   . ARG A 102 ? 0.3203 0.2804 0.2867 -0.0484 0.0421  -0.0648 394 ARG A O   
697  C CB  . ARG A 102 ? 0.3320 0.2758 0.3264 -0.0019 0.0310  -0.0490 394 ARG A CB  
698  C CG  . ARG A 102 ? 0.3900 0.3168 0.3869 0.0150  0.0337  -0.0467 394 ARG A CG  
699  C CD  . ARG A 102 ? 0.4182 0.3534 0.4268 0.0310  0.0325  -0.0456 394 ARG A CD  
700  N NE  . ARG A 102 ? 0.3009 0.2577 0.3209 0.0314  0.0219  -0.0415 394 ARG A NE  
701  C CZ  . ARG A 102 ? 0.2433 0.2048 0.2685 0.0359  0.0160  -0.0365 394 ARG A CZ  
702  N NH1 . ARG A 102 ? 0.2373 0.1896 0.2591 0.0405  0.0172  -0.0333 394 ARG A NH1 
703  N NH2 . ARG A 102 ? 0.1947 0.1686 0.2276 0.0349  0.0105  -0.0352 394 ARG A NH2 
704  N N   . SER A 103 ? 0.3185 0.2907 0.2868 0.0409  0.0102  -0.0242 395 SER A N   
705  C CA  . SER A 103 ? 0.3112 0.2894 0.2660 0.0471  0.0121  -0.0326 395 SER A CA  
706  C C   . SER A 103 ? 0.4105 0.3890 0.3513 0.0386  0.0068  -0.0468 395 SER A C   
707  O O   . SER A 103 ? 0.4012 0.3938 0.3278 0.0441  0.0063  -0.0523 395 SER A O   
708  C CB  . SER A 103 ? 0.2318 0.2302 0.1903 0.0509  0.0098  -0.0257 395 SER A CB  
709  O OG  . SER A 103 ? 0.2652 0.2676 0.2400 0.0530  0.0126  -0.0175 395 SER A OG  
710  N N   . MET A 104 ? 0.3843 0.3503 0.3283 0.0231  0.0022  -0.0512 396 MET A N   
711  C CA  . MET A 104 ? 0.3735 0.3465 0.3077 0.0087  -0.0041 -0.0676 396 MET A CA  
712  C C   . MET A 104 ? 0.3784 0.3387 0.2966 0.0165  -0.0015 -0.0873 396 MET A C   
713  O O   . MET A 104 ? 0.4466 0.4330 0.3518 0.0135  -0.0060 -0.1016 396 MET A O   
714  C CB  . MET A 104 ? 0.5419 0.4970 0.4842 -0.0158 -0.0084 -0.0659 396 MET A CB  
715  C CG  . MET A 104 ? 0.6262 0.6079 0.5657 -0.0395 -0.0159 -0.0801 396 MET A CG  
716  S SD  . MET A 104 ? 0.5186 0.4893 0.4701 -0.0769 -0.0196 -0.0677 396 MET A SD  
717  C CE  . MET A 104 ? 0.4412 0.3685 0.3850 -0.1009 -0.0247 -0.0944 396 MET A CE  
718  N N   . GLU A 105 ? 0.4293 0.3585 0.3483 0.0290  0.0052  -0.0905 397 GLU A N   
719  C CA  . GLU A 105 ? 0.3902 0.3131 0.2950 0.0393  0.0085  -0.1148 397 GLU A CA  
720  C C   . GLU A 105 ? 0.4186 0.3761 0.3126 0.0577  0.0172  -0.1101 397 GLU A C   
721  O O   . GLU A 105 ? 0.4511 0.4145 0.3343 0.0700  0.0230  -0.1287 397 GLU A O   
722  C CB  . GLU A 105 ? 0.4377 0.3104 0.3505 0.0472  0.0102  -0.1251 397 GLU A CB  
723  C CG  . GLU A 105 ? 0.5693 0.3963 0.4864 0.0251  0.0008  -0.1351 397 GLU A CG  
724  C CD  . GLU A 105 ? 0.5700 0.3743 0.5026 0.0128  -0.0024 -0.1049 397 GLU A CD  
725  O OE1 . GLU A 105 ? 0.6810 0.5138 0.6209 0.0212  0.0017  -0.0811 397 GLU A OE1 
726  O OE2 . GLU A 105 ? 0.9463 0.7054 0.8830 -0.0072 -0.0092 -0.1048 397 GLU A OE2 
727  N N   . HIS A 106 ? 0.3899 0.3707 0.2865 0.0588  0.0180  -0.0865 398 HIS A N   
728  C CA  . HIS A 106 ? 0.3328 0.3396 0.2203 0.0698  0.0261  -0.0740 398 HIS A CA  
729  C C   . HIS A 106 ? 0.3210 0.3496 0.1984 0.0671  0.0192  -0.0593 398 HIS A C   
730  O O   . HIS A 106 ? 0.3449 0.3692 0.2337 0.0670  0.0170  -0.0402 398 HIS A O   
731  C CB  . HIS A 106 ? 0.3149 0.3152 0.2208 0.0750  0.0339  -0.0577 398 HIS A CB  
732  C CG  . HIS A 106 ? 0.5322 0.5110 0.4509 0.0830  0.0372  -0.0691 398 HIS A CG  
733  N ND1 . HIS A 106 ? 0.4421 0.4326 0.3584 0.0984  0.0464  -0.0823 398 HIS A ND1 
734  C CD2 . HIS A 106 ? 0.4816 0.4292 0.4146 0.0801  0.0316  -0.0682 398 HIS A CD2 
735  C CE1 . HIS A 106 ? 0.5799 0.5418 0.5102 0.1087  0.0449  -0.0904 398 HIS A CE1 
736  N NE2 . HIS A 106 ? 0.5649 0.4973 0.5042 0.0965  0.0357  -0.0790 398 HIS A NE2 
737  N N   . PRO A 107 ? 0.3683 0.4215 0.2247 0.0675  0.0140  -0.0700 399 PRO A N   
738  C CA  . PRO A 107 ? 0.4007 0.4760 0.2478 0.0704  0.0041  -0.0556 399 PRO A CA  
739  C C   . PRO A 107 ? 0.4084 0.4831 0.2499 0.0785  0.0081  -0.0252 399 PRO A C   
740  O O   . PRO A 107 ? 0.3902 0.4727 0.2214 0.0797  0.0193  -0.0174 399 PRO A O   
741  C CB  . PRO A 107 ? 0.4461 0.5569 0.2689 0.0707  -0.0010 -0.0746 399 PRO A CB  
742  C CG  . PRO A 107 ? 0.4094 0.5040 0.2375 0.0615  0.0023  -0.1066 399 PRO A CG  
743  C CD  . PRO A 107 ? 0.4681 0.5314 0.3099 0.0666  0.0145  -0.0998 399 PRO A CD  
744  N N   . GLY A 108 ? 0.4304 0.4967 0.2799 0.0832  -0.0013 -0.0091 400 GLY A N   
745  C CA  . GLY A 108 ? 0.4288 0.4795 0.2753 0.0884  -0.0005 0.0203  400 GLY A CA  
746  C C   . GLY A 108 ? 0.5170 0.5428 0.3827 0.0796  0.0105  0.0285  400 GLY A C   
747  O O   . GLY A 108 ? 0.5442 0.5550 0.4079 0.0769  0.0131  0.0526  400 GLY A O   
748  N N   . LYS A 109 ? 0.3815 0.4030 0.2658 0.0737  0.0161  0.0107  401 LYS A N   
749  C CA  . LYS A 109 ? 0.3194 0.3299 0.2229 0.0670  0.0255  0.0159  401 LYS A CA  
750  C C   . LYS A 109 ? 0.3407 0.3419 0.2679 0.0652  0.0214  0.0033  401 LYS A C   
751  O O   . LYS A 109 ? 0.3627 0.3669 0.2899 0.0655  0.0155  -0.0103 401 LYS A O   
752  C CB  . LYS A 109 ? 0.3323 0.3622 0.2302 0.0661  0.0395  0.0103  401 LYS A CB  
753  C CG  . LYS A 109 ? 0.5738 0.6262 0.4497 0.0637  0.0473  0.0274  401 LYS A CG  
754  C CD  . LYS A 109 ? 0.4649 0.5515 0.3333 0.0679  0.0604  0.0122  401 LYS A CD  
755  C CE  . LYS A 109 ? 0.5892 0.7114 0.4412 0.0602  0.0723  0.0338  401 LYS A CE  
756  N NZ  . LYS A 109 ? 0.6207 0.7564 0.4400 0.0615  0.0668  0.0483  401 LYS A NZ  
757  N N   . LEU A 110 ? 0.2899 0.2850 0.2369 0.0605  0.0245  0.0088  402 LEU A N   
758  C CA  . LEU A 110 ? 0.3161 0.3127 0.2838 0.0587  0.0213  0.0001  402 LEU A CA  
759  C C   . LEU A 110 ? 0.2948 0.3010 0.2737 0.0578  0.0308  -0.0007 402 LEU A C   
760  O O   . LEU A 110 ? 0.3313 0.3466 0.3178 0.0533  0.0380  0.0064  402 LEU A O   
761  C CB  . LEU A 110 ? 0.2292 0.2201 0.2121 0.0571  0.0141  0.0011  402 LEU A CB  
762  C CG  . LEU A 110 ? 0.4120 0.3971 0.3891 0.0656  0.0020  -0.0020 402 LEU A CG  
763  C CD1 . LEU A 110 ? 0.2553 0.2302 0.2501 0.0681  -0.0055 -0.0073 402 LEU A CD1 
764  C CD2 . LEU A 110 ? 0.2550 0.2615 0.2298 0.0673  -0.0031 -0.0140 402 LEU A CD2 
765  N N   . LEU A 111 ? 0.3074 0.3126 0.2885 0.0617  0.0301  -0.0080 403 LEU A N   
766  C CA  . LEU A 111 ? 0.3197 0.3329 0.3124 0.0681  0.0361  -0.0082 403 LEU A CA  
767  C C   . LEU A 111 ? 0.2881 0.3149 0.3001 0.0649  0.0316  -0.0037 403 LEU A C   
768  O O   . LEU A 111 ? 0.2839 0.3076 0.2985 0.0654  0.0259  -0.0017 403 LEU A O   
769  C CB  . LEU A 111 ? 0.3107 0.3049 0.2950 0.0765  0.0355  -0.0168 403 LEU A CB  
770  C CG  . LEU A 111 ? 0.3973 0.3943 0.3904 0.0927  0.0409  -0.0202 403 LEU A CG  
771  C CD1 . LEU A 111 ? 0.5112 0.4833 0.4908 0.1029  0.0414  -0.0367 403 LEU A CD1 
772  C CD2 . LEU A 111 ? 0.3850 0.3790 0.3931 0.0966  0.0349  -0.0099 403 LEU A CD2 
773  N N   . PHE A 112 ? 0.2650 0.3097 0.2899 0.0588  0.0338  -0.0016 404 PHE A N   
774  C CA  . PHE A 112 ? 0.3375 0.4065 0.3813 0.0558  0.0297  -0.0023 404 PHE A CA  
775  C C   . PHE A 112 ? 0.2259 0.3142 0.2784 0.0673  0.0319  0.0020  404 PHE A C   
776  O O   . PHE A 112 ? 0.2182 0.3213 0.2769 0.0700  0.0256  0.0064  404 PHE A O   
777  C CB  . PHE A 112 ? 0.1948 0.2760 0.2524 0.0437  0.0314  -0.0053 404 PHE A CB  
778  C CG  . PHE A 112 ? 0.2041 0.2600 0.2572 0.0371  0.0249  -0.0093 404 PHE A CG  
779  C CD1 . PHE A 112 ? 0.2010 0.2643 0.2628 0.0372  0.0153  -0.0212 404 PHE A CD1 
780  C CD2 . PHE A 112 ? 0.2340 0.2629 0.2734 0.0340  0.0276  -0.0012 404 PHE A CD2 
781  C CE1 . PHE A 112 ? 0.2156 0.2551 0.2755 0.0380  0.0076  -0.0286 404 PHE A CE1 
782  C CE2 . PHE A 112 ? 0.2417 0.2427 0.2770 0.0337  0.0191  -0.0024 404 PHE A CE2 
783  C CZ  . PHE A 112 ? 0.2482 0.2521 0.2952 0.0376  0.0087  -0.0179 404 PHE A CZ  
784  N N   . ALA A 113 ? 0.2086 0.3019 0.2609 0.0765  0.0402  0.0016  405 ALA A N   
785  C CA  . ALA A 113 ? 0.2796 0.3874 0.3399 0.0959  0.0412  0.0037  405 ALA A CA  
786  C C   . ALA A 113 ? 0.3217 0.4164 0.3713 0.1093  0.0488  -0.0042 405 ALA A C   
787  O O   . ALA A 113 ? 0.2462 0.3376 0.2841 0.0998  0.0551  -0.0085 405 ALA A O   
788  C CB  . ALA A 113 ? 0.2305 0.3928 0.3141 0.0964  0.0434  0.0040  405 ALA A CB  
789  N N   . PRO A 114 ? 0.2456 0.3323 0.2976 0.1333  0.0474  -0.0069 406 PRO A N   
790  C CA  . PRO A 114 ? 0.2865 0.3685 0.3303 0.1501  0.0547  -0.0226 406 PRO A CA  
791  C C   . PRO A 114 ? 0.4166 0.5558 0.4677 0.1476  0.0679  -0.0283 406 PRO A C   
792  O O   . PRO A 114 ? 0.2978 0.4443 0.3362 0.1520  0.0762  -0.0409 406 PRO A O   
793  C CB  . PRO A 114 ? 0.3040 0.3686 0.3560 0.1810  0.0484  -0.0243 406 PRO A CB  
794  C CG  . PRO A 114 ? 0.3028 0.3374 0.3546 0.1723  0.0363  -0.0047 406 PRO A CG  
795  C CD  . PRO A 114 ? 0.2593 0.3338 0.3182 0.1477  0.0374  0.0044  406 PRO A CD  
796  N N   . ASN A 115 ? 0.2668 0.4529 0.3379 0.1376  0.0702  -0.0201 407 ASN A N   
797  C CA  . ASN A 115 ? 0.2714 0.5150 0.3517 0.1248  0.0831  -0.0215 407 ASN A CA  
798  C C   . ASN A 115 ? 0.3554 0.5913 0.4322 0.0888  0.0843  -0.0096 407 ASN A C   
799  O O   . ASN A 115 ? 0.2411 0.5200 0.3299 0.0690  0.0929  -0.0052 407 ASN A O   
800  C CB  . ASN A 115 ? 0.2599 0.5591 0.3658 0.1324  0.0823  -0.0231 407 ASN A CB  
801  C CG  . ASN A 115 ? 0.2253 0.5349 0.3479 0.1218  0.0731  -0.0144 407 ASN A CG  
802  O OD1 . ASN A 115 ? 0.2235 0.4927 0.3385 0.1189  0.0646  -0.0081 407 ASN A OD1 
803  N ND2 . ASN A 115 ? 0.2102 0.5723 0.3517 0.1119  0.0726  -0.0156 407 ASN A ND2 
804  N N   . LEU A 116 ? 0.2714 0.4530 0.3333 0.0800  0.0750  -0.0049 408 LEU A N   
805  C CA  . LEU A 116 ? 0.2816 0.4446 0.3403 0.0533  0.0727  0.0042  408 LEU A CA  
806  C C   . LEU A 116 ? 0.2224 0.3370 0.2554 0.0546  0.0672  0.0059  408 LEU A C   
807  O O   . LEU A 116 ? 0.2867 0.3724 0.3176 0.0541  0.0565  0.0048  408 LEU A O   
808  C CB  . LEU A 116 ? 0.4176 0.5842 0.4958 0.0437  0.0635  0.0029  408 LEU A CB  
809  C CG  . LEU A 116 ? 0.2958 0.4537 0.3816 0.0161  0.0622  0.0062  408 LEU A CG  
810  C CD1 . LEU A 116 ? 0.3905 0.5783 0.4819 -0.0029 0.0750  0.0145  408 LEU A CD1 
811  C CD2 . LEU A 116 ? 0.2507 0.4261 0.3587 0.0091  0.0533  -0.0041 408 LEU A CD2 
812  N N   . LEU A 117 ? 0.3588 0.4757 0.3722 0.0565  0.0747  0.0073  409 LEU A N   
813  C CA  . LEU A 117 ? 0.2733 0.3577 0.2614 0.0572  0.0694  0.0087  409 LEU A CA  
814  C C   . LEU A 117 ? 0.2885 0.3671 0.2672 0.0389  0.0709  0.0274  409 LEU A C   
815  O O   . LEU A 117 ? 0.3368 0.4440 0.3096 0.0295  0.0821  0.0380  409 LEU A O   
816  C CB  . LEU A 117 ? 0.3883 0.4822 0.3583 0.0728  0.0747  -0.0046 409 LEU A CB  
817  C CG  . LEU A 117 ? 0.4835 0.5558 0.4271 0.0735  0.0684  -0.0075 409 LEU A CG  
818  C CD1 . LEU A 117 ? 0.3776 0.4147 0.3247 0.0752  0.0553  -0.0146 409 LEU A CD1 
819  C CD2 . LEU A 117 ? 0.3748 0.4689 0.3006 0.0861  0.0754  -0.0251 409 LEU A CD2 
820  N N   . LEU A 118 ? 0.2707 0.3139 0.2481 0.0344  0.0592  0.0325  410 LEU A N   
821  C CA  . LEU A 118 ? 0.4467 0.4682 0.4180 0.0204  0.0565  0.0519  410 LEU A CA  
822  C C   . LEU A 118 ? 0.3281 0.3293 0.2726 0.0303  0.0484  0.0590  410 LEU A C   
823  O O   . LEU A 118 ? 0.3765 0.3705 0.3176 0.0437  0.0393  0.0447  410 LEU A O   
824  C CB  . LEU A 118 ? 0.3076 0.3043 0.3018 0.0121  0.0472  0.0483  410 LEU A CB  
825  C CG  . LEU A 118 ? 0.3081 0.3325 0.3304 0.0002  0.0527  0.0398  410 LEU A CG  
826  C CD1 . LEU A 118 ? 0.4137 0.4133 0.4558 -0.0109 0.0426  0.0329  410 LEU A CD1 
827  C CD2 . LEU A 118 ? 0.3337 0.3923 0.3577 -0.0165 0.0677  0.0528  410 LEU A CD2 
828  N N   . ASP A 119 ? 0.4473 0.4453 0.3729 0.0223  0.0513  0.0831  411 ASP A N   
829  C CA  . ASP A 119 ? 0.5925 0.5764 0.4917 0.0334  0.0416  0.0947  411 ASP A CA  
830  C C   . ASP A 119 ? 0.6130 0.5469 0.5182 0.0337  0.0275  0.1091  411 ASP A C   
831  O O   . ASP A 119 ? 0.4694 0.3783 0.3989 0.0228  0.0258  0.1065  411 ASP A O   
832  C CB  . ASP A 119 ? 0.5749 0.5911 0.4446 0.0284  0.0517  0.1149  411 ASP A CB  
833  C CG  . ASP A 119 ? 0.7164 0.7319 0.5872 0.0036  0.0616  0.1459  411 ASP A CG  
834  O OD1 . ASP A 119 ? 0.7632 0.7302 0.6450 -0.0072 0.0536  0.1634  411 ASP A OD1 
835  O OD2 . ASP A 119 ? 0.9147 0.9805 0.7758 -0.0062 0.0775  0.1514  411 ASP A OD2 
836  N N   . ARG A 120 ? 0.5631 0.4846 0.4466 0.0488  0.0158  0.1216  412 ARG A N   
837  C CA  . ARG A 120 ? 0.5242 0.3955 0.4135 0.0590  -0.0009 0.1314  412 ARG A CA  
838  C C   . ARG A 120 ? 0.7283 0.5546 0.6212 0.0387  0.0010  0.1612  412 ARG A C   
839  O O   . ARG A 120 ? 0.6266 0.4037 0.5406 0.0384  -0.0092 0.1561  412 ARG A O   
840  C CB  . ARG A 120 ? 0.5557 0.4323 0.4191 0.0829  -0.0144 0.1422  412 ARG A CB  
841  C CG  . ARG A 120 ? 0.6252 0.4576 0.4976 0.1051  -0.0347 0.1436  412 ARG A CG  
842  C CD  . ARG A 120 ? 0.5920 0.4542 0.4460 0.1334  -0.0486 0.1413  412 ARG A CD  
843  N NE  . ARG A 120 ? 0.6526 0.4768 0.5145 0.1616  -0.0694 0.1443  412 ARG A NE  
844  C CZ  . ARG A 120 ? 0.6961 0.4644 0.5467 0.1706  -0.0800 0.1797  412 ARG A CZ  
845  N NH1 . ARG A 120 ? 0.9240 0.6732 0.7527 0.1485  -0.0706 0.2196  412 ARG A NH1 
846  N NH2 . ARG A 120 ? 0.7720 0.5118 0.6405 0.1970  -0.0990 0.1727  412 ARG A NH2 
847  N N   . ASN A 121 ? 0.5513 0.3963 0.4246 0.0192  0.0140  0.1908  413 ASN A N   
848  C CA  . ASN A 121 ? 0.6404 0.4424 0.5138 -0.0066 0.0159  0.2267  413 ASN A CA  
849  C C   . ASN A 121 ? 0.6152 0.4042 0.5248 -0.0325 0.0225  0.2099  413 ASN A C   
850  O O   . ASN A 121 ? 0.6624 0.3922 0.5844 -0.0505 0.0160  0.2251  413 ASN A O   
851  C CB  . ASN A 121 ? 0.6429 0.4872 0.4859 -0.0252 0.0310  0.2626  413 ASN A CB  
852  C CG  . ASN A 121 ? 0.7806 0.6236 0.5846 -0.0051 0.0205  0.2930  413 ASN A CG  
853  O OD1 . ASN A 121 ? 0.8120 0.5976 0.6127 0.0146  0.0008  0.3056  413 ASN A OD1 
854  N ND2 . ASN A 121 ? 0.9785 0.8905 0.7529 -0.0069 0.0328  0.3029  413 ASN A ND2 
855  N N   . GLN A 122 ? 0.6882 0.5304 0.6154 -0.0346 0.0337  0.1784  414 GLN A N   
856  C CA  . GLN A 122 ? 0.6552 0.4989 0.6171 -0.0562 0.0384  0.1601  414 GLN A CA  
857  C C   . GLN A 122 ? 0.7459 0.5431 0.7313 -0.0441 0.0214  0.1336  414 GLN A C   
858  O O   . GLN A 122 ? 0.8304 0.6149 0.8432 -0.0647 0.0210  0.1207  414 GLN A O   
859  C CB  . GLN A 122 ? 0.6179 0.5333 0.5906 -0.0545 0.0526  0.1361  414 GLN A CB  
860  C CG  . GLN A 122 ? 0.6544 0.6262 0.6092 -0.0656 0.0707  0.1541  414 GLN A CG  
861  C CD  . GLN A 122 ? 0.5980 0.6324 0.5608 -0.0510 0.0810  0.1264  414 GLN A CD  
862  O OE1 . GLN A 122 ? 0.5762 0.6169 0.5263 -0.0248 0.0771  0.1099  414 GLN A OE1 
863  N NE2 . GLN A 122 ? 0.6091 0.6896 0.5943 -0.0681 0.0932  0.1208  414 GLN A NE2 
864  N N   . GLY A 123 ? 0.6619 0.4425 0.6380 -0.0118 0.0074  0.1221  415 GLY A N   
865  C CA  . GLY A 123 ? 0.6610 0.4046 0.6578 0.0031  -0.0090 0.0960  415 GLY A CA  
866  C C   . GLY A 123 ? 0.8179 0.4818 0.8156 0.0021  -0.0233 0.1126  415 GLY A C   
867  O O   . GLY A 123 ? 0.8159 0.4441 0.8374 0.0067  -0.0353 0.0865  415 GLY A O   
868  N N   . LYS A 124 ? 0.8926 0.5270 0.8641 -0.0029 -0.0232 0.1555  416 LYS A N   
869  C CA  . LYS A 124 ? 0.7512 0.2970 0.7209 -0.0038 -0.0383 0.1796  416 LYS A CA  
870  C C   . LYS A 124 ? 0.8816 0.3833 0.8767 -0.0447 -0.0352 0.1796  416 LYS A C   
871  O O   . LYS A 124 ? 0.9107 0.3401 0.9109 -0.0430 -0.0456 0.1794  416 LYS A O   
872  C CB  . LYS A 124 ? 0.8330 0.3656 0.7645 -0.0032 -0.0379 0.2336  416 LYS A CB  
873  C CG  . LYS A 124 ? 1.0271 0.5760 0.9348 0.0419  -0.0508 0.2359  416 LYS A CG  
874  C CD  . LYS A 124 ? 1.0804 0.6188 0.9481 0.0446  -0.0489 0.2835  416 LYS A CD  
875  C CE  . LYS A 124 ? 0.9592 0.5735 0.7964 0.0567  -0.0455 0.2950  416 LYS A CE  
876  N NZ  . LYS A 124 ? 0.9667 0.5709 0.7635 0.0807  -0.0598 0.3192  416 LYS A NZ  
877  N N   . SER A 125 ? 0.8730 0.4330 0.8816 -0.0782 -0.0163 0.1717  417 SER A N   
878  C CA  . SER A 125 ? 0.8234 0.3555 0.8585 -0.1224 -0.0127 0.1697  417 SER A CA  
879  C C   . SER A 125 ? 0.9097 0.4011 0.9777 -0.1141 -0.0288 0.1222  417 SER A C   
880  O O   . SER A 125 ? 0.9044 0.3397 0.9855 -0.1389 -0.0326 0.1176  417 SER A O   
881  C CB  . SER A 125 ? 0.9048 0.5273 0.9500 -0.1529 0.0099  0.1655  417 SER A CB  
882  O OG  . SER A 125 ? 0.8501 0.5457 0.8965 -0.1238 0.0149  0.1347  417 SER A OG  
883  N N   . VAL A 126 ? 0.9903 0.5232 1.0655 -0.0782 -0.0343 0.0817  418 VAL A N   
884  C CA  . VAL A 126 ? 0.9912 0.5017 1.0941 -0.0638 -0.0497 0.0325  418 VAL A CA  
885  C C   . VAL A 126 ? 0.8770 0.3349 0.9680 -0.0182 -0.0686 0.0279  418 VAL A C   
886  O O   . VAL A 126 ? 0.9149 0.4036 0.9861 0.0138  -0.0702 0.0372  418 VAL A O   
887  C CB  . VAL A 126 ? 0.8567 0.4597 0.9739 -0.0546 -0.0428 -0.0072 418 VAL A CB  
888  C CG1 . VAL A 126 ? 0.8401 0.4331 0.9816 -0.0360 -0.0588 -0.0589 418 VAL A CG1 
889  C CG2 . VAL A 126 ? 0.7715 0.4322 0.9022 -0.0941 -0.0255 -0.0046 418 VAL A CG2 
890  N N   . GLU A 127 ? 0.8447 0.2463 0.9406 -0.0141 -0.0767 0.0108  419 GLU A N   
891  C CA  . GLU A 127 ? 0.9178 0.2869 1.0012 0.0304  -0.0887 0.0072  419 GLU A CA  
892  C C   . GLU A 127 ? 1.0206 0.4524 1.1162 0.0678  -0.0966 -0.0384 419 GLU A C   
893  O O   . GLU A 127 ? 0.8236 0.2911 0.9420 0.0608  -0.0975 -0.0810 419 GLU A O   
894  C CB  . GLU A 127 ? 1.0067 0.2944 1.0956 0.0236  -0.0945 0.0009  419 GLU A CB  
895  C CG  . GLU A 127 ? 1.1630 0.4069 1.2411 0.0676  -0.1059 0.0080  419 GLU A CG  
896  C CD  . GLU A 127 ? 1.2613 0.5383 1.3574 0.1066  -0.1182 -0.0451 419 GLU A CD  
897  O OE1 . GLU A 127 ? 1.3368 0.6285 1.4264 0.1486  -0.1264 -0.0426 419 GLU A OE1 
898  O OE2 . GLU A 127 ? 1.3380 0.6357 1.4552 0.0941  -0.1198 -0.0893 419 GLU A OE2 
899  N N   . GLY A 128 ? 1.0381 0.4941 1.1181 0.1052  -0.1014 -0.0287 420 GLY A N   
900  C CA  . GLY A 128 ? 0.7405 0.2700 0.8285 0.1357  -0.1061 -0.0650 420 GLY A CA  
901  C C   . GLY A 128 ? 0.7396 0.3402 0.8230 0.1308  -0.0977 -0.0640 420 GLY A C   
902  O O   . GLY A 128 ? 0.6762 0.3438 0.7618 0.1524  -0.0992 -0.0874 420 GLY A O   
903  N N   . MET A 129 ? 0.7669 0.3966 0.6260 -0.0742 -0.0194 0.0856  421 MET A N   
904  C CA  . MET A 129 ? 0.5648 0.2686 0.4654 -0.0692 -0.0233 0.0826  421 MET A CA  
905  C C   . MET A 129 ? 0.5131 0.2538 0.4391 -0.0392 -0.0186 0.0871  421 MET A C   
906  O O   . MET A 129 ? 0.5492 0.3251 0.4964 -0.0236 -0.0184 0.0791  421 MET A O   
907  C CB  . MET A 129 ? 0.5021 0.2496 0.4207 -0.0993 -0.0304 0.0920  421 MET A CB  
908  C CG  . MET A 129 ? 0.5561 0.3715 0.5123 -0.0948 -0.0330 0.0893  421 MET A CG  
909  S SD  . MET A 129 ? 0.6119 0.4796 0.5885 -0.1290 -0.0401 0.1029  421 MET A SD  
910  C CE  . MET A 129 ? 0.6662 0.5845 0.6720 -0.1192 -0.0431 0.0951  421 MET A CE  
911  N N   . VAL A 130 ? 0.6293 0.3616 0.5506 -0.0334 -0.0153 0.1005  422 VAL A N   
912  C CA  . VAL A 130 ? 0.5511 0.3243 0.4937 -0.0119 -0.0130 0.1062  422 VAL A CA  
913  C C   . VAL A 130 ? 0.4632 0.2321 0.4074 0.0173  -0.0099 0.1003  422 VAL A C   
914  O O   . VAL A 130 ? 0.4752 0.2867 0.4396 0.0307  -0.0105 0.0997  422 VAL A O   
915  C CB  . VAL A 130 ? 0.5598 0.3255 0.4937 -0.0143 -0.0110 0.1239  422 VAL A CB  
916  C CG1 . VAL A 130 ? 0.5923 0.2993 0.4986 0.0004  -0.0067 0.1314  422 VAL A CG1 
917  C CG2 . VAL A 130 ? 0.6116 0.4293 0.5659 -0.0022 -0.0104 0.1290  422 VAL A CG2 
918  N N   . GLU A 131 ? 0.5241 0.2418 0.4449 0.0267  -0.0056 0.0964  423 GLU A N   
919  C CA  . GLU A 131 ? 0.5120 0.2323 0.4371 0.0560  -0.0009 0.0930  423 GLU A CA  
920  C C   . GLU A 131 ? 0.4989 0.2584 0.4446 0.0559  -0.0041 0.0788  423 GLU A C   
921  O O   . GLU A 131 ? 0.4785 0.2770 0.4441 0.0719  -0.0045 0.0794  423 GLU A O   
922  C CB  . GLU A 131 ? 0.5418 0.1939 0.4335 0.0682  0.0080  0.0914  423 GLU A CB  
923  C CG  . GLU A 131 ? 0.7203 0.3333 0.5929 0.0791  0.0136  0.1083  423 GLU A CG  
924  C CD  . GLU A 131 ? 0.8767 0.4502 0.7258 0.0486  0.0107  0.1126  423 GLU A CD  
925  O OE1 . GLU A 131 ? 1.0241 0.5934 0.8711 0.0492  0.0110  0.1283  423 GLU A OE1 
926  O OE2 . GLU A 131 ? 0.8565 0.4123 0.6926 0.0212  0.0067  0.1006  423 GLU A OE2 
927  N N   . ILE A 132 ? 0.4336 0.1841 0.3737 0.0356  -0.0073 0.0674  424 ILE A N   
928  C CA  . ILE A 132 ? 0.4125 0.2007 0.3722 0.0338  -0.0108 0.0564  424 ILE A CA  
929  C C   . ILE A 132 ? 0.3811 0.2226 0.3685 0.0292  -0.0148 0.0603  424 ILE A C   
930  O O   . ILE A 132 ? 0.3820 0.2565 0.3867 0.0376  -0.0156 0.0554  424 ILE A O   
931  C CB  . ILE A 132 ? 0.4456 0.2142 0.3913 0.0118  -0.0145 0.0466  424 ILE A CB  
932  C CG1 . ILE A 132 ? 0.6485 0.3484 0.5539 0.0089  -0.0095 0.0431  424 ILE A CG1 
933  C CG2 . ILE A 132 ? 0.4259 0.2221 0.3853 0.0161  -0.0162 0.0360  424 ILE A CG2 
934  C CD1 . ILE A 132 ? 0.7670 0.4425 0.6585 0.0333  -0.0006 0.0347  424 ILE A CD1 
935  N N   . PHE A 133 ? 0.3798 0.2270 0.3682 0.0151  -0.0162 0.0694  425 PHE A N   
936  C CA  . PHE A 133 ? 0.3699 0.2617 0.3786 0.0128  -0.0164 0.0730  425 PHE A CA  
937  C C   . PHE A 133 ? 0.3237 0.2348 0.3382 0.0308  -0.0149 0.0746  425 PHE A C   
938  O O   . PHE A 133 ? 0.2690 0.2102 0.2960 0.0335  -0.0148 0.0693  425 PHE A O   
939  C CB  . PHE A 133 ? 0.4085 0.3009 0.4138 -0.0031 -0.0159 0.0849  425 PHE A CB  
940  C CG  . PHE A 133 ? 0.4252 0.3610 0.4496 -0.0102 -0.0139 0.0874  425 PHE A CG  
941  C CD1 . PHE A 133 ? 0.3350 0.2966 0.3660 0.0009  -0.0094 0.0879  425 PHE A CD1 
942  C CD2 . PHE A 133 ? 0.3450 0.2959 0.3785 -0.0282 -0.0156 0.0905  425 PHE A CD2 
943  C CE1 . PHE A 133 ? 0.3635 0.3582 0.4073 -0.0018 -0.0038 0.0897  425 PHE A CE1 
944  C CE2 . PHE A 133 ? 0.4373 0.4310 0.4904 -0.0296 -0.0109 0.0956  425 PHE A CE2 
945  C CZ  . PHE A 133 ? 0.3974 0.4095 0.4544 -0.0145 -0.0034 0.0944  425 PHE A CZ  
946  N N   . ASP A 134 ? 0.3784 0.2715 0.3818 0.0424  -0.0139 0.0831  426 ASP A N   
947  C CA  . ASP A 134 ? 0.4265 0.3450 0.4353 0.0560  -0.0147 0.0883  426 ASP A CA  
948  C C   . ASP A 134 ? 0.3167 0.2517 0.3354 0.0670  -0.0159 0.0800  426 ASP A C   
949  O O   . ASP A 134 ? 0.2683 0.2348 0.2945 0.0683  -0.0186 0.0793  426 ASP A O   
950  C CB  . ASP A 134 ? 0.3972 0.2967 0.3941 0.0676  -0.0136 0.1039  426 ASP A CB  
951  C CG  . ASP A 134 ? 0.4017 0.2930 0.3889 0.0555  -0.0130 0.1150  426 ASP A CG  
952  O OD1 . ASP A 134 ? 0.4542 0.3658 0.4470 0.0405  -0.0129 0.1113  426 ASP A OD1 
953  O OD2 . ASP A 134 ? 0.4743 0.3387 0.4479 0.0623  -0.0114 0.1287  426 ASP A OD2 
954  N N   . MET A 135 ? 0.3397 0.2524 0.3550 0.0727  -0.0137 0.0735  427 MET A N   
955  C CA  . MET A 135 ? 0.3653 0.2964 0.3904 0.0819  -0.0139 0.0666  427 MET A CA  
956  C C   . MET A 135 ? 0.2676 0.2223 0.3039 0.0694  -0.0169 0.0560  427 MET A C   
957  O O   . MET A 135 ? 0.3102 0.2909 0.3550 0.0719  -0.0190 0.0536  427 MET A O   
958  C CB  . MET A 135 ? 0.3700 0.2689 0.3843 0.0908  -0.0088 0.0612  427 MET A CB  
959  C CG  . MET A 135 ? 0.4470 0.3194 0.4487 0.1111  -0.0021 0.0721  427 MET A CG  
960  S SD  . MET A 135 ? 0.5691 0.3966 0.5501 0.1242  0.0082  0.0630  427 MET A SD  
961  C CE  . MET A 135 ? 0.4444 0.2313 0.4043 0.0947  0.0046  0.0500  427 MET A CE  
962  N N   . LEU A 136 ? 0.2454 0.1918 0.2811 0.0557  -0.0170 0.0514  428 LEU A N   
963  C CA  . LEU A 136 ? 0.2630 0.2303 0.3094 0.0481  -0.0178 0.0446  428 LEU A CA  
964  C C   . LEU A 136 ? 0.2854 0.2730 0.3331 0.0469  -0.0168 0.0468  428 LEU A C   
965  O O   . LEU A 136 ? 0.2457 0.2465 0.2966 0.0462  -0.0164 0.0408  428 LEU A O   
966  C CB  . LEU A 136 ? 0.2232 0.1850 0.2717 0.0353  -0.0179 0.0440  428 LEU A CB  
967  C CG  . LEU A 136 ? 0.2931 0.2352 0.3350 0.0303  -0.0202 0.0391  428 LEU A CG  
968  C CD1 . LEU A 136 ? 0.2520 0.1857 0.2897 0.0127  -0.0226 0.0436  428 LEU A CD1 
969  C CD2 . LEU A 136 ? 0.2204 0.1776 0.2713 0.0316  -0.0216 0.0318  428 LEU A CD2 
970  N N   . LEU A 137 ? 0.3013 0.2873 0.3421 0.0457  -0.0159 0.0553  429 LEU A N   
971  C CA  . LEU A 137 ? 0.3049 0.3071 0.3399 0.0433  -0.0145 0.0568  429 LEU A CA  
972  C C   . LEU A 137 ? 0.2945 0.3110 0.3264 0.0470  -0.0192 0.0563  429 LEU A C   
973  O O   . LEU A 137 ? 0.3482 0.3745 0.3730 0.0411  -0.0189 0.0504  429 LEU A O   
974  C CB  . LEU A 137 ? 0.3113 0.3100 0.3378 0.0405  -0.0131 0.0680  429 LEU A CB  
975  C CG  . LEU A 137 ? 0.2914 0.2868 0.3205 0.0318  -0.0080 0.0712  429 LEU A CG  
976  C CD1 . LEU A 137 ? 0.2665 0.2597 0.2851 0.0280  -0.0066 0.0838  429 LEU A CD1 
977  C CD2 . LEU A 137 ? 0.3373 0.3485 0.3713 0.0300  -0.0012 0.0643  429 LEU A CD2 
978  N N   . ALA A 138 ? 0.2809 0.2982 0.3161 0.0564  -0.0229 0.0634  430 ALA A N   
979  C CA  . ALA A 138 ? 0.2240 0.2659 0.2607 0.0591  -0.0283 0.0673  430 ALA A CA  
980  C C   . ALA A 138 ? 0.2285 0.2789 0.2710 0.0548  -0.0293 0.0566  430 ALA A C   
981  O O   . ALA A 138 ? 0.3740 0.4438 0.4120 0.0463  -0.0338 0.0558  430 ALA A O   
982  C CB  . ALA A 138 ? 0.2758 0.3203 0.3183 0.0754  -0.0292 0.0806  430 ALA A CB  
983  N N   . THR A 139 ? 0.3274 0.3624 0.3768 0.0579  -0.0258 0.0492  431 THR A N   
984  C CA  . THR A 139 ? 0.2685 0.3094 0.3223 0.0534  -0.0263 0.0404  431 THR A CA  
985  C C   . THR A 139 ? 0.2943 0.3308 0.3391 0.0419  -0.0245 0.0325  431 THR A C   
986  O O   . THR A 139 ? 0.3074 0.3500 0.3471 0.0342  -0.0264 0.0280  431 THR A O   
987  C CB  . THR A 139 ? 0.2873 0.3126 0.3473 0.0582  -0.0234 0.0353  431 THR A CB  
988  O OG1 . THR A 139 ? 0.3048 0.3205 0.3644 0.0700  -0.0217 0.0410  431 THR A OG1 
989  C CG2 . THR A 139 ? 0.2932 0.3284 0.3581 0.0559  -0.0243 0.0298  431 THR A CG2 
990  N N   . SER A 140 ? 0.2517 0.2760 0.2924 0.0409  -0.0195 0.0316  432 SER A N   
991  C CA  . SER A 140 ? 0.3081 0.3251 0.3375 0.0352  -0.0137 0.0251  432 SER A CA  
992  C C   . SER A 140 ? 0.2944 0.3158 0.3033 0.0261  -0.0159 0.0241  432 SER A C   
993  O O   . SER A 140 ? 0.3945 0.4046 0.3868 0.0185  -0.0128 0.0158  432 SER A O   
994  C CB  . SER A 140 ? 0.3335 0.3450 0.3654 0.0380  -0.0063 0.0278  432 SER A CB  
995  O OG  . SER A 140 ? 0.4777 0.4814 0.5020 0.0386  0.0030  0.0224  432 SER A OG  
996  N N   . SER A 141 ? 0.2769 0.3120 0.2833 0.0257  -0.0213 0.0331  433 SER A N   
997  C CA  . SER A 141 ? 0.3292 0.3751 0.3153 0.0137  -0.0265 0.0344  433 SER A CA  
998  C C   . SER A 141 ? 0.3191 0.3805 0.3059 0.0048  -0.0348 0.0338  433 SER A C   
999  O O   . SER A 141 ? 0.3344 0.3948 0.2982 -0.0122 -0.0380 0.0288  433 SER A O   
1000 C CB  . SER A 141 ? 0.3072 0.3695 0.2936 0.0169  -0.0314 0.0485  433 SER A CB  
1001 O OG  . SER A 141 ? 0.5990 0.6480 0.5816 0.0209  -0.0237 0.0501  433 SER A OG  
1002 N N   . ARG A 142 ? 0.3174 0.3923 0.3275 0.0144  -0.0379 0.0390  434 ARG A N   
1003 C CA  . ARG A 142 ? 0.2494 0.3455 0.2643 0.0065  -0.0446 0.0407  434 ARG A CA  
1004 C C   . ARG A 142 ? 0.2782 0.3518 0.2801 -0.0056 -0.0414 0.0273  434 ARG A C   
1005 O O   . ARG A 142 ? 0.3120 0.3916 0.2985 -0.0244 -0.0470 0.0255  434 ARG A O   
1006 C CB  . ARG A 142 ? 0.3430 0.4550 0.3837 0.0233  -0.0445 0.0485  434 ARG A CB  
1007 C CG  . ARG A 142 ? 0.3319 0.4720 0.3821 0.0174  -0.0494 0.0524  434 ARG A CG  
1008 C CD  . ARG A 142 ? 0.4537 0.6335 0.5004 0.0036  -0.0600 0.0645  434 ARG A CD  
1009 N NE  . ARG A 142 ? 0.5110 0.7257 0.5705 -0.0033 -0.0647 0.0713  434 ARG A NE  
1010 C CZ  . ARG A 142 ? 0.6047 0.8606 0.6621 -0.0224 -0.0756 0.0824  434 ARG A CZ  
1011 N NH1 . ARG A 142 ? 0.5743 0.8401 0.6143 -0.0374 -0.0839 0.0869  434 ARG A NH1 
1012 N NH2 . ARG A 142 ? 0.5403 0.8314 0.6124 -0.0288 -0.0789 0.0901  434 ARG A NH2 
1013 N N   . PHE A 143 ? 0.3172 0.3646 0.3237 0.0038  -0.0325 0.0196  435 PHE A N   
1014 C CA  . PHE A 143 ? 0.2926 0.3139 0.2857 -0.0034 -0.0273 0.0093  435 PHE A CA  
1015 C C   . PHE A 143 ? 0.3565 0.3537 0.3155 -0.0164 -0.0234 0.0014  435 PHE A C   
1016 O O   . PHE A 143 ? 0.3948 0.3726 0.3313 -0.0313 -0.0232 -0.0056 435 PHE A O   
1017 C CB  . PHE A 143 ? 0.3158 0.3206 0.3223 0.0113  -0.0189 0.0066  435 PHE A CB  
1018 C CG  . PHE A 143 ? 0.4358 0.4527 0.4642 0.0182  -0.0218 0.0099  435 PHE A CG  
1019 C CD1 . PHE A 143 ? 0.4778 0.5172 0.5131 0.0139  -0.0287 0.0143  435 PHE A CD1 
1020 C CD2 . PHE A 143 ? 0.4703 0.4792 0.5111 0.0283  -0.0173 0.0097  435 PHE A CD2 
1021 C CE1 . PHE A 143 ? 0.4529 0.5013 0.5040 0.0215  -0.0290 0.0164  435 PHE A CE1 
1022 C CE2 . PHE A 143 ? 0.3441 0.3612 0.3986 0.0324  -0.0199 0.0115  435 PHE A CE2 
1023 C CZ  . PHE A 143 ? 0.3387 0.3728 0.3967 0.0300  -0.0247 0.0138  435 PHE A CZ  
1024 N N   . ARG A 144 ? 0.3578 0.3522 0.3086 -0.0120 -0.0192 0.0022  436 ARG A N   
1025 C CA  . ARG A 144 ? 0.3873 0.3557 0.3003 -0.0228 -0.0129 -0.0064 436 ARG A CA  
1026 C C   . ARG A 144 ? 0.3457 0.3239 0.2334 -0.0478 -0.0246 -0.0066 436 ARG A C   
1027 O O   . ARG A 144 ? 0.4324 0.3791 0.2828 -0.0651 -0.0217 -0.0175 436 ARG A O   
1028 C CB  . ARG A 144 ? 0.3902 0.3609 0.3021 -0.0128 -0.0062 -0.0031 436 ARG A CB  
1029 C CG  . ARG A 144 ? 0.4520 0.3924 0.3235 -0.0187 0.0055  -0.0130 436 ARG A CG  
1030 C CD  . ARG A 144 ? 0.4405 0.3931 0.3136 -0.0108 0.0104  -0.0064 436 ARG A CD  
1031 N NE  . ARG A 144 ? 0.6186 0.5874 0.5305 0.0070  0.0129  0.0029  436 ARG A NE  
1032 C CZ  . ARG A 144 ? 0.4801 0.4731 0.4117 0.0105  0.0059  0.0150  436 ARG A CZ  
1033 N NH1 . ARG A 144 ? 0.4901 0.4989 0.4112 0.0015  -0.0037 0.0219  436 ARG A NH1 
1034 N NH2 . ARG A 144 ? 0.5392 0.5393 0.4994 0.0222  0.0082  0.0216  436 ARG A NH2 
1035 N N   . MET A 145 ? 0.3376 0.3588 0.2434 -0.0506 -0.0376 0.0067  437 MET A N   
1036 C CA  . MET A 145 ? 0.3809 0.4253 0.2684 -0.0759 -0.0513 0.0114  437 MET A CA  
1037 C C   . MET A 145 ? 0.3645 0.4073 0.2484 -0.0929 -0.0567 0.0081  437 MET A C   
1038 O O   . MET A 145 ? 0.5074 0.5502 0.3608 -0.1222 -0.0652 0.0059  437 MET A O   
1039 C CB  . MET A 145 ? 0.3710 0.4685 0.2861 -0.0691 -0.0628 0.0311  437 MET A CB  
1040 N N   . MET A 146 ? 0.4484 0.4901 0.3602 -0.0780 -0.0524 0.0083  438 MET A N   
1041 C CA  . MET A 146 ? 0.4445 0.4844 0.3542 -0.0932 -0.0562 0.0066  438 MET A CA  
1042 C C   . MET A 146 ? 0.4133 0.3928 0.2896 -0.1008 -0.0455 -0.0093 438 MET A C   
1043 O O   . MET A 146 ? 0.4239 0.3925 0.2886 -0.1188 -0.0487 -0.0113 438 MET A O   
1044 C CB  . MET A 146 ? 0.3898 0.4558 0.3412 -0.0737 -0.0558 0.0149  438 MET A CB  
1045 C CG  . MET A 146 ? 0.5125 0.6376 0.4930 -0.0690 -0.0655 0.0323  438 MET A CG  
1046 S SD  . MET A 146 ? 0.5546 0.6980 0.5726 -0.0465 -0.0608 0.0380  438 MET A SD  
1047 C CE  . MET A 146 ? 0.4797 0.6438 0.4930 -0.0739 -0.0684 0.0419  438 MET A CE  
1048 N N   . ASN A 147 ? 0.4466 0.3871 0.3069 -0.0867 -0.0318 -0.0189 439 ASN A N   
1049 C CA  . ASN A 147 ? 0.5855 0.4672 0.4180 -0.0841 -0.0173 -0.0315 439 ASN A CA  
1050 C C   . ASN A 147 ? 0.4050 0.2853 0.2634 -0.0731 -0.0152 -0.0280 439 ASN A C   
1051 O O   . ASN A 147 ? 0.4529 0.3027 0.2905 -0.0868 -0.0139 -0.0322 439 ASN A O   
1052 C CB  . ASN A 147 ? 0.4936 0.3340 0.2700 -0.1152 -0.0180 -0.0426 439 ASN A CB  
1053 C CG  . ASN A 147 ? 0.6650 0.4332 0.4037 -0.1070 0.0019  -0.0563 439 ASN A CG  
1054 O OD1 . ASN A 147 ? 0.6552 0.4093 0.4015 -0.0792 0.0174  -0.0581 439 ASN A OD1 
1055 N ND2 . ASN A 147 ? 0.9237 0.6457 0.6208 -0.1311 0.0024  -0.0645 439 ASN A ND2 
1056 N N   . LEU A 148 ? 0.3954 0.3069 0.2961 -0.0503 -0.0152 -0.0197 440 LEU A N   
1057 C CA  . LEU A 148 ? 0.3911 0.3057 0.3159 -0.0397 -0.0139 -0.0156 440 LEU A CA  
1058 C C   . LEU A 148 ? 0.3513 0.2175 0.2587 -0.0305 0.0001  -0.0213 440 LEU A C   
1059 O O   . LEU A 148 ? 0.4513 0.2965 0.3506 -0.0156 0.0122  -0.0247 440 LEU A O   
1060 C CB  . LEU A 148 ? 0.2906 0.2390 0.2545 -0.0188 -0.0153 -0.0079 440 LEU A CB  
1061 C CG  . LEU A 148 ? 0.3187 0.2746 0.3053 -0.0097 -0.0153 -0.0035 440 LEU A CG  
1062 C CD1 . LEU A 148 ? 0.2571 0.2365 0.2491 -0.0236 -0.0245 0.0009  440 LEU A CD1 
1063 C CD2 . LEU A 148 ? 0.3378 0.3137 0.3518 0.0083  -0.0149 0.0013  440 LEU A CD2 
1064 N N   . GLN A 149 ? 0.3643 0.2145 0.2667 -0.0380 -0.0006 -0.0203 441 GLN A N   
1065 C CA  . GLN A 149 ? 0.4686 0.2705 0.3537 -0.0278 0.0129  -0.0225 441 GLN A CA  
1066 C C   . GLN A 149 ? 0.3948 0.2169 0.3165 -0.0050 0.0151  -0.0126 441 GLN A C   
1067 O O   . GLN A 149 ? 0.3783 0.2419 0.3297 -0.0051 0.0049  -0.0063 441 GLN A O   
1068 C CB  . GLN A 149 ? 0.4852 0.2511 0.3379 -0.0516 0.0110  -0.0257 441 GLN A CB  
1069 C CG  . GLN A 149 ? 0.4916 0.2321 0.2999 -0.0802 0.0078  -0.0360 441 GLN A CG  
1070 C CD  . GLN A 149 ? 0.5403 0.2283 0.3108 -0.0705 0.0244  -0.0472 441 GLN A CD  
1071 O OE1 . GLN A 149 ? 0.8010 0.4343 0.5491 -0.0565 0.0408  -0.0503 441 GLN A OE1 
1072 N NE2 . GLN A 149 ? 0.5380 0.2426 0.3004 -0.0757 0.0216  -0.0519 441 GLN A NE2 
1073 N N   . GLY A 150 ? 0.4412 0.2339 0.3583 0.0150  0.0294  -0.0104 442 GLY A N   
1074 C CA  . GLY A 150 ? 0.4004 0.2158 0.3506 0.0346  0.0304  0.0015  442 GLY A CA  
1075 C C   . GLY A 150 ? 0.3789 0.2020 0.3373 0.0255  0.0219  0.0075  442 GLY A C   
1076 O O   . GLY A 150 ? 0.4192 0.2787 0.4070 0.0316  0.0150  0.0155  442 GLY A O   
1077 N N   . GLU A 151 ? 0.4452 0.2323 0.3738 0.0085  0.0224  0.0039  443 GLU A N   
1078 C CA  . GLU A 151 ? 0.3915 0.1878 0.3258 -0.0033 0.0145  0.0106  443 GLU A CA  
1079 C C   . GLU A 151 ? 0.3837 0.2336 0.3412 -0.0157 0.0003  0.0112  443 GLU A C   
1080 O O   . GLU A 151 ? 0.3617 0.2379 0.3380 -0.0151 -0.0050 0.0187  443 GLU A O   
1081 C CB  . GLU A 151 ? 0.5037 0.2483 0.3974 -0.0241 0.0175  0.0068  443 GLU A CB  
1082 C CG  . GLU A 151 ? 0.5580 0.2397 0.4247 -0.0081 0.0345  0.0082  443 GLU A CG  
1083 C CD  . GLU A 151 ? 0.6661 0.3032 0.4977 -0.0061 0.0466  -0.0046 443 GLU A CD  
1084 O OE1 . GLU A 151 ? 0.6759 0.3405 0.5123 -0.0128 0.0410  -0.0125 443 GLU A OE1 
1085 O OE2 . GLU A 151 ? 0.8681 0.4403 0.6647 0.0033  0.0629  -0.0062 443 GLU A OE2 
1086 N N   . GLU A 152 ? 0.3961 0.2626 0.3510 -0.0254 -0.0047 0.0045  444 GLU A N   
1087 C CA  . GLU A 152 ? 0.3028 0.2206 0.2814 -0.0305 -0.0152 0.0073  444 GLU A CA  
1088 C C   . GLU A 152 ? 0.2473 0.1921 0.2543 -0.0095 -0.0151 0.0100  444 GLU A C   
1089 O O   . GLU A 152 ? 0.2989 0.2758 0.3243 -0.0074 -0.0201 0.0139  444 GLU A O   
1090 C CB  . GLU A 152 ? 0.3443 0.2740 0.3117 -0.0460 -0.0209 0.0029  444 GLU A CB  
1091 C CG  . GLU A 152 ? 0.3759 0.2879 0.3139 -0.0752 -0.0251 0.0013  444 GLU A CG  
1092 C CD  . GLU A 152 ? 0.3810 0.3037 0.3036 -0.0922 -0.0315 -0.0024 444 GLU A CD  
1093 O OE1 . GLU A 152 ? 0.4140 0.3219 0.3281 -0.0820 -0.0265 -0.0087 444 GLU A OE1 
1094 O OE2 . GLU A 152 ? 0.4134 0.3641 0.3330 -0.1165 -0.0419 0.0029  444 GLU A OE2 
1095 N N   . PHE A 153 ? 0.3263 0.2574 0.3344 0.0051  -0.0084 0.0082  445 PHE A N   
1096 C CA  . PHE A 153 ? 0.3118 0.2669 0.3433 0.0196  -0.0095 0.0112  445 PHE A CA  
1097 C C   . PHE A 153 ? 0.2679 0.2340 0.3135 0.0254  -0.0113 0.0182  445 PHE A C   
1098 O O   . PHE A 153 ? 0.2685 0.2583 0.3276 0.0273  -0.0163 0.0193  445 PHE A O   
1099 C CB  . PHE A 153 ? 0.3251 0.2676 0.3554 0.0315  -0.0014 0.0106  445 PHE A CB  
1100 C CG  . PHE A 153 ? 0.2803 0.2445 0.3331 0.0430  -0.0024 0.0167  445 PHE A CG  
1101 C CD1 . PHE A 153 ? 0.2490 0.2345 0.3126 0.0413  -0.0086 0.0157  445 PHE A CD1 
1102 C CD2 . PHE A 153 ? 0.3082 0.2714 0.3700 0.0544  0.0029  0.0252  445 PHE A CD2 
1103 C CE1 . PHE A 153 ? 0.2089 0.2092 0.2872 0.0462  -0.0105 0.0208  445 PHE A CE1 
1104 C CE2 . PHE A 153 ? 0.2654 0.2541 0.3472 0.0595  -0.0002 0.0325  445 PHE A CE2 
1105 C CZ  . PHE A 153 ? 0.2645 0.2693 0.3523 0.0531  -0.0074 0.0293  445 PHE A CZ  
1106 N N   . VAL A 154 ? 0.2520 0.1980 0.2912 0.0284  -0.0067 0.0233  446 VAL A N   
1107 C CA  . VAL A 154 ? 0.2600 0.2192 0.3112 0.0329  -0.0095 0.0323  446 VAL A CA  
1108 C C   . VAL A 154 ? 0.2249 0.2007 0.2759 0.0212  -0.0161 0.0318  446 VAL A C   
1109 O O   . VAL A 154 ? 0.2645 0.2598 0.3246 0.0229  -0.0201 0.0358  446 VAL A O   
1110 C CB  . VAL A 154 ? 0.3435 0.2769 0.3878 0.0416  -0.0021 0.0412  446 VAL A CB  
1111 C CG1 . VAL A 154 ? 0.2652 0.1867 0.3111 0.0576  0.0077  0.0432  446 VAL A CG1 
1112 C CG2 . VAL A 154 ? 0.2980 0.1975 0.3176 0.0296  0.0009  0.0386  446 VAL A CG2 
1113 N N   . CYS A 155 ? 0.2173 0.1887 0.2569 0.0079  -0.0171 0.0277  447 CYS A N   
1114 C CA  . CYS A 155 ? 0.2555 0.2520 0.2985 -0.0017 -0.0217 0.0293  447 CYS A CA  
1115 C C   . CYS A 155 ? 0.2019 0.2270 0.2578 0.0048  -0.0240 0.0256  447 CYS A C   
1116 O O   . CYS A 155 ? 0.2799 0.3234 0.3409 0.0074  -0.0247 0.0272  447 CYS A O   
1117 C CB  . CYS A 155 ? 0.2576 0.2492 0.2869 -0.0203 -0.0232 0.0288  447 CYS A CB  
1118 S SG  . CYS A 155 ? 0.3550 0.3038 0.3606 -0.0326 -0.0198 0.0336  447 CYS A SG  
1119 N N   . LEU A 156 ? 0.2370 0.2619 0.2945 0.0083  -0.0240 0.0208  448 LEU A N   
1120 C CA  . LEU A 156 ? 0.2509 0.2949 0.3175 0.0165  -0.0247 0.0186  448 LEU A CA  
1121 C C   . LEU A 156 ? 0.2252 0.2662 0.2956 0.0254  -0.0244 0.0177  448 LEU A C   
1122 O O   . LEU A 156 ? 0.2658 0.3163 0.3363 0.0301  -0.0237 0.0161  448 LEU A O   
1123 C CB  . LEU A 156 ? 0.1887 0.2300 0.2545 0.0179  -0.0250 0.0158  448 LEU A CB  
1124 C CG  . LEU A 156 ? 0.2530 0.3060 0.3135 0.0063  -0.0279 0.0173  448 LEU A CG  
1125 C CD1 . LEU A 156 ? 0.3394 0.3944 0.3993 0.0097  -0.0289 0.0161  448 LEU A CD1 
1126 C CD2 . LEU A 156 ? 0.2511 0.3372 0.3203 0.0039  -0.0295 0.0234  448 LEU A CD2 
1127 N N   . LYS A 157 ? 0.2012 0.2288 0.2725 0.0275  -0.0243 0.0196  449 LYS A N   
1128 C CA  . LYS A 157 ? 0.2659 0.2962 0.3405 0.0306  -0.0264 0.0211  449 LYS A CA  
1129 C C   . LYS A 157 ? 0.2727 0.3107 0.3427 0.0270  -0.0285 0.0237  449 LYS A C   
1130 O O   . LYS A 157 ? 0.2594 0.3006 0.3237 0.0260  -0.0304 0.0211  449 LYS A O   
1131 C CB  . LYS A 157 ? 0.2107 0.2356 0.2918 0.0343  -0.0256 0.0271  449 LYS A CB  
1132 C CG  . LYS A 157 ? 0.2394 0.2736 0.3262 0.0337  -0.0294 0.0300  449 LYS A CG  
1133 C CD  . LYS A 157 ? 0.2770 0.3147 0.3750 0.0396  -0.0266 0.0379  449 LYS A CD  
1134 C CE  . LYS A 157 ? 0.2610 0.2933 0.3614 0.0471  -0.0216 0.0462  449 LYS A CE  
1135 N NZ  . LYS A 157 ? 0.2691 0.3136 0.3837 0.0568  -0.0178 0.0587  449 LYS A NZ  
1136 N N   . SER A 158 ? 0.1930 0.2304 0.2610 0.0232  -0.0278 0.0288  450 SER A N   
1137 C CA  . SER A 158 ? 0.2391 0.2857 0.3014 0.0189  -0.0293 0.0327  450 SER A CA  
1138 C C   . SER A 158 ? 0.2020 0.2612 0.2586 0.0183  -0.0265 0.0270  450 SER A C   
1139 O O   . SER A 158 ? 0.2212 0.2866 0.2687 0.0174  -0.0262 0.0261  450 SER A O   
1140 C CB  . SER A 158 ? 0.2064 0.2456 0.2664 0.0144  -0.0285 0.0412  450 SER A CB  
1141 O OG  . SER A 158 ? 0.4976 0.5230 0.5618 0.0203  -0.0279 0.0482  450 SER A OG  
1142 N N   . ILE A 159 ? 0.1874 0.2524 0.2482 0.0196  -0.0237 0.0243  451 ILE A N   
1143 C CA  . ILE A 159 ? 0.1899 0.2728 0.2494 0.0242  -0.0188 0.0221  451 ILE A CA  
1144 C C   . ILE A 159 ? 0.1748 0.2477 0.2263 0.0341  -0.0160 0.0148  451 ILE A C   
1145 O O   . ILE A 159 ? 0.2876 0.3637 0.3279 0.0391  -0.0102 0.0119  451 ILE A O   
1146 C CB  . ILE A 159 ? 0.2100 0.3083 0.2787 0.0231  -0.0180 0.0246  451 ILE A CB  
1147 C CG1 . ILE A 159 ? 0.3385 0.4460 0.4075 0.0081  -0.0203 0.0316  451 ILE A CG1 
1148 C CG2 . ILE A 159 ? 0.1883 0.3081 0.2602 0.0351  -0.0114 0.0250  451 ILE A CG2 
1149 C CD1 . ILE A 159 ? 0.2012 0.3178 0.2742 -0.0009 -0.0233 0.0340  451 ILE A CD1 
1150 N N   . ILE A 160 ? 0.2181 0.2753 0.2716 0.0363  -0.0188 0.0116  452 ILE A N   
1151 C CA  . ILE A 160 ? 0.2636 0.3037 0.3050 0.0415  -0.0168 0.0050  452 ILE A CA  
1152 C C   . ILE A 160 ? 0.2564 0.2880 0.2809 0.0343  -0.0189 0.0022  452 ILE A C   
1153 O O   . ILE A 160 ? 0.2981 0.3155 0.3019 0.0375  -0.0137 -0.0048 452 ILE A O   
1154 C CB  . ILE A 160 ? 0.2479 0.2756 0.2951 0.0409  -0.0206 0.0046  452 ILE A CB  
1155 C CG1 . ILE A 160 ? 0.2673 0.3018 0.3245 0.0481  -0.0181 0.0064  452 ILE A CG1 
1156 C CG2 . ILE A 160 ? 0.2400 0.2453 0.2709 0.0392  -0.0209 -0.0011 452 ILE A CG2 
1157 C CD1 . ILE A 160 ? 0.2720 0.2986 0.3353 0.0459  -0.0214 0.0076  452 ILE A CD1 
1158 N N   . LEU A 161 ? 0.1986 0.2370 0.2286 0.0249  -0.0260 0.0086  453 LEU A N   
1159 C CA  . LEU A 161 ? 0.2308 0.2680 0.2456 0.0153  -0.0307 0.0091  453 LEU A CA  
1160 C C   . LEU A 161 ? 0.2280 0.2680 0.2246 0.0164  -0.0244 0.0053  453 LEU A C   
1161 O O   . LEU A 161 ? 0.2716 0.2987 0.2425 0.0110  -0.0238 -0.0014 453 LEU A O   
1162 C CB  . LEU A 161 ? 0.2084 0.2593 0.2370 0.0095  -0.0381 0.0214  453 LEU A CB  
1163 C CG  . LEU A 161 ? 0.2686 0.3283 0.2852 -0.0013 -0.0451 0.0275  453 LEU A CG  
1164 C CD1 . LEU A 161 ? 0.3112 0.3625 0.3111 -0.0122 -0.0510 0.0221  453 LEU A CD1 
1165 C CD2 . LEU A 161 ? 0.2045 0.2792 0.2393 -0.0009 -0.0504 0.0437  453 LEU A CD2 
1166 N N   . LEU A 162 ? 0.2482 0.3046 0.2549 0.0215  -0.0191 0.0095  454 LEU A N   
1167 C CA  . LEU A 162 ? 0.2647 0.3316 0.2574 0.0224  -0.0120 0.0090  454 LEU A CA  
1168 C C   . LEU A 162 ? 0.2638 0.3292 0.2484 0.0371  0.0011  0.0019  454 LEU A C   
1169 O O   . LEU A 162 ? 0.3184 0.3836 0.2823 0.0410  0.0102  -0.0021 454 LEU A O   
1170 C CB  . LEU A 162 ? 0.2197 0.3087 0.2271 0.0175  -0.0130 0.0203  454 LEU A CB  
1171 C CG  . LEU A 162 ? 0.2422 0.3295 0.2549 0.0073  -0.0228 0.0301  454 LEU A CG  
1172 C CD1 . LEU A 162 ? 0.3559 0.4513 0.3811 0.0027  -0.0227 0.0400  454 LEU A CD1 
1173 C CD2 . LEU A 162 ? 0.2336 0.3234 0.2269 -0.0004 -0.0261 0.0326  454 LEU A CD2 
1174 N N   . ASN A 163 ? 0.2717 0.3365 0.2709 0.0472  0.0035  0.0015  455 ASN A N   
1175 C CA  . ASN A 163 ? 0.3028 0.3729 0.2998 0.0654  0.0168  -0.0003 455 ASN A CA  
1176 C C   . ASN A 163 ? 0.3218 0.3539 0.2945 0.0757  0.0236  -0.0111 455 ASN A C   
1177 O O   . ASN A 163 ? 0.3286 0.3539 0.2856 0.0928  0.0386  -0.0146 455 ASN A O   
1178 C CB  . ASN A 163 ? 0.2225 0.3178 0.2478 0.0705  0.0155  0.0085  455 ASN A CB  
1179 C CG  . ASN A 163 ? 0.2337 0.3483 0.2635 0.0913  0.0291  0.0128  455 ASN A CG  
1180 O OD1 . ASN A 163 ? 0.2903 0.4325 0.3214 0.0966  0.0380  0.0182  455 ASN A OD1 
1181 N ND2 . ASN A 163 ? 0.2429 0.3458 0.2760 0.1046  0.0315  0.0126  455 ASN A ND2 
1182 N N   . SER A 164 ? 0.2870 0.2927 0.2546 0.0660  0.0142  -0.0157 456 SER A N   
1183 C CA  . SER A 164 ? 0.4528 0.4185 0.3977 0.0732  0.0198  -0.0243 456 SER A CA  
1184 C C   . SER A 164 ? 0.4182 0.3505 0.3204 0.0744  0.0298  -0.0360 456 SER A C   
1185 O O   . SER A 164 ? 0.4491 0.3472 0.3278 0.0900  0.0431  -0.0427 456 SER A O   
1186 C CB  . SER A 164 ? 0.5213 0.4707 0.4692 0.0576  0.0067  -0.0249 456 SER A CB  
1187 O OG  . SER A 164 ? 0.4193 0.3866 0.3970 0.0622  0.0027  -0.0170 456 SER A OG  
1188 N N   . GLY A 165 ? 0.4264 0.3645 0.3144 0.0587  0.0248  -0.0382 457 GLY A N   
1189 C CA  . GLY A 165 ? 0.4336 0.3381 0.2742 0.0556  0.0334  -0.0507 457 GLY A CA  
1190 C C   . GLY A 165 ? 0.4778 0.4022 0.3095 0.0664  0.0467  -0.0502 457 GLY A C   
1191 O O   . GLY A 165 ? 0.5720 0.4683 0.3596 0.0626  0.0548  -0.0613 457 GLY A O   
1192 N N   . VAL A 166 ? 0.4852 0.4570 0.3542 0.0776  0.0497  -0.0375 458 VAL A N   
1193 C CA  . VAL A 166 ? 0.4297 0.4294 0.2943 0.0837  0.0609  -0.0337 458 VAL A CA  
1194 C C   . VAL A 166 ? 0.4567 0.4432 0.2991 0.1117  0.0860  -0.0392 458 VAL A C   
1195 O O   . VAL A 166 ? 0.5770 0.5775 0.4035 0.1177  0.0991  -0.0393 458 VAL A O   
1196 C CB  . VAL A 166 ? 0.4287 0.4836 0.3387 0.0812  0.0544  -0.0168 458 VAL A CB  
1197 C CG1 . VAL A 166 ? 0.3579 0.4381 0.2953 0.1031  0.0646  -0.0085 458 VAL A CG1 
1198 C CG2 . VAL A 166 ? 0.3573 0.4401 0.2611 0.0738  0.0579  -0.0111 458 VAL A CG2 
1199 N N   . TYR A 167 ? 0.4859 0.4456 0.3260 0.1311  0.0948  -0.0424 459 TYR A N   
1200 C CA  . TYR A 167 ? 0.5863 0.5285 0.4045 0.1634  0.1215  -0.0458 459 TYR A CA  
1201 C C   . TYR A 167 ? 0.6580 0.5215 0.4138 0.1644  0.1320  -0.0661 459 TYR A C   
1202 O O   . TYR A 167 ? 0.8281 0.6597 0.5589 0.1944  0.1560  -0.0705 459 TYR A O   
1203 C CB  . TYR A 167 ? 0.4909 0.4556 0.3457 0.1887  0.1272  -0.0324 459 TYR A CB  
1204 C CG  . TYR A 167 ? 0.5870 0.6206 0.4981 0.1797  0.1123  -0.0139 459 TYR A CG  
1205 C CD1 . TYR A 167 ? 0.7152 0.8095 0.6506 0.1851  0.1190  -0.0002 459 TYR A CD1 
1206 C CD2 . TYR A 167 ? 0.5680 0.6040 0.5040 0.1639  0.0924  -0.0103 459 TYR A CD2 
1207 C CE1 . TYR A 167 ? 0.5541 0.7048 0.5341 0.1719  0.1047  0.0158  459 TYR A CE1 
1208 C CE2 . TYR A 167 ? 0.5663 0.6559 0.5447 0.1536  0.0798  0.0043  459 TYR A CE2 
1209 C CZ  . TYR A 167 ? 0.6240 0.7684 0.6226 0.1560  0.0853  0.0169  459 TYR A CZ  
1210 O OH  . TYR A 167 ? 0.4354 0.6266 0.4695 0.1408  0.0720  0.0306  459 TYR A OH  
1211 N N   . THR A 168 ? 0.6777 0.5086 0.4057 0.1322  0.1151  -0.0775 460 THR A N   
1212 C CA  . THR A 168 ? 0.8426 0.5952 0.5067 0.1244  0.1213  -0.0971 460 THR A CA  
1213 C C   . THR A 168 ? 0.8633 0.6041 0.4891 0.0910  0.1097  -0.1073 460 THR A C   
1214 O O   . THR A 168 ? 0.9668 0.6620 0.5559 0.0641  0.0978  -0.1185 460 THR A O   
1215 C CB  . THR A 168 ? 0.7983 0.5151 0.4651 0.1149  0.1091  -0.0988 460 THR A CB  
1216 O OG1 . THR A 168 ? 0.7109 0.4733 0.4240 0.0911  0.0828  -0.0873 460 THR A OG1 
1217 N N   . PHE A 169 ? 0.9617 0.7460 0.5947 0.0904  0.1125  -0.1018 461 PHE A N   
1218 C CA  . PHE A 169 ? 0.9370 0.7147 0.5319 0.0604  0.1025  -0.1090 461 PHE A CA  
1219 C C   . PHE A 169 ? 0.9918 0.7021 0.5078 0.0637  0.1235  -0.1308 461 PHE A C   
1220 O O   . PHE A 169 ? 1.2038 0.8954 0.7073 0.0969  0.1506  -0.1350 461 PHE A O   
1221 C CB  . PHE A 169 ? 0.8055 0.6502 0.4324 0.0584  0.0990  -0.0942 461 PHE A CB  
1222 C CG  . PHE A 169 ? 0.7813 0.6726 0.4575 0.0363  0.0715  -0.0778 461 PHE A CG  
1223 C CD1 . PHE A 169 ? 0.9156 0.7906 0.5954 0.0142  0.0505  -0.0784 461 PHE A CD1 
1224 C CD2 . PHE A 169 ? 0.9324 0.8822 0.6494 0.0382  0.0681  -0.0607 461 PHE A CD2 
1225 C CE1 . PHE A 169 ? 0.7327 0.6493 0.4568 -0.0009 0.0288  -0.0622 461 PHE A CE1 
1226 C CE2 . PHE A 169 ? 0.8700 0.8529 0.6265 0.0210  0.0458  -0.0459 461 PHE A CE2 
1227 C CZ  . PHE A 169 ? 0.6113 0.5777 0.3718 0.0038  0.0273  -0.0467 461 PHE A CZ  
1228 N N   . SER A 172 ? 0.9428 0.7779 0.4130 0.0982  0.1869  -0.1203 464 SER A N   
1229 C CA  . SER A 172 ? 0.9024 0.7593 0.3706 0.1197  0.2119  -0.1188 464 SER A CA  
1230 C C   . SER A 172 ? 1.0679 0.9555 0.5124 0.0977  0.2083  -0.1157 464 SER A C   
1231 O O   . SER A 172 ? 1.0368 0.9640 0.4919 0.1114  0.2261  -0.1077 464 SER A O   
1232 C CB  . SER A 172 ? 1.2206 1.0129 0.6480 0.1339  0.2294  -0.1376 464 SER A CB  
1233 O OG  . SER A 172 ? 1.3198 1.0600 0.6861 0.1034  0.2183  -0.1561 464 SER A OG  
1234 N N   . THR A 173 ? 1.1491 1.0211 0.5640 0.0619  0.1838  -0.1196 465 THR A N   
1235 C CA  . THR A 173 ? 1.0848 0.9858 0.4772 0.0383  0.1759  -0.1136 465 THR A CA  
1236 C C   . THR A 173 ? 0.9128 0.8860 0.3554 0.0397  0.1719  -0.0868 465 THR A C   
1237 O O   . THR A 173 ? 0.7931 0.7985 0.3013 0.0501  0.1638  -0.0725 465 THR A O   
1238 C CB  . THR A 173 ? 1.0902 0.9639 0.4510 -0.0020 0.1455  -0.1190 465 THR A CB  
1239 O OG1 . THR A 173 ? 0.9360 0.8449 0.3405 -0.0203 0.1200  -0.1006 465 THR A OG1 
1240 C CG2 . THR A 173 ? 1.2476 1.0522 0.5785 -0.0061 0.1427  -0.1401 465 THR A CG2 
1241 N N   . LEU A 174 ? 0.3790 0.7852 0.2754 -0.0325 0.0937  -0.0575 466 LEU A N   
1242 C CA  . LEU A 174 ? 0.5384 0.8930 0.3731 -0.0539 0.1005  -0.0290 466 LEU A CA  
1243 C C   . LEU A 174 ? 0.5568 0.8510 0.3695 -0.0318 0.0761  0.0020  466 LEU A C   
1244 O O   . LEU A 174 ? 0.5426 0.8017 0.3481 -0.0399 0.0778  0.0196  466 LEU A O   
1245 C CB  . LEU A 174 ? 0.6314 0.9743 0.3818 -0.0804 0.1131  -0.0216 466 LEU A CB  
1246 C CG  . LEU A 174 ? 0.7246 1.0081 0.4095 -0.1084 0.1226  0.0064  466 LEU A CG  
1247 C CD1 . LEU A 174 ? 0.7050 1.0040 0.4417 -0.1267 0.1423  -0.0048 466 LEU A CD1 
1248 C CD2 . LEU A 174 ? 0.6732 0.9344 0.2934 -0.1324 0.1325  0.0091  466 LEU A CD2 
1249 N N   . LYS A 175 ? 0.4957 0.7800 0.3018 -0.0039 0.0533  0.0051  467 LYS A N   
1250 C CA  . LYS A 175 ? 0.4724 0.7088 0.2730 0.0191  0.0299  0.0254  467 LYS A CA  
1251 C C   . LYS A 175 ? 0.4725 0.7161 0.3397 0.0284  0.0304  0.0199  467 LYS A C   
1252 O O   . LYS A 175 ? 0.5569 0.7602 0.4160 0.0297  0.0242  0.0382  467 LYS A O   
1253 C CB  . LYS A 175 ? 0.4373 0.6735 0.2336 0.0476  0.0068  0.0197  467 LYS A CB  
1254 C CG  . LYS A 175 ? 0.6864 0.8888 0.5007 0.0732  -0.0153 0.0283  467 LYS A CG  
1255 C CD  . LYS A 175 ? 0.7705 1.0091 0.6464 0.0981  -0.0228 0.0035  467 LYS A CD  
1256 C CE  . LYS A 175 ? 0.5890 0.8440 0.5284 0.0978  -0.0122 -0.0049 467 LYS A CE  
1257 N NZ  . LYS A 175 ? 0.5875 0.8586 0.5767 0.1203  -0.0213 -0.0233 467 LYS A NZ  
1258 N N   . SER A 176 ? 0.4607 0.7524 0.3918 0.0345  0.0363  -0.0054 468 SER A N   
1259 C CA  . SER A 176 ? 0.3479 0.6407 0.3343 0.0420  0.0341  -0.0097 468 SER A CA  
1260 C C   . SER A 176 ? 0.4140 0.6939 0.4009 0.0215  0.0458  -0.0016 468 SER A C   
1261 O O   . SER A 176 ? 0.4107 0.6676 0.4158 0.0265  0.0399  0.0067  468 SER A O   
1262 C CB  . SER A 176 ? 0.4397 0.7810 0.4893 0.0504  0.0355  -0.0379 468 SER A CB  
1263 O OG  . SER A 176 ? 0.7127 1.0630 0.7713 0.0716  0.0238  -0.0463 468 SER A OG  
1264 N N   . LEU A 177 ? 0.3689 0.6642 0.3355 -0.0032 0.0636  -0.0061 469 LEU A N   
1265 C CA  . LEU A 177 ? 0.3516 0.6365 0.3208 -0.0244 0.0762  -0.0019 469 LEU A CA  
1266 C C   . LEU A 177 ? 0.3759 0.6017 0.2912 -0.0287 0.0712  0.0296  469 LEU A C   
1267 O O   . LEU A 177 ? 0.3969 0.6032 0.3253 -0.0338 0.0722  0.0368  469 LEU A O   
1268 C CB  . LEU A 177 ? 0.4279 0.7498 0.3942 -0.0530 0.1002  -0.0211 469 LEU A CB  
1269 C CG  . LEU A 177 ? 0.5373 0.9225 0.5691 -0.0503 0.1051  -0.0586 469 LEU A CG  
1270 C CD1 . LEU A 177 ? 0.3660 0.7895 0.3880 -0.0805 0.1306  -0.0808 469 LEU A CD1 
1271 C CD2 . LEU A 177 ? 0.3841 0.7800 0.4850 -0.0416 0.0967  -0.0725 469 LEU A CD2 
1272 N N   . GLU A 178 ? 0.3940 0.5891 0.2495 -0.0257 0.0631  0.0473  470 GLU A N   
1273 C CA  . GLU A 178 ? 0.4367 0.5712 0.2447 -0.0256 0.0521  0.0762  470 GLU A CA  
1274 C C   . GLU A 178 ? 0.4071 0.5228 0.2476 0.0003  0.0330  0.0805  470 GLU A C   
1275 O O   . GLU A 178 ? 0.5119 0.5937 0.3483 -0.0026 0.0299  0.0945  470 GLU A O   
1276 C CB  . GLU A 178 ? 0.5045 0.6063 0.2405 -0.0254 0.0411  0.0925  470 GLU A CB  
1277 C CG  . GLU A 178 ? 0.5762 0.6760 0.2558 -0.0594 0.0618  0.0967  470 GLU A CG  
1278 C CD  . GLU A 178 ? 0.7055 0.7858 0.3175 -0.0569 0.0493  0.1057  470 GLU A CD  
1279 O OE1 . GLU A 178 ? 0.9008 0.9700 0.5158 -0.0258 0.0223  0.1072  470 GLU A OE1 
1280 O OE2 . GLU A 178 ? 0.7848 0.8606 0.3395 -0.0871 0.0665  0.1094  470 GLU A OE2 
1281 N N   . GLU A 179 ? 0.4551 0.5935 0.3286 0.0235  0.0219  0.0665  471 GLU A N   
1282 C CA  . GLU A 179 ? 0.4824 0.6060 0.3855 0.0440  0.0078  0.0664  471 GLU A CA  
1283 C C   . GLU A 179 ? 0.3599 0.4888 0.3025 0.0372  0.0156  0.0627  471 GLU A C   
1284 O O   . GLU A 179 ? 0.3545 0.4539 0.2984 0.0408  0.0094  0.0721  471 GLU A O   
1285 C CB  . GLU A 179 ? 0.3385 0.4894 0.2713 0.0654  -0.0009 0.0483  471 GLU A CB  
1286 C CG  . GLU A 179 ? 0.4167 0.5621 0.3137 0.0766  -0.0136 0.0489  471 GLU A CG  
1287 C CD  . GLU A 179 ? 0.5313 0.6406 0.4179 0.0966  -0.0355 0.0547  471 GLU A CD  
1288 O OE1 . GLU A 179 ? 0.4012 0.5258 0.3253 0.1153  -0.0429 0.0374  471 GLU A OE1 
1289 O OE2 . GLU A 179 ? 0.6822 0.7474 0.5257 0.0927  -0.0453 0.0742  471 GLU A OE2 
1290 N N   . LYS A 180 ? 0.3185 0.4849 0.2948 0.0281  0.0271  0.0467  472 LYS A N   
1291 C CA  . LYS A 180 ? 0.4434 0.6127 0.4564 0.0236  0.0293  0.0414  472 LYS A CA  
1292 C C   . LYS A 180 ? 0.3021 0.4447 0.2952 0.0070  0.0356  0.0551  472 LYS A C   
1293 O O   . LYS A 180 ? 0.3734 0.4960 0.3786 0.0089  0.0305  0.0601  472 LYS A O   
1294 C CB  . LYS A 180 ? 0.3908 0.6048 0.4468 0.0188  0.0355  0.0181  472 LYS A CB  
1295 C CG  . LYS A 180 ? 0.4726 0.7079 0.5615 0.0360  0.0267  0.0034  472 LYS A CG  
1296 C CD  . LYS A 180 ? 0.5380 0.8108 0.6763 0.0326  0.0277  -0.0204 472 LYS A CD  
1297 C CE  . LYS A 180 ? 0.5456 0.8565 0.7034 0.0406  0.0282  -0.0390 472 LYS A CE  
1298 N NZ  . LYS A 180 ? 0.5008 0.8238 0.6937 0.0331  0.0268  -0.0608 472 LYS A NZ  
1299 N N   A ASP A 181 ? 0.3505 0.4917 0.3111 -0.0114 0.0478  0.0606  473 ASP A N   
1300 C CA  A ASP A 181 ? 0.4162 0.5290 0.3557 -0.0296 0.0556  0.0737  473 ASP A CA  
1301 C C   A ASP A 181 ? 0.4362 0.4997 0.3482 -0.0192 0.0415  0.0953  473 ASP A C   
1302 O O   A ASP A 181 ? 0.4486 0.4914 0.3682 -0.0237 0.0409  0.1013  473 ASP A O   
1303 C CB  A ASP A 181 ? 0.4294 0.5449 0.3299 -0.0550 0.0735  0.0761  473 ASP A CB  
1304 C CG  A ASP A 181 ? 0.6565 0.7340 0.5263 -0.0757 0.0819  0.0928  473 ASP A CG  
1305 O OD1 A ASP A 181 ? 0.8454 0.8750 0.6652 -0.0742 0.0723  0.1168  473 ASP A OD1 
1306 O OD2 A ASP A 181 ? 0.6322 0.7268 0.5306 -0.0929 0.0963  0.0801  473 ASP A OD2 
1307 N N   . HIS A 182 ? 0.5178 0.5637 0.4020 -0.0042 0.0282  0.1038  474 HIS A N   
1308 C CA  . HIS A 182 ? 0.4233 0.4255 0.2898 0.0081  0.0117  0.1184  474 HIS A CA  
1309 C C   . HIS A 182 ? 0.3631 0.3695 0.2716 0.0219  0.0053  0.1093  474 HIS A C   
1310 O O   . HIS A 182 ? 0.4741 0.4522 0.3821 0.0220  0.0001  0.1167  474 HIS A O   
1311 C CB  . HIS A 182 ? 0.5503 0.5372 0.3860 0.0241  -0.0050 0.1231  474 HIS A CB  
1312 C CG  . HIS A 182 ? 0.5168 0.4625 0.3435 0.0399  -0.0259 0.1315  474 HIS A CG  
1313 N ND1 . HIS A 182 ? 0.7138 0.6124 0.5084 0.0312  -0.0322 0.1503  474 HIS A ND1 
1314 C CD2 . HIS A 182 ? 0.5307 0.4767 0.3812 0.0633  -0.0419 0.1200  474 HIS A CD2 
1315 C CE1 . HIS A 182 ? 0.6592 0.5316 0.4606 0.0505  -0.0537 0.1494  474 HIS A CE1 
1316 N NE2 . HIS A 182 ? 0.5887 0.4911 0.4250 0.0696  -0.0587 0.1296  474 HIS A NE2 
1317 N N   . ILE A 183 ? 0.4065 0.4458 0.3489 0.0318  0.0058  0.0927  475 ILE A N   
1318 C CA  . ILE A 183 ? 0.3467 0.3860 0.3201 0.0401  0.0018  0.0846  475 ILE A CA  
1319 C C   . ILE A 183 ? 0.3946 0.4273 0.3796 0.0269  0.0074  0.0870  475 ILE A C   
1320 O O   . ILE A 183 ? 0.3594 0.3720 0.3487 0.0288  0.0030  0.0890  475 ILE A O   
1321 C CB  . ILE A 183 ? 0.2895 0.3607 0.2922 0.0490  0.0021  0.0679  475 ILE A CB  
1322 C CG1 . ILE A 183 ? 0.3366 0.4120 0.3345 0.0652  -0.0056 0.0619  475 ILE A CG1 
1323 C CG2 . ILE A 183 ? 0.2399 0.3068 0.2663 0.0496  0.0008  0.0617  475 ILE A CG2 
1324 C CD1 . ILE A 183 ? 0.2998 0.4097 0.3244 0.0720  -0.0034 0.0453  475 ILE A CD1 
1325 N N   . HIS A 184 ? 0.3282 0.3800 0.3206 0.0131  0.0171  0.0833  476 HIS A N   
1326 C CA  . HIS A 184 ? 0.3968 0.4453 0.4054 0.0019  0.0204  0.0813  476 HIS A CA  
1327 C C   . HIS A 184 ? 0.3204 0.3373 0.3051 -0.0085 0.0233  0.0958  476 HIS A C   
1328 O O   . HIS A 184 ? 0.3291 0.3337 0.3251 -0.0125 0.0215  0.0958  476 HIS A O   
1329 C CB  . HIS A 184 ? 0.2998 0.3830 0.3333 -0.0091 0.0290  0.0660  476 HIS A CB  
1330 C CG  . HIS A 184 ? 0.3567 0.4650 0.4244 0.0011  0.0212  0.0497  476 HIS A CG  
1331 N ND1 . HIS A 184 ? 0.3456 0.4407 0.4280 0.0090  0.0088  0.0477  476 HIS A ND1 
1332 C CD2 . HIS A 184 ? 0.2444 0.3868 0.3322 0.0038  0.0231  0.0347  476 HIS A CD2 
1333 C CE1 . HIS A 184 ? 0.3219 0.4371 0.4301 0.0160  0.0019  0.0342  476 HIS A CE1 
1334 N NE2 . HIS A 184 ? 0.4116 0.5580 0.5278 0.0141  0.0102  0.0248  476 HIS A NE2 
1335 N N   . ARG A 185 ? 0.3446 0.3448 0.2941 -0.0132 0.0259  0.1084  477 ARG A N   
1336 C CA  . ARG A 185 ? 0.3999 0.3616 0.3238 -0.0221 0.0253  0.1242  477 ARG A CA  
1337 C C   . ARG A 185 ? 0.3981 0.3332 0.3251 -0.0065 0.0103  0.1280  477 ARG A C   
1338 O O   . ARG A 185 ? 0.4253 0.3386 0.3550 -0.0118 0.0091  0.1325  477 ARG A O   
1339 C CB  . ARG A 185 ? 0.5377 0.4786 0.4143 -0.0314 0.0279  0.1388  477 ARG A CB  
1340 C CG  . ARG A 185 ? 0.5830 0.5453 0.4496 -0.0558 0.0485  0.1344  477 ARG A CG  
1341 C CD  . ARG A 185 ? 0.6824 0.6688 0.5892 -0.0696 0.0618  0.1192  477 ARG A CD  
1342 N NE  . ARG A 185 ? 0.7449 0.7817 0.6891 -0.0693 0.0686  0.0959  477 ARG A NE  
1343 N N   . VAL A 186 ? 0.4646 0.4043 0.3951 0.0118  -0.0001 0.1227  478 VAL A N   
1344 C CA  . VAL A 186 ? 0.4655 0.3872 0.4057 0.0249  -0.0118 0.1191  478 VAL A CA  
1345 C C   . VAL A 186 ? 0.3926 0.3258 0.3603 0.0225  -0.0077 0.1084  478 VAL A C   
1346 O O   . VAL A 186 ? 0.4101 0.3257 0.3834 0.0228  -0.0115 0.1068  478 VAL A O   
1347 C CB  . VAL A 186 ? 0.5364 0.4639 0.4776 0.0435  -0.0224 0.1110  478 VAL A CB  
1348 C CG1 . VAL A 186 ? 0.3666 0.2828 0.3260 0.0548  -0.0314 0.0996  478 VAL A CG1 
1349 C CG2 . VAL A 186 ? 0.4464 0.3546 0.3529 0.0470  -0.0320 0.1229  478 VAL A CG2 
1350 N N   . LEU A 187 ? 0.3514 0.3120 0.3350 0.0198  -0.0017 0.1001  479 LEU A N   
1351 C CA  . LEU A 187 ? 0.3269 0.2907 0.3278 0.0166  -0.0018 0.0922  479 LEU A CA  
1352 C C   . LEU A 187 ? 0.3236 0.2748 0.3260 0.0049  0.0000  0.0963  479 LEU A C   
1353 O O   . LEU A 187 ? 0.3476 0.2868 0.3542 0.0036  -0.0036 0.0928  479 LEU A O   
1354 C CB  . LEU A 187 ? 0.2921 0.2816 0.3090 0.0167  -0.0008 0.0833  479 LEU A CB  
1355 C CG  . LEU A 187 ? 0.2390 0.2388 0.2610 0.0270  -0.0029 0.0752  479 LEU A CG  
1356 C CD1 . LEU A 187 ? 0.2103 0.2348 0.2500 0.0271  -0.0035 0.0673  479 LEU A CD1 
1357 C CD2 . LEU A 187 ? 0.2528 0.2358 0.2727 0.0268  -0.0052 0.0703  479 LEU A CD2 
1358 N N   . ASP A 188 ? 0.3211 0.2758 0.3199 -0.0056 0.0068  0.1017  480 ASP A N   
1359 C CA  . ASP A 188 ? 0.3008 0.2442 0.3043 -0.0180 0.0103  0.1034  480 ASP A CA  
1360 C C   . ASP A 188 ? 0.4669 0.3785 0.4587 -0.0163 0.0054  0.1115  480 ASP A C   
1361 O O   . ASP A 188 ? 0.4616 0.3637 0.4635 -0.0210 0.0039  0.1082  480 ASP A O   
1362 C CB  . ASP A 188 ? 0.3092 0.2616 0.3084 -0.0335 0.0228  0.1057  480 ASP A CB  
1363 C CG  . ASP A 188 ? 0.4609 0.4500 0.4855 -0.0374 0.0275  0.0898  480 ASP A CG  
1364 O OD1 . ASP A 188 ? 0.3688 0.3692 0.4146 -0.0282 0.0176  0.0792  480 ASP A OD1 
1365 O OD2 . ASP A 188 ? 0.3780 0.3828 0.4004 -0.0509 0.0406  0.0867  480 ASP A OD2 
1366 N N   . LYS A 189 ? 0.4402 0.3351 0.4131 -0.0085 0.0005  0.1199  481 LYS A N   
1367 C CA  . LYS A 189 ? 0.3763 0.2402 0.3438 -0.0048 -0.0079 0.1243  481 LYS A CA  
1368 C C   . LYS A 189 ? 0.3804 0.2476 0.3655 0.0043  -0.0135 0.1104  481 LYS A C   
1369 O O   . LYS A 189 ? 0.3861 0.2364 0.3782 0.0031  -0.0175 0.1074  481 LYS A O   
1370 C CB  . LYS A 189 ? 0.4220 0.2640 0.3658 0.0034  -0.0174 0.1346  481 LYS A CB  
1371 C CG  . LYS A 189 ? 0.5218 0.3300 0.4657 0.0109  -0.0318 0.1359  481 LYS A CG  
1372 C CD  . LYS A 189 ? 0.6680 0.4464 0.6023 -0.0039 -0.0298 0.1484  481 LYS A CD  
1373 C CE  . LYS A 189 ? 0.7528 0.5050 0.6474 -0.0137 -0.0296 0.1682  481 LYS A CE  
1374 N NZ  . LYS A 189 ? 0.7954 0.5330 0.6824 -0.0351 -0.0159 0.1755  481 LYS A NZ  
1375 N N   . ILE A 190 ? 0.3564 0.2444 0.3478 0.0110  -0.0126 0.1006  482 ILE A N   
1376 C CA  . ILE A 190 ? 0.3144 0.2050 0.3158 0.0127  -0.0132 0.0866  482 ILE A CA  
1377 C C   . ILE A 190 ? 0.4363 0.3265 0.4413 0.0018  -0.0110 0.0848  482 ILE A C   
1378 O O   . ILE A 190 ? 0.4016 0.2829 0.4091 -0.0014 -0.0122 0.0765  482 ILE A O   
1379 C CB  . ILE A 190 ? 0.3188 0.2275 0.3219 0.0187  -0.0109 0.0775  482 ILE A CB  
1380 C CG1 . ILE A 190 ? 0.3232 0.2342 0.3264 0.0315  -0.0154 0.0758  482 ILE A CG1 
1381 C CG2 . ILE A 190 ? 0.2690 0.1763 0.2745 0.0146  -0.0080 0.0630  482 ILE A CG2 
1382 C CD1 . ILE A 190 ? 0.4210 0.3533 0.4284 0.0368  -0.0119 0.0679  482 ILE A CD1 
1383 N N   . THR A 191 ? 0.3148 0.2160 0.3221 -0.0040 -0.0090 0.0892  483 THR A N   
1384 C CA  . THR A 191 ? 0.3238 0.2242 0.3382 -0.0121 -0.0114 0.0849  483 THR A CA  
1385 C C   . THR A 191 ? 0.3112 0.1962 0.3305 -0.0181 -0.0108 0.0866  483 THR A C   
1386 O O   . THR A 191 ? 0.3947 0.2724 0.4167 -0.0214 -0.0147 0.0794  483 THR A O   
1387 C CB  . THR A 191 ? 0.3642 0.2832 0.3899 -0.0156 -0.0111 0.0836  483 THR A CB  
1388 O OG1 . THR A 191 ? 0.3553 0.2871 0.3797 -0.0093 -0.0138 0.0806  483 THR A OG1 
1389 C CG2 . THR A 191 ? 0.3508 0.2686 0.3885 -0.0212 -0.0182 0.0754  483 THR A CG2 
1390 N N   . ASP A 192 ? 0.3341 0.2110 0.3514 -0.0208 -0.0064 0.0964  484 ASP A N   
1391 C CA  . ASP A 192 ? 0.4243 0.2805 0.4455 -0.0268 -0.0066 0.0992  484 ASP A CA  
1392 C C   . ASP A 192 ? 0.4228 0.2658 0.4463 -0.0196 -0.0134 0.0919  484 ASP A C   
1393 O O   . ASP A 192 ? 0.4214 0.2554 0.4553 -0.0239 -0.0154 0.0856  484 ASP A O   
1394 C CB  . ASP A 192 ? 0.3906 0.2305 0.3984 -0.0320 -0.0025 0.1139  484 ASP A CB  
1395 C CG  . ASP A 192 ? 0.4685 0.3248 0.4752 -0.0443 0.0090  0.1166  484 ASP A CG  
1396 O OD1 . ASP A 192 ? 0.4601 0.3407 0.4855 -0.0471 0.0112  0.1047  484 ASP A OD1 
1397 O OD2 . ASP A 192 ? 0.5559 0.3996 0.5420 -0.0518 0.0148  0.1290  484 ASP A OD2 
1398 N N   . THR A 193 ? 0.4101 0.2550 0.4281 -0.0091 -0.0166 0.0888  485 THR A N   
1399 C CA  . THR A 193 ? 0.5201 0.3585 0.5467 -0.0032 -0.0214 0.0751  485 THR A CA  
1400 C C   . THR A 193 ? 0.4271 0.2754 0.4549 -0.0096 -0.0179 0.0607  485 THR A C   
1401 O O   . THR A 193 ? 0.5186 0.3610 0.5558 -0.0123 -0.0193 0.0485  485 THR A O   
1402 C CB  . THR A 193 ? 0.4697 0.3125 0.4952 0.0090  -0.0248 0.0702  485 THR A CB  
1403 O OG1 . THR A 193 ? 0.4752 0.3019 0.4922 0.0152  -0.0321 0.0846  485 THR A OG1 
1404 C CG2 . THR A 193 ? 0.4437 0.2858 0.4863 0.0140  -0.0282 0.0487  485 THR A CG2 
1405 N N   . LEU A 194 ? 0.3840 0.2448 0.4001 -0.0127 -0.0150 0.0615  486 LEU A N   
1406 C CA  . LEU A 194 ? 0.4539 0.3151 0.4592 -0.0207 -0.0146 0.0512  486 LEU A CA  
1407 C C   . LEU A 194 ? 0.4121 0.2662 0.4224 -0.0274 -0.0190 0.0499  486 LEU A C   
1408 O O   . LEU A 194 ? 0.4510 0.3000 0.4567 -0.0334 -0.0196 0.0380  486 LEU A O   
1409 C CB  . LEU A 194 ? 0.4150 0.2828 0.4049 -0.0219 -0.0157 0.0554  486 LEU A CB  
1410 C CG  . LEU A 194 ? 0.4616 0.3333 0.4395 -0.0217 -0.0098 0.0484  486 LEU A CG  
1411 C CD1 . LEU A 194 ? 0.3607 0.2344 0.3258 -0.0225 -0.0137 0.0548  486 LEU A CD1 
1412 C CD2 . LEU A 194 ? 0.3653 0.2294 0.3299 -0.0322 -0.0043 0.0327  486 LEU A CD2 
1413 N N   . ILE A 195 ? 0.4118 0.2676 0.4328 -0.0280 -0.0210 0.0593  487 ILE A N   
1414 C CA  . ILE A 195 ? 0.3364 0.1883 0.3687 -0.0342 -0.0249 0.0550  487 ILE A CA  
1415 C C   . ILE A 195 ? 0.3859 0.2266 0.4313 -0.0354 -0.0234 0.0500  487 ILE A C   
1416 O O   . ILE A 195 ? 0.4223 0.2599 0.4726 -0.0400 -0.0267 0.0388  487 ILE A O   
1417 C CB  . ILE A 195 ? 0.4363 0.2966 0.4831 -0.0370 -0.0237 0.0613  487 ILE A CB  
1418 C CG1 . ILE A 195 ? 0.4626 0.3354 0.5050 -0.0350 -0.0302 0.0592  487 ILE A CG1 
1419 C CG2 . ILE A 195 ? 0.4401 0.2972 0.5066 -0.0440 -0.0249 0.0544  487 ILE A CG2 
1420 C CD1 . ILE A 195 ? 0.4622 0.3294 0.4978 -0.0361 -0.0441 0.0487  487 ILE A CD1 
1421 N N   . HIS A 196 ? 0.4582 0.2907 0.5092 -0.0307 -0.0210 0.0572  488 HIS A N   
1422 C CA  . HIS A 196 ? 0.4407 0.2582 0.5074 -0.0298 -0.0238 0.0518  488 HIS A CA  
1423 C C   . HIS A 196 ? 0.5119 0.3344 0.5820 -0.0287 -0.0250 0.0314  488 HIS A C   
1424 O O   . HIS A 196 ? 0.4591 0.2768 0.5454 -0.0316 -0.0274 0.0192  488 HIS A O   
1425 C CB  . HIS A 196 ? 0.4247 0.2259 0.4908 -0.0230 -0.0268 0.0640  488 HIS A CB  
1426 C CG  . HIS A 196 ? 0.6319 0.4136 0.7157 -0.0184 -0.0354 0.0565  488 HIS A CG  
1427 N ND1 . HIS A 196 ? 0.6652 0.4242 0.7594 -0.0240 -0.0385 0.0632  488 HIS A ND1 
1428 C CD2 . HIS A 196 ? 0.6041 0.3857 0.7013 -0.0088 -0.0423 0.0399  488 HIS A CD2 
1429 C CE1 . HIS A 196 ? 0.5720 0.3150 0.6847 -0.0165 -0.0498 0.0528  488 HIS A CE1 
1430 N NE2 . HIS A 196 ? 0.6693 0.4280 0.7867 -0.0067 -0.0525 0.0366  488 HIS A NE2 
1431 N N   . LEU A 197 ? 0.4518 0.2852 0.5076 -0.0266 -0.0215 0.0251  489 LEU A N   
1432 C CA  . LEU A 197 ? 0.4134 0.2540 0.4682 -0.0311 -0.0177 0.0025  489 LEU A CA  
1433 C C   . LEU A 197 ? 0.4113 0.2526 0.4509 -0.0427 -0.0176 -0.0043 489 LEU A C   
1434 O O   . LEU A 197 ? 0.5754 0.4193 0.6194 -0.0492 -0.0154 -0.0239 489 LEU A O   
1435 C CB  . LEU A 197 ? 0.3972 0.2481 0.4376 -0.0303 -0.0110 -0.0029 489 LEU A CB  
1436 C CG  . LEU A 197 ? 0.4254 0.2787 0.4841 -0.0175 -0.0131 -0.0061 489 LEU A CG  
1437 C CD1 . LEU A 197 ? 0.3645 0.2294 0.4082 -0.0170 -0.0060 -0.0070 489 LEU A CD1 
1438 C CD2 . LEU A 197 ? 0.4212 0.2775 0.5089 -0.0150 -0.0147 -0.0327 489 LEU A CD2 
1439 N N   . MET A 198 ? 0.4762 0.3156 0.4991 -0.0450 -0.0217 0.0091  490 MET A N   
1440 C CA  . MET A 198 ? 0.3951 0.2307 0.4005 -0.0535 -0.0276 0.0029  490 MET A CA  
1441 C C   . MET A 198 ? 0.5333 0.3671 0.5638 -0.0542 -0.0325 -0.0026 490 MET A C   
1442 O O   . MET A 198 ? 0.4710 0.3034 0.4946 -0.0610 -0.0357 -0.0169 490 MET A O   
1443 C CB  . MET A 198 ? 0.3966 0.2294 0.3824 -0.0528 -0.0356 0.0155  490 MET A CB  
1444 C CG  . MET A 198 ? 0.4138 0.2420 0.3652 -0.0568 -0.0332 0.0171  490 MET A CG  
1445 S SD  . MET A 198 ? 0.5064 0.3311 0.4464 -0.0517 -0.0457 0.0318  490 MET A SD  
1446 C CE  . MET A 198 ? 0.4008 0.2277 0.3239 -0.0521 -0.0343 0.0357  490 MET A CE  
1447 N N   . ALA A 199 ? 0.5431 0.3756 0.6003 -0.0492 -0.0323 0.0078  491 ALA A N   
1448 C CA  . ALA A 199 ? 0.5605 0.3892 0.6448 -0.0517 -0.0346 0.0018  491 ALA A CA  
1449 C C   . ALA A 199 ? 0.6040 0.4296 0.7049 -0.0515 -0.0330 -0.0133 491 ALA A C   
1450 O O   . ALA A 199 ? 0.6332 0.4595 0.7493 -0.0556 -0.0359 -0.0277 491 ALA A O   
1451 C CB  . ALA A 199 ? 0.4555 0.2789 0.5582 -0.0511 -0.0315 0.0171  491 ALA A CB  
1452 N N   . LYS A 200 ? 0.5414 0.3655 0.6441 -0.0459 -0.0298 -0.0138 492 LYS A N   
1453 C CA  . LYS A 200 ? 0.4937 0.3179 0.6198 -0.0439 -0.0306 -0.0339 492 LYS A CA  
1454 C C   . LYS A 200 ? 0.6718 0.5106 0.7867 -0.0531 -0.0258 -0.0590 492 LYS A C   
1455 O O   . LYS A 200 ? 0.6226 0.4667 0.7624 -0.0543 -0.0259 -0.0821 492 LYS A O   
1456 C CB  . LYS A 200 ? 0.5513 0.3721 0.6846 -0.0338 -0.0316 -0.0322 492 LYS A CB  
1457 C CG  . LYS A 200 ? 0.7567 0.5597 0.9235 -0.0251 -0.0421 -0.0347 492 LYS A CG  
1458 C CD  . LYS A 200 ? 0.7307 0.5321 0.9062 -0.0129 -0.0478 -0.0408 492 LYS A CD  
1459 C CE  . LYS A 200 ? 0.7862 0.6030 0.9932 -0.0110 -0.0490 -0.0780 492 LYS A CE  
1460 N NZ  . LYS A 200 ? 0.9067 0.7262 1.1292 0.0021  -0.0560 -0.0900 492 LYS A NZ  
1461 N N   . ALA A 201 ? 0.5999 0.4429 0.6761 -0.0607 -0.0224 -0.0558 493 ALA A N   
1462 C CA  . ALA A 201 ? 0.5585 0.4087 0.6091 -0.0741 -0.0170 -0.0766 493 ALA A CA  
1463 C C   . ALA A 201 ? 0.6250 0.4713 0.6641 -0.0807 -0.0251 -0.0806 493 ALA A C   
1464 O O   . ALA A 201 ? 0.6608 0.5088 0.6706 -0.0936 -0.0224 -0.0970 493 ALA A O   
1465 C CB  . ALA A 201 ? 0.4612 0.3095 0.4676 -0.0812 -0.0105 -0.0703 493 ALA A CB  
1466 N N   . GLY A 202 ? 0.5431 0.3840 0.6031 -0.0736 -0.0346 -0.0682 494 GLY A N   
1467 C CA  . GLY A 202 ? 0.5329 0.3724 0.5909 -0.0774 -0.0445 -0.0755 494 GLY A CA  
1468 C C   . GLY A 202 ? 0.6530 0.4843 0.6809 -0.0770 -0.0566 -0.0627 494 GLY A C   
1469 O O   . GLY A 202 ? 0.6663 0.4960 0.6947 -0.0778 -0.0690 -0.0706 494 GLY A O   
1470 N N   . LEU A 203 ? 0.5297 0.3559 0.5351 -0.0744 -0.0559 -0.0458 495 LEU A N   
1471 C CA  . LEU A 203 ? 0.5683 0.3854 0.5500 -0.0721 -0.0712 -0.0359 495 LEU A CA  
1472 C C   . LEU A 203 ? 0.5559 0.3803 0.5782 -0.0644 -0.0787 -0.0333 495 LEU A C   
1473 O O   . LEU A 203 ? 0.4601 0.2925 0.5174 -0.0613 -0.0680 -0.0269 495 LEU A O   
1474 C CB  . LEU A 203 ? 0.5520 0.3641 0.5091 -0.0706 -0.0677 -0.0202 495 LEU A CB  
1475 C CG  . LEU A 203 ? 0.5705 0.3665 0.4709 -0.0814 -0.0680 -0.0208 495 LEU A CG  
1476 C CD1 . LEU A 203 ? 0.6709 0.4722 0.5621 -0.0933 -0.0512 -0.0377 495 LEU A CD1 
1477 C CD2 . LEU A 203 ? 0.5119 0.3045 0.3991 -0.0782 -0.0648 -0.0053 495 LEU A CD2 
1478 N N   . THR A 204 ? 0.5512 0.3711 0.5673 -0.0626 -0.0980 -0.0401 496 THR A N   
1479 C CA  . THR A 204 ? 0.5970 0.4282 0.6556 -0.0567 -0.1046 -0.0434 496 THR A CA  
1480 C C   . THR A 204 ? 0.5572 0.3940 0.6226 -0.0520 -0.1019 -0.0295 496 THR A C   
1481 O O   . THR A 204 ? 0.5362 0.3652 0.5698 -0.0511 -0.1009 -0.0174 496 THR A O   
1482 C CB  . THR A 204 ? 0.7302 0.5565 0.7845 -0.0535 -0.1303 -0.0592 496 THR A CB  
1483 O OG1 . THR A 204 ? 0.6347 0.4468 0.6556 -0.0485 -0.1501 -0.0526 496 THR A OG1 
1484 C CG2 . THR A 204 ? 0.6623 0.4794 0.6908 -0.0596 -0.1351 -0.0721 496 THR A CG2 
1485 N N   . LEU A 205 ? 0.4349 0.3958 0.7678 -0.0723 -0.0788 -0.0520 497 LEU A N   
1486 C CA  . LEU A 205 ? 0.4801 0.4444 0.8007 -0.0624 -0.0677 -0.0158 497 LEU A CA  
1487 C C   . LEU A 205 ? 0.5050 0.5025 0.7950 -0.0528 -0.0676 -0.0101 497 LEU A C   
1488 O O   . LEU A 205 ? 0.4729 0.4679 0.7368 -0.0389 -0.0570 0.0058  497 LEU A O   
1489 C CB  . LEU A 205 ? 0.4070 0.3734 0.7659 -0.0768 -0.0627 0.0043  497 LEU A CB  
1490 C CG  . LEU A 205 ? 0.5226 0.4804 0.8705 -0.0745 -0.0457 0.0382  497 LEU A CG  
1491 C CD1 . LEU A 205 ? 0.4923 0.4122 0.8223 -0.0672 -0.0464 0.0486  497 LEU A CD1 
1492 C CD2 . LEU A 205 ? 0.4626 0.4248 0.8502 -0.0946 -0.0383 0.0549  497 LEU A CD2 
1493 N N   . GLN A 206 ? 0.4612 0.4895 0.7570 -0.0619 -0.0816 -0.0217 498 GLN A N   
1494 C CA  . GLN A 206 ? 0.3997 0.4574 0.6750 -0.0535 -0.0873 -0.0123 498 GLN A CA  
1495 C C   . GLN A 206 ? 0.3976 0.4461 0.6250 -0.0424 -0.0865 -0.0213 498 GLN A C   
1496 O O   . GLN A 206 ? 0.3250 0.3789 0.5340 -0.0284 -0.0811 -0.0060 498 GLN A O   
1497 C CB  . GLN A 206 ? 0.3339 0.4272 0.6266 -0.0696 -0.1101 -0.0181 498 GLN A CB  
1498 C CG  . GLN A 206 ? 0.4013 0.5257 0.6890 -0.0624 -0.1220 0.0005  498 GLN A CG  
1499 C CD  . GLN A 206 ? 0.4605 0.6217 0.7626 -0.0819 -0.1527 -0.0004 498 GLN A CD  
1500 O OE1 . GLN A 206 ? 0.4538 0.6174 0.7552 -0.1028 -0.1641 -0.0225 498 GLN A OE1 
1501 N NE2 . GLN A 206 ? 0.3345 0.5248 0.6541 -0.0765 -0.1683 0.0241  498 GLN A NE2 
1502 N N   . GLN A 207 ? 0.3721 0.4072 0.5845 -0.0496 -0.0893 -0.0491 499 GLN A N   
1503 C CA  . GLN A 207 ? 0.3631 0.3922 0.5357 -0.0414 -0.0848 -0.0609 499 GLN A CA  
1504 C C   . GLN A 207 ? 0.4259 0.4273 0.5952 -0.0224 -0.0698 -0.0474 499 GLN A C   
1505 O O   . GLN A 207 ? 0.3709 0.3731 0.5105 -0.0116 -0.0654 -0.0445 499 GLN A O   
1506 C CB  . GLN A 207 ? 0.4202 0.4447 0.5872 -0.0559 -0.0858 -0.1010 499 GLN A CB  
1507 C CG  . GLN A 207 ? 0.3931 0.4503 0.5436 -0.0806 -0.1026 -0.1182 499 GLN A CG  
1508 C CD  . GLN A 207 ? 0.7137 0.7673 0.8572 -0.0991 -0.0976 -0.1670 499 GLN A CD  
1509 O OE1 . GLN A 207 ? 0.5478 0.5734 0.7322 -0.0984 -0.0881 -0.1887 499 GLN A OE1 
1510 N NE2 . GLN A 207 ? 0.6309 0.7130 0.7247 -0.1180 -0.1033 -0.1851 499 GLN A NE2 
1511 N N   . GLN A 208 ? 0.3771 0.3549 0.5755 -0.0210 -0.0640 -0.0367 500 GLN A N   
1512 C CA  . GLN A 208 ? 0.3291 0.2833 0.5201 -0.0080 -0.0550 -0.0190 500 GLN A CA  
1513 C C   . GLN A 208 ? 0.3229 0.2905 0.4901 0.0007  -0.0471 0.0039  500 GLN A C   
1514 O O   . GLN A 208 ? 0.3853 0.3473 0.5263 0.0119  -0.0426 0.0080  500 GLN A O   
1515 C CB  . GLN A 208 ? 0.3563 0.2843 0.5809 -0.0145 -0.0545 -0.0057 500 GLN A CB  
1516 C CG  . GLN A 208 ? 0.3539 0.2596 0.6160 -0.0199 -0.0610 -0.0292 500 GLN A CG  
1517 C CD  . GLN A 208 ? 0.4452 0.3249 0.7488 -0.0295 -0.0640 -0.0101 500 GLN A CD  
1518 O OE1 . GLN A 208 ? 0.4457 0.3166 0.7398 -0.0303 -0.0612 0.0245  500 GLN A OE1 
1519 N NE2 . GLN A 208 ? 0.4499 0.3174 0.7981 -0.0403 -0.0695 -0.0328 500 GLN A NE2 
1520 N N   . HIS A 209 ? 0.3425 0.3287 0.5257 -0.0050 -0.0439 0.0160  501 HIS A N   
1521 C CA  . HIS A 209 ? 0.3645 0.3647 0.5382 0.0029  -0.0325 0.0308  501 HIS A CA  
1522 C C   . HIS A 209 ? 0.3509 0.3663 0.5065 0.0124  -0.0391 0.0259  501 HIS A C   
1523 O O   . HIS A 209 ? 0.3263 0.3396 0.4648 0.0228  -0.0301 0.0323  501 HIS A O   
1524 C CB  . HIS A 209 ? 0.4264 0.4479 0.6370 -0.0053 -0.0259 0.0397  501 HIS A CB  
1525 C CG  . HIS A 209 ? 0.5553 0.5644 0.7846 -0.0193 -0.0187 0.0477  501 HIS A CG  
1526 N ND1 . HIS A 209 ? 0.4169 0.4445 0.6883 -0.0320 -0.0167 0.0508  501 HIS A ND1 
1527 C CD2 . HIS A 209 ? 0.4110 0.3912 0.6262 -0.0246 -0.0153 0.0573  501 HIS A CD2 
1528 C CE1 . HIS A 209 ? 0.3589 0.3684 0.6381 -0.0455 -0.0098 0.0613  501 HIS A CE1 
1529 N NE2 . HIS A 209 ? 0.4862 0.4659 0.7314 -0.0414 -0.0105 0.0675  501 HIS A NE2 
1530 N N   . GLN A 210 ? 0.3115 0.3425 0.4688 0.0056  -0.0556 0.0152  502 GLN A N   
1531 C CA  . GLN A 210 ? 0.3109 0.3578 0.4479 0.0093  -0.0650 0.0170  502 GLN A CA  
1532 C C   . GLN A 210 ? 0.3561 0.3859 0.4563 0.0170  -0.0588 0.0089  502 GLN A C   
1533 O O   . GLN A 210 ? 0.3608 0.3927 0.4472 0.0260  -0.0561 0.0185  502 GLN A O   
1534 C CB  . GLN A 210 ? 0.2964 0.3666 0.4329 -0.0070 -0.0862 0.0090  502 GLN A CB  
1535 C CG  . GLN A 210 ? 0.2875 0.3839 0.4666 -0.0131 -0.0988 0.0237  502 GLN A CG  
1536 C CD  . GLN A 210 ? 0.3079 0.4299 0.4817 -0.0342 -0.1251 0.0171  502 GLN A CD  
1537 O OE1 . GLN A 210 ? 0.3445 0.4637 0.4791 -0.0470 -0.1292 -0.0044 502 GLN A OE1 
1538 N NE2 . GLN A 210 ? 0.3105 0.4604 0.5259 -0.0401 -0.1427 0.0337  502 GLN A NE2 
1539 N N   . ARG A 211 ? 0.2978 0.3106 0.3911 0.0137  -0.0563 -0.0094 503 ARG A N   
1540 C CA  . ARG A 211 ? 0.3180 0.3183 0.3885 0.0211  -0.0501 -0.0188 503 ARG A CA  
1541 C C   . ARG A 211 ? 0.3036 0.2863 0.3709 0.0340  -0.0405 -0.0031 503 ARG A C   
1542 O O   . ARG A 211 ? 0.3468 0.3274 0.3947 0.0415  -0.0368 -0.0021 503 ARG A O   
1543 C CB  . ARG A 211 ? 0.3040 0.2920 0.3856 0.0153  -0.0490 -0.0454 503 ARG A CB  
1544 C CG  . ARG A 211 ? 0.2893 0.2703 0.3597 0.0221  -0.0415 -0.0593 503 ARG A CG  
1545 C CD  . ARG A 211 ? 0.3057 0.2773 0.4029 0.0168  -0.0374 -0.0919 503 ARG A CD  
1546 N NE  . ARG A 211 ? 0.3054 0.2737 0.4058 0.0241  -0.0281 -0.1070 503 ARG A NE  
1547 C CZ  . ARG A 211 ? 0.3170 0.3057 0.3947 0.0153  -0.0188 -0.1307 503 ARG A CZ  
1548 N NH1 . ARG A 211 ? 0.3339 0.3473 0.3760 -0.0031 -0.0211 -0.1388 503 ARG A NH1 
1549 N NH2 . ARG A 211 ? 0.3161 0.3029 0.4076 0.0224  -0.0080 -0.1449 503 ARG A NH2 
1550 N N   . LEU A 212 ? 0.3119 0.2835 0.3950 0.0332  -0.0363 0.0090  504 LEU A N   
1551 C CA  . LEU A 212 ? 0.3034 0.2634 0.3734 0.0388  -0.0272 0.0240  504 LEU A CA  
1552 C C   . LEU A 212 ? 0.3500 0.3238 0.4092 0.0449  -0.0195 0.0292  504 LEU A C   
1553 O O   . LEU A 212 ? 0.3417 0.3083 0.3810 0.0508  -0.0143 0.0309  504 LEU A O   
1554 C CB  . LEU A 212 ? 0.2848 0.2366 0.3673 0.0298  -0.0221 0.0378  504 LEU A CB  
1555 C CG  . LEU A 212 ? 0.3145 0.2585 0.3730 0.0275  -0.0114 0.0527  504 LEU A CG  
1556 C CD1 . LEU A 212 ? 0.2910 0.2166 0.3317 0.0315  -0.0208 0.0562  504 LEU A CD1 
1557 C CD2 . LEU A 212 ? 0.3056 0.2473 0.3716 0.0123  -0.0037 0.0678  504 LEU A CD2 
1558 N N   . ALA A 213 ? 0.2887 0.2820 0.3684 0.0432  -0.0206 0.0318  505 ALA A N   
1559 C CA  . ALA A 213 ? 0.2617 0.2665 0.3489 0.0505  -0.0153 0.0375  505 ALA A CA  
1560 C C   . ALA A 213 ? 0.3220 0.3270 0.3893 0.0554  -0.0238 0.0360  505 ALA A C   
1561 O O   . ALA A 213 ? 0.2860 0.2855 0.3475 0.0625  -0.0164 0.0383  505 ALA A O   
1562 C CB  . ALA A 213 ? 0.3064 0.3342 0.4348 0.0479  -0.0202 0.0440  505 ALA A CB  
1563 N N   . GLN A 214 ? 0.2794 0.2915 0.3355 0.0486  -0.0374 0.0301  506 GLN A N   
1564 C CA  . GLN A 214 ? 0.3371 0.3535 0.3700 0.0479  -0.0431 0.0294  506 GLN A CA  
1565 C C   . GLN A 214 ? 0.3477 0.3466 0.3613 0.0546  -0.0329 0.0220  506 GLN A C   
1566 O O   . GLN A 214 ? 0.3606 0.3589 0.3645 0.0581  -0.0311 0.0271  506 GLN A O   
1567 C CB  . GLN A 214 ? 0.3794 0.4099 0.3968 0.0333  -0.0545 0.0181  506 GLN A CB  
1568 C CG  . GLN A 214 ? 0.4218 0.4745 0.4540 0.0222  -0.0711 0.0274  506 GLN A CG  
1569 C CD  . GLN A 214 ? 0.5254 0.5890 0.5417 0.0039  -0.0788 0.0067  506 GLN A CD  
1570 O OE1 . GLN A 214 ? 0.4027 0.4568 0.4027 0.0009  -0.0687 -0.0172 506 GLN A OE1 
1571 N NE2 . GLN A 214 ? 0.3181 0.4031 0.3455 -0.0094 -0.0966 0.0134  506 GLN A NE2 
1572 N N   . LEU A 215 ? 0.3307 0.3152 0.3442 0.0556  -0.0287 0.0127  507 LEU A N   
1573 C CA  . LEU A 215 ? 0.4074 0.3784 0.4102 0.0611  -0.0244 0.0082  507 LEU A CA  
1574 C C   . LEU A 215 ? 0.3329 0.2958 0.3287 0.0663  -0.0172 0.0183  507 LEU A C   
1575 O O   . LEU A 215 ? 0.3075 0.2665 0.2923 0.0695  -0.0153 0.0167  507 LEU A O   
1576 C CB  . LEU A 215 ? 0.3054 0.2628 0.3215 0.0603  -0.0273 0.0014  507 LEU A CB  
1577 C CG  . LEU A 215 ? 0.3278 0.2900 0.3577 0.0553  -0.0298 -0.0196 507 LEU A CG  
1578 C CD1 . LEU A 215 ? 0.2715 0.2151 0.3318 0.0572  -0.0338 -0.0237 507 LEU A CD1 
1579 C CD2 . LEU A 215 ? 0.4034 0.3772 0.4212 0.0545  -0.0249 -0.0336 507 LEU A CD2 
1580 N N   . LEU A 216 ? 0.3080 0.2701 0.3112 0.0648  -0.0109 0.0254  508 LEU A N   
1581 C CA  . LEU A 216 ? 0.3130 0.2695 0.3071 0.0655  0.0010  0.0273  508 LEU A CA  
1582 C C   . LEU A 216 ? 0.3605 0.3233 0.3672 0.0713  0.0064  0.0266  508 LEU A C   
1583 O O   . LEU A 216 ? 0.2813 0.2368 0.2802 0.0723  0.0153  0.0215  508 LEU A O   
1584 C CB  . LEU A 216 ? 0.2833 0.2407 0.2818 0.0581  0.0117  0.0312  508 LEU A CB  
1585 C CG  . LEU A 216 ? 0.3987 0.3452 0.3855 0.0494  0.0048  0.0389  508 LEU A CG  
1586 C CD1 . LEU A 216 ? 0.2925 0.2431 0.2818 0.0376  0.0177  0.0454  508 LEU A CD1 
1587 C CD2 . LEU A 216 ? 0.2940 0.2277 0.2539 0.0471  -0.0019 0.0421  508 LEU A CD2 
1588 N N   . LEU A 217 ? 0.3265 0.3022 0.3552 0.0732  -0.0013 0.0327  509 LEU A N   
1589 C CA  . LEU A 217 ? 0.2808 0.2603 0.3304 0.0782  -0.0020 0.0392  509 LEU A CA  
1590 C C   . LEU A 217 ? 0.3289 0.3026 0.3576 0.0780  -0.0076 0.0400  509 LEU A C   
1591 O O   . LEU A 217 ? 0.3201 0.2887 0.3630 0.0814  -0.0052 0.0443  509 LEU A O   
1592 C CB  . LEU A 217 ? 0.2378 0.2353 0.3177 0.0770  -0.0158 0.0529  509 LEU A CB  
1593 C CG  . LEU A 217 ? 0.3383 0.3455 0.4593 0.0790  -0.0080 0.0531  509 LEU A CG  
1594 C CD1 . LEU A 217 ? 0.3269 0.3553 0.4819 0.0763  -0.0283 0.0694  509 LEU A CD1 
1595 C CD2 . LEU A 217 ? 0.2822 0.2830 0.4341 0.0865  0.0124  0.0453  509 LEU A CD2 
1596 N N   . ILE A 218 ? 0.3265 0.3010 0.3290 0.0733  -0.0133 0.0343  510 ILE A N   
1597 C CA  . ILE A 218 ? 0.4196 0.3917 0.4058 0.0714  -0.0141 0.0315  510 ILE A CA  
1598 C C   . ILE A 218 ? 0.3707 0.3281 0.3524 0.0752  -0.0056 0.0246  510 ILE A C   
1599 O O   . ILE A 218 ? 0.3870 0.3408 0.3672 0.0745  -0.0044 0.0248  510 ILE A O   
1600 C CB  . ILE A 218 ? 0.3540 0.3333 0.3253 0.0655  -0.0174 0.0203  510 ILE A CB  
1601 C CG1 . ILE A 218 ? 0.3474 0.3443 0.3145 0.0558  -0.0255 0.0231  510 ILE A CG1 
1602 C CG2 . ILE A 218 ? 0.3901 0.3703 0.3521 0.0631  -0.0139 0.0136  510 ILE A CG2 
1603 C CD1 . ILE A 218 ? 0.4467 0.4502 0.4065 0.0487  -0.0241 0.0030  510 ILE A CD1 
1604 N N   . LEU A 219 ? 0.3147 0.2646 0.2917 0.0757  -0.0003 0.0193  511 LEU A N   
1605 C CA  . LEU A 219 ? 0.3363 0.2753 0.3003 0.0737  0.0055  0.0121  511 LEU A CA  
1606 C C   . LEU A 219 ? 0.3444 0.2784 0.3232 0.0752  0.0167  0.0077  511 LEU A C   
1607 O O   . LEU A 219 ? 0.3595 0.2853 0.3297 0.0719  0.0201  -0.0010 511 LEU A O   
1608 C CB  . LEU A 219 ? 0.3540 0.2892 0.3025 0.0677  0.0080  0.0115  511 LEU A CB  
1609 C CG  . LEU A 219 ? 0.3685 0.3028 0.3131 0.0660  -0.0051 0.0178  511 LEU A CG  
1610 C CD1 . LEU A 219 ? 0.3839 0.3114 0.3077 0.0556  -0.0065 0.0244  511 LEU A CD1 
1611 C CD2 . LEU A 219 ? 0.2737 0.2087 0.2235 0.0694  -0.0157 0.0146  511 LEU A CD2 
1612 N N   . SER A 220 ? 0.2876 0.2262 0.2964 0.0798  0.0212  0.0128  512 SER A N   
1613 C CA  . SER A 220 ? 0.2832 0.2150 0.3246 0.0835  0.0308  0.0087  512 SER A CA  
1614 C C   . SER A 220 ? 0.3116 0.2383 0.3588 0.0839  0.0213  0.0182  512 SER A C   
1615 O O   . SER A 220 ? 0.2899 0.2039 0.3507 0.0834  0.0286  0.0095  512 SER A O   
1616 C CB  . SER A 220 ? 0.3086 0.2491 0.3968 0.0898  0.0335  0.0161  512 SER A CB  
1617 O OG  . SER A 220 ? 0.4534 0.3980 0.5460 0.0874  0.0515  0.0013  512 SER A OG  
1618 N N   . HIS A 221 ? 0.3289 0.2660 0.3648 0.0816  0.0066  0.0341  513 HIS A N   
1619 C CA  . HIS A 221 ? 0.3232 0.2591 0.3576 0.0767  -0.0003 0.0450  513 HIS A CA  
1620 C C   . HIS A 221 ? 0.3179 0.2483 0.3298 0.0726  0.0042  0.0305  513 HIS A C   
1621 O O   . HIS A 221 ? 0.3418 0.2644 0.3632 0.0689  0.0053  0.0322  513 HIS A O   
1622 C CB  . HIS A 221 ? 0.3655 0.3192 0.3842 0.0692  -0.0133 0.0612  513 HIS A CB  
1623 C CG  . HIS A 221 ? 0.6374 0.5948 0.6470 0.0584  -0.0177 0.0739  513 HIS A CG  
1624 N ND1 . HIS A 221 ? 0.6177 0.5685 0.6536 0.0552  -0.0250 0.0972  513 HIS A ND1 
1625 C CD2 . HIS A 221 ? 0.4717 0.4399 0.4537 0.0483  -0.0148 0.0673  513 HIS A CD2 
1626 C CE1 . HIS A 221 ? 0.5481 0.5052 0.5647 0.0412  -0.0266 0.1071  513 HIS A CE1 
1627 N NE2 . HIS A 221 ? 0.6278 0.5975 0.6117 0.0367  -0.0183 0.0867  513 HIS A NE2 
1628 N N   . ILE A 222 ? 0.3462 0.2805 0.3346 0.0722  0.0041  0.0187  514 ILE A N   
1629 C CA  . ILE A 222 ? 0.3253 0.2574 0.3011 0.0683  0.0032  0.0079  514 ILE A CA  
1630 C C   . ILE A 222 ? 0.3619 0.2799 0.3398 0.0658  0.0099  -0.0038 514 ILE A C   
1631 O O   . ILE A 222 ? 0.3522 0.2665 0.3320 0.0605  0.0088  -0.0096 514 ILE A O   
1632 C CB  . ILE A 222 ? 0.3619 0.2998 0.3238 0.0689  -0.0031 0.0031  514 ILE A CB  
1633 C CG1 . ILE A 222 ? 0.3054 0.2575 0.2707 0.0689  -0.0062 0.0053  514 ILE A CG1 
1634 C CG2 . ILE A 222 ? 0.3251 0.2611 0.2821 0.0649  -0.0094 -0.0043 514 ILE A CG2 
1635 C CD1 . ILE A 222 ? 0.2905 0.2446 0.2577 0.0712  -0.0122 0.0001  514 ILE A CD1 
1636 N N   . ARG A 223 ? 0.3009 0.2126 0.2802 0.0671  0.0192  -0.0109 515 ARG A N   
1637 C CA  . ARG A 223 ? 0.3306 0.2303 0.3135 0.0615  0.0312  -0.0294 515 ARG A CA  
1638 C C   . ARG A 223 ? 0.3124 0.2009 0.3334 0.0641  0.0353  -0.0281 515 ARG A C   
1639 O O   . ARG A 223 ? 0.3580 0.2362 0.3826 0.0571  0.0391  -0.0424 515 ARG A O   
1640 C CB  . ARG A 223 ? 0.3276 0.2270 0.3109 0.0606  0.0468  -0.0410 515 ARG A CB  
1641 C CG  . ARG A 223 ? 0.4012 0.2901 0.3924 0.0525  0.0661  -0.0687 515 ARG A CG  
1642 C CD  . ARG A 223 ? 0.5000 0.3905 0.4389 0.0344  0.0642  -0.0835 515 ARG A CD  
1643 N NE  . ARG A 223 ? 0.5800 0.4812 0.4824 0.0270  0.0635  -0.0772 515 ARG A NE  
1644 C CZ  . ARG A 223 ? 0.5955 0.5005 0.4706 0.0108  0.0817  -0.0957 515 ARG A CZ  
1645 N NH1 . ARG A 223 ? 0.5212 0.4212 0.3991 -0.0004 0.1037  -0.1283 515 ARG A NH1 
1646 N NH2 . ARG A 223 ? 0.5943 0.5089 0.4397 0.0031  0.0799  -0.0830 515 ARG A NH2 
1647 N N   . HIS A 224 ? 0.3306 0.2209 0.3827 0.0720  0.0319  -0.0088 516 HIS A N   
1648 C CA  . HIS A 224 ? 0.2992 0.1775 0.3931 0.0731  0.0306  0.0020  516 HIS A CA  
1649 C C   . HIS A 224 ? 0.3000 0.1785 0.3802 0.0644  0.0226  0.0091  516 HIS A C   
1650 O O   . HIS A 224 ? 0.3161 0.1794 0.4211 0.0599  0.0260  0.0047  516 HIS A O   
1651 C CB  . HIS A 224 ? 0.2944 0.1793 0.4188 0.0796  0.0204  0.0301  516 HIS A CB  
1652 C CG  . HIS A 224 ? 0.3224 0.1946 0.4937 0.0788  0.0129  0.0517  516 HIS A CG  
1653 N ND1 . HIS A 224 ? 0.3781 0.2363 0.6114 0.0853  0.0188  0.0480  516 HIS A ND1 
1654 C CD2 . HIS A 224 ? 0.4192 0.2927 0.5852 0.0693  -0.0001 0.0779  516 HIS A CD2 
1655 C CE1 . HIS A 224 ? 0.3998 0.2527 0.6606 0.0788  0.0061  0.0725  516 HIS A CE1 
1656 N NE2 . HIS A 224 ? 0.3887 0.2444 0.6151 0.0710  -0.0053 0.0959  516 HIS A NE2 
1657 N N   . MET A 225 ? 0.2868 0.1830 0.3339 0.0609  0.0143  0.0173  517 MET A N   
1658 C CA  . MET A 225 ? 0.3153 0.2173 0.3544 0.0515  0.0110  0.0198  517 MET A CA  
1659 C C   . MET A 225 ? 0.3038 0.1987 0.3382 0.0467  0.0138  -0.0032 517 MET A C   
1660 O O   . MET A 225 ? 0.3424 0.2332 0.3904 0.0383  0.0138  -0.0045 517 MET A O   
1661 C CB  . MET A 225 ? 0.3132 0.2381 0.3268 0.0491  0.0065  0.0244  517 MET A CB  
1662 C CG  . MET A 225 ? 0.3376 0.2743 0.3467 0.0453  0.0023  0.0463  517 MET A CG  
1663 S SD  . MET A 225 ? 0.3879 0.3529 0.3698 0.0373  0.0042  0.0396  517 MET A SD  
1664 C CE  . MET A 225 ? 0.2807 0.2439 0.2580 0.0503  0.0026  0.0190  517 MET A CE  
1665 N N   . SER A 226 ? 0.3811 0.2762 0.3945 0.0485  0.0145  -0.0197 518 SER A N   
1666 C CA  . SER A 226 ? 0.3647 0.2567 0.3649 0.0391  0.0123  -0.0394 518 SER A CA  
1667 C C   . SER A 226 ? 0.3461 0.2185 0.3679 0.0328  0.0226  -0.0559 518 SER A C   
1668 O O   . SER A 226 ? 0.4035 0.2730 0.4306 0.0223  0.0192  -0.0661 518 SER A O   
1669 C CB  . SER A 226 ? 0.3473 0.2439 0.3141 0.0375  0.0095  -0.0476 518 SER A CB  
1670 O OG  . SER A 226 ? 0.5312 0.4287 0.4774 0.0237  0.0017  -0.0621 518 SER A OG  
1671 N N   . ASN A 227 ? 0.3438 0.2032 0.3867 0.0389  0.0359  -0.0612 519 ASN A N   
1672 C CA  . ASN A 227 ? 0.3713 0.2094 0.4494 0.0343  0.0489  -0.0817 519 ASN A CA  
1673 C C   . ASN A 227 ? 0.4164 0.2439 0.5333 0.0325  0.0433  -0.0651 519 ASN A C   
1674 O O   . ASN A 227 ? 0.4513 0.2656 0.5844 0.0218  0.0463  -0.0826 519 ASN A O   
1675 C CB  . ASN A 227 ? 0.3791 0.2079 0.4910 0.0440  0.0653  -0.0894 519 ASN A CB  
1676 C CG  . ASN A 227 ? 0.5275 0.3675 0.6015 0.0406  0.0762  -0.1089 519 ASN A CG  
1677 O OD1 . ASN A 227 ? 0.4742 0.3213 0.5588 0.0504  0.0816  -0.1005 519 ASN A OD1 
1678 N ND2 . ASN A 227 ? 0.4414 0.2850 0.4699 0.0236  0.0780  -0.1329 519 ASN A ND2 
1679 N N   . LYS A 228 ? 0.3668 0.2007 0.4963 0.0393  0.0346  -0.0309 520 LYS A N   
1680 C CA  . LYS A 228 ? 0.3888 0.2162 0.5460 0.0323  0.0285  -0.0087 520 LYS A CA  
1681 C C   . LYS A 228 ? 0.3912 0.2319 0.5249 0.0197  0.0238  -0.0144 520 LYS A C   
1682 O O   . LYS A 228 ? 0.4409 0.2716 0.6006 0.0089  0.0239  -0.0125 520 LYS A O   
1683 C CB  . LYS A 228 ? 0.4840 0.3217 0.6442 0.0357  0.0189  0.0304  520 LYS A CB  
1684 C CG  . LYS A 228 ? 0.5627 0.3886 0.7633 0.0473  0.0179  0.0433  520 LYS A CG  
1685 C CD  . LYS A 228 ? 0.5528 0.3497 0.8213 0.0461  0.0184  0.0512  520 LYS A CD  
1686 C CE  . LYS A 228 ? 0.5852 0.3818 0.8949 0.0571  0.0236  0.0406  520 LYS A CE  
1687 N NZ  . LYS A 228 ? 0.7156 0.4975 1.0795 0.0534  0.0308  0.0254  520 LYS A NZ  
1688 N N   . GLY A 229 ? 0.4177 0.2812 0.5114 0.0208  0.0189  -0.0206 521 GLY A N   
1689 C CA  . GLY A 229 ? 0.3670 0.2464 0.4521 0.0107  0.0128  -0.0275 521 GLY A CA  
1690 C C   . GLY A 229 ? 0.5134 0.3829 0.6015 0.0004  0.0112  -0.0549 521 GLY A C   
1691 O O   . GLY A 229 ? 0.4822 0.3578 0.5846 -0.0113 0.0065  -0.0588 521 GLY A O   
1692 N N   A MET A 230 ? 0.4001 0.2568 0.4742 0.0015  0.0162  -0.0762 522 MET A N   
1693 N N   B MET A 230 ? 0.4007 0.2576 0.4745 0.0015  0.0161  -0.0761 522 MET A N   
1694 C CA  A MET A 230 ? 0.4155 0.2644 0.4834 -0.0138 0.0157  -0.1069 522 MET A CA  
1695 C CA  B MET A 230 ? 0.4146 0.2634 0.4824 -0.0138 0.0158  -0.1069 522 MET A CA  
1696 C C   A MET A 230 ? 0.4671 0.2916 0.5815 -0.0215 0.0251  -0.1170 522 MET A C   
1697 C C   B MET A 230 ? 0.4682 0.2929 0.5828 -0.0214 0.0250  -0.1165 522 MET A C   
1698 O O   A MET A 230 ? 0.4589 0.2819 0.5798 -0.0377 0.0201  -0.1348 522 MET A O   
1699 O O   B MET A 230 ? 0.4581 0.2817 0.5796 -0.0375 0.0197  -0.1335 522 MET A O   
1700 C CB  A MET A 230 ? 0.4398 0.2849 0.4738 -0.0159 0.0236  -0.1299 522 MET A CB  
1701 C CB  B MET A 230 ? 0.4390 0.2834 0.4742 -0.0155 0.0242  -0.1300 522 MET A CB  
1702 C CG  A MET A 230 ? 0.4456 0.3129 0.4316 -0.0158 0.0094  -0.1211 522 MET A CG  
1703 C CG  B MET A 230 ? 0.4585 0.3111 0.4542 -0.0367 0.0149  -0.1557 522 MET A CG  
1704 S SD  A MET A 230 ? 0.5374 0.4105 0.4681 -0.0408 0.0032  -0.1500 522 MET A SD  
1705 S SD  B MET A 230 ? 0.4517 0.3349 0.4221 -0.0407 -0.0168 -0.1336 522 MET A SD  
1706 C CE  A MET A 230 ? 0.4493 0.3402 0.3377 -0.0346 -0.0094 -0.1259 522 MET A CE  
1707 C CE  B MET A 230 ? 0.4346 0.3277 0.3595 -0.0333 -0.0198 -0.1208 522 MET A CE  
1708 N N   . GLU A 231 ? 0.4552 0.2601 0.6086 -0.0109 0.0361  -0.1041 523 GLU A N   
1709 C CA  . GLU A 231 ? 0.4539 0.2318 0.6643 -0.0173 0.0424  -0.1067 523 GLU A CA  
1710 C C   . GLU A 231 ? 0.4564 0.2427 0.6808 -0.0272 0.0322  -0.0816 523 GLU A C   
1711 O O   . GLU A 231 ? 0.4717 0.2433 0.7288 -0.0413 0.0331  -0.0928 523 GLU A O   
1712 C CB  . GLU A 231 ? 0.4574 0.2140 0.7165 -0.0028 0.0505  -0.0897 523 GLU A CB  
1713 C CG  . GLU A 231 ? 0.7033 0.4589 0.9557 0.0091  0.0632  -0.1098 523 GLU A CG  
1714 C CD  . GLU A 231 ? 0.8542 0.6126 1.1351 0.0260  0.0596  -0.0744 523 GLU A CD  
1715 O OE1 . GLU A 231 ? 0.8146 0.5687 1.1257 0.0261  0.0478  -0.0366 523 GLU A OE1 
1716 O OE2 . GLU A 231 ? 0.8049 0.5741 1.0746 0.0356  0.0669  -0.0825 523 GLU A OE2 
1717 N N   . HIS A 232 ? 0.4188 0.2299 0.6204 -0.0225 0.0251  -0.0508 524 HIS A N   
1718 C CA  . HIS A 232 ? 0.5425 0.3682 0.7550 -0.0349 0.0211  -0.0299 524 HIS A CA  
1719 C C   . HIS A 232 ? 0.5651 0.4095 0.7690 -0.0471 0.0145  -0.0529 524 HIS A C   
1720 O O   . HIS A 232 ? 0.5206 0.3645 0.7544 -0.0627 0.0143  -0.0521 524 HIS A O   
1721 C CB  . HIS A 232 ? 0.3962 0.2474 0.5837 -0.0296 0.0199  0.0005  524 HIS A CB  
1722 C CG  . HIS A 232 ? 0.5279 0.4002 0.7226 -0.0456 0.0220  0.0186  524 HIS A CG  
1723 N ND1 . HIS A 232 ? 0.5036 0.4117 0.6787 -0.0477 0.0231  0.0132  524 HIS A ND1 
1724 C CD2 . HIS A 232 ? 0.5261 0.3898 0.7501 -0.0622 0.0254  0.0415  524 HIS A CD2 
1725 C CE1 . HIS A 232 ? 0.5936 0.5176 0.7840 -0.0653 0.0306  0.0279  524 HIS A CE1 
1726 N NE2 . HIS A 232 ? 0.5049 0.4025 0.7204 -0.0758 0.0314  0.0476  524 HIS A NE2 
1727 N N   . LEU A 233 ? 0.4981 0.3599 0.6655 -0.0419 0.0067  -0.0703 525 LEU A N   
1728 C CA  . LEU A 233 ? 0.4655 0.3478 0.6293 -0.0539 -0.0066 -0.0872 525 LEU A CA  
1729 C C   . LEU A 233 ? 0.5393 0.4021 0.7155 -0.0705 -0.0086 -0.1168 525 LEU A C   
1730 O O   . LEU A 233 ? 0.5571 0.4314 0.7534 -0.0865 -0.0181 -0.1254 525 LEU A O   
1731 C CB  . LEU A 233 ? 0.4916 0.3945 0.6165 -0.0457 -0.0194 -0.0914 525 LEU A CB  
1732 C CG  . LEU A 233 ? 0.5655 0.4938 0.6883 -0.0332 -0.0200 -0.0701 525 LEU A CG  
1733 C CD1 . LEU A 233 ? 0.3990 0.3424 0.4948 -0.0265 -0.0361 -0.0734 525 LEU A CD1 
1734 C CD2 . LEU A 233 ? 0.4850 0.4370 0.6454 -0.0418 -0.0186 -0.0628 525 LEU A CD2 
1735 N N   . TYR A 234 ? 0.4659 0.3012 0.6350 -0.0685 0.0018  -0.1363 526 TYR A N   
1736 C CA  . TYR A 234 ? 0.7282 0.5430 0.9115 -0.0867 0.0050  -0.1723 526 TYR A CA  
1737 C C   . TYR A 234 ? 0.6399 0.4333 0.8846 -0.0952 0.0118  -0.1661 526 TYR A C   
1738 O O   . TYR A 234 ? 0.9564 0.7403 1.2210 -0.1150 0.0094  -0.1931 526 TYR A O   
1739 C CB  . TYR A 234 ? 0.6258 0.4183 0.7949 -0.0828 0.0215  -0.2001 526 TYR A CB  
1740 C CG  . TYR A 234 ? 0.8675 0.6471 1.0315 -0.1063 0.0263  -0.2492 526 TYR A CG  
1741 C CD1 . TYR A 234 ? 0.9729 0.7746 1.0759 -0.1246 0.0127  -0.2717 526 TYR A CD1 
1742 C CD2 . TYR A 234 ? 0.8385 0.5967 1.0474 -0.1069 0.0406  -0.2585 526 TYR A CD2 
1743 C CE1 . TYR A 234 ? 0.7730 0.5744 0.8548 -0.1444 0.0150  -0.3033 526 TYR A CE1 
1744 C CE2 . TYR A 234 ? 0.9198 0.6773 1.1152 -0.1244 0.0452  -0.2949 526 TYR A CE2 
1745 C CZ  . TYR A 234 ? 0.9752 0.7540 1.1042 -0.1437 0.0332  -0.3177 526 TYR A CZ  
1746 O OH  . TYR A 234 ? 1.0819 0.8610 1.1925 -0.1640 0.0374  -0.3529 526 TYR A OH  
1747 N N   . SER A 235 ? 0.7257 1.0037 0.9972 -0.3919 0.1067  0.1341  527 SER A N   
1748 C CA  . SER A 235 ? 0.6901 1.0163 1.0775 -0.3887 0.1067  0.1557  527 SER A CA  
1749 C C   . SER A 235 ? 0.7634 1.2039 1.2484 -0.3954 0.0923  0.2116  527 SER A C   
1750 O O   . SER A 235 ? 0.6611 1.1547 1.2334 -0.3950 0.0723  0.2435  527 SER A O   
1751 C CB  . SER A 235 ? 0.6599 0.9763 1.0257 -0.3500 0.1569  0.1525  527 SER A CB  
1752 O OG  . SER A 235 ? 0.6680 1.0679 1.0561 -0.3303 0.1915  0.1820  527 SER A OG  
1753 N N   . MET A 236 ? 0.7553 1.2410 1.2274 -0.3934 0.0964  0.2362  528 MET A N   
1754 C CA  . MET A 236 ? 0.6831 1.2823 1.2588 -0.3827 0.0775  0.3091  528 MET A CA  
1755 C C   . MET A 236 ? 0.7457 1.3232 1.3757 -0.4180 0.0086  0.3169  528 MET A C   
1756 O O   . MET A 236 ? 0.8004 1.2786 1.3983 -0.4488 -0.0340 0.2631  528 MET A O   
1757 C CB  . MET A 236 ? 0.6611 1.3350 1.1899 -0.3386 0.1326  0.3370  528 MET A CB  
1758 C CG  . MET A 236 ? 0.6819 1.3117 1.0922 -0.3068 0.1924  0.2932  528 MET A CG  
1759 S SD  . MET A 236 ? 1.0266 1.7222 1.4802 -0.2617 0.2172  0.3242  528 MET A SD  
1760 C CE  . MET A 236 ? 0.6846 1.4744 1.0868 -0.1851 0.2608  0.3623  528 MET A CE  
1761 N N   . LEU A 244 ? 0.9678 1.0168 0.7177 -0.2855 -0.0932 -0.1614 536 LEU A N   
1762 C CA  . LEU A 244 ? 0.8447 0.9189 0.5592 -0.2623 -0.0538 -0.1571 536 LEU A CA  
1763 C C   . LEU A 244 ? 0.7756 0.8482 0.4496 -0.2311 -0.0715 -0.1805 536 LEU A C   
1764 O O   . LEU A 244 ? 0.7969 0.9054 0.4756 -0.2141 -0.0573 -0.1790 536 LEU A O   
1765 C CB  . LEU A 244 ? 0.8082 0.8545 0.4696 -0.2605 -0.0184 -0.1441 536 LEU A CB  
1766 C CG  . LEU A 244 ? 0.8170 0.8849 0.4577 -0.2379 0.0153  -0.1340 536 LEU A CG  
1767 C CD1 . LEU A 244 ? 0.9974 1.1310 0.6991 -0.2331 0.0238  -0.1224 536 LEU A CD1 
1768 C CD2 . LEU A 244 ? 0.8287 0.8785 0.4404 -0.2395 0.0473  -0.1164 536 LEU A CD2 
1769 N N   . SER A 245 ? 0.9217 0.9597 0.5586 -0.2178 -0.1045 -0.1980 537 SER A N   
1770 C CA  . SER A 245 ? 1.0380 1.0904 0.6472 -0.1718 -0.1192 -0.2039 537 SER A CA  
1771 C C   . SER A 245 ? 0.8208 0.9329 0.4762 -0.1672 -0.1335 -0.2209 537 SER A C   
1772 O O   . SER A 245 ? 0.8421 0.9979 0.5089 -0.1430 -0.1221 -0.2116 537 SER A O   
1773 C CB  . SER A 245 ? 1.0718 1.0798 0.6474 -0.1332 -0.1493 -0.2078 537 SER A CB  
1774 O OG  . SER A 245 ? 1.2399 1.2006 0.8031 -0.1587 -0.1458 -0.2049 537 SER A OG  
1775 N N   . ASP A 246 ? 0.8222 0.9317 0.5244 -0.1860 -0.1609 -0.2348 538 ASP A N   
1776 C CA  . ASP A 246 ? 0.7739 0.9343 0.5301 -0.1828 -0.1728 -0.2437 538 ASP A CA  
1777 C C   . ASP A 246 ? 0.7294 0.9418 0.5276 -0.1988 -0.1280 -0.2204 538 ASP A C   
1778 O O   . ASP A 246 ? 0.7615 1.0280 0.5825 -0.1841 -0.1204 -0.2238 538 ASP A O   
1779 C CB  . ASP A 246 ? 0.8898 1.0233 0.6941 -0.2055 -0.2203 -0.2534 538 ASP A CB  
1780 N N   . LEU A 247 ? 0.7475 0.9499 0.5553 -0.2227 -0.0984 -0.1953 539 LEU A N   
1781 C CA  . LEU A 247 ? 0.7386 0.9872 0.5696 -0.2233 -0.0581 -0.1736 539 LEU A CA  
1782 C C   . LEU A 247 ? 0.6907 0.9426 0.4746 -0.1940 -0.0413 -0.1808 539 LEU A C   
1783 O O   . LEU A 247 ? 0.6721 0.9680 0.4765 -0.1821 -0.0284 -0.1792 539 LEU A O   
1784 C CB  . LEU A 247 ? 0.7883 1.0360 0.6352 -0.2401 -0.0321 -0.1400 539 LEU A CB  
1785 C CG  . LEU A 247 ? 0.8269 1.1165 0.6692 -0.2209 0.0108  -0.1185 539 LEU A CG  
1786 C CD1 . LEU A 247 ? 0.8800 1.2304 0.7828 -0.2259 0.0151  -0.1018 539 LEU A CD1 
1787 C CD2 . LEU A 247 ? 0.8356 1.1322 0.6759 -0.2185 0.0397  -0.0839 539 LEU A CD2 
1788 N N   . LEU A 248 ? 0.6911 0.8950 0.4177 -0.1833 -0.0464 -0.1832 540 LEU A N   
1789 C CA  . LEU A 248 ? 0.7049 0.9057 0.3998 -0.1570 -0.0470 -0.1789 540 LEU A CA  
1790 C C   . LEU A 248 ? 0.6225 0.8801 0.3522 -0.1360 -0.0681 -0.1842 540 LEU A C   
1791 O O   . LEU A 248 ? 0.5906 0.8816 0.3421 -0.1210 -0.0681 -0.1773 540 LEU A O   
1792 C CB  . LEU A 248 ? 0.6834 0.8244 0.3184 -0.1523 -0.0546 -0.1686 540 LEU A CB  
1793 C CG  . LEU A 248 ? 0.7164 0.8050 0.3125 -0.1662 -0.0310 -0.1590 540 LEU A CG  
1794 C CD1 . LEU A 248 ? 0.7194 0.7497 0.2773 -0.1575 -0.0386 -0.1393 540 LEU A CD1 
1795 C CD2 . LEU A 248 ? 0.7254 0.8140 0.3117 -0.1494 -0.0172 -0.1553 540 LEU A CD2 
1796 N N   . LEU A 249 ? 0.6228 0.8949 0.3605 -0.1297 -0.0904 -0.1964 541 LEU A N   
1797 C CA  . LEU A 249 ? 0.6743 1.0079 0.4545 -0.0990 -0.1059 -0.1944 541 LEU A CA  
1798 C C   . LEU A 249 ? 0.6324 1.0335 0.4723 -0.1158 -0.0936 -0.2060 541 LEU A C   
1799 O O   . LEU A 249 ? 0.6442 1.1049 0.5272 -0.0979 -0.0927 -0.1956 541 LEU A O   
1800 C CB  . LEU A 249 ? 0.6728 0.9881 0.4416 -0.0766 -0.1313 -0.2044 541 LEU A CB  
1801 C CG  . LEU A 249 ? 0.8139 1.1867 0.6169 -0.0312 -0.1437 -0.1957 541 LEU A CG  
1802 C CD1 . LEU A 249 ? 0.7306 1.1558 0.5660 -0.0065 -0.1338 -0.1579 541 LEU A CD1 
1803 C CD2 . LEU A 249 ? 0.6601 0.9897 0.4176 0.0045  -0.1676 -0.1978 541 LEU A CD2 
1804 N N   . GLU A 250 ? 0.5753 0.9611 0.4335 -0.1476 -0.0812 -0.2122 542 GLU A N   
1805 C CA  . GLU A 250 ? 0.5473 0.9904 0.4663 -0.1620 -0.0656 -0.2098 542 GLU A CA  
1806 C C   . GLU A 250 ? 0.5223 0.9940 0.4494 -0.1540 -0.0390 -0.1975 542 GLU A C   
1807 O O   . GLU A 250 ? 0.5581 1.0951 0.5349 -0.1499 -0.0331 -0.1977 542 GLU A O   
1808 C CB  . GLU A 250 ? 0.5899 1.0123 0.5331 -0.1964 -0.0607 -0.1983 542 GLU A CB  
1809 C CG  . GLU A 250 ? 0.6737 1.1522 0.6842 -0.2140 -0.0556 -0.1897 542 GLU A CG  
1810 C CD  . GLU A 250 ? 0.7673 1.2807 0.8015 -0.1992 -0.0855 -0.2162 542 GLU A CD  
1811 O OE1 . GLU A 250 ? 0.7699 1.2448 0.7931 -0.1961 -0.1279 -0.2346 542 GLU A OE1 
1812 O OE2 . GLU A 250 ? 0.7092 1.2912 0.7736 -0.1855 -0.0703 -0.2189 542 GLU A OE2 
1813 N N   . MET A 251 ? 0.5609 0.9821 0.4386 -0.1484 -0.0269 -0.1887 543 MET A N   
1814 C CA  . MET A 251 ? 0.5634 0.9938 0.4351 -0.1295 -0.0167 -0.1838 543 MET A CA  
1815 C C   . MET A 251 ? 0.5123 0.9544 0.3950 -0.1063 -0.0485 -0.1818 543 MET A C   
1816 O O   . MET A 251 ? 0.4874 0.9674 0.4060 -0.0934 -0.0552 -0.1795 543 MET A O   
1817 C CB  . MET A 251 ? 0.6314 1.0015 0.4402 -0.1203 0.0003  -0.1767 543 MET A CB  
1818 C CG  . MET A 251 ? 0.7012 1.0558 0.5017 -0.1404 0.0220  -0.1634 543 MET A CG  
1819 S SD  . MET A 251 ? 0.8429 1.1852 0.5944 -0.1111 0.0560  -0.1449 543 MET A SD  
1820 C CE  . MET A 251 ? 0.7974 1.1296 0.5567 -0.1352 0.0709  -0.1181 543 MET A CE  
1821 N N   . LEU A 252 ? 0.5685 0.9830 0.4268 -0.0988 -0.0713 -0.1745 544 LEU A N   
1822 C CA  . LEU A 252 ? 0.4605 0.8998 0.3438 -0.0737 -0.1058 -0.1516 544 LEU A CA  
1823 C C   . LEU A 252 ? 0.4511 0.9729 0.4176 -0.0578 -0.1077 -0.1395 544 LEU A C   
1824 O O   . LEU A 252 ? 0.5156 1.0593 0.5388 -0.0380 -0.1192 -0.1108 544 LEU A O   
1825 C CB  . LEU A 252 ? 0.4862 0.8662 0.3204 -0.0636 -0.1204 -0.1295 544 LEU A CB  
1826 C CG  . LEU A 252 ? 0.5407 0.8314 0.3055 -0.0699 -0.1238 -0.1245 544 LEU A CG  
1827 C CD1 . LEU A 252 ? 0.5655 0.8004 0.2803 -0.0699 -0.1247 -0.1062 544 LEU A CD1 
1828 C CD2 . LEU A 252 ? 0.5634 0.8431 0.3505 -0.0514 -0.1612 -0.1002 544 LEU A CD2 
1829 N N   . ASP A 253 ? 0.4222 0.9690 0.3946 -0.0634 -0.0957 -0.1569 545 ASP A N   
1830 C CA  . ASP A 253 ? 0.3962 1.0047 0.4304 -0.0424 -0.0903 -0.1484 545 ASP A CA  
1831 C C   . ASP A 253 ? 0.3201 0.9702 0.4000 -0.0638 -0.0671 -0.1613 545 ASP A C   
1832 O O   . ASP A 253 ? 0.3447 1.0151 0.4364 -0.0814 -0.0559 -0.1805 545 ASP A O   
1833 C CB  . ASP A 253 ? 0.3763 0.9777 0.3852 -0.0303 -0.0987 -0.1640 545 ASP A CB  
1834 C CG  . ASP A 253 ? 0.3435 0.9972 0.3946 0.0039  -0.0943 -0.1546 545 ASP A CG  
1835 O OD1 . ASP A 253 ? 0.3039 0.9762 0.3913 0.0171  -0.0821 -0.1248 545 ASP A OD1 
1836 O OD2 . ASP A 253 ? 0.3742 1.0265 0.4097 0.0171  -0.1062 -0.1763 545 ASP A OD2 
1837 N N   . ALA A 254 ? 0.4274 1.0765 0.5300 -0.0609 -0.0649 -0.1463 546 ALA A N   
1838 C CA  . ALA A 254 ? 0.3633 1.0356 0.4961 -0.0739 -0.0421 -0.1516 546 ALA A CA  
1839 C C   . ALA A 254 ? 0.3892 1.0507 0.5514 -0.0542 -0.0370 -0.1274 546 ALA A C   
1840 O O   . ALA A 254 ? 0.3188 0.9618 0.4897 -0.0292 -0.0513 -0.1011 546 ALA A O   
1841 C CB  . ALA A 254 ? 0.3056 0.9701 0.4392 -0.0731 -0.0512 -0.1519 546 ALA A CB  
1842 N N   . HIS A 255 ? 0.3462 1.0101 0.5192 -0.0676 -0.0177 -0.1317 547 HIS A N   
1843 C CA  . HIS A 255 ? 0.4476 1.0949 0.6384 -0.0547 -0.0153 -0.1122 547 HIS A CA  
1844 C C   . HIS A 255 ? 0.4635 1.1074 0.6743 -0.0504 -0.0196 -0.0984 547 HIS A C   
1845 O O   . HIS A 255 ? 0.4609 1.0857 0.6808 -0.0510 -0.0301 -0.0971 547 HIS A O   
1846 C CB  . HIS A 255 ? 0.2437 0.9020 0.4317 -0.0722 0.0014  -0.1250 547 HIS A CB  
1847 C CG  . HIS A 255 ? 0.2695 0.9194 0.4598 -0.0972 0.0175  -0.1282 547 HIS A CG  
1848 N ND1 . HIS A 255 ? 0.3319 0.9763 0.5250 -0.0970 0.0223  -0.1225 547 HIS A ND1 
1849 C CD2 . HIS A 255 ? 0.2729 0.9421 0.4635 -0.1244 0.0307  -0.1372 547 HIS A CD2 
1850 C CE1 . HIS A 255 ? 0.4769 1.1414 0.6639 -0.1185 0.0418  -0.1269 547 HIS A CE1 
1851 N NE2 . HIS A 255 ? 0.4279 1.1014 0.6173 -0.1372 0.0481  -0.1292 547 HIS A NE2 
1852 N N   . ARG A 256 ? 0.4463 1.1090 0.6680 -0.0451 -0.0167 -0.0885 548 ARG A N   
1853 C CA  . ARG A 256 ? 0.3172 0.9776 0.5698 -0.0427 -0.0237 -0.0745 548 ARG A CA  
1854 C C   . ARG A 256 ? 0.4376 1.1071 0.6826 -0.0565 -0.0059 -0.0841 548 ARG A C   
1855 O O   . ARG A 256 ? 0.6180 1.2956 0.8873 -0.0534 -0.0094 -0.0714 548 ARG A O   
1856 C CB  . ARG A 256 ? 0.2370 0.9106 0.5226 -0.0254 -0.0409 -0.0433 548 ARG A CB  
1857 N N   . LEU A 257 ? 0.3287 0.9954 0.5471 -0.0732 0.0109  -0.1017 549 LEU A N   
1858 C CA  . LEU A 257 ? 0.4973 1.1699 0.7084 -0.0877 0.0251  -0.1051 549 LEU A CA  
1859 C C   . LEU A 257 ? 0.5399 1.2069 0.7577 -0.0919 0.0307  -0.1045 549 LEU A C   
1860 O O   . LEU A 257 ? 0.6797 1.3483 0.8884 -0.1057 0.0453  -0.1045 549 LEU A O   
1861 C CB  . LEU A 257 ? 0.4114 1.0820 0.6093 -0.1050 0.0370  -0.1133 549 LEU A CB  
1862 C CG  . LEU A 257 ? 0.2603 0.9406 0.4547 -0.0976 0.0295  -0.1198 549 LEU A CG  
1863 C CD1 . LEU A 257 ? 0.3597 1.0366 0.5593 -0.1166 0.0381  -0.1251 549 LEU A CD1 
1864 C CD2 . LEU A 257 ? 0.2591 0.9627 0.4536 -0.0818 0.0225  -0.1148 549 LEU A CD2 
1865 N N   . LEU B 14  ? 1.0738 1.0406 0.8565 0.1201  -0.0479 -0.4072 306 LEU B N   
1866 C CA  . LEU B 14  ? 1.0074 0.9467 0.7887 0.1186  -0.1077 -0.4020 306 LEU B CA  
1867 C C   . LEU B 14  ? 0.9268 0.8914 0.8107 0.1057  -0.1293 -0.3628 306 LEU B C   
1868 O O   . LEU B 14  ? 0.9496 0.9047 0.8768 0.1016  -0.1762 -0.3615 306 LEU B O   
1869 C CB  . LEU B 14  ? 1.0165 0.9263 0.6837 0.1172  -0.1189 -0.3905 306 LEU B CB  
1870 C CG  . LEU B 14  ? 1.1856 1.0542 0.7545 0.1233  -0.1205 -0.4172 306 LEU B CG  
1871 C CD1 . LEU B 14  ? 1.1659 1.0166 0.7828 0.1294  -0.1688 -0.4432 306 LEU B CD1 
1872 C CD2 . LEU B 14  ? 1.2814 1.1563 0.8080 0.1236  -0.0560 -0.4339 306 LEU B CD2 
1873 N N   . ALA B 15  ? 0.9051 0.9029 0.8268 0.0978  -0.0936 -0.3319 307 ALA B N   
1874 C CA  . ALA B 15  ? 0.7201 0.7421 0.7383 0.0874  -0.1050 -0.3010 307 ALA B CA  
1875 C C   . ALA B 15  ? 0.7843 0.8060 0.8804 0.0914  -0.1125 -0.3197 307 ALA B C   
1876 O O   . ALA B 15  ? 0.7095 0.7417 0.8793 0.0813  -0.1258 -0.2946 307 ALA B O   
1877 C CB  . ALA B 15  ? 0.7392 0.7901 0.7633 0.0793  -0.0687 -0.2653 307 ALA B CB  
1878 N N   . LEU B 16  ? 0.7343 0.7410 0.8116 0.1068  -0.1040 -0.3635 308 LEU B N   
1879 C CA  . LEU B 16  ? 0.7677 0.7631 0.9142 0.1162  -0.1185 -0.3887 308 LEU B CA  
1880 C C   . LEU B 16  ? 0.8643 0.8245 1.0428 0.1114  -0.1725 -0.3983 308 LEU B C   
1881 O O   . LEU B 16  ? 0.7948 0.7339 1.0309 0.1173  -0.1922 -0.4162 308 LEU B O   
1882 C CB  . LEU B 16  ? 0.7017 0.6955 0.8164 0.1368  -0.0903 -0.4357 308 LEU B CB  
1883 C CG  . LEU B 16  ? 0.6940 0.7249 0.7746 0.1375  -0.0321 -0.4308 308 LEU B CG  
1884 C CD1 . LEU B 16  ? 0.7772 0.8055 0.8091 0.1486  -0.0029 -0.4606 308 LEU B CD1 
1885 C CD2 . LEU B 16  ? 0.6177 0.6826 0.7831 0.1359  -0.0161 -0.4116 308 LEU B CD2 
1886 N N   . SER B 17  ? 0.8066 0.7588 0.9540 0.1009  -0.1994 -0.3871 309 SER B N   
1887 C CA  . SER B 17  ? 0.7702 0.6952 0.9567 0.0916  -0.2523 -0.3954 309 SER B CA  
1888 C C   . SER B 17  ? 0.7589 0.7058 1.0194 0.0670  -0.2665 -0.3480 309 SER B C   
1889 O O   . SER B 17  ? 0.7931 0.7280 1.0949 0.0531  -0.3062 -0.3467 309 SER B O   
1890 C CB  . SER B 17  ? 0.8646 0.7710 0.9751 0.0969  -0.2750 -0.4129 309 SER B CB  
1891 O OG  . SER B 17  ? 1.0223 0.9138 1.0494 0.1161  -0.2490 -0.4437 309 SER B OG  
1892 N N   . LEU B 18  ? 0.6561 0.6369 0.9339 0.0605  -0.2328 -0.3092 310 LEU B N   
1893 C CA  . LEU B 18  ? 0.6820 0.6850 1.0250 0.0381  -0.2385 -0.2661 310 LEU B CA  
1894 C C   . LEU B 18  ? 0.7098 0.6898 1.1228 0.0277  -0.2529 -0.2602 310 LEU B C   
1895 O O   . LEU B 18  ? 0.6536 0.6048 1.0692 0.0423  -0.2552 -0.2872 310 LEU B O   
1896 C CB  . LEU B 18  ? 0.4945 0.5344 0.8239 0.0368  -0.1992 -0.2304 310 LEU B CB  
1897 C CG  . LEU B 18  ? 0.6126 0.6764 0.8954 0.0384  -0.1902 -0.2162 310 LEU B CG  
1898 C CD1 . LEU B 18  ? 0.7094 0.7518 0.9107 0.0540  -0.1969 -0.2477 310 LEU B CD1 
1899 C CD2 . LEU B 18  ? 0.4957 0.5851 0.7666 0.0389  -0.1513 -0.1873 310 LEU B CD2 
1900 N N   . THR B 19  ? 0.6164 0.6078 1.0865 0.0024  -0.2627 -0.2248 311 THR B N   
1901 C CA  . THR B 19  ? 0.5465 0.5122 1.0720 -0.0117 -0.2711 -0.2059 311 THR B CA  
1902 C C   . THR B 19  ? 0.4496 0.4375 0.9723 -0.0126 -0.2367 -0.1691 311 THR B C   
1903 O O   . THR B 19  ? 0.4524 0.4781 0.9406 -0.0063 -0.2079 -0.1571 311 THR B O   
1904 C CB  . THR B 19  ? 0.5175 0.4781 1.0865 -0.0380 -0.2874 -0.1785 311 THR B CB  
1905 O OG1 . THR B 19  ? 0.5466 0.5569 1.1203 -0.0519 -0.2704 -0.1518 311 THR B OG1 
1906 C CG2 . THR B 19  ? 0.5702 0.5019 1.1356 -0.0321 -0.3195 -0.2102 311 THR B CG2 
1907 N N   . ALA B 20  ? 0.4486 0.4055 1.0045 -0.0198 -0.2444 -0.1518 312 ALA B N   
1908 C CA  . ALA B 20  ? 0.4135 0.3842 0.9634 -0.0213 -0.2195 -0.1166 312 ALA B CA  
1909 C C   . ALA B 20  ? 0.4690 0.4795 1.0204 -0.0442 -0.1994 -0.0771 312 ALA B C   
1910 O O   . ALA B 20  ? 0.3380 0.3792 0.8610 -0.0380 -0.1711 -0.0605 312 ALA B O   
1911 C CB  . ALA B 20  ? 0.4510 0.3706 1.0312 -0.0258 -0.2405 -0.1025 312 ALA B CB  
1912 N N   . ASP B 21  ? 0.4187 0.4315 1.0081 -0.0705 -0.2136 -0.0647 313 ASP B N   
1913 C CA  . ASP B 21  ? 0.4593 0.5178 1.0574 -0.0900 -0.1902 -0.0322 313 ASP B CA  
1914 C C   . ASP B 21  ? 0.3914 0.4977 0.9657 -0.0742 -0.1775 -0.0483 313 ASP B C   
1915 O O   . ASP B 21  ? 0.4071 0.5510 0.9671 -0.0737 -0.1500 -0.0281 313 ASP B O   
1916 C CB  . ASP B 21  ? 0.4057 0.4559 1.0375 -0.1164 -0.1989 -0.0162 313 ASP B CB  
1917 C CG  . ASP B 21  ? 0.6707 0.6730 1.3172 -0.1364 -0.2066 0.0123  313 ASP B CG  
1918 O OD1 . ASP B 21  ? 0.6646 0.6623 1.2957 -0.1419 -0.1903 0.0413  313 ASP B OD1 
1919 O OD2 . ASP B 21  ? 0.5058 0.4712 1.1748 -0.1460 -0.2313 0.0065  313 ASP B OD2 
1920 N N   . GLN B 22  ? 0.3770 0.4761 0.9387 -0.0596 -0.1989 -0.0850 314 GLN B N   
1921 C CA  . GLN B 22  ? 0.4386 0.5687 0.9616 -0.0421 -0.1911 -0.0982 314 GLN B CA  
1922 C C   . GLN B 22  ? 0.3686 0.5010 0.8328 -0.0210 -0.1618 -0.0977 314 GLN B C   
1923 O O   . GLN B 22  ? 0.4127 0.5720 0.8475 -0.0126 -0.1455 -0.0909 314 GLN B O   
1924 C CB  . GLN B 22  ? 0.3821 0.4935 0.8906 -0.0319 -0.2241 -0.1369 314 GLN B CB  
1925 C CG  . GLN B 22  ? 0.3970 0.5097 0.9442 -0.0480 -0.2460 -0.1344 314 GLN B CG  
1926 C CD  . GLN B 22  ? 0.4966 0.5754 1.0245 -0.0372 -0.2825 -0.1733 314 GLN B CD  
1927 O OE1 . GLN B 22  ? 0.4783 0.5275 0.9656 -0.0200 -0.2908 -0.2045 314 GLN B OE1 
1928 N NE2 . GLN B 22  ? 0.5018 0.5858 1.0571 -0.0467 -0.3031 -0.1741 314 GLN B NE2 
1929 N N   . MET B 23  ? 0.4379 0.5422 0.8906 -0.0123 -0.1571 -0.1060 315 MET B N   
1930 C CA  . MET B 23  ? 0.4043 0.5165 0.8175 0.0031  -0.1289 -0.1042 315 MET B CA  
1931 C C   . MET B 23  ? 0.2905 0.4256 0.7088 -0.0060 -0.1077 -0.0677 315 MET B C   
1932 O O   . MET B 23  ? 0.3218 0.4766 0.7064 0.0023  -0.0864 -0.0622 315 MET B O   
1933 C CB  . MET B 23  ? 0.4003 0.4845 0.8190 0.0152  -0.1319 -0.1239 315 MET B CB  
1934 C CG  . MET B 23  ? 0.5538 0.6515 0.9517 0.0277  -0.1050 -0.1219 315 MET B CG  
1935 S SD  . MET B 23  ? 0.5962 0.7132 0.9328 0.0409  -0.0788 -0.1434 315 MET B SD  
1936 C CE  . MET B 23  ? 0.4027 0.4949 0.7286 0.0553  -0.0914 -0.1917 315 MET B CE  
1937 N N   . VAL B 24  ? 0.3117 0.4395 0.7661 -0.0242 -0.1134 -0.0426 316 VAL B N   
1938 C CA  . VAL B 24  ? 0.3175 0.4650 0.7675 -0.0339 -0.0922 -0.0091 316 VAL B CA  
1939 C C   . VAL B 24  ? 0.2666 0.4557 0.7139 -0.0355 -0.0787 -0.0036 316 VAL B C   
1940 O O   . VAL B 24  ? 0.2829 0.4912 0.7018 -0.0273 -0.0576 0.0055  316 VAL B O   
1941 C CB  . VAL B 24  ? 0.3375 0.4639 0.8178 -0.0571 -0.0999 0.0189  316 VAL B CB  
1942 C CG1 . VAL B 24  ? 0.4701 0.6182 0.9346 -0.0681 -0.0742 0.0521  316 VAL B CG1 
1943 C CG2 . VAL B 24  ? 0.2994 0.3784 0.7807 -0.0503 -0.1184 0.0145  316 VAL B CG2 
1944 N N   . SER B 25  ? 0.2611 0.4635 0.7426 -0.0445 -0.0945 -0.0118 317 SER B N   
1945 C CA  . SER B 25  ? 0.2309 0.4764 0.7248 -0.0436 -0.0874 -0.0092 317 SER B CA  
1946 C C   . SER B 25  ? 0.2027 0.4514 0.6455 -0.0187 -0.0834 -0.0247 317 SER B C   
1947 O O   . SER B 25  ? 0.2694 0.5449 0.7039 -0.0111 -0.0691 -0.0167 317 SER B O   
1948 C CB  . SER B 25  ? 0.2293 0.4800 0.7610 -0.0550 -0.1097 -0.0195 317 SER B CB  
1949 O OG  . SER B 25  ? 0.4506 0.6999 1.0197 -0.0814 -0.1038 0.0014  317 SER B OG  
1950 N N   . ALA B 26  ? 0.2777 0.4963 0.6836 -0.0062 -0.0948 -0.0472 318 ALA B N   
1951 C CA  . ALA B 26  ? 0.3145 0.5281 0.6629 0.0124  -0.0886 -0.0579 318 ALA B CA  
1952 C C   . ALA B 26  ? 0.2572 0.4720 0.5763 0.0173  -0.0603 -0.0434 318 ALA B C   
1953 O O   . ALA B 26  ? 0.3371 0.5579 0.6254 0.0269  -0.0512 -0.0391 318 ALA B O   
1954 C CB  . ALA B 26  ? 0.2518 0.4341 0.5627 0.0213  -0.1010 -0.0856 318 ALA B CB  
1955 N N   . LEU B 27  ? 0.2284 0.4333 0.5580 0.0115  -0.0509 -0.0365 319 LEU B N   
1956 C CA  . LEU B 27  ? 0.2438 0.4489 0.5499 0.0156  -0.0301 -0.0256 319 LEU B CA  
1957 C C   . LEU B 27  ? 0.2843 0.5105 0.5968 0.0115  -0.0182 -0.0033 319 LEU B C   
1958 O O   . LEU B 27  ? 0.2931 0.5220 0.5767 0.0190  -0.0046 0.0011  319 LEU B O   
1959 C CB  . LEU B 27  ? 0.1661 0.3541 0.4859 0.0137  -0.0311 -0.0273 319 LEU B CB  
1960 C CG  . LEU B 27  ? 0.2967 0.4695 0.6103 0.0225  -0.0349 -0.0554 319 LEU B CG  
1961 C CD1 . LEU B 27  ? 0.2047 0.3643 0.5464 0.0248  -0.0404 -0.0594 319 LEU B CD1 
1962 C CD2 . LEU B 27  ? 0.2931 0.4702 0.5630 0.0303  -0.0163 -0.0658 319 LEU B CD2 
1963 N N   . LEU B 28  ? 0.1747 0.4153 0.5245 -0.0017 -0.0215 0.0097  320 LEU B N   
1964 C CA  . LEU B 28  ? 0.2612 0.5280 0.6164 -0.0056 -0.0041 0.0277  320 LEU B CA  
1965 C C   . LEU B 28  ? 0.3368 0.6277 0.6881 0.0084  -0.0017 0.0188  320 LEU B C   
1966 O O   . LEU B 28  ? 0.3394 0.6404 0.6708 0.0175  0.0140  0.0238  320 LEU B O   
1967 C CB  . LEU B 28  ? 0.1806 0.4611 0.5799 -0.0273 -0.0032 0.0439  320 LEU B CB  
1968 C CG  . LEU B 28  ? 0.2110 0.4591 0.6090 -0.0423 -0.0073 0.0605  320 LEU B CG  
1969 C CD1 . LEU B 28  ? 0.2024 0.4608 0.6410 -0.0691 -0.0039 0.0807  320 LEU B CD1 
1970 C CD2 . LEU B 28  ? 0.1827 0.4167 0.5354 -0.0362 0.0057  0.0732  320 LEU B CD2 
1971 N N   . ASP B 29  ? 0.2705 0.5659 0.6383 0.0126  -0.0215 0.0039  321 ASP B N   
1972 C CA  . ASP B 29  ? 0.2211 0.5323 0.5850 0.0292  -0.0284 -0.0049 321 ASP B CA  
1973 C C   . ASP B 29  ? 0.3440 0.6248 0.6454 0.0454  -0.0259 -0.0095 321 ASP B C   
1974 O O   . ASP B 29  ? 0.3594 0.6439 0.6486 0.0610  -0.0293 -0.0119 321 ASP B O   
1975 C CB  . ASP B 29  ? 0.3970 0.7139 0.7892 0.0298  -0.0584 -0.0201 321 ASP B CB  
1976 C CG  . ASP B 29  ? 0.5430 0.8920 0.9954 0.0125  -0.0593 -0.0149 321 ASP B CG  
1977 O OD1 . ASP B 29  ? 0.6501 1.0285 1.1172 0.0087  -0.0363 -0.0037 321 ASP B OD1 
1978 O OD2 . ASP B 29  ? 0.4930 0.8331 0.9681 0.0018  -0.0812 -0.0238 321 ASP B OD2 
1979 N N   . ALA B 30  ? 0.3220 0.5727 0.5886 0.0415  -0.0203 -0.0112 322 ALA B N   
1980 C CA  . ALA B 30  ? 0.3395 0.5621 0.5515 0.0500  -0.0139 -0.0141 322 ALA B CA  
1981 C C   . ALA B 30  ? 0.3084 0.5293 0.5074 0.0505  0.0050  -0.0038 322 ALA B C   
1982 O O   . ALA B 30  ? 0.4013 0.5986 0.5615 0.0539  0.0108  -0.0047 322 ALA B O   
1983 C CB  . ALA B 30  ? 0.3341 0.5335 0.5232 0.0447  -0.0134 -0.0255 322 ALA B CB  
1984 N N   . GLU B 31  ? 0.2085 0.4502 0.4347 0.0454  0.0140  0.0062  323 GLU B N   
1985 C CA  . GLU B 31  ? 0.2754 0.5106 0.4822 0.0459  0.0276  0.0134  323 GLU B CA  
1986 C C   . GLU B 31  ? 0.2655 0.4919 0.4447 0.0604  0.0299  0.0103  323 GLU B C   
1987 O O   . GLU B 31  ? 0.2354 0.4780 0.4276 0.0717  0.0258  0.0072  323 GLU B O   
1988 C CB  . GLU B 31  ? 0.2015 0.4568 0.4288 0.0381  0.0369  0.0260  323 GLU B CB  
1989 C CG  . GLU B 31  ? 0.1827 0.4246 0.4163 0.0251  0.0332  0.0338  323 GLU B CG  
1990 C CD  . GLU B 31  ? 0.2118 0.4303 0.4214 0.0278  0.0309  0.0290  323 GLU B CD  
1991 O OE1 . GLU B 31  ? 0.3635 0.5756 0.5505 0.0298  0.0352  0.0347  323 GLU B OE1 
1992 O OE2 . GLU B 31  ? 0.3358 0.5444 0.5506 0.0277  0.0252  0.0175  323 GLU B OE2 
1993 N N   . PRO B 32  ? 0.2351 0.4355 0.3823 0.0607  0.0339  0.0093  324 PRO B N   
1994 C CA  . PRO B 32  ? 0.2020 0.3833 0.3215 0.0736  0.0326  0.0063  324 PRO B CA  
1995 C C   . PRO B 32  ? 0.3049 0.5028 0.4291 0.0839  0.0405  0.0058  324 PRO B C   
1996 O O   . PRO B 32  ? 0.3326 0.5492 0.4677 0.0764  0.0499  0.0114  324 PRO B O   
1997 C CB  . PRO B 32  ? 0.2163 0.3663 0.3090 0.0639  0.0355  0.0059  324 PRO B CB  
1998 C CG  . PRO B 32  ? 0.3710 0.5352 0.4850 0.0517  0.0399  0.0075  324 PRO B CG  
1999 C CD  . PRO B 32  ? 0.2793 0.4669 0.4222 0.0491  0.0372  0.0093  324 PRO B CD  
2000 N N   . PRO B 33  ? 0.3667 0.5550 0.4788 0.1020  0.0367  -0.0015 325 PRO B N   
2001 C CA  . PRO B 33  ? 0.3728 0.5781 0.4859 0.1150  0.0480  -0.0078 325 PRO B CA  
2002 C C   . PRO B 33  ? 0.2980 0.4765 0.3755 0.1103  0.0516  -0.0090 325 PRO B C   
2003 O O   . PRO B 33  ? 0.3223 0.4686 0.3817 0.0992  0.0433  -0.0067 325 PRO B O   
2004 C CB  . PRO B 33  ? 0.2629 0.4588 0.3766 0.1399  0.0369  -0.0197 325 PRO B CB  
2005 C CG  . PRO B 33  ? 0.3273 0.4755 0.4123 0.1354  0.0185  -0.0148 325 PRO B CG  
2006 C CD  . PRO B 33  ? 0.2396 0.3969 0.3325 0.1132  0.0206  -0.0048 325 PRO B CD  
2007 N N   . ILE B 34  ? 0.3346 0.5288 0.4028 0.1182  0.0647  -0.0141 326 ILE B N   
2008 C CA  . ILE B 34  ? 0.4364 0.6027 0.4640 0.1179  0.0632  -0.0193 326 ILE B CA  
2009 C C   . ILE B 34  ? 0.3221 0.4575 0.3289 0.1388  0.0548  -0.0372 326 ILE B C   
2010 O O   . ILE B 34  ? 0.3412 0.4942 0.3542 0.1608  0.0634  -0.0505 326 ILE B O   
2011 C CB  . ILE B 34  ? 0.4290 0.6186 0.4400 0.1160  0.0808  -0.0160 326 ILE B CB  
2012 C CG1 . ILE B 34  ? 0.3464 0.5476 0.3707 0.0932  0.0811  0.0045  326 ILE B CG1 
2013 C CG2 . ILE B 34  ? 0.3831 0.5396 0.3420 0.1224  0.0750  -0.0276 326 ILE B CG2 
2014 C CD1 . ILE B 34  ? 0.3747 0.5911 0.3747 0.0867  0.0984  0.0152  326 ILE B CD1 
2015 N N   . LEU B 35  ? 0.4093 0.4989 0.3969 0.1316  0.0379  -0.0386 327 LEU B N   
2016 C CA  . LEU B 35  ? 0.3858 0.4322 0.3523 0.1478  0.0248  -0.0532 327 LEU B CA  
2017 C C   . LEU B 35  ? 0.5612 0.5891 0.4931 0.1574  0.0231  -0.0707 327 LEU B C   
2018 O O   . LEU B 35  ? 0.4834 0.5234 0.4002 0.1471  0.0279  -0.0683 327 LEU B O   
2019 C CB  . LEU B 35  ? 0.4114 0.4127 0.3717 0.1304  0.0094  -0.0445 327 LEU B CB  
2020 C CG  . LEU B 35  ? 0.4182 0.4275 0.3957 0.1207  0.0101  -0.0289 327 LEU B CG  
2021 C CD1 . LEU B 35  ? 0.4380 0.3945 0.3949 0.1054  -0.0004 -0.0210 327 LEU B CD1 
2022 C CD2 . LEU B 35  ? 0.3766 0.4073 0.3698 0.1446  0.0086  -0.0324 327 LEU B CD2 
2023 N N   . TYR B 36  ? 0.4689 0.4610 0.3836 0.1789  0.0124  -0.0896 328 TYR B N   
2024 C CA  . TYR B 36  ? 0.5226 0.4898 0.3990 0.1928  0.0079  -0.1129 328 TYR B CA  
2025 C C   . TYR B 36  ? 0.5599 0.4609 0.4172 0.1816  -0.0195 -0.1184 328 TYR B C   
2026 O O   . TYR B 36  ? 0.5641 0.4319 0.4342 0.1721  -0.0321 -0.1078 328 TYR B O   
2027 C CB  . TYR B 36  ? 0.5598 0.5367 0.4345 0.2300  0.0167  -0.1379 328 TYR B CB  
2028 C CG  . TYR B 36  ? 0.5494 0.5916 0.4291 0.2386  0.0496  -0.1414 328 TYR B CG  
2029 C CD1 . TYR B 36  ? 0.5129 0.6119 0.4401 0.2337  0.0675  -0.1252 328 TYR B CD1 
2030 C CD2 . TYR B 36  ? 0.5990 0.6437 0.4326 0.2491  0.0632  -0.1606 328 TYR B CD2 
2031 C CE1 . TYR B 36  ? 0.4952 0.6539 0.4317 0.2356  0.1004  -0.1256 328 TYR B CE1 
2032 C CE2 . TYR B 36  ? 0.6446 0.7474 0.4761 0.2523  0.0990  -0.1603 328 TYR B CE2 
2033 C CZ  . TYR B 36  ? 0.5479 0.7077 0.4356 0.2422  0.1182  -0.1407 328 TYR B CZ  
2034 O OH  . TYR B 36  ? 0.6239 0.8327 0.5189 0.2303  0.1517  -0.1332 328 TYR B OH  
2035 N N   . SER B 37  ? 0.5990 0.4785 0.4225 0.1807  -0.0294 -0.1344 329 SER B N   
2036 C CA  . SER B 37  ? 0.6454 0.4611 0.4551 0.1708  -0.0582 -0.1453 329 SER B CA  
2037 C C   . SER B 37  ? 0.7811 0.5479 0.5797 0.1969  -0.0706 -0.1643 329 SER B C   
2038 O O   . SER B 37  ? 0.7252 0.5063 0.5119 0.2310  -0.0601 -0.1849 329 SER B O   
2039 C CB  . SER B 37  ? 0.6852 0.4881 0.4581 0.1688  -0.0718 -0.1632 329 SER B CB  
2040 O OG  . SER B 37  ? 0.7868 0.5280 0.5533 0.1578  -0.1032 -0.1769 329 SER B OG  
2041 N N   . GLU B 38  ? 0.7773 0.4855 0.5824 0.1804  -0.0926 -0.1574 330 GLU B N   
2042 C CA  . GLU B 38  ? 0.8161 0.4604 0.6073 0.2034  -0.1127 -0.1734 330 GLU B CA  
2043 C C   . GLU B 38  ? 1.0084 0.6047 0.7657 0.2152  -0.1345 -0.2079 330 GLU B C   
2044 O O   . GLU B 38  ? 1.1964 0.7189 0.9463 0.2043  -0.1631 -0.2136 330 GLU B O   
2045 C CB  . GLU B 38  ? 0.8545 0.4457 0.6566 0.1770  -0.1270 -0.1474 330 GLU B CB  
2046 C CG  . GLU B 38  ? 0.9826 0.5317 0.7789 0.2043  -0.1398 -0.1464 330 GLU B CG  
2047 C CD  . GLU B 38  ? 0.9508 0.4391 0.7414 0.1740  -0.1528 -0.1150 330 GLU B CD  
2048 O OE1 . GLU B 38  ? 1.2001 0.6165 0.9768 0.1538  -0.1737 -0.1156 330 GLU B OE1 
2049 O OE2 . GLU B 38  ? 0.8507 0.3607 0.6475 0.1686  -0.1420 -0.0894 330 GLU B OE2 
2050 N N   . TYR B 39  ? 0.9663 0.6002 0.6982 0.2362  -0.1214 -0.2310 331 TYR B N   
2051 C CA  . TYR B 39  ? 1.0529 0.6483 0.7407 0.2461  -0.1411 -0.2654 331 TYR B CA  
2052 C C   . TYR B 39  ? 1.2474 0.8564 0.9204 0.2833  -0.1296 -0.2897 331 TYR B C   
2053 O O   . TYR B 39  ? 1.2761 0.9470 0.9615 0.3025  -0.0976 -0.2878 331 TYR B O   
2054 C CB  . TYR B 39  ? 1.0393 0.6772 0.7070 0.2288  -0.1334 -0.2609 331 TYR B CB  
2055 C CG  . TYR B 39  ? 1.2447 0.8666 0.8538 0.2460  -0.1432 -0.2938 331 TYR B CG  
2056 C CD1 . TYR B 39  ? 1.1540 0.7164 0.7513 0.2411  -0.1777 -0.3124 331 TYR B CD1 
2057 C CD2 . TYR B 39  ? 1.2175 0.8928 0.7906 0.2590  -0.1141 -0.2957 331 TYR B CD2 
2058 C CE1 . TYR B 39  ? 1.4280 0.9833 0.9763 0.2529  -0.1852 -0.3358 331 TYR B CE1 
2059 C CE2 . TYR B 39  ? 1.2797 0.9449 0.7992 0.2677  -0.1190 -0.3161 331 TYR B CE2 
2060 C CZ  . TYR B 39  ? 1.3425 0.9476 0.8484 0.2668  -0.1554 -0.3378 331 TYR B CZ  
2061 O OH  . TYR B 39  ? 1.2223 0.8155 0.6705 0.2772  -0.1609 -0.3599 331 TYR B OH  
2062 N N   . ASP B 40  ? 1.0198 0.9954 1.2531 0.0397  -0.0146 -0.4124 332 ASP B N   
2063 C CA  . ASP B 40  ? 0.9907 1.0058 1.2693 0.0643  -0.0283 -0.4645 332 ASP B CA  
2064 C C   . ASP B 40  ? 1.0046 1.0752 1.3205 0.0349  0.0231  -0.4867 332 ASP B C   
2065 O O   . ASP B 40  ? 0.9986 1.0357 1.2800 0.0102  0.0444  -0.4566 332 ASP B O   
2066 C CB  . ASP B 40  ? 1.0953 1.0353 1.3268 0.0875  -0.0631 -0.4498 332 ASP B CB  
2067 C CG  . ASP B 40  ? 1.2010 1.1464 1.4547 0.1421  -0.1041 -0.4948 332 ASP B CG  
2068 O OD1 . ASP B 40  ? 1.1682 1.1849 1.4861 0.1568  -0.0895 -0.5444 332 ASP B OD1 
2069 O OD2 . ASP B 40  ? 1.2878 1.1646 1.4935 0.1727  -0.1484 -0.4791 332 ASP B OD2 
2070 N N   . PRO B 41  ? 0.9627 1.1168 1.3457 0.0334  0.0434  -0.5375 333 PRO B N   
2071 C CA  . PRO B 41  ? 0.8787 1.0755 1.2887 0.0046  0.0971  -0.5604 333 PRO B CA  
2072 C C   . PRO B 41  ? 0.8777 1.0544 1.2819 0.0215  0.0967  -0.5782 333 PRO B C   
2073 O O   . PRO B 41  ? 0.8645 1.0537 1.2691 -0.0037 0.1413  -0.5906 333 PRO B O   
2074 C CB  . PRO B 41  ? 0.8620 1.1558 1.3507 0.0007  0.1125  -0.6141 333 PRO B CB  
2075 C CG  . PRO B 41  ? 0.8858 1.1787 1.3725 0.0153  0.0689  -0.6068 333 PRO B CG  
2076 C CD  . PRO B 41  ? 1.0083 1.2246 1.4456 0.0544  0.0176  -0.5764 333 PRO B CD  
2077 N N   . THR B 42  ? 0.9141 1.0464 1.2994 0.0629  0.0499  -0.5796 334 THR B N   
2078 C CA  . THR B 42  ? 1.0660 1.1571 1.4272 0.0820  0.0488  -0.5970 334 THR B CA  
2079 C C   . THR B 42  ? 1.0500 1.0334 1.3177 0.0682  0.0266  -0.5480 334 THR B C   
2080 O O   . THR B 42  ? 1.0634 1.0006 1.2885 0.0584  0.0391  -0.5526 334 THR B O   
2081 C CB  . THR B 42  ? 1.0404 1.1532 1.4438 0.1441  0.0163  -0.6399 334 THR B CB  
2082 O OG1 . THR B 42  ? 1.0346 1.0724 1.3852 0.1735  -0.0391 -0.6110 334 THR B OG1 
2083 C CG2 . THR B 42  ? 0.9334 1.1669 1.4394 0.1555  0.0223  -0.6806 334 THR B CG2 
2084 N N   . ARG B 43  ? 1.0734 1.0133 1.3043 0.0636  -0.0049 -0.5014 335 ARG B N   
2085 C CA  . ARG B 43  ? 1.1860 1.0355 1.3372 0.0422  -0.0252 -0.4518 335 ARG B CA  
2086 C C   . ARG B 43  ? 1.2300 1.0903 1.3657 -0.0119 0.0082  -0.4106 335 ARG B C   
2087 O O   . ARG B 43  ? 1.2175 1.1388 1.3924 -0.0283 0.0430  -0.4078 335 ARG B O   
2088 C CB  . ARG B 43  ? 1.2644 1.0655 1.3845 0.0563  -0.0652 -0.4159 335 ARG B CB  
2089 N N   . PRO B 44  ? 1.2377 1.0368 1.3121 -0.0406 -0.0031 -0.3772 336 PRO B N   
2090 C CA  . PRO B 44  ? 1.1923 1.0092 1.2545 -0.0881 0.0235  -0.3370 336 PRO B CA  
2091 C C   . PRO B 44  ? 1.1737 1.0218 1.2561 -0.1018 0.0333  -0.2831 336 PRO B C   
2092 O O   . PRO B 44  ? 1.2174 1.0452 1.2972 -0.0868 0.0103  -0.2611 336 PRO B O   
2093 C CB  . PRO B 44  ? 1.2868 1.0272 1.2757 -0.1155 -0.0063 -0.3109 336 PRO B CB  
2094 C CG  . PRO B 44  ? 1.3833 1.0566 1.3407 -0.0865 -0.0481 -0.3190 336 PRO B CG  
2095 C CD  . PRO B 44  ? 1.4175 1.1248 1.4247 -0.0328 -0.0412 -0.3766 336 PRO B CD  
2096 N N   . PHE B 45  ? 1.1137 1.0031 1.2083 -0.1280 0.0716  -0.2610 337 PHE B N   
2097 C CA  . PHE B 45  ? 1.0833 0.9978 1.1911 -0.1383 0.0911  -0.2057 337 PHE B CA  
2098 C C   . PHE B 45  ? 1.1263 1.0209 1.2071 -0.1659 0.0693  -0.1373 337 PHE B C   
2099 O O   . PHE B 45  ? 1.1719 1.0432 1.2201 -0.1905 0.0483  -0.1319 337 PHE B O   
2100 C CB  . PHE B 45  ? 0.9601 0.9197 1.0858 -0.1498 0.1448  -0.2105 337 PHE B CB  
2101 C CG  . PHE B 45  ? 0.8961 0.8727 1.0314 -0.1486 0.1749  -0.1647 337 PHE B CG  
2102 C CD1 . PHE B 45  ? 0.8955 0.8662 1.0422 -0.1270 0.1740  -0.1724 337 PHE B CD1 
2103 C CD2 . PHE B 45  ? 0.8220 0.8138 0.9472 -0.1664 0.2049  -0.1127 337 PHE B CD2 
2104 C CE1 . PHE B 45  ? 0.8296 0.7992 0.9701 -0.1249 0.2076  -0.1309 337 PHE B CE1 
2105 C CE2 . PHE B 45  ? 0.8667 0.8653 0.9947 -0.1584 0.2394  -0.0690 337 PHE B CE2 
2106 C CZ  . PHE B 45  ? 0.8774 0.8599 1.0094 -0.1386 0.2435  -0.0790 337 PHE B CZ  
2107 N N   . SER B 46  ? 1.1184 1.0223 1.2114 -0.1639 0.0755  -0.0843 338 SER B N   
2108 C CA  . SER B 46  ? 1.1283 1.0310 1.2129 -0.1903 0.0573  -0.0148 338 SER B CA  
2109 C C   . SER B 46  ? 1.0464 0.9816 1.1579 -0.1822 0.0921  0.0423  338 SER B C   
2110 O O   . SER B 46  ? 1.0457 0.9752 1.1636 -0.1556 0.1179  0.0260  338 SER B O   
2111 C CB  . SER B 46  ? 1.1428 0.9869 1.1965 -0.1943 0.0086  -0.0123 338 SER B CB  
2112 O OG  . SER B 46  ? 1.1107 0.9633 1.1662 -0.2241 -0.0047 0.0580  338 SER B OG  
2113 N N   . GLU B 47  ? 0.9779 0.9465 1.1032 -0.2055 0.0924  0.1106  339 GLU B N   
2114 C CA  . GLU B 47  ? 0.9280 0.9293 1.0814 -0.1932 0.1307  0.1729  339 GLU B CA  
2115 C C   . GLU B 47  ? 0.9615 0.9349 1.1148 -0.1882 0.1179  0.2058  339 GLU B C   
2116 O O   . GLU B 47  ? 0.8289 0.8026 0.9909 -0.1658 0.1565  0.2379  339 GLU B O   
2117 C CB  . GLU B 47  ? 0.9301 0.9941 1.1098 -0.2141 0.1387  0.2363  339 GLU B CB  
2118 N N   . ALA B 48  ? 1.0512 0.9885 1.1838 -0.2093 0.0684  0.1987  340 ALA B N   
2119 C CA  . ALA B 48  ? 1.0763 0.9735 1.1970 -0.2073 0.0574  0.2271  340 ALA B CA  
2120 C C   . ALA B 48  ? 1.1734 1.0127 1.2641 -0.1675 0.0693  0.1856  340 ALA B C   
2121 O O   . ALA B 48  ? 1.1440 0.9533 1.2231 -0.1556 0.0840  0.2174  340 ALA B O   
2122 C CB  . ALA B 48  ? 1.0139 0.8673 1.1021 -0.2415 0.0022  0.2224  340 ALA B CB  
2123 N N   . SER B 49  ? 1.1000 0.9249 1.1776 -0.1481 0.0631  0.1160  341 SER B N   
2124 C CA  . SER B 49  ? 1.0411 0.8242 1.0956 -0.1133 0.0667  0.0729  341 SER B CA  
2125 C C   . SER B 49  ? 0.9694 0.7810 1.0375 -0.0978 0.1185  0.0698  341 SER B C   
2126 O O   . SER B 49  ? 1.0075 0.7940 1.0578 -0.0758 0.1202  0.0267  341 SER B O   
2127 C CB  . SER B 49  ? 1.1410 0.9011 1.1819 -0.0996 0.0286  -0.0012 341 SER B CB  
2128 O OG  . SER B 49  ? 1.1241 0.9313 1.1902 -0.1121 0.0378  -0.0302 341 SER B OG  
2129 N N   . MET B 50  ? 0.9476 0.8136 0.9651 0.0167  -0.0761 -0.2402 342 MET B N   
2130 C CA  . MET B 50  ? 0.8227 0.7217 0.8132 0.0250  -0.0679 -0.2137 342 MET B CA  
2131 C C   . MET B 50  ? 0.6404 0.5598 0.6748 0.0174  -0.0622 -0.1790 342 MET B C   
2132 O O   . MET B 50  ? 0.7070 0.6433 0.7296 0.0256  -0.0470 -0.1546 342 MET B O   
2133 C CB  . MET B 50  ? 0.9635 0.8757 0.9042 0.0263  -0.0906 -0.2257 342 MET B CB  
2134 C CG  . MET B 50  ? 0.9374 0.8597 0.8179 0.0392  -0.0744 -0.2098 342 MET B CG  
2135 S SD  . MET B 50  ? 1.1093 1.0333 0.9151 0.0446  -0.1025 -0.2148 342 MET B SD  
2136 C CE  . MET B 50  ? 0.8972 0.8462 0.7670 0.0335  -0.1420 -0.2150 342 MET B CE  
2137 N N   . MET B 51  ? 0.6521 0.5693 0.7369 0.0004  -0.0714 -0.1780 343 MET B N   
2138 C CA  . MET B 51  ? 0.6493 0.5802 0.7707 -0.0064 -0.0594 -0.1462 343 MET B CA  
2139 C C   . MET B 51  ? 0.6987 0.6023 0.8256 0.0012  -0.0367 -0.1282 343 MET B C   
2140 O O   . MET B 51  ? 0.7207 0.6359 0.8476 0.0067  -0.0244 -0.1005 343 MET B O   
2141 C CB  . MET B 51  ? 0.5856 0.5237 0.7622 -0.0292 -0.0694 -0.1518 343 MET B CB  
2142 C CG  . MET B 51  ? 0.9117 0.8659 1.0896 -0.0353 -0.1001 -0.1841 343 MET B CG  
2143 S SD  . MET B 51  ? 1.0053 1.0009 1.1435 -0.0185 -0.1177 -0.1745 343 MET B SD  
2144 C CE  . MET B 51  ? 0.9032 0.8795 0.9763 -0.0080 -0.1414 -0.2101 343 MET B CE  
2145 N N   . GLY B 52  ? 0.5654 0.4291 0.6952 0.0035  -0.0340 -0.1451 344 GLY B N   
2146 C CA  . GLY B 52  ? 0.4614 0.2950 0.5924 0.0173  -0.0183 -0.1297 344 GLY B CA  
2147 C C   . GLY B 52  ? 0.4421 0.3009 0.5487 0.0393  -0.0095 -0.1204 344 GLY B C   
2148 O O   . GLY B 52  ? 0.6300 0.4883 0.7414 0.0489  -0.0012 -0.0967 344 GLY B O   
2149 N N   . LEU B 53  ? 0.4428 0.3230 0.5213 0.0462  -0.0107 -0.1398 345 LEU B N   
2150 C CA  . LEU B 53  ? 0.4970 0.4052 0.5582 0.0613  0.0025  -0.1332 345 LEU B CA  
2151 C C   . LEU B 53  ? 0.4445 0.3834 0.5030 0.0549  0.0039  -0.1054 345 LEU B C   
2152 O O   . LEU B 53  ? 0.3817 0.3361 0.4457 0.0637  0.0135  -0.0904 345 LEU B O   
2153 C CB  . LEU B 53  ? 0.5116 0.4285 0.5354 0.0663  0.0072  -0.1598 345 LEU B CB  
2154 C CG  . LEU B 53  ? 0.6666 0.5588 0.6898 0.0805  0.0140  -0.1902 345 LEU B CG  
2155 C CD1 . LEU B 53  ? 0.7219 0.6222 0.6965 0.0838  0.0228  -0.2159 345 LEU B CD1 
2156 C CD2 . LEU B 53  ? 0.6110 0.5071 0.6654 0.1003  0.0271  -0.1837 345 LEU B CD2 
2157 N N   . LEU B 54  ? 0.4496 0.3982 0.5027 0.0411  -0.0077 -0.1010 346 LEU B N   
2158 C CA  . LEU B 54  ? 0.4480 0.4214 0.4965 0.0376  -0.0068 -0.0773 346 LEU B CA  
2159 C C   . LEU B 54  ? 0.3125 0.2816 0.3907 0.0337  -0.0030 -0.0540 346 LEU B C   
2160 O O   . LEU B 54  ? 0.4293 0.4133 0.5028 0.0364  0.0029  -0.0348 346 LEU B O   
2161 C CB  . LEU B 54  ? 0.3998 0.3852 0.4324 0.0301  -0.0234 -0.0829 346 LEU B CB  
2162 C CG  . LEU B 54  ? 0.5186 0.5012 0.5009 0.0359  -0.0264 -0.1016 346 LEU B CG  
2163 C CD1 . LEU B 54  ? 0.4771 0.4641 0.4391 0.0327  -0.0518 -0.1105 346 LEU B CD1 
2164 C CD2 . LEU B 54  ? 0.4632 0.4551 0.4144 0.0421  -0.0068 -0.0891 346 LEU B CD2 
2165 N N   . THR B 55  ? 0.3893 0.3333 0.4931 0.0262  -0.0044 -0.0559 347 THR B N   
2166 C CA  . THR B 55  ? 0.4760 0.4051 0.5954 0.0231  0.0047  -0.0321 347 THR B CA  
2167 C C   . THR B 55  ? 0.4402 0.3535 0.5481 0.0413  0.0106  -0.0219 347 THR B C   
2168 O O   . THR B 55  ? 0.3538 0.2712 0.4544 0.0462  0.0149  -0.0010 347 THR B O   
2169 C CB  . THR B 55  ? 0.4743 0.3731 0.6208 0.0067  0.0062  -0.0361 347 THR B CB  
2170 O OG1 . THR B 55  ? 0.5396 0.4653 0.7100 -0.0105 -0.0014 -0.0454 347 THR B OG1 
2171 C CG2 . THR B 55  ? 0.4414 0.3102 0.5891 0.0047  0.0211  -0.0095 347 THR B CG2 
2172 N N   . ASN B 56  ? 0.3428 0.2392 0.4501 0.0536  0.0087  -0.0392 348 ASN B N   
2173 C CA  . ASN B 56  ? 0.3835 0.2720 0.4892 0.0756  0.0096  -0.0342 348 ASN B CA  
2174 C C   . ASN B 56  ? 0.3207 0.2534 0.4210 0.0826  0.0118  -0.0305 348 ASN B C   
2175 O O   . ASN B 56  ? 0.4195 0.3556 0.5209 0.0943  0.0090  -0.0168 348 ASN B O   
2176 C CB  . ASN B 56  ? 0.4032 0.2714 0.5157 0.0900  0.0081  -0.0591 348 ASN B CB  
2177 C CG  . ASN B 56  ? 0.5965 0.4601 0.7175 0.1177  0.0051  -0.0574 348 ASN B CG  
2178 O OD1 . ASN B 56  ? 0.4957 0.4016 0.6249 0.1284  0.0076  -0.0643 348 ASN B OD1 
2179 N ND2 . ASN B 56  ? 0.5744 0.3851 0.6949 0.1295  -0.0009 -0.0488 348 ASN B ND2 
2180 N N   . LEU B 57  ? 0.3187 0.2814 0.4098 0.0750  0.0160  -0.0430 349 LEU B N   
2181 C CA  . LEU B 57  ? 0.3336 0.3321 0.4192 0.0763  0.0224  -0.0394 349 LEU B CA  
2182 C C   . LEU B 57  ? 0.3276 0.3322 0.4068 0.0688  0.0198  -0.0157 349 LEU B C   
2183 O O   . LEU B 57  ? 0.3022 0.3232 0.3851 0.0741  0.0203  -0.0086 349 LEU B O   
2184 C CB  . LEU B 57  ? 0.3768 0.3917 0.4403 0.0683  0.0304  -0.0543 349 LEU B CB  
2185 C CG  . LEU B 57  ? 0.3701 0.4131 0.4221 0.0633  0.0419  -0.0492 349 LEU B CG  
2186 C CD1 . LEU B 57  ? 0.2464 0.3131 0.3276 0.0741  0.0516  -0.0589 349 LEU B CD1 
2187 C CD2 . LEU B 57  ? 0.3982 0.4409 0.4111 0.0547  0.0500  -0.0585 349 LEU B CD2 
2188 N N   . ALA B 58  ? 0.3091 0.3032 0.3827 0.0569  0.0168  -0.0065 350 ALA B N   
2189 C CA  . ALA B 58  ? 0.2918 0.2910 0.3596 0.0517  0.0174  0.0132  350 ALA B CA  
2190 C C   . ALA B 58  ? 0.3350 0.3151 0.4032 0.0600  0.0170  0.0285  350 ALA B C   
2191 O O   . ALA B 58  ? 0.2920 0.2797 0.3493 0.0627  0.0167  0.0398  350 ALA B O   
2192 C CB  . ALA B 58  ? 0.2832 0.2812 0.3562 0.0393  0.0155  0.0155  350 ALA B CB  
2193 N N   . ASP B 59  ? 0.2504 0.1989 0.3244 0.0648  0.0157  0.0287  351 ASP B N   
2194 C CA  . ASP B 59  ? 0.3298 0.2479 0.3903 0.0757  0.0136  0.0460  351 ASP B CA  
2195 C C   . ASP B 59  ? 0.3954 0.3297 0.4546 0.0950  0.0023  0.0429  351 ASP B C   
2196 O O   . ASP B 59  ? 0.4051 0.3321 0.4451 0.1029  -0.0039 0.0567  351 ASP B O   
2197 C CB  . ASP B 59  ? 0.3409 0.2118 0.4034 0.0779  0.0145  0.0471  351 ASP B CB  
2198 C CG  . ASP B 59  ? 0.4226 0.2775 0.4940 0.0548  0.0268  0.0508  351 ASP B CG  
2199 O OD1 . ASP B 59  ? 0.4887 0.3733 0.5666 0.0413  0.0325  0.0526  351 ASP B OD1 
2200 O OD2 . ASP B 59  ? 0.4315 0.2441 0.5074 0.0502  0.0306  0.0504  351 ASP B OD2 
2201 N N   . ARG B 60  ? 0.3495 0.3081 0.4304 0.1025  -0.0002 0.0222  352 ARG B N   
2202 C CA  . ARG B 60  ? 0.3240 0.3095 0.4202 0.1192  -0.0100 0.0138  352 ARG B CA  
2203 C C   . ARG B 60  ? 0.2491 0.2715 0.3445 0.1079  -0.0071 0.0145  352 ARG B C   
2204 O O   . ARG B 60  ? 0.2919 0.3299 0.3936 0.1174  -0.0189 0.0143  352 ARG B O   
2205 C CB  . ARG B 60  ? 0.4162 0.4202 0.5423 0.1295  -0.0071 -0.0114 352 ARG B CB  
2206 C CG  . ARG B 60  ? 0.3601 0.3222 0.4893 0.1474  -0.0142 -0.0147 352 ARG B CG  
2207 C CD  . ARG B 60  ? 0.3443 0.3279 0.5060 0.1627  -0.0107 -0.0433 352 ARG B CD  
2208 N NE  . ARG B 60  ? 0.4334 0.4198 0.5898 0.1467  0.0059  -0.0595 352 ARG B NE  
2209 C CZ  . ARG B 60  ? 0.2933 0.3208 0.4566 0.1380  0.0215  -0.0768 352 ARG B CZ  
2210 N NH1 . ARG B 60  ? 0.3726 0.4460 0.5587 0.1397  0.0263  -0.0815 352 ARG B NH1 
2211 N NH2 . ARG B 60  ? 0.4298 0.4495 0.5740 0.1260  0.0329  -0.0902 352 ARG B NH2 
2212 N N   . GLU B 61  ? 0.3546 0.3879 0.4413 0.0887  0.0059  0.0142  353 GLU B N   
2213 C CA  . GLU B 61  ? 0.2993 0.3542 0.3788 0.0773  0.0097  0.0172  353 GLU B CA  
2214 C C   . GLU B 61  ? 0.3660 0.4037 0.4232 0.0778  0.0029  0.0350  353 GLU B C   
2215 O O   . GLU B 61  ? 0.2907 0.3418 0.3443 0.0747  -0.0003 0.0350  353 GLU B O   
2216 C CB  . GLU B 61  ? 0.3201 0.3790 0.3860 0.0614  0.0221  0.0155  353 GLU B CB  
2217 C CG  . GLU B 61  ? 0.2951 0.3724 0.3684 0.0578  0.0337  -0.0023 353 GLU B CG  
2218 C CD  . GLU B 61  ? 0.3784 0.4507 0.4217 0.0444  0.0426  0.0000  353 GLU B CD  
2219 O OE1 . GLU B 61  ? 0.3311 0.3877 0.3600 0.0437  0.0377  0.0009  353 GLU B OE1 
2220 O OE2 . GLU B 61  ? 0.4492 0.5306 0.4829 0.0346  0.0530  0.0007  353 GLU B OE2 
2221 N N   . LEU B 62  ? 0.2827 0.2889 0.3238 0.0798  0.0034  0.0487  354 LEU B N   
2222 C CA  . LEU B 62  ? 0.3730 0.3597 0.3863 0.0800  0.0034  0.0652  354 LEU B CA  
2223 C C   . LEU B 62  ? 0.3746 0.3573 0.3749 0.0954  -0.0132 0.0666  354 LEU B C   
2224 O O   . LEU B 62  ? 0.3114 0.2919 0.2887 0.0947  -0.0163 0.0715  354 LEU B O   
2225 C CB  . LEU B 62  ? 0.4060 0.3587 0.4082 0.0770  0.0129  0.0786  354 LEU B CB  
2226 C CG  . LEU B 62  ? 0.4384 0.3765 0.4163 0.0706  0.0252  0.0935  354 LEU B CG  
2227 C CD1 . LEU B 62  ? 0.3625 0.3289 0.3501 0.0606  0.0310  0.0878  354 LEU B CD1 
2228 C CD2 . LEU B 62  ? 0.5529 0.4618 0.5314 0.0623  0.0407  0.1039  354 LEU B CD2 
2229 N N   . VAL B 63  ? 0.3202 0.3014 0.3350 0.1118  -0.0269 0.0599  355 VAL B N   
2230 C CA  . VAL B 63  ? 0.3616 0.3416 0.3673 0.1313  -0.0504 0.0586  355 VAL B CA  
2231 C C   . VAL B 63  ? 0.3655 0.3905 0.3945 0.1246  -0.0575 0.0421  355 VAL B C   
2232 O O   . VAL B 63  ? 0.3440 0.3660 0.3505 0.1279  -0.0712 0.0437  355 VAL B O   
2233 C CB  . VAL B 63  ? 0.3430 0.3156 0.3684 0.1545  -0.0659 0.0518  355 VAL B CB  
2234 C CG1 . VAL B 63  ? 0.4377 0.4060 0.4505 0.1680  -0.0908 0.0513  355 VAL B CG1 
2235 C CG2 . VAL B 63  ? 0.4318 0.3550 0.4384 0.1538  -0.0541 0.0658  355 VAL B CG2 
2236 N N   . HIS B 64  ? 0.3008 0.3645 0.3723 0.1134  -0.0467 0.0249  356 HIS B N   
2237 C CA  . HIS B 64  ? 0.3077 0.4107 0.4051 0.1008  -0.0469 0.0092  356 HIS B CA  
2238 C C   . HIS B 64  ? 0.2735 0.3633 0.3399 0.0823  -0.0362 0.0184  356 HIS B C   
2239 O O   . HIS B 64  ? 0.2723 0.3785 0.3465 0.0733  -0.0417 0.0087  356 HIS B O   
2240 C CB  . HIS B 64  ? 0.1874 0.3268 0.3286 0.0909  -0.0296 -0.0088 356 HIS B CB  
2241 C CG  . HIS B 64  ? 0.1964 0.3563 0.3779 0.1115  -0.0392 -0.0241 356 HIS B CG  
2242 N ND1 . HIS B 64  ? 0.2018 0.4030 0.4306 0.1230  -0.0569 -0.0439 356 HIS B ND1 
2243 C CD2 . HIS B 64  ? 0.2054 0.3503 0.3906 0.1246  -0.0350 -0.0252 356 HIS B CD2 
2244 C CE1 . HIS B 64  ? 0.2158 0.4240 0.4721 0.1424  -0.0614 -0.0541 356 HIS B CE1 
2245 N NE2 . HIS B 64  ? 0.2170 0.3914 0.4489 0.1462  -0.0489 -0.0445 356 HIS B NE2 
2246 N N   . MET B 65  ? 0.2821 0.3431 0.3183 0.0768  -0.0220 0.0345  357 MET B N   
2247 C CA  . MET B 65  ? 0.3311 0.3768 0.3386 0.0660  -0.0140 0.0429  357 MET B CA  
2248 C C   . MET B 65  ? 0.3205 0.3475 0.2962 0.0756  -0.0283 0.0474  357 MET B C   
2249 O O   . MET B 65  ? 0.3120 0.3352 0.2725 0.0682  -0.0283 0.0441  357 MET B O   
2250 C CB  . MET B 65  ? 0.2952 0.3220 0.2883 0.0622  0.0012  0.0559  357 MET B CB  
2251 C CG  . MET B 65  ? 0.2591 0.2776 0.2346 0.0534  0.0107  0.0605  357 MET B CG  
2252 S SD  . MET B 65  ? 0.3441 0.3499 0.3154 0.0534  0.0234  0.0721  357 MET B SD  
2253 C CE  . MET B 65  ? 0.2151 0.2365 0.2096 0.0473  0.0246  0.0644  357 MET B CE  
2254 N N   . ILE B 66  ? 0.3867 0.3948 0.3448 0.0931  -0.0406 0.0550  358 ILE B N   
2255 C CA  . ILE B 66  ? 0.3549 0.3385 0.2688 0.1053  -0.0562 0.0597  358 ILE B CA  
2256 C C   . ILE B 66  ? 0.4141 0.4254 0.3465 0.1070  -0.0810 0.0391  358 ILE B C   
2257 O O   . ILE B 66  ? 0.4117 0.4136 0.3160 0.1045  -0.0888 0.0340  358 ILE B O   
2258 C CB  . ILE B 66  ? 0.5139 0.4620 0.3967 0.1247  -0.0645 0.0748  358 ILE B CB  
2259 C CG1 . ILE B 66  ? 0.5591 0.4880 0.4451 0.1151  -0.0384 0.0886  358 ILE B CG1 
2260 C CG2 . ILE B 66  ? 0.5774 0.4937 0.4068 0.1270  -0.0698 0.0794  358 ILE B CG2 
2261 C CD1 . ILE B 66  ? 0.5013 0.4218 0.3721 0.0993  -0.0128 0.0959  358 ILE B CD1 
2262 N N   . ASN B 67  ? 0.4081 0.4562 0.3925 0.1109  -0.0933 0.0238  359 ASN B N   
2263 C CA  . ASN B 67  ? 0.3571 0.4434 0.3776 0.1091  -0.1158 -0.0006 359 ASN B CA  
2264 C C   . ASN B 67  ? 0.3553 0.4544 0.3884 0.0812  -0.0997 -0.0107 359 ASN B C   
2265 O O   . ASN B 67  ? 0.4746 0.5819 0.5090 0.0756  -0.1167 -0.0262 359 ASN B O   
2266 C CB  . ASN B 67  ? 0.3270 0.4586 0.4142 0.1164  -0.1233 -0.0175 359 ASN B CB  
2267 C CG  . ASN B 67  ? 0.5015 0.6167 0.5777 0.1495  -0.1482 -0.0114 359 ASN B CG  
2268 O OD1 . ASN B 67  ? 0.4968 0.5624 0.5101 0.1591  -0.1555 0.0065  359 ASN B OD1 
2269 N ND2 . ASN B 67  ? 0.5355 0.6809 0.6653 0.1554  -0.1472 -0.0243 359 ASN B ND2 
2270 N N   . TRP B 68  ? 0.3746 0.4708 0.4138 0.0641  -0.0691 -0.0026 360 TRP B N   
2271 C CA  . TRP B 68  ? 0.3009 0.3954 0.3417 0.0398  -0.0528 -0.0078 360 TRP B CA  
2272 C C   . TRP B 68  ? 0.4170 0.4725 0.4051 0.0410  -0.0548 -0.0001 360 TRP B C   
2273 O O   . TRP B 68  ? 0.3740 0.4252 0.3606 0.0275  -0.0580 -0.0126 360 TRP B O   
2274 C CB  . TRP B 68  ? 0.2776 0.3696 0.3241 0.0273  -0.0240 0.0016  360 TRP B CB  
2275 C CG  . TRP B 68  ? 0.3434 0.4110 0.3675 0.0097  -0.0076 0.0062  360 TRP B CG  
2276 C CD1 . TRP B 68  ? 0.3299 0.4023 0.3708 -0.0131 0.0031  -0.0045 360 TRP B CD1 
2277 C CD2 . TRP B 68  ? 0.3351 0.3666 0.3177 0.0145  0.0006  0.0224  360 TRP B CD2 
2278 N NE1 . TRP B 68  ? 0.3191 0.3522 0.3235 -0.0204 0.0152  0.0062  360 TRP B NE1 
2279 C CE2 . TRP B 68  ? 0.3479 0.3598 0.3199 -0.0017 0.0123  0.0214  360 TRP B CE2 
2280 C CE3 . TRP B 68  ? 0.3521 0.3665 0.3094 0.0304  0.0009  0.0367  360 TRP B CE3 
2281 C CZ2 . TRP B 68  ? 0.3775 0.3549 0.3156 0.0029  0.0198  0.0332  360 TRP B CZ2 
2282 C CZ3 . TRP B 68  ? 0.2794 0.2687 0.2116 0.0317  0.0113  0.0461  360 TRP B CZ3 
2283 C CH2 . TRP B 68  ? 0.3359 0.3078 0.2591 0.0207  0.0184  0.0438  360 TRP B CH2 
2284 N N   . ALA B 69  ? 0.3511 0.3768 0.2974 0.0558  -0.0503 0.0183  361 ALA B N   
2285 C CA  . ALA B 69  ? 0.3875 0.3782 0.2845 0.0587  -0.0462 0.0240  361 ALA B CA  
2286 C C   . ALA B 69  ? 0.5453 0.5276 0.4157 0.0666  -0.0723 0.0105  361 ALA B C   
2287 O O   . ALA B 69  ? 0.5154 0.4772 0.3587 0.0614  -0.0724 0.0022  361 ALA B O   
2288 C CB  . ALA B 69  ? 0.3892 0.3561 0.2555 0.0706  -0.0310 0.0448  361 ALA B CB  
2289 N N   . LYS B 70  ? 0.5005 0.4959 0.3760 0.0815  -0.0976 0.0063  362 LYS B N   
2290 C CA  . LYS B 70  ? 0.5852 0.5744 0.4332 0.0925  -0.1307 -0.0090 362 LYS B CA  
2291 C C   . LYS B 70  ? 0.5522 0.5666 0.4382 0.0723  -0.1424 -0.0369 362 LYS B C   
2292 O O   . LYS B 70  ? 0.6224 0.6227 0.4775 0.0749  -0.1649 -0.0529 362 LYS B O   
2293 C CB  . LYS B 70  ? 0.5767 0.5791 0.4325 0.1155  -0.1608 -0.0096 362 LYS B CB  
2294 C CG  . LYS B 70  ? 0.6716 0.6284 0.4662 0.1361  -0.1551 0.0167  362 LYS B CG  
2295 C CD  . LYS B 70  ? 0.7747 0.6883 0.4988 0.1388  -0.1524 0.0196  362 LYS B CD  
2296 C CE  . LYS B 70  ? 0.9264 0.8093 0.6126 0.1543  -0.1591 0.0312  362 LYS B CE  
2297 N NZ  . LYS B 70  ? 0.9257 0.7614 0.5447 0.1537  -0.1344 0.0451  362 LYS B NZ  
2298 N N   . ARG B 71  ? 0.5052 0.5528 0.4543 0.0506  -0.1261 -0.0440 363 ARG B N   
2299 C CA  . ARG B 71  ? 0.4948 0.5658 0.4881 0.0254  -0.1310 -0.0700 363 ARG B CA  
2300 C C   . ARG B 71  ? 0.5117 0.5491 0.4867 0.0035  -0.1032 -0.0660 363 ARG B C   
2301 O O   . ARG B 71  ? 0.5100 0.5539 0.5150 -0.0214 -0.1024 -0.0855 363 ARG B O   
2302 C CB  . ARG B 71  ? 0.5113 0.6385 0.5855 0.0134  -0.1267 -0.0821 363 ARG B CB  
2303 C CG  . ARG B 71  ? 0.4498 0.6122 0.5515 0.0392  -0.1560 -0.0886 363 ARG B CG  
2304 C CD  . ARG B 71  ? 0.4659 0.6882 0.6542 0.0278  -0.1463 -0.1047 363 ARG B CD  
2305 N NE  . ARG B 71  ? 0.5600 0.8165 0.8058 -0.0037 -0.1438 -0.1328 363 ARG B NE  
2306 C CZ  . ARG B 71  ? 0.5173 0.8324 0.8473 -0.0201 -0.1322 -0.1536 363 ARG B CZ  
2307 N NH1 . ARG B 71  ? 0.4691 0.8160 0.8345 -0.0050 -0.1234 -0.1511 363 ARG B NH1 
2308 N NH2 . ARG B 71  ? 0.3390 0.6803 0.7204 -0.0538 -0.1265 -0.1791 363 ARG B NH2 
2309 N N   . VAL B 72  ? 0.5034 0.5045 0.4340 0.0121  -0.0809 -0.0425 364 VAL B N   
2310 C CA  . VAL B 72  ? 0.4839 0.4462 0.3894 0.0001  -0.0607 -0.0391 364 VAL B CA  
2311 C C   . VAL B 72  ? 0.5363 0.4694 0.4014 0.0039  -0.0785 -0.0561 364 VAL B C   
2312 O O   . VAL B 72  ? 0.6088 0.5263 0.4267 0.0261  -0.0891 -0.0518 364 VAL B O   
2313 C CB  . VAL B 72  ? 0.4550 0.3951 0.3324 0.0130  -0.0372 -0.0136 364 VAL B CB  
2314 C CG1 . VAL B 72  ? 0.5444 0.4413 0.3910 0.0102  -0.0232 -0.0127 364 VAL B CG1 
2315 C CG2 . VAL B 72  ? 0.4024 0.3660 0.3151 0.0065  -0.0216 -0.0014 364 VAL B CG2 
2316 N N   . PRO B 73  ? 0.5371 0.4572 0.4144 -0.0182 -0.0811 -0.0762 365 PRO B N   
2317 C CA  . PRO B 73  ? 0.5334 0.4259 0.3730 -0.0155 -0.1026 -0.0987 365 PRO B CA  
2318 C C   . PRO B 73  ? 0.6016 0.4463 0.3708 0.0067  -0.0902 -0.0870 365 PRO B C   
2319 O O   . PRO B 73  ? 0.5721 0.3910 0.3319 0.0076  -0.0630 -0.0719 365 PRO B O   
2320 C CB  . PRO B 73  ? 0.5750 0.4534 0.4452 -0.0484 -0.0976 -0.1188 365 PRO B CB  
2321 C CG  . PRO B 73  ? 0.6100 0.5177 0.5374 -0.0692 -0.0761 -0.1083 365 PRO B CG  
2322 C CD  . PRO B 73  ? 0.4936 0.4232 0.4197 -0.0487 -0.0644 -0.0810 365 PRO B CD  
2323 N N   . GLY B 74  ? 0.5956 0.4291 0.3142 0.0264  -0.1103 -0.0948 366 GLY B N   
2324 C CA  . GLY B 74  ? 0.6812 0.4730 0.3308 0.0478  -0.0947 -0.0863 366 GLY B CA  
2325 C C   . GLY B 74  ? 0.7124 0.5117 0.3413 0.0684  -0.0788 -0.0581 366 GLY B C   
2326 O O   . GLY B 74  ? 0.6863 0.4552 0.2568 0.0857  -0.0638 -0.0521 366 GLY B O   
2327 N N   . PHE B 75  ? 0.6455 0.4821 0.3206 0.0656  -0.0787 -0.0422 367 PHE B N   
2328 C CA  . PHE B 75  ? 0.7849 0.6239 0.4453 0.0811  -0.0618 -0.0161 367 PHE B CA  
2329 C C   . PHE B 75  ? 0.6444 0.4660 0.2448 0.1007  -0.0800 -0.0135 367 PHE B C   
2330 O O   . PHE B 75  ? 0.6633 0.4615 0.2235 0.1118  -0.0574 0.0022  367 PHE B O   
2331 C CB  . PHE B 75  ? 0.6362 0.5141 0.3593 0.0729  -0.0586 -0.0035 367 PHE B CB  
2332 C CG  . PHE B 75  ? 0.5971 0.4749 0.3143 0.0838  -0.0391 0.0213  367 PHE B CG  
2333 C CD1 . PHE B 75  ? 0.4580 0.3299 0.1813 0.0829  -0.0089 0.0335  367 PHE B CD1 
2334 C CD2 . PHE B 75  ? 0.5468 0.4293 0.2558 0.0954  -0.0525 0.0308  367 PHE B CD2 
2335 C CE1 . PHE B 75  ? 0.5257 0.4009 0.2527 0.0886  0.0090  0.0526  367 PHE B CE1 
2336 C CE2 . PHE B 75  ? 0.6719 0.5478 0.3765 0.1015  -0.0327 0.0527  367 PHE B CE2 
2337 C CZ  . PHE B 75  ? 0.5045 0.3799 0.2234 0.0949  -0.0010 0.0620  367 PHE B CZ  
2338 N N   . VAL B 76  ? 0.7710 0.6073 0.3762 0.1031  -0.1189 -0.0293 368 VAL B N   
2339 C CA  . VAL B 76  ? 0.8362 0.6579 0.3997 0.1204  -0.1360 -0.0248 368 VAL B CA  
2340 C C   . VAL B 76  ? 0.8072 0.5903 0.3085 0.1259  -0.1308 -0.0334 368 VAL B C   
2341 O O   . VAL B 76  ? 0.8630 0.6253 0.3226 0.1389  -0.1338 -0.0249 368 VAL B O   
2342 C CB  . VAL B 76  ? 0.9086 0.7630 0.5071 0.1236  -0.1810 -0.0423 368 VAL B CB  
2343 C CG1 . VAL B 76  ? 0.8504 0.7401 0.5054 0.1259  -0.1832 -0.0297 368 VAL B CG1 
2344 C CG2 . VAL B 76  ? 0.6720 0.5459 0.3006 0.1071  -0.2067 -0.0774 368 VAL B CG2 
2345 N N   . ASP B 77  ? 0.7451 0.5136 0.2360 0.1168  -0.1228 -0.0509 369 ASP B N   
2346 C CA  . ASP B 77  ? 0.8231 0.5545 0.2568 0.1231  -0.1134 -0.0599 369 ASP B CA  
2347 C C   . ASP B 77  ? 0.8259 0.5368 0.2313 0.1317  -0.0704 -0.0360 369 ASP B C   
2348 O O   . ASP B 77  ? 0.8945 0.5764 0.2466 0.1405  -0.0623 -0.0380 369 ASP B O   
2349 C CB  . ASP B 77  ? 0.8694 0.5868 0.3064 0.1109  -0.1131 -0.0861 369 ASP B CB  
2350 C CG  . ASP B 77  ? 0.9609 0.6979 0.4325 0.0957  -0.1549 -0.1160 369 ASP B CG  
2351 O OD1 . ASP B 77  ? 0.9828 0.7358 0.4531 0.1011  -0.1880 -0.1241 369 ASP B OD1 
2352 O OD2 . ASP B 77  ? 0.9971 0.7326 0.5020 0.0770  -0.1534 -0.1323 369 ASP B OD2 
2353 N N   . LEU B 78  ? 0.8172 0.5451 0.2608 0.1277  -0.0432 -0.0158 370 LEU B N   
2354 C CA  . LEU B 78  ? 0.8358 0.5546 0.2713 0.1314  -0.0034 0.0037  370 LEU B CA  
2355 C C   . LEU B 78  ? 0.8059 0.5152 0.2170 0.1375  -0.0056 0.0207  370 LEU B C   
2356 O O   . LEU B 78  ? 0.8281 0.5450 0.2433 0.1407  -0.0363 0.0219  370 LEU B O   
2357 C CB  . LEU B 78  ? 0.8049 0.5497 0.2981 0.1238  0.0216  0.0165  370 LEU B CB  
2358 C CG  . LEU B 78  ? 0.7109 0.4606 0.2280 0.1190  0.0227  0.0032  370 LEU B CG  
2359 C CD1 . LEU B 78  ? 0.6874 0.4665 0.2615 0.1126  0.0359  0.0182  370 LEU B CD1 
2360 C CD2 . LEU B 78  ? 0.7735 0.4998 0.2673 0.1258  0.0460  -0.0083 370 LEU B CD2 
2361 N N   . THR B 79  ? 0.8419 0.5330 0.2282 0.1395  0.0278  0.0329  371 THR B N   
2362 C CA  . THR B 79  ? 0.8841 0.5577 0.2436 0.1430  0.0322  0.0513  371 THR B CA  
2363 C C   . THR B 79  ? 0.8768 0.5757 0.2925 0.1351  0.0347  0.0673  371 THR B C   
2364 O O   . THR B 79  ? 0.7427 0.4729 0.2165 0.1262  0.0429  0.0666  371 THR B O   
2365 C CB  . THR B 79  ? 1.0374 0.6858 0.3591 0.1433  0.0721  0.0595  371 THR B CB  
2366 O OG1 . THR B 79  ? 1.0134 0.6864 0.3903 0.1322  0.1068  0.0690  371 THR B OG1 
2367 C CG2 . THR B 79  ? 0.9941 0.6248 0.2742 0.1496  0.0773  0.0405  371 THR B CG2 
2368 N N   . LEU B 80  ? 0.8468 0.5212 0.2774 0.1437  -0.0671 -0.0307 372 LEU B N   
2369 C CA  . LEU B 80  ? 0.7910 0.4716 0.2476 0.1339  -0.0675 -0.0104 372 LEU B CA  
2370 C C   . LEU B 80  ? 0.8259 0.5280 0.3061 0.1215  -0.0281 0.0076  372 LEU B C   
2371 O O   . LEU B 80  ? 0.7864 0.5111 0.3247 0.1102  -0.0246 0.0156  372 LEU B O   
2372 C CB  . LEU B 80  ? 0.7955 0.4540 0.2269 0.1334  -0.0824 0.0043  372 LEU B CB  
2373 C CG  . LEU B 80  ? 0.8906 0.5471 0.3534 0.1370  -0.1205 -0.0043 372 LEU B CG  
2374 C CD1 . LEU B 80  ? 0.8725 0.5055 0.3084 0.1377  -0.1312 0.0105  372 LEU B CD1 
2375 C CD2 . LEU B 80  ? 0.7074 0.3873 0.2299 0.1306  -0.1240 -0.0033 372 LEU B CD2 
2376 N N   . HIS B 81  ? 0.8114 0.5087 0.2488 0.1241  0.0017  0.0130  373 HIS B N   
2377 C CA  . HIS B 81  ? 0.9492 0.6731 0.4178 0.1126  0.0396  0.0283  373 HIS B CA  
2378 C C   . HIS B 81  ? 0.7793 0.5397 0.3218 0.1092  0.0450  0.0149  373 HIS B C   
2379 O O   . HIS B 81  ? 0.7985 0.5843 0.3932 0.0967  0.0574  0.0268  373 HIS B O   
2380 C CB  . HIS B 81  ? 0.8037 0.5234 0.2238 0.1174  0.0712  0.0326  373 HIS B CB  
2381 C CG  . HIS B 81  ? 0.9501 0.6991 0.4015 0.1066  0.1117  0.0488  373 HIS B CG  
2382 N ND1 . HIS B 81  ? 1.0560 0.8079 0.5178 0.0899  0.1258  0.0765  373 HIS B ND1 
2383 C CD2 . HIS B 81  ? 0.8640 0.6438 0.3488 0.1094  0.1388  0.0403  373 HIS B CD2 
2384 C CE1 . HIS B 81  ? 0.9954 0.7808 0.4968 0.0818  0.1597  0.0843  373 HIS B CE1 
2385 N NE2 . HIS B 81  ? 0.9639 0.7678 0.4801 0.0945  0.1685  0.0629  373 HIS B NE2 
2386 N N   . ASP B 82  ? 0.7357 0.4962 0.2822 0.1201  0.0339  -0.0097 374 ASP B N   
2387 C CA  . ASP B 82  ? 0.7020 0.4915 0.3143 0.1178  0.0380  -0.0206 374 ASP B CA  
2388 C C   . ASP B 82  ? 0.6363 0.4371 0.3015 0.1097  0.0142  -0.0202 374 ASP B C   
2389 O O   . ASP B 82  ? 0.6505 0.4779 0.3707 0.1025  0.0225  -0.0161 374 ASP B O   
2390 C CB  . ASP B 82  ? 0.6343 0.4144 0.2333 0.1316  0.0336  -0.0465 374 ASP B CB  
2391 C CG  . ASP B 82  ? 0.8258 0.5993 0.3762 0.1423  0.0623  -0.0498 374 ASP B CG  
2392 O OD1 . ASP B 82  ? 0.8429 0.6271 0.3828 0.1368  0.0904  -0.0296 374 ASP B OD1 
2393 O OD2 . ASP B 82  ? 0.8742 0.6318 0.3983 0.1563  0.0574  -0.0731 374 ASP B OD2 
2394 N N   . GLN B 83  ? 0.6674 0.4494 0.3164 0.1123  -0.0154 -0.0246 375 GLN B N   
2395 C CA  . GLN B 83  ? 0.5172 0.3123 0.2157 0.1061  -0.0349 -0.0240 375 GLN B CA  
2396 C C   . GLN B 83  ? 0.5971 0.4050 0.3180 0.0952  -0.0234 -0.0037 375 GLN B C   
2397 O O   . GLN B 83  ? 0.5879 0.4185 0.3594 0.0890  -0.0231 -0.0025 375 GLN B O   
2398 C CB  . GLN B 83  ? 0.5609 0.3353 0.2385 0.1126  -0.0682 -0.0318 375 GLN B CB  
2399 C CG  . GLN B 83  ? 0.6481 0.4121 0.3169 0.1215  -0.0877 -0.0553 375 GLN B CG  
2400 C CD  . GLN B 83  ? 0.6781 0.4270 0.3363 0.1277  -0.1242 -0.0632 375 GLN B CD  
2401 O OE1 . GLN B 83  ? 0.7092 0.4656 0.3926 0.1249  -0.1356 -0.0546 375 GLN B OE1 
2402 N NE2 . GLN B 83  ? 0.7869 0.5142 0.4082 0.1376  -0.1442 -0.0813 375 GLN B NE2 
2403 N N   . VAL B 84  ? 0.6490 0.4401 0.3305 0.0924  -0.0145 0.0124  376 VAL B N   
2404 C CA  . VAL B 84  ? 0.5497 0.3479 0.2524 0.0806  -0.0060 0.0308  376 VAL B CA  
2405 C C   . VAL B 84  ? 0.4986 0.3269 0.2399 0.0724  0.0202  0.0356  376 VAL B C   
2406 O O   . VAL B 84  ? 0.5341 0.3802 0.3178 0.0640  0.0200  0.0408  376 VAL B O   
2407 C CB  . VAL B 84  ? 0.6012 0.3691 0.2517 0.0783  -0.0034 0.0489  376 VAL B CB  
2408 C CG1 . VAL B 84  ? 0.5742 0.3493 0.2484 0.0631  0.0122  0.0684  376 VAL B CG1 
2409 C CG2 . VAL B 84  ? 0.8206 0.5602 0.4451 0.0866  -0.0355 0.0463  376 VAL B CG2 
2410 N N   . HIS B 85  ? 0.6149 0.4495 0.3420 0.0764  0.0418  0.0325  377 HIS B N   
2411 C CA  . HIS B 85  ? 0.5083 0.3740 0.2756 0.0708  0.0660  0.0369  377 HIS B CA  
2412 C C   . HIS B 85  ? 0.4872 0.3756 0.3069 0.0722  0.0573  0.0260  377 HIS B C   
2413 O O   . HIS B 85  ? 0.4846 0.3974 0.3465 0.0650  0.0647  0.0328  377 HIS B O   
2414 C CB  . HIS B 85  ? 0.5831 0.4508 0.3237 0.0786  0.0915  0.0334  377 HIS B CB  
2415 C CG  . HIS B 85  ? 0.6598 0.5621 0.4479 0.0779  0.1133  0.0327  377 HIS B CG  
2416 N ND1 . HIS B 85  ? 0.7793 0.6927 0.5921 0.0883  0.1115  0.0160  377 HIS B ND1 
2417 C CD2 . HIS B 85  ? 0.7437 0.6720 0.5633 0.0683  0.1355  0.0469  377 HIS B CD2 
2418 C CE1 . HIS B 85  ? 0.6449 0.5889 0.4995 0.0872  0.1310  0.0200  377 HIS B CE1 
2419 N NE2 . HIS B 85  ? 0.7083 0.6644 0.5700 0.0749  0.1455  0.0380  377 HIS B NE2 
2420 N N   . LEU B 86  ? 0.4654 0.3454 0.2832 0.0809  0.0406  0.0100  378 LEU B N   
2421 C CA  . LEU B 86  ? 0.4077 0.3058 0.2725 0.0811  0.0334  0.0031  378 LEU B CA  
2422 C C   . LEU B 86  ? 0.4811 0.3865 0.3710 0.0736  0.0198  0.0101  378 LEU B C   
2423 O O   . LEU B 86  ? 0.4153 0.3414 0.3422 0.0701  0.0227  0.0135  378 LEU B O   
2424 C CB  . LEU B 86  ? 0.3962 0.2818 0.2563 0.0897  0.0193  -0.0147 378 LEU B CB  
2425 C CG  . LEU B 86  ? 0.4556 0.3332 0.2970 0.0996  0.0309  -0.0271 378 LEU B CG  
2426 C CD1 . LEU B 86  ? 0.5789 0.4424 0.4250 0.1054  0.0121  -0.0457 378 LEU B CD1 
2427 C CD2 . LEU B 86  ? 0.4646 0.3654 0.3380 0.1005  0.0530  -0.0225 378 LEU B CD2 
2428 N N   . LEU B 87  ? 0.4446 0.3320 0.3122 0.0730  0.0041  0.0115  379 LEU B N   
2429 C CA  . LEU B 87  ? 0.4396 0.3320 0.3284 0.0687  -0.0082 0.0157  379 LEU B CA  
2430 C C   . LEU B 87  ? 0.4348 0.3361 0.3356 0.0592  0.0021  0.0287  379 LEU B C   
2431 O O   . LEU B 87  ? 0.4286 0.3448 0.3587 0.0562  -0.0015 0.0295  379 LEU B O   
2432 C CB  . LEU B 87  ? 0.4618 0.3311 0.3248 0.0728  -0.0281 0.0137  379 LEU B CB  
2433 C CG  . LEU B 87  ? 0.6410 0.5092 0.5120 0.0807  -0.0463 -0.0009 379 LEU B CG  
2434 C CD1 . LEU B 87  ? 0.5208 0.3644 0.3602 0.0871  -0.0671 -0.0026 379 LEU B CD1 
2435 C CD2 . LEU B 87  ? 0.5078 0.3987 0.4241 0.0795  -0.0500 -0.0043 379 LEU B CD2 
2436 N N   . GLU B 88  ? 0.4466 0.3389 0.3251 0.0541  0.0149  0.0390  380 GLU B N   
2437 C CA  . GLU B 88  ? 0.5217 0.4230 0.4184 0.0423  0.0238  0.0516  380 GLU B CA  
2438 C C   . GLU B 88  ? 0.3891 0.3226 0.3270 0.0402  0.0347  0.0505  380 GLU B C   
2439 O O   . GLU B 88  ? 0.4176 0.3635 0.3826 0.0322  0.0322  0.0555  380 GLU B O   
2440 C CB  . GLU B 88  ? 0.5513 0.4381 0.4184 0.0358  0.0392  0.0652  380 GLU B CB  
2441 C CG  . GLU B 88  ? 0.6332 0.5296 0.5252 0.0203  0.0490  0.0794  380 GLU B CG  
2442 C CD  . GLU B 88  ? 0.7942 0.6747 0.6568 0.0120  0.0670  0.0963  380 GLU B CD  
2443 O OE1 . GLU B 88  ? 0.8531 0.7036 0.6659 0.0182  0.0633  0.0989  380 GLU B OE1 
2444 O OE2 . GLU B 88  ? 0.9208 0.8194 0.8108 -0.0009 0.0847  0.1077  380 GLU B OE2 
2445 N N   . SER B 89  ? 0.3976 0.3426 0.3406 0.0485  0.0440  0.0430  381 SER B N   
2446 C CA  . SER B 89  ? 0.3400 0.3132 0.3212 0.0493  0.0533  0.0428  381 SER B CA  
2447 C C   . SER B 89  ? 0.2936 0.2756 0.2977 0.0538  0.0399  0.0367  381 SER B C   
2448 O O   . SER B 89  ? 0.3164 0.3194 0.3509 0.0537  0.0419  0.0394  381 SER B O   
2449 C CB  . SER B 89  ? 0.4116 0.3902 0.3876 0.0579  0.0712  0.0377  381 SER B CB  
2450 O OG  . SER B 89  ? 0.6748 0.6781 0.6893 0.0623  0.0767  0.0361  381 SER B OG  
2451 N N   . ALA B 90  ? 0.3028 0.2704 0.2939 0.0580  0.0266  0.0298  382 ALA B N   
2452 C CA  . ALA B 90  ? 0.2952 0.2713 0.3064 0.0621  0.0187  0.0258  382 ALA B CA  
2453 C C   . ALA B 90  ? 0.2320 0.2063 0.2442 0.0602  0.0055  0.0258  382 ALA B C   
2454 O O   . ALA B 90  ? 0.3134 0.2971 0.3406 0.0632  0.0022  0.0247  382 ALA B O   
2455 C CB  . ALA B 90  ? 0.2805 0.2465 0.2866 0.0688  0.0167  0.0162  382 ALA B CB  
2456 N N   . TRP B 91  ? 0.2752 0.2365 0.2710 0.0561  -0.0011 0.0275  383 TRP B N   
2457 C CA  . TRP B 91  ? 0.3223 0.2780 0.3165 0.0581  -0.0144 0.0238  383 TRP B CA  
2458 C C   . TRP B 91  ? 0.3184 0.2893 0.3295 0.0578  -0.0165 0.0248  383 TRP B C   
2459 O O   . TRP B 91  ? 0.3134 0.2887 0.3285 0.0633  -0.0215 0.0200  383 TRP B O   
2460 C CB  . TRP B 91  ? 0.2660 0.1994 0.2385 0.0550  -0.0223 0.0261  383 TRP B CB  
2461 C CG  . TRP B 91  ? 0.4070 0.3390 0.3828 0.0451  -0.0197 0.0342  383 TRP B CG  
2462 C CD1 . TRP B 91  ? 0.2943 0.2258 0.2671 0.0369  -0.0076 0.0434  383 TRP B CD1 
2463 C CD2 . TRP B 91  ? 0.3524 0.2837 0.3376 0.0420  -0.0294 0.0331  383 TRP B CD2 
2464 N NE1 . TRP B 91  ? 0.3825 0.3149 0.3687 0.0266  -0.0098 0.0493  383 TRP B NE1 
2465 C CE2 . TRP B 91  ? 0.4172 0.3471 0.4092 0.0297  -0.0252 0.0419  383 TRP B CE2 
2466 C CE3 . TRP B 91  ? 0.3391 0.2711 0.3276 0.0488  -0.0407 0.0243  383 TRP B CE3 
2467 C CZ2 . TRP B 91  ? 0.4189 0.3454 0.4223 0.0230  -0.0358 0.0410  383 TRP B CZ2 
2468 C CZ3 . TRP B 91  ? 0.3427 0.2698 0.3355 0.0447  -0.0500 0.0224  383 TRP B CZ3 
2469 C CH2 . TRP B 91  ? 0.3601 0.2831 0.3610 0.0313  -0.0494 0.0301  383 TRP B CH2 
2470 N N   . LEU B 92  ? 0.3260 0.3063 0.3471 0.0520  -0.0128 0.0305  384 LEU B N   
2471 C CA  . LEU B 92  ? 0.3082 0.3007 0.3400 0.0528  -0.0189 0.0301  384 LEU B CA  
2472 C C   . LEU B 92  ? 0.3033 0.3109 0.3451 0.0599  -0.0141 0.0313  384 LEU B C   
2473 O O   . LEU B 92  ? 0.3045 0.3171 0.3434 0.0648  -0.0185 0.0297  384 LEU B O   
2474 C CB  . LEU B 92  ? 0.3218 0.3221 0.3674 0.0440  -0.0201 0.0352  384 LEU B CB  
2475 C CG  . LEU B 92  ? 0.3990 0.4073 0.4508 0.0446  -0.0327 0.0323  384 LEU B CG  
2476 C CD1 . LEU B 92  ? 0.3094 0.3001 0.3421 0.0479  -0.0444 0.0235  384 LEU B CD1 
2477 C CD2 . LEU B 92  ? 0.3409 0.3588 0.4145 0.0340  -0.0368 0.0362  384 LEU B CD2 
2478 N N   . GLU B 93  ? 0.2559 0.2684 0.3069 0.0611  -0.0043 0.0345  385 GLU B N   
2479 C CA  . GLU B 93  ? 0.3043 0.3249 0.3653 0.0672  0.0000  0.0375  385 GLU B CA  
2480 C C   . GLU B 93  ? 0.3454 0.3610 0.4018 0.0703  -0.0004 0.0340  385 GLU B C   
2481 O O   . GLU B 93  ? 0.2667 0.2892 0.3274 0.0739  0.0020  0.0385  385 GLU B O   
2482 C CB  . GLU B 93  ? 0.1985 0.2196 0.2704 0.0690  0.0094  0.0388  385 GLU B CB  
2483 C CG  . GLU B 93  ? 0.2327 0.2680 0.3210 0.0693  0.0125  0.0439  385 GLU B CG  
2484 C CD  . GLU B 93  ? 0.3290 0.3636 0.4247 0.0724  0.0242  0.0417  385 GLU B CD  
2485 O OE1 . GLU B 93  ? 0.4348 0.4621 0.5177 0.0688  0.0300  0.0379  385 GLU B OE1 
2486 O OE2 . GLU B 93  ? 0.3166 0.3556 0.4278 0.0798  0.0278  0.0438  385 GLU B OE2 
2487 N N   . ILE B 94  ? 0.2551 0.2597 0.3039 0.0692  -0.0033 0.0270  386 ILE B N   
2488 C CA  . ILE B 94  ? 0.2376 0.2422 0.2913 0.0719  -0.0047 0.0225  386 ILE B CA  
2489 C C   . ILE B 94  ? 0.2810 0.2922 0.3303 0.0755  -0.0078 0.0209  386 ILE B C   
2490 O O   . ILE B 94  ? 0.3007 0.3222 0.3592 0.0787  -0.0023 0.0222  386 ILE B O   
2491 C CB  . ILE B 94  ? 0.2636 0.2548 0.3108 0.0715  -0.0111 0.0145  386 ILE B CB  
2492 C CG1 . ILE B 94  ? 0.2309 0.2142 0.2772 0.0702  -0.0070 0.0134  386 ILE B CG1 
2493 C CG2 . ILE B 94  ? 0.2379 0.2340 0.2989 0.0744  -0.0153 0.0086  386 ILE B CG2 
2494 C CD1 . ILE B 94  ? 0.4071 0.3929 0.4737 0.0707  -0.0041 0.0120  386 ILE B CD1 
2495 N N   . LEU B 95  ? 0.2255 0.2297 0.2608 0.0752  -0.0156 0.0179  387 LEU B N   
2496 C CA  . LEU B 95  ? 0.2769 0.2840 0.3041 0.0807  -0.0197 0.0133  387 LEU B CA  
2497 C C   . LEU B 95  ? 0.2665 0.2867 0.2915 0.0838  -0.0141 0.0193  387 LEU B C   
2498 O O   . LEU B 95  ? 0.3198 0.3479 0.3394 0.0908  -0.0097 0.0174  387 LEU B O   
2499 C CB  . LEU B 95  ? 0.2712 0.2632 0.2852 0.0783  -0.0314 0.0088  387 LEU B CB  
2500 C CG  . LEU B 95  ? 0.3386 0.3119 0.3464 0.0781  -0.0395 0.0038  387 LEU B CG  
2501 C CD1 . LEU B 95  ? 0.3542 0.3095 0.3504 0.0748  -0.0508 0.0013  387 LEU B CD1 
2502 C CD2 . LEU B 95  ? 0.3703 0.3477 0.3838 0.0880  -0.0407 -0.0042 387 LEU B CD2 
2503 N N   . MET B 96  ? 0.2080 0.2314 0.2362 0.0800  -0.0137 0.0270  388 MET B N   
2504 C CA  . MET B 96  ? 0.2804 0.3132 0.3025 0.0842  -0.0126 0.0340  388 MET B CA  
2505 C C   . MET B 96  ? 0.2942 0.3340 0.3218 0.0876  0.0004  0.0428  388 MET B C   
2506 O O   . MET B 96  ? 0.3117 0.3573 0.3253 0.0938  0.0050  0.0462  388 MET B O   
2507 C CB  . MET B 96  ? 0.2485 0.2847 0.2799 0.0804  -0.0175 0.0398  388 MET B CB  
2508 C CG  . MET B 96  ? 0.2733 0.3064 0.3025 0.0755  -0.0307 0.0335  388 MET B CG  
2509 S SD  . MET B 96  ? 0.3062 0.3525 0.3575 0.0714  -0.0357 0.0405  388 MET B SD  
2510 C CE  . MET B 96  ? 0.2772 0.3207 0.3261 0.0653  -0.0551 0.0320  388 MET B CE  
2511 N N   . ILE B 97  ? 0.2315 0.2691 0.2782 0.0834  0.0069  0.0466  389 ILE B N   
2512 C CA  . ILE B 97  ? 0.2475 0.2884 0.3051 0.0839  0.0185  0.0563  389 ILE B CA  
2513 C C   . ILE B 97  ? 0.2354 0.2837 0.2972 0.0849  0.0258  0.0523  389 ILE B C   
2514 O O   . ILE B 97  ? 0.2874 0.3431 0.3525 0.0860  0.0381  0.0622  389 ILE B O   
2515 C CB  . ILE B 97  ? 0.2661 0.2989 0.3443 0.0793  0.0208  0.0580  389 ILE B CB  
2516 C CG1 . ILE B 97  ? 0.3039 0.3352 0.3949 0.0786  0.0308  0.0712  389 ILE B CG1 
2517 C CG2 . ILE B 97  ? 0.2555 0.2828 0.3427 0.0753  0.0175  0.0457  389 ILE B CG2 
2518 C CD1 . ILE B 97  ? 0.1821 0.2009 0.2947 0.0746  0.0316  0.0699  389 ILE B CD1 
2519 N N   . GLY B 98  ? 0.2582 0.3052 0.3215 0.0852  0.0192  0.0391  390 GLY B N   
2520 C CA  . GLY B 98  ? 0.2306 0.2887 0.3015 0.0892  0.0251  0.0335  390 GLY B CA  
2521 C C   . GLY B 98  ? 0.2613 0.3270 0.3086 0.0981  0.0302  0.0336  390 GLY B C   
2522 O O   . GLY B 98  ? 0.2687 0.3490 0.3210 0.1021  0.0447  0.0370  390 GLY B O   
2523 N N   . LEU B 99  ? 0.2853 0.3416 0.3071 0.1012  0.0186  0.0294  391 LEU B N   
2524 C CA  . LEU B 99  ? 0.3477 0.4071 0.3402 0.1108  0.0198  0.0273  391 LEU B CA  
2525 C C   . LEU B 99  ? 0.3217 0.3882 0.3027 0.1127  0.0324  0.0440  391 LEU B C   
2526 O O   . LEU B 99  ? 0.4056 0.4813 0.3695 0.1207  0.0456  0.0467  391 LEU B O   
2527 C CB  . LEU B 99  ? 0.3209 0.3667 0.2939 0.1111  0.0006  0.0191  391 LEU B CB  
2528 C CG  . LEU B 99  ? 0.3194 0.3639 0.2573 0.1209  -0.0044 0.0150  391 LEU B CG  
2529 C CD1 . LEU B 99  ? 0.2928 0.3420 0.2158 0.1332  0.0046  0.0036  391 LEU B CD1 
2530 C CD2 . LEU B 99  ? 0.3615 0.3925 0.2910 0.1175  -0.0268 0.0061  391 LEU B CD2 
2531 N N   . VAL B 100 ? 0.3599 0.4212 0.3486 0.1065  0.0292  0.0561  392 VAL B N   
2532 C CA  . VAL B 100 ? 0.2784 0.3411 0.2560 0.1086  0.0386  0.0747  392 VAL B CA  
2533 C C   . VAL B 100 ? 0.3337 0.4056 0.3276 0.1060  0.0608  0.0854  392 VAL B C   
2534 O O   . VAL B 100 ? 0.3120 0.3877 0.2860 0.1106  0.0747  0.0995  392 VAL B O   
2535 C CB  . VAL B 100 ? 0.2951 0.3494 0.2863 0.1038  0.0298  0.0837  392 VAL B CB  
2536 C CG1 . VAL B 100 ? 0.2815 0.3324 0.2682 0.1055  0.0396  0.1051  392 VAL B CG1 
2537 C CG2 . VAL B 100 ? 0.2512 0.3026 0.2291 0.1066  0.0100  0.0763  392 VAL B CG2 
2538 N N   . TRP B 101 ? 0.3581 0.4338 0.3882 0.0983  0.0641  0.0792  393 TRP B N   
2539 C CA  . TRP B 101 ? 0.2855 0.3723 0.3429 0.0927  0.0833  0.0887  393 TRP B CA  
2540 C C   . TRP B 101 ? 0.2879 0.3936 0.3353 0.1006  0.0997  0.0862  393 TRP B C   
2541 O O   . TRP B 101 ? 0.3460 0.4608 0.3910 0.1003  0.1209  0.1027  393 TRP B O   
2542 C CB  . TRP B 101 ? 0.3036 0.3902 0.4026 0.0835  0.0774  0.0788  393 TRP B CB  
2543 C CG  . TRP B 101 ? 0.3094 0.4125 0.4461 0.0769  0.0933  0.0832  393 TRP B CG  
2544 C CD1 . TRP B 101 ? 0.2220 0.3435 0.3837 0.0784  0.0952  0.0702  393 TRP B CD1 
2545 C CD2 . TRP B 101 ? 0.2370 0.3404 0.3962 0.0673  0.1091  0.1025  393 TRP B CD2 
2546 N NE1 . TRP B 101 ? 0.3743 0.5122 0.5773 0.0694  0.1115  0.0794  393 TRP B NE1 
2547 C CE2 . TRP B 101 ? 0.2685 0.3939 0.4701 0.0613  0.1209  0.1000  393 TRP B CE2 
2548 C CE3 . TRP B 101 ? 0.3196 0.4057 0.4700 0.0633  0.1134  0.1223  393 TRP B CE3 
2549 C CZ2 . TRP B 101 ? 0.3132 0.4444 0.5506 0.0487  0.1382  0.1172  393 TRP B CZ2 
2550 C CZ3 . TRP B 101 ? 0.3147 0.4014 0.4955 0.0521  0.1299  0.1401  393 TRP B CZ3 
2551 C CH2 . TRP B 101 ? 0.3399 0.4492 0.5647 0.0436  0.1427  0.1378  393 TRP B CH2 
2552 N N   . ARG B 102 ? 0.3084 0.4191 0.3494 0.1085  0.0916  0.0664  394 ARG B N   
2553 C CA  . ARG B 102 ? 0.4234 0.5528 0.4564 0.1191  0.1077  0.0605  394 ARG B CA  
2554 C C   . ARG B 102 ? 0.3760 0.5012 0.3540 0.1318  0.1119  0.0632  394 ARG B C   
2555 O O   . ARG B 102 ? 0.4057 0.5460 0.3691 0.1428  0.1297  0.0597  394 ARG B O   
2556 C CB  . ARG B 102 ? 0.4669 0.6000 0.5145 0.1254  0.0958  0.0372  394 ARG B CB  
2557 C CG  . ARG B 102 ? 0.4128 0.5239 0.4314 0.1303  0.0711  0.0227  394 ARG B CG  
2558 C CD  . ARG B 102 ? 0.3137 0.4236 0.3510 0.1351  0.0591  0.0036  394 ARG B CD  
2559 N NE  . ARG B 102 ? 0.3837 0.4695 0.3956 0.1380  0.0365  -0.0085 394 ARG B NE  
2560 C CZ  . ARG B 102 ? 0.3022 0.3704 0.3203 0.1284  0.0193  -0.0087 394 ARG B CZ  
2561 N NH1 . ARG B 102 ? 0.3326 0.4027 0.3764 0.1176  0.0201  -0.0003 394 ARG B NH1 
2562 N NH2 . ARG B 102 ? 0.2859 0.3331 0.2834 0.1297  0.0016  -0.0177 394 ARG B NH2 
2563 N N   . SER B 103 ? 0.4040 0.5102 0.3515 0.1318  0.0957  0.0681  395 SER B N   
2564 C CA  . SER B 103 ? 0.4242 0.5242 0.3173 0.1435  0.0955  0.0723  395 SER B CA  
2565 C C   . SER B 103 ? 0.4987 0.5977 0.3778 0.1411  0.1115  0.1001  395 SER B C   
2566 O O   . SER B 103 ? 0.5714 0.6619 0.4008 0.1510  0.1086  0.1074  395 SER B O   
2567 C CB  . SER B 103 ? 0.3661 0.4477 0.2377 0.1452  0.0653  0.0614  395 SER B CB  
2568 O OG  . SER B 103 ? 0.3459 0.4235 0.2305 0.1455  0.0506  0.0388  395 SER B OG  
2569 N N   . MET B 104 ? 0.5214 0.6261 0.4424 0.1284  0.1264  0.1158  396 MET B N   
2570 C CA  . MET B 104 ? 0.6198 0.7175 0.5327 0.1239  0.1403  0.1448  396 MET B CA  
2571 C C   . MET B 104 ? 0.6293 0.7363 0.5012 0.1338  0.1664  0.1583  396 MET B C   
2572 O O   . MET B 104 ? 0.5958 0.6890 0.4173 0.1420  0.1649  0.1737  396 MET B O   
2573 C CB  . MET B 104 ? 0.5432 0.6434 0.5150 0.1070  0.1501  0.1552  396 MET B CB  
2574 C CG  . MET B 104 ? 0.3565 0.4361 0.3475 0.0994  0.1296  0.1580  396 MET B CG  
2575 S SD  . MET B 104 ? 0.5539 0.6288 0.6035 0.0811  0.1418  0.1730  396 MET B SD  
2576 C CE  . MET B 104 ? 0.4443 0.5044 0.4665 0.0812  0.1603  0.2099  396 MET B CE  
2582 N N   . HIS B 106 ? 0.5630 0.6820 0.3337 0.1689  0.1754  0.1276  398 HIS B N   
2583 C CA  . HIS B 106 ? 0.6113 0.7201 0.3252 0.1859  0.1594  0.1071  398 HIS B CA  
2584 C C   . HIS B 106 ? 0.6530 0.7380 0.3302 0.1884  0.1301  0.1129  398 HIS B C   
2585 O O   . HIS B 106 ? 0.7454 0.8221 0.4235 0.1901  0.1024  0.0976  398 HIS B O   
2586 C CB  . HIS B 106 ? 0.6625 0.7778 0.3889 0.1940  0.1484  0.0754  398 HIS B CB  
2587 C CG  . HIS B 106 ? 0.6669 0.8066 0.4401 0.1914  0.1714  0.0676  398 HIS B CG  
2588 N ND1 . HIS B 106 ? 0.6294 0.7782 0.3876 0.2017  0.1847  0.0537  398 HIS B ND1 
2589 C CD2 . HIS B 106 ? 0.6856 0.8425 0.5236 0.1794  0.1807  0.0707  398 HIS B CD2 
2590 C CE1 . HIS B 106 ? 0.7346 0.9069 0.5481 0.1960  0.2011  0.0492  398 HIS B CE1 
2591 N NE2 . HIS B 106 ? 0.5891 0.7661 0.4520 0.1820  0.1972  0.0589  398 HIS B NE2 
2592 N N   . PRO B 107 ? 0.6778 0.7513 0.3278 0.1874  0.1333  0.1340  399 PRO B N   
2593 C CA  . PRO B 107 ? 0.7578 0.8107 0.3828 0.1892  0.1029  0.1389  399 PRO B CA  
2594 C C   . PRO B 107 ? 0.7442 0.7878 0.3285 0.2018  0.0747  0.1121  399 PRO B C   
2595 O O   . PRO B 107 ? 0.7166 0.7612 0.2667 0.2124  0.0819  0.0975  399 PRO B O   
2596 C CB  . PRO B 107 ? 0.7571 0.8000 0.3571 0.1873  0.1163  0.1651  399 PRO B CB  
2597 C CG  . PRO B 107 ? 0.6997 0.7583 0.3330 0.1775  0.1535  0.1798  399 PRO B CG  
2598 C CD  . PRO B 107 ? 0.7314 0.8103 0.3777 0.1829  0.1639  0.1552  399 PRO B CD  
2599 N N   . GLY B 108 ? 0.6988 0.7331 0.2921 0.1995  0.0417  0.1050  400 GLY B N   
2600 C CA  . GLY B 108 ? 0.7211 0.7455 0.2883 0.2070  0.0107  0.0789  400 GLY B CA  
2601 C C   . GLY B 108 ? 0.6901 0.7185 0.2690 0.2099  0.0056  0.0509  400 GLY B C   
2602 O O   . GLY B 108 ? 0.6681 0.6852 0.2276 0.2152  -0.0194 0.0270  400 GLY B O   
2603 N N   . LYS B 109 ? 0.6906 0.7330 0.3028 0.2060  0.0271  0.0525  401 LYS B N   
2604 C CA  . LYS B 109 ? 0.6457 0.6898 0.2757 0.2075  0.0229  0.0254  401 LYS B CA  
2605 C C   . LYS B 109 ? 0.5688 0.6204 0.2693 0.1892  0.0252  0.0288  401 LYS B C   
2606 O O   . LYS B 109 ? 0.5126 0.5721 0.2433 0.1787  0.0391  0.0509  401 LYS B O   
2607 C CB  . LYS B 109 ? 0.6497 0.7034 0.2609 0.2200  0.0503  0.0155  401 LYS B CB  
2608 N N   . LEU B 110 ? 0.5033 0.5489 0.2266 0.1861  0.0102  0.0064  402 LEU B N   
2609 C CA  . LEU B 110 ? 0.4995 0.5488 0.2802 0.1713  0.0102  0.0064  402 LEU B CA  
2610 C C   . LEU B 110 ? 0.5369 0.5915 0.3315 0.1774  0.0218  -0.0100 402 LEU B C   
2611 O O   . LEU B 110 ? 0.4761 0.5187 0.2505 0.1874  0.0093  -0.0323 402 LEU B O   
2612 C CB  . LEU B 110 ? 0.4092 0.4447 0.2074 0.1608  -0.0194 -0.0016 402 LEU B CB  
2613 C CG  . LEU B 110 ? 0.5203 0.5556 0.3221 0.1539  -0.0320 0.0142  402 LEU B CG  
2614 C CD1 . LEU B 110 ? 0.4959 0.5237 0.3257 0.1422  -0.0561 0.0057  402 LEU B CD1 
2615 C CD2 . LEU B 110 ? 0.3796 0.4257 0.2072 0.1470  -0.0120 0.0375  402 LEU B CD2 
2616 N N   . LEU B 111 ? 0.4929 0.5646 0.3246 0.1720  0.0436  -0.0001 403 LEU B N   
2617 C CA  . LEU B 111 ? 0.4216 0.5037 0.2754 0.1788  0.0546  -0.0142 403 LEU B CA  
2618 C C   . LEU B 111 ? 0.4374 0.5091 0.3295 0.1684  0.0366  -0.0221 403 LEU B C   
2619 O O   . LEU B 111 ? 0.3555 0.4366 0.2874 0.1580  0.0427  -0.0132 403 LEU B O   
2620 C CB  . LEU B 111 ? 0.4158 0.5251 0.2929 0.1784  0.0867  0.0005  403 LEU B CB  
2621 C CG  . LEU B 111 ? 0.5058 0.6346 0.4097 0.1884  0.1018  -0.0133 403 LEU B CG  
2622 C CD1 . LEU B 111 ? 0.4433 0.5787 0.3044 0.2096  0.1171  -0.0252 403 LEU B CD1 
2623 C CD2 . LEU B 111 ? 0.4678 0.6233 0.4229 0.1777  0.1245  0.0029  403 LEU B CD2 
2624 N N   . PHE B 112 ? 0.4611 0.5105 0.3384 0.1709  0.0129  -0.0390 404 PHE B N   
2625 C CA  . PHE B 112 ? 0.3684 0.4036 0.2741 0.1622  -0.0034 -0.0451 404 PHE B CA  
2626 C C   . PHE B 112 ? 0.3930 0.4380 0.3265 0.1695  0.0053  -0.0532 404 PHE B C   
2627 O O   . PHE B 112 ? 0.4715 0.5159 0.4364 0.1606  0.0009  -0.0490 404 PHE B O   
2628 C CB  . PHE B 112 ? 0.3562 0.3634 0.2411 0.1632  -0.0290 -0.0605 404 PHE B CB  
2629 C CG  . PHE B 112 ? 0.4528 0.4525 0.3226 0.1536  -0.0427 -0.0534 404 PHE B CG  
2630 C CD1 . PHE B 112 ? 0.4308 0.4312 0.2629 0.1629  -0.0452 -0.0567 404 PHE B CD1 
2631 C CD2 . PHE B 112 ? 0.4932 0.4867 0.3863 0.1368  -0.0534 -0.0438 404 PHE B CD2 
2632 C CE1 . PHE B 112 ? 0.5173 0.5131 0.3400 0.1553  -0.0617 -0.0510 404 PHE B CE1 
2633 C CE2 . PHE B 112 ? 0.4060 0.3978 0.2937 0.1290  -0.0661 -0.0381 404 PHE B CE2 
2634 C CZ  . PHE B 112 ? 0.4324 0.4258 0.2873 0.1382  -0.0720 -0.0418 404 PHE B CZ  
2635 N N   . ALA B 113 ? 0.4452 0.5005 0.3671 0.1871  0.0171  -0.0657 405 ALA B N   
2636 C CA  . ALA B 113 ? 0.3804 0.4518 0.3334 0.1975  0.0271  -0.0747 405 ALA B CA  
2637 C C   . ALA B 113 ? 0.3825 0.4787 0.3231 0.2117  0.0534  -0.0774 405 ALA B C   
2638 O O   . ALA B 113 ? 0.5258 0.6172 0.4211 0.2195  0.0582  -0.0788 405 ALA B O   
2639 C CB  . ALA B 113 ? 0.3637 0.4090 0.3177 0.2049  0.0046  -0.0939 405 ALA B CB  
2640 N N   . PRO B 114 ? 0.4076 0.5289 0.3875 0.2110  0.0697  -0.0762 406 PRO B N   
2641 C CA  . PRO B 114 ? 0.4118 0.5559 0.3834 0.2194  0.0968  -0.0764 406 PRO B CA  
2642 C C   . PRO B 114 ? 0.4605 0.5871 0.3881 0.2358  0.0910  -0.0958 406 PRO B C   
2643 O O   . PRO B 114 ? 0.4998 0.6372 0.3984 0.2436  0.1111  -0.0946 406 PRO B O   
2644 C CB  . PRO B 114 ? 0.3958 0.5660 0.4282 0.2160  0.1080  -0.0773 406 PRO B CB  
2645 C CG  . PRO B 114 ? 0.3493 0.5173 0.4170 0.2012  0.0938  -0.0673 406 PRO B CG  
2646 C CD  . PRO B 114 ? 0.3780 0.5090 0.4123 0.2018  0.0648  -0.0737 406 PRO B CD  
2647 N N   . ASN B 115 ? 0.4806 0.5779 0.4013 0.2405  0.0635  -0.1129 407 ASN B N   
2648 C CA  . ASN B 115 ? 0.5133 0.5881 0.3936 0.2548  0.0527  -0.1328 407 ASN B CA  
2649 C C   . ASN B 115 ? 0.5250 0.5676 0.3610 0.2531  0.0283  -0.1369 407 ASN B C   
2650 O O   . ASN B 115 ? 0.7673 0.7847 0.5736 0.2621  0.0115  -0.1547 407 ASN B O   
2651 C CB  . ASN B 115 ? 0.5382 0.5994 0.4434 0.2612  0.0378  -0.1492 407 ASN B CB  
2652 C CG  . ASN B 115 ? 0.5757 0.6121 0.5002 0.2496  0.0100  -0.1469 407 ASN B CG  
2653 O OD1 . ASN B 115 ? 0.4793 0.5161 0.4107 0.2362  0.0063  -0.1326 407 ASN B OD1 
2654 N ND2 . ASN B 115 ? 0.7038 0.7171 0.6353 0.2548  -0.0089 -0.1600 407 ASN B ND2 
2655 N N   . LEU B 116 ? 0.6245 0.6243 0.4283 0.2351  0.0823  -0.0817 408 LEU B N   
2656 C CA  . LEU B 116 ? 0.5371 0.5485 0.3301 0.2281  0.0761  -0.1063 408 LEU B CA  
2657 C C   . LEU B 116 ? 0.5099 0.5702 0.3327 0.2397  0.0695  -0.0994 408 LEU B C   
2658 O O   . LEU B 116 ? 0.4689 0.5562 0.3356 0.2285  0.0676  -0.1011 408 LEU B O   
2659 C CB  . LEU B 116 ? 0.5231 0.5260 0.3310 0.2037  0.0800  -0.1214 408 LEU B CB  
2660 C CG  . LEU B 116 ? 0.5800 0.5804 0.3642 0.1935  0.0747  -0.1497 408 LEU B CG  
2661 C CD1 . LEU B 116 ? 0.6244 0.5854 0.3541 0.1965  0.0691  -0.1665 408 LEU B CD1 
2662 C CD2 . LEU B 116 ? 0.5992 0.5955 0.3995 0.1754  0.0827  -0.1573 408 LEU B CD2 
2663 N N   . LEU B 117 ? 0.5578 0.6325 0.3570 0.2642  0.0658  -0.0904 409 LEU B N   
2664 C CA  . LEU B 117 ? 0.5227 0.6481 0.3466 0.2789  0.0604  -0.0809 409 LEU B CA  
2665 C C   . LEU B 117 ? 0.5857 0.7275 0.3723 0.2853  0.0476  -0.1076 409 LEU B C   
2666 O O   . LEU B 117 ? 0.6118 0.7306 0.3445 0.2972  0.0424  -0.1175 409 LEU B O   
2667 C CB  . LEU B 117 ? 0.5216 0.6588 0.3474 0.3037  0.0668  -0.0458 409 LEU B CB  
2668 C CG  . LEU B 117 ? 0.5895 0.7783 0.4429 0.3184  0.0648  -0.0273 409 LEU B CG  
2669 C CD1 . LEU B 117 ? 0.5305 0.7380 0.4601 0.2924  0.0634  -0.0245 409 LEU B CD1 
2670 C CD2 . LEU B 117 ? 0.5951 0.7893 0.4364 0.3426  0.0754  0.0105  409 LEU B CD2 
2671 N N   . LEU B 118 ? 0.5475 0.7300 0.3652 0.2759  0.0397  -0.1214 410 LEU B N   
2672 C CA  . LEU B 118 ? 0.5624 0.7638 0.3504 0.2738  0.0232  -0.1527 410 LEU B CA  
2673 C C   . LEU B 118 ? 0.6043 0.8746 0.4216 0.2913  0.0169  -0.1442 410 LEU B C   
2674 O O   . LEU B 118 ? 0.6023 0.9041 0.4817 0.2909  0.0238  -0.1199 410 LEU B O   
2675 C CB  . LEU B 118 ? 0.5568 0.7488 0.3548 0.2411  0.0176  -0.1832 410 LEU B CB  
2676 C CG  . LEU B 118 ? 0.6740 0.8019 0.4408 0.2214  0.0215  -0.1971 410 LEU B CG  
2677 C CD1 . LEU B 118 ? 0.6791 0.7644 0.3854 0.2303  0.0117  -0.2086 410 LEU B CD1 
2678 C CD2 . LEU B 118 ? 0.6293 0.7324 0.4206 0.2177  0.0416  -0.1722 410 LEU B CD2 
2679 N N   . ASP B 119 ? 0.6572 0.9467 0.4327 0.3019  -0.0001 -0.1635 411 ASP B N   
2680 C CA  . ASP B 119 ? 0.5677 0.9246 0.3700 0.3120  -0.0103 -0.1573 411 ASP B CA  
2681 C C   . ASP B 119 ? 0.5717 0.9380 0.3885 0.2728  -0.0356 -0.1875 411 ASP B C   
2682 O O   . ASP B 119 ? 0.6215 0.9472 0.4305 0.2423  -0.0412 -0.2118 411 ASP B O   
2683 C CB  . ASP B 119 ? 0.7218 1.0999 0.4727 0.3544  -0.0135 -0.1451 411 ASP B CB  
2684 C CG  . ASP B 119 ? 0.8025 1.1396 0.4841 0.3502  -0.0377 -0.1778 411 ASP B CG  
2685 O OD1 . ASP B 119 ? 0.9919 1.3115 0.6671 0.3173  -0.0597 -0.2158 411 ASP B OD1 
2686 O OD2 . ASP B 119 ? 0.9274 1.2506 0.5698 0.3805  -0.0351 -0.1637 411 ASP B OD2 
2687 N N   . ARG B 120 ? 0.6563 1.0795 0.4999 0.2747  -0.0499 -0.1818 412 ARG B N   
2688 C CA  . ARG B 120 ? 0.5792 1.0204 0.4474 0.2385  -0.0739 -0.2057 412 ARG B CA  
2689 C C   . ARG B 120 ? 0.6779 1.0741 0.4923 0.2219  -0.0978 -0.2449 412 ARG B C   
2690 O O   . ARG B 120 ? 0.6311 1.0124 0.4715 0.1834  -0.1089 -0.2640 412 ARG B O   
2691 C CB  . ARG B 120 ? 0.7341 1.2433 0.6289 0.2500  -0.0872 -0.1934 412 ARG B CB  
2692 C CG  . ARG B 120 ? 0.6092 1.1672 0.5804 0.2560  -0.0706 -0.1596 412 ARG B CG  
2693 C CD  . ARG B 120 ? 0.5997 1.2230 0.6002 0.2597  -0.0873 -0.1518 412 ARG B CD  
2694 N NE  . ARG B 120 ? 0.4849 1.1192 0.5096 0.2203  -0.1084 -0.1777 412 ARG B NE  
2695 C CZ  . ARG B 120 ? 0.6421 1.2843 0.6366 0.2106  -0.1371 -0.2027 412 ARG B CZ  
2696 N NH1 . ARG B 120 ? 0.5871 1.2272 0.5169 0.2398  -0.1505 -0.2105 412 ARG B NH1 
2697 N NH2 . ARG B 120 ? 0.5086 1.1636 0.5405 0.1730  -0.1540 -0.2206 412 ARG B NH2 
2698 N N   . ASN B 121 ? 0.7208 1.0966 0.4644 0.2529  -0.1064 -0.2564 413 ASN B N   
2699 C CA  . ASN B 121 ? 0.8154 1.1555 0.5128 0.2420  -0.1383 -0.2996 413 ASN B CA  
2700 C C   . ASN B 121 ? 0.8306 1.1009 0.5234 0.2136  -0.1347 -0.3189 413 ASN B C   
2701 O O   . ASN B 121 ? 1.0152 1.2593 0.7118 0.1851  -0.1618 -0.3516 413 ASN B O   
2702 C CB  . ASN B 121 ? 0.9507 1.2823 0.5901 0.2832  -0.1434 -0.2968 413 ASN B CB  
2703 C CG  . ASN B 121 ? 1.1753 1.5787 0.8196 0.3108  -0.1512 -0.2805 413 ASN B CG  
2704 O OD1 . ASN B 121 ? 1.1482 1.5905 0.8223 0.2910  -0.1746 -0.2941 413 ASN B OD1 
2705 N ND2 . ASN B 121 ? 1.1289 1.5531 0.7504 0.3569  -0.1306 -0.2471 413 ASN B ND2 
2706 N N   . GLN B 122 ? 0.7932 1.0339 0.4840 0.2209  -0.1029 -0.2979 414 GLN B N   
2707 C CA  . GLN B 122 ? 0.9241 1.1058 0.6196 0.1928  -0.0962 -0.3098 414 GLN B CA  
2708 C C   . GLN B 122 ? 0.8419 1.0423 0.6096 0.1493  -0.0952 -0.3048 414 GLN B C   
2709 O O   . GLN B 122 ? 0.9103 1.0706 0.6904 0.1206  -0.0976 -0.3169 414 GLN B O   
2710 C CB  . GLN B 122 ? 0.9121 1.0618 0.5908 0.2127  -0.0625 -0.2853 414 GLN B CB  
2711 C CG  . GLN B 122 ? 0.8469 0.9481 0.4735 0.2347  -0.0605 -0.2805 414 GLN B CG  
2712 C CD  . GLN B 122 ? 0.9678 1.0932 0.5895 0.2723  -0.0402 -0.2416 414 GLN B CD  
2713 O OE1 . GLN B 122 ? 0.9947 1.1782 0.6346 0.2908  -0.0404 -0.2260 414 GLN B OE1 
2714 N NE2 . GLN B 122 ? 0.8522 0.9364 0.4539 0.2838  -0.0234 -0.2244 414 GLN B NE2 
2715 N N   . GLY B 123 ? 0.9181 1.1806 0.7361 0.1463  -0.0909 -0.2852 415 GLY B N   
2716 C CA  . GLY B 123 ? 0.7020 0.9910 0.5862 0.1106  -0.0898 -0.2798 415 GLY B CA  
2717 C C   . GLY B 123 ? 0.7802 1.0896 0.6902 0.0829  -0.1213 -0.3000 415 GLY B C   
2718 O O   . GLY B 123 ? 0.8572 1.1742 0.8180 0.0494  -0.1216 -0.2980 415 GLY B O   
2719 N N   . LYS B 124 ? 0.9308 1.2533 0.8090 0.0984  -0.1482 -0.3178 416 LYS B N   
2720 C CA  . LYS B 124 ? 0.8049 1.1488 0.7104 0.0737  -0.1834 -0.3402 416 LYS B CA  
2721 C C   . LYS B 124 ? 0.8832 1.1713 0.7933 0.0439  -0.2034 -0.3679 416 LYS B C   
2722 O O   . LYS B 124 ? 0.8570 1.1605 0.8149 0.0133  -0.2296 -0.3815 416 LYS B O   
2723 C CB  . LYS B 124 ? 0.7820 1.1545 0.6452 0.1041  -0.2094 -0.3551 416 LYS B CB  
2724 C CG  . LYS B 124 ? 0.7664 1.1905 0.6244 0.1395  -0.1887 -0.3231 416 LYS B CG  
2725 C CD  . LYS B 124 ? 0.7464 1.2155 0.5763 0.1665  -0.2152 -0.3322 416 LYS B CD  
2726 C CE  . LYS B 124 ? 0.8109 1.2832 0.6534 0.1402  -0.2589 -0.3698 416 LYS B CE  
2727 N N   . SER B 125 ? 1.0793 1.3034 0.9480 0.0519  -0.1922 -0.3750 417 SER B N   
2728 C CA  . SER B 125 ? 1.1626 1.3284 1.0414 0.0252  -0.2110 -0.4001 417 SER B CA  
2729 C C   . SER B 125 ? 1.1923 1.3637 1.1508 -0.0178 -0.1985 -0.3800 417 SER B C   
2730 O O   . SER B 125 ? 1.2554 1.3841 1.2424 -0.0446 -0.2138 -0.3942 417 SER B O   
2731 C CB  . SER B 125 ? 1.1557 1.2535 0.9722 0.0471  -0.1974 -0.4079 417 SER B CB  
2732 O OG  . SER B 125 ? 1.0973 1.1710 0.9409 0.0304  -0.1641 -0.3820 417 SER B OG  
2733 N N   . VAL B 126 ? 1.0966 1.3208 1.0946 -0.0223 -0.1715 -0.3466 418 VAL B N   
2734 C CA  . VAL B 126 ? 0.9805 1.2175 1.0452 -0.0531 -0.1517 -0.3213 418 VAL B CA  
2735 C C   . VAL B 126 ? 0.9769 1.2896 1.1006 -0.0661 -0.1545 -0.3062 418 VAL B C   
2736 O O   . VAL B 126 ? 0.9202 1.2773 1.0310 -0.0436 -0.1488 -0.2990 418 VAL B O   
2737 C CB  . VAL B 126 ? 0.9680 1.1907 1.0150 -0.0380 -0.1099 -0.2951 418 VAL B CB  
2738 C CG1 . VAL B 126 ? 0.9436 1.1872 1.0540 -0.0633 -0.0885 -0.2672 418 VAL B CG1 
2739 C CG2 . VAL B 126 ? 1.0792 1.2281 1.0677 -0.0239 -0.1069 -0.3090 418 VAL B CG2 
2740 N N   . GLU B 127 ? 1.0178 1.3463 1.2119 -0.1016 -0.1624 -0.2986 419 GLU B N   
2741 C CA  . GLU B 127 ? 0.9391 1.3404 1.1947 -0.1155 -0.1653 -0.2833 419 GLU B CA  
2742 C C   . GLU B 127 ? 0.7875 1.2333 1.0527 -0.0995 -0.1267 -0.2519 419 GLU B C   
2743 O O   . GLU B 127 ? 0.7046 1.1393 0.9803 -0.1017 -0.0979 -0.2309 419 GLU B O   
2744 C CB  . GLU B 127 ? 0.7252 1.1317 1.0611 -0.1565 -0.1793 -0.2768 419 GLU B CB  
2745 N N   . GLY B 128 ? 0.6467 1.1441 0.9098 -0.0809 -0.1276 -0.2496 420 GLY B N   
2746 C CA  . GLY B 128 ? 0.6150 1.1585 0.8955 -0.0638 -0.0984 -0.2265 420 GLY B CA  
2747 C C   . GLY B 128 ? 0.5357 1.0587 0.7653 -0.0287 -0.0793 -0.2254 420 GLY B C   
2748 O O   . GLY B 128 ? 0.4515 1.0134 0.6986 -0.0105 -0.0616 -0.2122 420 GLY B O   
2749 N N   . MET B 129 ? 0.6872 0.6640 0.7245 0.0180  -0.2333 -0.1178 421 MET B N   
2750 C CA  . MET B 129 ? 0.7790 0.7460 0.7914 0.0458  -0.2137 -0.1131 421 MET B CA  
2751 C C   . MET B 129 ? 0.6199 0.6225 0.6189 0.0710  -0.2039 -0.1128 421 MET B C   
2752 O O   . MET B 129 ? 0.5852 0.6040 0.5847 0.0831  -0.1807 -0.0989 421 MET B O   
2753 C CB  . MET B 129 ? 0.6884 0.6012 0.6686 0.0590  -0.2252 -0.1310 421 MET B CB  
2754 C CG  . MET B 129 ? 0.7556 0.6711 0.7144 0.0912  -0.2071 -0.1354 421 MET B CG  
2755 S SD  . MET B 129 ? 0.9463 0.8035 0.8848 0.1082  -0.2182 -0.1564 421 MET B SD  
2756 C CE  . MET B 129 ? 0.7755 0.5855 0.7280 0.0746  -0.2360 -0.1423 421 MET B CE  
2757 N N   . VAL B 130 ? 0.5762 0.5864 0.5590 0.0776  -0.2232 -0.1272 422 VAL B N   
2758 C CA  . VAL B 130 ? 0.5769 0.6064 0.5303 0.1014  -0.2164 -0.1259 422 VAL B CA  
2759 C C   . VAL B 130 ? 0.4552 0.5251 0.4354 0.1017  -0.2038 -0.1047 422 VAL B C   
2760 O O   . VAL B 130 ? 0.5789 0.6562 0.5354 0.1196  -0.1893 -0.0952 422 VAL B O   
2761 C CB  . VAL B 130 ? 0.6864 0.7088 0.6085 0.1076  -0.2451 -0.1461 422 VAL B CB  
2762 C CG1 . VAL B 130 ? 0.5981 0.6557 0.5538 0.0959  -0.2673 -0.1432 422 VAL B CG1 
2763 C CG2 . VAL B 130 ? 0.7634 0.7800 0.6282 0.1335  -0.2346 -0.1495 422 VAL B CG2 
2764 N N   . GLU B 131 ? 0.5554 0.6506 0.5844 0.0815  -0.2076 -0.0978 423 GLU B N   
2765 C CA  . GLU B 131 ? 0.3970 0.5313 0.4556 0.0848  -0.1954 -0.0818 423 GLU B CA  
2766 C C   . GLU B 131 ? 0.3737 0.5011 0.4288 0.0903  -0.1647 -0.0655 423 GLU B C   
2767 O O   . GLU B 131 ? 0.3970 0.5352 0.4431 0.1063  -0.1529 -0.0545 423 GLU B O   
2768 C CB  . GLU B 131 ? 0.3713 0.5413 0.4877 0.0608  -0.2027 -0.0829 423 GLU B CB  
2769 N N   . ILE B 132 ? 0.3351 0.4397 0.3948 0.0768  -0.1547 -0.0638 424 ILE B N   
2770 C CA  . ILE B 132 ? 0.3307 0.4268 0.3860 0.0825  -0.1306 -0.0510 424 ILE B CA  
2771 C C   . ILE B 132 ? 0.3185 0.3971 0.3377 0.1038  -0.1230 -0.0552 424 ILE B C   
2772 O O   . ILE B 132 ? 0.3577 0.4423 0.3729 0.1133  -0.1040 -0.0447 424 ILE B O   
2773 C CB  . ILE B 132 ? 0.3974 0.4694 0.4626 0.0627  -0.1272 -0.0475 424 ILE B CB  
2774 C CG1 . ILE B 132 ? 0.4171 0.5145 0.5174 0.0382  -0.1241 -0.0403 424 ILE B CG1 
2775 C CG2 . ILE B 132 ? 0.3067 0.3643 0.3624 0.0716  -0.1093 -0.0381 424 ILE B CG2 
2776 C CD1 . ILE B 132 ? 0.4522 0.5179 0.5523 0.0109  -0.1271 -0.0379 424 ILE B CD1 
2777 N N   . PHE B 133 ? 0.3545 0.4131 0.3476 0.1105  -0.1364 -0.0723 425 PHE B N   
2778 C CA  . PHE B 133 ? 0.3940 0.4438 0.3528 0.1298  -0.1252 -0.0799 425 PHE B CA  
2779 C C   . PHE B 133 ? 0.4227 0.4911 0.3617 0.1402  -0.1146 -0.0684 425 PHE B C   
2780 O O   . PHE B 133 ? 0.4250 0.4952 0.3508 0.1483  -0.0926 -0.0623 425 PHE B O   
2781 C CB  . PHE B 133 ? 0.4190 0.4461 0.3494 0.1361  -0.1425 -0.1038 425 PHE B CB  
2782 C CG  . PHE B 133 ? 0.4482 0.4638 0.3554 0.1534  -0.1280 -0.1184 425 PHE B CG  
2783 C CD1 . PHE B 133 ? 0.4578 0.4873 0.3335 0.1662  -0.1085 -0.1180 425 PHE B CD1 
2784 C CD2 . PHE B 133 ? 0.4495 0.4401 0.3665 0.1567  -0.1336 -0.1333 425 PHE B CD2 
2785 C CE1 . PHE B 133 ? 0.4688 0.4978 0.3299 0.1803  -0.0904 -0.1345 425 PHE B CE1 
2786 C CE2 . PHE B 133 ? 0.4673 0.4557 0.3725 0.1761  -0.1203 -0.1514 425 PHE B CE2 
2787 C CZ  . PHE B 133 ? 0.4743 0.4872 0.3549 0.1870  -0.0964 -0.1532 425 PHE B CZ  
2788 N N   . ASP B 134 ? 0.4350 0.5156 0.3727 0.1394  -0.1319 -0.0654 426 ASP B N   
2789 C CA  . ASP B 134 ? 0.3927 0.4800 0.3046 0.1510  -0.1282 -0.0529 426 ASP B CA  
2790 C C   . ASP B 134 ? 0.4359 0.5354 0.3728 0.1500  -0.1101 -0.0332 426 ASP B C   
2791 O O   . ASP B 134 ? 0.4185 0.5104 0.3290 0.1576  -0.0952 -0.0214 426 ASP B O   
2792 C CB  . ASP B 134 ? 0.4195 0.5158 0.3273 0.1541  -0.1586 -0.0570 426 ASP B CB  
2793 C CG  . ASP B 134 ? 0.5837 0.6609 0.4455 0.1597  -0.1769 -0.0756 426 ASP B CG  
2794 O OD1 . ASP B 134 ? 0.5998 0.6576 0.4222 0.1658  -0.1605 -0.0830 426 ASP B OD1 
2795 O OD2 . ASP B 134 ? 0.5732 0.6574 0.4401 0.1583  -0.2077 -0.0854 426 ASP B OD2 
2796 N N   . MET B 135 ? 0.3558 0.4714 0.3397 0.1388  -0.1104 -0.0299 427 MET B N   
2797 C CA  . MET B 135 ? 0.3983 0.5227 0.4026 0.1389  -0.0931 -0.0148 427 MET B CA  
2798 C C   . MET B 135 ? 0.3671 0.4766 0.3603 0.1388  -0.0701 -0.0104 427 MET B C   
2799 O O   . MET B 135 ? 0.4139 0.5210 0.4024 0.1428  -0.0558 0.0017  427 MET B O   
2800 C CB  . MET B 135 ? 0.3094 0.4544 0.3604 0.1253  -0.0940 -0.0147 427 MET B CB  
2801 C CG  . MET B 135 ? 0.4184 0.5938 0.4973 0.1290  -0.1083 -0.0155 427 MET B CG  
2802 S SD  . MET B 135 ? 0.5090 0.7193 0.6455 0.1068  -0.1072 -0.0216 427 MET B SD  
2803 C CE  . MET B 135 ? 0.2746 0.4578 0.3999 0.0847  -0.1115 -0.0293 427 MET B CE  
2804 N N   . LEU B 136 ? 0.3250 0.4236 0.3167 0.1347  -0.0685 -0.0217 428 LEU B N   
2805 C CA  . LEU B 136 ? 0.3994 0.4912 0.3885 0.1371  -0.0499 -0.0220 428 LEU B CA  
2806 C C   . LEU B 136 ? 0.3320 0.4225 0.2873 0.1458  -0.0364 -0.0217 428 LEU B C   
2807 O O   . LEU B 136 ? 0.3398 0.4332 0.2968 0.1449  -0.0169 -0.0148 428 LEU B O   
2808 C CB  . LEU B 136 ? 0.3380 0.4170 0.3354 0.1354  -0.0565 -0.0369 428 LEU B CB  
2809 C CG  . LEU B 136 ? 0.2574 0.3275 0.2797 0.1226  -0.0646 -0.0328 428 LEU B CG  
2810 C CD1 . LEU B 136 ? 0.2817 0.3264 0.3010 0.1210  -0.0806 -0.0474 428 LEU B CD1 
2811 C CD2 . LEU B 136 ? 0.2333 0.3047 0.2698 0.1212  -0.0509 -0.0230 428 LEU B CD2 
2812 N N   . LEU B 137 ? 0.3582 0.4433 0.2796 0.1519  -0.0461 -0.0292 429 LEU B N   
2813 C CA  . LEU B 137 ? 0.3710 0.4507 0.2478 0.1573  -0.0311 -0.0270 429 LEU B CA  
2814 C C   . LEU B 137 ? 0.3788 0.4520 0.2399 0.1565  -0.0263 -0.0044 429 LEU B C   
2815 O O   . LEU B 137 ? 0.4156 0.4824 0.2527 0.1533  -0.0046 0.0047  429 LEU B O   
2816 C CB  . LEU B 137 ? 0.4193 0.4890 0.2541 0.1644  -0.0459 -0.0413 429 LEU B CB  
2817 C CG  . LEU B 137 ? 0.4316 0.4996 0.2671 0.1688  -0.0466 -0.0675 429 LEU B CG  
2818 C CD1 . LEU B 137 ? 0.4974 0.5514 0.2883 0.1756  -0.0660 -0.0825 429 LEU B CD1 
2819 C CD2 . LEU B 137 ? 0.4368 0.5154 0.2698 0.1717  -0.0156 -0.0752 429 LEU B CD2 
2820 N N   . ALA B 138 ? 0.4663 0.5407 0.3424 0.1589  -0.0463 0.0039  430 ALA B N   
2821 C CA  . ALA B 138 ? 0.4541 0.5171 0.3180 0.1627  -0.0464 0.0233  430 ALA B CA  
2822 C C   . ALA B 138 ? 0.4317 0.4950 0.3213 0.1553  -0.0254 0.0332  430 ALA B C   
2823 O O   . ALA B 138 ? 0.4639 0.5076 0.3300 0.1545  -0.0159 0.0485  430 ALA B O   
2824 C CB  . ALA B 138 ? 0.3746 0.4474 0.2609 0.1707  -0.0737 0.0241  430 ALA B CB  
2825 N N   . THR B 139 ? 0.3371 0.4166 0.2699 0.1488  -0.0204 0.0249  431 THR B N   
2826 C CA  . THR B 139 ? 0.3728 0.4518 0.3275 0.1418  -0.0037 0.0314  431 THR B CA  
2827 C C   . THR B 139 ? 0.4271 0.5034 0.3664 0.1353  0.0185  0.0311  431 THR B C   
2828 O O   . THR B 139 ? 0.3386 0.4058 0.2767 0.1284  0.0322  0.0420  431 THR B O   
2829 C CB  . THR B 139 ? 0.3573 0.4491 0.3517 0.1366  -0.0068 0.0227  431 THR B CB  
2830 O OG1 . THR B 139 ? 0.4375 0.5382 0.4461 0.1380  -0.0238 0.0198  431 THR B OG1 
2831 C CG2 . THR B 139 ? 0.2858 0.3743 0.2993 0.1315  0.0035  0.0298  431 THR B CG2 
2832 N N   . SER B 140 ? 0.3891 0.4748 0.3194 0.1366  0.0229  0.0165  432 SER B N   
2833 C CA  . SER B 140 ? 0.3843 0.4783 0.3060 0.1305  0.0478  0.0119  432 SER B CA  
2834 C C   . SER B 140 ? 0.4217 0.4966 0.2928 0.1248  0.0609  0.0279  432 SER B C   
2835 O O   . SER B 140 ? 0.5072 0.5830 0.3762 0.1117  0.0843  0.0348  432 SER B O   
2836 C CB  . SER B 140 ? 0.4154 0.5242 0.3372 0.1376  0.0488  -0.0115 432 SER B CB  
2837 O OG  . SER B 140 ? 0.7199 0.8500 0.6545 0.1331  0.0742  -0.0221 432 SER B OG  
2838 N N   . SER B 141 ? 0.5036 0.5585 0.3320 0.1329  0.0442  0.0346  433 SER B N   
2839 C CA  . SER B 141 ? 0.5436 0.5679 0.3125 0.1286  0.0507  0.0537  433 SER B CA  
2840 C C   . SER B 141 ? 0.5985 0.5999 0.3745 0.1232  0.0501  0.0747  433 SER B C   
2841 O O   . SER B 141 ? 0.6085 0.5847 0.3491 0.1103  0.0672  0.0910  433 SER B O   
2842 C CB  . SER B 141 ? 0.5930 0.5987 0.3158 0.1422  0.0243  0.0548  433 SER B CB  
2843 O OG  . SER B 141 ? 0.8604 0.8258 0.5194 0.1405  0.0233  0.0768  433 SER B OG  
2844 N N   . ARG B 142 ? 0.5027 0.5101 0.3216 0.1317  0.0315  0.0737  434 ARG B N   
2845 C CA  . ARG B 142 ? 0.4462 0.4317 0.2749 0.1297  0.0302  0.0886  434 ARG B CA  
2846 C C   . ARG B 142 ? 0.4873 0.4786 0.3396 0.1112  0.0553  0.0891  434 ARG B C   
2847 O O   . ARG B 142 ? 0.4860 0.4470 0.3195 0.1006  0.0639  0.1047  434 ARG B O   
2848 C CB  . ARG B 142 ? 0.5221 0.5207 0.3935 0.1430  0.0092  0.0824  434 ARG B CB  
2849 C CG  . ARG B 142 ? 0.4121 0.3903 0.2972 0.1442  0.0079  0.0919  434 ARG B CG  
2850 C CD  . ARG B 142 ? 0.6522 0.5855 0.4917 0.1534  -0.0047 0.1097  434 ARG B CD  
2851 N NE  . ARG B 142 ? 0.4829 0.3914 0.3354 0.1577  -0.0085 0.1157  434 ARG B NE  
2852 C CZ  . ARG B 142 ? 0.5145 0.3701 0.3272 0.1576  -0.0122 0.1335  434 ARG B CZ  
2853 N NH1 . ARG B 142 ? 0.6685 0.4891 0.4207 0.1512  -0.0110 0.1502  434 ARG B NH1 
2854 N NH2 . ARG B 142 ? 0.6039 0.4361 0.4323 0.1636  -0.0175 0.1346  434 ARG B NH2 
2855 N N   . PHE B 143 ? 0.4075 0.4348 0.3015 0.1072  0.0642  0.0714  435 PHE B N   
2856 C CA  . PHE B 143 ? 0.5057 0.5466 0.4276 0.0905  0.0854  0.0679  435 PHE B CA  
2857 C C   . PHE B 143 ? 0.4666 0.5017 0.3538 0.0735  0.1116  0.0752  435 PHE B C   
2858 O O   . PHE B 143 ? 0.4420 0.4678 0.3340 0.0545  0.1277  0.0841  435 PHE B O   
2859 C CB  . PHE B 143 ? 0.4625 0.5414 0.4308 0.0941  0.0851  0.0458  435 PHE B CB  
2860 C CG  . PHE B 143 ? 0.4656 0.5464 0.4689 0.1006  0.0671  0.0415  435 PHE B CG  
2861 C CD1 . PHE B 143 ? 0.3870 0.4451 0.3850 0.1040  0.0560  0.0532  435 PHE B CD1 
2862 C CD2 . PHE B 143 ? 0.3977 0.5004 0.4357 0.1041  0.0614  0.0251  435 PHE B CD2 
2863 C CE1 . PHE B 143 ? 0.4079 0.4693 0.4321 0.1081  0.0442  0.0480  435 PHE B CE1 
2864 C CE2 . PHE B 143 ? 0.3027 0.4010 0.3611 0.1072  0.0462  0.0234  435 PHE B CE2 
2865 C CZ  . PHE B 143 ? 0.2592 0.3390 0.3097 0.1078  0.0400  0.0346  435 PHE B CZ  
2866 N N   . ARG B 144 ? 0.5013 0.5409 0.3511 0.0778  0.1172  0.0709  436 ARG B N   
2867 C CA  . ARG B 144 ? 0.5494 0.5844 0.3566 0.0600  0.1465  0.0772  436 ARG B CA  
2868 C C   . ARG B 144 ? 0.6130 0.5923 0.3613 0.0485  0.1469  0.1068  436 ARG B C   
2869 O O   . ARG B 144 ? 0.6990 0.6681 0.4235 0.0232  0.1751  0.1178  436 ARG B O   
2870 C CB  . ARG B 144 ? 0.6215 0.6701 0.3945 0.0705  0.1497  0.0630  436 ARG B CB  
2871 C CG  . ARG B 144 ? 0.7869 0.8721 0.5634 0.0567  0.1868  0.0471  436 ARG B CG  
2872 C CD  . ARG B 144 ? 0.7648 0.8664 0.5178 0.0733  0.1853  0.0250  436 ARG B CD  
2873 N NE  . ARG B 144 ? 0.6856 0.7503 0.3876 0.0896  0.1539  0.0334  436 ARG B NE  
2874 C CZ  . ARG B 144 ? 0.7858 0.8575 0.5095 0.1098  0.1249  0.0177  436 ARG B CZ  
2875 N NH1 . ARG B 144 ? 0.5597 0.6643 0.3460 0.1175  0.1216  -0.0045 436 ARG B NH1 
2876 N NH2 . ARG B 144 ? 0.8468 0.8894 0.5280 0.1217  0.0964  0.0247  436 ARG B NH2 
2877 N N   . MET B 145 ? 0.6771 0.6193 0.4023 0.0660  0.1158  0.1195  437 MET B N   
2878 C CA  . MET B 145 ? 0.7089 0.5892 0.3760 0.0600  0.1095  0.1474  437 MET B CA  
2879 C C   . MET B 145 ? 0.7267 0.5877 0.4225 0.0446  0.1155  0.1572  437 MET B C   
2880 O O   . MET B 145 ? 0.7298 0.5467 0.3829 0.0230  0.1291  0.1781  437 MET B O   
2881 C CB  . MET B 145 ? 0.7528 0.6050 0.3958 0.0883  0.0704  0.1535  437 MET B CB  
2882 N N   . MET B 146 ? 0.7047 0.5930 0.4670 0.0535  0.1050  0.1427  438 MET B N   
2883 C CA  . MET B 146 ? 0.6320 0.5034 0.4228 0.0399  0.1083  0.1473  438 MET B CA  
2884 C C   . MET B 146 ? 0.5905 0.4943 0.4147 0.0106  0.1390  0.1394  438 MET B C   
2885 O O   . MET B 146 ? 0.5608 0.4484 0.4052 -0.0065 0.1430  0.1435  438 MET B O   
2886 C CB  . MET B 146 ? 0.6563 0.5443 0.4987 0.0600  0.0864  0.1332  438 MET B CB  
2887 C CG  . MET B 146 ? 0.7233 0.5846 0.5478 0.0875  0.0573  0.1384  438 MET B CG  
2888 S SD  . MET B 146 ? 0.7057 0.6020 0.5919 0.1063  0.0415  0.1178  438 MET B SD  
2889 C CE  . MET B 146 ? 0.5013 0.3734 0.4077 0.0907  0.0487  0.1183  438 MET B CE  
2890 N N   . ASN B 147 ? 0.6964 0.6470 0.5303 0.0054  0.1593  0.1256  439 ASN B N   
2891 C CA  . ASN B 147 ? 0.5810 0.5788 0.4618 -0.0177 0.1875  0.1111  439 ASN B CA  
2892 C C   . ASN B 147 ? 0.5551 0.5777 0.5065 -0.0140 0.1738  0.0954  439 ASN B C   
2893 O O   . ASN B 147 ? 0.4881 0.5066 0.4656 -0.0356 0.1809  0.0973  439 ASN B O   
2894 C CB  . ASN B 147 ? 0.6346 0.6068 0.4830 -0.0542 0.2166  0.1295  439 ASN B CB  
2895 C CG  . ASN B 147 ? 0.7887 0.8231 0.6902 -0.0796 0.2503  0.1113  439 ASN B CG  
2896 O OD1 . ASN B 147 ? 0.7040 0.7903 0.6213 -0.0724 0.2660  0.0913  439 ASN B OD1 
2897 N ND2 . ASN B 147 ? 0.8958 0.9264 0.8282 -0.1087 0.2607  0.1155  439 ASN B ND2 
2898 N N   . LEU B 148 ? 0.5779 0.6223 0.5552 0.0123  0.1524  0.0802  440 LEU B N   
2899 C CA  . LEU B 148 ? 0.4380 0.4995 0.4690 0.0185  0.1361  0.0664  440 LEU B CA  
2900 C C   . LEU B 148 ? 0.3552 0.4644 0.4416 0.0031  0.1511  0.0482  440 LEU B C   
2901 O O   . LEU B 148 ? 0.3817 0.5320 0.4829 0.0036  0.1668  0.0341  440 LEU B O   
2902 C CB  . LEU B 148 ? 0.4113 0.4846 0.4508 0.0453  0.1139  0.0554  440 LEU B CB  
2903 C CG  . LEU B 148 ? 0.4780 0.5600 0.5577 0.0525  0.0953  0.0437  440 LEU B CG  
2904 C CD1 . LEU B 148 ? 0.3239 0.3673 0.3913 0.0517  0.0843  0.0550  440 LEU B CD1 
2905 C CD2 . LEU B 148 ? 0.4156 0.5106 0.5004 0.0724  0.0789  0.0334  440 LEU B CD2 
2906 N N   . GLN B 149 ? 0.3697 0.4753 0.4890 -0.0092 0.1447  0.0458  441 GLN B N   
2907 C CA  . GLN B 149 ? 0.3564 0.5104 0.5375 -0.0230 0.1527  0.0264  441 GLN B CA  
2908 C C   . GLN B 149 ? 0.3004 0.4787 0.5217 -0.0005 0.1264  0.0062  441 GLN B C   
2909 O O   . GLN B 149 ? 0.2462 0.3960 0.4471 0.0178  0.1036  0.0104  441 GLN B O   
2910 C CB  . GLN B 149 ? 0.3503 0.4854 0.5456 -0.0516 0.1569  0.0332  441 GLN B CB  
2911 C CG  . GLN B 149 ? 0.4039 0.5073 0.5563 -0.0795 0.1834  0.0553  441 GLN B CG  
2912 C CD  . GLN B 149 ? 0.4237 0.5745 0.5844 -0.0956 0.2186  0.0491  441 GLN B CD  
2913 O OE1 . GLN B 149 ? 0.4353 0.6420 0.6567 -0.1133 0.2342  0.0306  441 GLN B OE1 
2914 N NE2 . GLN B 149 ? 0.4539 0.5857 0.5546 -0.0887 0.2309  0.0623  441 GLN B NE2 
2915 N N   . GLY B 150 ? 0.3237 0.5554 0.6023 -0.0022 0.1299  -0.0164 442 GLY B N   
2916 C CA  . GLY B 150 ? 0.2863 0.5350 0.5990 0.0199  0.1012  -0.0350 442 GLY B CA  
2917 C C   . GLY B 150 ? 0.2761 0.4944 0.5910 0.0189  0.0747  -0.0321 442 GLY B C   
2918 O O   . GLY B 150 ? 0.3212 0.5215 0.6248 0.0381  0.0490  -0.0347 442 GLY B O   
2919 N N   . GLU B 151 ? 0.2289 0.4373 0.5537 -0.0055 0.0812  -0.0270 443 GLU B N   
2920 C CA  . GLU B 151 ? 0.2736 0.4478 0.5932 -0.0069 0.0566  -0.0260 443 GLU B CA  
2921 C C   . GLU B 151 ? 0.2775 0.3975 0.5368 0.0065  0.0487  -0.0089 443 GLU B C   
2922 O O   . GLU B 151 ? 0.3606 0.4568 0.6074 0.0167  0.0263  -0.0120 443 GLU B O   
2923 C CB  . GLU B 151 ? 0.3354 0.5055 0.6763 -0.0382 0.0655  -0.0249 443 GLU B CB  
2924 C CG  . GLU B 151 ? 0.2598 0.4933 0.6730 -0.0553 0.0739  -0.0452 443 GLU B CG  
2925 C CD  . GLU B 151 ? 0.3021 0.5670 0.7221 -0.0747 0.1139  -0.0402 443 GLU B CD  
2926 O OE1 . GLU B 151 ? 0.3151 0.5486 0.6777 -0.0712 0.1307  -0.0204 443 GLU B OE1 
2927 O OE2 . GLU B 151 ? 0.3938 0.7164 0.8762 -0.0940 0.1286  -0.0571 443 GLU B OE2 
2928 N N   . GLU B 152 ? 0.3670 0.4687 0.5881 0.0071  0.0664  0.0078  444 GLU B N   
2929 C CA  . GLU B 152 ? 0.3256 0.3869 0.5000 0.0229  0.0582  0.0204  444 GLU B CA  
2930 C C   . GLU B 152 ? 0.3794 0.4536 0.5479 0.0451  0.0467  0.0150  444 GLU B C   
2931 O O   . GLU B 152 ? 0.3094 0.3617 0.4565 0.0568  0.0340  0.0173  444 GLU B O   
2932 C CB  . GLU B 152 ? 0.3133 0.3493 0.4497 0.0181  0.0751  0.0393  444 GLU B CB  
2933 C CG  . GLU B 152 ? 0.3731 0.3813 0.5036 -0.0067 0.0861  0.0493  444 GLU B CG  
2934 C CD  . GLU B 152 ? 0.4001 0.3767 0.4837 -0.0112 0.1005  0.0703  444 GLU B CD  
2935 O OE1 . GLU B 152 ? 0.4010 0.4019 0.4756 -0.0110 0.1155  0.0727  444 GLU B OE1 
2936 O OE2 . GLU B 152 ? 0.4325 0.3559 0.4843 -0.0131 0.0947  0.0836  444 GLU B OE2 
2937 N N   . PHE B 153 ? 0.3239 0.4328 0.5110 0.0498  0.0521  0.0066  445 PHE B N   
2938 C CA  . PHE B 153 ? 0.2800 0.3939 0.4591 0.0684  0.0399  0.0018  445 PHE B CA  
2939 C C   . PHE B 153 ? 0.2877 0.3949 0.4768 0.0755  0.0157  -0.0074 445 PHE B C   
2940 O O   . PHE B 153 ? 0.2207 0.3081 0.3846 0.0847  0.0046  -0.0032 445 PHE B O   
2941 C CB  . PHE B 153 ? 0.2864 0.4345 0.4829 0.0733  0.0496  -0.0089 445 PHE B CB  
2942 C CG  . PHE B 153 ? 0.2142 0.3669 0.4161 0.0910  0.0309  -0.0203 445 PHE B CG  
2943 C CD1 . PHE B 153 ? 0.3818 0.5145 0.5514 0.1003  0.0242  -0.0132 445 PHE B CD1 
2944 C CD2 . PHE B 153 ? 0.2590 0.4344 0.5000 0.0979  0.0177  -0.0387 445 PHE B CD2 
2945 C CE1 . PHE B 153 ? 0.2402 0.3683 0.4106 0.1127  0.0063  -0.0220 445 PHE B CE1 
2946 C CE2 . PHE B 153 ? 0.1989 0.3621 0.4315 0.1119  -0.0024 -0.0451 445 PHE B CE2 
2947 C CZ  . PHE B 153 ? 0.2491 0.3855 0.4447 0.1169  -0.0069 -0.0357 445 PHE B CZ  
2948 N N   . VAL B 154 ? 0.2170 0.3403 0.4414 0.0700  0.0067  -0.0199 446 VAL B N   
2949 C CA  . VAL B 154 ? 0.1947 0.3053 0.4205 0.0776  -0.0208 -0.0280 446 VAL B CA  
2950 C C   . VAL B 154 ? 0.2957 0.3673 0.4847 0.0738  -0.0268 -0.0190 446 VAL B C   
2951 O O   . VAL B 154 ? 0.2998 0.3491 0.4637 0.0808  -0.0442 -0.0191 446 VAL B O   
2952 C CB  . VAL B 154 ? 0.1943 0.3349 0.4714 0.0743  -0.0334 -0.0461 446 VAL B CB  
2953 C CG1 . VAL B 154 ? 0.1740 0.3585 0.4908 0.0828  -0.0265 -0.0599 446 VAL B CG1 
2954 C CG2 . VAL B 154 ? 0.2842 0.4299 0.5801 0.0529  -0.0217 -0.0456 446 VAL B CG2 
2955 N N   . CYS B 155 ? 0.2344 0.2939 0.4155 0.0628  -0.0122 -0.0115 447 CYS B N   
2956 C CA  . CYS B 155 ? 0.2664 0.2897 0.4125 0.0634  -0.0157 -0.0063 447 CYS B CA  
2957 C C   . CYS B 155 ? 0.2752 0.2887 0.3893 0.0748  -0.0094 0.0029  447 CYS B C   
2958 O O   . CYS B 155 ? 0.3271 0.3215 0.4145 0.0791  -0.0155 0.0023  447 CYS B O   
2959 C CB  . CYS B 155 ? 0.3126 0.3190 0.4584 0.0512  -0.0044 -0.0017 447 CYS B CB  
2960 S SG  . CYS B 155 ? 0.3613 0.3693 0.5408 0.0323  -0.0160 -0.0148 447 CYS B SG  
2961 N N   . LEU B 156 ? 0.2918 0.3204 0.4082 0.0783  0.0033  0.0101  448 LEU B N   
2962 C CA  . LEU B 156 ? 0.2928 0.3188 0.3876 0.0875  0.0068  0.0166  448 LEU B CA  
2963 C C   . LEU B 156 ? 0.2934 0.3204 0.3810 0.0909  -0.0053 0.0128  448 LEU B C   
2964 O O   . LEU B 156 ? 0.3146 0.3322 0.3811 0.0924  -0.0049 0.0157  448 LEU B O   
2965 C CB  . LEU B 156 ? 0.2716 0.3115 0.3682 0.0902  0.0182  0.0234  448 LEU B CB  
2966 C CG  . LEU B 156 ? 0.3956 0.4218 0.4823 0.0879  0.0290  0.0328  448 LEU B CG  
2967 C CD1 . LEU B 156 ? 0.3770 0.4096 0.4501 0.0947  0.0346  0.0405  448 LEU B CD1 
2968 C CD2 . LEU B 156 ? 0.3890 0.3898 0.4618 0.0923  0.0260  0.0338  448 LEU B CD2 
2969 N N   . LYS B 157 ? 0.2357 0.2731 0.3408 0.0919  -0.0161 0.0059  449 LYS B N   
2970 C CA  . LYS B 157 ? 0.2849 0.3108 0.3771 0.0955  -0.0324 0.0037  449 LYS B CA  
2971 C C   . LYS B 157 ? 0.3569 0.3553 0.4217 0.0916  -0.0439 0.0040  449 LYS B C   
2972 O O   . LYS B 157 ? 0.3062 0.2856 0.3402 0.0891  -0.0477 0.0093  449 LYS B O   
2973 C CB  . LYS B 157 ? 0.3378 0.3776 0.4576 0.1022  -0.0459 -0.0072 449 LYS B CB  
2974 C CG  . LYS B 157 ? 0.3371 0.3914 0.4648 0.1091  -0.0408 -0.0094 449 LYS B CG  
2975 C CD  . LYS B 157 ? 0.3583 0.4092 0.4957 0.1162  -0.0594 -0.0202 449 LYS B CD  
2976 C CE  . LYS B 157 ? 0.2990 0.3699 0.4700 0.1169  -0.0655 -0.0328 449 LYS B CE  
2977 N NZ  . LYS B 157 ? 0.3493 0.4276 0.5347 0.1238  -0.0753 -0.0460 449 LYS B NZ  
2978 N N   . SER B 158 ? 0.2662 0.2604 0.3383 0.0886  -0.0491 -0.0019 450 SER B N   
2979 C CA  . SER B 158 ? 0.3124 0.2774 0.3513 0.0855  -0.0612 -0.0038 450 SER B CA  
2980 C C   . SER B 158 ? 0.3378 0.2911 0.3447 0.0827  -0.0433 0.0016  450 SER B C   
2981 O O   . SER B 158 ? 0.3248 0.2559 0.2920 0.0793  -0.0464 0.0030  450 SER B O   
2982 C CB  . SER B 158 ? 0.3199 0.2842 0.3774 0.0822  -0.0724 -0.0142 450 SER B CB  
2983 O OG  . SER B 158 ? 0.5816 0.5679 0.6799 0.0852  -0.0875 -0.0229 450 SER B OG  
2984 N N   . ILE B 159 ? 0.2761 0.2440 0.2984 0.0848  -0.0247 0.0040  451 ILE B N   
2985 C CA  . ILE B 159 ? 0.3286 0.2935 0.3313 0.0870  -0.0086 0.0053  451 ILE B CA  
2986 C C   . ILE B 159 ? 0.2660 0.2403 0.2569 0.0846  -0.0023 0.0113  451 ILE B C   
2987 O O   . ILE B 159 ? 0.3790 0.3477 0.3439 0.0806  0.0065  0.0101  451 ILE B O   
2988 C CB  . ILE B 159 ? 0.2731 0.2470 0.2957 0.0933  0.0036  0.0070  451 ILE B CB  
2989 C CG1 . ILE B 159 ? 0.3402 0.2950 0.3673 0.0906  -0.0015 0.0015  451 ILE B CG1 
2990 C CG2 . ILE B 159 ? 0.2527 0.2322 0.2660 0.1010  0.0175  0.0056  451 ILE B CG2 
2991 C CD1 . ILE B 159 ? 0.2842 0.2377 0.3269 0.0928  0.0067  0.0073  451 ILE B CD1 
2992 N N   . ILE B 160 ? 0.2950 0.2839 0.3043 0.0850  -0.0056 0.0163  452 ILE B N   
2993 C CA  . ILE B 160 ? 0.3071 0.3017 0.3077 0.0794  -0.0024 0.0214  452 ILE B CA  
2994 C C   . ILE B 160 ? 0.3667 0.3328 0.3300 0.0689  -0.0116 0.0240  452 ILE B C   
2995 O O   . ILE B 160 ? 0.3706 0.3345 0.3117 0.0581  -0.0005 0.0276  452 ILE B O   
2996 C CB  . ILE B 160 ? 0.2982 0.3059 0.3210 0.0829  -0.0086 0.0233  452 ILE B CB  
2997 C CG1 . ILE B 160 ? 0.2975 0.3290 0.3426 0.0908  0.0024  0.0238  452 ILE B CG1 
2998 C CG2 . ILE B 160 ? 0.3007 0.3019 0.3104 0.0739  -0.0126 0.0276  452 ILE B CG2 
2999 C CD1 . ILE B 160 ? 0.2624 0.3048 0.3228 0.0952  -0.0023 0.0232  452 ILE B CD1 
3000 N N   . LEU B 161 ? 0.2884 0.2322 0.2435 0.0711  -0.0326 0.0221  453 LEU B N   
3001 C CA  . LEU B 161 ? 0.3364 0.2422 0.2465 0.0630  -0.0478 0.0263  453 LEU B CA  
3002 C C   . LEU B 161 ? 0.4089 0.3007 0.2778 0.0544  -0.0345 0.0259  453 LEU B C   
3003 O O   . LEU B 161 ? 0.4433 0.3130 0.2685 0.0404  -0.0298 0.0334  453 LEU B O   
3004 C CB  . LEU B 161 ? 0.3486 0.2370 0.2639 0.0720  -0.0772 0.0206  453 LEU B CB  
3005 C CG  . LEU B 161 ? 0.4213 0.2613 0.2836 0.0676  -0.1017 0.0249  453 LEU B CG  
3006 C CD1 . LEU B 161 ? 0.4392 0.2518 0.2735 0.0595  -0.1080 0.0368  453 LEU B CD1 
3007 C CD2 . LEU B 161 ? 0.4462 0.2791 0.3267 0.0806  -0.1341 0.0146  453 LEU B CD2 
3008 N N   . LEU B 162 ? 0.3759 0.2775 0.2548 0.0613  -0.0270 0.0165  454 LEU B N   
3009 C CA  . LEU B 162 ? 0.4728 0.3587 0.3105 0.0567  -0.0159 0.0110  454 LEU B CA  
3010 C C   . LEU B 162 ? 0.4131 0.3272 0.2564 0.0546  0.0157  0.0083  454 LEU B C   
3011 O O   . LEU B 162 ? 0.4799 0.3851 0.2838 0.0475  0.0307  0.0038  454 LEU B O   
3012 C CB  . LEU B 162 ? 0.4327 0.3100 0.2771 0.0657  -0.0260 -0.0011 454 LEU B CB  
3013 C CG  . LEU B 162 ? 0.4774 0.3307 0.3167 0.0669  -0.0593 -0.0033 454 LEU B CG  
3014 C CD1 . LEU B 162 ? 0.4844 0.3431 0.3546 0.0726  -0.0670 -0.0154 454 LEU B CD1 
3015 C CD2 . LEU B 162 ? 0.5151 0.3254 0.2859 0.0597  -0.0734 -0.0019 454 LEU B CD2 
3016 N N   . ASN B 163 ? 0.3862 0.3355 0.2767 0.0612  0.0257  0.0093  455 ASN B N   
3017 C CA  . ASN B 163 ? 0.4401 0.4224 0.3479 0.0645  0.0508  0.0029  455 ASN B CA  
3018 C C   . ASN B 163 ? 0.3471 0.3526 0.2603 0.0502  0.0640  0.0093  455 ASN B C   
3019 O O   . ASN B 163 ? 0.4871 0.5215 0.4071 0.0476  0.0872  0.0015  455 ASN B O   
3020 C CB  . ASN B 163 ? 0.3013 0.3048 0.2547 0.0822  0.0501  -0.0008 455 ASN B CB  
3021 C CG  . ASN B 163 ? 0.3639 0.3998 0.3392 0.0923  0.0696  -0.0104 455 ASN B CG  
3022 O OD1 . ASN B 163 ? 0.3678 0.4041 0.3269 0.0954  0.0836  -0.0228 455 ASN B OD1 
3023 N ND2 . ASN B 163 ? 0.3589 0.4233 0.3715 0.0992  0.0691  -0.0072 455 ASN B ND2 
3024 N N   . SER B 164 ? 0.4364 0.4312 0.3495 0.0407  0.0498  0.0209  456 SER B N   
3025 C CA  . SER B 164 ? 0.5003 0.5176 0.4281 0.0265  0.0593  0.0259  456 SER B CA  
3026 C C   . SER B 164 ? 0.5142 0.5221 0.4020 0.0012  0.0765  0.0301  456 SER B C   
3027 O O   . SER B 164 ? 0.5394 0.5688 0.4416 -0.0161 0.0875  0.0335  456 SER B O   
3028 C CB  . SER B 164 ? 0.4805 0.4830 0.4179 0.0254  0.0372  0.0346  456 SER B CB  
3029 O OG  . SER B 164 ? 0.4069 0.4311 0.3846 0.0443  0.0303  0.0302  456 SER B OG  
3030 N N   . GLY B 165 ? 0.5020 0.4784 0.3383 -0.0038 0.0797  0.0297  457 GLY B N   
3031 C CA  . GLY B 165 ? 0.5954 0.5570 0.3816 -0.0313 0.0986  0.0358  457 GLY B CA  
3032 C C   . GLY B 165 ? 0.6177 0.5877 0.3737 -0.0318 0.1247  0.0230  457 GLY B C   
3033 O O   . GLY B 165 ? 0.6941 0.6576 0.4057 -0.0569 0.1477  0.0266  457 GLY B O   
3034 N N   . VAL B 166 ? 0.6550 0.6371 0.4314 -0.0056 0.1231  0.0072  458 VAL B N   
3035 C CA  . VAL B 166 ? 0.8236 0.8039 0.5642 -0.0023 0.1436  -0.0084 458 VAL B CA  
3036 C C   . VAL B 166 ? 0.7389 0.7737 0.4985 -0.0121 0.1849  -0.0210 458 VAL B C   
3037 O O   . VAL B 166 ? 0.8606 0.8921 0.5730 -0.0221 0.2102  -0.0306 458 VAL B O   
3038 C CB  . VAL B 166 ? 0.8501 0.8270 0.6129 0.0277  0.1301  -0.0237 458 VAL B CB  
3039 C CG1 . VAL B 166 ? 0.7931 0.7206 0.5339 0.0319  0.0934  -0.0144 458 VAL B CG1 
3040 C CG2 . VAL B 166 ? 0.6514 0.6733 0.4904 0.0474  0.1307  -0.0297 458 VAL B CG2 
3041 N N   A TYR B 167 ? 0.7390 0.8275 0.5678 -0.0093 0.1925  -0.0234 459 TYR B N   
3042 N N   B TYR B 167 ? 0.7398 0.8277 0.5679 -0.0098 0.1924  -0.0230 459 TYR B N   
3043 C CA  A TYR B 167 ? 0.7157 0.8681 0.5783 -0.0174 0.2301  -0.0389 459 TYR B CA  
3044 C CA  B TYR B 167 ? 0.7157 0.8685 0.5798 -0.0173 0.2295  -0.0386 459 TYR B CA  
3045 C C   A TYR B 167 ? 0.6413 0.8029 0.4926 -0.0576 0.2460  -0.0237 459 TYR B C   
3046 C C   B TYR B 167 ? 0.6279 0.8018 0.5066 -0.0507 0.2391  -0.0244 459 TYR B C   
3047 O O   A TYR B 167 ? 0.7338 0.9415 0.6038 -0.0723 0.2766  -0.0325 459 TYR B O   
3048 O O   B TYR B 167 ? 0.7479 0.9557 0.6261 -0.0740 0.2714  -0.0293 459 TYR B O   
3049 C CB  A TYR B 167 ? 0.5808 0.7904 0.5296 0.0108  0.2267  -0.0537 459 TYR B CB  
3050 C CB  B TYR B 167 ? 0.5925 0.7970 0.5331 0.0172  0.2285  -0.0587 459 TYR B CB  
3051 C CG  A TYR B 167 ? 0.5641 0.7478 0.5253 0.0457  0.1989  -0.0578 459 TYR B CG  
3052 C CG  B TYR B 167 ? 0.5472 0.7290 0.5149 0.0412  0.1915  -0.0504 459 TYR B CG  
3053 C CD1 A TYR B 167 ? 0.6036 0.7771 0.5508 0.0682  0.2047  -0.0769 459 TYR B CD1 
3054 C CD1 B TYR B 167 ? 0.6321 0.7957 0.6049 0.0301  0.1684  -0.0300 459 TYR B CD1 
3055 C CD2 A TYR B 167 ? 0.5800 0.7479 0.5649 0.0542  0.1683  -0.0435 459 TYR B CD2 
3056 C CD2 B TYR B 167 ? 0.5307 0.7074 0.5164 0.0740  0.1812  -0.0638 459 TYR B CD2 
3057 C CE1 A TYR B 167 ? 0.4658 0.6102 0.4229 0.0951  0.1794  -0.0791 459 TYR B CE1 
3058 C CE1 B TYR B 167 ? 0.4635 0.6103 0.4577 0.0499  0.1401  -0.0239 459 TYR B CE1 
3059 C CE2 A TYR B 167 ? 0.5424 0.6864 0.5363 0.0804  0.1469  -0.0455 459 TYR B CE2 
3060 C CE2 B TYR B 167 ? 0.5498 0.7044 0.5548 0.0908  0.1518  -0.0545 459 TYR B CE2 
3061 C CZ  A TYR B 167 ? 0.5418 0.6723 0.5221 0.0992  0.1519  -0.0621 459 TYR B CZ  
3062 C CZ  B TYR B 167 ? 0.3979 0.5411 0.4071 0.0782  0.1334  -0.0349 459 TYR B CZ  
3063 O OH  A TYR B 167 ? 0.4142 0.5151 0.4013 0.1203  0.1305  -0.0625 459 TYR B OH  
3064 O OH  B TYR B 167 ? 0.4456 0.5709 0.4710 0.0930  0.1093  -0.0270 459 TYR B OH  
3065 N N   . LEU B 177 ? 1.3499 1.1153 0.5488 -0.0535 0.2025  -0.0626 469 LEU B N   
3066 C CA  . LEU B 177 ? 1.3326 1.1395 0.5934 -0.0246 0.2114  -0.0918 469 LEU B CA  
3067 C C   . LEU B 177 ? 1.2306 0.9896 0.4882 -0.0050 0.1684  -0.0983 469 LEU B C   
3068 O O   . LEU B 177 ? 1.1934 0.9672 0.5100 0.0129  0.1613  -0.1050 469 LEU B O   
3069 C CB  . LEU B 177 ? 1.2296 1.0725 0.4817 -0.0138 0.2431  -0.1209 469 LEU B CB  
3070 N N   . GLU B 178 ? 1.2386 1.0046 0.5118 -0.0156 0.0609  -0.0355 470 GLU B N   
3071 C CA  . GLU B 178 ? 1.1815 0.9379 0.4539 -0.0216 0.0149  -0.0408 470 GLU B CA  
3072 C C   . GLU B 178 ? 1.1523 0.9367 0.4803 -0.0200 -0.0145 -0.0207 470 GLU B C   
3073 O O   . GLU B 178 ? 1.2029 0.9922 0.5581 -0.0217 -0.0457 -0.0263 470 GLU B O   
3074 C CB  . GLU B 178 ? 1.2569 0.9803 0.4591 -0.0354 -0.0147 -0.0381 470 GLU B CB  
3075 N N   . GLU B 179 ? 1.1855 0.9878 0.5335 -0.0171 -0.0052 0.0030  471 GLU B N   
3076 C CA  . GLU B 179 ? 0.9978 0.8253 0.4019 -0.0127 -0.0287 0.0211  471 GLU B CA  
3077 C C   . GLU B 179 ? 0.9263 0.7761 0.3886 -0.0010 -0.0128 0.0069  471 GLU B C   
3078 O O   . GLU B 179 ? 0.8685 0.7440 0.3934 0.0017  -0.0396 0.0087  471 GLU B O   
3079 C CB  . GLU B 179 ? 0.9028 0.7386 0.3144 -0.0120 -0.0188 0.0487  471 GLU B CB  
3080 N N   . LYS B 180 ? 1.0388 0.8927 0.5093 0.0069  0.0323  -0.0066 472 LYS B N   
3081 C CA  . LYS B 180 ? 0.8865 0.7714 0.4347 0.0185  0.0458  -0.0200 472 LYS B CA  
3082 C C   . LYS B 180 ? 0.7708 0.6420 0.3141 0.0170  0.0272  -0.0413 472 LYS B C   
3083 O O   . LYS B 180 ? 0.7701 0.6669 0.3793 0.0220  0.0164  -0.0443 472 LYS B O   
3084 C CB  . LYS B 180 ? 0.9640 0.8558 0.5245 0.0273  0.0950  -0.0282 472 LYS B CB  
3085 C CG  . LYS B 180 ? 1.0084 0.9194 0.5913 0.0272  0.1146  -0.0066 472 LYS B CG  
3086 C CD  . LYS B 180 ? 0.9707 0.9070 0.6080 0.0363  0.1544  -0.0132 472 LYS B CD  
3087 C CE  . LYS B 180 ? 0.9586 0.8847 0.5841 0.0387  0.1742  -0.0361 472 LYS B CE  
3088 N NZ  . LYS B 180 ? 1.0028 0.9294 0.6123 0.0345  0.2034  -0.0317 472 LYS B NZ  
3089 N N   . ASP B 181 ? 0.8987 0.7271 0.3630 0.0086  0.0233  -0.0560 473 ASP B N   
3090 C CA  . ASP B 181 ? 0.9584 0.7682 0.4164 0.0044  0.0029  -0.0767 473 ASP B CA  
3091 C C   . ASP B 181 ? 0.8487 0.6750 0.3426 -0.0038 -0.0458 -0.0647 473 ASP B C   
3092 O O   . ASP B 181 ? 0.8368 0.6762 0.3814 -0.0027 -0.0570 -0.0730 473 ASP B O   
3093 C CB  . ASP B 181 ? 0.9965 0.7717 0.3913 -0.0048 0.0040  -0.0906 473 ASP B CB  
3094 C CG  . ASP B 181 ? 1.2077 0.9718 0.6016 0.0053  0.0457  -0.1136 473 ASP B CG  
3095 O OD1 . ASP B 181 ? 1.2002 0.9745 0.6433 0.0158  0.0576  -0.1252 473 ASP B OD1 
3096 O OD2 . ASP B 181 ? 1.2551 1.0007 0.6019 0.0036  0.0658  -0.1191 473 ASP B OD2 
3097 N N   . HIS B 182 ? 0.9162 0.7451 0.3934 -0.0117 -0.0741 -0.0428 474 HIS B N   
3098 C CA  . HIS B 182 ? 0.7626 0.6154 0.2905 -0.0176 -0.1183 -0.0288 474 HIS B CA  
3099 C C   . HIS B 182 ? 0.6996 0.6022 0.3275 -0.0055 -0.1085 -0.0200 474 HIS B C   
3100 O O   . HIS B 182 ? 0.6491 0.5728 0.3317 -0.0076 -0.1293 -0.0197 474 HIS B O   
3101 C CB  . HIS B 182 ? 0.7586 0.6088 0.2629 -0.0250 -0.1468 -0.0048 474 HIS B CB  
3102 C CG  . HIS B 182 ? 0.7763 0.6567 0.3461 -0.0280 -0.1884 0.0118  474 HIS B CG  
3103 N ND1 . HIS B 182 ? 0.8085 0.6873 0.3909 -0.0396 -0.2200 0.0062  474 HIS B ND1 
3104 C CD2 . HIS B 182 ? 0.6766 0.5919 0.3118 -0.0199 -0.1994 0.0336  474 HIS B CD2 
3105 C CE1 . HIS B 182 ? 0.8426 0.7575 0.4990 -0.0381 -0.2455 0.0242  474 HIS B CE1 
3106 N NE2 . HIS B 182 ? 0.7457 0.6834 0.4362 -0.0251 -0.2325 0.0400  474 HIS B NE2 
3107 N N   . ILE B 183 ? 0.5742 0.4944 0.2248 0.0058  -0.0767 -0.0128 475 ILE B N   
3108 C CA  . ILE B 183 ? 0.5044 0.4650 0.2379 0.0164  -0.0667 -0.0068 475 ILE B CA  
3109 C C   . ILE B 183 ? 0.5755 0.5420 0.3400 0.0199  -0.0549 -0.0248 475 ILE B C   
3110 O O   . ILE B 183 ? 0.4758 0.4681 0.2988 0.0219  -0.0634 -0.0218 475 ILE B O   
3111 C CB  . ILE B 183 ? 0.4992 0.4713 0.2442 0.0248  -0.0377 0.0030  475 ILE B CB  
3112 C CG1 . ILE B 183 ? 0.6768 0.6418 0.3984 0.0210  -0.0523 0.0248  475 ILE B CG1 
3113 C CG2 . ILE B 183 ? 0.4604 0.4669 0.2798 0.0341  -0.0280 0.0051  475 ILE B CG2 
3114 C CD1 . ILE B 183 ? 0.4874 0.4559 0.2113 0.0254  -0.0241 0.0352  475 ILE B CD1 
3115 N N   . HIS B 184 ? 0.6069 0.5474 0.3321 0.0210  -0.0337 -0.0432 476 HIS B N   
3116 C CA  . HIS B 184 ? 0.6467 0.5875 0.4011 0.0255  -0.0235 -0.0589 476 HIS B CA  
3117 C C   . HIS B 184 ? 0.5124 0.4421 0.2692 0.0144  -0.0543 -0.0654 476 HIS B C   
3118 O O   . HIS B 184 ? 0.5313 0.4740 0.3352 0.0158  -0.0554 -0.0680 476 HIS B O   
3119 C CB  . HIS B 184 ? 0.6203 0.5342 0.3369 0.0320  0.0087  -0.0771 476 HIS B CB  
3120 C CG  . HIS B 184 ? 0.7128 0.6475 0.4545 0.0436  0.0420  -0.0709 476 HIS B CG  
3121 N ND1 . HIS B 184 ? 0.6949 0.6640 0.5046 0.0516  0.0481  -0.0626 476 HIS B ND1 
3122 C CD2 . HIS B 184 ? 0.7745 0.7001 0.4828 0.0467  0.0703  -0.0709 476 HIS B CD2 
3123 C CE1 . HIS B 184 ? 0.7303 0.7117 0.5519 0.0584  0.0750  -0.0579 476 HIS B CE1 
3124 N NE2 . HIS B 184 ? 0.7487 0.7063 0.5134 0.0558  0.0910  -0.0622 476 HIS B NE2 
3125 N N   . ARG B 185 ? 0.5601 0.4649 0.2663 0.0015  -0.0812 -0.0666 477 ARG B N   
3126 C CA  . ARG B 185 ? 0.5492 0.4455 0.2640 -0.0123 -0.1152 -0.0711 477 ARG B CA  
3127 C C   . ARG B 185 ? 0.5695 0.5105 0.3612 -0.0138 -0.1346 -0.0515 477 ARG B C   
3128 O O   . ARG B 185 ? 0.6179 0.5688 0.4524 -0.0196 -0.1447 -0.0536 477 ARG B O   
3129 C CB  . ARG B 185 ? 0.6299 0.4881 0.2699 -0.0276 -0.1444 -0.0757 477 ARG B CB  
3130 C CG  . ARG B 185 ? 0.7700 0.5762 0.3240 -0.0275 -0.1231 -0.0993 477 ARG B CG  
3131 C CD  . ARG B 185 ? 0.8446 0.6156 0.3406 -0.0452 -0.1531 -0.1063 477 ARG B CD  
3132 N NE  . ARG B 185 ? 1.1979 0.9642 0.6471 -0.0476 -0.1540 -0.0928 477 ARG B NE  
3133 C CZ  . ARG B 185 ? 1.2219 0.9664 0.6152 -0.0418 -0.1201 -0.1004 477 ARG B CZ  
3134 N NH1 . ARG B 185 ? 1.1546 0.8836 0.5381 -0.0313 -0.0806 -0.1216 477 ARG B NH1 
3135 N NH2 . ARG B 185 ? 1.0991 0.8393 0.4522 -0.0460 -0.1251 -0.0848 477 ARG B NH2 
3136 N N   . VAL B 186 ? 0.4843 0.4510 0.2952 -0.0086 -0.1377 -0.0323 478 VAL B N   
3137 C CA  . VAL B 186 ? 0.4356 0.4446 0.3219 -0.0064 -0.1488 -0.0155 478 VAL B CA  
3138 C C   . VAL B 186 ? 0.3807 0.4125 0.3161 0.0042  -0.1197 -0.0177 478 VAL B C   
3139 O O   . VAL B 186 ? 0.4173 0.4730 0.4068 0.0019  -0.1243 -0.0128 478 VAL B O   
3140 C CB  . VAL B 186 ? 0.4860 0.5102 0.3791 -0.0010 -0.1577 0.0043  478 VAL B CB  
3141 C CG1 . VAL B 186 ? 0.3705 0.4370 0.3448 0.0044  -0.1633 0.0191  478 VAL B CG1 
3142 C CG2 . VAL B 186 ? 0.4647 0.4637 0.3050 -0.0130 -0.1922 0.0098  478 VAL B CG2 
3143 N N   . LEU B 187 ? 0.3944 0.4193 0.3116 0.0147  -0.0899 -0.0238 479 LEU B N   
3144 C CA  . LEU B 187 ? 0.3765 0.4173 0.3318 0.0232  -0.0670 -0.0261 479 LEU B CA  
3145 C C   . LEU B 187 ? 0.3642 0.3928 0.3277 0.0171  -0.0700 -0.0369 479 LEU B C   
3146 O O   . LEU B 187 ? 0.3662 0.4126 0.3720 0.0179  -0.0653 -0.0322 479 LEU B O   
3147 C CB  . LEU B 187 ? 0.3511 0.3856 0.2875 0.0337  -0.0393 -0.0306 479 LEU B CB  
3148 C CG  . LEU B 187 ? 0.4275 0.4812 0.3791 0.0408  -0.0297 -0.0179 479 LEU B CG  
3149 C CD1 . LEU B 187 ? 0.3345 0.3815 0.2699 0.0475  -0.0040 -0.0222 479 LEU B CD1 
3150 C CD2 . LEU B 187 ? 0.2544 0.3353 0.2579 0.0447  -0.0286 -0.0103 479 LEU B CD2 
3151 N N   . ASP B 188 ? 0.4019 0.3957 0.3211 0.0104  -0.0773 -0.0514 480 ASP B N   
3152 C CA  . ASP B 188 ? 0.4903 0.4652 0.4159 0.0033  -0.0829 -0.0621 480 ASP B CA  
3153 C C   . ASP B 188 ? 0.4368 0.4294 0.4032 -0.0107 -0.1086 -0.0520 480 ASP B C   
3154 O O   . ASP B 188 ? 0.3879 0.3835 0.3876 -0.0151 -0.1074 -0.0510 480 ASP B O   
3155 C CB  . ASP B 188 ? 0.4519 0.3793 0.3150 -0.0014 -0.0859 -0.0826 480 ASP B CB  
3156 C CG  . ASP B 188 ? 0.4565 0.3666 0.2955 0.0138  -0.0528 -0.0951 480 ASP B CG  
3157 O OD1 . ASP B 188 ? 0.4211 0.3563 0.2986 0.0260  -0.0327 -0.0872 480 ASP B OD1 
3158 O OD2 . ASP B 188 ? 0.5898 0.4608 0.3718 0.0132  -0.0467 -0.1130 480 ASP B OD2 
3159 N N   . LYS B 189 ? 0.4382 0.4439 0.4067 -0.0180 -0.1320 -0.0424 481 LYS B N   
3160 C CA  . LYS B 189 ? 0.4301 0.4587 0.4489 -0.0312 -0.1565 -0.0312 481 LYS B CA  
3161 C C   . LYS B 189 ? 0.3646 0.4359 0.4483 -0.0237 -0.1393 -0.0160 481 LYS B C   
3162 O O   . LYS B 189 ? 0.3625 0.4500 0.4926 -0.0331 -0.1434 -0.0095 481 LYS B O   
3163 C CB  . LYS B 189 ? 0.4031 0.4354 0.4120 -0.0397 -0.1893 -0.0231 481 LYS B CB  
3164 C CG  . LYS B 189 ? 0.4439 0.4936 0.5024 -0.0574 -0.2214 -0.0145 481 LYS B CG  
3165 C CD  . LYS B 189 ? 0.5432 0.5710 0.5631 -0.0721 -0.2623 -0.0156 481 LYS B CD  
3166 C CE  . LYS B 189 ? 0.7573 0.7887 0.8146 -0.0899 -0.2812 -0.0131 481 LYS B CE  
3167 N NZ  . LYS B 189 ? 0.7872 0.7734 0.8048 -0.1029 -0.2854 -0.0342 481 LYS B NZ  
3168 N N   . ILE B 190 ? 0.2993 0.3867 0.3848 -0.0082 -0.1190 -0.0104 482 ILE B N   
3169 C CA  . ILE B 190 ? 0.3807 0.5002 0.5149 -0.0006 -0.0997 0.0002  482 ILE B CA  
3170 C C   . ILE B 190 ? 0.3428 0.4536 0.4799 -0.0008 -0.0814 -0.0045 482 ILE B C   
3171 O O   . ILE B 190 ? 0.3191 0.4494 0.4945 -0.0036 -0.0724 0.0041  482 ILE B O   
3172 C CB  . ILE B 190 ? 0.4007 0.5307 0.5290 0.0145  -0.0847 0.0046  482 ILE B CB  
3173 C CG1 . ILE B 190 ? 0.3277 0.4643 0.4565 0.0147  -0.1053 0.0132  482 ILE B CG1 
3174 C CG2 . ILE B 190 ? 0.1930 0.3485 0.3610 0.0220  -0.0639 0.0116  482 ILE B CG2 
3175 C CD1 . ILE B 190 ? 0.3278 0.4638 0.4410 0.0275  -0.0933 0.0171  482 ILE B CD1 
3176 N N   . THR B 191 ? 0.2882 0.3685 0.3854 0.0025  -0.0747 -0.0171 483 THR B N   
3177 C CA  . THR B 191 ? 0.3536 0.4207 0.4550 0.0022  -0.0632 -0.0200 483 THR B CA  
3178 C C   . THR B 191 ? 0.3247 0.3849 0.4475 -0.0143 -0.0778 -0.0179 483 THR B C   
3179 O O   . THR B 191 ? 0.3767 0.4436 0.5255 -0.0182 -0.0692 -0.0092 483 THR B O   
3180 C CB  . THR B 191 ? 0.3871 0.4227 0.4498 0.0105  -0.0546 -0.0344 483 THR B CB  
3181 O OG1 . THR B 191 ? 0.3876 0.4332 0.4382 0.0236  -0.0399 -0.0339 483 THR B OG1 
3182 C CG2 . THR B 191 ? 0.3848 0.4054 0.4577 0.0121  -0.0459 -0.0349 483 THR B CG2 
3183 N N   . ASP B 192 ? 0.2967 0.3413 0.4063 -0.0261 -0.1013 -0.0249 484 ASP B N   
3184 C CA  . ASP B 192 ? 0.3285 0.3674 0.4640 -0.0452 -0.1194 -0.0223 484 ASP B CA  
3185 C C   . ASP B 192 ? 0.3598 0.4431 0.5564 -0.0520 -0.1192 -0.0031 484 ASP B C   
3186 O O   . ASP B 192 ? 0.3039 0.3924 0.5354 -0.0649 -0.1187 0.0053  484 ASP B O   
3187 C CB  . ASP B 192 ? 0.3724 0.3843 0.4773 -0.0582 -0.1494 -0.0344 484 ASP B CB  
3188 C CG  . ASP B 192 ? 0.5199 0.4823 0.5612 -0.0520 -0.1447 -0.0563 484 ASP B CG  
3189 O OD1 . ASP B 192 ? 0.5111 0.4635 0.5444 -0.0380 -0.1197 -0.0605 484 ASP B OD1 
3190 O OD2 . ASP B 192 ? 0.6164 0.5490 0.6155 -0.0613 -0.1659 -0.0695 484 ASP B OD2 
3191 N N   . THR B 193 ? 0.2912 0.4061 0.5036 -0.0430 -0.1173 0.0046  485 THR B N   
3192 C CA  . THR B 193 ? 0.2579 0.4164 0.5325 -0.0454 -0.1112 0.0214  485 THR B CA  
3193 C C   . THR B 193 ? 0.3013 0.4702 0.5885 -0.0391 -0.0788 0.0282  485 THR B C   
3194 O O   . THR B 193 ? 0.2350 0.4245 0.5661 -0.0489 -0.0701 0.0402  485 THR B O   
3195 C CB  . THR B 193 ? 0.2288 0.4124 0.5157 -0.0339 -0.1157 0.0268  485 THR B CB  
3196 O OG1 . THR B 193 ? 0.2654 0.4364 0.5345 -0.0419 -0.1498 0.0233  485 THR B OG1 
3197 C CG2 . THR B 193 ? 0.2884 0.5126 0.6378 -0.0325 -0.1033 0.0414  485 THR B CG2 
3198 N N   . LEU B 194 ? 0.2574 0.4118 0.5056 -0.0242 -0.0613 0.0218  486 LEU B N   
3199 C CA  . LEU B 194 ? 0.2839 0.4422 0.5330 -0.0194 -0.0355 0.0281  486 LEU B CA  
3200 C C   . LEU B 194 ? 0.2591 0.3981 0.5098 -0.0326 -0.0351 0.0325  486 LEU B C   
3201 O O   . LEU B 194 ? 0.2565 0.4080 0.5285 -0.0389 -0.0190 0.0452  486 LEU B O   
3202 C CB  . LEU B 194 ? 0.2322 0.3765 0.4409 -0.0034 -0.0244 0.0204  486 LEU B CB  
3203 C CG  . LEU B 194 ? 0.3203 0.4854 0.5329 0.0093  -0.0111 0.0221  486 LEU B CG  
3204 C CD1 . LEU B 194 ? 0.3306 0.4797 0.5064 0.0213  -0.0062 0.0141  486 LEU B CD1 
3205 C CD2 . LEU B 194 ? 0.2922 0.4753 0.5259 0.0084  0.0104  0.0316  486 LEU B CD2 
3206 N N   . ILE B 195 ? 0.2792 0.3842 0.5053 -0.0369 -0.0508 0.0223  487 ILE B N   
3207 C CA  . ILE B 195 ? 0.2898 0.3696 0.5186 -0.0493 -0.0531 0.0263  487 ILE B CA  
3208 C C   . ILE B 195 ? 0.2789 0.3761 0.5546 -0.0702 -0.0607 0.0382  487 ILE B C   
3209 O O   . ILE B 195 ? 0.2629 0.3580 0.5563 -0.0813 -0.0507 0.0519  487 ILE B O   
3210 C CB  . ILE B 195 ? 0.3271 0.3633 0.5215 -0.0476 -0.0676 0.0094  487 ILE B CB  
3211 C CG1 . ILE B 195 ? 0.4248 0.4468 0.5868 -0.0278 -0.0544 0.0025  487 ILE B CG1 
3212 C CG2 . ILE B 195 ? 0.2908 0.2967 0.4951 -0.0638 -0.0768 0.0123  487 ILE B CG2 
3213 C CD1 . ILE B 195 ? 0.2985 0.3082 0.4618 -0.0257 -0.0435 0.0141  487 ILE B CD1 
3214 N N   . HIS B 196 ? 0.2830 0.3985 0.5819 -0.0768 -0.0795 0.0355  488 HIS B N   
3215 C CA  . HIS B 196 ? 0.2831 0.4228 0.6394 -0.0973 -0.0889 0.0484  488 HIS B CA  
3216 C C   . HIS B 196 ? 0.2807 0.4630 0.6803 -0.0955 -0.0599 0.0664  488 HIS B C   
3217 O O   . HIS B 196 ? 0.3205 0.5166 0.7622 -0.1122 -0.0526 0.0810  488 HIS B O   
3218 C CB  . HIS B 196 ? 0.3191 0.4711 0.6919 -0.1034 -0.1198 0.0429  488 HIS B CB  
3219 C CG  . HIS B 196 ? 0.4366 0.6157 0.8645 -0.1185 -0.1272 0.0559  488 HIS B CG  
3220 N ND1 . HIS B 196 ? 0.4656 0.6854 0.9292 -0.1087 -0.1088 0.0671  488 HIS B ND1 
3221 C CD2 . HIS B 196 ? 0.4989 0.6630 0.9407 -0.1386 -0.1470 0.0569  488 HIS B CD2 
3222 C CE1 . HIS B 196 ? 0.3949 0.6279 0.8982 -0.1224 -0.1173 0.0756  488 HIS B CE1 
3223 N NE2 . HIS B 196 ? 0.5286 0.7298 1.0200 -0.1411 -0.1411 0.0705  488 HIS B NE2 
3224 N N   . LEU B 197 ? 0.3673 0.5675 0.7541 -0.0754 -0.0408 0.0648  489 LEU B N   
3225 C CA  . LEU B 197 ? 0.2390 0.4729 0.6565 -0.0712 -0.0090 0.0778  489 LEU B CA  
3226 C C   . LEU B 197 ? 0.2814 0.4984 0.6789 -0.0777 0.0144  0.0876  489 LEU B C   
3227 O O   . LEU B 197 ? 0.2359 0.4701 0.6596 -0.0861 0.0357  0.1006  489 LEU B O   
3228 C CB  . LEU B 197 ? 0.2850 0.5290 0.6810 -0.0482 0.0042  0.0700  489 LEU B CB  
3229 C CG  . LEU B 197 ? 0.2788 0.5374 0.6881 -0.0389 -0.0096 0.0644  489 LEU B CG  
3230 C CD1 . LEU B 197 ? 0.1844 0.4404 0.5634 -0.0183 -0.0003 0.0559  489 LEU B CD1 
3231 C CD2 . LEU B 197 ? 0.2795 0.5625 0.7305 -0.0422 0.0019  0.0726  489 LEU B CD2 
3232 N N   . MET B 198 ? 0.2196 0.3973 0.5614 -0.0718 0.0105  0.0806  490 MET B N   
3233 C CA  . MET B 198 ? 0.2666 0.4237 0.5845 -0.0776 0.0275  0.0926  490 MET B CA  
3234 C C   . MET B 198 ? 0.3095 0.4502 0.6504 -0.1003 0.0176  0.1039  490 MET B C   
3235 O O   . MET B 198 ? 0.3498 0.4872 0.6930 -0.1119 0.0361  0.1217  490 MET B O   
3236 C CB  . MET B 198 ? 0.3143 0.4375 0.5751 -0.0630 0.0228  0.0837  490 MET B CB  
3237 C CG  . MET B 198 ? 0.2576 0.3915 0.4991 -0.0432 0.0234  0.0694  490 MET B CG  
3238 S SD  . MET B 198 ? 0.3493 0.4486 0.5447 -0.0285 0.0093  0.0563  490 MET B SD  
3239 C CE  . MET B 198 ? 0.2634 0.3805 0.4388 -0.0112 0.0228  0.0501  490 MET B CE  
3240 N N   . ALA B 199 ? 0.3506 0.4768 0.7042 -0.1083 -0.0115 0.0939  491 ALA B N   
3241 C CA  . ALA B 199 ? 0.3488 0.4576 0.7295 -0.1325 -0.0241 0.1032  491 ALA B CA  
3242 C C   . ALA B 199 ? 0.2946 0.4452 0.7366 -0.1492 -0.0111 0.1204  491 ALA B C   
3243 O O   . ALA B 199 ? 0.3700 0.5111 0.8195 -0.1638 -0.0003 0.1350  491 ALA B O   
3244 C CB  . ALA B 199 ? 0.3326 0.4142 0.7079 -0.1376 -0.0592 0.0848  491 ALA B CB  
3245 N N   . LYS B 200 ? 0.4169 0.6055 0.8823 -0.1390 -0.0106 0.1139  492 LYS B N   
3246 C CA  . LYS B 200 ? 0.4134 0.6358 0.9189 -0.1437 0.0052  0.1233  492 LYS B CA  
3247 C C   . LYS B 200 ? 0.2945 0.5283 0.7886 -0.1392 0.0467  0.1353  492 LYS B C   
3248 O O   . LYS B 200 ? 0.3783 0.6299 0.9001 -0.1489 0.0646  0.1461  492 LYS B O   
3249 C CB  . LYS B 200 ? 0.3146 0.5687 0.8450 -0.1309 -0.0050 0.1143  492 LYS B CB  
3250 C CG  . LYS B 200 ? 0.4092 0.6535 0.9509 -0.1399 -0.0465 0.1055  492 LYS B CG  
3251 C CD  . LYS B 200 ? 0.4685 0.7078 1.0427 -0.1635 -0.0589 0.1141  492 LYS B CD  
3252 C CE  . LYS B 200 ? 0.5963 0.8361 1.1882 -0.1710 -0.0976 0.1069  492 LYS B CE  
3253 N NZ  . LYS B 200 ? 0.5763 0.8586 1.2093 -0.1608 -0.0949 0.1117  492 LYS B NZ  
3254 N N   . ALA B 201 ? 0.3410 0.5634 0.7916 -0.1255 0.0621  0.1333  493 ALA B N   
3255 C CA  . ALA B 201 ? 0.3141 0.5368 0.7368 -0.1229 0.0990  0.1433  493 ALA B CA  
3256 C C   . ALA B 201 ? 0.4945 0.6852 0.8952 -0.1412 0.1046  0.1609  493 ALA B C   
3257 O O   . ALA B 201 ? 0.5052 0.6919 0.8768 -0.1433 0.1340  0.1716  493 ALA B O   
3258 C CB  . ALA B 201 ? 0.2766 0.4940 0.6545 -0.1027 0.1103  0.1350  493 ALA B CB  
3259 N N   . GLY B 202 ? 0.4123 0.5748 0.8203 -0.1544 0.0761  0.1632  494 GLY B N   
3260 C CA  . GLY B 202 ? 0.4230 0.5474 0.8096 -0.1705 0.0765  0.1798  494 GLY B CA  
3261 C C   . GLY B 202 ? 0.4807 0.5623 0.8173 -0.1641 0.0678  0.1843  494 GLY B C   
3262 O O   . GLY B 202 ? 0.5818 0.6256 0.8945 -0.1746 0.0659  0.1994  494 GLY B O   
3263 N N   . LEU B 203 ? 0.4079 0.4891 0.7133 -0.1403 0.0589  0.1640  495 LEU B N   
3264 C CA  . LEU B 203 ? 0.4769 0.5177 0.7264 -0.1260 0.0467  0.1593  495 LEU B CA  
3265 C C   . LEU B 203 ? 0.4910 0.4902 0.7444 -0.1310 0.0177  0.1544  495 LEU B C   
3266 O O   . LEU B 203 ? 0.3838 0.3853 0.6673 -0.1358 -0.0003 0.1402  495 LEU B O   
3267 C CB  . LEU B 203 ? 0.3318 0.3854 0.5574 -0.1012 0.0434  0.1381  495 LEU B CB  
3268 C CG  . LEU B 203 ? 0.5164 0.5864 0.7092 -0.0903 0.0676  0.1404  495 LEU B CG  
3269 C CD1 . LEU B 203 ? 0.4016 0.5124 0.6273 -0.0973 0.0961  0.1460  495 LEU B CD1 
3270 C CD2 . LEU B 203 ? 0.3781 0.4508 0.5486 -0.0681 0.0573  0.1198  495 LEU B CD2 
3271 N N   . THR B 204 ? 0.5148 0.4726 0.7357 -0.1297 0.0121  0.1660  496 THR B N   
3272 C CA  . THR B 204 ? 0.4556 0.3678 0.6778 -0.1294 -0.0131 0.1592  496 THR B CA  
3273 C C   . THR B 204 ? 0.4151 0.3240 0.6258 -0.1063 -0.0277 0.1303  496 THR B C   
3274 O O   . THR B 204 ? 0.4031 0.3409 0.6004 -0.0905 -0.0200 0.1198  496 THR B O   
3275 C CB  . THR B 204 ? 0.5080 0.3774 0.7015 -0.1298 -0.0161 0.1808  496 THR B CB  
3276 O OG1 . THR B 204 ? 0.5779 0.4460 0.7347 -0.1068 -0.0176 0.1765  496 THR B OG1 
3277 C CG2 . THR B 204 ? 0.5222 0.3970 0.7126 -0.1516 0.0047  0.2121  496 THR B CG2 
3278 N N   . LEU B 205 ? 0.4452 0.3153 0.6603 -0.1050 -0.0472 0.1171  497 LEU B N   
3279 C CA  . LEU B 205 ? 0.4196 0.2826 0.6215 -0.0841 -0.0567 0.0894  497 LEU B CA  
3280 C C   . LEU B 205 ? 0.4341 0.2994 0.6111 -0.0606 -0.0511 0.0901  497 LEU B C   
3281 O O   . LEU B 205 ? 0.4383 0.3243 0.6061 -0.0445 -0.0482 0.0732  497 LEU B O   
3282 C CB  . LEU B 205 ? 0.5078 0.3200 0.7129 -0.0863 -0.0744 0.0749  497 LEU B CB  
3283 C CG  . LEU B 205 ? 0.6889 0.4999 0.9087 -0.1030 -0.0876 0.0583  497 LEU B CG  
3284 C CD1 . LEU B 205 ? 0.6155 0.3660 0.8284 -0.1048 -0.1043 0.0410  497 LEU B CD1 
3285 C CD2 . LEU B 205 ? 0.4756 0.3226 0.6855 -0.0924 -0.0863 0.0392  497 LEU B CD2 
3286 N N   . GLN B 206 ? 0.4298 0.2736 0.5968 -0.0598 -0.0514 0.1115  498 GLN B N   
3287 C CA  . GLN B 206 ? 0.5614 0.4096 0.7084 -0.0404 -0.0510 0.1154  498 GLN B CA  
3288 C C   . GLN B 206 ? 0.4193 0.3106 0.5499 -0.0398 -0.0364 0.1184  498 GLN B C   
3289 O O   . GLN B 206 ? 0.3922 0.3004 0.5133 -0.0233 -0.0360 0.1073  498 GLN B O   
3290 C CB  . GLN B 206 ? 0.5099 0.3228 0.6479 -0.0420 -0.0598 0.1412  498 GLN B CB  
3291 C CG  . GLN B 206 ? 0.5157 0.3334 0.6355 -0.0247 -0.0654 0.1491  498 GLN B CG  
3292 C CD  . GLN B 206 ? 0.5648 0.3443 0.6759 -0.0260 -0.0801 0.1771  498 GLN B CD  
3293 O OE1 . GLN B 206 ? 0.6036 0.3661 0.7018 -0.0455 -0.0775 0.2005  498 GLN B OE1 
3294 N NE2 . GLN B 206 ? 0.5163 0.2828 0.6377 -0.0053 -0.0956 0.1770  498 GLN B NE2 
3295 N N   . GLN B 207 ? 0.3922 0.3004 0.5216 -0.0578 -0.0226 0.1328  499 GLN B N   
3296 C CA  . GLN B 207 ? 0.3684 0.3134 0.4825 -0.0563 -0.0051 0.1329  499 GLN B CA  
3297 C C   . GLN B 207 ? 0.3295 0.3060 0.4604 -0.0472 -0.0027 0.1091  499 GLN B C   
3298 O O   . GLN B 207 ? 0.3289 0.3285 0.4457 -0.0375 0.0061  0.1027  499 GLN B O   
3299 C CB  . GLN B 207 ? 0.4110 0.3677 0.5266 -0.0768 0.0146  0.1523  499 GLN B CB  
3300 C CG  . GLN B 207 ? 0.4419 0.3694 0.5249 -0.0865 0.0169  0.1797  499 GLN B CG  
3301 C CD  . GLN B 207 ? 0.4704 0.4069 0.5602 -0.1095 0.0402  0.1997  499 GLN B CD  
3302 O OE1 . GLN B 207 ? 0.5093 0.4662 0.6436 -0.1209 0.0467  0.1957  499 GLN B OE1 
3303 N NE2 . GLN B 207 ? 0.5268 0.4482 0.5722 -0.1175 0.0526  0.2225  499 GLN B NE2 
3304 N N   . GLN B 208 ? 0.3170 0.2906 0.4741 -0.0512 -0.0121 0.0962  500 GLN B N   
3305 C CA  . GLN B 208 ? 0.3338 0.3332 0.5021 -0.0444 -0.0132 0.0765  500 GLN B CA  
3306 C C   . GLN B 208 ? 0.2796 0.2758 0.4290 -0.0236 -0.0177 0.0610  500 GLN B C   
3307 O O   . GLN B 208 ? 0.3115 0.3330 0.4538 -0.0147 -0.0101 0.0553  500 GLN B O   
3308 C CB  . GLN B 208 ? 0.2992 0.2892 0.4913 -0.0562 -0.0271 0.0671  500 GLN B CB  
3309 C CG  . GLN B 208 ? 0.3191 0.3282 0.5450 -0.0780 -0.0226 0.0807  500 GLN B CG  
3310 C CD  . GLN B 208 ? 0.4217 0.4116 0.6696 -0.0937 -0.0430 0.0734  500 GLN B CD  
3311 O OE1 . GLN B 208 ? 0.3759 0.3572 0.6155 -0.0883 -0.0585 0.0532  500 GLN B OE1 
3312 N NE2 . GLN B 208 ? 0.3638 0.3440 0.6360 -0.1149 -0.0433 0.0899  500 GLN B NE2 
3313 N N   . HIS B 209 ? 0.2959 0.2606 0.4407 -0.0156 -0.0284 0.0543  501 HIS B N   
3314 C CA  . HIS B 209 ? 0.3262 0.2913 0.4614 0.0037  -0.0292 0.0404  501 HIS B CA  
3315 C C   . HIS B 209 ? 0.3247 0.3004 0.4484 0.0127  -0.0256 0.0512  501 HIS B C   
3316 O O   . HIS B 209 ? 0.3114 0.3009 0.4322 0.0255  -0.0236 0.0419  501 HIS B O   
3317 C CB  . HIS B 209 ? 0.4128 0.3419 0.5514 0.0119  -0.0372 0.0290  501 HIS B CB  
3318 C CG  . HIS B 209 ? 0.4179 0.3168 0.5623 0.0129  -0.0440 0.0442  501 HIS B CG  
3319 N ND1 . HIS B 209 ? 0.5297 0.3905 0.6823 0.0055  -0.0521 0.0439  501 HIS B ND1 
3320 C CD2 . HIS B 209 ? 0.4133 0.3108 0.5559 0.0202  -0.0470 0.0607  501 HIS B CD2 
3321 C CE1 . HIS B 209 ? 0.5236 0.3609 0.6811 0.0092  -0.0584 0.0613  501 HIS B CE1 
3322 N NE2 . HIS B 209 ? 0.4649 0.3248 0.6157 0.0180  -0.0567 0.0724  501 HIS B NE2 
3323 N N   . GLN B 210 ? 0.3343 0.3024 0.4490 0.0044  -0.0258 0.0714  502 GLN B N   
3324 C CA  . GLN B 210 ? 0.3507 0.3265 0.4451 0.0095  -0.0257 0.0814  502 GLN B CA  
3325 C C   . GLN B 210 ? 0.3675 0.3737 0.4501 0.0079  -0.0122 0.0758  502 GLN B C   
3326 O O   . GLN B 210 ? 0.3251 0.3422 0.3978 0.0170  -0.0134 0.0703  502 GLN B O   
3327 C CB  . GLN B 210 ? 0.3219 0.2757 0.3985 -0.0008 -0.0300 0.1056  502 GLN B CB  
3328 C CG  . GLN B 210 ? 0.3463 0.2689 0.4314 0.0070  -0.0483 0.1151  502 GLN B CG  
3329 C CD  . GLN B 210 ? 0.4653 0.3620 0.5282 -0.0051 -0.0547 0.1429  502 GLN B CD  
3330 O OE1 . GLN B 210 ? 0.4325 0.3361 0.4657 -0.0187 -0.0430 0.1545  502 GLN B OE1 
3331 N NE2 . GLN B 210 ? 0.4856 0.3502 0.5616 0.0003  -0.0717 0.1543  502 GLN B NE2 
3332 N N   . ARG B 211 ? 0.2806 0.3006 0.3694 -0.0035 0.0004  0.0772  503 ARG B N   
3333 C CA  . ARG B 211 ? 0.3258 0.3728 0.4094 -0.0028 0.0153  0.0717  503 ARG B CA  
3334 C C   . ARG B 211 ? 0.2965 0.3602 0.3944 0.0081  0.0126  0.0536  503 ARG B C   
3335 O O   . ARG B 211 ? 0.2589 0.3361 0.3473 0.0150  0.0184  0.0474  503 ARG B O   
3336 C CB  . ARG B 211 ? 0.2653 0.3263 0.3638 -0.0164 0.0311  0.0797  503 ARG B CB  
3337 C CG  . ARG B 211 ? 0.2761 0.3639 0.3751 -0.0134 0.0501  0.0745  503 ARG B CG  
3338 C CD  . ARG B 211 ? 0.2552 0.3592 0.3755 -0.0263 0.0702  0.0853  503 ARG B CD  
3339 N NE  . ARG B 211 ? 0.3415 0.4712 0.4699 -0.0202 0.0912  0.0791  503 ARG B NE  
3340 C CZ  . ARG B 211 ? 0.4544 0.5798 0.5479 -0.0182 0.1119  0.0804  503 ARG B CZ  
3341 N NH1 . ARG B 211 ? 0.4176 0.5152 0.4616 -0.0235 0.1113  0.0897  503 ARG B NH1 
3342 N NH2 . ARG B 211 ? 0.4475 0.5938 0.5540 -0.0106 0.1324  0.0721  503 ARG B NH2 
3343 N N   . LEU B 212 ? 0.2128 0.2715 0.3289 0.0085  0.0036  0.0450  504 LEU B N   
3344 C CA  . LEU B 212 ? 0.2965 0.3653 0.4167 0.0178  0.0006  0.0297  504 LEU B CA  
3345 C C   . LEU B 212 ? 0.2486 0.3149 0.3569 0.0305  -0.0008 0.0250  504 LEU B C   
3346 O O   . LEU B 212 ? 0.2795 0.3605 0.3850 0.0366  0.0032  0.0185  504 LEU B O   
3347 C CB  . LEU B 212 ? 0.1928 0.2468 0.3213 0.0149  -0.0097 0.0204  504 LEU B CB  
3348 C CG  . LEU B 212 ? 0.2159 0.2715 0.3367 0.0238  -0.0123 0.0051  504 LEU B CG  
3349 C CD1 . LEU B 212 ? 0.1714 0.2510 0.2987 0.0211  -0.0120 0.0040  504 LEU B CD1 
3350 C CD2 . LEU B 212 ? 0.2581 0.2860 0.3726 0.0226  -0.0209 -0.0065 504 LEU B CD2 
3351 N N   . ALA B 213 ? 0.2545 0.3025 0.3607 0.0343  -0.0076 0.0299  505 ALA B N   
3352 C CA  . ALA B 213 ? 0.1894 0.2393 0.2952 0.0453  -0.0110 0.0281  505 ALA B CA  
3353 C C   . ALA B 213 ? 0.2151 0.2771 0.3050 0.0434  -0.0091 0.0335  505 ALA B C   
3354 O O   . ALA B 213 ? 0.2428 0.3161 0.3342 0.0493  -0.0087 0.0274  505 ALA B O   
3355 C CB  . ALA B 213 ? 0.2290 0.2582 0.3442 0.0503  -0.0212 0.0354  505 ALA B CB  
3356 N N   . GLN B 214 ? 0.2566 0.3132 0.3281 0.0341  -0.0067 0.0446  506 GLN B N   
3357 C CA  . GLN B 214 ? 0.2084 0.2692 0.2544 0.0315  -0.0029 0.0468  506 GLN B CA  
3358 C C   . GLN B 214 ? 0.3122 0.3913 0.3621 0.0344  0.0093  0.0347  506 GLN B C   
3359 O O   . GLN B 214 ? 0.2897 0.3711 0.3274 0.0372  0.0088  0.0296  506 GLN B O   
3360 C CB  . GLN B 214 ? 0.2737 0.3228 0.2931 0.0203  0.0037  0.0601  506 GLN B CB  
3361 C CG  . GLN B 214 ? 0.3370 0.3627 0.3432 0.0166  -0.0116 0.0764  506 GLN B CG  
3362 C CD  . GLN B 214 ? 0.4468 0.4598 0.4370 0.0036  -0.0019 0.0915  506 GLN B CD  
3363 O OE1 . GLN B 214 ? 0.4018 0.4267 0.3892 -0.0030 0.0188  0.0898  506 GLN B OE1 
3364 N NE2 . GLN B 214 ? 0.4432 0.4325 0.4275 -0.0001 -0.0161 0.1081  506 GLN B NE2 
3365 N N   . LEU B 215 ? 0.2560 0.3462 0.3245 0.0331  0.0176  0.0309  507 LEU B N   
3366 C CA  . LEU B 215 ? 0.2182 0.3250 0.2955 0.0369  0.0265  0.0223  507 LEU B CA  
3367 C C   . LEU B 215 ? 0.2532 0.3632 0.3367 0.0451  0.0197  0.0137  507 LEU B C   
3368 O O   . LEU B 215 ? 0.2557 0.3701 0.3346 0.0488  0.0232  0.0089  507 LEU B O   
3369 C CB  . LEU B 215 ? 0.2466 0.3659 0.3483 0.0326  0.0311  0.0233  507 LEU B CB  
3370 C CG  . LEU B 215 ? 0.2681 0.3946 0.3743 0.0247  0.0461  0.0316  507 LEU B CG  
3371 C CD1 . LEU B 215 ? 0.2381 0.3827 0.3816 0.0198  0.0464  0.0334  507 LEU B CD1 
3372 C CD2 . LEU B 215 ? 0.3202 0.4504 0.4106 0.0293  0.0621  0.0281  507 LEU B CD2 
3373 N N   . LEU B 216 ? 0.2072 0.3122 0.3001 0.0476  0.0121  0.0114  508 LEU B N   
3374 C CA  . LEU B 216 ? 0.2541 0.3624 0.3517 0.0545  0.0109  0.0042  508 LEU B CA  
3375 C C   . LEU B 216 ? 0.2311 0.3391 0.3278 0.0577  0.0074  0.0055  508 LEU B C   
3376 O O   . LEU B 216 ? 0.2144 0.3288 0.3158 0.0609  0.0096  0.0016  508 LEU B O   
3377 C CB  . LEU B 216 ? 0.1640 0.2635 0.2669 0.0566  0.0083  -0.0007 508 LEU B CB  
3378 C CG  . LEU B 216 ? 0.2551 0.3521 0.3583 0.0504  0.0058  -0.0026 508 LEU B CG  
3379 C CD1 . LEU B 216 ? 0.1957 0.2770 0.2929 0.0523  0.0031  -0.0117 508 LEU B CD1 
3380 C CD2 . LEU B 216 ? 0.2161 0.3282 0.3217 0.0490  0.0071  -0.0024 508 LEU B CD2 
3381 N N   . LEU B 217 ? 0.1876 0.2875 0.2792 0.0555  0.0000  0.0126  509 LEU B N   
3382 C CA  . LEU B 217 ? 0.2229 0.3233 0.3159 0.0563  -0.0093 0.0153  509 LEU B CA  
3383 C C   . LEU B 217 ? 0.3008 0.4009 0.3739 0.0518  -0.0077 0.0123  509 LEU B C   
3384 O O   . LEU B 217 ? 0.3089 0.4107 0.3862 0.0511  -0.0155 0.0112  509 LEU B O   
3385 C CB  . LEU B 217 ? 0.1895 0.2781 0.2796 0.0546  -0.0229 0.0262  509 LEU B CB  
3386 C CG  . LEU B 217 ? 0.2406 0.3270 0.3597 0.0626  -0.0270 0.0283  509 LEU B CG  
3387 C CD1 . LEU B 217 ? 0.3246 0.3968 0.4431 0.0615  -0.0439 0.0425  509 LEU B CD1 
3388 C CD2 . LEU B 217 ? 0.1585 0.2598 0.3079 0.0704  -0.0245 0.0227  509 LEU B CD2 
3389 N N   . ILE B 218 ? 0.3083 0.4056 0.3634 0.0488  0.0029  0.0106  510 ILE B N   
3390 C CA  . ILE B 218 ? 0.3984 0.4919 0.4358 0.0473  0.0091  0.0042  510 ILE B CA  
3391 C C   . ILE B 218 ? 0.3206 0.4226 0.3764 0.0521  0.0122  -0.0022 510 ILE B C   
3392 O O   . ILE B 218 ? 0.2752 0.3703 0.3232 0.0509  0.0109  -0.0073 510 ILE B O   
3393 C CB  . ILE B 218 ? 0.3946 0.4864 0.4179 0.0455  0.0252  0.0039  510 ILE B CB  
3394 C CG1 . ILE B 218 ? 0.4601 0.5377 0.4536 0.0380  0.0239  0.0121  510 ILE B CG1 
3395 C CG2 . ILE B 218 ? 0.4351 0.5227 0.4483 0.0482  0.0367  -0.0056 510 ILE B CG2 
3396 C CD1 . ILE B 218 ? 0.4505 0.5307 0.4381 0.0350  0.0440  0.0150  510 ILE B CD1 
3397 N N   . LEU B 219 ? 0.2601 0.3727 0.3360 0.0562  0.0153  -0.0018 511 LEU B N   
3398 C CA  . LEU B 219 ? 0.2655 0.3830 0.3524 0.0595  0.0182  -0.0047 511 LEU B CA  
3399 C C   . LEU B 219 ? 0.2723 0.3898 0.3675 0.0581  0.0125  -0.0044 511 LEU B C   
3400 O O   . LEU B 219 ? 0.2548 0.3709 0.3537 0.0578  0.0146  -0.0057 511 LEU B O   
3401 C CB  . LEU B 219 ? 0.2560 0.3782 0.3512 0.0613  0.0200  -0.0039 511 LEU B CB  
3402 C CG  . LEU B 219 ? 0.3237 0.4492 0.4207 0.0604  0.0221  -0.0029 511 LEU B CG  
3403 C CD1 . LEU B 219 ? 0.3815 0.5086 0.4814 0.0608  0.0186  -0.0029 511 LEU B CD1 
3404 C CD2 . LEU B 219 ? 0.1990 0.3253 0.2971 0.0616  0.0286  -0.0037 511 LEU B CD2 
3405 N N   A SER B 220 ? 0.2595 0.3791 0.3632 0.0571  0.0046  -0.0011 512 SER B N   
3406 N N   B SER B 220 ? 0.2608 0.3804 0.3644 0.0570  0.0046  -0.0011 512 SER B N   
3407 C CA  A SER B 220 ? 0.3311 0.4560 0.4539 0.0547  -0.0021 0.0010  512 SER B CA  
3408 C CA  B SER B 220 ? 0.2910 0.4160 0.4140 0.0547  -0.0020 0.0009  512 SER B CA  
3409 C C   A SER B 220 ? 0.3617 0.4759 0.4710 0.0473  -0.0116 -0.0014 512 SER B C   
3410 C C   B SER B 220 ? 0.3346 0.4490 0.4445 0.0473  -0.0121 -0.0012 512 SER B C   
3411 O O   A SER B 220 ? 0.2742 0.3901 0.3978 0.0431  -0.0144 -0.0015 512 SER B O   
3412 O O   B SER B 220 ? 0.2744 0.3912 0.4000 0.0428  -0.0161 -0.0009 512 SER B O   
3413 C CB  A SER B 220 ? 0.2792 0.4104 0.4223 0.0570  -0.0107 0.0065  512 SER B CB  
3414 C CB  B SER B 220 ? 0.2536 0.3855 0.3980 0.0573  -0.0097 0.0063  512 SER B CB  
3415 O OG  A SER B 220 ? 0.2613 0.4009 0.4242 0.0642  0.0009  0.0057  512 SER B OG  
3416 O OG  B SER B 220 ? 0.3040 0.4256 0.4313 0.0545  -0.0223 0.0103  512 SER B OG  
3417 N N   . HIS B 221 ? 0.2577 0.3578 0.3367 0.0445  -0.0154 -0.0037 513 HIS B N   
3418 C CA  . HIS B 221 ? 0.2441 0.3260 0.2982 0.0373  -0.0229 -0.0097 513 HIS B CA  
3419 C C   . HIS B 221 ? 0.2779 0.3516 0.3275 0.0399  -0.0098 -0.0178 513 HIS B C   
3420 O O   . HIS B 221 ? 0.2247 0.2838 0.2682 0.0342  -0.0159 -0.0234 513 HIS B O   
3421 C CB  . HIS B 221 ? 0.3521 0.4172 0.3659 0.0337  -0.0259 -0.0103 513 HIS B CB  
3422 C CG  . HIS B 221 ? 0.4114 0.4502 0.3864 0.0258  -0.0324 -0.0196 513 HIS B CG  
3423 N ND1 . HIS B 221 ? 0.4927 0.5214 0.4614 0.0153  -0.0571 -0.0189 513 HIS B ND1 
3424 C CD2 . HIS B 221 ? 0.3205 0.3390 0.2608 0.0266  -0.0172 -0.0309 513 HIS B CD2 
3425 C CE1 . HIS B 221 ? 0.4033 0.4017 0.3269 0.0087  -0.0586 -0.0309 513 HIS B CE1 
3426 N NE2 . HIS B 221 ? 0.4317 0.4228 0.3369 0.0166  -0.0320 -0.0392 513 HIS B NE2 
3427 N N   . ILE B 222 ? 0.2241 0.3054 0.2793 0.0480  0.0055  -0.0176 514 ILE B N   
3428 C CA  . ILE B 222 ? 0.2832 0.3578 0.3415 0.0526  0.0155  -0.0222 514 ILE B CA  
3429 C C   . ILE B 222 ? 0.2145 0.2928 0.2948 0.0508  0.0121  -0.0178 514 ILE B C   
3430 O O   . ILE B 222 ? 0.2182 0.2815 0.2985 0.0496  0.0126  -0.0211 514 ILE B O   
3431 C CB  . ILE B 222 ? 0.3007 0.3861 0.3663 0.0608  0.0278  -0.0202 514 ILE B CB  
3432 C CG1 . ILE B 222 ? 0.2583 0.3390 0.3043 0.0611  0.0364  -0.0239 514 ILE B CG1 
3433 C CG2 . ILE B 222 ? 0.2610 0.3426 0.3397 0.0674  0.0340  -0.0208 514 ILE B CG2 
3434 C CD1 . ILE B 222 ? 0.2778 0.3753 0.3405 0.0658  0.0460  -0.0191 514 ILE B CD1 
3435 N N   . ARG B 223 ? 0.2322 0.3277 0.3307 0.0504  0.0107  -0.0103 515 ARG B N   
3436 C CA  . ARG B 223 ? 0.1916 0.2917 0.3098 0.0467  0.0113  -0.0047 515 ARG B CA  
3437 C C   . ARG B 223 ? 0.2480 0.3405 0.3743 0.0365  -0.0003 -0.0061 515 ARG B C   
3438 O O   . ARG B 223 ? 0.2285 0.3130 0.3647 0.0311  0.0000  -0.0039 515 ARG B O   
3439 C CB  . ARG B 223 ? 0.2016 0.3201 0.3355 0.0489  0.0164  0.0011  515 ARG B CB  
3440 C CG  . ARG B 223 ? 0.1841 0.3090 0.3366 0.0451  0.0240  0.0080  515 ARG B CG  
3441 C CD  . ARG B 223 ? 0.2963 0.4118 0.4337 0.0474  0.0321  0.0121  515 ARG B CD  
3442 N NE  . ARG B 223 ? 0.4019 0.5208 0.5235 0.0541  0.0371  0.0114  515 ARG B NE  
3443 C CZ  . ARG B 223 ? 0.4878 0.6113 0.6045 0.0549  0.0476  0.0143  515 ARG B CZ  
3444 N NH1 . ARG B 223 ? 0.3270 0.4558 0.4568 0.0504  0.0587  0.0200  515 ARG B NH1 
3445 N NH2 . ARG B 223 ? 0.4029 0.5242 0.5005 0.0595  0.0481  0.0108  515 ARG B NH2 
3446 N N   . HIS B 224 ? 0.2271 0.3201 0.3491 0.0322  -0.0132 -0.0083 516 HIS B N   
3447 C CA  . HIS B 224 ? 0.1813 0.2656 0.3089 0.0202  -0.0309 -0.0097 516 HIS B CA  
3448 C C   . HIS B 224 ? 0.2684 0.3219 0.3694 0.0158  -0.0327 -0.0202 516 HIS B C   
3449 O O   . HIS B 224 ? 0.2830 0.3260 0.3964 0.0054  -0.0414 -0.0207 516 HIS B O   
3450 C CB  . HIS B 224 ? 0.2704 0.3562 0.3891 0.0169  -0.0484 -0.0088 516 HIS B CB  
3451 C CG  . HIS B 224 ? 0.2953 0.3728 0.4195 0.0026  -0.0736 -0.0089 516 HIS B CG  
3452 N ND1 . HIS B 224 ? 0.3790 0.4789 0.5544 -0.0041 -0.0843 0.0007  516 HIS B ND1 
3453 C CD2 . HIS B 224 ? 0.3642 0.4126 0.4489 -0.0073 -0.0910 -0.0178 516 HIS B CD2 
3454 C CE1 . HIS B 224 ? 0.3300 0.4171 0.5023 -0.0187 -0.1115 -0.0009 516 HIS B CE1 
3455 N NE2 . HIS B 224 ? 0.3875 0.4402 0.4993 -0.0213 -0.1169 -0.0131 516 HIS B NE2 
3456 N N   . MET B 225 ? 0.2667 0.3045 0.3343 0.0234  -0.0229 -0.0290 517 MET B N   
3457 C CA  . MET B 225 ? 0.3130 0.3185 0.3560 0.0229  -0.0196 -0.0415 517 MET B CA  
3458 C C   . MET B 225 ? 0.3005 0.3018 0.3665 0.0262  -0.0110 -0.0377 517 MET B C   
3459 O O   . MET B 225 ? 0.3429 0.3169 0.4046 0.0204  -0.0156 -0.0444 517 MET B O   
3460 C CB  . MET B 225 ? 0.3116 0.3072 0.3228 0.0329  -0.0046 -0.0502 517 MET B CB  
3461 C CG  . MET B 225 ? 0.3379 0.3257 0.3124 0.0271  -0.0124 -0.0541 517 MET B CG  
3462 S SD  . MET B 225 ? 0.4439 0.4133 0.3772 0.0362  0.0120  -0.0661 517 MET B SD  
3463 C CE  . MET B 225 ? 0.3514 0.3581 0.3245 0.0493  0.0292  -0.0536 517 MET B CE  
3464 N N   . SER B 226 ? 0.2725 0.2963 0.3592 0.0345  -0.0002 -0.0267 518 SER B N   
3465 C CA  . SER B 226 ? 0.2804 0.2985 0.3835 0.0369  0.0059  -0.0191 518 SER B CA  
3466 C C   . SER B 226 ? 0.2901 0.3071 0.4145 0.0231  -0.0018 -0.0115 518 SER B C   
3467 O O   . SER B 226 ? 0.3106 0.3054 0.4403 0.0192  -0.0023 -0.0097 518 SER B O   
3468 C CB  . SER B 226 ? 0.2421 0.2823 0.3538 0.0461  0.0152  -0.0084 518 SER B CB  
3469 O OG  . SER B 226 ? 0.6302 0.6614 0.7505 0.0481  0.0185  0.0014  518 SER B OG  
3470 N N   . ASN B 227 ? 0.2904 0.3311 0.4324 0.0158  -0.0071 -0.0058 519 ASN B N   
3471 C CA  . ASN B 227 ? 0.2864 0.3324 0.4592 0.0015  -0.0129 0.0027  519 ASN B CA  
3472 C C   . ASN B 227 ? 0.3075 0.3251 0.4751 -0.0116 -0.0306 -0.0068 519 ASN B C   
3473 O O   . ASN B 227 ? 0.3397 0.3418 0.5230 -0.0222 -0.0330 -0.0023 519 ASN B O   
3474 C CB  . ASN B 227 ? 0.2936 0.3736 0.4947 -0.0012 -0.0145 0.0097  519 ASN B CB  
3475 C CG  . ASN B 227 ? 0.3845 0.4862 0.5885 0.0100  0.0046  0.0170  519 ASN B CG  
3476 O OD1 . ASN B 227 ? 0.3764 0.4728 0.5725 0.0131  0.0180  0.0235  519 ASN B OD1 
3477 N ND2 . ASN B 227 ? 0.2999 0.4221 0.5120 0.0156  0.0042  0.0163  519 ASN B ND2 
3478 N N   . LYS B 228 ? 0.3121 0.3183 0.4531 -0.0126 -0.0439 -0.0199 520 LYS B N   
3479 C CA  . LYS B 228 ? 0.3902 0.3609 0.5121 -0.0255 -0.0622 -0.0327 520 LYS B CA  
3480 C C   . LYS B 228 ? 0.3998 0.3310 0.4977 -0.0193 -0.0520 -0.0436 520 LYS B C   
3481 O O   . LYS B 228 ? 0.4753 0.3730 0.5698 -0.0313 -0.0632 -0.0511 520 LYS B O   
3482 C CB  . LYS B 228 ? 0.3814 0.3444 0.4673 -0.0278 -0.0777 -0.0437 520 LYS B CB  
3483 C CG  . LYS B 228 ? 0.3911 0.3901 0.5044 -0.0323 -0.0916 -0.0317 520 LYS B CG  
3484 C CD  . LYS B 228 ? 0.4787 0.4736 0.6109 -0.0531 -0.1231 -0.0304 520 LYS B CD  
3485 C CE  . LYS B 228 ? 0.5012 0.5409 0.6869 -0.0552 -0.1335 -0.0134 520 LYS B CE  
3486 N NZ  . LYS B 228 ? 0.5658 0.6144 0.7995 -0.0757 -0.1590 -0.0062 520 LYS B NZ  
3487 N N   . GLY B 229 ? 0.3962 0.3300 0.4819 -0.0008 -0.0321 -0.0444 521 GLY B N   
3488 C CA  . GLY B 229 ? 0.4150 0.3155 0.4905 0.0085  -0.0214 -0.0518 521 GLY B CA  
3489 C C   . GLY B 229 ? 0.4214 0.3135 0.5269 0.0027  -0.0216 -0.0381 521 GLY B C   
3490 O O   . GLY B 229 ? 0.5615 0.4140 0.6636 -0.0025 -0.0264 -0.0454 521 GLY B O   
3491 N N   . MET B 230 ? 0.3975 0.3227 0.5291 0.0030  -0.0153 -0.0181 522 MET B N   
3492 C CA  . MET B 230 ? 0.4632 0.3820 0.6195 -0.0055 -0.0137 -0.0012 522 MET B CA  
3493 C C   . MET B 230 ? 0.5888 0.4926 0.7621 -0.0278 -0.0288 -0.0024 522 MET B C   
3494 O O   . MET B 230 ? 0.6273 0.4992 0.8093 -0.0362 -0.0320 0.0015  522 MET B O   
3495 C CB  . MET B 230 ? 0.3387 0.2959 0.5108 -0.0041 -0.0025 0.0182  522 MET B CB  
3496 C CG  . MET B 230 ? 0.3816 0.3496 0.5382 0.0143  0.0080  0.0219  522 MET B CG  
3497 S SD  . MET B 230 ? 0.5363 0.4717 0.6895 0.0241  0.0102  0.0317  522 MET B SD  
3498 C CE  . MET B 230 ? 0.3778 0.3415 0.5216 0.0347  0.0176  0.0471  522 MET B CE  
3499 N N   . GLU B 231 ? 0.5363 0.4621 0.7179 -0.0385 -0.0408 -0.0063 523 GLU B N   
3500 C CA  . GLU B 231 ? 0.4620 0.3773 0.6650 -0.0617 -0.0610 -0.0075 523 GLU B CA  
3501 C C   . GLU B 231 ? 0.6215 0.4816 0.7923 -0.0671 -0.0755 -0.0287 523 GLU B C   
3502 O O   . GLU B 231 ? 0.7414 0.5768 0.9280 -0.0871 -0.0912 -0.0292 523 GLU B O   
3503 C CB  . GLU B 231 ? 0.4659 0.4173 0.6853 -0.0688 -0.0748 -0.0070 523 GLU B CB  
3504 C CG  . GLU B 231 ? 0.6821 0.6212 0.9162 -0.0924 -0.1050 -0.0126 523 GLU B CG  
3505 C CD  . GLU B 231 ? 0.7070 0.6837 0.9612 -0.0965 -0.1215 -0.0089 523 GLU B CD  
3506 O OE1 . GLU B 231 ? 0.9796 0.9388 1.2181 -0.1098 -0.1516 -0.0198 523 GLU B OE1 
3507 O OE2 . GLU B 231 ? 0.6036 0.6241 0.8873 -0.0863 -0.1056 0.0047  523 GLU B OE2 
3508 N N   . HIS B 232 ? 0.6350 0.4732 0.7612 -0.0502 -0.0686 -0.0468 524 HIS B N   
3509 C CA  . HIS B 232 ? 0.7711 0.5522 0.8591 -0.0518 -0.0759 -0.0707 524 HIS B CA  
3510 C C   . HIS B 232 ? 0.8506 0.5960 0.9420 -0.0405 -0.0614 -0.0705 524 HIS B C   
3511 O O   . HIS B 232 ? 0.8870 0.5875 0.9795 -0.0526 -0.0717 -0.0772 524 HIS B O   
3512 C CB  . HIS B 232 ? 0.6891 0.4635 0.7267 -0.0391 -0.0710 -0.0905 524 HIS B CB  
3513 C CG  . HIS B 232 ? 0.8245 0.5375 0.8133 -0.0391 -0.0729 -0.1185 524 HIS B CG  
3514 N ND1 . HIS B 232 ? 0.7516 0.4390 0.7195 -0.0169 -0.0482 -0.1316 524 HIS B ND1 
3515 C CD2 . HIS B 232 ? 0.8658 0.5359 0.8216 -0.0584 -0.0960 -0.1370 524 HIS B CD2 
3516 C CE1 . HIS B 232 ? 0.9954 0.6249 0.9174 -0.0209 -0.0517 -0.1586 524 HIS B CE1 
3517 N NE2 . HIS B 232 ? 0.9938 0.6092 0.9026 -0.0471 -0.0821 -0.1631 524 HIS B NE2 
3518 N N   . LEU B 233 ? 0.8346 0.5980 0.9306 -0.0179 -0.0404 -0.0618 525 LEU B N   
3519 C CA  . LEU B 233 ? 0.9151 0.6462 1.0185 -0.0040 -0.0292 -0.0594 525 LEU B CA  
3520 C C   . LEU B 233 ? 1.0098 0.7280 1.1454 -0.0190 -0.0362 -0.0388 525 LEU B C   
3521 O O   . LEU B 233 ? 1.0645 0.7343 1.2024 -0.0179 -0.0375 -0.0421 525 LEU B O   
3522 C CB  . LEU B 233 ? 0.7132 0.4746 0.8235 0.0202  -0.0112 -0.0489 525 LEU B CB  
3523 C CG  . LEU B 233 ? 0.6913 0.4728 0.7778 0.0347  -0.0005 -0.0637 525 LEU B CG  
3524 C CD1 . LEU B 233 ? 0.6216 0.4350 0.7262 0.0544  0.0127  -0.0494 525 LEU B CD1 
3525 C CD2 . LEU B 233 ? 0.7668 0.5026 0.8216 0.0421  0.0060  -0.0922 525 LEU B CD2 
3526 N N   . TYR B 234 ? 1.1854 1.4560 0.7567 0.2204  -0.4781 -0.2080 526 TYR B N   
3527 C CA  . TYR B 234 ? 1.1376 1.4557 0.8196 0.1570  -0.5141 -0.2076 526 TYR B CA  
3528 C C   . TYR B 234 ? 1.1984 1.5950 0.9329 0.1130  -0.5816 -0.2025 526 TYR B C   
3529 O O   . TYR B 234 ? 1.3243 1.7804 1.1665 0.0565  -0.6097 -0.1908 526 TYR B O   
3530 C CB  . TYR B 234 ? 1.0233 1.4069 0.7935 0.1679  -0.4741 -0.1663 526 TYR B CB  
3531 C CG  . TYR B 234 ? 0.9545 1.2489 0.6990 0.1776  -0.4095 -0.1698 526 TYR B CG  
3532 C CD1 . TYR B 234 ? 1.0563 1.2891 0.7017 0.2294  -0.3613 -0.1691 526 TYR B CD1 
3533 C CD2 . TYR B 234 ? 1.1327 1.4039 0.9558 0.1312  -0.3931 -0.1691 526 TYR B CD2 
3534 C CE1 . TYR B 234 ? 1.0035 1.1662 0.6383 0.2306  -0.3026 -0.1656 526 TYR B CE1 
3535 C CE2 . TYR B 234 ? 1.1567 1.3517 0.9605 0.1375  -0.3347 -0.1684 526 TYR B CE2 
3536 C CZ  . TYR B 234 ? 1.1141 1.2604 0.8279 0.1850  -0.2920 -0.1661 526 TYR B CZ  
3537 O OH  . TYR B 234 ? 1.0176 1.1036 0.7231 0.1865  -0.2388 -0.1609 526 TYR B OH  
3538 N N   . SER B 235 ? 1.2948 1.6962 0.9584 0.1357  -0.6069 -0.2073 527 SER B N   
3539 C CA  . SER B 235 ? 1.3937 1.8353 1.0728 0.0834  -0.6802 -0.2175 527 SER B CA  
3540 C C   . SER B 235 ? 1.5260 1.8497 1.1201 0.0501  -0.7056 -0.2734 527 SER B C   
3541 O O   . SER B 235 ? 1.5986 1.9424 1.2045 -0.0071 -0.7649 -0.2893 527 SER B O   
3542 C CB  . SER B 235 ? 1.4593 1.9581 1.0973 0.1231  -0.7003 -0.1975 527 SER B CB  
3543 O OG  . SER B 235 ? 1.5727 2.1055 1.2107 0.0702  -0.7760 -0.2102 527 SER B OG  
3544 N N   . VAL B 241 ? 0.9677 0.8637 1.0033 -0.0997 -0.3284 -0.2523 533 VAL B N   
3545 C CA  . VAL B 241 ? 0.8525 0.7491 0.9772 -0.1344 -0.3093 -0.2317 533 VAL B CA  
3546 C C   . VAL B 241 ? 0.7889 0.6998 0.9370 -0.1023 -0.2464 -0.1953 533 VAL B C   
3547 O O   . VAL B 241 ? 0.9311 0.9044 1.1549 -0.1068 -0.2283 -0.1556 533 VAL B O   
3548 C CB  . VAL B 241 ? 1.0510 0.8450 1.1375 -0.1596 -0.3110 -0.2614 533 VAL B CB  
3549 C CG1 . VAL B 241 ? 0.9645 0.7724 1.1396 -0.1982 -0.2911 -0.2329 533 VAL B CG1 
3550 C CG2 . VAL B 241 ? 0.9668 0.7273 0.9833 -0.1776 -0.3530 -0.2925 533 VAL B CG2 
3551 N N   . VAL B 242 ? 0.7129 0.5644 0.7918 -0.0692 -0.2139 -0.2068 534 VAL B N   
3552 C CA  . VAL B 242 ? 0.7456 0.6050 0.8347 -0.0434 -0.1619 -0.1753 534 VAL B CA  
3553 C C   . VAL B 242 ? 0.7161 0.6381 0.7974 -0.0168 -0.1521 -0.1484 534 VAL B C   
3554 O O   . VAL B 242 ? 0.6439 0.5719 0.6640 0.0067  -0.1647 -0.1621 534 VAL B O   
3555 C CB  . VAL B 242 ? 0.8554 0.6516 0.8803 -0.0173 -0.1345 -0.1905 534 VAL B CB  
3556 C CG1 . VAL B 242 ? 0.7703 0.5726 0.8207 -0.0065 -0.0902 -0.1580 534 VAL B CG1 
3557 C CG2 . VAL B 242 ? 0.7949 0.5149 0.7976 -0.0335 -0.1491 -0.2235 534 VAL B CG2 
3558 N N   . PRO B 243 ? 0.6124 0.5716 0.7419 -0.0146 -0.1273 -0.1094 535 PRO B N   
3559 C CA  . PRO B 243 ? 0.6177 0.6211 0.7261 0.0144  -0.1149 -0.0823 535 PRO B CA  
3560 C C   . PRO B 243 ? 0.6007 0.5695 0.6370 0.0426  -0.0857 -0.0814 535 PRO B C   
3561 O O   . PRO B 243 ? 0.5420 0.4671 0.5658 0.0399  -0.0646 -0.0863 535 PRO B O   
3562 C CB  . PRO B 243 ? 0.5876 0.6131 0.7513 0.0127  -0.0893 -0.0408 535 PRO B CB  
3563 C CG  . PRO B 243 ? 0.6736 0.6527 0.8705 -0.0103 -0.0761 -0.0453 535 PRO B CG  
3564 C CD  . PRO B 243 ? 0.4822 0.4305 0.6727 -0.0325 -0.1053 -0.0874 535 PRO B CD  
3565 N N   . LEU B 244 ? 0.6023 0.5969 0.5938 0.0701  -0.0843 -0.0713 536 LEU B N   
3566 C CA  . LEU B 244 ? 0.5969 0.5640 0.5219 0.0942  -0.0563 -0.0661 536 LEU B CA  
3567 C C   . LEU B 244 ? 0.5650 0.5010 0.4937 0.0881  -0.0184 -0.0375 536 LEU B C   
3568 O O   . LEU B 244 ? 0.5669 0.4771 0.4659 0.0902  0.0019  -0.0360 536 LEU B O   
3569 C CB  . LEU B 244 ? 0.5936 0.5896 0.4689 0.1258  -0.0587 -0.0552 536 LEU B CB  
3570 C CG  . LEU B 244 ? 0.6152 0.5853 0.4190 0.1512  -0.0289 -0.0463 536 LEU B CG  
3571 C CD1 . LEU B 244 ? 0.6114 0.5603 0.3828 0.1577  -0.0337 -0.0756 536 LEU B CD1 
3572 C CD2 . LEU B 244 ? 0.6095 0.6035 0.3635 0.1852  -0.0284 -0.0310 536 LEU B CD2 
3573 N N   . SER B 245 ? 0.6145 0.5530 0.5771 0.0812  -0.0093 -0.0125 537 SER B N   
3574 C CA  . SER B 245 ? 0.6238 0.5171 0.5735 0.0751  0.0213  0.0127  537 SER B CA  
3575 C C   . SER B 245 ? 0.4929 0.3582 0.4655 0.0530  0.0243  -0.0008 537 SER B C   
3576 O O   . SER B 245 ? 0.5207 0.3567 0.4675 0.0468  0.0420  0.0104  537 SER B O   
3577 C CB  . SER B 245 ? 0.5272 0.4196 0.4987 0.0801  0.0313  0.0414  537 SER B CB  
3578 O OG  . SER B 245 ? 0.5533 0.4732 0.5968 0.0642  0.0148  0.0332  537 SER B OG  
3579 N N   . ASP B 246 ? 0.4413 0.3153 0.4617 0.0397  0.0061  -0.0226 538 ASP B N   
3580 C CA  . ASP B 246 ? 0.5236 0.3697 0.5587 0.0269  0.0106  -0.0354 538 ASP B CA  
3581 C C   . ASP B 246 ? 0.4986 0.3451 0.4958 0.0385  0.0157  -0.0476 538 ASP B C   
3582 O O   . ASP B 246 ? 0.4316 0.2662 0.4277 0.0349  0.0310  -0.0391 538 ASP B O   
3583 C CB  . ASP B 246 ? 0.4264 0.2701 0.5072 0.0122  -0.0089 -0.0574 538 ASP B CB  
3584 C CG  . ASP B 246 ? 0.4875 0.3283 0.6177 -0.0004 -0.0029 -0.0369 538 ASP B CG  
3585 O OD1 . ASP B 246 ? 0.3985 0.2310 0.5169 0.0078  0.0170  -0.0073 538 ASP B OD1 
3586 O OD2 . ASP B 246 ? 0.6478 0.4876 0.8224 -0.0176 -0.0166 -0.0487 538 ASP B OD2 
3587 N N   . LEU B 247 ? 0.4733 0.3379 0.4387 0.0552  0.0032  -0.0642 539 LEU B N   
3588 C CA  . LEU B 247 ? 0.5368 0.4024 0.4605 0.0750  0.0142  -0.0709 539 LEU B CA  
3589 C C   . LEU B 247 ? 0.5229 0.3983 0.4241 0.0779  0.0404  -0.0388 539 LEU B C   
3590 O O   . LEU B 247 ? 0.5364 0.4198 0.4325 0.0819  0.0584  -0.0283 539 LEU B O   
3591 C CB  . LEU B 247 ? 0.5355 0.4063 0.4166 0.0964  -0.0066 -0.0969 539 LEU B CB  
3592 C CG  . LEU B 247 ? 0.8047 0.6548 0.6416 0.1211  -0.0029 -0.1183 539 LEU B CG  
3593 C CD1 . LEU B 247 ? 0.7823 0.6053 0.6469 0.1122  0.0040  -0.1255 539 LEU B CD1 
3594 C CD2 . LEU B 247 ? 0.8712 0.7037 0.6607 0.1345  -0.0363 -0.1529 539 LEU B CD2 
3595 N N   . LEU B 248 ? 0.5307 0.4054 0.4172 0.0759  0.0439  -0.0195 540 LEU B N   
3596 C CA  . LEU B 248 ? 0.5146 0.3796 0.3700 0.0715  0.0677  0.0114  540 LEU B CA  
3597 C C   . LEU B 248 ? 0.5328 0.3767 0.4124 0.0425  0.0764  0.0292  540 LEU B C   
3598 O O   . LEU B 248 ? 0.5891 0.4376 0.4601 0.0302  0.0904  0.0492  540 LEU B O   
3599 C CB  . LEU B 248 ? 0.5054 0.3565 0.3250 0.0811  0.0712  0.0279  540 LEU B CB  
3600 C CG  . LEU B 248 ? 0.5402 0.4174 0.3265 0.1128  0.0620  0.0169  540 LEU B CG  
3601 C CD1 . LEU B 248 ? 0.5930 0.4587 0.3460 0.1276  0.0690  0.0394  540 LEU B CD1 
3602 C CD2 . LEU B 248 ? 0.5359 0.4223 0.2813 0.1304  0.0767  0.0176  540 LEU B CD2 
3603 N N   . LEU B 249 ? 0.5237 0.3472 0.4343 0.0305  0.0670  0.0248  541 LEU B N   
3604 C CA  . LEU B 249 ? 0.4513 0.2495 0.3771 0.0067  0.0708  0.0389  541 LEU B CA  
3605 C C   . LEU B 249 ? 0.5918 0.4214 0.5465 0.0039  0.0721  0.0342  541 LEU B C   
3606 O O   . LEU B 249 ? 0.6966 0.5313 0.6536 -0.0151 0.0773  0.0553  541 LEU B O   
3607 C CB  . LEU B 249 ? 0.6282 0.3993 0.5794 0.0035  0.0640  0.0346  541 LEU B CB  
3608 C CG  . LEU B 249 ? 0.5712 0.3137 0.4945 0.0032  0.0666  0.0528  541 LEU B CG  
3609 C CD1 . LEU B 249 ? 0.4147 0.1735 0.3766 0.0046  0.0547  0.0463  541 LEU B CD1 
3610 C CD2 . LEU B 249 ? 0.5037 0.2513 0.4047 -0.0140 0.0592  0.0630  541 LEU B CD2 
3611 N N   . GLU B 250 ? 0.5606 0.4100 0.5336 0.0234  0.0665  0.0085  542 GLU B N   
3612 C CA  . GLU B 250 ? 0.5602 0.4352 0.5510 0.0332  0.0733  0.0063  542 GLU B CA  
3613 C C   . GLU B 250 ? 0.5392 0.4559 0.5147 0.0412  0.0902  0.0275  542 GLU B C   
3614 O O   . GLU B 250 ? 0.5949 0.5468 0.5949 0.0378  0.1001  0.0478  542 GLU B O   
3615 C CB  . GLU B 250 ? 0.5091 0.3733 0.4988 0.0561  0.0651  -0.0274 542 GLU B CB  
3616 C CG  . GLU B 250 ? 0.6696 0.5439 0.6671 0.0757  0.0761  -0.0297 542 GLU B CG  
3617 C CD  . GLU B 250 ? 0.7485 0.5878 0.7191 0.1000  0.0684  -0.0651 542 GLU B CD  
3618 O OE1 . GLU B 250 ? 0.8440 0.6511 0.8128 0.0871  0.0472  -0.0885 542 GLU B OE1 
3619 O OE2 . GLU B 250 ? 0.7588 0.6009 0.7067 0.1320  0.0832  -0.0673 542 GLU B OE2 
3620 N N   . MET B 251 ? 0.5572 0.4765 0.4954 0.0532  0.0949  0.0275  543 MET B N   
3621 C CA  . MET B 251 ? 0.5305 0.4873 0.4528 0.0620  0.1162  0.0523  543 MET B CA  
3622 C C   . MET B 251 ? 0.5674 0.5317 0.5035 0.0226  0.1226  0.0900  543 MET B C   
3623 O O   . MET B 251 ? 0.4928 0.5046 0.4441 0.0180  0.1395  0.1193  543 MET B O   
3624 C CB  . MET B 251 ? 0.5513 0.4991 0.4214 0.0859  0.1198  0.0443  543 MET B CB  
3625 C CG  . MET B 251 ? 0.5097 0.4535 0.3519 0.1257  0.1119  0.0102  543 MET B CG  
3626 S SD  . MET B 251 ? 0.7124 0.6455 0.4878 0.1536  0.1078  0.0002  543 MET B SD  
3627 C CE  . MET B 251 ? 0.6266 0.5334 0.3811 0.1749  0.0736  -0.0505 543 MET B CE  
3628 N N   . LEU B 252 ? 0.5950 0.5102 0.5223 -0.0064 0.1093  0.0921  544 LEU B N   
3629 C CA  . LEU B 252 ? 0.5680 0.4648 0.4889 -0.0489 0.1084  0.1233  544 LEU B CA  
3630 C C   . LEU B 252 ? 0.6079 0.5386 0.5786 -0.0725 0.0991  0.1374  544 LEU B C   
3631 O O   . LEU B 252 ? 0.5865 0.5191 0.5589 -0.1131 0.0940  0.1667  544 LEU B O   
3632 C CB  . LEU B 252 ? 0.5234 0.3402 0.3996 -0.0620 0.0990  0.1197  544 LEU B CB  
3633 C CG  . LEU B 252 ? 0.6362 0.4230 0.4572 -0.0440 0.1086  0.1196  544 LEU B CG  
3634 C CD1 . LEU B 252 ? 0.7453 0.4961 0.5541 -0.0312 0.0942  0.1025  544 LEU B CD1 
3635 C CD2 . LEU B 252 ? 0.6610 0.4569 0.4711 -0.0653 0.1038  0.1382  544 LEU B CD2 
3636 N N   . ASP B 253 ? 0.4758 0.4309 0.4832 -0.0493 0.0952  0.1188  545 ASP B N   
3637 C CA  . ASP B 253 ? 0.5928 0.5849 0.6458 -0.0628 0.0871  0.1334  545 ASP B CA  
3638 C C   . ASP B 253 ? 0.4602 0.5446 0.5544 -0.0559 0.1026  0.1632  545 ASP B C   
3639 O O   . ASP B 253 ? 0.4336 0.5676 0.5723 -0.0697 0.0949  0.1852  545 ASP B O   
3640 C CB  . ASP B 253 ? 0.4406 0.4154 0.5098 -0.0355 0.0821  0.1050  545 ASP B CB  
3641 N N   . ALA B 254 ? 0.3932 0.5067 0.4739 -0.0311 0.1252  0.1680  546 ALA B N   
3642 C CA  . ALA B 254 ? 0.4890 0.6954 0.6087 -0.0166 0.1480  0.2033  546 ALA B CA  
3643 C C   . ALA B 254 ? 0.6414 0.8774 0.7712 -0.0636 0.1518  0.2459  546 ALA B C   
3644 O O   . ALA B 254 ? 0.7469 0.9869 0.8999 -0.1095 0.1252  0.2578  546 ALA B O   
3645 C CB  . ALA B 254 ? 0.4173 0.6324 0.5067 0.0442  0.1745  0.1873  546 ALA B CB  
3646 N N   . HIS C .   ? 0.6203 1.4948 1.3906 0.1981  0.2928  -0.3084 601 HIS A N   
3647 C CA  . HIS C .   ? 0.6381 1.5016 1.4739 0.2014  0.3142  -0.3079 601 HIS A CA  
3648 C C   . HIS C .   ? 0.6540 1.5077 1.5144 0.1965  0.3284  -0.3188 601 HIS A C   
3649 O O   . HIS C .   ? 0.7167 1.5590 1.5309 0.1843  0.3529  -0.3370 601 HIS A O   
3650 C CB  . HIS C .   ? 0.6696 1.5133 1.4782 0.2017  0.3463  -0.3122 601 HIS A CB  
3651 C CG  . HIS C .   ? 0.6653 1.5027 1.4703 0.2106  0.3457  -0.2976 601 HIS A CG  
3652 N ND1 . HIS C .   ? 0.6385 1.4922 1.4869 0.2117  0.3233  -0.2848 601 HIS A ND1 
3653 C CD2 . HIS C .   ? 0.6899 1.5038 1.4474 0.2177  0.3691  -0.2934 601 HIS A CD2 
3654 C CE1 . HIS C .   ? 0.6476 1.4864 1.4731 0.2157  0.3370  -0.2768 601 HIS A CE1 
3655 N NE2 . HIS C .   ? 0.6797 1.4893 1.4482 0.2230  0.3650  -0.2795 601 HIS A NE2 
# 
