data_9G4M
# 
_entry.id   9G4M 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.404 
_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   9G4M         pdb_00009g4m 10.2210/pdb9g4m/pdb 
WWPDB D_1292140326 ?            ?                   
# 
_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       2025-06-11 
_pdbx_audit_revision_history.part_number         ? 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        9G4M 
_pdbx_database_status.recvd_initial_deposition_date   2024-07-15 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBE 
_pdbx_database_status.process_site                    PDBE 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           N 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              joerg.benz@roche.com 
_pdbx_contact_author.name_first         Joerg 
_pdbx_contact_author.name_last          Benz 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-4189-6873 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Guberman, M.'      1  ? 
'Hentsch, A.'       2  ? 
'Radetzki, S.'      3  ? 
'Kaushik, S.'       4  ? 
'Huizenga, M.'      5  ? 
'van der Stelt, M.' 6  ? 
'Paul, J.'          7  ? 
'Schippers, M.'     8  ? 
'Hochstrasser, R.'  9  ? 
'von Kries, J.P.'   10 ? 
'Blaising, J.'      11 ? 
'Lipstein, N.'      12 ? 
'Nazare, M.'        13 ? 
'Grether, U.'       14 ? 
'Kuhn, B.'          15 ? 
'Walter, A.'        16 ? 
'Benz, J.'          17 ? 
# 
_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                   GE 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            Angew.Chem.Int.Ed.Engl. 
_citation.journal_id_ASTM           ACIEAY 
_citation.journal_id_CSD            0179 
_citation.journal_id_ISSN           1521-3773 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            64 
_citation.language                  ? 
_citation.page_first                e202413405 
_citation.page_last                 e202413405 
_citation.title                     'A Highly Selective and Versatile Probe Platform for Visualization of Monoacylglycerol Lipase.' 
_citation.year                      2025 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1002/anie.202413405 
_citation.pdbx_database_id_PubMed   39916545 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Hentsch, A.'        1  0000-0001-6968-1199 
primary 'Guberman, M.'       2  0000-0002-2407-4771 
primary 'Radetzki, S.'       3  0000-0003-2688-2868 
primary 'Kaushik, S.'        4  0000-0002-5757-764X 
primary 'Huizenga, M.'       5  ?                   
primary 'Paul, J.'           6  ?                   
primary 'Schippers, M.'      7  ?                   
primary 'Benz, J.'           8  ?                   
primary 'Kuhn, B.'           9  0000-0002-4301-562X 
primary 'Heer, D.'           10 0009-0003-2089-4339 
primary 'Topp, A.'           11 0009-0002-5511-2870 
primary 'Esteves Gloria, L.' 12 ?                   
primary 'Walter, A.'         13 ?                   
primary 'Hochstrasser, R.'   14 ?                   
primary 'Wittwer, M.B.'      15 0000-0003-1359-4795 
primary 'von Kries, J.P.'    16 ?                   
primary 'Collin, L.'         17 ?                   
primary 'Blaising, J.'       18 0000-0002-3367-6184 
primary 'van der Stelt, M.'  19 ?                   
primary 'Lipstein, N.'       20 0000-0002-0755-5899 
primary 'Grether, U.'        21 0000-0002-3164-9270 
primary 'Nazare, M.'         22 0000-0002-1602-2330 
# 
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 'Monoglyceride lipase' 35465.512 1   3.1.1.23 ? ? ? 
2 non-polymer syn 
;3-[2,2-bis(fluoranyl)-10,12-dimethyl-1$l^{4},3-diaza-2$l^{4}-boratricyclo[7.3.0.0^{3,7}]dodeca-1(12),4,6,8,10-pentaen-4-yl]-~{N}-[2-[2-[[2-[(6-oxidanylidene-7-oxa-2,5-diazaspiro[3.4]octan-2-yl)carbonyl]-2-azaspiro[3.3]heptan-6-yl]methyl]phenoxy]ethyl]propanamide
;
674.545   1   ?        ? ? ? 
3 non-polymer syn 1,2-ETHANEDIOL 62.068    8   ?        ? ? ? 
4 water       nat water 18.015    210 ?        ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'MGL,HU-K5,Lysophospholipase homolog,Lysophospholipase-like,Monoacylglycerol lipase,MAGL' 
# 
_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       
;MGSSHHHHHHSSGENLYFQGMPEESSPRRTPQSIPYQDLPHLVNADGQYLFCRYWAPTGTPKALIFVSHGAGEHSGRYEE
LARMLMGLDLLVFAHDHVGHGQSEGERMVVSDFHVFVRDVLQHVDSMQKDYPGLPVFLLGHSMGGAIAILTAAERPGHFA
GMVLISPLVLANPESATTFKVLAAKVLNSVLPNLSSGPIDSSVLSRNKTEVDIYNSDPLICRAGLKVCFGIQLLNAVSRV
ERALPKLTVPFLLLQGSADRLCDSKGAYLLMELAKSQDKTLKIYEGAYHVLHKELPEVTNSVFHEINMWVSQRTATAGTA
SPP
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MGSSHHHHHHSSGENLYFQGMPEESSPRRTPQSIPYQDLPHLVNADGQYLFCRYWAPTGTPKALIFVSHGAGEHSGRYEE
LARMLMGLDLLVFAHDHVGHGQSEGERMVVSDFHVFVRDVLQHVDSMQKDYPGLPVFLLGHSMGGAIAILTAAERPGHFA
GMVLISPLVLANPESATTFKVLAAKVLNSVLPNLSSGPIDSSVLSRNKTEVDIYNSDPLICRAGLKVCFGIQLLNAVSRV
ERALPKLTVPFLLLQGSADRLCDSKGAYLLMELAKSQDKTLKIYEGAYHVLHKELPEVTNSVFHEINMWVSQRTATAGTA
SPP
;
_entity_poly.pdbx_strand_id                 A 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 
;3-[2,2-bis(fluoranyl)-10,12-dimethyl-1$l^{4},3-diaza-2$l^{4}-boratricyclo[7.3.0.0^{3,7}]dodeca-1(12),4,6,8,10-pentaen-4-yl]-~{N}-[2-[2-[[2-[(6-oxidanylidene-7-oxa-2,5-diazaspiro[3.4]octan-2-yl)carbonyl]-2-azaspiro[3.3]heptan-6-yl]methyl]phenoxy]ethyl]propanamide
;
A1IIH 
3 1,2-ETHANEDIOL EDO   
4 water HOH   
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   MET n 
1 2   GLY n 
1 3   SER n 
1 4   SER n 
1 5   HIS n 
1 6   HIS n 
1 7   HIS n 
1 8   HIS n 
1 9   HIS n 
1 10  HIS n 
1 11  SER n 
1 12  SER n 
1 13  GLY n 
1 14  GLU n 
1 15  ASN n 
1 16  LEU n 
1 17  TYR n 
1 18  PHE n 
1 19  GLN n 
1 20  GLY n 
1 21  MET n 
1 22  PRO n 
1 23  GLU n 
1 24  GLU n 
1 25  SER n 
1 26  SER n 
1 27  PRO n 
1 28  ARG n 
1 29  ARG n 
1 30  THR n 
1 31  PRO n 
1 32  GLN n 
1 33  SER n 
1 34  ILE n 
1 35  PRO n 
1 36  TYR n 
1 37  GLN n 
1 38  ASP n 
1 39  LEU n 
1 40  PRO n 
1 41  HIS n 
1 42  LEU n 
1 43  VAL n 
1 44  ASN n 
1 45  ALA n 
1 46  ASP n 
1 47  GLY n 
1 48  GLN n 
1 49  TYR n 
1 50  LEU n 
1 51  PHE n 
1 52  CYS n 
1 53  ARG n 
1 54  TYR n 
1 55  TRP n 
1 56  ALA n 
1 57  PRO n 
1 58  THR n 
1 59  GLY n 
1 60  THR n 
1 61  PRO n 
1 62  LYS n 
1 63  ALA n 
1 64  LEU n 
1 65  ILE n 
1 66  PHE n 
1 67  VAL n 
1 68  SER n 
1 69  HIS n 
1 70  GLY n 
1 71  ALA n 
1 72  GLY n 
1 73  GLU n 
1 74  HIS n 
1 75  SER n 
1 76  GLY n 
1 77  ARG n 
1 78  TYR n 
1 79  GLU n 
1 80  GLU n 
1 81  LEU n 
1 82  ALA n 
1 83  ARG n 
1 84  MET n 
1 85  LEU n 
1 86  MET n 
1 87  GLY n 
1 88  LEU n 
1 89  ASP n 
1 90  LEU n 
1 91  LEU n 
1 92  VAL n 
1 93  PHE n 
1 94  ALA n 
1 95  HIS n 
1 96  ASP n 
1 97  HIS n 
1 98  VAL n 
1 99  GLY n 
1 100 HIS n 
1 101 GLY n 
1 102 GLN n 
1 103 SER n 
1 104 GLU n 
1 105 GLY n 
1 106 GLU n 
1 107 ARG n 
1 108 MET n 
1 109 VAL n 
1 110 VAL n 
1 111 SER n 
1 112 ASP n 
1 113 PHE n 
1 114 HIS n 
1 115 VAL n 
1 116 PHE n 
1 117 VAL n 
1 118 ARG n 
1 119 ASP n 
1 120 VAL n 
1 121 LEU n 
1 122 GLN n 
1 123 HIS n 
1 124 VAL n 
1 125 ASP n 
1 126 SER n 
1 127 MET n 
1 128 GLN n 
1 129 LYS n 
1 130 ASP n 
1 131 TYR n 
1 132 PRO n 
1 133 GLY n 
1 134 LEU n 
1 135 PRO n 
1 136 VAL n 
1 137 PHE n 
1 138 LEU n 
1 139 LEU n 
1 140 GLY n 
1 141 HIS n 
1 142 SER n 
1 143 MET n 
1 144 GLY n 
1 145 GLY n 
1 146 ALA n 
1 147 ILE n 
1 148 ALA n 
1 149 ILE n 
1 150 LEU n 
1 151 THR n 
1 152 ALA n 
1 153 ALA n 
1 154 GLU n 
1 155 ARG n 
1 156 PRO n 
1 157 GLY n 
1 158 HIS n 
1 159 PHE n 
1 160 ALA n 
1 161 GLY n 
1 162 MET n 
1 163 VAL n 
1 164 LEU n 
1 165 ILE n 
1 166 SER n 
1 167 PRO n 
1 168 LEU n 
1 169 VAL n 
1 170 LEU n 
1 171 ALA n 
1 172 ASN n 
1 173 PRO n 
1 174 GLU n 
1 175 SER n 
1 176 ALA n 
1 177 THR n 
1 178 THR n 
1 179 PHE n 
1 180 LYS n 
1 181 VAL n 
1 182 LEU n 
1 183 ALA n 
1 184 ALA n 
1 185 LYS n 
1 186 VAL n 
1 187 LEU n 
1 188 ASN n 
1 189 SER n 
1 190 VAL n 
1 191 LEU n 
1 192 PRO n 
1 193 ASN n 
1 194 LEU n 
1 195 SER n 
1 196 SER n 
1 197 GLY n 
1 198 PRO n 
1 199 ILE n 
1 200 ASP n 
1 201 SER n 
1 202 SER n 
1 203 VAL n 
1 204 LEU n 
1 205 SER n 
1 206 ARG n 
1 207 ASN n 
1 208 LYS n 
1 209 THR n 
1 210 GLU n 
1 211 VAL n 
1 212 ASP n 
1 213 ILE n 
1 214 TYR n 
1 215 ASN n 
1 216 SER n 
1 217 ASP n 
1 218 PRO n 
1 219 LEU n 
1 220 ILE n 
1 221 CYS n 
1 222 ARG n 
1 223 ALA n 
1 224 GLY n 
1 225 LEU n 
1 226 LYS n 
1 227 VAL n 
1 228 CYS n 
1 229 PHE n 
1 230 GLY n 
1 231 ILE n 
1 232 GLN n 
1 233 LEU n 
1 234 LEU n 
1 235 ASN n 
1 236 ALA n 
1 237 VAL n 
1 238 SER n 
1 239 ARG n 
1 240 VAL n 
1 241 GLU n 
1 242 ARG n 
1 243 ALA n 
1 244 LEU n 
1 245 PRO n 
1 246 LYS n 
1 247 LEU n 
1 248 THR n 
1 249 VAL n 
1 250 PRO n 
1 251 PHE n 
1 252 LEU n 
1 253 LEU n 
1 254 LEU n 
1 255 GLN n 
1 256 GLY n 
1 257 SER n 
1 258 ALA n 
1 259 ASP n 
1 260 ARG n 
1 261 LEU n 
1 262 CYS n 
1 263 ASP n 
1 264 SER n 
1 265 LYS n 
1 266 GLY n 
1 267 ALA n 
1 268 TYR n 
1 269 LEU n 
1 270 LEU n 
1 271 MET n 
1 272 GLU n 
1 273 LEU n 
1 274 ALA n 
1 275 LYS n 
1 276 SER n 
1 277 GLN n 
1 278 ASP n 
1 279 LYS n 
1 280 THR n 
1 281 LEU n 
1 282 LYS n 
1 283 ILE n 
1 284 TYR n 
1 285 GLU n 
1 286 GLY n 
1 287 ALA n 
1 288 TYR n 
1 289 HIS n 
1 290 VAL n 
1 291 LEU n 
1 292 HIS n 
1 293 LYS n 
1 294 GLU n 
1 295 LEU n 
1 296 PRO n 
1 297 GLU n 
1 298 VAL n 
1 299 THR n 
1 300 ASN n 
1 301 SER n 
1 302 VAL n 
1 303 PHE n 
1 304 HIS n 
1 305 GLU n 
1 306 ILE n 
1 307 ASN n 
1 308 MET n 
1 309 TRP n 
1 310 VAL n 
1 311 SER n 
1 312 GLN n 
1 313 ARG n 
1 314 THR n 
1 315 ALA n 
1 316 THR n 
1 317 ALA n 
1 318 GLY n 
1 319 THR n 
1 320 ALA n 
1 321 SER n 
1 322 PRO n 
1 323 PRO 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                   323 
_entity_src_gen.gene_src_common_name               human 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 MGLL 
_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 
A1IIH non-polymer         . 
;3-[2,2-bis(fluoranyl)-10,12-dimethyl-1$l^{4},3-diaza-2$l^{4}-boratricyclo[7.3.0.0^{3,7}]dodeca-1(12),4,6,8,10-pentaen-4-yl]-~{N}-[2-[2-[[2-[(6-oxidanylidene-7-oxa-2,5-diazaspiro[3.4]octan-2-yl)carbonyl]-2-azaspiro[3.3]heptan-6-yl]methyl]phenoxy]ethyl]propanamide
;
?                 'C35 H41 B F2 N6 O5' 674.545 
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 
EDO   non-polymer         . 1,2-ETHANEDIOL 'ETHYLENE GLYCOL' 'C2 H6 O2'           62.068  
GLN   'L-peptide linking' y GLUTAMINE ?                 'C5 H10 N2 O3'       146.144 
GLU   'L-peptide linking' y 'GLUTAMIC ACID' ?                 'C5 H9 N O4'         147.129 
GLY   'peptide linking'   y GLYCINE ?                 'C2 H5 N O2'         75.067  
HIS   'L-peptide linking' y HISTIDINE ?                 'C6 H10 N3 O2 1'     156.162 
HOH   non-polymer         . WATER ?                 'H2 O'               18.015  
ILE   'L-peptide linking' y ISOLEUCINE ?                 'C6 H13 N O2'        131.173 
LEU   'L-peptide linking' y LEUCINE ?                 'C6 H13 N O2'        131.173 
LYS   'L-peptide linking' y LYSINE ?                 'C6 H15 N2 O2 1'     147.195 
MET   'L-peptide linking' y METHIONINE ?                 'C5 H11 N O2 S'      149.211 
PHE   'L-peptide linking' y PHENYLALANINE ?                 'C9 H11 N O2'        165.189 
PRO   'L-peptide linking' y PROLINE ?                 'C5 H9 N O2'         115.130 
SER   'L-peptide linking' y SERINE ?                 'C3 H7 N O3'         105.093 
THR   'L-peptide linking' y THREONINE ?                 'C4 H9 N O3'         119.119 
TRP   'L-peptide linking' y TRYPTOPHAN ?                 'C11 H12 N2 O2'      204.225 
TYR   'L-peptide linking' y TYROSINE ?                 'C9 H11 N O3'        181.189 
VAL   'L-peptide linking' y VALINE ?                 'C5 H11 N O2'        117.146 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   MET 1   -19 ?   ?   ?   A . n 
A 1 2   GLY 2   -18 ?   ?   ?   A . n 
A 1 3   SER 3   -17 ?   ?   ?   A . n 
A 1 4   SER 4   -16 ?   ?   ?   A . n 
A 1 5   HIS 5   -15 ?   ?   ?   A . n 
A 1 6   HIS 6   -14 ?   ?   ?   A . n 
A 1 7   HIS 7   -13 ?   ?   ?   A . n 
A 1 8   HIS 8   -12 ?   ?   ?   A . n 
A 1 9   HIS 9   -11 ?   ?   ?   A . n 
A 1 10  HIS 10  -10 ?   ?   ?   A . n 
A 1 11  SER 11  -9  ?   ?   ?   A . n 
A 1 12  SER 12  -8  ?   ?   ?   A . n 
A 1 13  GLY 13  -7  ?   ?   ?   A . n 
A 1 14  GLU 14  -6  ?   ?   ?   A . n 
A 1 15  ASN 15  -5  ?   ?   ?   A . n 
A 1 16  LEU 16  -4  ?   ?   ?   A . n 
A 1 17  TYR 17  -3  ?   ?   ?   A . n 
A 1 18  PHE 18  -2  ?   ?   ?   A . n 
A 1 19  GLN 19  -1  ?   ?   ?   A . n 
A 1 20  GLY 20  0   ?   ?   ?   A . n 
A 1 21  MET 21  1   ?   ?   ?   A . n 
A 1 22  PRO 22  2   ?   ?   ?   A . n 
A 1 23  GLU 23  3   ?   ?   ?   A . n 
A 1 24  GLU 24  4   ?   ?   ?   A . n 
A 1 25  SER 25  5   ?   ?   ?   A . n 
A 1 26  SER 26  6   6   SER SER A . n 
A 1 27  PRO 27  7   7   PRO PRO A . n 
A 1 28  ARG 28  8   8   ARG ARG A . n 
A 1 29  ARG 29  9   9   ARG ARG A . n 
A 1 30  THR 30  10  10  THR THR A . n 
A 1 31  PRO 31  11  11  PRO PRO A . n 
A 1 32  GLN 32  12  12  GLN GLN A . n 
A 1 33  SER 33  13  13  SER SER A . n 
A 1 34  ILE 34  14  14  ILE ILE A . n 
A 1 35  PRO 35  15  15  PRO PRO A . n 
A 1 36  TYR 36  16  16  TYR TYR A . n 
A 1 37  GLN 37  17  17  GLN GLN A . n 
A 1 38  ASP 38  18  18  ASP ASP A . n 
A 1 39  LEU 39  19  19  LEU LEU A . n 
A 1 40  PRO 40  20  20  PRO PRO A . n 
A 1 41  HIS 41  21  21  HIS HIS A . n 
A 1 42  LEU 42  22  22  LEU LEU A . n 
A 1 43  VAL 43  23  23  VAL VAL A . n 
A 1 44  ASN 44  24  24  ASN ASN A . n 
A 1 45  ALA 45  25  25  ALA ALA A . n 
A 1 46  ASP 46  26  26  ASP ASP A . n 
A 1 47  GLY 47  27  27  GLY GLY A . n 
A 1 48  GLN 48  28  28  GLN GLN A . n 
A 1 49  TYR 49  29  29  TYR TYR A . n 
A 1 50  LEU 50  30  30  LEU LEU A . n 
A 1 51  PHE 51  31  31  PHE PHE A . n 
A 1 52  CYS 52  32  32  CYS CYS A . n 
A 1 53  ARG 53  33  33  ARG ARG A . n 
A 1 54  TYR 54  34  34  TYR TYR A . n 
A 1 55  TRP 55  35  35  TRP TRP A . n 
A 1 56  ALA 56  36  36  ALA ALA A . n 
A 1 57  PRO 57  37  37  PRO PRO A . n 
A 1 58  THR 58  38  38  THR THR A . n 
A 1 59  GLY 59  39  39  GLY GLY A . n 
A 1 60  THR 60  40  40  THR THR A . n 
A 1 61  PRO 61  41  41  PRO PRO A . n 
A 1 62  LYS 62  42  42  LYS LYS A . n 
A 1 63  ALA 63  43  43  ALA ALA A . n 
A 1 64  LEU 64  44  44  LEU LEU A . n 
A 1 65  ILE 65  45  45  ILE ILE A . n 
A 1 66  PHE 66  46  46  PHE PHE A . n 
A 1 67  VAL 67  47  47  VAL VAL A . n 
A 1 68  SER 68  48  48  SER SER A . n 
A 1 69  HIS 69  49  49  HIS HIS A . n 
A 1 70  GLY 70  50  50  GLY GLY A . n 
A 1 71  ALA 71  51  51  ALA ALA A . n 
A 1 72  GLY 72  52  52  GLY GLY A . n 
A 1 73  GLU 73  53  53  GLU GLU A . n 
A 1 74  HIS 74  54  54  HIS HIS A . n 
A 1 75  SER 75  55  55  SER SER A . n 
A 1 76  GLY 76  56  56  GLY GLY A . n 
A 1 77  ARG 77  57  57  ARG ARG A . n 
A 1 78  TYR 78  58  58  TYR TYR A . n 
A 1 79  GLU 79  59  59  GLU GLU A . n 
A 1 80  GLU 80  60  60  GLU GLU A . n 
A 1 81  LEU 81  61  61  LEU LEU A . n 
A 1 82  ALA 82  62  62  ALA ALA A . n 
A 1 83  ARG 83  63  63  ARG ARG A . n 
A 1 84  MET 84  64  64  MET MET A . n 
A 1 85  LEU 85  65  65  LEU LEU A . n 
A 1 86  MET 86  66  66  MET MET A . n 
A 1 87  GLY 87  67  67  GLY GLY A . n 
A 1 88  LEU 88  68  68  LEU LEU A . n 
A 1 89  ASP 89  69  69  ASP ASP A . n 
A 1 90  LEU 90  70  70  LEU LEU A . n 
A 1 91  LEU 91  71  71  LEU LEU A . n 
A 1 92  VAL 92  72  72  VAL VAL A . n 
A 1 93  PHE 93  73  73  PHE PHE A . n 
A 1 94  ALA 94  74  74  ALA ALA A . n 
A 1 95  HIS 95  75  75  HIS HIS A . n 
A 1 96  ASP 96  76  76  ASP ASP A . n 
A 1 97  HIS 97  77  77  HIS HIS A . n 
A 1 98  VAL 98  78  78  VAL VAL A . n 
A 1 99  GLY 99  79  79  GLY GLY A . n 
A 1 100 HIS 100 80  80  HIS HIS A . n 
A 1 101 GLY 101 81  81  GLY GLY A . n 
A 1 102 GLN 102 82  82  GLN GLN A . n 
A 1 103 SER 103 83  83  SER SER A . n 
A 1 104 GLU 104 84  84  GLU GLU A . n 
A 1 105 GLY 105 85  85  GLY GLY A . n 
A 1 106 GLU 106 86  86  GLU GLU A . n 
A 1 107 ARG 107 87  87  ARG ARG A . n 
A 1 108 MET 108 88  88  MET MET A . n 
A 1 109 VAL 109 89  89  VAL VAL A . n 
A 1 110 VAL 110 90  90  VAL VAL A . n 
A 1 111 SER 111 91  91  SER SER A . n 
A 1 112 ASP 112 92  92  ASP ASP A . n 
A 1 113 PHE 113 93  93  PHE PHE A . n 
A 1 114 HIS 114 94  94  HIS HIS A . n 
A 1 115 VAL 115 95  95  VAL VAL A . n 
A 1 116 PHE 116 96  96  PHE PHE A . n 
A 1 117 VAL 117 97  97  VAL VAL A . n 
A 1 118 ARG 118 98  98  ARG ARG A . n 
A 1 119 ASP 119 99  99  ASP ASP A . n 
A 1 120 VAL 120 100 100 VAL VAL A . n 
A 1 121 LEU 121 101 101 LEU LEU A . n 
A 1 122 GLN 122 102 102 GLN GLN A . n 
A 1 123 HIS 123 103 103 HIS HIS A . n 
A 1 124 VAL 124 104 104 VAL VAL A . n 
A 1 125 ASP 125 105 105 ASP ASP A . n 
A 1 126 SER 126 106 106 SER SER A . n 
A 1 127 MET 127 107 107 MET MET A . n 
A 1 128 GLN 128 108 108 GLN GLN A . n 
A 1 129 LYS 129 109 109 LYS LYS A . n 
A 1 130 ASP 130 110 110 ASP ASP A . n 
A 1 131 TYR 131 111 111 TYR TYR A . n 
A 1 132 PRO 132 112 112 PRO PRO A . n 
A 1 133 GLY 133 113 113 GLY GLY A . n 
A 1 134 LEU 134 114 114 LEU LEU A . n 
A 1 135 PRO 135 115 115 PRO PRO A . n 
A 1 136 VAL 136 116 116 VAL VAL A . n 
A 1 137 PHE 137 117 117 PHE PHE A . n 
A 1 138 LEU 138 118 118 LEU LEU A . n 
A 1 139 LEU 139 119 119 LEU LEU A . n 
A 1 140 GLY 140 120 120 GLY GLY A . n 
A 1 141 HIS 141 121 121 HIS HIS A . n 
A 1 142 SER 142 122 122 SER SER A . n 
A 1 143 MET 143 123 123 MET MET A . n 
A 1 144 GLY 144 124 124 GLY GLY A . n 
A 1 145 GLY 145 125 125 GLY GLY A . n 
A 1 146 ALA 146 126 126 ALA ALA A . n 
A 1 147 ILE 147 127 127 ILE ILE A . n 
A 1 148 ALA 148 128 128 ALA ALA A . n 
A 1 149 ILE 149 129 129 ILE ILE A . n 
A 1 150 LEU 150 130 130 LEU LEU A . n 
A 1 151 THR 151 131 131 THR THR A . n 
A 1 152 ALA 152 132 132 ALA ALA A . n 
A 1 153 ALA 153 133 133 ALA ALA A . n 
A 1 154 GLU 154 134 134 GLU GLU A . n 
A 1 155 ARG 155 135 135 ARG ARG A . n 
A 1 156 PRO 156 136 136 PRO PRO A . n 
A 1 157 GLY 157 137 137 GLY GLY A . n 
A 1 158 HIS 158 138 138 HIS HIS A . n 
A 1 159 PHE 159 139 139 PHE PHE A . n 
A 1 160 ALA 160 140 140 ALA ALA A . n 
A 1 161 GLY 161 141 141 GLY GLY A . n 
A 1 162 MET 162 142 142 MET MET A . n 
A 1 163 VAL 163 143 143 VAL VAL A . n 
A 1 164 LEU 164 144 144 LEU LEU A . n 
A 1 165 ILE 165 145 145 ILE ILE A . n 
A 1 166 SER 166 146 146 SER SER A . n 
A 1 167 PRO 167 147 147 PRO PRO A . n 
A 1 168 LEU 168 148 148 LEU LEU A . n 
A 1 169 VAL 169 149 149 VAL VAL A . n 
A 1 170 LEU 170 150 150 LEU LEU A . n 
A 1 171 ALA 171 151 151 ALA ALA A . n 
A 1 172 ASN 172 152 152 ASN ASN A . n 
A 1 173 PRO 173 153 153 PRO PRO A . n 
A 1 174 GLU 174 154 154 GLU GLU A . n 
A 1 175 SER 175 155 155 SER SER A . n 
A 1 176 ALA 176 156 156 ALA ALA A . n 
A 1 177 THR 177 157 157 THR THR A . n 
A 1 178 THR 178 158 158 THR THR A . n 
A 1 179 PHE 179 159 159 PHE PHE A . n 
A 1 180 LYS 180 160 160 LYS LYS A . n 
A 1 181 VAL 181 161 161 VAL VAL A . n 
A 1 182 LEU 182 162 162 LEU LEU A . n 
A 1 183 ALA 183 163 163 ALA ALA A . n 
A 1 184 ALA 184 164 164 ALA ALA A . n 
A 1 185 LYS 185 165 165 LYS LYS A . n 
A 1 186 VAL 186 166 166 VAL VAL A . n 
A 1 187 LEU 187 167 167 LEU LEU A . n 
A 1 188 ASN 188 168 168 ASN ASN A . n 
A 1 189 SER 189 169 169 SER SER A . n 
A 1 190 VAL 190 170 170 VAL VAL A . n 
A 1 191 LEU 191 171 171 LEU LEU A . n 
A 1 192 PRO 192 172 172 PRO PRO A . n 
A 1 193 ASN 193 173 173 ASN ASN A . n 
A 1 194 LEU 194 174 174 LEU LEU A . n 
A 1 195 SER 195 175 175 SER SER A . n 
A 1 196 SER 196 176 176 SER SER A . n 
A 1 197 GLY 197 177 177 GLY GLY A . n 
A 1 198 PRO 198 178 178 PRO PRO A . n 
A 1 199 ILE 199 179 179 ILE ILE A . n 
A 1 200 ASP 200 180 180 ASP ASP A . n 
A 1 201 SER 201 181 181 SER SER A . n 
A 1 202 SER 202 182 182 SER SER A . n 
A 1 203 VAL 203 183 183 VAL VAL A . n 
A 1 204 LEU 204 184 184 LEU LEU A . n 
A 1 205 SER 205 185 185 SER SER A . n 
A 1 206 ARG 206 186 186 ARG ARG A . n 
A 1 207 ASN 207 187 187 ASN ASN A . n 
A 1 208 LYS 208 188 188 LYS LYS A . n 
A 1 209 THR 209 189 189 THR THR A . n 
A 1 210 GLU 210 190 190 GLU GLU A . n 
A 1 211 VAL 211 191 191 VAL VAL A . n 
A 1 212 ASP 212 192 192 ASP ASP A . n 
A 1 213 ILE 213 193 193 ILE ILE A . n 
A 1 214 TYR 214 194 194 TYR TYR A . n 
A 1 215 ASN 215 195 195 ASN ASN A . n 
A 1 216 SER 216 196 196 SER SER A . n 
A 1 217 ASP 217 197 197 ASP ASP A . n 
A 1 218 PRO 218 198 198 PRO PRO A . n 
A 1 219 LEU 219 199 199 LEU LEU A . n 
A 1 220 ILE 220 200 200 ILE ILE A . n 
A 1 221 CYS 221 201 201 CYS CYS A . n 
A 1 222 ARG 222 202 202 ARG ARG A . n 
A 1 223 ALA 223 203 203 ALA ALA A . n 
A 1 224 GLY 224 204 204 GLY GLY A . n 
A 1 225 LEU 225 205 205 LEU LEU A . n 
A 1 226 LYS 226 206 206 LYS LYS A . n 
A 1 227 VAL 227 207 207 VAL VAL A . n 
A 1 228 CYS 228 208 208 CYS CYS A . n 
A 1 229 PHE 229 209 209 PHE PHE A . n 
A 1 230 GLY 230 210 210 GLY GLY A . n 
A 1 231 ILE 231 211 211 ILE ILE A . n 
A 1 232 GLN 232 212 212 GLN GLN A . n 
A 1 233 LEU 233 213 213 LEU LEU A . n 
A 1 234 LEU 234 214 214 LEU LEU A . n 
A 1 235 ASN 235 215 215 ASN ASN A . n 
A 1 236 ALA 236 216 216 ALA ALA A . n 
A 1 237 VAL 237 217 217 VAL VAL A . n 
A 1 238 SER 238 218 218 SER SER A . n 
A 1 239 ARG 239 219 219 ARG ARG A . n 
A 1 240 VAL 240 220 220 VAL VAL A . n 
A 1 241 GLU 241 221 221 GLU GLU A . n 
A 1 242 ARG 242 222 222 ARG ARG A . n 
A 1 243 ALA 243 223 223 ALA ALA A . n 
A 1 244 LEU 244 224 224 LEU LEU A . n 
A 1 245 PRO 245 225 225 PRO PRO A . n 
A 1 246 LYS 246 226 226 LYS LYS A . n 
A 1 247 LEU 247 227 227 LEU LEU A . n 
A 1 248 THR 248 228 228 THR THR A . n 
A 1 249 VAL 249 229 229 VAL VAL A . n 
A 1 250 PRO 250 230 230 PRO PRO A . n 
A 1 251 PHE 251 231 231 PHE PHE A . n 
A 1 252 LEU 252 232 232 LEU LEU A . n 
A 1 253 LEU 253 233 233 LEU LEU A . n 
A 1 254 LEU 254 234 234 LEU LEU A . n 
A 1 255 GLN 255 235 235 GLN GLN A . n 
A 1 256 GLY 256 236 236 GLY GLY A . n 
A 1 257 SER 257 237 237 SER SER A . n 
A 1 258 ALA 258 238 238 ALA ALA A . n 
A 1 259 ASP 259 239 239 ASP ASP A . n 
A 1 260 ARG 260 240 240 ARG ARG A . n 
A 1 261 LEU 261 241 241 LEU LEU A . n 
A 1 262 CYS 262 242 242 CYS CYS A . n 
A 1 263 ASP 263 243 243 ASP ASP A . n 
A 1 264 SER 264 244 244 SER SER A . n 
A 1 265 LYS 265 245 245 LYS LYS A . n 
A 1 266 GLY 266 246 246 GLY GLY A . n 
A 1 267 ALA 267 247 247 ALA ALA A . n 
A 1 268 TYR 268 248 248 TYR TYR A . n 
A 1 269 LEU 269 249 249 LEU LEU A . n 
A 1 270 LEU 270 250 250 LEU LEU A . n 
A 1 271 MET 271 251 251 MET MET A . n 
A 1 272 GLU 272 252 252 GLU GLU A . n 
A 1 273 LEU 273 253 253 LEU LEU A . n 
A 1 274 ALA 274 254 254 ALA ALA A . n 
A 1 275 LYS 275 255 255 LYS LYS A . n 
A 1 276 SER 276 256 256 SER SER A . n 
A 1 277 GLN 277 257 257 GLN GLN A . n 
A 1 278 ASP 278 258 258 ASP ASP A . n 
A 1 279 LYS 279 259 259 LYS LYS A . n 
A 1 280 THR 280 260 260 THR THR A . n 
A 1 281 LEU 281 261 261 LEU LEU A . n 
A 1 282 LYS 282 262 262 LYS LYS A . n 
A 1 283 ILE 283 263 263 ILE ILE A . n 
A 1 284 TYR 284 264 264 TYR TYR A . n 
A 1 285 GLU 285 265 265 GLU GLU A . n 
A 1 286 GLY 286 266 266 GLY GLY A . n 
A 1 287 ALA 287 267 267 ALA ALA A . n 
A 1 288 TYR 288 268 268 TYR TYR A . n 
A 1 289 HIS 289 269 269 HIS HIS A . n 
A 1 290 VAL 290 270 270 VAL VAL A . n 
A 1 291 LEU 291 271 271 LEU LEU A . n 
A 1 292 HIS 292 272 272 HIS HIS A . n 
A 1 293 LYS 293 273 273 LYS LYS A . n 
A 1 294 GLU 294 274 274 GLU GLU A . n 
A 1 295 LEU 295 275 275 LEU LEU A . n 
A 1 296 PRO 296 276 276 PRO PRO A . n 
A 1 297 GLU 297 277 277 GLU GLU A . n 
A 1 298 VAL 298 278 278 VAL VAL A . n 
A 1 299 THR 299 279 279 THR THR A . n 
A 1 300 ASN 300 280 280 ASN ASN A . n 
A 1 301 SER 301 281 281 SER SER A . n 
A 1 302 VAL 302 282 282 VAL VAL A . n 
A 1 303 PHE 303 283 283 PHE PHE A . n 
A 1 304 HIS 304 284 284 HIS HIS A . n 
A 1 305 GLU 305 285 285 GLU GLU A . n 
A 1 306 ILE 306 286 286 ILE ILE A . n 
A 1 307 ASN 307 287 287 ASN ASN A . n 
A 1 308 MET 308 288 288 MET MET A . n 
A 1 309 TRP 309 289 289 TRP TRP A . n 
A 1 310 VAL 310 290 290 VAL VAL A . n 
A 1 311 SER 311 291 291 SER SER A . n 
A 1 312 GLN 312 292 292 GLN GLN A . n 
A 1 313 ARG 313 293 293 ARG ARG A . n 
A 1 314 THR 314 294 294 THR THR A . n 
A 1 315 ALA 315 295 295 ALA ALA A . n 
A 1 316 THR 316 296 ?   ?   ?   A . n 
A 1 317 ALA 317 297 ?   ?   ?   A . n 
A 1 318 GLY 318 298 ?   ?   ?   A . n 
A 1 319 THR 319 299 ?   ?   ?   A . n 
A 1 320 ALA 320 300 ?   ?   ?   A . n 
A 1 321 SER 321 301 ?   ?   ?   A . n 
A 1 322 PRO 322 302 ?   ?   ?   A . n 
A 1 323 PRO 323 303 ?   ?   ?   A . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        A1IIH 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1IIH 
_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 
B 2 A1IIH 1   401 301 A1IIH XXX A . 
C 3 EDO   1   402 3   EDO   EDO A . 
D 3 EDO   1   403 4   EDO   EDO A . 
E 3 EDO   1   404 5   EDO   EDO A . 
F 3 EDO   1   405 6   EDO   EDO A . 
G 3 EDO   1   406 7   EDO   EDO A . 
H 3 EDO   1   407 8   EDO   EDO A . 
I 3 EDO   1   408 9   EDO   EDO A . 
J 3 EDO   1   409 10  EDO   EDO A . 
K 4 HOH   1   501 13  HOH   HOH A . 
K 4 HOH   2   502 257 HOH   HOH A . 
K 4 HOH   3   503 233 HOH   HOH A . 
K 4 HOH   4   504 29  HOH   HOH A . 
K 4 HOH   5   505 100 HOH   HOH A . 
K 4 HOH   6   506 102 HOH   HOH A . 
K 4 HOH   7   507 78  HOH   HOH A . 
K 4 HOH   8   508 212 HOH   HOH A . 
K 4 HOH   9   509 261 HOH   HOH A . 
K 4 HOH   10  510 164 HOH   HOH A . 
K 4 HOH   11  511 32  HOH   HOH A . 
K 4 HOH   12  512 167 HOH   HOH A . 
K 4 HOH   13  513 73  HOH   HOH A . 
K 4 HOH   14  514 230 HOH   HOH A . 
K 4 HOH   15  515 36  HOH   HOH A . 
K 4 HOH   16  516 10  HOH   HOH A . 
K 4 HOH   17  517 163 HOH   HOH A . 
K 4 HOH   18  518 87  HOH   HOH A . 
K 4 HOH   19  519 63  HOH   HOH A . 
K 4 HOH   20  520 47  HOH   HOH A . 
K 4 HOH   21  521 23  HOH   HOH A . 
K 4 HOH   22  522 155 HOH   HOH A . 
K 4 HOH   23  523 152 HOH   HOH A . 
K 4 HOH   24  524 22  HOH   HOH A . 
K 4 HOH   25  525 24  HOH   HOH A . 
K 4 HOH   26  526 42  HOH   HOH A . 
K 4 HOH   27  527 33  HOH   HOH A . 
K 4 HOH   28  528 31  HOH   HOH A . 
K 4 HOH   29  529 6   HOH   HOH A . 
K 4 HOH   30  530 56  HOH   HOH A . 
K 4 HOH   31  531 53  HOH   HOH A . 
K 4 HOH   32  532 17  HOH   HOH A . 
K 4 HOH   33  533 190 HOH   HOH A . 
K 4 HOH   34  534 112 HOH   HOH A . 
K 4 HOH   35  535 25  HOH   HOH A . 
K 4 HOH   36  536 14  HOH   HOH A . 
K 4 HOH   37  537 35  HOH   HOH A . 
K 4 HOH   38  538 12  HOH   HOH A . 
K 4 HOH   39  539 191 HOH   HOH A . 
K 4 HOH   40  540 109 HOH   HOH A . 
K 4 HOH   41  541 55  HOH   HOH A . 
K 4 HOH   42  542 141 HOH   HOH A . 
K 4 HOH   43  543 7   HOH   HOH A . 
K 4 HOH   44  544 243 HOH   HOH A . 
K 4 HOH   45  545 101 HOH   HOH A . 
K 4 HOH   46  546 50  HOH   HOH A . 
K 4 HOH   47  547 70  HOH   HOH A . 
K 4 HOH   48  548 9   HOH   HOH A . 
K 4 HOH   49  549 250 HOH   HOH A . 
K 4 HOH   50  550 2   HOH   HOH A . 
K 4 HOH   51  551 82  HOH   HOH A . 
K 4 HOH   52  552 172 HOH   HOH A . 
K 4 HOH   53  553 52  HOH   HOH A . 
K 4 HOH   54  554 94  HOH   HOH A . 
K 4 HOH   55  555 97  HOH   HOH A . 
K 4 HOH   56  556 3   HOH   HOH A . 
K 4 HOH   57  557 262 HOH   HOH A . 
K 4 HOH   58  558 4   HOH   HOH A . 
K 4 HOH   59  559 43  HOH   HOH A . 
K 4 HOH   60  560 241 HOH   HOH A . 
K 4 HOH   61  561 126 HOH   HOH A . 
K 4 HOH   62  562 18  HOH   HOH A . 
K 4 HOH   63  563 54  HOH   HOH A . 
K 4 HOH   64  564 166 HOH   HOH A . 
K 4 HOH   65  565 80  HOH   HOH A . 
K 4 HOH   66  566 91  HOH   HOH A . 
K 4 HOH   67  567 242 HOH   HOH A . 
K 4 HOH   68  568 160 HOH   HOH A . 
K 4 HOH   69  569 157 HOH   HOH A . 
K 4 HOH   70  570 263 HOH   HOH A . 
K 4 HOH   71  571 148 HOH   HOH A . 
K 4 HOH   72  572 20  HOH   HOH A . 
K 4 HOH   73  573 106 HOH   HOH A . 
K 4 HOH   74  574 134 HOH   HOH A . 
K 4 HOH   75  575 99  HOH   HOH A . 
K 4 HOH   76  576 71  HOH   HOH A . 
K 4 HOH   77  577 46  HOH   HOH A . 
K 4 HOH   78  578 66  HOH   HOH A . 
K 4 HOH   79  579 145 HOH   HOH A . 
K 4 HOH   80  580 149 HOH   HOH A . 
K 4 HOH   81  581 5   HOH   HOH A . 
K 4 HOH   82  582 44  HOH   HOH A . 
K 4 HOH   83  583 92  HOH   HOH A . 
K 4 HOH   84  584 39  HOH   HOH A . 
K 4 HOH   85  585 19  HOH   HOH A . 
K 4 HOH   86  586 130 HOH   HOH A . 
K 4 HOH   87  587 204 HOH   HOH A . 
K 4 HOH   88  588 236 HOH   HOH A . 
K 4 HOH   89  589 123 HOH   HOH A . 
K 4 HOH   90  590 125 HOH   HOH A . 
K 4 HOH   91  591 16  HOH   HOH A . 
K 4 HOH   92  592 95  HOH   HOH A . 
K 4 HOH   93  593 173 HOH   HOH A . 
K 4 HOH   94  594 26  HOH   HOH A . 
K 4 HOH   95  595 245 HOH   HOH A . 
K 4 HOH   96  596 30  HOH   HOH A . 
K 4 HOH   97  597 48  HOH   HOH A . 
K 4 HOH   98  598 74  HOH   HOH A . 
K 4 HOH   99  599 21  HOH   HOH A . 
K 4 HOH   100 600 83  HOH   HOH A . 
K 4 HOH   101 601 89  HOH   HOH A . 
K 4 HOH   102 602 143 HOH   HOH A . 
K 4 HOH   103 603 162 HOH   HOH A . 
K 4 HOH   104 604 45  HOH   HOH A . 
K 4 HOH   105 605 96  HOH   HOH A . 
K 4 HOH   106 606 28  HOH   HOH A . 
K 4 HOH   107 607 247 HOH   HOH A . 
K 4 HOH   108 608 62  HOH   HOH A . 
K 4 HOH   109 609 184 HOH   HOH A . 
K 4 HOH   110 610 59  HOH   HOH A . 
K 4 HOH   111 611 98  HOH   HOH A . 
K 4 HOH   112 612 49  HOH   HOH A . 
K 4 HOH   113 613 81  HOH   HOH A . 
K 4 HOH   114 614 198 HOH   HOH A . 
K 4 HOH   115 615 34  HOH   HOH A . 
K 4 HOH   116 616 8   HOH   HOH A . 
K 4 HOH   117 617 117 HOH   HOH A . 
K 4 HOH   118 618 132 HOH   HOH A . 
K 4 HOH   119 619 259 HOH   HOH A . 
K 4 HOH   120 620 40  HOH   HOH A . 
K 4 HOH   121 621 192 HOH   HOH A . 
K 4 HOH   122 622 224 HOH   HOH A . 
K 4 HOH   123 623 64  HOH   HOH A . 
K 4 HOH   124 624 115 HOH   HOH A . 
K 4 HOH   125 625 227 HOH   HOH A . 
K 4 HOH   126 626 232 HOH   HOH A . 
K 4 HOH   127 627 246 HOH   HOH A . 
K 4 HOH   128 628 258 HOH   HOH A . 
K 4 HOH   129 629 200 HOH   HOH A . 
K 4 HOH   130 630 41  HOH   HOH A . 
K 4 HOH   131 631 133 HOH   HOH A . 
K 4 HOH   132 632 108 HOH   HOH A . 
K 4 HOH   133 633 144 HOH   HOH A . 
K 4 HOH   134 634 188 HOH   HOH A . 
K 4 HOH   135 635 147 HOH   HOH A . 
K 4 HOH   136 636 253 HOH   HOH A . 
K 4 HOH   137 637 68  HOH   HOH A . 
K 4 HOH   138 638 88  HOH   HOH A . 
K 4 HOH   139 639 57  HOH   HOH A . 
K 4 HOH   140 640 154 HOH   HOH A . 
K 4 HOH   141 641 77  HOH   HOH A . 
K 4 HOH   142 642 249 HOH   HOH A . 
K 4 HOH   143 643 107 HOH   HOH A . 
K 4 HOH   144 644 244 HOH   HOH A . 
K 4 HOH   145 645 196 HOH   HOH A . 
K 4 HOH   146 646 118 HOH   HOH A . 
K 4 HOH   147 647 60  HOH   HOH A . 
K 4 HOH   148 648 122 HOH   HOH A . 
K 4 HOH   149 649 111 HOH   HOH A . 
K 4 HOH   150 650 114 HOH   HOH A . 
K 4 HOH   151 651 231 HOH   HOH A . 
K 4 HOH   152 652 79  HOH   HOH A . 
K 4 HOH   153 653 153 HOH   HOH A . 
K 4 HOH   154 654 169 HOH   HOH A . 
K 4 HOH   155 655 176 HOH   HOH A . 
K 4 HOH   156 656 86  HOH   HOH A . 
K 4 HOH   157 657 220 HOH   HOH A . 
K 4 HOH   158 658 197 HOH   HOH A . 
K 4 HOH   159 659 178 HOH   HOH A . 
K 4 HOH   160 660 146 HOH   HOH A . 
K 4 HOH   161 661 256 HOH   HOH A . 
K 4 HOH   162 662 219 HOH   HOH A . 
K 4 HOH   163 663 84  HOH   HOH A . 
K 4 HOH   164 664 93  HOH   HOH A . 
K 4 HOH   165 665 210 HOH   HOH A . 
K 4 HOH   166 666 223 HOH   HOH A . 
K 4 HOH   167 667 222 HOH   HOH A . 
K 4 HOH   168 668 260 HOH   HOH A . 
K 4 HOH   169 669 187 HOH   HOH A . 
K 4 HOH   170 670 105 HOH   HOH A . 
K 4 HOH   171 671 139 HOH   HOH A . 
K 4 HOH   172 672 179 HOH   HOH A . 
K 4 HOH   173 673 177 HOH   HOH A . 
K 4 HOH   174 674 237 HOH   HOH A . 
K 4 HOH   175 675 240 HOH   HOH A . 
K 4 HOH   176 676 193 HOH   HOH A . 
K 4 HOH   177 677 110 HOH   HOH A . 
K 4 HOH   178 678 135 HOH   HOH A . 
K 4 HOH   179 679 206 HOH   HOH A . 
K 4 HOH   180 680 116 HOH   HOH A . 
K 4 HOH   181 681 131 HOH   HOH A . 
K 4 HOH   182 682 248 HOH   HOH A . 
K 4 HOH   183 683 72  HOH   HOH A . 
K 4 HOH   184 684 208 HOH   HOH A . 
K 4 HOH   185 685 156 HOH   HOH A . 
K 4 HOH   186 686 186 HOH   HOH A . 
K 4 HOH   187 687 202 HOH   HOH A . 
K 4 HOH   188 688 214 HOH   HOH A . 
K 4 HOH   189 689 228 HOH   HOH A . 
K 4 HOH   190 690 209 HOH   HOH A . 
K 4 HOH   191 691 221 HOH   HOH A . 
K 4 HOH   192 692 120 HOH   HOH A . 
K 4 HOH   193 693 217 HOH   HOH A . 
K 4 HOH   194 694 218 HOH   HOH A . 
K 4 HOH   195 695 15  HOH   HOH A . 
K 4 HOH   196 696 235 HOH   HOH A . 
K 4 HOH   197 697 251 HOH   HOH A . 
K 4 HOH   198 698 255 HOH   HOH A . 
K 4 HOH   199 699 254 HOH   HOH A . 
K 4 HOH   200 700 194 HOH   HOH A . 
K 4 HOH   201 701 183 HOH   HOH A . 
K 4 HOH   202 702 65  HOH   HOH A . 
K 4 HOH   203 703 213 HOH   HOH A . 
K 4 HOH   204 704 119 HOH   HOH A . 
K 4 HOH   205 705 61  HOH   HOH A . 
K 4 HOH   206 706 252 HOH   HOH A . 
K 4 HOH   207 707 150 HOH   HOH A . 
K 4 HOH   208 708 189 HOH   HOH A . 
K 4 HOH   209 709 181 HOH   HOH A . 
K 4 HOH   210 710 58  HOH   HOH A . 
# 
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 ? ? ? 1.21.1_5286+SVN 1 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? XDS    ? ? ? .               2 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? SADABS ? ? ? .               3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHASER ? ? ? .               4 
# 
_cell.angle_alpha                  90.000 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.000 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.000 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9G4M 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     88.896 
_cell.length_a_esd                 ? 
_cell.length_b                     127.245 
_cell.length_b_esd                 ? 
_cell.length_c                     62.206 
_cell.length_c_esd                 ? 
_cell.volume                       703647.618 
_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                         9G4M 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                20 
_symmetry.space_group_name_Hall            'C 2c 2' 
_symmetry.space_group_name_H-M             'C 2 2 21' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
_exptl.absorpt_coefficient_mu     ? 
_exptl.absorpt_correction_T_max   ? 
_exptl.absorpt_correction_T_min   ? 
_exptl.absorpt_correction_type    ? 
_exptl.absorpt_process_details    ? 
_exptl.entry_id                   9G4M 
_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             2.48 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          50.40 
_exptl_crystal.description                  ? 
_exptl_crystal.F_000                        ? 
_exptl_crystal.id                           1 
_exptl_crystal.preparation                  ? 
_exptl_crystal.size_max                     ? 
_exptl_crystal.size_mid                     ? 
_exptl_crystal.size_min                     ? 
_exptl_crystal.size_rad                     ? 
_exptl_crystal.colour_lustre                ? 
_exptl_crystal.colour_modifier              ? 
_exptl_crystal.colour_primary               ? 
_exptl_crystal.density_meas                 ? 
_exptl_crystal.density_meas_esd             ? 
_exptl_crystal.density_meas_gt              ? 
_exptl_crystal.density_meas_lt              ? 
_exptl_crystal.density_meas_temp            ? 
_exptl_crystal.density_meas_temp_esd        ? 
_exptl_crystal.density_meas_temp_gt         ? 
_exptl_crystal.density_meas_temp_lt         ? 
_exptl_crystal.pdbx_crystal_image_url       ? 
_exptl_crystal.pdbx_crystal_image_format    ? 
_exptl_crystal.pdbx_mosaicity               ? 
_exptl_crystal.pdbx_mosaicity_esd           ? 
_exptl_crystal.pdbx_mosaic_method           ? 
_exptl_crystal.pdbx_mosaic_block_size       ? 
_exptl_crystal.pdbx_mosaic_block_size_esd   ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, SITTING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              ? 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    
;8 %v/v 1-Propan 
0.1 M MES pH 6.5
12 %w/v PEG MME 5K
;
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            293 
# 
_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 16M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2024-06-25 
_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   0.885603 
_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                        'ESRF BEAMLINE ID23-1' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.885603 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   ID23-1 
_diffrn_source.pdbx_synchrotron_site       ESRF 
# 
_reflns.B_iso_Wilson_estimate                          18.94 
_reflns.entry_id                                       9G4M 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.41 
_reflns.d_resolution_low                               72.87 
_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                                     68084 
_reflns.observed_criterion                             ? 
_reflns.observed_criterion_F_max                       ? 
_reflns.observed_criterion_F_min                       ? 
_reflns.observed_criterion_I_max                       ? 
_reflns.observed_criterion_I_min                       ? 
_reflns.observed_criterion_sigma_F                     ? 
_reflns.observed_criterion_sigma_I                     ? 
_reflns.percent_possible_obs                           99.9 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                10.36 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          8.97 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               ? 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                ? 
_reflns.pdbx_Rpim_I_all                                ? 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.997 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.093 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
_reflns_shell.d_res_high                                    1.41 
_reflns_shell.d_res_low                                     1.50 
_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                             11347 
_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                                  0.552 
_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                                  0.99 
_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                               28.38 
_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                                 9G4M 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            1.41 
_refine.ls_d_res_low                             36.16 
_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                     67897 
_refine.ls_number_reflns_R_free                  3323 
_refine.ls_number_reflns_R_work                  64574 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.63 
_refine.ls_percent_reflns_R_free                 4.89 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1586 
_refine.ls_R_factor_R_free                       0.1846 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1573 
_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                          1.33 
_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       'GeoStd + Monomer Library + CDL v1.2' 
_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             1.1000 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.9000 
_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                 22.7821 
_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                            0.1793 
_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                       1.41 
_refine_hist.d_res_low                        36.16 
_refine_hist.number_atoms_solvent             210 
_refine_hist.number_atoms_total               2535 
_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        2244 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         81 
_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' ? 0.0054  ? 2453 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 0.8378  ? 3348 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 0.0765  ? 376  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.0070  ? 452  ? f_plane_restr      ? ? 
'X-RAY DIFFRACTION' ? 13.8513 ? 950  ? f_dihedral_angle_d ? ? 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_obs 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.redundancy_reflns_all 
_refine_ls_shell.redundancy_reflns_obs 
_refine_ls_shell.wR_factor_all 
_refine_ls_shell.wR_factor_obs 
_refine_ls_shell.wR_factor_R_free 
_refine_ls_shell.wR_factor_R_work 
_refine_ls_shell.pdbx_R_complete 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.pdbx_phase_error 
_refine_ls_shell.pdbx_fsc_work 
_refine_ls_shell.pdbx_fsc_free 
_refine_ls_shell.R_factor_R_free 
'X-RAY DIFFRACTION' 1.41 1.43  . . 143 2609 98.64  . . . . 0.3684 . . . . . . . . . . . 0.3647 
'X-RAY DIFFRACTION' 1.43 1.45  . . 123 2663 99.11  . . . . 0.3421 . . . . . . . . . . . 0.3999 
'X-RAY DIFFRACTION' 1.45 1.47  . . 133 2632 98.89  . . . . 0.3264 . . . . . . . . . . . 0.3909 
'X-RAY DIFFRACTION' 1.47 1.50  . . 130 2679 99.19  . . . . 0.2997 . . . . . . . . . . . 0.2901 
'X-RAY DIFFRACTION' 1.50 1.52  . . 137 2654 99.22  . . . . 0.2799 . . . . . . . . . . . 0.3080 
'X-RAY DIFFRACTION' 1.52 1.55  . . 128 2672 99.47  . . . . 0.2612 . . . . . . . . . . . 0.2935 
'X-RAY DIFFRACTION' 1.55 1.58  . . 130 2668 99.43  . . . . 0.2443 . . . . . . . . . . . 0.2640 
'X-RAY DIFFRACTION' 1.58 1.61  . . 149 2629 99.43  . . . . 0.2269 . . . . . . . . . . . 0.2686 
'X-RAY DIFFRACTION' 1.61 1.65  . . 125 2706 99.86  . . . . 0.2235 . . . . . . . . . . . 0.2809 
'X-RAY DIFFRACTION' 1.65 1.69  . . 148 2678 99.68  . . . . 0.2100 . . . . . . . . . . . 0.2728 
'X-RAY DIFFRACTION' 1.69 1.73  . . 147 2648 99.79  . . . . 0.1876 . . . . . . . . . . . 0.2186 
'X-RAY DIFFRACTION' 1.73 1.78  . . 144 2675 99.68  . . . . 0.1621 . . . . . . . . . . . 0.1935 
'X-RAY DIFFRACTION' 1.78 1.83  . . 136 2660 99.89  . . . . 0.1528 . . . . . . . . . . . 0.1952 
'X-RAY DIFFRACTION' 1.83 1.89  . . 131 2727 99.90  . . . . 0.1413 . . . . . . . . . . . 0.1997 
'X-RAY DIFFRACTION' 1.89 1.96  . . 144 2657 99.57  . . . . 0.1350 . . . . . . . . . . . 0.1824 
'X-RAY DIFFRACTION' 1.96 2.03  . . 146 2687 99.93  . . . . 0.1281 . . . . . . . . . . . 0.1676 
'X-RAY DIFFRACTION' 2.03 2.13  . . 130 2700 99.82  . . . . 0.1194 . . . . . . . . . . . 0.1420 
'X-RAY DIFFRACTION' 2.13 2.24  . . 146 2674 99.89  . . . . 0.1227 . . . . . . . . . . . 0.1524 
'X-RAY DIFFRACTION' 2.24 2.38  . . 145 2716 99.83  . . . . 0.1242 . . . . . . . . . . . 0.1631 
'X-RAY DIFFRACTION' 2.38 2.56  . . 160 2690 100.00 . . . . 0.1353 . . . . . . . . . . . 0.1526 
'X-RAY DIFFRACTION' 2.56 2.82  . . 139 2734 99.97  . . . . 0.1346 . . . . . . . . . . . 0.1663 
'X-RAY DIFFRACTION' 2.82 3.23  . . 137 2755 100.00 . . . . 0.1412 . . . . . . . . . . . 0.1707 
'X-RAY DIFFRACTION' 3.23 4.07  . . 132 2773 99.86  . . . . 0.1388 . . . . . . . . . . . 0.1570 
'X-RAY DIFFRACTION' 4.07 36.16 . . 140 2888 99.90  . . . . 0.1628 . . . . . . . . . . . 0.1728 
# 
_struct.entry_id                     9G4M 
_struct.title                        'Crystal structure of monoacylglycerol lipase with BODIPY labeled probe' 
_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        9G4M 
_struct_keywords.text            'Hydrolase, Serine Esterase' 
_struct_keywords.pdbx_keywords   HYDROLASE 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 2 ? 
C N N 3 ? 
D N N 3 ? 
E N N 3 ? 
F N N 3 ? 
G N N 3 ? 
H N N 3 ? 
I N N 3 ? 
J N N 3 ? 
K N N 4 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    MGLL_HUMAN 
_struct_ref.pdbx_db_accession          Q99685 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;MPEESSPRRTPQSIPYQDLPHLVNADGQYLFCRYWKPTGTPKALIFVSHGAGEHSGRYEELARMLMGLDLLVFAHDHVGH
GQSEGERMVVSDFHVFVRDVLQHVDSMQKDYPGLPVFLLGHSMGGAIAILTAAERPGHFAGMVLISPLVLANPESATTFK
VLAAKVLNLVLPNLSLGPIDSSVLSRNKTEVDIYNSDPLICRAGLKVCFGIQLLNAVSRVERALPKLTVPFLLLQGSADR
LCDSKGAYLLMELAKSQDKTLKIYEGAYHVLHKELPEVTNSVFHEINMWVSQRTATAGTASPP
;
_struct_ref.pdbx_align_begin           1 
# 
_struct_ref_seq.align_id                      1 
_struct_ref_seq.ref_id                        1 
_struct_ref_seq.pdbx_PDB_id_code              9G4M 
_struct_ref_seq.pdbx_strand_id                A 
_struct_ref_seq.seq_align_beg                 21 
_struct_ref_seq.pdbx_seq_align_beg_ins_code   ? 
_struct_ref_seq.seq_align_end                 323 
_struct_ref_seq.pdbx_seq_align_end_ins_code   ? 
_struct_ref_seq.pdbx_db_accession             Q99685 
_struct_ref_seq.db_align_beg                  1 
_struct_ref_seq.pdbx_db_align_beg_ins_code    ? 
_struct_ref_seq.db_align_end                  303 
_struct_ref_seq.pdbx_db_align_end_ins_code    ? 
_struct_ref_seq.pdbx_auth_seq_align_beg       1 
_struct_ref_seq.pdbx_auth_seq_align_end       303 
# 
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 9G4M MET A 1   ? UNP Q99685 ?   ?   'initiating methionine' -19 1  
1 9G4M GLY A 2   ? UNP Q99685 ?   ?   'expression tag'        -18 2  
1 9G4M SER A 3   ? UNP Q99685 ?   ?   'expression tag'        -17 3  
1 9G4M SER A 4   ? UNP Q99685 ?   ?   'expression tag'        -16 4  
1 9G4M HIS A 5   ? UNP Q99685 ?   ?   'expression tag'        -15 5  
1 9G4M HIS A 6   ? UNP Q99685 ?   ?   'expression tag'        -14 6  
1 9G4M HIS A 7   ? UNP Q99685 ?   ?   'expression tag'        -13 7  
1 9G4M HIS A 8   ? UNP Q99685 ?   ?   'expression tag'        -12 8  
1 9G4M HIS A 9   ? UNP Q99685 ?   ?   'expression tag'        -11 9  
1 9G4M HIS A 10  ? UNP Q99685 ?   ?   'expression tag'        -10 10 
1 9G4M SER A 11  ? UNP Q99685 ?   ?   'expression tag'        -9  11 
1 9G4M SER A 12  ? UNP Q99685 ?   ?   'expression tag'        -8  12 
1 9G4M GLY A 13  ? UNP Q99685 ?   ?   'expression tag'        -7  13 
1 9G4M GLU A 14  ? UNP Q99685 ?   ?   'expression tag'        -6  14 
1 9G4M ASN A 15  ? UNP Q99685 ?   ?   'expression tag'        -5  15 
1 9G4M LEU A 16  ? UNP Q99685 ?   ?   'expression tag'        -4  16 
1 9G4M TYR A 17  ? UNP Q99685 ?   ?   'expression tag'        -3  17 
1 9G4M PHE A 18  ? UNP Q99685 ?   ?   'expression tag'        -2  18 
1 9G4M GLN A 19  ? UNP Q99685 ?   ?   'expression tag'        -1  19 
1 9G4M GLY A 20  ? UNP Q99685 ?   ?   'expression tag'        0   20 
1 9G4M ALA A 56  ? UNP Q99685 LYS 36  'engineered mutation'   36  21 
1 9G4M SER A 189 ? UNP Q99685 LEU 169 'engineered mutation'   169 22 
1 9G4M SER A 196 ? UNP Q99685 LEU 176 'engineered mutation'   176 23 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_and_software_defined_assembly 
_pdbx_struct_assembly.method_details       PISA 
_pdbx_struct_assembly.oligomeric_details   monomeric 
_pdbx_struct_assembly.oligomeric_count     1 
# 
loop_
_pdbx_struct_assembly_prop.biol_id 
_pdbx_struct_assembly_prop.type 
_pdbx_struct_assembly_prop.value 
_pdbx_struct_assembly_prop.details 
1 'ABSA (A^2)' 1530  ? 
1 MORE         22    ? 
1 'SSA (A^2)'  11880 ? 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F,G,H,I,J,K 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   'gel filtration' 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 PRO A 35  ? LEU A 39  ? PRO A 15  LEU A 19  5 ? 5  
HELX_P HELX_P2  AA2 HIS A 74  ? ARG A 77  ? HIS A 54  ARG A 57  5 ? 4  
HELX_P HELX_P3  AA3 TYR A 78  ? LEU A 88  ? TYR A 58  LEU A 68  1 ? 11 
HELX_P HELX_P4  AA4 PHE A 113 ? TYR A 131 ? PHE A 93  TYR A 111 1 ? 19 
HELX_P HELX_P5  AA5 SER A 142 ? ARG A 155 ? SER A 122 ARG A 135 1 ? 14 
HELX_P HELX_P6  AA6 ASN A 172 ? SER A 189 ? ASN A 152 SER A 169 1 ? 18 
HELX_P HELX_P7  AA7 ASP A 200 ? LEU A 204 ? ASP A 180 LEU A 184 5 ? 5  
HELX_P HELX_P8  AA8 ASN A 207 ? ASP A 217 ? ASN A 187 ASP A 197 1 ? 11 
HELX_P HELX_P9  AA9 LYS A 226 ? LEU A 244 ? LYS A 206 LEU A 224 1 ? 19 
HELX_P HELX_P10 AB1 PRO A 245 ? LEU A 247 ? PRO A 225 LEU A 227 5 ? 3  
HELX_P HELX_P11 AB2 ASP A 263 ? ALA A 274 ? ASP A 243 ALA A 254 1 ? 12 
HELX_P HELX_P12 AB3 VAL A 290 ? GLU A 294 ? VAL A 270 GLU A 274 5 ? 5  
HELX_P HELX_P13 AB4 LEU A 295 ? ALA A 315 ? LEU A 275 ALA A 295 1 ? 21 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
_struct_sheet.id               AA1 
_struct_sheet.type             ? 
_struct_sheet.number_strands   8 
_struct_sheet.details          ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? anti-parallel 
AA1 3 4 ? parallel      
AA1 4 5 ? parallel      
AA1 5 6 ? parallel      
AA1 6 7 ? parallel      
AA1 7 8 ? 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 HIS A 41  ? VAL A 43  ? HIS A 21  VAL A 23  
AA1 2 TYR A 49  ? TRP A 55  ? TYR A 29  TRP A 35  
AA1 3 LEU A 90  ? HIS A 95  ? LEU A 70  HIS A 75  
AA1 4 ALA A 63  ? SER A 68  ? ALA A 43  SER A 48  
AA1 5 VAL A 136 ? HIS A 141 ? VAL A 116 HIS A 121 
AA1 6 GLY A 161 ? ILE A 165 ? GLY A 141 ILE A 145 
AA1 7 PHE A 251 ? GLY A 256 ? PHE A 231 GLY A 236 
AA1 8 LYS A 279 ? TYR A 284 ? LYS A 259 TYR A 264 
# 
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 42  ? N LEU A 22  O LEU A 50  ? O LEU A 30  
AA1 2 3 N TRP A 55  ? N TRP A 35  O VAL A 92  ? O VAL A 72  
AA1 3 4 O LEU A 91  ? O LEU A 71  N ALA A 63  ? N ALA A 43  
AA1 4 5 N SER A 68  ? N SER A 48  O LEU A 139 ? O LEU A 119 
AA1 5 6 N LEU A 138 ? N LEU A 118 O VAL A 163 ? O VAL A 143 
AA1 6 7 N LEU A 164 ? N LEU A 144 O LEU A 252 ? O LEU A 232 
AA1 7 8 N LEU A 253 ? N LEU A 233 O THR A 280 ? O THR A 260 
# 
_pdbx_entry_details.entry_id                   9G4M 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_pdbx_validate_close_contact.id 
_pdbx_validate_close_contact.PDB_model_num 
_pdbx_validate_close_contact.auth_atom_id_1 
_pdbx_validate_close_contact.auth_asym_id_1 
_pdbx_validate_close_contact.auth_comp_id_1 
_pdbx_validate_close_contact.auth_seq_id_1 
_pdbx_validate_close_contact.PDB_ins_code_1 
_pdbx_validate_close_contact.label_alt_id_1 
_pdbx_validate_close_contact.auth_atom_id_2 
_pdbx_validate_close_contact.auth_asym_id_2 
_pdbx_validate_close_contact.auth_comp_id_2 
_pdbx_validate_close_contact.auth_seq_id_2 
_pdbx_validate_close_contact.PDB_ins_code_2 
_pdbx_validate_close_contact.label_alt_id_2 
_pdbx_validate_close_contact.dist 
1 1 O A HOH 508 ? ? O A HOH 694 ? ? 2.18 
2 1 O A HOH 617 ? ? O A HOH 686 ? ? 2.18 
3 1 O A HOH 512 ? ? O A HOH 680 ? ? 2.19 
# 
loop_
_pdbx_validate_symm_contact.id 
_pdbx_validate_symm_contact.PDB_model_num 
_pdbx_validate_symm_contact.auth_atom_id_1 
_pdbx_validate_symm_contact.auth_asym_id_1 
_pdbx_validate_symm_contact.auth_comp_id_1 
_pdbx_validate_symm_contact.auth_seq_id_1 
_pdbx_validate_symm_contact.PDB_ins_code_1 
_pdbx_validate_symm_contact.label_alt_id_1 
_pdbx_validate_symm_contact.site_symmetry_1 
_pdbx_validate_symm_contact.auth_atom_id_2 
_pdbx_validate_symm_contact.auth_asym_id_2 
_pdbx_validate_symm_contact.auth_comp_id_2 
_pdbx_validate_symm_contact.auth_seq_id_2 
_pdbx_validate_symm_contact.PDB_ins_code_2 
_pdbx_validate_symm_contact.label_alt_id_2 
_pdbx_validate_symm_contact.site_symmetry_2 
_pdbx_validate_symm_contact.dist 
1 1 O A HOH 647 ? ? 1_555 O A HOH 663 ? ? 6_555 2.11 
2 1 O A HOH 638 ? ? 1_555 O A HOH 667 ? ? 6_555 2.13 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 GLU A 53  ? ? -98.72  -153.41 
2 1 SER A 122 ? ? 61.09   -124.07 
3 1 SER A 176 ? ? -116.67 -162.06 
4 1 TYR A 268 ? ? -88.12  -155.22 
5 1 GLU A 274 ? ? -102.49 -161.38 
# 
loop_
_space_group_symop.id 
_space_group_symop.operation_xyz 
1 x,y,z               
2 x,-y,-z             
3 -x,y,-z+1/2         
4 -x,-y,z+1/2         
5 x+1/2,y+1/2,z       
6 x+1/2,-y+1/2,-z     
7 -x+1/2,y+1/2,-z+1/2 
8 -x+1/2,-y+1/2,z+1/2 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1  1 Y 1 A MET -19 ? A MET 1   
2  1 Y 1 A GLY -18 ? A GLY 2   
3  1 Y 1 A SER -17 ? A SER 3   
4  1 Y 1 A SER -16 ? A SER 4   
5  1 Y 1 A HIS -15 ? A HIS 5   
6  1 Y 1 A HIS -14 ? A HIS 6   
7  1 Y 1 A HIS -13 ? A HIS 7   
8  1 Y 1 A HIS -12 ? A HIS 8   
9  1 Y 1 A HIS -11 ? A HIS 9   
10 1 Y 1 A HIS -10 ? A HIS 10  
11 1 Y 1 A SER -9  ? A SER 11  
12 1 Y 1 A SER -8  ? A SER 12  
13 1 Y 1 A GLY -7  ? A GLY 13  
14 1 Y 1 A GLU -6  ? A GLU 14  
15 1 Y 1 A ASN -5  ? A ASN 15  
16 1 Y 1 A LEU -4  ? A LEU 16  
17 1 Y 1 A TYR -3  ? A TYR 17  
18 1 Y 1 A PHE -2  ? A PHE 18  
19 1 Y 1 A GLN -1  ? A GLN 19  
20 1 Y 1 A GLY 0   ? A GLY 20  
21 1 Y 1 A MET 1   ? A MET 21  
22 1 Y 1 A PRO 2   ? A PRO 22  
23 1 Y 1 A GLU 3   ? A GLU 23  
24 1 Y 1 A GLU 4   ? A GLU 24  
25 1 Y 1 A SER 5   ? A SER 25  
26 1 Y 1 A THR 296 ? A THR 316 
27 1 Y 1 A ALA 297 ? A ALA 317 
28 1 Y 1 A GLY 298 ? A GLY 318 
29 1 Y 1 A THR 299 ? A THR 319 
30 1 Y 1 A ALA 300 ? A ALA 320 
31 1 Y 1 A SER 301 ? A SER 321 
32 1 Y 1 A PRO 302 ? A PRO 322 
33 1 Y 1 A PRO 303 ? A PRO 323 
# 
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 
A1IIH N1   N N N 1   
A1IIH C7   C Y N 2   
A1IIH C8   C Y N 3   
A1IIH N2   N N N 4   
A1IIH C9   C Y N 5   
A1IIH O1   O N N 6   
A1IIH C1   C N N 7   
A1IIH C5   C N N 8   
A1IIH C6   C Y N 9   
A1IIH N3   N N N 10  
A1IIH C4   C N N 11  
A1IIH O4   O N N 12  
A1IIH C3   C N N 13  
A1IIH O3   O N N 14  
A1IIH C2   C N N 15  
A1IIH N4   N N N 16  
A1IIH N    N N N 17  
A1IIH C    C N N 18  
A1IIH O    O N N 19  
A1IIH B    B N N 20  
A1IIH C10  C N N 21  
A1IIH C11  C N N 22  
A1IIH C12  C N N 23  
A1IIH C13  C N N 24  
A1IIH C14  C N N 25  
A1IIH C15  C Y N 26  
A1IIH C16  C Y N 27  
A1IIH C17  C Y N 28  
A1IIH C18  C Y N 29  
A1IIH C19  C Y N 30  
A1IIH C20  C Y N 31  
A1IIH C21  C N N 32  
A1IIH C22  C N N 33  
A1IIH C23  C N N 34  
A1IIH C24  C N N 35  
A1IIH C25  C N N 36  
A1IIH C26  C N N 37  
A1IIH C27  C N N 38  
A1IIH C28  C N N 39  
A1IIH C29  C N N 40  
A1IIH C30  C N N 41  
A1IIH C31  C N N 42  
A1IIH C32  C N N 43  
A1IIH C33  C N N 44  
A1IIH C34  C N N 45  
A1IIH F    F N N 46  
A1IIH F1   F N N 47  
A1IIH N5   N Y N 48  
A1IIH O2   O N N 49  
A1IIH H11  H N N 50  
A1IIH H5   H N N 51  
A1IIH H6   H N N 52  
A1IIH H4   H N N 53  
A1IIH H3   H N N 54  
A1IIH H35  H N N 55  
A1IIH H2   H N N 56  
A1IIH H    H N N 57  
A1IIH H1   H N N 58  
A1IIH H7   H N N 59  
A1IIH H8   H N N 60  
A1IIH H10  H N N 61  
A1IIH H9   H N N 62  
A1IIH H12  H N N 63  
A1IIH H13  H N N 64  
A1IIH H14  H N N 65  
A1IIH H15  H N N 66  
A1IIH H16  H N N 67  
A1IIH H17  H N N 68  
A1IIH H18  H N N 69  
A1IIH H19  H N N 70  
A1IIH H20  H N N 71  
A1IIH H21  H N N 72  
A1IIH H22  H N N 73  
A1IIH H23  H N N 74  
A1IIH H24  H N N 75  
A1IIH H26  H N N 76  
A1IIH H25  H N N 77  
A1IIH H27  H N N 78  
A1IIH H28  H N N 79  
A1IIH H29  H N N 80  
A1IIH H30  H N N 81  
A1IIH H32  H N N 82  
A1IIH H31  H N N 83  
A1IIH H34  H N N 84  
A1IIH H33  H N N 85  
A1IIH H37  H N N 86  
A1IIH H36  H N N 87  
A1IIH H40  H N N 88  
A1IIH H39  H N N 89  
A1IIH H38  H N N 90  
ALA   N    N N N 91  
ALA   CA   C N S 92  
ALA   C    C N N 93  
ALA   O    O N N 94  
ALA   CB   C N N 95  
ALA   OXT  O N N 96  
ALA   H    H N N 97  
ALA   H2   H N N 98  
ALA   HA   H N N 99  
ALA   HB1  H N N 100 
ALA   HB2  H N N 101 
ALA   HB3  H N N 102 
ALA   HXT  H N N 103 
ARG   N    N N N 104 
ARG   CA   C N S 105 
ARG   C    C N N 106 
ARG   O    O N N 107 
ARG   CB   C N N 108 
ARG   CG   C N N 109 
ARG   CD   C N N 110 
ARG   NE   N N N 111 
ARG   CZ   C N N 112 
ARG   NH1  N N N 113 
ARG   NH2  N N N 114 
ARG   OXT  O N N 115 
ARG   H    H N N 116 
ARG   H2   H N N 117 
ARG   HA   H N N 118 
ARG   HB2  H N N 119 
ARG   HB3  H N N 120 
ARG   HG2  H N N 121 
ARG   HG3  H N N 122 
ARG   HD2  H N N 123 
ARG   HD3  H N N 124 
ARG   HE   H N N 125 
ARG   HH11 H N N 126 
ARG   HH12 H N N 127 
ARG   HH21 H N N 128 
ARG   HH22 H N N 129 
ARG   HXT  H N N 130 
ASN   N    N N N 131 
ASN   CA   C N S 132 
ASN   C    C N N 133 
ASN   O    O N N 134 
ASN   CB   C N N 135 
ASN   CG   C N N 136 
ASN   OD1  O N N 137 
ASN   ND2  N N N 138 
ASN   OXT  O N N 139 
ASN   H    H N N 140 
ASN   H2   H N N 141 
ASN   HA   H N N 142 
ASN   HB2  H N N 143 
ASN   HB3  H N N 144 
ASN   HD21 H N N 145 
ASN   HD22 H N N 146 
ASN   HXT  H N N 147 
ASP   N    N N N 148 
ASP   CA   C N S 149 
ASP   C    C N N 150 
ASP   O    O N N 151 
ASP   CB   C N N 152 
ASP   CG   C N N 153 
ASP   OD1  O N N 154 
ASP   OD2  O N N 155 
ASP   OXT  O N N 156 
ASP   H    H N N 157 
ASP   H2   H N N 158 
ASP   HA   H N N 159 
ASP   HB2  H N N 160 
ASP   HB3  H N N 161 
ASP   HD2  H N N 162 
ASP   HXT  H N N 163 
CYS   N    N N N 164 
CYS   CA   C N R 165 
CYS   C    C N N 166 
CYS   O    O N N 167 
CYS   CB   C N N 168 
CYS   SG   S N N 169 
CYS   OXT  O N N 170 
CYS   H    H N N 171 
CYS   H2   H N N 172 
CYS   HA   H N N 173 
CYS   HB2  H N N 174 
CYS   HB3  H N N 175 
CYS   HG   H N N 176 
CYS   HXT  H N N 177 
EDO   C1   C N N 178 
EDO   O1   O N N 179 
EDO   C2   C N N 180 
EDO   O2   O N N 181 
EDO   H11  H N N 182 
EDO   H12  H N N 183 
EDO   HO1  H N N 184 
EDO   H21  H N N 185 
EDO   H22  H N N 186 
EDO   HO2  H N N 187 
GLN   N    N N N 188 
GLN   CA   C N S 189 
GLN   C    C N N 190 
GLN   O    O N N 191 
GLN   CB   C N N 192 
GLN   CG   C N N 193 
GLN   CD   C N N 194 
GLN   OE1  O N N 195 
GLN   NE2  N N N 196 
GLN   OXT  O N N 197 
GLN   H    H N N 198 
GLN   H2   H N N 199 
GLN   HA   H N N 200 
GLN   HB2  H N N 201 
GLN   HB3  H N N 202 
GLN   HG2  H N N 203 
GLN   HG3  H N N 204 
GLN   HE21 H N N 205 
GLN   HE22 H N N 206 
GLN   HXT  H N N 207 
GLU   N    N N N 208 
GLU   CA   C N S 209 
GLU   C    C N N 210 
GLU   O    O N N 211 
GLU   CB   C N N 212 
GLU   CG   C N N 213 
GLU   CD   C N N 214 
GLU   OE1  O N N 215 
GLU   OE2  O N N 216 
GLU   OXT  O N N 217 
GLU   H    H N N 218 
GLU   H2   H N N 219 
GLU   HA   H N N 220 
GLU   HB2  H N N 221 
GLU   HB3  H N N 222 
GLU   HG2  H N N 223 
GLU   HG3  H N N 224 
GLU   HE2  H N N 225 
GLU   HXT  H N N 226 
GLY   N    N N N 227 
GLY   CA   C N N 228 
GLY   C    C N N 229 
GLY   O    O N N 230 
GLY   OXT  O N N 231 
GLY   H    H N N 232 
GLY   H2   H N N 233 
GLY   HA2  H N N 234 
GLY   HA3  H N N 235 
GLY   HXT  H N N 236 
HIS   N    N N N 237 
HIS   CA   C N S 238 
HIS   C    C N N 239 
HIS   O    O N N 240 
HIS   CB   C N N 241 
HIS   CG   C Y N 242 
HIS   ND1  N Y N 243 
HIS   CD2  C Y N 244 
HIS   CE1  C Y N 245 
HIS   NE2  N Y N 246 
HIS   OXT  O N N 247 
HIS   H    H N N 248 
HIS   H2   H N N 249 
HIS   HA   H N N 250 
HIS   HB2  H N N 251 
HIS   HB3  H N N 252 
HIS   HD1  H N N 253 
HIS   HD2  H N N 254 
HIS   HE1  H N N 255 
HIS   HE2  H N N 256 
HIS   HXT  H N N 257 
HOH   O    O N N 258 
HOH   H1   H N N 259 
HOH   H2   H N N 260 
ILE   N    N N N 261 
ILE   CA   C N S 262 
ILE   C    C N N 263 
ILE   O    O N N 264 
ILE   CB   C N S 265 
ILE   CG1  C N N 266 
ILE   CG2  C N N 267 
ILE   CD1  C N N 268 
ILE   OXT  O N N 269 
ILE   H    H N N 270 
ILE   H2   H N N 271 
ILE   HA   H N N 272 
ILE   HB   H N N 273 
ILE   HG12 H N N 274 
ILE   HG13 H N N 275 
ILE   HG21 H N N 276 
ILE   HG22 H N N 277 
ILE   HG23 H N N 278 
ILE   HD11 H N N 279 
ILE   HD12 H N N 280 
ILE   HD13 H N N 281 
ILE   HXT  H N N 282 
LEU   N    N N N 283 
LEU   CA   C N S 284 
LEU   C    C N N 285 
LEU   O    O N N 286 
LEU   CB   C N N 287 
LEU   CG   C N N 288 
LEU   CD1  C N N 289 
LEU   CD2  C N N 290 
LEU   OXT  O N N 291 
LEU   H    H N N 292 
LEU   H2   H N N 293 
LEU   HA   H N N 294 
LEU   HB2  H N N 295 
LEU   HB3  H N N 296 
LEU   HG   H N N 297 
LEU   HD11 H N N 298 
LEU   HD12 H N N 299 
LEU   HD13 H N N 300 
LEU   HD21 H N N 301 
LEU   HD22 H N N 302 
LEU   HD23 H N N 303 
LEU   HXT  H N N 304 
LYS   N    N N N 305 
LYS   CA   C N S 306 
LYS   C    C N N 307 
LYS   O    O N N 308 
LYS   CB   C N N 309 
LYS   CG   C N N 310 
LYS   CD   C N N 311 
LYS   CE   C N N 312 
LYS   NZ   N N N 313 
LYS   OXT  O N N 314 
LYS   H    H N N 315 
LYS   H2   H N N 316 
LYS   HA   H N N 317 
LYS   HB2  H N N 318 
LYS   HB3  H N N 319 
LYS   HG2  H N N 320 
LYS   HG3  H N N 321 
LYS   HD2  H N N 322 
LYS   HD3  H N N 323 
LYS   HE2  H N N 324 
LYS   HE3  H N N 325 
LYS   HZ1  H N N 326 
LYS   HZ2  H N N 327 
LYS   HZ3  H N N 328 
LYS   HXT  H N N 329 
MET   N    N N N 330 
MET   CA   C N S 331 
MET   C    C N N 332 
MET   O    O N N 333 
MET   CB   C N N 334 
MET   CG   C N N 335 
MET   SD   S N N 336 
MET   CE   C N N 337 
MET   OXT  O N N 338 
MET   H    H N N 339 
MET   H2   H N N 340 
MET   HA   H N N 341 
MET   HB2  H N N 342 
MET   HB3  H N N 343 
MET   HG2  H N N 344 
MET   HG3  H N N 345 
MET   HE1  H N N 346 
MET   HE2  H N N 347 
MET   HE3  H N N 348 
MET   HXT  H N N 349 
PHE   N    N N N 350 
PHE   CA   C N S 351 
PHE   C    C N N 352 
PHE   O    O N N 353 
PHE   CB   C N N 354 
PHE   CG   C Y N 355 
PHE   CD1  C Y N 356 
PHE   CD2  C Y N 357 
PHE   CE1  C Y N 358 
PHE   CE2  C Y N 359 
PHE   CZ   C Y N 360 
PHE   OXT  O N N 361 
PHE   H    H N N 362 
PHE   H2   H N N 363 
PHE   HA   H N N 364 
PHE   HB2  H N N 365 
PHE   HB3  H N N 366 
PHE   HD1  H N N 367 
PHE   HD2  H N N 368 
PHE   HE1  H N N 369 
PHE   HE2  H N N 370 
PHE   HZ   H N N 371 
PHE   HXT  H N N 372 
PRO   N    N N N 373 
PRO   CA   C N S 374 
PRO   C    C N N 375 
PRO   O    O N N 376 
PRO   CB   C N N 377 
PRO   CG   C N N 378 
PRO   CD   C N N 379 
PRO   OXT  O N N 380 
PRO   H    H N N 381 
PRO   HA   H N N 382 
PRO   HB2  H N N 383 
PRO   HB3  H N N 384 
PRO   HG2  H N N 385 
PRO   HG3  H N N 386 
PRO   HD2  H N N 387 
PRO   HD3  H N N 388 
PRO   HXT  H N N 389 
SER   N    N N N 390 
SER   CA   C N S 391 
SER   C    C N N 392 
SER   O    O N N 393 
SER   CB   C N N 394 
SER   OG   O N N 395 
SER   OXT  O N N 396 
SER   H    H N N 397 
SER   H2   H N N 398 
SER   HA   H N N 399 
SER   HB2  H N N 400 
SER   HB3  H N N 401 
SER   HG   H N N 402 
SER   HXT  H N N 403 
THR   N    N N N 404 
THR   CA   C N S 405 
THR   C    C N N 406 
THR   O    O N N 407 
THR   CB   C N R 408 
THR   OG1  O N N 409 
THR   CG2  C N N 410 
THR   OXT  O N N 411 
THR   H    H N N 412 
THR   H2   H N N 413 
THR   HA   H N N 414 
THR   HB   H N N 415 
THR   HG1  H N N 416 
THR   HG21 H N N 417 
THR   HG22 H N N 418 
THR   HG23 H N N 419 
THR   HXT  H N N 420 
TRP   N    N N N 421 
TRP   CA   C N S 422 
TRP   C    C N N 423 
TRP   O    O N N 424 
TRP   CB   C N N 425 
TRP   CG   C Y N 426 
TRP   CD1  C Y N 427 
TRP   CD2  C Y N 428 
TRP   NE1  N Y N 429 
TRP   CE2  C Y N 430 
TRP   CE3  C Y N 431 
TRP   CZ2  C Y N 432 
TRP   CZ3  C Y N 433 
TRP   CH2  C Y N 434 
TRP   OXT  O N N 435 
TRP   H    H N N 436 
TRP   H2   H N N 437 
TRP   HA   H N N 438 
TRP   HB2  H N N 439 
TRP   HB3  H N N 440 
TRP   HD1  H N N 441 
TRP   HE1  H N N 442 
TRP   HE3  H N N 443 
TRP   HZ2  H N N 444 
TRP   HZ3  H N N 445 
TRP   HH2  H N N 446 
TRP   HXT  H N N 447 
TYR   N    N N N 448 
TYR   CA   C N S 449 
TYR   C    C N N 450 
TYR   O    O N N 451 
TYR   CB   C N N 452 
TYR   CG   C Y N 453 
TYR   CD1  C Y N 454 
TYR   CD2  C Y N 455 
TYR   CE1  C Y N 456 
TYR   CE2  C Y N 457 
TYR   CZ   C Y N 458 
TYR   OH   O N N 459 
TYR   OXT  O N N 460 
TYR   H    H N N 461 
TYR   H2   H N N 462 
TYR   HA   H N N 463 
TYR   HB2  H N N 464 
TYR   HB3  H N N 465 
TYR   HD1  H N N 466 
TYR   HD2  H N N 467 
TYR   HE1  H N N 468 
TYR   HE2  H N N 469 
TYR   HH   H N N 470 
TYR   HXT  H N N 471 
VAL   N    N N N 472 
VAL   CA   C N S 473 
VAL   C    C N N 474 
VAL   O    O N N 475 
VAL   CB   C N N 476 
VAL   CG1  C N N 477 
VAL   CG2  C N N 478 
VAL   OXT  O N N 479 
VAL   H    H N N 480 
VAL   H2   H N N 481 
VAL   HA   H N N 482 
VAL   HB   H N N 483 
VAL   HG11 H N N 484 
VAL   HG12 H N N 485 
VAL   HG13 H N N 486 
VAL   HG21 H N N 487 
VAL   HG22 H N N 488 
VAL   HG23 H N N 489 
VAL   HXT  H N N 490 
# 
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 
A1IIH C   C1   sing N N 1   
A1IIH C1  C2   doub N N 2   
A1IIH C2  C3   sing N N 3   
A1IIH C3  N    doub N N 4   
A1IIH N   C4   sing N N 5   
A1IIH C1  C4   sing N N 6   
A1IIH C4  C5   doub N N 7   
A1IIH C5  C6   sing N N 8   
A1IIH C6  C7   doub Y N 9   
A1IIH C7  C8   sing Y N 10  
A1IIH C8  C9   doub Y N 11  
A1IIH C10 C9   sing N N 12  
A1IIH C11 C10  sing N N 13  
A1IIH C12 C11  sing N N 14  
A1IIH O   C12  doub N N 15  
A1IIH N1  C12  sing N N 16  
A1IIH C13 N1   sing N N 17  
A1IIH C14 C13  sing N N 18  
A1IIH O1  C14  sing N N 19  
A1IIH C15 O1   sing N N 20  
A1IIH C15 C16  doub Y N 21  
A1IIH C16 C17  sing Y N 22  
A1IIH C17 C18  doub Y N 23  
A1IIH C18 C19  sing Y N 24  
A1IIH C19 C20  doub Y N 25  
A1IIH C20 C15  sing Y N 26  
A1IIH C21 C20  sing N N 27  
A1IIH C22 C21  sing N N 28  
A1IIH C22 C23  sing N N 29  
A1IIH C23 C24  sing N N 30  
A1IIH C24 C25  sing N N 31  
A1IIH C25 C22  sing N N 32  
A1IIH C24 C26  sing N N 33  
A1IIH C26 N2   sing N N 34  
A1IIH N2  C27  sing N N 35  
A1IIH C27 C24  sing N N 36  
A1IIH C28 N2   sing N N 37  
A1IIH O2  C28  doub N N 38  
A1IIH N3  C28  sing N N 39  
A1IIH N3  C29  sing N N 40  
A1IIH C29 C30  sing N N 41  
A1IIH C30 C31  sing N N 42  
A1IIH C31 O3   sing N N 43  
A1IIH O3  C32  sing N N 44  
A1IIH O4  C32  doub N N 45  
A1IIH C32 N4   sing N N 46  
A1IIH N4  C30  sing N N 47  
A1IIH C30 C33  sing N N 48  
A1IIH C33 N3   sing N N 49  
A1IIH C9  N5   sing Y N 50  
A1IIH C6  N5   sing Y N 51  
A1IIH N5  B    sing N N 52  
A1IIH N   B    sing N N 53  
A1IIH F   B    sing N N 54  
A1IIH B   F1   sing N N 55  
A1IIH C34 C3   sing N N 56  
A1IIH N1  H11  sing N N 57  
A1IIH C7  H5   sing N N 58  
A1IIH C8  H6   sing N N 59  
A1IIH C5  H4   sing N N 60  
A1IIH C2  H3   sing N N 61  
A1IIH N4  H35  sing N N 62  
A1IIH C   H2   sing N N 63  
A1IIH C   H    sing N N 64  
A1IIH C   H1   sing N N 65  
A1IIH C10 H7   sing N N 66  
A1IIH C10 H8   sing N N 67  
A1IIH C11 H10  sing N N 68  
A1IIH C11 H9   sing N N 69  
A1IIH C13 H12  sing N N 70  
A1IIH C13 H13  sing N N 71  
A1IIH C14 H14  sing N N 72  
A1IIH C14 H15  sing N N 73  
A1IIH C16 H16  sing N N 74  
A1IIH C17 H17  sing N N 75  
A1IIH C18 H18  sing N N 76  
A1IIH C19 H19  sing N N 77  
A1IIH C21 H20  sing N N 78  
A1IIH C21 H21  sing N N 79  
A1IIH C22 H22  sing N N 80  
A1IIH C23 H23  sing N N 81  
A1IIH C23 H24  sing N N 82  
A1IIH C25 H26  sing N N 83  
A1IIH C25 H25  sing N N 84  
A1IIH C26 H27  sing N N 85  
A1IIH C26 H28  sing N N 86  
A1IIH C27 H29  sing N N 87  
A1IIH C27 H30  sing N N 88  
A1IIH C29 H32  sing N N 89  
A1IIH C29 H31  sing N N 90  
A1IIH C31 H34  sing N N 91  
A1IIH C31 H33  sing N N 92  
A1IIH C33 H37  sing N N 93  
A1IIH C33 H36  sing N N 94  
A1IIH C34 H40  sing N N 95  
A1IIH C34 H39  sing N N 96  
A1IIH C34 H38  sing N N 97  
ALA   N   CA   sing N N 98  
ALA   N   H    sing N N 99  
ALA   N   H2   sing N N 100 
ALA   CA  C    sing N N 101 
ALA   CA  CB   sing N N 102 
ALA   CA  HA   sing N N 103 
ALA   C   O    doub N N 104 
ALA   C   OXT  sing N N 105 
ALA   CB  HB1  sing N N 106 
ALA   CB  HB2  sing N N 107 
ALA   CB  HB3  sing N N 108 
ALA   OXT HXT  sing N N 109 
ARG   N   CA   sing N N 110 
ARG   N   H    sing N N 111 
ARG   N   H2   sing N N 112 
ARG   CA  C    sing N N 113 
ARG   CA  CB   sing N N 114 
ARG   CA  HA   sing N N 115 
ARG   C   O    doub N N 116 
ARG   C   OXT  sing N N 117 
ARG   CB  CG   sing N N 118 
ARG   CB  HB2  sing N N 119 
ARG   CB  HB3  sing N N 120 
ARG   CG  CD   sing N N 121 
ARG   CG  HG2  sing N N 122 
ARG   CG  HG3  sing N N 123 
ARG   CD  NE   sing N N 124 
ARG   CD  HD2  sing N N 125 
ARG   CD  HD3  sing N N 126 
ARG   NE  CZ   sing N N 127 
ARG   NE  HE   sing N N 128 
ARG   CZ  NH1  sing N N 129 
ARG   CZ  NH2  doub N N 130 
ARG   NH1 HH11 sing N N 131 
ARG   NH1 HH12 sing N N 132 
ARG   NH2 HH21 sing N N 133 
ARG   NH2 HH22 sing N N 134 
ARG   OXT HXT  sing N N 135 
ASN   N   CA   sing N N 136 
ASN   N   H    sing N N 137 
ASN   N   H2   sing N N 138 
ASN   CA  C    sing N N 139 
ASN   CA  CB   sing N N 140 
ASN   CA  HA   sing N N 141 
ASN   C   O    doub N N 142 
ASN   C   OXT  sing N N 143 
ASN   CB  CG   sing N N 144 
ASN   CB  HB2  sing N N 145 
ASN   CB  HB3  sing N N 146 
ASN   CG  OD1  doub N N 147 
ASN   CG  ND2  sing N N 148 
ASN   ND2 HD21 sing N N 149 
ASN   ND2 HD22 sing N N 150 
ASN   OXT HXT  sing N N 151 
ASP   N   CA   sing N N 152 
ASP   N   H    sing N N 153 
ASP   N   H2   sing N N 154 
ASP   CA  C    sing N N 155 
ASP   CA  CB   sing N N 156 
ASP   CA  HA   sing N N 157 
ASP   C   O    doub N N 158 
ASP   C   OXT  sing N N 159 
ASP   CB  CG   sing N N 160 
ASP   CB  HB2  sing N N 161 
ASP   CB  HB3  sing N N 162 
ASP   CG  OD1  doub N N 163 
ASP   CG  OD2  sing N N 164 
ASP   OD2 HD2  sing N N 165 
ASP   OXT HXT  sing N N 166 
CYS   N   CA   sing N N 167 
CYS   N   H    sing N N 168 
CYS   N   H2   sing N N 169 
CYS   CA  C    sing N N 170 
CYS   CA  CB   sing N N 171 
CYS   CA  HA   sing N N 172 
CYS   C   O    doub N N 173 
CYS   C   OXT  sing N N 174 
CYS   CB  SG   sing N N 175 
CYS   CB  HB2  sing N N 176 
CYS   CB  HB3  sing N N 177 
CYS   SG  HG   sing N N 178 
CYS   OXT HXT  sing N N 179 
EDO   C1  O1   sing N N 180 
EDO   C1  C2   sing N N 181 
EDO   C1  H11  sing N N 182 
EDO   C1  H12  sing N N 183 
EDO   O1  HO1  sing N N 184 
EDO   C2  O2   sing N N 185 
EDO   C2  H21  sing N N 186 
EDO   C2  H22  sing N N 187 
EDO   O2  HO2  sing N N 188 
GLN   N   CA   sing N N 189 
GLN   N   H    sing N N 190 
GLN   N   H2   sing N N 191 
GLN   CA  C    sing N N 192 
GLN   CA  CB   sing N N 193 
GLN   CA  HA   sing N N 194 
GLN   C   O    doub N N 195 
GLN   C   OXT  sing N N 196 
GLN   CB  CG   sing N N 197 
GLN   CB  HB2  sing N N 198 
GLN   CB  HB3  sing N N 199 
GLN   CG  CD   sing N N 200 
GLN   CG  HG2  sing N N 201 
GLN   CG  HG3  sing N N 202 
GLN   CD  OE1  doub N N 203 
GLN   CD  NE2  sing N N 204 
GLN   NE2 HE21 sing N N 205 
GLN   NE2 HE22 sing N N 206 
GLN   OXT HXT  sing N N 207 
GLU   N   CA   sing N N 208 
GLU   N   H    sing N N 209 
GLU   N   H2   sing N N 210 
GLU   CA  C    sing N N 211 
GLU   CA  CB   sing N N 212 
GLU   CA  HA   sing N N 213 
GLU   C   O    doub N N 214 
GLU   C   OXT  sing N N 215 
GLU   CB  CG   sing N N 216 
GLU   CB  HB2  sing N N 217 
GLU   CB  HB3  sing N N 218 
GLU   CG  CD   sing N N 219 
GLU   CG  HG2  sing N N 220 
GLU   CG  HG3  sing N N 221 
GLU   CD  OE1  doub N N 222 
GLU   CD  OE2  sing N N 223 
GLU   OE2 HE2  sing N N 224 
GLU   OXT HXT  sing N N 225 
GLY   N   CA   sing N N 226 
GLY   N   H    sing N N 227 
GLY   N   H2   sing N N 228 
GLY   CA  C    sing N N 229 
GLY   CA  HA2  sing N N 230 
GLY   CA  HA3  sing N N 231 
GLY   C   O    doub N N 232 
GLY   C   OXT  sing N N 233 
GLY   OXT HXT  sing N N 234 
HIS   N   CA   sing N N 235 
HIS   N   H    sing N N 236 
HIS   N   H2   sing N N 237 
HIS   CA  C    sing N N 238 
HIS   CA  CB   sing N N 239 
HIS   CA  HA   sing N N 240 
HIS   C   O    doub N N 241 
HIS   C   OXT  sing N N 242 
HIS   CB  CG   sing N N 243 
HIS   CB  HB2  sing N N 244 
HIS   CB  HB3  sing N N 245 
HIS   CG  ND1  sing Y N 246 
HIS   CG  CD2  doub Y N 247 
HIS   ND1 CE1  doub Y N 248 
HIS   ND1 HD1  sing N N 249 
HIS   CD2 NE2  sing Y N 250 
HIS   CD2 HD2  sing N N 251 
HIS   CE1 NE2  sing Y N 252 
HIS   CE1 HE1  sing N N 253 
HIS   NE2 HE2  sing N N 254 
HIS   OXT HXT  sing N N 255 
HOH   O   H1   sing N N 256 
HOH   O   H2   sing N N 257 
ILE   N   CA   sing N N 258 
ILE   N   H    sing N N 259 
ILE   N   H2   sing N N 260 
ILE   CA  C    sing N N 261 
ILE   CA  CB   sing N N 262 
ILE   CA  HA   sing N N 263 
ILE   C   O    doub N N 264 
ILE   C   OXT  sing N N 265 
ILE   CB  CG1  sing N N 266 
ILE   CB  CG2  sing N N 267 
ILE   CB  HB   sing N N 268 
ILE   CG1 CD1  sing N N 269 
ILE   CG1 HG12 sing N N 270 
ILE   CG1 HG13 sing N N 271 
ILE   CG2 HG21 sing N N 272 
ILE   CG2 HG22 sing N N 273 
ILE   CG2 HG23 sing N N 274 
ILE   CD1 HD11 sing N N 275 
ILE   CD1 HD12 sing N N 276 
ILE   CD1 HD13 sing N N 277 
ILE   OXT HXT  sing N N 278 
LEU   N   CA   sing N N 279 
LEU   N   H    sing N N 280 
LEU   N   H2   sing N N 281 
LEU   CA  C    sing N N 282 
LEU   CA  CB   sing N N 283 
LEU   CA  HA   sing N N 284 
LEU   C   O    doub N N 285 
LEU   C   OXT  sing N N 286 
LEU   CB  CG   sing N N 287 
LEU   CB  HB2  sing N N 288 
LEU   CB  HB3  sing N N 289 
LEU   CG  CD1  sing N N 290 
LEU   CG  CD2  sing N N 291 
LEU   CG  HG   sing N N 292 
LEU   CD1 HD11 sing N N 293 
LEU   CD1 HD12 sing N N 294 
LEU   CD1 HD13 sing N N 295 
LEU   CD2 HD21 sing N N 296 
LEU   CD2 HD22 sing N N 297 
LEU   CD2 HD23 sing N N 298 
LEU   OXT HXT  sing N N 299 
LYS   N   CA   sing N N 300 
LYS   N   H    sing N N 301 
LYS   N   H2   sing N N 302 
LYS   CA  C    sing N N 303 
LYS   CA  CB   sing N N 304 
LYS   CA  HA   sing N N 305 
LYS   C   O    doub N N 306 
LYS   C   OXT  sing N N 307 
LYS   CB  CG   sing N N 308 
LYS   CB  HB2  sing N N 309 
LYS   CB  HB3  sing N N 310 
LYS   CG  CD   sing N N 311 
LYS   CG  HG2  sing N N 312 
LYS   CG  HG3  sing N N 313 
LYS   CD  CE   sing N N 314 
LYS   CD  HD2  sing N N 315 
LYS   CD  HD3  sing N N 316 
LYS   CE  NZ   sing N N 317 
LYS   CE  HE2  sing N N 318 
LYS   CE  HE3  sing N N 319 
LYS   NZ  HZ1  sing N N 320 
LYS   NZ  HZ2  sing N N 321 
LYS   NZ  HZ3  sing N N 322 
LYS   OXT HXT  sing N N 323 
MET   N   CA   sing N N 324 
MET   N   H    sing N N 325 
MET   N   H2   sing N N 326 
MET   CA  C    sing N N 327 
MET   CA  CB   sing N N 328 
MET   CA  HA   sing N N 329 
MET   C   O    doub N N 330 
MET   C   OXT  sing N N 331 
MET   CB  CG   sing N N 332 
MET   CB  HB2  sing N N 333 
MET   CB  HB3  sing N N 334 
MET   CG  SD   sing N N 335 
MET   CG  HG2  sing N N 336 
MET   CG  HG3  sing N N 337 
MET   SD  CE   sing N N 338 
MET   CE  HE1  sing N N 339 
MET   CE  HE2  sing N N 340 
MET   CE  HE3  sing N N 341 
MET   OXT HXT  sing N N 342 
PHE   N   CA   sing N N 343 
PHE   N   H    sing N N 344 
PHE   N   H2   sing N N 345 
PHE   CA  C    sing N N 346 
PHE   CA  CB   sing N N 347 
PHE   CA  HA   sing N N 348 
PHE   C   O    doub N N 349 
PHE   C   OXT  sing N N 350 
PHE   CB  CG   sing N N 351 
PHE   CB  HB2  sing N N 352 
PHE   CB  HB3  sing N N 353 
PHE   CG  CD1  doub Y N 354 
PHE   CG  CD2  sing Y N 355 
PHE   CD1 CE1  sing Y N 356 
PHE   CD1 HD1  sing N N 357 
PHE   CD2 CE2  doub Y N 358 
PHE   CD2 HD2  sing N N 359 
PHE   CE1 CZ   doub Y N 360 
PHE   CE1 HE1  sing N N 361 
PHE   CE2 CZ   sing Y N 362 
PHE   CE2 HE2  sing N N 363 
PHE   CZ  HZ   sing N N 364 
PHE   OXT HXT  sing N N 365 
PRO   N   CA   sing N N 366 
PRO   N   CD   sing N N 367 
PRO   N   H    sing N N 368 
PRO   CA  C    sing N N 369 
PRO   CA  CB   sing N N 370 
PRO   CA  HA   sing N N 371 
PRO   C   O    doub N N 372 
PRO   C   OXT  sing N N 373 
PRO   CB  CG   sing N N 374 
PRO   CB  HB2  sing N N 375 
PRO   CB  HB3  sing N N 376 
PRO   CG  CD   sing N N 377 
PRO   CG  HG2  sing N N 378 
PRO   CG  HG3  sing N N 379 
PRO   CD  HD2  sing N N 380 
PRO   CD  HD3  sing N N 381 
PRO   OXT HXT  sing N N 382 
SER   N   CA   sing N N 383 
SER   N   H    sing N N 384 
SER   N   H2   sing N N 385 
SER   CA  C    sing N N 386 
SER   CA  CB   sing N N 387 
SER   CA  HA   sing N N 388 
SER   C   O    doub N N 389 
SER   C   OXT  sing N N 390 
SER   CB  OG   sing N N 391 
SER   CB  HB2  sing N N 392 
SER   CB  HB3  sing N N 393 
SER   OG  HG   sing N N 394 
SER   OXT HXT  sing N N 395 
THR   N   CA   sing N N 396 
THR   N   H    sing N N 397 
THR   N   H2   sing N N 398 
THR   CA  C    sing N N 399 
THR   CA  CB   sing N N 400 
THR   CA  HA   sing N N 401 
THR   C   O    doub N N 402 
THR   C   OXT  sing N N 403 
THR   CB  OG1  sing N N 404 
THR   CB  CG2  sing N N 405 
THR   CB  HB   sing N N 406 
THR   OG1 HG1  sing N N 407 
THR   CG2 HG21 sing N N 408 
THR   CG2 HG22 sing N N 409 
THR   CG2 HG23 sing N N 410 
THR   OXT HXT  sing N N 411 
TRP   N   CA   sing N N 412 
TRP   N   H    sing N N 413 
TRP   N   H2   sing N N 414 
TRP   CA  C    sing N N 415 
TRP   CA  CB   sing N N 416 
TRP   CA  HA   sing N N 417 
TRP   C   O    doub N N 418 
TRP   C   OXT  sing N N 419 
TRP   CB  CG   sing N N 420 
TRP   CB  HB2  sing N N 421 
TRP   CB  HB3  sing N N 422 
TRP   CG  CD1  doub Y N 423 
TRP   CG  CD2  sing Y N 424 
TRP   CD1 NE1  sing Y N 425 
TRP   CD1 HD1  sing N N 426 
TRP   CD2 CE2  doub Y N 427 
TRP   CD2 CE3  sing Y N 428 
TRP   NE1 CE2  sing Y N 429 
TRP   NE1 HE1  sing N N 430 
TRP   CE2 CZ2  sing Y N 431 
TRP   CE3 CZ3  doub Y N 432 
TRP   CE3 HE3  sing N N 433 
TRP   CZ2 CH2  doub Y N 434 
TRP   CZ2 HZ2  sing N N 435 
TRP   CZ3 CH2  sing Y N 436 
TRP   CZ3 HZ3  sing N N 437 
TRP   CH2 HH2  sing N N 438 
TRP   OXT HXT  sing N N 439 
TYR   N   CA   sing N N 440 
TYR   N   H    sing N N 441 
TYR   N   H2   sing N N 442 
TYR   CA  C    sing N N 443 
TYR   CA  CB   sing N N 444 
TYR   CA  HA   sing N N 445 
TYR   C   O    doub N N 446 
TYR   C   OXT  sing N N 447 
TYR   CB  CG   sing N N 448 
TYR   CB  HB2  sing N N 449 
TYR   CB  HB3  sing N N 450 
TYR   CG  CD1  doub Y N 451 
TYR   CG  CD2  sing Y N 452 
TYR   CD1 CE1  sing Y N 453 
TYR   CD1 HD1  sing N N 454 
TYR   CD2 CE2  doub Y N 455 
TYR   CD2 HD2  sing N N 456 
TYR   CE1 CZ   doub Y N 457 
TYR   CE1 HE1  sing N N 458 
TYR   CE2 CZ   sing Y N 459 
TYR   CE2 HE2  sing N N 460 
TYR   CZ  OH   sing N N 461 
TYR   OH  HH   sing N N 462 
TYR   OXT HXT  sing N N 463 
VAL   N   CA   sing N N 464 
VAL   N   H    sing N N 465 
VAL   N   H2   sing N N 466 
VAL   CA  C    sing N N 467 
VAL   CA  CB   sing N N 468 
VAL   CA  HA   sing N N 469 
VAL   C   O    doub N N 470 
VAL   C   OXT  sing N N 471 
VAL   CB  CG1  sing N N 472 
VAL   CB  CG2  sing N N 473 
VAL   CB  HB   sing N N 474 
VAL   CG1 HG11 sing N N 475 
VAL   CG1 HG12 sing N N 476 
VAL   CG1 HG13 sing N N 477 
VAL   CG2 HG21 sing N N 478 
VAL   CG2 HG22 sing N N 479 
VAL   CG2 HG23 sing N N 480 
VAL   OXT HXT  sing N N 481 
# 
_pdbx_audit_support.funding_organization   'Not funded' 
_pdbx_audit_support.country                ? 
_pdbx_audit_support.grant_number           ? 
_pdbx_audit_support.ordinal                1 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'experimental model' 
_pdbx_initial_refinement_model.source_name      PDB 
_pdbx_initial_refinement_model.accession_code   3pe6 
_pdbx_initial_refinement_model.details          ? 
# 
_space_group.name_H-M_alt     'C 2 2 21' 
_space_group.name_Hall        'C 2c 2' 
_space_group.IT_number        20 
_space_group.crystal_system   orthorhombic 
_space_group.id               1 
# 
_atom_sites.entry_id                    9G4M 
_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]   0.011249 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000000 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.007859 
_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]   0.016076 
_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 
_atom_type.scat_dispersion_real 
_atom_type.scat_dispersion_imag 
_atom_type.scat_Cromer_Mann_a1 
_atom_type.scat_Cromer_Mann_a2 
_atom_type.scat_Cromer_Mann_a3 
_atom_type.scat_Cromer_Mann_a4 
_atom_type.scat_Cromer_Mann_b1 
_atom_type.scat_Cromer_Mann_b2 
_atom_type.scat_Cromer_Mann_b3 
_atom_type.scat_Cromer_Mann_b4 
_atom_type.scat_Cromer_Mann_c 
_atom_type.scat_source 
_atom_type.scat_dispersion_source 
B ? ? 2.74417 2.23879 ? ? 37.84921 1.85376  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
C ? ? 3.54356 2.42580 ? ? 25.62398 1.50364  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
F ? ? 4.90428 4.07044 ? ? 12.99538 1.63651  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
N ? ? 4.01032 2.96436 ? ? 19.97189 1.75589  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
O ? ? 4.49882 3.47563 ? ? 15.80542 1.70748  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
S ? ? 9.55732 6.39887 ? ? 1.23737  29.19336 ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N N   . SER   A 1 26  ? 20.09254 52.79459 1.42805   1.000 68.35862 ? 6   SER   A N   1 
ATOM   2    C CA  . SER   A 1 26  ? 20.55556 51.73708 0.53145   1.000 66.88917 ? 6   SER   A CA  1 
ATOM   3    C C   . SER   A 1 26  ? 20.69203 50.40297 1.26476   1.000 62.51750 ? 6   SER   A C   1 
ATOM   4    O O   . SER   A 1 26  ? 21.62735 50.20590 2.03831   1.000 62.68741 ? 6   SER   A O   1 
ATOM   5    C CB  . SER   A 1 26  ? 21.88081 52.12575 -0.12708  1.000 69.50507 ? 6   SER   A CB  1 
ATOM   6    O OG  . SER   A 1 26  ? 22.81978 52.57966 0.83378   1.000 71.45649 ? 6   SER   A OG  1 
ATOM   7    N N   . PRO   A 1 27  ? 19.76001 49.48736 1.00641   1.000 57.87656 ? 7   PRO   A N   1 
ATOM   8    C CA  . PRO   A 1 27  ? 19.75189 48.21752 1.74370   1.000 53.14702 ? 7   PRO   A CA  1 
ATOM   9    C C   . PRO   A 1 27  ? 20.90658 47.31874 1.33845   1.000 46.39135 ? 7   PRO   A C   1 
ATOM   10   O O   . PRO   A 1 27  ? 21.55159 47.50193 0.30318   1.000 47.50353 ? 7   PRO   A O   1 
ATOM   11   C CB  . PRO   A 1 27  ? 18.40881 47.59739 1.33928   1.000 55.10127 ? 7   PRO   A CB  1 
ATOM   12   C CG  . PRO   A 1 27  ? 18.13307 48.16059 -0.01300  1.000 56.19086 ? 7   PRO   A CG  1 
ATOM   13   C CD  . PRO   A 1 27  ? 18.66656 49.57534 0.03494   1.000 57.25539 ? 7   PRO   A CD  1 
ATOM   14   N N   . ARG   A 1 28  ? 21.17537 46.33213 2.19678   1.000 40.04044 ? 8   ARG   A N   1 
ATOM   15   C CA  . ARG   A 1 28  ? 22.12613 45.28116 1.86219   1.000 34.62658 ? 8   ARG   A CA  1 
ATOM   16   C C   . ARG   A 1 28  ? 21.58098 44.46780 0.69727   1.000 31.66409 ? 8   ARG   A C   1 
ATOM   17   O O   . ARG   A 1 28  ? 20.42236 44.04304 0.71319   1.000 32.06240 ? 8   ARG   A O   1 
ATOM   18   C CB  . ARG   A 1 28  ? 22.33748 44.36235 3.06892   1.000 33.05842 ? 8   ARG   A CB  1 
ATOM   19   C CG  . ARG   A 1 28  ? 23.03576 45.02715 4.24310   1.000 33.38346 ? 8   ARG   A CG  1 
ATOM   20   C CD  . ARG   A 1 28  ? 24.54450 45.06508 4.04499   1.000 31.96150 ? 8   ARG   A CD  1 
ATOM   21   N NE  . ARG   A 1 28  ? 25.17721 43.79793 4.39598   1.000 29.29540 ? 8   ARG   A NE  1 
ATOM   22   C CZ  . ARG   A 1 28  ? 25.54256 43.47245 5.62834   1.000 26.63160 ? 8   ARG   A CZ  1 
ATOM   23   N NH1 . ARG   A 1 28  ? 25.31968 44.28208 6.65602   1.000 28.58322 ? 8   ARG   A NH1 1 
ATOM   24   N NH2 . ARG   A 1 28  ? 26.15677 42.31407 5.83646   1.000 24.58480 ? 8   ARG   A NH2 1 
ATOM   25   N N   . ARG   A 1 29  ? 22.41848 44.24570 -0.31055  1.000 30.32240 ? 9   ARG   A N   1 
ATOM   26   C CA  . ARG   A 1 29  ? 22.01856 43.53640 -1.51713  1.000 29.18702 ? 9   ARG   A CA  1 
ATOM   27   C C   . ARG   A 1 29  ? 22.89774 42.31337 -1.73771  1.000 27.80344 ? 9   ARG   A C   1 
ATOM   28   O O   . ARG   A 1 29  ? 24.04468 42.25760 -1.27628  1.000 29.27260 ? 9   ARG   A O   1 
ATOM   29   C CB  . ARG   A 1 29  ? 22.13283 44.44172 -2.74502  1.000 30.70328 ? 9   ARG   A CB  1 
ATOM   30   C CG  . ARG   A 1 29  ? 21.20054 45.63931 -2.72002  1.000 33.97168 ? 9   ARG   A CG  1 
ATOM   31   C CD  . ARG   A 1 29  ? 21.52438 46.60013 -3.85392  1.000 37.62428 ? 9   ARG   A CD  1 
ATOM   32   N NE  . ARG   A 1 29  ? 20.72519 47.81568 -3.77721  1.000 42.90610 ? 9   ARG   A NE  1 
ATOM   33   C CZ  . ARG   A 1 29  ? 19.54417 47.96693 -4.35927  1.000 45.72440 ? 9   ARG   A CZ  1 
ATOM   34   N NH1 . ARG   A 1 29  ? 19.00018 46.99697 -5.07845  1.000 46.27746 ? 9   ARG   A NH1 1 
ATOM   35   N NH2 . ARG   A 1 29  ? 18.89605 49.12112 -4.22228  1.000 47.52326 ? 9   ARG   A NH2 1 
ATOM   36   N N   . THR   A 1 30  ? 22.34427 41.32879 -2.45451  1.000 23.95324 ? 10  THR   A N   1 
ATOM   37   C CA  . THR   A 1 30  ? 23.12474 40.18341 -2.89852  1.000 24.07731 ? 10  THR   A CA  1 
ATOM   38   C C   . THR   A 1 30  ? 24.23983 40.66766 -3.81548  1.000 25.24993 ? 10  THR   A C   1 
ATOM   39   O O   . THR   A 1 30  ? 24.19728 41.80768 -4.31249  1.000 26.43168 ? 10  THR   A O   1 
ATOM   40   C CB  . THR   A 1 30  ? 22.24456 39.19823 -3.68125  1.000 23.59109 ? 10  THR   A CB  1 
ATOM   41   O OG1 . THR   A 1 30  ? 21.81358 39.80837 -4.91387  1.000 23.96545 ? 10  THR   A OG1 1 
ATOM   42   C CG2 . THR   A 1 30  ? 21.03283 38.77430 -2.86295  1.000 22.85080 ? 10  THR   A CG2 1 
ATOM   43   N N   . PRO   A 1 31  ? 25.25687 39.83547 -4.06744  1.000 24.86311 ? 11  PRO   A N   1 
ATOM   44   C CA  . PRO   A 1 31  ? 26.25784 40.19345 -5.08953  1.000 25.79676 ? 11  PRO   A CA  1 
ATOM   45   C C   . PRO   A 1 31  ? 25.65226 40.49326 -6.45008  1.000 27.54414 ? 11  PRO   A C   1 
ATOM   46   O O   . PRO   A 1 31  ? 26.31792 41.12743 -7.28563  1.000 29.86188 ? 11  PRO   A O   1 
ATOM   47   C CB  . PRO   A 1 31  ? 27.16572 38.95445 -5.12569  1.000 25.91884 ? 11  PRO   A CB  1 
ATOM   48   C CG  . PRO   A 1 31  ? 27.05061 38.38240 -3.76794  1.000 26.84193 ? 11  PRO   A CG  1 
ATOM   49   C CD  . PRO   A 1 31  ? 25.60753 38.58088 -3.37990  1.000 25.47528 ? 11  PRO   A CD  1 
ATOM   50   N N   . GLN   A 1 32  ? 24.41583 40.06926 -6.70333  1.000 27.91099 ? 12  GLN   A N   1 
ATOM   51   C CA  . GLN   A 1 32  ? 23.70112 40.35870 -7.93912  1.000 27.73161 ? 12  GLN   A CA  1 
ATOM   52   C C   . GLN   A 1 32  ? 22.75707 41.55232 -7.79722  1.000 28.96355 ? 12  GLN   A C   1 
ATOM   53   O O   . GLN   A 1 32  ? 21.90368 41.76694 -8.66689  1.000 30.65834 ? 12  GLN   A O   1 
ATOM   54   C CB  . GLN   A 1 32  ? 22.95228 39.10955 -8.42335  1.000 27.24246 ? 12  GLN   A CB  1 
ATOM   55   C CG  . GLN   A 1 32  ? 23.84455 37.86154 -8.62455  1.000 27.22688 ? 12  GLN   A CG  1 
ATOM   56   C CD  . GLN   A 1 32  ? 24.20917 37.15615 -7.31840  1.000 26.36563 ? 12  GLN   A CD  1 
ATOM   57   O OE1 . GLN   A 1 32  ? 23.42702 37.14725 -6.36920  1.000 26.87483 ? 12  GLN   A OE1 1 
ATOM   58   N NE2 . GLN   A 1 32  ? 25.40405 36.56706 -7.26738  1.000 25.35886 ? 12  GLN   A NE2 1 
ATOM   59   N N   . SER   A 1 33  ? 22.88043 42.31255 -6.70788  1.000 28.71312 ? 13  SER   A N   1 
ATOM   60   C CA  . SER   A 1 33  ? 22.20396 43.59415 -6.49544  1.000 29.22798 ? 13  SER   A CA  1 
ATOM   61   C C   . SER   A 1 33  ? 20.73772 43.47691 -6.09065  1.000 28.05014 ? 13  SER   A C   1 
ATOM   62   O O   . SER   A 1 33  ? 20.00989 44.47001 -6.15795  1.000 30.20269 ? 13  SER   A O   1 
ATOM   63   C CB  . SER   A 1 33  ? 22.35761 44.55784 -7.68239  1.000 31.82737 ? 13  SER   A CB  1 
ATOM   64   O OG  . SER   A 1 33  ? 23.71331 44.92206 -7.88519  1.000 35.27005 ? 13  SER   A OG  1 
ATOM   65   N N   . ILE   A 1 34  ? 20.26888 42.30779 -5.66701  1.000 27.23652 ? 14  ILE   A N   1 
ATOM   66   C CA  . ILE   A 1 34  ? 18.89525 42.18221 -5.17470  1.000 26.82811 ? 14  ILE   A CA  1 
ATOM   67   C C   . ILE   A 1 34  ? 18.88279 42.48052 -3.68047  1.000 26.56429 ? 14  ILE   A C   1 
ATOM   68   O O   . ILE   A 1 34  ? 19.68420 41.89907 -2.93674  1.000 26.05560 ? 14  ILE   A O   1 
ATOM   69   C CB  . ILE   A 1 34  ? 18.32136 40.78374 -5.44805  1.000 28.44597 ? 14  ILE   A CB  1 
ATOM   70   C CG1 . ILE   A 1 34  ? 18.37104 40.45707 -6.94265  1.000 29.01353 ? 14  ILE   A CG1 1 
ATOM   71   C CG2 . ILE   A 1 34  ? 16.89944 40.70135 -4.92298  1.000 28.14144 ? 14  ILE   A CG2 1 
ATOM   72   C CD1 . ILE   A 1 34  ? 17.77069 39.10723 -7.29362  1.000 31.04863 ? 14  ILE   A CD1 1 
ATOM   73   N N   . PRO   A 1 35  ? 18.00579 43.35765 -3.18809  1.000 26.77772 ? 15  PRO   A N   1 
ATOM   74   C CA  . PRO   A 1 35  ? 17.94658 43.59086 -1.73808  1.000 26.47725 ? 15  PRO   A CA  1 
ATOM   75   C C   . PRO   A 1 35  ? 17.61715 42.30507 -0.99247  1.000 25.21410 ? 15  PRO   A C   1 
ATOM   76   O O   . PRO   A 1 35  ? 16.69368 41.57731 -1.35868  1.000 26.25427 ? 15  PRO   A O   1 
ATOM   77   C CB  . PRO   A 1 35  ? 16.81664 44.61743 -1.58880  1.000 28.12374 ? 15  PRO   A CB  1 
ATOM   78   C CG  . PRO   A 1 35  ? 16.72443 45.28810 -2.92632  1.000 29.81046 ? 15  PRO   A CG  1 
ATOM   79   C CD  . PRO   A 1 35  ? 17.06167 44.21516 -3.92520  1.000 27.84334 ? 15  PRO   A CD  1 
ATOM   80   N N   . TYR   A 1 36  ? 18.38176 42.03385 0.07268   1.000 25.17779 ? 16  TYR   A N   1 
ATOM   81   C CA  . TYR   A 1 36  ? 18.06905 40.88844 0.92017   1.000 24.58549 ? 16  TYR   A CA  1 
ATOM   82   C C   . TYR   A 1 36  ? 16.68217 40.99692 1.54000   1.000 26.37991 ? 16  TYR   A C   1 
ATOM   83   O O   . TYR   A 1 36  ? 16.05183 39.96930 1.81419   1.000 27.41134 ? 16  TYR   A O   1 
ATOM   84   C CB  . TYR   A 1 36  ? 19.14242 40.67373 1.99349   1.000 23.52907 ? 16  TYR   A CB  1 
ATOM   85   C CG  . TYR   A 1 36  ? 20.38008 40.00708 1.44423   1.000 22.62391 ? 16  TYR   A CG  1 
ATOM   86   C CD1 . TYR   A 1 36  ? 20.37044 38.65810 1.09203   1.000 22.20136 ? 16  TYR   A CD1 1 
ATOM   87   C CD2 . TYR   A 1 36  ? 21.55094 40.72919 1.24947   1.000 22.57520 ? 16  TYR   A CD2 1 
ATOM   88   C CE1 . TYR   A 1 36  ? 21.50140 38.04281 0.57019   1.000 21.93733 ? 16  TYR   A CE1 1 
ATOM   89   C CE2 . TYR   A 1 36  ? 22.68796 40.11937 0.73088   1.000 21.75044 ? 16  TYR   A CE2 1 
ATOM   90   C CZ  . TYR   A 1 36  ? 22.65499 38.78563 0.39120   1.000 20.93801 ? 16  TYR   A CZ  1 
ATOM   91   O OH  . TYR   A 1 36  ? 23.79468 38.22663 -0.12924  1.000 22.47468 ? 16  TYR   A OH  1 
ATOM   92   N N   . GLN   A 1 37  ? 16.18354 42.21941 1.76452   1.000 28.55753 ? 17  GLN   A N   1 
ATOM   93   C CA  . GLN   A 1 37  ? 14.82501 42.36103 2.28254   1.000 31.19594 ? 17  GLN   A CA  1 
ATOM   94   C C   . GLN   A 1 37  ? 13.78652 41.77497 1.33354   1.000 31.80881 ? 17  GLN   A C   1 
ATOM   95   O O   . GLN   A 1 37  ? 12.65761 41.50455 1.75584   1.000 34.66562 ? 17  GLN   A O   1 
ATOM   96   C CB  . GLN   A 1 37  ? 14.50735 43.82204 2.62397   1.000 34.08534 ? 17  GLN   A CB  1 
ATOM   97   C CG  . GLN   A 1 37  ? 14.56820 44.76007 1.44750   1.000 38.02277 ? 17  GLN   A CG  1 
ATOM   98   C CD  . GLN   A 1 37  ? 14.33320 46.20385 1.84364   1.000 43.60743 ? 17  GLN   A CD  1 
ATOM   99   O OE1 . GLN   A 1 37  ? 14.42357 46.56480 3.01923   1.000 46.82901 ? 17  GLN   A OE1 1 
ATOM   100  N NE2 . GLN   A 1 37  ? 14.02687 47.03894 0.86104   1.000 45.48447 ? 17  GLN   A NE2 1 
ATOM   101  N N   . ASP   A 1 38  ? 14.14857 41.54334 0.07362   1.000 28.67988 ? 18  ASP   A N   1 
ATOM   102  C CA  . ASP   A 1 38  ? 13.24452 40.94572 -0.89805  1.000 30.52253 ? 18  ASP   A CA  1 
ATOM   103  C C   . ASP   A 1 38  ? 13.40004 39.43125 -1.01813  1.000 28.35756 ? 18  ASP   A C   1 
ATOM   104  O O   . ASP   A 1 38  ? 12.73255 38.83199 -1.86569  1.000 30.81566 ? 18  ASP   A O   1 
ATOM   105  C CB  . ASP   A 1 38  ? 13.45281 41.56332 -2.28682  1.000 33.82948 ? 18  ASP   A CB  1 
ATOM   106  C CG  . ASP   A 1 38  ? 13.17176 43.05886 -2.32467  1.000 38.01640 ? 18  ASP   A CG  1 
ATOM   107  O OD1 . ASP   A 1 38  ? 12.43173 43.56579 -1.45651  1.000 37.96084 ? 18  ASP   A OD1 1 
ATOM   108  O OD2 . ASP   A 1 38  ? 13.69129 43.73068 -3.23861  1.000 41.26693 ? 18  ASP   A OD2 1 
ATOM   109  N N   . LEU   A 1 39  ? 14.24691 38.79715 -0.20808  1.000 25.38429 ? 19  LEU   A N   1 
ATOM   110  C CA  . LEU   A 1 39  ? 14.57299 37.38378 -0.36935  1.000 24.15725 ? 19  LEU   A CA  1 
ATOM   111  C C   . LEU   A 1 39  ? 14.62032 36.69247 0.98486   1.000 23.83916 ? 19  LEU   A C   1 
ATOM   112  O O   . LEU   A 1 39  ? 14.90358 37.33333 2.00297   1.000 24.97556 ? 19  LEU   A O   1 
ATOM   113  C CB  . LEU   A 1 39  ? 15.95065 37.21885 -1.02636  1.000 24.90240 ? 19  LEU   A CB  1 
ATOM   114  C CG  . LEU   A 1 39  ? 16.08294 37.79842 -2.42762  1.000 26.61542 ? 19  LEU   A CG  1 
ATOM   115  C CD1 . LEU   A 1 39  ? 17.51465 37.70135 -2.88248  1.000 27.30088 ? 19  LEU   A CD1 1 
ATOM   116  C CD2 . LEU   A 1 39  ? 15.14259 37.07358 -3.38203  1.000 27.02915 ? 19  LEU   A CD2 1 
ATOM   117  N N   . PRO   A 1 40  ? 14.37326 35.38168 1.02562   1.000 22.65579 ? 20  PRO   A N   1 
ATOM   118  C CA  . PRO   A 1 40  ? 14.61677 34.63955 2.26769   1.000 21.33836 ? 20  PRO   A CA  1 
ATOM   119  C C   . PRO   A 1 40  ? 16.10205 34.67674 2.57976   1.000 20.36760 ? 20  PRO   A C   1 
ATOM   120  O O   . PRO   A 1 40  ? 16.94288 34.51645 1.68964   1.000 20.59599 ? 20  PRO   A O   1 
ATOM   121  C CB  . PRO   A 1 40  ? 14.15502 33.21345 1.93055   1.000 22.28392 ? 20  PRO   A CB  1 
ATOM   122  C CG  . PRO   A 1 40  ? 13.37280 33.32703 0.65701   1.000 24.22637 ? 20  PRO   A CG  1 
ATOM   123  C CD  . PRO   A 1 40  ? 13.96025 34.49287 -0.07351  1.000 23.87517 ? 20  PRO   A CD  1 
ATOM   124  N N   . HIS   A 1 41  ? 16.43050 34.90125 3.84743   1.000 20.30828 ? 21  HIS   A N   1 
ATOM   125  C CA  . HIS   A 1 41  ? 17.83188 35.08303 4.19789   1.000 20.87132 ? 21  HIS   A CA  1 
ATOM   126  C C   . HIS   A 1 41  ? 18.03752 34.80294 5.67893   1.000 21.92263 ? 21  HIS   A C   1 
ATOM   127  O O   . HIS   A 1 41  ? 17.08778 34.63197 6.44981   1.000 24.18188 ? 21  HIS   A O   1 
ATOM   128  C CB  . HIS   A 1 41  ? 18.31708 36.49724 3.84633   1.000 21.15171 ? 21  HIS   A CB  1 
ATOM   129  C CG  . HIS   A 1 41  ? 17.58500 37.57613 4.57542   1.000 23.70155 ? 21  HIS   A CG  1 
ATOM   130  N ND1 . HIS   A 1 41  ? 16.46385 38.19285 4.06180   1.000 26.04975 ? 21  HIS   A ND1 1 
ATOM   131  C CD2 . HIS   A 1 41  ? 17.80667 38.14219 5.78556   1.000 25.63247 ? 21  HIS   A CD2 1 
ATOM   132  C CE1 . HIS   A 1 41  ? 16.03319 39.09947 4.91980   1.000 28.98978 ? 21  HIS   A CE1 1 
ATOM   133  N NE2 . HIS   A 1 41  ? 16.82556 39.08325 5.97728   1.000 27.93284 ? 21  HIS   A NE2 1 
ATOM   134  N N   . LEU   A 1 42  ? 19.30876 34.77192 6.06139   1.000 20.79090 ? 22  LEU   A N   1 
ATOM   135  C CA  . LEU   A 1 42  ? 19.73632 34.55448 7.43308   1.000 22.14236 ? 22  LEU   A CA  1 
ATOM   136  C C   . LEU   A 1 42  ? 21.04503 35.31117 7.58008   1.000 21.45506 ? 22  LEU   A C   1 
ATOM   137  O O   . LEU   A 1 42  ? 21.86417 35.29890 6.66042   1.000 25.91909 ? 22  LEU   A O   1 
ATOM   138  C CB  . LEU   A 1 42  ? 19.99491 33.05212 7.64910   1.000 25.30852 ? 22  LEU   A CB  1 
ATOM   139  C CG  . LEU   A 1 42  ? 20.30674 32.46793 9.02080   1.000 31.19189 ? 22  LEU   A CG  1 
ATOM   140  C CD1 . LEU   A 1 42  ? 19.07310 32.50072 9.90430   1.000 32.48055 ? 22  LEU   A CD1 1 
ATOM   141  C CD2 . LEU   A 1 42  ? 20.80522 31.02212 8.85993   1.000 30.66183 ? 22  LEU   A CD2 1 
ATOM   142  N N   . VAL   A 1 43  ? 21.24710 35.97632 8.71501   1.000 19.23475 ? 23  VAL   A N   1 
ATOM   143  C CA  . VAL   A 1 43  ? 22.51254 36.65714 8.98405   1.000 20.70699 ? 23  VAL   A CA  1 
ATOM   144  C C   . VAL   A 1 43  ? 23.37159 35.74711 9.85343   1.000 21.01972 ? 23  VAL   A C   1 
ATOM   145  O O   . VAL   A 1 43  ? 22.93475 35.31651 10.92677  1.000 22.19754 ? 23  VAL   A O   1 
ATOM   146  C CB  . VAL   A 1 43  ? 22.29570 38.02337 9.65174   1.000 21.92237 ? 23  VAL   A CB  1 
ATOM   147  C CG1 . VAL   A 1 43  ? 23.64244 38.71230 9.87250   1.000 22.79328 ? 23  VAL   A CG1 1 
ATOM   148  C CG2 . VAL   A 1 43  ? 21.37565 38.90258 8.80554   1.000 23.87463 ? 23  VAL   A CG2 1 
ATOM   149  N N   . ASN   A 1 44  ? 24.58828 35.44915 9.39183   1.000 20.28131 ? 24  ASN   A N   1 
ATOM   150  C CA  . ASN   A 1 44  ? 25.45351 34.52786 10.11711  1.000 19.88991 ? 24  ASN   A CA  1 
ATOM   151  C C   . ASN   A 1 44  ? 26.16359 35.24076 11.27097  1.000 21.17414 ? 24  ASN   A C   1 
ATOM   152  O O   . ASN   A 1 44  ? 25.98748 36.44200 11.50881  1.000 21.92023 ? 24  ASN   A O   1 
ATOM   153  C CB  . ASN   A 1 44  ? 26.38925 33.76082 9.16647   1.000 20.41208 ? 24  ASN   A CB  1 
ATOM   154  C CG  . ASN   A 1 44  ? 27.57997 34.59074 8.66696   1.000 20.07876 ? 24  ASN   A CG  1 
ATOM   155  O OD1 . ASN   A 1 44  ? 27.80144 35.74257 9.07538   1.000 19.82696 ? 24  ASN   A OD1 1 
ATOM   156  N ND2 . ASN   A 1 44  ? 28.36472 33.98808 7.78220   1.000 21.42692 ? 24  ASN   A ND2 1 
ATOM   157  N N   . ALA   A 1 45  ? 26.98998 34.48304 11.99370  1.000 22.12056 ? 25  ALA   A N   1 
ATOM   158  C CA  . ALA   A 1 45  ? 27.67567 35.00680 13.16867  1.000 23.60354 ? 25  ALA   A CA  1 
ATOM   159  C C   . ALA   A 1 45  ? 28.70839 36.07413 12.82638  1.000 24.47925 ? 25  ALA   A C   1 
ATOM   160  O O   . ALA   A 1 45  ? 29.08773 36.85342 13.70703  1.000 27.17653 ? 25  ALA   A O   1 
ATOM   161  C CB  . ALA   A 1 45  ? 28.31991 33.86017 13.95777  1.000 26.98632 ? 25  ALA   A CB  1 
ATOM   162  N N   . ASP   A 1 46  ? 29.16361 36.13849 11.57546  1.000 24.84326 ? 26  ASP   A N   1 
ATOM   163  C CA  . ASP   A 1 46  ? 30.06018 37.19534 11.12067  1.000 24.45312 ? 26  ASP   A CA  1 
ATOM   164  C C   . ASP   A 1 46  ? 29.31749 38.39727 10.54935  1.000 25.05702 ? 26  ASP   A C   1 
ATOM   165  O O   . ASP   A 1 46  ? 29.95549 39.30480 10.00151  1.000 28.09245 ? 26  ASP   A O   1 
ATOM   166  C CB  . ASP   A 1 46  ? 31.04905 36.63846 10.09275  1.000 25.73058 ? 26  ASP   A CB  1 
ATOM   167  C CG  . ASP   A 1 46  ? 32.01329 35.64069 10.70365  1.000 27.96574 ? 26  ASP   A CG  1 
ATOM   168  O OD1 . ASP   A 1 46  ? 32.48037 35.90742 11.83084  1.000 30.42011 ? 26  ASP   A OD1 1 
ATOM   169  O OD2 . ASP   A 1 46  ? 32.30052 34.59916 10.07279  1.000 29.17460 ? 26  ASP   A OD2 1 
ATOM   170  N N   . GLY   A 1 47  ? 27.99444 38.43845 10.67903  1.000 23.78568 ? 27  GLY   A N   1 
ATOM   171  C CA  . GLY   A 1 47  ? 27.22550 39.55122 10.15598  1.000 23.00434 ? 27  GLY   A CA  1 
ATOM   172  C C   . GLY   A 1 47  ? 27.01854 39.52032 8.66084   1.000 23.37351 ? 27  GLY   A C   1 
ATOM   173  O O   . GLY   A 1 47  ? 26.66312 40.54517 8.07720   1.000 24.41072 ? 27  GLY   A O   1 
ATOM   174  N N   . GLN   A 1 48  ? 27.23113 38.37157 8.01815   1.000 21.23005 ? 28  GLN   A N   1 
ATOM   175  C CA  . GLN   A 1 48  ? 27.06277 38.23485 6.58033   1.000 20.98349 ? 28  GLN   A CA  1 
ATOM   176  C C   . GLN   A 1 48  ? 25.69484 37.64156 6.26697   1.000 20.78340 ? 28  GLN   A C   1 
ATOM   177  O O   . GLN   A 1 48  ? 25.24059 36.71065 6.94518   1.000 21.50159 ? 28  GLN   A O   1 
ATOM   178  C CB  . GLN   A 1 48  ? 28.14058 37.32076 5.99588   1.000 22.61870 ? 28  GLN   A CB  1 
ATOM   179  C CG  . GLN   A 1 48  ? 29.55943 37.84123 6.19761   1.000 23.33526 ? 28  GLN   A CG  1 
ATOM   180  C CD  . GLN   A 1 48  ? 30.59308 36.77716 5.90940   1.000 23.39815 ? 28  GLN   A CD  1 
ATOM   181  O OE1 . GLN   A 1 48  ? 30.58043 35.71183 6.52272   1.000 22.76984 ? 28  GLN   A OE1 1 
ATOM   182  N NE2 . GLN   A 1 48  ? 31.48161 37.04948 4.96626   1.000 24.02580 ? 28  GLN   A NE2 1 
ATOM   183  N N   . TYR   A 1 49  ? 25.05214 38.17355 5.22537   1.000 20.33609 ? 29  TYR   A N   1 
ATOM   184  C CA  . TYR   A 1 49  ? 23.75561 37.67286 4.79272   1.000 19.62563 ? 29  TYR   A CA  1 
ATOM   185  C C   . TYR   A 1 49  ? 23.92608 36.42443 3.93769   1.000 20.25754 ? 29  TYR   A C   1 
ATOM   186  O O   . TYR   A 1 49  ? 24.68059 36.42521 2.95583   1.000 20.19817 ? 29  TYR   A O   1 
ATOM   187  C CB  . TYR   A 1 49  ? 23.01221 38.72933 3.97852   1.000 18.92658 ? 29  TYR   A CB  1 
ATOM   188  C CG  . TYR   A 1 49  ? 22.30618 39.77579 4.80231   1.000 20.39706 ? 29  TYR   A CG  1 
ATOM   189  C CD1 . TYR   A 1 49  ? 23.02073 40.78697 5.43533   1.000 23.06722 ? 29  TYR   A CD1 1 
ATOM   190  C CD2 . TYR   A 1 49  ? 20.92429 39.76728 4.93351   1.000 21.47318 ? 29  TYR   A CD2 1 
ATOM   191  C CE1 . TYR   A 1 49  ? 22.37989 41.75775 6.18643   1.000 22.61219 ? 29  TYR   A CE1 1 
ATOM   192  C CE2 . TYR   A 1 49  ? 20.26744 40.74691 5.67925   1.000 21.27925 ? 29  TYR   A CE2 1 
ATOM   193  C CZ  . TYR   A 1 49  ? 21.00265 41.73670 6.30178   1.000 21.69352 ? 29  TYR   A CZ  1 
ATOM   194  O OH  . TYR   A 1 49  ? 20.36162 42.70176 7.04787   1.000 22.24465 ? 29  TYR   A OH  1 
ATOM   195  N N   . LEU   A 1 50  ? 23.20830 35.36930 4.30168   1.000 20.23873 ? 30  LEU   A N   1 
ATOM   196  C CA  . LEU   A 1 50  ? 23.13873 34.14171 3.51831   1.000 19.12926 ? 30  LEU   A CA  1 
ATOM   197  C C   . LEU   A 1 50  ? 21.77253 34.05887 2.86295   1.000 19.10308 ? 30  LEU   A C   1 
ATOM   198  O O   . LEU   A 1 50  ? 20.75056 34.22524 3.53794   1.000 20.07151 ? 30  LEU   A O   1 
ATOM   199  C CB  . LEU   A 1 50  ? 23.31468 32.91374 4.41594   1.000 19.01749 ? 30  LEU   A CB  1 
ATOM   200  C CG  . LEU   A 1 50  ? 24.60037 32.88374 5.23899   1.000 21.08743 ? 30  LEU   A CG  1 
ATOM   201  C CD1 . LEU   A 1 50  ? 24.71840 31.58535 6.01761   1.000 22.66844 ? 30  LEU   A CD1 1 
ATOM   202  C CD2 . LEU   A 1 50  ? 25.79408 33.09313 4.32853   1.000 23.96226 ? 30  LEU   A CD2 1 
ATOM   203  N N   . PHE   A 1 51  ? 21.75728 33.79934 1.55948   1.000 19.25507 ? 31  PHE   A N   1 
ATOM   204  C CA  . PHE   A 1 51  ? 20.51108 33.56797 0.83792   1.000 18.22372 ? 31  PHE   A CA  1 
ATOM   205  C C   . PHE   A 1 51  ? 19.97425 32.18137 1.17157   1.000 19.57034 ? 31  PHE   A C   1 
ATOM   206  O O   . PHE   A 1 51  ? 20.73014 31.20961 1.15212   1.000 19.40913 ? 31  PHE   A O   1 
ATOM   207  C CB  . PHE   A 1 51  ? 20.76702 33.66795 -0.66260  1.000 18.02764 ? 31  PHE   A CB  1 
ATOM   208  C CG  . PHE   A 1 51  ? 19.61494 33.21145 -1.49599  1.000 19.02667 ? 31  PHE   A CG  1 
ATOM   209  C CD1 . PHE   A 1 51  ? 18.51130 34.02659 -1.69550  1.000 21.38790 ? 31  PHE   A CD1 1 
ATOM   210  C CD2 . PHE   A 1 51  ? 19.62470 31.95408 -2.07560  1.000 20.32546 ? 31  PHE   A CD2 1 
ATOM   211  C CE1 . PHE   A 1 51  ? 17.44496 33.58858 -2.46778  1.000 23.08754 ? 31  PHE   A CE1 1 
ATOM   212  C CE2 . PHE   A 1 51  ? 18.56883 31.51861 -2.84180  1.000 22.61562 ? 31  PHE   A CE2 1 
ATOM   213  C CZ  . PHE   A 1 51  ? 17.47648 32.32859 -3.03804  1.000 23.14392 ? 31  PHE   A CZ  1 
ATOM   214  N N   . CYS   A 1 52  ? 18.67302 32.08196 1.44950   1.000 17.84791 ? 32  CYS   A N   1 
ATOM   215  C CA  . CYS   A 1 52  ? 18.04713 30.82983 1.86640   1.000 19.83196 ? 32  CYS   A CA  1 
ATOM   216  C C   . CYS   A 1 52  ? 16.96778 30.37556 0.88688   1.000 19.06375 ? 32  CYS   A C   1 
ATOM   217  O O   . CYS   A 1 52  ? 16.35734 31.18111 0.17632   1.000 20.16669 ? 32  CYS   A O   1 
ATOM   218  C CB  . CYS   A 1 52  ? 17.39439 30.96967 3.24482   1.000 20.51979 ? 32  CYS   A CB  1 
ATOM   219  S SG  . CYS   A 1 52  ? 18.54102 31.35297 4.56758   1.000 21.43485 ? 32  CYS   A SG  1 
ATOM   220  N N   . ARG   A 1 53  ? 16.72132 29.05646 0.88269   1.000 18.20888 ? 33  ARG   A N   1 
ATOM   221  C CA  . ARG   A 1 53  ? 15.66183 28.44501 0.09302   1.000 19.00019 ? 33  ARG   A CA  1 
ATOM   222  C C   . ARG   A 1 53  ? 14.88944 27.46127 0.95802   1.000 18.85540 ? 33  ARG   A C   1 
ATOM   223  O O   . ARG   A 1 53  ? 15.46472 26.78113 1.81430   1.000 19.92683 ? 33  ARG   A O   1 
ATOM   224  C CB  . ARG   A 1 53  ? 16.21272 27.62880 -1.08069  1.000 22.68773 ? 33  ARG   A CB  1 
ATOM   225  C CG  . ARG   A 1 53  ? 16.90856 28.41851 -2.12410  1.000 23.08396 ? 33  ARG   A CG  1 
ATOM   226  C CD  . ARG   A 1 53  ? 17.18081 27.55533 -3.35400  1.000 22.37213 ? 33  ARG   A CD  1 
ATOM   227  N NE  . ARG   A 1 53  ? 18.02161 28.28558 -4.28930  1.000 22.07624 ? 33  ARG   A NE  1 
ATOM   228  C CZ  . ARG   A 1 53  ? 17.56459 29.04638 -5.27047  1.000 24.20758 ? 33  ARG   A CZ  1 
ATOM   229  N NH1 . ARG   A 1 53  ? 16.26766 29.12979 -5.53513  1.000 27.66304 ? 33  ARG   A NH1 1 
ATOM   230  N NH2 . ARG   A 1 53  ? 18.42923 29.74173 -6.00511  1.000 24.00136 ? 33  ARG   A NH2 1 
ATOM   231  N N   . TYR   A 1 54  ? 13.59011 27.35538 0.68731   1.000 21.49602 ? 34  TYR   A N   1 
ATOM   232  C CA  . TYR   A 1 54  ? 12.70285 26.46363 1.41396   1.000 22.21477 ? 34  TYR   A CA  1 
ATOM   233  C C   . TYR   A 1 54  ? 11.77429 25.78960 0.42585   1.000 22.82431 ? 34  TYR   A C   1 
ATOM   234  O O   . TYR   A 1 54  ? 11.24811 26.43564 -0.48584  1.000 24.35310 ? 34  TYR   A O   1 
ATOM   235  C CB  . TYR   A 1 54  ? 11.87164 27.22280 2.46599   1.000 22.45905 ? 34  TYR   A CB  1 
ATOM   236  C CG  . TYR   A 1 54  ? 12.77090 27.92831 3.43540   1.000 21.31613 ? 34  TYR   A CG  1 
ATOM   237  C CD1 . TYR   A 1 54  ? 13.29695 27.25421 4.52750   1.000 20.22489 ? 34  TYR   A CD1 1 
ATOM   238  C CD2 . TYR   A 1 54  ? 13.16223 29.24343 3.21853   1.000 19.85886 ? 34  TYR   A CD2 1 
ATOM   239  C CE1 . TYR   A 1 54  ? 14.16494 27.86523 5.39504   1.000 20.61389 ? 34  TYR   A CE1 1 
ATOM   240  C CE2 . TYR   A 1 54  ? 14.03411 29.88201 4.09401   1.000 20.06179 ? 34  TYR   A CE2 1 
ATOM   241  C CZ  . TYR   A 1 54  ? 14.53597 29.17730 5.17922   1.000 21.52682 ? 34  TYR   A CZ  1 
ATOM   242  O OH  . TYR   A 1 54  ? 15.40866 29.76759 6.05932   1.000 22.61472 ? 34  TYR   A OH  1 
ATOM   243  N N   . TRP   A 1 55  ? 11.57234 24.48927 0.61799   1.000 22.51410 ? 35  TRP   A N   1 
ATOM   244  C CA  . TRP   A 1 55  ? 10.56906 23.73676 -0.12473  1.000 23.60296 ? 35  TRP   A CA  1 
ATOM   245  C C   . TRP   A 1 55  ? 9.76482  22.97886 0.92704   1.000 25.09447 ? 35  TRP   A C   1 
ATOM   246  O O   . TRP   A 1 55  ? 10.18909 21.91482 1.39169   1.000 25.53927 ? 35  TRP   A O   1 
ATOM   247  C CB  . TRP   A 1 55  ? 11.21602 22.75537 -1.08420  1.000 23.67175 ? 35  TRP   A CB  1 
ATOM   248  C CG  . TRP   A 1 55  ? 12.18002 23.28447 -2.12162  1.000 23.13972 ? 35  TRP   A CG  1 
ATOM   249  C CD1 . TRP   A 1 55  ? 11.91479 23.49805 -3.43881  1.000 23.72672 ? 35  TRP   A CD1 1 
ATOM   250  C CD2 . TRP   A 1 55  ? 13.57943 23.56150 -1.94772  1.000 23.52212 ? 35  TRP   A CD2 1 
ATOM   251  N NE1 . TRP   A 1 55  ? 13.05083 23.90572 -4.09615  1.000 24.98250 ? 35  TRP   A NE1 1 
ATOM   252  C CE2 . TRP   A 1 55  ? 14.08672 23.95227 -3.20314  1.000 24.36631 ? 35  TRP   A CE2 1 
ATOM   253  C CE3 . TRP   A 1 55  ? 14.45418 23.50508 -0.85525  1.000 24.76353 ? 35  TRP   A CE3 1 
ATOM   254  C CZ2 . TRP   A 1 55  ? 15.42196 24.28294 -3.39802  1.000 24.79531 ? 35  TRP   A CZ2 1 
ATOM   255  C CZ3 . TRP   A 1 55  ? 15.78433 23.84331 -1.05058  1.000 23.79225 ? 35  TRP   A CZ3 1 
ATOM   256  C CH2 . TRP   A 1 55  ? 16.25476 24.22231 -2.31288  1.000 25.41915 ? 35  TRP   A CH2 1 
ATOM   257  N N   . ALA   A 1 56  ? 8.60959  23.51527 1.29279   1.000 26.47757 ? 36  ALA   A N   1 
ATOM   258  C CA  . ALA   A 1 56  ? 7.80100  22.90972 2.33095   1.000 27.82593 ? 36  ALA   A CA  1 
ATOM   259  C C   . ALA   A 1 56  ? 6.56744  22.26545 1.71860   1.000 30.83396 ? 36  ALA   A C   1 
ATOM   260  O O   . ALA   A 1 56  ? 6.02795  22.77635 0.73044   1.000 31.24269 ? 36  ALA   A O   1 
ATOM   261  C CB  . ALA   A 1 56  ? 7.36591  23.97026 3.34883   1.000 27.78591 ? 36  ALA   A CB  1 
ATOM   262  N N   . PRO   A 1 57  ? 6.10689  21.14358 2.26314   1.000 32.66883 ? 37  PRO   A N   1 
ATOM   263  C CA  . PRO   A 1 57  ? 4.90569  20.49925 1.73000   1.000 36.70262 ? 37  PRO   A CA  1 
ATOM   264  C C   . PRO   A 1 57  ? 3.65078  21.23341 2.18389   1.000 41.44149 ? 37  PRO   A C   1 
ATOM   265  O O   . PRO   A 1 57  ? 3.66997  22.05641 3.10133   1.000 40.21572 ? 37  PRO   A O   1 
ATOM   266  C CB  . PRO   A 1 57  ? 4.96687  19.09915 2.34577   1.000 35.37718 ? 37  PRO   A CB  1 
ATOM   267  C CG  . PRO   A 1 57  ? 5.67204  19.30172 3.64501   1.000 33.94357 ? 37  PRO   A CG  1 
ATOM   268  C CD  . PRO   A 1 57  ? 6.66940  20.41364 3.41308   1.000 32.99027 ? 37  PRO   A CD  1 
ATOM   269  N N   . THR   A 1 58  ? 2.54239  20.91887 1.50782   1.000 45.40542 ? 38  THR   A N   1 
ATOM   270  C CA  . THR   A 1 58  ? 1.25900  21.49265 1.89560   1.000 50.26784 ? 38  THR   A CA  1 
ATOM   271  C C   . THR   A 1 58  ? 0.74974  20.87113 3.19107   1.000 53.28132 ? 38  THR   A C   1 
ATOM   272  O O   . THR   A 1 58  ? 0.13346  21.55770 4.01426   1.000 54.08125 ? 38  THR   A O   1 
ATOM   273  C CB  . THR   A 1 58  ? 0.24765  21.31288 0.76377   1.000 52.16768 ? 38  THR   A CB  1 
ATOM   274  O OG1 . THR   A 1 58  ? 0.01572  19.91602 0.55541   1.000 53.99481 ? 38  THR   A OG1 1 
ATOM   275  C CG2 . THR   A 1 58  ? 0.78967  21.91519 -0.52214  1.000 52.58188 ? 38  THR   A CG2 1 
ATOM   276  N N   . GLY   A 1 59  ? 1.00764  19.58101 3.39538   1.000 53.60016 ? 39  GLY   A N   1 
ATOM   277  C CA  . GLY   A 1 59  ? 0.64970  18.91482 4.62762   1.000 53.60375 ? 39  GLY   A CA  1 
ATOM   278  C C   . GLY   A 1 59  ? 1.66542  19.16716 5.72748   1.000 53.54930 ? 39  GLY   A C   1 
ATOM   279  O O   . GLY   A 1 59  ? 2.60433  19.95326 5.59058   1.000 53.63216 ? 39  GLY   A O   1 
ATOM   280  N N   . THR   A 1 60  ? 1.46525  18.47268 6.84298   1.000 52.43451 ? 40  THR   A N   1 
ATOM   281  C CA  . THR   A 1 60  ? 2.37312  18.61043 7.97547   1.000 51.50303 ? 40  THR   A CA  1 
ATOM   282  C C   . THR   A 1 60  ? 3.67370  17.87604 7.67288   1.000 47.15888 ? 40  THR   A C   1 
ATOM   283  O O   . THR   A 1 60  ? 3.63803  16.72914 7.21139   1.000 48.08507 ? 40  THR   A O   1 
ATOM   284  C CB  . THR   A 1 60  ? 1.73476  18.02766 9.23149   1.000 55.06287 ? 40  THR   A CB  1 
ATOM   285  O OG1 . THR   A 1 60  ? 1.35470  16.67015 8.98354   1.000 57.95531 ? 40  THR   A OG1 1 
ATOM   286  C CG2 . THR   A 1 60  ? 0.50130  18.82747 9.62792   1.000 56.07448 ? 40  THR   A CG2 1 
ATOM   287  N N   . PRO   A 1 61  ? 4.83078  18.49050 7.91228   1.000 43.26857 ? 41  PRO   A N   1 
ATOM   288  C CA  . PRO   A 1 61  ? 6.09684  17.83713 7.55621   1.000 39.14236 ? 41  PRO   A CA  1 
ATOM   289  C C   . PRO   A 1 61  ? 6.38038  16.64566 8.45777   1.000 36.06028 ? 41  PRO   A C   1 
ATOM   290  O O   . PRO   A 1 61  ? 6.08912  16.66138 9.65666   1.000 36.54446 ? 41  PRO   A O   1 
ATOM   291  C CB  . PRO   A 1 61  ? 7.14209  18.94340 7.75853   1.000 40.58189 ? 41  PRO   A CB  1 
ATOM   292  C CG  . PRO   A 1 61  ? 6.36088  20.21901 7.83085   1.000 42.21042 ? 41  PRO   A CG  1 
ATOM   293  C CD  . PRO   A 1 61  ? 5.03772  19.85644 8.41586   1.000 42.30691 ? 41  PRO   A CD  1 
ATOM   294  N N   . LYS   A 1 62  ? 6.94705  15.59995 7.85984   1.000 33.52160 ? 42  LYS   A N   1 
ATOM   295  C CA  . LYS   A 1 62  ? 7.37754  14.42690 8.60777   1.000 32.06534 ? 42  LYS   A CA  1 
ATOM   296  C C   . LYS   A 1 62  ? 8.80947  14.54267 9.10645   1.000 30.30222 ? 42  LYS   A C   1 
ATOM   297  O O   . LYS   A 1 62  ? 9.17110  13.86643 10.07672  1.000 32.49271 ? 42  LYS   A O   1 
ATOM   298  C CB  . LYS   A 1 62  ? 7.24860  13.17576 7.73539   1.000 33.88160 ? 42  LYS   A CB  1 
ATOM   299  C CG  . LYS   A 1 62  ? 5.81646  12.89302 7.30205   1.000 38.17567 ? 42  LYS   A CG  1 
ATOM   300  C CD  . LYS   A 1 62  ? 5.69811  11.58019 6.54908   1.000 42.12628 ? 42  LYS   A CD  1 
ATOM   301  C CE  . LYS   A 1 62  ? 4.24732  11.29087 6.18994   1.000 45.21111 ? 42  LYS   A CE  1 
ATOM   302  N NZ  . LYS   A 1 62  ? 4.14379  10.49591 4.93496   1.000 47.18514 ? 42  LYS   A NZ  1 
ATOM   303  N N   . ALA   A 1 63  ? 9.62419  15.37763 8.46716   1.000 27.99045 ? 43  ALA   A N   1 
ATOM   304  C CA  . ALA   A 1 63  ? 11.01514 15.56623 8.84937   1.000 25.92081 ? 43  ALA   A CA  1 
ATOM   305  C C   . ALA   A 1 63  ? 11.50616 16.84971 8.20247   1.000 24.43001 ? 43  ALA   A C   1 
ATOM   306  O O   . ALA   A 1 63  ? 10.84642 17.42391 7.33471   1.000 25.75112 ? 43  ALA   A O   1 
ATOM   307  C CB  . ALA   A 1 63  ? 11.88648 14.38731 8.40169   1.000 26.17529 ? 43  ALA   A CB  1 
ATOM   308  N N   . LEU   A 1 64  ? 12.67403 17.29365 8.64615   1.000 22.96824 ? 44  LEU   A N   1 
ATOM   309  C CA  . LEU   A 1 64  ? 13.39481 18.39360 8.02611   1.000 22.41109 ? 44  LEU   A CA  1 
ATOM   310  C C   . LEU   A 1 64  ? 14.62722 17.82927 7.34608   1.000 22.37578 ? 44  LEU   A C   1 
ATOM   311  O O   . LEU   A 1 64  ? 15.20308 16.84382 7.80812   1.000 23.17580 ? 44  LEU   A O   1 
ATOM   312  C CB  . LEU   A 1 64  ? 13.87853 19.38230 9.08599   1.000 23.66793 ? 44  LEU   A CB  1 
ATOM   313  C CG  . LEU   A 1 64  ? 12.81292 19.93750 10.02015  1.000 27.48807 ? 44  LEU   A CG  1 
ATOM   314  C CD1 . LEU   A 1 64  ? 13.44818 20.83135 11.07984  1.000 28.24223 ? 44  LEU   A CD1 1 
ATOM   315  C CD2 . LEU   A 1 64  ? 11.75436 20.67233 9.22608   1.000 30.49048 ? 44  LEU   A CD2 1 
ATOM   316  N N   . ILE   A 1 65  ? 15.05057 18.46404 6.25536   1.000 21.35037 ? 45  ILE   A N   1 
ATOM   317  C CA  . ILE   A 1 65  ? 16.29186 18.05584 5.60813   1.000 20.53712 ? 45  ILE   A CA  1 
ATOM   318  C C   . ILE   A 1 65  ? 17.00929 19.28818 5.06675   1.000 19.69807 ? 45  ILE   A C   1 
ATOM   319  O O   . ILE   A 1 65  ? 16.43399 20.06051 4.28842   1.000 20.32738 ? 45  ILE   A O   1 
ATOM   320  C CB  . ILE   A 1 65  ? 16.09227 16.95982 4.53716   1.000 20.69194 ? 45  ILE   A CB  1 
ATOM   321  C CG1 . ILE   A 1 65  ? 17.43784 16.50438 3.95907   1.000 22.24020 ? 45  ILE   A CG1 1 
ATOM   322  C CG2 . ILE   A 1 65  ? 15.12055 17.40739 3.44935   1.000 22.48019 ? 45  ILE   A CG2 1 
ATOM   323  C CD1 . ILE   A 1 65  ? 17.39831 15.13121 3.26690   1.000 22.90188 ? 45  ILE   A CD1 1 
ATOM   324  N N   . PHE   A 1 66  ? 18.24640 19.49041 5.51435   1.000 18.42387 ? 46  PHE   A N   1 
ATOM   325  C CA  . PHE   A 1 66  ? 19.10370 20.55262 5.01071   1.000 18.24049 ? 46  PHE   A CA  1 
ATOM   326  C C   . PHE   A 1 66  ? 19.93741 20.05415 3.83762   1.000 17.43846 ? 46  PHE   A C   1 
ATOM   327  O O   . PHE   A 1 66  ? 20.59543 19.01248 3.93133   1.000 17.95443 ? 46  PHE   A O   1 
ATOM   328  C CB  . PHE   A 1 66  ? 20.04056 21.08305 6.10142   1.000 17.34155 ? 46  PHE   A CB  1 
ATOM   329  C CG  . PHE   A 1 66  ? 20.89416 22.23002 5.63054   1.000 17.59353 ? 46  PHE   A CG  1 
ATOM   330  C CD1 . PHE   A 1 66  ? 20.41337 23.52898 5.68911   1.000 19.31111 ? 46  PHE   A CD1 1 
ATOM   331  C CD2 . PHE   A 1 66  ? 22.15502 22.00538 5.08817   1.000 18.13583 ? 46  PHE   A CD2 1 
ATOM   332  C CE1 . PHE   A 1 66  ? 21.18403 24.60806 5.23167   1.000 18.53729 ? 46  PHE   A CE1 1 
ATOM   333  C CE2 . PHE   A 1 66  ? 22.93066 23.06190 4.62322   1.000 18.46252 ? 46  PHE   A CE2 1 
ATOM   334  C CZ  . PHE   A 1 66  ? 22.43924 24.38102 4.70588   1.000 19.04541 ? 46  PHE   A CZ  1 
ATOM   335  N N   . VAL   A 1 67  ? 19.93195 20.81938 2.74596   1.000 16.71824 ? 47  VAL   A N   1 
ATOM   336  C CA  . VAL   A 1 67  ? 20.69178 20.50114 1.54527   1.000 16.60288 ? 47  VAL   A CA  1 
ATOM   337  C C   . VAL   A 1 67  ? 21.91229 21.40962 1.48030   1.000 17.75898 ? 47  VAL   A C   1 
ATOM   338  O O   . VAL   A 1 67  ? 21.78782 22.64858 1.50181   1.000 18.95488 ? 47  VAL   A O   1 
ATOM   339  C CB  . VAL   A 1 67  ? 19.82048 20.64660 0.28804   1.000 17.96936 ? 47  VAL   A CB  1 
ATOM   340  C CG1 . VAL   A 1 67  ? 20.66257 20.45595 -0.97433  1.000 18.95383 ? 47  VAL   A CG1 1 
ATOM   341  C CG2 . VAL   A 1 67  ? 18.66462 19.65155 0.33082   1.000 19.00043 ? 47  VAL   A CG2 1 
ATOM   342  N N   . SER   A 1 68  ? 23.08986 20.79227 1.37657   1.000 17.28552 ? 48  SER   A N   1 
ATOM   343  C CA  . SER   A 1 68  ? 24.38019 21.46736 1.45616   1.000 17.45121 ? 48  SER   A CA  1 
ATOM   344  C C   . SER   A 1 68  ? 25.08043 21.35906 0.10564   1.000 17.05763 ? 48  SER   A C   1 
ATOM   345  O O   . SER   A 1 68  ? 25.58408 20.28518 -0.25556  1.000 16.70826 ? 48  SER   A O   1 
ATOM   346  C CB  . SER   A 1 68  ? 25.21403 20.83542 2.57222   1.000 17.74746 ? 48  SER   A CB  1 
ATOM   347  O OG  . SER   A 1 68  ? 26.49003 21.44281 2.66549   1.000 19.26011 ? 48  SER   A OG  1 
ATOM   348  N N   . HIS   A 1 69  ? 25.12386 22.47260 -0.63464  1.000 16.50332 ? 49  HIS   A N   1 
ATOM   349  C CA  . HIS   A 1 69  ? 25.75239 22.48308 -1.94509  1.000 15.98815 ? 49  HIS   A CA  1 
ATOM   350  C C   . HIS   A 1 69  ? 27.27633 22.52195 -1.81488  1.000 17.29857 ? 49  HIS   A C   1 
ATOM   351  O O   . HIS   A 1 69  ? 27.83308 22.70207 -0.72776  1.000 17.91914 ? 49  HIS   A O   1 
ATOM   352  C CB  . HIS   A 1 69  ? 25.23618 23.66055 -2.78270  1.000 16.85080 ? 49  HIS   A CB  1 
ATOM   353  C CG  . HIS   A 1 69  ? 25.76153 24.99877 -2.36046  1.000 16.95517 ? 49  HIS   A CG  1 
ATOM   354  N ND1 . HIS   A 1 69  ? 27.02698 25.43877 -2.69239  1.000 16.71999 ? 49  HIS   A ND1 1 
ATOM   355  C CD2 . HIS   A 1 69  ? 25.17287 26.01756 -1.68648  1.000 18.05235 ? 49  HIS   A CD2 1 
ATOM   356  C CE1 . HIS   A 1 69  ? 27.20325 26.66394 -2.22200  1.000 16.42452 ? 49  HIS   A CE1 1 
ATOM   357  N NE2 . HIS   A 1 69  ? 26.09291 27.03888 -1.60598  1.000 17.10674 ? 49  HIS   A NE2 1 
ATOM   358  N N   . GLY   A 1 70  ? 27.95845 22.35002 -2.94732  1.000 17.11156 ? 50  GLY   A N   1 
ATOM   359  C CA  . GLY   A 1 70  ? 29.40172 22.27539 -2.97272  1.000 16.79093 ? 50  GLY   A CA  1 
ATOM   360  C C   . GLY   A 1 70  ? 30.08326 23.54841 -3.46654  1.000 15.95984 ? 50  GLY   A C   1 
ATOM   361  O O   . GLY   A 1 70  ? 29.46721 24.59705 -3.68940  1.000 16.78336 ? 50  GLY   A O   1 
ATOM   362  N N   . ALA   A 1 71  ? 31.39805 23.41892 -3.66014  1.000 14.90786 ? 51  ALA   A N   1 
ATOM   363  C CA  . ALA   A 1 71  ? 32.23761 24.54123 -4.05563  1.000 16.41871 ? 51  ALA   A CA  1 
ATOM   364  C C   . ALA   A 1 71  ? 31.83478 25.04922 -5.43341  1.000 18.12414 ? 51  ALA   A C   1 
ATOM   365  O O   . ALA   A 1 71  ? 31.52669 24.26585 -6.33982  1.000 19.51231 ? 51  ALA   A O   1 
ATOM   366  C CB  . ALA   A 1 71  ? 33.69877 24.09804 -4.08933  1.000 18.20340 ? 51  ALA   A CB  1 
ATOM   367  N N   . GLY   A 1 72  ? 31.83787 26.37891 -5.58005  1.000 18.48223 ? 52  GLY   A N   1 
ATOM   368  C CA  . GLY   A 1 72  ? 31.55854 27.02576 -6.84065  1.000 20.03527 ? 52  GLY   A CA  1 
ATOM   369  C C   . GLY   A 1 72  ? 30.08794 27.15824 -7.18454  1.000 20.83767 ? 52  GLY   A C   1 
ATOM   370  O O   . GLY   A 1 72  ? 29.69736 28.08575 -7.90108  1.000 24.87188 ? 52  GLY   A O   1 
ATOM   371  N N   . GLU   A 1 73  ? 29.25821 26.23405 -6.70179  1.000 17.51927 ? 53  GLU   A N   1 
ATOM   372  C CA  . GLU   A 1 73  ? 27.85538 26.22358 -7.09987  1.000 17.05599 ? 53  GLU   A CA  1 
ATOM   373  C C   . GLU   A 1 73  ? 26.97753 26.89206 -6.04537  1.000 16.27997 ? 53  GLU   A C   1 
ATOM   374  O O   . GLU   A 1 73  ? 27.44225 27.77692 -5.32341  1.000 18.14994 ? 53  GLU   A O   1 
ATOM   375  C CB  . GLU   A 1 73  ? 27.38869 24.80359 -7.44115  1.000 17.79738 ? 53  GLU   A CB  1 
ATOM   376  C CG  . GLU   A 1 73  ? 27.60460 23.78737 -6.31266  1.000 17.74909 ? 53  GLU   A CG  1 
ATOM   377  C CD  . GLU   A 1 73  ? 26.73987 22.54166 -6.43022  1.000 18.09104 ? 53  GLU   A CD  1 
ATOM   378  O OE1 . GLU   A 1 73  ? 25.95385 22.39982 -7.39557  1.000 19.96389 ? 53  GLU   A OE1 1 
ATOM   379  O OE2 . GLU   A 1 73  ? 26.85769 21.69027 -5.53164  1.000 18.42684 ? 53  GLU   A OE2 1 
ATOM   380  N N   . HIS   A 1 74  ? 25.70671 26.50895 -5.97126  1.000 17.52280 ? 54  HIS   A N   1 
ATOM   381  C CA  . HIS   A 1 74  ? 24.75052 27.20187 -5.12129  1.000 18.31213 ? 54  HIS   A CA  1 
ATOM   382  C C   . HIS   A 1 74  ? 23.52506 26.31317 -4.95208  1.000 17.79239 ? 54  HIS   A C   1 
ATOM   383  O O   . HIS   A 1 74  ? 23.38346 25.27027 -5.60844  1.000 19.16475 ? 54  HIS   A O   1 
ATOM   384  C CB  . HIS   A 1 74  ? 24.36804 28.57349 -5.71324  1.000 16.93699 ? 54  HIS   A CB  1 
ATOM   385  C CG  . HIS   A 1 74  ? 23.68484 28.47268 -7.04390  1.000 17.38988 ? 54  HIS   A CG  1 
ATOM   386  N ND1 . HIS   A 1 74  ? 22.31557 28.52221 -7.18359  1.000 18.88748 ? 54  HIS   A ND1 1 
ATOM   387  C CD2 . HIS   A 1 74  ? 24.18375 28.27397 -8.28834  1.000 19.14594 ? 54  HIS   A CD2 1 
ATOM   388  C CE1 . HIS   A 1 74  ? 21.99967 28.38221 -8.45935  1.000 18.83464 ? 54  HIS   A CE1 1 
ATOM   389  N NE2 . HIS   A 1 74  ? 23.11481 28.22148 -9.14971  1.000 19.33558 ? 54  HIS   A NE2 1 
ATOM   390  N N   . SER   A 1 75  ? 22.64066 26.73680 -4.04122  1.000 17.18293 ? 55  SER   A N   1 
ATOM   391  C CA  . SER   A 1 75  ? 21.51196 25.90297 -3.62962  1.000 17.42965 ? 55  SER   A CA  1 
ATOM   392  C C   . SER   A 1 75  ? 20.46164 25.72120 -4.72230  1.000 17.61364 ? 55  SER   A C   1 
ATOM   393  O O   . SER   A 1 75  ? 19.68111 24.75949 -4.65476  1.000 19.65212 ? 55  SER   A O   1 
ATOM   394  C CB  . SER   A 1 75  ? 20.85459 26.49434 -2.38340  1.000 18.83772 ? 55  SER   A CB  1 
ATOM   395  O OG  . SER   A 1 75  ? 20.35670 27.79126 -2.67523  1.000 20.53038 ? 55  SER   A OG  1 
ATOM   396  N N   . GLY   A 1 76  ? 20.40710 26.61162 -5.71794  1.000 17.04563 ? 56  GLY   A N   1 
ATOM   397  C CA  . GLY   A 1 76  ? 19.40914 26.46464 -6.76454  1.000 18.08518 ? 56  GLY   A CA  1 
ATOM   398  C C   . GLY   A 1 76  ? 19.63215 25.25142 -7.64167  1.000 18.78775 ? 56  GLY   A C   1 
ATOM   399  O O   . GLY   A 1 76  ? 18.71935 24.83240 -8.36525  1.000 20.43577 ? 56  GLY   A O   1 
ATOM   400  N N   . ARG   A 1 77  ? 20.82228 24.67345 -7.58770  1.000 18.18250 ? 57  ARG   A N   1 
ATOM   401  C CA  . ARG   A 1 77  ? 21.08891 23.46506 -8.35043  1.000 18.49364 ? 57  ARG   A CA  1 
ATOM   402  C C   . ARG   A 1 77  ? 20.43985 22.22490 -7.75588  1.000 19.01229 ? 57  ARG   A C   1 
ATOM   403  O O   . ARG   A 1 77  ? 20.51659 21.15777 -8.36893  1.000 20.38861 ? 57  ARG   A O   1 
ATOM   404  C CB  . ARG   A 1 77  ? 22.59252 23.30607 -8.53120  1.000 21.87485 ? 57  ARG   A CB  1 
ATOM   405  C CG  . ARG   A 1 77  ? 23.04817 24.29829 -9.62219  1.000 24.58022 ? 57  ARG   A CG  1 
ATOM   406  C CD  . ARG   A 1 77  ? 24.52548 24.40369 -9.83382  1.000 22.48040 ? 57  ARG   A CD  1 
ATOM   407  N NE  . ARG   A 1 77  ? 25.16516 23.12734 -10.12239 1.000 19.13620 ? 57  ARG   A NE  1 
ATOM   408  C CZ  . ARG   A 1 77  ? 25.20172 22.53933 -11.30983 1.000 19.34329 ? 57  ARG   A CZ  1 
ATOM   409  N NH1 . ARG   A 1 77  ? 24.53845 23.02659 -12.35013 1.000 19.90328 ? 57  ARG   A NH1 1 
ATOM   410  N NH2 . ARG   A 1 77  ? 25.92348 21.43163 -11.45782 1.000 19.17816 ? 57  ARG   A NH2 1 
ATOM   411  N N   . TYR   A 1 78  ? 19.78559 22.34953 -6.60350  1.000 17.88575 ? 58  TYR   A N   1 
ATOM   412  C CA  . TYR   A 1 78  ? 19.16346 21.22040 -5.91992  1.000 17.82400 ? 58  TYR   A CA  1 
ATOM   413  C C   . TYR   A 1 78  ? 17.64418 21.22992 -6.04399  1.000 19.40582 ? 58  TYR   A C   1 
ATOM   414  O O   . TYR   A 1 78  ? 16.96871 20.47107 -5.34482  1.000 21.12367 ? 58  TYR   A O   1 
ATOM   415  C CB  . TYR   A 1 78  ? 19.66011 21.12261 -4.46818  1.000 18.61515 ? 58  TYR   A CB  1 
ATOM   416  C CG  . TYR   A 1 78  ? 21.12365 20.77206 -4.49671  1.000 18.67338 ? 58  TYR   A CG  1 
ATOM   417  C CD1 . TYR   A 1 78  ? 22.09124 21.75925 -4.73607  1.000 18.17950 ? 58  TYR   A CD1 1 
ATOM   418  C CD2 . TYR   A 1 78  ? 21.54741 19.44531 -4.38409  1.000 19.02617 ? 58  TYR   A CD2 1 
ATOM   419  C CE1 . TYR   A 1 78  ? 23.43362 21.43903 -4.83883  1.000 18.57653 ? 58  TYR   A CE1 1 
ATOM   420  C CE2 . TYR   A 1 78  ? 22.89108 19.12042 -4.47574  1.000 19.31809 ? 58  TYR   A CE2 1 
ATOM   421  C CZ  . TYR   A 1 78  ? 23.82684 20.12088 -4.70965  1.000 17.99248 ? 58  TYR   A CZ  1 
ATOM   422  O OH  . TYR   A 1 78  ? 25.15756 19.80368 -4.81603  1.000 18.57989 ? 58  TYR   A OH  1 
ATOM   423  N N   . GLU   A 1 79  ? 17.10862 22.03202 -6.97020  1.000 21.37752 ? 59  GLU   A N   1 
ATOM   424  C CA  . GLU   A 1 79  ? 15.66525 22.18466 -7.12345  1.000 21.89734 ? 59  GLU   A CA  1 
ATOM   425  C C   . GLU   A 1 79  ? 14.95980 20.84411 -7.29526  1.000 22.00601 ? 59  GLU   A C   1 
ATOM   426  O O   . GLU   A 1 79  ? 13.97808 20.55359 -6.60249  1.000 21.94568 ? 59  GLU   A O   1 
ATOM   427  C CB  . GLU   A 1 79  ? 15.38078 23.07569 -8.32728  1.000 25.71886 ? 59  GLU   A CB  1 
ATOM   428  C CG  . GLU   A 1 79  ? 13.95682 23.50510 -8.41090  1.000 32.91655 ? 59  GLU   A CG  1 
ATOM   429  C CD  . GLU   A 1 79  ? 13.59264 24.45650 -7.28421  1.000 37.65911 ? 59  GLU   A CD  1 
ATOM   430  O OE1 . GLU   A 1 79  ? 14.42921 25.30370 -6.90462  1.000 39.30808 ? 59  GLU   A OE1 1 
ATOM   431  O OE2 . GLU   A 1 79  ? 12.47251 24.34711 -6.76612  1.000 42.94142 ? 59  GLU   A OE2 1 
ATOM   432  N N   . GLU   A 1 80  ? 15.44227 20.01354 -8.22355  1.000 21.37922 ? 60  GLU   A N   1 
ATOM   433  C CA  . GLU   A 1 80  ? 14.74662 18.76336 -8.51715  1.000 22.67163 ? 60  GLU   A CA  1 
ATOM   434  C C   . GLU   A 1 80  ? 14.81614 17.78989 -7.34875  1.000 22.58735 ? 60  GLU   A C   1 
ATOM   435  O O   . GLU   A 1 80  ? 13.80629 17.16221 -7.00396  1.000 22.91391 ? 60  GLU   A O   1 
ATOM   436  C CB  . GLU   A 1 80  ? 15.29809 18.12529 -9.79041  1.000 26.38530 ? 60  GLU   A CB  1 
ATOM   437  C CG  . GLU   A 1 80  ? 14.82349 18.81107 -11.05361 1.000 37.79922 ? 60  GLU   A CG  1 
ATOM   438  C CD  . GLU   A 1 80  ? 13.31357 18.98100 -11.08089 1.000 48.47166 ? 60  GLU   A CD  1 
ATOM   439  O OE1 . GLU   A 1 80  ? 12.84243 20.13756 -11.08253 1.000 52.46720 ? 60  GLU   A OE1 1 
ATOM   440  O OE2 . GLU   A 1 80  ? 12.59590 17.95843 -11.08686 1.000 54.17670 ? 60  GLU   A OE2 1 
ATOM   441  N N   . LEU   A 1 81  ? 15.99782 17.63531 -6.73916  1.000 21.30760 ? 61  LEU   A N   1 
ATOM   442  C CA  . LEU   A 1 81  ? 16.10686 16.78275 -5.56087  1.000 22.05959 ? 61  LEU   A CA  1 
ATOM   443  C C   . LEU   A 1 81  ? 15.20654 17.27525 -4.44584  1.000 21.78532 ? 61  LEU   A C   1 
ATOM   444  O O   . LEU   A 1 81  ? 14.55377 16.47753 -3.76251  1.000 22.40598 ? 61  LEU   A O   1 
ATOM   445  C CB  . LEU   A 1 81  ? 17.54484 16.75111 -5.05036  1.000 22.96519 ? 61  LEU   A CB  1 
ATOM   446  C CG  . LEU   A 1 81  ? 18.53944 15.75107 -5.60740  1.000 25.46019 ? 61  LEU   A CG  1 
ATOM   447  C CD1 . LEU   A 1 81  ? 19.91819 16.04777 -5.01394  1.000 25.04121 ? 61  LEU   A CD1 1 
ATOM   448  C CD2 . LEU   A 1 81  ? 18.09333 14.31324 -5.30060  1.000 25.96615 ? 61  LEU   A CD2 1 
ATOM   449  N N   . ALA   A 1 82  ? 15.18295 18.59061 -4.23047  1.000 21.52522 ? 62  ALA   A N   1 
ATOM   450  C CA  . ALA   A 1 82  ? 14.37866 19.15462 -3.15196  1.000 22.57747 ? 62  ALA   A CA  1 
ATOM   451  C C   . ALA   A 1 82  ? 12.89986 18.91565 -3.39811  1.000 23.06657 ? 62  ALA   A C   1 
ATOM   452  O O   . ALA   A 1 82  ? 12.14968 18.61214 -2.46557  1.000 23.78297 ? 62  ALA   A O   1 
ATOM   453  C CB  . ALA   A 1 82  ? 14.66556 20.64955 -3.00694  1.000 20.93410 ? 62  ALA   A CB  1 
ATOM   454  N N   . ARG   A 1 83  ? 12.45926 19.04740 -4.65017  1.000 24.15693 ? 63  ARG   A N   1 
ATOM   455  C CA  . ARG   A 1 83  ? 11.05049 18.82663 -4.94745  1.000 26.53234 ? 63  ARG   A CA  1 
ATOM   456  C C   . ARG   A 1 83  ? 10.66297 17.37072 -4.75118  1.000 25.42775 ? 63  ARG   A C   1 
ATOM   457  O O   . ARG   A 1 83  ? 9.54521  17.08176 -4.30285  1.000 26.65996 ? 63  ARG   A O   1 
ATOM   458  C CB  . ARG   A 1 83  ? 10.72349 19.34555 -6.34461  1.000 30.07813 ? 63  ARG   A CB  1 
ATOM   459  C CG  . ARG   A 1 83  ? 10.80848 20.85895 -6.37396  1.000 34.53260 ? 63  ARG   A CG  1 
ATOM   460  C CD  . ARG   A 1 83  ? 10.71361 21.45204 -7.75085  1.000 40.55618 ? 63  ARG   A CD  1 
ATOM   461  N NE  . ARG   A 1 83  ? 10.71902 22.90726 -7.65666  1.000 45.10739 ? 63  ARG   A NE  1 
ATOM   462  C CZ  . ARG   A 1 83  ? 9.68755  23.63524 -7.24518  1.000 47.71556 ? 63  ARG   A CZ  1 
ATOM   463  N NH1 . ARG   A 1 83  ? 8.53756  23.07779 -6.89920  1.000 49.12491 ? 63  ARG   A NH1 1 
ATOM   464  N NH2 . ARG   A 1 83  ? 9.81480  24.95597 -7.17170  1.000 48.49718 ? 63  ARG   A NH2 1 
ATOM   465  N N   . MET   A 1 84  ? 11.57195 16.44384 -5.05580  1.000 23.93636 ? 64  MET   A N   1 
ATOM   466  C CA  A MET   A 1 84  ? 11.31360 15.03464 -4.77129  0.626 24.20160 ? 64  MET   A CA  1 
ATOM   467  C CA  B MET   A 1 84  ? 11.30040 15.03979 -4.77226  0.374 23.83867 ? 64  MET   A CA  1 
ATOM   468  C C   . MET   A 1 84  ? 11.16696 14.80602 -3.27129  1.000 24.57792 ? 64  MET   A C   1 
ATOM   469  O O   . MET   A 1 84  ? 10.24277 14.11837 -2.81697  1.000 27.16357 ? 64  MET   A O   1 
ATOM   470  C CB  A MET   A 1 84  ? 12.44264 14.16865 -5.34572  0.626 25.15858 ? 64  MET   A CB  1 
ATOM   471  C CB  B MET   A 1 84  ? 12.40142 14.15658 -5.36001  0.374 23.81491 ? 64  MET   A CB  1 
ATOM   472  C CG  A MET   A 1 84  ? 12.33834 12.67501 -5.00958  0.626 27.89251 ? 64  MET   A CG  1 
ATOM   473  C CG  B MET   A 1 84  ? 12.08010 12.67503 -5.28613  0.374 25.45208 ? 64  MET   A CG  1 
ATOM   474  S SD  A MET   A 1 84  ? 13.09605 12.18205 -3.44156  0.626 29.02818 ? 64  MET   A SD  1 
ATOM   475  S SD  B MET   A 1 84  ? 13.55061 11.64348 -5.31651  0.374 26.55097 ? 64  MET   A SD  1 
ATOM   476  C CE  A MET   A 1 84  ? 14.83655 12.29497 -3.83431  0.626 28.29286 ? 64  MET   A CE  1 
ATOM   477  C CE  B MET   A 1 84  ? 14.28260 12.04649 -3.72862  0.374 24.97504 ? 64  MET   A CE  1 
ATOM   478  N N   . LEU   A 1 85  ? 12.08476 15.37216 -2.48522  1.000 23.05657 ? 65  LEU   A N   1 
ATOM   479  C CA  . LEU   A 1 85  ? 12.03516 15.18494 -1.03705  1.000 23.83742 ? 65  LEU   A CA  1 
ATOM   480  C C   . LEU   A 1 85  ? 10.80499 15.85170 -0.43329  1.000 24.53686 ? 65  LEU   A C   1 
ATOM   481  O O   . LEU   A 1 85  ? 10.19004 15.31618 0.49630   1.000 24.60232 ? 65  LEU   A O   1 
ATOM   482  C CB  . LEU   A 1 85  ? 13.31716 15.71988 -0.40299  1.000 23.36873 ? 65  LEU   A CB  1 
ATOM   483  C CG  . LEU   A 1 85  ? 14.56601 14.90683 -0.75033  1.000 23.71517 ? 65  LEU   A CG  1 
ATOM   484  C CD1 . LEU   A 1 85  ? 15.82386 15.72458 -0.50959  1.000 24.61148 ? 65  LEU   A CD1 1 
ATOM   485  C CD2 . LEU   A 1 85  ? 14.57578 13.61904 0.07556   1.000 26.33487 ? 65  LEU   A CD2 1 
ATOM   486  N N   . MET   A 1 86  ? 10.43901 17.03032 -0.93339  1.000 26.05463 ? 66  MET   A N   1 
ATOM   487  C CA  A MET   A 1 86  ? 9.21884  17.65933 -0.44779  0.395 28.21320 ? 66  MET   A CA  1 
ATOM   488  C CA  B MET   A 1 86  ? 9.21256  17.68049 -0.48036  0.605 27.91061 ? 66  MET   A CA  1 
ATOM   489  C C   . MET   A 1 86  ? 7.99853  16.80668 -0.76991  1.000 29.14150 ? 66  MET   A C   1 
ATOM   490  O O   . MET   A 1 86  ? 7.04239  16.76854 0.01475   1.000 29.34738 ? 66  MET   A O   1 
ATOM   491  C CB  A MET   A 1 86  ? 9.09336  19.07625 -1.01030  0.395 29.00148 ? 66  MET   A CB  1 
ATOM   492  C CB  B MET   A 1 86  ? 9.08635  19.04876 -1.15776  0.605 28.08442 ? 66  MET   A CB  1 
ATOM   493  C CG  A MET   A 1 86  ? 7.98702  19.89214 -0.37622  0.395 30.67032 ? 66  MET   A CG  1 
ATOM   494  C CG  B MET   A 1 86  ? 7.71840  19.70143 -1.06205  0.605 30.37388 ? 66  MET   A CG  1 
ATOM   495  S SD  A MET   A 1 86  ? 6.55235  19.99053 -1.45366  0.395 33.16291 ? 66  MET   A SD  1 
ATOM   496  S SD  B MET   A 1 86  ? 7.70637  21.34149 -1.81784  0.605 30.86577 ? 66  MET   A SD  1 
ATOM   497  C CE  A MET   A 1 86  ? 7.23020  20.94495 -2.80948  0.395 32.88971 ? 66  MET   A CE  1 
ATOM   498  C CE  B MET   A 1 86  ? 8.32737  21.00604 -3.45854  0.605 29.21168 ? 66  MET   A CE  1 
ATOM   499  N N   . GLY   A 1 87  ? 8.02506  16.08933 -1.89271  1.000 30.10820 ? 67  GLY   A N   1 
ATOM   500  C CA  . GLY   A 1 87  ? 6.94301  15.18079 -2.22932  1.000 30.05702 ? 67  GLY   A CA  1 
ATOM   501  C C   . GLY   A 1 87  ? 6.80035  14.01706 -1.27041  1.000 31.28881 ? 67  GLY   A C   1 
ATOM   502  O O   . GLY   A 1 87  ? 5.74826  13.37011 -1.24710  1.000 32.64517 ? 67  GLY   A O   1 
ATOM   503  N N   . LEU   A 1 88  ? 7.83987  13.72288 -0.49177  1.000 31.15499 ? 68  LEU   A N   1 
ATOM   504  C CA  . LEU   A 1 88  ? 7.76785  12.76011 0.59862   1.000 31.19150 ? 68  LEU   A CA  1 
ATOM   505  C C   . LEU   A 1 88  ? 7.28302  13.39542 1.89217   1.000 33.94253 ? 68  LEU   A C   1 
ATOM   506  O O   . LEU   A 1 88  ? 7.31682  12.74386 2.94168   1.000 35.14351 ? 68  LEU   A O   1 
ATOM   507  C CB  . LEU   A 1 88  ? 9.13750  12.11818 0.83069   1.000 32.73565 ? 68  LEU   A CB  1 
ATOM   508  C CG  . LEU   A 1 88  ? 9.71723  11.26075 -0.28896  1.000 35.32203 ? 68  LEU   A CG  1 
ATOM   509  C CD1 . LEU   A 1 88  ? 11.15729 10.89229 0.03381   1.000 36.58164 ? 68  LEU   A CD1 1 
ATOM   510  C CD2 . LEU   A 1 88  ? 8.86514  10.01451 -0.48651  1.000 36.23829 ? 68  LEU   A CD2 1 
ATOM   511  N N   . ASP   A 1 89  ? 6.85178  14.65724 1.83477   1.000 32.78546 ? 69  ASP   A N   1 
ATOM   512  C CA  . ASP   A 1 89  ? 6.39280  15.41291 2.99756   1.000 33.42318 ? 69  ASP   A CA  1 
ATOM   513  C C   . ASP   A 1 89  ? 7.52571  15.76157 3.95321   1.000 31.80930 ? 69  ASP   A C   1 
ATOM   514  O O   . ASP   A 1 89  ? 7.31310  15.88063 5.16183   1.000 33.84228 ? 69  ASP   A O   1 
ATOM   515  C CB  . ASP   A 1 89  ? 5.21597  14.75365 3.72467   1.000 39.55185 ? 69  ASP   A CB  1 
ATOM   516  C CG  . ASP   A 1 89  ? 3.93884  14.80113 2.91648   1.000 46.62633 ? 69  ASP   A CG  1 
ATOM   517  O OD1 . ASP   A 1 89  ? 3.79192  15.71737 2.07869   1.000 48.70726 ? 69  ASP   A OD1 1 
ATOM   518  O OD2 . ASP   A 1 89  ? 3.08048  13.92153 3.11927   1.000 51.76997 ? 69  ASP   A OD2 1 
ATOM   519  N N   . LEU   A 1 90  ? 8.73101  15.93320 3.42190   1.000 28.93816 ? 70  LEU   A N   1 
ATOM   520  C CA  . LEU   A 1 90  ? 9.82055  16.54523 4.16468   1.000 26.49436 ? 70  LEU   A CA  1 
ATOM   521  C C   . LEU   A 1 90  ? 9.86867  18.02861 3.84582   1.000 25.95381 ? 70  LEU   A C   1 
ATOM   522  O O   . LEU   A 1 90  ? 9.57993  18.44468 2.72065   1.000 25.82839 ? 70  LEU   A O   1 
ATOM   523  C CB  . LEU   A 1 90  ? 11.17373 15.92309 3.81776   1.000 26.49380 ? 70  LEU   A CB  1 
ATOM   524  C CG  . LEU   A 1 90  ? 11.48667 14.60046 4.52359   1.000 29.07868 ? 70  LEU   A CG  1 
ATOM   525  C CD1 . LEU   A 1 90  ? 10.90933 13.45139 3.73247   1.000 31.42994 ? 70  LEU   A CD1 1 
ATOM   526  C CD2 . LEU   A 1 90  ? 12.98372 14.42464 4.72669   1.000 28.65888 ? 70  LEU   A CD2 1 
ATOM   527  N N   . LEU   A 1 91  ? 10.22990 18.81854 4.84446   1.000 24.93948 ? 71  LEU   A N   1 
ATOM   528  C CA  . LEU   A 1 91  ? 10.49625 20.23507 4.65156   1.000 24.68771 ? 71  LEU   A CA  1 
ATOM   529  C C   . LEU   A 1 91  ? 11.97799 20.36504 4.32821   1.000 23.67525 ? 71  LEU   A C   1 
ATOM   530  O O   . LEU   A 1 91  ? 12.83519 20.08359 5.17201   1.000 24.03417 ? 71  LEU   A O   1 
ATOM   531  C CB  . LEU   A 1 91  ? 10.11500 21.02561 5.89839   1.000 26.30898 ? 71  LEU   A CB  1 
ATOM   532  C CG  . LEU   A 1 91  ? 9.91023  22.52679 5.67763   1.000 28.68571 ? 71  LEU   A CG  1 
ATOM   533  C CD1 . LEU   A 1 91  ? 9.27278  23.11153 6.91248   1.000 29.05335 ? 71  LEU   A CD1 1 
ATOM   534  C CD2 . LEU   A 1 91  ? 11.20858 23.26092 5.35304   1.000 29.85383 ? 71  LEU   A CD2 1 
ATOM   535  N N   . VAL   A 1 92  ? 12.27281 20.77862 3.10336   1.000 22.24089 ? 72  VAL   A N   1 
ATOM   536  C CA  . VAL   A 1 92  ? 13.63590 20.89441 2.61279   1.000 21.57057 ? 72  VAL   A CA  1 
ATOM   537  C C   . VAL   A 1 92  ? 14.06297 22.34009 2.76950   1.000 19.99550 ? 72  VAL   A C   1 
ATOM   538  O O   . VAL   A 1 92  ? 13.28765 23.25985 2.48724   1.000 21.95876 ? 72  VAL   A O   1 
ATOM   539  C CB  . VAL   A 1 92  ? 13.70991 20.46439 1.13787   1.000 20.68750 ? 72  VAL   A CB  1 
ATOM   540  C CG1 . VAL   A 1 92  ? 15.16063 20.37756 0.69142   1.000 20.10864 ? 72  VAL   A CG1 1 
ATOM   541  C CG2 . VAL   A 1 92  ? 12.97449 19.13532 0.93716   1.000 21.87264 ? 72  VAL   A CG2 1 
ATOM   542  N N   . PHE   A 1 93  ? 15.28919 22.55004 3.22545   1.000 18.97377 ? 73  PHE   A N   1 
ATOM   543  C CA  . PHE   A 1 93  ? 15.79413 23.90729 3.35538   1.000 18.71231 ? 73  PHE   A CA  1 
ATOM   544  C C   . PHE   A 1 93  ? 17.27858 23.93158 3.02634   1.000 18.24222 ? 73  PHE   A C   1 
ATOM   545  O O   . PHE   A 1 93  ? 17.96506 22.90880 3.08200   1.000 18.88429 ? 73  PHE   A O   1 
ATOM   546  C CB  . PHE   A 1 93  ? 15.44943 24.55245 4.71722   1.000 19.74816 ? 73  PHE   A CB  1 
ATOM   547  C CG  . PHE   A 1 93  ? 16.08878 23.88409 5.91378   1.000 20.27011 ? 73  PHE   A CG  1 
ATOM   548  C CD1 . PHE   A 1 93  ? 15.71553 22.60217 6.30893   1.000 20.60447 ? 73  PHE   A CD1 1 
ATOM   549  C CD2 . PHE   A 1 93  ? 17.03296 24.55944 6.67222   1.000 20.45755 ? 73  PHE   A CD2 1 
ATOM   550  C CE1 . PHE   A 1 93  ? 16.29868 22.00108 7.41625   1.000 21.25268 ? 73  PHE   A CE1 1 
ATOM   551  C CE2 . PHE   A 1 93  ? 17.61753 23.96270 7.78562   1.000 21.62721 ? 73  PHE   A CE2 1 
ATOM   552  C CZ  . PHE   A 1 93  ? 17.24611 22.68775 8.15563   1.000 20.73460 ? 73  PHE   A CZ  1 
ATOM   553  N N   . ALA   A 1 94  ? 17.76210 25.11380 2.65142   1.000 19.45799 ? 74  ALA   A N   1 
ATOM   554  C CA  . ALA   A 1 94  ? 19.13972 25.25582 2.21363   1.000 17.32629 ? 74  ALA   A CA  1 
ATOM   555  C C   . ALA   A 1 94  ? 19.52207 26.71611 2.33043   1.000 17.50561 ? 74  ALA   A C   1 
ATOM   556  O O   . ALA   A 1 94  ? 18.66506 27.59345 2.44881   1.000 17.61454 ? 74  ALA   A O   1 
ATOM   557  C CB  . ALA   A 1 94  ? 19.31137 24.82181 0.75429   1.000 18.85015 ? 74  ALA   A CB  1 
ATOM   558  N N   . HIS   A 1 95  ? 20.82280 26.96403 2.27227   1.000 17.07914 ? 75  HIS   A N   1 
ATOM   559  C CA  . HIS   A 1 95  ? 21.31209 28.30588 2.01111   1.000 18.39032 ? 75  HIS   A CA  1 
ATOM   560  C C   . HIS   A 1 95  ? 22.53531 28.21966 1.11513   1.000 17.73738 ? 75  HIS   A C   1 
ATOM   561  O O   . HIS   A 1 95  ? 23.15981 27.16218 0.97430   1.000 18.80902 ? 75  HIS   A O   1 
ATOM   562  C CB  . HIS   A 1 95  ? 21.57478 29.11161 3.29502   1.000 17.76456 ? 75  HIS   A CB  1 
ATOM   563  C CG  . HIS   A 1 95  ? 22.60214 28.51096 4.20322   1.000 17.85666 ? 75  HIS   A CG  1 
ATOM   564  N ND1 . HIS   A 1 95  ? 22.28087 27.99720 5.44198   1.000 18.15452 ? 75  HIS   A ND1 1 
ATOM   565  C CD2 . HIS   A 1 95  ? 23.94334 28.37412 4.07424   1.000 19.92957 ? 75  HIS   A CD2 1 
ATOM   566  C CE1 . HIS   A 1 95  ? 23.37669 27.55638 6.03203   1.000 18.16311 ? 75  HIS   A CE1 1 
ATOM   567  N NE2 . HIS   A 1 95  ? 24.39968 27.77168 5.22460   1.000 18.57298 ? 75  HIS   A NE2 1 
ATOM   568  N N   . ASP   A 1 96  ? 22.86398 29.34714 0.48747   1.000 16.03560 ? 76  ASP   A N   1 
ATOM   569  C CA  . ASP   A 1 96  ? 24.11757 29.44479 -0.24239  1.000 16.22492 ? 76  ASP   A CA  1 
ATOM   570  C C   . ASP   A 1 96  ? 25.21585 29.70633 0.77979   1.000 16.58515 ? 76  ASP   A C   1 
ATOM   571  O O   . ASP   A 1 96  ? 25.09081 30.61350 1.61306   1.000 18.17179 ? 76  ASP   A O   1 
ATOM   572  C CB  . ASP   A 1 96  ? 24.05681 30.54265 -1.30485  1.000 18.06749 ? 76  ASP   A CB  1 
ATOM   573  C CG  . ASP   A 1 96  ? 23.10471 30.20394 -2.44253  1.000 18.43427 ? 76  ASP   A CG  1 
ATOM   574  O OD1 . ASP   A 1 96  ? 22.64279 29.03594 -2.51300  1.000 19.89589 ? 76  ASP   A OD1 1 
ATOM   575  O OD2 . ASP   A 1 96  ? 22.80146 31.10820 -3.25716  1.000 18.83197 ? 76  ASP   A OD2 1 
ATOM   576  N N   . HIS   A 1 97  ? 26.24482 28.86008 0.77006   1.000 17.21167 ? 77  HIS   A N   1 
ATOM   577  C CA  . HIS   A 1 97  ? 27.35206 29.04244 1.68796   1.000 16.84559 ? 77  HIS   A CA  1 
ATOM   578  C C   . HIS   A 1 97  ? 27.99150 30.40740 1.44759   1.000 17.63503 ? 77  HIS   A C   1 
ATOM   579  O O   . HIS   A 1 97  ? 27.89327 30.98374 0.35691   1.000 18.76466 ? 77  HIS   A O   1 
ATOM   580  C CB  . HIS   A 1 97  ? 28.40259 27.95858 1.46738   1.000 17.35629 ? 77  HIS   A CB  1 
ATOM   581  C CG  . HIS   A 1 97  ? 27.88695 26.56695 1.66380   1.000 17.23631 ? 77  HIS   A CG  1 
ATOM   582  N ND1 . HIS   A 1 97  ? 27.29453 26.15074 2.83656   1.000 18.26639 ? 77  HIS   A ND1 1 
ATOM   583  C CD2 . HIS   A 1 97  ? 27.89298 25.49070 0.84037   1.000 18.95930 ? 77  HIS   A CD2 1 
ATOM   584  C CE1 . HIS   A 1 97  ? 26.94464 24.87910 2.72042   1.000 19.17029 ? 77  HIS   A CE1 1 
ATOM   585  N NE2 . HIS   A 1 97  ? 27.30616 24.45378 1.52359   1.000 19.27283 ? 77  HIS   A NE2 1 
ATOM   586  N N   . VAL   A 1 98  ? 28.65318 30.92599 2.48685   1.000 18.31615 ? 78  VAL   A N   1 
ATOM   587  C CA  A VAL   A 1 98  ? 29.31085 32.21109 2.33608   0.621 20.49589 ? 78  VAL   A CA  1 
ATOM   588  C CA  B VAL   A 1 98  ? 29.36703 32.19344 2.37106   0.379 19.95504 ? 78  VAL   A CA  1 
ATOM   589  C C   . VAL   A 1 98  ? 30.24427 32.16972 1.12774   1.000 20.33025 ? 78  VAL   A C   1 
ATOM   590  O O   . VAL   A 1 98  ? 30.86500 31.14720 0.81223   1.000 19.70820 ? 78  VAL   A O   1 
ATOM   591  C CB  A VAL   A 1 98  ? 30.00536 32.62646 3.64562   0.621 21.77139 ? 78  VAL   A CB  1 
ATOM   592  C CB  B VAL   A 1 98  ? 30.20379 32.42322 3.64329   0.379 20.15633 ? 78  VAL   A CB  1 
ATOM   593  C CG1 A VAL   A 1 98  ? 31.19002 31.72823 3.94039   0.621 21.34706 ? 78  VAL   A CG1 1 
ATOM   594  C CG1 B VAL   A 1 98  ? 31.34379 33.40432 3.38480   0.379 21.01212 ? 78  VAL   A CG1 1 
ATOM   595  C CG2 A VAL   A 1 98  ? 30.40473 34.09926 3.59998   0.621 23.07841 ? 78  VAL   A CG2 1 
ATOM   596  C CG2 B VAL   A 1 98  ? 29.32243 32.91701 4.77815   0.379 19.64967 ? 78  VAL   A CG2 1 
ATOM   597  N N   . GLY   A 1 99  ? 30.29479 33.28760 0.40743   1.000 19.27364 ? 79  GLY   A N   1 
ATOM   598  C CA  . GLY   A 1 99  ? 31.11012 33.36109 -0.78707  1.000 18.25161 ? 79  GLY   A CA  1 
ATOM   599  C C   . GLY   A 1 99  ? 30.54227 32.66682 -2.00251  1.000 18.15062 ? 79  GLY   A C   1 
ATOM   600  O O   . GLY   A 1 99  ? 31.24469 32.56253 -3.01404  1.000 20.36549 ? 79  GLY   A O   1 
ATOM   601  N N   . HIS   A 1 100 ? 29.29659 32.18986 -1.94337  1.000 17.04736 ? 80  HIS   A N   1 
ATOM   602  C CA  . HIS   A 1 100 ? 28.69992 31.43997 -3.04047  1.000 17.77090 ? 80  HIS   A CA  1 
ATOM   603  C C   . HIS   A 1 100 ? 27.33181 32.00289 -3.39138  1.000 17.91110 ? 80  HIS   A C   1 
ATOM   604  O O   . HIS   A 1 100 ? 26.63508 32.56039 -2.54084  1.000 19.41051 ? 80  HIS   A O   1 
ATOM   605  C CB  . HIS   A 1 100 ? 28.52118 29.95346 -2.66693  1.000 17.49482 ? 80  HIS   A CB  1 
ATOM   606  C CG  . HIS   A 1 100 ? 29.80524 29.20447 -2.59840  1.000 19.29227 ? 80  HIS   A CG  1 
ATOM   607  N ND1 . HIS   A 1 100 ? 30.69745 29.35209 -1.55909  1.000 20.07863 ? 80  HIS   A ND1 1 
ATOM   608  C CD2 . HIS   A 1 100 ? 30.35882 28.31029 -3.45174  1.000 20.13677 ? 80  HIS   A CD2 1 
ATOM   609  C CE1 . HIS   A 1 100 ? 31.74416 28.57279 -1.77275  1.000 21.90115 ? 80  HIS   A CE1 1 
ATOM   610  N NE2 . HIS   A 1 100 ? 31.55982 27.92509 -2.90981  1.000 23.01139 ? 80  HIS   A NE2 1 
ATOM   611  N N   . GLY   A 1 101 ? 26.95060 31.82113 -4.65233  1.000 18.82768 ? 81  GLY   A N   1 
ATOM   612  C CA  . GLY   A 1 101 ? 25.60135 32.09196 -5.10102  1.000 19.65589 ? 81  GLY   A CA  1 
ATOM   613  C C   . GLY   A 1 101 ? 25.12276 33.48891 -4.75886  1.000 19.72745 ? 81  GLY   A C   1 
ATOM   614  O O   . GLY   A 1 101 ? 25.76398 34.48651 -5.10991  1.000 21.02628 ? 81  GLY   A O   1 
ATOM   615  N N   . GLN   A 1 102 ? 23.99530 33.56939 -4.06045  1.000 17.84150 ? 82  GLN   A N   1 
ATOM   616  C CA  . GLN   A 1 102 ? 23.37438 34.83864 -3.71837  1.000 18.04943 ? 82  GLN   A CA  1 
ATOM   617  C C   . GLN   A 1 102 ? 23.69654 35.28307 -2.29946  1.000 18.87988 ? 82  GLN   A C   1 
ATOM   618  O O   . GLN   A 1 102 ? 23.12293 36.26357 -1.81883  1.000 19.85462 ? 82  GLN   A O   1 
ATOM   619  C CB  . GLN   A 1 102 ? 21.86784 34.74837 -3.94804  1.000 19.51150 ? 82  GLN   A CB  1 
ATOM   620  C CG  . GLN   A 1 102 ? 21.52583 34.36895 -5.38258  1.000 19.74377 ? 82  GLN   A CG  1 
ATOM   621  C CD  . GLN   A 1 102 ? 20.03268 34.32845 -5.61784  1.000 21.53629 ? 82  GLN   A CD  1 
ATOM   622  O OE1 . GLN   A 1 102 ? 19.37898 35.36593 -5.65803  1.000 25.87410 ? 82  GLN   A OE1 1 
ATOM   623  N NE2 . GLN   A 1 102 ? 19.48045 33.12939 -5.74202  1.000 21.64173 ? 82  GLN   A NE2 1 
ATOM   624  N N   . SER   A 1 103 ? 24.60948 34.59921 -1.62870  1.000 18.73142 ? 83  SER   A N   1 
ATOM   625  C CA  . SER   A 1 103 ? 25.03792 34.99616 -0.29898  1.000 16.70169 ? 83  SER   A CA  1 
ATOM   626  C C   . SER   A 1 103 ? 26.19518 35.98109 -0.40024  1.000 18.30747 ? 83  SER   A C   1 
ATOM   627  O O   . SER   A 1 103 ? 26.84129 36.11540 -1.44126  1.000 20.14970 ? 83  SER   A O   1 
ATOM   628  C CB  . SER   A 1 103 ? 25.47253 33.76719 0.49908   1.000 17.71319 ? 83  SER   A CB  1 
ATOM   629  O OG  . SER   A 1 103 ? 24.33362 32.97924 0.81282   1.000 17.69259 ? 83  SER   A OG  1 
ATOM   630  N N   . GLU   A 1 104 ? 26.45484 36.66523 0.70729   1.000 19.54160 ? 84  GLU   A N   1 
ATOM   631  C CA  . GLU   A 1 104 ? 27.53270 37.63952 0.73814   1.000 19.26471 ? 84  GLU   A CA  1 
ATOM   632  C C   . GLU   A 1 104 ? 28.88468 36.93892 0.84946   1.000 20.59380 ? 84  GLU   A C   1 
ATOM   633  O O   . GLU   A 1 104 ? 28.98066 35.72108 1.05299   1.000 21.62112 ? 84  GLU   A O   1 
ATOM   634  C CB  . GLU   A 1 104 ? 27.33271 38.61175 1.89727   1.000 20.49228 ? 84  GLU   A CB  1 
ATOM   635  C CG  . GLU   A 1 104 ? 26.21365 39.62370 1.65421   1.000 22.59392 ? 84  GLU   A CG  1 
ATOM   636  C CD  . GLU   A 1 104 ? 26.10699 40.66073 2.76265   1.000 24.17209 ? 84  GLU   A CD  1 
ATOM   637  O OE1 . GLU   A 1 104 ? 26.35747 40.31062 3.94012   1.000 24.31956 ? 84  GLU   A OE1 1 
ATOM   638  O OE2 . GLU   A 1 104 ? 25.78545 41.83288 2.45348   1.000 27.11283 ? 84  GLU   A OE2 1 
ATOM   639  N N   . GLY   A 1 105 ? 29.93636 37.72602 0.71818   1.000 22.09804 ? 85  GLY   A N   1 
ATOM   640  C CA  . GLY   A 1 105 ? 31.29485 37.25179 0.91785   1.000 23.77577 ? 85  GLY   A CA  1 
ATOM   641  C C   . GLY   A 1 105 ? 32.08206 37.30335 -0.37631  1.000 24.66626 ? 85  GLY   A C   1 
ATOM   642  O O   . GLY   A 1 105 ? 31.54143 37.07291 -1.46312  1.000 25.13057 ? 85  GLY   A O   1 
ATOM   643  N N   . GLU   A 1 106 ? 33.37186 37.61813 -0.26656  1.000 25.63029 ? 86  GLU   A N   1 
ATOM   644  C CA  . GLU   A 1 106 ? 34.23912 37.52697 -1.43095  1.000 28.24648 ? 86  GLU   A CA  1 
ATOM   645  C C   . GLU   A 1 106 ? 34.12695 36.12913 -2.03062  1.000 26.40542 ? 86  GLU   A C   1 
ATOM   646  O O   . GLU   A 1 106 ? 34.07399 35.12836 -1.30703  1.000 25.86180 ? 86  GLU   A O   1 
ATOM   647  C CB  . GLU   A 1 106 ? 35.68323 37.81243 -1.02881  1.000 34.48493 ? 86  GLU   A CB  1 
ATOM   648  C CG  . GLU   A 1 106 ? 36.62256 37.96809 -2.20922  1.000 45.18417 ? 86  GLU   A CG  1 
ATOM   649  C CD  . GLU   A 1 106 ? 38.04006 38.31700 -1.79004  1.000 52.60822 ? 86  GLU   A CD  1 
ATOM   650  O OE1 . GLU   A 1 106 ? 38.93311 38.32259 -2.66711  1.000 55.31711 ? 86  GLU   A OE1 1 
ATOM   651  O OE2 . GLU   A 1 106 ? 38.25823 38.58407 -0.58590  1.000 55.31750 ? 86  GLU   A OE2 1 
ATOM   652  N N   . ARG   A 1 107 ? 34.05573 36.06876 -3.35921  1.000 25.56781 ? 87  ARG   A N   1 
ATOM   653  C CA  . ARG   A 1 107 ? 33.70120 34.81729 -4.02507  1.000 26.13155 ? 87  ARG   A CA  1 
ATOM   654  C C   . ARG   A 1 107 ? 34.73931 33.73914 -3.76136  1.000 28.12618 ? 87  ARG   A C   1 
ATOM   655  O O   . ARG   A 1 107 ? 35.94280 33.96098 -3.92541  1.000 28.76025 ? 87  ARG   A O   1 
ATOM   656  C CB  . ARG   A 1 107 ? 33.55271 35.02297 -5.53281  1.000 27.49090 ? 87  ARG   A CB  1 
ATOM   657  C CG  . ARG   A 1 107 ? 32.50091 36.05497 -5.95948  1.000 30.37028 ? 87  ARG   A CG  1 
ATOM   658  C CD  . ARG   A 1 107 ? 31.08193 35.57728 -5.65329  1.000 29.80458 ? 87  ARG   A CD  1 
ATOM   659  N NE  . ARG   A 1 107 ? 30.72132 35.84745 -4.27184  1.000 27.36763 ? 87  ARG   A NE  1 
ATOM   660  C CZ  . ARG   A 1 107 ? 29.54443 35.58553 -3.72346  1.000 25.66004 ? 87  ARG   A CZ  1 
ATOM   661  N NH1 . ARG   A 1 107 ? 28.56959 35.01794 -4.41126  1.000 26.31782 ? 87  ARG   A NH1 1 
ATOM   662  N NH2 . ARG   A 1 107 ? 29.34268 35.90402 -2.45085  1.000 23.35528 ? 87  ARG   A NH2 1 
ATOM   663  N N   . MET   A 1 108 ? 34.25238 32.56320 -3.35750  1.000 28.24379 ? 88  MET   A N   1 
ATOM   664  C CA  . MET   A 1 108 ? 35.07226 31.37085 -3.15629  1.000 30.23828 ? 88  MET   A CA  1 
ATOM   665  C C   . MET   A 1 108 ? 36.29491 31.63770 -2.27689  1.000 29.26629 ? 88  MET   A C   1 
ATOM   666  O O   . MET   A 1 108 ? 37.41288 31.21139 -2.57031  1.000 31.40874 ? 88  MET   A O   1 
ATOM   667  C CB  . MET   A 1 108 ? 35.41522 30.67018 -4.47585  1.000 32.30308 ? 88  MET   A CB  1 
ATOM   668  C CG  . MET   A 1 108 ? 34.18873 30.09824 -5.18804  1.000 32.69242 ? 88  MET   A CG  1 
ATOM   669  S SD  . MET   A 1 108 ? 34.59268 29.03832 -6.58734  1.000 36.56421 ? 88  MET   A SD  1 
ATOM   670  C CE  . MET   A 1 108 ? 35.08864 27.57145 -5.70450  1.000 37.51006 ? 88  MET   A CE  1 
ATOM   671  N N   A VAL   A 1 109 ? 36.09444 32.37800 -1.19533  0.457 27.72452 ? 89  VAL   A N   1 
ATOM   672  N N   B VAL   A 1 109 ? 36.03335 32.34686 -1.17106  0.543 27.52304 ? 89  VAL   A N   1 
ATOM   673  C CA  A VAL   A 1 109 ? 37.06239 32.39886 -0.11190  0.457 27.82182 ? 89  VAL   A CA  1 
ATOM   674  C CA  B VAL   A 1 109 ? 36.96722 32.64160 -0.08821  0.543 28.04512 ? 89  VAL   A CA  1 
ATOM   675  C C   A VAL   A 1 109 ? 36.29750 32.25722 1.19087   0.457 25.49564 ? 89  VAL   A C   1 
ATOM   676  C C   B VAL   A 1 109 ? 36.25580 32.26964 1.21029   0.543 25.58806 ? 89  VAL   A C   1 
ATOM   677  O O   A VAL   A 1 109 ? 35.11104 32.57635 1.28677   0.457 24.75224 ? 89  VAL   A O   1 
ATOM   678  O O   B VAL   A 1 109 ? 35.03930 32.45725 1.32231   0.543 24.70498 ? 89  VAL   A O   1 
ATOM   679  C CB  A VAL   A 1 109 ? 38.00735 33.62352 -0.08536  0.457 29.09589 ? 89  VAL   A CB  1 
ATOM   680  C CB  B VAL   A 1 109 ? 37.30750 34.15350 -0.07708  0.543 30.11841 ? 89  VAL   A CB  1 
ATOM   681  C CG1 A VAL   A 1 109 ? 38.88926 33.65588 -1.33193  0.457 30.07664 ? 89  VAL   A CG1 1 
ATOM   682  C CG1 B VAL   A 1 109 ? 38.12867 34.53403 1.15066   0.543 29.07771 ? 89  VAL   A CG1 1 
ATOM   683  C CG2 A VAL   A 1 109 ? 37.21791 34.90576 0.06754   0.457 28.47567 ? 89  VAL   A CG2 1 
ATOM   684  C CG2 B VAL   A 1 109 ? 38.01991 34.57245 -1.35930  0.543 30.22490 ? 89  VAL   A CG2 1 
ATOM   685  N N   . VAL   A 1 110 ? 36.99293 31.73909 2.18904   1.000 24.51692 ? 90  VAL   A N   1 
ATOM   686  C CA  . VAL   A 1 110 ? 36.42231 31.51929 3.51292   1.000 24.72487 ? 90  VAL   A CA  1 
ATOM   687  C C   . VAL   A 1 110 ? 37.54789 31.62332 4.53110   1.000 24.88143 ? 90  VAL   A C   1 
ATOM   688  O O   . VAL   A 1 110 ? 38.64813 31.10914 4.31051   1.000 24.93577 ? 90  VAL   A O   1 
ATOM   689  C CB  . VAL   A 1 110 ? 35.63941 30.18369 3.59034   1.000 23.05109 ? 90  VAL   A CB  1 
ATOM   690  C CG1 . VAL   A 1 110 ? 36.58299 28.97476 3.55164   1.000 23.04052 ? 90  VAL   A CG1 1 
ATOM   691  C CG2 . VAL   A 1 110 ? 34.74271 30.14968 4.82756   1.000 22.95016 ? 90  VAL   A CG2 1 
ATOM   692  N N   . SER   A 1 111 ? 37.28109 32.32638 5.63501   1.000 25.05887 ? 91  SER   A N   1 
ATOM   693  C CA  . SER   A 1 111 ? 38.32848 32.55453 6.62532   1.000 26.73294 ? 91  SER   A CA  1 
ATOM   694  C C   . SER   A 1 111 ? 38.82162 31.23606 7.19834   1.000 25.95237 ? 91  SER   A C   1 
ATOM   695  O O   . SER   A 1 111 ? 40.02158 31.05660 7.43742   1.000 26.89584 ? 91  SER   A O   1 
ATOM   696  C CB  . SER   A 1 111 ? 37.80741 33.46119 7.73772   1.000 27.38672 ? 91  SER   A CB  1 
ATOM   697  O OG  . SER   A 1 111 ? 36.68609 32.88765 8.38322   1.000 28.96656 ? 91  SER   A OG  1 
ATOM   698  N N   . ASP   A 1 112 ? 37.90373 30.30045 7.41510   1.000 25.12520 ? 92  ASP   A N   1 
ATOM   699  C CA  . ASP   A 1 112 ? 38.22901 28.95729 7.85990   1.000 24.24583 ? 92  ASP   A CA  1 
ATOM   700  C C   . ASP   A 1 112 ? 37.05973 28.06910 7.47700   1.000 22.18070 ? 92  ASP   A C   1 
ATOM   701  O O   . ASP   A 1 112 ? 35.90498 28.49855 7.54802   1.000 22.44759 ? 92  ASP   A O   1 
ATOM   702  C CB  . ASP   A 1 112 ? 38.43969 28.90638 9.37804   1.000 24.87954 ? 92  ASP   A CB  1 
ATOM   703  C CG  . ASP   A 1 112 ? 38.81819 27.51610 9.86088   1.000 28.10246 ? 92  ASP   A CG  1 
ATOM   704  O OD1 . ASP   A 1 112 ? 40.02017 27.17850 9.81787   1.000 30.45139 ? 92  ASP   A OD1 1 
ATOM   705  O OD2 . ASP   A 1 112 ? 37.91680 26.75098 10.26432  1.000 29.01537 ? 92  ASP   A OD2 1 
ATOM   706  N N   . PHE   A 1 113 ? 37.36192 26.82893 7.08532   1.000 20.59404 ? 93  PHE   A N   1 
ATOM   707  C CA  . PHE   A 1 113 ? 36.31145 25.92832 6.62461   1.000 20.41062 ? 93  PHE   A CA  1 
ATOM   708  C C   . PHE   A 1 113 ? 35.18368 25.77577 7.64180   1.000 21.30393 ? 93  PHE   A C   1 
ATOM   709  O O   . PHE   A 1 113 ? 34.02640 25.57019 7.24959   1.000 22.12173 ? 93  PHE   A O   1 
ATOM   710  C CB  . PHE   A 1 113 ? 36.89894 24.56858 6.25739   1.000 21.31342 ? 93  PHE   A CB  1 
ATOM   711  C CG  . PHE   A 1 113 ? 35.98696 23.73867 5.40867   1.000 21.35844 ? 93  PHE   A CG  1 
ATOM   712  C CD1 . PHE   A 1 113 ? 35.93255 23.93462 4.03223   1.000 20.06291 ? 93  PHE   A CD1 1 
ATOM   713  C CD2 . PHE   A 1 113 ? 35.16832 22.77451 5.98376   1.000 20.32193 ? 93  PHE   A CD2 1 
ATOM   714  C CE1 . PHE   A 1 113 ? 35.08322 23.19304 3.23999   1.000 19.26073 ? 93  PHE   A CE1 1 
ATOM   715  C CE2 . PHE   A 1 113 ? 34.31320 22.01419 5.19169   1.000 19.34656 ? 93  PHE   A CE2 1 
ATOM   716  C CZ  . PHE   A 1 113 ? 34.27551 22.21910 3.81425   1.000 20.16052 ? 93  PHE   A CZ  1 
ATOM   717  N N   . HIS   A 1 114 ? 35.48654 25.89195 8.94227   1.000 23.39291 ? 94  HIS   A N   1 
ATOM   718  C CA  . HIS   A 1 114 ? 34.45111 25.70745 9.95338   1.000 25.68463 ? 94  HIS   A CA  1 
ATOM   719  C C   . HIS   A 1 114 ? 33.33448 26.73745 9.85873   1.000 22.96065 ? 94  HIS   A C   1 
ATOM   720  O O   . HIS   A 1 114 ? 32.24453 26.48800 10.38596  1.000 23.89911 ? 94  HIS   A O   1 
ATOM   721  C CB  . HIS   A 1 114 ? 35.01772 25.72099 11.37172  1.000 32.65748 ? 94  HIS   A CB  1 
ATOM   722  C CG  . HIS   A 1 114 ? 34.05660 25.18856 12.39068  1.000 40.83177 ? 94  HIS   A CG  1 
ATOM   723  N ND1 . HIS   A 1 114 ? 33.70635 23.85544 12.45388  1.000 44.73554 ? 94  HIS   A ND1 1 
ATOM   724  C CD2 . HIS   A 1 114 ? 33.33658 25.81290 13.35412  1.000 44.41233 ? 94  HIS   A CD2 1 
ATOM   725  C CE1 . HIS   A 1 114 ? 32.83203 23.67819 13.42971  1.000 46.41335 ? 94  HIS   A CE1 1 
ATOM   726  N NE2 . HIS   A 1 114 ? 32.58749 24.85076 13.98851  1.000 46.00534 ? 94  HIS   A NE2 1 
ATOM   727  N N   . VAL   A 1 115 ? 33.58453 27.89418 9.23262   1.000 21.58226 ? 95  VAL   A N   1 
ATOM   728  C CA  . VAL   A 1 115 ? 32.50985 28.85770 8.98249   1.000 19.15480 ? 95  VAL   A CA  1 
ATOM   729  C C   . VAL   A 1 115 ? 31.31636 28.17461 8.32835   1.000 19.46985 ? 95  VAL   A C   1 
ATOM   730  O O   . VAL   A 1 115 ? 30.15721 28.39313 8.71562   1.000 18.85304 ? 95  VAL   A O   1 
ATOM   731  C CB  . VAL   A 1 115 ? 33.03540 30.02613 8.12281   1.000 21.81071 ? 95  VAL   A CB  1 
ATOM   732  C CG1 . VAL   A 1 115 ? 31.87561 30.83664 7.53159   1.000 22.67577 ? 95  VAL   A CG1 1 
ATOM   733  C CG2 . VAL   A 1 115 ? 33.93390 30.91655 8.95419   1.000 22.90182 ? 95  VAL   A CG2 1 
ATOM   734  N N   . PHE   A 1 116 ? 31.58346 27.32667 7.33020   1.000 18.64777 ? 96  PHE   A N   1 
ATOM   735  C CA  . PHE   A 1 116 ? 30.49616 26.66692 6.62139   1.000 18.42607 ? 96  PHE   A CA  1 
ATOM   736  C C   . PHE   A 1 116 ? 29.68362 25.79547 7.56919   1.000 19.60424 ? 96  PHE   A C   1 
ATOM   737  O O   . PHE   A 1 116 ? 28.44887 25.76384 7.49784   1.000 20.21831 ? 96  PHE   A O   1 
ATOM   738  C CB  . PHE   A 1 116 ? 31.06148 25.78902 5.50378   1.000 18.21863 ? 96  PHE   A CB  1 
ATOM   739  C CG  . PHE   A 1 116 ? 31.74932 26.53604 4.38383   1.000 18.44161 ? 96  PHE   A CG  1 
ATOM   740  C CD1 . PHE   A 1 116 ? 31.24690 27.73012 3.88593   1.000 19.70038 ? 96  PHE   A CD1 1 
ATOM   741  C CD2 . PHE   A 1 116 ? 32.88331 25.99583 3.78897   1.000 18.16627 ? 96  PHE   A CD2 1 
ATOM   742  C CE1 . PHE   A 1 116 ? 31.87680 28.38402 2.83127   1.000 18.81351 ? 96  PHE   A CE1 1 
ATOM   743  C CE2 . PHE   A 1 116 ? 33.52230 26.63452 2.72191   1.000 19.28103 ? 96  PHE   A CE2 1 
ATOM   744  C CZ  . PHE   A 1 116 ? 33.01999 27.83518 2.24978   1.000 19.37731 ? 96  PHE   A CZ  1 
ATOM   745  N N   . VAL   A 1 117 ? 30.36897 25.05641 8.44389   1.000 19.67879 ? 97  VAL   A N   1 
ATOM   746  C CA  . VAL   A 1 117 ? 29.69620 24.15305 9.37348   1.000 20.33967 ? 97  VAL   A CA  1 
ATOM   747  C C   . VAL   A 1 117 ? 28.91672 24.94835 10.41001  1.000 20.37094 ? 97  VAL   A C   1 
ATOM   748  O O   . VAL   A 1 117 ? 27.76358 24.63414 10.73013  1.000 20.97111 ? 97  VAL   A O   1 
ATOM   749  C CB  . VAL   A 1 117 ? 30.73453 23.23057 10.03463  1.000 20.70056 ? 97  VAL   A CB  1 
ATOM   750  C CG1 . VAL   A 1 117 ? 30.07607 22.34575 11.10348  1.000 22.08330 ? 97  VAL   A CG1 1 
ATOM   751  C CG2 . VAL   A 1 117 ? 31.47044 22.39447 8.96025   1.000 21.29459 ? 97  VAL   A CG2 1 
ATOM   752  N N   . ARG   A 1 118 ? 29.54929 25.97902 10.96680  1.000 19.19287 ? 98  ARG   A N   1 
ATOM   753  C CA  . ARG   A 1 118 ? 28.86823 26.85580 11.91417  1.000 19.86500 ? 98  ARG   A CA  1 
ATOM   754  C C   . ARG   A 1 118 ? 27.57064 27.39748 11.32813  1.000 20.61912 ? 98  ARG   A C   1 
ATOM   755  O O   . ARG   A 1 118 ? 26.52783 27.41095 12.00165  1.000 20.40806 ? 98  ARG   A O   1 
ATOM   756  C CB  . ARG   A 1 118 ? 29.79883 28.00811 12.27621  1.000 20.86988 ? 98  ARG   A CB  1 
ATOM   757  C CG  . ARG   A 1 118 ? 29.20958 29.02081 13.22752  1.000 22.72876 ? 98  ARG   A CG  1 
ATOM   758  C CD  . ARG   A 1 118 ? 30.01497 30.30115 13.13041  1.000 23.75512 ? 98  ARG   A CD  1 
ATOM   759  N NE  . ARG   A 1 118 ? 29.80559 30.97123 11.85195  1.000 23.29278 ? 98  ARG   A NE  1 
ATOM   760  C CZ  . ARG   A 1 118 ? 30.52408 31.99920 11.42149  1.000 22.36565 ? 98  ARG   A CZ  1 
ATOM   761  N NH1 . ARG   A 1 118 ? 31.55476 32.46031 12.11507  1.000 23.43760 ? 98  ARG   A NH1 1 
ATOM   762  N NH2 . ARG   A 1 118 ? 30.20061 32.57943 10.26872  1.000 22.12141 ? 98  ARG   A NH2 1 
ATOM   763  N N   . ASP   A 1 119 ? 27.61550 27.84166 10.06836  1.000 19.23597 ? 99  ASP   A N   1 
ATOM   764  C CA  . ASP   A 1 119 ? 26.43919 28.45614 9.45682   1.000 18.48608 ? 99  ASP   A CA  1 
ATOM   765  C C   . ASP   A 1 119 ? 25.34859 27.42285 9.18694   1.000 18.73183 ? 99  ASP   A C   1 
ATOM   766  O O   . ASP   A 1 119 ? 24.16068 27.72339 9.33605   1.000 19.00882 ? 99  ASP   A O   1 
ATOM   767  C CB  . ASP   A 1 119 ? 26.81709 29.21942 8.17970   1.000 19.18150 ? 99  ASP   A CB  1 
ATOM   768  C CG  . ASP   A 1 119 ? 27.64445 30.47708 8.45660   1.000 20.43702 ? 99  ASP   A CG  1 
ATOM   769  O OD1 . ASP   A 1 119 ? 27.84988 30.83112 9.64425   1.000 20.65855 ? 99  ASP   A OD1 1 
ATOM   770  O OD2 . ASP   A 1 119 ? 28.09722 31.11248 7.47428   1.000 20.84716 ? 99  ASP   A OD2 1 
ATOM   771  N N   . VAL   A 1 120 ? 25.72278 26.20231 8.78918   1.000 18.55005 ? 100 VAL   A N   1 
ATOM   772  C CA  . VAL   A 1 120 ? 24.71991 25.14334 8.66110   1.000 18.48384 ? 100 VAL   A CA  1 
ATOM   773  C C   . VAL   A 1 120 ? 24.05095 24.89241 10.00575  1.000 20.34446 ? 100 VAL   A C   1 
ATOM   774  O O   . VAL   A 1 120 ? 22.82402 24.79592 10.09954  1.000 20.22449 ? 100 VAL   A O   1 
ATOM   775  C CB  . VAL   A 1 120 ? 25.33759 23.85424 8.07986   1.000 17.87931 ? 100 VAL   A CB  1 
ATOM   776  C CG1 . VAL   A 1 120 ? 24.34344 22.69609 8.17943   1.000 20.25506 ? 100 VAL   A CG1 1 
ATOM   777  C CG2 . VAL   A 1 120 ? 25.74181 24.07499 6.61678   1.000 18.37209 ? 100 VAL   A CG2 1 
ATOM   778  N N   . LEU   A 1 121 ? 24.85282 24.79611 11.07184  1.000 20.25920 ? 101 LEU   A N   1 
ATOM   779  C CA  . LEU   A 1 121 ? 24.29133 24.53173 12.39142  1.000 19.62715 ? 101 LEU   A CA  1 
ATOM   780  C C   . LEU   A 1 121 ? 23.35469 25.64756 12.83727  1.000 21.09495 ? 101 LEU   A C   1 
ATOM   781  O O   . LEU   A 1 121 ? 22.31553 25.38327 13.45611  1.000 22.77848 ? 101 LEU   A O   1 
ATOM   782  C CB  . LEU   A 1 121 ? 25.40867 24.30922 13.40792  1.000 21.36285 ? 101 LEU   A CB  1 
ATOM   783  C CG  . LEU   A 1 121 ? 26.11251 22.96080 13.24260  1.000 23.07718 ? 101 LEU   A CG  1 
ATOM   784  C CD1 . LEU   A 1 121 ? 27.36599 22.92257 14.09718  1.000 25.72213 ? 101 LEU   A CD1 1 
ATOM   785  C CD2 . LEU   A 1 121 ? 25.17378 21.80003 13.60621  1.000 24.58799 ? 101 LEU   A CD2 1 
ATOM   786  N N   . GLN   A 1 122 ? 23.70208 26.90300 12.53525  1.000 20.33738 ? 102 GLN   A N   1 
ATOM   787  C CA  . GLN   A 1 122 ? 22.80573 27.99783 12.87578  1.000 19.61690 ? 102 GLN   A CA  1 
ATOM   788  C C   . GLN   A 1 122 ? 21.45838 27.82770 12.19214  1.000 19.97697 ? 102 GLN   A C   1 
ATOM   789  O O   . GLN   A 1 122 ? 20.40326 28.01006 12.81288  1.000 21.04029 ? 102 GLN   A O   1 
ATOM   790  C CB  . GLN   A 1 122 ? 23.42493 29.33699 12.47731  1.000 19.12865 ? 102 GLN   A CB  1 
ATOM   791  C CG  . GLN   A 1 122 ? 22.51794 30.53032 12.78215  1.000 19.75757 ? 102 GLN   A CG  1 
ATOM   792  C CD  . GLN   A 1 122 ? 22.97336 31.80973 12.09955  1.000 21.61814 ? 102 GLN   A CD  1 
ATOM   793  O OE1 . GLN   A 1 122 ? 24.06644 31.87001 11.53498  1.000 25.04651 ? 102 GLN   A OE1 1 
ATOM   794  N NE2 . GLN   A 1 122 ? 22.12520 32.83372 12.12665  1.000 22.74108 ? 102 GLN   A NE2 1 
ATOM   795  N N   . HIS   A 1 123 ? 21.47607 27.49345 10.90648  1.000 19.65305 ? 103 HIS   A N   1 
ATOM   796  C CA  . HIS   A 1 123 ? 20.23145 27.37523 10.15790  1.000 19.70250 ? 103 HIS   A CA  1 
ATOM   797  C C   . HIS   A 1 123 ? 19.43323 26.16663 10.62952  1.000 19.79143 ? 103 HIS   A C   1 
ATOM   798  O O   . HIS   A 1 123 ? 18.21523 26.25485 10.82161  1.000 21.79393 ? 103 HIS   A O   1 
ATOM   799  C CB  . HIS   A 1 123 ? 20.55107 27.28592 8.66584   1.000 19.34682 ? 103 HIS   A CB  1 
ATOM   800  C CG  . HIS   A 1 123 ? 19.40728 27.63668 7.76941   1.000 20.39020 ? 103 HIS   A CG  1 
ATOM   801  N ND1 . HIS   A 1 123 ? 19.55209 27.76412 6.40556   1.000 20.91258 ? 103 HIS   A ND1 1 
ATOM   802  C CD2 . HIS   A 1 123 ? 18.10892 27.91021 8.03864   1.000 20.19384 ? 103 HIS   A CD2 1 
ATOM   803  C CE1 . HIS   A 1 123 ? 18.39058 28.09493 5.86868   1.000 22.38339 ? 103 HIS   A CE1 1 
ATOM   804  N NE2 . HIS   A 1 123 ? 17.49826 28.19622 6.83936   1.000 21.25412 ? 103 HIS   A NE2 1 
ATOM   805  N N   . VAL   A 1 124 ? 20.11071 25.03650 10.84698  1.000 20.09464 ? 104 VAL   A N   1 
ATOM   806  C CA  . VAL   A 1 124 ? 19.44007 23.85437 11.38044  1.000 20.49432 ? 104 VAL   A CA  1 
ATOM   807  C C   . VAL   A 1 124 ? 18.81013 24.16225 12.73610  1.000 21.11547 ? 104 VAL   A C   1 
ATOM   808  O O   . VAL   A 1 124 ? 17.65312 23.81276 12.99924  1.000 22.33335 ? 104 VAL   A O   1 
ATOM   809  C CB  . VAL   A 1 124 ? 20.42402 22.67528 11.47435  1.000 21.19154 ? 104 VAL   A CB  1 
ATOM   810  C CG1 . VAL   A 1 124 ? 19.81479 21.54678 12.28385  1.000 24.32167 ? 104 VAL   A CG1 1 
ATOM   811  C CG2 . VAL   A 1 124 ? 20.81173 22.19247 10.08414  1.000 21.69056 ? 104 VAL   A CG2 1 
ATOM   812  N N   . ASP   A 1 125 ? 19.56644 24.80944 13.62491  1.000 20.91214 ? 105 ASP   A N   1 
ATOM   813  C CA  . ASP   A 1 125 ? 19.03467 25.11120 14.95276  1.000 23.17198 ? 105 ASP   A CA  1 
ATOM   814  C C   . ASP   A 1 125 ? 17.82939 26.03621 14.85944  1.000 23.24864 ? 105 ASP   A C   1 
ATOM   815  O O   . ASP   A 1 125 ? 16.85453 25.88091 15.60014  1.000 25.94388 ? 105 ASP   A O   1 
ATOM   816  C CB  . ASP   A 1 125 ? 20.11776 25.74028 15.82869  1.000 24.64327 ? 105 ASP   A CB  1 
ATOM   817  C CG  . ASP   A 1 125 ? 21.19536 24.75008 16.23317  1.000 27.45776 ? 105 ASP   A CG  1 
ATOM   818  O OD1 . ASP   A 1 125 ? 21.00601 23.52878 16.03862  1.000 27.76003 ? 105 ASP   A OD1 1 
ATOM   819  O OD2 . ASP   A 1 125 ? 22.24156 25.19730 16.74854  1.000 28.94986 ? 105 ASP   A OD2 1 
ATOM   820  N N   . SER   A 1 126 ? 17.87609 26.99752 13.94171  1.000 23.96828 ? 106 SER   A N   1 
ATOM   821  C CA  A SER   A 1 126 ? 16.74867 27.90639 13.75960  0.593 24.77991 ? 106 SER   A CA  1 
ATOM   822  C CA  C SER   A 1 126 ? 16.74774 27.90327 13.77001  0.407 25.33072 ? 106 SER   A CA  1 
ATOM   823  C C   . SER   A 1 126 ? 15.51441 27.15766 13.27216  1.000 25.54777 ? 106 SER   A C   1 
ATOM   824  O O   . SER   A 1 126 ? 14.40471 27.38884 13.76415  1.000 27.44409 ? 106 SER   A O   1 
ATOM   825  C CB  A SER   A 1 126 ? 17.12946 29.00397 12.76716  0.593 24.69688 ? 106 SER   A CB  1 
ATOM   826  C CB  C SER   A 1 126 ? 17.13580 29.03007 12.81547  0.407 26.23281 ? 106 SER   A CB  1 
ATOM   827  O OG  A SER   A 1 126 ? 16.09709 29.96850 12.64374  0.593 24.57579 ? 106 SER   A OG  1 
ATOM   828  O OG  C SER   A 1 126 ? 18.25277 29.74762 13.31859  0.407 26.80719 ? 106 SER   A OG  1 
ATOM   829  N N   . MET   A 1 127 ? 15.68943 26.25219 12.30393  1.000 24.96964 ? 107 MET   A N   1 
ATOM   830  C CA  . MET   A 1 127 ? 14.55038 25.49505 11.79027  1.000 25.83184 ? 107 MET   A CA  1 
ATOM   831  C C   . MET   A 1 127 ? 14.02293 24.50108 12.81954  1.000 28.12770 ? 107 MET   A C   1 
ATOM   832  O O   . MET   A 1 127 ? 12.80945 24.27569 12.90460  1.000 29.28399 ? 107 MET   A O   1 
ATOM   833  C CB  . MET   A 1 127 ? 14.92596 24.78349 10.49173  1.000 26.47828 ? 107 MET   A CB  1 
ATOM   834  C CG  . MET   A 1 127 ? 15.03163 25.72781 9.30790   1.000 29.69767 ? 107 MET   A CG  1 
ATOM   835  S SD  . MET   A 1 127 ? 13.43057 26.45221 8.88447   1.000 31.31298 ? 107 MET   A SD  1 
ATOM   836  C CE  . MET   A 1 127 ? 12.65576 25.10672 7.98843   1.000 32.11233 ? 107 MET   A CE  1 
ATOM   837  N N   . GLN   A 1 128 ? 14.91566 23.89459 13.60688  1.000 29.21869 ? 108 GLN   A N   1 
ATOM   838  C CA  . GLN   A 1 128 ? 14.47571 22.96622 14.64527  1.000 31.78320 ? 108 GLN   A CA  1 
ATOM   839  C C   . GLN   A 1 128 ? 13.57689 23.65611 15.66616  1.000 33.15539 ? 108 GLN   A C   1 
ATOM   840  O O   . GLN   A 1 128 ? 12.63984 23.04015 16.18612  1.000 34.73462 ? 108 GLN   A O   1 
ATOM   841  C CB  . GLN   A 1 128 ? 15.69078 22.33916 15.33034  1.000 34.84333 ? 108 GLN   A CB  1 
ATOM   842  C CG  . GLN   A 1 128 ? 15.35673 21.24918 16.33491  1.000 41.70649 ? 108 GLN   A CG  1 
ATOM   843  C CD  . GLN   A 1 128 ? 15.08509 19.90531 15.67341  1.000 46.52972 ? 108 GLN   A CD  1 
ATOM   844  O OE1 . GLN   A 1 128 ? 15.97596 19.06303 15.57185  1.000 46.93869 ? 108 GLN   A OE1 1 
ATOM   845  N NE2 . GLN   A 1 128 ? 13.84870 19.70019 15.22323  1.000 49.41019 ? 108 GLN   A NE2 1 
ATOM   846  N N   . LYS   A 1 129 ? 13.84030 24.93184 15.95696  1.000 35.24479 ? 109 LYS   A N   1 
ATOM   847  C CA  . LYS   A 1 129 ? 12.97025 25.70186 16.84329  1.000 38.62205 ? 109 LYS   A CA  1 
ATOM   848  C C   . LYS   A 1 129 ? 11.58830 25.89140 16.23535  1.000 39.72945 ? 109 LYS   A C   1 
ATOM   849  O O   . LYS   A 1 129 ? 10.57050 25.78852 16.93143  1.000 40.85972 ? 109 LYS   A O   1 
ATOM   850  C CB  . LYS   A 1 129 ? 13.58111 27.07924 17.09163  1.000 39.17808 ? 109 LYS   A CB  1 
ATOM   851  C CG  . LYS   A 1 129 ? 14.80206 27.09968 17.95246  1.000 41.57731 ? 109 LYS   A CG  1 
ATOM   852  C CD  . LYS   A 1 129 ? 14.96221 28.48619 18.54030  1.000 43.73958 ? 109 LYS   A CD  1 
ATOM   853  C CE  . LYS   A 1 129 ? 14.93440 29.56001 17.45509  1.000 44.96926 ? 109 LYS   A CE  1 
ATOM   854  N NZ  . LYS   A 1 129 ? 13.91922 30.60710 17.74074  1.000 45.34177 ? 109 LYS   A NZ  1 
ATOM   855  N N   . ASP   A 1 130 ? 11.53823 26.21989 14.94247  1.000 40.50614 ? 110 ASP   A N   1 
ATOM   856  C CA  . ASP   A 1 130 ? 10.26613 26.48549 14.28264  1.000 42.39660 ? 110 ASP   A CA  1 
ATOM   857  C C   . ASP   A 1 130 ? 9.44852  25.21341 14.10433  1.000 42.27440 ? 110 ASP   A C   1 
ATOM   858  O O   . ASP   A 1 130 ? 8.21461  25.26861 14.08584  1.000 42.74775 ? 110 ASP   A O   1 
ATOM   859  C CB  . ASP   A 1 130 ? 10.50477 27.15610 12.92605  1.000 45.50444 ? 110 ASP   A CB  1 
ATOM   860  C CG  . ASP   A 1 130 ? 11.10288 28.55069 13.04996  1.000 49.75754 ? 110 ASP   A CG  1 
ATOM   861  O OD1 . ASP   A 1 130 ? 11.33297 29.01222 14.18907  1.000 50.83160 ? 110 ASP   A OD1 1 
ATOM   862  O OD2 . ASP   A 1 130 ? 11.34206 29.19033 12.00158  1.000 52.14857 ? 110 ASP   A OD2 1 
ATOM   863  N N   . TYR   A 1 131 ? 10.10662 24.06425 13.97854  1.000 41.54200 ? 111 TYR   A N   1 
ATOM   864  C CA  . TYR   A 1 131 ? 9.43410  22.78710 13.73818  1.000 42.20943 ? 111 TYR   A CA  1 
ATOM   865  C C   . TYR   A 1 131 ? 9.93109  21.77024 14.75611  1.000 42.10034 ? 111 TYR   A C   1 
ATOM   866  O O   . TYR   A 1 131 ? 10.60636 20.79541 14.40655  1.000 42.25976 ? 111 TYR   A O   1 
ATOM   867  C CB  . TYR   A 1 131 ? 9.66609  22.32058 12.29957  1.000 41.96979 ? 111 TYR   A CB  1 
ATOM   868  C CG  . TYR   A 1 131 ? 9.21123  23.33706 11.27402  1.000 43.46835 ? 111 TYR   A CG  1 
ATOM   869  C CD1 . TYR   A 1 131 ? 10.06805 24.33569 10.82880  1.000 44.10228 ? 111 TYR   A CD1 1 
ATOM   870  C CD2 . TYR   A 1 131 ? 7.91649  23.31238 10.76601  1.000 45.10920 ? 111 TYR   A CD2 1 
ATOM   871  C CE1 . TYR   A 1 131 ? 9.65356  25.27660 9.89788   1.000 45.77749 ? 111 TYR   A CE1 1 
ATOM   872  C CE2 . TYR   A 1 131 ? 7.49206  24.25083 9.83309   1.000 45.86223 ? 111 TYR   A CE2 1 
ATOM   873  C CZ  . TYR   A 1 131 ? 8.36425  25.23196 9.40639   1.000 46.72413 ? 111 TYR   A CZ  1 
ATOM   874  O OH  . TYR   A 1 131 ? 7.95082  26.16833 8.48090   1.000 47.75972 ? 111 TYR   A OH  1 
ATOM   875  N N   . PRO   A 1 132 ? 9.61292  21.96944 16.03334  1.000 43.83031 ? 112 PRO   A N   1 
ATOM   876  C CA  . PRO   A 1 132 ? 10.14817 21.08522 17.07115  1.000 44.49441 ? 112 PRO   A CA  1 
ATOM   877  C C   . PRO   A 1 132 ? 9.58162  19.68172 16.94994  1.000 44.49743 ? 112 PRO   A C   1 
ATOM   878  O O   . PRO   A 1 132 ? 8.49080  19.45606 16.41936  1.000 45.75254 ? 112 PRO   A O   1 
ATOM   879  C CB  . PRO   A 1 132 ? 9.68563  21.74413 18.37299  1.000 45.15865 ? 112 PRO   A CB  1 
ATOM   880  C CG  . PRO   A 1 132 ? 8.45759  22.49848 17.98865  1.000 45.44733 ? 112 PRO   A CG  1 
ATOM   881  C CD  . PRO   A 1 132 ? 8.70331  22.98729 16.59048  1.000 45.01710 ? 112 PRO   A CD  1 
ATOM   882  N N   . GLY   A 1 133 ? 10.35527 18.72616 17.46085  1.000 43.49317 ? 113 GLY   A N   1 
ATOM   883  C CA  . GLY   A 1 133 ? 9.98046  17.33202 17.42672  1.000 42.47655 ? 113 GLY   A CA  1 
ATOM   884  C C   . GLY   A 1 133 ? 10.31406 16.60353 16.14330  1.000 42.21276 ? 113 GLY   A C   1 
ATOM   885  O O   . GLY   A 1 133 ? 10.37872 15.36935 16.15207  1.000 43.60732 ? 113 GLY   A O   1 
ATOM   886  N N   . LEU   A 1 134 ? 10.54198 17.32523 15.03331  1.000 39.23754 ? 114 LEU   A N   1 
ATOM   887  C CA  . LEU   A 1 134 ? 10.78701 16.66220 13.75733  1.000 37.36607 ? 114 LEU   A CA  1 
ATOM   888  C C   . LEU   A 1 134 ? 12.23322 16.17834 13.66865  1.000 35.49776 ? 114 LEU   A C   1 
ATOM   889  O O   . LEU   A 1 134 ? 13.15575 16.89453 14.07124  1.000 37.57028 ? 114 LEU   A O   1 
ATOM   890  C CB  . LEU   A 1 134 ? 10.52313 17.61801 12.59685  1.000 38.13632 ? 114 LEU   A CB  1 
ATOM   891  C CG  . LEU   A 1 134 ? 9.07785  18.03475 12.33516  1.000 39.54323 ? 114 LEU   A CG  1 
ATOM   892  C CD1 . LEU   A 1 134 ? 8.97962  18.80293 11.01728  1.000 38.58937 ? 114 LEU   A CD1 1 
ATOM   893  C CD2 . LEU   A 1 134 ? 8.16207  16.81986 12.33564  1.000 40.13997 ? 114 LEU   A CD2 1 
ATOM   894  N N   . PRO   A 1 135 ? 12.45738 14.98308 13.12963  1.000 32.75203 ? 115 PRO   A N   1 
ATOM   895  C CA  . PRO   A 1 135 ? 13.82953 14.55551 12.84576  1.000 30.95348 ? 115 PRO   A CA  1 
ATOM   896  C C   . PRO   A 1 135 ? 14.42561 15.40089 11.73530  1.000 28.66376 ? 115 PRO   A C   1 
ATOM   897  O O   . PRO   A 1 135 ? 13.71719 15.93623 10.87846  1.000 28.48856 ? 115 PRO   A O   1 
ATOM   898  C CB  . PRO   A 1 135 ? 13.66921 13.09575 12.40506  1.000 33.00690 ? 115 PRO   A CB  1 
ATOM   899  C CG  . PRO   A 1 135 ? 12.25618 12.98293 11.94028  1.000 34.95820 ? 115 PRO   A CG  1 
ATOM   900  C CD  . PRO   A 1 135 ? 11.45930 13.96404 12.75648  1.000 33.20950 ? 115 PRO   A CD  1 
ATOM   901  N N   . VAL   A 1 136 ? 15.74865 15.52125 11.75861  1.000 25.13974 ? 116 VAL   A N   1 
ATOM   902  C CA  A VAL   A 1 136 ? 16.46963 16.35923 10.81223  0.235 23.95305 ? 116 VAL   A CA  1 
ATOM   903  C CA  B VAL   A 1 136 ? 16.49075 16.36867 10.83246  0.765 23.11421 ? 116 VAL   A CA  1 
ATOM   904  C C   . VAL   A 1 136 ? 17.50831 15.51296 10.09250  1.000 22.90819 ? 116 VAL   A C   1 
ATOM   905  O O   . VAL   A 1 136 ? 18.29756 14.80149 10.72597  1.000 24.12122 ? 116 VAL   A O   1 
ATOM   906  C CB  A VAL   A 1 136 ? 17.09347 17.60178 11.47843  0.235 24.90172 ? 116 VAL   A CB  1 
ATOM   907  C CB  B VAL   A 1 136 ? 17.20592 17.50544 11.58257  0.765 25.12199 ? 116 VAL   A CB  1 
ATOM   908  C CG1 A VAL   A 1 136 ? 17.96190 17.21337 12.66340  0.235 24.91611 ? 116 VAL   A CG1 1 
ATOM   909  C CG1 B VAL   A 1 136 ? 17.92921 18.40803 10.59962  0.765 27.04755 ? 116 VAL   A CG1 1 
ATOM   910  C CG2 A VAL   A 1 136 ? 17.88851 18.40527 10.45966  0.235 25.73205 ? 116 VAL   A CG2 1 
ATOM   911  C CG2 B VAL   A 1 136 ? 16.21362 18.27354 12.44815  0.765 25.65301 ? 116 VAL   A CG2 1 
ATOM   912  N N   . PHE   A 1 137 ? 17.49251 15.58874 8.76851   1.000 21.27239 ? 117 PHE   A N   1 
ATOM   913  C CA  . PHE   A 1 137 ? 18.44388 14.92268 7.89677   1.000 21.15991 ? 117 PHE   A CA  1 
ATOM   914  C C   . PHE   A 1 137 ? 19.35273 15.96422 7.26353   1.000 19.35524 ? 117 PHE   A C   1 
ATOM   915  O O   . PHE   A 1 137 ? 19.02549 17.15214 7.19164   1.000 20.27328 ? 117 PHE   A O   1 
ATOM   916  C CB  . PHE   A 1 137 ? 17.72600 14.16281 6.77372   1.000 20.62874 ? 117 PHE   A CB  1 
ATOM   917  C CG  . PHE   A 1 137 ? 16.94297 12.98450 7.24593   1.000 22.30271 ? 117 PHE   A CG  1 
ATOM   918  C CD1 . PHE   A 1 137 ? 15.67700 13.14021 7.77962   1.000 24.24754 ? 117 PHE   A CD1 1 
ATOM   919  C CD2 . PHE   A 1 137 ? 17.47056 11.70612 7.12915   1.000 23.37899 ? 117 PHE   A CD2 1 
ATOM   920  C CE1 . PHE   A 1 137 ? 14.95350 12.03917 8.21869   1.000 25.33839 ? 117 PHE   A CE1 1 
ATOM   921  C CE2 . PHE   A 1 137 ? 16.75300 10.59201 7.56549   1.000 23.73238 ? 117 PHE   A CE2 1 
ATOM   922  C CZ  . PHE   A 1 137 ? 15.49403 10.75764 8.10446   1.000 26.02781 ? 117 PHE   A CZ  1 
ATOM   923  N N   . LEU   A 1 138 ? 20.50914 15.50392 6.80012   1.000 19.45156 ? 118 LEU   A N   1 
ATOM   924  C CA  . LEU   A 1 138 ? 21.43158 16.31167 6.01903   1.000 19.52585 ? 118 LEU   A CA  1 
ATOM   925  C C   . LEU   A 1 138 ? 21.63416 15.65287 4.66691   1.000 18.36241 ? 118 LEU   A C   1 
ATOM   926  O O   . LEU   A 1 138 ? 21.65160 14.42561 4.56577   1.000 19.66640 ? 118 LEU   A O   1 
ATOM   927  C CB  . LEU   A 1 138 ? 22.78978 16.41288 6.71956   1.000 19.19609 ? 118 LEU   A CB  1 
ATOM   928  C CG  . LEU   A 1 138 ? 22.79696 17.07202 8.10111   1.000 19.42613 ? 118 LEU   A CG  1 
ATOM   929  C CD1 . LEU   A 1 138 ? 24.13484 16.81100 8.78176   1.000 20.87842 ? 118 LEU   A CD1 1 
ATOM   930  C CD2 . LEU   A 1 138 ? 22.50075 18.58245 8.01073   1.000 23.49475 ? 118 LEU   A CD2 1 
ATOM   931  N N   . LEU   A 1 139 ? 21.76965 16.45977 3.62219   1.000 18.39770 ? 119 LEU   A N   1 
ATOM   932  C CA  . LEU   A 1 139 ? 22.15457 15.95603 2.31132   1.000 18.22807 ? 119 LEU   A CA  1 
ATOM   933  C C   . LEU   A 1 139 ? 23.22921 16.88260 1.77529   1.000 17.45627 ? 119 LEU   A C   1 
ATOM   934  O O   . LEU   A 1 139 ? 23.04625 18.10056 1.78212   1.000 18.99230 ? 119 LEU   A O   1 
ATOM   935  C CB  . LEU   A 1 139 ? 20.95105 15.91115 1.36253   1.000 19.25253 ? 119 LEU   A CB  1 
ATOM   936  C CG  . LEU   A 1 139 ? 21.17572 15.35017 -0.05296  1.000 19.87840 ? 119 LEU   A CG  1 
ATOM   937  C CD1 . LEU   A 1 139 ? 19.91260 14.69276 -0.56201  1.000 22.21352 ? 119 LEU   A CD1 1 
ATOM   938  C CD2 . LEU   A 1 139 ? 21.65262 16.42398 -1.04914  1.000 19.60025 ? 119 LEU   A CD2 1 
ATOM   939  N N   . GLY   A 1 140 ? 24.33625 16.32683 1.31767   1.000 15.71063 ? 120 GLY   A N   1 
ATOM   940  C CA  . GLY   A 1 140 ? 25.44641 17.14752 0.85977   1.000 15.83592 ? 120 GLY   A CA  1 
ATOM   941  C C   . GLY   A 1 140 ? 26.16049 16.48975 -0.29841  1.000 15.84292 ? 120 GLY   A C   1 
ATOM   942  O O   . GLY   A 1 140 ? 26.27305 15.25813 -0.36039  1.000 17.81051 ? 120 GLY   A O   1 
ATOM   943  N N   . HIS   A 1 141 ? 26.62632 17.31063 -1.23720  1.000 15.71503 ? 121 HIS   A N   1 
ATOM   944  C CA  . HIS   A 1 141 ? 27.40825 16.84832 -2.37551  1.000 16.01569 ? 121 HIS   A CA  1 
ATOM   945  C C   . HIS   A 1 141 ? 28.78580 17.48893 -2.30978  1.000 16.81456 ? 121 HIS   A C   1 
ATOM   946  O O   . HIS   A 1 141 ? 28.90207 18.69867 -2.07815  1.000 17.01137 ? 121 HIS   A O   1 
ATOM   947  C CB  . HIS   A 1 141 ? 26.70746 17.19926 -3.70501  1.000 16.30049 ? 121 HIS   A CB  1 
ATOM   948  C CG  . HIS   A 1 141 ? 27.59253 17.15249 -4.91702  1.000 16.62364 ? 121 HIS   A CG  1 
ATOM   949  N ND1 . HIS   A 1 141 ? 28.24449 16.01036 -5.33823  1.000 15.90089 ? 121 HIS   A ND1 1 
ATOM   950  C CD2 . HIS   A 1 141 ? 27.90677 18.11639 -5.81758  1.000 17.62546 ? 121 HIS   A CD2 1 
ATOM   951  C CE1 . HIS   A 1 141 ? 28.92606 16.27711 -6.44218  1.000 16.36956 ? 121 HIS   A CE1 1 
ATOM   952  N NE2 . HIS   A 1 141 ? 28.74005 17.55169 -6.75160  1.000 16.82272 ? 121 HIS   A NE2 1 
ATOM   953  N N   . SER   A 1 142 ? 29.82650 16.67109 -2.47588  1.000 16.85163 ? 122 SER   A N   1 
ATOM   954  C CA  . SER   A 1 142 ? 31.19401 17.14899 -2.70075  1.000 16.58985 ? 122 SER   A CA  1 
ATOM   955  C C   . SER   A 1 142 ? 31.64563 17.97676 -1.50296  1.000 15.87314 ? 122 SER   A C   1 
ATOM   956  O O   . SER   A 1 142 ? 31.61390 17.46189 -0.36969  1.000 16.92919 ? 122 SER   A O   1 
ATOM   957  C CB  . SER   A 1 142 ? 31.25011 17.82749 -4.07084  1.000 16.90810 ? 122 SER   A CB  1 
ATOM   958  O OG  . SER   A 1 142 ? 32.59578 18.01013 -4.46475  1.000 17.59058 ? 122 SER   A OG  1 
ATOM   959  N N   . MET   A 1 143 ? 32.07237 19.23135 -1.67938  1.000 15.66769 ? 123 MET   A N   1 
ATOM   960  C CA  . MET   A 1 143 ? 32.41585 20.04528 -0.51416  1.000 16.93385 ? 123 MET   A CA  1 
ATOM   961  C C   . MET   A 1 143 ? 31.25042 20.10475 0.46926   1.000 17.27344 ? 123 MET   A C   1 
ATOM   962  O O   . MET   A 1 143 ? 31.45134 20.12324 1.69299   1.000 17.15473 ? 123 MET   A O   1 
ATOM   963  C CB  . MET   A 1 143 ? 32.78975 21.46598 -0.94362  1.000 18.26382 ? 123 MET   A CB  1 
ATOM   964  C CG  . MET   A 1 143 ? 33.25424 22.34705 0.21948   1.000 19.04079 ? 123 MET   A CG  1 
ATOM   965  S SD  . MET   A 1 143 ? 33.48477 24.08159 -0.26716  1.000 19.76922 ? 123 MET   A SD  1 
ATOM   966  C CE  . MET   A 1 143 ? 31.79682 24.63407 -0.20508  1.000 19.13529 ? 123 MET   A CE  1 
ATOM   967  N N   . GLY   A 1 144 ? 30.02257 20.16790 -0.05439  1.000 16.42384 ? 124 GLY   A N   1 
ATOM   968  C CA  . GLY   A 1 144 ? 28.85284 20.17912 0.80643   1.000 16.87395 ? 124 GLY   A CA  1 
ATOM   969  C C   . GLY   A 1 144 ? 28.67319 18.89231 1.58407   1.000 17.22118 ? 124 GLY   A C   1 
ATOM   970  O O   . GLY   A 1 144 ? 28.06276 18.89535 2.65616   1.000 17.62457 ? 124 GLY   A O   1 
ATOM   971  N N   . GLY   A 1 145 ? 29.19453 17.78184 1.05697   1.000 17.27804 ? 125 GLY   A N   1 
ATOM   972  C CA  . GLY   A 1 145 ? 29.17292 16.53128 1.80577   1.000 17.73793 ? 125 GLY   A CA  1 
ATOM   973  C C   . GLY   A 1 145 ? 30.18957 16.51441 2.93019   1.000 17.12161 ? 125 GLY   A C   1 
ATOM   974  O O   . GLY   A 1 145 ? 29.92998 15.96835 4.00538   1.000 18.33870 ? 125 GLY   A O   1 
ATOM   975  N N   . ALA   A 1 146 ? 31.36099 17.11702 2.70525   1.000 17.02638 ? 126 ALA   A N   1 
ATOM   976  C CA  . ALA   A 1 146 ? 32.29880 17.29715 3.81156   1.000 17.30671 ? 126 ALA   A CA  1 
ATOM   977  C C   . ALA   A 1 146 ? 31.69258 18.17608 4.89812   1.000 17.70102 ? 126 ALA   A C   1 
ATOM   978  O O   . ALA   A 1 146 ? 31.81703 17.87867 6.09255   1.000 19.01481 ? 126 ALA   A O   1 
ATOM   979  C CB  . ALA   A 1 146 ? 33.61659 17.88020 3.31134   1.000 17.96804 ? 126 ALA   A CB  1 
ATOM   980  N N   . ILE   A 1 147 ? 31.02256 19.25987 4.49982   1.000 16.99260 ? 127 ILE   A N   1 
ATOM   981  C CA  . ILE   A 1 147 ? 30.31122 20.09728 5.46155   1.000 16.27800 ? 127 ILE   A CA  1 
ATOM   982  C C   . ILE   A 1 147 ? 29.28693 19.27871 6.24041   1.000 18.13784 ? 127 ILE   A C   1 
ATOM   983  O O   . ILE   A 1 147 ? 29.18699 19.39364 7.46787   1.000 18.98680 ? 127 ILE   A O   1 
ATOM   984  C CB  . ILE   A 1 147 ? 29.67490 21.30079 4.74245   1.000 16.16890 ? 127 ILE   A CB  1 
ATOM   985  C CG1 . ILE   A 1 147 ? 30.77060 22.21630 4.19156   1.000 16.35656 ? 127 ILE   A CG1 1 
ATOM   986  C CG2 . ILE   A 1 147 ? 28.75486 22.07857 5.69609   1.000 19.15999 ? 127 ILE   A CG2 1 
ATOM   987  C CD1 . ILE   A 1 147 ? 30.26551 23.23945 3.16624   1.000 16.85949 ? 127 ILE   A CD1 1 
ATOM   988  N N   . ALA   A 1 148 ? 28.52479 18.42288 5.54772   1.000 17.33151 ? 128 ALA   A N   1 
ATOM   989  C CA  . ALA   A 1 148 ? 27.52292 17.60399 6.23403   1.000 18.40788 ? 128 ALA   A CA  1 
ATOM   990  C C   . ALA   A 1 148 ? 28.17068 16.63592 7.22206   1.000 18.04658 ? 128 ALA   A C   1 
ATOM   991  O O   . ALA   A 1 148 ? 27.68821 16.47529 8.34867   1.000 19.31311 ? 128 ALA   A O   1 
ATOM   992  C CB  . ALA   A 1 148 ? 26.66247 16.84671 5.21941   1.000 17.66877 ? 128 ALA   A CB  1 
ATOM   993  N N   . ILE   A 1 149 ? 29.24656 15.95839 6.81205   1.000 18.48383 ? 129 ILE   A N   1 
ATOM   994  C CA  . ILE   A 1 149 ? 29.95598 15.06901 7.73384   1.000 19.07934 ? 129 ILE   A CA  1 
ATOM   995  C C   . ILE   A 1 149 ? 30.38315 15.82364 8.98825   1.000 19.53262 ? 129 ILE   A C   1 
ATOM   996  O O   . ILE   A 1 149 ? 30.18175 15.35877 10.11927  1.000 20.47121 ? 129 ILE   A O   1 
ATOM   997  C CB  . ILE   A 1 149 ? 31.17098 14.42855 7.04154   1.000 17.97690 ? 129 ILE   A CB  1 
ATOM   998  C CG1 . ILE   A 1 149 ? 30.72022 13.42898 5.96270   1.000 18.30308 ? 129 ILE   A CG1 1 
ATOM   999  C CG2 . ILE   A 1 149 ? 32.10314 13.77657 8.09838   1.000 20.30068 ? 129 ILE   A CG2 1 
ATOM   1000 C CD1 . ILE   A 1 149 ? 31.81425 13.06401 4.98169   1.000 19.33014 ? 129 ILE   A CD1 1 
ATOM   1001 N N   . LEU   A 1 150 ? 31.00496 16.99185 8.80568   1.000 19.93158 ? 130 LEU   A N   1 
ATOM   1002 C CA  . LEU   A 1 150 ? 31.49987 17.73748 9.95597   1.000 20.79759 ? 130 LEU   A CA  1 
ATOM   1003 C C   . LEU   A 1 150 ? 30.35541 18.26995 10.80678  1.000 21.55430 ? 130 LEU   A C   1 
ATOM   1004 O O   . LEU   A 1 150 ? 30.48821 18.35656 12.03177  1.000 23.17895 ? 130 LEU   A O   1 
ATOM   1005 C CB  . LEU   A 1 150 ? 32.41725 18.86867 9.49321   1.000 21.74388 ? 130 LEU   A CB  1 
ATOM   1006 C CG  . LEU   A 1 150 ? 33.68791 18.38884 8.78838   1.000 22.11594 ? 130 LEU   A CG  1 
ATOM   1007 C CD1 . LEU   A 1 150 ? 34.50329 19.55992 8.26032   1.000 23.10662 ? 130 LEU   A CD1 1 
ATOM   1008 C CD2 . LEU   A 1 150 ? 34.53303 17.54885 9.73249   1.000 22.32599 ? 130 LEU   A CD2 1 
ATOM   1009 N N   . THR   A 1 151 ? 29.22779 18.60860 10.18069  1.000 20.47344 ? 131 THR   A N   1 
ATOM   1010 C CA  . THR   A 1 151 ? 28.05229 19.04905 10.92629  1.000 21.03519 ? 131 THR   A CA  1 
ATOM   1011 C C   . THR   A 1 151 ? 27.50929 17.92659 11.80252  1.000 22.47291 ? 131 THR   A C   1 
ATOM   1012 O O   . THR   A 1 151 ? 27.22758 18.12855 12.99082  1.000 23.29106 ? 131 THR   A O   1 
ATOM   1013 C CB  . THR   A 1 151 ? 26.99314 19.52712 9.93352   1.000 21.08033 ? 131 THR   A CB  1 
ATOM   1014 O OG1 . THR   A 1 151 ? 27.49766 20.66087 9.21515   1.000 20.32319 ? 131 THR   A OG1 1 
ATOM   1015 C CG2 . THR   A 1 151 ? 25.70381 19.90698 10.63658  1.000 22.14373 ? 131 THR   A CG2 1 
ATOM   1016 N N   . ALA   A 1 152 ? 27.36444 16.73092 11.22946  1.000 22.44622 ? 132 ALA   A N   1 
ATOM   1017 C CA  . ALA   A 1 152 ? 26.86964 15.59189 11.99653  1.000 22.70848 ? 132 ALA   A CA  1 
ATOM   1018 C C   . ALA   A 1 152 ? 27.84715 15.19899 13.09494  1.000 25.34540 ? 132 ALA   A C   1 
ATOM   1019 O O   . ALA   A 1 152 ? 27.43111 14.80550 14.18947  1.000 28.59084 ? 132 ALA   A O   1 
ATOM   1020 C CB  . ALA   A 1 152 ? 26.61632 14.39985 11.06499  1.000 22.41175 ? 132 ALA   A CB  1 
ATOM   1021 N N   . ALA   A 1 153 ? 29.15224 15.29247 12.82476  1.000 24.70715 ? 133 ALA   A N   1 
ATOM   1022 C CA  . ALA   A 1 153 ? 30.13654 14.92806 13.84125  1.000 26.87144 ? 133 ALA   A CA  1 
ATOM   1023 C C   . ALA   A 1 153 ? 30.09766 15.86808 15.04030  1.000 28.28363 ? 133 ALA   A C   1 
ATOM   1024 O O   . ALA   A 1 153 ? 30.43650 15.45721 16.15456  1.000 30.25821 ? 133 ALA   A O   1 
ATOM   1025 C CB  . ALA   A 1 153 ? 31.53806 14.88612 13.23380  1.000 28.71986 ? 133 ALA   A CB  1 
ATOM   1026 N N   . GLU   A 1 154 ? 29.68440 17.12015 14.84119  1.000 29.49921 ? 134 GLU   A N   1 
ATOM   1027 C CA  . GLU   A 1 154 ? 29.54861 18.05116 15.95629  1.000 31.90592 ? 134 GLU   A CA  1 
ATOM   1028 C C   . GLU   A 1 154 ? 28.33812 17.74291 16.82052  1.000 31.62272 ? 134 GLU   A C   1 
ATOM   1029 O O   . GLU   A 1 154 ? 28.27554 18.20484 17.96323  1.000 32.37557 ? 134 GLU   A O   1 
ATOM   1030 C CB  . GLU   A 1 154 ? 29.37481 19.47638 15.43453  1.000 35.95051 ? 134 GLU   A CB  1 
ATOM   1031 C CG  . GLU   A 1 154 ? 30.50940 19.95517 14.59589  1.000 42.95459 ? 134 GLU   A CG  1 
ATOM   1032 C CD  . GLU   A 1 154 ? 31.23830 21.10988 15.21841  1.000 49.27597 ? 134 GLU   A CD  1 
ATOM   1033 O OE1 . GLU   A 1 154 ? 30.56762 22.01407 15.76323  1.000 52.44804 ? 134 GLU   A OE1 1 
ATOM   1034 O OE2 . GLU   A 1 154 ? 32.48556 21.10676 15.16217  1.000 52.08802 ? 134 GLU   A OE2 1 
ATOM   1035 N N   . ARG   A 1 155 ? 27.36442 17.00719 16.29346  1.000 31.22096 ? 135 ARG   A N   1 
ATOM   1036 C CA  . ARG   A 1 155 ? 26.10141 16.75719 16.98642  1.000 31.24482 ? 135 ARG   A CA  1 
ATOM   1037 C C   . ARG   A 1 155 ? 25.79222 15.26252 16.97030  1.000 31.40121 ? 135 ARG   A C   1 
ATOM   1038 O O   . ARG   A 1 155 ? 24.78824 14.82592 16.40144  1.000 33.85426 ? 135 ARG   A O   1 
ATOM   1039 C CB  . ARG   A 1 155 ? 24.97557 17.56122 16.33647  1.000 31.42856 ? 135 ARG   A CB  1 
ATOM   1040 C CG  . ARG   A 1 155 ? 25.21485 19.08424 16.26409  1.000 33.08481 ? 135 ARG   A CG  1 
ATOM   1041 C CD  . ARG   A 1 155 ? 24.97701 19.77182 17.60788  1.000 34.61588 ? 135 ARG   A CD  1 
ATOM   1042 N NE  . ARG   A 1 155 ? 25.17481 21.21985 17.52971  1.000 34.61799 ? 135 ARG   A NE  1 
ATOM   1043 C CZ  . ARG   A 1 155 ? 24.24748 22.08940 17.14276  1.000 35.93285 ? 135 ARG   A CZ  1 
ATOM   1044 N NH1 . ARG   A 1 155 ? 23.04867 21.69086 16.74693  1.000 35.43760 ? 135 ARG   A NH1 1 
ATOM   1045 N NH2 . ARG   A 1 155 ? 24.53211 23.39396 17.14252  1.000 35.82269 ? 135 ARG   A NH2 1 
ATOM   1046 N N   . PRO   A 1 156 ? 26.63768 14.44408 17.58936  1.000 33.97000 ? 136 PRO   A N   1 
ATOM   1047 C CA  . PRO   A 1 156 ? 26.36884 13.00091 17.59757  1.000 35.78253 ? 136 PRO   A CA  1 
ATOM   1048 C C   . PRO   A 1 156 ? 25.02386 12.71306 18.25023  1.000 36.51495 ? 136 PRO   A C   1 
ATOM   1049 O O   . PRO   A 1 156 ? 24.68198 13.28111 19.29145  1.000 36.72715 ? 136 PRO   A O   1 
ATOM   1050 C CB  . PRO   A 1 156 ? 27.53572 12.42440 18.40680  1.000 37.92672 ? 136 PRO   A CB  1 
ATOM   1051 C CG  . PRO   A 1 156 ? 28.02474 13.56918 19.23642  1.000 38.01060 ? 136 PRO   A CG  1 
ATOM   1052 C CD  . PRO   A 1 156 ? 27.80860 14.79730 18.41039  1.000 35.61584 ? 136 PRO   A CD  1 
ATOM   1053 N N   . GLY   A 1 157 ? 24.23626 11.86157 17.59270  1.000 36.93804 ? 137 GLY   A N   1 
ATOM   1054 C CA  . GLY   A 1 157 ? 22.93143 11.47502 18.07814  1.000 37.16644 ? 137 GLY   A CA  1 
ATOM   1055 C C   . GLY   A 1 157 ? 21.78521 12.38606 17.69103  1.000 39.02193 ? 137 GLY   A C   1 
ATOM   1056 O O   . GLY   A 1 157 ? 20.62493 12.01446 17.91197  1.000 40.76302 ? 137 GLY   A O   1 
ATOM   1057 N N   . HIS   A 1 158 ? 22.05747 13.55665 17.11092  1.000 35.84102 ? 138 HIS   A N   1 
ATOM   1058 C CA  . HIS   A 1 158 ? 21.00656 14.54457 16.89494  1.000 36.61942 ? 138 HIS   A CA  1 
ATOM   1059 C C   . HIS   A 1 158 ? 20.42104 14.53866 15.49201  1.000 33.08914 ? 138 HIS   A C   1 
ATOM   1060 O O   . HIS   A 1 158 ? 19.30367 15.03188 15.30406  1.000 36.48078 ? 138 HIS   A O   1 
ATOM   1061 C CB  . HIS   A 1 158 ? 21.51547 15.94864 17.22749  1.000 43.32348 ? 138 HIS   A CB  1 
ATOM   1062 C CG  . HIS   A 1 158 ? 21.82320 16.13679 18.67750  1.000 48.44526 ? 138 HIS   A CG  1 
ATOM   1063 N ND1 . HIS   A 1 158 ? 20.83887 16.27564 19.63087  1.000 52.36856 ? 138 HIS   A ND1 1 
ATOM   1064 C CD2 . HIS   A 1 158 ? 23.00204 16.18381 19.34118  1.000 51.77549 ? 138 HIS   A CD2 1 
ATOM   1065 C CE1 . HIS   A 1 158 ? 21.39838 16.41705 20.81993  1.000 54.86031 ? 138 HIS   A CE1 1 
ATOM   1066 N NE2 . HIS   A 1 158 ? 22.71042 16.36393 20.67164  1.000 54.88952 ? 138 HIS   A NE2 1 
ATOM   1067 N N   . PHE   A 1 159 ? 21.13825 14.02098 14.50956  1.000 27.06119 ? 139 PHE   A N   1 
ATOM   1068 C CA  . PHE   A 1 159 ? 20.62486 13.93650 13.15274  1.000 24.49161 ? 139 PHE   A CA  1 
ATOM   1069 C C   . PHE   A 1 159 ? 20.09180 12.53478 12.89684  1.000 24.92963 ? 139 PHE   A C   1 
ATOM   1070 O O   . PHE   A 1 159 ? 20.64498 11.54873 13.39141  1.000 26.42277 ? 139 PHE   A O   1 
ATOM   1071 C CB  . PHE   A 1 159 ? 21.70906 14.28829 12.13528  1.000 22.75722 ? 139 PHE   A CB  1 
ATOM   1072 C CG  . PHE   A 1 159 ? 22.07709 15.74025 12.14267  1.000 23.05808 ? 139 PHE   A CG  1 
ATOM   1073 C CD1 . PHE   A 1 159 ? 21.27977 16.67016 11.48616  1.000 24.54040 ? 139 PHE   A CD1 1 
ATOM   1074 C CD2 . PHE   A 1 159 ? 23.19731 16.18340 12.82032  1.000 23.76143 ? 139 PHE   A CD2 1 
ATOM   1075 C CE1 . PHE   A 1 159 ? 21.60111 18.02268 11.49966  1.000 25.42961 ? 139 PHE   A CE1 1 
ATOM   1076 C CE2 . PHE   A 1 159 ? 23.52780 17.54057 12.83652  1.000 23.42406 ? 139 PHE   A CE2 1 
ATOM   1077 C CZ  . PHE   A 1 159 ? 22.72947 18.45788 12.17282  1.000 24.47601 ? 139 PHE   A CZ  1 
ATOM   1078 N N   . ALA   A 1 160 ? 18.99647 12.46222 12.14134  1.000 24.36156 ? 140 ALA   A N   1 
ATOM   1079 C CA  . ALA   A 1 160 ? 18.36764 11.18811 11.83091  1.000 24.16443 ? 140 ALA   A CA  1 
ATOM   1080 C C   . ALA   A 1 160 ? 19.08347 10.45812 10.70596  1.000 22.60746 ? 140 ALA   A C   1 
ATOM   1081 O O   . ALA   A 1 160 ? 18.98829 9.22745  10.61330  1.000 23.90114 ? 140 ALA   A O   1 
ATOM   1082 C CB  . ALA   A 1 160 ? 16.90274 11.42147 11.45647  1.000 26.32578 ? 140 ALA   A CB  1 
ATOM   1083 N N   . GLY   A 1 161 ? 19.80196 11.17907 9.85606   1.000 22.50120 ? 141 GLY   A N   1 
ATOM   1084 C CA  . GLY   A 1 161 ? 20.46334 10.54432 8.74307   1.000 21.66297 ? 141 GLY   A CA  1 
ATOM   1085 C C   . GLY   A 1 161 ? 21.15258 11.57421 7.88041   1.000 20.10432 ? 141 GLY   A C   1 
ATOM   1086 O O   . GLY   A 1 161 ? 20.87810 12.77618 7.96133   1.000 22.29468 ? 141 GLY   A O   1 
ATOM   1087 N N   . MET   A 1 162 ? 22.04529 11.07211 7.04339   1.000 20.93331 ? 142 MET   A N   1 
ATOM   1088 C CA  A MET   A 1 162 ? 22.81608 11.91130 6.15222   0.630 19.91881 ? 142 MET   A CA  1 
ATOM   1089 C CA  B MET   A 1 162 ? 22.85565 11.89553 6.15427   0.370 21.12342 ? 142 MET   A CA  1 
ATOM   1090 C C   . MET   A 1 162 ? 22.89565 11.21162 4.80086   1.000 18.37949 ? 142 MET   A C   1 
ATOM   1091 O O   . MET   A 1 162 ? 23.18418 10.01289 4.73181   1.000 19.34265 ? 142 MET   A O   1 
ATOM   1092 C CB  A MET   A 1 162 ? 24.20177 12.12276 6.76906   0.630 22.20418 ? 142 MET   A CB  1 
ATOM   1093 C CB  B MET   A 1 162 ? 24.31026 11.97548 6.63195   0.370 24.63893 ? 142 MET   A CB  1 
ATOM   1094 C CG  A MET   A 1 162 ? 25.14628 12.97462 6.00143   0.630 21.33852 ? 142 MET   A CG  1 
ATOM   1095 C CG  B MET   A 1 162 ? 24.60758 12.89894 7.77553   0.370 25.70384 ? 142 MET   A CG  1 
ATOM   1096 S SD  A MET   A 1 162 ? 26.64576 13.19623 6.97938   0.630 21.39745 ? 142 MET   A SD  1 
ATOM   1097 S SD  B MET   A 1 162 ? 26.36162 13.34121 7.72789   0.370 26.84820 ? 142 MET   A SD  1 
ATOM   1098 C CE  A MET   A 1 162 ? 27.24299 11.51321 7.10625   0.630 23.64829 ? 142 MET   A CE  1 
ATOM   1099 C CE  B MET   A 1 162 ? 27.13724 11.77263 7.34611   0.370 27.78841 ? 142 MET   A CE  1 
ATOM   1100 N N   . VAL   A 1 163 ? 22.62473 11.96109 3.73566   1.000 18.46462 ? 143 VAL   A N   1 
ATOM   1101 C CA  . VAL   A 1 163 ? 22.76208 11.47720 2.36851   1.000 19.02878 ? 143 VAL   A CA  1 
ATOM   1102 C C   . VAL   A 1 163 ? 23.96375 12.18652 1.77791   1.000 17.04860 ? 143 VAL   A C   1 
ATOM   1103 O O   . VAL   A 1 163 ? 24.00393 13.42525 1.75620   1.000 17.99990 ? 143 VAL   A O   1 
ATOM   1104 C CB  . VAL   A 1 163 ? 21.50640 11.76277 1.53131   1.000 19.54435 ? 143 VAL   A CB  1 
ATOM   1105 C CG1 . VAL   A 1 163 ? 21.76754 11.42450 0.05869   1.000 21.29965 ? 143 VAL   A CG1 1 
ATOM   1106 C CG2 . VAL   A 1 163 ? 20.30369 10.98375 2.08357   1.000 20.19184 ? 143 VAL   A CG2 1 
ATOM   1107 N N   . LEU   A 1 164 ? 24.94588 11.42114 1.30823   1.000 15.86216 ? 144 LEU   A N   1 
ATOM   1108 C CA  . LEU   A 1 164 ? 26.19209 11.97556 0.78320   1.000 16.49527 ? 144 LEU   A CA  1 
ATOM   1109 C C   . LEU   A 1 164 ? 26.34413 11.58638 -0.68103  1.000 18.16598 ? 144 LEU   A C   1 
ATOM   1110 O O   . LEU   A 1 164 ? 26.39629 10.39675 -1.01056  1.000 18.68550 ? 144 LEU   A O   1 
ATOM   1111 C CB  . LEU   A 1 164 ? 27.38990 11.46399 1.58256   1.000 18.31660 ? 144 LEU   A CB  1 
ATOM   1112 C CG  . LEU   A 1 164 ? 27.41215 11.82451 3.06916   1.000 19.45419 ? 144 LEU   A CG  1 
ATOM   1113 C CD1 . LEU   A 1 164 ? 28.57845 11.16204 3.76408   1.000 21.52477 ? 144 LEU   A CD1 1 
ATOM   1114 C CD2 . LEU   A 1 164 ? 27.45039 13.36080 3.26812   1.000 20.43607 ? 144 LEU   A CD2 1 
ATOM   1115 N N   . ILE   A 1 165 ? 26.45621 12.58093 -1.55042  1.000 16.57280 ? 145 ILE   A N   1 
ATOM   1116 C CA  . ILE   A 1 165 ? 26.67217 12.36561 -2.97139  1.000 16.02436 ? 145 ILE   A CA  1 
ATOM   1117 C C   . ILE   A 1 165 ? 28.10461 12.78745 -3.25456  1.000 15.66055 ? 145 ILE   A C   1 
ATOM   1118 O O   . ILE   A 1 165 ? 28.42244 13.97907 -3.20379  1.000 17.51246 ? 145 ILE   A O   1 
ATOM   1119 C CB  . ILE   A 1 165 ? 25.68451 13.17201 -3.82424  1.000 17.37328 ? 145 ILE   A CB  1 
ATOM   1120 C CG1 . ILE   A 1 165 ? 24.23790 12.88181 -3.39117  1.000 18.36355 ? 145 ILE   A CG1 1 
ATOM   1121 C CG2 . ILE   A 1 165 ? 25.91094 12.88416 -5.30524  1.000 18.06030 ? 145 ILE   A CG2 1 
ATOM   1122 C CD1 . ILE   A 1 165 ? 23.18872 13.72312 -4.12041  1.000 20.05299 ? 145 ILE   A CD1 1 
ATOM   1123 N N   . SER   A 1 166 ? 28.97876 11.81645 -3.52621  1.000 17.15930 ? 146 SER   A N   1 
ATOM   1124 C CA  A SER   A 1 166 ? 30.39778 12.03777 -3.79114  0.781 16.74450 ? 146 SER   A CA  1 
ATOM   1125 C CA  B SER   A 1 166 ? 30.39602 12.04594 -3.79879  0.219 17.05173 ? 146 SER   A CA  1 
ATOM   1126 C C   . SER   A 1 166 ? 30.98278 13.08612 -2.83542  1.000 17.31948 ? 146 SER   A C   1 
ATOM   1127 O O   . SER   A 1 166 ? 31.49662 14.11977 -3.27726  1.000 17.82602 ? 146 SER   A O   1 
ATOM   1128 C CB  A SER   A 1 166 ? 30.66078 12.40296 -5.24974  0.781 18.20446 ? 146 SER   A CB  1 
ATOM   1129 C CB  B SER   A 1 166 ? 30.62678 12.45302 -5.24953  0.219 17.73074 ? 146 SER   A CB  1 
ATOM   1130 O OG  A SER   A 1 166 ? 29.73790 13.35949 -5.73850  0.781 17.74905 ? 146 SER   A OG  1 
ATOM   1131 O OG  B SER   A 1 166 ? 29.67541 11.85512 -6.10756  0.219 17.74380 ? 146 SER   A OG  1 
ATOM   1132 N N   . PRO   A 1 167 ? 30.91037 12.84609 -1.52153  1.000 17.03803 ? 147 PRO   A N   1 
ATOM   1133 C CA  . PRO   A 1 167 ? 31.42835 13.82428 -0.56092  1.000 17.59582 ? 147 PRO   A CA  1 
ATOM   1134 C C   . PRO   A 1 167 ? 32.93345 13.94231 -0.67602  1.000 18.18995 ? 147 PRO   A C   1 
ATOM   1135 O O   . PRO   A 1 167 ? 33.63097 12.99328 -1.04785  1.000 18.78604 ? 147 PRO   A O   1 
ATOM   1136 C CB  . PRO   A 1 167 ? 31.04347 13.21937 0.79756   1.000 18.04971 ? 147 PRO   A CB  1 
ATOM   1137 C CG  . PRO   A 1 167 ? 31.07861 11.70311 0.52494   1.000 17.44993 ? 147 PRO   A CG  1 
ATOM   1138 C CD  . PRO   A 1 167 ? 30.50409 11.58006 -0.87336  1.000 17.30344 ? 147 PRO   A CD  1 
ATOM   1139 N N   . LEU   A 1 168 ? 33.43290 15.13354 -0.33808  1.000 17.63677 ? 148 LEU   A N   1 
ATOM   1140 C CA  . LEU   A 1 168 ? 34.86658 15.36881 -0.27341  1.000 18.59197 ? 148 LEU   A CA  1 
ATOM   1141 C C   . LEU   A 1 168 ? 35.43574 14.68285 0.96904   1.000 19.63424 ? 148 LEU   A C   1 
ATOM   1142 O O   . LEU   A 1 168 ? 35.40004 15.24286 2.06846   1.000 20.01461 ? 148 LEU   A O   1 
ATOM   1143 C CB  . LEU   A 1 168 ? 35.16388 16.87626 -0.29013  1.000 18.29737 ? 148 LEU   A CB  1 
ATOM   1144 C CG  . LEU   A 1 168 ? 36.63372 17.27778 -0.16658  1.000 20.06620 ? 148 LEU   A CG  1 
ATOM   1145 C CD1 . LEU   A 1 168 ? 37.48438 16.59280 -1.22371  1.000 20.06929 ? 148 LEU   A CD1 1 
ATOM   1146 C CD2 . LEU   A 1 168 ? 36.77300 18.79848 -0.25635  1.000 21.41646 ? 148 LEU   A CD2 1 
ATOM   1147 N N   . VAL   A 1 169 ? 35.90320 13.44361 0.80903   1.000 18.03406 ? 149 VAL   A N   1 
ATOM   1148 C CA  . VAL   A 1 169 ? 36.62815 12.71834 1.84585   1.000 19.58641 ? 149 VAL   A CA  1 
ATOM   1149 C C   . VAL   A 1 169 ? 38.11106 12.62453 1.50696   1.000 20.76972 ? 149 VAL   A C   1 
ATOM   1150 O O   . VAL   A 1 169 ? 38.97390 12.89443 2.34320   1.000 22.29076 ? 149 VAL   A O   1 
ATOM   1151 C CB  . VAL   A 1 169 ? 36.01460 11.31678 2.09268   1.000 18.86594 ? 149 VAL   A CB  1 
ATOM   1152 C CG1 . VAL   A 1 169 ? 36.78631 10.56683 3.18853   1.000 19.27839 ? 149 VAL   A CG1 1 
ATOM   1153 C CG2 . VAL   A 1 169 ? 34.53943 11.43458 2.46002   1.000 20.80411 ? 149 VAL   A CG2 1 
ATOM   1154 N N   . LEU   A 1 170 ? 38.42099 12.25013 0.27536   1.000 19.93081 ? 150 LEU   A N   1 
ATOM   1155 C CA  . LEU   A 1 170 ? 39.77411 12.32365 -0.24939  1.000 20.55440 ? 150 LEU   A CA  1 
ATOM   1156 C C   . LEU   A 1 170 ? 39.69697 13.07077 -1.56307  1.000 20.28190 ? 150 LEU   A C   1 
ATOM   1157 O O   . LEU   A 1 170 ? 38.85587 12.76142 -2.41331  1.000 21.79915 ? 150 LEU   A O   1 
ATOM   1158 C CB  . LEU   A 1 170 ? 40.37694 10.93589 -0.47888  1.000 23.26629 ? 150 LEU   A CB  1 
ATOM   1159 C CG  . LEU   A 1 170 ? 40.76434 10.20878 0.80575   1.000 27.31802 ? 150 LEU   A CG  1 
ATOM   1160 C CD1 . LEU   A 1 170 ? 41.33561 8.85689  0.45120   1.000 28.31091 ? 150 LEU   A CD1 1 
ATOM   1161 C CD2 . LEU   A 1 170 ? 41.76836 11.01987 1.63100   1.000 29.28935 ? 150 LEU   A CD2 1 
ATOM   1162 N N   . ALA   A 1 171 ? 40.54961 14.06780 -1.71368  1.000 21.39337 ? 151 ALA   A N   1 
ATOM   1163 C CA  . ALA   A 1 171 ? 40.59176 14.80090 -2.95958  1.000 23.01476 ? 151 ALA   A CA  1 
ATOM   1164 C C   . ALA   A 1 171 ? 41.21269 13.93529 -4.04414  1.000 23.53340 ? 151 ALA   A C   1 
ATOM   1165 O O   . ALA   A 1 171 ? 42.02260 13.04161 -3.77264  1.000 24.37980 ? 151 ALA   A O   1 
ATOM   1166 C CB  . ALA   A 1 171 ? 41.43295 16.06280 -2.79102  1.000 23.77407 ? 151 ALA   A CB  1 
ATOM   1167 N N   . ASN   A 1 172 ? 40.80418 14.19452 -5.27645  1.000 24.45474 ? 152 ASN   A N   1 
ATOM   1168 C CA  . ASN   A 1 172 ? 41.50683 13.65147 -6.41953  1.000 25.70122 ? 152 ASN   A CA  1 
ATOM   1169 C C   . ASN   A 1 172 ? 43.00775 13.85462 -6.21558  1.000 27.29076 ? 152 ASN   A C   1 
ATOM   1170 O O   . ASN   A 1 172 ? 43.43567 14.97449 -5.90891  1.000 28.85715 ? 152 ASN   A O   1 
ATOM   1171 C CB  . ASN   A 1 172 ? 41.04875 14.40340 -7.66790  1.000 26.08632 ? 152 ASN   A CB  1 
ATOM   1172 C CG  . ASN   A 1 172 ? 42.01518 14.26792 -8.80138  1.000 29.82114 ? 152 ASN   A CG  1 
ATOM   1173 O OD1 . ASN   A 1 172 ? 42.64448 15.24199 -9.21165  1.000 31.63134 ? 152 ASN   A OD1 1 
ATOM   1174 N ND2 . ASN   A 1 172 ? 42.15967 13.04678 -9.31228  1.000 30.97653 ? 152 ASN   A ND2 1 
ATOM   1175 N N   . PRO   A 1 173 ? 43.82289 12.80486 -6.33076  1.000 28.39011 ? 153 PRO   A N   1 
ATOM   1176 C CA  . PRO   A 1 173 ? 45.23921 12.94392 -5.94968  1.000 32.00567 ? 153 PRO   A CA  1 
ATOM   1177 C C   . PRO   A 1 173 ? 46.01937 13.96558 -6.76283  1.000 33.68153 ? 153 PRO   A C   1 
ATOM   1178 O O   . PRO   A 1 173 ? 46.85914 14.67052 -6.19111  1.000 34.85150 ? 153 PRO   A O   1 
ATOM   1179 C CB  . PRO   A 1 173 ? 45.79262 11.51659 -6.08108  1.000 32.72847 ? 153 PRO   A CB  1 
ATOM   1180 C CG  . PRO   A 1 173 ? 44.78357 10.77595 -6.89646  1.000 33.16269 ? 153 PRO   A CG  1 
ATOM   1181 C CD  . PRO   A 1 173 ? 43.45868 11.41169 -6.62623  1.000 29.72947 ? 153 PRO   A CD  1 
ATOM   1182 N N   . GLU   A 1 174 ? 45.77310 14.07976 -8.07360  1.000 33.94889 ? 154 GLU   A N   1 
ATOM   1183 C CA  . GLU   A 1 174 ? 46.43439 15.13049 -8.84703  1.000 36.10914 ? 154 GLU   A CA  1 
ATOM   1184 C C   . GLU   A 1 174 ? 46.09891 16.51419 -8.29892  1.000 37.23387 ? 154 GLU   A C   1 
ATOM   1185 O O   . GLU   A 1 174 ? 46.98423 17.36698 -8.15077  1.000 38.24747 ? 154 GLU   A O   1 
ATOM   1186 C CB  . GLU   A 1 174 ? 46.05053 15.02991 -10.32314 1.000 39.74345 ? 154 GLU   A CB  1 
ATOM   1187 C CG  . GLU   A 1 174 ? 46.61454 13.81201 -11.03784 1.000 42.63493 ? 154 GLU   A CG  1 
ATOM   1188 C CD  . GLU   A 1 174 ? 45.71915 12.59347 -10.93915 1.000 45.37629 ? 154 GLU   A CD  1 
ATOM   1189 O OE1 . GLU   A 1 174 ? 44.72874 12.63161 -10.17593 1.000 45.87438 ? 154 GLU   A OE1 1 
ATOM   1190 O OE2 . GLU   A 1 174 ? 46.00961 11.59262 -11.63362 1.000 47.75501 ? 154 GLU   A OE2 1 
ATOM   1191 N N   . SER   A 1 175 ? 44.82229 16.75609 -7.99177  1.000 38.42199 ? 155 SER   A N   1 
ATOM   1192 C CA  . SER   A 1 175 ? 44.43076 18.03857 -7.41042  1.000 37.61180 ? 155 SER   A CA  1 
ATOM   1193 C C   . SER   A 1 175 ? 45.09359 18.25556 -6.05523  1.000 38.72568 ? 155 SER   A C   1 
ATOM   1194 O O   . SER   A 1 175 ? 45.56775 19.35918 -5.75558  1.000 39.83233 ? 155 SER   A O   1 
ATOM   1195 C CB  . SER   A 1 175 ? 42.91001 18.10248 -7.27771  1.000 35.50576 ? 155 SER   A CB  1 
ATOM   1196 O OG  . SER   A 1 175 ? 42.28694 17.89480 -8.53031  1.000 33.53314 ? 155 SER   A OG  1 
ATOM   1197 N N   . ALA   A 1 176 ? 45.14008 17.21131 -5.22389  1.000 38.25938 ? 156 ALA   A N   1 
ATOM   1198 C CA  . ALA   A 1 176 ? 45.74074 17.34485 -3.90133  1.000 39.65953 ? 156 ALA   A CA  1 
ATOM   1199 C C   . ALA   A 1 176 ? 47.21969 17.69267 -3.99926  1.000 40.31994 ? 156 ALA   A C   1 
ATOM   1200 O O   . ALA   A 1 176 ? 47.70685 18.57174 -3.28016  1.000 42.26920 ? 156 ALA   A O   1 
ATOM   1201 C CB  . ALA   A 1 176 ? 45.53625 16.06070 -3.09766  1.000 40.14437 ? 156 ALA   A CB  1 
ATOM   1202 N N   . THR   A 1 177 ? 47.94729 17.02123 -4.89100  1.000 39.83569 ? 157 THR   A N   1 
ATOM   1203 C CA  . THR   A 1 177 ? 49.36710 17.31215 -5.05184  1.000 43.09127 ? 157 THR   A CA  1 
ATOM   1204 C C   . THR   A 1 177 ? 49.59030 18.72038 -5.59264  1.000 44.34003 ? 157 THR   A C   1 
ATOM   1205 O O   . THR   A 1 177 ? 50.49309 19.42961 -5.13219  1.000 45.01032 ? 157 THR   A O   1 
ATOM   1206 C CB  . THR   A 1 177 ? 50.00670 16.26673 -5.96172  1.000 44.65297 ? 157 THR   A CB  1 
ATOM   1207 O OG1 . THR   A 1 177 ? 49.90703 14.97886 -5.34302  1.000 45.10581 ? 157 THR   A OG1 1 
ATOM   1208 C CG2 . THR   A 1 177 ? 51.47194 16.59927 -6.20915  1.000 45.25090 ? 157 THR   A CG2 1 
ATOM   1209 N N   . THR   A 1 178 ? 48.78004 19.14034 -6.56889  1.000 44.94125 ? 158 THR   A N   1 
ATOM   1210 C CA  . THR   A 1 178 ? 48.89713 20.49210 -7.10979  1.000 44.49989 ? 158 THR   A CA  1 
ATOM   1211 C C   . THR   A 1 178 ? 48.76778 21.53165 -6.00798  1.000 44.72865 ? 158 THR   A C   1 
ATOM   1212 O O   . THR   A 1 178 ? 49.61575 22.42070 -5.87014  1.000 46.12556 ? 158 THR   A O   1 
ATOM   1213 C CB  . THR   A 1 178 ? 47.82342 20.72324 -8.17553  1.000 44.67870 ? 158 THR   A CB  1 
ATOM   1214 O OG1 . THR   A 1 178 ? 48.11133 19.92682 -9.33213  1.000 45.93002 ? 158 THR   A OG1 1 
ATOM   1215 C CG2 . THR   A 1 178 ? 47.76109 22.19861 -8.57023  1.000 44.00310 ? 158 THR   A CG2 1 
ATOM   1216 N N   . PHE   A 1 179 ? 47.71636 21.42683 -5.19983  1.000 43.21788 ? 159 PHE   A N   1 
ATOM   1217 C CA  . PHE   A 1 179 ? 47.49136 22.44565 -4.18594  1.000 44.12523 ? 159 PHE   A CA  1 
ATOM   1218 C C   . PHE   A 1 179 ? 48.40096 22.28896 -2.97913  1.000 44.54289 ? 159 PHE   A C   1 
ATOM   1219 O O   . PHE   A 1 179 ? 48.72188 23.29043 -2.33260  1.000 45.83207 ? 159 PHE   A O   1 
ATOM   1220 C CB  . PHE   A 1 179 ? 46.02177 22.49519 -3.78701  1.000 42.35382 ? 159 PHE   A CB  1 
ATOM   1221 C CG  . PHE   A 1 179 ? 45.19289 23.30231 -4.72255  1.000 43.82129 ? 159 PHE   A CG  1 
ATOM   1222 C CD1 . PHE   A 1 179 ? 44.73392 22.75176 -5.91049  1.000 45.07111 ? 159 PHE   A CD1 1 
ATOM   1223 C CD2 . PHE   A 1 179 ? 44.90226 24.62763 -4.43941  1.000 44.37806 ? 159 PHE   A CD2 1 
ATOM   1224 C CE1 . PHE   A 1 179 ? 43.97086 23.49666 -6.78887  1.000 45.65797 ? 159 PHE   A CE1 1 
ATOM   1225 C CE2 . PHE   A 1 179 ? 44.14026 25.37974 -5.31311  1.000 45.44973 ? 159 PHE   A CE2 1 
ATOM   1226 C CZ  . PHE   A 1 179 ? 43.67088 24.81134 -6.48874  1.000 45.76066 ? 159 PHE   A CZ  1 
ATOM   1227 N N   . LYS   A 1 180 ? 48.82056 21.06427 -2.64999  1.000 43.48298 ? 160 LYS   A N   1 
ATOM   1228 C CA  . LYS   A 1 180 ? 49.77844 20.90993 -1.56031  1.000 43.31645 ? 160 LYS   A CA  1 
ATOM   1229 C C   . LYS   A 1 180 ? 51.08991 21.60760 -1.88960  1.000 41.68274 ? 160 LYS   A C   1 
ATOM   1230 O O   . LYS   A 1 180 ? 51.70078 22.23596 -1.01957  1.000 41.38875 ? 160 LYS   A O   1 
ATOM   1231 C CB  . LYS   A 1 180 ? 50.01231 19.43391 -1.23665  1.000 44.47315 ? 160 LYS   A CB  1 
ATOM   1232 C CG  . LYS   A 1 180 ? 48.95968 18.81381 -0.32721  1.000 46.92779 ? 160 LYS   A CG  1 
ATOM   1233 C CD  . LYS   A 1 180 ? 49.29152 17.36027 -0.03174  1.000 49.51448 ? 160 LYS   A CD  1 
ATOM   1234 C CE  . LYS   A 1 180 ? 48.04300 16.49617 -0.00791  1.000 52.51428 ? 160 LYS   A CE  1 
ATOM   1235 N NZ  . LYS   A 1 180 ? 48.29377 15.15034 -0.61406  1.000 54.59567 ? 160 LYS   A NZ  1 
ATOM   1236 N N   . VAL   A 1 181 ? 51.53016 21.52034 -3.14659  1.000 42.39831 ? 161 VAL   A N   1 
ATOM   1237 C CA  . VAL   A 1 181 ? 52.75262 22.20590 -3.55944  1.000 43.11107 ? 161 VAL   A CA  1 
ATOM   1238 C C   . VAL   A 1 181 ? 52.55155 23.71517 -3.54101  1.000 43.20823 ? 161 VAL   A C   1 
ATOM   1239 O O   . VAL   A 1 181 ? 53.38699 24.46332 -3.01917  1.000 44.40514 ? 161 VAL   A O   1 
ATOM   1240 C CB  . VAL   A 1 181 ? 53.21522 21.70091 -4.93808  1.000 45.75097 ? 161 VAL   A CB  1 
ATOM   1241 C CG1 . VAL   A 1 181 ? 54.23141 22.65412 -5.54619  1.000 46.93247 ? 161 VAL   A CG1 1 
ATOM   1242 C CG2 . VAL   A 1 181 ? 53.80194 20.30454 -4.81180  1.000 45.83204 ? 161 VAL   A CG2 1 
ATOM   1243 N N   . LEU   A 1 182 ? 51.44337 24.18311 -4.11894  1.000 40.91278 ? 162 LEU   A N   1 
ATOM   1244 C CA  . LEU   A 1 182 ? 51.13770 25.60908 -4.10175  1.000 40.81657 ? 162 LEU   A CA  1 
ATOM   1245 C C   . LEU   A 1 182 ? 50.91085 26.11054 -2.68380  1.000 41.52592 ? 162 LEU   A C   1 
ATOM   1246 O O   . LEU   A 1 182 ? 51.26856 27.24968 -2.35901  1.000 40.10433 ? 162 LEU   A O   1 
ATOM   1247 C CB  . LEU   A 1 182 ? 49.90531 25.88885 -4.95635  1.000 40.04680 ? 162 LEU   A CB  1 
ATOM   1248 C CG  . LEU   A 1 182 ? 50.11937 25.90777 -6.46315  1.000 41.21994 ? 162 LEU   A CG  1 
ATOM   1249 C CD1 . LEU   A 1 182 ? 48.79019 26.13396 -7.16733  1.000 40.95147 ? 162 LEU   A CD1 1 
ATOM   1250 C CD2 . LEU   A 1 182 ? 51.12452 26.98830 -6.83127  1.000 43.26492 ? 162 LEU   A CD2 1 
ATOM   1251 N N   . ALA   A 1 183 ? 50.29786 25.28468 -1.82925  1.000 43.79395 ? 163 ALA   A N   1 
ATOM   1252 C CA  . ALA   A 1 183 ? 50.08639 25.69307 -0.44440  1.000 45.35495 ? 163 ALA   A CA  1 
ATOM   1253 C C   . ALA   A 1 183 ? 51.40295 26.00116 0.24719   1.000 47.00991 ? 163 ALA   A C   1 
ATOM   1254 O O   . ALA   A 1 183 ? 51.44374 26.83240 1.16061   1.000 46.98090 ? 163 ALA   A O   1 
ATOM   1255 C CB  . ALA   A 1 183 ? 49.32911 24.61309 0.32676   1.000 46.41595 ? 163 ALA   A CB  1 
ATOM   1256 N N   . ALA   A 1 184 ? 52.48584 25.34484 -0.17719  1.000 49.62343 ? 164 ALA   A N   1 
ATOM   1257 C CA  . ALA   A 1 184 ? 53.80348 25.63579 0.37416   1.000 50.82438 ? 164 ALA   A CA  1 
ATOM   1258 C C   . ALA   A 1 184 ? 54.21342 27.07221 0.08695   1.000 52.05879 ? 164 ALA   A C   1 
ATOM   1259 O O   . ALA   A 1 184 ? 54.81533 27.73766 0.93723   1.000 54.17395 ? 164 ALA   A O   1 
ATOM   1260 C CB  . ALA   A 1 184 ? 54.82305 24.66540 -0.21489  1.000 51.84279 ? 164 ALA   A CB  1 
ATOM   1261 N N   . LYS   A 1 185 ? 53.90257 27.56468 -1.11055  1.000 51.13397 ? 165 LYS   A N   1 
ATOM   1262 C CA  . LYS   A 1 185 ? 54.17632 28.95820 -1.43693  1.000 52.01147 ? 165 LYS   A CA  1 
ATOM   1263 C C   . LYS   A 1 185 ? 53.32941 29.89088 -0.57883  1.000 47.63553 ? 165 LYS   A C   1 
ATOM   1264 O O   . LYS   A 1 185 ? 53.84938 30.81624 0.05582   1.000 47.22984 ? 165 LYS   A O   1 
ATOM   1265 C CB  . LYS   A 1 185 ? 53.89420 29.19294 -2.92346  1.000 56.53235 ? 165 LYS   A CB  1 
ATOM   1266 C CG  . LYS   A 1 185 ? 54.86973 30.12942 -3.62260  1.000 60.49930 ? 165 LYS   A CG  1 
ATOM   1267 C CD  . LYS   A 1 185 ? 54.48840 30.32206 -5.08612  1.000 62.52894 ? 165 LYS   A CD  1 
ATOM   1268 C CE  . LYS   A 1 185 ? 54.43078 28.99267 -5.82507  1.000 64.63913 ? 165 LYS   A CE  1 
ATOM   1269 N NZ  . LYS   A 1 185 ? 54.07522 29.17485 -7.26311  1.000 66.83880 ? 165 LYS   A NZ  1 
ATOM   1270 N N   . VAL   A 1 186 ? 52.02074 29.64060 -0.52696  1.000 43.76202 ? 166 VAL   A N   1 
ATOM   1271 C CA  . VAL   A 1 186 ? 51.09415 30.57709 0.09786   1.000 41.78764 ? 166 VAL   A CA  1 
ATOM   1272 C C   . VAL   A 1 186 ? 51.21366 30.55488 1.61664   1.000 40.34806 ? 166 VAL   A C   1 
ATOM   1273 O O   . VAL   A 1 186 ? 51.05854 31.59210 2.27258   1.000 40.82573 ? 166 VAL   A O   1 
ATOM   1274 C CB  . VAL   A 1 186 ? 49.66098 30.31471 -0.41045  1.000 42.83356 ? 166 VAL   A CB  1 
ATOM   1275 C CG1 . VAL   A 1 186 ? 48.62385 30.91438 0.51798   1.000 44.26722 ? 166 VAL   A CG1 1 
ATOM   1276 C CG2 . VAL   A 1 186 ? 49.49736 30.87518 -1.80724  1.000 44.16935 ? 166 VAL   A CG2 1 
ATOM   1277 N N   . LEU   A 1 187 ? 51.50161 29.39444 2.20806   1.000 38.53953 ? 167 LEU   A N   1 
ATOM   1278 C CA  . LEU   A 1 187 ? 51.62571 29.33586 3.66056   1.000 37.19014 ? 167 LEU   A CA  1 
ATOM   1279 C C   . LEU   A 1 187 ? 52.94712 29.89335 4.17658   1.000 35.50461 ? 167 LEU   A C   1 
ATOM   1280 O O   . LEU   A 1 187 ? 53.04956 30.18603 5.37189   1.000 35.97170 ? 167 LEU   A O   1 
ATOM   1281 C CB  . LEU   A 1 187 ? 51.40040 27.91104 4.17597   1.000 38.93345 ? 167 LEU   A CB  1 
ATOM   1282 C CG  . LEU   A 1 187 ? 49.93887 27.45146 4.14614   1.000 40.82516 ? 167 LEU   A CG  1 
ATOM   1283 C CD1 . LEU   A 1 187 ? 49.77372 26.09018 4.79785   1.000 43.12365 ? 167 LEU   A CD1 1 
ATOM   1284 C CD2 . LEU   A 1 187 ? 49.04628 28.48003 4.82118   1.000 41.51785 ? 167 LEU   A CD2 1 
ATOM   1285 N N   . ASN   A 1 188 ? 53.95127 30.06342 3.31502   1.000 35.31961 ? 168 ASN   A N   1 
ATOM   1286 C CA  . ASN   A 1 188 ? 55.24505 30.59121 3.73341   1.000 35.50956 ? 168 ASN   A CA  1 
ATOM   1287 C C   . ASN   A 1 188 ? 55.54072 31.98779 3.20932   1.000 36.41040 ? 168 ASN   A C   1 
ATOM   1288 O O   . ASN   A 1 188 ? 56.51578 32.60561 3.65362   1.000 39.71369 ? 168 ASN   A O   1 
ATOM   1289 C CB  . ASN   A 1 188 ? 56.37713 29.64183 3.32159   1.000 37.46731 ? 168 ASN   A CB  1 
ATOM   1290 C CG  . ASN   A 1 188 ? 56.34814 28.34475 4.09209   1.000 38.79265 ? 168 ASN   A CG  1 
ATOM   1291 O OD1 . ASN   A 1 188 ? 56.68749 28.30758 5.27596   1.000 40.03153 ? 168 ASN   A OD1 1 
ATOM   1292 N ND2 . ASN   A 1 188 ? 55.94309 27.27182 3.42875   1.000 39.70201 ? 168 ASN   A ND2 1 
ATOM   1293 N N   . SER   A 1 189 ? 54.74467 32.49510 2.27973   1.000 32.67383 ? 169 SER   A N   1 
ATOM   1294 C CA  . SER   A 1 189 ? 54.85763 33.86362 1.81243   1.000 33.20213 ? 169 SER   A CA  1 
ATOM   1295 C C   . SER   A 1 189 ? 53.49875 34.51990 1.95818   1.000 33.17546 ? 169 SER   A C   1 
ATOM   1296 O O   . SER   A 1 189 ? 52.52385 33.89367 2.38726   1.000 35.67057 ? 169 SER   A O   1 
ATOM   1297 C CB  . SER   A 1 189 ? 55.35049 33.92499 0.36105   1.000 33.28907 ? 169 SER   A CB  1 
ATOM   1298 O OG  . SER   A 1 189 ? 56.76611 33.85694 0.31460   1.000 35.81821 ? 169 SER   A OG  1 
ATOM   1299 N N   . VAL   A 1 190 ? 53.44079 35.79758 1.61991   1.000 32.01742 ? 170 VAL   A N   1 
ATOM   1300 C CA  . VAL   A 1 190 ? 52.19144 36.54073 1.59156   1.000 32.18226 ? 170 VAL   A CA  1 
ATOM   1301 C C   . VAL   A 1 190 ? 51.79906 36.65178 0.12621   1.000 31.54804 ? 170 VAL   A C   1 
ATOM   1302 O O   . VAL   A 1 190 ? 52.28375 37.52988 -0.59798  1.000 31.81880 ? 170 VAL   A O   1 
ATOM   1303 C CB  . VAL   A 1 190 ? 52.32558 37.90579 2.26684   1.000 32.90941 ? 170 VAL   A CB  1 
ATOM   1304 C CG1 . VAL   A 1 190 ? 50.99007 38.61854 2.24952   1.000 35.72387 ? 170 VAL   A CG1 1 
ATOM   1305 C CG2 . VAL   A 1 190 ? 52.81980 37.72405 3.68910   1.000 33.82163 ? 170 VAL   A CG2 1 
ATOM   1306 N N   . LEU   A 1 191 ? 50.93693 35.73293 -0.31049  1.000 30.60320 ? 171 LEU   A N   1 
ATOM   1307 C CA  . LEU   A 1 191 ? 50.46667 35.66765 -1.69596  1.000 31.72276 ? 171 LEU   A CA  1 
ATOM   1308 C C   . LEU   A 1 191 ? 48.95866 35.45591 -1.68912  1.000 35.69090 ? 171 LEU   A C   1 
ATOM   1309 O O   . LEU   A 1 191 ? 48.45825 34.39757 -2.08782  1.000 34.95841 ? 171 LEU   A O   1 
ATOM   1310 C CB  . LEU   A 1 191 ? 51.18048 34.54474 -2.45073  1.000 31.40640 ? 171 LEU   A CB  1 
ATOM   1311 C CG  . LEU   A 1 191 ? 52.68170 34.73607 -2.67886  1.000 30.91549 ? 171 LEU   A CG  1 
ATOM   1312 C CD1 . LEU   A 1 191 ? 53.31814 33.41627 -3.07788  1.000 31.12992 ? 171 LEU   A CD1 1 
ATOM   1313 C CD2 . LEU   A 1 191 ? 52.93067 35.80222 -3.74987  1.000 30.32984 ? 171 LEU   A CD2 1 
ATOM   1314 N N   . PRO   A 1 192 ? 48.19661 36.47052 -1.26871  1.000 40.60672 ? 172 PRO   A N   1 
ATOM   1315 C CA  . PRO   A 1 192 ? 46.76288 36.25391 -1.00300  1.000 43.23996 ? 172 PRO   A CA  1 
ATOM   1316 C C   . PRO   A 1 192 ? 45.93954 35.87010 -2.22232  1.000 45.00425 ? 172 PRO   A C   1 
ATOM   1317 O O   . PRO   A 1 192 ? 44.90985 35.19922 -2.07052  1.000 47.01703 ? 172 PRO   A O   1 
ATOM   1318 C CB  . PRO   A 1 192 ? 46.31071 37.59621 -0.40955  1.000 43.47867 ? 172 PRO   A CB  1 
ATOM   1319 C CG  . PRO   A 1 192 ? 47.29688 38.59457 -0.94140  1.000 42.50726 ? 172 PRO   A CG  1 
ATOM   1320 C CD  . PRO   A 1 192 ? 48.60471 37.86378 -1.01736  1.000 41.85576 ? 172 PRO   A CD  1 
ATOM   1321 N N   . ASN   A 1 193 ? 46.35398 36.26055 -3.42683  1.000 45.60236 ? 173 ASN   A N   1 
ATOM   1322 C CA  . ASN   A 1 193 ? 45.54215 36.04856 -4.61801  1.000 45.41661 ? 173 ASN   A CA  1 
ATOM   1323 C C   . ASN   A 1 193 ? 46.08339 34.96141 -5.53438  1.000 41.92725 ? 173 ASN   A C   1 
ATOM   1324 O O   . ASN   A 1 193 ? 45.59806 34.82189 -6.66137  1.000 43.68553 ? 173 ASN   A O   1 
ATOM   1325 C CB  . ASN   A 1 193 ? 45.36441 37.35958 -5.38359  1.000 48.39856 ? 173 ASN   A CB  1 
ATOM   1326 C CG  . ASN   A 1 193 ? 44.65570 38.40943 -4.56433  1.000 50.80382 ? 173 ASN   A CG  1 
ATOM   1327 O OD1 . ASN   A 1 193 ? 43.69315 38.11055 -3.85528  1.000 52.79382 ? 173 ASN   A OD1 1 
ATOM   1328 N ND2 . ASN   A 1 193 ? 45.13526 39.64606 -4.64132  1.000 50.29543 ? 173 ASN   A ND2 1 
ATOM   1329 N N   . LEU   A 1 194 ? 47.06951 34.18965 -5.08792  1.000 38.18186 ? 174 LEU   A N   1 
ATOM   1330 C CA  . LEU   A 1 194 ? 47.60497 33.13611 -5.93363  1.000 36.98548 ? 174 LEU   A CA  1 
ATOM   1331 C C   . LEU   A 1 194 ? 46.50142 32.12913 -6.22819  1.000 35.78200 ? 174 LEU   A C   1 
ATOM   1332 O O   . LEU   A 1 194 ? 45.76688 31.71816 -5.32742  1.000 34.66944 ? 174 LEU   A O   1 
ATOM   1333 C CB  . LEU   A 1 194 ? 48.77683 32.45078 -5.23519  1.000 38.50442 ? 174 LEU   A CB  1 
ATOM   1334 C CG  . LEU   A 1 194 ? 49.72696 31.68938 -6.15984  1.000 40.60667 ? 174 LEU   A CG  1 
ATOM   1335 C CD1 . LEU   A 1 194 ? 50.45058 32.65055 -7.08685  1.000 41.02546 ? 174 LEU   A CD1 1 
ATOM   1336 C CD2 . LEU   A 1 194 ? 50.71724 30.86702 -5.35292  1.000 41.19772 ? 174 LEU   A CD2 1 
ATOM   1337 N N   . SER   A 1 195 ? 46.36091 31.76845 -7.50016  1.000 36.55945 ? 175 SER   A N   1 
ATOM   1338 C CA  . SER   A 1 195 ? 45.30513 30.88222 -7.95743  1.000 38.07424 ? 175 SER   A CA  1 
ATOM   1339 C C   . SER   A 1 195 ? 45.89919 29.70379 -8.70997  1.000 36.65896 ? 175 SER   A C   1 
ATOM   1340 O O   . SER   A 1 195 ? 47.02065 29.75978 -9.22478  1.000 37.48702 ? 175 SER   A O   1 
ATOM   1341 C CB  . SER   A 1 195 ? 44.33656 31.60524 -8.90406  1.000 41.53779 ? 175 SER   A CB  1 
ATOM   1342 O OG  . SER   A 1 195 ? 43.56938 32.57676 -8.21964  1.000 45.40566 ? 175 SER   A OG  1 
ATOM   1343 N N   . SER   A 1 196 ? 45.11750 28.63364 -8.77780  1.000 35.21111 ? 176 SER   A N   1 
ATOM   1344 C CA  . SER   A 1 196 ? 45.43699 27.52069 -9.65640  1.000 37.64336 ? 176 SER   A CA  1 
ATOM   1345 C C   . SER   A 1 196 ? 44.32560 27.41070 -10.68792 1.000 35.92652 ? 176 SER   A C   1 
ATOM   1346 O O   . SER   A 1 196 ? 43.56515 28.36323 -10.88067 1.000 35.33247 ? 176 SER   A O   1 
ATOM   1347 C CB  . SER   A 1 196 ? 45.58667 26.22736 -8.85842  1.000 42.31068 ? 176 SER   A CB  1 
ATOM   1348 O OG  . SER   A 1 196 ? 45.85261 25.12675 -9.71330  1.000 47.57480 ? 176 SER   A OG  1 
ATOM   1349 N N   . GLY   A 1 197 ? 44.21373 26.26880 -11.35404 1.000 34.93888 ? 177 GLY   A N   1 
ATOM   1350 C CA  . GLY   A 1 197 ? 43.18865 26.09309 -12.35147 1.000 32.82119 ? 177 GLY   A CA  1 
ATOM   1351 C C   . GLY   A 1 197 ? 41.80649 26.03926 -11.73365 1.000 30.56793 ? 177 GLY   A C   1 
ATOM   1352 O O   . GLY   A 1 197 ? 41.64552 25.92445 -10.51341 1.000 29.53229 ? 177 GLY   A O   1 
ATOM   1353 N N   A PRO   A 1 198 ? 40.77859 26.13034 -12.56636 0.500 29.66514 ? 178 PRO   A N   1 
ATOM   1354 N N   B PRO   A 1 198 ? 40.77859 26.13034 -12.56636 0.500 29.66514 ? 178 PRO   A N   1 
ATOM   1355 C CA  A PRO   A 1 198 ? 39.40813 26.01210 -12.06704 0.500 28.12082 ? 178 PRO   A CA  1 
ATOM   1356 C CA  B PRO   A 1 198 ? 39.40813 26.01210 -12.06704 0.500 28.12082 ? 178 PRO   A CA  1 
ATOM   1357 C C   A PRO   A 1 198 ? 39.05939 24.55246 -11.80799 0.500 26.19437 ? 178 PRO   A C   1 
ATOM   1358 C C   B PRO   A 1 198 ? 39.05939 24.55246 -11.80799 0.500 26.19437 ? 178 PRO   A C   1 
ATOM   1359 O O   A PRO   A 1 198 ? 39.78366 23.62889 -12.18062 0.500 27.93642 ? 178 PRO   A O   1 
ATOM   1360 O O   B PRO   A 1 198 ? 39.78366 23.62889 -12.18062 0.500 27.93642 ? 178 PRO   A O   1 
ATOM   1361 C CB  A PRO   A 1 198 ? 38.57757 26.55906 -13.23154 0.500 29.38886 ? 178 PRO   A CB  1 
ATOM   1362 C CB  B PRO   A 1 198 ? 38.57757 26.55906 -13.23154 0.500 29.38886 ? 178 PRO   A CB  1 
ATOM   1363 C CG  A PRO   A 1 198 ? 39.37717 26.18106 -14.44090 0.500 30.21512 ? 178 PRO   A CG  1 
ATOM   1364 C CG  B PRO   A 1 198 ? 39.37717 26.18106 -14.44090 0.500 30.21512 ? 178 PRO   A CG  1 
ATOM   1365 C CD  A PRO   A 1 198 ? 40.82151 26.34872 -14.02380 0.500 29.77459 ? 178 PRO   A CD  1 
ATOM   1366 C CD  B PRO   A 1 198 ? 40.82151 26.34872 -14.02380 0.500 29.77459 ? 178 PRO   A CD  1 
ATOM   1367 N N   . ILE   A 1 199 ? 37.92397 24.35595 -11.14198 1.000 24.28698 ? 179 ILE   A N   1 
ATOM   1368 C CA  . ILE   A 1 199 ? 37.33778 23.02538 -11.09347 1.000 22.57564 ? 179 ILE   A CA  1 
ATOM   1369 C C   . ILE   A 1 199 ? 36.94522 22.64960 -12.51758 1.000 22.93437 ? 179 ILE   A C   1 
ATOM   1370 O O   . ILE   A 1 199 ? 36.17973 23.36627 -13.17278 1.000 23.90090 ? 179 ILE   A O   1 
ATOM   1371 C CB  . ILE   A 1 199 ? 36.14929 23.00947 -10.13015 1.000 24.39313 ? 179 ILE   A CB  1 
ATOM   1372 C CG1 . ILE   A 1 199 ? 36.64841 23.15919 -8.68932  1.000 26.60597 ? 179 ILE   A CG1 1 
ATOM   1373 C CG2 . ILE   A 1 199 ? 35.32997 21.73852 -10.30797 1.000 26.57520 ? 179 ILE   A CG2 1 
ATOM   1374 C CD1 . ILE   A 1 199 ? 35.54396 23.35390 -7.67919  1.000 26.71882 ? 179 ILE   A CD1 1 
ATOM   1375 N N   . ASP   A 1 200 ? 37.49375 21.54558 -13.02200 1.000 22.05615 ? 180 ASP   A N   1 
ATOM   1376 C CA  . ASP   A 1 200 ? 37.29270 21.20356 -14.42770 1.000 21.98321 ? 180 ASP   A CA  1 
ATOM   1377 C C   . ASP   A 1 200 ? 35.85510 20.75432 -14.66062 1.000 22.09118 ? 180 ASP   A C   1 
ATOM   1378 O O   . ASP   A 1 200 ? 35.39046 19.79881 -14.03276 1.000 23.43006 ? 180 ASP   A O   1 
ATOM   1379 C CB  . ASP   A 1 200 ? 38.25908 20.11033 -14.85686 1.000 25.00709 ? 180 ASP   A CB  1 
ATOM   1380 C CG  . ASP   A 1 200 ? 38.06128 19.71875 -16.30579 1.000 29.78720 ? 180 ASP   A CG  1 
ATOM   1381 O OD1 . ASP   A 1 200 ? 38.46849 20.49458 -17.18426 1.000 33.90301 ? 180 ASP   A OD1 1 
ATOM   1382 O OD2 . ASP   A 1 200 ? 37.46845 18.65366 -16.56934 1.000 34.01268 ? 180 ASP   A OD2 1 
ATOM   1383 N N   . SER   A 1 201 ? 35.15542 21.43474 -15.57225 1.000 22.68741 ? 181 SER   A N   1 
ATOM   1384 C CA  A SER   A 1 201 ? 33.74753 21.12059 -15.78962 0.898 23.36835 ? 181 SER   A CA  1 
ATOM   1385 C CA  B SER   A 1 201 ? 33.74658 21.13410 -15.81363 0.102 21.92754 ? 181 SER   A CA  1 
ATOM   1386 C C   . SER   A 1 201 ? 33.55773 19.80497 -16.53414 1.000 21.20966 ? 181 SER   A C   1 
ATOM   1387 O O   . SER   A 1 201 ? 32.55430 19.12264 -16.31766 1.000 21.32881 ? 181 SER   A O   1 
ATOM   1388 C CB  A SER   A 1 201 ? 33.04701 22.25644 -16.53761 0.898 23.75810 ? 181 SER   A CB  1 
ATOM   1389 C CB  B SER   A 1 201 ? 33.10310 22.25282 -16.63313 0.102 21.40499 ? 181 SER   A CB  1 
ATOM   1390 O OG  A SER   A 1 201 ? 33.59592 22.42447 -17.83275 0.898 23.80644 ? 181 SER   A OG  1 
ATOM   1391 O OG  B SER   A 1 201 ? 33.25875 23.50849 -16.00046 0.102 20.80827 ? 181 SER   A OG  1 
ATOM   1392 N N   . SER   A 1 202 ? 34.49412 19.42928 -17.40415 1.000 21.18527 ? 182 SER   A N   1 
ATOM   1393 C CA  . SER   A 1 202 ? 34.30552 18.21290 -18.19103 1.000 23.17526 ? 182 SER   A CA  1 
ATOM   1394 C C   . SER   A 1 202 ? 34.29859 16.94664 -17.33744 1.000 23.95300 ? 182 SER   A C   1 
ATOM   1395 O O   . SER   A 1 202 ? 33.72336 15.93633 -17.75918 1.000 25.94858 ? 182 SER   A O   1 
ATOM   1396 C CB  . SER   A 1 202 ? 35.36372 18.10913 -19.28953 1.000 26.40099 ? 182 SER   A CB  1 
ATOM   1397 O OG  . SER   A 1 202 ? 36.62236 17.77134 -18.73654 1.000 28.82719 ? 182 SER   A OG  1 
ATOM   1398 N N   . VAL   A 1 203 ? 34.91735 16.96628 -16.15003 1.000 20.42029 ? 183 VAL   A N   1 
ATOM   1399 C CA  . VAL   A 1 203 ? 34.88654 15.79321 -15.27524 1.000 20.34122 ? 183 VAL   A CA  1 
ATOM   1400 C C   . VAL   A 1 203 ? 33.69337 15.79900 -14.33267 1.000 19.17929 ? 183 VAL   A C   1 
ATOM   1401 O O   . VAL   A 1 203 ? 33.55476 14.88656 -13.50309 1.000 19.31714 ? 183 VAL   A O   1 
ATOM   1402 C CB  . VAL   A 1 203 ? 36.20153 15.58943 -14.49280 1.000 21.95161 ? 183 VAL   A CB  1 
ATOM   1403 C CG1 . VAL   A 1 203 ? 37.39209 15.49770 -15.45285 1.000 23.93705 ? 183 VAL   A CG1 1 
ATOM   1404 C CG2 . VAL   A 1 203 ? 36.39813 16.70151 -13.44132 1.000 22.59573 ? 183 VAL   A CG2 1 
ATOM   1405 N N   . LEU   A 1 204 ? 32.82303 16.80428 -14.42012 1.000 18.42219 ? 184 LEU   A N   1 
ATOM   1406 C CA  . LEU   A 1 204 ? 31.67650 16.83205 -13.51067 1.000 18.27938 ? 184 LEU   A CA  1 
ATOM   1407 C C   . LEU   A 1 204 ? 30.67296 15.73677 -13.84451 1.000 18.75951 ? 184 LEU   A C   1 
ATOM   1408 O O   . LEU   A 1 204 ? 30.04752 15.16755 -12.94385 1.000 19.61147 ? 184 LEU   A O   1 
ATOM   1409 C CB  . LEU   A 1 204 ? 30.98256 18.18640 -13.57406 1.000 18.92652 ? 184 LEU   A CB  1 
ATOM   1410 C CG  . LEU   A 1 204 ? 31.76416 19.36202 -13.00021 1.000 19.09471 ? 184 LEU   A CG  1 
ATOM   1411 C CD1 . LEU   A 1 204 ? 31.01598 20.65402 -13.33250 1.000 20.12457 ? 184 LEU   A CD1 1 
ATOM   1412 C CD2 . LEU   A 1 204 ? 31.89094 19.18608 -11.50179 1.000 20.14513 ? 184 LEU   A CD2 1 
ATOM   1413 N N   . SER   A 1 205 ? 30.46822 15.46154 -15.12872 1.000 19.02217 ? 185 SER   A N   1 
ATOM   1414 C CA  . SER   A 1 205 ? 29.38990 14.57162 -15.52853 1.000 18.47120 ? 185 SER   A CA  1 
ATOM   1415 C C   . SER   A 1 205 ? 29.63475 14.08789 -16.94472 1.000 17.87236 ? 185 SER   A C   1 
ATOM   1416 O O   . SER   A 1 205 ? 30.14293 14.83513 -17.78296 1.000 19.17210 ? 185 SER   A O   1 
ATOM   1417 C CB  . SER   A 1 205 ? 28.04391 15.30198 -15.47958 1.000 19.18110 ? 185 SER   A CB  1 
ATOM   1418 O OG  . SER   A 1 205 ? 26.99090 14.44151 -15.88233 1.000 19.11419 ? 185 SER   A OG  1 
ATOM   1419 N N   . ARG   A 1 206 ? 29.25354 12.84114 -17.20749 1.000 19.86753 ? 186 ARG   A N   1 
ATOM   1420 C CA  . ARG   A 1 206 ? 29.23507 12.36020 -18.58186 1.000 20.07953 ? 186 ARG   A CA  1 
ATOM   1421 C C   . ARG   A 1 206 ? 28.08287 12.94932 -19.37354 1.000 21.17934 ? 186 ARG   A C   1 
ATOM   1422 O O   . ARG   A 1 206 ? 28.08634 12.85635 -20.60615 1.000 22.60677 ? 186 ARG   A O   1 
ATOM   1423 C CB  . ARG   A 1 206 ? 29.14741 10.83813 -18.60052 1.000 20.20270 ? 186 ARG   A CB  1 
ATOM   1424 C CG  . ARG   A 1 206 ? 30.40018 10.16939 -18.06952 1.000 20.90146 ? 186 ARG   A CG  1 
ATOM   1425 C CD  . ARG   A 1 206 ? 30.20754 8.65897  -17.95706 1.000 21.02086 ? 186 ARG   A CD  1 
ATOM   1426 N NE  . ARG   A 1 206 ? 29.09540 8.35393  -17.06391 1.000 20.51486 ? 186 ARG   A NE  1 
ATOM   1427 C CZ  . ARG   A 1 206 ? 28.58707 7.14251  -16.88645 1.000 21.32651 ? 186 ARG   A CZ  1 
ATOM   1428 N NH1 . ARG   A 1 206 ? 29.05256 6.08983  -17.54940 1.000 21.67892 ? 186 ARG   A NH1 1 
ATOM   1429 N NH2 . ARG   A 1 206 ? 27.58464 6.98168  -16.02758 1.000 21.72014 ? 186 ARG   A NH2 1 
ATOM   1430 N N   . ASN   A 1 207 ? 27.11165 13.54956 -18.69145 1.000 20.22709 ? 187 ASN   A N   1 
ATOM   1431 C CA  . ASN   A 1 207 ? 25.98122 14.19099 -19.34330 1.000 20.74836 ? 187 ASN   A CA  1 
ATOM   1432 C C   . ASN   A 1 207 ? 26.44649 15.55506 -19.84462 1.000 19.70991 ? 187 ASN   A C   1 
ATOM   1433 O O   . ASN   A 1 207 ? 26.63721 16.48758 -19.04992 1.000 20.63625 ? 187 ASN   A O   1 
ATOM   1434 C CB  . ASN   A 1 207 ? 24.83840 14.30170 -18.33758 1.000 21.44707 ? 187 ASN   A CB  1 
ATOM   1435 C CG  . ASN   A 1 207 ? 23.56224 14.83530 -18.95129 1.000 23.82992 ? 187 ASN   A CG  1 
ATOM   1436 O OD1 . ASN   A 1 207 ? 23.60272 15.64866 -19.86487 1.000 24.75146 ? 187 ASN   A OD1 1 
ATOM   1437 N ND2 . ASN   A 1 207 ? 22.41669 14.39580 -18.42841 1.000 23.88822 ? 187 ASN   A ND2 1 
ATOM   1438 N N   . LYS   A 1 208 ? 26.64839 15.66810 -21.16300 1.000 20.74886 ? 188 LYS   A N   1 
ATOM   1439 C CA  . LYS   A 1 208 ? 27.18526 16.91046 -21.71475 1.000 21.06541 ? 188 LYS   A CA  1 
ATOM   1440 C C   . LYS   A 1 208 ? 26.24934 18.08521 -21.49565 1.000 21.55863 ? 188 LYS   A C   1 
ATOM   1441 O O   . LYS   A 1 208 ? 26.71262 19.22552 -21.35210 1.000 21.29742 ? 188 LYS   A O   1 
ATOM   1442 C CB  . LYS   A 1 208 ? 27.46370 16.75092 -23.20281 1.000 23.05771 ? 188 LYS   A CB  1 
ATOM   1443 C CG  . LYS   A 1 208 ? 28.58600 15.79690 -23.51489 1.000 26.86754 ? 188 LYS   A CG  1 
ATOM   1444 C CD  . LYS   A 1 208 ? 28.74797 15.68131 -25.02469 1.000 31.11580 ? 188 LYS   A CD  1 
ATOM   1445 C CE  . LYS   A 1 208 ? 29.85350 14.72538 -25.40252 1.000 34.37099 ? 188 LYS   A CE  1 
ATOM   1446 N NZ  . LYS   A 1 208 ? 29.88098 14.50792 -26.87549 1.000 36.74141 ? 188 LYS   A NZ  1 
ATOM   1447 N N   . THR   A 1 209 ? 24.93675 17.84068 -21.48916 1.000 21.45922 ? 189 THR   A N   1 
ATOM   1448 C CA  . THR   A 1 209 ? 24.00011 18.93293 -21.25854 1.000 21.46004 ? 189 THR   A CA  1 
ATOM   1449 C C   . THR   A 1 209 ? 24.17147 19.50278 -19.85588 1.000 20.34112 ? 189 THR   A C   1 
ATOM   1450 O O   . THR   A 1 209 ? 24.11906 20.72163 -19.66527 1.000 20.89744 ? 189 THR   A O   1 
ATOM   1451 C CB  . THR   A 1 209 ? 22.57286 18.45256 -21.49650 1.000 24.96417 ? 189 THR   A CB  1 
ATOM   1452 O OG1 . THR   A 1 209 ? 22.47311 17.94663 -22.82803 1.000 30.13172 ? 189 THR   A OG1 1 
ATOM   1453 C CG2 . THR   A 1 209 ? 21.57708 19.59144 -21.33099 1.000 25.33564 ? 189 THR   A CG2 1 
ATOM   1454 N N   . GLU   A 1 210 ? 24.41135 18.64008 -18.86340 1.000 20.85475 ? 190 GLU   A N   1 
ATOM   1455 C CA  . GLU   A 1 210 ? 24.65529 19.12994 -17.50775 1.000 19.32662 ? 190 GLU   A CA  1 
ATOM   1456 C C   . GLU   A 1 210 ? 25.97435 19.88990 -17.41515 1.000 19.97916 ? 190 GLU   A C   1 
ATOM   1457 O O   . GLU   A 1 210 ? 26.07393 20.87383 -16.67197 1.000 20.13641 ? 190 GLU   A O   1 
ATOM   1458 C CB  . GLU   A 1 210 ? 24.58690 17.97766 -16.49875 1.000 19.34898 ? 190 GLU   A CB  1 
ATOM   1459 C CG  . GLU   A 1 210 ? 23.19289 17.41656 -16.33589 1.000 21.48961 ? 190 GLU   A CG  1 
ATOM   1460 C CD  . GLU   A 1 210 ? 22.23273 18.35644 -15.62268 1.000 26.10337 ? 190 GLU   A CD  1 
ATOM   1461 O OE1 . GLU   A 1 210 ? 22.66133 19.40876 -15.11110 1.000 24.77310 ? 190 GLU   A OE1 1 
ATOM   1462 O OE2 . GLU   A 1 210 ? 21.03045 18.02142 -15.55955 1.000 32.67433 ? 190 GLU   A OE2 1 
ATOM   1463 N N   . VAL   A 1 211 ? 26.99816 19.45887 -18.15589 1.000 19.42978 ? 191 VAL   A N   1 
ATOM   1464 C CA  . VAL   A 1 211 ? 28.23929 20.23114 -18.19456 1.000 19.80564 ? 191 VAL   A CA  1 
ATOM   1465 C C   . VAL   A 1 211 ? 27.97754 21.61423 -18.77963 1.000 19.90971 ? 191 VAL   A C   1 
ATOM   1466 O O   . VAL   A 1 211 ? 28.42326 22.63467 -18.23633 1.000 19.97927 ? 191 VAL   A O   1 
ATOM   1467 C CB  . VAL   A 1 211 ? 29.33537 19.46658 -18.96390 1.000 20.64495 ? 191 VAL   A CB  1 
ATOM   1468 C CG1 . VAL   A 1 211 ? 30.56526 20.34967 -19.12862 1.000 22.07360 ? 191 VAL   A CG1 1 
ATOM   1469 C CG2 . VAL   A 1 211 ? 29.69483 18.17227 -18.22356 1.000 21.89907 ? 191 VAL   A CG2 1 
ATOM   1470 N N   . ASP   A 1 212 ? 27.22836 21.66710 -19.88292 1.000 19.68283 ? 192 ASP   A N   1 
ATOM   1471 C CA  . ASP   A 1 212 ? 26.90090 22.94568 -20.51378 1.000 20.00587 ? 192 ASP   A CA  1 
ATOM   1472 C C   . ASP   A 1 212 ? 26.07012 23.83164 -19.59345 1.000 20.22462 ? 192 ASP   A C   1 
ATOM   1473 O O   . ASP   A 1 212 ? 26.26203 25.05437 -19.56111 1.000 20.86388 ? 192 ASP   A O   1 
ATOM   1474 C CB  . ASP   A 1 212 ? 26.15247 22.69626 -21.81854 1.000 21.10360 ? 192 ASP   A CB  1 
ATOM   1475 C CG  . ASP   A 1 212 ? 27.06014 22.21065 -22.91933 1.000 24.80424 ? 192 ASP   A CG  1 
ATOM   1476 O OD1 . ASP   A 1 212 ? 28.25949 22.54883 -22.87722 1.000 29.41953 ? 192 ASP   A OD1 1 
ATOM   1477 O OD2 . ASP   A 1 212 ? 26.57588 21.50286 -23.83196 1.000 25.22451 ? 192 ASP   A OD2 1 
ATOM   1478 N N   . ILE   A 1 213 ? 25.13969 23.23927 -18.83847 1.000 19.70470 ? 193 ILE   A N   1 
ATOM   1479 C CA  . ILE   A 1 213 ? 24.34047 24.01775 -17.89288 1.000 18.85619 ? 193 ILE   A CA  1 
ATOM   1480 C C   . ILE   A 1 213 ? 25.23073 24.61329 -16.81341 1.000 20.56518 ? 193 ILE   A C   1 
ATOM   1481 O O   . ILE   A 1 213 ? 25.11170 25.79400 -16.46823 1.000 21.95122 ? 193 ILE   A O   1 
ATOM   1482 C CB  . ILE   A 1 213 ? 23.21644 23.15410 -17.29470 1.000 20.30228 ? 193 ILE   A CB  1 
ATOM   1483 C CG1 . ILE   A 1 213 ? 22.12543 22.90041 -18.34387 1.000 20.45234 ? 193 ILE   A CG1 1 
ATOM   1484 C CG2 . ILE   A 1 213 ? 22.65890 23.79489 -16.01284 1.000 20.02065 ? 193 ILE   A CG2 1 
ATOM   1485 C CD1 . ILE   A 1 213 ? 21.15147 21.79226 -17.95591 1.000 22.54621 ? 193 ILE   A CD1 1 
ATOM   1486 N N   . TYR   A 1 214 ? 26.13527 23.79882 -16.26088 1.000 19.56975 ? 194 TYR   A N   1 
ATOM   1487 C CA  . TYR   A 1 214 ? 27.08803 24.29332 -15.27361 1.000 18.10408 ? 194 TYR   A CA  1 
ATOM   1488 C C   . TYR   A 1 214 ? 27.87314 25.47432 -15.82916 1.000 19.36613 ? 194 TYR   A C   1 
ATOM   1489 O O   . TYR   A 1 214 ? 28.06507 26.48816 -15.14432 1.000 21.08644 ? 194 TYR   A O   1 
ATOM   1490 C CB  . TYR   A 1 214 ? 28.03930 23.15468 -14.88348 1.000 18.24932 ? 194 TYR   A CB  1 
ATOM   1491 C CG  . TYR   A 1 214 ? 29.17047 23.57350 -13.96481 1.000 19.49623 ? 194 TYR   A CG  1 
ATOM   1492 C CD1 . TYR   A 1 214 ? 30.37863 24.04597 -14.48340 1.000 21.07900 ? 194 TYR   A CD1 1 
ATOM   1493 C CD2 . TYR   A 1 214 ? 29.03453 23.50028 -12.58387 1.000 21.02150 ? 194 TYR   A CD2 1 
ATOM   1494 C CE1 . TYR   A 1 214 ? 31.41090 24.43800 -13.65266 1.000 21.20874 ? 194 TYR   A CE1 1 
ATOM   1495 C CE2 . TYR   A 1 214 ? 30.06942 23.89229 -11.74343 1.000 21.85504 ? 194 TYR   A CE2 1 
ATOM   1496 C CZ  . TYR   A 1 214 ? 31.25094 24.36494 -12.28676 1.000 21.04871 ? 194 TYR   A CZ  1 
ATOM   1497 O OH  . TYR   A 1 214 ? 32.29066 24.74720 -11.47270 1.000 23.91216 ? 194 TYR   A OH  1 
ATOM   1498 N N   . ASN   A 1 215 ? 28.31337 25.37503 -17.08001 1.000 19.32753 ? 195 ASN   A N   1 
ATOM   1499 C CA  . ASN   A 1 215 ? 29.11275 26.44080 -17.67133 1.000 20.06259 ? 195 ASN   A CA  1 
ATOM   1500 C C   . ASN   A 1 215 ? 28.29254 27.65548 -18.08182 1.000 20.61339 ? 195 ASN   A C   1 
ATOM   1501 O O   . ASN   A 1 215 ? 28.88110 28.67540 -18.46035 1.000 21.98191 ? 195 ASN   A O   1 
ATOM   1502 C CB  . ASN   A 1 215 ? 29.90228 25.89276 -18.86312 1.000 20.71254 ? 195 ASN   A CB  1 
ATOM   1503 C CG  . ASN   A 1 215 ? 31.09482 25.05899 -18.42634 1.000 22.23792 ? 195 ASN   A CG  1 
ATOM   1504 O OD1 . ASN   A 1 215 ? 31.72403 25.34819 -17.40555 1.000 24.53682 ? 195 ASN   A OD1 1 
ATOM   1505 N ND2 . ASN   A 1 215 ? 31.41575 24.02570 -19.19752 1.000 23.58119 ? 195 ASN   A ND2 1 
ATOM   1506 N N   . SER   A 1 216 ? 26.95974 27.57816 -17.98866 1.000 19.85236 ? 196 SER   A N   1 
ATOM   1507 C CA  . SER   A 1 216 ? 26.06829 28.65981 -18.38740 1.000 21.55819 ? 196 SER   A CA  1 
ATOM   1508 C C   . SER   A 1 216 ? 25.45702 29.40752 -17.21792 1.000 20.99308 ? 196 SER   A C   1 
ATOM   1509 O O   . SER   A 1 216 ? 24.87749 30.47985 -17.42943 1.000 23.56684 ? 196 SER   A O   1 
ATOM   1510 C CB  . SER   A 1 216 ? 24.91034 28.10688 -19.23219 1.000 21.76159 ? 196 SER   A CB  1 
ATOM   1511 O OG  . SER   A 1 216 ? 25.39092 27.51465 -20.41137 1.000 21.81063 ? 196 SER   A OG  1 
ATOM   1512 N N   . ASP   A 1 217 ? 25.55301 28.87705 -16.01016 1.000 19.78958 ? 197 ASP   A N   1 
ATOM   1513 C CA  . ASP   A 1 217 ? 24.83803 29.40309 -14.85556 1.000 20.76572 ? 197 ASP   A CA  1 
ATOM   1514 C C   . ASP   A 1 217 ? 25.60234 30.59232 -14.28405 1.000 21.41135 ? 197 ASP   A C   1 
ATOM   1515 O O   . ASP   A 1 217 ? 26.70438 30.42639 -13.74942 1.000 23.52919 ? 197 ASP   A O   1 
ATOM   1516 C CB  . ASP   A 1 217 ? 24.69472 28.28066 -13.81734 1.000 21.72705 ? 197 ASP   A CB  1 
ATOM   1517 C CG  . ASP   A 1 217 ? 23.86552 28.67921 -12.60832 1.000 22.98282 ? 197 ASP   A CG  1 
ATOM   1518 O OD1 . ASP   A 1 217 ? 23.59636 29.88857 -12.40094 1.000 24.32436 ? 197 ASP   A OD1 1 
ATOM   1519 O OD2 . ASP   A 1 217 ? 23.49217 27.75735 -11.85045 1.000 22.52927 ? 197 ASP   A OD2 1 
ATOM   1520 N N   . PRO   A 1 218 ? 25.04608 31.80481 -14.35636 1.000 22.81996 ? 198 PRO   A N   1 
ATOM   1521 C CA  . PRO   A 1 218 ? 25.77837 32.97700 -13.84885 1.000 23.44755 ? 198 PRO   A CA  1 
ATOM   1522 C C   . PRO   A 1 218 ? 25.94647 32.99654 -12.33329 1.000 24.29143 ? 198 PRO   A C   1 
ATOM   1523 O O   . PRO   A 1 218 ? 26.73353 33.81320 -11.83481 1.000 26.90467 ? 198 PRO   A O   1 
ATOM   1524 C CB  . PRO   A 1 218 ? 24.96171 34.17302 -14.37296 1.000 25.34569 ? 198 PRO   A CB  1 
ATOM   1525 C CG  . PRO   A 1 218 ? 23.58220 33.62711 -14.59553 1.000 26.93076 ? 198 PRO   A CG  1 
ATOM   1526 C CD  . PRO   A 1 218 ? 23.71420 32.14485 -14.88556 1.000 24.77258 ? 198 PRO   A CD  1 
ATOM   1527 N N   . LEU   A 1 219 ? 25.26686 32.12318 -11.58777 1.000 22.49793 ? 199 LEU   A N   1 
ATOM   1528 C CA  . LEU   A 1 219 ? 25.46520 32.02515 -10.14570 1.000 21.30533 ? 199 LEU   A CA  1 
ATOM   1529 C C   . LEU   A 1 219 ? 26.56151 31.04348 -9.77151  1.000 23.92703 ? 199 LEU   A C   1 
ATOM   1530 O O   . LEU   A 1 219 ? 26.82480 30.85582 -8.57963  1.000 25.47003 ? 199 LEU   A O   1 
ATOM   1531 C CB  . LEU   A 1 219 ? 24.16040 31.64148 -9.43571  1.000 21.74705 ? 199 LEU   A CB  1 
ATOM   1532 C CG  . LEU   A 1 219 ? 23.06022 32.70259 -9.45443  1.000 24.13319 ? 199 LEU   A CG  1 
ATOM   1533 C CD1 . LEU   A 1 219 ? 21.82647 32.19949 -8.72143  1.000 24.56946 ? 199 LEU   A CD1 1 
ATOM   1534 C CD2 . LEU   A 1 219 ? 23.57192 33.99330 -8.81980  1.000 25.82681 ? 199 LEU   A CD2 1 
ATOM   1535 N N   . ILE   A 1 220 ? 27.20377 30.41383 -10.75307 1.000 23.13994 ? 200 ILE   A N   1 
ATOM   1536 C CA  . ILE   A 1 220 ? 28.31014 29.49719 -10.50586 1.000 22.01844 ? 200 ILE   A CA  1 
ATOM   1537 C C   . ILE   A 1 220 ? 29.60873 30.24908 -10.74019 1.000 22.80316 ? 200 ILE   A C   1 
ATOM   1538 O O   . ILE   A 1 220 ? 29.77033 30.93381 -11.76078 1.000 24.63337 ? 200 ILE   A O   1 
ATOM   1539 C CB  . ILE   A 1 220 ? 28.22396 28.24819 -11.39608 1.000 20.63864 ? 200 ILE   A CB  1 
ATOM   1540 C CG1 . ILE   A 1 220 ? 26.98177 27.42904 -11.04823 1.000 19.67518 ? 200 ILE   A CG1 1 
ATOM   1541 C CG2 . ILE   A 1 220 ? 29.44641 27.37520 -11.20193 1.000 21.54291 ? 200 ILE   A CG2 1 
ATOM   1542 C CD1 . ILE   A 1 220 ? 26.79607 26.19544 -11.90802 1.000 21.65171 ? 200 ILE   A CD1 1 
ATOM   1543 N N   . CYS   A 1 221 ? 30.52442 30.14409 -9.78916  1.000 23.25683 ? 201 CYS   A N   1 
ATOM   1544 C CA  . CYS   A 1 221 ? 31.85076 30.71332 -9.94243  1.000 24.87795 ? 201 CYS   A CA  1 
ATOM   1545 C C   . CYS   A 1 221 ? 32.74620 29.65927 -10.57283 1.000 25.32710 ? 201 CYS   A C   1 
ATOM   1546 O O   . CYS   A 1 221 ? 32.94182 28.57912 -9.99712  1.000 27.26921 ? 201 CYS   A O   1 
ATOM   1547 C CB  . CYS   A 1 221 ? 32.41885 31.13030 -8.59075  1.000 28.32332 ? 201 CYS   A CB  1 
ATOM   1548 S SG  . CYS   A 1 221 ? 34.04875 31.88212 -8.76440  0.946 29.98486 ? 201 CYS   A SG  1 
ATOM   1549 N N   . ARG   A 1 222 ? 33.28126 29.96774 -11.75508 1.000 25.01307 ? 202 ARG   A N   1 
ATOM   1550 C CA  . ARG   A 1 222 ? 34.12299 29.03543 -12.49447 1.000 27.01329 ? 202 ARG   A CA  1 
ATOM   1551 C C   . ARG   A 1 222 ? 35.54587 29.55228 -12.66064 1.000 27.39398 ? 202 ARG   A C   1 
ATOM   1552 O O   . ARG   A 1 222 ? 36.27680 29.08778 -13.53978 1.000 29.28543 ? 202 ARG   A O   1 
ATOM   1553 C CB  . ARG   A 1 222 ? 33.49265 28.69500 -13.84561 1.000 27.11701 ? 202 ARG   A CB  1 
ATOM   1554 C CG  . ARG   A 1 222 ? 32.17359 27.95120 -13.72472 1.000 26.01984 ? 202 ARG   A CG  1 
ATOM   1555 C CD  . ARG   A 1 222 ? 31.54054 27.71243 -15.08775 1.000 27.55448 ? 202 ARG   A CD  1 
ATOM   1556 N NE  . ARG   A 1 222 ? 31.24694 28.99259 -15.71379 1.000 28.58137 ? 202 ARG   A NE  1 
ATOM   1557 C CZ  . ARG   A 1 222 ? 30.10152 29.64528 -15.57728 1.000 32.61015 ? 202 ARG   A CZ  1 
ATOM   1558 N NH1 . ARG   A 1 222 ? 29.06346 29.10208 -14.95976 1.000 31.70625 ? 202 ARG   A NH1 1 
ATOM   1559 N NH2 . ARG   A 1 222 ? 29.99968 30.88256 -16.05635 1.000 35.42288 ? 202 ARG   A NH2 1 
ATOM   1560 N N   . ALA   A 1 223 ? 35.95541 30.50233 -11.83036 1.000 27.56216 ? 203 ALA   A N   1 
ATOM   1561 C CA  . ALA   A 1 223 ? 37.30568 31.02564 -11.91328 1.000 29.13022 ? 203 ALA   A CA  1 
ATOM   1562 C C   . ALA   A 1 223 ? 38.30122 29.99049 -11.40306 1.000 28.18295 ? 203 ALA   A C   1 
ATOM   1563 O O   . ALA   A 1 223 ? 37.93843 28.98113 -10.78715 1.000 28.46994 ? 203 ALA   A O   1 
ATOM   1564 C CB  . ALA   A 1 223 ? 37.42510 32.29838 -11.07795 1.000 30.85140 ? 203 ALA   A CB  1 
ATOM   1565 N N   . GLY   A 1 224 ? 39.57861 30.24661 -11.67207 1.000 27.15668 ? 204 GLY   A N   1 
ATOM   1566 C CA  . GLY   A 1 224 ? 40.61689 29.43396 -11.06481 1.000 28.11861 ? 204 GLY   A CA  1 
ATOM   1567 C C   . GLY   A 1 224 ? 40.49003 29.44200 -9.55126  1.000 28.69631 ? 204 GLY   A C   1 
ATOM   1568 O O   . GLY   A 1 224 ? 40.13594 30.45520 -8.94175  1.000 30.96207 ? 204 GLY   A O   1 
ATOM   1569 N N   . LEU   A 1 225 ? 40.75762 28.29188 -8.94108  1.000 27.36908 ? 205 LEU   A N   1 
ATOM   1570 C CA  . LEU   A 1 225 ? 40.63177 28.18004 -7.49694  1.000 27.42724 ? 205 LEU   A CA  1 
ATOM   1571 C C   . LEU   A 1 225 ? 41.73560 28.97532 -6.81654  1.000 27.53663 ? 205 LEU   A C   1 
ATOM   1572 O O   . LEU   A 1 225 ? 42.91674 28.79999 -7.12266  1.000 29.45973 ? 205 LEU   A O   1 
ATOM   1573 C CB  . LEU   A 1 225 ? 40.74517 26.71757 -7.08712  1.000 31.03025 ? 205 LEU   A CB  1 
ATOM   1574 C CG  . LEU   A 1 225 ? 39.65128 26.19746 -6.17439  1.000 36.36977 ? 205 LEU   A CG  1 
ATOM   1575 C CD1 . LEU   A 1 225 ? 38.31842 26.41678 -6.85561  1.000 38.74900 ? 205 LEU   A CD1 1 
ATOM   1576 C CD2 . LEU   A 1 225 ? 39.87719 24.72587 -5.89680  1.000 36.75358 ? 205 LEU   A CD2 1 
ATOM   1577 N N   . LYS   A 1 226 ? 41.35234 29.85275 -5.89454  1.000 26.82487 ? 206 LYS   A N   1 
ATOM   1578 C CA  . LYS   A 1 226 ? 42.34910 30.51592 -5.07073  1.000 27.95702 ? 206 LYS   A CA  1 
ATOM   1579 C C   . LYS   A 1 226 ? 43.05920 29.46808 -4.22509  1.000 26.83977 ? 206 LYS   A C   1 
ATOM   1580 O O   . LYS   A 1 226 ? 42.42802 28.55507 -3.68307  1.000 24.93122 ? 206 LYS   A O   1 
ATOM   1581 C CB  . LYS   A 1 226 ? 41.67289 31.52726 -4.14430  1.000 32.34779 ? 206 LYS   A CB  1 
ATOM   1582 C CG  . LYS   A 1 226 ? 41.01092 32.71156 -4.83966  1.000 37.82927 ? 206 LYS   A CG  1 
ATOM   1583 C CD  . LYS   A 1 226 ? 42.02798 33.68379 -5.39878  1.000 43.19554 ? 206 LYS   A CD  1 
ATOM   1584 C CE  . LYS   A 1 226 ? 41.34611 34.97043 -5.86795  1.000 46.58678 ? 206 LYS   A CE  1 
ATOM   1585 N NZ  . LYS   A 1 226 ? 40.04807 34.69277 -6.55103  1.000 50.45853 ? 206 LYS   A NZ  1 
ATOM   1586 N N   . VAL   A 1 227 ? 44.38143 29.59755 -4.11200  1.000 27.05777 ? 207 VAL   A N   1 
ATOM   1587 C CA  . VAL   A 1 227 ? 45.13984 28.64359 -3.30980  1.000 26.72731 ? 207 VAL   A CA  1 
ATOM   1588 C C   . VAL   A 1 227 ? 44.65346 28.64106 -1.86391  1.000 26.54782 ? 207 VAL   A C   1 
ATOM   1589 O O   . VAL   A 1 227 ? 44.57506 27.58441 -1.22473  1.000 26.31330 ? 207 VAL   A O   1 
ATOM   1590 C CB  . VAL   A 1 227 ? 46.65563 28.89548 -3.43201  1.000 27.90644 ? 207 VAL   A CB  1 
ATOM   1591 C CG1 . VAL   A 1 227 ? 47.41578 27.91171 -2.56963  1.000 27.93147 ? 207 VAL   A CG1 1 
ATOM   1592 C CG2 . VAL   A 1 227 ? 47.09300 28.75268 -4.88214  1.000 28.87446 ? 207 VAL   A CG2 1 
ATOM   1593 N N   . CYS   A 1 228 ? 44.29401 29.81155 -1.32774  1.000 26.36838 ? 208 CYS   A N   1 
ATOM   1594 C CA  A CYS   A 1 228 ? 43.77900 29.86722 0.03920   0.429 27.57181 ? 208 CYS   A CA  1 
ATOM   1595 C CA  B CYS   A 1 228 ? 43.79536 29.83404 0.04222   0.571 27.87963 ? 208 CYS   A CA  1 
ATOM   1596 C C   . CYS   A 1 228 ? 42.49814 29.05082 0.18488   1.000 27.00666 ? 208 CYS   A C   1 
ATOM   1597 O O   . CYS   A 1 228 ? 42.27579 28.41004 1.21887   1.000 28.18817 ? 208 CYS   A O   1 
ATOM   1598 C CB  A CYS   A 1 228 ? 43.55857 31.31908 0.47632   0.429 30.41037 ? 208 CYS   A CB  1 
ATOM   1599 C CB  B CYS   A 1 228 ? 43.65930 31.26553 0.54982   0.571 30.34326 ? 208 CYS   A CB  1 
ATOM   1600 S SG  A CYS   A 1 228 ? 42.17443 32.18110 -0.33171  0.429 33.70186 ? 208 CYS   A SG  1 
ATOM   1601 S SG  B CYS   A 1 228 ? 45.26420 32.01372 0.81982   0.571 33.47025 ? 208 CYS   A SG  1 
ATOM   1602 N N   . PHE   A 1 229 ? 41.64381 29.06180 -0.84331  1.000 24.26420 ? 209 PHE   A N   1 
ATOM   1603 C CA  . PHE   A 1 229 ? 40.41743 28.27651 -0.78090  1.000 23.35489 ? 209 PHE   A CA  1 
ATOM   1604 C C   . PHE   A 1 229 ? 40.71965 26.79061 -0.90970  1.000 23.73280 ? 209 PHE   A C   1 
ATOM   1605 O O   . PHE   A 1 229 ? 40.14845 25.97223 -0.18090  1.000 24.16978 ? 209 PHE   A O   1 
ATOM   1606 C CB  . PHE   A 1 229 ? 39.43358 28.72168 -1.86353  1.000 24.11148 ? 209 PHE   A CB  1 
ATOM   1607 C CG  . PHE   A 1 229 ? 38.06551 28.12245 -1.71397  1.000 24.67733 ? 209 PHE   A CG  1 
ATOM   1608 C CD1 . PHE   A 1 229 ? 37.17931 28.61853 -0.76949  1.000 25.96793 ? 209 PHE   A CD1 1 
ATOM   1609 C CD2 . PHE   A 1 229 ? 37.66665 27.06375 -2.51277  1.000 25.81318 ? 209 PHE   A CD2 1 
ATOM   1610 C CE1 . PHE   A 1 229 ? 35.91904 28.06003 -0.61717  1.000 28.85414 ? 209 PHE   A CE1 1 
ATOM   1611 C CE2 . PHE   A 1 229 ? 36.40117 26.50822 -2.37103  1.000 27.55108 ? 209 PHE   A CE2 1 
ATOM   1612 C CZ  . PHE   A 1 229 ? 35.52849 27.00881 -1.41836  1.000 28.26799 ? 209 PHE   A CZ  1 
ATOM   1613 N N   . GLY   A 1 230 ? 41.62430 26.42626 -1.82080  1.000 22.90226 ? 210 GLY   A N   1 
ATOM   1614 C CA  . GLY   A 1 230 ? 42.04833 25.03898 -1.90627  1.000 22.70109 ? 210 GLY   A CA  1 
ATOM   1615 C C   . GLY   A 1 230 ? 42.64960 24.54016 -0.60605  1.000 21.68838 ? 210 GLY   A C   1 
ATOM   1616 O O   . GLY   A 1 230 ? 42.46375 23.37849 -0.23133  1.000 22.96731 ? 210 GLY   A O   1 
ATOM   1617 N N   . ILE   A 1 231 ? 43.36736 25.41432 0.10661   1.000 23.67431 ? 211 ILE   A N   1 
ATOM   1618 C CA  . ILE   A 1 231 ? 43.89416 25.05656 1.42265   1.000 24.34880 ? 211 ILE   A CA  1 
ATOM   1619 C C   . ILE   A 1 231 ? 42.75778 24.71922 2.37819   1.000 23.87883 ? 211 ILE   A C   1 
ATOM   1620 O O   . ILE   A 1 231 ? 42.83518 23.74644 3.14162   1.000 24.36877 ? 211 ILE   A O   1 
ATOM   1621 C CB  . ILE   A 1 231 ? 44.80264 26.17979 1.96031   1.000 25.49651 ? 211 ILE   A CB  1 
ATOM   1622 C CG1 . ILE   A 1 231 ? 46.14905 26.17666 1.22882   1.000 28.03956 ? 211 ILE   A CG1 1 
ATOM   1623 C CG2 . ILE   A 1 231 ? 45.02558 26.04368 3.46880   1.000 27.12514 ? 211 ILE   A CG2 1 
ATOM   1624 C CD1 . ILE   A 1 231 ? 47.02804 27.37285 1.56381   1.000 30.43617 ? 211 ILE   A CD1 1 
ATOM   1625 N N   . GLN   A 1 232 ? 41.67439 25.50107 2.33965   1.000 23.36056 ? 212 GLN   A N   1 
ATOM   1626 C CA  . GLN   A 1 232 ? 40.52279 25.18481 3.17955   1.000 21.53221 ? 212 GLN   A CA  1 
ATOM   1627 C C   . GLN   A 1 232 ? 39.86027 23.87032 2.76988   1.000 20.82146 ? 212 GLN   A C   1 
ATOM   1628 O O   . GLN   A 1 232 ? 39.35086 23.14556 3.63235   1.000 21.28018 ? 212 GLN   A O   1 
ATOM   1629 C CB  . GLN   A 1 232 ? 39.53160 26.34683 3.18603   1.000 21.62946 ? 212 GLN   A CB  1 
ATOM   1630 C CG  . GLN   A 1 232 ? 40.11632 27.61831 3.81426   1.000 22.86181 ? 212 GLN   A CG  1 
ATOM   1631 C CD  . GLN   A 1 232 ? 40.51301 27.42415 5.28038   1.000 25.64110 ? 212 GLN   A CD  1 
ATOM   1632 O OE1 . GLN   A 1 232 ? 39.93774 26.59342 5.99266   1.000 26.41780 ? 212 GLN   A OE1 1 
ATOM   1633 N NE2 . GLN   A 1 232 ? 41.48425 28.20326 5.73847   1.000 27.80264 ? 212 GLN   A NE2 1 
ATOM   1634 N N   . LEU   A 1 233 ? 39.85163 23.54701 1.47274   1.000 22.09202 ? 213 LEU   A N   1 
ATOM   1635 C CA  . LEU   A 1 233 ? 39.38116 22.22488 1.05644   1.000 20.15217 ? 213 LEU   A CA  1 
ATOM   1636 C C   . LEU   A 1 233 ? 40.26836 21.12009 1.61984   1.000 21.54330 ? 213 LEU   A C   1 
ATOM   1637 O O   . LEU   A 1 233 ? 39.77185 20.06810 2.03343   1.000 21.28285 ? 213 LEU   A O   1 
ATOM   1638 C CB  . LEU   A 1 233 ? 39.30477 22.13088 -0.46894  1.000 20.15590 ? 213 LEU   A CB  1 
ATOM   1639 C CG  . LEU   A 1 233 ? 38.26415 23.04541 -1.13661  1.000 19.48316 ? 213 LEU   A CG  1 
ATOM   1640 C CD1 . LEU   A 1 233 ? 38.30831 22.93737 -2.66131  1.000 19.12247 ? 213 LEU   A CD1 1 
ATOM   1641 C CD2 . LEU   A 1 233 ? 36.85309 22.77581 -0.61044  1.000 22.17471 ? 213 LEU   A CD2 1 
ATOM   1642 N N   . LEU   A 1 234 ? 41.58431 21.33721 1.64097   1.000 21.53899 ? 214 LEU   A N   1 
ATOM   1643 C CA  . LEU   A 1 234 ? 42.47574 20.37071 2.27262   1.000 22.29009 ? 214 LEU   A CA  1 
ATOM   1644 C C   . LEU   A 1 234 ? 42.25898 20.32066 3.78112   1.000 22.53291 ? 214 LEU   A C   1 
ATOM   1645 O O   . LEU   A 1 234 ? 42.34353 19.24443 4.39230   1.000 23.06117 ? 214 LEU   A O   1 
ATOM   1646 C CB  . LEU   A 1 234 ? 43.92776 20.69947 1.93129   1.000 26.02771 ? 214 LEU   A CB  1 
ATOM   1647 C CG  . LEU   A 1 234 ? 44.30648 20.60729 0.45610   1.000 28.33347 ? 214 LEU   A CG  1 
ATOM   1648 C CD1 . LEU   A 1 234 ? 45.74096 21.07123 0.24672   1.000 30.39989 ? 214 LEU   A CD1 1 
ATOM   1649 C CD2 . LEU   A 1 234 ? 44.11516 19.19482 -0.06211  1.000 28.40357 ? 214 LEU   A CD2 1 
ATOM   1650 N N   . ASN   A 1 235 ? 41.98343 21.47252 4.40117   1.000 22.72780 ? 215 ASN   A N   1 
ATOM   1651 C CA  . ASN   A 1 235 ? 41.59063 21.47404 5.80728   1.000 23.16658 ? 215 ASN   A CA  1 
ATOM   1652 C C   . ASN   A 1 235 ? 40.34488 20.62845 6.02086   1.000 23.40472 ? 215 ASN   A C   1 
ATOM   1653 O O   . ASN   A 1 235 ? 40.25199 19.88392 7.00497   1.000 24.30870 ? 215 ASN   A O   1 
ATOM   1654 C CB  . ASN   A 1 235 ? 41.34090 22.90271 6.29725   1.000 24.22996 ? 215 ASN   A CB  1 
ATOM   1655 C CG  . ASN   A 1 235 ? 42.62045 23.68252 6.49785   1.000 27.05732 ? 215 ASN   A CG  1 
ATOM   1656 O OD1 . ASN   A 1 235 ? 43.71158 23.10889 6.53399   1.000 28.65592 ? 215 ASN   A OD1 1 
ATOM   1657 N ND2 . ASN   A 1 235 ? 42.49612 24.99909 6.64009   1.000 27.95222 ? 215 ASN   A ND2 1 
ATOM   1658 N N   . ALA   A 1 236 ? 39.37320 20.74299 5.11151   1.000 22.78373 ? 216 ALA   A N   1 
ATOM   1659 C CA  . ALA   A 1 236 ? 38.16476 19.93341 5.20055   1.000 21.49574 ? 216 ALA   A CA  1 
ATOM   1660 C C   . ALA   A 1 236 ? 38.49638 18.44200 5.18058   1.000 21.50373 ? 216 ALA   A C   1 
ATOM   1661 O O   . ALA   A 1 236 ? 37.96334 17.67144 5.98761   1.000 22.68322 ? 216 ALA   A O   1 
ATOM   1662 C CB  . ALA   A 1 236 ? 37.20097 20.31085 4.07407   1.000 21.58981 ? 216 ALA   A CB  1 
ATOM   1663 N N   . VAL   A 1 237 ? 39.39488 18.02168 4.28086   1.000 21.95668 ? 217 VAL   A N   1 
ATOM   1664 C CA  . VAL   A 1 237 ? 39.78194 16.61267 4.20807   1.000 21.64158 ? 217 VAL   A CA  1 
ATOM   1665 C C   . VAL   A 1 237 ? 40.40273 16.16268 5.52523   1.000 23.09321 ? 217 VAL   A C   1 
ATOM   1666 O O   . VAL   A 1 237 ? 40.07346 15.09190 6.06026   1.000 23.31715 ? 217 VAL   A O   1 
ATOM   1667 C CB  . VAL   A 1 237 ? 40.72761 16.37773 3.01387   1.000 21.24129 ? 217 VAL   A CB  1 
ATOM   1668 C CG1 . VAL   A 1 237 ? 41.35397 14.98062 3.07825   1.000 22.39046 ? 217 VAL   A CG1 1 
ATOM   1669 C CG2 . VAL   A 1 237 ? 39.98781 16.58686 1.69694   1.000 22.30433 ? 217 VAL   A CG2 1 
ATOM   1670 N N   . SER   A 1 238 ? 41.30122 16.98524 6.07813   1.000 23.55279 ? 218 SER   A N   1 
ATOM   1671 C CA  A SER   A 1 238 ? 41.95662 16.62617 7.33185   0.424 25.45874 ? 218 SER   A CA  1 
ATOM   1672 C CA  B SER   A 1 238 ? 41.95715 16.62910 7.33234   0.576 25.57797 ? 218 SER   A CA  1 
ATOM   1673 C C   . SER   A 1 238 ? 40.95140 16.53081 8.47261   1.000 25.51027 ? 218 SER   A C   1 
ATOM   1674 O O   . SER   A 1 238 ? 41.01968 15.61003 9.29608   1.000 25.75234 ? 218 SER   A O   1 
ATOM   1675 C CB  A SER   A 1 238 ? 43.04678 17.64552 7.66244   0.424 27.28213 ? 218 SER   A CB  1 
ATOM   1676 C CB  B SER   A 1 238 ? 43.03540 17.66099 7.66066   0.576 27.60744 ? 218 SER   A CB  1 
ATOM   1677 O OG  A SER   A 1 238 ? 44.07224 17.63205 6.68454   0.424 29.48663 ? 218 SER   A OG  1 
ATOM   1678 O OG  B SER   A 1 238 ? 43.67990 17.35109 8.88075   0.576 30.00789 ? 218 SER   A OG  1 
ATOM   1679 N N   . ARG   A 1 239 ? 40.00921 17.47197 8.53695   1.000 23.37258 ? 219 ARG   A N   1 
ATOM   1680 C CA  . ARG   A 1 239 ? 39.03140 17.45788 9.61657   1.000 22.64644 ? 219 ARG   A CA  1 
ATOM   1681 C C   . ARG   A 1 239 ? 38.03913 16.31955 9.46113   1.000 22.46043 ? 219 ARG   A C   1 
ATOM   1682 O O   . ARG   A 1 239 ? 37.61558 15.73461 10.46553  1.000 21.89274 ? 219 ARG   A O   1 
ATOM   1683 C CB  . ARG   A 1 239 ? 38.32885 18.80558 9.69972   1.000 25.16916 ? 219 ARG   A CB  1 
ATOM   1684 C CG  . ARG   A 1 239 ? 39.29581 19.90472 10.10164  1.000 27.43718 ? 219 ARG   A CG  1 
ATOM   1685 C CD  . ARG   A 1 239 ? 38.70109 21.27384 9.94368   1.000 29.37471 ? 219 ARG   A CD  1 
ATOM   1686 N NE  . ARG   A 1 239 ? 39.72807 22.30037 10.06838  1.000 32.59582 ? 219 ARG   A NE  1 
ATOM   1687 C CZ  . ARG   A 1 239 ? 39.48212 23.60192 10.06014  1.000 34.25772 ? 219 ARG   A CZ  1 
ATOM   1688 N NH1 . ARG   A 1 239 ? 38.24672 24.07012 9.97417   1.000 34.92695 ? 219 ARG   A NH1 1 
ATOM   1689 N NH2 . ARG   A 1 239 ? 40.50019 24.45436 10.14102  1.000 34.45585 ? 219 ARG   A NH2 1 
ATOM   1690 N N   . VAL   A 1 240 ? 37.66630 15.98285 8.22272   1.000 22.60727 ? 220 VAL   A N   1 
ATOM   1691 C CA  . VAL   A 1 240 ? 36.80425 14.82170 8.00905   1.000 21.06895 ? 220 VAL   A CA  1 
ATOM   1692 C C   . VAL   A 1 240 ? 37.47766 13.55745 8.52694   1.000 22.46053 ? 220 VAL   A C   1 
ATOM   1693 O O   . VAL   A 1 240 ? 36.84719 12.73825 9.20372   1.000 22.66043 ? 220 VAL   A O   1 
ATOM   1694 C CB  . VAL   A 1 240 ? 36.38015 14.70821 6.53065   1.000 20.54055 ? 220 VAL   A CB  1 
ATOM   1695 C CG1 . VAL   A 1 240 ? 35.77638 13.32869 6.24228   1.000 22.81957 ? 220 VAL   A CG1 1 
ATOM   1696 C CG2 . VAL   A 1 240 ? 35.36619 15.80352 6.18710   1.000 21.85072 ? 220 VAL   A CG2 1 
ATOM   1697 N N   . GLU   A 1 241 ? 38.77533 13.39681 8.25331   1.000 23.74049 ? 221 GLU   A N   1 
ATOM   1698 C CA  . GLU   A 1 241 ? 39.48228 12.21417 8.73583   1.000 27.46455 ? 221 GLU   A CA  1 
ATOM   1699 C C   . GLU   A 1 241 ? 39.42160 12.12292 10.25273  1.000 26.98233 ? 221 GLU   A C   1 
ATOM   1700 O O   . GLU   A 1 241 ? 39.18645 11.04465 10.81148  1.000 27.99404 ? 221 GLU   A O   1 
ATOM   1701 C CB  . GLU   A 1 241 ? 40.93600 12.22221 8.26881   1.000 32.54015 ? 221 GLU   A CB  1 
ATOM   1702 C CG  . GLU   A 1 241 ? 41.67916 10.95290 8.66954   1.000 39.57277 ? 221 GLU   A CG  1 
ATOM   1703 C CD  . GLU   A 1 241 ? 43.13576 11.19594 8.98066   1.000 48.28809 ? 221 GLU   A CD  1 
ATOM   1704 O OE1 . GLU   A 1 241 ? 43.76580 12.01357 8.27760   1.000 50.75975 ? 221 GLU   A OE1 1 
ATOM   1705 O OE2 . GLU   A 1 241 ? 43.65135 10.56826 9.93564   1.000 53.48807 ? 221 GLU   A OE2 1 
ATOM   1706 N N   . ARG   A 1 242 ? 39.64364 13.24849 10.93978  1.000 26.84564 ? 222 ARG   A N   1 
ATOM   1707 C CA  . ARG   A 1 242 ? 39.59350 13.23721 12.39609  1.000 28.07904 ? 222 ARG   A CA  1 
ATOM   1708 C C   . ARG   A 1 242 ? 38.17726 13.04271 12.91595  1.000 27.66249 ? 222 ARG   A C   1 
ATOM   1709 O O   . ARG   A 1 242 ? 37.99982 12.55601 14.03836  1.000 30.83797 ? 222 ARG   A O   1 
ATOM   1710 C CB  . ARG   A 1 242 ? 40.20911 14.52096 12.96549  1.000 33.70311 ? 222 ARG   A CB  1 
ATOM   1711 C CG  . ARG   A 1 242 ? 41.72864 14.47769 13.05544  1.000 41.61501 ? 222 ARG   A CG  1 
ATOM   1712 C CD  . ARG   A 1 242 ? 42.28113 15.67567 13.81066  1.000 49.24203 ? 222 ARG   A CD  1 
ATOM   1713 N NE  . ARG   A 1 242 ? 42.00531 16.92673 13.11370  1.000 55.58355 ? 222 ARG   A NE  1 
ATOM   1714 C CZ  . ARG   A 1 242 ? 42.87317 17.55456 12.33140  1.000 59.28158 ? 222 ARG   A CZ  1 
ATOM   1715 N NH1 . ARG   A 1 242 ? 44.09465 17.08402 12.13698  1.000 62.15059 ? 222 ARG   A NH1 1 
ATOM   1716 N NH2 . ARG   A 1 242 ? 42.50722 18.68363 11.73131  1.000 59.03129 ? 222 ARG   A NH2 1 
ATOM   1717 N N   . ALA   A 1 243 ? 37.16996 13.37997 12.11489  1.000 25.46646 ? 223 ALA   A N   1 
ATOM   1718 C CA  . ALA   A 1 243 ? 35.78875 13.30596 12.57613  1.000 25.01023 ? 223 ALA   A CA  1 
ATOM   1719 C C   . ALA   A 1 243 ? 35.20827 11.89979 12.48056  1.000 26.91042 ? 223 ALA   A C   1 
ATOM   1720 O O   . ALA   A 1 243 ? 34.27192 11.57511 13.21883  1.000 28.85221 ? 223 ALA   A O   1 
ATOM   1721 C CB  . ALA   A 1 243 ? 34.92561 14.27807 11.77018  1.000 25.14771 ? 223 ALA   A CB  1 
ATOM   1722 N N   . LEU   A 1 244 ? 35.74276 11.06237 11.59658  1.000 27.47589 ? 224 LEU   A N   1 
ATOM   1723 C CA  . LEU   A 1 244 ? 35.12874 9.76141  11.33878  1.000 31.17178 ? 224 LEU   A CA  1 
ATOM   1724 C C   . LEU   A 1 244 ? 34.94603 8.89677  12.58173  1.000 34.37703 ? 224 LEU   A C   1 
ATOM   1725 O O   . LEU   A 1 244 ? 33.87048 8.28921  12.71583  1.000 32.89606 ? 224 LEU   A O   1 
ATOM   1726 C CB  . LEU   A 1 244 ? 35.87792 9.02395  10.21994  1.000 33.04356 ? 224 LEU   A CB  1 
ATOM   1727 C CG  . LEU   A 1 244 ? 35.90363 9.73999  8.86861   1.000 33.15350 ? 224 LEU   A CG  1 
ATOM   1728 C CD1 . LEU   A 1 244 ? 36.37275 8.80304  7.78129   1.000 32.30694 ? 224 LEU   A CD1 1 
ATOM   1729 C CD2 . LEU   A 1 244 ? 34.53787 10.33435 8.53104   1.000 33.36039 ? 224 LEU   A CD2 1 
ATOM   1730 N N   . PRO   A 1 245 ? 35.90302 8.79943  13.51172  1.000 38.58323 ? 225 PRO   A N   1 
ATOM   1731 C CA  . PRO   A 1 245 ? 35.63995 8.02374  14.73835  1.000 41.21191 ? 225 PRO   A CA  1 
ATOM   1732 C C   . PRO   A 1 245 ? 34.48708 8.56469  15.57036  1.000 40.97248 ? 225 PRO   A C   1 
ATOM   1733 O O   . PRO   A 1 245 ? 33.96027 7.83499  16.41821  1.000 42.64534 ? 225 PRO   A O   1 
ATOM   1734 C CB  . PRO   A 1 245 ? 36.96898 8.09544  15.50746  1.000 42.74908 ? 225 PRO   A CB  1 
ATOM   1735 C CG  . PRO   A 1 245 ? 37.99732 8.46871  14.48612  1.000 42.60097 ? 225 PRO   A CG  1 
ATOM   1736 C CD  . PRO   A 1 245 ? 37.29000 9.30370  13.46766  1.000 41.10671 ? 225 PRO   A CD  1 
ATOM   1737 N N   . LYS   A 1 246 ? 34.08299 9.81458  15.36901  1.000 40.42299 ? 226 LYS   A N   1 
ATOM   1738 C CA  . LYS   A 1 246 ? 32.95497 10.39236 16.08355  1.000 42.01547 ? 226 LYS   A CA  1 
ATOM   1739 C C   . LYS   A 1 246 ? 31.65531 10.30026 15.30237  1.000 38.52524 ? 226 LYS   A C   1 
ATOM   1740 O O   . LYS   A 1 246 ? 30.60709 10.69129 15.82530  1.000 40.27317 ? 226 LYS   A O   1 
ATOM   1741 C CB  . LYS   A 1 246 ? 33.22006 11.86894 16.40838  1.000 47.76071 ? 226 LYS   A CB  1 
ATOM   1742 C CG  . LYS   A 1 246 ? 34.67354 12.23410 16.62645  1.000 52.61469 ? 226 LYS   A CG  1 
ATOM   1743 C CD  . LYS   A 1 246 ? 34.80411 13.72173 16.91313  1.000 56.46105 ? 226 LYS   A CD  1 
ATOM   1744 C CE  . LYS   A 1 246 ? 36.25504 14.17270 16.92000  1.000 59.53062 ? 226 LYS   A CE  1 
ATOM   1745 N NZ  . LYS   A 1 246 ? 36.36521 15.65866 16.92403  1.000 61.45242 ? 226 LYS   A NZ  1 
ATOM   1746 N N   . LEU   A 1 247 ? 31.69590 9.82101  14.06079  1.000 32.82784 ? 227 LEU   A N   1 
ATOM   1747 C CA  . LEU   A 1 247 ? 30.53858 9.86862  13.17813  1.000 29.52982 ? 227 LEU   A CA  1 
ATOM   1748 C C   . LEU   A 1 247 ? 29.70261 8.62130  13.42546  1.000 29.03988 ? 227 LEU   A C   1 
ATOM   1749 O O   . LEU   A 1 247 ? 30.15202 7.50278  13.16016  1.000 32.90658 ? 227 LEU   A O   1 
ATOM   1750 C CB  . LEU   A 1 247 ? 30.98667 9.96180  11.72208  1.000 28.70013 ? 227 LEU   A CB  1 
ATOM   1751 C CG  . LEU   A 1 247 ? 29.92659 10.30433 10.66828  1.000 28.19156 ? 227 LEU   A CG  1 
ATOM   1752 C CD1 . LEU   A 1 247 ? 29.33983 11.69783 10.89090  1.000 29.77011 ? 227 LEU   A CD1 1 
ATOM   1753 C CD2 . LEU   A 1 247 ? 30.51380 10.16544 9.26540   1.000 27.11457 ? 227 LEU   A CD2 1 
ATOM   1754 N N   . THR   A 1 248 ? 28.49231 8.81058  13.94283  1.000 25.32006 ? 228 THR   A N   1 
ATOM   1755 C CA  . THR   A 1 248 ? 27.58754 7.70519  14.23399  1.000 24.38948 ? 228 THR   A CA  1 
ATOM   1756 C C   . THR   A 1 248 ? 26.26090 7.82321  13.50492  1.000 23.98122 ? 228 THR   A C   1 
ATOM   1757 O O   . THR   A 1 248 ? 25.43570 6.90776  13.60321  1.000 24.49891 ? 228 THR   A O   1 
ATOM   1758 C CB  . THR   A 1 248 ? 27.30296 7.60469  15.74305  1.000 27.25028 ? 228 THR   A CB  1 
ATOM   1759 O OG1 . THR   A 1 248 ? 26.72677 8.83325  16.20884  1.000 28.04232 ? 228 THR   A OG1 1 
ATOM   1760 C CG2 . THR   A 1 248 ? 28.57269 7.32047  16.52449  1.000 29.59201 ? 228 THR   A CG2 1 
ATOM   1761 N N   . VAL   A 1 249 ? 26.03162 8.92175  12.79564  1.000 23.86736 ? 229 VAL   A N   1 
ATOM   1762 C CA  . VAL   A 1 249 ? 24.74405 9.17290  12.14070  1.000 23.23131 ? 229 VAL   A CA  1 
ATOM   1763 C C   . VAL   A 1 249 ? 24.51682 8.12156  11.05692  1.000 22.15829 ? 229 VAL   A C   1 
ATOM   1764 O O   . VAL   A 1 249 ? 25.47996 7.71421  10.38194  1.000 21.39593 ? 229 VAL   A O   1 
ATOM   1765 C CB  . VAL   A 1 249 ? 24.73734 10.58990 11.55014  1.000 24.56158 ? 229 VAL   A CB  1 
ATOM   1766 C CG1 . VAL   A 1 249 ? 25.78855 10.72265 10.44252  1.000 24.59690 ? 229 VAL   A CG1 1 
ATOM   1767 C CG2 . VAL   A 1 249 ? 23.36278 10.96117 11.03248  1.000 25.00058 ? 229 VAL   A CG2 1 
ATOM   1768 N N   . PRO   A 1 250 ? 23.29145 7.64033  10.85898  1.000 22.40651 ? 230 PRO   A N   1 
ATOM   1769 C CA  . PRO   A 1 250 ? 23.02427 6.79075  9.69044   1.000 21.32403 ? 230 PRO   A CA  1 
ATOM   1770 C C   . PRO   A 1 250 ? 23.35608 7.54851  8.41631   1.000 21.06645 ? 230 PRO   A C   1 
ATOM   1771 O O   . PRO   A 1 250 ? 23.12079 8.75493  8.32498   1.000 21.68733 ? 230 PRO   A O   1 
ATOM   1772 C CB  . PRO   A 1 250 ? 21.51798 6.52791  9.79095   1.000 21.30029 ? 230 PRO   A CB  1 
ATOM   1773 C CG  . PRO   A 1 250 ? 21.21527 6.64476  11.26159  1.000 20.97400 ? 230 PRO   A CG  1 
ATOM   1774 C CD  . PRO   A 1 250 ? 22.11512 7.76033  11.74106  1.000 22.61230 ? 230 PRO   A CD  1 
ATOM   1775 N N   . PHE   A 1 251 ? 23.91881 6.84618  7.42969   1.000 19.33204 ? 231 PHE   A N   1 
ATOM   1776 C CA  . PHE   A 1 251 ? 24.17939 7.52217  6.16403   1.000 18.51805 ? 231 PHE   A CA  1 
ATOM   1777 C C   . PHE   A 1 251 ? 24.04827 6.60129  4.95866   1.000 18.49656 ? 231 PHE   A C   1 
ATOM   1778 O O   . PHE   A 1 251 ? 24.28895 5.38751  5.03202   1.000 17.89454 ? 231 PHE   A O   1 
ATOM   1779 C CB  . PHE   A 1 251 ? 25.49160 8.33485  6.11700   1.000 19.93818 ? 231 PHE   A CB  1 
ATOM   1780 C CG  . PHE   A 1 251 ? 26.75388 7.51042  6.21629   1.000 19.28674 ? 231 PHE   A CG  1 
ATOM   1781 C CD1 . PHE   A 1 251 ? 27.34457 6.96304  5.07499   1.000 19.92741 ? 231 PHE   A CD1 1 
ATOM   1782 C CD2 . PHE   A 1 251 ? 27.38798 7.34814  7.43844   1.000 20.33027 ? 231 PHE   A CD2 1 
ATOM   1783 C CE1 . PHE   A 1 251 ? 28.51613 6.24121  5.16258   1.000 21.07256 ? 231 PHE   A CE1 1 
ATOM   1784 C CE2 . PHE   A 1 251 ? 28.56463 6.63270  7.53746   1.000 19.80903 ? 231 PHE   A CE2 1 
ATOM   1785 C CZ  . PHE   A 1 251 ? 29.13081 6.07720  6.39700   1.000 21.31147 ? 231 PHE   A CZ  1 
ATOM   1786 N N   . LEU   A 1 252 ? 23.65524 7.22263  3.85000   1.000 18.21834 ? 232 LEU   A N   1 
ATOM   1787 C CA  . LEU   A 1 252 ? 23.69943 6.65250  2.51782   1.000 18.23898 ? 232 LEU   A CA  1 
ATOM   1788 C C   . LEU   A 1 252 ? 24.78133 7.39478  1.74875   1.000 17.38031 ? 232 LEU   A C   1 
ATOM   1789 O O   . LEU   A 1 252 ? 24.80862 8.63506  1.73842   1.000 18.36929 ? 232 LEU   A O   1 
ATOM   1790 C CB  . LEU   A 1 252 ? 22.35742 6.83711  1.81096   1.000 18.63462 ? 232 LEU   A CB  1 
ATOM   1791 C CG  . LEU   A 1 252 ? 22.32235 6.42800  0.33412   1.000 18.35042 ? 232 LEU   A CG  1 
ATOM   1792 C CD1 . LEU   A 1 252 ? 22.55697 4.90114  0.16110   1.000 19.43463 ? 232 LEU   A CD1 1 
ATOM   1793 C CD2 . LEU   A 1 252 ? 20.99899 6.88339  -0.28821  1.000 19.45408 ? 232 LEU   A CD2 1 
ATOM   1794 N N   . LEU   A 1 253 ? 25.67997 6.64280  1.12779   1.000 16.37357 ? 233 LEU   A N   1 
ATOM   1795 C CA  . LEU   A 1 253 ? 26.84210 7.18811  0.44243   1.000 16.98085 ? 233 LEU   A CA  1 
ATOM   1796 C C   . LEU   A 1 253 ? 26.79109 6.74202  -1.01268  1.000 17.13165 ? 233 LEU   A C   1 
ATOM   1797 O O   . LEU   A 1 253 ? 26.77983 5.53832  -1.29085  1.000 17.81806 ? 233 LEU   A O   1 
ATOM   1798 C CB  . LEU   A 1 253 ? 28.11255 6.67494  1.12499   1.000 17.82678 ? 233 LEU   A CB  1 
ATOM   1799 C CG  . LEU   A 1 253 ? 29.47032 6.97162  0.50125   1.000 19.78808 ? 233 LEU   A CG  1 
ATOM   1800 C CD1 . LEU   A 1 253 ? 29.67693 8.47527  0.35779   1.000 20.44885 ? 233 LEU   A CD1 1 
ATOM   1801 C CD2 . LEU   A 1 253 ? 30.58581 6.34812  1.34979   1.000 20.40968 ? 233 LEU   A CD2 1 
ATOM   1802 N N   . LEU   A 1 254 ? 26.75666 7.70462  -1.93632  1.000 16.68760 ? 234 LEU   A N   1 
ATOM   1803 C CA  . LEU   A 1 254 ? 26.69024 7.43903  -3.37024  1.000 15.63287 ? 234 LEU   A CA  1 
ATOM   1804 C C   . LEU   A 1 254 ? 27.96426 7.95800  -4.01765  1.000 16.01850 ? 234 LEU   A C   1 
ATOM   1805 O O   . LEU   A 1 254 ? 28.34535 9.11148  -3.79466  1.000 17.73357 ? 234 LEU   A O   1 
ATOM   1806 C CB  . LEU   A 1 254 ? 25.46450 8.11578  -4.00027  1.000 17.78653 ? 234 LEU   A CB  1 
ATOM   1807 C CG  . LEU   A 1 254 ? 24.13457 7.86536  -3.28436  1.000 19.76645 ? 234 LEU   A CG  1 
ATOM   1808 C CD1 . LEU   A 1 254 ? 23.01594 8.66606  -3.94038  1.000 21.57443 ? 234 LEU   A CD1 1 
ATOM   1809 C CD2 . LEU   A 1 254 ? 23.79410 6.36691  -3.26069  1.000 20.72374 ? 234 LEU   A CD2 1 
ATOM   1810 N N   . GLN   A 1 255 ? 28.61563 7.12315  -4.82569  1.000 15.97097 ? 235 GLN   A N   1 
ATOM   1811 C CA  . GLN   A 1 255 ? 29.93690 7.46446  -5.34247  1.000 16.81566 ? 235 GLN   A CA  1 
ATOM   1812 C C   . GLN   A 1 255 ? 30.11627 6.88753  -6.73805  1.000 17.71986 ? 235 GLN   A C   1 
ATOM   1813 O O   . GLN   A 1 255 ? 29.81390 5.71237  -6.96217  1.000 18.63537 ? 235 GLN   A O   1 
ATOM   1814 C CB  . GLN   A 1 255 ? 31.02225 6.90420  -4.41371  1.000 17.02442 ? 235 GLN   A CB  1 
ATOM   1815 C CG  . GLN   A 1 255 ? 32.44412 7.15348  -4.89318  1.000 17.29021 ? 235 GLN   A CG  1 
ATOM   1816 C CD  . GLN   A 1 255 ? 32.79612 8.61922  -4.87312  1.000 18.77578 ? 235 GLN   A CD  1 
ATOM   1817 O OE1 . GLN   A 1 255 ? 32.48602 9.33130  -3.90953  1.000 19.27291 ? 235 GLN   A OE1 1 
ATOM   1818 N NE2 . GLN   A 1 255 ? 33.43841 9.08389  -5.93203  1.000 20.00437 ? 235 GLN   A NE2 1 
ATOM   1819 N N   . GLY   A 1 256 ? 30.61852 7.70441  -7.66478  1.000 16.64590 ? 236 GLY   A N   1 
ATOM   1820 C CA  . GLY   A 1 256 ? 30.94771 7.22536  -8.99661  1.000 16.53793 ? 236 GLY   A CA  1 
ATOM   1821 C C   . GLY   A 1 256 ? 32.36205 6.66725  -9.04939  1.000 17.42216 ? 236 GLY   A C   1 
ATOM   1822 O O   . GLY   A 1 256 ? 33.26854 7.17189  -8.39518  1.000 18.73859 ? 236 GLY   A O   1 
ATOM   1823 N N   . SER   A 1 257 ? 32.54181 5.61572  -9.84614  1.000 17.20269 ? 237 SER   A N   1 
ATOM   1824 C CA  . SER   A 1 257 ? 33.84783 4.96946  -9.89632  1.000 18.68045 ? 237 SER   A CA  1 
ATOM   1825 C C   . SER   A 1 257 ? 34.87471 5.75946  -10.70247 1.000 20.16635 ? 237 SER   A C   1 
ATOM   1826 O O   . SER   A 1 257 ? 36.07508 5.49290  -10.57842 1.000 21.40587 ? 237 SER   A O   1 
ATOM   1827 C CB  . SER   A 1 257 ? 33.71571 3.55320  -10.46207 1.000 19.88674 ? 237 SER   A CB  1 
ATOM   1828 O OG  . SER   A 1 257 ? 33.52657 3.56326  -11.86512 1.000 22.08911 ? 237 SER   A OG  1 
ATOM   1829 N N   . ALA   A 1 258 ? 34.43702 6.70421  -11.53501 1.000 19.12820 ? 238 ALA   A N   1 
ATOM   1830 C CA  . ALA   A 1 258 ? 35.33101 7.48259  -12.38342 1.000 19.15810 ? 238 ALA   A CA  1 
ATOM   1831 C C   . ALA   A 1 258 ? 35.35452 8.94617  -11.96861 1.000 20.06107 ? 238 ALA   A C   1 
ATOM   1832 O O   . ALA   A 1 258 ? 35.47454 9.83989  -12.80872 1.000 23.11758 ? 238 ALA   A O   1 
ATOM   1833 C CB  . ALA   A 1 258 ? 34.94123 7.34320  -13.85440 1.000 20.60075 ? 238 ALA   A CB  1 
ATOM   1834 N N   . ASP   A 1 259 ? 35.23553 9.19194  -10.67140 1.000 19.20439 ? 239 ASP   A N   1 
ATOM   1835 C CA  . ASP   A 1 259 ? 35.17167 10.54381 -10.12514 1.000 18.44422 ? 239 ASP   A CA  1 
ATOM   1836 C C   . ASP   A 1 259 ? 36.58924 11.09630 -10.04448 1.000 19.37744 ? 239 ASP   A C   1 
ATOM   1837 O O   . ASP   A 1 259 ? 37.41621 10.59658 -9.27376  1.000 20.50371 ? 239 ASP   A O   1 
ATOM   1838 C CB  . ASP   A 1 259 ? 34.53090 10.46555 -8.74155  1.000 17.42894 ? 239 ASP   A CB  1 
ATOM   1839 C CG  . ASP   A 1 259 ? 34.21371 11.82531 -8.15563  1.000 17.24532 ? 239 ASP   A CG  1 
ATOM   1840 O OD1 . ASP   A 1 259 ? 34.90485 12.81552 -8.50360  1.000 19.24919 ? 239 ASP   A OD1 1 
ATOM   1841 O OD2 . ASP   A 1 259 ? 33.27296 11.89608 -7.32869  1.000 17.88105 ? 239 ASP   A OD2 1 
ATOM   1842 N N   . ARG   A 1 260 ? 36.86776 12.13654 -10.83267 1.000 18.46021 ? 240 ARG   A N   1 
ATOM   1843 C CA  . ARG   A 1 260 ? 38.17392 12.77728 -10.86085 1.000 19.20674 ? 240 ARG   A CA  1 
ATOM   1844 C C   . ARG   A 1 260 ? 38.23663 14.00977 -9.97366  1.000 20.68628 ? 240 ARG   A C   1 
ATOM   1845 O O   . ARG   A 1 260 ? 39.17557 14.80169 -10.09622 1.000 23.15449 ? 240 ARG   A O   1 
ATOM   1846 C CB  . ARG   A 1 260 ? 38.55168 13.15706 -12.29335 1.000 21.18189 ? 240 ARG   A CB  1 
ATOM   1847 C CG  . ARG   A 1 260 ? 38.42652 12.01987 -13.29922 1.000 27.65651 ? 240 ARG   A CG  1 
ATOM   1848 C CD  . ARG   A 1 260 ? 39.26152 10.81593 -12.90812 1.000 35.12728 ? 240 ARG   A CD  1 
ATOM   1849 N NE  . ARG   A 1 260 ? 40.69382 11.08564 -12.95442 1.000 43.99805 ? 240 ARG   A NE  1 
ATOM   1850 C CZ  . ARG   A 1 260 ? 41.45461 10.94088 -14.03290 1.000 49.77575 ? 240 ARG   A CZ  1 
ATOM   1851 N NH1 . ARG   A 1 260 ? 40.94331 10.57569 -15.19796 1.000 51.10992 ? 240 ARG   A NH1 1 
ATOM   1852 N NH2 . ARG   A 1 260 ? 42.76300 11.16529 -13.93910 1.000 53.29181 ? 240 ARG   A NH2 1 
ATOM   1853 N N   . LEU   A 1 261 ? 37.25453 14.19952 -9.09817  1.000 18.45256 ? 241 LEU   A N   1 
ATOM   1854 C CA  . LEU   A 1 261 ? 37.24771 15.31880 -8.16391  1.000 18.11889 ? 241 LEU   A CA  1 
ATOM   1855 C C   . LEU   A 1 261 ? 37.31265 14.84752 -6.72396  1.000 19.43983 ? 241 LEU   A C   1 
ATOM   1856 O O   . LEU   A 1 261 ? 38.19982 15.27971 -5.97426  1.000 20.43144 ? 241 LEU   A O   1 
ATOM   1857 C CB  . LEU   A 1 261 ? 36.00710 16.19287 -8.39296  1.000 18.72022 ? 241 LEU   A CB  1 
ATOM   1858 C CG  . LEU   A 1 261 ? 36.13756 17.05040 -9.65628  1.000 19.18930 ? 241 LEU   A CG  1 
ATOM   1859 C CD1 . LEU   A 1 261 ? 34.82196 17.67762 -10.07231 1.000 19.56994 ? 241 LEU   A CD1 1 
ATOM   1860 C CD2 . LEU   A 1 261 ? 37.18186 18.12589 -9.41167  1.000 21.87808 ? 241 LEU   A CD2 1 
ATOM   1861 N N   . CYS   A 1 262 ? 36.40887 13.95875 -6.32227  1.000 18.57213 ? 242 CYS   A N   1 
ATOM   1862 C CA  . CYS   A 1 262 ? 36.48767 13.27488 -5.03586  1.000 18.69381 ? 242 CYS   A CA  1 
ATOM   1863 C C   . CYS   A 1 262 ? 36.86952 11.82883 -5.31762  1.000 21.64546 ? 242 CYS   A C   1 
ATOM   1864 O O   . CYS   A 1 262 ? 36.10120 11.09701 -5.95036  1.000 23.01059 ? 242 CYS   A O   1 
ATOM   1865 C CB  . CYS   A 1 262 ? 35.15494 13.36815 -4.30544  1.000 19.57352 ? 242 CYS   A CB  1 
ATOM   1866 S SG  . CYS   A 1 262 ? 34.80666 15.06149 -3.77775  0.883 19.18540 ? 242 CYS   A SG  1 
ATOM   1867 N N   . ASP   A 1 263 ? 38.06262 11.43619 -4.85544  1.000 21.38485 ? 243 ASP   A N   1 
ATOM   1868 C CA  . ASP   A 1 263 ? 38.60581 10.09841 -5.08639  1.000 23.58887 ? 243 ASP   A CA  1 
ATOM   1869 C C   . ASP   A 1 263 ? 37.67371 9.06635  -4.46560  1.000 21.96832 ? 243 ASP   A C   1 
ATOM   1870 O O   . ASP   A 1 263 ? 37.27396 9.19274  -3.30372  1.000 21.10621 ? 243 ASP   A O   1 
ATOM   1871 C CB  . ASP   A 1 263 ? 39.99953 10.05320 -4.42830  1.000 26.46349 ? 243 ASP   A CB  1 
ATOM   1872 C CG  . ASP   A 1 263 ? 40.78347 8.74522  -4.66204  1.000 28.98640 ? 243 ASP   A CG  1 
ATOM   1873 O OD1 . ASP   A 1 263 ? 40.23615 7.71929  -5.09368  1.000 26.13124 ? 243 ASP   A OD1 1 
ATOM   1874 O OD2 . ASP   A 1 263 ? 42.00188 8.75294  -4.36832  0.546 31.46624 ? 243 ASP   A OD2 1 
ATOM   1875 N N   . SER   A 1 264 ? 37.31592 8.04018  -5.24636  1.000 21.13281 ? 244 SER   A N   1 
ATOM   1876 C CA  . SER   A 1 264 ? 36.40881 7.02339  -4.72280  1.000 20.60172 ? 244 SER   A CA  1 
ATOM   1877 C C   . SER   A 1 264 ? 37.00169 6.30325  -3.51438  1.000 20.53081 ? 244 SER   A C   1 
ATOM   1878 O O   . SER   A 1 264 ? 36.25407 5.77557  -2.68295  1.000 20.62725 ? 244 SER   A O   1 
ATOM   1879 C CB  . SER   A 1 264 ? 36.04319 6.02089  -5.81350  1.000 22.37579 ? 244 SER   A CB  1 
ATOM   1880 O OG  . SER   A 1 264 ? 37.18025 5.25571  -6.17315  1.000 23.53568 ? 244 SER   A OG  1 
ATOM   1881 N N   . LYS   A 1 265 ? 38.33360 6.28434  -3.39500  1.000 19.82922 ? 245 LYS   A N   1 
ATOM   1882 C CA  . LYS   A 1 265 ? 38.97962 5.73991  -2.20514  1.000 20.42763 ? 245 LYS   A CA  1 
ATOM   1883 C C   . LYS   A 1 265 ? 38.45283 6.38873  -0.93314  1.000 20.68945 ? 245 LYS   A C   1 
ATOM   1884 O O   . LYS   A 1 265 ? 38.34094 5.72440  0.10273   1.000 21.49103 ? 245 LYS   A O   1 
ATOM   1885 C CB  . LYS   A 1 265 ? 40.49704 5.91835  -2.31018  1.000 23.06375 ? 245 LYS   A CB  1 
ATOM   1886 C CG  . LYS   A 1 265 ? 41.30030 5.38138  -1.11647  1.000 29.06170 ? 245 LYS   A CG  1 
ATOM   1887 C CD  . LYS   A 1 265 ? 41.13813 3.87597  -0.91706  1.000 36.00676 ? 245 LYS   A CD  1 
ATOM   1888 C CE  . LYS   A 1 265 ? 41.94914 3.39102  0.29714   1.000 40.72743 ? 245 LYS   A CE  1 
ATOM   1889 N NZ  . LYS   A 1 265 ? 41.70132 1.95831  0.67366   1.000 44.51382 ? 245 LYS   A NZ  1 
ATOM   1890 N N   . GLY   A 1 266 ? 38.10286 7.67670  -0.98732  1.000 20.86422 ? 246 GLY   A N   1 
ATOM   1891 C CA  . GLY   A 1 266 ? 37.53971 8.32011  0.18836   1.000 21.36830 ? 246 GLY   A CA  1 
ATOM   1892 C C   . GLY   A 1 266 ? 36.18843 7.75330  0.58197   1.000 20.45275 ? 246 GLY   A C   1 
ATOM   1893 O O   . GLY   A 1 266 ? 35.86723 7.66297  1.76946   1.000 20.63809 ? 246 GLY   A O   1 
ATOM   1894 N N   . ALA   A 1 267 ? 35.37266 7.37061  -0.40451  1.000 18.85969 ? 247 ALA   A N   1 
ATOM   1895 C CA  . ALA   A 1 267 ? 34.09505 6.75336  -0.07473  1.000 19.84110 ? 247 ALA   A CA  1 
ATOM   1896 C C   . ALA   A 1 267 ? 34.31140 5.41547  0.62560   1.000 19.28171 ? 247 ALA   A C   1 
ATOM   1897 O O   . ALA   A 1 267 ? 33.64765 5.11003  1.62503   1.000 19.82530 ? 247 ALA   A O   1 
ATOM   1898 C CB  . ALA   A 1 267 ? 33.24369 6.58357  -1.33610  1.000 19.19258 ? 247 ALA   A CB  1 
ATOM   1899 N N   . TYR   A 1 268 ? 35.25762 4.61452  0.13147   1.000 19.21042 ? 248 TYR   A N   1 
ATOM   1900 C CA  . TYR   A 1 268 ? 35.54192 3.34349  0.78718   1.000 19.61812 ? 248 TYR   A CA  1 
ATOM   1901 C C   . TYR   A 1 268 ? 36.09087 3.56766  2.19316   1.000 19.70080 ? 248 TYR   A C   1 
ATOM   1902 O O   . TYR   A 1 268 ? 35.73313 2.84674  3.13219   1.000 20.75332 ? 248 TYR   A O   1 
ATOM   1903 C CB  . TYR   A 1 268 ? 36.51344 2.51455  -0.05642  1.000 21.31204 ? 248 TYR   A CB  1 
ATOM   1904 C CG  . TYR   A 1 268 ? 35.95798 2.09497  -1.40137  1.000 21.38529 ? 248 TYR   A CG  1 
ATOM   1905 C CD1 . TYR   A 1 268 ? 34.91100 1.19128  -1.48654  1.000 22.55032 ? 248 TYR   A CD1 1 
ATOM   1906 C CD2 . TYR   A 1 268 ? 36.47455 2.60911  -2.58636  1.000 21.42800 ? 248 TYR   A CD2 1 
ATOM   1907 C CE1 . TYR   A 1 268 ? 34.39726 0.80306  -2.71193  1.000 23.69658 ? 248 TYR   A CE1 1 
ATOM   1908 C CE2 . TYR   A 1 268 ? 35.96647 2.22697  -3.81828  1.000 22.17020 ? 248 TYR   A CE2 1 
ATOM   1909 C CZ  . TYR   A 1 268 ? 34.92676 1.32202  -3.87289  1.000 22.12681 ? 248 TYR   A CZ  1 
ATOM   1910 O OH  . TYR   A 1 268 ? 34.40201 0.93688  -5.08423  1.000 22.77040 ? 248 TYR   A OH  1 
ATOM   1911 N N   . LEU   A 1 269 ? 36.95360 4.56954  2.36218   1.000 20.10211 ? 249 LEU   A N   1 
ATOM   1912 C CA  . LEU   A 1 269 ? 37.49571 4.84692  3.69038   1.000 20.42232 ? 249 LEU   A CA  1 
ATOM   1913 C C   . LEU   A 1 269 ? 36.41818 5.34641  4.64432   1.000 20.90304 ? 249 LEU   A C   1 
ATOM   1914 O O   . LEU   A 1 269 ? 36.44989 5.03809  5.84336   1.000 21.13565 ? 249 LEU   A O   1 
ATOM   1915 C CB  . LEU   A 1 269 ? 38.64420 5.84953  3.60086   1.000 24.97135 ? 249 LEU   A CB  1 
ATOM   1916 C CG  . LEU   A 1 269 ? 39.97511 5.25403  3.13406   1.000 28.81211 ? 249 LEU   A CG  1 
ATOM   1917 C CD1 . LEU   A 1 269 ? 40.99230 6.36604  2.91971   1.000 29.94910 ? 249 LEU   A CD1 1 
ATOM   1918 C CD2 . LEU   A 1 269 ? 40.49249 4.22209  4.13012   1.000 29.13486 ? 249 LEU   A CD2 1 
ATOM   1919 N N   . LEU   A 1 270 ? 35.46598 6.13505  4.13889   1.000 19.90977 ? 250 LEU   A N   1 
ATOM   1920 C CA  . LEU   A 1 270 ? 34.35312 6.56469  4.97823   1.000 20.35054 ? 250 LEU   A CA  1 
ATOM   1921 C C   . LEU   A 1 270 ? 33.54590 5.36318  5.46587   1.000 20.79740 ? 250 LEU   A C   1 
ATOM   1922 O O   . LEU   A 1 270 ? 33.17518 5.28487  6.64523   1.000 21.07098 ? 250 LEU   A O   1 
ATOM   1923 C CB  . LEU   A 1 270 ? 33.48324 7.55993  4.20407   1.000 20.80230 ? 250 LEU   A CB  1 
ATOM   1924 C CG  . LEU   A 1 270 ? 32.17746 8.00183  4.85512   1.000 21.09401 ? 250 LEU   A CG  1 
ATOM   1925 C CD1 . LEU   A 1 270 ? 32.45195 8.64482  6.19904   1.000 22.89240 ? 250 LEU   A CD1 1 
ATOM   1926 C CD2 . LEU   A 1 270 ? 31.39927 8.95364  3.93392   1.000 23.12067 ? 250 LEU   A CD2 1 
ATOM   1927 N N   . MET   A 1 271 ? 33.28265 4.40647  4.57503   1.000 19.95360 ? 251 MET   A N   1 
ATOM   1928 C CA  . MET   A 1 271 ? 32.57222 3.19734  4.97795   1.000 19.94391 ? 251 MET   A CA  1 
ATOM   1929 C C   . MET   A 1 271 ? 33.35867 2.42541  6.02370   1.000 20.39375 ? 251 MET   A C   1 
ATOM   1930 O O   . MET   A 1 271 ? 32.77605 1.83837  6.94010   1.000 23.30907 ? 251 MET   A O   1 
ATOM   1931 C CB  . MET   A 1 271 ? 32.30436 2.30175  3.76449   1.000 20.60410 ? 251 MET   A CB  1 
ATOM   1932 C CG  . MET   A 1 271 ? 31.21414 2.82130  2.85226   1.000 21.35339 ? 251 MET   A CG  1 
ATOM   1933 S SD  . MET   A 1 271 ? 29.58298 2.91782  3.57709   1.000 20.71415 ? 251 MET   A SD  1 
ATOM   1934 C CE  . MET   A 1 271 ? 29.13888 1.16547  3.72022   1.000 19.98512 ? 251 MET   A CE  1 
ATOM   1935 N N   . GLU   A 1 272 ? 34.68220 2.42887  5.91605   1.000 20.74134 ? 252 GLU   A N   1 
ATOM   1936 C CA  . GLU   A 1 272 ? 35.48569 1.63525  6.83288   1.000 20.56832 ? 252 GLU   A CA  1 
ATOM   1937 C C   . GLU   A 1 272 ? 35.62545 2.30832  8.19290   1.000 20.71002 ? 252 GLU   A C   1 
ATOM   1938 O O   . GLU   A 1 272 ? 35.59915 1.62844  9.22568   1.000 23.90515 ? 252 GLU   A O   1 
ATOM   1939 C CB  . GLU   A 1 272 ? 36.86589 1.37133  6.23149   1.000 22.19630 ? 252 GLU   A CB  1 
ATOM   1940 C CG  . GLU   A 1 272 ? 37.72988 0.49876  7.12162   1.000 25.79034 ? 252 GLU   A CG  1 
ATOM   1941 C CD  . GLU   A 1 272 ? 39.15059 0.34942  6.62902   1.000 31.87837 ? 252 GLU   A CD  1 
ATOM   1942 O OE1 . GLU   A 1 272 ? 39.52618 1.01131  5.64415   1.000 33.38325 ? 252 GLU   A OE1 1 
ATOM   1943 O OE2 . GLU   A 1 272 ? 39.89861 -0.43781 7.24087   1.000 36.79893 ? 252 GLU   A OE2 1 
ATOM   1944 N N   . LEU   A 1 273 ? 35.78063 3.63725  8.21589   1.000 20.27134 ? 253 LEU   A N   1 
ATOM   1945 C CA  . LEU   A 1 273 ? 36.20841 4.31253  9.43264   1.000 21.22065 ? 253 LEU   A CA  1 
ATOM   1946 C C   . LEU   A 1 273 ? 35.07930 4.96192  10.22334  1.000 22.48400 ? 253 LEU   A C   1 
ATOM   1947 O O   . LEU   A 1 273 ? 35.25224 5.19438  11.42254  1.000 24.07339 ? 253 LEU   A O   1 
ATOM   1948 C CB  . LEU   A 1 273 ? 37.29423 5.34942  9.11606   1.000 24.39231 ? 253 LEU   A CB  1 
ATOM   1949 C CG  . LEU   A 1 273 ? 38.56491 4.74167  8.51620   1.000 27.33901 ? 253 LEU   A CG  1 
ATOM   1950 C CD1 . LEU   A 1 273 ? 39.56872 5.82351  8.13936   1.000 30.25284 ? 253 LEU   A CD1 1 
ATOM   1951 C CD2 . LEU   A 1 273 ? 39.18728 3.72576  9.47795   1.000 29.42514 ? 253 LEU   A CD2 1 
ATOM   1952 N N   . ALA   A 1 274 ? 33.94167 5.26337  9.59849   1.000 19.86924 ? 254 ALA   A N   1 
ATOM   1953 C CA  . ALA   A 1 274 ? 32.81690 5.80782  10.34968  1.000 20.45897 ? 254 ALA   A CA  1 
ATOM   1954 C C   . ALA   A 1 274 ? 32.29839 4.77161  11.33538  1.000 23.62454 ? 254 ALA   A C   1 
ATOM   1955 O O   . ALA   A 1 274 ? 32.24197 3.57646  11.03500  1.000 23.67953 ? 254 ALA   A O   1 
ATOM   1956 C CB  . ALA   A 1 274 ? 31.69029 6.18776  9.39695   1.000 22.02603 ? 254 ALA   A CB  1 
ATOM   1957 N N   . LYS   A 1 275 ? 31.90910 5.22477  12.52102  1.000 25.49680 ? 255 LYS   A N   1 
ATOM   1958 C CA  A LYS   A 1 275 ? 31.40007 4.33394  13.55703  0.274 27.45619 ? 255 LYS   A CA  1 
ATOM   1959 C CA  B LYS   A 1 275 ? 31.41077 4.29502  13.52411  0.726 27.65509 ? 255 LYS   A CA  1 
ATOM   1960 C C   . LYS   A 1 275 ? 29.91292 4.03935  13.41283  1.000 27.35216 ? 255 LYS   A C   1 
ATOM   1961 O O   . LYS   A 1 275 ? 29.37447 3.24760  14.19523  1.000 28.97510 ? 255 LYS   A O   1 
ATOM   1962 C CB  A LYS   A 1 275 ? 31.69389 4.91348  14.94462  0.274 29.61224 ? 255 LYS   A CB  1 
ATOM   1963 C CB  B LYS   A 1 275 ? 31.81562 4.75350  14.92861  0.726 30.82174 ? 255 LYS   A CB  1 
ATOM   1964 C CG  A LYS   A 1 275 ? 33.16385 4.86939  15.33079  0.274 31.56007 ? 255 LYS   A CG  1 
ATOM   1965 C CG  B LYS   A 1 275 ? 33.32754 4.71238  15.14228  0.726 33.32438 ? 255 LYS   A CG  1 
ATOM   1966 C CD  A LYS   A 1 275 ? 33.61519 3.44413  15.61427  0.274 33.51774 ? 255 LYS   A CD  1 
ATOM   1967 C CD  B LYS   A 1 275 ? 33.87405 3.31432  14.85008  0.726 35.86481 ? 255 LYS   A CD  1 
ATOM   1968 C CE  A LYS   A 1 275 ? 35.10365 3.38572  15.91865  0.274 34.28356 ? 255 LYS   A CE  1 
ATOM   1969 C CE  B LYS   A 1 275 ? 35.39623 3.24749  14.95351  0.726 38.87659 ? 255 LYS   A CE  1 
ATOM   1970 N NZ  A LYS   A 1 275 ? 35.50302 4.42906  16.90020  0.274 34.53242 ? 255 LYS   A NZ  1 
ATOM   1971 N NZ  B LYS   A 1 275 ? 36.07479 3.77800  13.73541  0.726 39.51618 ? 255 LYS   A NZ  1 
ATOM   1972 N N   . SER   A 1 276 ? 29.25248 4.64366  12.42822  1.000 24.92446 ? 256 SER   A N   1 
ATOM   1973 C CA  A SER   A 1 276 ? 27.81251 4.49291  12.25454  0.740 23.89628 ? 256 SER   A CA  1 
ATOM   1974 C CA  B SER   A 1 276 ? 27.81391 4.49277  12.26608  0.260 24.15612 ? 256 SER   A CA  1 
ATOM   1975 C C   . SER   A 1 276 ? 27.42594 3.02705  12.12759  1.000 23.97477 ? 256 SER   A C   1 
ATOM   1976 O O   . SER   A 1 276 ? 28.07556 2.25605  11.41745  1.000 25.25787 ? 256 SER   A O   1 
ATOM   1977 C CB  A SER   A 1 276 ? 27.37973 5.20768  10.97723  0.740 22.97017 ? 256 SER   A CB  1 
ATOM   1978 C CB  B SER   A 1 276 ? 27.36471 5.24477  11.01613  0.260 23.41932 ? 256 SER   A CB  1 
ATOM   1979 O OG  A SER   A 1 276 ? 27.79358 6.56246  10.97807  0.740 22.30515 ? 256 SER   A OG  1 
ATOM   1980 O OG  B SER   A 1 276 ? 26.03421 4.90488  10.67389  0.260 22.34692 ? 256 SER   A OG  1 
ATOM   1981 N N   . GLN   A 1 277 ? 26.33999 2.65507  12.79783  1.000 24.12731 ? 257 GLN   A N   1 
ATOM   1982 C CA  . GLN   A 1 277 ? 25.79353 1.31432  12.66906  1.000 25.60533 ? 257 GLN   A CA  1 
ATOM   1983 C C   . GLN   A 1 277 ? 24.90500 1.14752  11.44878  1.000 23.41457 ? 257 GLN   A C   1 
ATOM   1984 O O   . GLN   A 1 277 ? 24.56487 0.00939  11.11136  1.000 26.17002 ? 257 GLN   A O   1 
ATOM   1985 C CB  . GLN   A 1 277 ? 24.98132 0.95268  13.90398  1.000 29.97427 ? 257 GLN   A CB  1 
ATOM   1986 C CG  . GLN   A 1 277 ? 25.81261 0.76707  15.13109  1.000 35.63635 ? 257 GLN   A CG  1 
ATOM   1987 C CD  . GLN   A 1 277 ? 24.98469 0.25423  16.27077  1.000 43.08383 ? 257 GLN   A CD  1 
ATOM   1988 O OE1 . GLN   A 1 277 ? 24.62845 1.00511  17.17643  1.000 47.86989 ? 257 GLN   A OE1 1 
ATOM   1989 N NE2 . GLN   A 1 277 ? 24.64957 -1.02540 16.22611  1.000 46.43770 ? 257 GLN   A NE2 1 
ATOM   1990 N N   . ASP   A 1 278 ? 24.53019 2.23623  10.77801  1.000 20.99758 ? 258 ASP   A N   1 
ATOM   1991 C CA  . ASP   A 1 278 ? 23.64390 2.18605  9.61721   1.000 18.99427 ? 258 ASP   A CA  1 
ATOM   1992 C C   . ASP   A 1 278 ? 24.33599 2.92770  8.48059   1.000 19.57870 ? 258 ASP   A C   1 
ATOM   1993 O O   . ASP   A 1 278 ? 24.16302 4.13940  8.31564   1.000 21.40581 ? 258 ASP   A O   1 
ATOM   1994 C CB  . ASP   A 1 278 ? 22.29094 2.80483  9.97998   1.000 21.81314 ? 258 ASP   A CB  1 
ATOM   1995 C CG  . ASP   A 1 278 ? 21.30067 2.78421  8.82807   1.000 24.79732 ? 258 ASP   A CG  1 
ATOM   1996 O OD1 . ASP   A 1 278 ? 21.59996 2.18375  7.77463   1.000 23.71783 ? 258 ASP   A OD1 1 
ATOM   1997 O OD2 . ASP   A 1 278 ? 20.21043 3.37519  8.98364   1.000 26.13399 ? 258 ASP   A OD2 1 
ATOM   1998 N N   . LYS   A 1 279 ? 25.12828 2.20176  7.69871   1.000 18.49544 ? 259 LYS   A N   1 
ATOM   1999 C CA  . LYS   A 1 279 ? 25.88098 2.80662  6.61200   1.000 18.97353 ? 259 LYS   A CA  1 
ATOM   2000 C C   . LYS   A 1 279 ? 25.81576 1.94342  5.36285   1.000 17.80441 ? 259 LYS   A C   1 
ATOM   2001 O O   . LYS   A 1 279 ? 25.99509 0.72223  5.42626   1.000 18.67963 ? 259 LYS   A O   1 
ATOM   2002 C CB  . LYS   A 1 279 ? 27.32913 3.12493  7.00832   1.000 23.16096 ? 259 LYS   A CB  1 
ATOM   2003 C CG  . LYS   A 1 279 ? 28.05188 2.04526  7.75490   1.000 23.88507 ? 259 LYS   A CG  1 
ATOM   2004 C CD  . LYS   A 1 279 ? 29.45259 2.51011  8.19609   1.000 24.15258 ? 259 LYS   A CD  1 
ATOM   2005 C CE  . LYS   A 1 279 ? 30.14663 1.38762  8.97132   1.000 22.28184 ? 259 LYS   A CE  1 
ATOM   2006 N NZ  . LYS   A 1 279 ? 31.57861 1.62139  9.29895   1.000 20.25163 ? 259 LYS   A NZ  1 
ATOM   2007 N N   . THR   A 1 280 ? 25.55278 2.59306  4.23277   1.000 17.68880 ? 260 THR   A N   1 
ATOM   2008 C CA  . THR   A 1 280 ? 25.32233 1.93191  2.96026   1.000 18.43435 ? 260 THR   A CA  1 
ATOM   2009 C C   . THR   A 1 280 ? 26.06820 2.70043  1.88689   1.000 18.60930 ? 260 THR   A C   1 
ATOM   2010 O O   . THR   A 1 280 ? 26.00197 3.93680  1.84315   1.000 19.31642 ? 260 THR   A O   1 
ATOM   2011 C CB  . THR   A 1 280 ? 23.83223 1.96914  2.61195   1.000 19.90671 ? 260 THR   A CB  1 
ATOM   2012 O OG1 . THR   A 1 280 ? 23.07616 1.35233  3.66282   1.000 21.13102 ? 260 THR   A OG1 1 
ATOM   2013 C CG2 . THR   A 1 280 ? 23.56092 1.27019  1.28582   1.000 21.43961 ? 260 THR   A CG2 1 
ATOM   2014 N N   . LEU   A 1 281 ? 26.75772 1.96715  1.01566   1.000 17.68171 ? 261 LEU   A N   1 
ATOM   2015 C CA  . LEU   A 1 281 ? 27.49492 2.53461  -0.10345  1.000 16.82468 ? 261 LEU   A CA  1 
ATOM   2016 C C   . LEU   A 1 281 ? 26.92041 1.97863  -1.39540  1.000 17.76735 ? 261 LEU   A C   1 
ATOM   2017 O O   . LEU   A 1 281 ? 26.70044 0.76320  -1.51278  1.000 18.85386 ? 261 LEU   A O   1 
ATOM   2018 C CB  . LEU   A 1 281 ? 28.98001 2.17165  -0.01743  1.000 19.11752 ? 261 LEU   A CB  1 
ATOM   2019 C CG  . LEU   A 1 281 ? 29.80220 2.42196  -1.28706  1.000 19.37189 ? 261 LEU   A CG  1 
ATOM   2020 C CD1 . LEU   A 1 281 ? 29.91935 3.92094  -1.58955  1.000 19.74183 ? 261 LEU   A CD1 1 
ATOM   2021 C CD2 . LEU   A 1 281 ? 31.18070 1.78852  -1.18877  1.000 20.95752 ? 261 LEU   A CD2 1 
ATOM   2022 N N   . LYS   A 1 282 ? 26.66247 2.85784  -2.35260  1.000 18.33077 ? 262 LYS   A N   1 
ATOM   2023 C CA  . LYS   A 1 282 ? 26.32939 2.45108  -3.70931  1.000 18.77566 ? 262 LYS   A CA  1 
ATOM   2024 C C   . LYS   A 1 282 ? 27.35701 3.05844  -4.64625  1.000 18.46434 ? 262 LYS   A C   1 
ATOM   2025 O O   . LYS   A 1 282 ? 27.58610 4.27146  -4.61491  1.000 18.65191 ? 262 LYS   A O   1 
ATOM   2026 C CB  . LYS   A 1 282 ? 24.91608 2.89250  -4.08779  1.000 22.05204 ? 262 LYS   A CB  1 
ATOM   2027 C CG  . LYS   A 1 282 ? 24.39971 2.25676  -5.36063  1.000 29.07210 ? 262 LYS   A CG  1 
ATOM   2028 C CD  . LYS   A 1 282 ? 22.92508 2.57293  -5.56785  1.000 32.65298 ? 262 LYS   A CD  1 
ATOM   2029 C CE  . LYS   A 1 282 ? 22.44389 2.03212  -6.90333  1.000 35.50041 ? 262 LYS   A CE  1 
ATOM   2030 N NZ  . LYS   A 1 282 ? 22.57708 0.55435  -6.94374  1.000 37.45515 ? 262 LYS   A NZ  1 
ATOM   2031 N N   . ILE   A 1 283 ? 27.98837 2.21318  -5.45899  1.000 18.97908 ? 263 ILE   A N   1 
ATOM   2032 C CA  . ILE   A 1 283 ? 28.98237 2.63479  -6.44057  1.000 19.10937 ? 263 ILE   A CA  1 
ATOM   2033 C C   . ILE   A 1 283 ? 28.31795 2.63978  -7.80636  1.000 19.97289 ? 263 ILE   A C   1 
ATOM   2034 O O   . ILE   A 1 283 ? 27.69796 1.64437  -8.21089  1.000 20.56283 ? 263 ILE   A O   1 
ATOM   2035 C CB  . ILE   A 1 283 ? 30.19668 1.68837  -6.44819  1.000 18.85446 ? 263 ILE   A CB  1 
ATOM   2036 C CG1 . ILE   A 1 283 ? 31.00484 1.81128  -5.14749  1.000 19.69541 ? 263 ILE   A CG1 1 
ATOM   2037 C CG2 . ILE   A 1 283 ? 31.06941 1.95629  -7.68279  1.000 19.03798 ? 263 ILE   A CG2 1 
ATOM   2038 C CD1 . ILE   A 1 283 ? 31.80512 3.12279  -5.01923  1.000 19.32407 ? 263 ILE   A CD1 1 
ATOM   2039 N N   . TYR   A 1 284 ? 28.45250 3.74847  -8.52054  1.000 19.03300 ? 264 TYR   A N   1 
ATOM   2040 C CA  . TYR   A 1 284 ? 27.95434 3.87289  -9.88639  1.000 19.09863 ? 264 TYR   A CA  1 
ATOM   2041 C C   . TYR   A 1 284 ? 29.11889 3.67585  -10.84852 1.000 17.71119 ? 264 TYR   A C   1 
ATOM   2042 O O   . TYR   A 1 284 ? 30.01140 4.52757  -10.94617 1.000 18.48143 ? 264 TYR   A O   1 
ATOM   2043 C CB  . TYR   A 1 284 ? 27.25478 5.21300  -10.08743 1.000 19.96209 ? 264 TYR   A CB  1 
ATOM   2044 C CG  . TYR   A 1 284 ? 25.94106 5.25655  -9.35305  1.000 19.92162 ? 264 TYR   A CG  1 
ATOM   2045 C CD1 . TYR   A 1 284 ? 24.78454 4.77825  -9.95487  1.000 19.32839 ? 264 TYR   A CD1 1 
ATOM   2046 C CD2 . TYR   A 1 284 ? 25.85888 5.72883  -8.04107  1.000 20.50006 ? 264 TYR   A CD2 1 
ATOM   2047 C CE1 . TYR   A 1 284 ? 23.57896 4.79026  -9.29207  1.000 19.96351 ? 264 TYR   A CE1 1 
ATOM   2048 C CE2 . TYR   A 1 284 ? 24.64799 5.73472  -7.36120  1.000 19.99447 ? 264 TYR   A CE2 1 
ATOM   2049 C CZ  . TYR   A 1 284 ? 23.51332 5.26433  -7.99836  1.000 20.34961 ? 264 TYR   A CZ  1 
ATOM   2050 O OH  . TYR   A 1 284 ? 22.30760 5.26851  -7.34908  1.000 22.26297 ? 264 TYR   A OH  1 
ATOM   2051 N N   . GLU   A 1 285 ? 29.11319 2.53686  -11.54453 1.000 18.69840 ? 265 GLU   A N   1 
ATOM   2052 C CA  . GLU   A 1 285 ? 30.25172 2.12713  -12.35279 1.000 19.48065 ? 265 GLU   A CA  1 
ATOM   2053 C C   . GLU   A 1 285 ? 30.37773 3.01830  -13.58167 1.000 21.07558 ? 265 GLU   A C   1 
ATOM   2054 O O   . GLU   A 1 285 ? 29.44510 3.12193  -14.38515 1.000 23.41409 ? 265 GLU   A O   1 
ATOM   2055 C CB  . GLU   A 1 285 ? 30.07571 0.66431  -12.76267 1.000 21.64573 ? 265 GLU   A CB  1 
ATOM   2056 C CG  . GLU   A 1 285 ? 31.27860 0.07920  -13.45581 1.000 26.18830 ? 265 GLU   A CG  1 
ATOM   2057 C CD  . GLU   A 1 285 ? 32.51695 0.04218  -12.57579 1.000 29.06913 ? 265 GLU   A CD  1 
ATOM   2058 O OE1 . GLU   A 1 285 ? 32.40719 0.16467  -11.32641 1.000 28.17525 ? 265 GLU   A OE1 1 
ATOM   2059 O OE2 . GLU   A 1 285 ? 33.61054 -0.11023 -13.14797 1.000 32.49873 ? 265 GLU   A OE2 1 
ATOM   2060 N N   . GLY   A 1 286 ? 31.53492 3.66389  -13.72475 1.000 20.65272 ? 266 GLY   A N   1 
ATOM   2061 C CA  . GLY   A 1 286 ? 31.79089 4.54756  -14.83868 1.000 20.40385 ? 266 GLY   A CA  1 
ATOM   2062 C C   . GLY   A 1 286 ? 31.33752 5.97946  -14.63487 1.000 20.35711 ? 266 GLY   A C   1 
ATOM   2063 O O   . GLY   A 1 286 ? 31.69357 6.84382  -15.44641 1.000 20.70733 ? 266 GLY   A O   1 
ATOM   2064 N N   . ALA   A 1 287 ? 30.58434 6.26042  -13.57314 1.000 19.31686 ? 267 ALA   A N   1 
ATOM   2065 C CA  . ALA   A 1 287 ? 29.98438 7.57590  -13.41843 1.000 18.77373 ? 267 ALA   A CA  1 
ATOM   2066 C C   . ALA   A 1 287 ? 31.01381 8.58547  -12.92895 1.000 18.30473 ? 267 ALA   A C   1 
ATOM   2067 O O   . ALA   A 1 287 ? 31.97750 8.24565  -12.23443 1.000 18.65393 ? 267 ALA   A O   1 
ATOM   2068 C CB  . ALA   A 1 287 ? 28.80697 7.51945  -12.44415 1.000 20.08515 ? 267 ALA   A CB  1 
ATOM   2069 N N   . TYR   A 1 288 ? 30.79167 9.83787  -13.29972 1.000 17.25404 ? 268 TYR   A N   1 
ATOM   2070 C CA  . TYR   A 1 288 ? 31.64201 10.94756 -12.89823 1.000 17.86811 ? 268 TYR   A CA  1 
ATOM   2071 C C   . TYR   A 1 288 ? 31.16186 11.51904 -11.56132 1.000 19.10153 ? 268 TYR   A C   1 
ATOM   2072 O O   . TYR   A 1 288 ? 30.49653 10.84151 -10.77879 1.000 22.03351 ? 268 TYR   A O   1 
ATOM   2073 C CB  . TYR   A 1 288 ? 31.66646 12.01630 -14.00079 1.000 18.23973 ? 268 TYR   A CB  1 
ATOM   2074 C CG  . TYR   A 1 288 ? 32.43777 11.65849 -15.25128 1.000 19.82081 ? 268 TYR   A CG  1 
ATOM   2075 C CD1 . TYR   A 1 288 ? 32.93984 10.36969 -15.46010 1.000 20.00621 ? 268 TYR   A CD1 1 
ATOM   2076 C CD2 . TYR   A 1 288 ? 32.66787 12.62170 -16.23473 1.000 20.93396 ? 268 TYR   A CD2 1 
ATOM   2077 C CE1 . TYR   A 1 288 ? 33.64010 10.06307 -16.62364 1.000 21.54041 ? 268 TYR   A CE1 1 
ATOM   2078 C CE2 . TYR   A 1 288 ? 33.36078 12.32019 -17.39469 1.000 22.66129 ? 268 TYR   A CE2 1 
ATOM   2079 C CZ  . TYR   A 1 288 ? 33.84498 11.04719 -17.58672 1.000 22.37773 ? 268 TYR   A CZ  1 
ATOM   2080 O OH  . TYR   A 1 288 ? 34.53745 10.76585 -18.74959 1.000 26.10122 ? 268 TYR   A OH  1 
ATOM   2081 N N   . HIS   A 1 289 ? 31.46444 12.78844 -11.29609 1.000 18.09616 ? 269 HIS   A N   1 
ATOM   2082 C CA  . HIS   A 1 289 ? 31.34663 13.35441 -9.95749  1.000 17.77885 ? 269 HIS   A CA  1 
ATOM   2083 C C   . HIS   A 1 289 ? 29.90385 13.68340 -9.57486  1.000 17.66131 ? 269 HIS   A C   1 
ATOM   2084 O O   . HIS   A 1 289 ? 29.46533 13.37876 -8.45666  1.000 17.98308 ? 269 HIS   A O   1 
ATOM   2085 C CB  . HIS   A 1 289 ? 32.21268 14.61385 -9.89069  1.000 17.39630 ? 269 HIS   A CB  1 
ATOM   2086 C CG  . HIS   A 1 289 ? 32.24912 15.27609 -8.54884  1.000 16.31959 ? 269 HIS   A CG  1 
ATOM   2087 N ND1 . HIS   A 1 289 ? 32.53248 14.60134 -7.38097  1.000 16.96609 ? 269 HIS   A ND1 1 
ATOM   2088 C CD2 . HIS   A 1 289 ? 32.08110 16.57564 -8.19870  1.000 17.35932 ? 269 HIS   A CD2 1 
ATOM   2089 C CE1 . HIS   A 1 289 ? 32.51180 15.44985 -6.36634  1.000 17.91346 ? 269 HIS   A CE1 1 
ATOM   2090 N NE2 . HIS   A 1 289 ? 32.25642 16.65819 -6.83970  1.000 17.36279 ? 269 HIS   A NE2 1 
ATOM   2091 N N   . VAL   A 1 290 ? 29.16055 14.35667 -10.44496 1.000 16.53777 ? 270 VAL   A N   1 
ATOM   2092 C CA  . VAL   A 1 290 ? 27.86800 14.94828 -10.04253 1.000 16.49504 ? 270 VAL   A CA  1 
ATOM   2093 C C   . VAL   A 1 290 ? 26.79182 13.91595 -10.35740 1.000 16.43407 ? 270 VAL   A C   1 
ATOM   2094 O O   . VAL   A 1 290 ? 26.10569 13.96770 -11.37675 1.000 17.81996 ? 270 VAL   A O   1 
ATOM   2095 C CB  . VAL   A 1 290 ? 27.62324 16.31484 -10.69100 1.000 17.43842 ? 270 VAL   A CB  1 
ATOM   2096 C CG1 . VAL   A 1 290 ? 26.36740 16.95901 -10.11002 1.000 18.54159 ? 270 VAL   A CG1 1 
ATOM   2097 C CG2 . VAL   A 1 290 ? 28.83435 17.20565 -10.46462 1.000 17.84671 ? 270 VAL   A CG2 1 
ATOM   2098 N N   . LEU   A 1 291 ? 26.60626 12.97249 -9.41961  1.000 17.06524 ? 271 LEU   A N   1 
ATOM   2099 C CA  . LEU   A 1 291 ? 25.75434 11.81148 -9.68684  1.000 16.54854 ? 271 LEU   A CA  1 
ATOM   2100 C C   . LEU   A 1 291 ? 24.28755 12.19247 -9.87543  1.000 18.22480 ? 271 LEU   A C   1 
ATOM   2101 O O   . LEU   A 1 291 ? 23.56576 11.51364 -10.61537 1.000 18.59602 ? 271 LEU   A O   1 
ATOM   2102 C CB  . LEU   A 1 291 ? 25.88513 10.80633 -8.55100  1.000 17.40781 ? 271 LEU   A CB  1 
ATOM   2103 C CG  . LEU   A 1 291 ? 27.27187 10.20822 -8.34090  1.000 17.39469 ? 271 LEU   A CG  1 
ATOM   2104 C CD1 . LEU   A 1 291 ? 27.26212 9.32471  -7.08825  1.000 17.45432 ? 271 LEU   A CD1 1 
ATOM   2105 C CD2 . LEU   A 1 291 ? 27.72497 9.40937  -9.57946  1.000 18.82998 ? 271 LEU   A CD2 1 
ATOM   2106 N N   . HIS   A 1 292 ? 23.82415 13.25920 -9.21218  1.000 16.94552 ? 272 HIS   A N   1 
ATOM   2107 C CA  . HIS   A 1 292 ? 22.44644 13.71105 -9.38058  1.000 16.78290 ? 272 HIS   A CA  1 
ATOM   2108 C C   . HIS   A 1 292 ? 22.25259 14.53251 -10.65328 1.000 17.68123 ? 272 HIS   A C   1 
ATOM   2109 O O   . HIS   A 1 292 ? 21.14043 15.00421 -10.91255 1.000 19.06870 ? 272 HIS   A O   1 
ATOM   2110 C CB  . HIS   A 1 292 ? 21.99974 14.50322 -8.15056  1.000 17.03241 ? 272 HIS   A CB  1 
ATOM   2111 C CG  . HIS   A 1 292 ? 22.93247 15.61892 -7.78692  1.000 17.39157 ? 272 HIS   A CG  1 
ATOM   2112 N ND1 . HIS   A 1 292 ? 24.21565 15.39603 -7.33168  1.000 17.69721 ? 272 HIS   A ND1 1 
ATOM   2113 C CD2 . HIS   A 1 292 ? 22.76161 16.96585 -7.79371  1.000 18.49696 ? 272 HIS   A CD2 1 
ATOM   2114 C CE1 . HIS   A 1 292 ? 24.79733 16.55732 -7.08406  1.000 18.31393 ? 272 HIS   A CE1 1 
ATOM   2115 N NE2 . HIS   A 1 292 ? 23.93523 17.52583 -7.35080  1.000 19.20830 ? 272 HIS   A NE2 1 
ATOM   2116 N N   . LYS   A 1 293 ? 23.30298 14.69095 -11.45540 1.000 17.11426 ? 273 LYS   A N   1 
ATOM   2117 C CA  . LYS   A 1 293 ? 23.25542 15.37302 -12.74575 1.000 17.98117 ? 273 LYS   A CA  1 
ATOM   2118 C C   . LYS   A 1 293 ? 24.08862 14.60877 -13.75341 1.000 18.60902 ? 273 LYS   A C   1 
ATOM   2119 O O   . LYS   A 1 293 ? 24.84549 15.19178 -14.53751 1.000 20.30061 ? 273 LYS   A O   1 
ATOM   2120 C CB  . LYS   A 1 293 ? 23.72241 16.82283 -12.61755 1.000 18.50154 ? 273 LYS   A CB  1 
ATOM   2121 C CG  . LYS   A 1 293 ? 22.84760 17.63953 -11.68116 1.000 17.19163 ? 273 LYS   A CG  1 
ATOM   2122 C CD  . LYS   A 1 293 ? 23.27522 19.10061 -11.63802 1.000 17.58311 ? 273 LYS   A CD  1 
ATOM   2123 C CE  . LYS   A 1 293 ? 22.49536 19.85014 -10.57910 1.000 19.21645 ? 273 LYS   A CE  1 
ATOM   2124 N NZ  . LYS   A 1 293 ? 21.01522 19.82893 -10.81363 1.000 20.39347 ? 273 LYS   A NZ  1 
ATOM   2125 N N   . GLU   A 1 294 ? 23.96132 13.28640 -13.73562 1.000 18.34427 ? 274 GLU   A N   1 
ATOM   2126 C CA  . GLU   A 1 294 ? 24.74161 12.39517 -14.57154 1.000 17.48689 ? 274 GLU   A CA  1 
ATOM   2127 C C   . GLU   A 1 294 ? 23.88870 11.91290 -15.75083 1.000 18.53937 ? 274 GLU   A C   1 
ATOM   2128 O O   . GLU   A 1 294 ? 22.87896 12.53968 -16.11070 1.000 20.15157 ? 274 GLU   A O   1 
ATOM   2129 C CB  . GLU   A 1 294 ? 25.30842 11.27182 -13.68756 1.000 19.06536 ? 274 GLU   A CB  1 
ATOM   2130 C CG  . GLU   A 1 294 ? 26.83112 11.22171 -13.63208 1.000 19.99436 ? 274 GLU   A CG  1 
ATOM   2131 C CD  . GLU   A 1 294 ? 27.43826 10.50003 -14.81594 1.000 21.29904 ? 274 GLU   A CD  1 
ATOM   2132 O OE1 . GLU   A 1 294 ? 26.70953 9.73212  -15.48091 1.000 22.04467 ? 274 GLU   A OE1 1 
ATOM   2133 O OE2 . GLU   A 1 294 ? 28.64641 10.70231 -15.08775 1.000 22.67274 ? 274 GLU   A OE2 1 
ATOM   2134 N N   . LEU   A 1 295 ? 24.30413 10.82095 -16.38587 1.000 19.65935 ? 275 LEU   A N   1 
ATOM   2135 C CA  . LEU   A 1 295 ? 23.46956 10.22583 -17.41555 1.000 20.05204 ? 275 LEU   A CA  1 
ATOM   2136 C C   . LEU   A 1 295 ? 22.13566 9.81862  -16.79401 1.000 21.31862 ? 275 LEU   A C   1 
ATOM   2137 O O   . LEU   A 1 295 ? 22.06985 9.51840  -15.59943 1.000 21.66781 ? 275 LEU   A O   1 
ATOM   2138 C CB  . LEU   A 1 295 ? 24.15537 9.00675  -18.02121 1.000 21.76773 ? 275 LEU   A CB  1 
ATOM   2139 C CG  . LEU   A 1 295 ? 25.49673 9.29455  -18.69624 1.000 22.31064 ? 275 LEU   A CG  1 
ATOM   2140 C CD1 . LEU   A 1 295 ? 26.08633 8.00200  -19.24097 1.000 23.31578 ? 275 LEU   A CD1 1 
ATOM   2141 C CD2 . LEU   A 1 295 ? 25.33934 10.33860 -19.80415 1.000 23.49933 ? 275 LEU   A CD2 1 
ATOM   2142 N N   . PRO   A 1 296 ? 21.05580 9.82513  -17.57722 1.000 23.66148 ? 276 PRO   A N   1 
ATOM   2143 C CA  . PRO   A 1 296 ? 19.72632 9.59379  -16.98819 1.000 25.38670 ? 276 PRO   A CA  1 
ATOM   2144 C C   . PRO   A 1 296 ? 19.60578 8.30071  -16.20226 1.000 26.17198 ? 276 PRO   A C   1 
ATOM   2145 O O   . PRO   A 1 296 ? 18.96104 8.29022  -15.14708 1.000 27.65785 ? 276 PRO   A O   1 
ATOM   2146 C CB  . PRO   A 1 296 ? 18.77982 9.64479  -18.19843 1.000 25.89450 ? 276 PRO   A CB  1 
ATOM   2147 C CG  . PRO   A 1 296 ? 19.65624 9.81326  -19.41718 1.000 27.65411 ? 276 PRO   A CG  1 
ATOM   2148 C CD  . PRO   A 1 296 ? 20.97850 10.30543 -18.96663 1.000 25.54308 ? 276 PRO   A CD  1 
ATOM   2149 N N   . GLU   A 1 297 ? 20.21257 7.20915  -16.67371 1.000 26.30021 ? 277 GLU   A N   1 
ATOM   2150 C CA  . GLU   A 1 297 ? 20.14681 5.95731  -15.91938 1.000 27.81580 ? 277 GLU   A CA  1 
ATOM   2151 C C   . GLU   A 1 297 ? 20.72571 6.12465  -14.51915 1.000 26.62516 ? 277 GLU   A C   1 
ATOM   2152 O O   . GLU   A 1 297 ? 20.20903 5.55408  -13.54911 1.000 28.77283 ? 277 GLU   A O   1 
ATOM   2153 C CB  . GLU   A 1 297 ? 20.88559 4.84474  -16.66457 1.000 33.12179 ? 277 GLU   A CB  1 
ATOM   2154 C CG  . GLU   A 1 297 ? 20.58002 4.76051  -18.14855 1.000 41.60868 ? 277 GLU   A CG  1 
ATOM   2155 C CD  . GLU   A 1 297 ? 21.58217 5.52868  -19.00224 1.000 46.24165 ? 277 GLU   A CD  1 
ATOM   2156 O OE1 . GLU   A 1 297 ? 21.53446 6.77417  -19.01464 1.000 44.57464 ? 277 GLU   A OE1 1 
ATOM   2157 O OE2 . GLU   A 1 297 ? 22.42324 4.87614  -19.66155 1.000 51.76017 ? 277 GLU   A OE2 1 
ATOM   2158 N N   . VAL   A 1 298 ? 21.79991 6.90369  -14.39497 1.000 22.99488 ? 278 VAL   A N   1 
ATOM   2159 C CA  . VAL   A 1 298 ? 22.42298 7.11566  -13.09173 1.000 21.08301 ? 278 VAL   A CA  1 
ATOM   2160 C C   . VAL   A 1 298 ? 21.56622 8.04360  -12.24658 1.000 21.09035 ? 278 VAL   A C   1 
ATOM   2161 O O   . VAL   A 1 298 ? 21.21877 7.73143  -11.10099 1.000 21.72048 ? 278 VAL   A O   1 
ATOM   2162 C CB  . VAL   A 1 298 ? 23.85065 7.66889  -13.26405 1.000 21.25022 ? 278 VAL   A CB  1 
ATOM   2163 C CG1 . VAL   A 1 298 ? 24.41647 8.13330  -11.92633 1.000 20.71511 ? 278 VAL   A CG1 1 
ATOM   2164 C CG2 . VAL   A 1 298 ? 24.76250 6.62831  -13.91373 1.000 23.00697 ? 278 VAL   A CG2 1 
ATOM   2165 N N   . THR   A 1 299 ? 21.19312 9.18878  -12.81317 1.000 20.95638 ? 279 THR   A N   1 
ATOM   2166 C CA  . THR   A 1 299 ? 20.42187 10.16695 -12.06307 1.000 21.42195 ? 279 THR   A CA  1 
ATOM   2167 C C   . THR   A 1 299 ? 19.09389 9.59100  -11.59186 1.000 22.57053 ? 279 THR   A C   1 
ATOM   2168 O O   . THR   A 1 299 ? 18.67747 9.83066  -10.45427 1.000 23.29507 ? 279 THR   A O   1 
ATOM   2169 C CB  . THR   A 1 299 ? 20.20932 11.39780 -12.93732 1.000 22.99010 ? 279 THR   A CB  1 
ATOM   2170 O OG1 . THR   A 1 299 ? 21.48683 11.95646 -13.24934 1.000 25.76829 ? 279 THR   A OG1 1 
ATOM   2171 C CG2 . THR   A 1 299 ? 19.37106 12.42931 -12.22041 1.000 24.94334 ? 279 THR   A CG2 1 
ATOM   2172 N N   . ASN   A 1 300 ? 18.41555 8.82184  -12.44480 1.000 22.83096 ? 280 ASN   A N   1 
ATOM   2173 C CA  . ASN   A 1 300 ? 17.15957 8.20827  -12.02037 1.000 25.00315 ? 280 ASN   A CA  1 
ATOM   2174 C C   . ASN   A 1 300 ? 17.37873 7.27680  -10.83762 1.000 22.99622 ? 280 ASN   A C   1 
ATOM   2175 O O   . ASN   A 1 300 ? 16.59815 7.28554  -9.87929  1.000 23.90464 ? 280 ASN   A O   1 
ATOM   2176 C CB  . ASN   A 1 300 ? 16.50400 7.45699  -13.18021 1.000 26.80366 ? 280 ASN   A CB  1 
ATOM   2177 C CG  . ASN   A 1 300 ? 15.97842 8.38822  -14.25011 1.000 33.15848 ? 280 ASN   A CG  1 
ATOM   2178 O OD1 . ASN   A 1 300 ? 15.76962 9.58223  -14.01284 1.000 36.51043 ? 280 ASN   A OD1 1 
ATOM   2179 N ND2 . ASN   A 1 300 ? 15.74810 7.84392  -15.43626 1.000 35.87326 ? 280 ASN   A ND2 1 
ATOM   2180 N N   . SER   A 1 301 ? 18.44428 6.47317  -10.88046 1.000 21.82312 ? 281 SER   A N   1 
ATOM   2181 C CA  . SER   A 1 301 ? 18.74657 5.59268  -9.75773  1.000 20.27350 ? 281 SER   A CA  1 
ATOM   2182 C C   . SER   A 1 301 ? 19.06438 6.39293  -8.50515  1.000 19.94479 ? 281 SER   A C   1 
ATOM   2183 O O   . SER   A 1 301 ? 18.57293 6.07473  -7.41862  1.000 21.49558 ? 281 SER   A O   1 
ATOM   2184 C CB  . SER   A 1 301 ? 19.91513 4.67860  -10.11311 1.000 21.10445 ? 281 SER   A CB  1 
ATOM   2185 O OG  . SER   A 1 301 ? 20.41097 4.02356  -8.95658  1.000 22.47885 ? 281 SER   A OG  1 
ATOM   2186 N N   . VAL   A 1 302 ? 19.87932 7.44299  -8.64379  1.000 20.46119 ? 282 VAL   A N   1 
ATOM   2187 C CA  . VAL   A 1 302 ? 20.23060 8.29126  -7.50525  1.000 19.55186 ? 282 VAL   A CA  1 
ATOM   2188 C C   . VAL   A 1 302 ? 18.97638 8.83452  -6.82851  1.000 19.76991 ? 282 VAL   A C   1 
ATOM   2189 O O   . VAL   A 1 302 ? 18.82545 8.74446  -5.60404  1.000 19.99105 ? 282 VAL   A O   1 
ATOM   2190 C CB  . VAL   A 1 302 ? 21.18269 9.41714  -7.95387  1.000 19.26226 ? 282 VAL   A CB  1 
ATOM   2191 C CG1 . VAL   A 1 302 ? 21.28121 10.51255 -6.88750  1.000 19.72486 ? 282 VAL   A CG1 1 
ATOM   2192 C CG2 . VAL   A 1 302 ? 22.56851 8.83629  -8.26574  1.000 18.81057 ? 282 VAL   A CG2 1 
ATOM   2193 N N   . PHE   A 1 303 ? 18.05637 9.40726  -7.61408  1.000 19.98898 ? 283 PHE   A N   1 
ATOM   2194 C CA  . PHE   A 1 303 ? 16.82870 9.94407  -7.02895  1.000 20.58472 ? 283 PHE   A CA  1 
ATOM   2195 C C   . PHE   A 1 303 ? 16.02678 8.84525  -6.34789  1.000 21.61679 ? 283 PHE   A C   1 
ATOM   2196 O O   . PHE   A 1 303 ? 15.51365 9.03660  -5.24080  1.000 21.88392 ? 283 PHE   A O   1 
ATOM   2197 C CB  . PHE   A 1 303 ? 15.98005 10.61757 -8.10671  1.000 21.21088 ? 283 PHE   A CB  1 
ATOM   2198 C CG  . PHE   A 1 303 ? 16.34326 12.05272 -8.36343  1.000 21.31728 ? 283 PHE   A CG  1 
ATOM   2199 C CD1 . PHE   A 1 303 ? 17.59194 12.39062 -8.84506  1.000 21.80183 ? 283 PHE   A CD1 1 
ATOM   2200 C CD2 . PHE   A 1 303 ? 15.41897 13.05990 -8.12802  1.000 21.22168 ? 283 PHE   A CD2 1 
ATOM   2201 C CE1 . PHE   A 1 303 ? 17.92812 13.72976 -9.08667  1.000 23.06600 ? 283 PHE   A CE1 1 
ATOM   2202 C CE2 . PHE   A 1 303 ? 15.74157 14.39700 -8.35742  1.000 22.60469 ? 283 PHE   A CE2 1 
ATOM   2203 C CZ  . PHE   A 1 303 ? 16.99536 14.72887 -8.84585  1.000 24.11045 ? 283 PHE   A CZ  1 
ATOM   2204 N N   . HIS   A 1 304 ? 15.91996 7.68092  -6.99884  1.000 21.71109 ? 284 HIS   A N   1 
ATOM   2205 C CA  . HIS   A 1 304 ? 15.16463 6.56682  -6.44197  1.000 23.39725 ? 284 HIS   A CA  1 
ATOM   2206 C C   . HIS   A 1 304 ? 15.77780 6.08097  -5.13242  1.000 22.96524 ? 284 HIS   A C   1 
ATOM   2207 O O   . HIS   A 1 304 ? 15.06067 5.83284  -4.15383  1.000 23.26413 ? 284 HIS   A O   1 
ATOM   2208 C CB  . HIS   A 1 304 ? 15.12803 5.43435  -7.46955  1.000 27.68762 ? 284 HIS   A CB  1 
ATOM   2209 C CG  . HIS   A 1 304 ? 14.45419 4.19169  -6.98365  1.000 37.45031 ? 284 HIS   A CG  1 
ATOM   2210 N ND1 . HIS   A 1 304 ? 13.08333 4.07426  -6.90131  1.000 43.47243 ? 284 HIS   A ND1 1 
ATOM   2211 C CD2 . HIS   A 1 304 ? 14.96071 3.00717  -6.56457  1.000 42.42546 ? 284 HIS   A CD2 1 
ATOM   2212 C CE1 . HIS   A 1 304 ? 12.77350 2.86940  -6.45323  1.000 45.73387 ? 284 HIS   A CE1 1 
ATOM   2213 N NE2 . HIS   A 1 304 ? 13.89456 2.20285  -6.23970  1.000 45.71270 ? 284 HIS   A NE2 1 
ATOM   2214 N N   . GLU   A 1 305 ? 17.10550 5.95329  -5.09043  1.000 21.09427 ? 285 GLU   A N   1 
ATOM   2215 C CA  . GLU   A 1 305 ? 17.75822 5.43530  -3.89412  1.000 20.77413 ? 285 GLU   A CA  1 
ATOM   2216 C C   . GLU   A 1 305 ? 17.63952 6.40596  -2.72568  1.000 19.41616 ? 285 GLU   A C   1 
ATOM   2217 O O   . GLU   A 1 305 ? 17.45486 5.98210  -1.57605  1.000 20.71620 ? 285 GLU   A O   1 
ATOM   2218 C CB  . GLU   A 1 305 ? 19.22611 5.12178  -4.18294  1.000 24.39584 ? 285 GLU   A CB  1 
ATOM   2219 C CG  . GLU   A 1 305 ? 19.45171 4.00656  -5.20225  1.000 26.99414 ? 285 GLU   A CG  1 
ATOM   2220 C CD  . GLU   A 1 305 ? 18.99495 2.63716  -4.71783  1.000 30.36792 ? 285 GLU   A CD  1 
ATOM   2221 O OE1 . GLU   A 1 305 ? 18.82568 2.44122  -3.49222  1.000 30.80714 ? 285 GLU   A OE1 1 
ATOM   2222 O OE2 . GLU   A 1 305 ? 18.79981 1.75112  -5.57602  1.000 33.45737 ? 285 GLU   A OE2 1 
ATOM   2223 N N   . ILE   A 1 306 ? 17.75936 7.71249  -2.99276  1.000 19.39752 ? 286 ILE   A N   1 
ATOM   2224 C CA  . ILE   A 1 306 ? 17.59808 8.68580  -1.91947  1.000 19.58529 ? 286 ILE   A CA  1 
ATOM   2225 C C   . ILE   A 1 306 ? 16.16404 8.67669  -1.41415  1.000 20.65692 ? 286 ILE   A C   1 
ATOM   2226 O O   . ILE   A 1 306 ? 15.91615 8.71249  -0.20144  1.000 21.69990 ? 286 ILE   A O   1 
ATOM   2227 C CB  . ILE   A 1 306 ? 18.03227 10.07990 -2.40525  1.000 19.69346 ? 286 ILE   A CB  1 
ATOM   2228 C CG1 . ILE   A 1 306 ? 19.53148 10.08274 -2.74040  1.000 19.18576 ? 286 ILE   A CG1 1 
ATOM   2229 C CG2 . ILE   A 1 306 ? 17.67608 11.15427 -1.36440  1.000 21.16210 ? 286 ILE   A CG2 1 
ATOM   2230 C CD1 . ILE   A 1 306 ? 20.02682 11.36677 -3.44989  1.000 20.14102 ? 286 ILE   A CD1 1 
ATOM   2231 N N   . ASN   A 1 307 ? 15.20142 8.64753  -2.33826  1.000 21.41220 ? 287 ASN   A N   1 
ATOM   2232 C CA  . ASN   A 1 307 ? 13.79361 8.57429  -1.96655  1.000 23.76404 ? 287 ASN   A CA  1 
ATOM   2233 C C   . ASN   A 1 307 ? 13.54894 7.41537  -1.00693  1.000 25.20642 ? 287 ASN   A C   1 
ATOM   2234 O O   . ASN   A 1 307 ? 12.98206 7.59117  0.07961   1.000 26.02024 ? 287 ASN   A O   1 
ATOM   2235 C CB  . ASN   A 1 307 ? 12.96981 8.40518  -3.24770  1.000 25.24918 ? 287 ASN   A CB  1 
ATOM   2236 C CG  . ASN   A 1 307 ? 11.46963 8.32140  -2.99597  1.000 31.09204 ? 287 ASN   A CG  1 
ATOM   2237 O OD1 . ASN   A 1 307 ? 10.99995 7.58607  -2.12751  1.000 33.62639 ? 287 ASN   A OD1 1 
ATOM   2238 N ND2 . ASN   A 1 307 ? 10.70849 9.07514  -3.77712  1.000 33.80273 ? 287 ASN   A ND2 1 
ATOM   2239 N N   . MET   A 1 308 ? 13.98741 6.21991  -1.39256  1.000 24.33886 ? 288 MET   A N   1 
ATOM   2240 C CA  . MET   A 1 308 ? 13.72164 5.03817  -0.58468  1.000 24.23522 ? 288 MET   A CA  1 
ATOM   2241 C C   . MET   A 1 308 ? 14.42982 5.11480  0.76065   1.000 23.90296 ? 288 MET   A C   1 
ATOM   2242 O O   . MET   A 1 308 ? 13.84586 4.76702  1.79870   1.000 25.22482 ? 288 MET   A O   1 
ATOM   2243 C CB  . MET   A 1 308 ? 14.18554 3.81001  -1.35046  1.000 27.59523 ? 288 MET   A CB  1 
ATOM   2244 C CG  . MET   A 1 308 ? 13.45104 3.59182  -2.66425  1.000 35.87273 ? 288 MET   A CG  1 
ATOM   2245 S SD  . MET   A 1 308 ? 13.56411 1.85096  -3.06270  1.000 43.35033 ? 288 MET   A SD  1 
ATOM   2246 C CE  . MET   A 1 308 ? 13.86101 1.29395  -1.38604  1.000 43.85204 ? 288 MET   A CE  1 
ATOM   2247 N N   . TRP   A 1 309 ? 15.68758 5.56937  0.76186   1.000 22.42403 ? 289 TRP   A N   1 
ATOM   2248 C CA  . TRP   A 1 309 ? 16.46827 5.57603  1.99217   1.000 21.43584 ? 289 TRP   A CA  1 
ATOM   2249 C C   . TRP   A 1 309 ? 15.88505 6.56690  2.99512   1.000 22.16724 ? 289 TRP   A C   1 
ATOM   2250 O O   . TRP   A 1 309 ? 15.73871 6.25336  4.18484   1.000 22.17031 ? 289 TRP   A O   1 
ATOM   2251 C CB  . TRP   A 1 309 ? 17.92658 5.90911  1.66156   1.000 20.31393 ? 289 TRP   A CB  1 
ATOM   2252 C CG  . TRP   A 1 309 ? 18.89046 5.69073  2.79949   1.000 20.31994 ? 289 TRP   A CG  1 
ATOM   2253 C CD1 . TRP   A 1 309 ? 19.62174 4.55656  3.05186   1.000 19.70503 ? 289 TRP   A CD1 1 
ATOM   2254 C CD2 . TRP   A 1 309 ? 19.24522 6.63182  3.82497   1.000 19.86546 ? 289 TRP   A CD2 1 
ATOM   2255 N NE1 . TRP   A 1 309 ? 20.40208 4.73390  4.17132   1.000 19.92650 ? 289 TRP   A NE1 1 
ATOM   2256 C CE2 . TRP   A 1 309 ? 20.18695 5.99348  4.67043   1.000 19.04251 ? 289 TRP   A CE2 1 
ATOM   2257 C CE3 . TRP   A 1 309 ? 18.86319 7.95238  4.11007   1.000 20.19964 ? 289 TRP   A CE3 1 
ATOM   2258 C CZ2 . TRP   A 1 309 ? 20.74564 6.62788  5.78238   1.000 19.45292 ? 289 TRP   A CZ2 1 
ATOM   2259 C CZ3 . TRP   A 1 309 ? 19.41892 8.57932  5.21711   1.000 19.45492 ? 289 TRP   A CZ3 1 
ATOM   2260 C CH2 . TRP   A 1 309 ? 20.34538 7.91861  6.03951   1.000 21.05834 ? 289 TRP   A CH2 1 
ATOM   2261 N N   . VAL   A 1 310 ? 15.51406 7.75737  2.52702   1.000 21.32921 ? 290 VAL   A N   1 
ATOM   2262 C CA  . VAL   A 1 310 ? 14.93486 8.75742  3.42237   1.000 23.40871 ? 290 VAL   A CA  1 
ATOM   2263 C C   . VAL   A 1 310 ? 13.54148 8.33465  3.86867   1.000 25.75242 ? 290 VAL   A C   1 
ATOM   2264 O O   . VAL   A 1 310 ? 13.16193 8.53290  5.03084   1.000 26.87222 ? 290 VAL   A O   1 
ATOM   2265 C CB  . VAL   A 1 310 ? 14.94242 10.14390 2.75338   1.000 22.78719 ? 290 VAL   A CB  1 
ATOM   2266 C CG1 . VAL   A 1 310 ? 14.23794 11.16239 3.63718   1.000 24.92450 ? 290 VAL   A CG1 1 
ATOM   2267 C CG2 . VAL   A 1 310 ? 16.37050 10.57563 2.46908   1.000 21.92994 ? 290 VAL   A CG2 1 
ATOM   2268 N N   . SER   A 1 311 ? 12.76395 7.73360  2.96001   1.000 27.01430 ? 291 SER   A N   1 
ATOM   2269 C CA  . SER   A 1 311 ? 11.42509 7.26743  3.31329   1.000 30.56902 ? 291 SER   A CA  1 
ATOM   2270 C C   . SER   A 1 311 ? 11.48074 6.26516  4.45422   1.000 31.44450 ? 291 SER   A C   1 
ATOM   2271 O O   . SER   A 1 311 ? 10.73246 6.37753  5.43321   1.000 33.41976 ? 291 SER   A O   1 
ATOM   2272 C CB  . SER   A 1 311 ? 10.75270 6.61807  2.10370   1.000 33.65488 ? 291 SER   A CB  1 
ATOM   2273 O OG  . SER   A 1 311 ? 10.42686 7.57600  1.11834   1.000 38.52506 ? 291 SER   A OG  1 
ATOM   2274 N N   . GLN   A 1 312 ? 12.35187 5.26220  4.33119   1.000 31.69409 ? 292 GLN   A N   1 
ATOM   2275 C CA  . GLN   A 1 312 ? 12.44646 4.22114  5.35009   1.000 33.92527 ? 292 GLN   A CA  1 
ATOM   2276 C C   . GLN   A 1 312 ? 12.79595 4.79791  6.70620   1.000 33.21508 ? 292 GLN   A C   1 
ATOM   2277 O O   . GLN   A 1 312 ? 12.39406 4.25107  7.73416   1.000 34.43821 ? 292 GLN   A O   1 
ATOM   2278 C CB  . GLN   A 1 312 ? 13.54126 3.23350  4.98237   1.000 39.49868 ? 292 GLN   A CB  1 
ATOM   2279 C CG  . GLN   A 1 312 ? 13.11046 2.10200  4.11509   1.000 48.14839 ? 292 GLN   A CG  1 
ATOM   2280 C CD  . GLN   A 1 312 ? 14.17354 1.77429  3.11163   1.000 53.60988 ? 292 GLN   A CD  1 
ATOM   2281 O OE1 . GLN   A 1 312 ? 15.36430 1.70609  3.44097   1.000 55.70659 ? 292 GLN   A OE1 1 
ATOM   2282 N NE2 . GLN   A 1 312 ? 13.76202 1.60788  1.86103   1.000 57.82142 ? 292 GLN   A NE2 1 
ATOM   2283 N N   . ARG   A 1 313 ? 13.56491 5.87765  6.73334   1.000 30.68427 ? 293 ARG   A N   1 
ATOM   2284 C CA  . ARG   A 1 313 ? 14.05746 6.41970  7.98593   1.000 28.01678 ? 293 ARG   A CA  1 
ATOM   2285 C C   . ARG   A 1 313 ? 13.20898 7.55551  8.52074   1.000 31.78314 ? 293 ARG   A C   1 
ATOM   2286 O O   . ARG   A 1 313 ? 13.45517 8.02555  9.63176   1.000 33.15290 ? 293 ARG   A O   1 
ATOM   2287 C CB  . ARG   A 1 313 ? 15.52511 6.81750  7.84006   1.000 25.74035 ? 293 ARG   A CB  1 
ATOM   2288 C CG  . ARG   A 1 313 ? 16.38371 5.57302  7.81728   1.000 23.79261 ? 293 ARG   A CG  1 
ATOM   2289 C CD  . ARG   A 1 313 ? 17.75092 5.76796  7.22723   1.000 23.53021 ? 293 ARG   A CD  1 
ATOM   2290 N NE  . ARG   A 1 313 ? 18.44208 4.48280  7.15709   1.000 24.08334 ? 293 ARG   A NE  1 
ATOM   2291 C CZ  . ARG   A 1 313 ? 18.25880 3.58753  6.19417   1.000 24.38029 ? 293 ARG   A CZ  1 
ATOM   2292 N NH1 . ARG   A 1 313 ? 17.39824 3.79841  5.20776   1.000 25.81617 ? 293 ARG   A NH1 1 
ATOM   2293 N NH2 . ARG   A 1 313 ? 18.94898 2.44699  6.22497   1.000 24.41197 ? 293 ARG   A NH2 1 
ATOM   2294 N N   . THR   A 1 314 ? 12.20656 7.99088  7.77278   1.000 36.12827 ? 294 THR   A N   1 
ATOM   2295 C CA  . THR   A 1 314 ? 11.23623 8.92444  8.32270   1.000 40.94217 ? 294 THR   A CA  1 
ATOM   2296 C C   . THR   A 1 314 ? 10.01487 8.20103  8.86110   1.000 47.75630 ? 294 THR   A C   1 
ATOM   2297 O O   . THR   A 1 314 ? 9.36978  8.69291  9.79555   1.000 51.51603 ? 294 THR   A O   1 
ATOM   2298 C CB  . THR   A 1 314 ? 10.83572 9.95973  7.26970   1.000 38.93312 ? 294 THR   A CB  1 
ATOM   2299 O OG1 . THR   A 1 314 ? 10.40585 9.29127  6.07505   1.000 42.44339 ? 294 THR   A OG1 1 
ATOM   2300 C CG2 . THR   A 1 314 ? 12.01688 10.83018 6.93449   1.000 35.18783 ? 294 THR   A CG2 1 
ATOM   2301 N N   . ALA   A 1 315 ? 9.70027  7.03833  8.30544   1.000 51.77519 ? 295 ALA   A N   1 
ATOM   2302 C CA  . ALA   A 1 315 ? 8.67417  6.17353  8.86191   1.000 56.96828 ? 295 ALA   A CA  1 
ATOM   2303 C C   . ALA   A 1 315 ? 9.19473  5.50714  10.13471  1.000 60.19858 ? 295 ALA   A C   1 
ATOM   2304 O O   . ALA   A 1 315 ? 10.40303 5.31388  10.29955  1.000 61.36364 ? 295 ALA   A O   1 
ATOM   2305 C CB  . ALA   A 1 315 ? 8.26097  5.12556  7.84364   1.000 57.06286 ? 295 ALA   A CB  1 
HETATM 2306 N N1  . A1IIH B 2 .   ? 40.41382 19.64603 -9.60486  1.000 23.14897 ? 401 A1IIH A N1  1 
HETATM 2307 C C7  . A1IIH B 2 .   ? 42.76447 14.52358 -12.79302 1.000 33.83008 ? 401 A1IIH A C7  1 
HETATM 2308 C C8  . A1IIH B 2 .   ? 41.87497 15.42761 -12.23833 1.000 32.82155 ? 401 A1IIH A C8  1 
HETATM 2309 N N2  . A1IIH B 2 .   ? 34.03370 20.51520 -5.39803  1.000 16.70995 ? 401 A1IIH A N2  1 
HETATM 2310 C C9  . A1IIH B 2 .   ? 42.42360 16.68524 -12.36312 1.000 31.62674 ? 401 A1IIH A C9  1 
HETATM 2311 O O1  . A1IIH B 2 .   ? 40.32973 20.35262 -6.76577  1.000 23.71782 ? 401 A1IIH A O1  1 
HETATM 2312 C C1  . A1IIH B 2 .   ? 47.20361 15.57897 -15.01211 1.000 36.91231 ? 401 A1IIH A C1  1 
HETATM 2313 C C5  . A1IIH B 2 .   ? 45.01909 14.85424 -13.93034 1.000 34.99987 ? 401 A1IIH A C5  1 
HETATM 2314 C C6  . A1IIH B 2 .   ? 43.84926 15.24662 -13.25425 1.000 33.89253 ? 401 A1IIH A C6  1 
HETATM 2315 N N3  . A1IIH B 2 .   ? 31.86934 20.48563 -6.19603  1.000 17.07694 ? 401 A1IIH A N3  1 
HETATM 2316 C C4  . A1IIH B 2 .   ? 45.97363 15.75592 -14.32804 1.000 35.70330 ? 401 A1IIH A C4  1 
HETATM 2317 O O4  . A1IIH B 2 .   ? 27.54163 20.17282 -9.53161  1.000 20.12703 ? 401 A1IIH A O4  1 
HETATM 2318 C C3  . A1IIH B 2 .   ? 46.86510 17.75754 -14.59311 1.000 38.13574 ? 401 A1IIH A C3  1 
HETATM 2319 O O3  . A1IIH B 2 .   ? 28.93045 21.89501 -9.18971  1.000 18.23829 ? 401 A1IIH A O3  1 
HETATM 2320 C C2  . A1IIH B 2 .   ? 47.73586 16.83029 -15.17174 1.000 36.50408 ? 401 A1IIH A C2  1 
HETATM 2321 N N4  . A1IIH B 2 .   ? 29.49019 19.93601 -8.33690  1.000 17.19693 ? 401 A1IIH A N4  1 
HETATM 2322 N N   . A1IIH B 2 .   ? 45.79801 17.11207 -14.07321 1.000 36.70003 ? 401 A1IIH A N   1 
HETATM 2323 C C   . A1IIH B 2 .   ? 47.79095 14.26049 -15.43255 1.000 38.49090 ? 401 A1IIH A C   1 
HETATM 2324 O O   . A1IIH B 2 .   ? 39.31556 19.94852 -11.53912 1.000 26.16823 ? 401 A1IIH A O   1 
HETATM 2325 B B   . A1IIH B 2 .   ? 44.60872 17.73554 -13.30618 1.000 37.15067 ? 401 A1IIH A B   1 
HETATM 2326 C C10 . A1IIH B 2 .   ? 41.85411 18.00671 -11.95022 1.000 30.19114 ? 401 A1IIH A C10 1 
HETATM 2327 C C11 . A1IIH B 2 .   ? 40.51677 17.90504 -11.26373 1.000 26.94421 ? 401 A1IIH A C11 1 
HETATM 2328 C C12 . A1IIH B 2 .   ? 40.02304 19.25655 -10.81540 1.000 23.76158 ? 401 A1IIH A C12 1 
HETATM 2329 C C13 . A1IIH B 2 .   ? 40.02191 20.92621 -9.03792  1.000 24.48029 ? 401 A1IIH A C13 1 
HETATM 2330 C C14 . A1IIH B 2 .   ? 40.79272 21.24374 -7.79054  1.000 24.83297 ? 401 A1IIH A C14 1 
HETATM 2331 C C15 . A1IIH B 2 .   ? 40.83514 20.52366 -5.50670  1.000 23.35150 ? 401 A1IIH A C15 1 
HETATM 2332 C C16 . A1IIH B 2 .   ? 41.76835 21.49816 -5.18635  1.000 24.81215 ? 401 A1IIH A C16 1 
HETATM 2333 C C17 . A1IIH B 2 .   ? 42.21703 21.60916 -3.88099  1.000 25.80017 ? 401 A1IIH A C17 1 
HETATM 2334 C C18 . A1IIH B 2 .   ? 41.74143 20.75953 -2.90848  1.000 24.29773 ? 401 A1IIH A C18 1 
HETATM 2335 C C19 . A1IIH B 2 .   ? 40.80892 19.78625 -3.23070  1.000 22.36396 ? 401 A1IIH A C19 1 
HETATM 2336 C C20 . A1IIH B 2 .   ? 40.33758 19.65280 -4.53282  1.000 21.90069 ? 401 A1IIH A C20 1 
HETATM 2337 C C21 . A1IIH B 2 .   ? 39.27060 18.63836 -4.86871  1.000 19.66694 ? 401 A1IIH A C21 1 
HETATM 2338 C C22 . A1IIH B 2 .   ? 37.86214 19.17321 -4.58789  1.000 17.84738 ? 401 A1IIH A C22 1 
HETATM 2339 C C23 . A1IIH B 2 .   ? 36.62930 18.29581 -4.90931  1.000 17.55650 ? 401 A1IIH A C23 1 
HETATM 2340 C C24 . A1IIH B 2 .   ? 35.92641 19.61941 -5.26846  1.000 16.78806 ? 401 A1IIH A C24 1 
HETATM 2341 C C25 . A1IIH B 2 .   ? 37.30887 20.21990 -5.58458  1.000 17.12594 ? 401 A1IIH A C25 1 
HETATM 2342 C C26 . A1IIH B 2 .   ? 34.78200 19.63964 -6.30507  1.000 17.45025 ? 401 A1IIH A C26 1 
HETATM 2343 C C27 . A1IIH B 2 .   ? 34.96892 20.33243 -4.28667  1.000 17.01673 ? 401 A1IIH A C27 1 
HETATM 2344 C C28 . A1IIH B 2 .   ? 32.70457 20.65018 -5.14863  1.000 16.38596 ? 401 A1IIH A C28 1 
HETATM 2345 C C29 . A1IIH B 2 .   ? 30.47636 20.94213 -6.20932  1.000 16.43498 ? 401 A1IIH A C29 1 
HETATM 2346 C C30 . A1IIH B 2 .   ? 30.50043 20.81876 -7.75389  1.000 16.65402 ? 401 A1IIH A C30 1 
HETATM 2347 C C31 . A1IIH B 2 .   ? 30.21361 22.10240 -8.54790  1.000 18.70226 ? 401 A1IIH A C31 1 
HETATM 2348 C C32 . A1IIH B 2 .   ? 28.57781 20.59053 -9.06727  1.000 17.79903 ? 401 A1IIH A C32 1 
HETATM 2349 C C33 . A1IIH B 2 .   ? 31.98808 20.40329 -7.65688  1.000 18.53810 ? 401 A1IIH A C33 1 
HETATM 2350 C C34 . A1IIH B 2 .   ? 47.02456 19.24676 -14.52720 1.000 39.77963 ? 401 A1IIH A C34 1 
HETATM 2351 F F   . A1IIH B 2 .   ? 45.06303 18.31503 -12.13349 1.000 38.49773 ? 401 A1IIH A F   1 
HETATM 2352 F F1  . A1IIH B 2 .   ? 43.97721 18.69666 -14.08497 1.000 39.32857 ? 401 A1IIH A F1  1 
HETATM 2353 N N5  . A1IIH B 2 .   ? 43.62991 16.58328 -12.97298 1.000 33.81746 ? 401 A1IIH A N5  1 
HETATM 2354 O O2  . A1IIH B 2 .   ? 32.28405 20.89914 -4.03234  1.000 16.96911 ? 401 A1IIH A O2  1 
HETATM 2355 C C1  . EDO   C 3 .   ? 29.14829 33.72057 -9.05515  1.000 38.40265 ? 402 EDO   A C1  1 
HETATM 2356 O O1  . EDO   C 3 .   ? 30.47503 34.19630 -9.10816  1.000 60.05291 ? 402 EDO   A O1  1 
HETATM 2357 C C2  . EDO   C 3 .   ? 28.61589 33.81724 -7.64696  1.000 32.86587 ? 402 EDO   A C2  1 
HETATM 2358 O O2  . EDO   C 3 .   ? 28.29129 35.15940 -7.34474  1.000 38.43634 ? 402 EDO   A O2  1 
HETATM 2359 C C1  . EDO   D 3 .   ? 39.44201 6.81501  -8.49942  1.000 42.26505 ? 403 EDO   A C1  1 
HETATM 2360 O O1  . EDO   D 3 .   ? 40.38576 7.83003  -8.24439  1.000 64.22531 ? 403 EDO   A O1  1 
HETATM 2361 C C2  . EDO   D 3 .   ? 38.18330 7.41871  -9.06515  1.000 31.96689 ? 403 EDO   A C2  1 
HETATM 2362 O O2  . EDO   D 3 .   ? 37.50752 8.17667  -8.08476  1.000 22.41291 ? 403 EDO   A O2  1 
HETATM 2363 C C1  . EDO   E 3 .   ? 36.53725 24.81260 -16.31567 1.000 43.46589 ? 404 EDO   A C1  1 
HETATM 2364 O O1  . EDO   E 3 .   ? 36.04498 23.71506 -17.05033 1.000 33.15818 ? 404 EDO   A O1  1 
HETATM 2365 C C2  . EDO   E 3 .   ? 35.40145 25.76258 -16.04367 1.000 37.29317 ? 404 EDO   A C2  1 
HETATM 2366 O O2  . EDO   E 3 .   ? 34.54968 25.80179 -17.16746 1.000 45.54336 ? 404 EDO   A O2  1 
HETATM 2367 C C1  . EDO   F 3 .   ? 11.11771 29.48757 6.74646   1.000 45.98425 ? 405 EDO   A C1  1 
HETATM 2368 O O1  . EDO   F 3 .   ? 10.91893 30.73667 7.36706   1.000 51.80156 ? 405 EDO   A O1  1 
HETATM 2369 C C2  . EDO   F 3 .   ? 10.54678 28.40536 7.62431   1.000 50.57739 ? 405 EDO   A C2  1 
HETATM 2370 O O2  . EDO   F 3 .   ? 9.21024  28.71980 7.93663   1.000 69.32569 ? 405 EDO   A O2  1 
HETATM 2371 C C1  . EDO   G 3 .   ? 18.93675 16.58390 -13.76515 1.000 58.36238 ? 406 EDO   A C1  1 
HETATM 2372 O O1  . EDO   G 3 .   ? 19.55833 17.75244 -13.27323 1.000 55.73164 ? 406 EDO   A O1  1 
HETATM 2373 C C2  . EDO   G 3 .   ? 18.13393 15.93699 -12.66961 1.000 48.36910 ? 406 EDO   A C2  1 
HETATM 2374 O O2  . EDO   G 3 .   ? 17.90504 16.87906 -11.64275 1.000 41.33054 ? 406 EDO   A O2  1 
HETATM 2375 C C1  . EDO   H 3 .   ? 19.59711 0.08481  -9.01750  1.000 39.61383 ? 407 EDO   A C1  1 
HETATM 2376 O O1  . EDO   H 3 .   ? 20.74863 0.63355  -9.62097  1.000 37.23489 ? 407 EDO   A O1  1 
HETATM 2377 C C2  . EDO   H 3 .   ? 18.44667 1.05333  -9.05166  1.000 96.96351 ? 407 EDO   A C2  1 
HETATM 2378 O O2  . EDO   H 3 .   ? 18.75511 2.14224  -8.21717  1.000 29.16823 ? 407 EDO   A O2  1 
HETATM 2379 C C1  . EDO   I 3 .   ? 30.80231 19.70471 -24.04307 1.000 60.78945 ? 408 EDO   A C1  1 
HETATM 2380 O O1  . EDO   I 3 .   ? 29.94464 19.65734 -22.92382 1.000 48.69866 ? 408 EDO   A O1  1 
HETATM 2381 C C2  . EDO   I 3 .   ? 30.45869 20.89308 -24.90649 1.000 60.85559 ? 408 EDO   A C2  1 
HETATM 2382 O O2  . EDO   I 3 .   ? 29.09814 20.84303 -25.27689 1.000 52.56710 ? 408 EDO   A O2  1 
HETATM 2383 C C1  . EDO   J 3 .   ? 15.27649 30.97687 9.32308   1.000 59.92842 ? 409 EDO   A C1  1 
HETATM 2384 O O1  . EDO   J 3 .   ? 14.00933 31.50882 9.00816   1.000 72.97632 ? 409 EDO   A O1  1 
HETATM 2385 C C2  . EDO   J 3 .   ? 15.15885 29.48641 9.51108   1.000 47.28816 ? 409 EDO   A C2  1 
HETATM 2386 O O2  . EDO   J 3 .   ? 14.24495 29.20414 10.54654  1.000 42.74629 ? 409 EDO   A O2  1 
HETATM 2387 O O   . HOH   K 4 .   ? 19.67193 17.15087 -10.16191 1.000 22.21873 ? 501 HOH   A O   1 
HETATM 2388 O O   . HOH   K 4 .   ? 4.30466  23.10039 5.23338   1.000 52.70287 ? 502 HOH   A O   1 
HETATM 2389 O O   . HOH   K 4 .   ? 13.58426 30.08201 14.29724  1.000 47.22429 ? 503 HOH   A O   1 
HETATM 2390 O O   . HOH   K 4 .   ? 24.09884 4.77750  12.25978  1.000 25.65290 ? 504 HOH   A O   1 
HETATM 2391 O O   . HOH   K 4 .   ? 11.47425 31.22644 18.02427  1.000 40.43142 ? 505 HOH   A O   1 
HETATM 2392 O O   . HOH   K 4 .   ? 26.00111 43.12967 0.27816   1.000 38.21646 ? 506 HOH   A O   1 
HETATM 2393 O O   . HOH   K 4 .   ? 29.44687 11.81853 -22.48800 1.000 49.37923 ? 507 HOH   A O   1 
HETATM 2394 O O   . HOH   K 4 .   ? 14.60833 10.94160 -12.20152 1.000 55.98814 ? 508 HOH   A O   1 
HETATM 2395 O O   . HOH   K 4 .   ? 6.75332  20.45868 14.84199  1.000 57.56251 ? 509 HOH   A O   1 
HETATM 2396 O O   . HOH   K 4 .   ? 30.33589 23.53105 -21.75921 1.000 31.57439 ? 510 HOH   A O   1 
HETATM 2397 O O   . HOH   K 4 .   ? 34.43303 -0.64891 9.47512   1.000 26.64627 ? 511 HOH   A O   1 
HETATM 2398 O O   . HOH   K 4 .   ? 21.77022 1.40046  -11.86625 1.000 56.13935 ? 512 HOH   A O   1 
HETATM 2399 O O   . HOH   K 4 .   ? 17.60636 7.01627  10.77932  1.000 47.55966 ? 513 HOH   A O   1 
HETATM 2400 O O   . HOH   K 4 .   ? 16.85609 31.78167 14.36655  1.000 40.46708 ? 514 HOH   A O   1 
HETATM 2401 O O   . HOH   K 4 .   ? 33.48222 34.62590 1.34646   1.000 23.99946 ? 515 HOH   A O   1 
HETATM 2402 O O   . HOH   K 4 .   ? 26.62994 31.54991 11.96974  1.000 19.68077 ? 516 HOH   A O   1 
HETATM 2403 O O   . HOH   K 4 .   ? 35.63374 3.27835  -13.40956 1.000 48.66150 ? 517 HOH   A O   1 
HETATM 2404 O O   . HOH   K 4 .   ? 32.80871 34.38509 7.50222   1.000 30.67551 ? 518 HOH   A O   1 
HETATM 2405 O O   . HOH   K 4 .   ? 32.75637 24.31723 -8.90744  1.000 32.20182 ? 519 HOH   A O   1 
HETATM 2406 O O   . HOH   K 4 .   ? 18.93717 3.79461  11.26260  1.000 43.32733 ? 520 HOH   A O   1 
HETATM 2407 O O   . HOH   K 4 .   ? 34.76552 12.68774 -12.66477 1.000 19.75041 ? 521 HOH   A O   1 
HETATM 2408 O O   . HOH   K 4 .   ? 42.22602 28.08598 8.66390   1.000 33.92088 ? 522 HOH   A O   1 
HETATM 2409 O O   . HOH   K 4 .   ? 8.96009  6.07057  -1.34966  1.000 50.80213 ? 523 HOH   A O   1 
HETATM 2410 O O   . HOH   K 4 .   ? 20.83003 37.70146 -6.21689  1.000 24.58884 ? 524 HOH   A O   1 
HETATM 2411 O O   . HOH   K 4 .   ? 22.91496 25.34557 -12.83622 1.000 22.13354 ? 525 HOH   A O   1 
HETATM 2412 O O   . HOH   K 4 .   ? 39.37227 12.62661 4.96897   1.000 25.45307 ? 526 HOH   A O   1 
HETATM 2413 O O   . HOH   K 4 .   ? 34.89259 2.29270  -7.33105  1.000 23.85197 ? 527 HOH   A O   1 
HETATM 2414 O O   . HOH   K 4 .   ? 16.94917 14.41238 14.19633  1.000 32.00825 ? 528 HOH   A O   1 
HETATM 2415 O O   . HOH   K 4 .   ? 22.49012 3.26666  5.49611   1.000 19.38203 ? 529 HOH   A O   1 
HETATM 2416 O O   . HOH   K 4 .   ? 35.60511 -1.61000 -12.17850 1.000 35.69996 ? 530 HOH   A O   1 
HETATM 2417 O O   . HOH   K 4 .   ? 29.48788 1.74228  16.40629  1.000 45.27618 ? 531 HOH   A O   1 
HETATM 2418 O O   . HOH   K 4 .   ? 23.29784 24.49673 0.28614   1.000 20.66556 ? 532 HOH   A O   1 
HETATM 2419 O O   . HOH   K 4 .   ? 33.64798 -0.21959 -15.82688 1.000 65.27334 ? 533 HOH   A O   1 
HETATM 2420 O O   . HOH   K 4 .   ? 24.70236 10.52254 15.31666  1.000 37.41461 ? 534 HOH   A O   1 
HETATM 2421 O O   . HOH   K 4 .   ? 33.51136 6.35320  -17.36016 1.000 26.43307 ? 535 HOH   A O   1 
HETATM 2422 O O   . HOH   K 4 .   ? 24.81270 20.88718 -14.30161 1.000 20.39761 ? 536 HOH   A O   1 
HETATM 2423 O O   . HOH   K 4 .   ? 27.56989 0.51869  -10.67392 1.000 32.93768 ? 537 HOH   A O   1 
HETATM 2424 O O   . HOH   K 4 .   ? 30.99866 10.36351 -7.90790  1.000 19.16432 ? 538 HOH   A O   1 
HETATM 2425 O O   . HOH   K 4 .   ? 22.55852 7.60824  -21.35952 1.000 50.18683 ? 539 HOH   A O   1 
HETATM 2426 O O   . HOH   K 4 .   ? 41.29261 31.12648 3.78933   1.000 38.18892 ? 540 HOH   A O   1 
HETATM 2427 O O   . HOH   K 4 .   ? 34.66482 25.53390 -12.64481 1.000 25.35060 ? 541 HOH   A O   1 
HETATM 2428 O O   . HOH   K 4 .   ? 58.89603 31.82591 4.67742   1.000 53.23595 ? 542 HOH   A O   1 
HETATM 2429 O O   . HOH   K 4 .   ? 25.18507 0.66917  -8.45892  1.000 20.43613 ? 543 HOH   A O   1 
HETATM 2430 O O   . HOH   K 4 .   ? 20.26075 16.81774 -23.91133 1.000 35.40843 ? 544 HOH   A O   1 
HETATM 2431 O O   . HOH   K 4 .   ? 15.16481 7.22492  11.57815  1.000 55.45571 ? 545 HOH   A O   1 
HETATM 2432 O O   . HOH   K 4 .   ? 34.46239 26.65342 -8.83064  1.000 31.02756 ? 546 HOH   A O   1 
HETATM 2433 O O   . HOH   K 4 .   ? 36.86118 3.90617  -8.51114  1.000 25.13768 ? 547 HOH   A O   1 
HETATM 2434 O O   . HOH   K 4 .   ? 28.55545 30.41708 -6.52920  1.000 21.81208 ? 548 HOH   A O   1 
HETATM 2435 O O   . HOH   K 4 .   ? 37.82480 35.78707 -4.67891  1.000 54.16271 ? 549 HOH   A O   1 
HETATM 2436 O O   . HOH   K 4 .   ? 21.08531 30.51964 -5.29706  1.000 19.68288 ? 550 HOH   A O   1 
HETATM 2437 O O   . HOH   K 4 .   ? 20.97955 14.30236 -15.25138 1.000 38.81283 ? 551 HOH   A O   1 
HETATM 2438 O O   . HOH   K 4 .   ? 22.20760 24.78865 19.44799  1.000 61.97954 ? 552 HOH   A O   1 
HETATM 2439 O O   . HOH   K 4 .   ? 36.35984 26.76104 -10.59711 1.000 23.93037 ? 553 HOH   A O   1 
HETATM 2440 O O   . HOH   K 4 .   ? 24.95671 19.99474 -8.22187  1.000 18.94695 ? 554 HOH   A O   1 
HETATM 2441 O O   . HOH   K 4 .   ? 18.05338 3.37412  -1.01850  1.000 34.23319 ? 555 HOH   A O   1 
HETATM 2442 O O   . HOH   K 4 .   ? 27.14651 27.21634 5.34986   1.000 18.71851 ? 556 HOH   A O   1 
HETATM 2443 O O   . HOH   K 4 .   ? 41.47483 5.45910  -6.02110  1.000 49.59390 ? 557 HOH   A O   1 
HETATM 2444 O O   . HOH   K 4 .   ? 33.66765 10.30969 -1.59612  1.000 19.36500 ? 558 HOH   A O   1 
HETATM 2445 O O   . HOH   K 4 .   ? 24.55650 13.20374 14.19934  1.000 35.25963 ? 559 HOH   A O   1 
HETATM 2446 O O   . HOH   K 4 .   ? 24.72403 -2.73228 14.07684  1.000 52.64487 ? 560 HOH   A O   1 
HETATM 2447 O O   . HOH   K 4 .   ? 37.53694 33.71097 -7.07573  1.000 66.62619 ? 561 HOH   A O   1 
HETATM 2448 O O   . HOH   K 4 .   ? 33.45359 30.64025 0.00671   1.000 23.42701 ? 562 HOH   A O   1 
HETATM 2449 O O   . HOH   K 4 .   ? 18.30772 23.15379 -10.50220 1.000 25.04993 ? 563 HOH   A O   1 
HETATM 2450 O O   . HOH   K 4 .   ? 15.49668 16.38566 15.98922  1.000 45.90355 ? 564 HOH   A O   1 
HETATM 2451 O O   . HOH   K 4 .   ? 18.15881 3.71752  -13.60794 1.000 35.46233 ? 565 HOH   A O   1 
HETATM 2452 O O   . HOH   K 4 .   ? 20.98267 30.41040 -11.66952 1.000 40.29098 ? 566 HOH   A O   1 
HETATM 2453 O O   . HOH   K 4 .   ? 38.89978 -2.31211 9.01686   1.000 39.37110 ? 567 HOH   A O   1 
HETATM 2454 O O   . HOH   K 4 .   ? 25.47468 43.20768 -9.15936  1.000 50.90760 ? 568 HOH   A O   1 
HETATM 2455 O O   . HOH   K 4 .   ? 13.01636 46.52115 -1.67413  1.000 50.62639 ? 569 HOH   A O   1 
HETATM 2456 O O   . HOH   K 4 .   ? 41.88743 22.64408 -13.70515 1.000 57.12161 ? 570 HOH   A O   1 
HETATM 2457 O O   . HOH   K 4 .   ? 26.94917 4.32500  -14.17604 1.000 47.35382 ? 571 HOH   A O   1 
HETATM 2458 O O   . HOH   K 4 .   ? 26.12234 27.82889 14.72060  1.000 29.07204 ? 572 HOH   A O   1 
HETATM 2459 O O   . HOH   K 4 .   ? 34.55265 38.40725 -4.78860  1.000 42.67561 ? 573 HOH   A O   1 
HETATM 2460 O O   . HOH   K 4 .   ? 33.22283 19.33928 13.12396  1.000 45.28526 ? 574 HOH   A O   1 
HETATM 2461 O O   . HOH   K 4 .   ? 44.15376 12.61977 -2.00891  1.000 39.50916 ? 575 HOH   A O   1 
HETATM 2462 O O   . HOH   K 4 .   ? 25.99896 -2.11130 12.24306  1.000 34.70208 ? 576 HOH   A O   1 
HETATM 2463 O O   . HOH   K 4 .   ? 26.37945 43.10279 9.18391   1.000 31.42046 ? 577 HOH   A O   1 
HETATM 2464 O O   . HOH   K 4 .   ? 17.67461 19.73228 -12.64081 1.000 33.88410 ? 578 HOH   A O   1 
HETATM 2465 O O   . HOH   K 4 .   ? 26.01593 8.76263  18.92197  1.000 44.86597 ? 579 HOH   A O   1 
HETATM 2466 O O   . HOH   K 4 .   ? 33.38999 29.18502 -17.52848 1.000 57.92018 ? 580 HOH   A O   1 
HETATM 2467 O O   . HOH   K 4 .   ? 28.42750 29.66181 5.08309   1.000 19.24621 ? 581 HOH   A O   1 
HETATM 2468 O O   . HOH   K 4 .   ? 16.78328 35.36376 -6.75613  1.000 40.91690 ? 582 HOH   A O   1 
HETATM 2469 O O   . HOH   K 4 .   ? 15.03831 32.56260 6.12978   1.000 36.66317 ? 583 HOH   A O   1 
HETATM 2470 O O   . HOH   K 4 .   ? 23.76125 27.49083 16.12843  1.000 31.75310 ? 584 HOH   A O   1 
HETATM 2471 O O   . HOH   K 4 .   ? 36.33442 11.12620 -1.47671  1.000 19.34636 ? 585 HOH   A O   1 
HETATM 2472 O O   . HOH   K 4 .   ? 40.88255 33.16083 -9.23236  1.000 41.85663 ? 586 HOH   A O   1 
HETATM 2473 O O   . HOH   K 4 .   ? 35.29230 34.34992 10.35489  1.000 53.00690 ? 587 HOH   A O   1 
HETATM 2474 O O   . HOH   K 4 .   ? 49.59461 33.87652 1.48903   1.000 37.48854 ? 588 HOH   A O   1 
HETATM 2475 O O   . HOH   K 4 .   ? 7.03826  18.36235 -4.71230  1.000 56.11321 ? 589 HOH   A O   1 
HETATM 2476 O O   . HOH   K 4 .   ? 45.00757 32.34086 -2.65325  1.000 33.74629 ? 590 HOH   A O   1 
HETATM 2477 O O   . HOH   K 4 .   ? 25.40469 4.40778  14.98933  1.000 27.46651 ? 591 HOH   A O   1 
HETATM 2478 O O   . HOH   K 4 .   ? 17.40701 24.69316 18.14141  1.000 42.85479 ? 592 HOH   A O   1 
HETATM 2479 O O   . HOH   K 4 .   ? 20.680   0.260    4.776     1.000 40.39518 ? 593 HOH   A O   1 
HETATM 2480 O O   . HOH   K 4 .   ? 14.42057 31.23410 -1.92820  1.000 33.23431 ? 594 HOH   A O   1 
HETATM 2481 O O   . HOH   K 4 .   ? 18.93769 21.60513 16.52983  1.000 54.84619 ? 595 HOH   A O   1 
HETATM 2482 O O   . HOH   K 4 .   ? 18.06895 44.21879 2.58473   1.000 34.81345 ? 596 HOH   A O   1 
HETATM 2483 O O   . HOH   K 4 .   ? 40.06807 11.04946 -8.25194  1.000 26.39122 ? 597 HOH   A O   1 
HETATM 2484 O O   . HOH   K 4 .   ? 20.58117 20.75153 -13.62130 1.000 34.53285 ? 598 HOH   A O   1 
HETATM 2485 O O   . HOH   K 4 .   ? 35.74840 22.77431 10.65343  1.000 50.42723 ? 599 HOH   A O   1 
HETATM 2486 O O   . HOH   K 4 .   ? 31.28379 5.61799  -19.33453 1.000 32.42232 ? 600 HOH   A O   1 
HETATM 2487 O O   . HOH   K 4 .   ? 37.25124 17.13049 12.97778  1.000 33.58523 ? 601 HOH   A O   1 
HETATM 2488 O O   . HOH   K 4 .   ? 7.77144  12.04204 11.84722  1.000 59.08119 ? 602 HOH   A O   1 
HETATM 2489 O O   . HOH   K 4 .   ? 32.49273 31.98430 14.82575  1.000 42.32054 ? 603 HOH   A O   1 
HETATM 2490 O O   . HOH   K 4 .   ? 38.54699 30.08117 -5.15888  1.000 33.48012 ? 604 HOH   A O   1 
HETATM 2491 O O   . HOH   K 4 .   ? 31.07818 31.71547 -5.79362  1.000 53.80668 ? 605 HOH   A O   1 
HETATM 2492 O O   . HOH   K 4 .   ? 17.73373 20.51729 -9.95871  1.000 23.08289 ? 606 HOH   A O   1 
HETATM 2493 O O   . HOH   K 4 .   ? 25.69378 13.60110 -22.99027 1.000 31.76020 ? 607 HOH   A O   1 
HETATM 2494 O O   . HOH   K 4 .   ? 25.78631 36.55845 -11.53061 1.000 35.39143 ? 608 HOH   A O   1 
HETATM 2495 O O   . HOH   K 4 .   ? 27.52496 37.22199 -9.27337  1.000 41.87980 ? 609 HOH   A O   1 
HETATM 2496 O O   . HOH   K 4 .   ? 8.31616  12.50854 -4.32868  1.000 45.63960 ? 610 HOH   A O   1 
HETATM 2497 O O   . HOH   K 4 .   ? 39.70854 30.91942 1.45198   1.000 29.78460 ? 611 HOH   A O   1 
HETATM 2498 O O   . HOH   K 4 .   ? 11.76745 16.04163 -8.78740  1.000 46.57833 ? 612 HOH   A O   1 
HETATM 2499 O O   . HOH   K 4 .   ? 29.58275 40.46504 -0.27281  1.000 31.86411 ? 613 HOH   A O   1 
HETATM 2500 O O   . HOH   K 4 .   ? 40.22407 11.72606 15.77220  1.000 59.51873 ? 614 HOH   A O   1 
HETATM 2501 O O   . HOH   K 4 .   ? 33.87858 35.76969 3.83602   1.000 27.47742 ? 615 HOH   A O   1 
HETATM 2502 O O   . HOH   K 4 .   ? 18.45563 18.57802 -8.05810  1.000 21.27352 ? 616 HOH   A O   1 
HETATM 2503 O O   . HOH   K 4 .   ? 22.37431 9.76001  14.96977  1.000 43.83268 ? 617 HOH   A O   1 
HETATM 2504 O O   . HOH   K 4 .   ? 27.69254 11.61942 14.38894  1.000 32.16766 ? 618 HOH   A O   1 
HETATM 2505 O O   . HOH   K 4 .   ? 28.35288 3.21732  -17.34596 1.000 49.25465 ? 619 HOH   A O   1 
HETATM 2506 O O   . HOH   K 4 .   ? 43.06989 14.21224 -0.15755  1.000 27.50087 ? 620 HOH   A O   1 
HETATM 2507 O O   . HOH   K 4 .   ? 19.86150 15.51352 -19.43744 1.000 47.83742 ? 621 HOH   A O   1 
HETATM 2508 O O   . HOH   K 4 .   ? 33.79576 21.22161 -20.54566 1.000 46.80840 ? 622 HOH   A O   1 
HETATM 2509 O O   . HOH   K 4 .   ? 14.07959 35.81759 5.42240   1.000 34.82515 ? 623 HOH   A O   1 
HETATM 2510 O O   . HOH   K 4 .   ? 43.20933 29.76944 3.88334   1.000 57.07906 ? 624 HOH   A O   1 
HETATM 2511 O O   . HOH   K 4 .   ? 24.06683 48.54052 2.43053   1.000 68.83321 ? 625 HOH   A O   1 
HETATM 2512 O O   . HOH   K 4 .   ? 27.97077 36.92026 16.47642  1.000 52.78402 ? 626 HOH   A O   1 
HETATM 2513 O O   . HOH   K 4 .   ? 29.66436 37.53137 -8.53677  1.000 54.35839 ? 627 HOH   A O   1 
HETATM 2514 O O   . HOH   K 4 .   ? 18.23154 0.85906  3.64576   1.000 59.72509 ? 628 HOH   A O   1 
HETATM 2515 O O   . HOH   K 4 .   ? 3.11639  18.95563 -0.69552  1.000 56.51551 ? 629 HOH   A O   1 
HETATM 2516 O O   . HOH   K 4 .   ? 31.92532 15.50746 -20.13254 1.000 41.82867 ? 630 HOH   A O   1 
HETATM 2517 O O   . HOH   K 4 .   ? 25.04685 45.71477 -0.33365  1.000 48.87116 ? 631 HOH   A O   1 
HETATM 2518 O O   . HOH   K 4 .   ? 16.33099 4.90410  -15.78280 1.000 50.49804 ? 632 HOH   A O   1 
HETATM 2519 O O   . HOH   K 4 .   ? 39.30569 3.44195  -5.02412  1.000 36.72028 ? 633 HOH   A O   1 
HETATM 2520 O O   . HOH   K 4 .   ? 37.23162 32.00691 11.22598  1.000 52.89340 ? 634 HOH   A O   1 
HETATM 2521 O O   . HOH   K 4 .   ? 29.21559 41.14202 4.50680   1.000 47.97491 ? 635 HOH   A O   1 
HETATM 2522 O O   . HOH   K 4 .   ? 42.85572 10.31124 -10.71927 1.000 55.63809 ? 636 HOH   A O   1 
HETATM 2523 O O   . HOH   K 4 .   ? 34.68850 33.90083 5.69088   1.000 32.40822 ? 637 HOH   A O   1 
HETATM 2524 O O   . HOH   K 4 .   ? 23.53102 37.00877 13.37308  1.000 39.04474 ? 638 HOH   A O   1 
HETATM 2525 O O   . HOH   K 4 .   ? 31.16910 39.77183 3.64801   1.000 31.52305 ? 639 HOH   A O   1 
HETATM 2526 O O   . HOH   K 4 .   ? 15.71631 -0.22686 -6.42436  1.000 54.31972 ? 640 HOH   A O   1 
HETATM 2527 O O   . HOH   K 4 .   ? 20.82102 22.59202 -12.07551 1.000 38.90758 ? 641 HOH   A O   1 
HETATM 2528 O O   . HOH   K 4 .   ? 38.84145 0.91980  2.66370   1.000 52.15233 ? 642 HOH   A O   1 
HETATM 2529 O O   . HOH   K 4 .   ? 37.67933 30.82130 -7.15201  1.000 35.80124 ? 643 HOH   A O   1 
HETATM 2530 O O   . HOH   K 4 .   ? 45.04676 26.63734 7.14643   1.000 41.16831 ? 644 HOH   A O   1 
HETATM 2531 O O   . HOH   K 4 .   ? 25.90177 44.36622 -4.38203  1.000 54.99743 ? 645 HOH   A O   1 
HETATM 2532 O O   . HOH   K 4 .   ? 16.47398 32.99035 -6.39891  1.000 45.05417 ? 646 HOH   A O   1 
HETATM 2533 O O   . HOH   K 4 .   ? 19.40349 46.02248 4.69818   1.000 39.20654 ? 647 HOH   A O   1 
HETATM 2534 O O   . HOH   K 4 .   ? 34.52159 38.16542 2.54641   1.000 31.91047 ? 648 HOH   A O   1 
HETATM 2535 O O   . HOH   K 4 .   ? 26.06873 4.33290  -16.56711 1.000 43.29324 ? 649 HOH   A O   1 
HETATM 2536 O O   . HOH   K 4 .   ? 30.82450 9.88273  18.81806  1.000 53.77237 ? 650 HOH   A O   1 
HETATM 2537 O O   . HOH   K 4 .   ? 3.94793  22.54176 -1.56817  1.000 64.79185 ? 651 HOH   A O   1 
HETATM 2538 O O   . HOH   K 4 .   ? 44.64324 17.28652 3.64814   1.000 38.68068 ? 652 HOH   A O   1 
HETATM 2539 O O   . HOH   K 4 .   ? 27.99954 22.29790 18.26958  1.000 50.67737 ? 653 HOH   A O   1 
HETATM 2540 O O   . HOH   K 4 .   ? 37.87606 26.45215 13.37117  1.000 57.86057 ? 654 HOH   A O   1 
HETATM 2541 O O   . HOH   K 4 .   ? 27.04026 41.44281 -1.63199  1.000 44.86806 ? 655 HOH   A O   1 
HETATM 2542 O O   . HOH   K 4 .   ? 13.64804 8.35082  -9.89719  1.000 67.32095 ? 656 HOH   A O   1 
HETATM 2543 O O   . HOH   K 4 .   ? 49.15434 37.21886 -4.51804  1.000 42.01309 ? 657 HOH   A O   1 
HETATM 2544 O O   . HOH   K 4 .   ? 17.61503 31.24321 -8.66197  1.000 49.54870 ? 658 HOH   A O   1 
HETATM 2545 O O   . HOH   K 4 .   ? 19.80331 17.57158 -18.45312 1.000 61.09585 ? 659 HOH   A O   1 
HETATM 2546 O O   . HOH   K 4 .   ? 43.40009 12.37710 5.11035   1.000 63.38976 ? 660 HOH   A O   1 
HETATM 2547 O O   . HOH   K 4 .   ? 45.79098 20.88140 5.49610   1.000 56.56580 ? 661 HOH   A O   1 
HETATM 2548 O O   . HOH   K 4 .   ? 7.92154  9.70930  4.04589   1.000 58.87661 ? 662 HOH   A O   1 
HETATM 2549 O O   . HOH   K 4 .   ? 26.80509 18.74163 -26.20699 1.000 49.42505 ? 663 HOH   A O   1 
HETATM 2550 O O   . HOH   K 4 .   ? 15.72823 36.56160 8.68263   1.000 46.81290 ? 664 HOH   A O   1 
HETATM 2551 O O   . HOH   K 4 .   ? 6.46493  10.23715 9.75341   1.000 65.55971 ? 665 HOH   A O   1 
HETATM 2552 O O   . HOH   K 4 .   ? 46.46629 24.84099 7.05123   1.000 57.53088 ? 666 HOH   A O   1 
HETATM 2553 O O   . HOH   K 4 .   ? 22.34612 27.61984 -16.51047 1.000 47.00478 ? 667 HOH   A O   1 
HETATM 2554 O O   . HOH   K 4 .   ? 39.73069 16.66526 -19.24093 1.000 53.47132 ? 668 HOH   A O   1 
HETATM 2555 O O   . HOH   K 4 .   ? 21.08770 27.11330 19.25592  1.000 43.70513 ? 669 HOH   A O   1 
HETATM 2556 O O   . HOH   K 4 .   ? 16.27426 27.13321 -9.04559  1.000 47.89046 ? 670 HOH   A O   1 
HETATM 2557 O O   . HOH   K 4 .   ? 32.15926 17.63003 -21.39124 1.000 58.08003 ? 671 HOH   A O   1 
HETATM 2558 O O   . HOH   K 4 .   ? 31.51457 39.57969 -3.74350  1.000 49.38559 ? 672 HOH   A O   1 
HETATM 2559 O O   . HOH   K 4 .   ? 43.06792 21.56462 10.00907  1.000 49.11786 ? 673 HOH   A O   1 
HETATM 2560 O O   . HOH   K 4 .   ? 19.48953 13.00540 -16.36114 1.000 50.86989 ? 674 HOH   A O   1 
HETATM 2561 O O   . HOH   K 4 .   ? 20.77510 19.19955 15.83341  1.000 44.96081 ? 675 HOH   A O   1 
HETATM 2562 O O   . HOH   K 4 .   ? 38.63639 5.21128  -12.95251 1.000 54.51994 ? 676 HOH   A O   1 
HETATM 2563 O O   . HOH   K 4 .   ? 37.59156 10.07683 -16.16533 1.000 63.31780 ? 677 HOH   A O   1 
HETATM 2564 O O   . HOH   K 4 .   ? 25.79882 38.75501 14.21023  1.000 52.67210 ? 678 HOH   A O   1 
HETATM 2565 O O   . HOH   K 4 .   ? 30.41130 41.70377 7.39847   1.000 66.29728 ? 679 HOH   A O   1 
HETATM 2566 O O   . HOH   K 4 .   ? 22.70423 3.05080  -12.96069 1.000 41.78277 ? 680 HOH   A O   1 
HETATM 2567 O O   . HOH   K 4 .   ? 27.22496 3.87698  17.01652  1.000 57.14071 ? 681 HOH   A O   1 
HETATM 2568 O O   . HOH   K 4 .   ? 12.181   37.768   4.331     1.000 42.87294 ? 682 HOH   A O   1 
HETATM 2569 O O   . HOH   K 4 .   ? 12.92108 27.52344 -4.48194  1.000 51.17382 ? 683 HOH   A O   1 
HETATM 2570 O O   . HOH   K 4 .   ? 35.29783 20.58844 12.20905  1.000 55.83381 ? 684 HOH   A O   1 
HETATM 2571 O O   . HOH   K 4 .   ? 11.76964 9.30127  -7.26204  1.000 54.46933 ? 685 HOH   A O   1 
HETATM 2572 O O   . HOH   K 4 .   ? 22.77389 7.83807  15.92738  1.000 60.80996 ? 686 HOH   A O   1 
HETATM 2573 O O   . HOH   K 4 .   ? 24.01051 41.91587 -11.65572 1.000 65.08407 ? 687 HOH   A O   1 
HETATM 2574 O O   . HOH   K 4 .   ? 40.78019 21.78865 13.68922  1.000 59.31085 ? 688 HOH   A O   1 
HETATM 2575 O O   . HOH   K 4 .   ? 17.00606 11.86260 15.33215  1.000 43.44739 ? 689 HOH   A O   1 
HETATM 2576 O O   . HOH   K 4 .   ? 18.94879 28.40174 -9.72372  1.000 61.27163 ? 690 HOH   A O   1 
HETATM 2577 O O   . HOH   K 4 .   ? 34.41801 29.16788 12.83022  1.000 50.93363 ? 691 HOH   A O   1 
HETATM 2578 O O   . HOH   K 4 .   ? 10.39086 3.02453  0.38384   1.000 61.66390 ? 692 HOH   A O   1 
HETATM 2579 O O   . HOH   K 4 .   ? 57.559   30.066   -5.632    1.000 59.53660 ? 693 HOH   A O   1 
HETATM 2580 O O   . HOH   K 4 .   ? 15.11219 13.06271 -12.22406 1.000 61.01337 ? 694 HOH   A O   1 
HETATM 2581 O O   . HOH   K 4 .   ? 26.37748 30.68803 14.62668  1.000 25.70163 ? 695 HOH   A O   1 
HETATM 2582 O O   . HOH   K 4 .   ? 24.25733 31.89241 15.57067  1.000 42.79107 ? 696 HOH   A O   1 
HETATM 2583 O O   . HOH   K 4 .   ? 15.44034 1.75992  8.67487   1.000 55.50003 ? 697 HOH   A O   1 
HETATM 2584 O O   . HOH   K 4 .   ? 46.77676 18.49911 3.80173   1.000 59.76735 ? 698 HOH   A O   1 
HETATM 2585 O O   . HOH   K 4 .   ? 44.91662 15.36856 1.60778   1.000 52.19806 ? 699 HOH   A O   1 
HETATM 2586 O O   . HOH   K 4 .   ? 7.73676  13.11937 14.00734  1.000 60.26942 ? 700 HOH   A O   1 
HETATM 2587 O O   . HOH   K 4 .   ? 23.64021 34.57935 15.55768  1.000 52.45567 ? 701 HOH   A O   1 
HETATM 2588 O O   . HOH   K 4 .   ? 21.81741 3.73191  13.64891  1.000 40.79514 ? 702 HOH   A O   1 
HETATM 2589 O O   . HOH   K 4 .   ? 41.19885 10.63664 5.14978   1.000 50.30907 ? 703 HOH   A O   1 
HETATM 2590 O O   . HOH   K 4 .   ? 20.87164 -1.41850 -13.52744 1.000 66.22006 ? 704 HOH   A O   1 
HETATM 2591 O O   . HOH   K 4 .   ? 16.36041 24.12708 -12.05646 1.000 52.90344 ? 705 HOH   A O   1 
HETATM 2592 O O   . HOH   K 4 .   ? 28.04822 26.65213 16.18560  1.000 41.86143 ? 706 HOH   A O   1 
HETATM 2593 O O   . HOH   K 4 .   ? 4.33976  17.78668 -3.92100  1.000 64.84787 ? 707 HOH   A O   1 
HETATM 2594 O O   . HOH   K 4 .   ? 19.83534 7.34621  15.01684  1.000 69.05918 ? 708 HOH   A O   1 
HETATM 2595 O O   . HOH   K 4 .   ? 21.28379 9.79087  -22.53914 1.000 67.44603 ? 709 HOH   A O   1 
HETATM 2596 O O   . HOH   K 4 .   ? 28.37161 31.41899 16.68208  1.000 51.62144 ? 710 HOH   A O   1 
# 
loop_
_atom_site_anisotrop.id 
_atom_site_anisotrop.type_symbol 
_atom_site_anisotrop.pdbx_label_atom_id 
_atom_site_anisotrop.pdbx_label_alt_id 
_atom_site_anisotrop.pdbx_label_comp_id 
_atom_site_anisotrop.pdbx_label_asym_id 
_atom_site_anisotrop.pdbx_label_seq_id 
_atom_site_anisotrop.pdbx_PDB_ins_code 
_atom_site_anisotrop.U[1][1] 
_atom_site_anisotrop.U[2][2] 
_atom_site_anisotrop.U[3][3] 
_atom_site_anisotrop.U[1][2] 
_atom_site_anisotrop.U[1][3] 
_atom_site_anisotrop.U[2][3] 
_atom_site_anisotrop.pdbx_auth_seq_id 
_atom_site_anisotrop.pdbx_auth_comp_id 
_atom_site_anisotrop.pdbx_auth_asym_id 
_atom_site_anisotrop.pdbx_auth_atom_id 
1    N N   . SER   A 26  ? 1.00215 0.47323 1.12194 -0.04107 -0.04625 0.00411  6   SER   A N   
2    C CA  . SER   A 26  ? 0.99536 0.46415 1.08197 -0.04499 -0.05918 -0.00200 6   SER   A CA  
3    C C   . SER   A 26  ? 0.97054 0.40453 1.00032 -0.05032 -0.06469 -0.02138 6   SER   A C   
4    O O   . SER   A 26  ? 0.97855 0.39645 1.00683 -0.07478 -0.05775 -0.03617 6   SER   A O   
5    C CB  . SER   A 26  ? 1.01007 0.50934 1.12147 -0.03800 -0.06749 -0.00263 6   SER   A CB  
6    O OG  . SER   A 26  ? 1.02408 0.53431 1.15663 -0.03199 -0.07149 -0.00179 6   SER   A OG  
7    N N   . PRO   A 27  ? 0.93699 0.36099 0.90107 -0.02068 -0.06497 -0.02881 7   PRO   A N   
8    C CA  . PRO   A 27  ? 0.89431 0.32375 0.80128 -0.00125 -0.04702 -0.04482 7   PRO   A CA  
9    C C   . PRO   A 27  ? 0.83078 0.28896 0.64292 -0.01181 -0.01879 -0.07860 7   PRO   A C   
10   O O   . PRO   A 27  ? 0.86070 0.29146 0.65276 -0.01257 0.06639  -0.08087 7   PRO   A O   
11   C CB  . PRO   A 27  ? 0.91766 0.32888 0.84706 0.01349  -0.05642 -0.03427 7   PRO   A CB  
12   C CG  . PRO   A 27  ? 0.92681 0.33945 0.86873 0.00469  -0.05916 -0.02622 7   PRO   A CG  
13   C CD  . PRO   A 27  ? 0.93675 0.34868 0.89001 -0.00562 -0.06798 -0.02851 7   PRO   A CD  
14   N N   . ARG   A 28  ? 0.75995 0.25866 0.50275 -0.00863 -0.03120 -0.07912 8   ARG   A N   
15   C CA  . ARG   A 28  ? 0.66475 0.24009 0.41082 -0.01169 -0.03900 -0.05876 8   ARG   A CA  
16   C C   . ARG   A 28  ? 0.61178 0.21987 0.37144 0.00264  -0.03558 -0.05090 8   ARG   A C   
17   O O   . ARG   A 28  ? 0.62766 0.22005 0.37052 0.00296  -0.00923 -0.02648 8   ARG   A O   
18   C CB  . ARG   A 28  ? 0.62362 0.25246 0.37999 -0.01279 -0.03292 -0.05921 8   ARG   A CB  
19   C CG  . ARG   A 28  ? 0.57305 0.26246 0.43291 0.00415  -0.00657 -0.02615 8   ARG   A CG  
20   C CD  . ARG   A 28  ? 0.52569 0.23837 0.45033 0.02685  -0.02593 -0.00317 8   ARG   A CD  
21   N NE  . ARG   A 28  ? 0.47732 0.21305 0.42273 0.02517  -0.01769 0.00833  8   ARG   A NE  
22   C CZ  . ARG   A 28  ? 0.43193 0.20057 0.37937 -0.00578 -0.00043 -0.01623 8   ARG   A CZ  
23   N NH1 . ARG   A 28  ? 0.41435 0.23403 0.43765 -0.02284 -0.00872 -0.00827 8   ARG   A NH1 
24   N NH2 . ARG   A 28  ? 0.40594 0.17401 0.35416 -0.02243 -0.00735 -0.00839 8   ARG   A NH2 
25   N N   . ARG   A 29  ? 0.56774 0.21646 0.36791 0.00367  -0.00426 -0.04325 9   ARG   A N   
26   C CA  . ARG   A 29  ? 0.53977 0.20102 0.36818 0.01757  0.00276  -0.02354 9   ARG   A CA  
27   C C   . ARG   A 29  ? 0.47804 0.21284 0.36552 0.00175  0.01027  -0.00511 9   ARG   A C   
28   O O   . ARG   A 29  ? 0.48301 0.22426 0.40496 -0.01668 0.02973  0.00366  9   ARG   A O   
29   C CB  . ARG   A 29  ? 0.57205 0.17579 0.41875 0.04246  0.00644  0.04202  9   ARG   A CB  
30   C CG  . ARG   A 29  ? 0.60146 0.17915 0.51015 0.03868  0.04584  0.05492  9   ARG   A CG  
31   C CD  . ARG   A 29  ? 0.64849 0.18198 0.59909 0.02193  0.06289  0.04597  9   ARG   A CD  
32   N NE  . ARG   A 29  ? 0.69577 0.23170 0.70277 0.01188  0.05464  0.05543  9   ARG   A NE  
33   C CZ  . ARG   A 29  ? 0.73409 0.23555 0.76768 0.01141  0.06408  0.04027  9   ARG   A CZ  
34   N NH1 . ARG   A 29  ? 0.74552 0.22937 0.78344 0.00531  0.08049  0.01108  9   ARG   A NH1 
35   N NH2 . ARG   A 29  ? 0.75129 0.23912 0.81525 0.03794  0.05977  0.03416  9   ARG   A NH2 
36   N N   . THR   A 30  ? 0.42553 0.17536 0.30922 -0.00916 -0.00302 -0.00184 10  THR   A N   
37   C CA  . THR   A 30  ? 0.38231 0.19126 0.34125 0.02756  0.02150  0.02051  10  THR   A CA  
38   C C   . THR   A 30  ? 0.38212 0.20173 0.37553 0.02057  0.01145  0.05010  10  THR   A C   
39   O O   . THR   A 30  ? 0.37922 0.21387 0.41119 0.04079  0.02030  0.02430  10  THR   A O   
40   C CB  . THR   A 30  ? 0.38872 0.20474 0.30289 0.02568  0.00703  0.03545  10  THR   A CB  
41   O OG1 . THR   A 30  ? 0.41483 0.21098 0.28477 0.03560  0.01009  0.05442  10  THR   A OG1 
42   C CG2 . THR   A 30  ? 0.37683 0.21741 0.27399 0.02296  0.03282  0.01473  10  THR   A CG2 
43   N N   . PRO   A 31  ? 0.37616 0.21967 0.34886 0.03115  0.01260  0.03057  11  PRO   A N   
44   C CA  . PRO   A 31  ? 0.41620 0.23233 0.33164 0.03198  0.01194  0.03788  11  PRO   A CA  
45   C C   . PRO   A 31  ? 0.45438 0.23841 0.35376 0.01596  0.02036  0.04766  11  PRO   A C   
46   O O   . PRO   A 31  ? 0.48520 0.26837 0.38105 0.00587  0.06030  0.06809  11  PRO   A O   
47   C CB  . PRO   A 31  ? 0.40748 0.23049 0.34683 0.03662  0.00330  0.06247  11  PRO   A CB  
48   C CG  . PRO   A 31  ? 0.39235 0.24364 0.38389 0.04670  0.01612  0.04334  11  PRO   A CG  
49   C CD  . PRO   A 31  ? 0.36379 0.22438 0.37978 0.06053  0.00563  0.07129  11  PRO   A CD  
50   N N   . GLN   A 32  ? 0.46900 0.22177 0.36972 0.02836  -0.01494 0.01570  12  GLN   A N   
51   C CA  . GLN   A 32  ? 0.48567 0.22501 0.34299 0.03497  -0.02227 0.01403  12  GLN   A CA  
52   C C   . GLN   A 32  ? 0.51707 0.24094 0.34247 0.03652  -0.01959 0.01354  12  GLN   A C   
53   O O   . GLN   A 32  ? 0.53226 0.25991 0.37270 0.04288  -0.02774 0.02893  12  GLN   A O   
54   C CB  . GLN   A 32  ? 0.48345 0.23168 0.31996 0.03854  -0.01993 -0.01179 12  GLN   A CB  
55   C CG  . GLN   A 32  ? 0.47812 0.23300 0.32337 0.04132  0.01975  0.01146  12  GLN   A CG  
56   C CD  . GLN   A 32  ? 0.45830 0.20995 0.33352 0.03548  0.03135  -0.01391 12  GLN   A CD  
57   O OE1 . GLN   A 32  ? 0.47960 0.20855 0.33297 0.03179  0.01756  -0.00772 12  GLN   A OE1 
58   N NE2 . GLN   A 32  ? 0.41114 0.21479 0.33758 0.03706  0.00860  0.00808  12  GLN   A NE2 
59   N N   . SER   A 33  ? 0.51987 0.22846 0.34264 0.02059  0.05703  0.01331  13  SER   A N   
60   C CA  . SER   A 33  ? 0.53057 0.21833 0.36163 0.00854  0.06754  0.03514  13  SER   A CA  
61   C C   . SER   A 33  ? 0.50162 0.20425 0.35990 0.04089  0.03915  0.02488  13  SER   A C   
62   O O   . SER   A 33  ? 0.51698 0.20430 0.42628 0.04069  0.04418  0.03440  13  SER   A O   
63   C CB  . SER   A 33  ? 0.55121 0.25184 0.40625 -0.01296 0.10309  0.06490  13  SER   A CB  
64   O OG  . SER   A 33  ? 0.58530 0.29653 0.45827 -0.01985 0.08287  0.06867  13  SER   A OG  
65   N N   . ILE   A 34  ? 0.48308 0.21965 0.33213 0.02130  -0.00588 0.02825  14  ILE   A N   
66   C CA  . ILE   A 34  ? 0.46364 0.21256 0.34315 0.04149  0.00581  0.00555  14  ILE   A CA  
67   C C   . ILE   A 34  ? 0.47053 0.21343 0.32536 0.05839  -0.01098 0.01883  14  ILE   A C   
68   O O   . ILE   A 34  ? 0.48857 0.19863 0.30279 0.04025  -0.01467 0.02209  14  ILE   A O   
69   C CB  . ILE   A 34  ? 0.46808 0.23194 0.38080 0.03922  -0.01101 -0.03677 14  ILE   A CB  
70   C CG1 . ILE   A 34  ? 0.46669 0.24185 0.39384 0.04957  -0.02160 -0.07178 14  ILE   A CG1 
71   C CG2 . ILE   A 34  ? 0.45723 0.22742 0.38460 0.02480  -0.02176 -0.03441 14  ILE   A CG2 
72   C CD1 . ILE   A 34  ? 0.46665 0.25966 0.45340 0.06605  -0.04426 -0.06644 14  ILE   A CD1 
73   N N   . PRO   A 35  ? 0.46865 0.21840 0.33038 0.07963  -0.03857 0.04283  15  PRO   A N   
74   C CA  . PRO   A 35  ? 0.46852 0.22383 0.31366 0.09559  -0.02400 0.03839  15  PRO   A CA  
75   C C   . PRO   A 35  ? 0.45495 0.22974 0.27333 0.08590  -0.01311 -0.00405 15  PRO   A C   
76   O O   . PRO   A 35  ? 0.45990 0.24851 0.28913 0.07769  -0.00166 -0.01296 15  PRO   A O   
77   C CB  . PRO   A 35  ? 0.48275 0.23667 0.34915 0.11609  -0.00918 0.03765  15  PRO   A CB  
78   C CG  . PRO   A 35  ? 0.50023 0.25700 0.37543 0.09910  0.00100  0.03158  15  PRO   A CG  
79   C CD  . PRO   A 35  ? 0.47711 0.22805 0.35276 0.10997  -0.00806 0.01822  15  PRO   A CD  
80   N N   . TYR   A 36  ? 0.43301 0.22658 0.29706 0.09761  0.00361  -0.02576 16  TYR   A N   
81   C CA  . TYR   A 36  ? 0.42108 0.22731 0.28575 0.08226  0.00195  -0.01119 16  TYR   A CA  
82   C C   . TYR   A 36  ? 0.44796 0.23044 0.32392 0.08681  -0.00003 -0.02712 16  TYR   A C   
83   O O   . TYR   A 36  ? 0.44690 0.22758 0.36703 0.06175  0.01041  -0.00133 16  TYR   A O   
84   C CB  . TYR   A 36  ? 0.38129 0.21874 0.29397 0.08611  0.00680  -0.01775 16  TYR   A CB  
85   C CG  . TYR   A 36  ? 0.38039 0.17952 0.29970 0.07263  0.02748  -0.02354 16  TYR   A CG  
86   C CD1 . TYR   A 36  ? 0.37325 0.16657 0.30373 0.07285  0.01503  -0.03791 16  TYR   A CD1 
87   C CD2 . TYR   A 36  ? 0.37338 0.18815 0.29622 0.05477  0.04662  -0.03747 16  TYR   A CD2 
88   C CE1 . TYR   A 36  ? 0.36768 0.17499 0.29085 0.06023  -0.00469 -0.04380 16  TYR   A CE1 
89   C CE2 . TYR   A 36  ? 0.36751 0.16744 0.29147 0.03709  0.04571  -0.05768 16  TYR   A CE2 
90   C CZ  . TYR   A 36  ? 0.35219 0.15668 0.28669 0.04254  0.01849  -0.02453 16  TYR   A CZ  
91   O OH  . TYR   A 36  ? 0.35413 0.14817 0.35163 0.04143  0.01732  -0.01775 16  TYR   A OH  
92   N N   . GLN   A 37  ? 0.47088 0.23010 0.38407 0.10748  -0.03283 -0.05432 17  GLN   A N   
93   C CA  . GLN   A 37  ? 0.51018 0.23554 0.43959 0.08786  -0.05963 -0.08088 17  GLN   A CA  
94   C C   . GLN   A 37  ? 0.50393 0.24770 0.45696 0.07085  -0.03168 -0.06877 17  GLN   A C   
95   O O   . GLN   A 37  ? 0.52277 0.26314 0.53122 0.06436  -0.02399 -0.07346 17  GLN   A O   
96   C CB  . GLN   A 37  ? 0.55160 0.24283 0.50066 0.08498  -0.10319 -0.10770 17  GLN   A CB  
97   C CG  . GLN   A 37  ? 0.59135 0.25232 0.60102 0.11701  -0.14336 -0.11465 17  GLN   A CG  
98   C CD  . GLN   A 37  ? 0.65916 0.30504 0.69269 0.13292  -0.17230 -0.08894 17  GLN   A CD  
99   O OE1 . GLN   A 37  ? 0.68041 0.35071 0.74817 0.14454  -0.20354 -0.09528 17  GLN   A OE1 
100  N NE2 . GLN   A 37  ? 0.67855 0.32502 0.72463 0.13260  -0.18270 -0.02193 17  GLN   A NE2 
101  N N   . ASP   A 38  ? 0.47749 0.21682 0.39540 0.06179  -0.02186 -0.07005 18  ASP   A N   
102  C CA  . ASP   A 38  ? 0.47941 0.22729 0.45303 0.05150  -0.01093 -0.02980 18  ASP   A CA  
103  C C   . ASP   A 38  ? 0.44232 0.21958 0.41556 0.04866  0.00652  -0.03958 18  ASP   A C   
104  O O   . ASP   A 38  ? 0.45055 0.23795 0.48235 0.06103  -0.00774 -0.06849 18  ASP   A O   
105  C CB  . ASP   A 38  ? 0.50643 0.24943 0.52950 0.06502  -0.02660 0.01611  18  ASP   A CB  
106  C CG  . ASP   A 38  ? 0.53257 0.30991 0.60197 0.07792  -0.04731 0.06341  18  ASP   A CG  
107  O OD1 . ASP   A 38  ? 0.52548 0.31754 0.59932 0.11500  -0.03596 0.03339  18  ASP   A OD1 
108  O OD2 . ASP   A 38  ? 0.55871 0.35105 0.65820 0.06363  -0.04597 0.10131  18  ASP   A OD2 
109  N N   . LEU   A 39  ? 0.42080 0.19507 0.34862 0.07269  0.03089  0.00526  19  LEU   A N   
110  C CA  . LEU   A 39  ? 0.40185 0.20719 0.30883 0.06550  0.03811  -0.01021 19  LEU   A CA  
111  C C   . LEU   A 39  ? 0.39480 0.19508 0.31590 0.04527  -0.00695 -0.02264 19  LEU   A C   
112  O O   . LEU   A 39  ? 0.43214 0.21461 0.30221 0.01675  0.02639  -0.02101 19  LEU   A O   
113  C CB  . LEU   A 39  ? 0.40397 0.23313 0.30908 0.07497  0.05601  0.00806  19  LEU   A CB  
114  C CG  . LEU   A 39  ? 0.39978 0.24932 0.36216 0.06601  0.04524  0.01655  19  LEU   A CG  
115  C CD1 . LEU   A 39  ? 0.38005 0.27164 0.38562 0.08469  0.02648  0.03667  19  LEU   A CD1 
116  C CD2 . LEU   A 39  ? 0.41500 0.26374 0.34824 0.05996  0.00100  -0.00922 19  LEU   A CD2 
117  N N   . PRO   A 40  ? 0.33055 0.20128 0.32899 0.01294  -0.00275 -0.00200 20  PRO   A N   
118  C CA  . PRO   A 40  ? 0.30586 0.18588 0.31902 0.01826  0.01208  0.00202  20  PRO   A CA  
119  C C   . PRO   A 40  ? 0.30102 0.17525 0.29761 0.02432  0.02319  -0.02407 20  PRO   A C   
120  O O   . PRO   A 40  ? 0.28346 0.18709 0.31200 0.04132  0.02223  -0.01450 20  PRO   A O   
121  C CB  . PRO   A 40  ? 0.31186 0.21134 0.32349 -0.00085 -0.01783 -0.00889 20  PRO   A CB  
122  C CG  . PRO   A 40  ? 0.33893 0.21641 0.36515 0.01453  -0.01073 -0.00055 20  PRO   A CG  
123  C CD  . PRO   A 40  ? 0.32901 0.21698 0.36117 -0.02156 -0.03813 -0.00678 20  PRO   A CD  
124  N N   . HIS   A 41  ? 0.32541 0.16312 0.28309 0.00597  0.02780  -0.00902 21  HIS   A N   
125  C CA  . HIS   A 41  ? 0.35015 0.16280 0.28007 -0.01207 0.02298  -0.01070 21  HIS   A CA  
126  C C   . HIS   A 41  ? 0.37420 0.17971 0.27905 0.00048  0.04466  -0.00988 21  HIS   A C   
127  O O   . HIS   A 41  ? 0.38641 0.22106 0.31133 0.02787  0.07532  -0.00765 21  HIS   A O   
128  C CB  . HIS   A 41  ? 0.37694 0.15428 0.27245 0.01522  0.04069  -0.02544 21  HIS   A CB  
129  C CG  . HIS   A 41  ? 0.41646 0.16964 0.31445 0.02560  0.01486  -0.02422 21  HIS   A CG  
130  N ND1 . HIS   A 41  ? 0.44323 0.19317 0.35337 0.05708  0.05189  -0.05142 21  HIS   A ND1 
131  C CD2 . HIS   A 41  ? 0.43311 0.18536 0.35545 0.03372  0.02862  -0.05900 21  HIS   A CD2 
132  C CE1 . HIS   A 41  ? 0.46875 0.21489 0.41785 0.03923  0.02555  -0.06971 21  HIS   A CE1 
133  N NE2 . HIS   A 41  ? 0.46362 0.21116 0.38654 0.03891  0.00317  -0.07966 21  HIS   A NE2 
134  N N   . LEU   A 42  ? 0.36143 0.18267 0.24585 0.00147  0.01827  -0.00440 22  LEU   A N   
135  C CA  . LEU   A 42  ? 0.38725 0.19606 0.25800 -0.00927 -0.01757 0.01011  22  LEU   A CA  
136  C C   . LEU   A 42  ? 0.36149 0.22162 0.23208 -0.01699 -0.01443 -0.00717 22  LEU   A C   
137  O O   . LEU   A 42  ? 0.38615 0.31987 0.27879 -0.03648 0.02628  -0.03030 22  LEU   A O   
138  C CB  . LEU   A 42  ? 0.44603 0.20299 0.31259 -0.02532 -0.00510 0.05916  22  LEU   A CB  
139  C CG  . LEU   A 42  ? 0.47957 0.22380 0.48177 -0.01500 0.03761  -0.00341 22  LEU   A CG  
140  C CD1 . LEU   A 42  ? 0.50160 0.25641 0.47610 -0.02877 0.09305  -0.04771 22  LEU   A CD1 
141  C CD2 . LEU   A 42  ? 0.45327 0.18468 0.52706 -0.00622 0.04777  0.00044  22  LEU   A CD2 
142  N N   . VAL   A 43  ? 0.34906 0.15171 0.23006 -0.00352 -0.00954 -0.02946 23  VAL   A N   
143  C CA  . VAL   A 43  ? 0.38663 0.15809 0.24205 0.01805  0.03852  -0.01526 23  VAL   A CA  
144  C C   . VAL   A 43  ? 0.38628 0.15893 0.25344 0.03759  0.00605  -0.00743 23  VAL   A C   
145  O O   . VAL   A 43  ? 0.40636 0.14971 0.28733 0.03347  0.01983  -0.00738 23  VAL   A O   
146  C CB  . VAL   A 43  ? 0.40519 0.15684 0.27092 0.01162  0.02031  -0.02589 23  VAL   A CB  
147  C CG1 . VAL   A 43  ? 0.40515 0.17580 0.28509 0.00649  0.01973  -0.02935 23  VAL   A CG1 
148  C CG2 . VAL   A 43  ? 0.42822 0.16781 0.31109 0.02218  -0.00096 -0.01392 23  VAL   A CG2 
149  N N   . ASN   A 44  ? 0.36126 0.15851 0.25083 0.05039  0.00394  -0.02265 24  ASN   A N   
150  C CA  . ASN   A 44  ? 0.36633 0.16878 0.22062 0.04782  0.00649  -0.02216 24  ASN   A CA  
151  C C   . ASN   A 44  ? 0.38572 0.17489 0.24391 0.02968  -0.01192 -0.02192 24  ASN   A C   
152  O O   . ASN   A 44  ? 0.38186 0.18775 0.26326 0.03314  -0.00022 0.00988  24  ASN   A O   
153  C CB  . ASN   A 44  ? 0.35568 0.17100 0.24889 0.03652  0.01933  -0.00863 24  ASN   A CB  
154  C CG  . ASN   A 44  ? 0.35859 0.17424 0.23008 0.03022  0.00791  -0.00955 24  ASN   A CG  
155  O OD1 . ASN   A 44  ? 0.36531 0.14857 0.23945 0.00648  -0.02860 -0.01766 24  ASN   A OD1 
156  N ND2 . ASN   A 44  ? 0.38755 0.18402 0.24256 0.01961  0.00184  0.00696  24  ASN   A ND2 
157  N N   . ALA   A 45  ? 0.38726 0.20781 0.24541 0.02399  -0.02737 -0.00726 25  ALA   A N   
158  C CA  . ALA   A 45  ? 0.42890 0.20836 0.25957 0.00911  -0.05588 -0.01214 25  ALA   A CA  
159  C C   . ALA   A 45  ? 0.44460 0.21335 0.27215 -0.00653 -0.05027 -0.01771 25  ALA   A C   
160  O O   . ALA   A 45  ? 0.48067 0.23096 0.32095 -0.02924 -0.05209 -0.04704 25  ALA   A O   
161  C CB  . ALA   A 45  ? 0.45952 0.23087 0.33496 0.02164  -0.07640 -0.02068 25  ALA   A CB  
162  N N   . ASP   A 46  ? 0.42445 0.21641 0.30307 -0.01580 -0.05697 -0.02811 26  ASP   A N   
163  C CA  . ASP   A 46  ? 0.39977 0.22583 0.30351 -0.02162 -0.02558 -0.04694 26  ASP   A CA  
164  C C   . ASP   A 46  ? 0.42309 0.22579 0.30317 -0.02400 -0.04063 -0.04101 26  ASP   A C   
165  O O   . ASP   A 46  ? 0.42592 0.23509 0.40637 -0.03345 -0.07253 -0.01819 26  ASP   A O   
166  C CB  . ASP   A 46  ? 0.38118 0.27604 0.32043 -0.00872 -0.03928 -0.03647 26  ASP   A CB  
167  C CG  . ASP   A 46  ? 0.38884 0.30914 0.36460 -0.01237 -0.05688 -0.04856 26  ASP   A CG  
168  O OD1 . ASP   A 46  ? 0.42309 0.34818 0.38456 -0.00599 -0.05461 -0.06177 26  ASP   A OD1 
169  O OD2 . ASP   A 46  ? 0.38684 0.28717 0.43449 -0.03477 -0.02999 -0.02557 26  ASP   A OD2 
170  N N   . GLY   A 47  ? 0.43273 0.21923 0.25178 0.00504  -0.04613 -0.03781 27  GLY   A N   
171  C CA  . GLY   A 47  ? 0.43836 0.19735 0.23836 0.02691  -0.02102 -0.03315 27  GLY   A CA  
172  C C   . GLY   A 47  ? 0.41316 0.18817 0.28675 0.02533  -0.03316 -0.02287 27  GLY   A C   
173  O O   . GLY   A 47  ? 0.42024 0.19046 0.31679 0.00899  -0.04340 -0.00951 27  GLY   A O   
174  N N   . GLN   A 48  ? 0.38735 0.17522 0.24408 0.01802  -0.02474 -0.02541 28  GLN   A N   
175  C CA  . GLN   A 48  ? 0.37437 0.18439 0.23852 0.00213  -0.00653 -0.03265 28  GLN   A CA  
176  C C   . GLN   A 48  ? 0.35915 0.17689 0.25364 -0.01581 -0.02061 -0.01746 28  GLN   A C   
177  O O   . GLN   A 48  ? 0.37378 0.19249 0.25070 -0.00918 -0.02127 0.01384  28  GLN   A O   
178  C CB  . GLN   A 48  ? 0.36310 0.19752 0.29879 -0.02429 -0.02025 -0.02981 28  GLN   A CB  
179  C CG  . GLN   A 48  ? 0.34577 0.21345 0.32741 -0.02422 -0.00922 -0.00776 28  GLN   A CG  
180  C CD  . GLN   A 48  ? 0.35587 0.20537 0.32779 -0.03072 0.01932  -0.01481 28  GLN   A CD  
181  O OE1 . GLN   A 48  ? 0.35562 0.19658 0.31295 -0.04507 0.02272  -0.00501 28  GLN   A OE1 
182  N NE2 . GLN   A 48  ? 0.34165 0.22232 0.34890 -0.03405 0.02563  -0.04258 28  GLN   A NE2 
183  N N   . TYR   A 49  ? 0.34138 0.16644 0.26485 0.01387  -0.01586 -0.02357 29  TYR   A N   
184  C CA  . TYR   A 49  ? 0.33859 0.13819 0.26891 0.02142  -0.02761 -0.01284 29  TYR   A CA  
185  C C   . TYR   A 49  ? 0.35874 0.15943 0.25152 0.03249  -0.01571 -0.01889 29  TYR   A C   
186  O O   . TYR   A 49  ? 0.35549 0.16508 0.24687 0.00246  0.01177  -0.01937 29  TYR   A O   
187  C CB  . TYR   A 49  ? 0.30912 0.13360 0.27640 0.04140  0.00830  -0.00569 29  TYR   A CB  
188  C CG  . TYR   A 49  ? 0.34968 0.15441 0.27091 0.03116  -0.00110 -0.02090 29  TYR   A CG  
189  C CD1 . TYR   A 49  ? 0.39729 0.15335 0.32581 0.03463  0.00913  -0.03537 29  TYR   A CD1 
190  C CD2 . TYR   A 49  ? 0.35066 0.17376 0.29146 0.04774  -0.00762 -0.02025 29  TYR   A CD2 
191  C CE1 . TYR   A 49  ? 0.38141 0.16201 0.31574 0.04791  0.03337  -0.03216 29  TYR   A CE1 
192  C CE2 . TYR   A 49  ? 0.35967 0.15877 0.29008 0.04609  -0.00617 -0.02003 29  TYR   A CE2 
193  C CZ  . TYR   A 49  ? 0.37117 0.16672 0.28636 0.04482  0.03521  -0.01501 29  TYR   A CZ  
194  O OH  . TYR   A 49  ? 0.39615 0.17524 0.27380 0.04181  0.03988  -0.02937 29  TYR   A OH  
195  N N   . LEU   A 50  ? 0.37045 0.15731 0.24122 0.01914  -0.00390 -0.00739 30  LEU   A N   
196  C CA  . LEU   A 50  ? 0.34789 0.15495 0.22399 0.03495  -0.02664 -0.03543 30  LEU   A CA  
197  C C   . LEU   A 50  ? 0.33235 0.17839 0.21509 0.03067  -0.00986 -0.02793 30  LEU   A C   
198  O O   . LEU   A 50  ? 0.34559 0.19124 0.22579 0.00537  0.02090  -0.03322 30  LEU   A O   
199  C CB  . LEU   A 50  ? 0.32579 0.16015 0.23664 0.01961  -0.05325 0.00898  30  LEU   A CB  
200  C CG  . LEU   A 50  ? 0.34953 0.19132 0.26038 0.01201  -0.08207 0.01611  30  LEU   A CG  
201  C CD1 . LEU   A 50  ? 0.36646 0.17764 0.31719 0.01333  -0.08726 0.01664  30  LEU   A CD1 
202  C CD2 . LEU   A 50  ? 0.35838 0.22102 0.33105 -0.00863 -0.06624 -0.02663 30  LEU   A CD2 
203  N N   . PHE   A 51  ? 0.32664 0.17042 0.23455 0.00183  -0.03580 -0.01396 31  PHE   A N   
204  C CA  . PHE   A 51  ? 0.32274 0.16131 0.20837 0.00462  -0.00648 -0.02263 31  PHE   A CA  
205  C C   . PHE   A 51  ? 0.32295 0.16840 0.25224 0.00162  0.00281  0.00176  31  PHE   A C   
206  O O   . PHE   A 51  ? 0.30501 0.16153 0.27092 0.02109  0.01609  0.00514  31  PHE   A O   
207  C CB  . PHE   A 51  ? 0.34082 0.14240 0.20175 0.02224  0.01414  -0.03245 31  PHE   A CB  
208  C CG  . PHE   A 51  ? 0.32584 0.16840 0.22868 0.00744  0.00690  -0.01708 31  PHE   A CG  
209  C CD1 . PHE   A 51  ? 0.33947 0.18594 0.28723 0.01767  -0.01624 -0.03442 31  PHE   A CD1 
210  C CD2 . PHE   A 51  ? 0.35120 0.18008 0.24100 -0.00464 0.00328  -0.03802 31  PHE   A CD2 
211  C CE1 . PHE   A 51  ? 0.35926 0.20409 0.31387 0.02267  -0.00111 -0.01704 31  PHE   A CE1 
212  C CE2 . PHE   A 51  ? 0.37223 0.20652 0.28054 -0.00259 -0.00348 -0.05214 31  PHE   A CE2 
213  C CZ  . PHE   A 51  ? 0.36132 0.21452 0.30352 0.00258  0.01955  -0.02658 31  PHE   A CZ  
214  N N   . CYS   A 52  ? 0.29238 0.15667 0.22909 0.00418  0.04225  -0.00261 32  CYS   A N   
215  C CA  . CYS   A 52  ? 0.30769 0.16270 0.28313 -0.01382 0.04199  -0.01645 32  CYS   A CA  
216  C C   . CYS   A 52  ? 0.28298 0.15681 0.28454 0.01078  0.00192  -0.00236 32  CYS   A C   
217  O O   . CYS   A 52  ? 0.27975 0.18512 0.30137 0.02924  -0.00903 -0.00599 32  CYS   A O   
218  C CB  . CYS   A 52  ? 0.28966 0.18112 0.30889 0.00496  0.05733  -0.01224 32  CYS   A CB  
219  S SG  . CYS   A 52  ? 0.32401 0.19070 0.29972 0.01385  0.03333  -0.01674 32  CYS   A SG  
220  N N   . ARG   A 53  ? 0.28250 0.15540 0.25396 0.01228  0.03090  -0.01515 33  ARG   A N   
221  C CA  . ARG   A 53  ? 0.30033 0.17849 0.24311 0.03541  0.02009  0.00426  33  ARG   A CA  
222  C C   . ARG   A 53  ? 0.25768 0.19334 0.26540 0.00501  -0.00153 0.01474  33  ARG   A C   
223  O O   . ARG   A 53  ? 0.27069 0.20008 0.28635 -0.02455 -0.00848 -0.01508 33  ARG   A O   
224  C CB  . ARG   A 53  ? 0.35552 0.22484 0.28167 0.05922  0.04954  -0.00247 33  ARG   A CB  
225  C CG  . ARG   A 53  ? 0.36778 0.24189 0.26742 0.06333  0.06715  -0.01266 33  ARG   A CG  
226  C CD  . ARG   A 53  ? 0.36066 0.23612 0.25326 0.04081  0.03960  -0.02892 33  ARG   A CD  
227  N NE  . ARG   A 53  ? 0.35808 0.22913 0.25159 0.05449  0.01516  0.00143  33  ARG   A NE  
228  C CZ  . ARG   A 53  ? 0.37303 0.26614 0.28060 0.08700  0.00120  0.01807  33  ARG   A CZ  
229  N NH1 . ARG   A 53  ? 0.36615 0.30568 0.37924 0.08510  -0.00404 0.01682  33  ARG   A NH1 
230  N NH2 . ARG   A 53  ? 0.35847 0.24472 0.30874 0.06773  0.01168  0.01824  33  ARG   A NH2 
231  N N   . TYR   A 54  ? 0.28089 0.20142 0.33444 0.02441  0.02189  -0.01337 34  TYR   A N   
232  C CA  . TYR   A 54  ? 0.30551 0.20772 0.33083 0.00594  -0.00478 -0.02238 34  TYR   A CA  
233  C C   . TYR   A 54  ? 0.33152 0.20216 0.33354 -0.00222 -0.02173 -0.02199 34  TYR   A C   
234  O O   . TYR   A 54  ? 0.34896 0.19285 0.38349 0.01043  -0.01243 -0.00910 34  TYR   A O   
235  C CB  . TYR   A 54  ? 0.29447 0.20360 0.35527 0.01087  -0.00545 -0.01031 34  TYR   A CB  
236  C CG  . TYR   A 54  ? 0.27155 0.20429 0.33408 -0.01418 -0.00834 -0.02686 34  TYR   A CG  
237  C CD1 . TYR   A 54  ? 0.25120 0.19448 0.32277 -0.00919 0.01099  -0.01977 34  TYR   A CD1 
238  C CD2 . TYR   A 54  ? 0.25580 0.19674 0.30200 -0.01593 0.00870  -0.03728 34  TYR   A CD2 
239  C CE1 . TYR   A 54  ? 0.25741 0.19795 0.32788 -0.00273 0.03941  -0.05884 34  TYR   A CE1 
240  C CE2 . TYR   A 54  ? 0.24277 0.21027 0.30922 0.00944  0.00183  -0.04279 34  TYR   A CE2 
241  C CZ  . TYR   A 54  ? 0.28542 0.21114 0.32136 0.01293  0.02084  -0.05049 34  TYR   A CZ  
242  O OH  . TYR   A 54  ? 0.31020 0.22649 0.32257 0.00356  -0.01589 -0.04669 34  TYR   A OH  
243  N N   . TRP   A 55  ? 0.30782 0.20183 0.34579 -0.00099 -0.00899 -0.03651 35  TRP   A N   
244  C CA  . TRP   A 55  ? 0.30743 0.22457 0.36481 -0.01062 0.00268  -0.04637 35  TRP   A CA  
245  C C   . TRP   A 55  ? 0.30752 0.25495 0.39100 -0.00027 0.00668  -0.02685 35  TRP   A C   
246  O O   . TRP   A 55  ? 0.28480 0.26471 0.42087 -0.02581 0.01154  0.00213  35  TRP   A O   
247  C CB  . TRP   A 55  ? 0.31361 0.23352 0.35229 0.00066  0.01036  -0.01669 35  TRP   A CB  
248  C CG  . TRP   A 55  ? 0.31460 0.21624 0.34836 0.02057  0.00070  -0.01888 35  TRP   A CG  
249  C CD1 . TRP   A 55  ? 0.32392 0.21727 0.36032 0.00026  -0.00685 0.01950  35  TRP   A CD1 
250  C CD2 . TRP   A 55  ? 0.33477 0.19616 0.36280 0.00939  -0.02266 -0.01530 35  TRP   A CD2 
251  N NE1 . TRP   A 55  ? 0.33732 0.23153 0.38037 -0.00414 -0.01843 -0.00842 35  TRP   A NE1 
252  C CE2 . TRP   A 55  ? 0.34260 0.19441 0.38880 -0.00218 -0.04082 -0.00376 35  TRP   A CE2 
253  C CE3 . TRP   A 55  ? 0.36546 0.18158 0.39385 -0.00026 -0.02867 -0.02990 35  TRP   A CE3 
254  C CZ2 . TRP   A 55  ? 0.37430 0.17473 0.39308 -0.01940 0.00273  -0.01231 35  TRP   A CZ2 
255  C CZ3 . TRP   A 55  ? 0.36775 0.14704 0.38920 -0.03359 0.01839  0.02213  35  TRP   A CZ3 
256  C CH2 . TRP   A 55  ? 0.38530 0.16850 0.41201 -0.00364 0.00882  0.00786  35  TRP   A CH2 
257  N N   . ALA   A 56  ? 0.32310 0.27233 0.41060 0.03837  0.01451  -0.02087 36  ALA   A N   
258  C CA  . ALA   A 56  ? 0.32425 0.29513 0.43788 0.03872  0.01129  0.00735  36  ALA   A CA  
259  C C   . ALA   A 56  ? 0.33653 0.33077 0.50424 0.03539  0.04155  0.03625  36  ALA   A C   
260  O O   . ALA   A 56  ? 0.34494 0.34348 0.49865 0.02361  0.07875  0.02157  36  ALA   A O   
261  C CB  . ALA   A 56  ? 0.33695 0.30891 0.40987 0.05154  0.01413  0.00010  36  ALA   A CB  
262  N N   . PRO   A 57  ? 0.33088 0.34609 0.56430 0.00112  0.04316  0.01819  37  PRO   A N   
263  C CA  . PRO   A 57  ? 0.34985 0.39147 0.65322 0.00640  0.05510  0.02677  37  PRO   A CA  
264  C C   . PRO   A 57  ? 0.37586 0.45250 0.74623 0.01596  0.08939  0.04249  37  PRO   A C   
265  O O   . PRO   A 57  ? 0.36711 0.45040 0.71050 0.04045  0.09641  0.04353  37  PRO   A O   
266  C CB  . PRO   A 57  ? 0.35519 0.36877 0.62021 -0.00253 0.03105  0.01679  37  PRO   A CB  
267  C CG  . PRO   A 57  ? 0.33544 0.35729 0.59697 -0.01360 0.01432  0.02159  37  PRO   A CG  
268  C CD  . PRO   A 57  ? 0.32655 0.34853 0.57840 0.00404  0.02931  0.02042  37  PRO   A CD  
269  N N   . THR   A 58  ? 0.39637 0.50626 0.82257 -0.00005 0.11600  0.06643  38  THR   A N   
270  C CA  . THR   A 58  ? 0.44298 0.56344 0.90353 -0.03147 0.10457  0.10351  38  THR   A CA  
271  C C   . THR   A 58  ? 0.47073 0.59331 0.96041 -0.01725 0.13791  0.11419  38  THR   A C   
272  O O   . THR   A 58  ? 0.45776 0.60318 0.99390 0.00746  0.17709  0.10276  38  THR   A O   
273  C CB  . THR   A 58  ? 0.45579 0.58709 0.93925 -0.04755 0.05534  0.10956  38  THR   A CB  
274  O OG1 . THR   A 58  ? 0.46136 0.60598 0.98422 -0.06249 0.02159  0.11173  38  THR   A OG1 
275  C CG2 . THR   A 58  ? 0.46745 0.59323 0.93720 -0.04642 0.03746  0.10120  38  THR   A CG2 
276  N N   . GLY   A 59  ? 0.49472 0.59386 0.94798 -0.03910 0.15630  0.15214  39  GLY   A N   
277  C CA  . GLY   A 59  ? 0.51207 0.59754 0.92710 -0.03537 0.17359  0.17214  39  GLY   A CA  
278  C C   . GLY   A 59  ? 0.53414 0.59444 0.90605 -0.03397 0.19389  0.18201  39  GLY   A C   
279  O O   . GLY   A 59  ? 0.55787 0.58655 0.89336 -0.04861 0.17771  0.19905  39  GLY   A O   
280  N N   . THR   A 60  ? 0.52685 0.58719 0.87823 -0.01775 0.23429  0.17629  40  THR   A N   
281  C CA  . THR   A 60  ? 0.53046 0.56914 0.85727 -0.00891 0.23041  0.14533  40  THR   A CA  
282  C C   . THR   A 60  ? 0.48374 0.51247 0.79561 -0.01924 0.23329  0.09303  40  THR   A C   
283  O O   . THR   A 60  ? 0.46775 0.51846 0.84081 -0.04446 0.23653  0.12195  40  THR   A O   
284  C CB  . THR   A 60  ? 0.58959 0.59349 0.90905 0.01759  0.21278  0.13873  40  THR   A CB  
285  O OG1 . THR   A 60  ? 0.64990 0.61267 0.93947 0.02665  0.17476  0.13693  40  THR   A OG1 
286  C CG2 . THR   A 60  ? 0.60746 0.60323 0.91988 0.02644  0.23354  0.17043  40  THR   A CG2 
287  N N   . PRO   A 61  ? 0.47172 0.45726 0.71503 -0.01882 0.17908  0.03177  41  PRO   A N   
288  C CA  . PRO   A 61  ? 0.44241 0.41230 0.63253 -0.03897 0.16546  0.01235  41  PRO   A CA  
289  C C   . PRO   A 61  ? 0.42736 0.38781 0.55496 -0.06268 0.15552  0.00695  41  PRO   A C   
290  O O   . PRO   A 61  ? 0.46210 0.39387 0.53255 -0.06041 0.17215  -0.00072 41  PRO   A O   
291  C CB  . PRO   A 61  ? 0.47113 0.41759 0.65321 -0.02595 0.14130  0.00445  41  PRO   A CB  
292  C CG  . PRO   A 61  ? 0.49379 0.43078 0.67924 -0.01815 0.13445  -0.00184 41  PRO   A CG  
293  C CD  . PRO   A 61  ? 0.48322 0.43964 0.68461 -0.01602 0.16346  0.01145  41  PRO   A CD  
294  N N   . LYS   A 62  ? 0.40388 0.35372 0.51607 -0.07968 0.11008  0.00421  42  LYS   A N   
295  C CA  . LYS   A 62  ? 0.40733 0.33405 0.47696 -0.08454 0.08341  0.01139  42  LYS   A CA  
296  C C   . LYS   A 62  ? 0.40205 0.31043 0.43886 -0.04892 0.10920  0.01905  42  LYS   A C   
297  O O   . LYS   A 62  ? 0.42453 0.33513 0.47491 -0.06161 0.13943  0.03773  42  LYS   A O   
298  C CB  . LYS   A 62  ? 0.42101 0.35216 0.51418 -0.12771 0.04280  -0.00681 42  LYS   A CB  
299  C CG  . LYS   A 62  ? 0.47023 0.38662 0.59365 -0.14987 0.02302  -0.02528 42  LYS   A CG  
300  C CD  . LYS   A 62  ? 0.51521 0.42312 0.66228 -0.16079 0.01527  -0.06504 42  LYS   A CD  
301  C CE  . LYS   A 62  ? 0.55290 0.45769 0.70722 -0.16281 -0.00239 -0.08386 42  LYS   A CE  
302  N NZ  . LYS   A 62  ? 0.57205 0.47949 0.74128 -0.15727 -0.00659 -0.09096 42  LYS   A NZ  
303  N N   . ALA   A 63  ? 0.36591 0.26671 0.43089 -0.03647 0.10333  0.00964  43  ALA   A N   
304  C CA  . ALA   A 63  ? 0.33457 0.21907 0.43124 -0.01620 0.09545  0.01098  43  ALA   A CA  
305  C C   . ALA   A 63  ? 0.32316 0.21855 0.38652 -0.03498 0.08971  0.02042  43  ALA   A C   
306  O O   . ALA   A 63  ? 0.33181 0.24612 0.40049 -0.04611 0.07107  -0.01851 43  ALA   A O   
307  C CB  . ALA   A 63  ? 0.32039 0.22158 0.45257 0.03049  0.10909  -0.01917 43  ALA   A CB  
308  N N   . LEU   A 64  ? 0.28226 0.22294 0.36749 -0.02441 0.09749  0.00830  44  LEU   A N   
309  C CA  . LEU   A 64  ? 0.30920 0.21792 0.32440 -0.01443 0.11781  -0.01169 44  LEU   A CA  
310  C C   . LEU   A 64  ? 0.32886 0.20975 0.31156 -0.02072 0.10473  0.00350  44  LEU   A C   
311  O O   . LEU   A 64  ? 0.35153 0.20612 0.32292 0.01524  0.06936  0.01330  44  LEU   A O   
312  C CB  . LEU   A 64  ? 0.32855 0.23863 0.33210 0.00068  0.09632  -0.05652 44  LEU   A CB  
313  C CG  . LEU   A 64  ? 0.37557 0.27235 0.39650 0.04659  0.07020  -0.05502 44  LEU   A CG  
314  C CD1 . LEU   A 64  ? 0.39429 0.27699 0.40179 0.03725  0.11091  -0.07367 44  LEU   A CD1 
315  C CD2 . LEU   A 64  ? 0.40580 0.31900 0.43370 0.06120  0.02588  -0.06065 44  LEU   A CD2 
316  N N   . ILE   A 65  ? 0.32921 0.18590 0.29611 -0.02382 0.10309  -0.01375 45  ILE   A N   
317  C CA  . ILE   A 65  ? 0.29342 0.16950 0.31740 -0.01245 0.10618  -0.00346 45  ILE   A CA  
318  C C   . ILE   A 65  ? 0.28482 0.16292 0.30069 0.01131  0.05123  0.02159  45  ILE   A C   
319  O O   . ILE   A 65  ? 0.27776 0.15928 0.33531 -0.00415 0.04051  0.02679  45  ILE   A O   
320  C CB  . ILE   A 65  ? 0.28727 0.18142 0.31752 0.00550  0.05104  -0.02498 45  ILE   A CB  
321  C CG1 . ILE   A 65  ? 0.31123 0.16938 0.36442 0.00475  0.11040  -0.02988 45  ILE   A CG1 
322  C CG2 . ILE   A 65  ? 0.32628 0.20862 0.31924 0.01113  0.04365  0.00006  45  ILE   A CG2 
323  C CD1 . ILE   A 65  ? 0.32534 0.18437 0.36046 0.00424  0.09275  -0.02929 45  ILE   A CD1 
324  N N   . PHE   A 66  ? 0.24451 0.16582 0.28970 -0.00811 0.05137  0.00588  46  PHE   A N   
325  C CA  . PHE   A 66  ? 0.27218 0.16879 0.25208 -0.01484 0.04896  -0.00099 46  PHE   A CA  
326  C C   . PHE   A 66  ? 0.28194 0.15322 0.22742 0.01946  0.01024  -0.00424 46  PHE   A C   
327  O O   . PHE   A 66  ? 0.26274 0.15575 0.26370 0.03017  0.06485  0.00414  46  PHE   A O   
328  C CB  . PHE   A 66  ? 0.27130 0.17007 0.21753 -0.00737 0.02623  -0.00286 46  PHE   A CB  
329  C CG  . PHE   A 66  ? 0.27858 0.14705 0.24285 0.01217  0.01524  0.01035  46  PHE   A CG  
330  C CD1 . PHE   A 66  ? 0.31044 0.14495 0.27834 0.00479  -0.00979 0.01577  46  PHE   A CD1 
331  C CD2 . PHE   A 66  ? 0.26288 0.15991 0.26629 -0.01248 0.00690  -0.00791 46  PHE   A CD2 
332  C CE1 . PHE   A 66  ? 0.29434 0.16811 0.24187 -0.00669 -0.01999 0.01239  46  PHE   A CE1 
333  C CE2 . PHE   A 66  ? 0.27512 0.15354 0.27283 0.01350  0.01092  0.00183  46  PHE   A CE2 
334  C CZ  . PHE   A 66  ? 0.29267 0.16457 0.26640 0.03031  -0.02115 -0.01240 46  PHE   A CZ  
335  N N   . VAL   A 67  ? 0.27024 0.15989 0.20508 -0.00483 -0.00943 -0.00759 47  VAL   A N   
336  C CA  . VAL   A 67  ? 0.24912 0.16827 0.21344 -0.00601 -0.01087 -0.01199 47  VAL   A CA  
337  C C   . VAL   A 67  ? 0.25994 0.15465 0.26017 0.01138  0.00325  0.00048  47  VAL   A C   
338  O O   . VAL   A 67  ? 0.28326 0.15154 0.28540 0.00585  0.01113  -0.00962 47  VAL   A O   
339  C CB  . VAL   A 67  ? 0.21575 0.21701 0.25000 -0.00096 0.00040  -0.02447 47  VAL   A CB  
340  C CG1 . VAL   A 67  ? 0.22685 0.24462 0.24869 0.03052  0.03217  -0.02937 47  VAL   A CG1 
341  C CG2 . VAL   A 67  ? 0.19067 0.23948 0.29177 -0.01448 -0.00118 -0.02950 47  VAL   A CG2 
342  N N   . SER   A 68  ? 0.22702 0.17459 0.25516 0.00043  0.00020  0.00214  48  SER   A N   
343  C CA  . SER   A 68  ? 0.24449 0.16580 0.25278 0.01742  0.02398  0.00247  48  SER   A CA  
344  C C   . SER   A 68  ? 0.25476 0.13871 0.25464 0.00847  0.01918  0.03036  48  SER   A C   
345  O O   . SER   A 68  ? 0.24345 0.13268 0.25871 0.00807  0.01464  0.00218  48  SER   A O   
346  C CB  . SER   A 68  ? 0.26356 0.16718 0.24359 0.01089  0.01018  -0.00881 48  SER   A CB  
347  O OG  . SER   A 68  ? 0.24864 0.19112 0.29204 0.00852  0.02155  -0.01830 48  SER   A OG  
348  N N   . HIS   A 69  ? 0.28095 0.13038 0.21573 -0.03581 0.00757  0.03009  49  HIS   A N   
349  C CA  . HIS   A 69  ? 0.26729 0.13103 0.20916 -0.00309 0.00624  0.04882  49  HIS   A CA  
350  C C   . HIS   A 69  ? 0.27367 0.13843 0.24517 -0.00644 0.02468  0.02131  49  HIS   A C   
351  O O   . HIS   A 69  ? 0.29615 0.14670 0.23799 0.02222  0.01915  0.00788  49  HIS   A O   
352  C CB  . HIS   A 69  ? 0.29455 0.11930 0.22641 -0.01518 -0.01462 0.02958  49  HIS   A CB  
353  C CG  . HIS   A 69  ? 0.28405 0.12244 0.23773 -0.02250 -0.01351 0.02864  49  HIS   A CG  
354  N ND1 . HIS   A 69  ? 0.27908 0.12848 0.22773 -0.02497 -0.00976 0.00151  49  HIS   A ND1 
355  C CD2 . HIS   A 69  ? 0.29362 0.12934 0.26295 -0.01495 -0.02875 -0.00857 49  HIS   A CD2 
356  C CE1 . HIS   A 69  ? 0.26357 0.13553 0.22495 0.01790  -0.01318 -0.00513 49  HIS   A CE1 
357  N NE2 . HIS   A 69  ? 0.28448 0.14240 0.22310 0.02659  0.01784  0.00054  49  HIS   A NE2 
358  N N   . GLY   A 70  ? 0.26508 0.12601 0.25907 0.01096  0.01889  0.01658  50  GLY   A N   
359  C CA  . GLY   A 70  ? 0.24305 0.13716 0.25777 0.03221  0.01320  0.02464  50  GLY   A CA  
360  C C   . GLY   A 70  ? 0.21912 0.13091 0.25637 0.04168  0.03789  0.00372  50  GLY   A C   
361  O O   . GLY   A 70  ? 0.25694 0.13582 0.24493 0.00662  0.00048  0.00738  50  GLY   A O   
362  N N   . ALA   A 71  ? 0.19627 0.14451 0.22565 -0.01098 0.04125  0.00453  51  ALA   A N   
363  C CA  . ALA   A 71  ? 0.23097 0.15344 0.23943 -0.00252 0.00064  0.02168  51  ALA   A CA  
364  C C   . ALA   A 71  ? 0.28174 0.16426 0.24263 -0.02100 0.02052  0.01758  51  ALA   A C   
365  O O   . ALA   A 71  ? 0.29712 0.18168 0.26258 0.00387  -0.00179 0.01486  51  ALA   A O   
366  C CB  . ALA   A 71  ? 0.26762 0.16171 0.26232 0.03775  -0.00693 0.00641  51  ALA   A CB  
367  N N   . GLY   A 72  ? 0.30392 0.15191 0.24642 -0.01642 -0.00509 0.04417  52  GLY   A N   
368  C CA  . GLY   A 72  ? 0.30922 0.18706 0.26497 0.01286  -0.04633 0.05908  52  GLY   A CA  
369  C C   . GLY   A 72  ? 0.29965 0.19917 0.29292 0.01514  -0.04347 0.04384  52  GLY   A C   
370  O O   . GLY   A 72  ? 0.34887 0.24295 0.35319 0.00456  -0.02978 0.05763  52  GLY   A O   
371  N N   . GLU   A 73  ? 0.24316 0.16304 0.25945 -0.00540 -0.03116 0.01643  53  GLU   A N   
372  C CA  . GLU   A 73  ? 0.24864 0.15613 0.24327 -0.00343 0.00379  0.00721  53  GLU   A CA  
373  C C   . GLU   A 73  ? 0.25114 0.15692 0.21051 -0.00538 -0.03774 -0.01873 53  GLU   A C   
374  O O   . GLU   A 73  ? 0.27960 0.17151 0.23850 -0.01768 -0.01789 -0.00033 53  GLU   A O   
375  C CB  . GLU   A 73  ? 0.27169 0.15184 0.25269 -0.01503 0.02346  0.01707  53  GLU   A CB  
376  C CG  . GLU   A 73  ? 0.28009 0.14238 0.25192 -0.00582 0.04903  0.04901  53  GLU   A CG  
377  C CD  . GLU   A 73  ? 0.29902 0.15651 0.23184 0.01383  0.01078  0.02806  53  GLU   A CD  
378  O OE1 . GLU   A 73  ? 0.33592 0.17446 0.24815 0.01297  0.01279  0.00941  53  GLU   A OE1 
379  O OE2 . GLU   A 73  ? 0.29957 0.14359 0.25697 0.02288  0.01937  0.01688  53  GLU   A OE2 
380  N N   . HIS   A 74  ? 0.26368 0.15550 0.24661 0.02748  0.02236  0.01283  54  HIS   A N   
381  C CA  . HIS   A 74  ? 0.27729 0.15584 0.26265 0.03277  0.03488  0.01067  54  HIS   A CA  
382  C C   . HIS   A 74  ? 0.29338 0.15107 0.23157 0.02950  0.03106  0.00460  54  HIS   A C   
383  O O   . HIS   A 74  ? 0.32440 0.15045 0.25332 0.02341  0.02731  -0.00524 54  HIS   A O   
384  C CB  . HIS   A 74  ? 0.24458 0.16735 0.23160 0.04070  0.03405  0.00687  54  HIS   A CB  
385  C CG  . HIS   A 74  ? 0.27750 0.16098 0.22226 0.03999  -0.00521 0.01981  54  HIS   A CG  
386  N ND1 . HIS   A 74  ? 0.30205 0.16790 0.24768 0.03188  0.01449  -0.00939 54  HIS   A ND1 
387  C CD2 . HIS   A 74  ? 0.32186 0.17369 0.23191 0.03079  -0.01820 0.01546  54  HIS   A CD2 
388  C CE1 . HIS   A 74  ? 0.30845 0.18085 0.22634 0.03572  0.03076  -0.00008 54  HIS   A CE1 
389  N NE2 . HIS   A 74  ? 0.29747 0.18813 0.24907 0.06032  -0.00860 0.01400  54  HIS   A NE2 
390  N N   . SER   A 75  ? 0.28414 0.15928 0.20946 0.02964  0.01243  0.01806  55  SER   A N   
391  C CA  . SER   A 75  ? 0.28910 0.14944 0.22370 0.00666  0.00458  0.02086  55  SER   A CA  
392  C C   . SER   A 75  ? 0.27304 0.14824 0.24795 0.02544  0.01613  0.02788  55  SER   A C   
393  O O   . SER   A 75  ? 0.28231 0.18166 0.28272 -0.00058 0.02271  -0.00179 55  SER   A O   
394  C CB  . SER   A 75  ? 0.28929 0.16366 0.26279 0.02361  0.02357  -0.00570 55  SER   A CB  
395  O OG  . SER   A 75  ? 0.31492 0.17647 0.28867 -0.00225 0.02169  -0.03119 55  SER   A OG  
396  N N   . GLY   A 76  ? 0.28253 0.15616 0.20896 0.03735  -0.01789 0.01404  56  GLY   A N   
397  C CA  . GLY   A 76  ? 0.28199 0.17937 0.22579 0.04863  0.00312  -0.00642 56  GLY   A CA  
398  C C   . GLY   A 76  ? 0.28077 0.17785 0.25522 0.03464  -0.01239 -0.01785 56  GLY   A C   
399  O O   . GLY   A 76  ? 0.28046 0.20350 0.29251 0.02154  -0.02213 -0.01725 56  GLY   A O   
400  N N   . ARG   A 77  ? 0.29128 0.15238 0.24719 0.02341  0.04028  -0.00600 57  ARG   A N   
401  C CA  . ARG   A 77  ? 0.30196 0.14687 0.25385 0.01120  0.09035  -0.01290 57  ARG   A CA  
402  C C   . ARG   A 77  ? 0.27563 0.16829 0.27846 -0.00065 0.05909  -0.00609 57  ARG   A C   
403  O O   . ARG   A 77  ? 0.30582 0.17772 0.29113 0.00065  0.04976  -0.03236 57  ARG   A O   
404  C CB  . ARG   A 77  ? 0.32057 0.16059 0.34998 0.00123  0.09866  -0.00267 57  ARG   A CB  
405  C CG  . ARG   A 77  ? 0.32631 0.17680 0.43083 0.02209  0.07951  0.04445  57  ARG   A CG  
406  C CD  . ARG   A 77  ? 0.30758 0.18247 0.36411 0.02777  0.06433  0.02889  57  ARG   A CD  
407  N NE  . ARG   A 77  ? 0.31723 0.15939 0.25046 0.02570  0.03400  -0.00169 57  ARG   A NE  
408  C CZ  . ARG   A 77  ? 0.31939 0.16683 0.24873 0.01698  0.03716  0.02489  57  ARG   A CZ  
409  N NH1 . ARG   A 77  ? 0.30702 0.18980 0.25942 -0.00633 0.02578  0.03184  57  ARG   A NH1 
410  N NH2 . ARG   A 77  ? 0.31238 0.16263 0.25367 0.03382  0.00769  0.00052  57  ARG   A NH2 
411  N N   . TYR   A 78  ? 0.26821 0.17232 0.23905 0.02070  0.02778  0.03003  58  TYR   A N   
412  C CA  . TYR   A 78  ? 0.26704 0.16956 0.24062 -0.00138 -0.01458 0.01668  58  TYR   A CA  
413  C C   . TYR   A 78  ? 0.29314 0.18534 0.25885 0.02601  -0.04650 0.01396  58  TYR   A C   
414  O O   . TYR   A 78  ? 0.31032 0.20504 0.28724 0.00598  -0.00310 0.02693  58  TYR   A O   
415  C CB  . TYR   A 78  ? 0.27396 0.17992 0.25341 0.01016  -0.03046 -0.00745 58  TYR   A CB  
416  C CG  . TYR   A 78  ? 0.26324 0.17614 0.27012 0.03112  -0.01305 0.01614  58  TYR   A CG  
417  C CD1 . TYR   A 78  ? 0.26039 0.19025 0.24009 0.02008  -0.03956 -0.00529 58  TYR   A CD1 
418  C CD2 . TYR   A 78  ? 0.26800 0.17408 0.28083 0.03318  -0.00396 0.00114  58  TYR   A CD2 
419  C CE1 . TYR   A 78  ? 0.25858 0.18828 0.25896 0.03196  -0.02069 -0.01251 58  TYR   A CE1 
420  C CE2 . TYR   A 78  ? 0.23936 0.17963 0.31501 0.01184  0.02775  -0.00604 58  TYR   A CE2 
421  C CZ  . TYR   A 78  ? 0.24031 0.16973 0.27359 0.02800  -0.00695 -0.01685 58  TYR   A CZ  
422  O OH  . TYR   A 78  ? 0.25235 0.17270 0.28090 0.02972  -0.00359 -0.00089 58  TYR   A OH  
423  N N   . GLU   A 79  ? 0.33009 0.19480 0.28736 0.02734  -0.04380 -0.02996 59  GLU   A N   
424  C CA  . GLU   A 79  ? 0.34457 0.19915 0.28828 0.03791  -0.04765 -0.00491 59  GLU   A CA  
425  C C   . GLU   A 79  ? 0.32164 0.20356 0.31093 0.01271  -0.02572 -0.01000 59  GLU   A C   
426  O O   . GLU   A 79  ? 0.31750 0.21233 0.30401 0.01120  -0.01276 -0.01052 59  GLU   A O   
427  C CB  . GLU   A 79  ? 0.42212 0.22758 0.32750 0.07684  -0.03328 0.02777  59  GLU   A CB  
428  C CG  . GLU   A 79  ? 0.50454 0.32033 0.42581 0.10110  0.01317  0.02606  59  GLU   A CG  
429  C CD  . GLU   A 79  ? 0.54878 0.40126 0.48084 0.13639  0.06932  0.03006  59  GLU   A CD  
430  O OE1 . GLU   A 79  ? 0.58465 0.45203 0.45685 0.16798  0.04223  0.04378  59  GLU   A OE1 
431  O OE2 . GLU   A 79  ? 0.59326 0.44263 0.59569 0.12987  0.06887  0.05657  59  GLU   A OE2 
432  N N   . GLU   A 80  ? 0.32945 0.18910 0.29376 0.02024  -0.05741 -0.04440 60  GLU   A N   
433  C CA  . GLU   A 80  ? 0.37838 0.20190 0.28114 0.03176  -0.05315 -0.04921 60  GLU   A CA  
434  C C   . GLU   A 80  ? 0.33521 0.20266 0.32035 0.01146  -0.00339 -0.03646 60  GLU   A C   
435  O O   . GLU   A 80  ? 0.29960 0.21728 0.35375 0.00633  0.00842  -0.01598 60  GLU   A O   
436  C CB  . GLU   A 80  ? 0.43909 0.22637 0.33706 0.04431  -0.04033 -0.05666 60  GLU   A CB  
437  C CG  . GLU   A 80  ? 0.53885 0.30287 0.59448 0.02099  -0.06903 -0.03282 60  GLU   A CG  
438  C CD  . GLU   A 80  ? 0.64606 0.39705 0.79859 0.00628  -0.11511 0.01993  60  GLU   A CD  
439  O OE1 . GLU   A 80  ? 0.68990 0.44524 0.85838 0.00497  -0.14140 0.03739  60  GLU   A OE1 
440  O OE2 . GLU   A 80  ? 0.73682 0.43845 0.88320 -0.01071 -0.12710 0.02309  60  GLU   A OE2 
441  N N   . LEU   A 81  ? 0.30891 0.18492 0.31576 0.01991  0.01026  -0.02465 61  LEU   A N   
442  C CA  . LEU   A 81  ? 0.31688 0.18611 0.33517 0.02139  -0.02162 -0.01109 61  LEU   A CA  
443  C C   . LEU   A 81  ? 0.31719 0.18932 0.32123 0.00393  0.00177  -0.02579 61  LEU   A C   
444  O O   . LEU   A 81  ? 0.31821 0.18937 0.34374 -0.00150 0.03030  -0.01684 61  LEU   A O   
445  C CB  . LEU   A 81  ? 0.30619 0.18289 0.38349 0.00351  -0.00921 -0.01662 61  LEU   A CB  
446  C CG  . LEU   A 81  ? 0.32605 0.17669 0.46463 0.01746  -0.04165 -0.02421 61  LEU   A CG  
447  C CD1 . LEU   A 81  ? 0.29191 0.18365 0.47589 0.02787  -0.08667 -0.04454 61  LEU   A CD1 
448  C CD2 . LEU   A 81  ? 0.36758 0.15708 0.46194 0.03832  -0.03462 -0.01391 61  LEU   A CD2 
449  N N   . ALA   A 82  ? 0.31793 0.16246 0.33748 0.03050  0.01919  -0.04647 62  ALA   A N   
450  C CA  . ALA   A 82  ? 0.32232 0.16572 0.36980 0.02712  0.03827  -0.03457 62  ALA   A CA  
451  C C   . ALA   A 82  ? 0.30761 0.20022 0.36860 0.00901  0.03032  -0.01204 62  ALA   A C   
452  O O   . ALA   A 82  ? 0.31344 0.21706 0.37314 -0.02238 0.02967  0.02207  62  ALA   A O   
453  C CB  . ALA   A 82  ? 0.31782 0.13767 0.33990 0.00891  0.06072  -0.01182 62  ALA   A CB  
454  N N   . ARG   A 83  ? 0.30418 0.22386 0.38981 0.01119  -0.01328 -0.01721 63  ARG   A N   
455  C CA  . ARG   A 83  ? 0.32445 0.25143 0.43223 0.00954  -0.02758 0.01067  63  ARG   A CA  
456  C C   . ARG   A 83  ? 0.30063 0.24906 0.41644 -0.01714 0.00618  -0.00856 63  ARG   A C   
457  O O   . ARG   A 83  ? 0.30100 0.28067 0.43129 -0.03065 0.03306  -0.01549 63  ARG   A O   
458  C CB  . ARG   A 83  ? 0.36806 0.28539 0.48938 0.03989  -0.07243 0.02574  63  ARG   A CB  
459  C CG  . ARG   A 83  ? 0.41841 0.31306 0.58061 0.05861  -0.11965 0.03198  63  ARG   A CG  
460  C CD  . ARG   A 83  ? 0.48310 0.36577 0.69207 0.07473  -0.12101 0.00702  63  ARG   A CD  
461  N NE  . ARG   A 83  ? 0.54304 0.40657 0.76426 0.10220  -0.12880 0.00779  63  ARG   A NE  
462  C CZ  . ARG   A 83  ? 0.60682 0.44175 0.76440 0.09099  -0.13094 0.00222  63  ARG   A CZ  
463  N NH1 . ARG   A 83  ? 0.62277 0.46948 0.77427 0.08754  -0.14952 0.01510  63  ARG   A NH1 
464  N NH2 . ARG   A 83  ? 0.63965 0.45000 0.75302 0.11029  -0.10473 0.00854  63  ARG   A NH2 
465  N N   . MET   A 84  ? 0.31200 0.22622 0.37125 -0.00004 0.01471  -0.00748 64  MET   A N   
466  C CA  A MET   A 84  ? 0.31618 0.20490 0.39847 -0.01033 0.02398  -0.00381 64  MET   A CA  
467  C CA  B MET   A 84  ? 0.32710 0.20105 0.37761 -0.01027 0.01709  -0.00752 64  MET   A CA  
468  C C   . MET   A 84  ? 0.33218 0.20969 0.39197 -0.02174 0.01475  -0.01198 64  MET   A C   
469  O O   . MET   A 84  ? 0.37121 0.23647 0.42441 -0.03945 0.03934  -0.01310 64  MET   A O   
470  C CB  A MET   A 84  ? 0.34065 0.20578 0.40948 0.00408  0.03075  0.00003  64  MET   A CB  
471  C CB  B MET   A 84  ? 0.36145 0.19134 0.35207 -0.00661 0.01763  -0.01032 64  MET   A CB  
472  C CG  A MET   A 84  ? 0.37031 0.22885 0.46063 -0.00918 0.05796  0.00764  64  MET   A CG  
473  C CG  B MET   A 84  ? 0.40110 0.20293 0.36303 -0.02057 0.03235  -0.00814 64  MET   A CG  
474  S SD  A MET   A 84  ? 0.38841 0.24057 0.47396 -0.02504 0.10414  0.01318  64  MET   A SD  
475  S SD  B MET   A 84  ? 0.43348 0.20399 0.37134 -0.02716 0.03954  -0.01904 64  MET   A SD  
476  C CE  A MET   A 84  ? 0.36026 0.24904 0.46570 -0.02342 0.06243  0.01922  64  MET   A CE  
477  C CE  B MET   A 84  ? 0.41346 0.19417 0.34131 -0.03480 0.02640  -0.02494 64  MET   A CE  
478  N N   . LEU   A 85  ? 0.30741 0.19863 0.37000 -0.01501 -0.01093 0.00130  65  LEU   A N   
479  C CA  . LEU   A 85  ? 0.29529 0.23051 0.37992 -0.01257 0.03796  -0.00706 65  LEU   A CA  
480  C C   . LEU   A 85  ? 0.29479 0.23715 0.40035 -0.02267 0.05108  0.00172  65  LEU   A C   
481  O O   . LEU   A 85  ? 0.28660 0.25439 0.39379 -0.06108 0.07604  -0.00294 65  LEU   A O   
482  C CB  . LEU   A 85  ? 0.27195 0.24635 0.36961 -0.00912 0.05029  0.00482  65  LEU   A CB  
483  C CG  . LEU   A 85  ? 0.27977 0.25691 0.36439 -0.00064 0.05024  0.02535  65  LEU   A CG  
484  C CD1 . LEU   A 85  ? 0.29684 0.28479 0.35349 0.00356  0.03255  0.00671  65  LEU   A CD1 
485  C CD2 . LEU   A 85  ? 0.30729 0.29115 0.40217 0.00797  0.00573  0.04933  65  LEU   A CD2 
486  N N   . MET   A 86  ? 0.29767 0.24673 0.44555 0.02348  0.03083  -0.02036 66  MET   A N   
487  C CA  A MET   A 86  ? 0.30106 0.28439 0.48652 -0.00035 0.04819  -0.00732 66  MET   A CA  
488  C CA  B MET   A 86  ? 0.30026 0.27608 0.48414 0.01093  0.04835  0.01003  66  MET   A CA  
489  C C   . MET   A 86  ? 0.31756 0.29520 0.49448 -0.01723 0.04741  -0.01907 66  MET   A C   
490  O O   . MET   A 86  ? 0.32477 0.30840 0.48189 -0.04465 0.06621  -0.03079 66  MET   A O   
491  C CB  A MET   A 86  ? 0.29722 0.30404 0.50066 0.00848  0.05103  -0.01671 66  MET   A CB  
492  C CB  B MET   A 86  ? 0.30160 0.27099 0.49450 0.04355  0.03904  0.02134  66  MET   A CB  
493  C CG  A MET   A 86  ? 0.31313 0.33708 0.51512 -0.00462 0.04628  -0.01930 66  MET   A CG  
494  C CG  B MET   A 86  ? 0.34522 0.29151 0.51734 0.03454  0.01742  0.03011  66  MET   A CG  
495  S SD  A MET   A 86  ? 0.32765 0.37406 0.55833 -0.01720 0.03486  -0.01273 66  MET   A SD  
496  S SD  B MET   A 86  ? 0.37393 0.29837 0.50046 0.02045  -0.02992 0.01831  66  MET   A SD  
497  C CE  A MET   A 86  ? 0.33593 0.36759 0.54613 -0.02142 0.02752  -0.00979 66  MET   A CE  
498  C CE  B MET   A 86  ? 0.36574 0.27998 0.46420 0.03342  -0.03762 0.02439  66  MET   A CE  
499  N N   . GLY   A 87  ? 0.33177 0.29153 0.52067 -0.03388 0.04859  -0.02546 67  GLY   A N   
500  C CA  . GLY   A 87  ? 0.34679 0.28959 0.50565 -0.07484 0.04253  -0.03669 67  GLY   A CA  
501  C C   . GLY   A 87  ? 0.33596 0.29990 0.55298 -0.07109 0.05490  -0.04931 67  GLY   A C   
502  O O   . GLY   A 87  ? 0.32593 0.33209 0.58235 -0.06474 0.06427  -0.03734 67  GLY   A O   
503  N N   . LEU   A 88  ? 0.33177 0.29468 0.55730 -0.05259 0.07140  -0.06887 68  LEU   A N   
504  C CA  . LEU   A 88  ? 0.35010 0.28323 0.55181 -0.06712 0.10028  -0.06642 68  LEU   A CA  
505  C C   . LEU   A 88  ? 0.39053 0.30776 0.59137 -0.07307 0.08893  -0.03726 68  LEU   A C   
506  O O   . LEU   A 88  ? 0.42405 0.31818 0.59306 -0.09497 0.10105  -0.01621 68  LEU   A O   
507  C CB  . LEU   A 88  ? 0.36523 0.29287 0.58571 -0.06542 0.09007  -0.05684 68  LEU   A CB  
508  C CG  . LEU   A 88  ? 0.39831 0.30878 0.63498 -0.07889 0.07729  -0.06974 68  LEU   A CG  
509  C CD1 . LEU   A 88  ? 0.40615 0.33272 0.65107 -0.05745 0.07368  -0.05342 68  LEU   A CD1 
510  C CD2 . LEU   A 88  ? 0.42502 0.30670 0.64517 -0.07399 0.08962  -0.10261 68  LEU   A CD2 
511  N N   . ASP   A 89  ? 0.36482 0.29676 0.58412 -0.05610 0.09788  -0.03976 69  ASP   A N   
512  C CA  . ASP   A 89  ? 0.36757 0.30620 0.59617 -0.06120 0.13491  -0.02395 69  ASP   A CA  
513  C C   . ASP   A 89  ? 0.36625 0.29288 0.54948 -0.03714 0.13077  -0.00957 69  ASP   A C   
514  O O   . ASP   A 89  ? 0.39361 0.31404 0.57820 -0.02465 0.16415  -0.04503 69  ASP   A O   
515  C CB  . ASP   A 89  ? 0.40985 0.35046 0.74247 -0.07083 0.15346  -0.00159 69  ASP   A CB  
516  C CG  . ASP   A 89  ? 0.47419 0.40993 0.88747 -0.07996 0.16325  0.01959  69  ASP   A CG  
517  O OD1 . ASP   A 89  ? 0.49012 0.43898 0.92155 -0.04563 0.17525  0.04055  69  ASP   A OD1 
518  O OD2 . ASP   A 89  ? 0.51489 0.43181 1.02032 -0.09976 0.13702  0.01033  69  ASP   A OD2 
519  N N   . LEU   A 90  ? 0.33110 0.25358 0.51483 0.00159  0.07693  -0.00242 70  LEU   A N   
520  C CA  . LEU   A 90  ? 0.30067 0.22088 0.48512 0.01587  0.04198  -0.00234 70  LEU   A CA  
521  C C   . LEU   A 90  ? 0.33157 0.21737 0.43719 0.03272  0.03420  -0.00304 70  LEU   A C   
522  O O   . LEU   A 90  ? 0.36458 0.21720 0.39958 0.00436  0.02368  0.00206  70  LEU   A O   
523  C CB  . LEU   A 90  ? 0.29747 0.21980 0.48937 0.04001  0.07182  0.00239  70  LEU   A CB  
524  C CG  . LEU   A 90  ? 0.33962 0.23754 0.52770 0.03344  0.04939  0.01865  70  LEU   A CG  
525  C CD1 . LEU   A 90  ? 0.37625 0.22774 0.59020 0.00969  -0.02071 -0.01438 70  LEU   A CD1 
526  C CD2 . LEU   A 90  ? 0.34727 0.25171 0.48993 0.02395  0.06337  0.03583  70  LEU   A CD2 
527  N N   . LEU   A 91  ? 0.32282 0.20197 0.42279 0.02307  0.08247  -0.03003 71  LEU   A N   
528  C CA  . LEU   A 91  ? 0.32095 0.20942 0.40765 0.02860  0.09710  -0.02345 71  LEU   A CA  
529  C C   . LEU   A 91  ? 0.29921 0.22084 0.37950 0.00934  0.05929  0.00240  71  LEU   A C   
530  O O   . LEU   A 91  ? 0.29408 0.24016 0.37895 -0.00480 0.06544  0.00498  71  LEU   A O   
531  C CB  . LEU   A 91  ? 0.33890 0.21983 0.44090 0.00736  0.06842  -0.04824 71  LEU   A CB  
532  C CG  . LEU   A 91  ? 0.36307 0.23642 0.49044 0.02024  0.06984  -0.05680 71  LEU   A CG  
533  C CD1 . LEU   A 91  ? 0.37202 0.23882 0.49306 0.04079  0.09392  -0.09145 71  LEU   A CD1 
534  C CD2 . LEU   A 91  ? 0.38976 0.25842 0.48612 0.00890  0.09291  -0.06856 71  LEU   A CD2 
535  N N   . VAL   A 92  ? 0.28190 0.20117 0.36198 0.00455  0.04674  -0.01295 72  VAL   A N   
536  C CA  . VAL   A 92  ? 0.28942 0.18887 0.34130 -0.00469 0.03030  0.00251  72  VAL   A CA  
537  C C   . VAL   A 92  ? 0.27998 0.16894 0.31082 -0.00439 0.03568  0.00251  72  VAL   A C   
538  O O   . VAL   A 92  ? 0.27790 0.18408 0.37236 0.01937  0.04027  0.01222  72  VAL   A O   
539  C CB  . VAL   A 92  ? 0.26316 0.19519 0.32768 -0.02453 0.01657  -0.01011 72  VAL   A CB  
540  C CG1 . VAL   A 92  ? 0.24649 0.22271 0.29483 -0.00817 0.03044  0.00402  72  VAL   A CG1 
541  C CG2 . VAL   A 92  ? 0.29138 0.18008 0.35960 -0.01937 -0.00997 -0.01660 72  VAL   A CG2 
542  N N   . PHE   A 93  ? 0.28551 0.15276 0.28265 -0.01024 0.02883  0.01524  73  PHE   A N   
543  C CA  . PHE   A 93  ? 0.27711 0.14744 0.28643 -0.00669 0.05023  0.00344  73  PHE   A CA  
544  C C   . PHE   A 93  ? 0.26361 0.14116 0.28834 0.00329  0.01157  0.01713  73  PHE   A C   
545  O O   . PHE   A 93  ? 0.25053 0.15060 0.31639 0.01862  0.02518  0.01879  73  PHE   A O   
546  C CB  . PHE   A 93  ? 0.30082 0.16467 0.28485 0.01548  0.05749  -0.00032 73  PHE   A CB  
547  C CG  . PHE   A 93  ? 0.31704 0.17239 0.28074 0.00043  0.04233  0.01259  73  PHE   A CG  
548  C CD1 . PHE   A 93  ? 0.35387 0.17147 0.25754 0.01827  0.05131  0.02358  73  PHE   A CD1 
549  C CD2 . PHE   A 93  ? 0.30630 0.19311 0.27788 0.01399  0.04902  -0.00340 73  PHE   A CD2 
550  C CE1 . PHE   A 93  ? 0.34566 0.19117 0.27068 0.02042  0.04959  0.01050  73  PHE   A CE1 
551  C CE2 . PHE   A 93  ? 0.33170 0.20554 0.28449 0.02148  0.08289  0.00382  73  PHE   A CE2 
552  C CZ  . PHE   A 93  ? 0.32606 0.19136 0.27040 0.02407  0.09783  -0.00679 73  PHE   A CZ  
553  N N   . ALA   A 94  ? 0.28224 0.16487 0.29220 0.00958  0.03459  0.01574  74  ALA   A N   
554  C CA  . ALA   A 94  ? 0.26651 0.14416 0.24765 -0.00347 0.02870  -0.01977 74  ALA   A CA  
555  C C   . ALA   A 94  ? 0.25677 0.15356 0.25481 -0.00869 0.01078  -0.00732 74  ALA   A C   
556  O O   . ALA   A 94  ? 0.24396 0.16301 0.26230 0.01194  -0.00151 -0.01316 74  ALA   A O   
557  C CB  . ALA   A 94  ? 0.31487 0.18005 0.22130 0.02091  0.01494  -0.03231 74  ALA   A CB  
558  N N   . HIS   A 95  ? 0.24211 0.16361 0.24321 0.00371  0.02469  0.01758  75  HIS   A N   
559  C CA  . HIS   A 95  ? 0.26937 0.16418 0.26520 -0.02084 0.01636  0.01632  75  HIS   A CA  
560  C C   . HIS   A 95  ? 0.27167 0.16253 0.23975 0.00130  0.00208  0.02941  75  HIS   A C   
561  O O   . HIS   A 95  ? 0.27460 0.16852 0.27154 0.01340  0.02800  0.00244  75  HIS   A O   
562  C CB  . HIS   A 95  ? 0.30293 0.17907 0.19298 0.00419  -0.01638 0.00471  75  HIS   A CB  
563  C CG  . HIS   A 95  ? 0.31082 0.16133 0.20633 0.00474  0.00282  0.01261  75  HIS   A CG  
564  N ND1 . HIS   A 95  ? 0.32489 0.14895 0.21595 0.03742  0.02518  0.03339  75  HIS   A ND1 
565  C CD2 . HIS   A 95  ? 0.32056 0.17432 0.26236 0.02030  0.02060  0.02031  75  HIS   A CD2 
566  C CE1 . HIS   A 95  ? 0.31755 0.14978 0.22278 0.02373  0.00756  -0.00584 75  HIS   A CE1 
567  N NE2 . HIS   A 95  ? 0.31027 0.15408 0.24134 0.00101  0.03156  0.00097  75  HIS   A NE2 
568  N N   . ASP   A 96  ? 0.26586 0.14463 0.19879 -0.00869 0.03234  0.01650  76  ASP   A N   
569  C CA  . ASP   A 96  ? 0.27707 0.15016 0.18924 0.01500  0.06739  0.00772  76  ASP   A CA  
570  C C   . ASP   A 96  ? 0.27708 0.14811 0.20497 0.03503  0.04896  -0.02714 76  ASP   A C   
571  O O   . ASP   A 96  ? 0.31642 0.14924 0.22479 0.03167  0.02302  -0.00307 76  ASP   A O   
572  C CB  . ASP   A 96  ? 0.31469 0.15522 0.21658 0.01080  0.03274  0.00901  76  ASP   A CB  
573  C CG  . ASP   A 96  ? 0.32613 0.13735 0.23694 0.02489  0.02764  0.00270  76  ASP   A CG  
574  O OD1 . ASP   A 96  ? 0.35970 0.14698 0.24928 0.01972  -0.00980 0.00200  76  ASP   A OD1 
575  O OD2 . ASP   A 96  ? 0.30491 0.14797 0.26265 0.01599  -0.00407 0.01181  76  ASP   A OD2 
576  N N   . HIS   A 97  ? 0.24871 0.13911 0.26614 0.02208  0.03454  0.00723  77  HIS   A N   
577  C CA  . HIS   A 97  ? 0.24125 0.13260 0.26620 0.02560  0.01244  -0.02082 77  HIS   A CA  
578  C C   . HIS   A 97  ? 0.28408 0.14127 0.24469 0.00597  -0.03433 -0.00591 77  HIS   A C   
579  O O   . HIS   A 97  ? 0.31916 0.15863 0.23519 0.01112  -0.01071 0.01061  77  HIS   A O   
580  C CB  . HIS   A 97  ? 0.24264 0.13739 0.27944 0.01803  0.03072  -0.02344 77  HIS   A CB  
581  C CG  . HIS   A 97  ? 0.26129 0.13365 0.25997 -0.02051 0.01200  0.00366  77  HIS   A CG  
582  N ND1 . HIS   A 97  ? 0.27921 0.14857 0.26626 -0.02204 0.01093  -0.01360 77  HIS   A ND1 
583  C CD2 . HIS   A 97  ? 0.28426 0.13252 0.30360 -0.00737 0.01482  0.00748  77  HIS   A CD2 
584  C CE1 . HIS   A 97  ? 0.30829 0.15646 0.26363 -0.02064 0.00914  -0.01638 77  HIS   A CE1 
585  N NE2 . HIS   A 97  ? 0.30949 0.14366 0.27913 -0.01201 -0.02068 0.00665  77  HIS   A NE2 
586  N N   . VAL   A 98  ? 0.27313 0.15205 0.27075 -0.01179 -0.01690 -0.02725 78  VAL   A N   
587  C CA  A VAL   A 98  ? 0.29429 0.17756 0.30690 -0.02861 -0.02888 -0.00322 78  VAL   A CA  
588  C CA  B VAL   A 98  ? 0.29360 0.17614 0.28846 -0.01623 -0.01690 -0.00622 78  VAL   A CA  
589  C C   . VAL   A 98  ? 0.30814 0.16739 0.29692 -0.00918 -0.00372 0.00319  78  VAL   A C   
590  O O   . VAL   A 98  ? 0.30814 0.14948 0.29120 -0.01364 0.00438  0.01550  78  VAL   A O   
591  C CB  A VAL   A 98  ? 0.30376 0.17564 0.34781 -0.03358 -0.04684 -0.00323 78  VAL   A CB  
592  C CB  B VAL   A 98  ? 0.29823 0.18882 0.27880 -0.00616 -0.01723 -0.00346 78  VAL   A CB  
593  C CG1 A VAL   A 98  ? 0.28342 0.17016 0.35752 -0.02749 -0.06442 -0.00385 78  VAL   A CG1 
594  C CG1 B VAL   A 98  ? 0.30952 0.19804 0.29080 0.00382  -0.02293 -0.01347 78  VAL   A CG1 
595  C CG2 A VAL   A 98  ? 0.31614 0.17179 0.38895 -0.01796 -0.03867 0.01034  78  VAL   A CG2 
596  C CG2 B VAL   A 98  ? 0.28752 0.18891 0.27017 0.01012  -0.00059 0.01515  78  VAL   A CG2 
597  N N   . GLY   A 99  ? 0.28765 0.16790 0.27676 -0.02068 0.02366  0.01870  79  GLY   A N   
598  C CA  . GLY   A 99  ? 0.26877 0.16762 0.25708 -0.02287 -0.00395 0.00510  79  GLY   A CA  
599  C C   . GLY   A 99  ? 0.27841 0.15076 0.26047 0.00718  -0.01307 -0.00113 79  GLY   A C   
600  O O   . GLY   A 99  ? 0.29593 0.17705 0.30081 -0.01703 -0.02138 0.01970  79  GLY   A O   
601  N N   . HIS   A 100 ? 0.27618 0.12910 0.24244 -0.01208 -0.01652 -0.01977 80  HIS   A N   
602  C CA  . HIS   A 100 ? 0.29452 0.12500 0.25569 -0.00139 -0.00741 0.01123  80  HIS   A CA  
603  C C   . HIS   A 100 ? 0.32536 0.13588 0.21930 0.01745  0.02141  0.01036  80  HIS   A C   
604  O O   . HIS   A 100 ? 0.32403 0.14455 0.26893 0.00418  0.05561  0.00275  80  HIS   A O   
605  C CB  . HIS   A 100 ? 0.27401 0.11949 0.27122 0.03668  -0.01642 0.02058  80  HIS   A CB  
606  C CG  . HIS   A 100 ? 0.27848 0.13226 0.32228 0.01563  -0.03046 0.02814  80  HIS   A CG  
607  N ND1 . HIS   A 100 ? 0.27904 0.13712 0.34674 -0.00212 -0.03375 0.03000  80  HIS   A ND1 
608  C CD2 . HIS   A 100 ? 0.28980 0.13907 0.33623 0.00793  0.01071  -0.01777 80  HIS   A CD2 
609  C CE1 . HIS   A 100 ? 0.31079 0.15301 0.36834 0.02565  -0.02157 -0.01047 80  HIS   A CE1 
610  N NE2 . HIS   A 100 ? 0.31203 0.17237 0.38993 0.00697  0.00502  -0.00829 80  HIS   A NE2 
611  N N   . GLY   A 101 ? 0.35747 0.13393 0.22397 0.03149  0.00598  0.01894  81  GLY   A N   
612  C CA  . GLY   A 101 ? 0.35177 0.14179 0.25328 0.04658  0.02353  0.00093  81  GLY   A CA  
613  C C   . GLY   A 101 ? 0.34664 0.15345 0.24946 0.04826  0.04395  0.00244  81  GLY   A C   
614  O O   . GLY   A 101 ? 0.37288 0.16224 0.26378 0.02520  0.04489  0.04093  81  GLY   A O   
615  N N   . GLN   A 102 ? 0.29680 0.15525 0.22585 0.04369  0.01668  -0.00579 82  GLN   A N   
616  C CA  . GLN   A 102 ? 0.27910 0.16743 0.23926 0.06053  0.00059  -0.00363 82  GLN   A CA  
617  C C   . GLN   A 102 ? 0.29221 0.18140 0.24374 0.03313  0.01222  -0.00058 82  GLN   A C   
618  O O   . GLN   A 102 ? 0.31872 0.18272 0.25294 0.03630  0.00398  -0.00991 82  GLN   A O   
619  C CB  . GLN   A 102 ? 0.29846 0.17622 0.26667 0.04178  -0.00399 -0.01332 82  GLN   A CB  
620  C CG  . GLN   A 102 ? 0.31408 0.17404 0.26205 0.03238  -0.01495 -0.01858 82  GLN   A CG  
621  C CD  . GLN   A 102 ? 0.34045 0.19229 0.28555 0.02187  -0.05255 0.01070  82  GLN   A CD  
622  O OE1 . GLN   A 102 ? 0.37382 0.21180 0.39747 0.03374  -0.05391 -0.00092 82  GLN   A OE1 
623  N NE2 . GLN   A 102 ? 0.35480 0.20137 0.26612 -0.00042 -0.04543 -0.00163 82  GLN   A NE2 
624  N N   . SER   A 103 ? 0.30492 0.16901 0.23778 0.00121  0.01266  0.02636  83  SER   A N   
625  C CA  . SER   A 103 ? 0.27644 0.14005 0.21810 -0.01641 -0.01863 0.02117  83  SER   A CA  
626  C C   . SER   A 103 ? 0.31073 0.14014 0.24473 0.00004  -0.00415 -0.00804 83  SER   A C   
627  O O   . SER   A 103 ? 0.34094 0.16790 0.25676 0.00618  0.02262  -0.00662 83  SER   A O   
628  C CB  . SER   A 103 ? 0.30419 0.13088 0.23795 0.00556  -0.00148 0.01690  83  SER   A CB  
629  O OG  . SER   A 103 ? 0.30451 0.14191 0.22582 -0.01302 0.00941  0.00156  83  SER   A OG  
630  N N   . GLU   A 104 ? 0.31276 0.13324 0.29650 -0.01071 0.00176  -0.04536 84  GLU   A N   
631  C CA  . GLU   A 104 ? 0.31637 0.14682 0.26879 0.00239  0.01911  -0.03031 84  GLU   A CA  
632  C C   . GLU   A 104 ? 0.34030 0.16195 0.28022 0.00107  0.01163  -0.02058 84  GLU   A C   
633  O O   . GLU   A 104 ? 0.36271 0.16709 0.29170 -0.00448 -0.00109 -0.00282 84  GLU   A O   
634  C CB  . GLU   A 104 ? 0.34675 0.15008 0.28178 0.01764  0.01301  -0.03820 84  GLU   A CB  
635  C CG  . GLU   A 104 ? 0.36880 0.16023 0.32944 0.03356  0.02101  -0.02905 84  GLU   A CG  
636  C CD  . GLU   A 104 ? 0.40665 0.16629 0.34549 0.01845  0.02904  -0.02398 84  GLU   A CD  
637  O OE1 . GLU   A 104 ? 0.41523 0.17616 0.33264 -0.00071 0.03203  -0.03402 84  GLU   A OE1 
638  O OE2 . GLU   A 104 ? 0.46902 0.18883 0.37232 0.02106  -0.00197 -0.04307 84  GLU   A OE2 
639  N N   . GLY   A 105 ? 0.30822 0.20389 0.32752 -0.01370 -0.00396 -0.01877 85  GLY   A N   
640  C CA  . GLY   A 105 ? 0.33611 0.21358 0.35369 0.00455  0.00873  -0.01314 85  GLY   A CA  
641  C C   . GLY   A 105 ? 0.34568 0.20133 0.39019 -0.00045 0.00846  0.00143  85  GLY   A C   
642  O O   . GLY   A 105 ? 0.36588 0.22229 0.36668 0.00374  -0.00773 0.01220  85  GLY   A O   
643  N N   . GLU   A 106 ? 0.36024 0.20094 0.41266 -0.00311 0.03286  -0.02306 86  GLU   A N   
644  C CA  . GLU   A 106 ? 0.38965 0.23353 0.45005 -0.03805 0.06812  -0.03650 86  GLU   A CA  
645  C C   . GLU   A 106 ? 0.38682 0.23348 0.38299 -0.03369 0.02040  -0.01964 86  GLU   A C   
646  O O   . GLU   A 106 ? 0.40827 0.23079 0.34357 -0.01041 -0.00443 0.00759  86  GLU   A O   
647  C CB  . GLU   A 106 ? 0.43410 0.29834 0.57782 -0.08251 0.12086  -0.04061 86  GLU   A CB  
648  C CG  . GLU   A 106 ? 0.49952 0.42061 0.79666 -0.10971 0.13190  -0.03641 86  GLU   A CG  
649  C CD  . GLU   A 106 ? 0.55475 0.54488 0.89924 -0.12383 0.13948  -0.02761 86  GLU   A CD  
650  O OE1 . GLU   A 106 ? 0.59484 0.59259 0.91437 -0.12855 0.21672  -0.02419 86  GLU   A OE1 
651  O OE2 . GLU   A 106 ? 0.58664 0.58473 0.93045 -0.13293 0.11253  -0.02945 86  GLU   A OE2 
652  N N   . ARG   A 107 ? 0.37205 0.25139 0.34802 -0.01575 -0.00559 -0.01698 87  ARG   A N   
653  C CA  . ARG   A 107 ? 0.41599 0.25896 0.31793 0.01166  -0.02003 -0.00593 87  ARG   A CA  
654  C C   . ARG   A 107 ? 0.44303 0.28635 0.33929 -0.00881 0.00046  0.00957  87  ARG   A C   
655  O O   . ARG   A 107 ? 0.43294 0.31103 0.34879 0.03295  0.00966  0.02533  87  ARG   A O   
656  C CB  . ARG   A 107 ? 0.46155 0.26901 0.31397 0.03020  -0.03163 0.02705  87  ARG   A CB  
657  C CG  . ARG   A 107 ? 0.45654 0.28558 0.41181 0.02595  -0.02493 0.04617  87  ARG   A CG  
658  C CD  . ARG   A 107 ? 0.45749 0.27283 0.40212 -0.00135 -0.03137 -0.00075 87  ARG   A CD  
659  N NE  . ARG   A 107 ? 0.46085 0.23010 0.34890 0.03314  0.00448  -0.01181 87  ARG   A NE  
660  C CZ  . ARG   A 107 ? 0.42783 0.20137 0.34577 0.02267  0.00475  0.00112  87  ARG   A CZ  
661  N NH1 . ARG   A 107 ? 0.46059 0.20393 0.33544 0.02914  -0.03431 0.03508  87  ARG   A NH1 
662  N NH2 . ARG   A 107 ? 0.40989 0.18902 0.28849 0.02774  0.03616  -0.01053 87  ARG   A NH2 
663  N N   . MET   A 108 ? 0.46659 0.27744 0.32911 0.00739  0.01161  -0.01041 88  MET   A N   
664  C CA  . MET   A 108 ? 0.47706 0.31001 0.36185 0.01700  -0.00690 -0.01864 88  MET   A CA  
665  C C   . MET   A 108 ? 0.43023 0.31281 0.36895 0.01781  0.00788  0.01144  88  MET   A C   
666  O O   . MET   A 108 ? 0.42978 0.36605 0.39757 0.03031  0.04643  0.03118  88  MET   A O   
667  C CB  . MET   A 108 ? 0.54101 0.31830 0.36807 -0.01507 -0.01168 -0.05374 88  MET   A CB  
668  C CG  . MET   A 108 ? 0.58387 0.32466 0.33363 -0.00325 -0.01919 -0.07277 88  MET   A CG  
669  S SD  . MET   A 108 ? 0.59650 0.32782 0.46496 -0.03430 0.00974  -0.02547 88  MET   A SD  
670  C CE  . MET   A 108 ? 0.57350 0.31827 0.53344 -0.02036 0.01561  0.00721  88  MET   A CE  
671  N N   A VAL   A 109 ? 0.42130 0.28864 0.34347 0.01113  -0.00477 0.02690  89  VAL   A N   
672  N N   B VAL   A 109 ? 0.42274 0.28555 0.33746 0.00597  -0.00988 0.04718  89  VAL   A N   
673  C CA  A VAL   A 109 ? 0.39492 0.28410 0.37808 0.00347  0.00677  0.00929  89  VAL   A CA  
674  C CA  B VAL   A 109 ? 0.40105 0.28100 0.38354 -0.00973 0.00330  0.04954  89  VAL   A CA  
675  C C   A VAL   A 109 ? 0.37125 0.27584 0.32163 -0.01249 -0.00340 0.02602  89  VAL   A C   
676  C C   B VAL   A 109 ? 0.37229 0.27109 0.32885 -0.02509 -0.01613 0.03999  89  VAL   A C   
677  O O   A VAL   A 109 ? 0.36030 0.27179 0.30838 -0.00505 -0.00136 0.03349  89  VAL   A O   
678  O O   B VAL   A 109 ? 0.35305 0.25872 0.32691 -0.03095 -0.04073 0.03266  89  VAL   A O   
679  C CB  A VAL   A 109 ? 0.39752 0.28488 0.42311 0.01993  0.00340  -0.01093 89  VAL   A CB  
680  C CB  B VAL   A 109 ? 0.41162 0.30033 0.43242 0.00902  0.01317  0.05328  89  VAL   A CB  
681  C CG1 A VAL   A 109 ? 0.40725 0.29612 0.43940 0.03608  0.00051  -0.01400 89  VAL   A CG1 
682  C CG1 B VAL   A 109 ? 0.40326 0.29064 0.41093 0.01503  0.03741  0.03927  89  VAL   A CG1 
683  C CG2 A VAL   A 109 ? 0.39558 0.25036 0.43601 0.04042  -0.01028 -0.02804 89  VAL   A CG2 
684  C CG2 B VAL   A 109 ? 0.41464 0.29485 0.43892 0.02960  0.00939  0.09946  89  VAL   A CG2 
685  N N   . VAL   A 110 ? 0.34951 0.25792 0.32410 -0.03513 -0.00195 0.03834  90  VAL   A N   
686  C CA  . VAL   A 110 ? 0.32243 0.26649 0.35052 -0.03598 -0.00812 0.02363  90  VAL   A CA  
687  C C   . VAL   A 110 ? 0.33467 0.25898 0.35173 -0.02751 -0.02536 0.00808  90  VAL   A C   
688  O O   . VAL   A 110 ? 0.30154 0.27239 0.37352 -0.00730 -0.02601 -0.02641 90  VAL   A O   
689  C CB  . VAL   A 110 ? 0.29311 0.26706 0.31568 -0.02034 0.01552  0.01566  90  VAL   A CB  
690  C CG1 . VAL   A 110 ? 0.29247 0.25361 0.32935 0.01700  -0.01668 0.00052  90  VAL   A CG1 
691  C CG2 . VAL   A 110 ? 0.32252 0.28310 0.26637 -0.04369 -0.01303 0.02493  90  VAL   A CG2 
692  N N   . SER   A 111 ? 0.34870 0.23593 0.36750 -0.03797 -0.03962 0.00844  91  SER   A N   
693  C CA  . SER   A 111 ? 0.34279 0.25684 0.41610 -0.03559 -0.05456 0.00118  91  SER   A CA  
694  C C   . SER   A 111 ? 0.33878 0.25832 0.38898 -0.03792 -0.05977 -0.01345 91  SER   A C   
695  O O   . SER   A 111 ? 0.32957 0.28557 0.40678 -0.04539 -0.06840 -0.03249 91  SER   A O   
696  C CB  . SER   A 111 ? 0.35158 0.26932 0.41968 -0.06006 -0.03724 -0.03992 91  SER   A CB  
697  O OG  . SER   A 111 ? 0.38579 0.28003 0.43478 -0.03577 -0.06598 -0.04446 91  SER   A OG  
698  N N   . ASP   A 112 ? 0.33931 0.25141 0.36392 -0.02738 -0.05504 -0.01148 92  ASP   A N   
699  C CA  . ASP   A 112 ? 0.35799 0.23385 0.32940 -0.02300 -0.05020 -0.00484 92  ASP   A CA  
700  C C   . ASP   A 112 ? 0.32584 0.20263 0.31429 -0.02496 -0.03390 -0.01169 92  ASP   A C   
701  O O   . ASP   A 112 ? 0.33421 0.19678 0.32191 -0.02576 -0.03654 -0.01313 92  ASP   A O   
702  C CB  . ASP   A 112 ? 0.37496 0.24207 0.32828 -0.01874 -0.06684 0.02129  92  ASP   A CB  
703  C CG  . ASP   A 112 ? 0.39117 0.29135 0.38524 -0.02140 -0.05712 0.02443  92  ASP   A CG  
704  O OD1 . ASP   A 112 ? 0.40219 0.33021 0.42461 -0.02553 -0.05225 0.00369  92  ASP   A OD1 
705  O OD2 . ASP   A 112 ? 0.39857 0.31129 0.39259 -0.01958 -0.07152 -0.00752 92  ASP   A OD2 
706  N N   . PHE   A 113 ? 0.30571 0.19107 0.28570 -0.01136 -0.03874 -0.01374 93  PHE   A N   
707  C CA  . PHE   A 113 ? 0.31097 0.19884 0.26570 -0.01140 -0.00712 -0.02184 93  PHE   A CA  
708  C C   . PHE   A 113 ? 0.33928 0.21194 0.25824 -0.02669 -0.04092 -0.00574 93  PHE   A C   
709  O O   . PHE   A 113 ? 0.33717 0.20782 0.29554 0.00147  -0.03042 -0.01387 93  PHE   A O   
710  C CB  . PHE   A 113 ? 0.32867 0.17991 0.30123 -0.00943 -0.02601 -0.01394 93  PHE   A CB  
711  C CG  . PHE   A 113 ? 0.30466 0.19927 0.30759 -0.00134 -0.01924 -0.01401 93  PHE   A CG  
712  C CD1 . PHE   A 113 ? 0.28775 0.20390 0.27065 0.01640  -0.00008 -0.00413 93  PHE   A CD1 
713  C CD2 . PHE   A 113 ? 0.28881 0.18787 0.29546 0.01041  0.00599  -0.04526 93  PHE   A CD2 
714  C CE1 . PHE   A 113 ? 0.28331 0.19643 0.25207 0.00514  0.04278  -0.01475 93  PHE   A CE1 
715  C CE2 . PHE   A 113 ? 0.28997 0.19015 0.25497 0.01212  0.00561  -0.02546 93  PHE   A CE2 
716  C CZ  . PHE   A 113 ? 0.29359 0.20533 0.26709 0.00372  0.03163  0.00610  93  PHE   A CZ  
717  N N   . HIS   A 114 ? 0.38165 0.22438 0.28279 -0.02041 -0.02937 -0.01066 94  HIS   A N   
718  C CA  . HIS   A 114 ? 0.42704 0.25829 0.29057 -0.01182 -0.08147 0.03234  94  HIS   A CA  
719  C C   . HIS   A 114 ? 0.38401 0.22251 0.26588 0.00855  -0.08454 0.01514  94  HIS   A C   
720  O O   . HIS   A 114 ? 0.40499 0.21750 0.28556 0.01861  -0.03300 -0.01168 94  HIS   A O   
721  C CB  . HIS   A 114 ? 0.52216 0.32374 0.39494 -0.00949 -0.06704 0.09429  94  HIS   A CB  
722  C CG  . HIS   A 114 ? 0.64393 0.37844 0.52905 -0.02401 -0.08700 0.10272  94  HIS   A CG  
723  N ND1 . HIS   A 114 ? 0.68987 0.40013 0.60975 -0.05480 -0.05838 0.10178  94  HIS   A ND1 
724  C CD2 . HIS   A 114 ? 0.69563 0.39917 0.59267 -0.01893 -0.07204 0.07581  94  HIS   A CD2 
725  C CE1 . HIS   A 114 ? 0.72531 0.40457 0.63361 -0.05368 -0.06488 0.10597  94  HIS   A CE1 
726  N NE2 . HIS   A 114 ? 0.72545 0.41214 0.61040 -0.02993 -0.04789 0.09087  94  HIS   A NE2 
727  N N   . VAL   A 115 ? 0.35002 0.19584 0.27417 -0.00282 -0.05761 -0.00190 95  VAL   A N   
728  C CA  . VAL   A 115 ? 0.31650 0.16559 0.24571 -0.00576 -0.02219 -0.02802 95  VAL   A CA  
729  C C   . VAL   A 115 ? 0.31359 0.18161 0.24457 -0.01312 0.03309  -0.01711 95  VAL   A C   
730  O O   . VAL   A 115 ? 0.29162 0.17591 0.24880 -0.01100 0.02478  -0.02009 95  VAL   A O   
731  C CB  . VAL   A 115 ? 0.30768 0.19186 0.32916 -0.02662 -0.02886 -0.00967 95  VAL   A CB  
732  C CG1 . VAL   A 115 ? 0.31516 0.19193 0.35449 -0.00777 -0.01498 0.01862  95  VAL   A CG1 
733  C CG2 . VAL   A 115 ? 0.31056 0.19687 0.36274 -0.04213 -0.05755 -0.05092 95  VAL   A CG2 
734  N N   . PHE   A 116 ? 0.32190 0.17645 0.21018 0.00049  -0.01005 -0.01433 96  PHE   A N   
735  C CA  . PHE   A 116 ? 0.31121 0.17432 0.21458 -0.00369 -0.01399 -0.01910 96  PHE   A CA  
736  C C   . PHE   A 116 ? 0.33345 0.17314 0.23828 0.02883  0.02409  0.01507  96  PHE   A C   
737  O O   . PHE   A 116 ? 0.33977 0.16803 0.26040 0.03264  0.00669  -0.00169 96  PHE   A O   
738  C CB  . PHE   A 116 ? 0.29995 0.18896 0.20332 0.01939  0.03896  -0.04602 96  PHE   A CB  
739  C CG  . PHE   A 116 ? 0.28708 0.19062 0.22301 -0.00082 -0.01909 -0.03015 96  PHE   A CG  
740  C CD1 . PHE   A 116 ? 0.28122 0.20290 0.26441 -0.00812 0.00279  0.02309  96  PHE   A CD1 
741  C CD2 . PHE   A 116 ? 0.27230 0.19470 0.22324 -0.02538 0.02224  -0.02075 96  PHE   A CD2 
742  C CE1 . PHE   A 116 ? 0.24699 0.21134 0.25649 0.00410  0.02155  0.00611  96  PHE   A CE1 
743  C CE2 . PHE   A 116 ? 0.27750 0.19494 0.26015 -0.04393 0.01727  -0.01056 96  PHE   A CE2 
744  C CZ  . PHE   A 116 ? 0.26573 0.19801 0.27251 -0.01432 0.00341  -0.00371 96  PHE   A CZ  
745  N N   . VAL   A 117 ? 0.35795 0.15219 0.23756 0.02420  0.00558  0.01730  97  VAL   A N   
746  C CA  . VAL   A 117 ? 0.37131 0.15693 0.24457 0.03109  0.02159  0.01100  97  VAL   A CA  
747  C C   . VAL   A 117 ? 0.37125 0.15929 0.24346 0.04338  0.00231  0.01461  97  VAL   A C   
748  O O   . VAL   A 117 ? 0.36750 0.17261 0.25669 0.03349  0.00306  0.00955  97  VAL   A O   
749  C CB  . VAL   A 117 ? 0.37238 0.16306 0.25109 0.04525  0.00733  -0.00127 97  VAL   A CB  
750  C CG1 . VAL   A 117 ? 0.40849 0.17540 0.25517 0.03914  -0.00373 0.03804  97  VAL   A CG1 
751  C CG2 . VAL   A 117 ? 0.35013 0.19416 0.26481 0.07808  0.01116  -0.01124 97  VAL   A CG2 
752  N N   . ARG   A 118 ? 0.36491 0.14440 0.21993 0.04550  -0.02237 -0.01279 98  ARG   A N   
753  C CA  . ARG   A 118 ? 0.35009 0.16607 0.23862 0.03492  -0.00191 -0.03457 98  ARG   A CA  
754  C C   . ARG   A 118 ? 0.34365 0.17159 0.26819 0.02987  -0.01690 -0.00718 98  ARG   A C   
755  O O   . ARG   A 118 ? 0.36080 0.17570 0.23892 0.01239  0.00534  -0.00025 98  ARG   A O   
756  C CB  . ARG   A 118 ? 0.36559 0.17344 0.25393 0.01119  -0.01284 -0.05914 98  ARG   A CB  
757  C CG  . ARG   A 118 ? 0.38249 0.17793 0.30317 0.01248  -0.03472 -0.04227 98  ARG   A CG  
758  C CD  . ARG   A 118 ? 0.39378 0.19078 0.31803 0.00239  -0.03085 -0.02196 98  ARG   A CD  
759  N NE  . ARG   A 118 ? 0.35596 0.20306 0.32600 -0.00206 -0.02738 -0.01542 98  ARG   A NE  
760  C CZ  . ARG   A 118 ? 0.32577 0.22558 0.29845 0.01440  -0.06588 -0.02074 98  ARG   A CZ  
761  N NH1 . ARG   A 118 ? 0.31232 0.25515 0.32306 0.01443  -0.07325 -0.03298 98  ARG   A NH1 
762  N NH2 . ARG   A 118 ? 0.31363 0.22211 0.30478 0.03817  -0.05085 -0.00558 98  ARG   A NH2 
763  N N   . ASP   A 119 ? 0.34106 0.15054 0.23927 0.04084  -0.05671 0.01217  99  ASP   A N   
764  C CA  . ASP   A 119 ? 0.30525 0.15531 0.24183 0.01909  -0.01234 0.02596  99  ASP   A CA  
765  C C   . ASP   A 119 ? 0.31614 0.15124 0.24434 0.02821  0.01580  0.00729  99  ASP   A C   
766  O O   . ASP   A 119 ? 0.31522 0.15890 0.24813 0.02594  0.03333  0.00144  99  ASP   A O   
767  C CB  . ASP   A 119 ? 0.33924 0.15228 0.23729 -0.01907 0.01978  0.01639  99  ASP   A CB  
768  C CG  . ASP   A 119 ? 0.35272 0.16077 0.26303 0.00219  0.02989  0.00102  99  ASP   A CG  
769  O OD1 . ASP   A 119 ? 0.36363 0.17603 0.24528 0.01121  -0.00991 -0.00979 99  ASP   A OD1 
770  O OD2 . ASP   A 119 ? 0.38291 0.14785 0.26134 -0.00401 0.02538  -0.00057 99  ASP   A OD2 
771  N N   . VAL   A 120 ? 0.32876 0.14857 0.22749 0.01815  -0.00966 -0.01922 100 VAL   A N   
772  C CA  . VAL   A 120 ? 0.33224 0.15299 0.21707 0.00613  0.03260  -0.03648 100 VAL   A CA  
773  C C   . VAL   A 120 ? 0.37624 0.16229 0.23446 0.02299  0.02093  -0.02227 100 VAL   A C   
774  O O   . VAL   A 120 ? 0.36290 0.15521 0.25033 0.03204  0.00512  -0.00118 100 VAL   A O   
775  C CB  . VAL   A 120 ? 0.31790 0.15359 0.20784 -0.01455 0.01527  -0.02790 100 VAL   A CB  
776  C CG1 . VAL   A 120 ? 0.34437 0.17226 0.25297 -0.01249 0.00467  -0.03552 100 VAL   A CG1 
777  C CG2 . VAL   A 120 ? 0.32539 0.19462 0.17805 0.00043  0.01322  -0.01689 100 VAL   A CG2 
778  N N   . LEU   A 121 ? 0.41351 0.14958 0.20667 0.03953  0.01132  0.00936  101 LEU   A N   
779  C CA  . LEU   A 121 ? 0.38588 0.15053 0.20933 0.05131  0.02019  0.01573  101 LEU   A CA  
780  C C   . LEU   A 121 ? 0.41878 0.15441 0.22832 0.01251  0.03884  0.01445  101 LEU   A C   
781  O O   . LEU   A 121 ? 0.43232 0.17495 0.25821 0.02494  0.03894  0.01499  101 LEU   A O   
782  C CB  . LEU   A 121 ? 0.40510 0.17511 0.23148 0.06575  0.01106  0.02632  101 LEU   A CB  
783  C CG  . LEU   A 121 ? 0.43880 0.18439 0.25365 0.02712  0.01768  0.03407  101 LEU   A CG  
784  C CD1 . LEU   A 121 ? 0.44504 0.24337 0.28892 0.03642  -0.01888 0.01493  101 LEU   A CD1 
785  C CD2 . LEU   A 121 ? 0.49192 0.18307 0.25924 0.01223  0.01471  0.02320  101 LEU   A CD2 
786  N N   . GLN   A 122 ? 0.41522 0.12777 0.22974 0.02758  0.01344  -0.00595 102 GLN   A N   
787  C CA  . GLN   A 122 ? 0.38285 0.13253 0.22997 0.03341  0.02574  -0.01109 102 GLN   A CA  
788  C C   . GLN   A 122 ? 0.37147 0.16829 0.21928 0.01954  0.04128  -0.01290 102 GLN   A C   
789  O O   . GLN   A 122 ? 0.35747 0.19801 0.24396 0.03622  0.09134  0.00411  102 GLN   A O   
790  C CB  . GLN   A 122 ? 0.39273 0.11449 0.21958 0.03546  0.01184  0.00536  102 GLN   A CB  
791  C CG  . GLN   A 122 ? 0.37365 0.13417 0.24287 0.06622  0.03056  0.00675  102 GLN   A CG  
792  C CD  . GLN   A 122 ? 0.37672 0.17507 0.26960 0.04621  0.06445  -0.00752 102 GLN   A CD  
793  O OE1 . GLN   A 122 ? 0.40434 0.19258 0.35473 0.01583  0.04994  0.01857  102 GLN   A OE1 
794  N NE2 . GLN   A 122 ? 0.36180 0.17590 0.32635 0.05274  0.03224  0.00373  102 GLN   A NE2 
795  N N   . HIS   A 123 ? 0.36045 0.15975 0.22652 0.00762  0.01019  -0.01757 103 HIS   A N   
796  C CA  . HIS   A 123 ? 0.34696 0.17324 0.22840 0.00105  0.01602  -0.02688 103 HIS   A CA  
797  C C   . HIS   A 123 ? 0.34525 0.16487 0.24186 0.01357  0.03611  -0.01271 103 HIS   A C   
798  O O   . HIS   A 123 ? 0.36582 0.18863 0.27362 0.01512  0.05736  0.00095  103 HIS   A O   
799  C CB  . HIS   A 123 ? 0.32410 0.17590 0.23509 0.03453  0.01232  -0.00891 103 HIS   A CB  
800  C CG  . HIS   A 123 ? 0.35665 0.15375 0.26434 0.03923  -0.00035 -0.01138 103 HIS   A CG  
801  N ND1 . HIS   A 123 ? 0.36226 0.15742 0.27490 0.03813  -0.00585 -0.01188 103 HIS   A ND1 
802  C CD2 . HIS   A 123 ? 0.34657 0.15184 0.26886 0.03258  0.00195  -0.01276 103 HIS   A CD2 
803  C CE1 . HIS   A 123 ? 0.35763 0.18208 0.31076 0.03314  -0.00076 -0.02407 103 HIS   A CE1 
804  N NE2 . HIS   A 123 ? 0.34942 0.18384 0.27430 0.03887  0.04456  -0.02091 103 HIS   A NE2 
805  N N   . VAL   A 124 ? 0.34259 0.14786 0.27306 0.02077  0.02921  0.00847  104 VAL   A N   
806  C CA  . VAL   A 124 ? 0.34501 0.15288 0.28080 0.02185  0.05237  -0.00237 104 VAL   A CA  
807  C C   . VAL   A 124 ? 0.35903 0.17862 0.26464 0.01235  0.09220  -0.00887 104 VAL   A C   
808  O O   . VAL   A 124 ? 0.37694 0.18344 0.28819 0.00070  0.05729  0.00133  104 VAL   A O   
809  C CB  . VAL   A 124 ? 0.32037 0.16782 0.31700 0.04072  0.08219  -0.01350 104 VAL   A CB  
810  C CG1 . VAL   A 124 ? 0.33195 0.19264 0.39952 0.05713  0.09719  0.03957  104 VAL   A CG1 
811  C CG2 . VAL   A 124 ? 0.33732 0.19149 0.29534 0.02856  0.06761  -0.04135 104 VAL   A CG2 
812  N N   . ASP   A 125 ? 0.38695 0.17323 0.23439 -0.01139 0.09288  -0.02555 105 ASP   A N   
813  C CA  . ASP   A 125 ? 0.41753 0.20343 0.25948 0.00339  0.07706  -0.01344 105 ASP   A CA  
814  C C   . ASP   A 125 ? 0.40391 0.21033 0.26910 0.01352  0.12043  -0.02153 105 ASP   A C   
815  O O   . ASP   A 125 ? 0.44278 0.23009 0.31288 0.01203  0.15526  -0.01569 105 ASP   A O   
816  C CB  . ASP   A 125 ? 0.43772 0.22885 0.26976 -0.02681 0.01949  0.01108  105 ASP   A CB  
817  C CG  . ASP   A 125 ? 0.47557 0.25003 0.31767 -0.02292 0.02764  -0.01321 105 ASP   A CG  
818  O OD1 . ASP   A 125 ? 0.49858 0.24752 0.30865 -0.02240 0.00152  0.01363  105 ASP   A OD1 
819  O OD2 . ASP   A 125 ? 0.49626 0.27009 0.33361 0.01224  0.01528  -0.01127 105 ASP   A OD2 
820  N N   . SER   A 126 ? 0.38233 0.20082 0.32754 0.03882  0.08891  -0.00871 106 SER   A N   
821  C CA  A SER   A 126 ? 0.37421 0.21789 0.34942 0.03772  0.06658  -0.01532 106 SER   A CA  
822  C CA  C SER   A 126 ? 0.38712 0.21675 0.35858 0.01801  0.06861  -0.00829 106 SER   A CA  
823  C C   . SER   A 126 ? 0.38440 0.22380 0.36249 0.01412  0.08070  -0.03695 106 SER   A C   
824  O O   . SER   A 126 ? 0.40215 0.24336 0.39723 0.01018  0.09218  -0.05721 106 SER   A O   
825  C CB  A SER   A 126 ? 0.35767 0.22228 0.35842 0.03587  0.02905  0.01204  106 SER   A CB  
826  C CB  C SER   A 126 ? 0.39403 0.21947 0.38323 -0.00490 0.03543  0.02360  106 SER   A CB  
827  O OG  A SER   A 126 ? 0.35750 0.22040 0.35587 0.05124  -0.00260 0.01271  106 SER   A OG  
828  O OG  C SER   A 126 ? 0.40473 0.22073 0.39310 -0.01249 0.00046  0.03317  106 SER   A OG  
829  N N   . MET   A 127 ? 0.41044 0.22504 0.31325 0.02272  0.05732  -0.05486 107 MET   A N   
830  C CA  . MET   A 127 ? 0.41304 0.26530 0.30315 0.00824  0.06941  -0.03245 107 MET   A CA  
831  C C   . MET   A 127 ? 0.43932 0.27699 0.35241 -0.00044 0.08936  -0.04305 107 MET   A C   
832  O O   . MET   A 127 ? 0.41051 0.28315 0.41900 0.00566  0.08783  -0.05140 107 MET   A O   
833  C CB  . MET   A 127 ? 0.42794 0.27705 0.30106 0.02759  0.05593  -0.02223 107 MET   A CB  
834  C CG  . MET   A 127 ? 0.43200 0.31987 0.37651 0.02279  0.05432  0.00242  107 MET   A CG  
835  S SD  . MET   A 127 ? 0.44159 0.34822 0.39994 0.03006  0.05083  0.03223  107 MET   A SD  
836  C CE  . MET   A 127 ? 0.43406 0.33559 0.45046 0.02968  0.04481  0.01731  107 MET   A CE  
837  N N   . GLN   A 128 ? 0.48597 0.28527 0.33894 -0.01244 0.11868  -0.01075 108 GLN   A N   
838  C CA  . GLN   A 128 ? 0.53457 0.31154 0.36150 -0.06212 0.15249  0.00114  108 GLN   A CA  
839  C C   . GLN   A 128 ? 0.53122 0.34037 0.38816 -0.09579 0.17748  -0.00964 108 GLN   A C   
840  O O   . GLN   A 128 ? 0.55600 0.36639 0.39737 -0.10967 0.17196  -0.00238 108 GLN   A O   
841  C CB  . GLN   A 128 ? 0.61417 0.32342 0.38630 -0.03429 0.11688  0.04046  108 GLN   A CB  
842  C CG  . GLN   A 128 ? 0.69897 0.37603 0.50966 0.00510  0.07606  0.03116  108 GLN   A CG  
843  C CD  . GLN   A 128 ? 0.76574 0.44778 0.55439 0.05416  0.07250  0.00836  108 GLN   A CD  
844  O OE1 . GLN   A 128 ? 0.78022 0.47473 0.52850 0.10054  0.07598  -0.00241 108 GLN   A OE1 
845  N NE2 . GLN   A 128 ? 0.81572 0.45751 0.60413 0.05248  0.10994  0.01630  108 GLN   A NE2 
846  N N   . LYS   A 129 ? 0.53607 0.35806 0.44501 -0.09582 0.16779  -0.08800 109 LYS   A N   
847  C CA  . LYS   A 129 ? 0.53516 0.40359 0.52871 -0.07855 0.19838  -0.10506 109 LYS   A CA  
848  C C   . LYS   A 129 ? 0.53093 0.41072 0.56788 -0.07179 0.23104  -0.12685 109 LYS   A C   
849  O O   . LYS   A 129 ? 0.55292 0.43205 0.56751 -0.05399 0.23474  -0.11687 109 LYS   A O   
850  C CB  . LYS   A 129 ? 0.52824 0.43293 0.52742 -0.07101 0.18631  -0.11152 109 LYS   A CB  
851  C CG  . LYS   A 129 ? 0.56181 0.45577 0.56217 -0.07096 0.12390  -0.08012 109 LYS   A CG  
852  C CD  . LYS   A 129 ? 0.58283 0.45431 0.62477 -0.06723 0.07815  -0.03866 109 LYS   A CD  
853  C CE  . LYS   A 129 ? 0.59785 0.45559 0.65518 -0.06499 0.04496  -0.03114 109 LYS   A CE  
854  N NZ  . LYS   A 129 ? 0.60655 0.44019 0.67604 -0.07568 0.02777  -0.05957 109 LYS   A NZ  
855  N N   . ASP   A 130 ? 0.53886 0.40402 0.59617 -0.05201 0.22143  -0.16197 110 ASP   A N   
856  C CA  . ASP   A 130 ? 0.54485 0.40973 0.65630 -0.02893 0.18655  -0.19525 110 ASP   A CA  
857  C C   . ASP   A 130 ? 0.52585 0.42081 0.65958 -0.01693 0.19940  -0.21945 110 ASP   A C   
858  O O   . ASP   A 130 ? 0.51190 0.43220 0.68012 0.00914  0.19739  -0.21531 110 ASP   A O   
859  C CB  . ASP   A 130 ? 0.58479 0.40742 0.73675 -0.02297 0.11751  -0.17591 110 ASP   A CB  
860  C CG  . ASP   A 130 ? 0.63229 0.42978 0.82849 -0.01164 0.09724  -0.12848 110 ASP   A CG  
861  O OD1 . ASP   A 130 ? 0.64544 0.42676 0.85917 0.00277  0.10617  -0.15139 110 ASP   A OD1 
862  O OD2 . ASP   A 130 ? 0.66218 0.43966 0.87957 -0.02166 0.07731  -0.08032 110 ASP   A OD2 
863  N N   . TYR   A 131 ? 0.52510 0.42835 0.62495 -0.04872 0.19202  -0.22633 111 TYR   A N   
864  C CA  . TYR   A 131 ? 0.52782 0.44643 0.62952 -0.06532 0.19995  -0.20142 111 TYR   A CA  
865  C C   . TYR   A 131 ? 0.53386 0.43289 0.63287 -0.10671 0.22040  -0.20459 111 TYR   A C   
866  O O   . TYR   A 131 ? 0.52300 0.42663 0.65605 -0.11851 0.19034  -0.23896 111 TYR   A O   
867  C CB  . TYR   A 131 ? 0.53554 0.47294 0.58618 -0.04923 0.20131  -0.21208 111 TYR   A CB  
868  C CG  . TYR   A 131 ? 0.55372 0.52483 0.57305 -0.03924 0.20095  -0.19792 111 TYR   A CG  
869  C CD1 . TYR   A 131 ? 0.56212 0.53693 0.57664 -0.03439 0.17417  -0.20334 111 TYR   A CD1 
870  C CD2 . TYR   A 131 ? 0.57467 0.55162 0.58766 -0.03549 0.19636  -0.18215 111 TYR   A CD2 
871  C CE1 . TYR   A 131 ? 0.58072 0.55843 0.60018 -0.02625 0.14938  -0.18464 111 TYR   A CE1 
872  C CE2 . TYR   A 131 ? 0.58472 0.56633 0.59151 -0.02501 0.18859  -0.16727 111 TYR   A CE2 
873  C CZ  . TYR   A 131 ? 0.59918 0.57611 0.60001 -0.02045 0.16024  -0.16311 111 TYR   A CZ  
874  O OH  . TYR   A 131 ? 0.60965 0.59429 0.61072 -0.00083 0.15419  -0.16769 111 TYR   A OH  
875  N N   . PRO   A 132 ? 0.57490 0.43780 0.65265 -0.11098 0.21725  -0.17196 112 PRO   A N   
876  C CA  . PRO   A 132 ? 0.60832 0.44086 0.64140 -0.09784 0.20997  -0.14414 112 PRO   A CA  
877  C C   . PRO   A 132 ? 0.64273 0.43268 0.61528 -0.09625 0.22683  -0.11688 112 PRO   A C   
878  O O   . PRO   A 132 ? 0.66019 0.44951 0.62869 -0.10881 0.24998  -0.10479 112 PRO   A O   
879  C CB  . PRO   A 132 ? 0.60452 0.45209 0.65921 -0.09317 0.18694  -0.15758 112 PRO   A CB  
880  C CG  . PRO   A 132 ? 0.59573 0.46220 0.66886 -0.08807 0.21364  -0.15742 112 PRO   A CG  
881  C CD  . PRO   A 132 ? 0.58790 0.45307 0.66948 -0.08932 0.21752  -0.15383 112 PRO   A CD  
882  N N   . GLY   A 133 ? 0.64892 0.41633 0.58729 -0.06553 0.21350  -0.09067 113 GLY   A N   
883  C CA  . GLY   A 133 ? 0.64523 0.40235 0.56633 -0.06446 0.20630  -0.08675 113 GLY   A CA  
884  C C   . GLY   A 133 ? 0.63593 0.40338 0.56459 -0.03502 0.22620  -0.07120 113 GLY   A C   
885  O O   . GLY   A 133 ? 0.67799 0.39796 0.58093 -0.05671 0.22533  -0.06531 113 GLY   A O   
886  N N   . LEU   A 134 ? 0.57924 0.40443 0.50718 -0.01292 0.22897  -0.05033 114 LEU   A N   
887  C CA  . LEU   A 134 ? 0.52271 0.39018 0.50685 -0.01170 0.18659  -0.03687 114 LEU   A CA  
888  C C   . LEU   A 134 ? 0.50563 0.38702 0.45611 -0.02236 0.16668  -0.00734 114 LEU   A C   
889  O O   . LEU   A 134 ? 0.52914 0.42008 0.47828 -0.03586 0.19232  -0.02543 114 LEU   A O   
890  C CB  . LEU   A 134 ? 0.51398 0.38403 0.55100 0.00896  0.13586  -0.03389 114 LEU   A CB  
891  C CG  . LEU   A 134 ? 0.51580 0.38091 0.60576 0.01905  0.11829  -0.04377 114 LEU   A CG  
892  C CD1 . LEU   A 134 ? 0.52102 0.37384 0.57136 0.03433  0.10360  -0.04964 114 LEU   A CD1 
893  C CD2 . LEU   A 134 ? 0.50297 0.37995 0.64222 0.02218  0.12937  -0.06146 114 LEU   A CD2 
894  N N   . PRO   A 135 ? 0.47126 0.34603 0.42714 0.00005  0.14892  0.02489  115 PRO   A N   
895  C CA  . PRO   A 135 ? 0.45331 0.32847 0.39431 -0.00135 0.13685  0.04297  115 PRO   A CA  
896  C C   . PRO   A 135 ? 0.42370 0.28804 0.37735 -0.00901 0.11971  0.03094  115 PRO   A C   
897  O O   . PRO   A 135 ? 0.38987 0.32199 0.37058 -0.00568 0.13855  0.05230  115 PRO   A O   
898  C CB  . PRO   A 135 ? 0.45665 0.33156 0.46590 0.01110  0.11043  0.03969  115 PRO   A CB  
899  C CG  . PRO   A 135 ? 0.47249 0.34453 0.51123 0.00424  0.11989  0.02281  115 PRO   A CG  
900  C CD  . PRO   A 135 ? 0.46306 0.33500 0.46376 0.00062  0.15045  0.00670  115 PRO   A CD  
901  N N   . VAL   A 136 ? 0.39908 0.22893 0.32718 -0.01626 0.11948  0.01270  116 VAL   A N   
902  C CA  A VAL   A 136 ? 0.40028 0.20299 0.30684 -0.01541 0.10968  0.01297  116 VAL   A CA  
903  C CA  B VAL   A 136 ? 0.39406 0.18932 0.29485 -0.00876 0.13259  0.02876  116 VAL   A CA  
904  C C   . VAL   A 136 ? 0.39410 0.18817 0.28814 -0.00963 0.08999  0.01614  116 VAL   A C   
905  O O   . VAL   A 136 ? 0.40814 0.21221 0.29615 -0.00870 0.08839  0.00100  116 VAL   A O   
906  C CB  A VAL   A 136 ? 0.41134 0.20398 0.33083 -0.01761 0.10678  -0.01117 116 VAL   A CB  
907  C CB  B VAL   A 136 ? 0.41115 0.20646 0.33691 0.01160  0.11136  -0.03422 116 VAL   A CB  
908  C CG1 A VAL   A 136 ? 0.41235 0.20194 0.33240 -0.01968 0.10394  -0.00940 116 VAL   A CG1 
909  C CG1 B VAL   A 136 ? 0.44341 0.21061 0.37367 0.00483  0.09101  -0.02136 116 VAL   A CG1 
910  C CG2 A VAL   A 136 ? 0.42255 0.20385 0.35130 -0.02036 0.10135  -0.00968 116 VAL   A CG2 
911  C CG2 B VAL   A 136 ? 0.41080 0.21368 0.35021 0.02708  0.14221  -0.06318 116 VAL   A CG2 
912  N N   . PHE   A 137 ? 0.35989 0.17224 0.27612 -0.01775 0.09328  0.00246  117 PHE   A N   
913  C CA  . PHE   A 137 ? 0.32905 0.16526 0.30967 -0.00791 0.07463  -0.00653 117 PHE   A CA  
914  C C   . PHE   A 137 ? 0.29281 0.14425 0.29836 0.00964  0.04232  0.04016  117 PHE   A C   
915  O O   . PHE   A 137 ? 0.28960 0.14573 0.33497 0.02973  0.06416  0.02992  117 PHE   A O   
916  C CB  . PHE   A 137 ? 0.32611 0.15725 0.30044 -0.01602 0.07430  0.00296  117 PHE   A CB  
917  C CG  . PHE   A 137 ? 0.32964 0.18096 0.33680 -0.01372 0.11024  -0.00744 117 PHE   A CG  
918  C CD1 . PHE   A 137 ? 0.36266 0.20512 0.35351 -0.01487 0.10608  0.00921  117 PHE   A CD1 
919  C CD2 . PHE   A 137 ? 0.36227 0.17087 0.35516 -0.00713 0.09942  -0.01057 117 PHE   A CD2 
920  C CE1 . PHE   A 137 ? 0.37384 0.21296 0.37594 -0.02941 0.12395  0.01500  117 PHE   A CE1 
921  C CE2 . PHE   A 137 ? 0.35157 0.19873 0.35142 -0.01324 0.12247  0.01670  117 PHE   A CE2 
922  C CZ  . PHE   A 137 ? 0.38519 0.22991 0.37384 -0.01617 0.09441  0.01881  117 PHE   A CZ  
923  N N   . LEU   A 138 ? 0.28040 0.16057 0.29810 -0.00176 0.03439  0.03113  118 LEU   A N   
924  C CA  . LEU   A 138 ? 0.28830 0.17305 0.28054 -0.00889 0.02604  0.02195  118 LEU   A CA  
925  C C   . LEU   A 138 ? 0.28716 0.16572 0.24481 0.00882  0.03451  0.01359  118 LEU   A C   
926  O O   . LEU   A 138 ? 0.32166 0.14972 0.27585 0.02810  0.04490  0.01624  118 LEU   A O   
927  C CB  . LEU   A 138 ? 0.27145 0.17199 0.28592 0.00590  0.01941  0.00366  118 LEU   A CB  
928  C CG  . LEU   A 138 ? 0.29859 0.17815 0.26137 0.02485  -0.02840 -0.03857 118 LEU   A CG  
929  C CD1 . LEU   A 138 ? 0.29577 0.21808 0.27943 0.03006  -0.00989 -0.00685 118 LEU   A CD1 
930  C CD2 . LEU   A 138 ? 0.36030 0.18197 0.35043 0.03748  -0.02337 -0.01902 118 LEU   A CD2 
931  N N   . LEU   A 139 ? 0.28351 0.16522 0.25030 0.00423  0.06143  0.01082  119 LEU   A N   
932  C CA  . LEU   A 139 ? 0.27774 0.17241 0.24243 0.00086  0.05441  0.00869  119 LEU   A CA  
933  C C   . LEU   A 139 ? 0.26350 0.16468 0.23507 0.01161  0.05218  0.01393  119 LEU   A C   
934  O O   . LEU   A 139 ? 0.28000 0.13917 0.30246 0.02381  0.06111  0.02349  119 LEU   A O   
935  C CB  . LEU   A 139 ? 0.27246 0.20477 0.25428 0.00497  0.07299  0.00386  119 LEU   A CB  
936  C CG  . LEU   A 139 ? 0.27140 0.22300 0.26089 -0.02731 0.05968  0.00209  119 LEU   A CG  
937  C CD1 . LEU   A 139 ? 0.29201 0.24257 0.30944 -0.02113 0.02983  -0.00670 119 LEU   A CD1 
938  C CD2 . LEU   A 139 ? 0.27931 0.19953 0.26587 -0.03179 0.07365  -0.01906 119 LEU   A CD2 
939  N N   . GLY   A 140 ? 0.20971 0.13866 0.24856 -0.00941 0.01684  -0.02532 120 GLY   A N   
940  C CA  . GLY   A 140 ? 0.22318 0.14146 0.23705 -0.01254 0.03316  0.01312  120 GLY   A CA  
941  C C   . GLY   A 140 ? 0.24414 0.14388 0.21394 0.00653  0.04363  0.00646  120 GLY   A C   
942  O O   . GLY   A 140 ? 0.31945 0.11746 0.23981 0.00804  0.05519  0.00129  120 GLY   A O   
943  N N   . HIS   A 141 ? 0.23084 0.16123 0.20503 -0.01357 0.04559  0.00271  121 HIS   A N   
944  C CA  . HIS   A 141 ? 0.25703 0.17331 0.17819 -0.00983 0.00656  -0.00769 121 HIS   A CA  
945  C C   . HIS   A 141 ? 0.25539 0.16283 0.22065 0.00918  -0.00451 -0.01628 121 HIS   A C   
946  O O   . HIS   A 141 ? 0.26300 0.15455 0.22881 -0.00063 0.01307  -0.00486 121 HIS   A O   
947  C CB  . HIS   A 141 ? 0.27217 0.16847 0.17871 0.00058  0.00842  0.00131  121 HIS   A CB  
948  C CG  . HIS   A 141 ? 0.26620 0.14670 0.21873 -0.00409 0.00929  -0.00467 121 HIS   A CG  
949  N ND1 . HIS   A 141 ? 0.24550 0.14793 0.21073 -0.01898 0.03494  0.00699  121 HIS   A ND1 
950  C CD2 . HIS   A 141 ? 0.25931 0.16792 0.24246 -0.04522 0.01357  0.00038  121 HIS   A CD2 
951  C CE1 . HIS   A 141 ? 0.26203 0.13133 0.22860 -0.01874 0.01104  0.03155  121 HIS   A CE1 
952  N NE2 . HIS   A 141 ? 0.25612 0.17000 0.21307 -0.03578 -0.00443 0.02888  121 HIS   A NE2 
953  N N   . SER   A 142 ? 0.25422 0.14686 0.23920 0.01524  0.03771  0.01167  122 SER   A N   
954  C CA  . SER   A 142 ? 0.26201 0.15927 0.20906 -0.01007 0.01947  0.00836  122 SER   A CA  
955  C C   . SER   A 142 ? 0.26406 0.12368 0.21537 -0.00837 -0.00916 0.00165  122 SER   A C   
956  O O   . SER   A 142 ? 0.27731 0.13534 0.23059 -0.00057 0.01639  -0.00031 122 SER   A O   
957  C CB  . SER   A 142 ? 0.25058 0.14290 0.24895 -0.02662 0.04114  0.01379  122 SER   A CB  
958  O OG  . SER   A 142 ? 0.26033 0.15830 0.24973 -0.00554 0.03346  0.00228  122 SER   A OG  
959  N N   . MET   A 143 ? 0.23103 0.10307 0.26121 0.01815  0.02639  -0.02657 123 MET   A N   
960  C CA  . MET   A 143 ? 0.27561 0.10851 0.25929 -0.00700 0.01624  -0.03830 123 MET   A CA  
961  C C   . MET   A 143 ? 0.27942 0.14297 0.23393 0.00443  0.01047  0.00684  123 MET   A C   
962  O O   . MET   A 143 ? 0.27006 0.13704 0.24470 0.01306  0.00343  0.00603  123 MET   A O   
963  C CB  . MET   A 143 ? 0.30333 0.11690 0.27371 -0.02226 0.02070  -0.00856 123 MET   A CB  
964  C CG  . MET   A 143 ? 0.28991 0.14387 0.28968 -0.03295 0.00140  -0.00832 123 MET   A CG  
965  S SD  . MET   A 143 ? 0.29316 0.16406 0.29392 -0.02347 0.00594  -0.00867 123 MET   A SD  
966  C CE  . MET   A 143 ? 0.28714 0.14923 0.29068 0.00115  0.02064  0.00851  123 MET   A CE  
967  N N   . GLY   A 144 ? 0.22162 0.12071 0.28170 -0.00820 0.01504  0.02421  124 GLY   A N   
968  C CA  . GLY   A 144 ? 0.24496 0.13630 0.25988 -0.01162 0.07324  0.01638  124 GLY   A CA  
969  C C   . GLY   A 144 ? 0.27851 0.14947 0.22635 0.01541  0.00115  0.00026  124 GLY   A C   
970  O O   . GLY   A 144 ? 0.27865 0.14690 0.24411 0.00784  0.01167  -0.01282 124 GLY   A O   
971  N N   . GLY   A 145 ? 0.29381 0.12553 0.23715 0.01244  -0.00981 0.00090  125 GLY   A N   
972  C CA  . GLY   A 145 ? 0.30971 0.14848 0.21577 0.03415  -0.03250 -0.00268 125 GLY   A CA  
973  C C   . GLY   A 145 ? 0.27547 0.14116 0.23392 0.01901  -0.00784 -0.01226 125 GLY   A C   
974  O O   . GLY   A 145 ? 0.28870 0.15653 0.25156 0.01851  0.00647  -0.00040 125 GLY   A O   
975  N N   . ALA   A 146 ? 0.23800 0.15926 0.24966 -0.00014 -0.04890 -0.00549 126 ALA   A N   
976  C CA  . ALA   A 146 ? 0.24851 0.15860 0.25047 -0.00641 -0.02244 -0.01753 126 ALA   A CA  
977  C C   . ALA   A 146 ? 0.26615 0.14747 0.25894 0.01356  -0.00360 0.01202  126 ALA   A C   
978  O O   . ALA   A 146 ? 0.28939 0.17992 0.25317 0.00199  -0.00632 0.00060  126 ALA   A O   
979  C CB  . ALA   A 146 ? 0.27524 0.15740 0.25006 -0.00321 -0.00433 0.01998  126 ALA   A CB  
980  N N   . ILE   A 147 ? 0.26232 0.12872 0.25460 0.04300  -0.00763 -0.00336 127 ILE   A N   
981  C CA  . ILE   A 147 ? 0.24405 0.12828 0.24616 0.01851  -0.00211 0.00243  127 ILE   A CA  
982  C C   . ILE   A 147 ? 0.27827 0.15579 0.25510 0.00528  -0.00054 -0.00322 127 ILE   A C   
983  O O   . ILE   A 147 ? 0.32224 0.17843 0.22074 0.00877  -0.00354 -0.00481 127 ILE   A O   
984  C CB  . ILE   A 147 ? 0.23211 0.12010 0.26214 0.01805  0.02132  0.00789  127 ILE   A CB  
985  C CG1 . ILE   A 147 ? 0.22025 0.13358 0.26765 -0.01711 0.00474  0.03274  127 ILE   A CG1 
986  C CG2 . ILE   A 147 ? 0.27703 0.14760 0.30336 0.05019  0.01877  -0.01210 127 ILE   A CG2 
987  C CD1 . ILE   A 147 ? 0.24433 0.14696 0.24930 0.00064  -0.04777 0.03165  127 ILE   A CD1 
988  N N   . ALA   A 148 ? 0.23064 0.15807 0.26981 -0.02902 0.01836  0.01040  128 ALA   A N   
989  C CA  . ALA   A 148 ? 0.25694 0.17040 0.27207 -0.00823 -0.00066 0.01178  128 ALA   A CA  
990  C C   . ALA   A 148 ? 0.28472 0.15893 0.24204 0.02925  0.00913  0.00061  128 ALA   A C   
991  O O   . ALA   A 148 ? 0.31128 0.17205 0.25047 0.00799  -0.00059 0.01715  128 ALA   A O   
992  C CB  . ALA   A 148 ? 0.25163 0.15232 0.26738 -0.00149 0.00840  0.00198  128 ALA   A CB  
993  N N   . ILE   A 149 ? 0.28909 0.17468 0.23854 0.02612  0.01934  -0.01268 129 ILE   A N   
994  C CA  . ILE   A 149 ? 0.31549 0.17388 0.23556 0.02266  -0.00597 -0.00321 129 ILE   A CA  
995  C C   . ILE   A 149 ? 0.32618 0.17180 0.24418 0.00321  0.01023  0.00396  129 ILE   A C   
996  O O   . ILE   A 149 ? 0.34158 0.18032 0.25591 0.00221  0.01590  0.01538  129 ILE   A O   
997  C CB  . ILE   A 149 ? 0.28562 0.18185 0.21557 0.04075  0.01216  -0.01012 129 ILE   A CB  
998  C CG1 . ILE   A 149 ? 0.29510 0.16790 0.23244 0.02454  0.02209  -0.04288 129 ILE   A CG1 
999  C CG2 . ILE   A 149 ? 0.32437 0.19125 0.25572 0.04319  -0.02031 0.00250  129 ILE   A CG2 
1000 C CD1 . ILE   A 149 ? 0.29014 0.19491 0.24941 0.02989  0.02319  -0.03621 129 ILE   A CD1 
1001 N N   . LEU   A 150 ? 0.33679 0.15568 0.26484 0.01073  -0.01878 -0.01921 130 LEU   A N   
1002 C CA  . LEU   A 150 ? 0.35335 0.18721 0.24965 0.01671  0.00578  -0.01487 130 LEU   A CA  
1003 C C   . LEU   A 150 ? 0.37967 0.20697 0.23233 0.02842  0.02383  -0.02013 130 LEU   A C   
1004 O O   . LEU   A 150 ? 0.40709 0.25178 0.22183 0.03521  0.01387  -0.01100 130 LEU   A O   
1005 C CB  . LEU   A 150 ? 0.35665 0.19469 0.27483 -0.00748 -0.02298 -0.00447 130 LEU   A CB  
1006 C CG  . LEU   A 150 ? 0.32806 0.20873 0.30351 0.00128  -0.02228 0.03094  130 LEU   A CG  
1007 C CD1 . LEU   A 150 ? 0.34738 0.21306 0.31750 -0.02730 -0.00532 0.04014  130 LEU   A CD1 
1008 C CD2 . LEU   A 150 ? 0.31039 0.21486 0.32304 0.01976  -0.02718 0.02453  130 LEU   A CD2 
1009 N N   . THR   A 151 ? 0.35451 0.16252 0.26086 0.02266  0.04091  0.00448  131 THR   A N   
1010 C CA  . THR   A 151 ? 0.37867 0.16872 0.25185 0.00747  0.04675  0.02071  131 THR   A CA  
1011 C C   . THR   A 151 ? 0.40030 0.18120 0.27237 0.01793  0.02420  0.02015  131 THR   A C   
1012 O O   . THR   A 151 ? 0.42044 0.18170 0.28281 0.01001  0.03029  0.02381  131 THR   A O   
1013 C CB  . THR   A 151 ? 0.36614 0.17742 0.25740 0.01453  0.04903  0.02192  131 THR   A CB  
1014 O OG1 . THR   A 151 ? 0.35785 0.18134 0.23300 0.01565  0.00628  -0.00503 131 THR   A OG1 
1015 C CG2 . THR   A 151 ? 0.38890 0.18069 0.27177 0.00838  0.06221  0.00181  131 THR   A CG2 
1016 N N   . ALA   A 152 ? 0.40019 0.18522 0.26744 0.00146  0.01397  0.00461  132 ALA   A N   
1017 C CA  . ALA   A 152 ? 0.40507 0.21190 0.24585 0.01788  0.01711  0.02101  132 ALA   A CA  
1018 C C   . ALA   A 152 ? 0.44448 0.25423 0.26429 0.05529  0.00363  0.04004  132 ALA   A C   
1019 O O   . ALA   A 152 ? 0.49200 0.29881 0.29552 0.07099  0.02676  0.03949  132 ALA   A O   
1020 C CB  . ALA   A 152 ? 0.41973 0.18565 0.24617 0.01588  0.01761  -0.00837 132 ALA   A CB  
1021 N N   . ALA   A 153 ? 0.42800 0.26873 0.24202 0.07216  0.02553  0.03694  133 ALA   A N   
1022 C CA  . ALA   A 153 ? 0.45863 0.32534 0.23702 0.07547  0.03071  0.01770  133 ALA   A CA  
1023 C C   . ALA   A 153 ? 0.49471 0.34708 0.23286 0.07992  -0.00327 0.04138  133 ALA   A C   
1024 O O   . ALA   A 153 ? 0.51363 0.37678 0.25927 0.09902  -0.04324 0.03878  133 ALA   A O   
1025 C CB  . ALA   A 153 ? 0.44674 0.34871 0.29578 0.06920  0.05052  0.01340  133 ALA   A CB  
1026 N N   . GLU   A 154 ? 0.51709 0.33336 0.27038 0.06105  -0.00192 0.00195  134 GLU   A N   
1027 C CA  . GLU   A 154 ? 0.54290 0.34938 0.32000 0.05404  -0.01414 -0.01068 134 GLU   A CA  
1028 C C   . GLU   A 154 ? 0.57701 0.33211 0.29240 0.03673  -0.00641 0.02390  134 GLU   A C   
1029 O O   . GLU   A 154 ? 0.58281 0.35164 0.29567 0.02488  0.00369  -0.00674 134 GLU   A O   
1030 C CB  . GLU   A 154 ? 0.55094 0.38822 0.42679 0.03473  -0.02220 -0.03245 134 GLU   A CB  
1031 C CG  . GLU   A 154 ? 0.58009 0.44179 0.61020 0.00962  -0.05394 -0.09047 134 GLU   A CG  
1032 C CD  . GLU   A 154 ? 0.59888 0.50116 0.77222 -0.00337 -0.06808 -0.14044 134 GLU   A CD  
1033 O OE1 . GLU   A 154 ? 0.59217 0.52210 0.87852 -0.00820 -0.05415 -0.10031 134 GLU   A OE1 
1034 O OE2 . GLU   A 154 ? 0.62501 0.54064 0.81345 -0.00380 -0.07903 -0.19477 134 GLU   A OE2 
1035 N N   . ARG   A 155 ? 0.59235 0.29990 0.29400 0.04202  0.01144  0.01224  135 ARG   A N   
1036 C CA  . ARG   A 155 ? 0.61661 0.29111 0.27943 0.05630  0.01300  0.02593  135 ARG   A CA  
1037 C C   . ARG   A 155 ? 0.62615 0.30519 0.26176 0.07811  0.00680  0.05068  135 ARG   A C   
1038 O O   . ARG   A 155 ? 0.64152 0.29546 0.34933 0.10095  0.02778  0.03060  135 ARG   A O   
1039 C CB  . ARG   A 155 ? 0.63009 0.24766 0.31639 0.07902  0.02312  0.02014  135 ARG   A CB  
1040 C CG  . ARG   A 155 ? 0.66058 0.24531 0.35118 0.08752  0.02454  0.00849  135 ARG   A CG  
1041 C CD  . ARG   A 155 ? 0.69333 0.24765 0.37426 0.10461  0.04394  0.00910  135 ARG   A CD  
1042 N NE  . ARG   A 155 ? 0.71796 0.23246 0.36490 0.11463  0.03452  0.04066  135 ARG   A NE  
1043 C CZ  . ARG   A 155 ? 0.75411 0.23047 0.38070 0.10444  0.04498  0.02855  135 ARG   A CZ  
1044 N NH1 . ARG   A 155 ? 0.75251 0.23023 0.36373 0.09007  0.05276  -0.01035 135 ARG   A NH1 
1045 N NH2 . ARG   A 155 ? 0.75625 0.24287 0.36198 0.10426  0.03500  0.03402  135 ARG   A NH2 
1046 N N   . PRO   A 156 ? 0.64710 0.33496 0.30865 0.05420  0.02608  0.07452  136 PRO   A N   
1047 C CA  . PRO   A 156 ? 0.66621 0.35355 0.33981 0.05781  0.00947  0.06164  136 PRO   A CA  
1048 C C   . PRO   A 156 ? 0.67773 0.35507 0.35461 0.03351  0.02290  0.03121  136 PRO   A C   
1049 O O   . PRO   A 156 ? 0.68380 0.35439 0.35728 0.03847  0.00033  0.03095  136 PRO   A O   
1050 C CB  . PRO   A 156 ? 0.66914 0.37062 0.40128 0.07605  -0.01228 0.05325  136 PRO   A CB  
1051 C CG  . PRO   A 156 ? 0.66584 0.36013 0.41826 0.07039  -0.02265 0.07507  136 PRO   A CG  
1052 C CD  . PRO   A 156 ? 0.65738 0.35969 0.33616 0.05793  0.01126  0.08235  136 PRO   A CD  
1053 N N   . GLY   A 157 ? 0.68182 0.33888 0.38278 0.01991  0.07288  0.03297  137 GLY   A N   
1054 C CA  . GLY   A 157 ? 0.68018 0.34927 0.38271 0.02755  0.10892  0.03130  137 GLY   A CA  
1055 C C   . GLY   A 157 ? 0.67693 0.37900 0.42672 0.00929  0.13930  0.01536  137 GLY   A C   
1056 O O   . GLY   A 157 ? 0.71493 0.40014 0.43374 0.00472  0.18207  0.04374  137 GLY   A O   
1057 N N   . HIS   A 158 ? 0.66698 0.38035 0.31446 -0.00136 0.10960  -0.00464 138 HIS   A N   
1058 C CA  . HIS   A 158 ? 0.65983 0.41268 0.31886 0.00015  0.06911  -0.03404 138 HIS   A CA  
1059 C C   . HIS   A 158 ? 0.59980 0.35588 0.30156 0.01764  0.08189  -0.02940 138 HIS   A C   
1060 O O   . HIS   A 158 ? 0.62759 0.40485 0.35366 0.05668  0.09778  -0.05238 138 HIS   A O   
1061 C CB  . HIS   A 158 ? 0.70427 0.53114 0.41069 -0.02065 0.04830  -0.09147 138 HIS   A CB  
1062 C CG  . HIS   A 158 ? 0.75290 0.62456 0.46324 -0.02845 0.03278  -0.13604 138 HIS   A CG  
1063 N ND1 . HIS   A 158 ? 0.77002 0.66087 0.55888 -0.02517 0.00464  -0.12771 138 HIS   A ND1 
1064 C CD2 . HIS   A 158 ? 0.78037 0.66058 0.52628 -0.02624 0.05028  -0.13214 138 HIS   A CD2 
1065 C CE1 . HIS   A 158 ? 0.78727 0.67740 0.61978 -0.02854 -0.00306 -0.13292 138 HIS   A CE1 
1066 N NE2 . HIS   A 158 ? 0.79618 0.67828 0.61109 -0.02898 0.01079  -0.13866 138 HIS   A NE2 
1067 N N   . PHE   A 159 ? 0.51583 0.26363 0.24875 -0.00415 0.08946  -0.01580 139 PHE   A N   
1068 C CA  . PHE   A 159 ? 0.46125 0.21495 0.25437 -0.01674 0.04933  0.00330  139 PHE   A CA  
1069 C C   . PHE   A 159 ? 0.43921 0.21198 0.29603 -0.00198 0.04869  0.01957  139 PHE   A C   
1070 O O   . PHE   A 159 ? 0.45424 0.22646 0.32325 0.03407  0.03635  0.04358  139 PHE   A O   
1071 C CB  . PHE   A 159 ? 0.42630 0.18949 0.24888 -0.01156 0.09424  0.00097  139 PHE   A CB  
1072 C CG  . PHE   A 159 ? 0.43375 0.18131 0.26103 0.00450  0.05626  0.01992  139 PHE   A CG  
1073 C CD1 . PHE   A 159 ? 0.43376 0.18511 0.31355 0.04196  0.06083  -0.00533 139 PHE   A CD1 
1074 C CD2 . PHE   A 159 ? 0.41004 0.19152 0.30127 0.01954  0.04826  0.03466  139 PHE   A CD2 
1075 C CE1 . PHE   A 159 ? 0.43924 0.19115 0.33582 0.03846  0.06649  0.00144  139 PHE   A CE1 
1076 C CE2 . PHE   A 159 ? 0.42465 0.19477 0.27059 0.03989  0.06923  0.02507  139 PHE   A CE2 
1077 C CZ  . PHE   A 159 ? 0.42469 0.19734 0.30794 0.04686  0.05244  0.00088  139 PHE   A CZ  
1078 N N   . ALA   A 160 ? 0.43316 0.21381 0.27866 0.00173  0.09191  -0.00479 140 ALA   A N   
1079 C CA  . ALA   A 160 ? 0.39151 0.22718 0.29945 -0.01262 0.10710  -0.00261 140 ALA   A CA  
1080 C C   . ALA   A 160 ? 0.39202 0.18013 0.28683 0.00362  0.10418  0.02472  140 ALA   A C   
1081 O O   . ALA   A 160 ? 0.42082 0.17776 0.30955 0.01523  0.06300  0.03868  140 ALA   A O   
1082 C CB  . ALA   A 160 ? 0.39689 0.23922 0.36415 -0.00812 0.10151  -0.04649 140 ALA   A CB  
1083 N N   . GLY   A 161 ? 0.38953 0.18639 0.27902 0.00960  0.13239  0.02353  141 GLY   A N   
1084 C CA  . GLY   A 161 ? 0.38057 0.18529 0.25723 0.00404  0.10962  0.02835  141 GLY   A CA  
1085 C C   . GLY   A 161 ? 0.36321 0.16478 0.23589 0.00777  0.10702  0.00757  141 GLY   A C   
1086 O O   . GLY   A 161 ? 0.40428 0.15443 0.28839 0.00474  0.10383  0.00516  141 GLY   A O   
1087 N N   . MET   A 162 ? 0.36380 0.18230 0.24927 -0.00028 0.08905  0.01822  142 MET   A N   
1088 C CA  A MET   A 162 ? 0.33913 0.16304 0.25465 0.00302  0.05752  0.00306  142 MET   A CA  
1089 C CA  B MET   A 162 ? 0.34747 0.18831 0.26681 -0.00290 0.05991  0.00376  142 MET   A CA  
1090 C C   . MET   A 162 ? 0.33027 0.15281 0.21525 0.00839  0.05045  0.00315  142 MET   A C   
1091 O O   . MET   A 162 ? 0.33807 0.13769 0.25918 0.02870  0.02770  0.01304  142 MET   A O   
1092 C CB  A MET   A 162 ? 0.36456 0.17755 0.30155 -0.01093 0.02024  -0.01708 142 MET   A CB  
1093 C CB  B MET   A 162 ? 0.37673 0.23599 0.32344 -0.02564 0.03797  -0.01265 142 MET   A CB  
1094 C CG  A MET   A 162 ? 0.34415 0.17685 0.28977 -0.02476 0.02726  -0.02364 142 MET   A CG  
1095 C CG  B MET   A 162 ? 0.38000 0.25800 0.33862 -0.04018 0.02960  -0.02415 142 MET   A CG  
1096 S SD  A MET   A 162 ? 0.33561 0.20337 0.27403 -0.01445 0.03043  -0.03762 142 MET   A SD  
1097 S SD  B MET   A 162 ? 0.38090 0.29423 0.34498 -0.06290 0.01485  -0.02181 142 MET   A SD  
1098 C CE  A MET   A 162 ? 0.33973 0.23613 0.32267 -0.00901 0.02745  0.00911  142 MET   A CE  
1099 C CE  B MET   A 162 ? 0.39568 0.30802 0.35213 -0.05454 0.00569  -0.01201 142 MET   A CE  
1100 N N   . VAL   A 163 ? 0.32291 0.16751 0.21115 0.01234  0.01524  0.00203  143 VAL   A N   
1101 C CA  . VAL   A 163 ? 0.29324 0.16781 0.26196 -0.00163 0.03365  0.01429  143 VAL   A CA  
1102 C C   . VAL   A 163 ? 0.27665 0.14318 0.22794 -0.00430 0.04681  0.00780  143 VAL   A C   
1103 O O   . VAL   A 163 ? 0.29071 0.11289 0.28032 0.01935  0.04881  0.00186  143 VAL   A O   
1104 C CB  . VAL   A 163 ? 0.27015 0.18821 0.28424 -0.00404 0.02571  0.01406  143 VAL   A CB  
1105 C CG1 . VAL   A 163 ? 0.29169 0.18459 0.33301 -0.02105 -0.02177 -0.01649 143 VAL   A CG1 
1106 C CG2 . VAL   A 163 ? 0.23501 0.20372 0.32847 -0.00252 0.06999  0.04187  143 VAL   A CG2 
1107 N N   . LEU   A 164 ? 0.25199 0.13846 0.21224 -0.00562 0.04558  0.00788  144 LEU   A N   
1108 C CA  . LEU   A 164 ? 0.26944 0.15196 0.20535 -0.01162 0.01017  0.01895  144 LEU   A CA  
1109 C C   . LEU   A 164 ? 0.30551 0.14492 0.23979 0.00384  -0.00014 0.01711  144 LEU   A C   
1110 O O   . LEU   A 164 ? 0.33224 0.11932 0.25840 0.01304  0.02629  0.00645  144 LEU   A O   
1111 C CB  . LEU   A 164 ? 0.31622 0.17615 0.20358 0.02394  -0.01597 0.00172  144 LEU   A CB  
1112 C CG  . LEU   A 164 ? 0.32722 0.16888 0.24308 0.03320  -0.02011 0.00124  144 LEU   A CG  
1113 C CD1 . LEU   A 164 ? 0.33647 0.18799 0.29338 0.02260  -0.05324 0.01857  144 LEU   A CD1 
1114 C CD2 . LEU   A 164 ? 0.33918 0.15798 0.27932 0.01688  -0.01117 -0.03243 144 LEU   A CD2 
1115 N N   . ILE   A 165 ? 0.29060 0.14325 0.19584 0.00879  -0.01191 -0.00052 145 ILE   A N   
1116 C CA  . ILE   A 165 ? 0.25919 0.15791 0.19175 0.00354  -0.01466 0.00998  145 ILE   A CA  
1117 C C   . ILE   A 165 ? 0.24138 0.13493 0.21872 -0.00490 0.01580  0.00663  145 ILE   A C   
1118 O O   . ILE   A 165 ? 0.25882 0.13727 0.26930 -0.00633 0.03003  -0.01282 145 ILE   A O   
1119 C CB  . ILE   A 165 ? 0.26866 0.17919 0.21225 0.01658  -0.01076 0.01103  145 ILE   A CB  
1120 C CG1 . ILE   A 165 ? 0.26383 0.18030 0.25359 0.00034  -0.01127 0.02208  145 ILE   A CG1 
1121 C CG2 . ILE   A 165 ? 0.29020 0.17085 0.22516 0.02397  0.01348  0.01953  145 ILE   A CG2 
1122 C CD1 . ILE   A 165 ? 0.29762 0.17907 0.28523 -0.00045 -0.04189 0.01260  145 ILE   A CD1 
1123 N N   . SER   A 166 ? 0.26338 0.14043 0.24817 0.00722  0.03734  0.00833  146 SER   A N   
1124 C CA  A SER   A 166 ? 0.27467 0.14807 0.21347 -0.00824 -0.00692 -0.00531 146 SER   A CA  
1125 C CA  B SER   A 166 ? 0.28473 0.13872 0.22443 -0.01262 0.02085  0.00062  146 SER   A CA  
1126 C C   . SER   A 166 ? 0.29800 0.11913 0.24093 -0.00601 0.01589  0.01306  146 SER   A C   
1127 O O   . SER   A 166 ? 0.32157 0.12111 0.23463 -0.00815 0.04246  0.01256  146 SER   A O   
1128 C CB  A SER   A 166 ? 0.27967 0.15487 0.25714 0.01424  0.00392  0.00703  146 SER   A CB  
1129 C CB  B SER   A 166 ? 0.30313 0.15429 0.21627 -0.02775 0.02407  -0.00245 146 SER   A CB  
1130 O OG  A SER   A 166 ? 0.25640 0.13792 0.28007 0.02340  0.02748  0.01016  146 SER   A OG  
1131 O OG  B SER   A 166 ? 0.31000 0.16281 0.20136 -0.05316 0.03261  -0.01535 146 SER   A OG  
1132 N N   . PRO   A 167 ? 0.27067 0.13276 0.24394 -0.01098 0.02939  -0.01042 147 PRO   A N   
1133 C CA  . PRO   A 167 ? 0.29499 0.14770 0.22587 -0.01061 0.01266  0.02306  147 PRO   A CA  
1134 C C   . PRO   A 167 ? 0.29322 0.15212 0.24580 -0.01194 0.02043  0.01982  147 PRO   A C   
1135 O O   . PRO   A 167 ? 0.29518 0.15454 0.26406 -0.00241 0.00701  0.00128  147 PRO   A O   
1136 C CB  . PRO   A 167 ? 0.30769 0.14787 0.23025 0.00553  0.03342  0.03611  147 PRO   A CB  
1137 C CG  . PRO   A 167 ? 0.30368 0.14706 0.21228 -0.00903 -0.00731 0.02702  147 PRO   A CG  
1138 C CD  . PRO   A 167 ? 0.28437 0.13028 0.24280 -0.01516 0.00303  0.00293  147 PRO   A CD  
1139 N N   . LEU   A 168 ? 0.27088 0.15240 0.24684 -0.02745 0.01630  0.02055  148 LEU   A N   
1140 C CA  . LEU   A 168 ? 0.28708 0.15189 0.26745 -0.01198 -0.01488 0.00729  148 LEU   A CA  
1141 C C   . LEU   A 168 ? 0.28845 0.17287 0.28469 0.00809  -0.03854 0.00968  148 LEU   A C   
1142 O O   . LEU   A 168 ? 0.30743 0.17978 0.27325 0.00683  -0.01636 0.00566  148 LEU   A O   
1143 C CB  . LEU   A 168 ? 0.27233 0.13718 0.28571 -0.02691 0.00886  0.00411  148 LEU   A CB  
1144 C CG  . LEU   A 168 ? 0.28948 0.16593 0.30701 -0.01283 0.03161  -0.03244 148 LEU   A CG  
1145 C CD1 . LEU   A 168 ? 0.25891 0.20896 0.29467 0.00537  0.03195  -0.01809 148 LEU   A CD1 
1146 C CD2 . LEU   A 168 ? 0.31769 0.17236 0.32367 -0.03560 0.02066  -0.03365 148 LEU   A CD2 
1147 N N   . VAL   A 169 ? 0.27505 0.15205 0.25811 0.01585  -0.03293 0.02406  149 VAL   A N   
1148 C CA  . VAL   A 169 ? 0.27686 0.18444 0.28290 0.02157  -0.02865 0.02628  149 VAL   A CA  
1149 C C   . VAL   A 169 ? 0.27754 0.22665 0.28496 0.02761  -0.01673 0.01977  149 VAL   A C   
1150 O O   . VAL   A 169 ? 0.27608 0.27754 0.29333 0.02811  -0.00974 0.01122  149 VAL   A O   
1151 C CB  . VAL   A 169 ? 0.25892 0.18005 0.27784 0.00700  -0.00648 0.03951  149 VAL   A CB  
1152 C CG1 . VAL   A 169 ? 0.24823 0.19904 0.28522 0.00511  -0.05264 0.01055  149 VAL   A CG1 
1153 C CG2 . VAL   A 169 ? 0.27727 0.19465 0.31855 -0.01975 -0.00101 0.02056  149 VAL   A CG2 
1154 N N   . LEU   A 170 ? 0.27561 0.21658 0.26509 0.02741  0.01051  0.03014  150 LEU   A N   
1155 C CA  . LEU   A 170 ? 0.28852 0.21873 0.27372 0.03510  0.02118  0.03543  150 LEU   A CA  
1156 C C   . LEU   A 170 ? 0.27664 0.22066 0.27332 0.02495  0.00207  0.03152  150 LEU   A C   
1157 O O   . LEU   A 170 ? 0.27747 0.23809 0.31271 -0.00733 0.02812  0.02989  150 LEU   A O   
1158 C CB  . LEU   A 170 ? 0.32719 0.23360 0.32323 0.05129  -0.00499 0.02572  150 LEU   A CB  
1159 C CG  . LEU   A 170 ? 0.35371 0.24631 0.43794 0.05160  -0.01507 0.00993  150 LEU   A CG  
1160 C CD1 . LEU   A 170 ? 0.34079 0.23269 0.50220 0.10093  -0.03402 0.01160  150 LEU   A CD1 
1161 C CD2 . LEU   A 170 ? 0.37419 0.27885 0.45983 0.04508  -0.00758 0.00370  150 LEU   A CD2 
1162 N N   . ALA   A 171 ? 0.29903 0.21643 0.29738 -0.01526 0.02134  0.03318  151 ALA   A N   
1163 C CA  . ALA   A 171 ? 0.33761 0.22388 0.31296 -0.02754 0.00636  0.03476  151 ALA   A CA  
1164 C C   . ALA   A 171 ? 0.33045 0.24077 0.32294 -0.02487 0.00148  0.03366  151 ALA   A C   
1165 O O   . ALA   A 171 ? 0.32191 0.27514 0.32927 -0.00292 0.02133  0.02593  151 ALA   A O   
1166 C CB  . ALA   A 171 ? 0.34419 0.20019 0.35892 -0.06777 0.02019  0.01861  151 ALA   A CB  
1167 N N   . ASN   A 172 ? 0.34835 0.26536 0.31546 -0.02685 -0.00867 -0.00367 152 ASN   A N   
1168 C CA  . ASN   A 172 ? 0.36319 0.29707 0.31627 -0.02998 0.00478  0.02045  152 ASN   A CA  
1169 C C   . ASN   A 172 ? 0.37501 0.31391 0.34800 -0.00685 -0.00348 0.00928  152 ASN   A C   
1170 O O   . ASN   A 172 ? 0.36997 0.31316 0.41330 -0.01896 0.00516  0.01655  152 ASN   A O   
1171 C CB  . ASN   A 172 ? 0.39061 0.29716 0.30340 -0.01830 0.01905  -0.00185 152 ASN   A CB  
1172 C CG  . ASN   A 172 ? 0.42836 0.32419 0.38052 -0.03333 0.01985  -0.00691 152 ASN   A CG  
1173 O OD1 . ASN   A 172 ? 0.44029 0.33177 0.42979 -0.02818 0.00253  0.00820  152 ASN   A OD1 
1174 N ND2 . ASN   A 172 ? 0.44020 0.32658 0.41020 -0.02342 0.05565  -0.03061 152 ASN   A ND2 
1175 N N   . PRO   A 173 ? 0.36105 0.32685 0.39080 0.02997  0.04378  -0.01570 153 PRO   A N   
1176 C CA  . PRO   A 173 ? 0.38637 0.34958 0.48011 0.01272  0.04057  -0.02271 153 PRO   A CA  
1177 C C   . PRO   A 173 ? 0.39560 0.38741 0.49674 -0.01183 0.06296  -0.01051 153 PRO   A C   
1178 O O   . PRO   A 173 ? 0.40547 0.42698 0.49176 -0.00058 0.02717  -0.02521 153 PRO   A O   
1179 C CB  . PRO   A 173 ? 0.38813 0.32914 0.52627 0.03879  0.01036  -0.04836 153 PRO   A CB  
1180 C CG  . PRO   A 173 ? 0.39513 0.33595 0.52896 0.03632  0.01849  -0.05477 153 PRO   A CG  
1181 C CD  . PRO   A 173 ? 0.37092 0.31660 0.44207 0.03561  0.05771  -0.04768 153 PRO   A CD  
1182 N N   . GLU   A 174 ? 0.39735 0.38494 0.50760 -0.01251 0.09454  -0.02187 154 GLU   A N   
1183 C CA  . GLU   A 174 ? 0.42641 0.39176 0.55382 0.00358  0.14044  -0.00144 154 GLU   A CA  
1184 C C   . GLU   A 174 ? 0.42971 0.38407 0.60094 -0.01541 0.12749  0.04027  154 GLU   A C   
1185 O O   . GLU   A 174 ? 0.44563 0.38848 0.61913 -0.01031 0.10658  0.03624  154 GLU   A O   
1186 C CB  . GLU   A 174 ? 0.45125 0.39957 0.65924 0.01824  0.18745  -0.00085 154 GLU   A CB  
1187 C CG  . GLU   A 174 ? 0.47358 0.40182 0.74454 0.02424  0.19164  -0.02611 154 GLU   A CG  
1188 C CD  . GLU   A 174 ? 0.51779 0.40724 0.79906 0.02570  0.16745  -0.01380 154 GLU   A CD  
1189 O OE1 . GLU   A 174 ? 0.52054 0.40205 0.82043 0.02428  0.11035  -0.02375 154 GLU   A OE1 
1190 O OE2 . GLU   A 174 ? 0.55076 0.41247 0.85125 0.02113  0.17180  0.01919  154 GLU   A OE2 
1191 N N   . SER   A 175 ? 0.44661 0.38753 0.62573 -0.00770 0.10230  0.02303  155 SER   A N   
1192 C CA  . SER   A 175 ? 0.42160 0.38825 0.61922 -0.04026 0.02867  0.01261  155 SER   A CA  
1193 C C   . SER   A 175 ? 0.42667 0.41424 0.63049 -0.06787 0.00927  0.01377  155 SER   A C   
1194 O O   . SER   A 175 ? 0.43523 0.41451 0.66370 -0.08107 0.01894  0.00438  155 SER   A O   
1195 C CB  . SER   A 175 ? 0.40161 0.36230 0.58515 -0.01309 0.01042  0.01178  155 SER   A CB  
1196 O OG  . SER   A 175 ? 0.39059 0.35350 0.53002 -0.03122 -0.01244 0.03967  155 SER   A OG  
1197 N N   . ALA   A 176 ? 0.42267 0.44178 0.58924 -0.07126 -0.01208 0.03759  156 ALA   A N   
1198 C CA  . ALA   A 176 ? 0.42522 0.46948 0.61218 -0.07664 -0.02211 0.03622  156 ALA   A CA  
1199 C C   . ALA   A 176 ? 0.43446 0.48785 0.60966 -0.09341 -0.02335 0.05662  156 ALA   A C   
1200 O O   . ALA   A 176 ? 0.42951 0.51484 0.66169 -0.08369 -0.03368 0.06816  156 ALA   A O   
1201 C CB  . ALA   A 176 ? 0.43240 0.47787 0.61503 -0.06939 -0.02117 0.03190  156 ALA   A CB  
1202 N N   . THR   A 177 ? 0.43137 0.50497 0.57723 -0.09020 0.01366  0.05622  157 THR   A N   
1203 C CA  . THR   A 177 ? 0.47425 0.54001 0.62301 -0.10277 0.03028  0.01099  157 THR   A CA  
1204 C C   . THR   A 177 ? 0.49766 0.54005 0.64701 -0.12564 0.02943  -0.01985 157 THR   A C   
1205 O O   . THR   A 177 ? 0.50502 0.55362 0.65154 -0.12284 0.02835  -0.07600 157 THR   A O   
1206 C CB  . THR   A 177 ? 0.49312 0.56603 0.63746 -0.09250 0.05718  -0.01152 157 THR   A CB  
1207 O OG1 . THR   A 177 ? 0.52048 0.57498 0.61836 -0.08894 0.04837  -0.01029 157 THR   A OG1 
1208 C CG2 . THR   A 177 ? 0.48220 0.57726 0.65988 -0.09453 0.08347  -0.02240 157 THR   A CG2 
1209 N N   . THR   A 178 ? 0.52476 0.52192 0.66089 -0.13530 0.03802  -0.00835 158 THR   A N   
1210 C CA  . THR   A 178 ? 0.54132 0.48427 0.66521 -0.14359 0.03365  -0.04003 158 THR   A CA  
1211 C C   . THR   A 178 ? 0.51902 0.45914 0.72133 -0.14537 -0.01278 -0.04227 158 THR   A C   
1212 O O   . THR   A 178 ? 0.51837 0.46024 0.77395 -0.16383 -0.01853 -0.02770 158 THR   A O   
1213 C CB  . THR   A 178 ? 0.57191 0.49028 0.63539 -0.15170 0.08911  -0.03617 158 THR   A CB  
1214 O OG1 . THR   A 178 ? 0.62026 0.49384 0.63104 -0.15596 0.12283  0.00414  158 THR   A OG1 
1215 C CG2 . THR   A 178 ? 0.56799 0.50168 0.60224 -0.14919 0.10537  -0.05066 158 THR   A CG2 
1216 N N   . PHE   A 179 ? 0.49981 0.42356 0.71872 -0.11760 -0.01916 -0.09184 159 PHE   A N   
1217 C CA  . PHE   A 179 ? 0.46336 0.41098 0.80221 -0.10108 -0.03903 -0.08271 159 PHE   A CA  
1218 C C   . PHE   A 179 ? 0.44966 0.41609 0.82667 -0.07860 -0.09100 -0.06337 159 PHE   A C   
1219 O O   . PHE   A 179 ? 0.46328 0.41083 0.86731 -0.06873 -0.08748 -0.03315 159 PHE   A O   
1220 C CB  . PHE   A 179 ? 0.38818 0.37700 0.84408 -0.11886 -0.01841 -0.08756 159 PHE   A CB  
1221 C CG  . PHE   A 179 ? 0.37692 0.35802 0.93007 -0.11783 0.04896  -0.08439 159 PHE   A CG  
1222 C CD1 . PHE   A 179 ? 0.38514 0.35447 0.97289 -0.11821 0.07800  -0.07397 159 PHE   A CD1 
1223 C CD2 . PHE   A 179 ? 0.37841 0.34997 0.95779 -0.11797 0.07451  -0.07774 159 PHE   A CD2 
1224 C CE1 . PHE   A 179 ? 0.38528 0.35534 0.99417 -0.11466 0.08011  -0.08050 159 PHE   A CE1 
1225 C CE2 . PHE   A 179 ? 0.39076 0.34359 0.99253 -0.10823 0.08286  -0.06943 159 PHE   A CE2 
1226 C CZ  . PHE   A 179 ? 0.38193 0.35140 1.00538 -0.09860 0.07972  -0.05597 159 PHE   A CZ  
1227 N N   . LYS   A 180 ? 0.43005 0.41999 0.80211 -0.03908 -0.09629 -0.06510 160 LYS   A N   
1228 C CA  . LYS   A 180 ? 0.44246 0.43005 0.77332 -0.02313 -0.06670 -0.07171 160 LYS   A CA  
1229 C C   . LYS   A 180 ? 0.42452 0.42586 0.73338 -0.00079 -0.02939 -0.08448 160 LYS   A C   
1230 O O   . LYS   A 180 ? 0.42967 0.41782 0.72510 0.03336  -0.03604 -0.09287 160 LYS   A O   
1231 C CB  . LYS   A 180 ? 0.46251 0.43998 0.78729 -0.04430 -0.06623 -0.09068 160 LYS   A CB  
1232 C CG  . LYS   A 180 ? 0.50274 0.46429 0.81601 -0.05158 -0.07143 -0.07477 160 LYS   A CG  
1233 C CD  . LYS   A 180 ? 0.53612 0.49093 0.85427 -0.05552 -0.08615 -0.05294 160 LYS   A CD  
1234 C CE  . LYS   A 180 ? 0.58232 0.51770 0.89529 -0.05333 -0.08589 -0.05766 160 LYS   A CE  
1235 N NZ  . LYS   A 180 ? 0.61173 0.53600 0.92666 -0.05007 -0.08916 -0.03153 160 LYS   A NZ  
1236 N N   . VAL   A 181 ? 0.43332 0.44902 0.72860 -0.02753 0.03049  -0.10131 161 VAL   A N   
1237 C CA  . VAL   A 181 ? 0.44330 0.46434 0.73038 -0.06042 0.10309  -0.12566 161 VAL   A CA  
1238 C C   . VAL   A 181 ? 0.43186 0.48205 0.72781 -0.09854 0.05189  -0.12743 161 VAL   A C   
1239 O O   . VAL   A 181 ? 0.43220 0.48949 0.76549 -0.11639 0.02040  -0.13534 161 VAL   A O   
1240 C CB  . VAL   A 181 ? 0.48308 0.48043 0.77482 -0.05882 0.15159  -0.11867 161 VAL   A CB  
1241 C CG1 . VAL   A 181 ? 0.49578 0.48923 0.79820 -0.06654 0.20385  -0.11118 161 VAL   A CG1 
1242 C CG2 . VAL   A 181 ? 0.48478 0.48480 0.77183 -0.02702 0.18796  -0.13132 161 VAL   A CG2 
1243 N N   . LEU   A 182 ? 0.40054 0.48734 0.66661 -0.08591 0.02640  -0.09703 162 LEU   A N   
1244 C CA  . LEU   A 182 ? 0.40673 0.48911 0.65500 -0.07841 -0.00786 -0.05465 162 LEU   A CA  
1245 C C   . LEU   A 182 ? 0.42012 0.48564 0.67203 -0.05061 -0.04023 -0.01948 162 LEU   A C   
1246 O O   . LEU   A 182 ? 0.39400 0.47415 0.65563 -0.06472 -0.08485 -0.03283 162 LEU   A O   
1247 C CB  . LEU   A 182 ? 0.39606 0.49468 0.63086 -0.08341 -0.01665 -0.05836 162 LEU   A CB  
1248 C CG  . LEU   A 182 ? 0.40747 0.50723 0.65148 -0.08037 -0.00899 -0.04037 162 LEU   A CG  
1249 C CD1 . LEU   A 182 ? 0.41125 0.50706 0.63766 -0.06170 -0.03112 -0.03809 162 LEU   A CD1 
1250 C CD2 . LEU   A 182 ? 0.44158 0.51410 0.68819 -0.07269 0.01048  -0.03648 162 LEU   A CD2 
1251 N N   . ALA   A 183 ? 0.45594 0.48645 0.72158 -0.01941 -0.04799 0.02656  163 ALA   A N   
1252 C CA  . ALA   A 183 ? 0.47088 0.50194 0.75047 0.02075  -0.02829 0.04948  163 ALA   A CA  
1253 C C   . ALA   A 183 ? 0.48997 0.52954 0.76665 0.04736  -0.04292 0.04533  163 ALA   A C   
1254 O O   . ALA   A 183 ? 0.49021 0.51937 0.77548 0.06555  -0.00633 0.07271  163 ALA   A O   
1255 C CB  . ALA   A 183 ? 0.48749 0.49687 0.77924 0.03155  -0.02925 0.06021  163 ALA   A CB  
1256 N N   . ALA   A 184 ? 0.51722 0.56330 0.80494 0.05352  -0.08459 0.00391  164 ALA   A N   
1257 C CA  . ALA   A 184 ? 0.51528 0.59814 0.81767 0.02150  -0.13553 -0.04087 164 ALA   A CA  
1258 C C   . ALA   A 184 ? 0.53983 0.63516 0.80301 -0.01292 -0.16726 -0.08388 164 ALA   A C   
1259 O O   . ALA   A 184 ? 0.55982 0.64822 0.85033 -0.01295 -0.15736 -0.09230 164 ALA   A O   
1260 C CB  . ALA   A 184 ? 0.51660 0.61309 0.84011 0.01959  -0.13306 -0.04427 164 ALA   A CB  
1261 N N   . LYS   A 185 ? 0.56458 0.64877 0.72950 -0.05137 -0.17691 -0.09256 165 LYS   A N   
1262 C CA  . LYS   A 185 ? 0.59344 0.67649 0.70626 -0.07322 -0.15215 -0.06432 165 LYS   A CA  
1263 C C   . LYS   A 185 ? 0.56639 0.64536 0.59818 -0.12279 -0.12191 -0.05483 165 LYS   A C   
1264 O O   . LYS   A 185 ? 0.56718 0.64834 0.57900 -0.14426 -0.12559 -0.07875 165 LYS   A O   
1265 C CB  . LYS   A 185 ? 0.65419 0.72222 0.77157 -0.04597 -0.15121 -0.06077 165 LYS   A CB  
1266 C CG  . LYS   A 185 ? 0.70671 0.75789 0.83409 -0.01491 -0.17115 -0.06859 165 LYS   A CG  
1267 C CD  . LYS   A 185 ? 0.74188 0.78246 0.85148 0.01128  -0.18337 -0.08638 165 LYS   A CD  
1268 C CE  . LYS   A 185 ? 0.76968 0.79696 0.88935 0.02641  -0.17574 -0.10354 165 LYS   A CE  
1269 N NZ  . LYS   A 185 ? 0.78925 0.80883 0.94149 0.03206  -0.16154 -0.10533 165 LYS   A NZ  
1270 N N   . VAL   A 186 ? 0.53127 0.60472 0.52677 -0.14352 -0.09238 -0.00216 166 VAL   A N   
1271 C CA  . VAL   A 186 ? 0.50658 0.56992 0.51124 -0.14981 -0.10154 0.03241  166 VAL   A CA  
1272 C C   . VAL   A 186 ? 0.49677 0.52961 0.50666 -0.11880 -0.08188 0.07274  166 VAL   A C   
1273 O O   . VAL   A 186 ? 0.50728 0.51921 0.52470 -0.12999 -0.10702 0.06964  166 VAL   A O   
1274 C CB  . VAL   A 186 ? 0.51157 0.58649 0.52942 -0.15290 -0.15737 0.02737  166 VAL   A CB  
1275 C CG1 . VAL   A 186 ? 0.51178 0.59474 0.57543 -0.14848 -0.17997 0.03471  166 VAL   A CG1 
1276 C CG2 . VAL   A 186 ? 0.51814 0.58928 0.57082 -0.15816 -0.17555 0.03897  166 VAL   A CG2 
1277 N N   . LEU   A 187 ? 0.48796 0.49808 0.47830 -0.07347 -0.01403 0.08895  167 LEU   A N   
1278 C CA  . LEU   A 187 ? 0.49087 0.48043 0.44176 -0.04357 0.01756  0.07844  167 LEU   A CA  
1279 C C   . LEU   A 187 ? 0.49108 0.46808 0.38985 -0.02313 0.03264  0.04814  167 LEU   A C   
1280 O O   . LEU   A 187 ? 0.50721 0.48031 0.37924 -0.02648 0.07145  0.04136  167 LEU   A O   
1281 C CB  . LEU   A 187 ? 0.49210 0.48865 0.49855 -0.04895 0.02795  0.09214  167 LEU   A CB  
1282 C CG  . LEU   A 187 ? 0.49522 0.50667 0.54929 -0.05927 0.03524  0.08708  167 LEU   A CG  
1283 C CD1 . LEU   A 187 ? 0.50856 0.51928 0.61066 -0.07820 0.03727  0.08860  167 LEU   A CD1 
1284 C CD2 . LEU   A 187 ? 0.48872 0.52301 0.56576 -0.04497 0.05942  0.06889  167 LEU   A CD2 
1285 N N   . ASN   A 188 ? 0.48977 0.45463 0.39759 0.00357  0.02111  0.00162  168 ASN   A N   
1286 C CA  . ASN   A 188 ? 0.49330 0.43611 0.41979 0.00130  -0.02855 -0.01551 168 ASN   A CA  
1287 C C   . ASN   A 188 ? 0.49410 0.41845 0.47088 -0.02643 -0.03219 -0.01305 168 ASN   A C   
1288 O O   . ASN   A 188 ? 0.50887 0.40599 0.59408 -0.04715 -0.06415 0.01780  168 ASN   A O   
1289 C CB  . ASN   A 188 ? 0.52537 0.46610 0.43212 0.03042  -0.06192 -0.03786 168 ASN   A CB  
1290 C CG  . ASN   A 188 ? 0.56486 0.48109 0.42800 0.04873  -0.05119 -0.05299 168 ASN   A CG  
1291 O OD1 . ASN   A 188 ? 0.60490 0.49105 0.42506 0.05940  -0.05684 -0.06306 168 ASN   A OD1 
1292 N ND2 . ASN   A 188 ? 0.57430 0.48470 0.44949 0.05750  -0.02092 -0.09278 168 ASN   A ND2 
1293 N N   . SER   A 189 ? 0.46702 0.37853 0.39591 -0.02564 0.00129  -0.01178 169 SER   A N   
1294 C CA  . SER   A 189 ? 0.45648 0.38668 0.41837 -0.04203 0.07873  -0.03961 169 SER   A CA  
1295 C C   . SER   A 189 ? 0.45273 0.37971 0.42807 -0.05816 0.06122  -0.04554 169 SER   A C   
1296 O O   . SER   A 189 ? 0.46734 0.39839 0.48958 -0.05821 0.05755  -0.03362 169 SER   A O   
1297 C CB  . SER   A 189 ? 0.45203 0.38597 0.42682 -0.00534 0.13837  -0.01399 169 SER   A CB  
1298 O OG  . SER   A 189 ? 0.47472 0.37394 0.51226 0.04228  0.11473  0.00418  169 SER   A OG  
1299 N N   . VAL   A 190 ? 0.44704 0.37693 0.39255 -0.08256 0.04266  -0.01697 170 VAL   A N   
1300 C CA  . VAL   A 190 ? 0.44939 0.36984 0.40354 -0.11850 0.02668  -0.06963 170 VAL   A CA  
1301 C C   . VAL   A 190 ? 0.42145 0.37824 0.39899 -0.10952 0.04296  -0.05201 170 VAL   A C   
1302 O O   . VAL   A 190 ? 0.43476 0.37890 0.39530 -0.12348 0.03128  -0.05136 170 VAL   A O   
1303 C CB  . VAL   A 190 ? 0.48681 0.36601 0.39758 -0.12820 0.01145  -0.11310 170 VAL   A CB  
1304 C CG1 . VAL   A 190 ? 0.51964 0.37869 0.45901 -0.11354 0.02373  -0.08604 170 VAL   A CG1 
1305 C CG2 . VAL   A 190 ? 0.49491 0.39338 0.39677 -0.12056 0.03151  -0.09179 170 VAL   A CG2 
1306 N N   . LEU   A 191 ? 0.37100 0.37916 0.41262 -0.10780 0.05275  -0.05447 171 LEU   A N   
1307 C CA  . LEU   A 191 ? 0.35888 0.41645 0.42999 -0.08172 0.05962  -0.04601 171 LEU   A CA  
1308 C C   . LEU   A 191 ? 0.39353 0.44373 0.51883 -0.07122 0.06960  -0.03022 171 LEU   A C   
1309 O O   . LEU   A 191 ? 0.36291 0.43720 0.52815 -0.08637 0.08675  -0.00996 171 LEU   A O   
1310 C CB  . LEU   A 191 ? 0.33091 0.42040 0.44199 -0.08275 0.04698  -0.04589 171 LEU   A CB  
1311 C CG  . LEU   A 191 ? 0.31621 0.41856 0.43988 -0.10679 0.03096  -0.02747 171 LEU   A CG  
1312 C CD1 . LEU   A 191 ? 0.31704 0.42450 0.44125 -0.07660 0.01169  -0.03413 171 LEU   A CD1 
1313 C CD2 . LEU   A 191 ? 0.31212 0.42516 0.41511 -0.12824 0.04968  -0.02961 171 LEU   A CD2 
1314 N N   . PRO   A 192 ? 0.45380 0.48468 0.60439 -0.05412 0.08551  -0.05016 172 PRO   A N   
1315 C CA  . PRO   A 192 ? 0.48566 0.49743 0.65983 -0.05200 0.10383  -0.05068 172 PRO   A CA  
1316 C C   . PRO   A 192 ? 0.51337 0.50282 0.69376 -0.04614 0.07478  -0.02345 172 PRO   A C   
1317 O O   . PRO   A 192 ? 0.54188 0.50567 0.73888 -0.03053 0.08999  -0.05036 172 PRO   A O   
1318 C CB  . PRO   A 192 ? 0.49290 0.49419 0.66491 -0.04291 0.12097  -0.06501 172 PRO   A CB  
1319 C CG  . PRO   A 192 ? 0.48241 0.49341 0.63926 -0.04638 0.13775  -0.05200 172 PRO   A CG  
1320 C CD  . PRO   A 192 ? 0.47162 0.48290 0.63580 -0.04592 0.10600  -0.04900 172 PRO   A CD  
1321 N N   . ASN   A 193 ? 0.55520 0.50152 0.67596 -0.04292 0.00364  0.01678  173 ASN   A N   
1322 C CA  . ASN   A 193 ? 0.58309 0.49633 0.64621 -0.06259 -0.03322 0.07498  173 ASN   A CA  
1323 C C   . ASN   A 193 ? 0.54102 0.47068 0.58134 -0.12372 -0.06750 0.08066  173 ASN   A C   
1324 O O   . ASN   A 193 ? 0.55479 0.47445 0.63062 -0.13921 -0.08066 0.09021  173 ASN   A O   
1325 C CB  . ASN   A 193 ? 0.62201 0.52104 0.69588 -0.05305 -0.01480 0.10496  173 ASN   A CB  
1326 C CG  . ASN   A 193 ? 0.64517 0.54624 0.73890 -0.02678 -0.02538 0.12411  173 ASN   A CG  
1327 O OD1 . ASN   A 193 ? 0.65841 0.56294 0.78458 -0.01940 -0.02040 0.13455  173 ASN   A OD1 
1328 N ND2 . ASN   A 193 ? 0.64522 0.54629 0.71949 -0.01715 -0.03709 0.14138  173 ASN   A ND2 
1329 N N   . LEU   A 194 ? 0.49325 0.43063 0.52686 -0.15904 -0.05239 0.08543  174 LEU   A N   
1330 C CA  . LEU   A 194 ? 0.45948 0.44806 0.49774 -0.16722 -0.05309 0.04991  174 LEU   A CA  
1331 C C   . LEU   A 194 ? 0.44210 0.45628 0.46118 -0.15066 -0.04528 0.02169  174 LEU   A C   
1332 O O   . LEU   A 194 ? 0.44702 0.45696 0.41330 -0.14906 -0.03495 0.02780  174 LEU   A O   
1333 C CB  . LEU   A 194 ? 0.44676 0.46355 0.55268 -0.16252 -0.04581 0.03562  174 LEU   A CB  
1334 C CG  . LEU   A 194 ? 0.46856 0.48724 0.58707 -0.15522 -0.04355 0.02422  174 LEU   A CG  
1335 C CD1 . LEU   A 194 ? 0.47190 0.49779 0.58909 -0.17644 -0.04195 0.02582  174 LEU   A CD1 
1336 C CD2 . LEU   A 194 ? 0.47164 0.49424 0.59944 -0.13013 -0.05921 0.00466  174 LEU   A CD2 
1337 N N   . SER   A 195 ? 0.43041 0.47974 0.47894 -0.14157 -0.01211 -0.00977 175 SER   A N   
1338 C CA  . SER   A 195 ? 0.44143 0.49473 0.51048 -0.13119 0.00840  -0.04589 175 SER   A CA  
1339 C C   . SER   A 195 ? 0.41776 0.50563 0.46948 -0.14498 0.04739  -0.05569 175 SER   A C   
1340 O O   . SER   A 195 ? 0.42110 0.52244 0.48079 -0.16345 0.08555  -0.04114 175 SER   A O   
1341 C CB  . SER   A 195 ? 0.48701 0.51157 0.57966 -0.10338 -0.03860 -0.06590 175 SER   A CB  
1342 O OG  . SER   A 195 ? 0.54189 0.53079 0.65254 -0.09798 -0.06773 -0.04639 175 SER   A OG  
1343 N N   . SER   A 196 ? 0.39902 0.48865 0.45019 -0.14619 0.05181  -0.07677 176 SER   A N   
1344 C CA  . SER   A 196 ? 0.42355 0.47439 0.53233 -0.13233 0.02986  -0.11143 176 SER   A CA  
1345 C C   . SER   A 196 ? 0.40269 0.44923 0.51312 -0.11477 0.04505  -0.10953 176 SER   A C   
1346 O O   . SER   A 196 ? 0.41149 0.44862 0.48236 -0.10900 0.04521  -0.06848 176 SER   A O   
1347 C CB  . SER   A 196 ? 0.48605 0.50622 0.61535 -0.10722 0.00288  -0.10872 176 SER   A CB  
1348 O OG  . SER   A 196 ? 0.58111 0.54748 0.67904 -0.08945 -0.01412 -0.11431 176 SER   A OG  
1349 N N   . GLY   A 197 ? 0.37346 0.42591 0.52815 -0.10173 0.04454  -0.11956 177 GLY   A N   
1350 C CA  . GLY   A 197 ? 0.34571 0.40699 0.49435 -0.07671 0.06468  -0.11435 177 GLY   A CA  
1351 C C   . GLY   A 197 ? 0.33436 0.37624 0.45084 -0.06338 0.03655  -0.08405 177 GLY   A C   
1352 O O   . GLY   A 197 ? 0.31175 0.36486 0.44549 -0.05164 0.07428  -0.08589 177 GLY   A O   
1353 N N   A PRO   A 198 ? 0.33763 0.36984 0.41967 -0.05984 0.03746  -0.06952 178 PRO   A N   
1354 N N   B PRO   A 198 ? 0.33763 0.36984 0.41967 -0.05984 0.03746  -0.06952 178 PRO   A N   
1355 C CA  A PRO   A 198 ? 0.32754 0.34850 0.39242 -0.05392 0.03038  -0.06050 178 PRO   A CA  
1356 C CA  B PRO   A 198 ? 0.32754 0.34850 0.39242 -0.05392 0.03038  -0.06050 178 PRO   A CA  
1357 C C   A PRO   A 198 ? 0.31833 0.30932 0.36761 -0.04532 0.04801  -0.06416 178 PRO   A C   
1358 C C   B PRO   A 198 ? 0.31833 0.30932 0.36761 -0.04532 0.04801  -0.06416 178 PRO   A C   
1359 O O   A PRO   A 198 ? 0.33833 0.32495 0.39818 -0.03730 0.06156  -0.08199 178 PRO   A O   
1360 O O   B PRO   A 198 ? 0.33833 0.32495 0.39818 -0.03730 0.06156  -0.08199 178 PRO   A O   
1361 C CB  A PRO   A 198 ? 0.33830 0.36944 0.40891 -0.05112 0.04653  -0.06240 178 PRO   A CB  
1362 C CB  B PRO   A 198 ? 0.33830 0.36944 0.40891 -0.05112 0.04653  -0.06240 178 PRO   A CB  
1363 C CG  A PRO   A 198 ? 0.33781 0.38506 0.42517 -0.06180 0.04230  -0.06096 178 PRO   A CG  
1364 C CG  B PRO   A 198 ? 0.33781 0.38506 0.42517 -0.06180 0.04230  -0.06096 178 PRO   A CG  
1365 C CD  A PRO   A 198 ? 0.33352 0.38312 0.41466 -0.06332 0.04154  -0.06098 178 PRO   A CD  
1366 C CD  B PRO   A 198 ? 0.33352 0.38312 0.41466 -0.06332 0.04154  -0.06098 178 PRO   A CD  
1367 N N   . ILE   A 199 ? 0.31307 0.27767 0.33205 -0.04434 0.04489  -0.05936 179 ILE   A N   
1368 C CA  . ILE   A 199 ? 0.29642 0.26040 0.30095 -0.04065 0.06391  -0.01306 179 ILE   A CA  
1369 C C   . ILE   A 199 ? 0.32143 0.24327 0.30670 0.00439  0.04590  0.00690  179 ILE   A C   
1370 O O   . ILE   A 199 ? 0.31477 0.24330 0.35006 0.00512  0.02070  0.01856  179 ILE   A O   
1371 C CB  . ILE   A 199 ? 0.31634 0.26512 0.34536 -0.03435 0.10292  0.02007  179 ILE   A CB  
1372 C CG1 . ILE   A 199 ? 0.33057 0.27412 0.40622 0.01216  0.13087  0.01647  179 ILE   A CG1 
1373 C CG2 . ILE   A 199 ? 0.33308 0.23681 0.43984 -0.03953 0.08236  0.03272  179 ILE   A CG2 
1374 C CD1 . ILE   A 199 ? 0.34609 0.26659 0.40252 0.00363  0.16583  0.01095  179 ILE   A CD1 
1375 N N   . ASP   A 200 ? 0.32372 0.23087 0.28344 0.00462  0.05315  0.00855  180 ASP   A N   
1376 C CA  . ASP   A 200 ? 0.32055 0.21702 0.29769 0.04433  0.04080  0.00378  180 ASP   A CA  
1377 C C   . ASP   A 200 ? 0.32603 0.20556 0.30777 0.02511  0.01889  0.02851  180 ASP   A C   
1378 O O   . ASP   A 200 ? 0.31453 0.21822 0.35749 0.00269  0.01337  0.06759  180 ASP   A O   
1379 C CB  . ASP   A 200 ? 0.37597 0.24356 0.33063 0.04322  0.06067  -0.02011 180 ASP   A CB  
1380 C CG  . ASP   A 200 ? 0.46361 0.28582 0.38235 0.03412  0.07265  -0.04378 180 ASP   A CG  
1381 O OD1 . ASP   A 200 ? 0.53154 0.32251 0.43411 0.04333  0.05020  -0.02604 180 ASP   A OD1 
1382 O OD2 . ASP   A 200 ? 0.50300 0.33902 0.45030 0.01560  0.01912  -0.02767 180 ASP   A OD2 
1383 N N   . SER   A 201 ? 0.32707 0.21935 0.31559 0.01997  -0.01799 0.00116  181 SER   A N   
1384 C CA  A SER   A 201 ? 0.35490 0.20876 0.32423 0.01323  -0.00687 -0.00100 181 SER   A CA  
1385 C CA  B SER   A 201 ? 0.33720 0.20919 0.28675 0.00820  -0.00665 0.00419  181 SER   A CA  
1386 C C   . SER   A 201 ? 0.35111 0.20149 0.25328 0.00446  0.01152  0.00895  181 SER   A C   
1387 O O   . SER   A 201 ? 0.36514 0.18955 0.25571 -0.01148 0.02697  0.01677  181 SER   A O   
1388 C CB  A SER   A 201 ? 0.37754 0.20619 0.31897 0.02060  0.00266  0.02206  181 SER   A CB  
1389 C CB  B SER   A 201 ? 0.33536 0.20335 0.27458 -0.00231 -0.00385 0.01045  181 SER   A CB  
1390 O OG  A SER   A 201 ? 0.39269 0.21446 0.29738 -0.00388 0.02673  0.06343  181 SER   A OG  
1391 O OG  B SER   A 201 ? 0.32732 0.20368 0.25963 -0.01207 0.00190  0.02190  181 SER   A OG  
1392 N N   . SER   A 202 ? 0.35123 0.20996 0.24375 0.00046  0.03794  0.02662  182 SER   A N   
1393 C CA  . SER   A 202 ? 0.37357 0.24620 0.26079 0.00939  0.04416  0.00526  182 SER   A CA  
1394 C C   . SER   A 202 ? 0.39203 0.22634 0.29173 0.00709  -0.00487 0.01571  182 SER   A C   
1395 O O   . SER   A 202 ? 0.44894 0.21581 0.32118 0.01092  -0.02608 0.00546  182 SER   A O   
1396 C CB  . SER   A 202 ? 0.36325 0.31670 0.32317 0.03346  0.05663  -0.00588 182 SER   A CB  
1397 O OG  . SER   A 202 ? 0.39962 0.34864 0.34705 0.03584  0.08578  0.02450  182 SER   A OG  
1398 N N   . VAL   A 203 ? 0.33978 0.22006 0.21603 0.00745  0.04765  0.03332  183 VAL   A N   
1399 C CA  . VAL   A 203 ? 0.32766 0.21336 0.23186 -0.00263 0.02668  0.02534  183 VAL   A CA  
1400 C C   . VAL   A 203 ? 0.28901 0.19676 0.24295 0.00811  0.03693  0.02441  183 VAL   A C   
1401 O O   . VAL   A 203 ? 0.29863 0.18447 0.25087 -0.00282 0.02936  -0.00682 183 VAL   A O   
1402 C CB  . VAL   A 203 ? 0.33263 0.24221 0.25922 0.00820  0.03845  0.02226  183 VAL   A CB  
1403 C CG1 . VAL   A 203 ? 0.33039 0.28817 0.29094 0.00076  0.07214  0.04782  183 VAL   A CG1 
1404 C CG2 . VAL   A 203 ? 0.34606 0.24382 0.26865 -0.01614 0.02643  0.02202  183 VAL   A CG2 
1405 N N   . LEU   A 204 ? 0.27163 0.17241 0.25591 0.03895  0.04080  0.02521  184 LEU   A N   
1406 C CA  . LEU   A 204 ? 0.28519 0.15172 0.25762 0.01079  0.06266  -0.00666 184 LEU   A CA  
1407 C C   . LEU   A 204 ? 0.30240 0.14750 0.26288 0.02219  0.02132  -0.01231 184 LEU   A C   
1408 O O   . LEU   A 204 ? 0.31303 0.16873 0.26339 0.00655  0.02246  -0.00923 184 LEU   A O   
1409 C CB  . LEU   A 204 ? 0.30739 0.14033 0.27141 -0.00085 0.02227  0.00236  184 LEU   A CB  
1410 C CG  . LEU   A 204 ? 0.31635 0.14936 0.25981 -0.03395 0.01579  0.01854  184 LEU   A CG  
1411 C CD1 . LEU   A 204 ? 0.32451 0.14089 0.29924 0.01045  -0.00161 0.01253  184 LEU   A CD1 
1412 C CD2 . LEU   A 204 ? 0.31919 0.17473 0.27151 -0.02538 -0.04231 0.00896  184 LEU   A CD2 
1413 N N   . SER   A 205 ? 0.33143 0.15782 0.23350 0.01416  -0.01098 -0.00285 185 SER   A N   
1414 C CA  . SER   A 205 ? 0.31418 0.15513 0.23251 0.01489  0.01613  -0.03523 185 SER   A CA  
1415 C C   . SER   A 205 ? 0.31460 0.14958 0.21489 0.01633  0.00339  -0.01379 185 SER   A C   
1416 O O   . SER   A 205 ? 0.32680 0.15901 0.24264 -0.00862 0.04918  0.02763  185 SER   A O   
1417 C CB  . SER   A 205 ? 0.28318 0.15725 0.28837 -0.00055 -0.00340 -0.00514 185 SER   A CB  
1418 O OG  . SER   A 205 ? 0.29280 0.17392 0.25953 -0.01858 -0.00893 0.00640  185 SER   A OG  
1419 N N   . ARG   A 206 ? 0.34033 0.16906 0.24549 0.02006  -0.03866 -0.02056 186 ARG   A N   
1420 C CA  . ARG   A 206 ? 0.35735 0.16147 0.24411 0.03162  -0.06079 -0.02334 186 ARG   A CA  
1421 C C   . ARG   A 206 ? 0.37782 0.17849 0.24841 0.02303  -0.02701 -0.01376 186 ARG   A C   
1422 O O   . ARG   A 206 ? 0.40616 0.19605 0.25674 0.02684  -0.01446 -0.01412 186 ARG   A O   
1423 C CB  . ARG   A 206 ? 0.37173 0.13379 0.26208 0.03810  -0.02605 -0.00917 186 ARG   A CB  
1424 C CG  . ARG   A 206 ? 0.37019 0.14539 0.27858 0.04020  -0.00822 0.02286  186 ARG   A CG  
1425 C CD  . ARG   A 206 ? 0.35499 0.15288 0.29082 0.01873  0.03018  -0.00880 186 ARG   A CD  
1426 N NE  . ARG   A 206 ? 0.33238 0.16725 0.27984 0.00524  0.00640  0.00762  186 ARG   A NE  
1427 C CZ  . ARG   A 206 ? 0.33976 0.17104 0.29952 0.01759  0.00945  -0.00756 186 ARG   A CZ  
1428 N NH1 . ARG   A 206 ? 0.31755 0.17443 0.33172 0.04491  -0.01789 -0.05405 186 ARG   A NH1 
1429 N NH2 . ARG   A 206 ? 0.34876 0.19540 0.28111 0.03014  -0.00182 -0.01465 186 ARG   A NH2 
1430 N N   . ASN   A 207 ? 0.36644 0.16155 0.24055 0.00083  -0.03591 -0.01029 187 ASN   A N   
1431 C CA  . ASN   A 207 ? 0.36717 0.16751 0.25366 0.00346  -0.01749 0.01692  187 ASN   A CA  
1432 C C   . ASN   A 207 ? 0.35407 0.17608 0.21874 -0.00401 0.00858  0.02602  187 ASN   A C   
1433 O O   . ASN   A 207 ? 0.36374 0.18347 0.23687 0.00525  -0.00860 0.00958  187 ASN   A O   
1434 C CB  . ASN   A 207 ? 0.36190 0.18914 0.26385 -0.00016 -0.00553 0.03615  187 ASN   A CB  
1435 C CG  . ASN   A 207 ? 0.37740 0.21748 0.31055 -0.01496 -0.02929 0.01990  187 ASN   A CG  
1436 O OD1 . ASN   A 207 ? 0.39282 0.22554 0.32209 0.00733  -0.01456 0.03738  187 ASN   A OD1 
1437 N ND2 . ASN   A 207 ? 0.36922 0.22153 0.31689 -0.01754 -0.01156 0.01025  187 ASN   A ND2 
1438 N N   . LYS   A 208 ? 0.36880 0.19187 0.22769 0.00967  0.01650  0.05292  188 LYS   A N   
1439 C CA  . LYS   A 208 ? 0.37211 0.20817 0.22011 0.02887  0.05701  0.00681  188 LYS   A CA  
1440 C C   . LYS   A 208 ? 0.36698 0.21258 0.23958 0.01025  0.00782  -0.00892 188 LYS   A C   
1441 O O   . LYS   A 208 ? 0.37252 0.18248 0.25420 0.01807  0.00603  -0.00772 188 LYS   A O   
1442 C CB  . LYS   A 208 ? 0.41630 0.24534 0.21445 0.05297  0.06898  -0.01065 188 LYS   A CB  
1443 C CG  . LYS   A 208 ? 0.46682 0.29233 0.26170 0.07663  0.10683  -0.03241 188 LYS   A CG  
1444 C CD  . LYS   A 208 ? 0.52415 0.33609 0.32201 0.09425  0.08557  -0.04800 188 LYS   A CD  
1445 C CE  . LYS   A 208 ? 0.57791 0.36856 0.35946 0.08881  0.08630  -0.06249 188 LYS   A CE  
1446 N NZ  . LYS   A 208 ? 0.61446 0.39266 0.38889 0.07683  0.08566  -0.03470 188 LYS   A NZ  
1447 N N   . THR   A 209 ? 0.37870 0.22803 0.20863 0.04295  0.00818  0.01638  189 THR   A N   
1448 C CA  . THR   A 209 ? 0.36198 0.22452 0.22888 0.05989  -0.00268 0.00266  189 THR   A CA  
1449 C C   . THR   A 209 ? 0.36246 0.20768 0.20273 0.04879  -0.01480 0.02006  189 THR   A C   
1450 O O   . THR   A 209 ? 0.34394 0.18551 0.26456 0.03550  -0.00599 0.00632  189 THR   A O   
1451 C CB  . THR   A 209 ? 0.40003 0.27429 0.27420 0.08272  -0.05193 -0.04645 189 THR   A CB  
1452 O OG1 . THR   A 209 ? 0.41940 0.34617 0.37930 0.08913  -0.07121 -0.09086 189 THR   A OG1 
1453 C CG2 . THR   A 209 ? 0.38937 0.26384 0.30944 0.07082  -0.04727 -0.00893 189 THR   A CG2 
1454 N N   . GLU   A 210 ? 0.37181 0.21007 0.21051 0.03471  -0.01334 0.04846  190 GLU   A N   
1455 C CA  . GLU   A 210 ? 0.34032 0.18358 0.21042 0.01050  -0.00643 0.02203  190 GLU   A CA  
1456 C C   . GLU   A 210 ? 0.35213 0.17722 0.22977 0.01281  0.04085  0.01622  190 GLU   A C   
1457 O O   . GLU   A 210 ? 0.37606 0.16362 0.22542 0.01070  0.01213  0.01913  190 GLU   A O   
1458 C CB  . GLU   A 210 ? 0.30228 0.19047 0.24242 0.00312  0.01984  0.04823  190 GLU   A CB  
1459 C CG  . GLU   A 210 ? 0.33870 0.23697 0.24084 0.00141  0.00157  0.02674  190 GLU   A CG  
1460 C CD  . GLU   A 210 ? 0.37666 0.30827 0.30688 -0.00355 -0.03891 0.01480  190 GLU   A CD  
1461 O OE1 . GLU   A 210 ? 0.41494 0.26934 0.25698 0.05119  0.01098  0.02310  190 GLU   A OE1 
1462 O OE2 . GLU   A 210 ? 0.40994 0.39410 0.43743 -0.02449 0.01251  -0.03381 190 GLU   A OE2 
1463 N N   . VAL   A 211 ? 0.33234 0.17328 0.23263 0.00577  -0.00989 0.04417  191 VAL   A N   
1464 C CA  . VAL   A 211 ? 0.33443 0.15468 0.26342 0.01635  -0.00243 0.03426  191 VAL   A CA  
1465 C C   . VAL   A 211 ? 0.35142 0.15344 0.25161 0.00434  0.00208  0.04752  191 VAL   A C   
1466 O O   . VAL   A 211 ? 0.33313 0.17231 0.25369 0.00853  -0.00910 0.03102  191 VAL   A O   
1467 C CB  . VAL   A 211 ? 0.33966 0.14242 0.30233 -0.00309 -0.00342 0.04234  191 VAL   A CB  
1468 C CG1 . VAL   A 211 ? 0.33298 0.16041 0.34531 0.00697  0.00713  0.02935  191 VAL   A CG1 
1469 C CG2 . VAL   A 211 ? 0.38285 0.15415 0.29507 0.01805  0.01172  0.04317  191 VAL   A CG2 
1470 N N   . ASP   A 212 ? 0.37028 0.16223 0.21535 0.03911  -0.02229 0.04563  192 ASP   A N   
1471 C CA  . ASP   A 212 ? 0.36265 0.17818 0.21931 0.04314  -0.01647 0.02331  192 ASP   A CA  
1472 C C   . ASP   A 212 ? 0.37022 0.16890 0.22932 0.01472  -0.02813 0.00364  192 ASP   A C   
1473 O O   . ASP   A 212 ? 0.37234 0.15752 0.26287 0.01491  0.00389  0.01105  192 ASP   A O   
1474 C CB  . ASP   A 212 ? 0.37737 0.23259 0.19189 0.04958  -0.00928 0.02013  192 ASP   A CB  
1475 C CG  . ASP   A 212 ? 0.41664 0.28769 0.23812 0.05872  -0.02461 0.00568  192 ASP   A CG  
1476 O OD1 . ASP   A 212 ? 0.45602 0.37076 0.29102 0.02435  -0.01656 -0.05094 192 ASP   A OD1 
1477 O OD2 . ASP   A 212 ? 0.47109 0.26533 0.22200 0.09250  0.01069  0.01521  192 ASP   A OD2 
1478 N N   . ILE   A 213 ? 0.36154 0.17580 0.21135 0.04089  -0.02173 -0.00160 193 ILE   A N   
1479 C CA  . ILE   A 213 ? 0.34104 0.17336 0.20206 0.02747  -0.01665 -0.00919 193 ILE   A CA  
1480 C C   . ILE   A 213 ? 0.36819 0.18152 0.23167 0.03270  -0.03181 -0.00377 193 ILE   A C   
1481 O O   . ILE   A 213 ? 0.39424 0.17815 0.26165 0.02345  -0.01522 -0.00207 193 ILE   A O   
1482 C CB  . ILE   A 213 ? 0.31675 0.21238 0.24226 0.00024  -0.01303 -0.01420 193 ILE   A CB  
1483 C CG1 . ILE   A 213 ? 0.30198 0.21921 0.25590 -0.01309 -0.03173 -0.01064 193 ILE   A CG1 
1484 C CG2 . ILE   A 213 ? 0.32030 0.21433 0.22607 0.02162  -0.01668 -0.00946 193 ILE   A CG2 
1485 C CD1 . ILE   A 213 ? 0.31392 0.22489 0.31784 -0.01511 -0.03443 0.01496  193 ILE   A CD1 
1486 N N   . TYR   A 214 ? 0.34948 0.19406 0.20002 0.00990  -0.01524 0.00854  194 TYR   A N   
1487 C CA  . TYR   A 214 ? 0.31948 0.17358 0.19482 -0.01023 -0.00945 0.05198  194 TYR   A CA  
1488 C C   . TYR   A 214 ? 0.34179 0.16802 0.22601 0.00245  0.01493  0.03858  194 TYR   A C   
1489 O O   . TYR   A 214 ? 0.39306 0.16001 0.24812 0.00932  0.02880  0.02692  194 TYR   A O   
1490 C CB  . TYR   A 214 ? 0.31815 0.18167 0.19357 0.00281  -0.03705 0.03194  194 TYR   A CB  
1491 C CG  . TYR   A 214 ? 0.34268 0.16274 0.23535 -0.02636 -0.03102 0.03544  194 TYR   A CG  
1492 C CD1 . TYR   A 214 ? 0.35323 0.16629 0.28138 -0.01714 -0.03742 0.03186  194 TYR   A CD1 
1493 C CD2 . TYR   A 214 ? 0.37836 0.17354 0.24682 -0.00536 -0.03583 0.03308  194 TYR   A CD2 
1494 C CE1 . TYR   A 214 ? 0.37971 0.16074 0.26539 0.00126  -0.01515 0.04267  194 TYR   A CE1 
1495 C CE2 . TYR   A 214 ? 0.38016 0.17545 0.27478 0.01599  -0.02038 0.04521  194 TYR   A CE2 
1496 C CZ  . TYR   A 214 ? 0.38365 0.16299 0.25312 0.00204  -0.03468 0.02025  194 TYR   A CZ  
1497 O OH  . TYR   A 214 ? 0.40059 0.18880 0.31916 -0.01270 -0.06131 0.00975  194 TYR   A OH  
1498 N N   . ASN   A 215 ? 0.35549 0.17690 0.20197 0.00641  0.01887  0.01732  195 ASN   A N   
1499 C CA  . ASN   A 215 ? 0.34596 0.17936 0.23696 0.00959  0.00319  0.02949  195 ASN   A CA  
1500 C C   . ASN   A 215 ? 0.35697 0.18356 0.24269 0.01140  -0.01427 0.02056  195 ASN   A C   
1501 O O   . ASN   A 215 ? 0.35124 0.18673 0.29724 0.00398  -0.01057 0.04517  195 ASN   A O   
1502 C CB  . ASN   A 215 ? 0.34370 0.20859 0.23470 -0.00059 0.02061  0.02872  195 ASN   A CB  
1503 C CG  . ASN   A 215 ? 0.36071 0.23355 0.25068 0.00097  0.02671  0.01959  195 ASN   A CG  
1504 O OD1 . ASN   A 215 ? 0.37414 0.25938 0.29876 0.01853  0.01811  0.03474  195 ASN   A OD1 
1505 N ND2 . ASN   A 215 ? 0.35510 0.22780 0.31308 -0.01034 0.02778  0.00113  195 ASN   A ND2 
1506 N N   . SER   A 216 ? 0.35420 0.17689 0.22320 0.03847  -0.00962 0.02151  196 SER   A N   
1507 C CA  . SER   A 216 ? 0.39477 0.19008 0.23426 0.05195  -0.01284 -0.00382 196 SER   A CA  
1508 C C   . SER   A 216 ? 0.41365 0.17896 0.20503 0.04775  -0.00229 0.00290  196 SER   A C   
1509 O O   . SER   A 216 ? 0.44991 0.18255 0.26297 0.07399  -0.01752 -0.00134 196 SER   A O   
1510 C CB  . SER   A 216 ? 0.37806 0.20626 0.24253 0.04308  -0.00884 -0.00738 196 SER   A CB  
1511 O OG  . SER   A 216 ? 0.38568 0.20929 0.23373 0.04281  -0.01646 0.00568  196 SER   A OG  
1512 N N   . ASP   A 217 ? 0.37189 0.19249 0.18753 0.03426  -0.00386 0.00188  197 ASP   A N   
1513 C CA  . ASP   A 217 ? 0.39945 0.20470 0.18485 0.00366  0.02623  -0.00383 197 ASP   A CA  
1514 C C   . ASP   A 217 ? 0.38694 0.20111 0.22549 0.02974  0.00986  0.02395  197 ASP   A C   
1515 O O   . ASP   A 217 ? 0.39658 0.21190 0.28552 0.03650  -0.00405 0.00827  197 ASP   A O   
1516 C CB  . ASP   A 217 ? 0.42159 0.21070 0.19324 0.02437  0.00287  0.01105  197 ASP   A CB  
1517 C CG  . ASP   A 217 ? 0.41983 0.20518 0.24822 0.03966  -0.00304 0.02091  197 ASP   A CG  
1518 O OD1 . ASP   A 217 ? 0.41814 0.22727 0.27880 0.04332  0.04776  -0.00601 197 ASP   A OD1 
1519 O OD2 . ASP   A 217 ? 0.39994 0.19561 0.26047 0.04320  0.02943  0.02255  197 ASP   A OD2 
1520 N N   . PRO   A 218 ? 0.41878 0.20391 0.24436 0.01661  -0.01296 0.00766  198 PRO   A N   
1521 C CA  . PRO   A 218 ? 0.44233 0.20587 0.24270 0.03263  -0.03989 0.02055  198 PRO   A CA  
1522 C C   . PRO   A 218 ? 0.46753 0.22833 0.22711 0.02694  0.00210  -0.00005 198 PRO   A C   
1523 O O   . PRO   A 218 ? 0.49151 0.26663 0.26411 -0.01994 0.01170  -0.00180 198 PRO   A O   
1524 C CB  . PRO   A 218 ? 0.42174 0.20932 0.33196 0.01899  -0.05953 0.03760  198 PRO   A CB  
1525 C CG  . PRO   A 218 ? 0.41572 0.22753 0.37999 0.02980  -0.09313 -0.03316 198 PRO   A CG  
1526 C CD  . PRO   A 218 ? 0.41254 0.21018 0.31853 0.03454  -0.05649 0.00044  198 PRO   A CD  
1527 N N   . LEU   A 219 ? 0.43632 0.22758 0.19091 0.06520  0.01436  -0.00290 199 LEU   A N   
1528 C CA  . LEU   A 219 ? 0.39332 0.21371 0.20248 0.07453  0.03503  0.02153  199 LEU   A CA  
1529 C C   . LEU   A 219 ? 0.40977 0.23225 0.26709 0.05536  0.01181  0.01080  199 LEU   A C   
1530 O O   . LEU   A 219 ? 0.44767 0.23587 0.28421 0.04400  0.00641  -0.01777 199 LEU   A O   
1531 C CB  . LEU   A 219 ? 0.38124 0.20864 0.23640 0.08309  0.03729  -0.00537 199 LEU   A CB  
1532 C CG  . LEU   A 219 ? 0.37639 0.22361 0.31695 0.04938  0.04550  -0.00279 199 LEU   A CG  
1533 C CD1 . LEU   A 219 ? 0.35445 0.24364 0.33544 0.02185  0.05222  0.01117  199 LEU   A CD1 
1534 C CD2 . LEU   A 219 ? 0.41133 0.22701 0.34297 0.04059  0.02423  -0.02516 199 LEU   A CD2 
1535 N N   . ILE   A 220 ? 0.35459 0.22709 0.29753 0.07625  -0.00030 0.01771  200 ILE   A N   
1536 C CA  . ILE   A 220 ? 0.33137 0.22915 0.27608 0.04597  0.00248  0.02064  200 ILE   A CA  
1537 C C   . ILE   A 220 ? 0.35617 0.21868 0.29156 0.01248  -0.02504 0.01154  200 ILE   A C   
1538 O O   . ILE   A 220 ? 0.37347 0.25476 0.30773 0.03213  -0.03215 0.00715  200 ILE   A O   
1539 C CB  . ILE   A 220 ? 0.31144 0.22095 0.25178 0.04689  -0.00448 0.00314  200 ILE   A CB  
1540 C CG1 . ILE   A 220 ? 0.30619 0.21002 0.23135 0.03290  0.02942  -0.03323 200 ILE   A CG1 
1541 C CG2 . ILE   A 220 ? 0.30026 0.23373 0.28454 0.05379  -0.02332 0.00365  200 ILE   A CG2 
1542 C CD1 . ILE   A 220 ? 0.32099 0.21862 0.28305 0.04769  0.04875  0.00298  200 ILE   A CD1 
1543 N N   . CYS   A 221 ? 0.37881 0.21900 0.28584 -0.00035 -0.03827 0.00657  201 CYS   A N   
1544 C CA  . CYS   A 221 ? 0.38717 0.25036 0.30772 -0.02619 -0.03142 -0.02356 201 CYS   A CA  
1545 C C   . CYS   A 221 ? 0.39833 0.23911 0.32487 -0.00203 0.01318  -0.01007 201 CYS   A C   
1546 O O   . CYS   A 221 ? 0.39885 0.23727 0.39999 -0.03205 0.02508  0.03331  201 CYS   A O   
1547 C CB  . CYS   A 221 ? 0.40826 0.27702 0.39088 -0.05648 -0.05751 -0.02252 201 CYS   A CB  
1548 S SG  . CYS   A 221 ? 0.42992 0.29776 0.41160 -0.07444 -0.03740 -0.00088 201 CYS   A SG  
1549 N N   . ARG   A 222 ? 0.38159 0.24561 0.32318 -0.00815 0.02485  -0.02659 202 ARG   A N   
1550 C CA  . ARG   A 222 ? 0.39444 0.25666 0.37528 -0.01986 -0.00208 -0.03701 202 ARG   A CA  
1551 C C   . ARG   A 222 ? 0.40347 0.27322 0.36416 -0.03463 0.03296  -0.03094 202 ARG   A C   
1552 O O   . ARG   A 222 ? 0.43468 0.32331 0.35472 -0.03249 0.06139  -0.00616 202 ARG   A O   
1553 C CB  . ARG   A 222 ? 0.41202 0.25366 0.36464 -0.03747 -0.02210 -0.05005 202 ARG   A CB  
1554 C CG  . ARG   A 222 ? 0.40063 0.24300 0.34501 -0.02961 -0.06661 -0.01462 202 ARG   A CG  
1555 C CD  . ARG   A 222 ? 0.44757 0.23769 0.36169 0.00217  -0.08814 0.00011  202 ARG   A CD  
1556 N NE  . ARG   A 222 ? 0.46553 0.22629 0.39414 0.03339  -0.09673 0.02162  202 ARG   A NE  
1557 C CZ  . ARG   A 222 ? 0.53651 0.24790 0.45462 0.01684  -0.11721 0.00896  202 ARG   A CZ  
1558 N NH1 . ARG   A 222 ? 0.56204 0.23133 0.41132 0.00278  -0.08522 0.00141  202 ARG   A NH1 
1559 N NH2 . ARG   A 222 ? 0.56297 0.25323 0.52970 0.02679  -0.14503 0.01614  202 ARG   A NH2 
1560 N N   . ALA   A 223 ? 0.40368 0.27275 0.37080 -0.07353 -0.05188 -0.00911 203 ALA   A N   
1561 C CA  . ALA   A 223 ? 0.39040 0.29144 0.42497 -0.06400 -0.04816 0.00372  203 ALA   A CA  
1562 C C   . ALA   A 223 ? 0.36387 0.29486 0.41210 -0.05088 -0.02102 0.00442  203 ALA   A C   
1563 O O   . ALA   A 223 ? 0.37009 0.29257 0.41907 -0.03177 0.00030  -0.02255 203 ALA   A O   
1564 C CB  . ALA   A 223 ? 0.41698 0.28916 0.46607 -0.05002 -0.06784 -0.00261 203 ALA   A CB  
1565 N N   . GLY   A 224 ? 0.35280 0.30275 0.37628 -0.05566 0.00874  0.03484  204 GLY   A N   
1566 C CA  . GLY   A 224 ? 0.40051 0.31400 0.35387 -0.03576 -0.00825 0.03513  204 GLY   A CA  
1567 C C   . GLY   A 224 ? 0.41192 0.29988 0.37853 -0.04578 -0.02207 0.02862  204 GLY   A C   
1568 O O   . GLY   A 224 ? 0.42703 0.31930 0.43009 -0.03053 -0.03438 0.01791  204 GLY   A O   
1569 N N   . LEU   A 225 ? 0.39638 0.29536 0.34816 -0.06970 -0.01880 0.04486  205 LEU   A N   
1570 C CA  . LEU   A 225 ? 0.37499 0.29817 0.36895 -0.06486 -0.01536 0.05114  205 LEU   A CA  
1571 C C   . LEU   A 225 ? 0.36917 0.31589 0.36120 -0.07573 -0.00373 0.01874  205 LEU   A C   
1572 O O   . LEU   A 225 ? 0.38220 0.35741 0.37973 -0.05939 -0.03867 -0.04825 205 LEU   A O   
1573 C CB  . LEU   A 225 ? 0.39536 0.30412 0.47954 -0.04805 0.01715  0.09953  205 LEU   A CB  
1574 C CG  . LEU   A 225 ? 0.44101 0.33689 0.60399 -0.02535 0.00854  0.12045  205 LEU   A CG  
1575 C CD1 . LEU   A 225 ? 0.44696 0.35840 0.66692 -0.02538 0.00688  0.12302  205 LEU   A CD1 
1576 C CD2 . LEU   A 225 ? 0.46322 0.32771 0.60554 -0.01307 -0.00096 0.15299  205 LEU   A CD2 
1577 N N   . LYS   A 226 ? 0.37655 0.30198 0.34069 -0.08673 -0.00319 0.03565  206 LYS   A N   
1578 C CA  . LYS   A 226 ? 0.39232 0.30657 0.36334 -0.06510 -0.02626 0.01150  206 LYS   A CA  
1579 C C   . LYS   A 226 ? 0.37521 0.28776 0.35682 -0.07149 -0.01335 0.00342  206 LYS   A C   
1580 O O   . LYS   A 226 ? 0.35107 0.26581 0.33039 -0.07946 0.01163  0.01320  206 LYS   A O   
1581 C CB  . LYS   A 226 ? 0.45379 0.33087 0.44441 -0.03164 -0.05014 0.01742  206 LYS   A CB  
1582 C CG  . LYS   A 226 ? 0.52088 0.39377 0.52269 -0.01859 -0.09643 0.04931  206 LYS   A CG  
1583 C CD  . LYS   A 226 ? 0.56891 0.43847 0.63385 0.00283  -0.13958 0.07842  206 LYS   A CD  
1584 C CE  . LYS   A 226 ? 0.59728 0.46214 0.71066 0.01737  -0.17693 0.10487  206 LYS   A CE  
1585 N NZ  . LYS   A 226 ? 0.64750 0.48731 0.78239 0.01390  -0.13604 0.09561  206 LYS   A NZ  
1586 N N   . VAL   A 227 ? 0.37873 0.30371 0.34563 -0.05856 -0.02938 0.00860  207 VAL   A N   
1587 C CA  . VAL   A 227 ? 0.33510 0.31800 0.36242 -0.06838 -0.03621 0.00240  207 VAL   A CA  
1588 C C   . VAL   A 227 ? 0.31883 0.30418 0.38569 -0.07555 -0.02492 -0.00054 207 VAL   A C   
1589 O O   . VAL   A 227 ? 0.29698 0.31208 0.39073 -0.07273 -0.01533 0.01758  207 VAL   A O   
1590 C CB  . VAL   A 227 ? 0.33889 0.35611 0.36532 -0.05516 -0.00726 0.02896  207 VAL   A CB  
1591 C CG1 . VAL   A 227 ? 0.34338 0.36000 0.35789 -0.05225 -0.01196 0.03480  207 VAL   A CG1 
1592 C CG2 . VAL   A 227 ? 0.34829 0.36852 0.38029 -0.04416 0.02441  0.02120  207 VAL   A CG2 
1593 N N   . CYS   A 228 ? 0.35187 0.28849 0.36151 -0.07643 -0.02142 -0.03222 208 CYS   A N   
1594 C CA  A CYS   A 228 ? 0.38284 0.26874 0.39602 -0.07021 -0.00400 -0.04251 208 CYS   A CA  
1595 C CA  B CYS   A 228 ? 0.37020 0.28276 0.40634 -0.08406 -0.01205 -0.02991 208 CYS   A CA  
1596 C C   . CYS   A 228 ? 0.36142 0.26653 0.39819 -0.06967 -0.01701 -0.02498 208 CYS   A C   
1597 O O   . CYS   A 228 ? 0.36875 0.28246 0.41981 -0.05626 -0.01972 -0.02366 208 CYS   A O   
1598 C CB  A CYS   A 228 ? 0.43360 0.27318 0.44867 -0.05276 -0.00321 -0.04251 208 CYS   A CB  
1599 C CB  B CYS   A 228 ? 0.39031 0.30200 0.46059 -0.10528 -0.03109 -0.03151 208 CYS   A CB  
1600 S SG  A CYS   A 228 ? 0.48921 0.28957 0.50173 -0.04484 0.02080  -0.03702 208 CYS   A SG  
1601 S SG  B CYS   A 228 ? 0.41497 0.32112 0.53563 -0.13910 -0.00486 -0.05517 208 CYS   A SG  
1602 N N   . PHE   A 229 ? 0.35211 0.22287 0.34696 -0.05857 -0.02847 -0.03552 209 PHE   A N   
1603 C CA  . PHE   A 229 ? 0.31336 0.21299 0.36103 -0.03390 -0.02541 -0.00170 209 PHE   A CA  
1604 C C   . PHE   A 229 ? 0.31282 0.22714 0.36178 -0.03363 -0.03505 -0.00989 209 PHE   A C   
1605 O O   . PHE   A 229 ? 0.31967 0.23862 0.36005 -0.03753 -0.04305 0.01317  209 PHE   A O   
1606 C CB  . PHE   A 229 ? 0.29456 0.22739 0.39418 -0.03416 -0.01122 0.01282  209 PHE   A CB  
1607 C CG  . PHE   A 229 ? 0.28145 0.24123 0.41495 -0.03021 -0.03558 0.04444  209 PHE   A CG  
1608 C CD1 . PHE   A 229 ? 0.27549 0.26547 0.44571 -0.04571 0.00578  0.05787  209 PHE   A CD1 
1609 C CD2 . PHE   A 229 ? 0.28711 0.25661 0.43705 -0.05488 -0.06336 0.05318  209 PHE   A CD2 
1610 C CE1 . PHE   A 229 ? 0.30273 0.27411 0.51948 -0.04412 0.00961  0.03778  209 PHE   A CE1 
1611 C CE2 . PHE   A 229 ? 0.29706 0.25657 0.49319 -0.05095 -0.05162 0.05840  209 PHE   A CE2 
1612 C CZ  . PHE   A 229 ? 0.30721 0.25498 0.51187 -0.03376 -0.02253 0.06347  209 PHE   A CZ  
1613 N N   . GLY   A 230 ? 0.28750 0.22879 0.35389 -0.01518 -0.00855 -0.00293 210 GLY   A N   
1614 C CA  . GLY   A 230 ? 0.27714 0.23319 0.35221 -0.01658 0.04008  -0.01220 210 GLY   A CA  
1615 C C   . GLY   A 230 ? 0.25589 0.23527 0.33289 -0.02593 0.00143  0.00585  210 GLY   A C   
1616 O O   . GLY   A 230 ? 0.26023 0.22227 0.39015 -0.03309 -0.00939 0.00527  210 GLY   A O   
1617 N N   . ILE   A 231 ? 0.26822 0.27354 0.35776 -0.03336 -0.01781 -0.01653 211 ILE   A N   
1618 C CA  . ILE   A 231 ? 0.25969 0.28178 0.38368 -0.04283 -0.03921 -0.01773 211 ILE   A CA  
1619 C C   . ILE   A 231 ? 0.26855 0.25614 0.38260 -0.01935 -0.01804 -0.01872 211 ILE   A C   
1620 O O   . ILE   A 231 ? 0.27409 0.25756 0.39425 -0.03167 0.00367  0.01093  211 ILE   A O   
1621 C CB  . ILE   A 231 ? 0.27867 0.30316 0.38692 -0.05979 -0.05741 -0.00886 211 ILE   A CB  
1622 C CG1 . ILE   A 231 ? 0.27208 0.31756 0.47574 -0.05058 -0.05035 -0.03761 211 ILE   A CG1 
1623 C CG2 . ILE   A 231 ? 0.30940 0.32855 0.39268 -0.04196 -0.07316 -0.00706 211 ILE   A CG2 
1624 C CD1 . ILE   A 231 ? 0.27505 0.34145 0.53994 -0.06575 -0.07472 -0.03453 211 ILE   A CD1 
1625 N N   . GLN   A 232 ? 0.28679 0.22921 0.37160 -0.01485 -0.01381 -0.03451 212 GLN   A N   
1626 C CA  . GLN   A 232 ? 0.27621 0.20167 0.34025 -0.01328 -0.01434 -0.01393 212 GLN   A CA  
1627 C C   . GLN   A 232 ? 0.28904 0.19772 0.30436 -0.00951 -0.02452 -0.00231 212 GLN   A C   
1628 O O   . GLN   A 232 ? 0.29236 0.22074 0.29545 -0.00941 -0.01462 0.01391  212 GLN   A O   
1629 C CB  . GLN   A 232 ? 0.28837 0.20995 0.32350 0.01132  -0.02400 -0.04320 212 GLN   A CB  
1630 C CG  . GLN   A 232 ? 0.30351 0.23354 0.33160 -0.01722 -0.02673 -0.05111 212 GLN   A CG  
1631 C CD  . GLN   A 232 ? 0.32831 0.25614 0.38979 -0.02903 -0.03379 -0.07173 212 GLN   A CD  
1632 O OE1 . GLN   A 232 ? 0.31898 0.26366 0.42111 -0.02413 -0.03372 -0.08679 212 GLN   A OE1 
1633 N NE2 . GLN   A 232 ? 0.34032 0.28934 0.42671 -0.04017 -0.03627 -0.05823 212 GLN   A NE2 
1634 N N   . LEU   A 233 ? 0.28784 0.20235 0.34921 -0.01036 -0.04606 -0.04049 213 LEU   A N   
1635 C CA  . LEU   A 233 ? 0.25677 0.20325 0.30567 -0.00432 -0.05399 -0.01832 213 LEU   A CA  
1636 C C   . LEU   A 233 ? 0.26828 0.22000 0.33027 -0.00145 -0.01384 -0.02259 213 LEU   A C   
1637 O O   . LEU   A 233 ? 0.26442 0.22040 0.32383 -0.01295 -0.02961 -0.00126 213 LEU   A O   
1638 C CB  . LEU   A 233 ? 0.24561 0.21899 0.30123 -0.00432 -0.04409 -0.00181 213 LEU   A CB  
1639 C CG  . LEU   A 233 ? 0.22875 0.22782 0.28370 0.00848  -0.02022 0.01389  213 LEU   A CG  
1640 C CD1 . LEU   A 233 ? 0.24760 0.20928 0.26969 0.00784  -0.01641 -0.00006 213 LEU   A CD1 
1641 C CD2 . LEU   A 233 ? 0.24028 0.23756 0.36469 -0.02408 0.00418  0.02757  213 LEU   A CD2 
1642 N N   . LEU   A 234 ? 0.26512 0.23517 0.31809 0.00180  -0.03299 -0.00386 214 LEU   A N   
1643 C CA  . LEU   A 234 ? 0.28411 0.26429 0.29853 0.01733  -0.01229 0.00190  214 LEU   A CA  
1644 C C   . LEU   A 234 ? 0.28968 0.25156 0.31491 0.00910  -0.02160 0.01219  214 LEU   A C   
1645 O O   . LEU   A 234 ? 0.30688 0.23995 0.32939 0.01757  -0.02895 0.01696  214 LEU   A O   
1646 C CB  . LEU   A 234 ? 0.32845 0.30799 0.35249 0.01786  0.00405  0.02052  214 LEU   A CB  
1647 C CG  . LEU   A 234 ? 0.34784 0.34736 0.38134 0.03659  0.00484  0.02012  214 LEU   A CG  
1648 C CD1 . LEU   A 234 ? 0.35007 0.37612 0.42887 0.01467  0.04116  0.03419  214 LEU   A CD1 
1649 C CD2 . LEU   A 234 ? 0.37987 0.34652 0.35281 0.04813  -0.00073 0.00666  214 LEU   A CD2 
1650 N N   . ASN   A 235 ? 0.28630 0.24742 0.32984 0.01331  -0.04116 -0.01374 215 ASN   A N   
1651 C CA  . ASN   A 235 ? 0.32639 0.23566 0.31818 -0.00038 -0.01872 -0.02396 215 ASN   A CA  
1652 C C   . ASN   A 235 ? 0.34846 0.22499 0.31582 -0.00477 -0.02313 -0.00905 215 ASN   A C   
1653 O O   . ASN   A 235 ? 0.37087 0.23305 0.31970 0.01809  -0.04105 -0.00689 215 ASN   A O   
1654 C CB  . ASN   A 235 ? 0.35431 0.25511 0.31121 0.00152  -0.03154 -0.04750 215 ASN   A CB  
1655 C CG  . ASN   A 235 ? 0.37154 0.29131 0.36521 -0.02030 -0.05703 -0.04326 215 ASN   A CG  
1656 O OD1 . ASN   A 235 ? 0.35942 0.31876 0.41062 -0.02609 -0.06755 -0.05458 215 ASN   A OD1 
1657 N ND2 . ASN   A 235 ? 0.39085 0.29373 0.37748 -0.05171 -0.07600 -0.05798 215 ASN   A ND2 
1658 N N   . ALA   A 236 ? 0.33307 0.21206 0.32054 0.00685  0.01522  -0.01616 216 ALA   A N   
1659 C CA  . ALA   A 236 ? 0.30328 0.19670 0.31675 0.00926  -0.00910 0.00792  216 ALA   A CA  
1660 C C   . ALA   A 236 ? 0.30724 0.20157 0.30824 0.03710  0.00581  -0.02818 216 ALA   A C   
1661 O O   . ALA   A 236 ? 0.32754 0.22464 0.30967 0.03458  -0.01626 0.00936  216 ALA   A O   
1662 C CB  . ALA   A 236 ? 0.28947 0.20319 0.32766 0.01657  0.00505  0.02964  216 ALA   A CB  
1663 N N   . VAL   A 237 ? 0.31275 0.22176 0.29974 0.04380  0.01237  -0.01793 217 VAL   A N   
1664 C CA  . VAL   A 237 ? 0.31378 0.24150 0.26700 0.04706  0.01047  -0.01495 217 VAL   A CA  
1665 C C   . VAL   A 237 ? 0.33367 0.25544 0.28832 0.02966  -0.00140 -0.00679 217 VAL   A C   
1666 O O   . VAL   A 237 ? 0.34449 0.24367 0.29779 0.01747  -0.00503 0.02182  217 VAL   A O   
1667 C CB  . VAL   A 237 ? 0.31928 0.23031 0.25748 0.06314  -0.02857 -0.00639 217 VAL   A CB  
1668 C CG1 . VAL   A 237 ? 0.33005 0.22151 0.29918 0.04908  -0.03041 0.02454  217 VAL   A CG1 
1669 C CG2 . VAL   A 237 ? 0.31585 0.23906 0.29256 0.05135  -0.04191 -0.01078 217 VAL   A CG2 
1670 N N   . SER   A 238 ? 0.33734 0.28315 0.27440 0.01377  -0.06133 0.00014  218 SER   A N   
1671 C CA  A SER   A 238 ? 0.36306 0.30885 0.29540 0.01337  -0.05243 0.00264  218 SER   A CA  
1672 C CA  B SER   A 238 ? 0.36678 0.30808 0.29698 0.01249  -0.05132 0.00484  218 SER   A CA  
1673 C C   . SER   A 238 ? 0.37276 0.29455 0.30197 0.02333  -0.02593 0.00085  218 SER   A C   
1674 O O   . SER   A 238 ? 0.36224 0.30722 0.30902 0.03117  -0.01740 0.01984  218 SER   A O   
1675 C CB  A SER   A 238 ? 0.37141 0.34786 0.31733 0.01508  -0.07045 0.00233  218 SER   A CB  
1676 C CB  B SER   A 238 ? 0.38157 0.34479 0.32260 0.01461  -0.07039 0.01593  218 SER   A CB  
1677 O OG  A SER   A 238 ? 0.38294 0.37592 0.36150 0.01979  -0.08249 -0.01568 218 SER   A OG  
1678 O OG  B SER   A 238 ? 0.40067 0.36664 0.37285 0.01862  -0.07411 -0.00177 218 SER   A OG  
1679 N N   . ARG   A 239 ? 0.34925 0.25640 0.28240 0.02786  -0.01286 -0.01621 219 ARG   A N   
1680 C CA  . ARG   A 239 ? 0.35818 0.22017 0.28211 0.01068  -0.03386 -0.02366 219 ARG   A CA  
1681 C C   . ARG   A 239 ? 0.33913 0.22494 0.28932 0.00460  -0.05177 -0.02844 219 ARG   A C   
1682 O O   . ARG   A 239 ? 0.33067 0.22645 0.27471 0.02708  -0.05012 -0.01583 219 ARG   A O   
1683 C CB  . ARG   A 239 ? 0.40855 0.19842 0.34934 -0.00927 -0.01842 -0.02731 219 ARG   A CB  
1684 C CG  . ARG   A 239 ? 0.45834 0.19920 0.38495 -0.01889 -0.03405 -0.02656 219 ARG   A CG  
1685 C CD  . ARG   A 239 ? 0.49478 0.19755 0.42378 -0.02777 -0.03975 -0.03058 219 ARG   A CD  
1686 N NE  . ARG   A 239 ? 0.53688 0.23979 0.46183 -0.04467 -0.10108 -0.03389 219 ARG   A NE  
1687 C CZ  . ARG   A 239 ? 0.57106 0.26285 0.46773 -0.03878 -0.11101 -0.03450 219 ARG   A CZ  
1688 N NH1 . ARG   A 239 ? 0.57989 0.27242 0.47476 -0.03301 -0.16535 -0.01455 219 ARG   A NH1 
1689 N NH2 . ARG   A 239 ? 0.56827 0.27779 0.46311 -0.04492 -0.07783 -0.03238 219 ARG   A NH2 
1690 N N   . VAL   A 240 ? 0.33648 0.23485 0.28764 0.01444  -0.05926 -0.00854 220 VAL   A N   
1691 C CA  . VAL   A 240 ? 0.32855 0.20427 0.26769 0.01528  -0.07367 -0.00422 220 VAL   A CA  
1692 C C   . VAL   A 240 ? 0.31383 0.23792 0.30164 0.03898  -0.06960 -0.02784 220 VAL   A C   
1693 O O   . VAL   A 240 ? 0.30852 0.23156 0.32091 0.01490  -0.05229 -0.01018 220 VAL   A O   
1694 C CB  . VAL   A 240 ? 0.31633 0.20473 0.25939 0.02334  -0.05248 -0.01380 220 VAL   A CB  
1695 C CG1 . VAL   A 240 ? 0.34824 0.23481 0.28399 0.00042  -0.02918 -0.03356 220 VAL   A CG1 
1696 C CG2 . VAL   A 240 ? 0.31006 0.22932 0.29085 0.04413  -0.02554 0.00395  220 VAL   A CG2 
1697 N N   . GLU   A 241 ? 0.34443 0.26279 0.29482 0.06989  -0.09292 -0.00555 221 GLU   A N   
1698 C CA  . GLU   A 241 ? 0.39487 0.27741 0.37125 0.09029  -0.09456 0.02071  221 GLU   A CA  
1699 C C   . GLU   A 241 ? 0.41203 0.26243 0.35075 0.07192  -0.11085 0.02064  221 GLU   A C   
1700 O O   . GLU   A 241 ? 0.42373 0.26582 0.37410 0.05971  -0.06974 0.02179  221 GLU   A O   
1701 C CB  . GLU   A 241 ? 0.44132 0.32519 0.46987 0.12095  -0.09442 0.09584  221 GLU   A CB  
1702 C CG  . GLU   A 241 ? 0.49726 0.37814 0.62819 0.12598  -0.09777 0.14937  221 GLU   A CG  
1703 C CD  . GLU   A 241 ? 0.58676 0.45817 0.78980 0.10697  -0.07794 0.18265  221 GLU   A CD  
1704 O OE1 . GLU   A 241 ? 0.60693 0.47810 0.84361 0.10508  -0.03792 0.17222  221 GLU   A OE1 
1705 O OE2 . GLU   A 241 ? 0.63267 0.50308 0.89654 0.09341  -0.07603 0.16089  221 GLU   A OE2 
1706 N N   . ARG   A 242 ? 0.44005 0.27110 0.30886 0.02366  -0.10828 -0.00587 222 ARG   A N   
1707 C CA  . ARG   A 242 ? 0.46307 0.30269 0.30111 -0.03302 -0.11720 -0.00550 222 ARG   A CA  
1708 C C   . ARG   A 242 ? 0.48316 0.28849 0.27940 -0.06493 -0.08547 0.01417  222 ARG   A C   
1709 O O   . ARG   A 242 ? 0.52619 0.33728 0.30823 -0.08080 -0.07993 0.02511  222 ARG   A O   
1710 C CB  . ARG   A 242 ? 0.50800 0.37511 0.39746 -0.06997 -0.13545 -0.01206 222 ARG   A CB  
1711 C CG  . ARG   A 242 ? 0.56413 0.43636 0.58069 -0.11676 -0.12767 -0.02996 222 ARG   A CG  
1712 C CD  . ARG   A 242 ? 0.62642 0.49562 0.74894 -0.13463 -0.10862 -0.00439 222 ARG   A CD  
1713 N NE  . ARG   A 242 ? 0.65764 0.57053 0.88376 -0.14860 -0.08129 0.01484  222 ARG   A NE  
1714 C CZ  . ARG   A 242 ? 0.67084 0.62534 0.95625 -0.14638 -0.07281 0.02100  222 ARG   A CZ  
1715 N NH1 . ARG   A 242 ? 0.69224 0.64273 1.02648 -0.14241 -0.05694 0.02131  222 ARG   A NH1 
1716 N NH2 . ARG   A 242 ? 0.65409 0.63153 0.95729 -0.14342 -0.09883 0.02836  222 ARG   A NH2 
1717 N N   . ALA   A 243 ? 0.44888 0.23590 0.28283 -0.05144 -0.04761 -0.01562 223 ALA   A N   
1718 C CA  . ALA   A 243 ? 0.44423 0.22804 0.27800 -0.04325 -0.01047 0.01106  223 ALA   A CA  
1719 C C   . ALA   A 243 ? 0.45498 0.22542 0.34207 -0.03110 -0.02871 0.03187  223 ALA   A C   
1720 O O   . ALA   A 243 ? 0.44796 0.23824 0.41006 -0.02529 -0.04277 0.03936  223 ALA   A O   
1721 C CB  . ALA   A 243 ? 0.42549 0.24647 0.28355 -0.00845 -0.02039 0.01752  223 ALA   A CB  
1722 N N   . LEU   A 244 ? 0.46129 0.20580 0.37687 -0.04621 -0.08298 0.01741  224 LEU   A N   
1723 C CA  . LEU   A 244 ? 0.49015 0.24380 0.45043 -0.05134 -0.08103 0.01412  224 LEU   A CA  
1724 C C   . LEU   A 244 ? 0.51477 0.26171 0.52968 -0.04212 -0.10679 0.05876  224 LEU   A C   
1725 O O   . LEU   A 244 ? 0.47974 0.24992 0.52024 -0.03194 -0.08675 0.04097  224 LEU   A O   
1726 C CB  . LEU   A 244 ? 0.49007 0.25654 0.50889 -0.03234 -0.05579 -0.01443 224 LEU   A CB  
1727 C CG  . LEU   A 244 ? 0.49214 0.24628 0.52125 -0.04060 -0.06198 -0.02128 224 LEU   A CG  
1728 C CD1 . LEU   A 244 ? 0.50572 0.23872 0.48308 -0.04991 -0.03366 -0.05545 224 LEU   A CD1 
1729 C CD2 . LEU   A 244 ? 0.48607 0.25861 0.52287 -0.04544 -0.05163 -0.02767 224 LEU   A CD2 
1730 N N   . PRO   A 245 ? 0.56693 0.33052 0.56854 -0.05035 -0.16026 0.12841  225 PRO   A N   
1731 C CA  . PRO   A 245 ? 0.61393 0.39709 0.55484 -0.08079 -0.13673 0.13393  225 PRO   A CA  
1732 C C   . PRO   A 245 ? 0.65589 0.41499 0.48588 -0.10734 -0.09110 0.11486  225 PRO   A C   
1733 O O   . PRO   A 245 ? 0.69498 0.43758 0.48777 -0.11182 -0.08516 0.13151  225 PRO   A O   
1734 C CB  . PRO   A 245 ? 0.61047 0.41177 0.60203 -0.05740 -0.14926 0.15550  225 PRO   A CB  
1735 C CG  . PRO   A 245 ? 0.59884 0.39880 0.62100 -0.04506 -0.14135 0.17283  225 PRO   A CG  
1736 C CD  . PRO   A 245 ? 0.58254 0.36105 0.61828 -0.03892 -0.14294 0.15418  225 PRO   A CD  
1737 N N   . LYS   A 246 ? 0.67128 0.42245 0.44216 -0.11285 -0.05482 0.07926  226 LYS   A N   
1738 C CA  . LYS   A 246 ? 0.69311 0.43888 0.46441 -0.13323 0.00651  0.02325  226 LYS   A CA  
1739 C C   . LYS   A 246 ? 0.64300 0.41740 0.40338 -0.13984 0.04944  -0.03359 226 LYS   A C   
1740 O O   . LYS   A 246 ? 0.65349 0.44934 0.42737 -0.16154 0.06646  -0.07776 226 LYS   A O   
1741 C CB  . LYS   A 246 ? 0.76139 0.47010 0.58320 -0.15142 -0.00368 -0.01350 226 LYS   A CB  
1742 C CG  . LYS   A 246 ? 0.82687 0.49654 0.67571 -0.15684 -0.00572 -0.03232 226 LYS   A CG  
1743 C CD  . LYS   A 246 ? 0.87524 0.52396 0.74606 -0.16487 -0.00497 -0.04981 226 LYS   A CD  
1744 C CE  . LYS   A 246 ? 0.91003 0.54794 0.80393 -0.16696 0.00669  -0.05461 226 LYS   A CE  
1745 N NZ  . LYS   A 246 ? 0.93223 0.55678 0.84590 -0.16595 0.01438  -0.06236 226 LYS   A NZ  
1746 N N   . LEU   A 247 ? 0.58429 0.33189 0.33113 -0.11723 0.01595  -0.03721 227 LEU   A N   
1747 C CA  . LEU   A 247 ? 0.54221 0.27722 0.30257 -0.04329 0.04643  -0.03474 227 LEU   A CA  
1748 C C   . LEU   A 247 ? 0.53041 0.25060 0.32236 -0.04770 0.07954  -0.05828 227 LEU   A C   
1749 O O   . LEU   A 247 ? 0.55394 0.26556 0.43080 -0.04549 0.08562  -0.10314 227 LEU   A O   
1750 C CB  . LEU   A 247 ? 0.52631 0.26472 0.29944 0.03202  0.00844  -0.02734 227 LEU   A CB  
1751 C CG  . LEU   A 247 ? 0.53569 0.22565 0.30982 0.06093  0.00947  -0.01859 227 LEU   A CG  
1752 C CD1 . LEU   A 247 ? 0.51779 0.22479 0.38855 0.07988  0.07232  -0.01769 227 LEU   A CD1 
1753 C CD2 . LEU   A 247 ? 0.54057 0.22498 0.26469 0.06575  -0.01046 -0.01970 227 LEU   A CD2 
1754 N N   . THR   A 248 ? 0.49705 0.23440 0.23060 -0.03362 0.07806  0.00154  228 THR   A N   
1755 C CA  . THR   A 248 ? 0.48454 0.22575 0.21641 -0.01861 0.02922  0.01186  228 THR   A CA  
1756 C C   . THR   A 248 ? 0.46605 0.21135 0.23378 -0.00050 0.01834  -0.00792 228 THR   A C   
1757 O O   . THR   A 248 ? 0.45947 0.21160 0.25977 -0.01139 0.05004  0.01265  228 THR   A O   
1758 C CB  . THR   A 248 ? 0.51681 0.26123 0.25735 -0.00667 0.00045  -0.00121 228 THR   A CB  
1759 O OG1 . THR   A 248 ? 0.54403 0.24546 0.27599 -0.01136 0.02738  -0.01182 228 THR   A OG1 
1760 C CG2 . THR   A 248 ? 0.54347 0.30201 0.27888 0.00908  0.00056  0.01677  228 THR   A CG2 
1761 N N   . VAL   A 249 ? 0.45756 0.20479 0.24450 0.00348  -0.00091 0.01239  229 VAL   A N   
1762 C CA  . VAL   A 249 ? 0.44177 0.17862 0.26230 0.01301  0.02320  -0.00469 229 VAL   A CA  
1763 C C   . VAL   A 249 ? 0.41580 0.15965 0.26646 0.00693  0.05963  0.00213  229 VAL   A C   
1764 O O   . VAL   A 249 ? 0.40506 0.16028 0.24761 0.01803  0.04216  -0.00666 229 VAL   A O   
1765 C CB  . VAL   A 249 ? 0.47172 0.17719 0.28432 0.00971  0.05548  -0.01108 229 VAL   A CB  
1766 C CG1 . VAL   A 249 ? 0.47734 0.15473 0.30250 -0.00092 0.06283  -0.01310 229 VAL   A CG1 
1767 C CG2 . VAL   A 249 ? 0.47805 0.18539 0.28647 0.02810  0.05454  -0.02599 229 VAL   A CG2 
1768 N N   . PRO   A 250 ? 0.40948 0.17685 0.26501 0.01093  0.07216  -0.01861 230 PRO   A N   
1769 C CA  . PRO   A 250 ? 0.39986 0.16754 0.24282 0.00132  0.09157  -0.00333 230 PRO   A CA  
1770 C C   . PRO   A 250 ? 0.40861 0.16971 0.22212 0.01623  0.05425  -0.01295 230 PRO   A C   
1771 O O   . PRO   A 250 ? 0.42376 0.15563 0.24463 0.02864  0.03162  -0.00090 230 PRO   A O   
1772 C CB  . PRO   A 250 ? 0.39616 0.16867 0.24449 -0.00623 0.07875  -0.00038 230 PRO   A CB  
1773 C CG  . PRO   A 250 ? 0.41835 0.16786 0.21070 -0.01288 0.04313  -0.00460 230 PRO   A CG  
1774 C CD  . PRO   A 250 ? 0.40641 0.18646 0.26630 0.00451  0.06849  -0.01326 230 PRO   A CD  
1775 N N   . PHE   A 251 ? 0.37355 0.15819 0.20279 0.00972  0.03450  0.00659  231 PHE   A N   
1776 C CA  . PHE   A 251 ? 0.35684 0.15923 0.18754 0.00088  0.02728  -0.00774 231 PHE   A CA  
1777 C C   . PHE   A 251 ? 0.33698 0.13938 0.22643 0.02789  0.03009  0.02992  231 PHE   A C   
1778 O O   . PHE   A 251 ? 0.33061 0.12334 0.22596 0.02037  0.03701  0.01996  231 PHE   A O   
1779 C CB  . PHE   A 251 ? 0.34187 0.16129 0.25439 0.00645  0.03701  0.00083  231 PHE   A CB  
1780 C CG  . PHE   A 251 ? 0.34566 0.15274 0.23442 0.00616  0.03717  -0.01217 231 PHE   A CG  
1781 C CD1 . PHE   A 251 ? 0.34251 0.15257 0.26207 0.00412  0.02706  0.02718  231 PHE   A CD1 
1782 C CD2 . PHE   A 251 ? 0.36528 0.13965 0.26753 0.01418  0.00709  0.00041  231 PHE   A CD2 
1783 C CE1 . PHE   A 251 ? 0.37272 0.15856 0.26939 -0.01041 0.00111  0.02373  231 PHE   A CE1 
1784 C CE2 . PHE   A 251 ? 0.37184 0.12733 0.25349 0.00593  0.00249  0.00165  231 PHE   A CE2 
1785 C CZ  . PHE   A 251 ? 0.38108 0.15496 0.27370 0.00390  0.00978  0.01979  231 PHE   A CZ  
1786 N N   . LEU   A 252 ? 0.33684 0.13967 0.21570 0.01905  -0.00029 0.02317  232 LEU   A N   
1787 C CA  . LEU   A 252 ? 0.30400 0.14828 0.24072 0.01859  0.01715  0.00024  232 LEU   A CA  
1788 C C   . LEU   A 252 ? 0.29268 0.12022 0.24747 0.01224  0.03377  -0.01236 232 LEU   A C   
1789 O O   . LEU   A 252 ? 0.30157 0.12471 0.27167 -0.00552 0.05415  -0.00206 232 LEU   A O   
1790 C CB  . LEU   A 252 ? 0.27496 0.15392 0.27915 -0.00124 -0.00345 -0.00266 232 LEU   A CB  
1791 C CG  . LEU   A 252 ? 0.26716 0.15956 0.27052 0.03356  -0.01181 -0.00042 232 LEU   A CG  
1792 C CD1 . LEU   A 252 ? 0.30654 0.14957 0.28231 0.00697  0.00947  -0.00694 232 LEU   A CD1 
1793 C CD2 . LEU   A 252 ? 0.29946 0.17920 0.26050 0.03683  -0.00665 0.00623  232 LEU   A CD2 
1794 N N   . LEU   A 253 ? 0.27639 0.13025 0.21547 0.02063  0.03108  0.01825  233 LEU   A N   
1795 C CA  . LEU   A 253 ? 0.28372 0.13573 0.22575 0.02953  0.04223  0.00633  233 LEU   A CA  
1796 C C   . LEU   A 253 ? 0.30630 0.12361 0.22102 0.00669  0.02721  0.01385  233 LEU   A C   
1797 O O   . LEU   A 253 ? 0.32706 0.12131 0.22863 0.00088  0.00618  0.01823  233 LEU   A O   
1798 C CB  . LEU   A 253 ? 0.26303 0.15334 0.26097 0.03329  0.01718  0.00420  233 LEU   A CB  
1799 C CG  . LEU   A 253 ? 0.29243 0.14937 0.31007 0.01182  0.01130  0.02845  233 LEU   A CG  
1800 C CD1 . LEU   A 253 ? 0.29510 0.15248 0.32938 -0.00120 0.01027  0.02362  233 LEU   A CD1 
1801 C CD2 . LEU   A 253 ? 0.30546 0.15615 0.31387 0.02979  -0.03601 0.01536  233 LEU   A CD2 
1802 N N   . LEU   A 254 ? 0.29545 0.12827 0.21033 -0.02082 -0.00045 0.02478  234 LEU   A N   
1803 C CA  . LEU   A 254 ? 0.26654 0.12720 0.20024 0.00293  0.01248  0.03527  234 LEU   A CA  
1804 C C   . LEU   A 254 ? 0.28366 0.12080 0.20417 0.02930  0.04066  0.01409  234 LEU   A C   
1805 O O   . LEU   A 254 ? 0.31989 0.11198 0.24192 0.01462  0.02185  -0.00729 234 LEU   A O   
1806 C CB  . LEU   A 254 ? 0.29317 0.13917 0.24347 -0.02288 -0.01419 0.05000  234 LEU   A CB  
1807 C CG  . LEU   A 254 ? 0.28120 0.17171 0.29813 -0.00460 -0.01138 0.04856  234 LEU   A CG  
1808 C CD1 . LEU   A 254 ? 0.27336 0.17850 0.36787 0.01514  -0.01846 0.02800  234 LEU   A CD1 
1809 C CD2 . LEU   A 254 ? 0.31029 0.18731 0.28980 -0.01226 -0.00477 0.03624  234 LEU   A CD2 
1810 N N   . GLN   A 255 ? 0.25903 0.13028 0.21752 0.01617  0.02469  -0.00517 235 GLN   A N   
1811 C CA  . GLN   A 255 ? 0.27039 0.15494 0.21359 0.01501  0.03673  0.00222  235 GLN   A CA  
1812 C C   . GLN   A 255 ? 0.31153 0.14711 0.21463 0.00239  0.02795  0.01736  235 GLN   A C   
1813 O O   . GLN   A 255 ? 0.33491 0.12838 0.24477 -0.02297 0.03045  -0.00397 235 GLN   A O   
1814 C CB  . GLN   A 255 ? 0.25529 0.15729 0.23427 -0.01034 0.01263  0.01668  235 GLN   A CB  
1815 C CG  . GLN   A 255 ? 0.27582 0.14327 0.23787 -0.01113 0.04115  -0.00184 235 GLN   A CG  
1816 C CD  . GLN   A 255 ? 0.28759 0.15959 0.26621 0.00950  0.02624  -0.00374 235 GLN   A CD  
1817 O OE1 . GLN   A 255 ? 0.28241 0.16314 0.28673 0.02486  0.00958  -0.02891 235 GLN   A OE1 
1818 N NE2 . GLN   A 255 ? 0.29248 0.19442 0.27317 0.00804  0.02543  -0.00009 235 GLN   A NE2 
1819 N N   . GLY   A 256 ? 0.26259 0.15789 0.21200 -0.00194 0.03741  0.02315  236 GLY   A N   
1820 C CA  . GLY   A 256 ? 0.26055 0.16242 0.20539 0.01079  0.01306  0.00312  236 GLY   A CA  
1821 C C   . GLY   A 256 ? 0.27694 0.15342 0.23160 0.01195  0.01295  -0.02182 236 GLY   A C   
1822 O O   . GLY   A 256 ? 0.30041 0.17127 0.24030 -0.00362 -0.00992 -0.01382 236 GLY   A O   
1823 N N   . SER   A 257 ? 0.27220 0.14179 0.23963 0.01511  0.04475  -0.00048 237 SER   A N   
1824 C CA  . SER   A 257 ? 0.28480 0.16892 0.25605 0.02043  0.03791  -0.02492 237 SER   A CA  
1825 C C   . SER   A 257 ? 0.30101 0.18122 0.28401 0.00883  0.01230  -0.01055 237 SER   A C   
1826 O O   . SER   A 257 ? 0.29817 0.20288 0.31227 0.02972  0.00926  -0.00196 237 SER   A O   
1827 C CB  . SER   A 257 ? 0.33031 0.17514 0.25016 0.04032  0.03757  0.00936  237 SER   A CB  
1828 O OG  . SER   A 257 ? 0.38016 0.17257 0.28655 0.02970  0.05787  0.00279  237 SER   A OG  
1829 N N   . ALA   A 258 ? 0.31643 0.15097 0.25938 -0.01462 0.04092  -0.00142 238 ALA   A N   
1830 C CA  . ALA   A 258 ? 0.32425 0.16187 0.24180 -0.01126 0.03694  0.00817  238 ALA   A CA  
1831 C C   . ALA   A 258 ? 0.35033 0.17195 0.23994 0.00889  0.01774  -0.00194 238 ALA   A C   
1832 O O   . ALA   A 258 ? 0.41394 0.19226 0.27216 -0.02429 0.02576  -0.00057 238 ALA   A O   
1833 C CB  . ALA   A 258 ? 0.33386 0.19037 0.25850 -0.01453 0.05945  -0.00748 238 ALA   A CB  
1834 N N   . ASP   A 259 ? 0.32562 0.16520 0.23886 0.03533  -0.00317 -0.01271 239 ASP   A N   
1835 C CA  . ASP   A 259 ? 0.27771 0.15747 0.26562 0.01146  0.00963  -0.01954 239 ASP   A CA  
1836 C C   . ASP   A 259 ? 0.27962 0.17004 0.28660 -0.00281 0.02606  0.00871  239 ASP   A C   
1837 O O   . ASP   A 259 ? 0.27007 0.19932 0.30965 0.01837  0.01741  -0.00904 239 ASP   A O   
1838 C CB  . ASP   A 259 ? 0.25959 0.15527 0.24736 0.00106  0.04988  -0.00852 239 ASP   A CB  
1839 C CG  . ASP   A 259 ? 0.26778 0.14928 0.23818 -0.01282 0.04376  0.00910  239 ASP   A CG  
1840 O OD1 . ASP   A 259 ? 0.29146 0.14746 0.29246 0.00778  0.03575  0.01931  239 ASP   A OD1 
1841 O OD2 . ASP   A 259 ? 0.25708 0.14915 0.27317 0.01155  0.04277  0.01921  239 ASP   A OD2 
1842 N N   . ARG   A 260 ? 0.27762 0.16844 0.25534 -0.04111 0.01557  -0.00255 240 ARG   A N   
1843 C CA  . ARG   A 260 ? 0.28877 0.20032 0.24068 -0.00641 0.01946  -0.03441 240 ARG   A CA  
1844 C C   . ARG   A 260 ? 0.28537 0.20660 0.29402 -0.02757 0.01294  -0.03540 240 ARG   A C   
1845 O O   . ARG   A 260 ? 0.31432 0.23523 0.33022 -0.04267 0.02680  -0.05800 240 ARG   A O   
1846 C CB  . ARG   A 260 ? 0.37299 0.22424 0.20759 -0.01657 0.03834  -0.02708 240 ARG   A CB  
1847 C CG  . ARG   A 260 ? 0.46313 0.26694 0.32075 -0.01283 0.06829  -0.03892 240 ARG   A CG  
1848 C CD  . ARG   A 260 ? 0.55458 0.33544 0.44466 -0.02744 0.06667  -0.04101 240 ARG   A CD  
1849 N NE  . ARG   A 260 ? 0.64575 0.40506 0.62092 -0.04973 0.03777  -0.06766 240 ARG   A NE  
1850 C CZ  . ARG   A 260 ? 0.70324 0.43556 0.75245 -0.06400 0.01525  -0.07984 240 ARG   A CZ  
1851 N NH1 . ARG   A 260 ? 0.73360 0.43227 0.77608 -0.06102 -0.02112 -0.11628 240 ARG   A NH1 
1852 N NH2 . ARG   A 260 ? 0.71017 0.44687 0.86781 -0.07843 0.02574  -0.06175 240 ARG   A NH2 
1853 N N   . LEU   A 261 ? 0.26878 0.18254 0.24979 -0.00424 0.01911  -0.01916 241 LEU   A N   
1854 C CA  . LEU   A 261 ? 0.24817 0.19956 0.24071 -0.00998 0.00611  0.01679  241 LEU   A CA  
1855 C C   . LEU   A 261 ? 0.26444 0.21230 0.26188 -0.01281 0.01633  -0.00699 241 LEU   A C   
1856 O O   . LEU   A 261 ? 0.25161 0.22150 0.30319 -0.01643 -0.00889 -0.01537 241 LEU   A O   
1857 C CB  . LEU   A 261 ? 0.25753 0.19088 0.26287 0.00849  -0.02032 0.01162  241 LEU   A CB  
1858 C CG  . LEU   A 261 ? 0.25494 0.18983 0.28433 -0.02044 -0.03045 0.01653  241 LEU   A CG  
1859 C CD1 . LEU   A 261 ? 0.27050 0.21556 0.25751 0.00041  -0.00602 0.02675  241 LEU   A CD1 
1860 C CD2 . LEU   A 261 ? 0.28535 0.21884 0.32708 -0.03084 -0.02493 0.01892  241 LEU   A CD2 
1861 N N   . CYS   A 262 ? 0.25463 0.19721 0.25382 0.00549  0.02830  0.03036  242 CYS   A N   
1862 C CA  . CYS   A 262 ? 0.28272 0.17589 0.25167 0.03961  0.00057  0.00774  242 CYS   A CA  
1863 C C   . CYS   A 262 ? 0.33617 0.16885 0.31741 0.03510  -0.05135 -0.01399 242 CYS   A C   
1864 O O   . CYS   A 262 ? 0.36556 0.18535 0.32339 0.01661  -0.05014 0.00097  242 CYS   A O   
1865 C CB  . CYS   A 262 ? 0.30205 0.18616 0.25549 0.01867  0.01364  -0.01143 242 CYS   A CB  
1866 S SG  . CYS   A 262 ? 0.28448 0.17815 0.26633 -0.00343 -0.00167 0.00964  242 CYS   A SG  
1867 N N   . ASP   A 263 ? 0.33161 0.17507 0.30584 0.04409  -0.00435 0.01623  243 ASP   A N   
1868 C CA  . ASP   A 263 ? 0.34654 0.19390 0.35583 0.02455  0.03305  0.00792  243 ASP   A CA  
1869 C C   . ASP   A 263 ? 0.33287 0.18013 0.32170 0.03321  0.00774  0.00073  243 ASP   A C   
1870 O O   . ASP   A 263 ? 0.32108 0.18958 0.29128 0.03036  0.02046  0.02698  243 ASP   A O   
1871 C CB  . ASP   A 263 ? 0.31053 0.23972 0.45524 0.03648  0.10339  0.00720  243 ASP   A CB  
1872 C CG  . ASP   A 263 ? 0.32663 0.28311 0.49161 0.00946  0.12178  -0.00233 243 ASP   A CG  
1873 O OD1 . ASP   A 263 ? 0.34151 0.26214 0.38921 0.00466  0.07961  -0.00377 243 ASP   A OD1 
1874 O OD2 . ASP   A 263 ? 0.33742 0.30025 0.55790 0.03457  0.12596  0.02198  243 ASP   A OD2 
1875 N N   . SER   A 264 ? 0.32122 0.18453 0.29720 0.03010  0.00569  0.00941  244 SER   A N   
1876 C CA  . SER   A 264 ? 0.29025 0.18766 0.30486 0.01249  -0.01552 -0.00164 244 SER   A CA  
1877 C C   . SER   A 264 ? 0.29351 0.18154 0.30503 0.01511  0.01780  0.00758  244 SER   A C   
1878 O O   . SER   A 264 ? 0.28516 0.19307 0.30552 0.00816  0.02418  0.01916  244 SER   A O   
1879 C CB  . SER   A 264 ? 0.31315 0.21655 0.32048 0.02694  0.01977  -0.03704 244 SER   A CB  
1880 O OG  . SER   A 264 ? 0.34673 0.22689 0.32063 0.03123  0.02282  -0.02574 244 SER   A OG  
1881 N N   . LYS   A 265 ? 0.28567 0.17027 0.29748 0.04025  0.02232  0.00743  245 LYS   A N   
1882 C CA  . LYS   A 265 ? 0.28455 0.19031 0.30129 0.02479  0.00403  0.04345  245 LYS   A CA  
1883 C C   . LYS   A 265 ? 0.29385 0.17858 0.31368 0.02109  0.00849  0.02397  245 LYS   A C   
1884 O O   . LYS   A 265 ? 0.30276 0.20433 0.30947 0.03484  0.02773  0.03644  245 LYS   A O   
1885 C CB  . LYS   A 265 ? 0.34527 0.21752 0.31352 0.04681  -0.00304 0.03972  245 LYS   A CB  
1886 C CG  . LYS   A 265 ? 0.45473 0.25462 0.39486 0.04996  -0.05533 0.05234  245 LYS   A CG  
1887 C CD  . LYS   A 265 ? 0.55082 0.30462 0.51265 0.06173  -0.07107 0.06614  245 LYS   A CD  
1888 C CE  . LYS   A 265 ? 0.61554 0.33025 0.60167 0.06559  -0.08406 0.07764  245 LYS   A CE  
1889 N NZ  . LYS   A 265 ? 0.65955 0.36144 0.67033 0.06270  -0.09090 0.06022  245 LYS   A NZ  
1890 N N   . GLY   A 266 ? 0.30568 0.16754 0.31953 0.01962  0.01891  -0.00245 246 GLY   A N   
1891 C CA  . GLY   A 266 ? 0.30587 0.19331 0.31272 -0.02477 0.01629  0.02004  246 GLY   A CA  
1892 C C   . GLY   A 266 ? 0.30478 0.17744 0.29490 -0.00650 -0.00085 0.01667  246 GLY   A C   
1893 O O   . GLY   A 266 ? 0.33749 0.17361 0.27305 -0.00992 -0.00999 0.01867  246 GLY   A O   
1894 N N   . ALA   A 267 ? 0.27244 0.16466 0.27948 0.02917  -0.01104 0.05545  247 ALA   A N   
1895 C CA  . ALA   A 267 ? 0.29727 0.18173 0.27488 0.02428  0.00383  0.05404  247 ALA   A CA  
1896 C C   . ALA   A 267 ? 0.29686 0.17070 0.26506 0.03078  -0.00583 0.01814  247 ALA   A C   
1897 O O   . ALA   A 267 ? 0.29885 0.19158 0.26284 0.02408  0.00366  0.00757  247 ALA   A O   
1898 C CB  . ALA   A 267 ? 0.29518 0.20167 0.23238 0.03345  0.02440  0.03993  247 ALA   A CB  
1899 N N   . TYR   A 268 ? 0.29582 0.16751 0.26658 0.03698  -0.03126 0.02286  248 TYR   A N   
1900 C CA  . TYR   A 268 ? 0.30858 0.17249 0.26432 0.04473  0.00087  0.01270  248 TYR   A CA  
1901 C C   . TYR   A 268 ? 0.31754 0.18034 0.25066 0.02155  0.00134  0.00196  248 TYR   A C   
1902 O O   . TYR   A 268 ? 0.34102 0.18431 0.26320 0.04201  0.01613  0.02944  248 TYR   A O   
1903 C CB  . TYR   A 268 ? 0.32638 0.18971 0.29368 0.04165  0.00126  -0.02347 248 TYR   A CB  
1904 C CG  . TYR   A 268 ? 0.33900 0.18520 0.28834 -0.00152 0.01209  -0.03056 248 TYR   A CG  
1905 C CD1 . TYR   A 268 ? 0.36367 0.18490 0.30824 -0.01949 0.01046  -0.03341 248 TYR   A CD1 
1906 C CD2 . TYR   A 268 ? 0.34329 0.20829 0.26258 0.00778  0.00970  -0.03386 248 TYR   A CD2 
1907 C CE1 . TYR   A 268 ? 0.38533 0.20884 0.30620 -0.00042 0.01209  0.00652  248 TYR   A CE1 
1908 C CE2 . TYR   A 268 ? 0.35848 0.20374 0.28015 0.01221  -0.00877 -0.00883 248 TYR   A CE2 
1909 C CZ  . TYR   A 268 ? 0.36308 0.20287 0.27477 0.01794  -0.00808 -0.01376 248 TYR   A CZ  
1910 O OH  . TYR   A 268 ? 0.37213 0.18644 0.30661 0.02355  0.01566  -0.02729 248 TYR   A OH  
1911 N N   . LEU   A 269 ? 0.32531 0.17003 0.26845 0.00491  -0.02546 -0.02012 249 LEU   A N   
1912 C CA  . LEU   A 269 ? 0.31275 0.20742 0.25578 -0.00573 -0.01073 0.00611  249 LEU   A CA  
1913 C C   . LEU   A 269 ? 0.30625 0.18986 0.29811 0.00934  -0.01340 0.00148  249 LEU   A C   
1914 O O   . LEU   A 269 ? 0.32191 0.19000 0.29114 -0.00011 -0.00965 0.01080  249 LEU   A O   
1915 C CB  . LEU   A 269 ? 0.32212 0.24988 0.37680 -0.01011 0.02437  0.01648  249 LEU   A CB  
1916 C CG  . LEU   A 269 ? 0.35084 0.29216 0.45173 -0.01427 0.03479  0.03419  249 LEU   A CG  
1917 C CD1 . LEU   A 269 ? 0.34398 0.31455 0.47939 -0.03785 0.04796  0.03987  249 LEU   A CD1 
1918 C CD2 . LEU   A 269 ? 0.35806 0.30634 0.44260 0.00306  0.03441  0.01521  249 LEU   A CD2 
1919 N N   . LEU   A 270 ? 0.27447 0.17342 0.30859 0.03616  0.00373  -0.00490 250 LEU   A N   
1920 C CA  . LEU   A 270 ? 0.29587 0.17181 0.30555 0.04639  0.00093  0.01540  250 LEU   A CA  
1921 C C   . LEU   A 270 ? 0.31612 0.18443 0.28966 0.02404  0.00825  0.01702  250 LEU   A C   
1922 O O   . LEU   A 270 ? 0.33771 0.17731 0.28558 0.01376  -0.00735 -0.01076 250 LEU   A O   
1923 C CB  . LEU   A 270 ? 0.30884 0.18896 0.29259 0.06213  0.00044  0.00586  250 LEU   A CB  
1924 C CG  . LEU   A 270 ? 0.32415 0.20075 0.27657 0.05524  -0.01196 0.02091  250 LEU   A CG  
1925 C CD1 . LEU   A 270 ? 0.36621 0.22314 0.28046 0.04171  -0.00642 -0.01705 250 LEU   A CD1 
1926 C CD2 . LEU   A 270 ? 0.33356 0.18910 0.35582 0.04169  -0.02124 0.05812  250 LEU   A CD2 
1927 N N   . MET   A 271 ? 0.30917 0.17056 0.27842 0.01177  0.00749  0.02389  251 MET   A N   
1928 C CA  . MET   A 271 ? 0.31865 0.17084 0.26829 -0.02396 -0.01955 -0.00046 251 MET   A CA  
1929 C C   . MET   A 271 ? 0.32088 0.18079 0.27320 -0.01769 -0.02988 0.01210  251 MET   A C   
1930 O O   . MET   A 271 ? 0.35926 0.19247 0.33391 -0.00426 -0.01316 0.02811  251 MET   A O   
1931 C CB  . MET   A 271 ? 0.32166 0.21098 0.25022 -0.01576 -0.02582 0.00297  251 MET   A CB  
1932 C CG  . MET   A 271 ? 0.30304 0.21610 0.29219 -0.01801 -0.04788 -0.00402 251 MET   A CG  
1933 S SD  . MET   A 271 ? 0.29979 0.19023 0.29702 0.00944  0.01244  -0.01895 251 MET   A SD  
1934 C CE  . MET   A 271 ? 0.26898 0.18992 0.30043 0.00202  0.00771  0.03116  251 MET   A CE  
1935 N N   . GLU   A 272 ? 0.33069 0.17639 0.28099 -0.02953 -0.05063 0.00088  252 GLU   A N   
1936 C CA  . GLU   A 272 ? 0.33735 0.18821 0.25594 0.00245  -0.05972 -0.00221 252 GLU   A CA  
1937 C C   . GLU   A 272 ? 0.36349 0.17922 0.24418 -0.00143 -0.03163 0.02115  252 GLU   A C   
1938 O O   . GLU   A 272 ? 0.43219 0.20474 0.27136 0.00303  -0.03723 0.01788  252 GLU   A O   
1939 C CB  . GLU   A 272 ? 0.31893 0.21471 0.30972 0.05069  -0.03254 0.01697  252 GLU   A CB  
1940 C CG  . GLU   A 272 ? 0.32896 0.26594 0.38501 0.06189  -0.02724 0.06435  252 GLU   A CG  
1941 C CD  . GLU   A 272 ? 0.36018 0.32940 0.52166 0.09783  -0.03699 0.08589  252 GLU   A CD  
1942 O OE1 . GLU   A 272 ? 0.36997 0.34530 0.55314 0.09993  -0.04038 0.08267  252 GLU   A OE1 
1943 O OE2 . GLU   A 272 ? 0.38414 0.38135 0.63270 0.11963  -0.05729 0.10134  252 GLU   A OE2 
1944 N N   . LEU   A 273 ? 0.33599 0.17355 0.26068 -0.03113 -0.03265 0.00536  253 LEU   A N   
1945 C CA  . LEU   A 273 ? 0.33256 0.19389 0.27984 -0.02654 -0.05206 -0.00914 253 LEU   A CA  
1946 C C   . LEU   A 273 ? 0.35103 0.21197 0.29129 -0.00329 -0.05037 0.00063  253 LEU   A C   
1947 O O   . LEU   A 273 ? 0.36937 0.25347 0.29184 0.00008  -0.05141 -0.02183 253 LEU   A O   
1948 C CB  . LEU   A 273 ? 0.33804 0.24403 0.34472 -0.04049 -0.03694 -0.01248 253 LEU   A CB  
1949 C CG  . LEU   A 273 ? 0.35854 0.29583 0.38439 -0.03133 -0.01495 0.03393  253 LEU   A CG  
1950 C CD1 . LEU   A 273 ? 0.38142 0.34872 0.41933 -0.04427 -0.02618 0.03963  253 LEU   A CD1 
1951 C CD2 . LEU   A 273 ? 0.35604 0.32537 0.43661 -0.01452 0.00107  0.02918  253 LEU   A CD2 
1952 N N   . ALA   A 274 ? 0.31083 0.17575 0.26836 0.01063  -0.01373 0.00657  254 ALA   A N   
1953 C CA  . ALA   A 274 ? 0.32840 0.18724 0.26171 0.02768  0.01402  0.01652  254 ALA   A CA  
1954 C C   . ALA   A 274 ? 0.38136 0.24879 0.26748 0.00999  -0.01364 0.00479  254 ALA   A C   
1955 O O   . ALA   A 274 ? 0.39387 0.22848 0.27736 -0.01225 -0.01645 -0.01315 254 ALA   A O   
1956 C CB  . ALA   A 274 ? 0.33592 0.20143 0.29954 0.03778  -0.00442 0.03311  254 ALA   A CB  
1957 N N   . LYS   A 275 ? 0.42120 0.27946 0.26810 0.00892  -0.01208 0.00748  255 LYS   A N   
1958 C CA  A LYS   A 275 ? 0.44121 0.30475 0.29725 0.00158  0.00099  0.01333  255 LYS   A CA  
1959 C CA  B LYS   A 275 ? 0.43366 0.31273 0.30438 -0.01149 -0.00388 0.01750  255 LYS   A CA  
1960 C C   . LYS   A 275 ? 0.44967 0.30171 0.28787 -0.00058 0.00627  0.02617  255 LYS   A C   
1961 O O   . LYS   A 275 ? 0.45487 0.33864 0.30741 -0.01144 -0.01718 0.04290  255 LYS   A O   
1962 C CB  A LYS   A 275 ? 0.45989 0.33298 0.33226 0.00605  -0.00689 -0.00061 255 LYS   A CB  
1963 C CB  B LYS   A 275 ? 0.44826 0.36007 0.36275 -0.01028 -0.04376 0.00042  255 LYS   A CB  
1964 C CG  A LYS   A 275 ? 0.47377 0.35712 0.36825 0.00546  -0.00786 -0.01271 255 LYS   A CG  
1965 C CG  B LYS   A 275 ? 0.46204 0.39459 0.40955 -0.01549 -0.06530 -0.01627 255 LYS   A CG  
1966 C CD  A LYS   A 275 ? 0.49059 0.38295 0.39998 0.00674  -0.00324 -0.01340 255 LYS   A CD  
1967 C CD  B LYS   A 275 ? 0.48174 0.43215 0.44881 -0.01902 -0.06710 -0.03103 255 LYS   A CD  
1968 C CE  A LYS   A 275 ? 0.50614 0.39790 0.39859 0.00771  -0.00652 -0.01549 255 LYS   A CE  
1969 C CE  B LYS   A 275 ? 0.50825 0.46193 0.50695 -0.02692 -0.05747 -0.01747 255 LYS   A CE  
1970 N NZ  A LYS   A 275 ? 0.51361 0.40351 0.39495 0.01012  -0.01438 -0.01871 255 LYS   A NZ  
1971 N NZ  B LYS   A 275 ? 0.51641 0.47440 0.51063 -0.03204 -0.08688 0.00987  255 LYS   A NZ  
1972 N N   . SER   A 276 ? 0.45089 0.24671 0.24942 0.00008  0.01702  0.02515  256 SER   A N   
1973 C CA  A SER   A 276 ? 0.43784 0.21354 0.25656 -0.00793 0.02597  0.02346  256 SER   A CA  
1974 C CA  B SER   A 276 ? 0.45498 0.21236 0.25049 0.00655  0.02839  0.02512  256 SER   A CA  
1975 C C   . SER   A 276 ? 0.45218 0.20012 0.25863 0.01902  0.02493  0.01130  256 SER   A C   
1976 O O   . SER   A 276 ? 0.47699 0.20749 0.27521 0.02984  0.02012  -0.02876 256 SER   A O   
1977 C CB  A SER   A 276 ? 0.42156 0.19539 0.25581 0.00086  0.01218  0.04874  256 SER   A CB  
1978 C CB  B SER   A 276 ? 0.45933 0.19496 0.23555 0.01221  0.03224  0.04233  256 SER   A CB  
1979 O OG  A SER   A 276 ? 0.40534 0.17884 0.26332 -0.02110 0.02542  0.00642  256 SER   A OG  
1980 O OG  B SER   A 276 ? 0.45862 0.17787 0.21259 0.00928  0.03569  0.03577  256 SER   A OG  
1981 N N   . GLN   A 277 ? 0.47992 0.16875 0.26806 -0.00005 0.00153  0.02367  257 GLN   A N   
1982 C CA  . GLN   A 277 ? 0.52055 0.18384 0.26849 -0.00329 0.01730  -0.00958 257 GLN   A CA  
1983 C C   . GLN   A 277 ? 0.46662 0.15726 0.26576 0.01676  -0.02893 0.02293  257 GLN   A C   
1984 O O   . GLN   A 277 ? 0.50015 0.16183 0.33237 -0.02227 -0.06656 0.05113  257 GLN   A O   
1985 C CB  . GLN   A 277 ? 0.63310 0.22805 0.27773 -0.01900 0.03839  0.00944  257 GLN   A CB  
1986 C CG  . GLN   A 277 ? 0.72615 0.29916 0.32871 -0.02668 0.02422  0.03263  257 GLN   A CG  
1987 C CD  . GLN   A 277 ? 0.82666 0.36396 0.44637 -0.02235 0.03036  0.02385  257 GLN   A CD  
1988 O OE1 . GLN   A 277 ? 0.87786 0.40369 0.53728 -0.02678 0.03828  0.03487  257 GLN   A OE1 
1989 N NE2 . GLN   A 277 ? 0.85587 0.37668 0.53187 -0.02109 -0.00094 0.03933  257 GLN   A NE2 
1990 N N   . ASP   A 278 ? 0.39477 0.15289 0.25016 0.02321  -0.00112 0.02274  258 ASP   A N   
1991 C CA  . ASP   A 278 ? 0.35226 0.15008 0.21935 0.00792  0.02374  0.03019  258 ASP   A CA  
1992 C C   . ASP   A 278 ? 0.34683 0.14928 0.24780 0.00816  0.01080  0.00651  258 ASP   A C   
1993 O O   . ASP   A 278 ? 0.40006 0.13976 0.27350 0.00566  0.02803  0.01052  258 ASP   A O   
1994 C CB  . ASP   A 278 ? 0.37166 0.15382 0.30332 0.03485  0.03825  0.02746  258 ASP   A CB  
1995 C CG  . ASP   A 278 ? 0.39355 0.18374 0.36490 0.01689  0.03553  0.03687  258 ASP   A CG  
1996 O OD1 . ASP   A 278 ? 0.38379 0.18746 0.32992 0.01207  0.04030  0.03595  258 ASP   A OD1 
1997 O OD2 . ASP   A 278 ? 0.41780 0.20189 0.37328 0.01060  0.04564  0.04043  258 ASP   A OD2 
1998 N N   . LYS   A 279 ? 0.29989 0.19158 0.21127 0.01424  0.02496  0.02343  259 LYS   A N   
1999 C CA  . LYS   A 279 ? 0.29285 0.19834 0.22972 -0.01859 0.04697  0.01259  259 LYS   A CA  
2000 C C   . LYS   A 279 ? 0.31874 0.14275 0.21500 -0.00026 0.01679  0.00157  259 LYS   A C   
2001 O O   . LYS   A 279 ? 0.34395 0.12609 0.23970 0.00892  0.00809  0.01065  259 LYS   A O   
2002 C CB  . LYS   A 279 ? 0.29858 0.23923 0.34219 0.00557  0.02757  0.04005  259 LYS   A CB  
2003 C CG  . LYS   A 279 ? 0.32522 0.25048 0.33182 -0.00128 0.02199  0.06817  259 LYS   A CG  
2004 C CD  . LYS   A 279 ? 0.33886 0.25330 0.32553 -0.02461 0.00411  0.05733  259 LYS   A CD  
2005 C CE  . LYS   A 279 ? 0.33777 0.20086 0.30798 -0.01759 -0.03438 0.03227  259 LYS   A CE  
2006 N NZ  . LYS   A 279 ? 0.35429 0.17490 0.24027 -0.02096 -0.02375 0.00718  259 LYS   A NZ  
2007 N N   . THR   A 280 ? 0.31407 0.15928 0.19874 -0.00247 0.03043  0.00618  260 THR   A N   
2008 C CA  . THR   A 280 ? 0.32230 0.16549 0.21263 -0.00069 0.00893  0.00247  260 THR   A CA  
2009 C C   . THR   A 280 ? 0.31877 0.15318 0.23511 0.00459  0.03973  0.01046  260 THR   A C   
2010 O O   . THR   A 280 ? 0.35061 0.13165 0.25168 -0.00561 0.03760  0.02111  260 THR   A O   
2011 C CB  . THR   A 280 ? 0.33705 0.21218 0.20713 -0.01474 -0.00389 0.01017  260 THR   A CB  
2012 O OG1 . THR   A 280 ? 0.32760 0.20496 0.27032 -0.03231 0.03491  0.00212  260 THR   A OG1 
2013 C CG2 . THR   A 280 ? 0.36158 0.24274 0.21029 -0.00431 -0.01036 -0.00775 260 THR   A CG2 
2014 N N   . LEU   A 281 ? 0.29944 0.15973 0.21266 0.00330  0.02183  0.01565  261 LEU   A N   
2015 C CA  . LEU   A 281 ? 0.28828 0.14496 0.20602 0.01561  -0.01828 0.00449  261 LEU   A CA  
2016 C C   . LEU   A 281 ? 0.32255 0.13364 0.21889 0.00187  -0.00427 0.03708  261 LEU   A C   
2017 O O   . LEU   A 281 ? 0.34107 0.12270 0.25259 -0.00535 0.02527  0.00804  261 LEU   A O   
2018 C CB  . LEU   A 281 ? 0.29561 0.15741 0.27337 0.01877  0.00066  0.00484  261 LEU   A CB  
2019 C CG  . LEU   A 281 ? 0.29618 0.15003 0.28983 0.00001  0.02648  0.02049  261 LEU   A CG  
2020 C CD1 . LEU   A 281 ? 0.30369 0.16431 0.28210 0.01434  0.02795  0.00673  261 LEU   A CD1 
2021 C CD2 . LEU   A 281 ? 0.30812 0.18337 0.30480 -0.00597 0.03370  0.03337  261 LEU   A CD2 
2022 N N   . LYS   A 282 ? 0.31224 0.14967 0.23457 -0.00624 -0.00220 0.03280  262 LYS   A N   
2023 C CA  . LYS   A 282 ? 0.32429 0.16270 0.22640 -0.00992 -0.00008 0.02082  262 LYS   A CA  
2024 C C   . LYS   A 282 ? 0.34067 0.13339 0.22751 0.00657  0.01748  0.01124  262 LYS   A C   
2025 O O   . LYS   A 282 ? 0.36463 0.11962 0.22444 -0.00770 0.01837  0.00129  262 LYS   A O   
2026 C CB  . LYS   A 282 ? 0.34481 0.20841 0.28466 0.01726  -0.05489 -0.04044 262 LYS   A CB  
2027 C CG  . LYS   A 282 ? 0.36872 0.28092 0.45496 0.04124  -0.03802 -0.02281 262 LYS   A CG  
2028 C CD  . LYS   A 282 ? 0.37925 0.29316 0.56825 0.05468  -0.02131 -0.05324 262 LYS   A CD  
2029 C CE  . LYS   A 282 ? 0.43139 0.27801 0.63945 0.02146  0.01001  -0.06881 262 LYS   A CE  
2030 N NZ  . LYS   A 282 ? 0.47478 0.26263 0.68571 0.02272  0.04608  -0.09470 262 LYS   A NZ  
2031 N N   . ILE   A 283 ? 0.34194 0.16250 0.21668 0.00918  0.05876  -0.02049 263 ILE   A N   
2032 C CA  . ILE   A 283 ? 0.33009 0.16357 0.23241 0.01463  0.03691  0.00599  263 ILE   A CA  
2033 C C   . ILE   A 283 ? 0.37674 0.16915 0.21299 -0.00435 0.03048  0.00571  263 ILE   A C   
2034 O O   . ILE   A 283 ? 0.41801 0.15607 0.20722 -0.02492 0.00407  0.00989  263 ILE   A O   
2035 C CB  . ILE   A 283 ? 0.29408 0.16822 0.25409 0.02035  0.03628  0.00630  263 ILE   A CB  
2036 C CG1 . ILE   A 283 ? 0.30710 0.16457 0.27667 -0.03285 0.01784  0.01303  263 ILE   A CG1 
2037 C CG2 . ILE   A 283 ? 0.29501 0.17993 0.24842 0.01071  0.04152  0.00866  263 ILE   A CG2 
2038 C CD1 . ILE   A 283 ? 0.28931 0.15813 0.28679 -0.00561 0.03045  0.00216  263 ILE   A CD1 
2039 N N   . TYR   A 284 ? 0.34277 0.16287 0.21752 0.01028  0.01873  0.02113  264 TYR   A N   
2040 C CA  . TYR   A 284 ? 0.32424 0.16149 0.23993 0.03713  -0.01967 0.01654  264 TYR   A CA  
2041 C C   . TYR   A 284 ? 0.32081 0.13049 0.22165 0.01352  0.01080  0.01178  264 TYR   A C   
2042 O O   . TYR   A 284 ? 0.31355 0.13707 0.25159 -0.00329 0.04308  0.00383  264 TYR   A O   
2043 C CB  . TYR   A 284 ? 0.29898 0.16051 0.29898 0.03603  -0.01944 0.02106  264 TYR   A CB  
2044 C CG  . TYR   A 284 ? 0.30785 0.15454 0.29454 0.01382  0.03630  -0.00357 264 TYR   A CG  
2045 C CD1 . TYR   A 284 ? 0.26272 0.16911 0.30256 0.01038  0.00184  0.00634  264 TYR   A CD1 
2046 C CD2 . TYR   A 284 ? 0.32905 0.15166 0.29819 0.01787  0.07471  0.01488  264 TYR   A CD2 
2047 C CE1 . TYR   A 284 ? 0.28875 0.17916 0.29061 0.00533  0.04206  -0.00974 264 TYR   A CE1 
2048 C CE2 . TYR   A 284 ? 0.31799 0.15762 0.28409 0.01365  0.02333  0.01814  264 TYR   A CE2 
2049 C CZ  . TYR   A 284 ? 0.31106 0.16788 0.29425 -0.00618 0.05074  -0.00282 264 TYR   A CZ  
2050 O OH  . TYR   A 284 ? 0.32686 0.20221 0.31682 0.00421  0.04761  0.00224  264 TYR   A OH  
2051 N N   . GLU   A 285 ? 0.33410 0.13377 0.24258 0.01764  0.00399  -0.04112 265 GLU   A N   
2052 C CA  . GLU   A 285 ? 0.36112 0.13768 0.24138 0.02281  0.01609  -0.02451 265 GLU   A CA  
2053 C C   . GLU   A 285 ? 0.37908 0.16592 0.25578 0.01803  0.00614  -0.01969 265 GLU   A C   
2054 O O   . GLU   A 285 ? 0.40664 0.19535 0.28764 0.01739  -0.01845 0.01281  265 GLU   A O   
2055 C CB  . GLU   A 285 ? 0.39546 0.15498 0.27199 0.02572  0.06661  -0.00559 265 GLU   A CB  
2056 C CG  . GLU   A 285 ? 0.44221 0.21190 0.34093 0.04703  0.06936  -0.02374 265 GLU   A CG  
2057 C CD  . GLU   A 285 ? 0.45332 0.26606 0.38511 0.04660  0.14912  0.01813  265 GLU   A CD  
2058 O OE1 . GLU   A 285 ? 0.45870 0.19946 0.41238 0.03577  0.13399  0.06737  265 GLU   A OE1 
2059 O OE2 . GLU   A 285 ? 0.51389 0.34103 0.37988 0.05408  0.18022  0.00752  265 GLU   A OE2 
2060 N N   . GLY   A 286 ? 0.37879 0.12853 0.27739 0.02476  0.02086  -0.01608 266 GLY   A N   
2061 C CA  . GLY   A 286 ? 0.39309 0.14256 0.23960 0.03875  0.03194  0.01823  266 GLY   A CA  
2062 C C   . GLY   A 286 ? 0.37582 0.15226 0.24540 0.05084  0.00129  -0.00767 266 GLY   A C   
2063 O O   . GLY   A 286 ? 0.38193 0.17260 0.23226 0.04672  0.00640  0.01080  266 GLY   A O   
2064 N N   . ALA   A 287 ? 0.34626 0.14089 0.24680 0.05497  -0.01405 -0.03120 267 ALA   A N   
2065 C CA  . ALA   A 287 ? 0.32059 0.14291 0.24982 0.02688  0.02171  0.00594  267 ALA   A CA  
2066 C C   . ALA   A 287 ? 0.31451 0.14684 0.23414 0.03941  0.01760  0.01787  267 ALA   A C   
2067 O O   . ALA   A 287 ? 0.32612 0.14150 0.24115 0.04807  0.01148  0.00779  267 ALA   A O   
2068 C CB  . ALA   A 287 ? 0.34116 0.16902 0.25297 0.01302  0.02807  0.01544  267 ALA   A CB  
2069 N N   . TYR   A 288 ? 0.30072 0.12752 0.22734 0.02448  0.04981  -0.00845 268 TYR   A N   
2070 C CA  . TYR   A 288 ? 0.31763 0.14374 0.21754 -0.01674 0.04947  -0.01261 268 TYR   A CA  
2071 C C   . TYR   A 288 ? 0.33789 0.15657 0.23131 -0.01336 0.03980  -0.02955 268 TYR   A C   
2072 O O   . TYR   A 288 ? 0.39436 0.18833 0.25449 -0.04456 0.07626  -0.03382 268 TYR   A O   
2073 C CB  . TYR   A 288 ? 0.31212 0.17756 0.20335 -0.01438 0.04496  0.03395  268 TYR   A CB  
2074 C CG  . TYR   A 288 ? 0.33878 0.19328 0.22103 0.00258  0.02035  0.02069  268 TYR   A CG  
2075 C CD1 . TYR   A 288 ? 0.34296 0.20201 0.21517 0.00988  0.04122  0.03358  268 TYR   A CD1 
2076 C CD2 . TYR   A 288 ? 0.36240 0.20527 0.22773 -0.01693 0.06815  0.03706  268 TYR   A CD2 
2077 C CE1 . TYR   A 288 ? 0.37122 0.22195 0.22527 0.02664  0.05183  0.03028  268 TYR   A CE1 
2078 C CE2 . TYR   A 288 ? 0.38985 0.20899 0.26218 0.02278  0.06979  0.01519  268 TYR   A CE2 
2079 C CZ  . TYR   A 288 ? 0.39898 0.22683 0.22445 0.02799  0.07097  -0.00273 268 TYR   A CZ  
2080 O OH  . TYR   A 288 ? 0.46318 0.24978 0.27876 0.03004  0.09821  0.00744  268 TYR   A OH  
2081 N N   . HIS   A 289 ? 0.30989 0.15399 0.22369 -0.00366 0.02377  -0.02751 269 HIS   A N   
2082 C CA  . HIS   A 289 ? 0.29604 0.15325 0.22623 0.00100  0.01768  -0.01293 269 HIS   A CA  
2083 C C   . HIS   A 289 ? 0.29156 0.13683 0.24267 0.00367  0.01248  0.02823  269 HIS   A C   
2084 O O   . HIS   A 289 ? 0.30260 0.13062 0.25005 -0.02035 0.02208  0.01795  269 HIS   A O   
2085 C CB  . HIS   A 289 ? 0.26964 0.14484 0.24650 -0.02458 -0.00897 -0.00091 269 HIS   A CB  
2086 C CG  . HIS   A 289 ? 0.26249 0.14936 0.20822 -0.00949 0.01925  0.01482  269 HIS   A CG  
2087 N ND1 . HIS   A 289 ? 0.26218 0.14696 0.23549 0.01382  0.03273  0.00072  269 HIS   A ND1 
2088 C CD2 . HIS   A 289 ? 0.28223 0.16141 0.21594 -0.01469 0.01117  -0.01765 269 HIS   A CD2 
2089 C CE1 . HIS   A 289 ? 0.25918 0.13055 0.29090 0.02338  0.04145  -0.02644 269 HIS   A CE1 
2090 N NE2 . HIS   A 289 ? 0.26167 0.15607 0.24197 0.01225  0.03712  -0.02542 269 HIS   A NE2 
2091 N N   . VAL   A 290 ? 0.26377 0.12924 0.23536 0.02424  -0.00113 0.00655  270 VAL   A N   
2092 C CA  . VAL   A 290 ? 0.25834 0.11608 0.25232 0.02993  0.02555  0.00217  270 VAL   A CA  
2093 C C   . VAL   A 290 ? 0.29432 0.10707 0.22303 -0.00516 0.03204  -0.00473 270 VAL   A C   
2094 O O   . VAL   A 290 ? 0.29601 0.15600 0.22507 0.01096  -0.00080 0.01336  270 VAL   A O   
2095 C CB  . VAL   A 290 ? 0.25323 0.12772 0.28162 0.02261  -0.02216 0.00388  270 VAL   A CB  
2096 C CG1 . VAL   A 290 ? 0.27111 0.14071 0.29268 0.03453  -0.00440 0.00494  270 VAL   A CG1 
2097 C CG2 . VAL   A 290 ? 0.27349 0.13663 0.26798 -0.00588 0.00287  0.03601  270 VAL   A CG2 
2098 N N   . LEU   A 291 ? 0.29481 0.11963 0.23397 -0.01933 0.01345  0.01163  271 LEU   A N   
2099 C CA  . LEU   A 291 ? 0.26512 0.11663 0.24702 0.00648  -0.00917 0.02934  271 LEU   A CA  
2100 C C   . LEU   A 291 ? 0.27632 0.14820 0.26795 0.00727  -0.00382 0.01699  271 LEU   A C   
2101 O O   . LEU   A 291 ? 0.29239 0.16634 0.24784 0.00240  -0.00742 -0.00627 271 LEU   A O   
2102 C CB  . LEU   A 291 ? 0.25847 0.13515 0.26779 0.01161  0.00384  0.02617  271 LEU   A CB  
2103 C CG  . LEU   A 291 ? 0.24999 0.17313 0.23780 0.04139  0.00651  0.02861  271 LEU   A CG  
2104 C CD1 . LEU   A 291 ? 0.25077 0.19201 0.22040 0.02299  -0.00558 0.05413  271 LEU   A CD1 
2105 C CD2 . LEU   A 291 ? 0.27112 0.16956 0.27477 0.03960  0.04487  0.00990  271 LEU   A CD2 
2106 N N   . HIS   A 292 ? 0.24688 0.15414 0.24284 0.02269  0.02056  0.02849  272 HIS   A N   
2107 C CA  . HIS   A 292 ? 0.25832 0.15438 0.22498 0.02514  0.02436  0.00142  272 HIS   A CA  
2108 C C   . HIS   A 292 ? 0.27687 0.15491 0.24002 0.00803  0.01031  -0.00528 272 HIS   A C   
2109 O O   . HIS   A 292 ? 0.30250 0.15990 0.26213 -0.01567 -0.00256 -0.01568 272 HIS   A O   
2110 C CB  . HIS   A 292 ? 0.24928 0.13447 0.26340 -0.01200 0.00693  -0.01274 272 HIS   A CB  
2111 C CG  . HIS   A 292 ? 0.25212 0.15223 0.25645 -0.03496 -0.02070 0.00143  272 HIS   A CG  
2112 N ND1 . HIS   A 292 ? 0.26238 0.15564 0.25439 -0.00757 -0.00616 0.01489  272 HIS   A ND1 
2113 C CD2 . HIS   A 292 ? 0.27100 0.15935 0.27244 -0.01290 0.01299  -0.02597 272 HIS   A CD2 
2114 C CE1 . HIS   A 292 ? 0.29669 0.14227 0.25688 -0.02383 -0.01006 0.01844  272 HIS   A CE1 
2115 N NE2 . HIS   A 292 ? 0.28492 0.17085 0.27406 -0.00066 0.01007  -0.00064 272 HIS   A NE2 
2116 N N   . LYS   A 293 ? 0.27454 0.16631 0.20941 0.01355  0.03218  0.01865  273 LYS   A N   
2117 C CA  . LYS   A 293 ? 0.29506 0.14509 0.24306 0.01170  0.03378  -0.04078 273 LYS   A CA  
2118 C C   . LYS   A 293 ? 0.28851 0.15672 0.26182 0.00036  0.01684  -0.01422 273 LYS   A C   
2119 O O   . LYS   A 293 ? 0.32418 0.16220 0.28494 0.00748  0.03178  0.02619  273 LYS   A O   
2120 C CB  . LYS   A 293 ? 0.31925 0.13079 0.25293 0.02349  0.00993  -0.03285 273 LYS   A CB  
2121 C CG  . LYS   A 293 ? 0.29941 0.10400 0.24979 0.03944  0.05348  -0.02433 273 LYS   A CG  
2122 C CD  . LYS   A 293 ? 0.29031 0.10930 0.26847 0.02799  0.02466  -0.04770 273 LYS   A CD  
2123 C CE  . LYS   A 293 ? 0.26295 0.17464 0.29255 0.01257  0.05199  -0.03622 273 LYS   A CE  
2124 N NZ  . LYS   A 293 ? 0.26297 0.21012 0.30176 -0.02642 0.03918  -0.01737 273 LYS   A NZ  
2125 N N   . GLU   A 294 ? 0.29421 0.14455 0.25824 0.02943  0.01134  -0.02176 274 GLU   A N   
2126 C CA  . GLU   A 294 ? 0.29397 0.15823 0.21222 0.03665  -0.01782 -0.02477 274 GLU   A CA  
2127 C C   . GLU   A 294 ? 0.30659 0.17221 0.22562 0.03461  -0.00222 -0.00074 274 GLU   A C   
2128 O O   . GLU   A 294 ? 0.30642 0.19547 0.26378 0.03208  -0.02779 -0.01465 274 GLU   A O   
2129 C CB  . GLU   A 294 ? 0.29556 0.18556 0.24328 0.03429  -0.01771 -0.00895 274 GLU   A CB  
2130 C CG  . GLU   A 294 ? 0.30940 0.18552 0.26477 0.04298  0.00766  -0.01744 274 GLU   A CG  
2131 C CD  . GLU   A 294 ? 0.34274 0.19678 0.26975 0.03135  -0.02375 0.01781  274 GLU   A CD  
2132 O OE1 . GLU   A 294 ? 0.37787 0.20584 0.25389 0.02695  0.00224  -0.03052 274 GLU   A OE1 
2133 O OE2 . GLU   A 294 ? 0.35185 0.22329 0.28631 0.02875  0.00888  0.02102  274 GLU   A OE2 
2134 N N   . LEU   A 295 ? 0.31181 0.18436 0.25080 0.00990  -0.00239 -0.04180 275 LEU   A N   
2135 C CA  . LEU   A 295 ? 0.32183 0.22383 0.21623 0.02198  -0.01752 -0.04400 275 LEU   A CA  
2136 C C   . LEU   A 295 ? 0.34766 0.23878 0.22357 0.01769  -0.02334 -0.02020 275 LEU   A C   
2137 O O   . LEU   A 295 ? 0.36156 0.22515 0.23657 0.01336  -0.01148 -0.01467 275 LEU   A O   
2138 C CB  . LEU   A 295 ? 0.34520 0.23952 0.24235 0.01333  0.02104  -0.03716 275 LEU   A CB  
2139 C CG  . LEU   A 295 ? 0.34939 0.24539 0.25293 0.01836  0.00877  -0.02337 275 LEU   A CG  
2140 C CD1 . LEU   A 295 ? 0.35806 0.24508 0.28275 0.03702  0.02929  -0.06402 275 LEU   A CD1 
2141 C CD2 . LEU   A 295 ? 0.36053 0.25566 0.27667 0.01792  0.02090  -0.01859 275 LEU   A CD2 
2142 N N   . PRO   A 296 ? 0.35597 0.28191 0.26115 0.00351  -0.01703 -0.01955 276 PRO   A N   
2143 C CA  . PRO   A 296 ? 0.37156 0.31906 0.27396 -0.01908 -0.03007 -0.00767 276 PRO   A CA  
2144 C C   . PRO   A 296 ? 0.37612 0.33041 0.28789 -0.04442 -0.02788 -0.01979 276 PRO   A C   
2145 O O   . PRO   A 296 ? 0.36612 0.35497 0.32978 -0.05088 -0.03376 -0.04433 276 PRO   A O   
2146 C CB  . PRO   A 296 ? 0.37422 0.35143 0.25822 -0.03148 -0.05561 0.02970  276 PRO   A CB  
2147 C CG  . PRO   A 296 ? 0.38583 0.36622 0.29868 -0.03219 -0.07923 0.00838  276 PRO   A CG  
2148 C CD  . PRO   A 296 ? 0.37987 0.32860 0.26205 -0.03048 -0.06298 -0.00149 276 PRO   A CD  
2149 N N   . GLU   A 297 ? 0.40080 0.31122 0.28727 -0.04371 -0.04428 -0.01467 277 GLU   A N   
2150 C CA  . GLU   A 297 ? 0.45374 0.30246 0.30068 -0.03757 -0.03190 -0.01576 277 GLU   A CA  
2151 C C   . GLU   A 297 ? 0.43190 0.28273 0.29700 -0.06389 -0.02012 -0.00048 277 GLU   A C   
2152 O O   . GLU   A 297 ? 0.44555 0.31444 0.33325 -0.10657 -0.02462 -0.00187 277 GLU   A O   
2153 C CB  . GLU   A 297 ? 0.53952 0.35262 0.36634 -0.02312 0.03403  -0.08300 277 GLU   A CB  
2154 C CG  . GLU   A 297 ? 0.60118 0.41008 0.56968 -0.02161 0.12530  -0.09344 277 GLU   A CG  
2155 C CD  . GLU   A 297 ? 0.64556 0.45114 0.66027 -0.02957 0.20421  -0.11554 277 GLU   A CD  
2156 O OE1 . GLU   A 297 ? 0.62515 0.41907 0.64941 -0.07262 0.14918  -0.12570 277 GLU   A OE1 
2157 O OE2 . GLU   A 297 ? 0.69288 0.48254 0.79123 -0.01016 0.27514  -0.10965 277 GLU   A OE2 
2158 N N   . VAL   A 298 ? 0.37570 0.24414 0.25386 -0.03913 -0.01940 -0.03274 278 VAL   A N   
2159 C CA  . VAL   A 298 ? 0.33534 0.21649 0.24923 -0.00232 0.02985  -0.02868 278 VAL   A CA  
2160 C C   . VAL   A 298 ? 0.31186 0.19344 0.29604 -0.00206 0.00563  0.00036  278 VAL   A C   
2161 O O   . VAL   A 298 ? 0.30436 0.21125 0.30967 -0.01225 0.01307  -0.00815 278 VAL   A O   
2162 C CB  . VAL   A 298 ? 0.33957 0.19117 0.27666 0.00688  0.01076  -0.01580 278 VAL   A CB  
2163 C CG1 . VAL   A 298 ? 0.34137 0.17399 0.27172 0.03739  -0.02175 0.00365  278 VAL   A CG1 
2164 C CG2 . VAL   A 298 ? 0.36701 0.19945 0.30771 0.00619  -0.01119 -0.04822 278 VAL   A CG2 
2165 N N   . THR   A 299 ? 0.31436 0.19383 0.28805 -0.00836 -0.03940 -0.00180 279 THR   A N   
2166 C CA  . THR   A 299 ? 0.33726 0.18388 0.29280 0.00694  -0.00430 -0.01259 279 THR   A CA  
2167 C C   . THR   A 299 ? 0.36373 0.18639 0.30746 0.01006  -0.02701 0.00284  279 THR   A C   
2168 O O   . THR   A 299 ? 0.39641 0.19330 0.29540 0.01968  -0.03700 -0.02535 279 THR   A O   
2169 C CB  . THR   A 299 ? 0.37046 0.17843 0.32463 -0.01177 0.07098  0.00927  279 THR   A CB  
2170 O OG1 . THR   A 299 ? 0.40160 0.20396 0.37352 -0.02090 0.09384  0.00309  279 THR   A OG1 
2171 C CG2 . THR   A 299 ? 0.37882 0.21420 0.35471 0.00107  0.06157  -0.00923 279 THR   A CG2 
2172 N N   . ASN   A 300 ? 0.36199 0.20408 0.30140 -0.00573 -0.03811 -0.00346 280 ASN   A N   
2173 C CA  . ASN   A 300 ? 0.37664 0.25382 0.31955 -0.01808 -0.04002 0.00754  280 ASN   A CA  
2174 C C   . ASN   A 300 ? 0.33579 0.21361 0.32435 -0.03210 -0.02674 0.01620  280 ASN   A C   
2175 O O   . ASN   A 300 ? 0.31646 0.22826 0.36355 -0.03537 -0.00385 0.01439  280 ASN   A O   
2176 C CB  . ASN   A 300 ? 0.39893 0.30504 0.31445 -0.01296 -0.08579 -0.01391 280 ASN   A CB  
2177 C CG  . ASN   A 300 ? 0.46335 0.36634 0.43017 0.00042  -0.07890 -0.02678 280 ASN   A CG  
2178 O OD1 . ASN   A 300 ? 0.47474 0.38662 0.52587 0.02327  -0.09521 0.02350  280 ASN   A OD1 
2179 N ND2 . ASN   A 300 ? 0.48952 0.40018 0.47331 0.00575  -0.05141 -0.01682 280 ASN   A ND2 
2180 N N   . SER   A 301 ? 0.32309 0.19505 0.31104 -0.01042 -0.05692 0.00322  281 SER   A N   
2181 C CA  . SER   A 301 ? 0.31101 0.17955 0.27974 -0.01330 -0.01845 -0.00840 281 SER   A CA  
2182 C C   . SER   A 301 ? 0.30094 0.16194 0.29493 -0.01928 -0.02214 -0.00560 281 SER   A C   
2183 O O   . SER   A 301 ? 0.31828 0.18021 0.31825 -0.01504 -0.00375 0.00028  281 SER   A O   
2184 C CB  . SER   A 301 ? 0.31224 0.18120 0.30844 -0.00370 -0.00739 0.02669  281 SER   A CB  
2185 O OG  . SER   A 301 ? 0.33952 0.17697 0.33761 -0.00349 -0.05153 0.00404  281 SER   A OG  
2186 N N   . VAL   A 302 ? 0.28932 0.16614 0.32197 -0.02271 -0.02882 -0.01431 282 VAL   A N   
2187 C CA  . VAL   A 302 ? 0.28200 0.15839 0.30249 -0.02492 -0.01317 0.00043  282 VAL   A CA  
2188 C C   . VAL   A 302 ? 0.29618 0.16268 0.29231 0.00784  -0.02315 0.00550  282 VAL   A C   
2189 O O   . VAL   A 302 ? 0.30967 0.16765 0.28225 -0.00439 -0.02266 -0.00944 282 VAL   A O   
2190 C CB  . VAL   A 302 ? 0.25433 0.17782 0.29972 -0.05143 0.00738  0.00256  282 VAL   A CB  
2191 C CG1 . VAL   A 302 ? 0.27021 0.18340 0.29585 -0.04817 -0.00558 -0.02204 282 VAL   A CG1 
2192 C CG2 . VAL   A 302 ? 0.23217 0.20275 0.27980 -0.02653 -0.01301 0.00764  282 VAL   A CG2 
2193 N N   . PHE   A 303 ? 0.30379 0.16569 0.29002 0.00786  -0.02873 0.00027  283 PHE   A N   
2194 C CA  . PHE   A 303 ? 0.29022 0.16716 0.32475 -0.00278 0.00319  0.01399  283 PHE   A CA  
2195 C C   . PHE   A 303 ? 0.32021 0.18023 0.32091 -0.01269 -0.00843 0.00696  283 PHE   A C   
2196 O O   . PHE   A 303 ? 0.30408 0.19185 0.33556 0.01152  -0.01166 0.01010  283 PHE   A O   
2197 C CB  . PHE   A 303 ? 0.31511 0.17087 0.31993 0.02294  0.00325  0.00987  283 PHE   A CB  
2198 C CG  . PHE   A 303 ? 0.32154 0.17490 0.31352 0.02588  0.00673  -0.00875 283 PHE   A CG  
2199 C CD1 . PHE   A 303 ? 0.34393 0.17134 0.31310 0.00653  -0.00631 -0.00465 283 PHE   A CD1 
2200 C CD2 . PHE   A 303 ? 0.33231 0.17325 0.30076 0.02942  -0.00362 -0.00818 283 PHE   A CD2 
2201 C CE1 . PHE   A 303 ? 0.35696 0.17219 0.34726 0.01081  -0.04870 0.01349  283 PHE   A CE1 
2202 C CE2 . PHE   A 303 ? 0.34663 0.18662 0.32563 0.01875  -0.03953 -0.00315 283 PHE   A CE2 
2203 C CZ  . PHE   A 303 ? 0.37209 0.19230 0.35170 0.00925  -0.02622 -0.00687 283 PHE   A CZ  
2204 N N   . HIS   A 304 ? 0.33977 0.17172 0.31344 -0.03095 -0.00812 -0.01150 284 HIS   A N   
2205 C CA  . HIS   A 304 ? 0.37307 0.21723 0.29869 -0.05227 -0.01393 -0.01861 284 HIS   A CA  
2206 C C   . HIS   A 304 ? 0.35556 0.21235 0.30466 -0.03467 -0.01634 0.01606  284 HIS   A C   
2207 O O   . HIS   A 304 ? 0.35198 0.22912 0.30283 -0.00255 -0.01122 0.01055  284 HIS   A O   
2208 C CB  . HIS   A 304 ? 0.43606 0.23405 0.38189 -0.10171 0.01293  -0.04519 284 HIS   A CB  
2209 C CG  . HIS   A 304 ? 0.52981 0.31315 0.57998 -0.12150 0.01374  -0.01843 284 HIS   A CG  
2210 N ND1 . HIS   A 304 ? 0.58325 0.37472 0.69378 -0.11801 0.00221  0.01486  284 HIS   A ND1 
2211 C CD2 . HIS   A 304 ? 0.57477 0.35540 0.68180 -0.13102 0.01423  0.02846  284 HIS   A CD2 
2212 C CE1 . HIS   A 304 ? 0.61132 0.38378 0.74257 -0.12217 -0.00229 0.03086  284 HIS   A CE1 
2213 N NE2 . HIS   A 304 ? 0.61796 0.37009 0.74882 -0.13087 -0.00239 0.03519  284 HIS   A NE2 
2214 N N   . GLU   A 305 ? 0.30951 0.19197 0.30001 -0.03818 -0.00752 0.01759  285 GLU   A N   
2215 C CA  . GLU   A 305 ? 0.31778 0.19129 0.28025 -0.01748 0.00948  0.01173  285 GLU   A CA  
2216 C C   . GLU   A 305 ? 0.30390 0.17448 0.25934 -0.01628 -0.00290 0.02768  285 GLU   A C   
2217 O O   . GLU   A 305 ? 0.29893 0.20393 0.28426 0.01464  -0.00358 0.04158  285 GLU   A O   
2218 C CB  . GLU   A 305 ? 0.36483 0.20757 0.35453 -0.00478 0.02570  0.00139  285 GLU   A CB  
2219 C CG  . GLU   A 305 ? 0.42539 0.20241 0.39785 -0.01847 0.03475  0.01233  285 GLU   A CG  
2220 C CD  . GLU   A 305 ? 0.50340 0.21995 0.43049 -0.00759 0.04702  0.02012  285 GLU   A CD  
2221 O OE1 . GLU   A 305 ? 0.53619 0.23263 0.40171 0.00992  0.02520  0.03744  285 GLU   A OE1 
2222 O OE2 . GLU   A 305 ? 0.52634 0.22387 0.52102 -0.01903 0.06896  0.01044  285 GLU   A OE2 
2223 N N   . ILE   A 306 ? 0.27443 0.16253 0.30006 -0.03696 0.01841  0.00113  286 ILE   A N   
2224 C CA  . ILE   A 306 ? 0.26433 0.17710 0.30272 -0.04483 0.02203  0.00828  286 ILE   A CA  
2225 C C   . ILE   A 306 ? 0.26375 0.19632 0.32480 -0.02397 0.01421  0.01696  286 ILE   A C   
2226 O O   . ILE   A 306 ? 0.27544 0.22719 0.32187 -0.01626 0.03141  0.02897  286 ILE   A O   
2227 C CB  . ILE   A 306 ? 0.27863 0.18588 0.28375 -0.02395 0.04135  -0.01299 286 ILE   A CB  
2228 C CG1 . ILE   A 306 ? 0.27089 0.19576 0.26232 -0.02588 0.03356  0.02061  286 ILE   A CG1 
2229 C CG2 . ILE   A 306 ? 0.31874 0.20723 0.27809 -0.00907 0.03498  -0.03886 286 ILE   A CG2 
2230 C CD1 . ILE   A 306 ? 0.30222 0.18494 0.27811 -0.03741 0.02943  0.04494  286 ILE   A CD1 
2231 N N   . ASN   A 307 ? 0.26053 0.21988 0.33316 -0.02557 -0.01310 0.00315  287 ASN   A N   
2232 C CA  . ASN   A 307 ? 0.29665 0.25598 0.35029 -0.02425 0.00983  0.02202  287 ASN   A CA  
2233 C C   . ASN   A 307 ? 0.32457 0.25074 0.38242 -0.03244 0.00623  0.02156  287 ASN   A C   
2234 O O   . ASN   A 307 ? 0.33599 0.25006 0.40260 -0.01266 0.00889  0.03560  287 ASN   A O   
2235 C CB  . ASN   A 307 ? 0.30769 0.29261 0.35905 0.01109  -0.02255 0.00060  287 ASN   A CB  
2236 C CG  . ASN   A 307 ? 0.37265 0.34170 0.46701 0.02041  0.00961  0.01129  287 ASN   A CG  
2237 O OD1 . ASN   A 307 ? 0.40165 0.36403 0.51198 0.00350  0.00219  0.01102  287 ASN   A OD1 
2238 N ND2 . ASN   A 307 ? 0.39537 0.37425 0.51473 0.04812  0.01236  0.02242  287 ASN   A ND2 
2239 N N   . MET   A 308 ? 0.32918 0.24448 0.35111 -0.04017 0.00767  0.05453  288 MET   A N   
2240 C CA  . MET   A 308 ? 0.36880 0.24076 0.31127 -0.04465 0.02741  0.03906  288 MET   A CA  
2241 C C   . MET   A 308 ? 0.33898 0.24613 0.32309 -0.02904 0.04655  0.03026  288 MET   A C   
2242 O O   . MET   A 308 ? 0.33490 0.26869 0.35484 -0.02304 0.06893  0.01763  288 MET   A O   
2243 C CB  . MET   A 308 ? 0.45377 0.25408 0.34064 -0.05110 0.01102  0.01637  288 MET   A CB  
2244 C CG  . MET   A 308 ? 0.58180 0.31238 0.46881 -0.04244 0.00800  -0.01880 288 MET   A CG  
2245 S SD  . MET   A 308 ? 0.69906 0.37756 0.57049 -0.04462 -0.01594 -0.04277 288 MET   A SD  
2246 C CE  . MET   A 308 ? 0.71725 0.38375 0.56517 -0.03227 -0.01249 0.02036  288 MET   A CE  
2247 N N   . TRP   A 309 ? 0.33138 0.21938 0.30124 -0.00384 0.01686  0.00973  289 TRP   A N   
2248 C CA  . TRP   A 309 ? 0.31261 0.21081 0.29104 -0.00996 0.02319  0.01769  289 TRP   A CA  
2249 C C   . TRP   A 309 ? 0.31592 0.20110 0.32523 0.01337  0.04088  0.02098  289 TRP   A C   
2250 O O   . TRP   A 309 ? 0.30387 0.21378 0.32472 0.00102  0.04289  0.03214  289 TRP   A O   
2251 C CB  . TRP   A 309 ? 0.29457 0.19181 0.28546 -0.01610 0.01851  0.01219  289 TRP   A CB  
2252 C CG  . TRP   A 309 ? 0.31836 0.17252 0.28119 -0.01263 0.02008  0.00110  289 TRP   A CG  
2253 C CD1 . TRP   A 309 ? 0.33119 0.17393 0.24358 -0.01493 0.03710  0.01416  289 TRP   A CD1 
2254 C CD2 . TRP   A 309 ? 0.31367 0.15107 0.29005 -0.02393 0.04450  -0.00384 289 TRP   A CD2 
2255 N NE1 . TRP   A 309 ? 0.33989 0.17220 0.24503 -0.02037 0.01662  -0.02071 289 TRP   A NE1 
2256 C CE2 . TRP   A 309 ? 0.33329 0.14781 0.24242 -0.02150 0.04145  -0.01051 289 TRP   A CE2 
2257 C CE3 . TRP   A 309 ? 0.31148 0.15731 0.29871 -0.00240 0.05891  -0.01826 289 TRP   A CE3 
2258 C CZ2 . TRP   A 309 ? 0.32888 0.13574 0.27451 -0.00832 0.08209  -0.01277 289 TRP   A CZ2 
2259 C CZ3 . TRP   A 309 ? 0.31861 0.13236 0.28822 0.00231  0.03572  0.01928  289 TRP   A CZ3 
2260 C CH2 . TRP   A 309 ? 0.33486 0.13403 0.33123 0.00715  0.03714  0.03004  289 TRP   A CH2 
2261 N N   . VAL   A 310 ? 0.27585 0.18921 0.34534 0.04115  0.05089  0.01889  290 VAL   A N   
2262 C CA  . VAL   A 310 ? 0.30138 0.22565 0.36239 0.03655  0.08250  0.04131  290 VAL   A CA  
2263 C C   . VAL   A 310 ? 0.31220 0.28902 0.37725 0.03243  0.10850  0.05605  290 VAL   A C   
2264 O O   . VAL   A 310 ? 0.33665 0.31497 0.36940 0.02808  0.10379  0.03556  290 VAL   A O   
2265 C CB  . VAL   A 310 ? 0.28554 0.21400 0.36627 0.04311  0.06416  0.03380  290 VAL   A CB  
2266 C CG1 . VAL   A 310 ? 0.33093 0.23284 0.38325 0.04890  0.06433  0.02724  290 VAL   A CG1 
2267 C CG2 . VAL   A 310 ? 0.26823 0.22788 0.33713 0.02152  0.03394  0.01713  290 VAL   A CG2 
2268 N N   . SER   A 311 ? 0.30540 0.31688 0.40414 -0.01013 0.09546  0.08404  291 SER   A N   
2269 C CA  . SER   A 311 ? 0.34175 0.38384 0.43590 -0.03742 0.09235  0.08148  291 SER   A CA  
2270 C C   . SER   A 311 ? 0.37705 0.41279 0.40491 -0.04378 0.05880  0.06952  291 SER   A C   
2271 O O   . SER   A 311 ? 0.37023 0.44554 0.45403 -0.01268 0.05894  0.03666  291 SER   A O   
2272 C CB  . SER   A 311 ? 0.37825 0.42966 0.47083 -0.01691 0.05940  0.08466  291 SER   A CB  
2273 O OG  . SER   A 311 ? 0.42139 0.47721 0.56518 -0.00819 0.05460  0.04309  291 SER   A OG  
2274 N N   . GLN   A 312 ? 0.40573 0.39136 0.40714 -0.06200 0.04732  0.07670  292 GLN   A N   
2275 C CA  . GLN   A 312 ? 0.48777 0.40458 0.39666 -0.08884 0.04255  0.09566  292 GLN   A CA  
2276 C C   . GLN   A 312 ? 0.47380 0.38294 0.40529 -0.08186 0.07251  0.09759  292 GLN   A C   
2277 O O   . GLN   A 312 ? 0.48828 0.41712 0.40310 -0.09952 0.08703  0.11761  292 GLN   A O   
2278 C CB  . GLN   A 312 ? 0.61545 0.45691 0.42841 -0.09959 0.06355  0.03144  292 GLN   A CB  
2279 C CG  . GLN   A 312 ? 0.74259 0.56031 0.52652 -0.06909 0.04707  -0.00350 292 GLN   A CG  
2280 C CD  . GLN   A 312 ? 0.87059 0.62884 0.53750 -0.04401 0.02899  -0.04109 292 GLN   A CD  
2281 O OE1 . GLN   A 312 ? 0.95203 0.64130 0.52327 -0.00805 0.01002  -0.07784 292 GLN   A OE1 
2282 N NE2 . GLN   A 312 ? 0.92179 0.65803 0.61713 -0.05665 0.02966  -0.04175 292 GLN   A NE2 
2283 N N   . ARG   A 313 ? 0.44922 0.31962 0.39702 -0.05364 0.08483  0.07394  293 ARG   A N   
2284 C CA  . ARG   A 313 ? 0.43821 0.28915 0.33715 -0.00847 0.11385  0.04205  293 ARG   A CA  
2285 C C   . ARG   A 313 ? 0.50416 0.31135 0.39211 0.00941  0.15866  0.04570  293 ARG   A C   
2286 O O   . ARG   A 313 ? 0.48970 0.32407 0.44589 0.01050  0.15851  -0.00840 293 ARG   A O   
2287 C CB  . ARG   A 313 ? 0.38790 0.25330 0.33682 0.00351  0.09451  0.03635  293 ARG   A CB  
2288 C CG  . ARG   A 313 ? 0.33730 0.22728 0.33944 0.01080  0.05980  0.02179  293 ARG   A CG  
2289 C CD  . ARG   A 313 ? 0.33212 0.23999 0.32193 -0.00064 0.09197  0.03554  293 ARG   A CD  
2290 N NE  . ARG   A 313 ? 0.36052 0.22885 0.32569 -0.00845 0.06086  0.05359  293 ARG   A NE  
2291 C CZ  . ARG   A 313 ? 0.36357 0.23383 0.32895 -0.02090 0.01826  0.05962  293 ARG   A CZ  
2292 N NH1 . ARG   A 313 ? 0.37034 0.23816 0.37239 -0.01779 0.01311  0.03068  293 ARG   A NH1 
2293 N NH2 . ARG   A 313 ? 0.36511 0.24960 0.31283 -0.01593 0.00605  0.08828  293 ARG   A NH2 
2294 N N   . THR   A 314 ? 0.58687 0.34445 0.44139 0.02854  0.17044  0.02536  294 THR   A N   
2295 C CA  . THR   A 314 ? 0.68148 0.38119 0.49295 0.02046  0.14588  0.00773  294 THR   A CA  
2296 C C   . THR   A 314 ? 0.77711 0.43145 0.60597 -0.00963 0.15772  0.02297  294 THR   A C   
2297 O O   . THR   A 314 ? 0.81966 0.44746 0.69025 -0.01475 0.15594  0.02139  294 THR   A O   
2298 C CB  . THR   A 314 ? 0.68519 0.35916 0.43494 0.02571  0.07096  -0.00920 294 THR   A CB  
2299 O OG1 . THR   A 314 ? 0.71458 0.37758 0.52049 0.04413  0.04278  0.00231  294 THR   A OG1 
2300 C CG2 . THR   A 314 ? 0.65708 0.32560 0.35429 0.01450  0.08145  0.00779  294 THR   A CG2 
2301 N N   . ALA   A 315 ? 0.84555 0.46184 0.65983 -0.03035 0.13113  0.00234  295 ALA   A N   
2302 C CA  . ALA   A 315 ? 0.90372 0.50515 0.75566 -0.04452 0.08454  -0.01118 295 ALA   A CA  
2303 C C   . ALA   A 315 ? 0.93586 0.52718 0.82423 -0.04581 0.05474  0.00105  295 ALA   A C   
2304 O O   . ALA   A 315 ? 0.94663 0.53408 0.85083 -0.04940 0.04807  0.00337  295 ALA   A O   
2305 C CB  . ALA   A 315 ? 0.91034 0.51225 0.74554 -0.05494 0.08037  -0.04482 295 ALA   A CB  
2306 N N1  . A1IIH B .   ? 0.32927 0.23206 0.31823 -0.01480 0.02316  0.01732  401 A1IIH A N1  
2307 C C7  . A1IIH B .   ? 0.43998 0.32237 0.52303 -0.04716 0.13552  0.00495  401 A1IIH A C7  
2308 C C8  . A1IIH B .   ? 0.43627 0.30169 0.50910 -0.02818 0.12158  0.01457  401 A1IIH A C8  
2309 N N2  . A1IIH B .   ? 0.20809 0.17604 0.25077 -0.00378 0.03751  -0.00637 401 A1IIH A N2  
2310 C C9  . A1IIH B .   ? 0.42080 0.29732 0.48355 -0.01909 0.10332  -0.00775 401 A1IIH A C9  
2311 O O1  . A1IIH B .   ? 0.32688 0.25079 0.32350 0.00192  0.01800  0.01307  401 A1IIH A O1  
2312 C C1  . A1IIH B .   ? 0.45048 0.32928 0.62274 -0.00048 0.14266  -0.00814 401 A1IIH A C1  
2313 C C5  . A1IIH B .   ? 0.43171 0.34513 0.55300 -0.01878 0.15175  -0.00528 401 A1IIH A C5  
2314 C C6  . A1IIH B .   ? 0.43205 0.32452 0.53119 -0.02208 0.14539  -0.00104 401 A1IIH A C6  
2315 N N3  . A1IIH B .   ? 0.26252 0.16040 0.22593 0.02904  0.00368  0.01083  401 A1IIH A N3  
2316 C C4  . A1IIH B .   ? 0.43683 0.33021 0.58952 -0.01925 0.14585  0.00637  401 A1IIH A C4  
2317 O O4  . A1IIH B .   ? 0.35649 0.15379 0.25445 0.00770  -0.01940 0.00785  401 A1IIH A O4  
2318 C C3  . A1IIH B .   ? 0.44883 0.33353 0.66662 -0.02183 0.15347  0.01816  401 A1IIH A C3  
2319 O O3  . A1IIH B .   ? 0.29076 0.15191 0.25030 0.00983  -0.00973 -0.00031 401 A1IIH A O3  
2320 C C2  . A1IIH B .   ? 0.42721 0.32082 0.63896 -0.00717 0.14820  -0.00950 401 A1IIH A C2  
2321 N N4  . A1IIH B .   ? 0.29374 0.15007 0.20960 -0.02322 -0.01246 0.01262  401 A1IIH A N4  
2322 N N   . A1IIH B .   ? 0.43721 0.33789 0.61934 -0.01087 0.17285  0.00463  401 A1IIH A N   
2323 C C   . A1IIH B .   ? 0.47431 0.33695 0.65122 0.02542  0.12951  -0.02958 401 A1IIH A C   
2324 O O   . A1IIH B .   ? 0.38093 0.28875 0.32459 -0.01127 0.05390  0.05499  401 A1IIH A O   
2325 B B   . A1IIH B .   ? 0.45291 0.33953 0.61912 -0.01544 0.15254  0.01290  401 A1IIH A B   
2326 C C10 . A1IIH B .   ? 0.40965 0.30046 0.43701 0.00547  0.07408  0.00772  401 A1IIH A C10 
2327 C C11 . A1IIH B .   ? 0.37356 0.28237 0.36783 0.00486  0.03618  -0.00267 401 A1IIH A C11 
2328 C C12 . A1IIH B .   ? 0.33912 0.25310 0.31061 0.01127  0.05513  0.03082  401 A1IIH A C12 
2329 C C13 . A1IIH B .   ? 0.35135 0.24682 0.33197 0.00298  0.03606  0.00691  401 A1IIH A C13 
2330 C C14 . A1IIH B .   ? 0.35431 0.25410 0.33513 -0.02601 0.01249  0.02621  401 A1IIH A C14 
2331 C C15 . A1IIH B .   ? 0.29351 0.25744 0.33630 -0.01185 -0.01467 -0.04921 401 A1IIH A C15 
2332 C C16 . A1IIH B .   ? 0.30094 0.25688 0.38493 -0.01899 -0.01120 -0.05680 401 A1IIH A C16 
2333 C C17 . A1IIH B .   ? 0.31461 0.25757 0.40811 -0.01477 -0.01130 -0.05839 401 A1IIH A C17 
2334 C C18 . A1IIH B .   ? 0.28584 0.25551 0.38185 -0.03394 -0.01488 -0.06625 401 A1IIH A C18 
2335 C C19 . A1IIH B .   ? 0.26493 0.25670 0.32810 -0.00179 -0.01595 -0.05692 401 A1IIH A C19 
2336 C C20 . A1IIH B .   ? 0.24308 0.23654 0.35251 -0.00551 -0.03470 -0.04390 401 A1IIH A C20 
2337 C C21 . A1IIH B .   ? 0.20638 0.21511 0.32577 0.00743  -0.00247 -0.00922 401 A1IIH A C21 
2338 C C22 . A1IIH B .   ? 0.18078 0.19363 0.30370 0.01543  -0.00529 -0.00021 401 A1IIH A C22 
2339 C C23 . A1IIH B .   ? 0.19114 0.18460 0.29133 0.00805  -0.03184 -0.01047 401 A1IIH A C23 
2340 C C24 . A1IIH B .   ? 0.16980 0.19401 0.27406 0.00161  0.01666  0.01638  401 A1IIH A C24 
2341 C C25 . A1IIH B .   ? 0.17024 0.19372 0.28675 -0.00698 0.00534  0.00406  401 A1IIH A C25 
2342 C C26 . A1IIH B .   ? 0.20195 0.19983 0.26124 -0.01190 0.03171  0.01985  401 A1IIH A C26 
2343 C C27 . A1IIH B .   ? 0.19963 0.18815 0.25878 0.00480  -0.01011 0.00901  401 A1IIH A C27 
2344 C C28 . A1IIH B .   ? 0.25179 0.15846 0.21234 0.01094  0.02649  0.02005  401 A1IIH A C28 
2345 C C29 . A1IIH B .   ? 0.26269 0.16769 0.19407 0.03424  -0.00669 0.02176  401 A1IIH A C29 
2346 C C30 . A1IIH B .   ? 0.26127 0.15129 0.22021 0.00719  -0.02363 0.02444  401 A1IIH A C30 
2347 C C31 . A1IIH B .   ? 0.29591 0.17178 0.24292 0.02329  -0.00918 0.02515  401 A1IIH A C31 
2348 C C32 . A1IIH B .   ? 0.31393 0.14664 0.21571 -0.00365 -0.00274 0.01846  401 A1IIH A C32 
2349 C C33 . A1IIH B .   ? 0.26946 0.18113 0.25378 0.03185  -0.02035 0.03085  401 A1IIH A C33 
2350 C C34 . A1IIH B .   ? 0.46995 0.32928 0.71221 -0.01987 0.13563  0.02917  401 A1IIH A C34 
2351 F F   . A1IIH B .   ? 0.45647 0.34375 0.66252 -0.07577 0.11869  -0.04728 401 A1IIH A F   
2352 F F1  . A1IIH B .   ? 0.48930 0.36007 0.64494 0.01362  0.17214  0.08848  401 A1IIH A F1  
2353 N N5  . A1IIH B .   ? 0.42748 0.32170 0.53573 -0.01197 0.14114  -0.01504 401 A1IIH A N5  
2354 O O2  . A1IIH B .   ? 0.27597 0.14807 0.22071 0.01778  0.01824  0.01879  401 A1IIH A O2  
# 
