data_8RVF
# 
_entry.id   8RVF 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.403 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
_database_2.pdbx_database_accession 
_database_2.pdbx_DOI 
PDB   8RVF         pdb_00008rvf 10.2210/pdb8rvf/pdb 
WWPDB D_1292136260 ?            ?                   
# 
loop_
_pdbx_audit_revision_history.ordinal 
_pdbx_audit_revision_history.data_content_type 
_pdbx_audit_revision_history.major_revision 
_pdbx_audit_revision_history.minor_revision 
_pdbx_audit_revision_history.revision_date 
_pdbx_audit_revision_history.part_number 
1 'Structure model' 1 0 2025-02-12 ? 
2 'Structure model' 1 1 2025-04-02 ? 
3 'Structure model' 1 2 2025-04-09 ? 
# 
_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             ? 
# 
loop_
_pdbx_audit_revision_group.ordinal 
_pdbx_audit_revision_group.revision_ordinal 
_pdbx_audit_revision_group.data_content_type 
_pdbx_audit_revision_group.group 
1 2 'Structure model' 'Database references' 
2 3 'Structure model' 'Database references' 
# 
loop_
_pdbx_audit_revision_category.ordinal 
_pdbx_audit_revision_category.revision_ordinal 
_pdbx_audit_revision_category.data_content_type 
_pdbx_audit_revision_category.category 
1 2 'Structure model' citation        
2 2 'Structure model' citation_author 
3 3 'Structure model' citation        
4 3 'Structure model' citation_author 
# 
loop_
_pdbx_audit_revision_item.ordinal 
_pdbx_audit_revision_item.revision_ordinal 
_pdbx_audit_revision_item.data_content_type 
_pdbx_audit_revision_item.item 
1  2 'Structure model' '_citation.country'                 
2  2 'Structure model' '_citation.journal_abbrev'          
3  2 'Structure model' '_citation.journal_id_ASTM'         
4  2 'Structure model' '_citation.journal_id_CSD'          
5  2 'Structure model' '_citation.journal_id_ISSN'         
6  2 'Structure model' '_citation.pdbx_database_id_DOI'    
7  2 'Structure model' '_citation.pdbx_database_id_PubMed' 
8  2 'Structure model' '_citation.title'                   
9  2 'Structure model' '_citation.year'                    
10 3 'Structure model' '_citation.journal_volume'          
11 3 'Structure model' '_citation.page_first'              
12 3 'Structure model' '_citation.page_last'               
13 3 'Structure model' '_citation_author.identifier_ORCID' 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        8RVF 
_pdbx_database_status.recvd_initial_deposition_date   2024-02-01 
_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 
'Leibrock, L.' 1 ? 
'Hentsch, A.'  2 ? 
'Nazare, M.'   3 ? 
'Grether, U.'  4 ? 
'Kuhn, B.'     5 ? 
'Blaising, J.' 6 ? 
'Benz, J.'     7 ? 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   US 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            J.Am.Chem.Soc. 
_citation.journal_id_ASTM           JACSAT 
_citation.journal_id_CSD            ? 
_citation.journal_id_ISSN           1520-5126 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            147 
_citation.language                  ? 
_citation.page_first                10188 
_citation.page_last                 10202 
_citation.title                     
'Highly Specific Miniaturized Fluorescent Monoacylglycerol Lipase Probes Enable Translational Research.' 
_citation.year                      2025 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1021/jacs.4c15223 
_citation.pdbx_database_id_PubMed   40063733 
_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  ? 
primary 'Guberman, M.'      2  ? 
primary 'Radetzki, S.'      3  ? 
primary 'Kaushik, S.'       4  ? 
primary 'Huizenga, M.'      5  ? 
primary 'He, Y.'            6  ? 
primary 'Contzen, J.'       7  ? 
primary 'Kuhn, B.'          8  ? 
primary 'Benz, J.'          9  ? 
primary 'Schippers, M.'     10 ? 
primary 'Paul, J.'          11 ? 
primary 'Leibrock, L.'      12 ? 
primary 'Collin, L.'        13 ? 
primary 'Wittwer, M.'       14 ? 
primary 'Topp, A.'          15 ? 
primary 
;O'Hara, F.
;
16 ? 
primary 'Heer, D.'          17 ? 
primary 'Hochstrasser, R.'  18 ? 
primary 'Blaising, J.'      19 ? 
primary 'von Kries, J.P.'   20 ? 
primary 'Mu, L.'            21 ? 
primary 'van der Stelt, M.' 22 ? 
primary 'Mergenthaler, P.'  23 ? 
primary 'Lipstein, N.'      24 ? 
primary 'Grether, U.'       25 ? 
primary 'Nazare, M.'        26 ? 
# 
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 
;[6-[[2,2-bis(fluoranyl)-1$l^{4},3-diaza-2$l^{4}-boratricyclo[7.3.0.0^{3,7}]dodeca-1(12),4,6,8,10-pentaen-8-yl]methyl]-2-azaspiro[3.3]heptan-2-yl]-[6-(3-cyclopropyl-1,2,4-triazol-1-yl)-2-azaspiro[3.3]heptan-2-yl]methanone
;
531.408   1   ?        ? ? ? 
3 non-polymer syn 1,2-ETHANEDIOL 62.068    3   ?        ? ? ? 
4 water       nat water 18.015    307 ?        ? ? ? 
# 
_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 
;[6-[[2,2-bis(fluoranyl)-1$l^{4},3-diaza-2$l^{4}-boratricyclo[7.3.0.0^{3,7}]dodeca-1(12),4,6,8,10-pentaen-8-yl]methyl]-2-azaspiro[3.3]heptan-2-yl]-[6-(3-cyclopropyl-1,2,4-triazol-1-yl)-2-azaspiro[3.3]heptan-2-yl]methanone
;
A1H35 
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 
A1H35 non-polymer         . 
;[6-[[2,2-bis(fluoranyl)-1$l^{4},3-diaza-2$l^{4}-boratricyclo[7.3.0.0^{3,7}]dodeca-1(12),4,6,8,10-pentaen-8-yl]methyl]-2-azaspiro[3.3]heptan-2-yl]-[6-(3-cyclopropyl-1,2,4-triazol-1-yl)-2-azaspiro[3.3]heptan-2-yl]methanone
;
?                 'C28 H32 B F2 N7 O 1' 531.408 
ALA   'L-peptide linking' y ALANINE ?                 'C3 H7 N O2'          89.093  
ARG   'L-peptide linking' y ARGININE ?                 'C6 H15 N4 O2 1'      175.209 
ASN   'L-peptide linking' y ASPARAGINE ?                 'C4 H8 N2 O3'         132.118 
ASP   'L-peptide linking' y 'ASPARTIC ACID' ?                 'C4 H7 N O4'          133.103 
CYS   'L-peptide linking' y CYSTEINE ?                 'C3 H7 N O2 S'        121.158 
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        A1H35 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1H35 
_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 A1H35 1   401 301 A1H35 XXX A . 
C 3 EDO   1   402 2   EDO   EDO A . 
D 3 EDO   1   403 3   EDO   EDO A . 
E 3 EDO   1   404 4   EDO   EDO A . 
F 4 HOH   1   501 39  HOH   HOH A . 
F 4 HOH   2   502 388 HOH   HOH A . 
F 4 HOH   3   503 382 HOH   HOH A . 
F 4 HOH   4   504 48  HOH   HOH A . 
F 4 HOH   5   505 46  HOH   HOH A . 
F 4 HOH   6   506 101 HOH   HOH A . 
F 4 HOH   7   507 11  HOH   HOH A . 
F 4 HOH   8   508 47  HOH   HOH A . 
F 4 HOH   9   509 113 HOH   HOH A . 
F 4 HOH   10  510 305 HOH   HOH A . 
F 4 HOH   11  511 29  HOH   HOH A . 
F 4 HOH   12  512 127 HOH   HOH A . 
F 4 HOH   13  513 30  HOH   HOH A . 
F 4 HOH   14  514 75  HOH   HOH A . 
F 4 HOH   15  515 162 HOH   HOH A . 
F 4 HOH   16  516 84  HOH   HOH A . 
F 4 HOH   17  517 294 HOH   HOH A . 
F 4 HOH   18  518 118 HOH   HOH A . 
F 4 HOH   19  519 163 HOH   HOH A . 
F 4 HOH   20  520 395 HOH   HOH A . 
F 4 HOH   21  521 7   HOH   HOH A . 
F 4 HOH   22  522 18  HOH   HOH A . 
F 4 HOH   23  523 393 HOH   HOH A . 
F 4 HOH   24  524 138 HOH   HOH A . 
F 4 HOH   25  525 33  HOH   HOH A . 
F 4 HOH   26  526 10  HOH   HOH A . 
F 4 HOH   27  527 23  HOH   HOH A . 
F 4 HOH   28  528 291 HOH   HOH A . 
F 4 HOH   29  529 41  HOH   HOH A . 
F 4 HOH   30  530 26  HOH   HOH A . 
F 4 HOH   31  531 16  HOH   HOH A . 
F 4 HOH   32  532 36  HOH   HOH A . 
F 4 HOH   33  533 63  HOH   HOH A . 
F 4 HOH   34  534 397 HOH   HOH A . 
F 4 HOH   35  535 82  HOH   HOH A . 
F 4 HOH   36  536 165 HOH   HOH A . 
F 4 HOH   37  537 88  HOH   HOH A . 
F 4 HOH   38  538 229 HOH   HOH A . 
F 4 HOH   39  539 25  HOH   HOH A . 
F 4 HOH   40  540 71  HOH   HOH A . 
F 4 HOH   41  541 219 HOH   HOH A . 
F 4 HOH   42  542 57  HOH   HOH A . 
F 4 HOH   43  543 67  HOH   HOH A . 
F 4 HOH   44  544 21  HOH   HOH A . 
F 4 HOH   45  545 131 HOH   HOH A . 
F 4 HOH   46  546 95  HOH   HOH A . 
F 4 HOH   47  547 65  HOH   HOH A . 
F 4 HOH   48  548 12  HOH   HOH A . 
F 4 HOH   49  549 104 HOH   HOH A . 
F 4 HOH   50  550 5   HOH   HOH A . 
F 4 HOH   51  551 20  HOH   HOH A . 
F 4 HOH   52  552 216 HOH   HOH A . 
F 4 HOH   53  553 203 HOH   HOH A . 
F 4 HOH   54  554 141 HOH   HOH A . 
F 4 HOH   55  555 252 HOH   HOH A . 
F 4 HOH   56  556 31  HOH   HOH A . 
F 4 HOH   57  557 79  HOH   HOH A . 
F 4 HOH   58  558 55  HOH   HOH A . 
F 4 HOH   59  559 68  HOH   HOH A . 
F 4 HOH   60  560 59  HOH   HOH A . 
F 4 HOH   61  561 392 HOH   HOH A . 
F 4 HOH   62  562 185 HOH   HOH A . 
F 4 HOH   63  563 44  HOH   HOH A . 
F 4 HOH   64  564 64  HOH   HOH A . 
F 4 HOH   65  565 70  HOH   HOH A . 
F 4 HOH   66  566 287 HOH   HOH A . 
F 4 HOH   67  567 83  HOH   HOH A . 
F 4 HOH   68  568 14  HOH   HOH A . 
F 4 HOH   69  569 69  HOH   HOH A . 
F 4 HOH   70  570 4   HOH   HOH A . 
F 4 HOH   71  571 183 HOH   HOH A . 
F 4 HOH   72  572 3   HOH   HOH A . 
F 4 HOH   73  573 94  HOH   HOH A . 
F 4 HOH   74  574 385 HOH   HOH A . 
F 4 HOH   75  575 266 HOH   HOH A . 
F 4 HOH   76  576 293 HOH   HOH A . 
F 4 HOH   77  577 206 HOH   HOH A . 
F 4 HOH   78  578 126 HOH   HOH A . 
F 4 HOH   79  579 34  HOH   HOH A . 
F 4 HOH   80  580 45  HOH   HOH A . 
F 4 HOH   81  581 148 HOH   HOH A . 
F 4 HOH   82  582 89  HOH   HOH A . 
F 4 HOH   83  583 100 HOH   HOH A . 
F 4 HOH   84  584 6   HOH   HOH A . 
F 4 HOH   85  585 130 HOH   HOH A . 
F 4 HOH   86  586 43  HOH   HOH A . 
F 4 HOH   87  587 174 HOH   HOH A . 
F 4 HOH   88  588 177 HOH   HOH A . 
F 4 HOH   89  589 386 HOH   HOH A . 
F 4 HOH   90  590 396 HOH   HOH A . 
F 4 HOH   91  591 8   HOH   HOH A . 
F 4 HOH   92  592 54  HOH   HOH A . 
F 4 HOH   93  593 42  HOH   HOH A . 
F 4 HOH   94  594 24  HOH   HOH A . 
F 4 HOH   95  595 188 HOH   HOH A . 
F 4 HOH   96  596 107 HOH   HOH A . 
F 4 HOH   97  597 92  HOH   HOH A . 
F 4 HOH   98  598 184 HOH   HOH A . 
F 4 HOH   99  599 110 HOH   HOH A . 
F 4 HOH   100 600 136 HOH   HOH A . 
F 4 HOH   101 601 81  HOH   HOH A . 
F 4 HOH   102 602 78  HOH   HOH A . 
F 4 HOH   103 603 323 HOH   HOH A . 
F 4 HOH   104 604 144 HOH   HOH A . 
F 4 HOH   105 605 17  HOH   HOH A . 
F 4 HOH   106 606 122 HOH   HOH A . 
F 4 HOH   107 607 28  HOH   HOH A . 
F 4 HOH   108 608 333 HOH   HOH A . 
F 4 HOH   109 609 120 HOH   HOH A . 
F 4 HOH   110 610 103 HOH   HOH A . 
F 4 HOH   111 611 306 HOH   HOH A . 
F 4 HOH   112 612 399 HOH   HOH A . 
F 4 HOH   113 613 157 HOH   HOH A . 
F 4 HOH   114 614 15  HOH   HOH A . 
F 4 HOH   115 615 390 HOH   HOH A . 
F 4 HOH   116 616 121 HOH   HOH A . 
F 4 HOH   117 617 161 HOH   HOH A . 
F 4 HOH   118 618 80  HOH   HOH A . 
F 4 HOH   119 619 72  HOH   HOH A . 
F 4 HOH   120 620 394 HOH   HOH A . 
F 4 HOH   121 621 13  HOH   HOH A . 
F 4 HOH   122 622 265 HOH   HOH A . 
F 4 HOH   123 623 264 HOH   HOH A . 
F 4 HOH   124 624 117 HOH   HOH A . 
F 4 HOH   125 625 263 HOH   HOH A . 
F 4 HOH   126 626 230 HOH   HOH A . 
F 4 HOH   127 627 209 HOH   HOH A . 
F 4 HOH   128 628 304 HOH   HOH A . 
F 4 HOH   129 629 119 HOH   HOH A . 
F 4 HOH   130 630 154 HOH   HOH A . 
F 4 HOH   131 631 150 HOH   HOH A . 
F 4 HOH   132 632 51  HOH   HOH A . 
F 4 HOH   133 633 49  HOH   HOH A . 
F 4 HOH   134 634 99  HOH   HOH A . 
F 4 HOH   135 635 22  HOH   HOH A . 
F 4 HOH   136 636 204 HOH   HOH A . 
F 4 HOH   137 637 218 HOH   HOH A . 
F 4 HOH   138 638 225 HOH   HOH A . 
F 4 HOH   139 639 344 HOH   HOH A . 
F 4 HOH   140 640 156 HOH   HOH A . 
F 4 HOH   141 641 142 HOH   HOH A . 
F 4 HOH   142 642 111 HOH   HOH A . 
F 4 HOH   143 643 93  HOH   HOH A . 
F 4 HOH   144 644 38  HOH   HOH A . 
F 4 HOH   145 645 164 HOH   HOH A . 
F 4 HOH   146 646 91  HOH   HOH A . 
F 4 HOH   147 647 215 HOH   HOH A . 
F 4 HOH   148 648 373 HOH   HOH A . 
F 4 HOH   149 649 140 HOH   HOH A . 
F 4 HOH   150 650 189 HOH   HOH A . 
F 4 HOH   151 651 32  HOH   HOH A . 
F 4 HOH   152 652 232 HOH   HOH A . 
F 4 HOH   153 653 378 HOH   HOH A . 
F 4 HOH   154 654 87  HOH   HOH A . 
F 4 HOH   155 655 247 HOH   HOH A . 
F 4 HOH   156 656 268 HOH   HOH A . 
F 4 HOH   157 657 169 HOH   HOH A . 
F 4 HOH   158 658 281 HOH   HOH A . 
F 4 HOH   159 659 56  HOH   HOH A . 
F 4 HOH   160 660 135 HOH   HOH A . 
F 4 HOH   161 661 58  HOH   HOH A . 
F 4 HOH   162 662 338 HOH   HOH A . 
F 4 HOH   163 663 158 HOH   HOH A . 
F 4 HOH   164 664 128 HOH   HOH A . 
F 4 HOH   165 665 9   HOH   HOH A . 
F 4 HOH   166 666 251 HOH   HOH A . 
F 4 HOH   167 667 53  HOH   HOH A . 
F 4 HOH   168 668 245 HOH   HOH A . 
F 4 HOH   169 669 159 HOH   HOH A . 
F 4 HOH   170 670 186 HOH   HOH A . 
F 4 HOH   171 671 62  HOH   HOH A . 
F 4 HOH   172 672 143 HOH   HOH A . 
F 4 HOH   173 673 125 HOH   HOH A . 
F 4 HOH   174 674 109 HOH   HOH A . 
F 4 HOH   175 675 85  HOH   HOH A . 
F 4 HOH   176 676 74  HOH   HOH A . 
F 4 HOH   177 677 66  HOH   HOH A . 
F 4 HOH   178 678 90  HOH   HOH A . 
F 4 HOH   179 679 221 HOH   HOH A . 
F 4 HOH   180 680 257 HOH   HOH A . 
F 4 HOH   181 681 115 HOH   HOH A . 
F 4 HOH   182 682 176 HOH   HOH A . 
F 4 HOH   183 683 61  HOH   HOH A . 
F 4 HOH   184 684 116 HOH   HOH A . 
F 4 HOH   185 685 195 HOH   HOH A . 
F 4 HOH   186 686 96  HOH   HOH A . 
F 4 HOH   187 687 200 HOH   HOH A . 
F 4 HOH   188 688 318 HOH   HOH A . 
F 4 HOH   189 689 180 HOH   HOH A . 
F 4 HOH   190 690 222 HOH   HOH A . 
F 4 HOH   191 691 358 HOH   HOH A . 
F 4 HOH   192 692 210 HOH   HOH A . 
F 4 HOH   193 693 240 HOH   HOH A . 
F 4 HOH   194 694 398 HOH   HOH A . 
F 4 HOH   195 695 363 HOH   HOH A . 
F 4 HOH   196 696 192 HOH   HOH A . 
F 4 HOH   197 697 76  HOH   HOH A . 
F 4 HOH   198 698 98  HOH   HOH A . 
F 4 HOH   199 699 241 HOH   HOH A . 
F 4 HOH   200 700 35  HOH   HOH A . 
F 4 HOH   201 701 133 HOH   HOH A . 
F 4 HOH   202 702 52  HOH   HOH A . 
F 4 HOH   203 703 187 HOH   HOH A . 
F 4 HOH   204 704 208 HOH   HOH A . 
F 4 HOH   205 705 97  HOH   HOH A . 
F 4 HOH   206 706 178 HOH   HOH A . 
F 4 HOH   207 707 340 HOH   HOH A . 
F 4 HOH   208 708 227 HOH   HOH A . 
F 4 HOH   209 709 343 HOH   HOH A . 
F 4 HOH   210 710 231 HOH   HOH A . 
F 4 HOH   211 711 348 HOH   HOH A . 
F 4 HOH   212 712 106 HOH   HOH A . 
F 4 HOH   213 713 275 HOH   HOH A . 
F 4 HOH   214 714 380 HOH   HOH A . 
F 4 HOH   215 715 151 HOH   HOH A . 
F 4 HOH   216 716 223 HOH   HOH A . 
F 4 HOH   217 717 290 HOH   HOH A . 
F 4 HOH   218 718 242 HOH   HOH A . 
F 4 HOH   219 719 108 HOH   HOH A . 
F 4 HOH   220 720 175 HOH   HOH A . 
F 4 HOH   221 721 350 HOH   HOH A . 
F 4 HOH   222 722 244 HOH   HOH A . 
F 4 HOH   223 723 168 HOH   HOH A . 
F 4 HOH   224 724 259 HOH   HOH A . 
F 4 HOH   225 725 325 HOH   HOH A . 
F 4 HOH   226 726 319 HOH   HOH A . 
F 4 HOH   227 727 345 HOH   HOH A . 
F 4 HOH   228 728 191 HOH   HOH A . 
F 4 HOH   229 729 166 HOH   HOH A . 
F 4 HOH   230 730 213 HOH   HOH A . 
F 4 HOH   231 731 217 HOH   HOH A . 
F 4 HOH   232 732 316 HOH   HOH A . 
F 4 HOH   233 733 132 HOH   HOH A . 
F 4 HOH   234 734 309 HOH   HOH A . 
F 4 HOH   235 735 365 HOH   HOH A . 
F 4 HOH   236 736 207 HOH   HOH A . 
F 4 HOH   237 737 250 HOH   HOH A . 
F 4 HOH   238 738 256 HOH   HOH A . 
F 4 HOH   239 739 296 HOH   HOH A . 
F 4 HOH   240 740 198 HOH   HOH A . 
F 4 HOH   241 741 357 HOH   HOH A . 
F 4 HOH   242 742 145 HOH   HOH A . 
F 4 HOH   243 743 249 HOH   HOH A . 
F 4 HOH   244 744 313 HOH   HOH A . 
F 4 HOH   245 745 315 HOH   HOH A . 
F 4 HOH   246 746 302 HOH   HOH A . 
F 4 HOH   247 747 134 HOH   HOH A . 
F 4 HOH   248 748 269 HOH   HOH A . 
F 4 HOH   249 749 360 HOH   HOH A . 
F 4 HOH   250 750 60  HOH   HOH A . 
F 4 HOH   251 751 285 HOH   HOH A . 
F 4 HOH   252 752 212 HOH   HOH A . 
F 4 HOH   253 753 254 HOH   HOH A . 
F 4 HOH   254 754 73  HOH   HOH A . 
F 4 HOH   255 755 328 HOH   HOH A . 
F 4 HOH   256 756 300 HOH   HOH A . 
F 4 HOH   257 757 124 HOH   HOH A . 
F 4 HOH   258 758 201 HOH   HOH A . 
F 4 HOH   259 759 321 HOH   HOH A . 
F 4 HOH   260 760 173 HOH   HOH A . 
F 4 HOH   261 761 391 HOH   HOH A . 
F 4 HOH   262 762 288 HOH   HOH A . 
F 4 HOH   263 763 214 HOH   HOH A . 
F 4 HOH   264 764 171 HOH   HOH A . 
F 4 HOH   265 765 234 HOH   HOH A . 
F 4 HOH   266 766 199 HOH   HOH A . 
F 4 HOH   267 767 387 HOH   HOH A . 
F 4 HOH   268 768 237 HOH   HOH A . 
F 4 HOH   269 769 37  HOH   HOH A . 
F 4 HOH   270 770 301 HOH   HOH A . 
F 4 HOH   271 771 137 HOH   HOH A . 
F 4 HOH   272 772 102 HOH   HOH A . 
F 4 HOH   273 773 389 HOH   HOH A . 
F 4 HOH   274 774 377 HOH   HOH A . 
F 4 HOH   275 775 308 HOH   HOH A . 
F 4 HOH   276 776 172 HOH   HOH A . 
F 4 HOH   277 777 271 HOH   HOH A . 
F 4 HOH   278 778 341 HOH   HOH A . 
F 4 HOH   279 779 239 HOH   HOH A . 
F 4 HOH   280 780 202 HOH   HOH A . 
F 4 HOH   281 781 336 HOH   HOH A . 
F 4 HOH   282 782 179 HOH   HOH A . 
F 4 HOH   283 783 272 HOH   HOH A . 
F 4 HOH   284 784 361 HOH   HOH A . 
F 4 HOH   285 785 299 HOH   HOH A . 
F 4 HOH   286 786 347 HOH   HOH A . 
F 4 HOH   287 787 129 HOH   HOH A . 
F 4 HOH   288 788 190 HOH   HOH A . 
F 4 HOH   289 789 220 HOH   HOH A . 
F 4 HOH   290 790 182 HOH   HOH A . 
F 4 HOH   291 791 354 HOH   HOH A . 
F 4 HOH   292 792 123 HOH   HOH A . 
F 4 HOH   293 793 383 HOH   HOH A . 
F 4 HOH   294 794 147 HOH   HOH A . 
F 4 HOH   295 795 359 HOH   HOH A . 
F 4 HOH   296 796 193 HOH   HOH A . 
F 4 HOH   297 797 276 HOH   HOH A . 
F 4 HOH   298 798 155 HOH   HOH A . 
F 4 HOH   299 799 170 HOH   HOH A . 
F 4 HOH   300 800 160 HOH   HOH A . 
F 4 HOH   301 801 112 HOH   HOH A . 
F 4 HOH   302 802 282 HOH   HOH A . 
F 4 HOH   303 803 235 HOH   HOH A . 
F 4 HOH   304 804 181 HOH   HOH A . 
F 4 HOH   305 805 352 HOH   HOH A . 
F 4 HOH   306 806 320 HOH   HOH A . 
F 4 HOH   307 807 298 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       ? ? ? ? ? ? ? ? ? ? ? BUSTER ? ? ? 2.11.8 1 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? XDS    ? ? ? .      2 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? SADABS ? ? ? .      3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHASER ? ? ? .      4 
# 
_cell.angle_alpha                  90 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     8RVF 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     90.446 
_cell.length_a_esd                 ? 
_cell.length_b                     127.312 
_cell.length_b_esd                 ? 
_cell.length_c                     62.845 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        8 
_cell.reciprocal_angle_alpha       ? 
_cell.reciprocal_angle_beta        ? 
_cell.reciprocal_angle_gamma       ? 
_cell.reciprocal_angle_alpha_esd   ? 
_cell.reciprocal_angle_beta_esd    ? 
_cell.reciprocal_angle_gamma_esd   ? 
_cell.reciprocal_length_a          ? 
_cell.reciprocal_length_b          ? 
_cell.reciprocal_length_c          ? 
_cell.reciprocal_length_a_esd      ? 
_cell.reciprocal_length_b_esd      ? 
_cell.reciprocal_length_c_esd      ? 
_cell.pdbx_unique_axis             ? 
_cell.pdbx_esd_method              ? 
# 
_symmetry.entry_id                         8RVF 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                20 
_symmetry.space_group_name_Hall            ? 
_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                   8RVF 
_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             2.55 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          51.78 
_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    '0.1M MES pH 6.5, 11% PEG MME5K, 12% isopropanol' 
_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 EIGER2 S 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         2021-12-17 
_diffrn_detector.pdbx_frequency               ? 
_diffrn_detector.id                           ? 
_diffrn_detector.number_of_axes               ? 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   1.00000 
_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                        'SLS BEAMLINE X10SA' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        1.00000 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   X10SA 
_diffrn_source.pdbx_synchrotron_site       SLS 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       8RVF 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.43 
_reflns.d_resolution_low                               20.18 
_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                                     67210 
_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                           100 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                7.47 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          8.34 
_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                                   0.99 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.078 
_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                                    1.43 
_reflns_shell.d_res_low                                     1.53 
_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                             12202 
_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                                  0.661 
_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                                  1.00 
_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]                            -5.9126 
_refine.aniso_B[1][2]                            0 
_refine.aniso_B[1][3]                            0 
_refine.aniso_B[2][2]                            4.1436 
_refine.aniso_B[2][3]                            0 
_refine.aniso_B[3][3]                            1.7691 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               36.25 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               0.967 
_refine.correlation_coeff_Fo_to_Fc_free          0.961 
_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                                 8RVF 
_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                            1.43 
_refine.ls_d_res_low                             63.66 
_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                     67130 
_refine.ls_number_reflns_R_free                  3354 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.9 
_refine.ls_percent_reflns_R_free                 ? 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1948 
_refine.ls_R_factor_R_free                       0.2220 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1935 
_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                    ? 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          ? 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               THROUGHOUT 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       ? 
_refine.pdbx_R_Free_selection_details            RANDOM 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             ? 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             ? 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 ? 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   0.063 
_refine.pdbx_overall_SU_R_free_Blow_DPI          0.066 
_refine.pdbx_overall_SU_R_Blow_DPI               0.063 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_diffrn_id                           1 
_refine.overall_SU_B                             ? 
_refine.overall_SU_ML                            ? 
_refine.overall_SU_R_Cruickshank_DPI             0.06 
_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_analyze.entry_id                        8RVF 
_refine_analyze.pdbx_refine_id                  'X-RAY DIFFRACTION' 
_refine_analyze.Luzzati_coordinate_error_free   ? 
_refine_analyze.Luzzati_coordinate_error_obs    0.25 
_refine_analyze.Luzzati_d_res_low_free          ? 
_refine_analyze.Luzzati_d_res_low_obs           ? 
_refine_analyze.Luzzati_sigma_a_free            ? 
_refine_analyze.Luzzati_sigma_a_free_details    ? 
_refine_analyze.Luzzati_sigma_a_obs             ? 
_refine_analyze.Luzzati_sigma_a_obs_details     ? 
_refine_analyze.number_disordered_residues      ? 
_refine_analyze.occupancy_sum_hydrogen          ? 
_refine_analyze.occupancy_sum_non_hydrogen      ? 
_refine_analyze.RG_d_res_high                   ? 
_refine_analyze.RG_d_res_low                    ? 
_refine_analyze.RG_free                         ? 
_refine_analyze.RG_work                         ? 
_refine_analyze.RG_free_work_ratio              ? 
_refine_analyze.pdbx_Luzzati_d_res_high_obs     ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       1.43 
_refine_hist.d_res_low                        63.66 
_refine_hist.number_atoms_solvent             307 
_refine_hist.number_atoms_total               2602 
_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         51 
_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' ? 0.011 ? 2448 ? t_bond_d                  2  HARMONIC     
'X-RAY DIFFRACTION' ? 1.07  ? 3358 ? t_angle_deg               2  HARMONIC     
'X-RAY DIFFRACTION' ? ?     ? 869  ? t_dihedral_angle_d        2  SINUSOIDAL   
'X-RAY DIFFRACTION' ? ?     ? 445  ? t_gen_planes              5  HARMONIC     
'X-RAY DIFFRACTION' ? ?     ? 2448 ? t_it                      10 HARMONIC     
'X-RAY DIFFRACTION' ? ?     ? 308  ? t_chiral_improper_torsion 5  SEMIHARMONIC 
'X-RAY DIFFRACTION' ? ?     ? 2501 ? t_ideal_dist_contact      4  SEMIHARMONIC 
'X-RAY DIFFRACTION' ? 3.66  ? ?    ? t_omega_torsion           ?  ?            
'X-RAY DIFFRACTION' ? 15.85 ? ?    ? t_other_torsion           ?  ?            
# 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.d_res_high                       1.43 
_refine_ls_shell.d_res_low                        1.44 
_refine_ls_shell.number_reflns_all                ? 
_refine_ls_shell.number_reflns_obs                1343 
_refine_ls_shell.number_reflns_R_free             74 
_refine_ls_shell.number_reflns_R_work             ? 
_refine_ls_shell.percent_reflns_obs               99.85 
_refine_ls_shell.percent_reflns_R_free            ? 
_refine_ls_shell.R_factor_all                     ? 
_refine_ls_shell.R_factor_obs                     0.4822 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.R_factor_R_work                  0.4831 
_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                  0.466 
# 
_struct.entry_id                     8RVF 
_struct.title                        'CRYSTAL STRUCTURE OF HUMAN MONOGLYCERIDE LIPASE IN COMPLEX WITH COMPOUND 5' 
_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        8RVF 
_struct_keywords.text            'ALPHA/BETA HYDROLASE, 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 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              8RVF 
_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 8RVF MET A 1   ? UNP Q99685 ?   ?   'initiating methionine' -19 1  
1 8RVF GLY A 2   ? UNP Q99685 ?   ?   'expression tag'        -18 2  
1 8RVF SER A 3   ? UNP Q99685 ?   ?   'expression tag'        -17 3  
1 8RVF SER A 4   ? UNP Q99685 ?   ?   'expression tag'        -16 4  
1 8RVF HIS A 5   ? UNP Q99685 ?   ?   'expression tag'        -15 5  
1 8RVF HIS A 6   ? UNP Q99685 ?   ?   'expression tag'        -14 6  
1 8RVF HIS A 7   ? UNP Q99685 ?   ?   'expression tag'        -13 7  
1 8RVF HIS A 8   ? UNP Q99685 ?   ?   'expression tag'        -12 8  
1 8RVF HIS A 9   ? UNP Q99685 ?   ?   'expression tag'        -11 9  
1 8RVF HIS A 10  ? UNP Q99685 ?   ?   'expression tag'        -10 10 
1 8RVF SER A 11  ? UNP Q99685 ?   ?   'expression tag'        -9  11 
1 8RVF SER A 12  ? UNP Q99685 ?   ?   'expression tag'        -8  12 
1 8RVF GLY A 13  ? UNP Q99685 ?   ?   'expression tag'        -7  13 
1 8RVF GLU A 14  ? UNP Q99685 ?   ?   'expression tag'        -6  14 
1 8RVF ASN A 15  ? UNP Q99685 ?   ?   'expression tag'        -5  15 
1 8RVF LEU A 16  ? UNP Q99685 ?   ?   'expression tag'        -4  16 
1 8RVF TYR A 17  ? UNP Q99685 ?   ?   'expression tag'        -3  17 
1 8RVF PHE A 18  ? UNP Q99685 ?   ?   'expression tag'        -2  18 
1 8RVF GLN A 19  ? UNP Q99685 ?   ?   'expression tag'        -1  19 
1 8RVF GLY A 20  ? UNP Q99685 ?   ?   'expression tag'        0   20 
1 8RVF ALA A 56  ? UNP Q99685 LYS 36  'engineered mutation'   36  21 
1 8RVF SER A 189 ? UNP Q99685 LEU 169 'engineered mutation'   169 22 
1 8RVF 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 
# 
_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 
# 
_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]         1.0 
_pdbx_struct_oper_list.matrix[1][2]         0.0 
_pdbx_struct_oper_list.matrix[1][3]         0.0 
_pdbx_struct_oper_list.vector[1]            0.0 
_pdbx_struct_oper_list.matrix[2][1]         0.0 
_pdbx_struct_oper_list.matrix[2][2]         1.0 
_pdbx_struct_oper_list.matrix[2][3]         0.0 
_pdbx_struct_oper_list.vector[2]            0.0 
_pdbx_struct_oper_list.matrix[3][1]         0.0 
_pdbx_struct_oper_list.matrix[3][2]         0.0 
_pdbx_struct_oper_list.matrix[3][3]         1.0 
_pdbx_struct_oper_list.vector[3]            0.0 
# 
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 ? ARG A 313 ? LEU A 275 ARG A 293 1 ? 19 
# 
_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 GLY A 140 ? N GLY A 120 O ILE A 165 ? O ILE A 145 
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                   8RVF 
_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_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  ? ? -100.79 -156.76 
2 1 ASP A 69  ? ? 71.44   30.33   
3 1 SER A 122 ? ? 57.37   -121.78 
4 1 SER A 146 ? ? 39.07   61.96   
5 1 GLU A 274 ? ? -102.89 -159.46 
# 
_pdbx_refine_tls.id               1 
_pdbx_refine_tls.pdbx_refine_id   'X-RAY DIFFRACTION' 
_pdbx_refine_tls.details          ? 
_pdbx_refine_tls.method           ? 
_pdbx_refine_tls.origin_x         118.849 
_pdbx_refine_tls.origin_y         20.4231 
_pdbx_refine_tls.origin_z         -0.0518 
_pdbx_refine_tls.T[1][1]          0.1273 
_pdbx_refine_tls.T[1][1]_esd      ? 
_pdbx_refine_tls.T[1][2]          0.0068 
_pdbx_refine_tls.T[1][2]_esd      ? 
_pdbx_refine_tls.T[1][3]          -0.0047 
_pdbx_refine_tls.T[1][3]_esd      ? 
_pdbx_refine_tls.T[2][2]          -0.0813 
_pdbx_refine_tls.T[2][2]_esd      ? 
_pdbx_refine_tls.T[2][3]          -0.0008 
_pdbx_refine_tls.T[2][3]_esd      ? 
_pdbx_refine_tls.T[3][3]          -0.0493 
_pdbx_refine_tls.T[3][3]_esd      ? 
_pdbx_refine_tls.L[1][1]          0 
_pdbx_refine_tls.L[1][1]_esd      ? 
_pdbx_refine_tls.L[1][2]          -0.2754 
_pdbx_refine_tls.L[1][2]_esd      ? 
_pdbx_refine_tls.L[1][3]          0.0141 
_pdbx_refine_tls.L[1][3]_esd      ? 
_pdbx_refine_tls.L[2][2]          1.6555 
_pdbx_refine_tls.L[2][2]_esd      ? 
_pdbx_refine_tls.L[2][3]          -0.0423 
_pdbx_refine_tls.L[2][3]_esd      ? 
_pdbx_refine_tls.L[3][3]          0.2839 
_pdbx_refine_tls.L[3][3]_esd      ? 
_pdbx_refine_tls.S[1][1]          -0.0324 
_pdbx_refine_tls.S[1][1]_esd      ? 
_pdbx_refine_tls.S[1][2]          0.079 
_pdbx_refine_tls.S[1][2]_esd      ? 
_pdbx_refine_tls.S[1][3]          -0.017 
_pdbx_refine_tls.S[1][3]_esd      ? 
_pdbx_refine_tls.S[2][1]          0.079 
_pdbx_refine_tls.S[2][1]_esd      ? 
_pdbx_refine_tls.S[2][2]          0.0054 
_pdbx_refine_tls.S[2][2]_esd      ? 
_pdbx_refine_tls.S[2][3]          -0.0117 
_pdbx_refine_tls.S[2][3]_esd      ? 
_pdbx_refine_tls.S[3][1]          -0.017 
_pdbx_refine_tls.S[3][1]_esd      ? 
_pdbx_refine_tls.S[3][2]          -0.0117 
_pdbx_refine_tls.S[3][2]_esd      ? 
_pdbx_refine_tls.S[3][3]          0.0271 
_pdbx_refine_tls.S[3][3]_esd      ? 
# 
loop_
_pdbx_refine_tls_group.id 
_pdbx_refine_tls_group.pdbx_refine_id 
_pdbx_refine_tls_group.refine_tls_id 
_pdbx_refine_tls_group.beg_label_asym_id 
_pdbx_refine_tls_group.beg_label_seq_id 
_pdbx_refine_tls_group.beg_auth_asym_id 
_pdbx_refine_tls_group.beg_auth_seq_id 
_pdbx_refine_tls_group.beg_PDB_ins_code 
_pdbx_refine_tls_group.end_label_asym_id 
_pdbx_refine_tls_group.end_label_seq_id 
_pdbx_refine_tls_group.end_auth_asym_id 
_pdbx_refine_tls_group.end_auth_seq_id 
_pdbx_refine_tls_group.end_PDB_ins_code 
_pdbx_refine_tls_group.selection 
_pdbx_refine_tls_group.selection_details 
1 'X-RAY DIFFRACTION' 1 ? ? A 6   ? ? ? A 295 ? ? '{ A|* }' 
2 'X-RAY DIFFRACTION' 1 ? ? A 301 ? ? ? A 301 ? ? '{ A|* }' 
# 
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 
A1H35 N1   N N N 1   
A1H35 C7   C N N 2   
A1H35 C8   C N N 3   
A1H35 N2   N N N 4   
A1H35 C9   C N N 5   
A1H35 C1   C N N 6   
A1H35 C5   C N N 7   
A1H35 C6   C N N 8   
A1H35 N3   N Y N 9   
A1H35 C4   C N N 10  
A1H35 C3   C N N 11  
A1H35 C2   C N N 12  
A1H35 N4   N Y N 13  
A1H35 O    O N N 14  
A1H35 C12  C N N 15  
A1H35 C23  C N N 16  
A1H35 C14  C N N 17  
A1H35 C17  C N N 18  
A1H35 C16  C N N 19  
A1H35 N5   N Y N 20  
A1H35 C19  C Y N 21  
A1H35 C20  C N N 22  
A1H35 C22  C N N 23  
A1H35 C21  C N N 24  
A1H35 C18  C Y N 25  
A1H35 C15  C N N 26  
A1H35 C13  C N N 27  
A1H35 C10  C N N 28  
A1H35 C11  C N N 29  
A1H35 C    C N N 30  
A1H35 N    N N N 31  
A1H35 C24  C Y N 32  
A1H35 N6   N Y N 33  
A1H35 B    B N N 34  
A1H35 F1   F N N 35  
A1H35 F    F N N 36  
A1H35 C27  C Y N 37  
A1H35 C26  C Y N 38  
A1H35 C25  C Y N 39  
A1H35 H6   H N N 40  
A1H35 H7   H N N 41  
A1H35 H8   H N N 42  
A1H35 H9   H N N 43  
A1H35 H1   H N N 44  
A1H35 H4   H N N 45  
A1H35 H3   H N N 46  
A1H35 H5   H N N 47  
A1H35 H2   H N N 48  
A1H35 H28  H N N 49  
A1H35 H27  H N N 50  
A1H35 H20  H N N 51  
A1H35 H19  H N N 52  
A1H35 H18  H N N 53  
A1H35 H22  H N N 54  
A1H35 H25  H N N 55  
A1H35 H26  H N N 56  
A1H35 H23  H N N 57  
A1H35 H24  H N N 58  
A1H35 H21  H N N 59  
A1H35 H17  H N N 60  
A1H35 H16  H N N 61  
A1H35 H15  H N N 62  
A1H35 H14  H N N 63  
A1H35 H11  H N N 64  
A1H35 H10  H N N 65  
A1H35 H13  H N N 66  
A1H35 H12  H N N 67  
A1H35 H    H N N 68  
A1H35 H31  H N N 69  
A1H35 H30  H N N 70  
A1H35 H29  H N N 71  
ALA   N    N N N 72  
ALA   CA   C N S 73  
ALA   C    C N N 74  
ALA   O    O N N 75  
ALA   CB   C N N 76  
ALA   OXT  O N N 77  
ALA   H    H N N 78  
ALA   H2   H N N 79  
ALA   HA   H N N 80  
ALA   HB1  H N N 81  
ALA   HB2  H N N 82  
ALA   HB3  H N N 83  
ALA   HXT  H N N 84  
ARG   N    N N N 85  
ARG   CA   C N S 86  
ARG   C    C N N 87  
ARG   O    O N N 88  
ARG   CB   C N N 89  
ARG   CG   C N N 90  
ARG   CD   C N N 91  
ARG   NE   N N N 92  
ARG   CZ   C N N 93  
ARG   NH1  N N N 94  
ARG   NH2  N N N 95  
ARG   OXT  O N N 96  
ARG   H    H N N 97  
ARG   H2   H N N 98  
ARG   HA   H N N 99  
ARG   HB2  H N N 100 
ARG   HB3  H N N 101 
ARG   HG2  H N N 102 
ARG   HG3  H N N 103 
ARG   HD2  H N N 104 
ARG   HD3  H N N 105 
ARG   HE   H N N 106 
ARG   HH11 H N N 107 
ARG   HH12 H N N 108 
ARG   HH21 H N N 109 
ARG   HH22 H N N 110 
ARG   HXT  H N N 111 
ASN   N    N N N 112 
ASN   CA   C N S 113 
ASN   C    C N N 114 
ASN   O    O N N 115 
ASN   CB   C N N 116 
ASN   CG   C N N 117 
ASN   OD1  O N N 118 
ASN   ND2  N N N 119 
ASN   OXT  O N N 120 
ASN   H    H N N 121 
ASN   H2   H N N 122 
ASN   HA   H N N 123 
ASN   HB2  H N N 124 
ASN   HB3  H N N 125 
ASN   HD21 H N N 126 
ASN   HD22 H N N 127 
ASN   HXT  H N N 128 
ASP   N    N N N 129 
ASP   CA   C N S 130 
ASP   C    C N N 131 
ASP   O    O N N 132 
ASP   CB   C N N 133 
ASP   CG   C N N 134 
ASP   OD1  O N N 135 
ASP   OD2  O N N 136 
ASP   OXT  O N N 137 
ASP   H    H N N 138 
ASP   H2   H N N 139 
ASP   HA   H N N 140 
ASP   HB2  H N N 141 
ASP   HB3  H N N 142 
ASP   HD2  H N N 143 
ASP   HXT  H N N 144 
CYS   N    N N N 145 
CYS   CA   C N R 146 
CYS   C    C N N 147 
CYS   O    O N N 148 
CYS   CB   C N N 149 
CYS   SG   S N N 150 
CYS   OXT  O N N 151 
CYS   H    H N N 152 
CYS   H2   H N N 153 
CYS   HA   H N N 154 
CYS   HB2  H N N 155 
CYS   HB3  H N N 156 
CYS   HG   H N N 157 
CYS   HXT  H N N 158 
EDO   C1   C N N 159 
EDO   O1   O N N 160 
EDO   C2   C N N 161 
EDO   O2   O N N 162 
EDO   H11  H N N 163 
EDO   H12  H N N 164 
EDO   HO1  H N N 165 
EDO   H21  H N N 166 
EDO   H22  H N N 167 
EDO   HO2  H N N 168 
GLN   N    N N N 169 
GLN   CA   C N S 170 
GLN   C    C N N 171 
GLN   O    O N N 172 
GLN   CB   C N N 173 
GLN   CG   C N N 174 
GLN   CD   C N N 175 
GLN   OE1  O N N 176 
GLN   NE2  N N N 177 
GLN   OXT  O N N 178 
GLN   H    H N N 179 
GLN   H2   H N N 180 
GLN   HA   H N N 181 
GLN   HB2  H N N 182 
GLN   HB3  H N N 183 
GLN   HG2  H N N 184 
GLN   HG3  H N N 185 
GLN   HE21 H N N 186 
GLN   HE22 H N N 187 
GLN   HXT  H N N 188 
GLU   N    N N N 189 
GLU   CA   C N S 190 
GLU   C    C N N 191 
GLU   O    O N N 192 
GLU   CB   C N N 193 
GLU   CG   C N N 194 
GLU   CD   C N N 195 
GLU   OE1  O N N 196 
GLU   OE2  O N N 197 
GLU   OXT  O N N 198 
GLU   H    H N N 199 
GLU   H2   H N N 200 
GLU   HA   H N N 201 
GLU   HB2  H N N 202 
GLU   HB3  H N N 203 
GLU   HG2  H N N 204 
GLU   HG3  H N N 205 
GLU   HE2  H N N 206 
GLU   HXT  H N N 207 
GLY   N    N N N 208 
GLY   CA   C N N 209 
GLY   C    C N N 210 
GLY   O    O N N 211 
GLY   OXT  O N N 212 
GLY   H    H N N 213 
GLY   H2   H N N 214 
GLY   HA2  H N N 215 
GLY   HA3  H N N 216 
GLY   HXT  H N N 217 
HIS   N    N N N 218 
HIS   CA   C N S 219 
HIS   C    C N N 220 
HIS   O    O N N 221 
HIS   CB   C N N 222 
HIS   CG   C Y N 223 
HIS   ND1  N Y N 224 
HIS   CD2  C Y N 225 
HIS   CE1  C Y N 226 
HIS   NE2  N Y N 227 
HIS   OXT  O N N 228 
HIS   H    H N N 229 
HIS   H2   H N N 230 
HIS   HA   H N N 231 
HIS   HB2  H N N 232 
HIS   HB3  H N N 233 
HIS   HD1  H N N 234 
HIS   HD2  H N N 235 
HIS   HE1  H N N 236 
HIS   HE2  H N N 237 
HIS   HXT  H N N 238 
HOH   O    O N N 239 
HOH   H1   H N N 240 
HOH   H2   H N N 241 
ILE   N    N N N 242 
ILE   CA   C N S 243 
ILE   C    C N N 244 
ILE   O    O N N 245 
ILE   CB   C N S 246 
ILE   CG1  C N N 247 
ILE   CG2  C N N 248 
ILE   CD1  C N N 249 
ILE   OXT  O N N 250 
ILE   H    H N N 251 
ILE   H2   H N N 252 
ILE   HA   H N N 253 
ILE   HB   H N N 254 
ILE   HG12 H N N 255 
ILE   HG13 H N N 256 
ILE   HG21 H N N 257 
ILE   HG22 H N N 258 
ILE   HG23 H N N 259 
ILE   HD11 H N N 260 
ILE   HD12 H N N 261 
ILE   HD13 H N N 262 
ILE   HXT  H N N 263 
LEU   N    N N N 264 
LEU   CA   C N S 265 
LEU   C    C N N 266 
LEU   O    O N N 267 
LEU   CB   C N N 268 
LEU   CG   C N N 269 
LEU   CD1  C N N 270 
LEU   CD2  C N N 271 
LEU   OXT  O N N 272 
LEU   H    H N N 273 
LEU   H2   H N N 274 
LEU   HA   H N N 275 
LEU   HB2  H N N 276 
LEU   HB3  H N N 277 
LEU   HG   H N N 278 
LEU   HD11 H N N 279 
LEU   HD12 H N N 280 
LEU   HD13 H N N 281 
LEU   HD21 H N N 282 
LEU   HD22 H N N 283 
LEU   HD23 H N N 284 
LEU   HXT  H N N 285 
LYS   N    N N N 286 
LYS   CA   C N S 287 
LYS   C    C N N 288 
LYS   O    O N N 289 
LYS   CB   C N N 290 
LYS   CG   C N N 291 
LYS   CD   C N N 292 
LYS   CE   C N N 293 
LYS   NZ   N N N 294 
LYS   OXT  O N N 295 
LYS   H    H N N 296 
LYS   H2   H N N 297 
LYS   HA   H N N 298 
LYS   HB2  H N N 299 
LYS   HB3  H N N 300 
LYS   HG2  H N N 301 
LYS   HG3  H N N 302 
LYS   HD2  H N N 303 
LYS   HD3  H N N 304 
LYS   HE2  H N N 305 
LYS   HE3  H N N 306 
LYS   HZ1  H N N 307 
LYS   HZ2  H N N 308 
LYS   HZ3  H N N 309 
LYS   HXT  H N N 310 
MET   N    N N N 311 
MET   CA   C N S 312 
MET   C    C N N 313 
MET   O    O N N 314 
MET   CB   C N N 315 
MET   CG   C N N 316 
MET   SD   S N N 317 
MET   CE   C N N 318 
MET   OXT  O N N 319 
MET   H    H N N 320 
MET   H2   H N N 321 
MET   HA   H N N 322 
MET   HB2  H N N 323 
MET   HB3  H N N 324 
MET   HG2  H N N 325 
MET   HG3  H N N 326 
MET   HE1  H N N 327 
MET   HE2  H N N 328 
MET   HE3  H N N 329 
MET   HXT  H N N 330 
PHE   N    N N N 331 
PHE   CA   C N S 332 
PHE   C    C N N 333 
PHE   O    O N N 334 
PHE   CB   C N N 335 
PHE   CG   C Y N 336 
PHE   CD1  C Y N 337 
PHE   CD2  C Y N 338 
PHE   CE1  C Y N 339 
PHE   CE2  C Y N 340 
PHE   CZ   C Y N 341 
PHE   OXT  O N N 342 
PHE   H    H N N 343 
PHE   H2   H N N 344 
PHE   HA   H N N 345 
PHE   HB2  H N N 346 
PHE   HB3  H N N 347 
PHE   HD1  H N N 348 
PHE   HD2  H N N 349 
PHE   HE1  H N N 350 
PHE   HE2  H N N 351 
PHE   HZ   H N N 352 
PHE   HXT  H N N 353 
PRO   N    N N N 354 
PRO   CA   C N S 355 
PRO   C    C N N 356 
PRO   O    O N N 357 
PRO   CB   C N N 358 
PRO   CG   C N N 359 
PRO   CD   C N N 360 
PRO   OXT  O N N 361 
PRO   H    H N N 362 
PRO   HA   H N N 363 
PRO   HB2  H N N 364 
PRO   HB3  H N N 365 
PRO   HG2  H N N 366 
PRO   HG3  H N N 367 
PRO   HD2  H N N 368 
PRO   HD3  H N N 369 
PRO   HXT  H N N 370 
SER   N    N N N 371 
SER   CA   C N S 372 
SER   C    C N N 373 
SER   O    O N N 374 
SER   CB   C N N 375 
SER   OG   O N N 376 
SER   OXT  O N N 377 
SER   H    H N N 378 
SER   H2   H N N 379 
SER   HA   H N N 380 
SER   HB2  H N N 381 
SER   HB3  H N N 382 
SER   HG   H N N 383 
SER   HXT  H N N 384 
THR   N    N N N 385 
THR   CA   C N S 386 
THR   C    C N N 387 
THR   O    O N N 388 
THR   CB   C N R 389 
THR   OG1  O N N 390 
THR   CG2  C N N 391 
THR   OXT  O N N 392 
THR   H    H N N 393 
THR   H2   H N N 394 
THR   HA   H N N 395 
THR   HB   H N N 396 
THR   HG1  H N N 397 
THR   HG21 H N N 398 
THR   HG22 H N N 399 
THR   HG23 H N N 400 
THR   HXT  H N N 401 
TRP   N    N N N 402 
TRP   CA   C N S 403 
TRP   C    C N N 404 
TRP   O    O N N 405 
TRP   CB   C N N 406 
TRP   CG   C Y N 407 
TRP   CD1  C Y N 408 
TRP   CD2  C Y N 409 
TRP   NE1  N Y N 410 
TRP   CE2  C Y N 411 
TRP   CE3  C Y N 412 
TRP   CZ2  C Y N 413 
TRP   CZ3  C Y N 414 
TRP   CH2  C Y N 415 
TRP   OXT  O N N 416 
TRP   H    H N N 417 
TRP   H2   H N N 418 
TRP   HA   H N N 419 
TRP   HB2  H N N 420 
TRP   HB3  H N N 421 
TRP   HD1  H N N 422 
TRP   HE1  H N N 423 
TRP   HE3  H N N 424 
TRP   HZ2  H N N 425 
TRP   HZ3  H N N 426 
TRP   HH2  H N N 427 
TRP   HXT  H N N 428 
TYR   N    N N N 429 
TYR   CA   C N S 430 
TYR   C    C N N 431 
TYR   O    O N N 432 
TYR   CB   C N N 433 
TYR   CG   C Y N 434 
TYR   CD1  C Y N 435 
TYR   CD2  C Y N 436 
TYR   CE1  C Y N 437 
TYR   CE2  C Y N 438 
TYR   CZ   C Y N 439 
TYR   OH   O N N 440 
TYR   OXT  O N N 441 
TYR   H    H N N 442 
TYR   H2   H N N 443 
TYR   HA   H N N 444 
TYR   HB2  H N N 445 
TYR   HB3  H N N 446 
TYR   HD1  H N N 447 
TYR   HD2  H N N 448 
TYR   HE1  H N N 449 
TYR   HE2  H N N 450 
TYR   HH   H N N 451 
TYR   HXT  H N N 452 
VAL   N    N N N 453 
VAL   CA   C N S 454 
VAL   C    C N N 455 
VAL   O    O N N 456 
VAL   CB   C N N 457 
VAL   CG1  C N N 458 
VAL   CG2  C N N 459 
VAL   OXT  O N N 460 
VAL   H    H N N 461 
VAL   H2   H N N 462 
VAL   HA   H N N 463 
VAL   HB   H N N 464 
VAL   HG11 H N N 465 
VAL   HG12 H N N 466 
VAL   HG13 H N N 467 
VAL   HG21 H N N 468 
VAL   HG22 H N N 469 
VAL   HG23 H N N 470 
VAL   HXT  H N N 471 
# 
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 
A1H35 F   B    sing N N 1   
A1H35 F1  B    sing N N 2   
A1H35 B   N    sing N N 3   
A1H35 N   C    doub N N 4   
A1H35 C   C1   sing N N 5   
A1H35 C1  C2   doub N N 6   
A1H35 C2  C3   sing N N 7   
A1H35 N   C3   sing N N 8   
A1H35 C3  C4   doub N N 9   
A1H35 C4  C5   sing N N 10  
A1H35 C5  C6   sing N N 11  
A1H35 C6  C7   sing N N 12  
A1H35 C7  C8   sing N N 13  
A1H35 C9  C8   sing N N 14  
A1H35 C6  C9   sing N N 15  
A1H35 C8  C10  sing N N 16  
A1H35 C10 N1   sing N N 17  
A1H35 C11 N1   sing N N 18  
A1H35 C8  C11  sing N N 19  
A1H35 N1  C12  sing N N 20  
A1H35 C12 O    doub N N 21  
A1H35 N2  C12  sing N N 22  
A1H35 N2  C13  sing N N 23  
A1H35 C13 C14  sing N N 24  
A1H35 C14 C15  sing N N 25  
A1H35 C15 C16  sing N N 26  
A1H35 C16 C17  sing N N 27  
A1H35 C17 C14  sing N N 28  
A1H35 N3  C16  sing N N 29  
A1H35 N3  C18  sing Y N 30  
A1H35 C18 N4   doub Y N 31  
A1H35 N4  C19  sing Y N 32  
A1H35 C19 N5   doub Y N 33  
A1H35 N5  N3   sing Y N 34  
A1H35 C20 C19  sing N N 35  
A1H35 C20 C21  sing N N 36  
A1H35 C21 C22  sing N N 37  
A1H35 C22 C20  sing N N 38  
A1H35 C14 C23  sing N N 39  
A1H35 C23 N2   sing N N 40  
A1H35 C24 C4   sing N N 41  
A1H35 C24 C25  doub Y N 42  
A1H35 C25 C26  sing Y N 43  
A1H35 C26 C27  doub Y N 44  
A1H35 C27 N6   sing Y N 45  
A1H35 B   N6   sing N N 46  
A1H35 N6  C24  sing Y N 47  
A1H35 C7  H6   sing N N 48  
A1H35 C7  H7   sing N N 49  
A1H35 C9  H8   sing N N 50  
A1H35 C9  H9   sing N N 51  
A1H35 C1  H1   sing N N 52  
A1H35 C5  H4   sing N N 53  
A1H35 C5  H3   sing N N 54  
A1H35 C6  H5   sing N N 55  
A1H35 C2  H2   sing N N 56  
A1H35 C23 H28  sing N N 57  
A1H35 C23 H27  sing N N 58  
A1H35 C17 H20  sing N N 59  
A1H35 C17 H19  sing N N 60  
A1H35 C16 H18  sing N N 61  
A1H35 C20 H22  sing N N 62  
A1H35 C22 H25  sing N N 63  
A1H35 C22 H26  sing N N 64  
A1H35 C21 H23  sing N N 65  
A1H35 C21 H24  sing N N 66  
A1H35 C18 H21  sing N N 67  
A1H35 C15 H17  sing N N 68  
A1H35 C15 H16  sing N N 69  
A1H35 C13 H15  sing N N 70  
A1H35 C13 H14  sing N N 71  
A1H35 C10 H11  sing N N 72  
A1H35 C10 H10  sing N N 73  
A1H35 C11 H13  sing N N 74  
A1H35 C11 H12  sing N N 75  
A1H35 C   H    sing N N 76  
A1H35 C27 H31  sing N N 77  
A1H35 C26 H30  sing N N 78  
A1H35 C25 H29  sing N N 79  
ALA   N   CA   sing N N 80  
ALA   N   H    sing N N 81  
ALA   N   H2   sing N N 82  
ALA   CA  C    sing N N 83  
ALA   CA  CB   sing N N 84  
ALA   CA  HA   sing N N 85  
ALA   C   O    doub N N 86  
ALA   C   OXT  sing N N 87  
ALA   CB  HB1  sing N N 88  
ALA   CB  HB2  sing N N 89  
ALA   CB  HB3  sing N N 90  
ALA   OXT HXT  sing N N 91  
ARG   N   CA   sing N N 92  
ARG   N   H    sing N N 93  
ARG   N   H2   sing N N 94  
ARG   CA  C    sing N N 95  
ARG   CA  CB   sing N N 96  
ARG   CA  HA   sing N N 97  
ARG   C   O    doub N N 98  
ARG   C   OXT  sing N N 99  
ARG   CB  CG   sing N N 100 
ARG   CB  HB2  sing N N 101 
ARG   CB  HB3  sing N N 102 
ARG   CG  CD   sing N N 103 
ARG   CG  HG2  sing N N 104 
ARG   CG  HG3  sing N N 105 
ARG   CD  NE   sing N N 106 
ARG   CD  HD2  sing N N 107 
ARG   CD  HD3  sing N N 108 
ARG   NE  CZ   sing N N 109 
ARG   NE  HE   sing N N 110 
ARG   CZ  NH1  sing N N 111 
ARG   CZ  NH2  doub N N 112 
ARG   NH1 HH11 sing N N 113 
ARG   NH1 HH12 sing N N 114 
ARG   NH2 HH21 sing N N 115 
ARG   NH2 HH22 sing N N 116 
ARG   OXT HXT  sing N N 117 
ASN   N   CA   sing N N 118 
ASN   N   H    sing N N 119 
ASN   N   H2   sing N N 120 
ASN   CA  C    sing N N 121 
ASN   CA  CB   sing N N 122 
ASN   CA  HA   sing N N 123 
ASN   C   O    doub N N 124 
ASN   C   OXT  sing N N 125 
ASN   CB  CG   sing N N 126 
ASN   CB  HB2  sing N N 127 
ASN   CB  HB3  sing N N 128 
ASN   CG  OD1  doub N N 129 
ASN   CG  ND2  sing N N 130 
ASN   ND2 HD21 sing N N 131 
ASN   ND2 HD22 sing N N 132 
ASN   OXT HXT  sing N N 133 
ASP   N   CA   sing N N 134 
ASP   N   H    sing N N 135 
ASP   N   H2   sing N N 136 
ASP   CA  C    sing N N 137 
ASP   CA  CB   sing N N 138 
ASP   CA  HA   sing N N 139 
ASP   C   O    doub N N 140 
ASP   C   OXT  sing N N 141 
ASP   CB  CG   sing N N 142 
ASP   CB  HB2  sing N N 143 
ASP   CB  HB3  sing N N 144 
ASP   CG  OD1  doub N N 145 
ASP   CG  OD2  sing N N 146 
ASP   OD2 HD2  sing N N 147 
ASP   OXT HXT  sing N N 148 
CYS   N   CA   sing N N 149 
CYS   N   H    sing N N 150 
CYS   N   H2   sing N N 151 
CYS   CA  C    sing N N 152 
CYS   CA  CB   sing N N 153 
CYS   CA  HA   sing N N 154 
CYS   C   O    doub N N 155 
CYS   C   OXT  sing N N 156 
CYS   CB  SG   sing N N 157 
CYS   CB  HB2  sing N N 158 
CYS   CB  HB3  sing N N 159 
CYS   SG  HG   sing N N 160 
CYS   OXT HXT  sing N N 161 
EDO   C1  O1   sing N N 162 
EDO   C1  C2   sing N N 163 
EDO   C1  H11  sing N N 164 
EDO   C1  H12  sing N N 165 
EDO   O1  HO1  sing N N 166 
EDO   C2  O2   sing N N 167 
EDO   C2  H21  sing N N 168 
EDO   C2  H22  sing N N 169 
EDO   O2  HO2  sing N N 170 
GLN   N   CA   sing N N 171 
GLN   N   H    sing N N 172 
GLN   N   H2   sing N N 173 
GLN   CA  C    sing N N 174 
GLN   CA  CB   sing N N 175 
GLN   CA  HA   sing N N 176 
GLN   C   O    doub N N 177 
GLN   C   OXT  sing N N 178 
GLN   CB  CG   sing N N 179 
GLN   CB  HB2  sing N N 180 
GLN   CB  HB3  sing N N 181 
GLN   CG  CD   sing N N 182 
GLN   CG  HG2  sing N N 183 
GLN   CG  HG3  sing N N 184 
GLN   CD  OE1  doub N N 185 
GLN   CD  NE2  sing N N 186 
GLN   NE2 HE21 sing N N 187 
GLN   NE2 HE22 sing N N 188 
GLN   OXT HXT  sing N N 189 
GLU   N   CA   sing N N 190 
GLU   N   H    sing N N 191 
GLU   N   H2   sing N N 192 
GLU   CA  C    sing N N 193 
GLU   CA  CB   sing N N 194 
GLU   CA  HA   sing N N 195 
GLU   C   O    doub N N 196 
GLU   C   OXT  sing N N 197 
GLU   CB  CG   sing N N 198 
GLU   CB  HB2  sing N N 199 
GLU   CB  HB3  sing N N 200 
GLU   CG  CD   sing N N 201 
GLU   CG  HG2  sing N N 202 
GLU   CG  HG3  sing N N 203 
GLU   CD  OE1  doub N N 204 
GLU   CD  OE2  sing N N 205 
GLU   OE2 HE2  sing N N 206 
GLU   OXT HXT  sing N N 207 
GLY   N   CA   sing N N 208 
GLY   N   H    sing N N 209 
GLY   N   H2   sing N N 210 
GLY   CA  C    sing N N 211 
GLY   CA  HA2  sing N N 212 
GLY   CA  HA3  sing N N 213 
GLY   C   O    doub N N 214 
GLY   C   OXT  sing N N 215 
GLY   OXT HXT  sing N N 216 
HIS   N   CA   sing N N 217 
HIS   N   H    sing N N 218 
HIS   N   H2   sing N N 219 
HIS   CA  C    sing N N 220 
HIS   CA  CB   sing N N 221 
HIS   CA  HA   sing N N 222 
HIS   C   O    doub N N 223 
HIS   C   OXT  sing N N 224 
HIS   CB  CG   sing N N 225 
HIS   CB  HB2  sing N N 226 
HIS   CB  HB3  sing N N 227 
HIS   CG  ND1  sing Y N 228 
HIS   CG  CD2  doub Y N 229 
HIS   ND1 CE1  doub Y N 230 
HIS   ND1 HD1  sing N N 231 
HIS   CD2 NE2  sing Y N 232 
HIS   CD2 HD2  sing N N 233 
HIS   CE1 NE2  sing Y N 234 
HIS   CE1 HE1  sing N N 235 
HIS   NE2 HE2  sing N N 236 
HIS   OXT HXT  sing N N 237 
HOH   O   H1   sing N N 238 
HOH   O   H2   sing N N 239 
ILE   N   CA   sing N N 240 
ILE   N   H    sing N N 241 
ILE   N   H2   sing N N 242 
ILE   CA  C    sing N N 243 
ILE   CA  CB   sing N N 244 
ILE   CA  HA   sing N N 245 
ILE   C   O    doub N N 246 
ILE   C   OXT  sing N N 247 
ILE   CB  CG1  sing N N 248 
ILE   CB  CG2  sing N N 249 
ILE   CB  HB   sing N N 250 
ILE   CG1 CD1  sing N N 251 
ILE   CG1 HG12 sing N N 252 
ILE   CG1 HG13 sing N N 253 
ILE   CG2 HG21 sing N N 254 
ILE   CG2 HG22 sing N N 255 
ILE   CG2 HG23 sing N N 256 
ILE   CD1 HD11 sing N N 257 
ILE   CD1 HD12 sing N N 258 
ILE   CD1 HD13 sing N N 259 
ILE   OXT HXT  sing N N 260 
LEU   N   CA   sing N N 261 
LEU   N   H    sing N N 262 
LEU   N   H2   sing N N 263 
LEU   CA  C    sing N N 264 
LEU   CA  CB   sing N N 265 
LEU   CA  HA   sing N N 266 
LEU   C   O    doub N N 267 
LEU   C   OXT  sing N N 268 
LEU   CB  CG   sing N N 269 
LEU   CB  HB2  sing N N 270 
LEU   CB  HB3  sing N N 271 
LEU   CG  CD1  sing N N 272 
LEU   CG  CD2  sing N N 273 
LEU   CG  HG   sing N N 274 
LEU   CD1 HD11 sing N N 275 
LEU   CD1 HD12 sing N N 276 
LEU   CD1 HD13 sing N N 277 
LEU   CD2 HD21 sing N N 278 
LEU   CD2 HD22 sing N N 279 
LEU   CD2 HD23 sing N N 280 
LEU   OXT HXT  sing N N 281 
LYS   N   CA   sing N N 282 
LYS   N   H    sing N N 283 
LYS   N   H2   sing N N 284 
LYS   CA  C    sing N N 285 
LYS   CA  CB   sing N N 286 
LYS   CA  HA   sing N N 287 
LYS   C   O    doub N N 288 
LYS   C   OXT  sing N N 289 
LYS   CB  CG   sing N N 290 
LYS   CB  HB2  sing N N 291 
LYS   CB  HB3  sing N N 292 
LYS   CG  CD   sing N N 293 
LYS   CG  HG2  sing N N 294 
LYS   CG  HG3  sing N N 295 
LYS   CD  CE   sing N N 296 
LYS   CD  HD2  sing N N 297 
LYS   CD  HD3  sing N N 298 
LYS   CE  NZ   sing N N 299 
LYS   CE  HE2  sing N N 300 
LYS   CE  HE3  sing N N 301 
LYS   NZ  HZ1  sing N N 302 
LYS   NZ  HZ2  sing N N 303 
LYS   NZ  HZ3  sing N N 304 
LYS   OXT HXT  sing N N 305 
MET   N   CA   sing N N 306 
MET   N   H    sing N N 307 
MET   N   H2   sing N N 308 
MET   CA  C    sing N N 309 
MET   CA  CB   sing N N 310 
MET   CA  HA   sing N N 311 
MET   C   O    doub N N 312 
MET   C   OXT  sing N N 313 
MET   CB  CG   sing N N 314 
MET   CB  HB2  sing N N 315 
MET   CB  HB3  sing N N 316 
MET   CG  SD   sing N N 317 
MET   CG  HG2  sing N N 318 
MET   CG  HG3  sing N N 319 
MET   SD  CE   sing N N 320 
MET   CE  HE1  sing N N 321 
MET   CE  HE2  sing N N 322 
MET   CE  HE3  sing N N 323 
MET   OXT HXT  sing N N 324 
PHE   N   CA   sing N N 325 
PHE   N   H    sing N N 326 
PHE   N   H2   sing N N 327 
PHE   CA  C    sing N N 328 
PHE   CA  CB   sing N N 329 
PHE   CA  HA   sing N N 330 
PHE   C   O    doub N N 331 
PHE   C   OXT  sing N N 332 
PHE   CB  CG   sing N N 333 
PHE   CB  HB2  sing N N 334 
PHE   CB  HB3  sing N N 335 
PHE   CG  CD1  doub Y N 336 
PHE   CG  CD2  sing Y N 337 
PHE   CD1 CE1  sing Y N 338 
PHE   CD1 HD1  sing N N 339 
PHE   CD2 CE2  doub Y N 340 
PHE   CD2 HD2  sing N N 341 
PHE   CE1 CZ   doub Y N 342 
PHE   CE1 HE1  sing N N 343 
PHE   CE2 CZ   sing Y N 344 
PHE   CE2 HE2  sing N N 345 
PHE   CZ  HZ   sing N N 346 
PHE   OXT HXT  sing N N 347 
PRO   N   CA   sing N N 348 
PRO   N   CD   sing N N 349 
PRO   N   H    sing N N 350 
PRO   CA  C    sing N N 351 
PRO   CA  CB   sing N N 352 
PRO   CA  HA   sing N N 353 
PRO   C   O    doub N N 354 
PRO   C   OXT  sing N N 355 
PRO   CB  CG   sing N N 356 
PRO   CB  HB2  sing N N 357 
PRO   CB  HB3  sing N N 358 
PRO   CG  CD   sing N N 359 
PRO   CG  HG2  sing N N 360 
PRO   CG  HG3  sing N N 361 
PRO   CD  HD2  sing N N 362 
PRO   CD  HD3  sing N N 363 
PRO   OXT HXT  sing N N 364 
SER   N   CA   sing N N 365 
SER   N   H    sing N N 366 
SER   N   H2   sing N N 367 
SER   CA  C    sing N N 368 
SER   CA  CB   sing N N 369 
SER   CA  HA   sing N N 370 
SER   C   O    doub N N 371 
SER   C   OXT  sing N N 372 
SER   CB  OG   sing N N 373 
SER   CB  HB2  sing N N 374 
SER   CB  HB3  sing N N 375 
SER   OG  HG   sing N N 376 
SER   OXT HXT  sing N N 377 
THR   N   CA   sing N N 378 
THR   N   H    sing N N 379 
THR   N   H2   sing N N 380 
THR   CA  C    sing N N 381 
THR   CA  CB   sing N N 382 
THR   CA  HA   sing N N 383 
THR   C   O    doub N N 384 
THR   C   OXT  sing N N 385 
THR   CB  OG1  sing N N 386 
THR   CB  CG2  sing N N 387 
THR   CB  HB   sing N N 388 
THR   OG1 HG1  sing N N 389 
THR   CG2 HG21 sing N N 390 
THR   CG2 HG22 sing N N 391 
THR   CG2 HG23 sing N N 392 
THR   OXT HXT  sing N N 393 
TRP   N   CA   sing N N 394 
TRP   N   H    sing N N 395 
TRP   N   H2   sing N N 396 
TRP   CA  C    sing N N 397 
TRP   CA  CB   sing N N 398 
TRP   CA  HA   sing N N 399 
TRP   C   O    doub N N 400 
TRP   C   OXT  sing N N 401 
TRP   CB  CG   sing N N 402 
TRP   CB  HB2  sing N N 403 
TRP   CB  HB3  sing N N 404 
TRP   CG  CD1  doub Y N 405 
TRP   CG  CD2  sing Y N 406 
TRP   CD1 NE1  sing Y N 407 
TRP   CD1 HD1  sing N N 408 
TRP   CD2 CE2  doub Y N 409 
TRP   CD2 CE3  sing Y N 410 
TRP   NE1 CE2  sing Y N 411 
TRP   NE1 HE1  sing N N 412 
TRP   CE2 CZ2  sing Y N 413 
TRP   CE3 CZ3  doub Y N 414 
TRP   CE3 HE3  sing N N 415 
TRP   CZ2 CH2  doub Y N 416 
TRP   CZ2 HZ2  sing N N 417 
TRP   CZ3 CH2  sing Y N 418 
TRP   CZ3 HZ3  sing N N 419 
TRP   CH2 HH2  sing N N 420 
TRP   OXT HXT  sing N N 421 
TYR   N   CA   sing N N 422 
TYR   N   H    sing N N 423 
TYR   N   H2   sing N N 424 
TYR   CA  C    sing N N 425 
TYR   CA  CB   sing N N 426 
TYR   CA  HA   sing N N 427 
TYR   C   O    doub N N 428 
TYR   C   OXT  sing N N 429 
TYR   CB  CG   sing N N 430 
TYR   CB  HB2  sing N N 431 
TYR   CB  HB3  sing N N 432 
TYR   CG  CD1  doub Y N 433 
TYR   CG  CD2  sing Y N 434 
TYR   CD1 CE1  sing Y N 435 
TYR   CD1 HD1  sing N N 436 
TYR   CD2 CE2  doub Y N 437 
TYR   CD2 HD2  sing N N 438 
TYR   CE1 CZ   doub Y N 439 
TYR   CE1 HE1  sing N N 440 
TYR   CE2 CZ   sing Y N 441 
TYR   CE2 HE2  sing N N 442 
TYR   CZ  OH   sing N N 443 
TYR   OH  HH   sing N N 444 
TYR   OXT HXT  sing N N 445 
VAL   N   CA   sing N N 446 
VAL   N   H    sing N N 447 
VAL   N   H2   sing N N 448 
VAL   CA  C    sing N N 449 
VAL   CA  CB   sing N N 450 
VAL   CA  HA   sing N N 451 
VAL   C   O    doub N N 452 
VAL   C   OXT  sing N N 453 
VAL   CB  CG1  sing N N 454 
VAL   CB  CG2  sing N N 455 
VAL   CB  HB   sing N N 456 
VAL   CG1 HG11 sing N N 457 
VAL   CG1 HG12 sing N N 458 
VAL   CG1 HG13 sing N N 459 
VAL   CG2 HG21 sing N N 460 
VAL   CG2 HG22 sing N N 461 
VAL   CG2 HG23 sing N N 462 
VAL   OXT HXT  sing N N 463 
# 
_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          ? 
# 
_atom_sites.entry_id                    8RVF 
_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]   0.011056 
_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]   0.007855 
_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]   0.015912 
_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 
B 
C 
F 
N 
O 
S 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
_atom_site.pdbx_tls_group_id 
ATOM   1    N N   . SER   A 1 26  ? 111.199 52.361 3.267   1    52.57 ?  6   SER   A N   1 1 
ATOM   2    C CA  . SER   A 1 26  ? 110.854 51.646 2.032   1    52.94 ?  6   SER   A CA  1 1 
ATOM   3    C C   . SER   A 1 26  ? 110.844 50.142 2.281   1    50.65 ?  6   SER   A C   1 1 
ATOM   4    O O   . SER   A 1 26  ? 111.743 49.627 2.954   1    51.06 ?  6   SER   A O   1 1 
ATOM   5    C CB  . SER   A 1 26  ? 111.824 51.995 0.908   1    56.1  ?  6   SER   A CB  1 1 
ATOM   6    O OG  . SER   A 1 26  ? 111.335 51.488 -0.324  1    60.6  ?  6   SER   A OG  1 1 
ATOM   7    N N   . PRO   A 1 27  ? 109.791 49.448 1.799   1    48.04 ?  7   PRO   A N   1 1 
ATOM   8    C CA  . PRO   A 1 27  ? 109.678 47.993 2.045   1    44.95 ?  7   PRO   A CA  1 1 
ATOM   9    C C   . PRO   A 1 27  ? 110.884 47.17  1.625   1    39.85 ?  7   PRO   A C   1 1 
ATOM   10   O O   . PRO   A 1 27  ? 111.517 47.457 0.606   1    39.71 ?  7   PRO   A O   1 1 
ATOM   11   C CB  . PRO   A 1 27  ? 108.438 47.589 1.237   1    46.93 ?  7   PRO   A CB  1 1 
ATOM   12   C CG  . PRO   A 1 27  ? 107.631 48.866 1.133   1    48.99 ?  7   PRO   A CG  1 1 
ATOM   13   C CD  . PRO   A 1 27  ? 108.655 49.95  1.001   1    47.84 ?  7   PRO   A CD  1 1 
ATOM   14   N N   . ARG   A 1 28  ? 111.224 46.169 2.437   1    36.25 ?  8   ARG   A N   1 1 
ATOM   15   C CA  . ARG   A 1 28  ? 112.328 45.284 2.084   1    34.04 ?  8   ARG   A CA  1 1 
ATOM   16   C C   . ARG   A 1 28  ? 111.912 44.391 0.945   1    30.62 ?  8   ARG   A C   1 1 
ATOM   17   O O   . ARG   A 1 28  ? 110.762 43.96  0.91    1    29.76 ?  8   ARG   A O   1 1 
ATOM   18   C CB  . ARG   A 1 28  ? 112.782 44.43  3.233   1    36.21 ?  8   ARG   A CB  1 1 
ATOM   19   C CG  . ARG   A 1 28  ? 114.26  44.547 3.187   1    39.12 ?  8   ARG   A CG  1 1 
ATOM   20   C CD  . ARG   A 1 28  ? 114.862 44.99  4.485   1    34.62 ?  8   ARG   A CD  1 1 
ATOM   21   N NE  . ARG   A 1 28  ? 115.701 43.844 4.791   1    36.33 ?  8   ARG   A NE  1 1 
ATOM   22   C CZ  . ARG   A 1 28  ? 116.168 43.541 5.975   1    35.1  ?  8   ARG   A CZ  1 1 
ATOM   23   N NH1 . ARG   A 1 28  ? 115.924 44.34  7.02    1    35    ?  8   ARG   A NH1 1 1 
ATOM   24   N NH2 . ARG   A 1 28  ? 116.913 42.451 6.136   1    34.41 ?  8   ARG   A NH2 1 1 
ATOM   25   N N   . ARG   A 1 29  ? 112.791 44.264 -0.044  1    28.43 ?  9   ARG   A N   1 1 
ATOM   26   C CA  . ARG   A 1 29  ? 112.476 43.523 -1.262  1    27.69 ?  9   ARG   A CA  1 1 
ATOM   27   C C   . ARG   A 1 29  ? 113.409 42.342 -1.464  1    27.17 ?  9   ARG   A C   1 1 
ATOM   28   O O   . ARG   A 1 29  ? 114.569 42.344 -1.003  1    29.04 ?  9   ARG   A O   1 1 
ATOM   29   C CB  . ARG   A 1 29  ? 112.62  44.454 -2.472  1    28.86 ?  9   ARG   A CB  1 1 
ATOM   30   C CG  . ARG   A 1 29  ? 111.656 45.62  -2.424  1    33.32 ?  9   ARG   A CG  1 1 
ATOM   31   C CD  . ARG   A 1 29  ? 111.87  46.549 -3.606  1    37.91 ?  9   ARG   A CD  1 1 
ATOM   32   N NE  . ARG   A 1 29  ? 110.961 47.69  -3.499  1    42.04 ?  9   ARG   A NE  1 1 
ATOM   33   C CZ  . ARG   A 1 29  ? 109.786 47.776 -4.117  1    46.32 ?  9   ARG   A CZ  1 1 
ATOM   34   N NH1 . ARG   A 1 29  ? 109.396 46.821 -4.952  1    44.27 ?  9   ARG   A NH1 1 1 
ATOM   35   N NH2 . ARG   A 1 29  ? 109.024 48.858 -3.965  1    47.8  ?  9   ARG   A NH2 1 1 
ATOM   36   N N   . THR   A 1 30  ? 112.941 41.373 -2.256  1    25.09 ?  10  THR   A N   1 1 
ATOM   37   C CA  . THR   A 1 30  ? 113.804 40.236 -2.604  1    24.97 ?  10  THR   A CA  1 1 
ATOM   38   C C   . THR   A 1 30  ? 114.916 40.741 -3.532  1    26.92 ?  10  THR   A C   1 1 
ATOM   39   O O   . THR   A 1 30  ? 114.812 41.876 -4.045  1    26.53 ?  10  THR   A O   1 1 
ATOM   40   C CB  . THR   A 1 30  ? 112.975 39.215 -3.412  1    25.38 ?  10  THR   A CB  1 1 
ATOM   41   O OG1 . THR   A 1 30  ? 112.581 39.801 -4.676  1    27.56 ?  10  THR   A OG1 1 1 
ATOM   42   C CG2 . THR   A 1 30  ? 111.763 38.733 -2.666  1    24.61 ?  10  THR   A CG2 1 1 
ATOM   43   N N   . PRO   A 1 31  ? 115.923 39.909 -3.852  1    27.36 ?  11  PRO   A N   1 1 
ATOM   44   C CA  . PRO   A 1 31  ? 116.94  40.346 -4.819  1    27.38 ?  11  PRO   A CA  1 1 
ATOM   45   C C   . PRO   A 1 31  ? 116.344 40.573 -6.228  1    28.29 ?  11  PRO   A C   1 1 
ATOM   46   O O   . PRO   A 1 31  ? 116.985 41.247 -7.041  1    31.07 ?  11  PRO   A O   1 1 
ATOM   47   C CB  . PRO   A 1 31  ? 117.988 39.233 -4.766  1    28.86 ?  11  PRO   A CB  1 1 
ATOM   48   C CG  . PRO   A 1 31  ? 117.768 38.552 -3.422  1    29.1  ?  11  PRO   A CG  1 1 
ATOM   49   C CD  . PRO   A 1 31  ? 116.279 38.61  -3.236  1    27.42 ?  11  PRO   A CD  1 1 
ATOM   50   N N   . GLN   A 1 32  ? 115.098 40.141 -6.478  1    25.44 ?  12  GLN   A N   1 1 
ATOM   51   C CA  . GLN   A 1 32  ? 114.379 40.374 -7.75   1    26.17 ?  12  GLN   A CA  1 1 
ATOM   52   C C   . GLN   A 1 32  ? 113.376 41.553 -7.636  1    28.63 ?  12  GLN   A C   1 1 
ATOM   53   O O   . GLN   A 1 32  ? 112.516 41.713 -8.504  1    29.29 ?  12  GLN   A O   1 1 
ATOM   54   C CB  . GLN   A 1 32  ? 113.674 39.097 -8.249  1    25.74 ?  12  GLN   A CB  1 1 
ATOM   55   C CG  . GLN   A 1 32  ? 114.637 37.906 -8.391  1    24.88 ?  12  GLN   A CG  1 1 
ATOM   56   C CD  . GLN   A 1 32  ? 114.975 37.227 -7.055  1    26.64 ?  12  GLN   A CD  1 1 
ATOM   57   O OE1 . GLN   A 1 32  ? 114.167 37.221 -6.107  1    27.24 ?  12  GLN   A OE1 1 1 
ATOM   58   N NE2 . GLN   A 1 32  ? 116.164 36.61  -6.989  1    27.06 ?  12  GLN   A NE2 1 1 
ATOM   59   N N   . SER   A 1 33  ? 113.52  42.349 -6.559  1    28.74 ?  13  SER   A N   1 1 
ATOM   60   C CA  A SER   A 1 33  ? 112.797 43.564 -6.16   0.44 29.58 ?  13  SER   A CA  1 1 
ATOM   61   C CA  B SER   A 1 33  ? 112.766 43.577 -6.282  0.56 29.14 ?  13  SER   A CA  1 1 
ATOM   62   C C   . SER   A 1 33  ? 111.283 43.375 -5.922  1    30.29 ?  13  SER   A C   1 1 
ATOM   63   O O   . SER   A 1 33  ? 110.501 44.315 -6.11   1    33.47 ?  13  SER   A O   1 1 
ATOM   64   C CB  A SER   A 1 33  ? 113.059 44.727 -7.113  0.44 31.22 ?  13  SER   A CB  1 1 
ATOM   65   C CB  B SER   A 1 33  ? 112.897 44.581 -7.433  0.56 29.86 ?  13  SER   A CB  1 1 
ATOM   66   O OG  A SER   A 1 33  ? 112.51  44.457 -8.385  0.44 32.58 ?  13  SER   A OG  1 1 
ATOM   67   O OG  B SER   A 1 33  ? 114.261 44.791 -7.754  0.56 30.29 ?  13  SER   A OG  1 1 
ATOM   68   N N   . ILE   A 1 34  ? 110.874 42.216 -5.371  1    28.48 ?  14  ILE   A N   1 1 
ATOM   69   C CA  . ILE   A 1 34  ? 109.47  42.031 -4.995  1    27.99 ?  14  ILE   A CA  1 1 
ATOM   70   C C   . ILE   A 1 34  ? 109.387 42.314 -3.51   1    28.16 ?  14  ILE   A C   1 1 
ATOM   71   O O   . ILE   A 1 34  ? 110.191 41.756 -2.756  1    27.98 ?  14  ILE   A O   1 1 
ATOM   72   C CB  . ILE   A 1 34  ? 108.976 40.595 -5.265  1    28.43 ?  14  ILE   A CB  1 1 
ATOM   73   C CG1 . ILE   A 1 34  ? 109.075 40.299 -6.785  1    30.33 ?  14  ILE   A CG1 1 1 
ATOM   74   C CG2 . ILE   A 1 34  ? 107.545 40.428 -4.731  1    28.14 ?  14  ILE   A CG2 1 1 
ATOM   75   C CD1 . ILE   A 1 34  ? 108.324 39.021 -7.285  1    34.56 ?  14  ILE   A CD1 1 1 
ATOM   76   N N   . PRO   A 1 35  ? 108.46  43.162 -3.005  1    28.4  ?  15  PRO   A N   1 1 
ATOM   77   C CA  . PRO   A 1 35  ? 108.42  43.395 -1.542  1    27.28 ?  15  PRO   A CA  1 1 
ATOM   78   C C   . PRO   A 1 35  ? 108.154 42.096 -0.79   1    26.54 ?  15  PRO   A C   1 1 
ATOM   79   O O   . PRO   A 1 35  ? 107.248 41.359 -1.155  1    27.69 ?  15  PRO   A O   1 1 
ATOM   80   C CB  . PRO   A 1 35  ? 107.245 44.389 -1.364  1    28.73 ?  15  PRO   A CB  1 1 
ATOM   81   C CG  . PRO   A 1 35  ? 107.072 45.05  -2.748  1    29.8  ?  15  PRO   A CG  1 1 
ATOM   82   C CD  . PRO   A 1 35  ? 107.43  43.949 -3.73   1    28.29 ?  15  PRO   A CD  1 1 
ATOM   83   N N   . TYR   A 1 36  ? 108.912 41.832 0.305   1    25.8  ?  16  TYR   A N   1 1 
ATOM   84   C CA  . TYR   A 1 36  ? 108.644 40.65  1.127   1    26.6  ?  16  TYR   A CA  1 1 
ATOM   85   C C   . TYR   A 1 36  ? 107.257 40.714 1.749   1    27.99 ?  16  TYR   A C   1 1 
ATOM   86   O O   . TYR   A 1 36  ? 106.696 39.658 2.005   1    28.63 ?  16  TYR   A O   1 1 
ATOM   87   C CB  . TYR   A 1 36  ? 109.671 40.434 2.228   1    25.55 ?  16  TYR   A CB  1 1 
ATOM   88   C CG  . TYR   A 1 36  ? 110.948 39.844 1.696   1    23.77 ?  16  TYR   A CG  1 1 
ATOM   89   C CD1 . TYR   A 1 36  ? 111.026 38.489 1.343   1    23.18 ?  16  TYR   A CD1 1 1 
ATOM   90   C CD2 . TYR   A 1 36  ? 112.07  40.629 1.518   1    23.54 ?  16  TYR   A CD2 1 1 
ATOM   91   C CE1 . TYR   A 1 36  ? 112.188 37.952 0.819   1    22.75 ?  16  TYR   A CE1 1 1 
ATOM   92   C CE2 . TYR   A 1 36  ? 113.26  40.085 1.051   1    23.5  ?  16  TYR   A CE2 1 1 
ATOM   93   C CZ  . TYR   A 1 36  ? 113.289 38.756 0.629   1    22.95 ?  16  TYR   A CZ  1 1 
ATOM   94   O OH  . TYR   A 1 36  ? 114.449 38.242 0.119   1    24.24 ?  16  TYR   A OH  1 1 
ATOM   95   N N   . GLN   A 1 37  ? 106.658 41.936 1.922   1    27.85 ?  17  GLN   A N   1 1 
ATOM   96   C CA  . GLN   A 1 37  ? 105.276 41.972 2.46    1    29.54 ?  17  GLN   A CA  1 1 
ATOM   97   C C   . GLN   A 1 37  ? 104.249 41.356 1.53    1    30.59 ?  17  GLN   A C   1 1 
ATOM   98   O O   . GLN   A 1 37  ? 103.143 41.017 1.976   1    32.72 ?  17  GLN   A O   1 1 
ATOM   99   C CB  . GLN   A 1 37  ? 104.84  43.394 2.862   1    31.08 ?  17  GLN   A CB  1 1 
ATOM   100  C CG  . GLN   A 1 37  ? 104.772 44.307 1.656   1    35.99 ?  17  GLN   A CG  1 1 
ATOM   101  C CD  . GLN   A 1 37  ? 104.456 45.739 2.045   1    45.45 ?  17  GLN   A CD  1 1 
ATOM   102  O OE1 . GLN   A 1 37  ? 104.276 46.079 3.222   1    48.93 ?  17  GLN   A OE1 1 1 
ATOM   103  N NE2 . GLN   A 1 37  ? 104.392 46.601 1.052   1    46.7  ?  17  GLN   A NE2 1 1 
ATOM   104  N N   . ASP   A 1 38  ? 104.619 41.105 0.258   1    29.03 ?  18  ASP   A N   1 1 
ATOM   105  C CA  . ASP   A 1 38  ? 103.689 40.466 -0.669  1    29.55 ?  18  ASP   A CA  1 1 
ATOM   106  C C   . ASP   A 1 38  ? 103.956 38.948 -0.762  1    29.55 ?  18  ASP   A C   1 1 
ATOM   107  O O   . ASP   A 1 38  ? 103.312 38.296 -1.577  1    30.52 ?  18  ASP   A O   1 1 
ATOM   108  C CB  . ASP   A 1 38  ? 103.892 41.052 -2.064  1    31.72 ?  18  ASP   A CB  1 1 
ATOM   109  C CG  . ASP   A 1 38  ? 103.495 42.517 -2.236  1    40.78 ?  18  ASP   A CG  1 1 
ATOM   110  O OD1 . ASP   A 1 38  ? 102.937 43.107 -1.277  1    40.11 ?  18  ASP   A OD1 1 1 
ATOM   111  O OD2 . ASP   A 1 38  ? 103.764 43.076 -3.319  1    45.19 ?  18  ASP   A OD2 1 1 
ATOM   112  N N   . LEU   A 1 39  ? 104.929 38.395 0.005   1    28.08 ?  19  LEU   A N   1 1 
ATOM   113  C CA  . LEU   A 1 39  ? 105.315 36.991 -0.123  1    28.75 ?  19  LEU   A CA  1 1 
ATOM   114  C C   . LEU   A 1 39  ? 105.353 36.312 1.233   1    29.17 ?  19  LEU   A C   1 1 
ATOM   115  O O   . LEU   A 1 39  ? 105.67  36.948 2.253   1    28.88 ?  19  LEU   A O   1 1 
ATOM   116  C CB  . LEU   A 1 39  ? 106.748 36.956 -0.68   1    28.75 ?  19  LEU   A CB  1 1 
ATOM   117  C CG  . LEU   A 1 39  ? 106.926 37.565 -2.093  1    29.82 ?  19  LEU   A CG  1 1 
ATOM   118  C CD1 . LEU   A 1 39  ? 108.378 37.587 -2.487  1    30.45 ?  19  LEU   A CD1 1 1 
ATOM   119  C CD2 . LEU   A 1 39  ? 106.145 36.8   -3.126  1    30.4  ?  19  LEU   A CD2 1 1 
ATOM   120  N N   . PRO   A 1 40  ? 105.129 34.987 1.271   1    28.39 ?  20  PRO   A N   1 1 
ATOM   121  C CA  . PRO   A 1 40  ? 105.36  34.256 2.535   1    27.03 ?  20  PRO   A CA  1 1 
ATOM   122  C C   . PRO   A 1 40  ? 106.864 34.358 2.86    1    25.18 ?  20  PRO   A C   1 1 
ATOM   123  O O   . PRO   A 1 40  ? 107.718 34.198 1.948   1    24.58 ?  20  PRO   A O   1 1 
ATOM   124  C CB  . PRO   A 1 40  ? 104.961 32.797 2.199   1    28.8  ?  20  PRO   A CB  1 1 
ATOM   125  C CG  . PRO   A 1 40  ? 104.256 32.835 0.896   1    30.62 ?  20  PRO   A CG  1 1 
ATOM   126  C CD  . PRO   A 1 40  ? 104.777 34.072 0.159   1    29    ?  20  PRO   A CD  1 1 
ATOM   127  N N   . HIS   A 1 41  ? 107.184 34.663 4.128   1    24.96 ?  21  HIS   A N   1 1 
ATOM   128  C CA  . HIS   A 1 41  ? 108.584 34.847 4.484   1    24.78 ?  21  HIS   A CA  1 1 
ATOM   129  C C   . HIS   A 1 41  ? 108.816 34.588 5.949   1    25.89 ?  21  HIS   A C   1 1 
ATOM   130  O O   . HIS   A 1 41  ? 107.871 34.408 6.72    1    28.57 ?  21  HIS   A O   1 1 
ATOM   131  C CB  . HIS   A 1 41  ? 109.083 36.28  4.097   1    23.85 ?  21  HIS   A CB  1 1 
ATOM   132  C CG  . HIS   A 1 41  ? 108.4   37.392 4.842   1    25.85 ?  21  HIS   A CG  1 1 
ATOM   133  N ND1 . HIS   A 1 41  ? 107.201 37.922 4.396   1    28.88 ?  21  HIS   A ND1 1 1 
ATOM   134  C CD2 . HIS   A 1 41  ? 108.721 37.978 6.031   1    29.8  ?  21  HIS   A CD2 1 1 
ATOM   135  C CE1 . HIS   A 1 41  ? 106.869 38.878 5.272   1    30.27 ?  21  HIS   A CE1 1 1 
ATOM   136  N NE2 . HIS   A 1 41  ? 107.72  38.909 6.301   1    31.54 ?  21  HIS   A NE2 1 1 
ATOM   137  N N   . LEU   A 1 42  ? 110.072 34.569 6.315   1    25.23 ?  22  LEU   A N   1 1 
ATOM   138  C CA  . LEU   A 1 42  ? 110.52  34.393 7.702   1    26.66 ?  22  LEU   A CA  1 1 
ATOM   139  C C   . LEU   A 1 42  ? 111.807 35.213 7.822   1    28.17 ?  22  LEU   A C   1 1 
ATOM   140  O O   . LEU   A 1 42  ? 112.538 35.372 6.857   1    31.03 ?  22  LEU   A O   1 1 
ATOM   141  C CB  . LEU   A 1 42  ? 110.85  32.873 7.866   1    28.71 ?  22  LEU   A CB  1 1 
ATOM   142  C CG  . LEU   A 1 42  ? 111.103 32.315 9.208   1    36.11 ?  22  LEU   A CG  1 1 
ATOM   143  C CD1 . LEU   A 1 42  ? 109.825 32.38  10.068  1    37.11 ?  22  LEU   A CD1 1 1 
ATOM   144  C CD2 . LEU   A 1 42  ? 111.527 30.863 9.025   1    36.72 ?  22  LEU   A CD2 1 1 
ATOM   145  N N   . VAL   A 1 43  ? 112.061 35.845 8.978   1    23.39 ?  23  VAL   A N   1 1 
ATOM   146  C CA  . VAL   A 1 43  ? 113.324 36.553 9.166   1    24.16 ?  23  VAL   A CA  1 1 
ATOM   147  C C   . VAL   A 1 43  ? 114.238 35.688 10.064  1    25.15 ?  23  VAL   A C   1 1 
ATOM   148  O O   . VAL   A 1 43  ? 113.837 35.254 11.154  1    26.08 ?  23  VAL   A O   1 1 
ATOM   149  C CB  . VAL   A 1 43  ? 113.073 37.944 9.799   1    25.14 ?  23  VAL   A CB  1 1 
ATOM   150  C CG1 . VAL   A 1 43  ? 114.39  38.687 9.871   1    25.76 ?  23  VAL   A CG1 1 1 
ATOM   151  C CG2 . VAL   A 1 43  ? 112.067 38.75  8.977   1    25.45 ?  23  VAL   A CG2 1 1 
ATOM   152  N N   . ASN   A 1 44  ? 115.468 35.421 9.601   1    24.79 ?  24  ASN   A N   1 1 
ATOM   153  C CA  . ASN   A 1 44  ? 116.361 34.559 10.341  1    24.38 ?  24  ASN   A CA  1 1 
ATOM   154  C C   . ASN   A 1 44  ? 117.061 35.293 11.52   1    26.64 ?  24  ASN   A C   1 1 
ATOM   155  O O   . ASN   A 1 44  ? 116.837 36.503 11.759  1    27.42 ?  24  ASN   A O   1 1 
ATOM   156  C CB  . ASN   A 1 44  ? 117.34  33.8   9.394   1    25.67 ?  24  ASN   A CB  1 1 
ATOM   157  C CG  . ASN   A 1 44  ? 118.493 34.618 8.898   1    26.35 ?  24  ASN   A CG  1 1 
ATOM   158  O OD1 . ASN   A 1 44  ? 118.636 35.788 9.262   1    26.01 ?  24  ASN   A OD1 1 1 
ATOM   159  N ND2 . ASN   A 1 44  ? 119.312 34.067 7.985   1    25.08 ?  24  ASN   A ND2 1 1 
ATOM   160  N N   . ALA   A 1 45  ? 117.897 34.557 12.25   1    28.08 ?  25  ALA   A N   1 1 
ATOM   161  C CA  . ALA   A 1 45  ? 118.594 35.112 13.416  1    30.15 ?  25  ALA   A CA  1 1 
ATOM   162  C C   . ALA   A 1 45  ? 119.552 36.23  13.086  1    32.18 ?  25  ALA   A C   1 1 
ATOM   163  O O   . ALA   A 1 45  ? 119.855 37.034 13.98   1    34.76 ?  25  ALA   A O   1 1 
ATOM   164  C CB  . ALA   A 1 45  ? 119.315 34.016 14.183  1    30.13 ?  25  ALA   A CB  1 1 
ATOM   165  N N   . ASP   A 1 46  ? 120.011 36.327 11.844  1    31.53 ?  26  ASP   A N   1 1 
ATOM   166  C CA  . ASP   A 1 46  ? 120.875 37.389 11.377  1    32.25 ?  26  ASP   A CA  1 1 
ATOM   167  C C   . ASP   A 1 46  ? 120.098 38.574 10.796  1    32.04 ?  26  ASP   A C   1 1 
ATOM   168  O O   . ASP   A 1 46  ? 120.723 39.455 10.21   1    33.19 ?  26  ASP   A O   1 1 
ATOM   169  C CB  . ASP   A 1 46  ? 121.856 36.856 10.327  1    34.32 ?  26  ASP   A CB  1 1 
ATOM   170  C CG  . ASP   A 1 46  ? 122.863 35.918 10.936  1    41.96 ?  26  ASP   A CG  1 1 
ATOM   171  O OD1 . ASP   A 1 46  ? 123.296 36.181 12.071  1    46.19 ?  26  ASP   A OD1 1 1 
ATOM   172  O OD2 . ASP   A 1 46  ? 123.193 34.886 10.287  1    41    ?  26  ASP   A OD2 1 1 
ATOM   173  N N   . GLY   A 1 47  ? 118.765 38.568 10.88   1    30.05 ?  27  GLY   A N   1 1 
ATOM   174  C CA  . GLY   A 1 47  ? 117.939 39.638 10.333  1    28.64 ?  27  GLY   A CA  1 1 
ATOM   175  C C   . GLY   A 1 47  ? 117.747 39.587 8.831   1    28.57 ?  27  GLY   A C   1 1 
ATOM   176  O O   . GLY   A 1 47  ? 117.286 40.553 8.227   1    29.15 ?  27  GLY   A O   1 1 
ATOM   177  N N   . GLN   A 1 48  ? 118.063 38.437 8.213   1    26.5  ?  28  GLN   A N   1 1 
ATOM   178  C CA  . GLN   A 1 48  ? 117.893 38.272 6.763   1    26.58 ?  28  GLN   A CA  1 1 
ATOM   179  C C   . GLN   A 1 48  ? 116.535 37.638 6.461   1    25.42 ?  28  GLN   A C   1 1 
ATOM   180  O O   . GLN   A 1 48  ? 116.111 36.671 7.117   1    24.68 ?  28  GLN   A O   1 1 
ATOM   181  C CB  . GLN   A 1 48  ? 118.998 37.383 6.157   1    27.68 ?  28  GLN   A CB  1 1 
ATOM   182  C CG  . GLN   A 1 48  ? 120.399 37.938 6.344   1    29.7  ?  28  GLN   A CG  1 1 
ATOM   183  C CD  . GLN   A 1 48  ? 121.466 36.902 6.074   1    31.05 ?  28  GLN   A CD  1 1 
ATOM   184  O OE1 . GLN   A 1 48  ? 121.508 35.816 6.708   1    29.8  ?  28  GLN   A OE1 1 1 
ATOM   185  N NE2 . GLN   A 1 48  ? 122.34  37.22  5.14    1    33.14 ?  28  GLN   A NE2 1 1 
ATOM   186  N N   . TYR   A 1 49  ? 115.853 38.183 5.45    1    24.37 ?  29  TYR   A N   1 1 
ATOM   187  C CA  . TYR   A 1 49  ? 114.561 37.647 5.016   1    23.2  ?  29  TYR   A CA  1 1 
ATOM   188  C C   . TYR   A 1 49  ? 114.727 36.38  4.161   1    23.83 ?  29  TYR   A C   1 1 
ATOM   189  O O   . TYR   A 1 49  ? 115.498 36.413 3.18    1    24.39 ?  29  TYR   A O   1 1 
ATOM   190  C CB  . TYR   A 1 49  ? 113.801 38.689 4.178   1    22.73 ?  29  TYR   A CB  1 1 
ATOM   191  C CG  . TYR   A 1 49  ? 113.082 39.718 5.027   1    25    ?  29  TYR   A CG  1 1 
ATOM   192  C CD1 . TYR   A 1 49  ? 113.787 40.668 5.744   1    26.78 ?  29  TYR   A CD1 1 1 
ATOM   193  C CD2 . TYR   A 1 49  ? 111.7   39.724 5.124   1    25.62 ?  29  TYR   A CD2 1 1 
ATOM   194  C CE1 . TYR   A 1 49  ? 113.138 41.645 6.478   1    26.37 ?  29  TYR   A CE1 1 1 
ATOM   195  C CE2 . TYR   A 1 49  ? 111.032 40.721 5.824   1    26.04 ?  29  TYR   A CE2 1 1 
ATOM   196  C CZ  . TYR   A 1 49  ? 111.758 41.695 6.478   1    26.84 ?  29  TYR   A CZ  1 1 
ATOM   197  O OH  . TYR   A 1 49  ? 111.115 42.656 7.243   1    27.79 ?  29  TYR   A OH  1 1 
ATOM   198  N N   . LEU   A 1 50  ? 114     35.333 4.515   1    22.57 ?  30  LEU   A N   1 1 
ATOM   199  C CA  . LEU   A 1 50  ? 113.998 34.106 3.716   1    22.21 ?  30  LEU   A CA  1 1 
ATOM   200  C C   . LEU   A 1 50  ? 112.648 34.003 3.067   1    22.99 ?  30  LEU   A C   1 1 
ATOM   201  O O   . LEU   A 1 50  ? 111.614 34.074 3.747   1    23.3  ?  30  LEU   A O   1 1 
ATOM   202  C CB  . LEU   A 1 50  ? 114.22  32.858 4.641   1    22.39 ?  30  LEU   A CB  1 1 
ATOM   203  C CG  . LEU   A 1 50  ? 115.482 32.864 5.481   1    25.43 ?  30  LEU   A CG  1 1 
ATOM   204  C CD1 . LEU   A 1 50  ? 115.656 31.521 6.158   1    27.09 ?  30  LEU   A CD1 1 1 
ATOM   205  C CD2 . LEU   A 1 50  ? 116.727 33.148 4.63    1    27.08 ?  30  LEU   A CD2 1 1 
ATOM   206  N N   . PHE   A 1 51  ? 112.64  33.71  1.763   1    21.64 ?  31  PHE   A N   1 1 
ATOM   207  C CA  . PHE   A 1 51  ? 111.389 33.505 1.066   1    22.89 ?  31  PHE   A CA  1 1 
ATOM   208  C C   . PHE   A 1 51  ? 110.905 32.059 1.385   1    22.75 ?  31  PHE   A C   1 1 
ATOM   209  O O   . PHE   A 1 51  ? 111.712 31.107 1.325   1    22.59 ?  31  PHE   A O   1 1 
ATOM   210  C CB  . PHE   A 1 51  ? 111.676 33.587 -0.427  1    22.06 ?  31  PHE   A CB  1 1 
ATOM   211  C CG  . PHE   A 1 51  ? 110.538 33.055 -1.265  1    22.76 ?  31  PHE   A CG  1 1 
ATOM   212  C CD1 . PHE   A 1 51  ? 109.395 33.809 -1.463  1    24.76 ?  31  PHE   A CD1 1 1 
ATOM   213  C CD2 . PHE   A 1 51  ? 110.607 31.788 -1.841  1    23.98 ?  31  PHE   A CD2 1 1 
ATOM   214  C CE1 . PHE   A 1 51  ? 108.348 33.316 -2.234  1    26.2  ?  31  PHE   A CE1 1 1 
ATOM   215  C CE2 . PHE   A 1 51  ? 109.544 31.289 -2.584  1    25.56 ?  31  PHE   A CE2 1 1 
ATOM   216  C CZ  . PHE   A 1 51  ? 108.428 32.06  -2.771  1    25.94 ?  31  PHE   A CZ  1 1 
ATOM   217  N N   . CYS   A 1 52  ? 109.599 31.897 1.692   1    22.19 ?  32  CYS   A N   1 1 
ATOM   218  C CA  . CYS   A 1 52  ? 108.997 30.617 2.075   1    23.11 ?  32  CYS   A CA  1 1 
ATOM   219  C C   . CYS   A 1 52  ? 107.961 30.126 1.085   1    23.76 ?  32  CYS   A C   1 1 
ATOM   220  O O   . CYS   A 1 52  ? 107.274 30.923 0.442   1    24    ?  32  CYS   A O   1 1 
ATOM   221  C CB  . CYS   A 1 52  ? 108.359 30.718 3.463   1    24.44 ?  32  CYS   A CB  1 1 
ATOM   222  S SG  . CYS   A 1 52  ? 109.524 31.146 4.781   1    26.12 ?  32  CYS   A SG  1 1 
ATOM   223  N N   . ARG   A 1 53  ? 107.749 28.779 1.074   1    23.17 ?  33  ARG   A N   1 1 
ATOM   224  C CA  . ARG   A 1 53  ? 106.686 28.166 0.269   1    23.95 ?  33  ARG   A CA  1 1 
ATOM   225  C C   . ARG   A 1 53  ? 105.941 27.142 1.136   1    25.33 ?  33  ARG   A C   1 1 
ATOM   226  O O   . ARG   A 1 53  ? 106.561 26.49  1.984   1    25.16 ?  33  ARG   A O   1 1 
ATOM   227  C CB  . ARG   A 1 53  ? 107.267 27.366 -0.896  1    25.75 ?  33  ARG   A CB  1 1 
ATOM   228  C CG  . ARG   A 1 53  ? 107.945 28.178 -1.909  1    26.84 ?  33  ARG   A CG  1 1 
ATOM   229  C CD  . ARG   A 1 53  ? 108.203 27.316 -3.168  1    27.09 ?  33  ARG   A CD  1 1 
ATOM   230  N NE  . ARG   A 1 53  ? 109.025 28.101 -4.077  1    25.12 ?  33  ARG   A NE  1 1 
ATOM   231  C CZ  . ARG   A 1 53  ? 108.544 28.863 -5.048  1    26.49 ?  33  ARG   A CZ  1 1 
ATOM   232  N NH1 . ARG   A 1 53  ? 107.251 28.818 -5.358  1    27.14 ?  33  ARG   A NH1 1 1 
ATOM   233  N NH2 . ARG   A 1 53  ? 109.355 29.635 -5.757  1    25.83 ?  33  ARG   A NH2 1 1 
ATOM   234  N N   . TYR   A 1 54  ? 104.61  27.012 0.918   1    27.14 ?  34  TYR   A N   1 1 
ATOM   235  C CA  . TYR   A 1 54  ? 103.777 26.069 1.655   1    28.03 ?  34  TYR   A CA  1 1 
ATOM   236  C C   . TYR   A 1 54  ? 102.834 25.363 0.696   1    29.34 ?  34  TYR   A C   1 1 
ATOM   237  O O   . TYR   A 1 54  ? 102.328 25.993 -0.239  1    30.15 ?  34  TYR   A O   1 1 
ATOM   238  C CB  . TYR   A 1 54  ? 102.931 26.781 2.738   1    28.09 ?  34  TYR   A CB  1 1 
ATOM   239  C CG  . TYR   A 1 54  ? 103.795 27.531 3.729   1    27.31 ?  34  TYR   A CG  1 1 
ATOM   240  C CD1 . TYR   A 1 54  ? 104.401 26.87  4.789   1    27.29 ?  34  TYR   A CD1 1 1 
ATOM   241  C CD2 . TYR   A 1 54  ? 104.072 28.886 3.556   1    27.78 ?  34  TYR   A CD2 1 1 
ATOM   242  C CE1 . TYR   A 1 54  ? 105.286 27.522 5.636   1    26.96 ?  34  TYR   A CE1 1 1 
ATOM   243  C CE2 . TYR   A 1 54  ? 104.944 29.555 4.409   1    28.4  ?  34  TYR   A CE2 1 1 
ATOM   244  C CZ  . TYR   A 1 54  ? 105.574 28.858 5.424   1    28.02 ?  34  TYR   A CZ  1 1 
ATOM   245  O OH  . TYR   A 1 54  ? 106.448 29.492 6.27    1    28.76 ?  34  TYR   A OH  1 1 
ATOM   246  N N   . TRP   A 1 55  ? 102.623 24.059 0.911   1    28.43 ?  35  TRP   A N   1 1 
ATOM   247  C CA  . TRP   A 1 55  ? 101.688 23.267 0.136   1    29.52 ?  35  TRP   A CA  1 1 
ATOM   248  C C   . TRP   A 1 55  ? 100.919 22.459 1.18    1    31.24 ?  35  TRP   A C   1 1 
ATOM   249  O O   . TRP   A 1 55  ? 101.434 21.485 1.73    1    32.35 ?  35  TRP   A O   1 1 
ATOM   250  C CB  . TRP   A 1 55  ? 102.416 22.364 -0.864  1    28.72 ?  35  TRP   A CB  1 1 
ATOM   251  C CG  . TRP   A 1 55  ? 103.304 23.016 -1.892  1    28.25 ?  35  TRP   A CG  1 1 
ATOM   252  C CD1 . TRP   A 1 55  ? 102.993 23.238 -3.207  1    29.78 ?  35  TRP   A CD1 1 1 
ATOM   253  C CD2 . TRP   A 1 55  ? 104.709 23.317 -1.76   1    25.95 ?  35  TRP   A CD2 1 1 
ATOM   254  N NE1 . TRP   A 1 55  ? 104.115 23.646 -3.902  1    29.2  ?  35  TRP   A NE1 1 1 
ATOM   255  C CE2 . TRP   A 1 55  ? 105.183 23.686 -3.042  1    27.08 ?  35  TRP   A CE2 1 1 
ATOM   256  C CE3 . TRP   A 1 55  ? 105.617 23.275 -0.691  1    24.61 ?  35  TRP   A CE3 1 1 
ATOM   257  C CZ2 . TRP   A 1 55  ? 106.523 24.045 -3.277  1    25.16 ?  35  TRP   A CZ2 1 1 
ATOM   258  C CZ3 . TRP   A 1 55  ? 106.947 23.604 -0.933  1    23.69 ?  35  TRP   A CZ3 1 1 
ATOM   259  C CH2 . TRP   A 1 55  ? 107.395 23.928 -2.221  1    24.09 ?  35  TRP   A CH2 1 1 
ATOM   260  N N   . ALA   A 1 56  ? 99.711  22.893 1.517   1    32.6  ?  36  ALA   A N   1 1 
ATOM   261  C CA  . ALA   A 1 56  ? 98.922  22.25  2.572   1    35.07 ?  36  ALA   A CA  1 1 
ATOM   262  C C   . ALA   A 1 56  ? 97.724  21.511 2.019   1    38.32 ?  36  ALA   A C   1 1 
ATOM   263  O O   . ALA   A 1 56  ? 97.088  21.993 1.083   1    38.8  ?  36  ALA   A O   1 1 
ATOM   264  C CB  . ALA   A 1 56  ? 98.469  23.294 3.585   1    36.03 ?  36  ALA   A CB  1 1 
ATOM   265  N N   . PRO   A 1 57  ? 97.417  20.307 2.56    1    39.91 ?  37  PRO   A N   1 1 
ATOM   266  C CA  . PRO   A 1 57  ? 96.234  19.573 2.074   1    42.68 ?  37  PRO   A CA  1 1 
ATOM   267  C C   . PRO   A 1 57  ? 94.927  20.239 2.512   1    47.95 ?  37  PRO   A C   1 1 
ATOM   268  O O   . PRO   A 1 57  ? 94.938  21.098 3.392   1    48.03 ?  37  PRO   A O   1 1 
ATOM   269  C CB  . PRO   A 1 57  ? 96.387  18.179 2.705   1    42.27 ?  37  PRO   A CB  1 1 
ATOM   270  C CG  . PRO   A 1 57  ? 97.211  18.386 3.916   1    41.32 ?  37  PRO   A CG  1 1 
ATOM   271  C CD  . PRO   A 1 57  ? 98.088  19.601 3.671   1    39.51 ?  37  PRO   A CD  1 1 
ATOM   272  N N   . THR   A 1 58  ? 93.798  19.834 1.907   1    51.51 ?  38  THR   A N   1 1 
ATOM   273  C CA  . THR   A 1 58  ? 92.5    20.409 2.278   1    54.58 ?  38  THR   A CA  1 1 
ATOM   274  C C   . THR   A 1 58  ? 92.06   19.975 3.681   1    57.01 ?  38  THR   A C   1 1 
ATOM   275  O O   . THR   A 1 58  ? 91.362  20.721 4.36    1    57.83 ?  38  THR   A O   1 1 
ATOM   276  C CB  . THR   A 1 58  ? 91.445  20.122 1.205   1    56.46 ?  38  THR   A CB  1 1 
ATOM   277  O OG1 . THR   A 1 58  ? 91.371  18.711 0.993   1    58.39 ?  38  THR   A OG1 1 1 
ATOM   278  C CG2 . THR   A 1 58  ? 91.749  20.824 -0.107  1    56.8  ?  38  THR   A CG2 1 1 
ATOM   279  N N   . GLY   A 1 59  ? 92.477  18.788 4.112   1    58.05 ?  39  GLY   A N   1 1 
ATOM   280  C CA  . GLY   A 1 59  ? 92.111  18.284 5.429   1    59.08 ?  39  GLY   A CA  1 1 
ATOM   281  C C   . GLY   A 1 59  ? 93.157  18.494 6.509   1    59.15 ?  39  GLY   A C   1 1 
ATOM   282  O O   . GLY   A 1 59  ? 94.052  19.335 6.376   1    59.79 ?  39  GLY   A O   1 1 
ATOM   283  N N   . THR   A 1 60  ? 93.033  17.735 7.609   1    57.82 ?  40  THR   A N   1 1 
ATOM   284  C CA  . THR   A 1 60  ? 94.007  17.809 8.689   1    56.39 ?  40  THR   A CA  1 1 
ATOM   285  C C   . THR   A 1 60  ? 95.25   17.039 8.226   1    52.71 ?  40  THR   A C   1 1 
ATOM   286  O O   . THR   A 1 60  ? 95.132  15.914 7.741   1    52.86 ?  40  THR   A O   1 1 
ATOM   287  C CB  . THR   A 1 60  ? 93.406  17.243 9.98    1    58.98 ?  40  THR   A CB  1 1 
ATOM   288  O OG1 . THR   A 1 60  ? 92.47   18.203 10.493  1    61.3  ?  40  THR   A OG1 1 1 
ATOM   289  C CG2 . THR   A 1 60  ? 94.462  16.958 11.035  1    59.31 ?  40  THR   A CG2 1 1 
ATOM   290  N N   . PRO   A 1 61  ? 96.428  17.671 8.271   1    49.54 ?  41  PRO   A N   1 1 
ATOM   291  C CA  . PRO   A 1 61  ? 97.633  16.985 7.784   1    47.61 ?  41  PRO   A CA  1 1 
ATOM   292  C C   . PRO   A 1 61  ? 98.063  15.844 8.701   1    45.75 ?  41  PRO   A C   1 1 
ATOM   293  O O   . PRO   A 1 61  ? 97.896  15.93  9.915   1    46.82 ?  41  PRO   A O   1 1 
ATOM   294  C CB  . PRO   A 1 61  ? 98.684  18.099 7.697   1    48.27 ?  41  PRO   A CB  1 1 
ATOM   295  C CG  . PRO   A 1 61  ? 98.203  19.162 8.614   1    49.63 ?  41  PRO   A CG  1 1 
ATOM   296  C CD  . PRO   A 1 61  ? 96.714  19.034 8.755   1    48.67 ?  41  PRO   A CD  1 1 
ATOM   297  N N   . LYS   A 1 62  ? 98.562  14.758 8.117   1    42.93 ?  42  LYS   A N   1 1 
ATOM   298  C CA  . LYS   A 1 62  ? 99.059  13.628 8.888   1    41.26 ?  42  LYS   A CA  1 1 
ATOM   299  C C   . LYS   A 1 62  ? 100.457 13.93  9.446   1    38.28 ?  42  LYS   A C   1 1 
ATOM   300  O O   . LYS   A 1 62  ? 100.852 13.356 10.46   1    37.9  ?  42  LYS   A O   1 1 
ATOM   301  C CB  . LYS   A 1 62  ? 99.187  12.398 7.983   1    44.55 ?  42  LYS   A CB  1 1 
ATOM   302  C CG  . LYS   A 1 62  ? 97.885  11.874 7.415   1    51.45 ?  42  LYS   A CG  1 1 
ATOM   303  C CD  . LYS   A 1 62  ? 98.188  10.713 6.47    1    58.92 ?  42  LYS   A CD  1 1 
ATOM   304  C CE  . LYS   A 1 62  ? 96.973  10.075 5.827   1    64.49 ?  42  LYS   A CE  1 1 
ATOM   305  N NZ  . LYS   A 1 62  ? 97.347  9.272  4.624   1    66.96 ?  42  LYS   A NZ  1 1 
ATOM   306  N N   . ALA   A 1 63  ? 101.25  14.785 8.733   1    34.96 ?  43  ALA   A N   1 1 
ATOM   307  C CA  . ALA   A 1 63  ? 102.617 15.068 9.142   1    32.51 ?  43  ALA   A CA  1 1 
ATOM   308  C C   . ALA   A 1 63  ? 103.083 16.334 8.426   1    30.56 ?  43  ALA   A C   1 1 
ATOM   309  O O   . ALA   A 1 63  ? 102.422 16.797 7.503   1    30.15 ?  43  ALA   A O   1 1 
ATOM   310  C CB  . ALA   A 1 63  ? 103.53  13.885 8.763   1    32.26 ?  43  ALA   A CB  1 1 
ATOM   311  N N   . LEU   A 1 64  ? 104.186 16.882 8.861   1    29.71 ?  44  LEU   A N   1 1 
ATOM   312  C CA  . LEU   A 1 64  ? 104.837 18.005 8.229   1    28.9  ?  44  LEU   A CA  1 1 
ATOM   313  C C   . LEU   A 1 64  ? 106.09  17.496 7.535   1    27.32 ?  44  LEU   A C   1 1 
ATOM   314  O O   . LEU   A 1 64  ? 106.727 16.564 8.017   1    27.48 ?  44  LEU   A O   1 1 
ATOM   315  C CB  . LEU   A 1 64  ? 105.278 18.988 9.3     1    30.19 ?  44  LEU   A CB  1 1 
ATOM   316  C CG  . LEU   A 1 64  ? 104.179 19.499 10.256  1    33.96 ?  44  LEU   A CG  1 1 
ATOM   317  C CD1 . LEU   A 1 64  ? 104.799 20.432 11.308  1    35.33 ?  44  LEU   A CD1 1 1 
ATOM   318  C CD2 . LEU   A 1 64  ? 103.069 20.179 9.481   1    35.58 ?  44  LEU   A CD2 1 1 
ATOM   319  N N   . ILE   A 1 65  ? 106.501 18.178 6.442   1    25.79 ?  45  ILE   A N   1 1 
ATOM   320  C CA  . ILE   A 1 65  ? 107.75  17.783 5.793   1    25.33 ?  45  ILE   A CA  1 1 
ATOM   321  C C   . ILE   A 1 65  ? 108.43  19.023 5.262   1    24.86 ?  45  ILE   A C   1 1 
ATOM   322  O O   . ILE   A 1 65  ? 107.814 19.762 4.509   1    24.13 ?  45  ILE   A O   1 1 
ATOM   323  C CB  . ILE   A 1 65  ? 107.592 16.653 4.732   1    26.01 ?  45  ILE   A CB  1 1 
ATOM   324  C CG1 . ILE   A 1 65  ? 108.939 16.235 4.174   1    26.26 ?  45  ILE   A CG1 1 1 
ATOM   325  C CG2 . ILE   A 1 65  ? 106.608 17.033 3.637   1    26.63 ?  45  ILE   A CG2 1 1 
ATOM   326  C CD1 . ILE   A 1 65  ? 108.901 14.812 3.399   1    24.86 ?  45  ILE   A CD1 1 1 
ATOM   327  N N   . PHE   A 1 66  ? 109.692 19.228 5.631   1    23.12 ?  46  PHE   A N   1 1 
ATOM   328  C CA  . PHE   A 1 66  ? 110.459 20.36  5.127   1    22.62 ?  46  PHE   A CA  1 1 
ATOM   329  C C   . PHE   A 1 66  ? 111.312 19.888 3.936   1    22.33 ?  46  PHE   A C   1 1 
ATOM   330  O O   . PHE   A 1 66  ? 112.029 18.88  4.05    1    22.66 ?  46  PHE   A O   1 1 
ATOM   331  C CB  . PHE   A 1 66  ? 111.403 20.904 6.242   1    21.44 ?  46  PHE   A CB  1 1 
ATOM   332  C CG  . PHE   A 1 66  ? 112.206 22.088 5.748   1    21.68 ?  46  PHE   A CG  1 1 
ATOM   333  C CD1 . PHE   A 1 66  ? 111.709 23.377 5.863   1    22.3  ?  46  PHE   A CD1 1 1 
ATOM   334  C CD2 . PHE   A 1 66  ? 113.492 21.915 5.229   1    23.28 ?  46  PHE   A CD2 1 1 
ATOM   335  C CE1 . PHE   A 1 66  ? 112.428 24.453 5.381   1    22.8  ?  46  PHE   A CE1 1 1 
ATOM   336  C CE2 . PHE   A 1 66  ? 114.195 22.999 4.707   1    23.97 ?  46  PHE   A CE2 1 1 
ATOM   337  C CZ  . PHE   A 1 66  ? 113.684 24.265 4.844   1    22.55 ?  46  PHE   A CZ  1 1 
ATOM   338  N N   . VAL   A 1 67  ? 111.29  20.65  2.844   1    21.48 ?  47  VAL   A N   1 1 
ATOM   339  C CA  . VAL   A 1 67  ? 112.101 20.349 1.678   1    21.64 ?  47  VAL   A CA  1 1 
ATOM   340  C C   . VAL   A 1 67  ? 113.309 21.302 1.637   1    21.73 ?  47  VAL   A C   1 1 
ATOM   341  O O   . VAL   A 1 67  ? 113.156 22.557 1.652   1    22.72 ?  47  VAL   A O   1 1 
ATOM   342  C CB  . VAL   A 1 67  ? 111.233 20.532 0.441   1    23.83 ?  47  VAL   A CB  1 1 
ATOM   343  C CG1 . VAL   A 1 67  ? 112.097 20.369 -0.817  1    26.32 ?  47  VAL   A CG1 1 1 
ATOM   344  C CG2 . VAL   A 1 67  ? 110.112 19.5   0.437   1    24.88 ?  47  VAL   A CG2 1 1 
ATOM   345  N N   . SER   A 1 68  ? 114.504 20.72  1.598   1    21.37 ?  48  SER   A N   1 1 
ATOM   346  C CA  . SER   A 1 68  ? 115.768 21.44  1.644   1    20.79 ?  48  SER   A CA  1 1 
ATOM   347  C C   . SER   A 1 68  ? 116.45  21.34  0.272   1    21.27 ?  48  SER   A C   1 1 
ATOM   348  O O   . SER   A 1 68  ? 116.938 20.269 -0.129  1    21.18 ?  48  SER   A O   1 1 
ATOM   349  C CB  . SER   A 1 68  ? 116.624 20.868 2.779   1    23.47 ?  48  SER   A CB  1 1 
ATOM   350  O OG  . SER   A 1 68  ? 117.877 21.523 2.791   1    25.34 ?  48  SER   A OG  1 1 
ATOM   351  N N   . HIS   A 1 69  ? 116.495 22.491 -0.435  1    20.64 ?  49  HIS   A N   1 1 
ATOM   352  C CA  . HIS   A 1 69  ? 117.074 22.535 -1.743  1    19.79 ?  49  HIS   A CA  1 1 
ATOM   353  C C   . HIS   A 1 69  ? 118.609 22.578 -1.65   1    20.28 ?  49  HIS   A C   1 1 
ATOM   354  O O   . HIS   A 1 69  ? 119.18  22.802 -0.552  1    21    ?  49  HIS   A O   1 1 
ATOM   355  C CB  . HIS   A 1 69  ? 116.477 23.736 -2.559  1    19.77 ?  49  HIS   A CB  1 1 
ATOM   356  C CG  . HIS   A 1 69  ? 116.998 25.091 -2.162  1    19.32 ?  49  HIS   A CG  1 1 
ATOM   357  N ND1 . HIS   A 1 69  ? 118.26  25.515 -2.549  1    20.86 ?  49  HIS   A ND1 1 1 
ATOM   358  C CD2 . HIS   A 1 69  ? 116.368 26.098 -1.507  1    19.83 ?  49  HIS   A CD2 1 1 
ATOM   359  C CE1 . HIS   A 1 69  ? 118.382 26.758 -2.057  1    20.73 ?  49  HIS   A CE1 1 1 
ATOM   360  N NE2 . HIS   A 1 69  ? 117.264 27.141 -1.437  1    19.5  ?  49  HIS   A NE2 1 1 
ATOM   361  N N   . GLY   A 1 70  ? 119.26  22.419 -2.807  1    21.32 ?  50  GLY   A N   1 1 
ATOM   362  C CA  . GLY   A 1 70  ? 120.711 22.401 -2.853  1    21.37 ?  50  GLY   A CA  1 1 
ATOM   363  C C   . GLY   A 1 70  ? 121.343 23.704 -3.334  1    22.05 ?  50  GLY   A C   1 1 
ATOM   364  O O   . GLY   A 1 70  ? 120.681 24.73  -3.558  1    21.8  ?  50  GLY   A O   1 1 
ATOM   365  N N   . ALA   A 1 71  ? 122.663 23.651 -3.535  1    22.44 ?  51  ALA   A N   1 1 
ATOM   366  C CA  . ALA   A 1 71  ? 123.426 24.813 -3.936  1    22.8  ?  51  ALA   A CA  1 1 
ATOM   367  C C   . ALA   A 1 71  ? 123.017 25.29  -5.341  1    23.72 ?  51  ALA   A C   1 1 
ATOM   368  O O   . ALA   A 1 71  ? 122.787 24.491 -6.256  1    24.56 ?  51  ALA   A O   1 1 
ATOM   369  C CB  . ALA   A 1 71  ? 124.906 24.467 -3.946  1    24.92 ?  51  ALA   A CB  1 1 
ATOM   370  N N   . GLY   A 1 72  ? 122.943 26.615 -5.457  1    24.14 ?  52  GLY   A N   1 1 
ATOM   371  C CA  . GLY   A 1 72  ? 122.609 27.266 -6.709  1    25.45 ?  52  GLY   A CA  1 1 
ATOM   372  C C   . GLY   A 1 72  ? 121.146 27.292 -7.064  1    25.64 ?  52  GLY   A C   1 1 
ATOM   373  O O   . GLY   A 1 72  ? 120.716 28.177 -7.812  1    28.36 ?  52  GLY   A O   1 1 
ATOM   374  N N   . GLU   A 1 73  ? 120.352 26.373 -6.538  1    22.76 ?  53  GLU   A N   1 1 
ATOM   375  C CA  . GLU   A 1 73  ? 118.952 26.285 -6.953  1    21.33 ?  53  GLU   A CA  1 1 
ATOM   376  C C   . GLU   A 1 73  ? 118.068 26.956 -5.886  1    21.09 ?  53  GLU   A C   1 1 
ATOM   377  O O   . GLU   A 1 73  ? 118.512 27.918 -5.244  1    23.16 ?  53  GLU   A O   1 1 
ATOM   378  C CB  . GLU   A 1 73  ? 118.561 24.826 -7.306  1    22.12 ?  53  GLU   A CB  1 1 
ATOM   379  C CG  . GLU   A 1 73  ? 118.729 23.891 -6.109  1    21.02 ?  53  GLU   A CG  1 1 
ATOM   380  C CD  . GLU   A 1 73  ? 118.006 22.554 -6.198  1    23.3  ?  53  GLU   A CD  1 1 
ATOM   381  O OE1 . GLU   A 1 73  ? 117.355 22.313 -7.243  1    25.63 ?  53  GLU   A OE1 1 1 
ATOM   382  O OE2 . GLU   A 1 73  ? 118.086 21.756 -5.226  1    24.53 ?  53  GLU   A OE2 1 1 
ATOM   383  N N   . HIS   A 1 74  ? 116.791 26.584 -5.823  1    21.07 ?  54  HIS   A N   1 1 
ATOM   384  C CA  . HIS   A 1 74  ? 115.849 27.257 -4.949  1    20.85 ?  54  HIS   A CA  1 1 
ATOM   385  C C   . HIS   A 1 74  ? 114.642 26.354 -4.774  1    21.18 ?  54  HIS   A C   1 1 
ATOM   386  O O   . HIS   A 1 74  ? 114.517 25.317 -5.436  1    20.91 ?  54  HIS   A O   1 1 
ATOM   387  C CB  . HIS   A 1 74  ? 115.455 28.644 -5.529  1    20.88 ?  54  HIS   A CB  1 1 
ATOM   388  C CG  . HIS   A 1 74  ? 114.745 28.566 -6.832  1    21.18 ?  54  HIS   A CG  1 1 
ATOM   389  N ND1 . HIS   A 1 74  ? 113.354 28.601 -6.908  1    23.86 ?  54  HIS   A ND1 1 1 
ATOM   390  C CD2 . HIS   A 1 74  ? 115.252 28.438 -8.082  1    22.12 ?  54  HIS   A CD2 1 1 
ATOM   391  C CE1 . HIS   A 1 74  ? 113.061 28.517 -8.203  1    24.53 ?  54  HIS   A CE1 1 1 
ATOM   392  N NE2 . HIS   A 1 74  ? 114.163 28.373 -8.949  1    24.19 ?  54  HIS   A NE2 1 1 
ATOM   393  N N   . SER   A 1 75  ? 113.757 26.73  -3.853  1    20.82 ?  55  SER   A N   1 1 
ATOM   394  C CA  . SER   A 1 75  ? 112.622 25.869 -3.49   1    21.47 ?  55  SER   A CA  1 1 
ATOM   395  C C   . SER   A 1 75  ? 111.605 25.678 -4.604  1    23.2  ?  55  SER   A C   1 1 
ATOM   396  O O   . SER   A 1 75  ? 110.891 24.673 -4.581  1    23.87 ?  55  SER   A O   1 1 
ATOM   397  C CB  . SER   A 1 75  ? 111.917 26.458 -2.263  1    22.38 ?  55  SER   A CB  1 1 
ATOM   398  O OG  . SER   A 1 75  ? 111.376 27.741 -2.566  1    24.03 ?  55  SER   A OG  1 1 
ATOM   399  N N   . GLY   A 1 76  ? 111.586 26.565 -5.588  1    22.98 ?  56  GLY   A N   1 1 
ATOM   400  C CA  . GLY   A 1 76  ? 110.64  26.408 -6.693  1    23.99 ?  56  GLY   A CA  1 1 
ATOM   401  C C   . GLY   A 1 76  ? 110.926 25.212 -7.561  1    26.06 ?  56  GLY   A C   1 1 
ATOM   402  O O   . GLY   A 1 76  ? 110.032 24.77  -8.288  1    27.97 ?  56  GLY   A O   1 1 
ATOM   403  N N   . ARG   A 1 77  ? 112.14  24.655 -7.464  1    22.84 ?  57  ARG   A N   1 1 
ATOM   404  C CA  . ARG   A 1 77  ? 112.471 23.459 -8.24   1    24.15 ?  57  ARG   A CA  1 1 
ATOM   405  C C   . ARG   A 1 77  ? 111.766 22.208 -7.698  1    24.58 ?  57  ARG   A C   1 1 
ATOM   406  O O   . ARG   A 1 77  ? 111.818 21.15  -8.357  1    25.14 ?  57  ARG   A O   1 1 
ATOM   407  C CB  . ARG   A 1 77  ? 113.973 23.175 -8.118  1    26.38 ?  57  ARG   A CB  1 1 
ATOM   408  C CG  . ARG   A 1 77  ? 114.933 24.198 -8.691  1    32.62 ?  57  ARG   A CG  1 1 
ATOM   409  C CD  . ARG   A 1 77  ? 114.473 24.959 -9.929  1    39.23 ?  57  ARG   A CD  1 1 
ATOM   410  N NE  . ARG   A 1 77  ? 114.172 24.053 -11.041 1    39.38 ?  57  ARG   A NE  1 1 
ATOM   411  C CZ  . ARG   A 1 77  ? 113.182 24.245 -11.91  1    45.46 ?  57  ARG   A CZ  1 1 
ATOM   412  N NH1 . ARG   A 1 77  ? 112.986 23.379 -12.902 1    39.52 ?  57  ARG   A NH1 1 1 
ATOM   413  N NH2 . ARG   A 1 77  ? 112.393 25.319 -11.808 1    51.09 ?  57  ARG   A NH2 1 1 
ATOM   414  N N   . TYR   A 1 78  ? 111.107 22.279 -6.549  1    23.46 ?  58  TYR   A N   1 1 
ATOM   415  C CA  . TYR   A 1 78  ? 110.48  21.125 -5.894  1    24.05 ?  58  TYR   A CA  1 1 
ATOM   416  C C   . TYR   A 1 78  ? 108.96  21.148 -6.011  1    24.69 ?  58  TYR   A C   1 1 
ATOM   417  O O   . TYR   A 1 78  ? 108.301 20.385 -5.308  1    24.59 ?  58  TYR   A O   1 1 
ATOM   418  C CB  . TYR   A 1 78  ? 110.932 21.074 -4.423  1    23.58 ?  58  TYR   A CB  1 1 
ATOM   419  C CG  . TYR   A 1 78  ? 112.411 20.729 -4.393  1    23.96 ?  58  TYR   A CG  1 1 
ATOM   420  C CD1 . TYR   A 1 78  ? 113.381 21.72  -4.573  1    24.24 ?  58  TYR   A CD1 1 1 
ATOM   421  C CD2 . TYR   A 1 78  ? 112.838 19.406 -4.354  1    25.16 ?  58  TYR   A CD2 1 1 
ATOM   422  C CE1 . TYR   A 1 78  ? 114.724 21.405 -4.658  1    24.13 ?  58  TYR   A CE1 1 1 
ATOM   423  C CE2 . TYR   A 1 78  ? 114.188 19.087 -4.4    1    25.39 ?  58  TYR   A CE2 1 1 
ATOM   424  C CZ  . TYR   A 1 78  ? 115.124 20.091 -4.557  1    25.4  ?  58  TYR   A CZ  1 1 
ATOM   425  O OH  . TYR   A 1 78  ? 116.451 19.808 -4.722  1    25.3  ?  58  TYR   A OH  1 1 
ATOM   426  N N   . GLU   A 1 79  ? 108.406 21.936 -6.933  1    26.24 ?  59  GLU   A N   1 1 
ATOM   427  C CA  . GLU   A 1 79  ? 106.963 22.023 -7.093  1    28.01 ?  59  GLU   A CA  1 1 
ATOM   428  C C   . GLU   A 1 79  ? 106.259 20.669 -7.255  1    28.78 ?  59  GLU   A C   1 1 
ATOM   429  O O   . GLU   A 1 79  ? 105.31  20.366 -6.527  1    29.72 ?  59  GLU   A O   1 1 
ATOM   430  C CB  . GLU   A 1 79  ? 106.632 22.956 -8.263  1    30.8  ?  59  GLU   A CB  1 1 
ATOM   431  C CG  . GLU   A 1 79  ? 105.152 23.283 -8.317  1    36.32 ?  59  GLU   A CG  1 1 
ATOM   432  C CD  . GLU   A 1 79  ? 104.742 24.206 -7.186  1    42.13 ?  59  GLU   A CD  1 1 
ATOM   433  O OE1 . GLU   A 1 79  ? 105.571 25.035 -6.746  1    45.06 ?  59  GLU   A OE1 1 1 
ATOM   434  O OE2 . GLU   A 1 79  ? 103.57  24.118 -6.761  1    44.66 ?  59  GLU   A OE2 1 1 
ATOM   435  N N   . GLU   A 1 80  ? 106.742 19.858 -8.211  1    26.79 ?  60  GLU   A N   1 1 
ATOM   436  C CA  . GLU   A 1 80  ? 106.119 18.566 -8.464  1    26.68 ?  60  GLU   A CA  1 1 
ATOM   437  C C   . GLU   A 1 80  ? 106.249 17.616 -7.29   1    26.72 ?  60  GLU   A C   1 1 
ATOM   438  O O   . GLU   A 1 80  ? 105.265 16.963 -6.952  1    28.22 ?  60  GLU   A O   1 1 
ATOM   439  C CB  . GLU   A 1 80  ? 106.638 17.915 -9.752  1    31.23 ?  60  GLU   A CB  1 1 
ATOM   440  C CG  . GLU   A 1 80  ? 106.031 18.561 -10.987 1    42.07 ?  60  GLU   A CG  1 1 
ATOM   441  C CD  . GLU   A 1 80  ? 106.26  17.795 -12.275 1    59.04 ?  60  GLU   A CD  1 1 
ATOM   442  O OE1 . GLU   A 1 80  ? 106.565 16.579 -12.203 1    63.78 ?  60  GLU   A OE1 1 1 
ATOM   443  O OE2 . GLU   A 1 80  ? 106.149 18.418 -13.36  1    63.11 ?  60  GLU   A OE2 1 1 
ATOM   444  N N   . LEU   A 1 81  ? 107.443 17.493 -6.674  1    25.62 ?  61  LEU   A N   1 1 
ATOM   445  C CA  A LEU   A 1 81  ? 107.606 16.6   -5.515  0.5  25.64 ?  61  LEU   A CA  1 1 
ATOM   446  C CA  B LEU   A 1 81  ? 107.601 16.599 -5.541  0.5  26.26 ?  61  LEU   A CA  1 1 
ATOM   447  C C   . LEU   A 1 81  ? 106.709 17.044 -4.368  1    25.52 ?  61  LEU   A C   1 1 
ATOM   448  O O   . LEU   A 1 81  ? 106.089 16.216 -3.695  1    26.36 ?  61  LEU   A O   1 1 
ATOM   449  C CB  A LEU   A 1 81  ? 109.052 16.575 -4.98   0.5  26.28 ?  61  LEU   A CB  1 1 
ATOM   450  C CB  B LEU   A 1 81  ? 109.073 16.587 -5.144  0.5  27.97 ?  61  LEU   A CB  1 1 
ATOM   451  C CG  A LEU   A 1 81  ? 110.054 15.628 -5.611  0.5  26.78 ?  61  LEU   A CG  1 1 
ATOM   452  C CG  B LEU   A 1 81  ? 109.589 15.467 -4.276  0.5  30.31 ?  61  LEU   A CG  1 1 
ATOM   453  C CD1 A LEU   A 1 81  ? 111.473 15.95  -5.126  0.5  25.46 ?  61  LEU   A CD1 1 1 
ATOM   454  C CD1 B LEU   A 1 81  ? 109.243 14.097 -4.861  0.5  31.23 ?  61  LEU   A CD1 1 1 
ATOM   455  C CD2 A LEU   A 1 81  ? 109.693 14.158 -5.312  0.5  27.63 ?  61  LEU   A CD2 1 1 
ATOM   456  C CD2 B LEU   A 1 81  ? 111.095 15.614 -4.106  0.5  31.73 ?  61  LEU   A CD2 1 1 
ATOM   457  N N   . ALA   A 1 82  ? 106.66  18.37  -4.107  1    25.36 ?  62  ALA   A N   1 1 
ATOM   458  C CA  . ALA   A 1 82  ? 105.857 18.916 -3.024  1    26.01 ?  62  ALA   A CA  1 1 
ATOM   459  C C   . ALA   A 1 82  ? 104.381 18.642 -3.264  1    27.1  ?  62  ALA   A C   1 1 
ATOM   460  O O   . ALA   A 1 82  ? 103.711 18.24  -2.321  1    28.3  ?  62  ALA   A O   1 1 
ATOM   461  C CB  . ALA   A 1 82  ? 106.104 20.436 -2.889  1    26.5  ?  62  ALA   A CB  1 1 
ATOM   462  N N   . ARG   A 1 83  ? 103.896 18.761 -4.491  1    27.62 ?  63  ARG   A N   1 1 
ATOM   463  C CA  . ARG   A 1 83  ? 102.481 18.507 -4.77   1    29.57 ?  63  ARG   A CA  1 1 
ATOM   464  C C   . ARG   A 1 83  ? 102.14  17.028 -4.583  1    30.86 ?  63  ARG   A C   1 1 
ATOM   465  O O   . ARG   A 1 83  ? 101.088 16.715 -4.013  1    33.07 ?  63  ARG   A O   1 1 
ATOM   466  C CB  . ARG   A 1 83  ? 102.096 19.004 -6.139  1    31.89 ?  63  ARG   A CB  1 1 
ATOM   467  C CG  . ARG   A 1 83  ? 102.057 20.518 -6.148  1    36.47 ?  63  ARG   A CG  1 1 
ATOM   468  C CD  . ARG   A 1 83  ? 101.499 21.081 -7.42   1    42.42 ?  63  ARG   A CD  1 1 
ATOM   469  N NE  . ARG   A 1 83  ? 101.364 22.533 -7.276  1    47.29 ?  63  ARG   A NE  1 1 
ATOM   470  C CZ  . ARG   A 1 83  ? 100.264 23.149 -6.849  1    51.33 ?  63  ARG   A CZ  1 1 
ATOM   471  N NH1 . ARG   A 1 83  ? 99.165  22.452 -6.583  1    51.14 ?  63  ARG   A NH1 1 1 
ATOM   472  N NH2 . ARG   A 1 83  ? 100.243 24.47  -6.722  1    52.3  ?  63  ARG   A NH2 1 1 
ATOM   473  N N   . MET   A 1 84  ? 103.056 16.131 -4.935  1    30.81 ?  64  MET   A N   1 1 
ATOM   474  C CA  . MET   A 1 84  ? 102.878 14.686 -4.676  1    30.38 ?  64  MET   A CA  1 1 
ATOM   475  C C   . MET   A 1 84  ? 102.794 14.45  -3.16   1    30.71 ?  64  MET   A C   1 1 
ATOM   476  O O   . MET   A 1 84  ? 101.902 13.729 -2.693  1    32.22 ?  64  MET   A O   1 1 
ATOM   477  C CB  . MET   A 1 84  ? 104.063 13.881 -5.246  1    29.89 ?  64  MET   A CB  1 1 
ATOM   478  C CG  . MET   A 1 84  ? 103.982 12.349 -4.955  1    32.53 ?  64  MET   A CG  1 1 
ATOM   479  S SD  . MET   A 1 84  ? 104.763 11.84  -3.381  1    37.8  ?  64  MET   A SD  1 1 
ATOM   480  C CE  . MET   A 1 84  ? 106.484 11.902 -3.822  1    34.17 ?  64  MET   A CE  1 1 
ATOM   481  N N   . LEU   A 1 85  ? 103.699 15.084 -2.373  1    28.57 ?  65  LEU   A N   1 1 
ATOM   482  C CA  . LEU   A 1 85  ? 103.696 14.855 -0.915  1    28.76 ?  65  LEU   A CA  1 1 
ATOM   483  C C   . LEU   A 1 85  ? 102.417 15.424 -0.289  1    31.47 ?  65  LEU   A C   1 1 
ATOM   484  O O   . LEU   A 1 85  ? 101.818 14.805 0.592   1    32.39 ?  65  LEU   A O   1 1 
ATOM   485  C CB  . LEU   A 1 85  ? 104.947 15.455 -0.283  1    27.42 ?  65  LEU   A CB  1 1 
ATOM   486  C CG  . LEU   A 1 85  ? 106.254 14.722 -0.646  1    28.36 ?  65  LEU   A CG  1 1 
ATOM   487  C CD1 . LEU   A 1 85  ? 107.456 15.624 -0.395  1    29.56 ?  65  LEU   A CD1 1 1 
ATOM   488  C CD2 . LEU   A 1 85  ? 106.38  13.411 0.162   1    30.8  ?  65  LEU   A CD2 1 1 
ATOM   489  N N   . MET   A 1 86  ? 101.969 16.582 -0.771  1    32.03 ?  66  MET   A N   1 1 
ATOM   490  C CA  A MET   A 1 86  ? 100.73  17.182 -0.302  0.5  33.38 ?  66  MET   A CA  1 1 
ATOM   491  C CA  B MET   A 1 86  ? 100.73  17.184 -0.307  0.5  33.3  ?  66  MET   A CA  1 1 
ATOM   492  C C   . MET   A 1 86  ? 99.534  16.256 -0.623  1    34.49 ?  66  MET   A C   1 1 
ATOM   493  O O   . MET   A 1 86  ? 98.59   16.176 0.163   1    35.48 ?  66  MET   A O   1 1 
ATOM   494  C CB  A MET   A 1 86  ? 100.553 18.583 -0.909  0.5  33.66 ?  66  MET   A CB  1 1 
ATOM   495  C CB  B MET   A 1 86  ? 100.555 18.566 -0.952  0.5  33.37 ?  66  MET   A CB  1 1 
ATOM   496  C CG  A MET   A 1 86  ? 99.377  19.319 -0.337  0.5  36.36 ?  66  MET   A CG  1 1 
ATOM   497  C CG  B MET   A 1 86  ? 99.227  19.202 -0.646  0.5  35.68 ?  66  MET   A CG  1 1 
ATOM   498  S SD  A MET   A 1 86  ? 97.859  18.951 -1.235  0.5  41.48 ?  66  MET   A SD  1 1 
ATOM   499  S SD  B MET   A 1 86  ? 99.036  20.803 -1.442  0.5  38.97 ?  66  MET   A SD  1 1 
ATOM   500  C CE  A MET   A 1 86  ? 98.095  19.989 -2.68   0.5  41.04 ?  66  MET   A CE  1 1 
ATOM   501  C CE  B MET   A 1 86  ? 99.242  20.359 -3.136  0.5  32.75 ?  66  MET   A CE  1 1 
ATOM   502  N N   . GLY   A 1 87  ? 99.607  15.529 -1.746  1    35.39 ?  67  GLY   A N   1 1 
ATOM   503  C CA  . GLY   A 1 87  ? 98.585  14.557 -2.129  1    37.11 ?  67  GLY   A CA  1 1 
ATOM   504  C C   . GLY   A 1 87  ? 98.502  13.383 -1.164  1    38.32 ?  67  GLY   A C   1 1 
ATOM   505  O O   . GLY   A 1 87  ? 97.498  12.666 -1.145  1    39.46 ?  67  GLY   A O   1 1 
ATOM   506  N N   . LEU   A 1 88  ? 99.565  13.139 -0.365  1    37.6  ?  68  LEU   A N   1 1 
ATOM   507  C CA  . LEU   A 1 88  ? 99.565  12.119 0.698   1    37.54 ?  68  LEU   A CA  1 1 
ATOM   508  C C   . LEU   A 1 88  ? 99.069  12.681 2.027   1    38.13 ?  68  LEU   A C   1 1 
ATOM   509  O O   . LEU   A 1 88  ? 99.198  11.99  3.043   1    38.83 ?  68  LEU   A O   1 1 
ATOM   510  C CB  . LEU   A 1 88  ? 100.954 11.51  0.928   1    37.51 ?  68  LEU   A CB  1 1 
ATOM   511  C CG  . LEU   A 1 88  ? 101.696 11.041 -0.308  1    39.31 ?  68  LEU   A CG  1 1 
ATOM   512  C CD1 . LEU   A 1 88  ? 103.059 10.465 0.066   1    39.75 ?  68  LEU   A CD1 1 1 
ATOM   513  C CD2 . LEU   A 1 88  ? 100.857 10.064 -1.13   1    40.59 ?  68  LEU   A CD2 1 1 
ATOM   514  N N   . ASP   A 1 89  ? 98.524  13.922 2.028   1    37.51 ?  69  ASP   A N   1 1 
ATOM   515  C CA  . ASP   A 1 89  ? 98.009  14.634 3.182   1    37.82 ?  69  ASP   A CA  1 1 
ATOM   516  C C   . ASP   A 1 89  ? 99.103  15.104 4.121   1    36.67 ?  69  ASP   A C   1 1 
ATOM   517  O O   . ASP   A 1 89  ? 98.854  15.239 5.304   1    37.62 ?  69  ASP   A O   1 1 
ATOM   518  C CB  . ASP   A 1 89  ? 96.917  13.838 3.928   1    42.16 ?  69  ASP   A CB  1 1 
ATOM   519  C CG  . ASP   A 1 89  ? 95.623  13.746 3.143   1    51.02 ?  69  ASP   A CG  1 1 
ATOM   520  O OD1 . ASP   A 1 89  ? 94.879  12.763 3.345   1    53.88 ?  69  ASP   A OD1 1 1 
ATOM   521  O OD2 . ASP   A 1 89  ? 95.36   14.657 2.308   1    53.97 ?  69  ASP   A OD2 1 1 
ATOM   522  N N   . LEU   A 1 90  ? 100.296 15.403 3.598   1    34.79 ?  70  LEU   A N   1 1 
ATOM   523  C CA  . LEU   A 1 90  ? 101.348 16.028 4.408   1    33.14 ?  70  LEU   A CA  1 1 
ATOM   524  C C   . LEU   A 1 90  ? 101.332 17.537 4.105   1    31.54 ?  70  LEU   A C   1 1 
ATOM   525  O O   . LEU   A 1 90  ? 100.941 17.967 3.008   1    32.19 ?  70  LEU   A O   1 1 
ATOM   526  C CB  . LEU   A 1 90  ? 102.75  15.487 4.075   1    33.76 ?  70  LEU   A CB  1 1 
ATOM   527  C CG  . LEU   A 1 90  ? 103.121 14.141 4.755   1    36.46 ?  70  LEU   A CG  1 1 
ATOM   528  C CD1 . LEU   A 1 90  ? 102.613 13.007 3.954   1    38.2  ?  70  LEU   A CD1 1 1 
ATOM   529  C CD2 . LEU   A 1 90  ? 104.631 13.986 4.891   1    36.32 ?  70  LEU   A CD2 1 1 
ATOM   530  N N   . LEU   A 1 91  ? 101.726 18.324 5.085   1    30.44 ?  71  LEU   A N   1 1 
ATOM   531  C CA  . LEU   A 1 91  ? 101.857 19.759 4.904   1    29.93 ?  71  LEU   A CA  1 1 
ATOM   532  C C   . LEU   A 1 91  ? 103.334 19.956 4.578   1    28.81 ?  71  LEU   A C   1 1 
ATOM   533  O O   . LEU   A 1 91  ? 104.189 19.64  5.404   1    29.28 ?  71  LEU   A O   1 1 
ATOM   534  C CB  . LEU   A 1 91  ? 101.484 20.527 6.175   1    31.22 ?  71  LEU   A CB  1 1 
ATOM   535  C CG  . LEU   A 1 91  ? 101.18  22.005 5.932   1    34.88 ?  71  LEU   A CG  1 1 
ATOM   536  C CD1 . LEU   A 1 91  ? 100.516 22.605 7.142   1    36.31 ?  71  LEU   A CD1 1 1 
ATOM   537  C CD2 . LEU   A 1 91  ? 102.414 22.781 5.6     1    35.31 ?  71  LEU   A CD2 1 1 
ATOM   538  N N   . VAL   A 1 92  ? 103.609 20.366 3.357   1    27.56 ?  72  VAL   A N   1 1 
ATOM   539  C CA  . VAL   A 1 92  ? 104.958 20.519 2.833   1    26.23 ?  72  VAL   A CA  1 1 
ATOM   540  C C   . VAL   A 1 92  ? 105.359 21.989 2.993   1    25.27 ?  72  VAL   A C   1 1 
ATOM   541  O O   . VAL   A 1 92  ? 104.548 22.882 2.706   1    25.59 ?  72  VAL   A O   1 1 
ATOM   542  C CB  . VAL   A 1 92  ? 105.035 20.108 1.349   1    26.2  ?  72  VAL   A CB  1 1 
ATOM   543  C CG1 . VAL   A 1 92  ? 106.495 20.09  0.892   1    26.36 ?  72  VAL   A CG1 1 1 
ATOM   544  C CG2 . VAL   A 1 92  ? 104.387 18.737 1.127   1    25.96 ?  72  VAL   A CG2 1 1 
ATOM   545  N N   . PHE   A 1 93  ? 106.567 22.254 3.496   1    22.84 ?  73  PHE   A N   1 1 
ATOM   546  C CA  . PHE   A 1 93  ? 107.044 23.623 3.604   1    23.36 ?  73  PHE   A CA  1 1 
ATOM   547  C C   . PHE   A 1 93  ? 108.503 23.718 3.229   1    22.98 ?  73  PHE   A C   1 1 
ATOM   548  O O   . PHE   A 1 93  ? 109.211 22.71  3.257   1    22.98 ?  73  PHE   A O   1 1 
ATOM   549  C CB  . PHE   A 1 93  ? 106.733 24.202 4.987   1    24.09 ?  73  PHE   A CB  1 1 
ATOM   550  C CG  . PHE   A 1 93  ? 107.428 23.549 6.155   1    25.3  ?  73  PHE   A CG  1 1 
ATOM   551  C CD1 . PHE   A 1 93  ? 107.053 22.277 6.594   1    26.21 ?  73  PHE   A CD1 1 1 
ATOM   552  C CD2 . PHE   A 1 93  ? 108.336 24.262 6.925   1    26.2  ?  73  PHE   A CD2 1 1 
ATOM   553  C CE1 . PHE   A 1 93  ? 107.692 21.685 7.698   1    26.84 ?  73  PHE   A CE1 1 1 
ATOM   554  C CE2 . PHE   A 1 93  ? 108.918 23.694 8.043   1    26.92 ?  73  PHE   A CE2 1 1 
ATOM   555  C CZ  . PHE   A 1 93  ? 108.612 22.401 8.415   1    26.63 ?  73  PHE   A CZ  1 1 
ATOM   556  N N   . ALA   A 1 94  ? 108.966 24.9   2.862   1    22.95 ?  74  ALA   A N   1 1 
ATOM   557  C CA  . ALA   A 1 94  ? 110.34  25.067 2.403   1    22.11 ?  74  ALA   A CA  1 1 
ATOM   558  C C   . ALA   A 1 94  ? 110.664 26.564 2.504   1    22.28 ?  74  ALA   A C   1 1 
ATOM   559  O O   . ALA   A 1 94  ? 109.772 27.425 2.627   1    22.5  ?  74  ALA   A O   1 1 
ATOM   560  C CB  . ALA   A 1 94  ? 110.435 24.638 0.91    1    22.29 ?  74  ALA   A CB  1 1 
ATOM   561  N N   . HIS   A 1 95  ? 111.947 26.879 2.409   1    21.96 ?  75  HIS   A N   1 1 
ATOM   562  C CA  . HIS   A 1 95  ? 112.378 28.236 2.171   1    21.76 ?  75  HIS   A CA  1 1 
ATOM   563  C C   . HIS   A 1 95  ? 113.611 28.192 1.296   1    21.04 ?  75  HIS   A C   1 1 
ATOM   564  O O   . HIS   A 1 95  ? 114.262 27.135 1.147   1    21.95 ?  75  HIS   A O   1 1 
ATOM   565  C CB  . HIS   A 1 95  ? 112.666 29.027 3.47    1    21.18 ?  75  HIS   A CB  1 1 
ATOM   566  C CG  . HIS   A 1 95  ? 113.698 28.461 4.405   1    22.1  ?  75  HIS   A CG  1 1 
ATOM   567  N ND1 . HIS   A 1 95  ? 113.336 27.948 5.643   1    23.17 ?  75  HIS   A ND1 1 1 
ATOM   568  C CD2 . HIS   A 1 95  ? 115.042 28.32  4.245   1    23.56 ?  75  HIS   A CD2 1 1 
ATOM   569  C CE1 . HIS   A 1 95  ? 114.479 27.571 6.23    1    24.35 ?  75  HIS   A CE1 1 1 
ATOM   570  N NE2 . HIS   A 1 95  ? 115.538 27.774 5.418   1    24.16 ?  75  HIS   A NE2 1 1 
ATOM   571  N N   . ASP   A 1 96  ? 113.931 29.339 0.671   1    20.13 ?  76  ASP   A N   1 1 
ATOM   572  C CA  . ASP   A 1 96  ? 115.166 29.427 -0.068  1    19.79 ?  76  ASP   A CA  1 1 
ATOM   573  C C   . ASP   A 1 96  ? 116.236 29.715 0.936   1    20.14 ?  76  ASP   A C   1 1 
ATOM   574  O O   . ASP   A 1 96  ? 116.104 30.632 1.796   1    21.05 ?  76  ASP   A O   1 1 
ATOM   575  C CB  . ASP   A 1 96  ? 115.07  30.564 -1.121  1    19.99 ?  76  ASP   A CB  1 1 
ATOM   576  C CG  . ASP   A 1 96  ? 114.088 30.229 -2.239  1    23.73 ?  76  ASP   A CG  1 1 
ATOM   577  O OD1 . ASP   A 1 96  ? 113.703 29.044 -2.362  1    23.05 ?  76  ASP   A OD1 1 1 
ATOM   578  O OD2 . ASP   A 1 96  ? 113.788 31.124 -3.044  1    23.25 ?  76  ASP   A OD2 1 1 
ATOM   579  N N   . HIS   A 1 97  ? 117.313 28.935 0.877   1    20.59 ?  77  HIS   A N   1 1 
ATOM   580  C CA  . HIS   A 1 97  ? 118.405 29.139 1.817   1    21.05 ?  77  HIS   A CA  1 1 
ATOM   581  C C   . HIS   A 1 97  ? 119.012 30.532 1.603   1    22.78 ?  77  HIS   A C   1 1 
ATOM   582  O O   . HIS   A 1 97  ? 118.914 31.088 0.496   1    22.38 ?  77  HIS   A O   1 1 
ATOM   583  C CB  . HIS   A 1 97  ? 119.502 28.08  1.628   1    21.31 ?  77  HIS   A CB  1 1 
ATOM   584  C CG  . HIS   A 1 97  ? 119.036 26.662 1.844   1    21.24 ?  77  HIS   A CG  1 1 
ATOM   585  N ND1 . HIS   A 1 97  ? 118.444 26.267 3.035   1    22.65 ?  77  HIS   A ND1 1 1 
ATOM   586  C CD2 . HIS   A 1 97  ? 119.102 25.59  1.004   1    22.08 ?  77  HIS   A CD2 1 1 
ATOM   587  C CE1 . HIS   A 1 97  ? 118.149 24.965 2.883   1    22.2  ?  77  HIS   A CE1 1 1 
ATOM   588  N NE2 . HIS   A 1 97  ? 118.534 24.513 1.68    1    21.31 ?  77  HIS   A NE2 1 1 
ATOM   589  N N   . VAL   A 1 98  ? 119.689 31.077 2.623   1    23.69 ?  78  VAL   A N   1 1 
ATOM   590  C CA  A VAL   A 1 98  ? 120.346 32.391 2.464   0.63 24.23 ?  78  VAL   A CA  1 1 
ATOM   591  C CA  B VAL   A 1 98  ? 120.406 32.353 2.506   0.37 23.76 ?  78  VAL   A CA  1 1 
ATOM   592  C C   . VAL   A 1 98  ? 121.275 32.343 1.229   1    24.44 ?  78  VAL   A C   1 1 
ATOM   593  O O   . VAL   A 1 98  ? 121.858 31.319 0.893   1    24    ?  78  VAL   A O   1 1 
ATOM   594  C CB  A VAL   A 1 98  ? 121.096 32.853 3.748   0.63 26.23 ?  78  VAL   A CB  1 1 
ATOM   595  C CB  B VAL   A 1 98  ? 121.275 32.49  3.784   0.37 24.33 ?  78  VAL   A CB  1 1 
ATOM   596  C CG1 A VAL   A 1 98  ? 122.242 31.933 4.084   0.63 26.08 ?  78  VAL   A CG1 1 1 
ATOM   597  C CG1 B VAL   A 1 98  ? 122.496 33.379 3.57    0.37 25.13 ?  78  VAL   A CG1 1 1 
ATOM   598  C CG2 A VAL   A 1 98  ? 121.633 34.256 3.596   0.63 27.22 ?  78  VAL   A CG2 1 1 
ATOM   599  C CG2 B VAL   A 1 98  ? 120.428 32.992 4.936   0.37 24.07 ?  78  VAL   A CG2 1 1 
ATOM   600  N N   . GLY   A 1 99  ? 121.296 33.457 0.488   1    23.33 ?  79  GLY   A N   1 1 
ATOM   601  C CA  . GLY   A 1 99  ? 122.106 33.551 -0.709  1    24.24 ?  79  GLY   A CA  1 1 
ATOM   602  C C   . GLY   A 1 99  ? 121.56  32.827 -1.92   1    23.11 ?  79  GLY   A C   1 1 
ATOM   603  O O   . GLY   A 1 99  ? 122.233 32.739 -2.962  1    24.84 ?  79  GLY   A O   1 1 
ATOM   604  N N   . HIS   A 1 100 ? 120.295 32.382 -1.854  1    22.06 ?  80  HIS   A N   1 1 
ATOM   605  C CA  . HIS   A 1 100 ? 119.675 31.593 -2.942  1    20.79 ?  80  HIS   A CA  1 1 
ATOM   606  C C   . HIS   A 1 100 ? 118.3   32.118 -3.276  1    20.35 ?  80  HIS   A C   1 1 
ATOM   607  O O   . HIS   A 1 100 ? 117.614 32.663 -2.398  1    21.98 ?  80  HIS   A O   1 1 
ATOM   608  C CB  . HIS   A 1 100 ? 119.532 30.085 -2.515  1    21.47 ?  80  HIS   A CB  1 1 
ATOM   609  C CG  . HIS   A 1 100 ? 120.847 29.386 -2.476  1    21.83 ?  80  HIS   A CG  1 1 
ATOM   610  N ND1 . HIS   A 1 100 ? 121.724 29.589 -1.431  1    22.44 ?  80  HIS   A ND1 1 1 
ATOM   611  C CD2 . HIS   A 1 100 ? 121.392 28.495 -3.354  1    22.14 ?  80  HIS   A CD2 1 1 
ATOM   612  C CE1 . HIS   A 1 100 ? 122.786 28.836 -1.714  1    23.74 ?  80  HIS   A CE1 1 1 
ATOM   613  N NE2 . HIS   A 1 100 ? 122.64  28.184 -2.869  1    24.31 ?  80  HIS   A NE2 1 1 
ATOM   614  N N   . GLY   A 1 101 ? 117.86  31.874 -4.502  1    20.5  ?  81  GLY   A N   1 1 
ATOM   615  C CA  . GLY   A 1 101 ? 116.499 32.139 -4.933  1    21    ?  81  GLY   A CA  1 1 
ATOM   616  C C   . GLY   A 1 101 ? 116.013 33.543 -4.599  1    21.39 ?  81  GLY   A C   1 1 
ATOM   617  O O   . GLY   A 1 101 ? 116.696 34.543 -4.877  1    22.35 ?  81  GLY   A O   1 1 
ATOM   618  N N   . GLN   A 1 102 ? 114.889 33.608 -3.887  1    20.33 ?  82  GLN   A N   1 1 
ATOM   619  C CA  . GLN   A 1 102 ? 114.228 34.86  -3.518  1    20.98 ?  82  GLN   A CA  1 1 
ATOM   620  C C   . GLN   A 1 102 ? 114.554 35.287 -2.092  1    21.73 ?  82  GLN   A C   1 1 
ATOM   621  O O   . GLN   A 1 102 ? 113.957 36.276 -1.644  1    21    ?  82  GLN   A O   1 1 
ATOM   622  C CB  . GLN   A 1 102 ? 112.716 34.712 -3.664  1    21.52 ?  82  GLN   A CB  1 1 
ATOM   623  C CG  . GLN   A 1 102 ? 112.355 34.29  -5.108  1    23.13 ?  82  GLN   A CG  1 1 
ATOM   624  C CD  . GLN   A 1 102 ? 110.872 34.27  -5.298  1    23.5  ?  82  GLN   A CD  1 1 
ATOM   625  O OE1 . GLN   A 1 102 ? 110.206 35.34  -5.289  1    25    ?  82  GLN   A OE1 1 1 
ATOM   626  N NE2 . GLN   A 1 102 ? 110.34  33.09  -5.518  1    23.68 ?  82  GLN   A NE2 1 1 
ATOM   627  N N   . SER   A 1 103 ? 115.495 34.597 -1.399  1    21.39 ?  83  SER   A N   1 1 
ATOM   628  C CA  . SER   A 1 103 ? 115.933 35.01  -0.074  1    21.86 ?  83  SER   A CA  1 1 
ATOM   629  C C   . SER   A 1 103 ? 117.04  36.028 -0.192  1    23.11 ?  83  SER   A C   1 1 
ATOM   630  O O   . SER   A 1 103 ? 117.698 36.18  -1.236  1    23.36 ?  83  SER   A O   1 1 
ATOM   631  C CB  . SER   A 1 103 ? 116.418 33.793 0.707   1    21.62 ?  83  SER   A CB  1 1 
ATOM   632  O OG  . SER   A 1 103 ? 115.245 33.057 1.001   1    22.2  ?  83  SER   A OG  1 1 
ATOM   633  N N   . GLU   A 1 104 ? 117.284 36.733 0.922   1    23.37 ?  84  GLU   A N   1 1 
ATOM   634  C CA  . GLU   A 1 104 ? 118.338 37.755 0.935   1    24.6  ?  84  GLU   A CA  1 1 
ATOM   635  C C   . GLU   A 1 104 ? 119.713 37.091 1.068   1    27.13 ?  84  GLU   A C   1 1 
ATOM   636  O O   . GLU   A 1 104 ? 119.826 35.866 1.301   1    26.03 ?  84  GLU   A O   1 1 
ATOM   637  C CB  . GLU   A 1 104 ? 118.121 38.699 2.154   1    24.27 ?  84  GLU   A CB  1 1 
ATOM   638  C CG  . GLU   A 1 104 ? 116.968 39.653 1.881   1    24.51 ?  84  GLU   A CG  1 1 
ATOM   639  C CD  . GLU   A 1 104 ? 116.827 40.72  2.963   1    27.68 ?  84  GLU   A CD  1 1 
ATOM   640  O OE1 . GLU   A 1 104 ? 117.119 40.406 4.126   1    26.51 ?  84  GLU   A OE1 1 1 
ATOM   641  O OE2 . GLU   A 1 104 ? 116.467 41.882 2.642   1    29.8  ?  84  GLU   A OE2 1 1 
ATOM   642  N N   . GLY   A 1 105 ? 120.743 37.907 0.885   1    28.94 ?  85  GLY   A N   1 1 
ATOM   643  C CA  . GLY   A 1 105 ? 122.101 37.456 1.08    1    29.93 ?  85  GLY   A CA  1 1 
ATOM   644  C C   . GLY   A 1 105 ? 122.877 37.558 -0.197  1    31.03 ?  85  GLY   A C   1 1 
ATOM   645  O O   . GLY   A 1 105 ? 122.331 37.329 -1.279  1    32.04 ?  85  GLY   A O   1 1 
ATOM   646  N N   . GLU   A 1 106 ? 124.194 37.82  -0.107  1    31.25 ?  86  GLU   A N   1 1 
ATOM   647  C CA  . GLU   A 1 106 ? 125.064 37.796 -1.29   1    31.69 ?  86  GLU   A CA  1 1 
ATOM   648  C C   . GLU   A 1 106 ? 124.954 36.368 -1.934  1    30.93 ?  86  GLU   A C   1 1 
ATOM   649  O O   . GLU   A 1 106 ? 124.854 35.393 -1.191  1    30.24 ?  86  GLU   A O   1 1 
ATOM   650  C CB  . GLU   A 1 106 ? 126.517 38.019 -0.847  1    37.21 ?  86  GLU   A CB  1 1 
ATOM   651  C CG  . GLU   A 1 106 ? 127.45  38.305 -2.011  1    48.47 ?  86  GLU   A CG  1 1 
ATOM   652  C CD  . GLU   A 1 106 ? 128.919 38.466 -1.653  1    60.88 ?  86  GLU   A CD  1 1 
ATOM   653  O OE1 . GLU   A 1 106 ? 129.215 38.853 -0.498  1    62.28 ?  86  GLU   A OE1 1 1 
ATOM   654  O OE2 . GLU   A 1 106 ? 129.773 38.182 -2.528  1    64.37 ?  86  GLU   A OE2 1 1 
ATOM   655  N N   . ARG   A 1 107 ? 124.829 36.277 -3.261  1    31.11 ?  87  ARG   A N   1 1 
ATOM   656  C CA  . ARG   A 1 107 ? 124.593 34.994 -3.901  1    31.64 ?  87  ARG   A CA  1 1 
ATOM   657  C C   . ARG   A 1 107 ? 125.616 33.955 -3.626  1    31.71 ?  87  ARG   A C   1 1 
ATOM   658  O O   . ARG   A 1 107 ? 126.807 34.187 -3.847  1    32.6  ?  87  ARG   A O   1 1 
ATOM   659  C CB  . ARG   A 1 107 ? 124.432 35.128 -5.424  1    32.34 ?  87  ARG   A CB  1 1 
ATOM   660  C CG  . ARG   A 1 107 ? 123.401 36.193 -5.841  1    34.94 ?  87  ARG   A CG  1 1 
ATOM   661  C CD  . ARG   A 1 107 ? 121.958 35.78  -5.528  1    34.88 ?  87  ARG   A CD  1 1 
ATOM   662  N NE  . ARG   A 1 107 ? 121.573 36.058 -4.141  1    31.27 ?  87  ARG   A NE  1 1 
ATOM   663  C CZ  . ARG   A 1 107 ? 120.383 35.763 -3.616  1    30.3  ?  87  ARG   A CZ  1 1 
ATOM   664  N NH1 . ARG   A 1 107 ? 119.443 35.194 -4.362  1    28.53 ?  87  ARG   A NH1 1 1 
ATOM   665  N NH2 . ARG   A 1 107 ? 120.121 36.054 -2.351  1    28.46 ?  87  ARG   A NH2 1 1 
ATOM   666  N N   . MET   A 1 108 ? 125.162 32.781 -3.144  1    30.5  ?  88  MET   A N   1 1 
ATOM   667  C CA  A MET   A 1 108 ? 126.025 31.638 -2.907  0.5  30.58 ?  88  MET   A CA  1 1 
ATOM   668  C CA  B MET   A 1 108 ? 126.084 31.667 -2.971  0.5  31.55 ?  88  MET   A CA  1 1 
ATOM   669  C C   . MET   A 1 108 ? 127.254 31.965 -2.079  1    31.93 ?  88  MET   A C   1 1 
ATOM   670  O O   . MET   A 1 108 ? 128.396 31.612 -2.405  1    33.42 ?  88  MET   A O   1 1 
ATOM   671  C CB  A MET   A 1 108 ? 126.386 30.899 -4.207  0.5  29.66 ?  88  MET   A CB  1 1 
ATOM   672  C CB  B MET   A 1 108 ? 126.569 31.151 -4.352  0.5  32.92 ?  88  MET   A CB  1 1 
ATOM   673  C CG  A MET   A 1 108 ? 125.179 30.321 -4.886  0.5  28.33 ?  88  MET   A CG  1 1 
ATOM   674  C CG  B MET   A 1 108 ? 125.482 30.857 -5.303  0.5  36.08 ?  88  MET   A CG  1 1 
ATOM   675  S SD  A MET   A 1 108 ? 125.582 29.358 -6.363  0.5  26.44 ?  88  MET   A SD  1 1 
ATOM   676  S SD  B MET   A 1 108 ? 124.38  29.647 -4.617  0.5  45.59 ?  88  MET   A SD  1 1 
ATOM   677  C CE  A MET   A 1 108 ? 126.287 27.924 -5.614  0.5  26.65 ?  88  MET   A CE  1 1 
ATOM   678  C CE  B MET   A 1 108 ? 125.537 28.262 -4.386  0.5  45.35 ?  88  MET   A CE  1 1 
ATOM   679  N N   A VAL   A 1 109 ? 127.001 32.584 -0.957  0.44 31.42 ?  89  VAL   A N   1 1 
ATOM   680  N N   B VAL   A 1 109 ? 126.963 32.666 -0.978  0.56 31.81 ?  89  VAL   A N   1 1 
ATOM   681  C CA  A VAL   A 1 109 ? 127.979 32.749 0.089   0.44 31.61 ?  89  VAL   A CA  1 1 
ATOM   682  C CA  B VAL   A 1 109 ? 127.877 33.034 0.095   0.56 32.6  ?  89  VAL   A CA  1 1 
ATOM   683  C C   A VAL   A 1 109 ? 127.243 32.525 1.401   0.44 31.44 ?  89  VAL   A C   1 1 
ATOM   684  C C   B VAL   A 1 109 ? 127.205 32.61  1.422   0.56 31.98 ?  89  VAL   A C   1 1 
ATOM   685  O O   A VAL   A 1 109 ? 126.029 32.73  1.5     0.44 31.71 ?  89  VAL   A O   1 1 
ATOM   686  O O   B VAL   A 1 109 ? 125.994 32.795 1.562   0.56 32.28 ?  89  VAL   A O   1 1 
ATOM   687  C CB  A VAL   A 1 109 ? 128.825 34.041 0.095   0.44 32.25 ?  89  VAL   A CB  1 1 
ATOM   688  C CB  B VAL   A 1 109 ? 128.11  34.583 0.082   0.56 33.84 ?  89  VAL   A CB  1 1 
ATOM   689  C CG1 A VAL   A 1 109 ? 129.72  34.15  -1.132  0.44 32.54 ?  89  VAL   A CG1 1 1 
ATOM   690  C CG1 B VAL   A 1 109 ? 128.783 35.058 1.361   0.56 34.13 ?  89  VAL   A CG1 1 1 
ATOM   691  C CG2 A VAL   A 1 109 ? 127.959 35.272 0.258   0.44 32.18 ?  89  VAL   A CG2 1 1 
ATOM   692  C CG2 B VAL   A 1 109 ? 128.916 35.012 -1.135  0.56 34.38 ?  89  VAL   A CG2 1 1 
ATOM   693  N N   . VAL   A 1 110 ? 127.966 32.076 2.4     1    31.39 ?  90  VAL   A N   1 1 
ATOM   694  C CA  . VAL   A 1 110 ? 127.407 31.803 3.707   1    31.45 ?  90  VAL   A CA  1 1 
ATOM   695  C C   . VAL   A 1 110 ? 128.534 31.989 4.705   1    32.78 ?  90  VAL   A C   1 1 
ATOM   696  O O   . VAL   A 1 110 ? 129.669 31.564 4.439   1    33.9  ?  90  VAL   A O   1 1 
ATOM   697  C CB  . VAL   A 1 110 ? 126.642 30.445 3.81    1    31.64 ?  90  VAL   A CB  1 1 
ATOM   698  C CG1 . VAL   A 1 110 ? 127.592 29.241 3.828   1    31.85 ?  90  VAL   A CG1 1 1 
ATOM   699  C CG2 . VAL   A 1 110 ? 125.698 30.446 5.016   1    31.61 ?  90  VAL   A CG2 1 1 
ATOM   700  N N   . SER   A 1 111 ? 128.25  32.672 5.826   1    32.37 ?  91  SER   A N   1 1 
ATOM   701  C CA  . SER   A 1 111 ? 129.305 32.93  6.81    1    33.79 ?  91  SER   A CA  1 1 
ATOM   702  C C   . SER   A 1 111 ? 129.858 31.652 7.386   1    34.33 ?  91  SER   A C   1 1 
ATOM   703  O O   . SER   A 1 111 ? 131.07  31.499 7.563   1    35.3  ?  91  SER   A O   1 1 
ATOM   704  C CB  . SER   A 1 111 ? 128.806 33.872 7.901   1    35.1  ?  91  SER   A CB  1 1 
ATOM   705  O OG  . SER   A 1 111 ? 127.684 33.293 8.543   1    38    ?  91  SER   A OG  1 1 
ATOM   706  N N   . ASP   A 1 112 ? 128.963 30.705 7.664   1    32.73 ?  92  ASP   A N   1 1 
ATOM   707  C CA  . ASP   A 1 112 ? 129.331 29.372 8.11    1    32.18 ?  92  ASP   A CA  1 1 
ATOM   708  C C   . ASP   A 1 112 ? 128.205 28.459 7.69    1    31.15 ?  92  ASP   A C   1 1 
ATOM   709  O O   . ASP   A 1 112 ? 127.038 28.843 7.783   1    30.5  ?  92  ASP   A O   1 1 
ATOM   710  C CB  . ASP   A 1 112 ? 129.535 29.281 9.63    1    33.73 ?  92  ASP   A CB  1 1 
ATOM   711  C CG  . ASP   A 1 112 ? 129.969 27.884 10.07   1    37.47 ?  92  ASP   A CG  1 1 
ATOM   712  O OD1 . ASP   A 1 112 ? 131.201 27.607 10.056  1    38.61 ?  92  ASP   A OD1 1 1 
ATOM   713  O OD2 . ASP   A 1 112 ? 129.069 27.044 10.411  1    37.23 ?  92  ASP   A OD2 1 1 
ATOM   714  N N   . PHE   A 1 113 ? 128.533 27.223 7.282   1    29.84 ?  93  PHE   A N   1 1 
ATOM   715  C CA  . PHE   A 1 113 ? 127.521 26.264 6.825   1    28.73 ?  93  PHE   A CA  1 1 
ATOM   716  C C   . PHE   A 1 113 ? 126.382 26.066 7.847   1    29.32 ?  93  PHE   A C   1 1 
ATOM   717  O O   . PHE   A 1 113 ? 125.24  25.855 7.455   1    30.13 ?  93  PHE   A O   1 1 
ATOM   718  C CB  . PHE   A 1 113 ? 128.18  24.898 6.526   1    27.55 ?  93  PHE   A CB  1 1 
ATOM   719  C CG  . PHE   A 1 113 ? 127.296 24.051 5.632   1    27.61 ?  93  PHE   A CG  1 1 
ATOM   720  C CD1 . PHE   A 1 113 ? 127.221 24.298 4.26    1    27.05 ?  93  PHE   A CD1 1 1 
ATOM   721  C CD2 . PHE   A 1 113 ? 126.483 23.069 6.171   1    27.87 ?  93  PHE   A CD2 1 1 
ATOM   722  C CE1 . PHE   A 1 113 ? 126.398 23.518 3.437   1    27.41 ?  93  PHE   A CE1 1 1 
ATOM   723  C CE2 . PHE   A 1 113 ? 125.653 22.287 5.346   1    27.81 ?  93  PHE   A CE2 1 1 
ATOM   724  C CZ  . PHE   A 1 113 ? 125.628 22.514 3.983   1    27.29 ?  93  PHE   A CZ  1 1 
ATOM   725  N N   . HIS   A 1 114 ? 126.676 26.228 9.15    1    28.62 ?  94  HIS   A N   1 1 
ATOM   726  C CA  . HIS   A 1 114 ? 125.644 26.05  10.181  1    28.96 ?  94  HIS   A CA  1 1 
ATOM   727  C C   . HIS   A 1 114 ? 124.502 27.03  10.051  1    26.89 ?  94  HIS   A C   1 1 
ATOM   728  O O   . HIS   A 1 114 ? 123.396 26.705 10.501  1    27.41 ?  94  HIS   A O   1 1 
ATOM   729  C CB  . HIS   A 1 114 ? 126.23  26.056 11.615  1    32.24 ?  94  HIS   A CB  1 1 
ATOM   730  C CG  . HIS   A 1 114 ? 125.237 25.604 12.643  1    36.61 ?  94  HIS   A CG  1 1 
ATOM   731  N ND1 . HIS   A 1 114 ? 124.533 26.514 13.408  1    39.29 ?  94  HIS   A ND1 1 1 
ATOM   732  C CD2 . HIS   A 1 114 ? 124.788 24.362 12.923  1    38.71 ?  94  HIS   A CD2 1 1 
ATOM   733  C CE1 . HIS   A 1 114 ? 123.713 25.795 14.159  1    39.47 ?  94  HIS   A CE1 1 1 
ATOM   734  N NE2 . HIS   A 1 114 ? 123.829 24.498 13.905  1    40.34 ?  94  HIS   A NE2 1 1 
ATOM   735  N N   . VAL   A 1 115 ? 124.694 28.172 9.382   1    25.69 ?  95  VAL   A N   1 1 
ATOM   736  C CA  . VAL   A 1 115 ? 123.569 29.095 9.164   1    25.54 ?  95  VAL   A CA  1 1 
ATOM   737  C C   . VAL   A 1 115 ? 122.386 28.377 8.495   1    25.3  ?  95  VAL   A C   1 1 
ATOM   738  O O   . VAL   A 1 115 ? 121.23  28.58  8.889   1    25.66 ?  95  VAL   A O   1 1 
ATOM   739  C CB  . VAL   A 1 115 ? 124.052 30.276 8.321   1    27.35 ?  95  VAL   A CB  1 1 
ATOM   740  C CG1 . VAL   A 1 115 ? 122.871 31.089 7.782   1    27.65 ?  95  VAL   A CG1 1 1 
ATOM   741  C CG2 . VAL   A 1 115 ? 124.991 31.171 9.158   1    28.39 ?  95  VAL   A CG2 1 1 
ATOM   742  N N   . PHE   A 1 116 ? 122.69  27.513 7.52    1    24.66 ?  96  PHE   A N   1 1 
ATOM   743  C CA  . PHE   A 1 116 ? 121.614 26.826 6.803   1    24.02 ?  96  PHE   A CA  1 1 
ATOM   744  C C   . PHE   A 1 116 ? 120.839 25.923 7.758   1    24.46 ?  96  PHE   A C   1 1 
ATOM   745  O O   . PHE   A 1 116 ? 119.606 25.877 7.707   1    25.27 ?  96  PHE   A O   1 1 
ATOM   746  C CB  . PHE   A 1 116 ? 122.198 25.954 5.667   1    24.06 ?  96  PHE   A CB  1 1 
ATOM   747  C CG  . PHE   A 1 116 ? 122.889 26.736 4.585   1    23.64 ?  96  PHE   A CG  1 1 
ATOM   748  C CD1 . PHE   A 1 116 ? 122.33  27.911 4.077   1    24.44 ?  96  PHE   A CD1 1 1 
ATOM   749  C CD2 . PHE   A 1 116 ? 124.039 26.251 3.993   1    24.44 ?  96  PHE   A CD2 1 1 
ATOM   750  C CE1 . PHE   A 1 116 ? 122.944 28.576 3.013   1    25.32 ?  96  PHE   A CE1 1 1 
ATOM   751  C CE2 . PHE   A 1 116 ? 124.611 26.869 2.919   1    25.14 ?  96  PHE   A CE2 1 1 
ATOM   752  C CZ  . PHE   A 1 116 ? 124.083 28.054 2.449   1    24.79 ?  96  PHE   A CZ  1 1 
ATOM   753  N N   . VAL   A 1 117 ? 121.571 25.199 8.626   1    23.41 ?  97  VAL   A N   1 1 
ATOM   754  C CA  . VAL   A 1 117 ? 120.941 24.282 9.587   1    24.45 ?  97  VAL   A CA  1 1 
ATOM   755  C C   . VAL   A 1 117 ? 120.1   25.05  10.644  1    25.06 ?  97  VAL   A C   1 1 
ATOM   756  O O   . VAL   A 1 117 ? 118.929 24.735 10.913  1    25.52 ?  97  VAL   A O   1 1 
ATOM   757  C CB  . VAL   A 1 117 ? 122.054 23.465 10.257  1    25.93 ?  97  VAL   A CB  1 1 
ATOM   758  C CG1 . VAL   A 1 117 ? 121.48  22.55  11.341  1    27.28 ?  97  VAL   A CG1 1 1 
ATOM   759  C CG2 . VAL   A 1 117 ? 122.798 22.654 9.204   1    25.51 ?  97  VAL   A CG2 1 1 
ATOM   760  N N   . ARG   A 1 118 ? 120.678 26.118 11.208  1    24.73 ?  98  ARG   A N   1 1 
ATOM   761  C CA  . ARG   A 1 118 ? 119.972 26.998 12.144  1    25.15 ?  98  ARG   A CA  1 1 
ATOM   762  C C   . ARG   A 1 118 ? 118.66  27.5   11.563  1    24.59 ?  98  ARG   A C   1 1 
ATOM   763  O O   . ARG   A 1 118 ? 117.629 27.487 12.248  1    26.41 ?  98  ARG   A O   1 1 
ATOM   764  C CB  . ARG   A 1 118 ? 120.919 28.161 12.46   1    28.19 ?  98  ARG   A CB  1 1 
ATOM   765  C CG  . ARG   A 1 118 ? 120.345 29.202 13.425  1    29.35 ?  98  ARG   A CG  1 1 
ATOM   766  C CD  . ARG   A 1 118 ? 121.169 30.461 13.326  1    29.72 ?  98  ARG   A CD  1 1 
ATOM   767  N NE  . ARG   A 1 118 ? 120.868 31.135 12.068  1    30.32 ?  98  ARG   A NE  1 1 
ATOM   768  C CZ  . ARG   A 1 118 ? 121.521 32.188 11.599  1    31.12 ?  98  ARG   A CZ  1 1 
ATOM   769  N NH1 . ARG   A 1 118 ? 122.521 32.728 12.3    1    33.27 ?  98  ARG   A NH1 1 1 
ATOM   770  N NH2 . ARG   A 1 118 ? 121.156 32.743 10.452  1    29.82 ?  98  ARG   A NH2 1 1 
ATOM   771  N N   . ASP   A 1 119 ? 118.683 27.925 10.245  1    24.15 ?  99  ASP   A N   1 1 
ATOM   772  C CA  . ASP   A 1 119 ? 117.483 28.492 9.629   1    23.85 ?  99  ASP   A CA  1 1 
ATOM   773  C C   . ASP   A 1 119 ? 116.437 27.416 9.375   1    23.39 ?  99  ASP   A C   1 1 
ATOM   774  O O   . ASP   A 1 119 ? 115.234 27.674 9.562   1    24.43 ?  99  ASP   A O   1 1 
ATOM   775  C CB  . ASP   A 1 119 ? 117.838 29.273 8.367   1    23.29 ?  99  ASP   A CB  1 1 
ATOM   776  C CG  . ASP   A 1 119 ? 118.625 30.569 8.643   1    24.52 ?  99  ASP   A CG  1 1 
ATOM   777  O OD1 . ASP   A 1 119 ? 118.845 30.911 9.882   1    26.74 ?  99  ASP   A OD1 1 1 
ATOM   778  O OD2 . ASP   A 1 119 ? 119.06  31.219 7.646   1    25.22 ?  99  ASP   A OD2 1 1 
ATOM   779  N N   . VAL   A 1 120 ? 116.856 26.206 8.978   1    22.68 ?  100 VAL   A N   1 1 
ATOM   780  C CA  . VAL   A 1 120 ? 115.877 25.1   8.862   1    22.46 ?  100 VAL   A CA  1 1 
ATOM   781  C C   . VAL   A 1 120 ? 115.197 24.856 10.224  1    23.82 ?  100 VAL   A C   1 1 
ATOM   782  O O   . VAL   A 1 120 ? 113.976 24.748 10.312  1    24.32 ?  100 VAL   A O   1 1 
ATOM   783  C CB  . VAL   A 1 120 ? 116.545 23.815 8.334   1    22.63 ?  100 VAL   A CB  1 1 
ATOM   784  C CG1 . VAL   A 1 120 ? 115.592 22.614 8.426   1    23.08 ?  100 VAL   A CG1 1 1 
ATOM   785  C CG2 . VAL   A 1 120 ? 116.999 24.047 6.886   1    23.15 ?  100 VAL   A CG2 1 1 
ATOM   786  N N   . LEU   A 1 121 ? 116.012 24.797 11.273  1    23.34 ?  101 LEU   A N   1 1 
ATOM   787  C CA  . LEU   A 1 121 ? 115.475 24.545 12.621  1    25.01 ?  101 LEU   A CA  1 1 
ATOM   788  C C   . LEU   A 1 121 ? 114.51  25.637 13.077  1    25.09 ?  101 LEU   A C   1 1 
ATOM   789  O O   . LEU   A 1 121 ? 113.441 25.34  13.647  1    25.7  ?  101 LEU   A O   1 1 
ATOM   790  C CB  . LEU   A 1 121 ? 116.6   24.306 13.634  1    25.97 ?  101 LEU   A CB  1 1 
ATOM   791  C CG  . LEU   A 1 121 ? 117.336 23.01  13.458  1    28.58 ?  101 LEU   A CG  1 1 
ATOM   792  C CD1 . LEU   A 1 121 ? 118.59  23.028 14.286  1    30.31 ?  101 LEU   A CD1 1 1 
ATOM   793  C CD2 . LEU   A 1 121 ? 116.415 21.83  13.763  1    28.23 ?  101 LEU   A CD2 1 1 
ATOM   794  N N   . GLN   A 1 122 ? 114.81  26.904 12.734  1    24.27 ?  102 GLN   A N   1 1 
ATOM   795  C CA  . GLN   A 1 122 ? 113.905 27.999 13.08   1    23.86 ?  102 GLN   A CA  1 1 
ATOM   796  C C   . GLN   A 1 122 ? 112.559 27.78  12.384  1    25.17 ?  102 GLN   A C   1 1 
ATOM   797  O O   . GLN   A 1 122 ? 111.512 27.939 13.003  1    26.98 ?  102 GLN   A O   1 1 
ATOM   798  C CB  . GLN   A 1 122 ? 114.542 29.328 12.688  1    24.31 ?  102 GLN   A CB  1 1 
ATOM   799  C CG  . GLN   A 1 122 ? 113.597 30.501 12.979  1    24.77 ?  102 GLN   A CG  1 1 
ATOM   800  C CD  . GLN   A 1 122 ? 114.006 31.777 12.316  1    27.17 ?  102 GLN   A CD  1 1 
ATOM   801  O OE1 . GLN   A 1 122 ? 115.111 31.903 11.754  1    29.96 ?  102 GLN   A OE1 1 1 
ATOM   802  N NE2 . GLN   A 1 122 ? 113.109 32.744 12.358  1    28.76 ?  102 GLN   A NE2 1 1 
ATOM   803  N N   . HIS   A 1 123 ? 112.583 27.421 11.075  1    24.15 ?  103 HIS   A N   1 1 
ATOM   804  C CA  . HIS   A 1 123 ? 111.348 27.275 10.338  1    24.93 ?  103 HIS   A CA  1 1 
ATOM   805  C C   . HIS   A 1 123 ? 110.558 26.054 10.836  1    25.54 ?  103 HIS   A C   1 1 
ATOM   806  O O   . HIS   A 1 123 ? 109.321 26.148 11.019  1    26.93 ?  103 HIS   A O   1 1 
ATOM   807  C CB  . HIS   A 1 123 ? 111.676 27.141 8.827   1    23.69 ?  103 HIS   A CB  1 1 
ATOM   808  C CG  . HIS   A 1 123 ? 110.529 27.441 7.917   1    24.02 ?  103 HIS   A CG  1 1 
ATOM   809  N ND1 . HIS   A 1 123 ? 110.718 27.575 6.552   1    23.88 ?  103 HIS   A ND1 1 1 
ATOM   810  C CD2 . HIS   A 1 123 ? 109.223 27.673 8.2     1    24.31 ?  103 HIS   A CD2 1 1 
ATOM   811  C CE1 . HIS   A 1 123 ? 109.522 27.834 6.043   1    24.73 ?  103 HIS   A CE1 1 1 
ATOM   812  N NE2 . HIS   A 1 123 ? 108.602 27.959 7.015   1    24.65 ?  103 HIS   A NE2 1 1 
ATOM   813  N N   . VAL   A 1 124 ? 111.26  24.925 11.11   1    24.91 ?  104 VAL   A N   1 1 
ATOM   814  C CA  . VAL   A 1 124 ? 110.583 23.73  11.632  1    25.54 ?  104 VAL   A CA  1 1 
ATOM   815  C C   . VAL   A 1 124 ? 109.936 24.072 13.014  1    26.62 ?  104 VAL   A C   1 1 
ATOM   816  O O   . VAL   A 1 124 ? 108.761 23.774 13.272  1    28.04 ?  104 VAL   A O   1 1 
ATOM   817  C CB  . VAL   A 1 124 ? 111.597 22.585 11.807  1    26.8  ?  104 VAL   A CB  1 1 
ATOM   818  C CG1 . VAL   A 1 124 ? 110.998 21.449 12.66   1    28.52 ?  104 VAL   A CG1 1 1 
ATOM   819  C CG2 . VAL   A 1 124 ? 112.034 22.061 10.44   1    26.86 ?  104 VAL   A CG2 1 1 
ATOM   820  N N   . ASP   A 1 125 ? 110.677 24.785 13.84   1    27.25 ?  105 ASP   A N   1 1 
ATOM   821  C CA  . ASP   A 1 125 ? 110.164 25.151 15.17   1    28.99 ?  105 ASP   A CA  1 1 
ATOM   822  C C   . ASP   A 1 125 ? 108.93  26.044 15.06   1    30.24 ?  105 ASP   A C   1 1 
ATOM   823  O O   . ASP   A 1 125 ? 107.967 25.843 15.792  1    32.67 ?  105 ASP   A O   1 1 
ATOM   824  C CB  . ASP   A 1 125 ? 111.247 25.813 16.018  1    30.87 ?  105 ASP   A CB  1 1 
ATOM   825  C CG  . ASP   A 1 125 ? 112.341 24.847 16.443  1    34.9  ?  105 ASP   A CG  1 1 
ATOM   826  O OD1 . ASP   A 1 125 ? 112.105 23.603 16.396  1    35.6  ?  105 ASP   A OD1 1 1 
ATOM   827  O OD2 . ASP   A 1 125 ? 113.424 25.32  16.856  1    35.14 ?  105 ASP   A OD2 1 1 
ATOM   828  N N   . SER   A 1 126 ? 108.938 26.982 14.107  1    28.74 ?  106 SER   A N   1 1 
ATOM   829  C CA  A SER   A 1 126 ? 107.799 27.857 13.879  0.5  29.61 ?  106 SER   A CA  1 1 
ATOM   830  C CA  C SER   A 1 126 ? 107.798 27.846 13.881  0.49 29.89 ?  106 SER   A CA  1 1 
ATOM   831  C C   . SER   A 1 126 ? 106.584 27.044 13.427  1    31.85 ?  106 SER   A C   1 1 
ATOM   832  O O   . SER   A 1 126 ? 105.493 27.245 13.955  1    33.75 ?  106 SER   A O   1 1 
ATOM   833  C CB  A SER   A 1 126 ? 108.134 28.916 12.831  0.5  29.75 ?  106 SER   A CB  1 1 
ATOM   834  C CB  C SER   A 1 126 ? 108.154 28.903 12.849  0.49 30.74 ?  106 SER   A CB  1 1 
ATOM   835  O OG  A SER   A 1 126 ? 107.101 29.888 12.764  0.5  30.33 ?  106 SER   A OG  1 1 
ATOM   836  O OG  C SER   A 1 126 ? 109.15  29.724 13.427  0.49 32.46 ?  106 SER   A OG  1 1 
ATOM   837  N N   . MET   A 1 127 ? 106.76  26.118 12.456  1    31.52 ?  107 MET   A N   1 1 
ATOM   838  C CA  . MET   A 1 127 ? 105.644 25.307 11.984  1    33.54 ?  107 MET   A CA  1 1 
ATOM   839  C C   . MET   A 1 127 ? 105.055 24.374 13.032  1    35.99 ?  107 MET   A C   1 1 
ATOM   840  O O   . MET   A 1 127 ? 103.842 24.139 13.048  1    37.39 ?  107 MET   A O   1 1 
ATOM   841  C CB  . MET   A 1 127 ? 106.072 24.506 10.737  1    33.5  ?  107 MET   A CB  1 1 
ATOM   842  C CG  . MET   A 1 127 ? 106.254 25.405 9.568   1    35.58 ?  107 MET   A CG  1 1 
ATOM   843  S SD  . MET   A 1 127 ? 104.683 26.16  9.056   1    42.06 ?  107 MET   A SD  1 1 
ATOM   844  C CE  . MET   A 1 127 ? 103.956 24.833 8.233   1    38.62 ?  107 MET   A CE  1 1 
ATOM   845  N N   . GLN   A 1 128 ? 105.901 23.835 13.883  1    35.5  ?  108 GLN   A N   1 1 
ATOM   846  C CA  . GLN   A 1 128 ? 105.432 22.926 14.94   1    38.87 ?  108 GLN   A CA  1 1 
ATOM   847  C C   . GLN   A 1 128 ? 104.567 23.661 15.973  1    43.15 ?  108 GLN   A C   1 1 
ATOM   848  O O   . GLN   A 1 128 ? 103.721 23.038 16.599  1    45.24 ?  108 GLN   A O   1 1 
ATOM   849  C CB  . GLN   A 1 128 ? 106.604 22.211 15.557  1    39.25 ?  108 GLN   A CB  1 1 
ATOM   850  C CG  . GLN   A 1 128 ? 107.14  21.217 14.563  1    42.62 ?  108 GLN   A CG  1 1 
ATOM   851  C CD  . GLN   A 1 128 ? 107.872 20.141 15.289  1    48.57 ?  108 GLN   A CD  1 1 
ATOM   852  O OE1 . GLN   A 1 128 ? 109.076 20.244 15.533  1    51.17 ?  108 GLN   A OE1 1 1 
ATOM   853  N NE2 . GLN   A 1 128 ? 107.157 19.08  15.644  1    49.35 ?  108 GLN   A NE2 1 1 
ATOM   854  N N   . LYS   A 1 129 ? 104.738 24.976 16.119  1    45.94 ?  109 LYS   A N   1 1 
ATOM   855  C CA  . LYS   A 1 129 ? 103.884 25.77  16.998  1    48.09 ?  109 LYS   A CA  1 1 
ATOM   856  C C   . LYS   A 1 129 ? 102.493 25.87  16.371  1    50.03 ?  109 LYS   A C   1 1 
ATOM   857  O O   . LYS   A 1 129 ? 101.493 25.717 17.071  1    51.25 ?  109 LYS   A O   1 1 
ATOM   858  C CB  . LYS   A 1 129 ? 104.466 27.174 17.167  1    50.6  ?  109 LYS   A CB  1 1 
ATOM   859  C CG  . LYS   A 1 129 ? 105.596 27.228 18.163  1    55.4  ?  109 LYS   A CG  1 1 
ATOM   860  C CD  . LYS   A 1 129 ? 106.154 28.624 18.174  1    60.55 ?  109 LYS   A CD  1 1 
ATOM   861  C CE  . LYS   A 1 129 ? 105.209 29.611 18.804  1    63.74 ?  109 LYS   A CE  1 1 
ATOM   862  N NZ  . LYS   A 1 129 ? 104.945 30.744 17.881  1    65.92 ?  109 LYS   A NZ  1 1 
ATOM   863  N N   . ASP   A 1 130 ? 102.425 26.136 15.065  1    50.52 ?  110 ASP   A N   1 1 
ATOM   864  C CA  . ASP   A 1 130 ? 101.155 26.267 14.369  1    51.92 ?  110 ASP   A CA  1 1 
ATOM   865  C C   . ASP   A 1 130 ? 100.444 24.927 14.156  1    52.57 ?  110 ASP   A C   1 1 
ATOM   866  O O   . ASP   A 1 130 ? 99.229  24.911 13.954  1    53.51 ?  110 ASP   A O   1 1 
ATOM   867  C CB  . ASP   A 1 130 ? 101.352 26.971 13.025  1    54.64 ?  110 ASP   A CB  1 1 
ATOM   868  C CG  . ASP   A 1 130 ? 101.888 28.385 13.1    1    62.53 ?  110 ASP   A CG  1 1 
ATOM   869  O OD1 . ASP   A 1 130 ? 102.157 28.867 14.231  1    64.33 ?  110 ASP   A OD1 1 1 
ATOM   870  O OD2 . ASP   A 1 130 ? 102.043 29.01  12.037  1    65.72 ?  110 ASP   A OD2 1 1 
ATOM   871  N N   . TYR   A 1 131 ? 101.194 23.81  14.147  1    51.82 ?  111 TYR   A N   1 1 
ATOM   872  C CA  . TYR   A 1 131 ? 100.639 22.471 13.935  1    51.46 ?  111 TYR   A CA  1 1 
ATOM   873  C C   . TYR   A 1 131 ? 101.259 21.528 14.955  1    51.63 ?  111 TYR   A C   1 1 
ATOM   874  O O   . TYR   A 1 131 ? 102.116 20.718 14.607  1    52.63 ?  111 TYR   A O   1 1 
ATOM   875  C CB  . TYR   A 1 131 ? 100.916 21.983 12.488  1    51.07 ?  111 TYR   A CB  1 1 
ATOM   876  C CG  . TYR   A 1 131 ? 100.36  22.903 11.424  1    51.91 ?  111 TYR   A CG  1 1 
ATOM   877  C CD1 . TYR   A 1 131 ? 101.087 23.994 10.972  1    52.8  ?  111 TYR   A CD1 1 1 
ATOM   878  C CD2 . TYR   A 1 131 ? 99.08   22.72  10.916  1    53.04 ?  111 TYR   A CD2 1 1 
ATOM   879  C CE1 . TYR   A 1 131 ? 100.565 24.875 10.037  1    54.25 ?  111 TYR   A CE1 1 1 
ATOM   880  C CE2 . TYR   A 1 131 ? 98.552  23.587 9.964   1    54.04 ?  111 TYR   A CE2 1 1 
ATOM   881  C CZ  . TYR   A 1 131 ? 99.296  24.67  9.533   1    55.58 ?  111 TYR   A CZ  1 1 
ATOM   882  O OH  . TYR   A 1 131 ? 98.81   25.549 8.588   1    58.22 ?  111 TYR   A OH  1 1 
ATOM   883  N N   . PRO   A 1 132 ? 100.879 21.651 16.249  1    50.63 ?  112 PRO   A N   1 1 
ATOM   884  C CA  . PRO   A 1 132 ? 101.496 20.8   17.279  1    49.59 ?  112 PRO   A CA  1 1 
ATOM   885  C C   . PRO   A 1 132 ? 101.062 19.35  17.218  1    48.94 ?  112 PRO   A C   1 1 
ATOM   886  O O   . PRO   A 1 132 ? 99.982  19.038 16.712  1    49.69 ?  112 PRO   A O   1 1 
ATOM   887  C CB  . PRO   A 1 132 ? 101.024 21.439 18.593  1    50.5  ?  112 PRO   A CB  1 1 
ATOM   888  C CG  . PRO   A 1 132 ? 99.741  22.059 18.246  1    51.27 ?  112 PRO   A CG  1 1 
ATOM   889  C CD  . PRO   A 1 132 ? 99.911  22.595 16.847  1    49.98 ?  112 PRO   A CD  1 1 
ATOM   890  N N   . GLY   A 1 133 ? 101.903 18.485 17.772  1    47.55 ?  113 GLY   A N   1 1 
ATOM   891  C CA  . GLY   A 1 133 ? 101.64  17.056 17.823  1    46.86 ?  113 GLY   A CA  1 1 
ATOM   892  C C   . GLY   A 1 133 ? 101.863 16.304 16.529  1    45.46 ?  113 GLY   A C   1 1 
ATOM   893  O O   . GLY   A 1 133 ? 101.684 15.078 16.5    1    46.22 ?  113 GLY   A O   1 1 
ATOM   894  N N   . LEU   A 1 134 ? 102.258 16.998 15.448  1    43.34 ?  114 LEU   A N   1 1 
ATOM   895  C CA  . LEU   A 1 134 ? 102.47  16.313 14.175  1    41.86 ?  114 LEU   A CA  1 1 
ATOM   896  C C   . LEU   A 1 134 ? 103.896 15.868 13.985  1    39.62 ?  114 LEU   A C   1 1 
ATOM   897  O O   . LEU   A 1 134 ? 104.825 16.614 14.294  1    40.05 ?  114 LEU   A O   1 1 
ATOM   898  C CB  . LEU   A 1 134 ? 102.054 17.169 12.974  1    42.19 ?  114 LEU   A CB  1 1 
ATOM   899  C CG  . LEU   A 1 134 ? 100.578 17.497 12.823  1    44.86 ?  114 LEU   A CG  1 1 
ATOM   900  C CD1 . LEU   A 1 134 ? 100.343 18.293 11.55   1    45.82 ?  114 LEU   A CD1 1 1 
ATOM   901  C CD2 . LEU   A 1 134 ? 99.703  16.237 12.852  1    45.59 ?  114 LEU   A CD2 1 1 
ATOM   902  N N   . PRO   A 1 135 ? 104.083 14.671 13.413  1    37.38 ?  115 PRO   A N   1 1 
ATOM   903  C CA  . PRO   A 1 135 ? 105.451 14.222 13.077  1    35.04 ?  115 PRO   A CA  1 1 
ATOM   904  C C   . PRO   A 1 135 ? 106.075 15.128 12.018  1    31.74 ?  115 PRO   A C   1 1 
ATOM   905  O O   . PRO   A 1 135 ? 105.344 15.695 11.217  1    32.25 ?  115 PRO   A O   1 1 
ATOM   906  C CB  . PRO   A 1 135 ? 105.227 12.831 12.455  1    36.97 ?  115 PRO   A CB  1 1 
ATOM   907  C CG  . PRO   A 1 135 ? 103.837 12.421 12.898  1    38.44 ?  115 PRO   A CG  1 1 
ATOM   908  C CD  . PRO   A 1 135 ? 103.061 13.681 12.998  1    37.84 ?  115 PRO   A CD  1 1 
ATOM   909  N N   . VAL   A 1 136 ? 107.405 15.285 12.044  1    27.82 ?  116 VAL   A N   1 1 
ATOM   910  C CA  A VAL   A 1 136 ? 108.057 16.111 11.037  0.56 27.19 ?  116 VAL   A CA  1 1 
ATOM   911  C CA  B VAL   A 1 136 ? 108.105 16.126 11.073  0.44 26.72 ?  116 VAL   A CA  1 1 
ATOM   912  C C   . VAL   A 1 136 ? 109.16  15.339 10.332  1    26.19 ?  116 VAL   A C   1 1 
ATOM   913  O O   . VAL   A 1 136 ? 109.988 14.68  10.956  1    28.13 ?  116 VAL   A O   1 1 
ATOM   914  C CB  A VAL   A 1 136 ? 108.52  17.481 11.559  0.56 29.5  ?  116 VAL   A CB  1 1 
ATOM   915  C CB  B VAL   A 1 136 ? 108.754 17.348 11.739  0.44 27.8  ?  116 VAL   A CB  1 1 
ATOM   916  C CG1 A VAL   A 1 136 ? 109.574 17.331 12.646  0.56 31    ?  116 VAL   A CG1 1 1 
ATOM   917  C CG1 B VAL   A 1 136 ? 109.451 18.232 10.704  0.44 27.92 ?  116 VAL   A CG1 1 1 
ATOM   918  C CG2 A VAL   A 1 136 ? 109.015 18.37  10.418  0.56 28.96 ?  116 VAL   A CG2 1 1 
ATOM   919  C CG2 B VAL   A 1 136 ? 107.717 18.156 12.493  0.44 27.69 ?  116 VAL   A CG2 1 1 
ATOM   920  N N   . PHE   A 1 137 ? 109.133 15.392 9.004   1    24.57 ?  117 PHE   A N   1 1 
ATOM   921  C CA  . PHE   A 1 137 ? 110.111 14.724 8.162   1    23.94 ?  117 PHE   A CA  1 1 
ATOM   922  C C   . PHE   A 1 137 ? 110.967 15.804 7.47    1    23.68 ?  117 PHE   A C   1 1 
ATOM   923  O O   . PHE   A 1 137 ? 110.561 16.98  7.393   1    23.62 ?  117 PHE   A O   1 1 
ATOM   924  C CB  . PHE   A 1 137 ? 109.382 13.949 7.017   1    23.79 ?  117 PHE   A CB  1 1 
ATOM   925  C CG  . PHE   A 1 137 ? 108.668 12.723 7.515   1    26    ?  117 PHE   A CG  1 1 
ATOM   926  C CD1 . PHE   A 1 137 ? 107.417 12.82  8.09    1    28.32 ?  117 PHE   A CD1 1 1 
ATOM   927  C CD2 . PHE   A 1 137 ? 109.192 11.462 7.291   1    27.04 ?  117 PHE   A CD2 1 1 
ATOM   928  C CE1 . PHE   A 1 137 ? 106.751 11.676 8.547   1    29.38 ?  117 PHE   A CE1 1 1 
ATOM   929  C CE2 . PHE   A 1 137 ? 108.529 10.312 7.761   1    28.12 ?  117 PHE   A CE2 1 1 
ATOM   930  C CZ  . PHE   A 1 137 ? 107.321 10.437 8.395   1    28.96 ?  117 PHE   A CZ  1 1 
ATOM   931  N N   . LEU   A 1 138 ? 112.138 15.38  6.951   1    23.62 ?  118 LEU   A N   1 1 
ATOM   932  C CA  . LEU   A 1 138 ? 113.006 16.247 6.139   1    23.68 ?  118 LEU   A CA  1 1 
ATOM   933  C C   . LEU   A 1 138 ? 113.199 15.592 4.808   1    23.18 ?  118 LEU   A C   1 1 
ATOM   934  O O   . LEU   A 1 138 ? 113.263 14.357 4.716   1    23.3  ?  118 LEU   A O   1 1 
ATOM   935  C CB  . LEU   A 1 138 ? 114.395 16.361 6.769   1    23.92 ?  118 LEU   A CB  1 1 
ATOM   936  C CG  . LEU   A 1 138 ? 114.38  17.018 8.185   1    26.92 ?  118 LEU   A CG  1 1 
ATOM   937  C CD1 . LEU   A 1 138 ? 115.7   16.794 8.909   1    29.36 ?  118 LEU   A CD1 1 1 
ATOM   938  C CD2 . LEU   A 1 138 ? 113.973 18.5   8.103   1    28.33 ?  118 LEU   A CD2 1 1 
ATOM   939  N N   . LEU   A 1 139 ? 113.34  16.368 3.758   1    21.32 ?  119 LEU   A N   1 1 
ATOM   940  C CA  . LEU   A 1 139 ? 113.691 15.862 2.446   1    21.84 ?  119 LEU   A CA  1 1 
ATOM   941  C C   . LEU   A 1 139 ? 114.772 16.784 1.936   1    21.54 ?  119 LEU   A C   1 1 
ATOM   942  O O   . LEU   A 1 139 ? 114.542 18.01  1.941   1    21.64 ?  119 LEU   A O   1 1 
ATOM   943  C CB  . LEU   A 1 139 ? 112.479 15.836 1.509   1    23.66 ?  119 LEU   A CB  1 1 
ATOM   944  C CG  . LEU   A 1 139 ? 112.725 15.244 0.117   1    26.25 ?  119 LEU   A CG  1 1 
ATOM   945  C CD1 . LEU   A 1 139 ? 111.474 14.549 -0.413  1    27.25 ?  119 LEU   A CD1 1 1 
ATOM   946  C CD2 . LEU   A 1 139 ? 113.166 16.327 -0.868  1    25.55 ?  119 LEU   A CD2 1 1 
ATOM   947  N N   . GLY   A 1 140 ? 115.902 16.244 1.499   1    21.23 ?  120 GLY   A N   1 1 
ATOM   948  C CA  . GLY   A 1 140 ? 116.955 17.108 0.975   1    20.98 ?  120 GLY   A CA  1 1 
ATOM   949  C C   . GLY   A 1 140 ? 117.705 16.498 -0.185  1    21.04 ?  120 GLY   A C   1 1 
ATOM   950  O O   . GLY   A 1 140 ? 117.866 15.266 -0.248  1    21.37 ?  120 GLY   A O   1 1 
ATOM   951  N N   . HIS   A 1 141 ? 118.136 17.339 -1.11   1    19.65 ?  121 HIS   A N   1 1 
ATOM   952  C CA  . HIS   A 1 141 ? 118.944 16.904 -2.246  1    19.83 ?  121 HIS   A CA  1 1 
ATOM   953  C C   . HIS   A 1 141 ? 120.297 17.574 -2.213  1    19.62 ?  121 HIS   A C   1 1 
ATOM   954  O O   . HIS   A 1 141 ? 120.374 18.807 -2.032  1    20.41 ?  121 HIS   A O   1 1 
ATOM   955  C CB  . HIS   A 1 141 ? 118.208 17.308 -3.536  1    21.68 ?  121 HIS   A CB  1 1 
ATOM   956  C CG  . HIS   A 1 141 ? 119.053 17.185 -4.773  1    20.54 ?  121 HIS   A CG  1 1 
ATOM   957  N ND1 . HIS   A 1 141 ? 119.682 16.012 -5.129  1    20.73 ?  121 HIS   A ND1 1 1 
ATOM   958  C CD2 . HIS   A 1 141 ? 119.259 18.114 -5.747  1    21.69 ?  121 HIS   A CD2 1 1 
ATOM   959  C CE1 . HIS   A 1 141 ? 120.256 16.255 -6.313  1    21.62 ?  121 HIS   A CE1 1 1 
ATOM   960  N NE2 . HIS   A 1 141 ? 120.07  17.519 -6.691  1    23.15 ?  121 HIS   A NE2 1 1 
ATOM   961  N N   . SER   A 1 142 ? 121.366 16.779 -2.451  1    19.83 ?  122 SER   A N   1 1 
ATOM   962  C CA  . SER   A 1 142 ? 122.719 17.309 -2.631  1    20.56 ?  122 SER   A CA  1 1 
ATOM   963  C C   . SER   A 1 142 ? 123.191 18.15  -1.409  1    20.92 ?  122 SER   A C   1 1 
ATOM   964  O O   . SER   A 1 142 ? 123.124 17.645 -0.271  1    21.1  ?  122 SER   A O   1 1 
ATOM   965  C CB  . SER   A 1 142 ? 122.773 18.053 -3.972  1    23.2  ?  122 SER   A CB  1 1 
ATOM   966  O OG  . SER   A 1 142 ? 124.122 18.246 -4.372  1    24.69 ?  122 SER   A OG  1 1 
ATOM   967  N N   . MET   A 1 143 ? 123.563 19.454 -1.573  1    20.08 ?  123 MET   A N   1 1 
ATOM   968  C CA  . MET   A 1 143 ? 123.902 20.255 -0.375  1    21.08 ?  123 MET   A CA  1 1 
ATOM   969  C C   . MET   A 1 143 ? 122.728 20.273 0.62    1    21.2  ?  123 MET   A C   1 1 
ATOM   970  O O   . MET   A 1 143 ? 122.941 20.27  1.827   1    22.94 ?  123 MET   A O   1 1 
ATOM   971  C CB  . MET   A 1 143 ? 124.228 21.696 -0.773  1    22.17 ?  123 MET   A CB  1 1 
ATOM   972  C CG  . MET   A 1 143 ? 124.609 22.54  0.416   1    23.79 ?  123 MET   A CG  1 1 
ATOM   973  S SD  . MET   A 1 143 ? 124.796 24.275 -0.108  1    25.38 ?  123 MET   A SD  1 1 
ATOM   974  C CE  . MET   A 1 143 ? 123.055 24.811 -0.008  1    23.25 ?  123 MET   A CE  1 1 
ATOM   975  N N   . GLY   A 1 144 ? 121.502 20.265 0.098   1    19.97 ?  124 GLY   A N   1 1 
ATOM   976  C CA  . GLY   A 1 144 ? 120.281 20.24  0.906   1    20.27 ?  124 GLY   A CA  1 1 
ATOM   977  C C   . GLY   A 1 144 ? 120.176 18.963 1.739   1    21.1  ?  124 GLY   A C   1 1 
ATOM   978  O O   . GLY   A 1 144 ? 119.542 18.974 2.782   1    22.03 ?  124 GLY   A O   1 1 
ATOM   979  N N   . GLY   A 1 145 ? 120.731 17.864 1.235   1    21.73 ?  125 GLY   A N   1 1 
ATOM   980  C CA  . GLY   A 1 145 ? 120.776 16.577 1.931   1    21.62 ?  125 GLY   A CA  1 1 
ATOM   981  C C   . GLY   A 1 145 ? 121.792 16.637 3.058   1    22.18 ?  125 GLY   A C   1 1 
ATOM   982  O O   . GLY   A 1 145 ? 121.527 16.117 4.142   1    23.66 ?  125 GLY   A O   1 1 
ATOM   983  N N   . ALA   A 1 146 ? 122.946 17.314 2.834   1    23.41 ?  126 ALA   A N   1 1 
ATOM   984  C CA  . ALA   A 1 146 ? 123.925 17.536 3.927   1    24.65 ?  126 ALA   A CA  1 1 
ATOM   985  C C   . ALA   A 1 146 ? 123.261 18.39  5.021   1    24.2  ?  126 ALA   A C   1 1 
ATOM   986  O O   . ALA   A 1 146 ? 123.37  18.079 6.21    1    25.59 ?  126 ALA   A O   1 1 
ATOM   987  C CB  . ALA   A 1 146 ? 125.177 18.23  3.428   1    24.74 ?  126 ALA   A CB  1 1 
ATOM   988  N N   . ILE   A 1 147 ? 122.494 19.423 4.621   1    23.2  ?  127 ILE   A N   1 1 
ATOM   989  C CA  . ILE   A 1 147 ? 121.751 20.24  5.592   1    22.96 ?  127 ILE   A CA  1 1 
ATOM   990  C C   . ILE   A 1 147 ? 120.761 19.373 6.356   1    23.64 ?  127 ILE   A C   1 1 
ATOM   991  O O   . ILE   A 1 147 ? 120.739 19.484 7.587   1    24.36 ?  127 ILE   A O   1 1 
ATOM   992  C CB  . ILE   A 1 147 ? 121.027 21.397 4.884   1    23.39 ?  127 ILE   A CB  1 1 
ATOM   993  C CG1 . ILE   A 1 147 ? 122.064 22.369 4.312   1    23.04 ?  127 ILE   A CG1 1 1 
ATOM   994  C CG2 . ILE   A 1 147 ? 120.042 22.125 5.809   1    23.66 ?  127 ILE   A CG2 1 1 
ATOM   995  C CD1 . ILE   A 1 147 ? 121.464 23.437 3.256   1    23.16 ?  127 ILE   A CD1 1 1 
ATOM   996  N N   . ALA   A 1 148 ? 120     18.467 5.671   1    22.33 ?  128 ALA   A N   1 1 
ATOM   997  C CA  . ALA   A 1 148 ? 119.026 17.624 6.359   1    23.21 ?  128 ALA   A CA  1 1 
ATOM   998  C C   . ALA   A 1 148 ? 119.724 16.707 7.341   1    24.81 ?  128 ALA   A C   1 1 
ATOM   999  O O   . ALA   A 1 148 ? 119.226 16.52  8.466   1    24.66 ?  128 ALA   A O   1 1 
ATOM   1000 C CB  . ALA   A 1 148 ? 118.216 16.781 5.353   1    22.99 ?  128 ALA   A CB  1 1 
ATOM   1001 N N   . ILE   A 1 149 ? 120.858 16.089 6.934   1    24.12 ?  129 ILE   A N   1 1 
ATOM   1002 C CA  . ILE   A 1 149 ? 121.602 15.201 7.861   1    24.31 ?  129 ILE   A CA  1 1 
ATOM   1003 C C   . ILE   A 1 149 ? 122.037 15.984 9.123   1    25.08 ?  129 ILE   A C   1 1 
ATOM   1004 O O   . ILE   A 1 149 ? 121.869 15.472 10.24   1    25.64 ?  129 ILE   A O   1 1 
ATOM   1005 C CB  . ILE   A 1 149 ? 122.849 14.627 7.146   1    25.42 ?  129 ILE   A CB  1 1 
ATOM   1006 C CG1 . ILE   A 1 149 ? 122.416 13.596 6.074   1    26.57 ?  129 ILE   A CG1 1 1 
ATOM   1007 C CG2 . ILE   A 1 149 ? 123.878 13.979 8.162   1    26.57 ?  129 ILE   A CG2 1 1 
ATOM   1008 C CD1 . ILE   A 1 149 ? 123.513 13.284 5.142   1    26.66 ?  129 ILE   A CD1 1 1 
ATOM   1009 N N   . LEU   A 1 150 ? 122.612 17.185 8.946   1    25.22 ?  130 LEU   A N   1 1 
ATOM   1010 C CA  . LEU   A 1 150 ? 123.09  17.946 10.105  1    26.26 ?  130 LEU   A CA  1 1 
ATOM   1011 C C   . LEU   A 1 150 ? 121.93  18.426 10.954  1    27.62 ?  130 LEU   A C   1 1 
ATOM   1012 O O   . LEU   A 1 150 ? 122.065 18.5   12.179  1    31.31 ?  130 LEU   A O   1 1 
ATOM   1013 C CB  . LEU   A 1 150 ? 124.016 19.094 9.628   1    25.41 ?  130 LEU   A CB  1 1 
ATOM   1014 C CG  . LEU   A 1 150 ? 125.256 18.568 8.896   1    28.26 ?  130 LEU   A CG  1 1 
ATOM   1015 C CD1 . LEU   A 1 150 ? 126.072 19.666 8.332   1    28.48 ?  130 LEU   A CD1 1 1 
ATOM   1016 C CD2 . LEU   A 1 150 ? 126.122 17.661 9.785   1    29.86 ?  130 LEU   A CD2 1 1 
ATOM   1017 N N   . THR   A 1 151 ? 120.758 18.694 10.348  1    26.04 ?  131 THR   A N   1 1 
ATOM   1018 C CA  . THR   A 1 151 ? 119.593 19.156 11.108  1    26.68 ?  131 THR   A CA  1 1 
ATOM   1019 C C   . THR   A 1 151 ? 119.114 17.992 11.969  1    27.53 ?  131 THR   A C   1 1 
ATOM   1020 O O   . THR   A 1 151 ? 118.934 18.152 13.178  1    27.96 ?  131 THR   A O   1 1 
ATOM   1021 C CB  . THR   A 1 151 ? 118.513 19.598 10.092  1    26.84 ?  131 THR   A CB  1 1 
ATOM   1022 O OG1 . THR   A 1 151 ? 119.002 20.763 9.376   1    26.85 ?  131 THR   A OG1 1 1 
ATOM   1023 C CG2 . THR   A 1 151 ? 117.203 19.969 10.772  1    28.91 ?  131 THR   A CG2 1 1 
ATOM   1024 N N   . ALA   A 1 152 ? 118.993 16.791 11.387  1    26.52 ?  132 ALA   A N   1 1 
ATOM   1025 C CA  . ALA   A 1 152 ? 118.543 15.632 12.171  1    28.95 ?  132 ALA   A CA  1 1 
ATOM   1026 C C   . ALA   A 1 152 ? 119.576 15.283 13.236  1    32.67 ?  132 ALA   A C   1 1 
ATOM   1027 O O   . ALA   A 1 152 ? 119.18  14.9   14.345  1    35.65 ?  132 ALA   A O   1 1 
ATOM   1028 C CB  . ALA   A 1 152 ? 118.287 14.451 11.248  1    27.96 ?  132 ALA   A CB  1 1 
ATOM   1029 N N   . ALA   A 1 153 ? 120.885 15.44  12.947  1    33.1  ?  133 ALA   A N   1 1 
ATOM   1030 C CA  . ALA   A 1 153 ? 121.916 15.091 13.951  1    35.58 ?  133 ALA   A CA  1 1 
ATOM   1031 C C   . ALA   A 1 153 ? 121.909 16.048 15.146  1    36.52 ?  133 ALA   A C   1 1 
ATOM   1032 O O   . ALA   A 1 153 ? 122.312 15.659 16.257  1    37.89 ?  133 ALA   A O   1 1 
ATOM   1033 C CB  . ALA   A 1 153 ? 123.303 15.087 13.332  1    36.29 ?  133 ALA   A CB  1 1 
ATOM   1034 N N   . GLU   A 1 154 ? 121.511 17.282 14.918  1    35.13 ?  134 GLU   A N   1 1 
ATOM   1035 C CA  . GLU   A 1 154 ? 121.43  18.287 15.971  1    36.36 ?  134 GLU   A CA  1 1 
ATOM   1036 C C   . GLU   A 1 154 ? 120.237 18.01  16.915  1    37.62 ?  134 GLU   A C   1 1 
ATOM   1037 O O   . GLU   A 1 154 ? 120.249 18.479 18.064  1    39.76 ?  134 GLU   A O   1 1 
ATOM   1038 C CB  . GLU   A 1 154 ? 121.285 19.668 15.322  1    39.01 ?  134 GLU   A CB  1 1 
ATOM   1039 C CG  . GLU   A 1 154 ? 121.423 20.757 16.352  1    44.27 ?  134 GLU   A CG  1 1 
ATOM   1040 C CD  . GLU   A 1 154 ? 121.774 22.106 15.777  1    49.62 ?  134 GLU   A CD  1 1 
ATOM   1041 O OE1 . GLU   A 1 154 ? 122.552 22.131 14.799  1    49.68 ?  134 GLU   A OE1 1 1 
ATOM   1042 O OE2 . GLU   A 1 154 ? 121.304 23.133 16.32   1    54.18 ?  134 GLU   A OE2 1 1 
ATOM   1043 N N   . ARG   A 1 155 ? 119.187 17.297 16.439  1    35.35 ?  135 ARG   A N   1 1 
ATOM   1044 C CA  . ARG   A 1 155 ? 117.988 17.015 17.22   1    34.76 ?  135 ARG   A CA  1 1 
ATOM   1045 C C   . ARG   A 1 155 ? 117.658 15.516 17.198  1    36.1  ?  135 ARG   A C   1 1 
ATOM   1046 O O   . ARG   A 1 155 ? 116.641 15.1   16.649  1    35.05 ?  135 ARG   A O   1 1 
ATOM   1047 C CB  . ARG   A 1 155 ? 116.779 17.838 16.733  1    34.12 ?  135 ARG   A CB  1 1 
ATOM   1048 C CG  . ARG   A 1 155 ? 116.981 19.371 16.668  1    32.79 ?  135 ARG   A CG  1 1 
ATOM   1049 C CD  . ARG   A 1 155 ? 116.37  20.076 17.839  1    37.5  ?  135 ARG   A CD  1 1 
ATOM   1050 N NE  . ARG   A 1 155 ? 116.506 21.536 17.696  1    35.99 ?  135 ARG   A NE  1 1 
ATOM   1051 C CZ  . ARG   A 1 155 ? 115.523 22.351 17.338  1    36.36 ?  135 ARG   A CZ  1 1 
ATOM   1052 N NH1 . ARG   A 1 155 ? 114.343 21.86  16.977  1    34.93 ?  135 ARG   A NH1 1 1 
ATOM   1053 N NH2 . ARG   A 1 155 ? 115.739 23.66  17.245  1    33.42 ?  135 ARG   A NH2 1 1 
ATOM   1054 N N   . PRO   A 1 156 ? 118.523 14.676 17.79   1    38.9  ?  136 PRO   A N   1 1 
ATOM   1055 C CA  . PRO   A 1 156 ? 118.244 13.232 17.813  1    39.43 ?  136 PRO   A CA  1 1 
ATOM   1056 C C   . PRO   A 1 156 ? 116.899 12.904 18.448  1    38.59 ?  136 PRO   A C   1 1 
ATOM   1057 O O   . PRO   A 1 156 ? 116.511 13.475 19.474  1    38.02 ?  136 PRO   A O   1 1 
ATOM   1058 C CB  . PRO   A 1 156 ? 119.419 12.643 18.607  1    40.91 ?  136 PRO   A CB  1 1 
ATOM   1059 C CG  . PRO   A 1 156 ? 120.049 13.778 19.294  1    41.84 ?  136 PRO   A CG  1 1 
ATOM   1060 C CD  . PRO   A 1 156 ? 119.758 15.018 18.524  1    40.13 ?  136 PRO   A CD  1 1 
ATOM   1061 N N   . GLY   A 1 157 ? 116.154 12.089 17.736  1    37.71 ?  137 GLY   A N   1 1 
ATOM   1062 C CA  . GLY   A 1 157 ? 114.845 11.587 18.116  1    37.6  ?  137 GLY   A CA  1 1 
ATOM   1063 C C   . GLY   A 1 157 ? 113.671 12.476 17.797  1    37.71 ?  137 GLY   A C   1 1 
ATOM   1064 O O   . GLY   A 1 157 ? 112.528 12.053 17.986  1    39.92 ?  137 GLY   A O   1 1 
ATOM   1065 N N   . HIS   A 1 158 ? 113.927 13.686 17.26   1    35.39 ?  138 HIS   A N   1 1 
ATOM   1066 C CA  A HIS   A 1 158 ? 112.901 14.682 16.962  0.5  35.12 ?  138 HIS   A CA  1 1 
ATOM   1067 C CA  B HIS   A 1 158 ? 112.831 14.599 17.013  0.5  35.57 ?  138 HIS   A CA  1 1 
ATOM   1068 C C   . HIS   A 1 158 ? 112.222 14.485 15.618  1    35.38 ?  138 HIS   A C   1 1 
ATOM   1069 O O   . HIS   A 1 158 ? 111.038 14.837 15.452  1    37.84 ?  138 HIS   A O   1 1 
ATOM   1070 C CB  A HIS   A 1 158 ? 113.548 16.075 16.977  0.5  35.49 ?  138 HIS   A CB  1 1 
ATOM   1071 C CB  B HIS   A 1 158 ? 113.254 16.019 17.345  0.5  37.04 ?  138 HIS   A CB  1 1 
ATOM   1072 C CG  A HIS   A 1 158 ? 112.605 17.215 16.747  0.5  37.85 ?  138 HIS   A CG  1 1 
ATOM   1073 C CG  B HIS   A 1 158 ? 113.462 16.222 18.817  0.5  40.53 ?  138 HIS   A CG  1 1 
ATOM   1074 N ND1 A HIS   A 1 158 ? 111.94  17.815 17.8    0.5  40.36 ?  138 HIS   A ND1 1 1 
ATOM   1075 N ND1 B HIS   A 1 158 ? 114.716 16.1   19.4    0.5  42.48 ?  138 HIS   A ND1 1 1 
ATOM   1076 C CD2 A HIS   A 1 158 ? 112.294 17.871 15.602  0.5  38.93 ?  138 HIS   A CD2 1 1 
ATOM   1077 C CD2 B HIS   A 1 158 ? 112.561 16.516 19.785  0.5  42.65 ?  138 HIS   A CD2 1 1 
ATOM   1078 C CE1 A HIS   A 1 158 ? 111.247 18.807 17.264  0.5  40.87 ?  138 HIS   A CE1 1 1 
ATOM   1079 C CE1 B HIS   A 1 158 ? 114.545 16.37  20.684  0.5  43.52 ?  138 HIS   A CE1 1 1 
ATOM   1080 N NE2 A HIS   A 1 158 ? 111.411 18.859 15.939  0.5  39.94 ?  138 HIS   A NE2 1 1 
ATOM   1081 N NE2 B HIS   A 1 158 ? 113.266 16.62  20.967  0.5  43.7  ?  138 HIS   A NE2 1 1 
ATOM   1082 N N   . PHE   A 1 159 ? 113     14.044 14.619  1    31.89 ?  139 PHE   A N   1 1 
ATOM   1083 C CA  . PHE   A 1 159 ? 112.442 13.919 13.267  1    30.05 ?  139 PHE   A CA  1 1 
ATOM   1084 C C   . PHE   A 1 159 ? 111.928 12.496 13.025  1    29.6  ?  139 PHE   A C   1 1 
ATOM   1085 O O   . PHE   A 1 159 ? 112.546 11.526 13.472  1    30.18 ?  139 PHE   A O   1 1 
ATOM   1086 C CB  . PHE   A 1 159 ? 113.495 14.297 12.213  1    28.99 ?  139 PHE   A CB  1 1 
ATOM   1087 C CG  . PHE   A 1 159 ? 113.723 15.793 12.234  1    28.24 ?  139 PHE   A CG  1 1 
ATOM   1088 C CD1 . PHE   A 1 159 ? 112.856 16.649 11.577  1    27.8  ?  139 PHE   A CD1 1 1 
ATOM   1089 C CD2 . PHE   A 1 159 ? 114.797 16.337 12.919  1    27.79 ?  139 PHE   A CD2 1 1 
ATOM   1090 C CE1 . PHE   A 1 159 ? 113.038 18.033 11.643  1    28.11 ?  139 PHE   A CE1 1 1 
ATOM   1091 C CE2 . PHE   A 1 159 ? 114.993 17.716 12.956  1    27.76 ?  139 PHE   A CE2 1 1 
ATOM   1092 C CZ  . PHE   A 1 159 ? 114.113 18.545 12.312  1    27.61 ?  139 PHE   A CZ  1 1 
ATOM   1093 N N   . ALA   A 1 160 ? 110.777 12.376 12.353  1    29.18 ?  140 ALA   A N   1 1 
ATOM   1094 C CA  . ALA   A 1 160 ? 110.181 11.066 12.085  1    28.76 ?  140 ALA   A CA  1 1 
ATOM   1095 C C   . ALA   A 1 160 ? 110.935 10.313 10.978  1    28.51 ?  140 ALA   A C   1 1 
ATOM   1096 O O   . ALA   A 1 160 ? 110.863 9.081  10.917  1    29.91 ?  140 ALA   A O   1 1 
ATOM   1097 C CB  . ALA   A 1 160 ? 108.727 11.238 11.658  1    30.01 ?  140 ALA   A CB  1 1 
ATOM   1098 N N   . GLY   A 1 161 ? 111.568 11.04  10.058  1    26.16 ?  141 GLY   A N   1 1 
ATOM   1099 C CA  . GLY   A 1 161 ? 112.267 10.406 8.946   1    25.55 ?  141 GLY   A CA  1 1 
ATOM   1100 C C   . GLY   A 1 161 ? 112.889 11.445 8.027   1    24.68 ?  141 GLY   A C   1 1 
ATOM   1101 O O   . GLY   A 1 161 ? 112.572 12.636 8.092   1    25.1  ?  141 GLY   A O   1 1 
ATOM   1102 N N   . MET   A 1 162 ? 113.802 10.986 7.203   1    25.08 ?  142 MET   A N   1 1 
ATOM   1103 C CA  A MET   A 1 162 ? 114.532 11.834 6.29    0.5  24.45 ?  142 MET   A CA  1 1 
ATOM   1104 C CA  B MET   A 1 162 ? 114.481 11.849 6.231   0.5  24.82 ?  142 MET   A CA  1 1 
ATOM   1105 C C   . MET   A 1 162 ? 114.581 11.125 4.93    1    23.17 ?  142 MET   A C   1 1 
ATOM   1106 O O   . MET   A 1 162 ? 114.914 9.925  4.9     1    22.58 ?  142 MET   A O   1 1 
ATOM   1107 C CB  A MET   A 1 162 ? 115.948 11.941 6.879   0.5  25.72 ?  142 MET   A CB  1 1 
ATOM   1108 C CB  B MET   A 1 162 ? 115.936 12.14  6.591   0.5  27.18 ?  142 MET   A CB  1 1 
ATOM   1109 C CG  A MET   A 1 162 ? 116.838 12.942 6.234   0.5  25.94 ?  142 MET   A CG  1 1 
ATOM   1110 C CG  B MET   A 1 162 ? 116.165 12.807 7.884   0.5  30.96 ?  142 MET   A CG  1 1 
ATOM   1111 S SD  A MET   A 1 162 ? 118.385 13.108 7.177   0.5  25.37 ?  142 MET   A SD  1 1 
ATOM   1112 S SD  B MET   A 1 162 ? 117.804 13.511 7.738   0.5  36.63 ?  142 MET   A SD  1 1 
ATOM   1113 C CE  A MET   A 1 162 ? 118.993 11.417 7.169   0.5  25.4  ?  142 MET   A CE  1 1 
ATOM   1114 C CE  B MET   A 1 162 ? 118.818 12.139 7.656   0.5  28.74 ?  142 MET   A CE  1 1 
ATOM   1115 N N   . VAL   A 1 163 ? 114.353 11.853 3.844   1    21.54 ?  143 VAL   A N   1 1 
ATOM   1116 C CA  . VAL   A 1 163 ? 114.446 11.362 2.487   1    21.36 ?  143 VAL   A CA  1 1 
ATOM   1117 C C   . VAL   A 1 163 ? 115.62  12.129 1.892   1    20.82 ?  143 VAL   A C   1 1 
ATOM   1118 O O   . VAL   A 1 163 ? 115.623 13.385 1.879   1    21.46 ?  143 VAL   A O   1 1 
ATOM   1119 C CB  . VAL   A 1 163 ? 113.16  11.63  1.662   1    22.68 ?  143 VAL   A CB  1 1 
ATOM   1120 C CG1 . VAL   A 1 163 ? 113.37  11.291 0.187   1    23.56 ?  143 VAL   A CG1 1 1 
ATOM   1121 C CG2 . VAL   A 1 163 ? 111.984 10.839 2.241   1    25.27 ?  143 VAL   A CG2 1 1 
ATOM   1122 N N   . LEU   A 1 164 ? 116.645 11.401 1.447   1    20.75 ?  144 LEU   A N   1 1 
ATOM   1123 C CA  . LEU   A 1 164 ? 117.847 12.006 0.891   1    19.93 ?  144 LEU   A CA  1 1 
ATOM   1124 C C   . LEU   A 1 164 ? 118.001 11.634 -0.57   1    20.73 ?  144 LEU   A C   1 1 
ATOM   1125 O O   . LEU   A 1 164 ? 118.09  10.429 -0.884  1    20.9  ?  144 LEU   A O   1 1 
ATOM   1126 C CB  . LEU   A 1 164 ? 119.084 11.56  1.67    1    20.92 ?  144 LEU   A CB  1 1 
ATOM   1127 C CG  . LEU   A 1 164 ? 119.088 11.884 3.168   1    22.65 ?  144 LEU   A CG  1 1 
ATOM   1128 C CD1 . LEU   A 1 164 ? 120.204 11.176 3.904   1    25.62 ?  144 LEU   A CD1 1 1 
ATOM   1129 C CD2 . LEU   A 1 164 ? 119.133 13.359 3.417   1    23.06 ?  144 LEU   A CD2 1 1 
ATOM   1130 N N   . ILE   A 1 165 ? 118.147 12.647 -1.448  1    20.81 ?  145 ILE   A N   1 1 
ATOM   1131 C CA  . ILE   A 1 165 ? 118.373 12.392 -2.864  1    20.71 ?  145 ILE   A CA  1 1 
ATOM   1132 C C   . ILE   A 1 165 ? 119.766 12.852 -3.161  1    20.54 ?  145 ILE   A C   1 1 
ATOM   1133 O O   . ILE   A 1 165 ? 120.039 14.039 -3.075  1    20.79 ?  145 ILE   A O   1 1 
ATOM   1134 C CB  . ILE   A 1 165 ? 117.369 13.164 -3.701  1    21.7  ?  145 ILE   A CB  1 1 
ATOM   1135 C CG1 . ILE   A 1 165 ? 115.937 12.862 -3.2    1    23.98 ?  145 ILE   A CG1 1 1 
ATOM   1136 C CG2 . ILE   A 1 165 ? 117.588 12.904 -5.216  1    23    ?  145 ILE   A CG2 1 1 
ATOM   1137 C CD1 . ILE   A 1 165 ? 114.843 13.734 -3.958  1    25.5  ?  145 ILE   A CD1 1 1 
ATOM   1138 N N   . SER   A 1 166 ? 120.679 11.889 -3.447  1    20.77 ?  146 SER   A N   1 1 
ATOM   1139 C CA  A SER   A 1 166 ? 122.112 12.139 -3.694  0.37 20.92 ?  146 SER   A CA  1 1 
ATOM   1140 C CA  B SER   A 1 166 ? 122.092 12.177 -3.739  0.63 21.84 ?  146 SER   A CA  1 1 
ATOM   1141 C C   . SER   A 1 166 ? 122.671 13.212 -2.764  1    22.13 ?  146 SER   A C   1 1 
ATOM   1142 O O   . SER   A 1 166 ? 123.137 14.28  -3.179  1    22.18 ?  146 SER   A O   1 1 
ATOM   1143 C CB  A SER   A 1 166 ? 122.398 12.463 -5.155  0.37 20.52 ?  146 SER   A CB  1 1 
ATOM   1144 C CB  B SER   A 1 166 ? 122.264 12.657 -5.183  0.63 24.05 ?  146 SER   A CB  1 1 
ATOM   1145 O OG  A SER   A 1 166 ? 121.404 13.324 -5.68   0.37 18.99 ?  146 SER   A OG  1 1 
ATOM   1146 O OG  B SER   A 1 166 ? 121.435 11.935 -6.078  0.63 26.1  ?  146 SER   A OG  1 1 
ATOM   1147 N N   . PRO   A 1 167 ? 122.63  12.934 -1.461  1    21.5  ?  147 PRO   A N   1 1 
ATOM   1148 C CA  . PRO   A 1 167 ? 123.124 13.921 -0.493  1    22.76 ?  147 PRO   A CA  1 1 
ATOM   1149 C C   . PRO   A 1 167 ? 124.62  14.135 -0.612  1    23.37 ?  147 PRO   A C   1 1 
ATOM   1150 O O   . PRO   A 1 167 ? 125.347 13.205 -0.977  1    24.18 ?  147 PRO   A O   1 1 
ATOM   1151 C CB  . PRO   A 1 167 ? 122.754 13.307 0.868   1    21.78 ?  147 PRO   A CB  1 1 
ATOM   1152 C CG  . PRO   A 1 167 ? 122.851 11.813 0.606   1    21.72 ?  147 PRO   A CG  1 1 
ATOM   1153 C CD  . PRO   A 1 167 ? 122.196 11.68  -0.786  1    21.4  ?  147 PRO   A CD  1 1 
ATOM   1154 N N   . LEU   A 1 168 ? 125.062 15.346 -0.291  1    24.38 ?  148 LEU   A N   1 1 
ATOM   1155 C CA  . LEU   A 1 168 ? 126.482 15.632 -0.288  1    25.5  ?  148 LEU   A CA  1 1 
ATOM   1156 C C   . LEU   A 1 168 ? 127.088 15.004 0.988   1    26.47 ?  148 LEU   A C   1 1 
ATOM   1157 O O   . LEU   A 1 168 ? 126.928 15.534 2.116   1    27.41 ?  148 LEU   A O   1 1 
ATOM   1158 C CB  . LEU   A 1 168 ? 126.69  17.147 -0.307  1    27.16 ?  148 LEU   A CB  1 1 
ATOM   1159 C CG  . LEU   A 1 168 ? 128.143 17.609 -0.136  1    30.56 ?  148 LEU   A CG  1 1 
ATOM   1160 C CD1 . LEU   A 1 168 ? 129.026 17.017 -1.244  1    31.62 ?  148 LEU   A CD1 1 1 
ATOM   1161 C CD2 . LEU   A 1 168 ? 128.22  19.147 -0.147  1    32.7  ?  148 LEU   A CD2 1 1 
ATOM   1162 N N   . VAL   A 1 169 ? 127.748 13.865 0.789   1    28.09 ?  149 VAL   A N   1 1 
ATOM   1163 C CA  . VAL   A 1 169 ? 128.412 13.143 1.88    1    29.75 ?  149 VAL   A CA  1 1 
ATOM   1164 C C   . VAL   A 1 169 ? 129.894 13.103 1.571   1    33.26 ?  149 VAL   A C   1 1 
ATOM   1165 O O   . VAL   A 1 169 ? 130.718 13.375 2.429   1    34.08 ?  149 VAL   A O   1 1 
ATOM   1166 C CB  . VAL   A 1 169 ? 127.818 11.729 2.081   1    31    ?  149 VAL   A CB  1 1 
ATOM   1167 C CG1 . VAL   A 1 169 ? 128.633 10.985 3.139   1    32.27 ?  149 VAL   A CG1 1 1 
ATOM   1168 C CG2 . VAL   A 1 169 ? 126.367 11.858 2.523   1    31.78 ?  149 VAL   A CG2 1 1 
ATOM   1169 N N   . LEU   A 1 170 ? 130.236 12.719 0.337   1    35.26 ?  150 LEU   A N   1 1 
ATOM   1170 C CA  . LEU   A 1 170 ? 131.599 12.691 -0.154  1    37.67 ?  150 LEU   A CA  1 1 
ATOM   1171 C C   . LEU   A 1 170 ? 131.523 13.336 -1.546  1    40.08 ?  150 LEU   A C   1 1 
ATOM   1172 O O   . LEU   A 1 170 ? 130.709 12.909 -2.391  1    39.29 ?  150 LEU   A O   1 1 
ATOM   1173 C CB  . LEU   A 1 170 ? 132.097 11.248 -0.302  1    37.91 ?  150 LEU   A CB  1 1 
ATOM   1174 C CG  . LEU   A 1 170 ? 132.378 10.477 0.976   1    40.49 ?  150 LEU   A CG  1 1 
ATOM   1175 C CD1 . LEU   A 1 170 ? 132.837 9.09   0.637   1    41.31 ?  150 LEU   A CD1 1 1 
ATOM   1176 C CD2 . LEU   A 1 170 ? 133.469 11.133 1.791   1    41.56 ?  150 LEU   A CD2 1 1 
ATOM   1177 N N   . ALA   A 1 171 ? 132.339 14.36  -1.782  1    42.3  ?  151 ALA   A N   1 1 
ATOM   1178 C CA  . ALA   A 1 171 ? 132.391 14.982 -3.11   1    45.24 ?  151 ALA   A CA  1 1 
ATOM   1179 C C   . ALA   A 1 171 ? 133.137 14.037 -4.107  1    48.77 ?  151 ALA   A C   1 1 
ATOM   1180 O O   . ALA   A 1 171 ? 133.802 13.08  -3.695  1    48.38 ?  151 ALA   A O   1 1 
ATOM   1181 C CB  . ALA   A 1 171 ? 133.115 16.325 -3.016  1    45.3  ?  151 ALA   A CB  1 1 
ATOM   1182 N N   . ASN   A 1 172 ? 133.049 14.314 -5.427  1    51.82 ?  152 ASN   A N   1 1 
ATOM   1183 C CA  . ASN   A 1 172 ? 133.783 13.572 -6.452  1    55.67 ?  152 ASN   A CA  1 1 
ATOM   1184 C C   . ASN   A 1 172 ? 135.288 13.665 -6.128  1    58.8  ?  152 ASN   A C   1 1 
ATOM   1185 O O   . ASN   A 1 172 ? 135.793 14.768 -5.913  1    58.78 ?  152 ASN   A O   1 1 
ATOM   1186 C CB  . ASN   A 1 172 ? 133.518 14.196 -7.819  1    58.36 ?  152 ASN   A CB  1 1 
ATOM   1187 C CG  . ASN   A 1 172 ? 134.29  13.56  -8.952  1    64.41 ?  152 ASN   A CG  1 1 
ATOM   1188 O OD1 . ASN   A 1 172 ? 135.532 13.609 -9.009  1    66.39 ?  152 ASN   A OD1 1 1 
ATOM   1189 N ND2 . ASN   A 1 172 ? 133.567 12.956 -9.88   1    65.73 ?  152 ASN   A ND2 1 1 
ATOM   1190 N N   . PRO   A 1 173 ? 135.97  12.52  -6.006  1    60.97 ?  153 PRO   A N   1 1 
ATOM   1191 C CA  . PRO   A 1 173 ? 137.384 12.54  -5.602  1    62.8  ?  153 PRO   A CA  1 1 
ATOM   1192 C C   . PRO   A 1 173 ? 138.29  13.444 -6.425  1    65.46 ?  153 PRO   A C   1 1 
ATOM   1193 O O   . PRO   A 1 173 ? 139.095 14.173 -5.841  1    66.18 ?  153 PRO   A O   1 1 
ATOM   1194 C CB  . PRO   A 1 173 ? 137.802 11.071 -5.69   1    63.1  ?  153 PRO   A CB  1 1 
ATOM   1195 C CG  . PRO   A 1 173 ? 136.534 10.308 -5.51   1    63.14 ?  153 PRO   A CG  1 1 
ATOM   1196 C CD  . PRO   A 1 173 ? 135.47  11.144 -6.178  1    61.05 ?  153 PRO   A CD  1 1 
ATOM   1197 N N   . GLU   A 1 174 ? 138.146 13.429 -7.756  1    66.62 ?  154 GLU   A N   1 1 
ATOM   1198 C CA  . GLU   A 1 174 ? 138.969 14.264 -8.625  1    68.27 ?  154 GLU   A CA  1 1 
ATOM   1199 C C   . GLU   A 1 174 ? 138.683 15.762 -8.397  1    69    ?  154 GLU   A C   1 1 
ATOM   1200 O O   . GLU   A 1 174 ? 139.613 16.57  -8.367  1    69.49 ?  154 GLU   A O   1 1 
ATOM   1201 C CB  . GLU   A 1 174 ? 138.841 13.815 -10.111 1    71.46 ?  154 GLU   A CB  1 1 
ATOM   1202 C CG  . GLU   A 1 174 ? 138.285 14.821 -11.116 1    77.72 ?  154 GLU   A CG  1 1 
ATOM   1203 C CD  . GLU   A 1 174 ? 137.011 14.377 -11.812 1    86.04 ?  154 GLU   A CD  1 1 
ATOM   1204 O OE1 . GLU   A 1 174 ? 136.936 13.19  -12.207 1    87.7  ?  154 GLU   A OE1 1 1 
ATOM   1205 O OE2 . GLU   A 1 174 ? 136.082 15.207 -11.949 1    88.69 ?  154 GLU   A OE2 1 1 
ATOM   1206 N N   . SER   A 1 175 ? 137.411 16.119 -8.195  1    68.77 ?  155 SER   A N   1 1 
ATOM   1207 C CA  . SER   A 1 175 ? 137.034 17.507 -7.975  1    69.36 ?  155 SER   A CA  1 1 
ATOM   1208 C C   . SER   A 1 175 ? 137.446 18.017 -6.595  1    69.74 ?  155 SER   A C   1 1 
ATOM   1209 O O   . SER   A 1 175 ? 137.8   19.19  -6.458  1    70.12 ?  155 SER   A O   1 1 
ATOM   1210 C CB  . SER   A 1 175 ? 135.533 17.68  -8.156  1    70.86 ?  155 SER   A CB  1 1 
ATOM   1211 O OG  . SER   A 1 175 ? 135.135 17.265 -9.451  1    73.34 ?  155 SER   A OG  1 1 
ATOM   1212 N N   . ALA   A 1 176 ? 137.375 17.148 -5.572  1    69.31 ?  156 ALA   A N   1 1 
ATOM   1213 C CA  . ALA   A 1 176 ? 137.719 17.516 -4.2    1    69.49 ?  156 ALA   A CA  1 1 
ATOM   1214 C C   . ALA   A 1 176 ? 139.208 17.828 -4.05   1    69.3  ?  156 ALA   A C   1 1 
ATOM   1215 O O   . ALA   A 1 176 ? 139.551 18.836 -3.433  1    69.38 ?  156 ALA   A O   1 1 
ATOM   1216 C CB  . ALA   A 1 176 ? 137.31  16.407 -3.234  1    69.65 ?  156 ALA   A CB  1 1 
ATOM   1217 N N   . THR   A 1 177 ? 140.088 16.989 -4.629  1    68.67 ?  157 THR   A N   1 1 
ATOM   1218 C CA  . THR   A 1 177 ? 141.531 17.2   -4.532  1    68.73 ?  157 THR   A CA  1 1 
ATOM   1219 C C   . THR   A 1 177 ? 141.943 18.514 -5.186  1    68.37 ?  157 THR   A C   1 1 
ATOM   1220 O O   . THR   A 1 177 ? 142.754 19.249 -4.622  1    68.75 ?  157 THR   A O   1 1 
ATOM   1221 C CB  . THR   A 1 177 ? 142.291 15.996 -5.085  1    70.08 ?  157 THR   A CB  1 1 
ATOM   1222 O OG1 . THR   A 1 177 ? 141.858 14.822 -4.392  1    70.97 ?  157 THR   A OG1 1 1 
ATOM   1223 C CG2 . THR   A 1 177 ? 143.8   16.153 -4.956  1    70.67 ?  157 THR   A CG2 1 1 
ATOM   1224 N N   . THR   A 1 178 ? 141.345 18.835 -6.34   1    67.44 ?  158 THR   A N   1 1 
ATOM   1225 C CA  . THR   A 1 178 ? 141.632 20.074 -7.058  1    67.23 ?  158 THR   A CA  1 1 
ATOM   1226 C C   . THR   A 1 178 ? 141.189 21.285 -6.241  1    66.65 ?  158 THR   A C   1 1 
ATOM   1227 O O   . THR   A 1 178 ? 141.941 22.254 -6.103  1    66.46 ?  158 THR   A O   1 1 
ATOM   1228 C CB  . THR   A 1 178 ? 140.955 20.051 -8.434  1    68.51 ?  158 THR   A CB  1 1 
ATOM   1229 O OG1 . THR   A 1 178 ? 141.586 19.053 -9.228  1    69.89 ?  158 THR   A OG1 1 1 
ATOM   1230 C CG2 . THR   A 1 178 ? 141.007 21.402 -9.14   1    68.61 ?  158 THR   A CG2 1 1 
ATOM   1231 N N   . PHE   A 1 179 ? 139.974 21.217 -5.686  1    66.13 ?  159 PHE   A N   1 1 
ATOM   1232 C CA  . PHE   A 1 179 ? 139.453 22.313 -4.896  1    65.97 ?  159 PHE   A CA  1 1 
ATOM   1233 C C   . PHE   A 1 179 ? 140.251 22.51  -3.607  1    67.05 ?  159 PHE   A C   1 1 
ATOM   1234 O O   . PHE   A 1 179 ? 140.517 23.652 -3.256  1    67.08 ?  159 PHE   A O   1 1 
ATOM   1235 C CB  . PHE   A 1 179 ? 137.953 22.158 -4.611  1    64.73 ?  159 PHE   A CB  1 1 
ATOM   1236 C CG  . PHE   A 1 179 ? 137.443 23.361 -3.861  1    64.05 ?  159 PHE   A CG  1 1 
ATOM   1237 C CD1 . PHE   A 1 179 ? 137.212 24.556 -4.518  1    64.37 ?  159 PHE   A CD1 1 1 
ATOM   1238 C CD2 . PHE   A 1 179 ? 137.32  23.336 -2.483  1    64.01 ?  159 PHE   A CD2 1 1 
ATOM   1239 C CE1 . PHE   A 1 179 ? 136.811 25.68  -3.822  1    64.49 ?  159 PHE   A CE1 1 1 
ATOM   1240 C CE2 . PHE   A 1 179 ? 136.943 24.469 -1.788  1    64.32 ?  159 PHE   A CE2 1 1 
ATOM   1241 C CZ  . PHE   A 1 179 ? 136.692 25.631 -2.462  1    64.13 ?  159 PHE   A CZ  1 1 
ATOM   1242 N N   . LYS   A 1 180 ? 140.652 21.423 -2.923  1    67.77 ?  160 LYS   A N   1 1 
ATOM   1243 C CA  . LYS   A 1 180 ? 141.42  21.505 -1.674  1    69.14 ?  160 LYS   A CA  1 1 
ATOM   1244 C C   . LYS   A 1 180 ? 142.756 22.257 -1.827  1    70.12 ?  160 LYS   A C   1 1 
ATOM   1245 O O   . LYS   A 1 180 ? 143.242 22.855 -0.862  1    70.38 ?  160 LYS   A O   1 1 
ATOM   1246 C CB  . LYS   A 1 180 ? 141.618 20.118 -1.047  1    71.24 ?  160 LYS   A CB  1 1 
ATOM   1247 C CG  . LYS   A 1 180 ? 140.394 19.642 -0.27   1    74.9  ?  160 LYS   A CG  1 1 
ATOM   1248 C CD  . LYS   A 1 180 ? 140.512 18.198 0.173   1    79.2  ?  160 LYS   A CD  1 1 
ATOM   1249 C CE  . LYS   A 1 180 ? 139.267 17.738 0.896   1    82.85 ?  160 LYS   A CE  1 1 
ATOM   1250 N NZ  . LYS   A 1 180 ? 139.305 16.281 1.2     1    85.06 ?  160 LYS   A NZ  1 1 
ATOM   1251 N N   . VAL   A 1 181 ? 143.312 22.275 -3.047  1    70.32 ?  161 VAL   A N   1 1 
ATOM   1252 C CA  . VAL   A 1 181 ? 144.528 23.019 -3.349  1    70.74 ?  161 VAL   A CA  1 1 
ATOM   1253 C C   . VAL   A 1 181 ? 144.167 24.496 -3.455  1    70.46 ?  161 VAL   A C   1 1 
ATOM   1254 O O   . VAL   A 1 181 ? 144.818 25.336 -2.832  1    70.98 ?  161 VAL   A O   1 1 
ATOM   1255 C CB  . VAL   A 1 181 ? 145.195 22.503 -4.651  1    72.13 ?  161 VAL   A CB  1 1 
ATOM   1256 C CG1 . VAL   A 1 181 ? 146.307 23.447 -5.12   1    72.89 ?  161 VAL   A CG1 1 1 
ATOM   1257 C CG2 . VAL   A 1 181 ? 145.721 21.082 -4.468  1    72.55 ?  161 VAL   A CG2 1 1 
ATOM   1258 N N   . LEU   A 1 182 ? 143.106 24.813 -4.213  1    69.49 ?  162 LEU   A N   1 1 
ATOM   1259 C CA  . LEU   A 1 182 ? 142.614 26.179 -4.401  1    69.07 ?  162 LEU   A CA  1 1 
ATOM   1260 C C   . LEU   A 1 182 ? 142.168 26.808 -3.067  1    67.92 ?  162 LEU   A C   1 1 
ATOM   1261 O O   . LEU   A 1 182 ? 142.351 28.01  -2.855  1    67.98 ?  162 LEU   A O   1 1 
ATOM   1262 C CB  . LEU   A 1 182 ? 141.448 26.153 -5.391  1    69.49 ?  162 LEU   A CB  1 1 
ATOM   1263 C CG  . LEU   A 1 182 ? 141.015 27.478 -5.966  1    71.18 ?  162 LEU   A CG  1 1 
ATOM   1264 C CD1 . LEU   A 1 182 ? 142.135 28.113 -6.761  1    71.83 ?  162 LEU   A CD1 1 1 
ATOM   1265 C CD2 . LEU   A 1 182 ? 139.792 27.294 -6.85   1    72.1  ?  162 LEU   A CD2 1 1 
ATOM   1266 N N   . ALA   A 1 183 ? 141.599 25.983 -2.174  1    66.5  ?  163 ALA   A N   1 1 
ATOM   1267 C CA  . ALA   A 1 183 ? 141.151 26.372 -0.845  1    66.08 ?  163 ALA   A CA  1 1 
ATOM   1268 C C   . ALA   A 1 183 ? 142.342 26.767 0.027   1    65.65 ?  163 ALA   A C   1 1 
ATOM   1269 O O   . ALA   A 1 183 ? 142.225 27.681 0.826   1    65.38 ?  163 ALA   A O   1 1 
ATOM   1270 C CB  . ALA   A 1 183 ? 140.387 25.231 -0.192  1    66.16 ?  163 ALA   A CB  1 1 
ATOM   1271 N N   . ALA   A 1 184 ? 143.488 26.11  -0.141  1    65.28 ?  164 ALA   A N   1 1 
ATOM   1272 C CA  . ALA   A 1 184 ? 144.696 26.446 0.607   1    65.36 ?  164 ALA   A CA  1 1 
ATOM   1273 C C   . ALA   A 1 184 ? 145.219 27.836 0.233   1    64.79 ?  164 ALA   A C   1 1 
ATOM   1274 O O   . ALA   A 1 184 ? 145.684 28.57  1.101   1    65.33 ?  164 ALA   A O   1 1 
ATOM   1275 C CB  . ALA   A 1 184 ? 145.753 25.399 0.364   1    65.7  ?  164 ALA   A CB  1 1 
ATOM   1276 N N   . LYS   A 1 185 ? 145.07  28.225 -1.035  1    63.3  ?  165 LYS   A N   1 1 
ATOM   1277 C CA  . LYS   A 1 185 ? 145.456 29.537 -1.515  1    62.37 ?  165 LYS   A CA  1 1 
ATOM   1278 C C   . LYS   A 1 185 ? 144.606 30.618 -0.792  1    60.15 ?  165 LYS   A C   1 1 
ATOM   1279 O O   . LYS   A 1 185 ? 145.159 31.577 -0.249  1    60.02 ?  165 LYS   A O   1 1 
ATOM   1280 C CB  . LYS   A 1 185 ? 145.251 29.586 -3.039  1    65.08 ?  165 LYS   A CB  1 1 
ATOM   1281 C CG  . LYS   A 1 185 ? 146.089 30.622 -3.785  1    70.83 ?  165 LYS   A CG  1 1 
ATOM   1282 C CD  . LYS   A 1 185 ? 145.772 30.61  -5.293  1    76.42 ?  165 LYS   A CD  1 1 
ATOM   1283 C CE  . LYS   A 1 185 ? 145.965 29.25  -5.945  1    80.94 ?  165 LYS   A CE  1 1 
ATOM   1284 N NZ  . LYS   A 1 185 ? 145.564 29.256 -7.382  1    83.52 ?  165 LYS   A NZ  1 1 
ATOM   1285 N N   . VAL   A 1 186 ? 143.277 30.43  -0.734  1    58.07 ?  166 VAL   A N   1 1 
ATOM   1286 C CA  . VAL   A 1 186 ? 142.401 31.386 -0.07   1    56.9  ?  166 VAL   A CA  1 1 
ATOM   1287 C C   . VAL   A 1 186 ? 142.597 31.363 1.452   1    55.16 ?  166 VAL   A C   1 1 
ATOM   1288 O O   . VAL   A 1 186 ? 142.578 32.425 2.07    1    55.16 ?  166 VAL   A O   1 1 
ATOM   1289 C CB  . VAL   A 1 186 ? 140.923 31.205 -0.52   1    57.72 ?  166 VAL   A CB  1 1 
ATOM   1290 C CG1 . VAL   A 1 186 ? 139.914 31.653 0.541   1    58.3  ?  166 VAL   A CG1 1 1 
ATOM   1291 C CG2 . VAL   A 1 186 ? 140.681 31.934 -1.838  1    58.41 ?  166 VAL   A CG2 1 1 
ATOM   1292 N N   . LEU   A 1 187 ? 142.809 30.185 2.05    1    53.47 ?  167 LEU   A N   1 1 
ATOM   1293 C CA  . LEU   A 1 187 ? 143.026 30.087 3.492   1    52.96 ?  167 LEU   A CA  1 1 
ATOM   1294 C C   . LEU   A 1 187 ? 144.339 30.733 3.952   1    52.7  ?  167 LEU   A C   1 1 
ATOM   1295 O O   . LEU   A 1 187 ? 144.387 31.295 5.043   1    53.94 ?  167 LEU   A O   1 1 
ATOM   1296 C CB  . LEU   A 1 187 ? 142.938 28.635 3.981   1    53.2  ?  167 LEU   A CB  1 1 
ATOM   1297 C CG  . LEU   A 1 187 ? 141.546 28.015 3.896   1    55.22 ?  167 LEU   A CG  1 1 
ATOM   1298 C CD1 . LEU   A 1 187 ? 141.598 26.536 4.173   1    55.76 ?  167 LEU   A CD1 1 1 
ATOM   1299 C CD2 . LEU   A 1 187 ? 140.555 28.74  4.79    1    56.05 ?  167 LEU   A CD2 1 1 
ATOM   1300 N N   . ASN   A 1 188 ? 145.386 30.7   3.117   1    50.59 ?  168 ASN   A N   1 1 
ATOM   1301 C CA  . ASN   A 1 188 ? 146.673 31.292 3.476   1    49.03 ?  168 ASN   A CA  1 1 
ATOM   1302 C C   . ASN   A 1 188 ? 146.847 32.731 3.083   1    48.2  ?  168 ASN   A C   1 1 
ATOM   1303 O O   . ASN   A 1 188 ? 147.739 33.399 3.622   1    48.71 ?  168 ASN   A O   1 1 
ATOM   1304 C CB  . ASN   A 1 188 ? 147.796 30.522 2.818   1    49.5  ?  168 ASN   A CB  1 1 
ATOM   1305 C CG  . ASN   A 1 188 ? 148.19  29.293 3.573   1    51.44 ?  168 ASN   A CG  1 1 
ATOM   1306 O OD1 . ASN   A 1 188 ? 149.066 29.336 4.446   1    52.68 ?  168 ASN   A OD1 1 1 
ATOM   1307 N ND2 . ASN   A 1 188 ? 147.573 28.178 3.226   1    51.48 ?  168 ASN   A ND2 1 1 
ATOM   1308 N N   . SER   A 1 189 ? 146.055 33.216 2.137   1    47.05 ?  169 SER   A N   1 1 
ATOM   1309 C CA  A SER   A 1 189 ? 146.237 34.593 1.691   0.6  46.88 ?  169 SER   A CA  1 1 
ATOM   1310 C CA  B SER   A 1 189 ? 146.201 34.588 1.656   0.4  47.01 ?  169 SER   A CA  1 1 
ATOM   1311 C C   . SER   A 1 189 ? 144.901 35.385 1.71    1    47.37 ?  169 SER   A C   1 1 
ATOM   1312 O O   . SER   A 1 189 ? 143.873 34.854 2.152   1    48.79 ?  169 SER   A O   1 1 
ATOM   1313 C CB  A SER   A 1 189 ? 146.997 34.607 0.357   0.6  46.84 ?  169 SER   A CB  1 1 
ATOM   1314 C CB  B SER   A 1 189 ? 146.836 34.613 0.262   0.4  47.42 ?  169 SER   A CB  1 1 
ATOM   1315 O OG  A SER   A 1 189 ? 148.411 34.48  0.554   0.6  44.3  ?  169 SER   A OG  1 1 
ATOM   1316 O OG  B SER   A 1 189 ? 146.578 33.483 -0.55   0.4  46.87 ?  169 SER   A OG  1 1 
ATOM   1317 N N   . VAL   A 1 190 ? 144.929 36.684 1.336   1    46.47 ?  170 VAL   A N   1 1 
ATOM   1318 C CA  . VAL   A 1 190 ? 143.702 37.471 1.342   1    46.35 ?  170 VAL   A CA  1 1 
ATOM   1319 C C   . VAL   A 1 190 ? 143.292 37.533 -0.101  1    46.76 ?  170 VAL   A C   1 1 
ATOM   1320 O O   . VAL   A 1 190 ? 143.877 38.286 -0.855  1    46.5  ?  170 VAL   A O   1 1 
ATOM   1321 C CB  . VAL   A 1 190 ? 143.878 38.874 1.974   1    46.72 ?  170 VAL   A CB  1 1 
ATOM   1322 C CG1 . VAL   A 1 190 ? 142.561 39.639 1.97    1    46.4  ?  170 VAL   A CG1 1 1 
ATOM   1323 C CG2 . VAL   A 1 190 ? 144.437 38.758 3.388   1    47.64 ?  170 VAL   A CG2 1 1 
ATOM   1324 N N   . LEU   A 1 191 ? 142.364 36.684 -0.525  1    47.27 ?  171 LEU   A N   1 1 
ATOM   1325 C CA  . LEU   A 1 191 ? 141.917 36.65  -1.921  1    48.47 ?  171 LEU   A CA  1 1 
ATOM   1326 C C   . LEU   A 1 191 ? 140.39  36.535 -1.924  1    51.44 ?  171 LEU   A C   1 1 
ATOM   1327 O O   . LEU   A 1 191 ? 139.845 35.452 -2.128  1    51.07 ?  171 LEU   A O   1 1 
ATOM   1328 C CB  . LEU   A 1 191 ? 142.565 35.459 -2.652  1    47.31 ?  171 LEU   A CB  1 1 
ATOM   1329 C CG  . LEU   A 1 191 ? 144.086 35.595 -2.882  1    48.05 ?  171 LEU   A CG  1 1 
ATOM   1330 C CD1 . LEU   A 1 191 ? 144.7   34.266 -3.355  1    48.62 ?  171 LEU   A CD1 1 1 
ATOM   1331 C CD2 . LEU   A 1 191 ? 144.383 36.696 -3.885  1    48.37 ?  171 LEU   A CD2 1 1 
ATOM   1332 N N   . PRO   A 1 192 ? 139.695 37.665 -1.678  1    53.84 ?  172 PRO   A N   1 1 
ATOM   1333 C CA  . PRO   A 1 192 ? 138.226 37.618 -1.541  1    55.86 ?  172 PRO   A CA  1 1 
ATOM   1334 C C   . PRO   A 1 192 ? 137.383 37.226 -2.763  1    58.55 ?  172 PRO   A C   1 1 
ATOM   1335 O O   . PRO   A 1 192 ? 136.298 36.659 -2.58   1    58.98 ?  172 PRO   A O   1 1 
ATOM   1336 C CB  . PRO   A 1 192 ? 137.868 39.045 -1.098  1    55.75 ?  172 PRO   A CB  1 1 
ATOM   1337 C CG  . PRO   A 1 192 ? 139.019 39.879 -1.53   1    55.92 ?  172 PRO   A CG  1 1 
ATOM   1338 C CD  . PRO   A 1 192 ? 140.222 39.01  -1.375  1    53.49 ?  172 PRO   A CD  1 1 
ATOM   1339 N N   . ASN   A 1 193 ? 137.829 37.555 -3.984  1    59.91 ?  173 ASN   A N   1 1 
ATOM   1340 C CA  . ASN   A 1 193 ? 136.998 37.298 -5.164  1    61.79 ?  173 ASN   A CA  1 1 
ATOM   1341 C C   . ASN   A 1 193 ? 137.199 35.933 -5.824  1    62.18 ?  173 ASN   A C   1 1 
ATOM   1342 O O   . ASN   A 1 193 ? 136.464 35.61  -6.757  1    62.81 ?  173 ASN   A O   1 1 
ATOM   1343 C CB  . ASN   A 1 193 ? 137.174 38.414 -6.184  1    64.23 ?  173 ASN   A CB  1 1 
ATOM   1344 C CG  . ASN   A 1 193 ? 136.776 39.776 -5.64   1    69.83 ?  173 ASN   A CG  1 1 
ATOM   1345 O OD1 . ASN   A 1 193 ? 135.849 39.901 -4.814  1    71.75 ?  173 ASN   A OD1 1 1 
ATOM   1346 N ND2 . ASN   A 1 193 ? 137.474 40.828 -6.083  1    70.23 ?  173 ASN   A ND2 1 1 
ATOM   1347 N N   . LEU   A 1 194 ? 138.156 35.127 -5.34   1    61.52 ?  174 LEU   A N   1 1 
ATOM   1348 C CA  . LEU   A 1 194 ? 138.462 33.85  -5.962  1    61.57 ?  174 LEU   A CA  1 1 
ATOM   1349 C C   . LEU   A 1 194 ? 137.249 32.927 -6.12   1    61.58 ?  174 LEU   A C   1 1 
ATOM   1350 O O   . LEU   A 1 194 ? 136.463 32.749 -5.194  1    61.26 ?  174 LEU   A O   1 1 
ATOM   1351 C CB  . LEU   A 1 194 ? 139.608 33.138 -5.24   1    61.91 ?  174 LEU   A CB  1 1 
ATOM   1352 C CG  . LEU   A 1 194 ? 140.691 32.567 -6.152  1    63.99 ?  174 LEU   A CG  1 1 
ATOM   1353 C CD1 . LEU   A 1 194 ? 141.564 33.666 -6.709  1    64.86 ?  174 LEU   A CD1 1 1 
ATOM   1354 C CD2 . LEU   A 1 194 ? 141.534 31.529 -5.432  1    64.73 ?  174 LEU   A CD2 1 1 
ATOM   1355 N N   . SER   A 1 195 ? 137.075 32.411 -7.34   1    61.78 ?  175 SER   A N   1 1 
ATOM   1356 C CA  . SER   A 1 195 ? 136.017 31.484 -7.72   1    61.97 ?  175 SER   A CA  1 1 
ATOM   1357 C C   . SER   A 1 195 ? 136.609 30.37  -8.565  1    61.6  ?  175 SER   A C   1 1 
ATOM   1358 O O   . SER   A 1 195 ? 137.513 30.599 -9.367  1    62.27 ?  175 SER   A O   1 1 
ATOM   1359 C CB  . SER   A 1 195 ? 134.961 32.177 -8.577  1    63.63 ?  175 SER   A CB  1 1 
ATOM   1360 O OG  . SER   A 1 195 ? 134.379 33.316 -7.964  1    67.05 ?  175 SER   A OG  1 1 
ATOM   1361 N N   . SER   A 1 196 ? 136.056 29.18  -8.437  1    60.68 ?  176 SER   A N   1 1 
ATOM   1362 C CA  . SER   A 1 196 ? 136.411 28.061 -9.3    1    60.19 ?  176 SER   A CA  1 1 
ATOM   1363 C C   . SER   A 1 196 ? 135.402 28.086 -10.501 1    58.33 ?  176 SER   A C   1 1 
ATOM   1364 O O   . SER   A 1 196 ? 134.669 29.072 -10.686 1    57.7  ?  176 SER   A O   1 1 
ATOM   1365 C CB  . SER   A 1 196 ? 136.35  26.75  -8.515  1    62.13 ?  176 SER   A CB  1 1 
ATOM   1366 O OG  . SER   A 1 196 ? 135.083 26.59  -7.9    1    65.7  ?  176 SER   A OG  1 1 
ATOM   1367 N N   . GLY   A 1 197 ? 135.399 27.046 -11.326 1    57.2  ?  177 GLY   A N   1 1 
ATOM   1368 C CA  . GLY   A 1 197 ? 134.474 26.973 -12.45  1    56.68 ?  177 GLY   A CA  1 1 
ATOM   1369 C C   . GLY   A 1 197 ? 133.063 26.637 -11.999 1    55.57 ?  177 GLY   A C   1 1 
ATOM   1370 O O   . GLY   A 1 197 ? 132.842 26.188 -10.869 1    55.63 ?  177 GLY   A O   1 1 
ATOM   1371 N N   A PRO   A 1 198 ? 132.071 26.874 -12.866 0.5  55.14 ?  178 PRO   A N   1 1 
ATOM   1372 N N   B PRO   A 1 198 ? 132.071 26.874 -12.866 0.5  55.14 ?  178 PRO   A N   1 1 
ATOM   1373 C CA  A PRO   A 1 198 ? 130.682 26.558 -12.487 0.5  55.18 ?  178 PRO   A CA  1 1 
ATOM   1374 C CA  B PRO   A 1 198 ? 130.682 26.558 -12.487 0.5  55.18 ?  178 PRO   A CA  1 1 
ATOM   1375 C C   A PRO   A 1 198 ? 130.39  25.052 -12.449 0.5  55.58 ?  178 PRO   A C   1 1 
ATOM   1376 C C   B PRO   A 1 198 ? 130.39  25.052 -12.449 0.5  55.58 ?  178 PRO   A C   1 1 
ATOM   1377 O O   A PRO   A 1 198 ? 131.11  24.27  -13.066 0.5  55.76 ?  178 PRO   A O   1 1 
ATOM   1378 O O   B PRO   A 1 198 ? 131.11  24.27  -13.066 0.5  55.76 ?  178 PRO   A O   1 1 
ATOM   1379 C CB  A PRO   A 1 198 ? 129.859 27.247 -13.576 0.5  55.7  ?  178 PRO   A CB  1 1 
ATOM   1380 C CB  B PRO   A 1 198 ? 129.859 27.247 -13.576 0.5  55.7  ?  178 PRO   A CB  1 1 
ATOM   1381 C CG  A PRO   A 1 198 ? 130.764 27.308 -14.753 0.5  56.17 ?  178 PRO   A CG  1 1 
ATOM   1382 C CG  B PRO   A 1 198 ? 130.764 27.308 -14.753 0.5  56.17 ?  178 PRO   A CG  1 1 
ATOM   1383 C CD  A PRO   A 1 198 ? 132.162 27.443 -14.224 0.5  54.58 ?  178 PRO   A CD  1 1 
ATOM   1384 C CD  B PRO   A 1 198 ? 132.162 27.443 -14.224 0.5  54.58 ?  178 PRO   A CD  1 1 
ATOM   1385 N N   . ILE   A 1 199 ? 129.321 24.642 -11.741 1    55.35 ?  179 ILE   A N   1 1 
ATOM   1386 C CA  . ILE   A 1 199 ? 128.92  23.21  -11.678 1    55.15 ?  179 ILE   A CA  1 1 
ATOM   1387 C C   . ILE   A 1 199 ? 128.46  22.836 -13.111 1    54.41 ?  179 ILE   A C   1 1 
ATOM   1388 O O   . ILE   A 1 199 ? 127.577 23.525 -13.628 1    54.81 ?  179 ILE   A O   1 1 
ATOM   1389 C CB  . ILE   A 1 199 ? 127.764 23.04  -10.645 1    55.51 ?  179 ILE   A CB  1 1 
ATOM   1390 C CG1 . ILE   A 1 199 ? 128.25  23.253 -9.197  1    55.98 ?  179 ILE   A CG1 1 1 
ATOM   1391 C CG2 . ILE   A 1 199 ? 127.052 21.687 -10.806 1    56.12 ?  179 ILE   A CG2 1 1 
ATOM   1392 C CD1 . ILE   A 1 199 ? 127.148 23.654 -8.215  1    57.01 ?  179 ILE   A CD1 1 1 
ATOM   1393 N N   . ASP   A 1 200 ? 129.177 21.904 -13.814 1    53.01 ?  180 ASP   A N   1 1 
ATOM   1394 C CA  . ASP   A 1 200 ? 128.883 21.557 -15.228 1    51.21 ?  180 ASP   A CA  1 1 
ATOM   1395 C C   . ASP   A 1 200 ? 127.452 21.004 -15.394 1    46.26 ?  180 ASP   A C   1 1 
ATOM   1396 O O   . ASP   A 1 200 ? 127.137 19.961 -14.833 1    46.28 ?  180 ASP   A O   1 1 
ATOM   1397 C CB  . ASP   A 1 200 ? 129.926 20.583 -15.797 1    56.07 ?  180 ASP   A CB  1 1 
ATOM   1398 C CG  . ASP   A 1 200 ? 129.803 20.342 -17.291 1    65.56 ?  180 ASP   A CG  1 1 
ATOM   1399 O OD1 . ASP   A 1 200 ? 129.153 21.16  -17.976 1    67.71 ?  180 ASP   A OD1 1 1 
ATOM   1400 O OD2 . ASP   A 1 200 ? 130.363 19.341 -17.778 1    70.39 ?  180 ASP   A OD2 1 1 
ATOM   1401 N N   . SER   A 1 201 ? 126.604 21.693 -16.177 1    40.86 ?  181 SER   A N   1 1 
ATOM   1402 C CA  A SER   A 1 201 ? 125.2   21.31  -16.285 0.5  38.1  ?  181 SER   A CA  1 1 
ATOM   1403 C CA  B SER   A 1 201 ? 125.199 21.338 -16.351 0.5  39.1  ?  181 SER   A CA  1 1 
ATOM   1404 C C   . SER   A 1 201 ? 124.95  19.981 -16.972 1    36.38 ?  181 SER   A C   1 1 
ATOM   1405 O O   . SER   A 1 201 ? 123.968 19.332 -16.619 1    33.67 ?  181 SER   A O   1 1 
ATOM   1406 C CB  A SER   A 1 201 ? 124.359 22.406 -16.929 0.5  37.04 ?  181 SER   A CB  1 1 
ATOM   1407 C CB  B SER   A 1 201 ? 124.464 22.412 -17.143 0.5  40.89 ?  181 SER   A CB  1 1 
ATOM   1408 O OG  A SER   A 1 201 ? 124.764 22.649 -18.263 0.5  35.84 ?  181 SER   A OG  1 1 
ATOM   1409 O OG  B SER   A 1 201 ? 124.441 23.619 -16.401 0.5  44.27 ?  181 SER   A OG  1 1 
ATOM   1410 N N   . SER   A 1 202 ? 125.813 19.558 -17.912 1    35.72 ?  182 SER   A N   1 1 
ATOM   1411 C CA  . SER   A 1 202 ? 125.594 18.264 -18.58  1    36.66 ?  182 SER   A CA  1 1 
ATOM   1412 C C   . SER   A 1 202 ? 125.687 17.081 -17.61  1    34.63 ?  182 SER   A C   1 1 
ATOM   1413 O O   . SER   A 1 202 ? 125.091 16.026 -17.886 1    35.66 ?  182 SER   A O   1 1 
ATOM   1414 C CB  . SER   A 1 202 ? 126.538 18.054 -19.771 1    41.54 ?  182 SER   A CB  1 1 
ATOM   1415 O OG  . SER   A 1 202 ? 127.902 18.005 -19.373 1    45.97 ?  182 SER   A OG  1 1 
ATOM   1416 N N   . VAL   A 1 203 ? 126.462 17.211 -16.505 1    32.37 ?  183 VAL   A N   1 1 
ATOM   1417 C CA  . VAL   A 1 203 ? 126.569 16.08  -15.533 1    31.75 ?  183 VAL   A CA  1 1 
ATOM   1418 C C   . VAL   A 1 203 ? 125.425 16.022 -14.517 1    28.8  ?  183 VAL   A C   1 1 
ATOM   1419 O O   . VAL   A 1 203 ? 125.386 15.101 -13.687 1    27.94 ?  183 VAL   A O   1 1 
ATOM   1420 C CB  . VAL   A 1 203 ? 127.932 16.027 -14.786 1    35.28 ?  183 VAL   A CB  1 1 
ATOM   1421 C CG1 . VAL   A 1 203 ? 129.085 16.217 -15.754 1    37.14 ?  183 VAL   A CG1 1 1 
ATOM   1422 C CG2 . VAL   A 1 203 ? 127.993 17.071 -13.67  1    37.11 ?  183 VAL   A CG2 1 1 
ATOM   1423 N N   . LEU   A 1 204 ? 124.488 16.977 -14.585 1    26.73 ?  184 LEU   A N   1 1 
ATOM   1424 C CA  . LEU   A 1 204 ? 123.386 16.988 -13.635 1    25.21 ?  184 LEU   A CA  1 1 
ATOM   1425 C C   . LEU   A 1 204 ? 122.339 15.933 -13.902 1    25.11 ?  184 LEU   A C   1 1 
ATOM   1426 O O   . LEU   A 1 204 ? 121.77  15.381 -12.971 1    24.31 ?  184 LEU   A O   1 1 
ATOM   1427 C CB  . LEU   A 1 204 ? 122.734 18.369 -13.612 1    24.21 ?  184 LEU   A CB  1 1 
ATOM   1428 C CG  . LEU   A 1 204 ? 123.665 19.481 -13.067 1    24.63 ?  184 LEU   A CG  1 1 
ATOM   1429 C CD1 . LEU   A 1 204 ? 123.027 20.871 -13.317 1    24.48 ?  184 LEU   A CD1 1 1 
ATOM   1430 C CD2 . LEU   A 1 204 ? 123.876 19.289 -11.567 1    25.84 ?  184 LEU   A CD2 1 1 
ATOM   1431 N N   . SER   A 1 205 ? 122.04  15.667 -15.18  1    23.81 ?  185 SER   A N   1 1 
ATOM   1432 C CA  . SER   A 1 205 ? 120.984 14.758 -15.533 1    23.13 ?  185 SER   A CA  1 1 
ATOM   1433 C C   . SER   A 1 205 ? 121.18  14.315 -16.969 1    24.34 ?  185 SER   A C   1 1 
ATOM   1434 O O   . SER   A 1 205 ? 121.619 15.094 -17.812 1    26.21 ?  185 SER   A O   1 1 
ATOM   1435 C CB  . SER   A 1 205 ? 119.661 15.488 -15.446 1    23.93 ?  185 SER   A CB  1 1 
ATOM   1436 O OG  . SER   A 1 205 ? 118.563 14.707 -15.867 1    25.76 ?  185 SER   A OG  1 1 
ATOM   1437 N N   . ARG   A 1 206 ? 120.781 13.099 -17.25  1    25.08 ?  186 ARG   A N   1 1 
ATOM   1438 C CA  . ARG   A 1 206 ? 120.786 12.594 -18.625 1    25.25 ?  186 ARG   A CA  1 1 
ATOM   1439 C C   . ARG   A 1 206 ? 119.573 13.172 -19.388 1    26.57 ?  186 ARG   A C   1 1 
ATOM   1440 O O   . ARG   A 1 206 ? 119.541 13.026 -20.634 1    27.42 ?  186 ARG   A O   1 1 
ATOM   1441 C CB  . ARG   A 1 206 ? 120.694 11.058 -18.625 1    26.46 ?  186 ARG   A CB  1 1 
ATOM   1442 C CG  . ARG   A 1 206 ? 121.976 10.426 -18.121 1    27.79 ?  186 ARG   A CG  1 1 
ATOM   1443 C CD  . ARG   A 1 206 ? 121.832 8.906  -18.013 1    28.22 ?  186 ARG   A CD  1 1 
ATOM   1444 N NE  . ARG   A 1 206 ? 120.753 8.576  -17.087 1    28.97 ?  186 ARG   A NE  1 1 
ATOM   1445 C CZ  . ARG   A 1 206 ? 120.291 7.355  -16.839 1    27.98 ?  186 ARG   A CZ  1 1 
ATOM   1446 N NH1 . ARG   A 1 206 ? 120.776 6.298  -17.507 1    29    ?  186 ARG   A NH1 1 1 
ATOM   1447 N NH2 . ARG   A 1 206 ? 119.28  7.186  -16.013 1    28.25 ?  186 ARG   A NH2 1 1 
ATOM   1448 N N   . ASN   A 1 207 ? 118.565 13.764 -18.681 1    24.77 ?  187 ASN   A N   1 1 
ATOM   1449 C CA  . ASN   A 1 207 ? 117.39  14.316 -19.334 1    24.74 ?  187 ASN   A CA  1 1 
ATOM   1450 C C   . ASN   A 1 207 ? 117.781 15.714 -19.856 1    25.4  ?  187 ASN   A C   1 1 
ATOM   1451 O O   . ASN   A 1 207 ? 117.857 16.698 -19.085 1    25    ?  187 ASN   A O   1 1 
ATOM   1452 C CB  . ASN   A 1 207 ? 116.233 14.361 -18.345 1    24.62 ?  187 ASN   A CB  1 1 
ATOM   1453 C CG  . ASN   A 1 207 ? 114.929 14.776 -18.949 1    28.73 ?  187 ASN   A CG  1 1 
ATOM   1454 O OD1 . ASN   A 1 207 ? 114.86  15.641 -19.853 1    29.05 ?  187 ASN   A OD1 1 1 
ATOM   1455 N ND2 . ASN   A 1 207 ? 113.867 14.222 -18.419 1    27.79 ?  187 ASN   A ND2 1 1 
ATOM   1456 N N   . LYS   A 1 208 ? 117.978 15.812 -21.164 1    26.83 ?  188 LYS   A N   1 1 
ATOM   1457 C CA  . LYS   A 1 208 ? 118.376 17.084 -21.767 1    26.79 ?  188 LYS   A CA  1 1 
ATOM   1458 C C   . LYS   A 1 208 ? 117.348 18.207 -21.578 1    26.8  ?  188 LYS   A C   1 1 
ATOM   1459 O O   . LYS   A 1 208 ? 117.719 19.375 -21.507 1    28.02 ?  188 LYS   A O   1 1 
ATOM   1460 C CB  . LYS   A 1 208 ? 118.737 16.897 -23.257 1    29.26 ?  188 LYS   A CB  1 1 
ATOM   1461 C CG  . LYS   A 1 208 ? 119.914 15.955 -23.479 1    35.27 ?  188 LYS   A CG  1 1 
ATOM   1462 C CD  . LYS   A 1 208 ? 120.158 15.8   -24.968 1    43.33 ?  188 LYS   A CD  1 1 
ATOM   1463 C CE  . LYS   A 1 208 ? 121.385 14.975 -25.284 1    49.94 ?  188 LYS   A CE  1 1 
ATOM   1464 N NZ  . LYS   A 1 208 ? 121.673 15.003 -26.746 1    54.17 ?  188 LYS   A NZ  1 1 
ATOM   1465 N N   . THR   A 1 209 ? 116.042 17.853 -21.563 1    26.59 ?  189 THR   A N   1 1 
ATOM   1466 C CA  . THR   A 1 209 ? 115.008 18.883 -21.394 1    26.57 ?  189 THR   A CA  1 1 
ATOM   1467 C C   . THR   A 1 209 ? 115.147 19.498 -19.975 1    25.05 ?  189 THR   A C   1 1 
ATOM   1468 O O   . THR   A 1 209 ? 115.106 20.729 -19.813 1    25.54 ?  189 THR   A O   1 1 
ATOM   1469 C CB  . THR   A 1 209 ? 113.61  18.271 -21.518 1    31.37 ?  189 THR   A CB  1 1 
ATOM   1470 O OG1 . THR   A 1 209 ? 113.548 17.586 -22.77  1    37.86 ?  189 THR   A OG1 1 1 
ATOM   1471 C CG2 . THR   A 1 209 ? 112.52  19.329 -21.45  1    32.39 ?  189 THR   A CG2 1 1 
ATOM   1472 N N   . GLU   A 1 210 ? 115.415 18.612 -18.965 1    24.32 ?  190 GLU   A N   1 1 
ATOM   1473 C CA  . GLU   A 1 210 ? 115.602 19.145 -17.622 1    23.48 ?  190 GLU   A CA  1 1 
ATOM   1474 C C   . GLU   A 1 210 ? 116.844 20.015 -17.54  1    22.65 ?  190 GLU   A C   1 1 
ATOM   1475 O O   . GLU   A 1 210 ? 116.801 21.038 -16.87  1    23.4  ?  190 GLU   A O   1 1 
ATOM   1476 C CB  . GLU   A 1 210 ? 115.68  18.01  -16.574 1    24.8  ?  190 GLU   A CB  1 1 
ATOM   1477 C CG  . GLU   A 1 210 ? 114.377 17.25  -16.534 1    27.84 ?  190 GLU   A CG  1 1 
ATOM   1478 C CD  . GLU   A 1 210 ? 113.267 17.86  -15.697 1    35.94 ?  190 GLU   A CD  1 1 
ATOM   1479 O OE1 . GLU   A 1 210 ? 113.329 19.072 -15.368 1    32.26 ?  190 GLU   A OE1 1 1 
ATOM   1480 O OE2 . GLU   A 1 210 ? 112.382 17.076 -15.267 1    41.27 ?  190 GLU   A OE2 1 1 
ATOM   1481 N N   . VAL   A 1 211 ? 117.926 19.635 -18.208 1    24.16 ?  191 VAL   A N   1 1 
ATOM   1482 C CA  . VAL   A 1 211 ? 119.134 20.473 -18.199 1    25.12 ?  191 VAL   A CA  1 1 
ATOM   1483 C C   . VAL   A 1 211 ? 118.839 21.84  -18.861 1    24.95 ?  191 VAL   A C   1 1 
ATOM   1484 O O   . VAL   A 1 211 ? 119.226 22.887 -18.356 1    25.4  ?  191 VAL   A O   1 1 
ATOM   1485 C CB  . VAL   A 1 211 ? 120.318 19.767 -18.859 1    27.36 ?  191 VAL   A CB  1 1 
ATOM   1486 C CG1 . VAL   A 1 211 ? 121.509 20.703 -18.926 1    28.6  ?  191 VAL   A CG1 1 1 
ATOM   1487 C CG2 . VAL   A 1 211 ? 120.697 18.49  -18.065 1    28.11 ?  191 VAL   A CG2 1 1 
ATOM   1488 N N   . ASP   A 1 212 ? 118.096 21.792 -19.964 1    25.56 ?  192 ASP   A N   1 1 
ATOM   1489 C CA  . ASP   A 1 212 ? 117.712 23.06  -20.655 1    26.13 ?  192 ASP   A CA  1 1 
ATOM   1490 C C   . ASP   A 1 212 ? 116.852 23.981 -19.769 1    26.45 ?  192 ASP   A C   1 1 
ATOM   1491 O O   . ASP   A 1 212 ? 117.062 25.201 -19.702 1    26.91 ?  192 ASP   A O   1 1 
ATOM   1492 C CB  . ASP   A 1 212 ? 116.982 22.718 -21.948 1    27.52 ?  192 ASP   A CB  1 1 
ATOM   1493 C CG  . ASP   A 1 212 ? 117.926 22.25  -23.04  1    33.7  ?  192 ASP   A CG  1 1 
ATOM   1494 O OD1 . ASP   A 1 212 ? 119.128 22.642 -23.002 1    38.71 ?  192 ASP   A OD1 1 1 
ATOM   1495 O OD2 . ASP   A 1 212 ? 117.463 21.526 -23.958 1    31.77 ?  192 ASP   A OD2 1 1 
ATOM   1496 N N   . ILE   A 1 213 ? 115.937 23.377 -19.011 1    25.64 ?  193 ILE   A N   1 1 
ATOM   1497 C CA  . ILE   A 1 213 ? 115.105 24.135 -18.059 1    24.95 ?  193 ILE   A CA  1 1 
ATOM   1498 C C   . ILE   A 1 213 ? 115.974 24.727 -16.944 1    25.72 ?  193 ILE   A C   1 1 
ATOM   1499 O O   . ILE   A 1 213 ? 115.827 25.918 -16.607 1    25.3  ?  193 ILE   A O   1 1 
ATOM   1500 C CB  . ILE   A 1 213 ? 113.99  23.217 -17.486 1    26.1  ?  193 ILE   A CB  1 1 
ATOM   1501 C CG1 . ILE   A 1 213 ? 112.923 22.963 -18.557 1    27.4  ?  193 ILE   A CG1 1 1 
ATOM   1502 C CG2 . ILE   A 1 213 ? 113.341 23.87  -16.246 1    26.96 ?  193 ILE   A CG2 1 1 
ATOM   1503 C CD1 . ILE   A 1 213 ? 111.948 21.804 -18.214 1    30.2  ?  193 ILE   A CD1 1 1 
ATOM   1504 N N   . TYR   A 1 214 ? 116.91  23.921 -16.398 1    25.2  ?  194 TYR   A N   1 1 
ATOM   1505 C CA  . TYR   A 1 214 ? 117.821 24.415 -15.355 1    24.32 ?  194 TYR   A CA  1 1 
ATOM   1506 C C   . TYR   A 1 214 ? 118.617 25.625 -15.844 1    25.67 ?  194 TYR   A C   1 1 
ATOM   1507 O O   . TYR   A 1 214 ? 118.738 26.635 -15.129 1    25.85 ?  194 TYR   A O   1 1 
ATOM   1508 C CB  . TYR   A 1 214 ? 118.766 23.256 -14.956 1    23.81 ?  194 TYR   A CB  1 1 
ATOM   1509 C CG  . TYR   A 1 214 ? 119.965 23.687 -14.127 1    23.9  ?  194 TYR   A CG  1 1 
ATOM   1510 C CD1 . TYR   A 1 214 ? 119.914 23.677 -12.735 1    25.86 ?  194 TYR   A CD1 1 1 
ATOM   1511 C CD2 . TYR   A 1 214 ? 121.19  23.933 -14.723 1    26.63 ?  194 TYR   A CD2 1 1 
ATOM   1512 C CE1 . TYR   A 1 214 ? 121.007 24.076 -11.977 1    26.67 ?  194 TYR   A CE1 1 1 
ATOM   1513 C CE2 . TYR   A 1 214 ? 122.303 24.261 -13.973 1    28.64 ?  194 TYR   A CE2 1 1 
ATOM   1514 C CZ  . TYR   A 1 214 ? 122.209 24.326 -12.6   1    29.09 ?  194 TYR   A CZ  1 1 
ATOM   1515 O OH  . TYR   A 1 214 ? 123.332 24.653 -11.871 1    32.93 ?  194 TYR   A OH  1 1 
ATOM   1516 N N   . ASN   A 1 215 ? 119.107 25.523 -17.104 1    25.38 ?  195 ASN   A N   1 1 
ATOM   1517 C CA  . ASN   A 1 215 ? 119.875 26.61  -17.694 1    26.31 ?  195 ASN   A CA  1 1 
ATOM   1518 C C   . ASN   A 1 215 ? 119.052 27.828 -18.037 1    27.47 ?  195 ASN   A C   1 1 
ATOM   1519 O O   . ASN   A 1 215 ? 119.662 28.847 -18.356 1    29.3  ?  195 ASN   A O   1 1 
ATOM   1520 C CB  . ASN   A 1 215 ? 120.639 26.123 -18.918 1    28.62 ?  195 ASN   A CB  1 1 
ATOM   1521 C CG  . ASN   A 1 215 ? 121.851 25.287 -18.557 1    33.43 ?  195 ASN   A CG  1 1 
ATOM   1522 O OD1 . ASN   A 1 215 ? 122.459 25.476 -17.497 1    34.47 ?  195 ASN   A OD1 1 1 
ATOM   1523 N ND2 . ASN   A 1 215 ? 122.243 24.36  -19.418 1    35.32 ?  195 ASN   A ND2 1 1 
ATOM   1524 N N   . SER   A 1 216 ? 117.716 27.76  -17.967 1    25.6  ?  196 SER   A N   1 1 
ATOM   1525 C CA  . SER   A 1 216 ? 116.799 28.849 -18.341 1    26.95 ?  196 SER   A CA  1 1 
ATOM   1526 C C   . SER   A 1 216 ? 116.15  29.527 -17.158 1    27.19 ?  196 SER   A C   1 1 
ATOM   1527 O O   . SER   A 1 216 ? 115.526 30.566 -17.345 1    27.65 ?  196 SER   A O   1 1 
ATOM   1528 C CB  . SER   A 1 216 ? 115.647 28.274 -19.169 1    28.6  ?  196 SER   A CB  1 1 
ATOM   1529 O OG  . SER   A 1 216 ? 116.106 27.637 -20.335 1    29.25 ?  196 SER   A OG  1 1 
ATOM   1530 N N   . ASP   A 1 217 ? 116.258 28.973 -15.943 1    25.99 ?  197 ASP   A N   1 1 
ATOM   1531 C CA  . ASP   A 1 217 ? 115.578 29.549 -14.781 1    25.17 ?  197 ASP   A CA  1 1 
ATOM   1532 C C   . ASP   A 1 217 ? 116.402 30.708 -14.214 1    25.88 ?  197 ASP   A C   1 1 
ATOM   1533 O O   . ASP   A 1 217 ? 117.521 30.5   -13.746 1    25.21 ?  197 ASP   A O   1 1 
ATOM   1534 C CB  . ASP   A 1 217 ? 115.394 28.455 -13.71  1    24.83 ?  197 ASP   A CB  1 1 
ATOM   1535 C CG  . ASP   A 1 217 ? 114.673 28.898 -12.443 1    29.91 ?  197 ASP   A CG  1 1 
ATOM   1536 O OD1 . ASP   A 1 217 ? 114.476 30.147 -12.252 1    30.07 ?  197 ASP   A OD1 1 1 
ATOM   1537 O OD2 . ASP   A 1 217 ? 114.292 28.012 -11.656 1    31.27 ?  197 ASP   A OD2 1 1 
ATOM   1538 N N   . PRO   A 1 218 ? 115.881 31.939 -14.264 1    27.61 ?  198 PRO   A N   1 1 
ATOM   1539 C CA  . PRO   A 1 218 ? 116.67  33.075 -13.751 1    27.52 ?  198 PRO   A CA  1 1 
ATOM   1540 C C   . PRO   A 1 218 ? 116.928 33.064 -12.249 1    26.81 ?  198 PRO   A C   1 1 
ATOM   1541 O O   . PRO   A 1 218 ? 117.776 33.83  -11.778 1    28.55 ?  198 PRO   A O   1 1 
ATOM   1542 C CB  . PRO   A 1 218 ? 115.858 34.325 -14.156 1    29.15 ?  198 PRO   A CB  1 1 
ATOM   1543 C CG  . PRO   A 1 218 ? 114.608 33.857 -14.779 1    30.75 ?  198 PRO   A CG  1 1 
ATOM   1544 C CD  . PRO   A 1 218 ? 114.54  32.327 -14.735 1    28.37 ?  198 PRO   A CD  1 1 
ATOM   1545 N N   . LEU   A 1 219 ? 116.182 32.272 -11.496 1    25.81 ?  199 LEU   A N   1 1 
ATOM   1546 C CA  . LEU   A 1 219 ? 116.417 32.196 -10.033 1    25.61 ?  199 LEU   A CA  1 1 
ATOM   1547 C C   . LEU   A 1 219 ? 117.53  31.237 -9.683  1    26.32 ?  199 LEU   A C   1 1 
ATOM   1548 O O   . LEU   A 1 219 ? 117.876 31.119 -8.51   1    27.94 ?  199 LEU   A O   1 1 
ATOM   1549 C CB  . LEU   A 1 219 ? 115.164 31.748 -9.33   1    26.15 ?  199 LEU   A CB  1 1 
ATOM   1550 C CG  . LEU   A 1 219 ? 114.03  32.782 -9.272  1    27.85 ?  199 LEU   A CG  1 1 
ATOM   1551 C CD1 . LEU   A 1 219 ? 112.811 32.192 -8.593  1    27.8  ?  199 LEU   A CD1 1 1 
ATOM   1552 C CD2 . LEU   A 1 219 ? 114.464 34.065 -8.574  1    27.72 ?  199 LEU   A CD2 1 1 
ATOM   1553 N N   . ILE   A 1 220 ? 118.072 30.496 -10.675 1    25.14 ?  200 ILE   A N   1 1 
ATOM   1554 C CA  . ILE   A 1 220 ? 119.148 29.586 -10.412 1    25.5  ?  200 ILE   A CA  1 1 
ATOM   1555 C C   . ILE   A 1 220 ? 120.45  30.315 -10.648 1    27.82 ?  200 ILE   A C   1 1 
ATOM   1556 O O   . ILE   A 1 220 ? 120.607 31.005 -11.673 1    30.34 ?  200 ILE   A O   1 1 
ATOM   1557 C CB  . ILE   A 1 220 ? 119.004 28.348 -11.345 1    25.44 ?  200 ILE   A CB  1 1 
ATOM   1558 C CG1 . ILE   A 1 220 ? 117.732 27.563 -10.949 1    27.53 ?  200 ILE   A CG1 1 1 
ATOM   1559 C CG2 . ILE   A 1 220 ? 120.254 27.452 -11.195 1    26.42 ?  200 ILE   A CG2 1 1 
ATOM   1560 C CD1 . ILE   A 1 220 ? 117.536 26.18  -11.66  1    28.27 ?  200 ILE   A CD1 1 1 
ATOM   1561 N N   . CYS   A 1 221 ? 121.388 30.173 -9.729  1    28.38 ?  201 CYS   A N   1 1 
ATOM   1562 C CA  . CYS   A 1 221 ? 122.699 30.745 -9.874  1    29.94 ?  201 CYS   A CA  1 1 
ATOM   1563 C C   . CYS   A 1 221 ? 123.59  29.704 -10.501 1    32.18 ?  201 CYS   A C   1 1 
ATOM   1564 O O   . CYS   A 1 221 ? 123.839 28.631 -9.906  1    33.09 ?  201 CYS   A O   1 1 
ATOM   1565 C CB  . CYS   A 1 221 ? 123.249 31.194 -8.531  1    31.04 ?  201 CYS   A CB  1 1 
ATOM   1566 S SG  . CYS   A 1 221 ? 124.874 31.984 -8.65   0.79 33.8  ?  201 CYS   A SG  1 1 
ATOM   1567 N N   . ARG   A 1 222 ? 124.055 29.988 -11.708 1    33.35 ?  202 ARG   A N   1 1 
ATOM   1568 C CA  . ARG   A 1 222 ? 124.94  29.06  -12.404 1    35.81 ?  202 ARG   A CA  1 1 
ATOM   1569 C C   . ARG   A 1 222 ? 126.367 29.62  -12.536 1    39.21 ?  202 ARG   A C   1 1 
ATOM   1570 O O   . ARG   A 1 222 ? 127.149 29.103 -13.333 1    40.96 ?  202 ARG   A O   1 1 
ATOM   1571 C CB  . ARG   A 1 222 ? 124.355 28.688 -13.776 1    35.65 ?  202 ARG   A CB  1 1 
ATOM   1572 C CG  . ARG   A 1 222 ? 123.01  27.962 -13.665 1    35.21 ?  202 ARG   A CG  1 1 
ATOM   1573 C CD  . ARG   A 1 222 ? 122.334 27.761 -15.02  1    34.7  ?  202 ARG   A CD  1 1 
ATOM   1574 N NE  . ARG   A 1 222 ? 122.11  29.082 -15.618 1    35.67 ?  202 ARG   A NE  1 1 
ATOM   1575 C CZ  . ARG   A 1 222 ? 120.986 29.778 -15.497 1    37.23 ?  202 ARG   A CZ  1 1 
ATOM   1576 N NH1 . ARG   A 1 222 ? 119.914 29.233 -14.929 1    31.4  ?  202 ARG   A NH1 1 1 
ATOM   1577 N NH2 . ARG   A 1 222 ? 120.915 31.022 -15.965 1    37.67 ?  202 ARG   A NH2 1 1 
ATOM   1578 N N   . ALA   A 1 223 ? 126.728 30.609 -11.7   1    39.6  ?  203 ALA   A N   1 1 
ATOM   1579 C CA  . ALA   A 1 223 ? 128.061 31.19  -11.72  1    41.33 ?  203 ALA   A CA  1 1 
ATOM   1580 C C   . ALA   A 1 223 ? 129.066 30.202 -11.103 1    42.21 ?  203 ALA   A C   1 1 
ATOM   1581 O O   . ALA   A 1 223 ? 128.67  29.239 -10.422 1    42.36 ?  203 ALA   A O   1 1 
ATOM   1582 C CB  . ALA   A 1 223 ? 128.043 32.509 -10.951 1    41.55 ?  203 ALA   A CB  1 1 
ATOM   1583 N N   . GLY   A 1 224 ? 130.364 30.452 -11.303 1    42.59 ?  204 GLY   A N   1 1 
ATOM   1584 C CA  . GLY   A 1 224 ? 131.388 29.625 -10.684 1    42.74 ?  204 GLY   A CA  1 1 
ATOM   1585 C C   . GLY   A 1 224 ? 131.296 29.705 -9.173  1    42.38 ?  204 GLY   A C   1 1 
ATOM   1586 O O   . GLY   A 1 224 ? 130.871 30.734 -8.627  1    42.04 ?  204 GLY   A O   1 1 
ATOM   1587 N N   . LEU   A 1 225 ? 131.592 28.606 -8.5    1    42.09 ?  205 LEU   A N   1 1 
ATOM   1588 C CA  . LEU   A 1 225 ? 131.523 28.57  -7.046  1    42.78 ?  205 LEU   A CA  1 1 
ATOM   1589 C C   . LEU   A 1 225 ? 132.613 29.429 -6.464  1    41.31 ?  205 LEU   A C   1 1 
ATOM   1590 O O   . LEU   A 1 225 ? 133.774 29.223 -6.798  1    40.81 ?  205 LEU   A O   1 1 
ATOM   1591 C CB  . LEU   A 1 225 ? 131.711 27.136 -6.547  1    44.35 ?  205 LEU   A CB  1 1 
ATOM   1592 C CG  . LEU   A 1 225 ? 130.466 26.483 -5.952  1    47.57 ?  205 LEU   A CG  1 1 
ATOM   1593 C CD1 . LEU   A 1 225 ? 129.295 26.52  -6.958  1    48.91 ?  205 LEU   A CD1 1 1 
ATOM   1594 C CD2 . LEU   A 1 225 ? 130.755 25.053 -5.581  1    48.53 ?  205 LEU   A CD2 1 1 
ATOM   1595 N N   . LYS   A 1 226 ? 132.265 30.354 -5.562  1    40.02 ?  206 LYS   A N   1 1 
ATOM   1596 C CA  . LYS   A 1 226 ? 133.277 31.15  -4.89   1    39.51 ?  206 LYS   A CA  1 1 
ATOM   1597 C C   . LYS   A 1 226 ? 134.073 30.217 -3.962  1    38.58 ?  206 LYS   A C   1 1 
ATOM   1598 O O   . LYS   A 1 226 ? 133.507 29.275 -3.417  1    37.67 ?  206 LYS   A O   1 1 
ATOM   1599 C CB  . LYS   A 1 226 ? 132.621 32.29  -4.11   1    41.81 ?  206 LYS   A CB  1 1 
ATOM   1600 C CG  . LYS   A 1 226 ? 132.152 33.433 -5.009  1    47.72 ?  206 LYS   A CG  1 1 
ATOM   1601 C CD  . LYS   A 1 226 ? 130.869 34.075 -4.492  1    54.49 ?  206 LYS   A CD  1 1 
ATOM   1602 C CE  . LYS   A 1 226 ? 130.372 35.233 -5.343  1    60.36 ?  206 LYS   A CE  1 1 
ATOM   1603 N NZ  . LYS   A 1 226 ? 129.048 35.749 -4.858  1    62.88 ?  206 LYS   A NZ  1 1 
ATOM   1604 N N   . VAL   A 1 227 ? 135.385 30.403 -3.865  1    38.55 ?  207 VAL   A N   1 1 
ATOM   1605 C CA  . VAL   A 1 227 ? 136.219 29.56  -3.016  1    38.65 ?  207 VAL   A CA  1 1 
ATOM   1606 C C   . VAL   A 1 227 ? 135.737 29.568 -1.544  1    37.23 ?  207 VAL   A C   1 1 
ATOM   1607 O O   . VAL   A 1 227 ? 135.71  28.51  -0.917  1    36.24 ?  207 VAL   A O   1 1 
ATOM   1608 C CB  . VAL   A 1 227 ? 137.721 29.906 -3.174  1    41.08 ?  207 VAL   A CB  1 1 
ATOM   1609 C CG1 . VAL   A 1 227 ? 138.579 29.041 -2.263  1    41.48 ?  207 VAL   A CG1 1 1 
ATOM   1610 C CG2 . VAL   A 1 227 ? 138.16  29.737 -4.628  1    42.26 ?  207 VAL   A CG2 1 1 
ATOM   1611 N N   . CYS   A 1 228 ? 135.252 30.718 -1.034  1    36.85 ?  208 CYS   A N   1 1 
ATOM   1612 C CA  . CYS   A 1 228 ? 134.741 30.762 0.345   1    37.65 ?  208 CYS   A CA  1 1 
ATOM   1613 C C   . CYS   A 1 228 ? 133.523 29.834 0.519   1    36.63 ?  208 CYS   A C   1 1 
ATOM   1614 O O   . CYS   A 1 228 ? 133.392 29.191 1.559   1    37.73 ?  208 CYS   A O   1 1 
ATOM   1615 C CB  . CYS   A 1 228 ? 134.41  32.191 0.76    1    40.21 ?  208 CYS   A CB  1 1 
ATOM   1616 S SG  . CYS   A 1 228 ? 133.082 32.939 -0.21   1    49.46 ?  208 CYS   A SG  1 1 
ATOM   1617 N N   . PHE   A 1 229 ? 132.669 29.739 -0.501  1    34.65 ?  209 PHE   A N   1 1 
ATOM   1618 C CA  . PHE   A 1 229 ? 131.501 28.859 -0.441  1    33.82 ?  209 PHE   A CA  1 1 
ATOM   1619 C C   . PHE   A 1 229 ? 131.919 27.37  -0.558  1    34.53 ?  209 PHE   A C   1 1 
ATOM   1620 O O   . PHE   A 1 229 ? 131.42  26.526 0.195   1    34.47 ?  209 PHE   A O   1 1 
ATOM   1621 C CB  . PHE   A 1 229 ? 130.494 29.229 -1.53   1    32.5  ?  209 PHE   A CB  1 1 
ATOM   1622 C CG  . PHE   A 1 229 ? 129.166 28.529 -1.356  1    32.22 ?  209 PHE   A CG  1 1 
ATOM   1623 C CD1 . PHE   A 1 229 ? 128.249 28.978 -0.437  1    33.28 ?  209 PHE   A CD1 1 1 
ATOM   1624 C CD2 . PHE   A 1 229 ? 128.834 27.437 -2.135  1    33.1  ?  209 PHE   A CD2 1 1 
ATOM   1625 C CE1 . PHE   A 1 229 ? 127.009 28.366 -0.311  1    34.5  ?  209 PHE   A CE1 1 1 
ATOM   1626 C CE2 . PHE   A 1 229 ? 127.602 26.811 -1.984  1    33.28 ?  209 PHE   A CE2 1 1 
ATOM   1627 C CZ  . PHE   A 1 229 ? 126.705 27.278 -1.072  1    32.32 ?  209 PHE   A CZ  1 1 
ATOM   1628 N N   . GLY   A 1 230 ? 132.877 27.07  -1.438  1    33.85 ?  210 GLY   A N   1 1 
ATOM   1629 C CA  . GLY   A 1 230 ? 133.414 25.713 -1.561  1    33.49 ?  210 GLY   A CA  1 1 
ATOM   1630 C C   . GLY   A 1 230 ? 134.044 25.243 -0.259  1    34.19 ?  210 GLY   A C   1 1 
ATOM   1631 O O   . GLY   A 1 230 ? 133.909 24.076 0.129   1    33.39 ?  210 GLY   A O   1 1 
ATOM   1632 N N   . ILE   A 1 231 ? 134.691 26.181 0.473   1    34.98 ?  211 ILE   A N   1 1 
ATOM   1633 C CA  . ILE   A 1 231 ? 135.257 25.875 1.788   1    35.38 ?  211 ILE   A CA  1 1 
ATOM   1634 C C   . ILE   A 1 231 ? 134.132 25.472 2.754   1    33.11 ?  211 ILE   A C   1 1 
ATOM   1635 O O   . ILE   A 1 231 ? 134.306 24.547 3.541   1    33.77 ?  211 ILE   A O   1 1 
ATOM   1636 C CB  . ILE   A 1 231 ? 136.089 27.093 2.286   1    37.69 ?  211 ILE   A CB  1 1 
ATOM   1637 C CG1 . ILE   A 1 231 ? 137.427 27.159 1.518   1    39.27 ?  211 ILE   A CG1 1 1 
ATOM   1638 C CG2 . ILE   A 1 231 ? 136.356 26.994 3.771   1    38.85 ?  211 ILE   A CG2 1 1 
ATOM   1639 C CD1 . ILE   A 1 231 ? 138.181 28.486 1.701   1    40.41 ?  211 ILE   A CD1 1 1 
ATOM   1640 N N   . GLN   A 1 232 ? 132.968 26.157 2.678   1    31.83 ?  212 GLN   A N   1 1 
ATOM   1641 C CA  . GLN   A 1 232 ? 131.831 25.761 3.522   1    30.51 ?  212 GLN   A CA  1 1 
ATOM   1642 C C   . GLN   A 1 232 ? 131.244 24.405 3.137   1    31.03 ?  212 GLN   A C   1 1 
ATOM   1643 O O   . GLN   A 1 232 ? 130.788 23.67  4.014   1    31.94 ?  212 GLN   A O   1 1 
ATOM   1644 C CB  . GLN   A 1 232 ? 130.752 26.845 3.533   1    29.33 ?  212 GLN   A CB  1 1 
ATOM   1645 C CG  . GLN   A 1 232 ? 131.252 28.18  4.151   1    30.74 ?  212 GLN   A CG  1 1 
ATOM   1646 C CD  . GLN   A 1 232 ? 131.738 27.954 5.576   1    33.47 ?  212 GLN   A CD  1 1 
ATOM   1647 O OE1 . GLN   A 1 232 ? 131.196 27.133 6.341   1    34.32 ?  212 GLN   A OE1 1 1 
ATOM   1648 N NE2 . GLN   A 1 232 ? 132.758 28.739 5.998   1    36.1  ?  212 GLN   A NE2 1 1 
ATOM   1649 N N   . LEU   A 1 233 ? 131.284 24.046 1.838   1    30.55 ?  213 LEU   A N   1 1 
ATOM   1650 C CA  . LEU   A 1 233 ? 130.84  22.709 1.43    1    31.36 ?  213 LEU   A CA  1 1 
ATOM   1651 C C   . LEU   A 1 233 ? 131.829 21.68  1.975   1    32.82 ?  213 LEU   A C   1 1 
ATOM   1652 O O   . LEU   A 1 233 ? 131.398 20.623 2.419   1    33.49 ?  213 LEU   A O   1 1 
ATOM   1653 C CB  . LEU   A 1 233 ? 130.754 22.585 -0.068  1    31.6  ?  213 LEU   A CB  1 1 
ATOM   1654 C CG  . LEU   A 1 233 ? 129.69  23.403 -0.771  1    31.88 ?  213 LEU   A CG  1 1 
ATOM   1655 C CD1 . LEU   A 1 233 ? 129.736 23.161 -2.276  1    31.67 ?  213 LEU   A CD1 1 1 
ATOM   1656 C CD2 . LEU   A 1 233 ? 128.304 23.135 -0.22   1    33.04 ?  213 LEU   A CD2 1 1 
ATOM   1657 N N   . LEU   A 1 234 ? 133.144 21.996 1.996   1    33.65 ?  214 LEU   A N   1 1 
ATOM   1658 C CA  . LEU   A 1 234 ? 134.131 21.097 2.602   1    35.54 ?  214 LEU   A CA  1 1 
ATOM   1659 C C   . LEU   A 1 234 ? 133.846 20.986 4.114   1    35.7  ?  214 LEU   A C   1 1 
ATOM   1660 O O   . LEU   A 1 234 ? 133.989 19.896 4.664   1    36.86 ?  214 LEU   A O   1 1 
ATOM   1661 C CB  . LEU   A 1 234 ? 135.569 21.599 2.366   1    37.19 ?  214 LEU   A CB  1 1 
ATOM   1662 C CG  . LEU   A 1 234 ? 136.12  21.511 0.943   1    40.42 ?  214 LEU   A CG  1 1 
ATOM   1663 C CD1 . LEU   A 1 234 ? 137.553 22.06  0.895   1    41.85 ?  214 LEU   A CD1 1 1 
ATOM   1664 C CD2 . LEU   A 1 234 ? 136.112 20.081 0.417   1    41.48 ?  214 LEU   A CD2 1 1 
ATOM   1665 N N   . ASN   A 1 235 ? 133.387 22.09  4.774   1    34.89 ?  215 ASN   A N   1 1 
ATOM   1666 C CA  . ASN   A 1 235 ? 133.012 22.019 6.193   1    34.57 ?  215 ASN   A CA  1 1 
ATOM   1667 C C   . ASN   A 1 235 ? 131.793 21.118 6.36    1    33.96 ?  215 ASN   A C   1 1 
ATOM   1668 O O   . ASN   A 1 235 ? 131.758 20.293 7.267   1    34.77 ?  215 ASN   A O   1 1 
ATOM   1669 C CB  . ASN   A 1 235 ? 132.687 23.404 6.788   1    35.42 ?  215 ASN   A CB  1 1 
ATOM   1670 C CG  . ASN   A 1 235 ? 133.914 24.269 6.953   1    39.28 ?  215 ASN   A CG  1 1 
ATOM   1671 O OD1 . ASN   A 1 235 ? 135.034 23.758 7.061   1    41.24 ?  215 ASN   A OD1 1 1 
ATOM   1672 N ND2 . ASN   A 1 235 ? 133.736 25.592 6.953   1    40.04 ?  215 ASN   A ND2 1 1 
ATOM   1673 N N   . ALA   A 1 236 ? 130.812 21.216 5.445   1    32.2  ?  216 ALA   A N   1 1 
ATOM   1674 C CA  . ALA   A 1 236 ? 129.623 20.355 5.514   1    31.16 ?  216 ALA   A CA  1 1 
ATOM   1675 C C   . ALA   A 1 236 ? 130.018 18.867 5.425   1    31.55 ?  216 ALA   A C   1 1 
ATOM   1676 O O   . ALA   A 1 236 ? 129.513 18.064 6.193   1    32.16 ?  216 ALA   A O   1 1 
ATOM   1677 C CB  . ALA   A 1 236 ? 128.654 20.702 4.396   1    31.07 ?  216 ALA   A CB  1 1 
ATOM   1678 N N   . VAL   A 1 237 ? 130.943 18.521 4.522   1    31.4  ?  217 VAL   A N   1 1 
ATOM   1679 C CA  . VAL   A 1 237 ? 131.395 17.137 4.38    1    32.72 ?  217 VAL   A CA  1 1 
ATOM   1680 C C   . VAL   A 1 237 ? 132.084 16.653 5.685   1    33.65 ?  217 VAL   A C   1 1 
ATOM   1681 O O   . VAL   A 1 237 ? 131.816 15.537 6.145   1    34.08 ?  217 VAL   A O   1 1 
ATOM   1682 C CB  . VAL   A 1 237 ? 132.3   17.031 3.13    1    34.42 ?  217 VAL   A CB  1 1 
ATOM   1683 C CG1 . VAL   A 1 237 ? 133.07  15.71  3.112   1    35.82 ?  217 VAL   A CG1 1 1 
ATOM   1684 C CG2 . VAL   A 1 237 ? 131.462 17.184 1.851   1    34.75 ?  217 VAL   A CG2 1 1 
ATOM   1685 N N   . SER   A 1 238 ? 132.918 17.51  6.301   1    34.27 ?  218 SER   A N   1 1 
ATOM   1686 C CA  A SER   A 1 238 ? 133.602 17.148 7.552   0.5  35.18 ?  218 SER   A CA  1 1 
ATOM   1687 C CA  B SER   A 1 238 ? 133.596 17.128 7.544   0.5  34.81 ?  218 SER   A CA  1 1 
ATOM   1688 C C   . SER   A 1 238 ? 132.584 16.943 8.675   1    34.09 ?  218 SER   A C   1 1 
ATOM   1689 O O   . SER   A 1 238 ? 132.705 16.009 9.455   1    34.63 ?  218 SER   A O   1 1 
ATOM   1690 C CB  A SER   A 1 238 ? 134.589 18.244 7.968   0.5  38.54 ?  218 SER   A CB  1 1 
ATOM   1691 C CB  B SER   A 1 238 ? 134.628 18.182 7.942   0.5  37.14 ?  218 SER   A CB  1 1 
ATOM   1692 O OG  A SER   A 1 238 ? 135.576 18.491 6.981   0.5  42.81 ?  218 SER   A OG  1 1 
ATOM   1693 O OG  B SER   A 1 238 ? 135.261 17.828 9.159   0.5  39.56 ?  218 SER   A OG  1 1 
ATOM   1694 N N   . ARG   A 1 239 ? 131.591 17.84  8.765   1    31.88 ?  219 ARG   A N   1 1 
ATOM   1695 C CA  . ARG   A 1 239 ? 130.576 17.749 9.802   1    31.36 ?  219 ARG   A CA  1 1 
ATOM   1696 C C   . ARG   A 1 239 ? 129.647 16.566 9.61    1    31.14 ?  219 ARG   A C   1 1 
ATOM   1697 O O   . ARG   A 1 239 ? 129.245 15.952 10.596  1    31.17 ?  219 ARG   A O   1 1 
ATOM   1698 C CB  . ARG   A 1 239 ? 129.791 19.05  9.926   1    31.62 ?  219 ARG   A CB  1 1 
ATOM   1699 C CG  . ARG   A 1 239 ? 130.713 20.194 10.311  1    33.17 ?  219 ARG   A CG  1 1 
ATOM   1700 C CD  . ARG   A 1 239 ? 130.046 21.546 10.215  1    33.95 ?  219 ARG   A CD  1 1 
ATOM   1701 N NE  . ARG   A 1 239 ? 131.059 22.604 10.329  1    34.94 ?  219 ARG   A NE  1 1 
ATOM   1702 C CZ  . ARG   A 1 239 ? 130.799 23.905 10.235  1    35.65 ?  219 ARG   A CZ  1 1 
ATOM   1703 N NH1 . ARG   A 1 239 ? 129.55  24.33  10.053  1    34.96 ?  219 ARG   A NH1 1 1 
ATOM   1704 N NH2 . ARG   A 1 239 ? 131.78  24.792 10.339  1    34.68 ?  219 ARG   A NH2 1 1 
ATOM   1705 N N   . VAL   A 1 240 ? 129.304 16.227 8.348   1    30.23 ?  220 VAL   A N   1 1 
ATOM   1706 C CA  . VAL   A 1 240 ? 128.459 15.064 8.066   1    30.57 ?  220 VAL   A CA  1 1 
ATOM   1707 C C   . VAL   A 1 240 ? 129.183 13.803 8.522   1    31.37 ?  220 VAL   A C   1 1 
ATOM   1708 O O   . VAL   A 1 240 ? 128.571 12.996 9.2     1    30.52 ?  220 VAL   A O   1 1 
ATOM   1709 C CB  . VAL   A 1 240 ? 128.051 14.997 6.555   1    31.4  ?  220 VAL   A CB  1 1 
ATOM   1710 C CG1 . VAL   A 1 240 ? 127.56  13.572 6.176   1    31.56 ?  220 VAL   A CG1 1 1 
ATOM   1711 C CG2 . VAL   A 1 240 ? 126.965 16.021 6.236   1    32.26 ?  220 VAL   A CG2 1 1 
ATOM   1712 N N   . GLU   A 1 241 ? 130.487 13.681 8.22    1    32.8  ?  221 GLU   A N   1 1 
ATOM   1713 C CA  . GLU   A 1 241 ? 131.295 12.53  8.637   1    36.03 ?  221 GLU   A CA  1 1 
ATOM   1714 C C   . GLU   A 1 241 ? 131.271 12.362 10.159  1    37.73 ?  221 GLU   A C   1 1 
ATOM   1715 O O   . GLU   A 1 241 ? 131.088 11.244 10.642  1    38.62 ?  221 GLU   A O   1 1 
ATOM   1716 C CB  . GLU   A 1 241 ? 132.739 12.686 8.129   1    41.43 ?  221 GLU   A CB  1 1 
ATOM   1717 C CG  . GLU   A 1 241 ? 133.682 11.537 8.493   1    52.11 ?  221 GLU   A CG  1 1 
ATOM   1718 C CD  . GLU   A 1 241 ? 135.15  11.894 8.302   1    65.19 ?  221 GLU   A CD  1 1 
ATOM   1719 O OE1 . GLU   A 1 241 ? 135.443 12.744 7.427   1    68.62 ?  221 GLU   A OE1 1 1 
ATOM   1720 O OE2 . GLU   A 1 241 ? 136.005 11.339 9.032   1    69.06 ?  221 GLU   A OE2 1 1 
ATOM   1721 N N   . ARG   A 1 242 ? 131.386 13.466 10.92   1    37.77 ?  222 ARG   A N   1 1 
ATOM   1722 C CA  . ARG   A 1 242 ? 131.341 13.358 12.383  1    38.57 ?  222 ARG   A CA  1 1 
ATOM   1723 C C   . ARG   A 1 242 ? 129.927 13.067 12.905  1    37.95 ?  222 ARG   A C   1 1 
ATOM   1724 O O   . ARG   A 1 242 ? 129.787 12.461 13.974  1    39.45 ?  222 ARG   A O   1 1 
ATOM   1725 C CB  . ARG   A 1 242 ? 131.911 14.623 13.053  1    41.72 ?  222 ARG   A CB  1 1 
ATOM   1726 C CG  . ARG   A 1 242 ? 133.418 14.747 12.86   1    48.88 ?  222 ARG   A CG  1 1 
ATOM   1727 C CD  . ARG   A 1 242 ? 134.075 15.926 13.589  1    56.04 ?  222 ARG   A CD  1 1 
ATOM   1728 N NE  . ARG   A 1 242 ? 133.174 17.053 13.877  1    63.27 ?  222 ARG   A NE  1 1 
ATOM   1729 C CZ  . ARG   A 1 242 ? 133.116 18.181 13.172  1    67.94 ?  222 ARG   A CZ  1 1 
ATOM   1730 N NH1 . ARG   A 1 242 ? 133.906 18.357 12.118  1    68.33 ?  222 ARG   A NH1 1 1 
ATOM   1731 N NH2 . ARG   A 1 242 ? 132.274 19.146 13.522  1    68.43 ?  222 ARG   A NH2 1 1 
ATOM   1732 N N   . ALA   A 1 243 ? 128.891 13.439 12.139  1    35.16 ?  223 ALA   A N   1 1 
ATOM   1733 C CA  . ALA   A 1 243 ? 127.517 13.254 12.575  1    35.97 ?  223 ALA   A CA  1 1 
ATOM   1734 C C   . ALA   A 1 243 ? 126.989 11.836 12.359  1    38.08 ?  223 ALA   A C   1 1 
ATOM   1735 O O   . ALA   A 1 243 ? 126.107 11.421 13.106  1    38.74 ?  223 ALA   A O   1 1 
ATOM   1736 C CB  . ALA   A 1 243 ? 126.604 14.242 11.864  1    35.57 ?  223 ALA   A CB  1 1 
ATOM   1737 N N   . LEU   A 1 244 ? 127.502 11.12  11.377  1    39.53 ?  224 LEU   A N   1 1 
ATOM   1738 C CA  . LEU   A 1 244 ? 126.963 9.772  11.073  1    43.32 ?  224 LEU   A CA  1 1 
ATOM   1739 C C   . LEU   A 1 244 ? 126.851 8.816  12.262  1    47.52 ?  224 LEU   A C   1 1 
ATOM   1740 O O   . LEU   A 1 244 ? 125.746 8.298  12.468  1    47.8  ?  224 LEU   A O   1 1 
ATOM   1741 C CB  . LEU   A 1 244 ? 127.705 9.097  9.933   1    43.62 ?  224 LEU   A CB  1 1 
ATOM   1742 C CG  . LEU   A 1 244 ? 127.742 9.88   8.63    1    45.17 ?  224 LEU   A CG  1 1 
ATOM   1743 C CD1 . LEU   A 1 244 ? 128.372 9.081  7.534   1    45.99 ?  224 LEU   A CD1 1 1 
ATOM   1744 C CD2 . LEU   A 1 244 ? 126.356 10.361 8.2     1    46.17 ?  224 LEU   A CD2 1 1 
ATOM   1745 N N   . PRO   A 1 245 ? 127.887 8.614  13.117  1    50.42 ?  225 PRO   A N   1 1 
ATOM   1746 C CA  . PRO   A 1 245 ? 127.711 7.695  14.263  1    52.15 ?  225 PRO   A CA  1 1 
ATOM   1747 C C   . PRO   A 1 245 ? 126.665 8.146  15.293  1    53.4  ?  225 PRO   A C   1 1 
ATOM   1748 O O   . PRO   A 1 245 ? 126.369 7.416  16.233  1    55.47 ?  225 PRO   A O   1 1 
ATOM   1749 C CB  . PRO   A 1 245 ? 129.113 7.636  14.885  1    53.34 ?  225 PRO   A CB  1 1 
ATOM   1750 C CG  . PRO   A 1 245 ? 130.05  8.127  13.812  1    53.35 ?  225 PRO   A CG  1 1 
ATOM   1751 C CD  . PRO   A 1 245 ? 129.264 9.147  13.068  1    51.09 ?  225 PRO   A CD  1 1 
ATOM   1752 N N   . LYS   A 1 246 ? 126.117 9.33   15.132  1    51.85 ?  226 LYS   A N   1 1 
ATOM   1753 C CA  . LYS   A 1 246 ? 125.077 9.855  16.01   1    51.09 ?  226 LYS   A CA  1 1 
ATOM   1754 C C   . LYS   A 1 246 ? 123.7   9.851  15.333  1    47.86 ?  226 LYS   A C   1 1 
ATOM   1755 O O   . LYS   A 1 246 ? 122.714 10.248 15.969  1    49.49 ?  226 LYS   A O   1 1 
ATOM   1756 C CB  . LYS   A 1 246 ? 125.381 11.325 16.401  1    55.62 ?  226 LYS   A CB  1 1 
ATOM   1757 C CG  . LYS   A 1 246 ? 126.852 11.694 16.6    1    61.51 ?  226 LYS   A CG  1 1 
ATOM   1758 C CD  . LYS   A 1 246 ? 126.974 13.209 16.822  1    66.53 ?  226 LYS   A CD  1 1 
ATOM   1759 C CE  . LYS   A 1 246 ? 128.393 13.623 17.121  1    71.45 ?  226 LYS   A CE  1 1 
ATOM   1760 N NZ  . LYS   A 1 246 ? 128.505 15.087 17.34   1    74.71 ?  226 LYS   A NZ  1 1 
ATOM   1761 N N   . LEU   A 1 247 ? 123.651 9.604  14.01   1    42.9  ?  227 LEU   A N   1 1 
ATOM   1762 C CA  . LEU   A 1 247 ? 122.424 9.684  13.277  1    39.29 ?  227 LEU   A CA  1 1 
ATOM   1763 C C   . LEU   A 1 247 ? 121.616 8.423  13.546  1    35.53 ?  227 LEU   A C   1 1 
ATOM   1764 O O   . LEU   A 1 247 ? 122.094 7.308  13.344  1    36.9  ?  227 LEU   A O   1 1 
ATOM   1765 C CB  . LEU   A 1 247 ? 122.774 9.838  11.795  1    39.27 ?  227 LEU   A CB  1 1 
ATOM   1766 C CG  . LEU   A 1 247 ? 121.699 10.327 10.854  1    39.85 ?  227 LEU   A CG  1 1 
ATOM   1767 C CD1 . LEU   A 1 247 ? 121.287 11.772 11.176  1    39.9  ?  227 LEU   A CD1 1 1 
ATOM   1768 C CD2 . LEU   A 1 247 ? 122.174 10.169 9.397   1    38.44 ?  227 LEU   A CD2 1 1 
ATOM   1769 N N   . THR   A 1 248 ? 120.412 8.618  14.039  1    32.1  ?  228 THR   A N   1 1 
ATOM   1770 C CA  . THR   A 1 248 ? 119.482 7.537  14.328  1    31.53 ?  228 THR   A CA  1 1 
ATOM   1771 C C   . THR   A 1 248 ? 118.143 7.701  13.629  1    29.45 ?  228 THR   A C   1 1 
ATOM   1772 O O   . THR   A 1 248 ? 117.328 6.784  13.696  1    30.18 ?  228 THR   A O   1 1 
ATOM   1773 C CB  . THR   A 1 248 ? 119.219 7.485  15.852  1    33.79 ?  228 THR   A CB  1 1 
ATOM   1774 O OG1 . THR   A 1 248 ? 118.664 8.747  16.253  1    35.63 ?  228 THR   A OG1 1 1 
ATOM   1775 C CG2 . THR   A 1 248 ? 120.492 7.168  16.641  1    35.12 ?  228 THR   A CG2 1 1 
ATOM   1776 N N   . VAL   A 1 249 ? 117.906 8.834  12.938  1    28.06 ?  229 VAL   A N   1 1 
ATOM   1777 C CA  . VAL   A 1 249 ? 116.633 9.054  12.284  1    26.72 ?  229 VAL   A CA  1 1 
ATOM   1778 C C   . VAL   A 1 249 ? 116.391 8.002  11.148  1    25.94 ?  229 VAL   A C   1 1 
ATOM   1779 O O   . VAL   A 1 249 ? 117.32  7.623  10.445  1    25.95 ?  229 VAL   A O   1 1 
ATOM   1780 C CB  . VAL   A 1 249 ? 116.631 10.498 11.689  1    26.41 ?  229 VAL   A CB  1 1 
ATOM   1781 C CG1 . VAL   A 1 249 ? 117.634 10.615 10.543  1    27.44 ?  229 VAL   A CG1 1 1 
ATOM   1782 C CG2 . VAL   A 1 249 ? 115.245 10.86  11.212  1    27.4  ?  229 VAL   A CG2 1 1 
ATOM   1783 N N   . PRO   A 1 250 ? 115.153 7.554  10.953  1    25.4  ?  230 PRO   A N   1 1 
ATOM   1784 C CA  . PRO   A 1 250 ? 114.85  6.712  9.794   1    23.58 ?  230 PRO   A CA  1 1 
ATOM   1785 C C   . PRO   A 1 250 ? 115.171 7.463  8.49    1    23.18 ?  230 PRO   A C   1 1 
ATOM   1786 O O   . PRO   A 1 250 ? 114.94  8.679  8.42    1    25.09 ?  230 PRO   A O   1 1 
ATOM   1787 C CB  . PRO   A 1 250 ? 113.339 6.524  9.885   1    25.73 ?  230 PRO   A CB  1 1 
ATOM   1788 C CG  . PRO   A 1 250 ? 113.043 6.636  11.41   1    26.62 ?  230 PRO   A CG  1 1 
ATOM   1789 C CD  . PRO   A 1 250 ? 113.959 7.775  11.805  1    25.9  ?  230 PRO   A CD  1 1 
ATOM   1790 N N   . PHE   A 1 251 ? 115.712 6.74   7.487   1    22.79 ?  231 PHE   A N   1 1 
ATOM   1791 C CA  . PHE   A 1 251 ? 115.96  7.425  6.234   1    22.3  ?  231 PHE   A CA  1 1 
ATOM   1792 C C   . PHE   A 1 251 ? 115.876 6.533  5.033   1    20.92 ?  231 PHE   A C   1 1 
ATOM   1793 O O   . PHE   A 1 251 ? 116.068 5.299  5.114   1    20.33 ?  231 PHE   A O   1 1 
ATOM   1794 C CB  . PHE   A 1 251 ? 117.276 8.25   6.202   1    23    ?  231 PHE   A CB  1 1 
ATOM   1795 C CG  . PHE   A 1 251 ? 118.537 7.428  6.292   1    24.12 ?  231 PHE   A CG  1 1 
ATOM   1796 C CD1 . PHE   A 1 251 ? 119.13  6.894  5.151   1    24.1  ?  231 PHE   A CD1 1 1 
ATOM   1797 C CD2 . PHE   A 1 251 ? 119.187 7.262  7.505   1    25.34 ?  231 PHE   A CD2 1 1 
ATOM   1798 C CE1 . PHE   A 1 251 ? 120.313 6.185  5.236   1    24.8  ?  231 PHE   A CE1 1 1 
ATOM   1799 C CE2 . PHE   A 1 251 ? 120.384 6.573  7.581   1    25.11 ?  231 PHE   A CE2 1 1 
ATOM   1800 C CZ  . PHE   A 1 251 ? 120.957 6.063  6.458   1    24.82 ?  231 PHE   A CZ  1 1 
ATOM   1801 N N   . LEU   A 1 252 ? 115.521 7.176  3.906   1    21.3  ?  232 LEU   A N   1 1 
ATOM   1802 C CA  . LEU   A 1 252 ? 115.499 6.594  2.582   1    21.05 ?  232 LEU   A CA  1 1 
ATOM   1803 C C   . LEU   A 1 252 ? 116.561 7.362  1.785   1    19.94 ?  232 LEU   A C   1 1 
ATOM   1804 O O   . LEU   A 1 252 ? 116.579 8.603  1.826   1    21.24 ?  232 LEU   A O   1 1 
ATOM   1805 C CB  . LEU   A 1 252 ? 114.143 6.823  1.917   1    22.77 ?  232 LEU   A CB  1 1 
ATOM   1806 C CG  . LEU   A 1 252 ? 114.089 6.439  0.45    1    23.36 ?  232 LEU   A CG  1 1 
ATOM   1807 C CD1 . LEU   A 1 252 ? 114.381 4.892  0.291   1    23.6  ?  232 LEU   A CD1 1 1 
ATOM   1808 C CD2 . LEU   A 1 252 ? 112.747 6.832  -0.179  1    25.55 ?  232 LEU   A CD2 1 1 
ATOM   1809 N N   . LEU   A 1 253 ? 117.5   6.637  1.217   1    19.49 ?  233 LEU   A N   1 1 
ATOM   1810 C CA  . LEU   A 1 253 ? 118.606 7.218  0.472   1    20.24 ?  233 LEU   A CA  1 1 
ATOM   1811 C C   . LEU   A 1 253 ? 118.545 6.782  -0.957  1    20.64 ?  233 LEU   A C   1 1 
ATOM   1812 O O   . LEU   A 1 253 ? 118.592 5.594  -1.249  1    20.34 ?  233 LEU   A O   1 1 
ATOM   1813 C CB  . LEU   A 1 253 ? 119.865 6.758  1.163   1    22.43 ?  233 LEU   A CB  1 1 
ATOM   1814 C CG  . LEU   A 1 253 ? 121.196 7.055  0.544   1    24.96 ?  233 LEU   A CG  1 1 
ATOM   1815 C CD1 . LEU   A 1 253 ? 121.406 8.577  0.401   1    26.38 ?  233 LEU   A CD1 1 1 
ATOM   1816 C CD2 . LEU   A 1 253 ? 122.282 6.525  1.491   1    26.1  ?  233 LEU   A CD2 1 1 
ATOM   1817 N N   . LEU   A 1 254 ? 118.446 7.745  -1.871  1    20.5  ?  234 LEU   A N   1 1 
ATOM   1818 C CA  . LEU   A 1 254 ? 118.355 7.452  -3.306  1    20.68 ?  234 LEU   A CA  1 1 
ATOM   1819 C C   . LEU   A 1 254 ? 119.608 8.023  -3.942  1    20.94 ?  234 LEU   A C   1 1 
ATOM   1820 O O   . LEU   A 1 254 ? 119.958 9.19   -3.715  1    21.88 ?  234 LEU   A O   1 1 
ATOM   1821 C CB  . LEU   A 1 254 ? 117.115 8.149  -3.894  1    22    ?  234 LEU   A CB  1 1 
ATOM   1822 C CG  . LEU   A 1 254 ? 115.795 7.857  -3.191  1    24.52 ?  234 LEU   A CG  1 1 
ATOM   1823 C CD1 . LEU   A 1 254 ? 114.64  8.642  -3.86   1    26.21 ?  234 LEU   A CD1 1 1 
ATOM   1824 C CD2 . LEU   A 1 254 ? 115.48  6.336  -3.198  1    25.3  ?  234 LEU   A CD2 1 1 
ATOM   1825 N N   . GLN   A 1 255 ? 120.309 7.192  -4.745  1    20.03 ?  235 GLN   A N   1 1 
ATOM   1826 C CA  . GLN   A 1 255 ? 121.587 7.629  -5.316  1    19.9  ?  235 GLN   A CA  1 1 
ATOM   1827 C C   . GLN   A 1 255 ? 121.814 7.039  -6.722  1    20.83 ?  235 GLN   A C   1 1 
ATOM   1828 O O   . GLN   A 1 255 ? 121.543 5.844  -6.932  1    21    ?  235 GLN   A O   1 1 
ATOM   1829 C CB  . GLN   A 1 255 ? 122.696 7.077  -4.378  1    21.23 ?  235 GLN   A CB  1 1 
ATOM   1830 C CG  . GLN   A 1 255 ? 124.149 7.29   -4.875  1    21.34 ?  235 GLN   A CG  1 1 
ATOM   1831 C CD  . GLN   A 1 255 ? 124.548 8.749  -4.816  1    25.23 ?  235 GLN   A CD  1 1 
ATOM   1832 O OE1 . GLN   A 1 255 ? 124.308 9.478  -3.823  1    25.5  ?  235 GLN   A OE1 1 1 
ATOM   1833 N NE2 . GLN   A 1 255 ? 125.154 9.226  -5.896  1    27.37 ?  235 GLN   A NE2 1 1 
ATOM   1834 N N   . GLY   A 1 256 ? 122.329 7.86   -7.649  1    22    ?  236 GLY   A N   1 1 
ATOM   1835 C CA  . GLY   A 1 256 ? 122.661 7.379  -8.98   1    22.74 ?  236 GLY   A CA  1 1 
ATOM   1836 C C   . GLY   A 1 256 ? 124.07  6.829  -9.015  1    23.56 ?  236 GLY   A C   1 1 
ATOM   1837 O O   . GLY   A 1 256 ? 124.968 7.368  -8.357  1    24.82 ?  236 GLY   A O   1 1 
ATOM   1838 N N   . SER   A 1 257 ? 124.292 5.738  -9.794  1    23.69 ?  237 SER   A N   1 1 
ATOM   1839 C CA  . SER   A 1 257 ? 125.617 5.153  -9.832  1    24.77 ?  237 SER   A CA  1 1 
ATOM   1840 C C   . SER   A 1 257 ? 126.598 5.957  -10.657 1    27.63 ?  237 SER   A C   1 1 
ATOM   1841 O O   . SER   A 1 257 ? 127.809 5.758  -10.498 1    30.18 ?  237 SER   A O   1 1 
ATOM   1842 C CB  . SER   A 1 257 ? 125.55  3.725  -10.356 1    25.2  ?  237 SER   A CB  1 1 
ATOM   1843 O OG  . SER   A 1 257 ? 125.291 3.766  -11.751 1    28.59 ?  237 SER   A OG  1 1 
ATOM   1844 N N   . ALA   A 1 258 ? 126.11  6.844  -11.559 1    26.95 ?  238 ALA   A N   1 1 
ATOM   1845 C CA  . ALA   A 1 258 ? 127.001 7.613  -12.414 1    28.02 ?  238 ALA   A CA  1 1 
ATOM   1846 C C   . ALA   A 1 258 ? 127.01  9.111  -11.993 1    28.4  ?  238 ALA   A C   1 1 
ATOM   1847 O O   . ALA   A 1 258 ? 127.159 10.003 -12.814 1    30.83 ?  238 ALA   A O   1 1 
ATOM   1848 C CB  . ALA   A 1 258 ? 126.553 7.445  -13.86  1    29.03 ?  238 ALA   A CB  1 1 
ATOM   1849 N N   . ASP   A 1 259 ? 126.863 9.36   -10.694 1    26.24 ?  239 ASP   A N   1 1 
ATOM   1850 C CA  . ASP   A 1 259 ? 126.863 10.71  -10.154 1    26.83 ?  239 ASP   A CA  1 1 
ATOM   1851 C C   . ASP   A 1 259 ? 128.289 11.287 -10.156 1    28.77 ?  239 ASP   A C   1 1 
ATOM   1852 O O   . ASP   A 1 259 ? 129.163 10.764 -9.467  1    30.89 ?  239 ASP   A O   1 1 
ATOM   1853 C CB  . ASP   A 1 259 ? 126.253 10.635 -8.753  1    25.01 ?  239 ASP   A CB  1 1 
ATOM   1854 C CG  . ASP   A 1 259 ? 125.896 12.006 -8.177  1    26.02 ?  239 ASP   A CG  1 1 
ATOM   1855 O OD1 . ASP   A 1 259 ? 126.56  13.02  -8.565  1    25.35 ?  239 ASP   A OD1 1 1 
ATOM   1856 O OD2 . ASP   A 1 259 ? 124.982 12.071 -7.329  1    26.75 ?  239 ASP   A OD2 1 1 
ATOM   1857 N N   . ARG   A 1 260 ? 128.522 12.36  -10.927 1    28.95 ?  240 ARG   A N   1 1 
ATOM   1858 C CA  . ARG   A 1 260 ? 129.829 12.994 -10.962 1    30.73 ?  240 ARG   A CA  1 1 
ATOM   1859 C C   . ARG   A 1 260 ? 129.96  14.133 -9.95   1    31.47 ?  240 ARG   A C   1 1 
ATOM   1860 O O   . ARG   A 1 260 ? 131.03  14.73  -9.881  1    33.84 ?  240 ARG   A O   1 1 
ATOM   1861 C CB  . ARG   A 1 260 ? 130.151 13.526 -12.371 1    33.76 ?  240 ARG   A CB  1 1 
ATOM   1862 C CG  . ARG   A 1 260 ? 129.994 12.441 -13.437 1    41.64 ?  240 ARG   A CG  1 1 
ATOM   1863 C CD  . ARG   A 1 260 ? 131.303 12.142 -14.122 1    50.53 ?  240 ARG   A CD  1 1 
ATOM   1864 N NE  . ARG   A 1 260 ? 131.705 13.221 -15.021 1    58.04 ?  240 ARG   A NE  1 1 
ATOM   1865 C CZ  . ARG   A 1 260 ? 131.333 13.31  -16.296 1    63.18 ?  240 ARG   A CZ  1 1 
ATOM   1866 N NH1 . ARG   A 1 260 ? 131.746 14.325 -17.044 1    63.44 ?  240 ARG   A NH1 1 1 
ATOM   1867 N NH2 . ARG   A 1 260 ? 130.537 12.387 -16.832 1    63.85 ?  240 ARG   A NH2 1 1 
ATOM   1868 N N   . LEU   A 1 261 ? 128.906 14.443 -9.174  1    29.21 ?  241 LEU   A N   1 1 
ATOM   1869 C CA  . LEU   A 1 261 ? 128.929 15.534 -8.181  1    29.8  ?  241 LEU   A CA  1 1 
ATOM   1870 C C   . LEU   A 1 261 ? 129.093 14.988 -6.773  1    31.08 ?  241 LEU   A C   1 1 
ATOM   1871 O O   . LEU   A 1 261 ? 130.025 15.387 -6.074  1    32.59 ?  241 LEU   A O   1 1 
ATOM   1872 C CB  . LEU   A 1 261 ? 127.681 16.395 -8.336  1    30.21 ?  241 LEU   A CB  1 1 
ATOM   1873 C CG  . LEU   A 1 261 ? 127.724 17.239 -9.639  1    32.86 ?  241 LEU   A CG  1 1 
ATOM   1874 C CD1 . LEU   A 1 261 ? 126.465 18.007 -9.784  1    34.71 ?  241 LEU   A CD1 1 1 
ATOM   1875 C CD2 . LEU   A 1 261 ? 128.895 18.243 -9.594  1    34.76 ?  241 LEU   A CD2 1 1 
ATOM   1876 N N   . CYS   A 1 262 ? 128.191 14.097 -6.354  1    29.93 ?  242 CYS   A N   1 1 
ATOM   1877 C CA  . CYS   A 1 262 ? 128.253 13.388 -5.079  1    30.53 ?  242 CYS   A CA  1 1 
ATOM   1878 C C   . CYS   A 1 262 ? 128.572 11.97  -5.349  1    33.47 ?  242 CYS   A C   1 1 
ATOM   1879 O O   . CYS   A 1 262 ? 127.722 11.208 -5.835  1    32.81 ?  242 CYS   A O   1 1 
ATOM   1880 C CB  . CYS   A 1 262 ? 126.945 13.529 -4.327  1    29.92 ?  242 CYS   A CB  1 1 
ATOM   1881 S SG  . CYS   A 1 262 ? 126.646 15.223 -3.803  0.78 27.95 ?  242 CYS   A SG  1 1 
ATOM   1882 N N   . ASP   A 1 263 ? 129.807 11.585 -5.029  1    33.65 ?  243 ASP   A N   1 1 
ATOM   1883 C CA  . ASP   A 1 263 ? 130.26  10.241 -5.322  1    33.93 ?  243 ASP   A CA  1 1 
ATOM   1884 C C   . ASP   A 1 263 ? 129.412 9.19   -4.628  1    32.47 ?  243 ASP   A C   1 1 
ATOM   1885 O O   . ASP   A 1 263 ? 129.088 9.334  -3.451  1    31.6  ?  243 ASP   A O   1 1 
ATOM   1886 C CB  . ASP   A 1 263 ? 131.731 10.114 -4.971  1    37.05 ?  243 ASP   A CB  1 1 
ATOM   1887 C CG  . ASP   A 1 263 ? 132.345 8.936  -5.683  1    42.43 ?  243 ASP   A CG  1 1 
ATOM   1888 O OD1 . ASP   A 1 263 ? 132.749 9.094  -6.867  0.78 43.73 ?  243 ASP   A OD1 1 1 
ATOM   1889 O OD2 . ASP   A 1 263 ? 132.375 7.853  -5.093  0.97 40.8  ?  243 ASP   A OD2 1 1 
ATOM   1890 N N   . SER   A 1 264 ? 128.994 8.175  -5.381  1    31.82 ?  244 SER   A N   1 1 
ATOM   1891 C CA  . SER   A 1 264 ? 128.14  7.132  -4.828  1    32.33 ?  244 SER   A CA  1 1 
ATOM   1892 C C   . SER   A 1 264 ? 128.766 6.424  -3.616  1    31.98 ?  244 SER   A C   1 1 
ATOM   1893 O O   . SER   A 1 264 ? 128.031 5.908  -2.779  1    30.48 ?  244 SER   A O   1 1 
ATOM   1894 C CB  . SER   A 1 264 ? 127.751 6.134  -5.902  1    34.4  ?  244 SER   A CB  1 1 
ATOM   1895 O OG  . SER   A 1 264 ? 128.915 5.424  -6.302  1    36.39 ?  244 SER   A OG  1 1 
ATOM   1896 N N   . LYS   A 1 265 ? 130.102 6.475  -3.472  1    31.81 ?  245 LYS   A N   1 1 
ATOM   1897 C CA  . LYS   A 1 265 ? 130.774 5.914  -2.285  1    32.66 ?  245 LYS   A CA  1 1 
ATOM   1898 C C   . LYS   A 1 265 ? 130.249 6.551  -0.987  1    31.13 ?  245 LYS   A C   1 1 
ATOM   1899 O O   . LYS   A 1 265 ? 130.15  5.874  0.055   1    32.44 ?  245 LYS   A O   1 1 
ATOM   1900 C CB  . LYS   A 1 265 ? 132.292 6.109  -2.406  1    36.88 ?  245 LYS   A CB  1 1 
ATOM   1901 C CG  . LYS   A 1 265 ? 133.12  5.693  -1.187  1    45.89 ?  245 LYS   A CG  1 1 
ATOM   1902 C CD  . LYS   A 1 265 ? 134.555 6.259  -1.329  1    54.54 ?  245 LYS   A CD  1 1 
ATOM   1903 C CE  . LYS   A 1 265 ? 135.347 6.267  -0.046  1    60.83 ?  245 LYS   A CE  1 1 
ATOM   1904 N NZ  . LYS   A 1 265 ? 136.285 7.423  0.003   1    65.2  ?  245 LYS   A NZ  1 1 
ATOM   1905 N N   . GLY   A 1 266 ? 129.844 7.826  -1.068  1    28.32 ?  246 GLY   A N   1 1 
ATOM   1906 C CA  . GLY   A 1 266 ? 129.268 8.492  0.091   1    28.2  ?  246 GLY   A CA  1 1 
ATOM   1907 C C   . GLY   A 1 266 ? 127.95  7.884  0.522   1    27.15 ?  246 GLY   A C   1 1 
ATOM   1908 O O   . GLY   A 1 266 ? 127.7   7.775  1.721   1    27.33 ?  246 GLY   A O   1 1 
ATOM   1909 N N   . ALA   A 1 267 ? 127.1   7.456  -0.422  1    26.26 ?  247 ALA   A N   1 1 
ATOM   1910 C CA  . ALA   A 1 267 ? 125.817 6.867  -0.066  1    26.45 ?  247 ALA   A CA  1 1 
ATOM   1911 C C   . ALA   A 1 267 ? 126.073 5.507  0.636   1    26.81 ?  247 ALA   A C   1 1 
ATOM   1912 O O   . ALA   A 1 267 ? 125.402 5.193  1.616   1    27.33 ?  247 ALA   A O   1 1 
ATOM   1913 C CB  . ALA   A 1 267 ? 124.981 6.671  -1.329  1    26.84 ?  247 ALA   A CB  1 1 
ATOM   1914 N N   . TYR   A 1 268 ? 127.039 4.711  0.148   1    27.56 ?  248 TYR   A N   1 1 
ATOM   1915 C CA  . TYR   A 1 268 ? 127.355 3.424  0.793   1    28.61 ?  248 TYR   A CA  1 1 
ATOM   1916 C C   . TYR   A 1 268 ? 127.921 3.696  2.2     1    29.18 ?  248 TYR   A C   1 1 
ATOM   1917 O O   . TYR   A 1 268 ? 127.611 2.948  3.136   1    29.16 ?  248 TYR   A O   1 1 
ATOM   1918 C CB  . TYR   A 1 268 ? 128.345 2.62   -0.052  1    29.08 ?  248 TYR   A CB  1 1 
ATOM   1919 C CG  . TYR   A 1 268 ? 127.763 2.158  -1.381  1    29.82 ?  248 TYR   A CG  1 1 
ATOM   1920 C CD1 . TYR   A 1 268 ? 126.795 1.16   -1.435  1    30.8  ?  248 TYR   A CD1 1 1 
ATOM   1921 C CD2 . TYR   A 1 268 ? 128.211 2.685  -2.581  1    32.22 ?  248 TYR   A CD2 1 1 
ATOM   1922 C CE1 . TYR   A 1 268 ? 126.249 0.747  -2.65   1    30.86 ?  248 TYR   A CE1 1 1 
ATOM   1923 C CE2 . TYR   A 1 268 ? 127.673 2.278  -3.797  1    31.96 ?  248 TYR   A CE2 1 1 
ATOM   1924 C CZ  . TYR   A 1 268 ? 126.741 1.256  -3.831  1    31.95 ?  248 TYR   A CZ  1 1 
ATOM   1925 O OH  . TYR   A 1 268 ? 126.167 0.893  -5.035  1    33.07 ?  248 TYR   A OH  1 1 
ATOM   1926 N N   . LEU   A 1 269 ? 128.739 4.749  2.363   1    29.33 ?  249 LEU   A N   1 1 
ATOM   1927 C CA  . LEU   A 1 269 ? 129.317 5.129  3.653   1    31.32 ?  249 LEU   A CA  1 1 
ATOM   1928 C C   . LEU   A 1 269 ? 128.238 5.535  4.615   1    29.77 ?  249 LEU   A C   1 1 
ATOM   1929 O O   . LEU   A 1 269 ? 128.28  5.144  5.784   1    30.19 ?  249 LEU   A O   1 1 
ATOM   1930 C CB  . LEU   A 1 269 ? 130.321 6.277  3.488   1    35.04 ?  249 LEU   A CB  1 1 
ATOM   1931 C CG  . LEU   A 1 269 ? 131.766 5.88   3.726   1    42.73 ?  249 LEU   A CG  1 1 
ATOM   1932 C CD1 . LEU   A 1 269 ? 132.228 4.841  2.703   1    45.25 ?  249 LEU   A CD1 1 1 
ATOM   1933 C CD2 . LEU   A 1 269 ? 132.685 7.109  3.701   1    44.87 ?  249 LEU   A CD2 1 1 
ATOM   1934 N N   . LEU   A 1 270 ? 127.237 6.297  4.147   1    28.77 ?  250 LEU   A N   1 1 
ATOM   1935 C CA  . LEU   A 1 270 ? 126.125 6.692  5.008   1    28.64 ?  250 LEU   A CA  1 1 
ATOM   1936 C C   . LEU   A 1 270 ? 125.33  5.462  5.448   1    27.71 ?  250 LEU   A C   1 1 
ATOM   1937 O O   . LEU   A 1 270 ? 125.008 5.331  6.628   1    27.38 ?  250 LEU   A O   1 1 
ATOM   1938 C CB  . LEU   A 1 270 ? 125.23  7.641  4.21    1    29.61 ?  250 LEU   A CB  1 1 
ATOM   1939 C CG  . LEU   A 1 270 ? 123.893 8.038  4.819   1    31.93 ?  250 LEU   A CG  1 1 
ATOM   1940 C CD1 . LEU   A 1 270 ? 124.045 8.639  6.222   1    32.53 ?  250 LEU   A CD1 1 1 
ATOM   1941 C CD2 . LEU   A 1 270 ? 123.249 9.127  3.923   1    32.48 ?  250 LEU   A CD2 1 1 
ATOM   1942 N N   . MET   A 1 271 ? 125.063 4.5    4.519   1    27.02 ?  251 MET   A N   1 1 
ATOM   1943 C CA  . MET   A 1 271 ? 124.362 3.276  4.921   1    27.89 ?  251 MET   A CA  1 1 
ATOM   1944 C C   . MET   A 1 271 ? 125.158 2.508  5.942   1    28.79 ?  251 MET   A C   1 1 
ATOM   1945 O O   . MET   A 1 271 ? 124.555 1.884  6.811   1    29.32 ?  251 MET   A O   1 1 
ATOM   1946 C CB  . MET   A 1 271 ? 124.125 2.342  3.72    1    28.53 ?  251 MET   A CB  1 1 
ATOM   1947 C CG  . MET   A 1 271 ? 123.052 2.841  2.821   1    30.19 ?  251 MET   A CG  1 1 
ATOM   1948 S SD  . MET   A 1 271 ? 121.45  2.836  3.637   1    29.42 ?  251 MET   A SD  1 1 
ATOM   1949 C CE  . MET   A 1 271 ? 120.989 0.996  3.676   1    29.39 ?  251 MET   A CE  1 1 
ATOM   1950 N N   . GLU   A 1 272 ? 126.495 2.48   5.813   1    26.99 ?  252 GLU   A N   1 1 
ATOM   1951 C CA  . GLU   A 1 272 ? 127.312 1.726  6.753   1    27.27 ?  252 GLU   A CA  1 1 
ATOM   1952 C C   . GLU   A 1 272 ? 127.496 2.386  8.117   1    29.04 ?  252 GLU   A C   1 1 
ATOM   1953 O O   . GLU   A 1 272 ? 127.362 1.724  9.162   1    30.67 ?  252 GLU   A O   1 1 
ATOM   1954 C CB  . GLU   A 1 272 ? 128.677 1.47   6.113   1    28.75 ?  252 GLU   A CB  1 1 
ATOM   1955 C CG  . GLU   A 1 272 ? 129.504 0.512  6.954   1    37.2  ?  252 GLU   A CG  1 1 
ATOM   1956 C CD  . GLU   A 1 272 ? 130.977 0.489  6.608   1    52.42 ?  252 GLU   A CD  1 1 
ATOM   1957 O OE1 . GLU   A 1 272 ? 131.336 0.92   5.489   1    54.75 ?  252 GLU   A OE1 1 1 
ATOM   1958 O OE2 . GLU   A 1 272 ? 131.775 0.024  7.453   1    58.5  ?  252 GLU   A OE2 1 1 
ATOM   1959 N N   . LEU   A 1 273 ? 127.74  3.706  8.119   1    27.63 ?  253 LEU   A N   1 1 
ATOM   1960 C CA  . LEU   A 1 273 ? 128.096 4.367  9.381   1    29.14 ?  253 LEU   A CA  1 1 
ATOM   1961 C C   . LEU   A 1 273 ? 126.946 4.918  10.198  1    30.71 ?  253 LEU   A C   1 1 
ATOM   1962 O O   . LEU   A 1 273 ? 127.1   4.984  11.421  1    33.61 ?  253 LEU   A O   1 1 
ATOM   1963 C CB  . LEU   A 1 273 ? 129.151 5.472  9.141   1    31.1  ?  253 LEU   A CB  1 1 
ATOM   1964 C CG  . LEU   A 1 273 ? 130.434 4.947  8.477   1    36.13 ?  253 LEU   A CG  1 1 
ATOM   1965 C CD1 . LEU   A 1 273 ? 131.344 6.071  8.074   1    38.83 ?  253 LEU   A CD1 1 1 
ATOM   1966 C CD2 . LEU   A 1 273 ? 131.177 3.971  9.397   1    38.45 ?  253 LEU   A CD2 1 1 
ATOM   1967 N N   . ALA   A 1 274 ? 125.783 5.25   9.588   1    29.1  ?  254 ALA   A N   1 1 
ATOM   1968 C CA  . ALA   A 1 274 ? 124.646 5.72   10.377  1    30.41 ?  254 ALA   A CA  1 1 
ATOM   1969 C C   . ALA   A 1 274 ? 124.184 4.626  11.357  1    31.82 ?  254 ALA   A C   1 1 
ATOM   1970 O O   . ALA   A 1 274 ? 124.197 3.438  11.013  1    32.24 ?  254 ALA   A O   1 1 
ATOM   1971 C CB  . ALA   A 1 274 ? 123.48  6.078  9.459   1    30.52 ?  254 ALA   A CB  1 1 
ATOM   1972 N N   . LYS   A 1 275 ? 123.737 5.03   12.54   1    32.36 ?  255 LYS   A N   1 1 
ATOM   1973 C CA  A LYS   A 1 275 ? 123.245 4.049  13.519  0.5  33.41 ?  255 LYS   A CA  1 1 
ATOM   1974 C CA  B LYS   A 1 275 ? 123.246 4.056  13.523  0.5  33.39 ?  255 LYS   A CA  1 1 
ATOM   1975 C C   . LYS   A 1 275 ? 121.756 3.765  13.387  1    32.36 ?  255 LYS   A C   1 1 
ATOM   1976 O O   . LYS   A 1 275 ? 121.243 2.891  14.087  1    32.55 ?  255 LYS   A O   1 1 
ATOM   1977 C CB  A LYS   A 1 275 ? 123.604 4.439  14.963  0.5  36.43 ?  255 LYS   A CB  1 1 
ATOM   1978 C CB  B LYS   A 1 275 ? 123.603 4.474  14.957  0.5  36.31 ?  255 LYS   A CB  1 1 
ATOM   1979 C CG  A LYS   A 1 275 ? 125.105 4.437  15.233  0.5  41.62 ?  255 LYS   A CG  1 1 
ATOM   1980 C CG  B LYS   A 1 275 ? 125.072 4.854  15.11   0.5  41.28 ?  255 LYS   A CG  1 1 
ATOM   1981 C CD  A LYS   A 1 275 ? 125.76  3.083  15.03   0.5  46.85 ?  255 LYS   A CD  1 1 
ATOM   1982 C CD  B LYS   A 1 275 ? 126.05  3.733  14.758  0.5  45.42 ?  255 LYS   A CD  1 1 
ATOM   1983 C CE  A LYS   A 1 275 ? 127.2   3.103  15.474  0.5  51.17 ?  255 LYS   A CE  1 1 
ATOM   1984 C CE  B LYS   A 1 275 ? 127.483 4.193  14.854  0.5  49.47 ?  255 LYS   A CE  1 1 
ATOM   1985 N NZ  A LYS   A 1 275 ? 127.31  3.361  16.935  0.5  54.1  ?  255 LYS   A NZ  1 1 
ATOM   1986 N NZ  B LYS   A 1 275 ? 128.275 3.839  13.647  0.5  51.1  ?  255 LYS   A NZ  1 1 
ATOM   1987 N N   . SER   A 1 276 ? 121.063 4.485  12.472  1    29.28 ?  256 SER   A N   1 1 
ATOM   1988 C CA  A SER   A 1 276 ? 119.632 4.345  12.268  0.85 27.8  ?  256 SER   A CA  1 1 
ATOM   1989 C CA  B SER   A 1 276 ? 119.635 4.331  12.238  0.15 28.13 ?  256 SER   A CA  1 1 
ATOM   1990 C C   . SER   A 1 276 ? 119.172 2.873  12.158  1    27.3  ?  256 SER   A C   1 1 
ATOM   1991 O O   . SER   A 1 276 ? 119.727 2.104  11.376  1    28.38 ?  256 SER   A O   1 1 
ATOM   1992 C CB  A SER   A 1 276 ? 119.222 5.064  10.989  0.85 27.11 ?  256 SER   A CB  1 1 
ATOM   1993 C CB  B SER   A 1 276 ? 119.259 5.033  10.94   0.15 28.36 ?  256 SER   A CB  1 1 
ATOM   1994 O OG  A SER   A 1 276 ? 119.715 6.4    11.012  0.85 28.71 ?  256 SER   A OG  1 1 
ATOM   1995 O OG  B SER   A 1 276 ? 117.879 4.892  10.657  0.15 29.25 ?  256 SER   A OG  1 1 
ATOM   1996 N N   . GLN   A 1 277 ? 118.118 2.533  12.878  1    26.11 ?  257 GLN   A N   1 1 
ATOM   1997 C CA  . GLN   A 1 277 ? 117.546 1.18   12.795  1    27.56 ?  257 GLN   A CA  1 1 
ATOM   1998 C C   . GLN   A 1 277 ? 116.657 1.021  11.535  1    27.11 ?  257 GLN   A C   1 1 
ATOM   1999 O O   . GLN   A 1 277 ? 116.39  -0.127 11.124  1    28.29 ?  257 GLN   A O   1 1 
ATOM   2000 C CB  . GLN   A 1 277 ? 116.755 0.851  14.062  1    31.16 ?  257 GLN   A CB  1 1 
ATOM   2001 C CG  . GLN   A 1 277 ? 117.69  0.634  15.242  1    36.29 ?  257 GLN   A CG  1 1 
ATOM   2002 C CD  . GLN   A 1 277 ? 118.431 -0.697 15.202  1    44.18 ?  257 GLN   A CD  1 1 
ATOM   2003 O OE1 . GLN   A 1 277 ? 119.599 -0.797 15.6    1    48.55 ?  257 GLN   A OE1 1 1 
ATOM   2004 N NE2 . GLN   A 1 277 ? 117.781 -1.77  14.746  1    42.29 ?  257 GLN   A NE2 1 1 
ATOM   2005 N N   . ASP   A 1 278 ? 116.281 2.158  10.866  1    26.37 ?  258 ASP   A N   1 1 
ATOM   2006 C CA  . ASP   A 1 278 ? 115.456 2.056  9.686   1    25.74 ?  258 ASP   A CA  1 1 
ATOM   2007 C C   . ASP   A 1 278 ? 116.164 2.796  8.571   1    23.46 ?  258 ASP   A C   1 1 
ATOM   2008 O O   . ASP   A 1 278 ? 116.075 4.019  8.508   1    23.5  ?  258 ASP   A O   1 1 
ATOM   2009 C CB  . ASP   A 1 278 ? 114.094 2.638  10.007  1    27.61 ?  258 ASP   A CB  1 1 
ATOM   2010 C CG  . ASP   A 1 278 ? 113.108 2.694  8.852   1    30.33 ?  258 ASP   A CG  1 1 
ATOM   2011 O OD1 . ASP   A 1 278 ? 113.394 2.071  7.762   1    29.22 ?  258 ASP   A OD1 1 1 
ATOM   2012 O OD2 . ASP   A 1 278 ? 112.065 3.377  9.014   1    32.38 ?  258 ASP   A OD2 1 1 
ATOM   2013 N N   . LYS   A 1 279 ? 116.939 2.068  7.762   1    22.8  ?  259 LYS   A N   1 1 
ATOM   2014 C CA  . LYS   A 1 279 ? 117.693 2.686  6.673   1    23.23 ?  259 LYS   A CA  1 1 
ATOM   2015 C C   . LYS   A 1 279 ? 117.619 1.86   5.401   1    22.66 ?  259 LYS   A C   1 1 
ATOM   2016 O O   . LYS   A 1 279 ? 117.791 0.643  5.429   1    22.9  ?  259 LYS   A O   1 1 
ATOM   2017 C CB  . LYS   A 1 279 ? 119.147 3.01   7.046   1    25.61 ?  259 LYS   A CB  1 1 
ATOM   2018 C CG  . LYS   A 1 279 ? 119.887 1.914  7.777   1    28.75 ?  259 LYS   A CG  1 1 
ATOM   2019 C CD  . LYS   A 1 279 ? 121.269 2.417  8.235   1    30.69 ?  259 LYS   A CD  1 1 
ATOM   2020 C CE  . LYS   A 1 279 ? 121.96  1.273  8.94    1    29.37 ?  259 LYS   A CE  1 1 
ATOM   2021 N NZ  . LYS   A 1 279 ? 123.404 1.547  9.23    1    29.35 ?  259 LYS   A NZ  1 1 
ATOM   2022 N N   . THR   A 1 280 ? 117.385 2.533  4.268   1    21.47 ?  260 THR   A N   1 1 
ATOM   2023 C CA  . THR   A 1 280 ? 117.194 1.879  2.996   1    21.87 ?  260 THR   A CA  1 1 
ATOM   2024 C C   . THR   A 1 280 ? 117.93  2.666  1.948   1    21.24 ?  260 THR   A C   1 1 
ATOM   2025 O O   . THR   A 1 280 ? 117.823 3.905  1.949   1    21.92 ?  260 THR   A O   1 1 
ATOM   2026 C CB  . THR   A 1 280 ? 115.695 1.907  2.631   1    25.92 ?  260 THR   A CB  1 1 
ATOM   2027 O OG1 . THR   A 1 280 ? 114.948 1.296  3.682   1    29.18 ?  260 THR   A OG1 1 1 
ATOM   2028 C CG2 . THR   A 1 280 ? 115.382 1.187  1.282   1    27.83 ?  260 THR   A CG2 1 1 
ATOM   2029 N N   . LEU   A 1 281 ? 118.571 1.98   1.032   1    20.32 ?  261 LEU   A N   1 1 
ATOM   2030 C CA  . LEU   A 1 281 ? 119.294 2.548  -0.105  1    20.88 ?  261 LEU   A CA  1 1 
ATOM   2031 C C   . LEU   A 1 281 ? 118.745 2.031  -1.397  1    21.2  ?  261 LEU   A C   1 1 
ATOM   2032 O O   . LEU   A 1 281 ? 118.598 0.808  -1.557  1    20.41 ?  261 LEU   A O   1 1 
ATOM   2033 C CB  . LEU   A 1 281 ? 120.801 2.191  -0.009  1    22.62 ?  261 LEU   A CB  1 1 
ATOM   2034 C CG  . LEU   A 1 281 ? 121.68  2.448  -1.258  1    23.97 ?  261 LEU   A CG  1 1 
ATOM   2035 C CD1 . LEU   A 1 281 ? 121.773 3.987  -1.615  1    25.22 ?  261 LEU   A CD1 1 1 
ATOM   2036 C CD2 . LEU   A 1 281 ? 123.105 1.927  -1.022  1    26.53 ?  261 LEU   A CD2 1 1 
ATOM   2037 N N   . LYS   A 1 282 ? 118.463 2.91   -2.358  1    21.3  ?  262 LYS   A N   1 1 
ATOM   2038 C CA  . LYS   A 1 282 ? 118.072 2.487  -3.682  1    22.01 ?  262 LYS   A CA  1 1 
ATOM   2039 C C   . LYS   A 1 282 ? 119.06  3.117  -4.633  1    22.4  ?  262 LYS   A C   1 1 
ATOM   2040 O O   . LYS   A 1 282 ? 119.28  4.353  -4.551  1    21.18 ?  262 LYS   A O   1 1 
ATOM   2041 C CB  . LYS   A 1 282 ? 116.624 2.878  -4.005  1    22.84 ?  262 LYS   A CB  1 1 
ATOM   2042 C CG  . LYS   A 1 282 ? 116.191 2.332  -5.353  1    28.43 ?  262 LYS   A CG  1 1 
ATOM   2043 C CD  . LYS   A 1 282 ? 114.664 2.383  -5.449  1    32.95 ?  262 LYS   A CD  1 1 
ATOM   2044 C CE  . LYS   A 1 282 ? 114.144 2.077  -6.822  1    36.62 ?  262 LYS   A CE  1 1 
ATOM   2045 N NZ  . LYS   A 1 282 ? 114.049 0.614  -7.011  1    37.21 ?  262 LYS   A NZ  1 1 
ATOM   2046 N N   . ILE   A 1 283 ? 119.742 2.296  -5.438  1    22.55 ?  263 ILE   A N   1 1 
ATOM   2047 C CA  . ILE   A 1 283 ? 120.724 2.75   -6.422  1    22.49 ?  263 ILE   A CA  1 1 
ATOM   2048 C C   . ILE   A 1 283 ? 120.061 2.744  -7.767  1    23.64 ?  263 ILE   A C   1 1 
ATOM   2049 O O   . ILE   A 1 283 ? 119.428 1.745  -8.164  1    24.78 ?  263 ILE   A O   1 1 
ATOM   2050 C CB  . ILE   A 1 283 ? 121.978 1.82   -6.435  1    24.27 ?  263 ILE   A CB  1 1 
ATOM   2051 C CG1 . ILE   A 1 283 ? 122.794 1.935  -5.126  1    24.7  ?  263 ILE   A CG1 1 1 
ATOM   2052 C CG2 . ILE   A 1 283 ? 122.878 2.115  -7.676  1    24.9  ?  263 ILE   A CG2 1 1 
ATOM   2053 C CD1 . ILE   A 1 283 ? 123.621 3.26   -4.989  1    27.12 ?  263 ILE   A CD1 1 1 
ATOM   2054 N N   . TYR   A 1 284 ? 120.276 3.844  -8.536  1    22.05 ?  264 TYR   A N   1 1 
ATOM   2055 C CA  . TYR   A 1 284 ? 119.745 3.947  -9.914  1    23.17 ?  264 TYR   A CA  1 1 
ATOM   2056 C C   . TYR   A 1 284 ? 120.926 3.813  -10.863 1    23.78 ?  264 TYR   A C   1 1 
ATOM   2057 O O   . TYR   A 1 284 ? 121.773 4.712  -10.983 1    24.37 ?  264 TYR   A O   1 1 
ATOM   2058 C CB  . TYR   A 1 284 ? 119.005 5.296  -10.109 1    23.54 ?  264 TYR   A CB  1 1 
ATOM   2059 C CG  . TYR   A 1 284 ? 117.686 5.322  -9.383  1    23.06 ?  264 TYR   A CG  1 1 
ATOM   2060 C CD1 . TYR   A 1 284 ? 116.542 4.806  -9.975  1    25.09 ?  264 TYR   A CD1 1 1 
ATOM   2061 C CD2 . TYR   A 1 284 ? 117.606 5.735  -8.06   1    23.93 ?  264 TYR   A CD2 1 1 
ATOM   2062 C CE1 . TYR   A 1 284 ? 115.321 4.824  -9.315  1    25.81 ?  264 TYR   A CE1 1 1 
ATOM   2063 C CE2 . TYR   A 1 284 ? 116.396 5.726  -7.373  1    24.34 ?  264 TYR   A CE2 1 1 
ATOM   2064 C CZ  . TYR   A 1 284 ? 115.259 5.251  -8.004  1    25.56 ?  264 TYR   A CZ  1 1 
ATOM   2065 O OH  . TYR   A 1 284 ? 114.05  5.286  -7.362  1    27.58 ?  264 TYR   A OH  1 1 
ATOM   2066 N N   . GLU   A 1 285 ? 121.007 2.631  -11.51  1    23.74 ?  265 GLU   A N   1 1 
ATOM   2067 C CA  . GLU   A 1 285 ? 122.141 2.308  -12.325 1    24.71 ?  265 GLU   A CA  1 1 
ATOM   2068 C C   . GLU   A 1 285 ? 122.222 3.225  -13.551 1    26.51 ?  265 GLU   A C   1 1 
ATOM   2069 O O   . GLU   A 1 285 ? 121.265 3.293  -14.321 1    28.38 ?  265 GLU   A O   1 1 
ATOM   2070 C CB  . GLU   A 1 285 ? 122.004 0.826  -12.75  1    26.89 ?  265 GLU   A CB  1 1 
ATOM   2071 C CG  . GLU   A 1 285 ? 123.274 0.251  -13.336 1    30.75 ?  265 GLU   A CG  1 1 
ATOM   2072 C CD  . GLU   A 1 285 ? 124.48  0.251  -12.411 1    37.1  ?  265 GLU   A CD  1 1 
ATOM   2073 O OE1 . GLU   A 1 285 ? 124.338 0.333  -11.158 1    32.63 ?  265 GLU   A OE1 1 1 
ATOM   2074 O OE2 . GLU   A 1 285 ? 125.598 0.151  -12.971 1    40.61 ?  265 GLU   A OE2 1 1 
ATOM   2075 N N   . GLY   A 1 286 ? 123.354 3.888  -13.722 1    26.12 ?  266 GLY   A N   1 1 
ATOM   2076 C CA  . GLY   A 1 286 ? 123.594 4.786  -14.84  1    25.8  ?  266 GLY   A CA  1 1 
ATOM   2077 C C   . GLY   A 1 286 ? 123.1   6.221  -14.643 1    25.02 ?  266 GLY   A C   1 1 
ATOM   2078 O O   . GLY   A 1 286 ? 123.389 7.083  -15.493 1    25.7  ?  266 GLY   A O   1 1 
ATOM   2079 N N   . ALA   A 1 287 ? 122.314 6.45   -13.575 1    24.9  ?  267 ALA   A N   1 1 
ATOM   2080 C CA  . ALA   A 1 287 ? 121.747 7.792  -13.383 1    24.49 ?  267 ALA   A CA  1 1 
ATOM   2081 C C   . ALA   A 1 287 ? 122.736 8.806  -12.899 1    24.62 ?  267 ALA   A C   1 1 
ATOM   2082 O O   . ALA   A 1 287 ? 123.71  8.494  -12.202 1    24.25 ?  267 ALA   A O   1 1 
ATOM   2083 C CB  . ALA   A 1 287 ? 120.534 7.726  -12.469 1    23.88 ?  267 ALA   A CB  1 1 
ATOM   2084 N N   . TYR   A 1 288 ? 122.462 10.067 -13.26  1    23.98 ?  268 TYR   A N   1 1 
ATOM   2085 C CA  . TYR   A 1 288 ? 123.316 11.154 -12.857 1    24.2  ?  268 TYR   A CA  1 1 
ATOM   2086 C C   . TYR   A 1 288 ? 122.85  11.734 -11.511 1    24.66 ?  268 TYR   A C   1 1 
ATOM   2087 O O   . TYR   A 1 288 ? 122.142 11.066 -10.783 1    25.84 ?  268 TYR   A O   1 1 
ATOM   2088 C CB  . TYR   A 1 288 ? 123.326 12.193 -13.967 1    25.34 ?  268 TYR   A CB  1 1 
ATOM   2089 C CG  . TYR   A 1 288 ? 124.09  11.852 -15.219 1    26.08 ?  268 TYR   A CG  1 1 
ATOM   2090 C CD1 . TYR   A 1 288 ? 124.592 10.569 -15.441 1    27.37 ?  268 TYR   A CD1 1 1 
ATOM   2091 C CD2 . TYR   A 1 288 ? 124.317 12.815 -16.188 1    27.9  ?  268 TYR   A CD2 1 1 
ATOM   2092 C CE1 . TYR   A 1 288 ? 125.25  10.254 -16.634 1    28.54 ?  268 TYR   A CE1 1 1 
ATOM   2093 C CE2 . TYR   A 1 288 ? 124.989 12.52  -17.357 1    30.08 ?  268 TYR   A CE2 1 1 
ATOM   2094 C CZ  . TYR   A 1 288 ? 125.46  11.244 -17.575 1    31.35 ?  268 TYR   A CZ  1 1 
ATOM   2095 O OH  . TYR   A 1 288 ? 126.088 10.999 -18.777 1    34.24 ?  268 TYR   A OH  1 1 
ATOM   2096 N N   . HIS   A 1 289 ? 123.312 12.916 -11.168 1    23.34 ?  269 HIS   A N   1 1 
ATOM   2097 C CA  . HIS   A 1 289 ? 123.059 13.502 -9.846  1    21.97 ?  269 HIS   A CA  1 1 
ATOM   2098 C C   . HIS   A 1 289 ? 121.603 13.764 -9.494  1    21.63 ?  269 HIS   A C   1 1 
ATOM   2099 O O   . HIS   A 1 289 ? 121.152 13.469 -8.365  1    21.94 ?  269 HIS   A O   1 1 
ATOM   2100 C CB  . HIS   A 1 289 ? 123.873 14.813 -9.767  1    22.3  ?  269 HIS   A CB  1 1 
ATOM   2101 C CG  . HIS   A 1 289 ? 123.908 15.445 -8.405  1    21.86 ?  269 HIS   A CG  1 1 
ATOM   2102 N ND1 . HIS   A 1 289 ? 124.263 14.709 -7.289  1    23.37 ?  269 HIS   A ND1 1 1 
ATOM   2103 C CD2 . HIS   A 1 289 ? 123.683 16.734 -8.03   1    21.94 ?  269 HIS   A CD2 1 1 
ATOM   2104 C CE1 . HIS   A 1 289 ? 124.245 15.555 -6.26   1    23.18 ?  269 HIS   A CE1 1 1 
ATOM   2105 N NE2 . HIS   A 1 289 ? 123.891 16.786 -6.662  1    21.93 ?  269 HIS   A NE2 1 1 
ATOM   2106 N N   . VAL   A 1 290 ? 120.872 14.45  -10.386 1    20.29 ?  270 VAL   A N   1 1 
ATOM   2107 C CA  . VAL   A 1 290 ? 119.563 14.998 -9.993  1    20.59 ?  270 VAL   A CA  1 1 
ATOM   2108 C C   . VAL   A 1 290 ? 118.475 14.032 -10.306 1    22.15 ?  270 VAL   A C   1 1 
ATOM   2109 O O   . VAL   A 1 290 ? 117.778 14.128 -11.316 1    22.86 ?  270 VAL   A O   1 1 
ATOM   2110 C CB  . VAL   A 1 290 ? 119.366 16.391 -10.656 1    20.61 ?  270 VAL   A CB  1 1 
ATOM   2111 C CG1 . VAL   A 1 290 ? 118.137 17.055 -10.043 1    21.32 ?  270 VAL   A CG1 1 1 
ATOM   2112 C CG2 . VAL   A 1 290 ? 120.606 17.282 -10.412 1    20.35 ?  270 VAL   A CG2 1 1 
ATOM   2113 N N   . LEU   A 1 291 ? 118.293 13.056 -9.402  1    21.32 ?  271 LEU   A N   1 1 
ATOM   2114 C CA  . LEU   A 1 291 ? 117.408 11.919 -9.673  1    21.69 ?  271 LEU   A CA  1 1 
ATOM   2115 C C   . LEU   A 1 291 ? 115.959 12.287 -9.848  1    22.7  ?  271 LEU   A C   1 1 
ATOM   2116 O O   . LEU   A 1 291 ? 115.249 11.581 -10.587 1    23.46 ?  271 LEU   A O   1 1 
ATOM   2117 C CB  . LEU   A 1 291 ? 117.525 10.909 -8.517  1    21.59 ?  271 LEU   A CB  1 1 
ATOM   2118 C CG  . LEU   A 1 291 ? 118.916 10.343 -8.283  1    23    ?  271 LEU   A CG  1 1 
ATOM   2119 C CD1 . LEU   A 1 291 ? 118.884 9.373  -7.065  1    23.04 ?  271 LEU   A CD1 1 1 
ATOM   2120 C CD2 . LEU   A 1 291 ? 119.395 9.575  -9.502  1    24.28 ?  271 LEU   A CD2 1 1 
ATOM   2121 N N   . HIS   A 1 292 ? 115.505 13.364 -9.196  1    22.11 ?  272 HIS   A N   1 1 
ATOM   2122 C CA  . HIS   A 1 292 ? 114.092 13.768 -9.34   1    22    ?  272 HIS   A CA  1 1 
ATOM   2123 C C   . HIS   A 1 292 ? 113.866 14.638 -10.613 1    23.43 ?  272 HIS   A C   1 1 
ATOM   2124 O O   . HIS   A 1 292 ? 112.768 15.113 -10.855 1    24.52 ?  272 HIS   A O   1 1 
ATOM   2125 C CB  . HIS   A 1 292 ? 113.604 14.516 -8.098  1    21.77 ?  272 HIS   A CB  1 1 
ATOM   2126 C CG  . HIS   A 1 292 ? 114.518 15.642 -7.731  1    21.68 ?  272 HIS   A CG  1 1 
ATOM   2127 N ND1 . HIS   A 1 292 ? 115.839 15.417 -7.318  1    22.02 ?  272 HIS   A ND1 1 1 
ATOM   2128 C CD2 . HIS   A 1 292 ? 114.293 16.981 -7.73   1    24.34 ?  272 HIS   A CD2 1 1 
ATOM   2129 C CE1 . HIS   A 1 292 ? 116.349 16.616 -7.086  1    23.95 ?  272 HIS   A CE1 1 1 
ATOM   2130 N NE2 . HIS   A 1 292 ? 115.453 17.575 -7.289  1    25.7  ?  272 HIS   A NE2 1 1 
ATOM   2131 N N   . LYS   A 1 293 ? 114.93  14.83  -11.405 1    21.76 ?  273 LYS   A N   1 1 
ATOM   2132 C CA  . LYS   A 1 293 ? 114.862 15.533 -12.697 1    21.92 ?  273 LYS   A CA  1 1 
ATOM   2133 C C   . LYS   A 1 293 ? 115.704 14.775 -13.739 1    23.26 ?  273 LYS   A C   1 1 
ATOM   2134 O O   . LYS   A 1 293 ? 116.419 15.385 -14.537 1    25.22 ?  273 LYS   A O   1 1 
ATOM   2135 C CB  . LYS   A 1 293 ? 115.364 16.954 -12.537 1    23.17 ?  273 LYS   A CB  1 1 
ATOM   2136 C CG  . LYS   A 1 293 ? 114.385 17.718 -11.629 1    26.57 ?  273 LYS   A CG  1 1 
ATOM   2137 C CD  . LYS   A 1 293 ? 114.396 19.135 -11.677 1    32.64 ?  273 LYS   A CD  1 1 
ATOM   2138 C CE  . LYS   A 1 293 ? 113.499 19.724 -10.605 1    30    ?  273 LYS   A CE  1 1 
ATOM   2139 N NZ  . LYS   A 1 293 ? 112.06  19.759 -11.016 1    28.72 ?  273 LYS   A NZ  1 1 
ATOM   2140 N N   . GLU   A 1 294 ? 115.624 13.435 -13.7   1    22.96 ?  274 GLU   A N   1 1 
ATOM   2141 C CA  . GLU   A 1 294 ? 116.397 12.54  -14.54  1    22.96 ?  274 GLU   A CA  1 1 
ATOM   2142 C C   . GLU   A 1 294 ? 115.511 11.998 -15.675 1    25.47 ?  274 GLU   A C   1 1 
ATOM   2143 O O   . GLU   A 1 294 ? 114.487 12.6   -15.992 1    26.65 ?  274 GLU   A O   1 1 
ATOM   2144 C CB  . GLU   A 1 294 ? 116.981 11.411 -13.624 1    24.45 ?  274 GLU   A CB  1 1 
ATOM   2145 C CG  . GLU   A 1 294 ? 118.51  11.442 -13.619 1    25.31 ?  274 GLU   A CG  1 1 
ATOM   2146 C CD  . GLU   A 1 294 ? 119.131 10.709 -14.801 1    26.56 ?  274 GLU   A CD  1 1 
ATOM   2147 O OE1 . GLU   A 1 294 ? 118.421 9.908  -15.441 1    27.22 ?  274 GLU   A OE1 1 1 
ATOM   2148 O OE2 . GLU   A 1 294 ? 120.313 10.968 -15.113 1    28.79 ?  274 GLU   A OE2 1 1 
ATOM   2149 N N   . LEU   A 1 295 ? 115.882 10.874 -16.294 1    26.31 ?  275 LEU   A N   1 1 
ATOM   2150 C CA  . LEU   A 1 295 ? 115.047 10.295 -17.358 1    26.95 ?  275 LEU   A CA  1 1 
ATOM   2151 C C   . LEU   A 1 295 ? 113.709 9.911  -16.735 1    29.18 ?  275 LEU   A C   1 1 
ATOM   2152 O O   . LEU   A 1 295 ? 113.647 9.571  -15.535 1    29.29 ?  275 LEU   A O   1 1 
ATOM   2153 C CB  . LEU   A 1 295 ? 115.75  9.056  -17.962 1    27.51 ?  275 LEU   A CB  1 1 
ATOM   2154 C CG  . LEU   A 1 295 ? 117.099 9.345  -18.6   1    29.52 ?  275 LEU   A CG  1 1 
ATOM   2155 C CD1 . LEU   A 1 295 ? 117.693 8.067  -19.17  1    31.23 ?  275 LEU   A CD1 1 1 
ATOM   2156 C CD2 . LEU   A 1 295 ? 116.979 10.384 -19.748 1    30.01 ?  275 LEU   A CD2 1 1 
ATOM   2157 N N   . PRO   A 1 296 ? 112.62  10.032 -17.485 1    31.6  ?  276 PRO   A N   1 1 
ATOM   2158 C CA  . PRO   A 1 296 ? 111.302 9.696  -16.935 1    33.31 ?  276 PRO   A CA  1 1 
ATOM   2159 C C   . PRO   A 1 296 ? 111.209 8.4    -16.143 1    34.26 ?  276 PRO   A C   1 1 
ATOM   2160 O O   . PRO   A 1 296 ? 110.583 8.42   -15.099 1    35.8  ?  276 PRO   A O   1 1 
ATOM   2161 C CB  . PRO   A 1 296 ? 110.401 9.661  -18.185 1    35.27 ?  276 PRO   A CB  1 1 
ATOM   2162 C CG  . PRO   A 1 296 ? 111.045 10.613 -19.104 1    35.99 ?  276 PRO   A CG  1 1 
ATOM   2163 C CD  . PRO   A 1 296 ? 112.522 10.479 -18.896 1    32.69 ?  276 PRO   A CD  1 1 
ATOM   2164 N N   . GLU   A 1 297 ? 111.821 7.28   -16.589 1    32.49 ?  277 GLU   A N   1 1 
ATOM   2165 C CA  . GLU   A 1 297 ? 111.746 6.026  -15.837 1    33.8  ?  277 GLU   A CA  1 1 
ATOM   2166 C C   . GLU   A 1 297 ? 112.387 6.171  -14.456 1    33.24 ?  277 GLU   A C   1 1 
ATOM   2167 O O   . GLU   A 1 297 ? 111.898 5.561  -13.505 1    35.13 ?  277 GLU   A O   1 1 
ATOM   2168 C CB  . GLU   A 1 297 ? 112.387 4.878  -16.625 1    38.66 ?  277 GLU   A CB  1 1 
ATOM   2169 C CG  . GLU   A 1 297 ? 111.532 4.42   -17.802 1    50.17 ?  277 GLU   A CG  1 1 
ATOM   2170 C CD  . GLU   A 1 297 ? 111.751 2.991  -18.277 1    64.81 ?  277 GLU   A CD  1 1 
ATOM   2171 O OE1 . GLU   A 1 297 ? 111.785 2.072  -17.424 1    68.18 ?  277 GLU   A OE1 1 1 
ATOM   2172 O OE2 . GLU   A 1 297 ? 111.86  2.787  -19.509 1    69.65 ?  277 GLU   A OE2 1 1 
ATOM   2173 N N   . VAL   A 1 298 ? 113.467 6.98   -14.34  1    30.9  ?  278 VAL   A N   1 1 
ATOM   2174 C CA  . VAL   A 1 298 ? 114.141 7.185  -13.063 1    28.98 ?  278 VAL   A CA  1 1 
ATOM   2175 C C   . VAL   A 1 298 ? 113.302 8.117  -12.192 1    27.11 ?  278 VAL   A C   1 1 
ATOM   2176 O O   . VAL   A 1 298 ? 112.929 7.761  -11.074 1    27.83 ?  278 VAL   A O   1 1 
ATOM   2177 C CB  . VAL   A 1 298 ? 115.582 7.718  -13.241 1    28.67 ?  278 VAL   A CB  1 1 
ATOM   2178 C CG1 . VAL   A 1 298 ? 116.17  8.207  -11.917 1    28.29 ?  278 VAL   A CG1 1 1 
ATOM   2179 C CG2 . VAL   A 1 298 ? 116.465 6.65   -13.907 1    29.03 ?  278 VAL   A CG2 1 1 
ATOM   2180 N N   . THR   A 1 299 ? 112.914 9.284  -12.746 1    26.29 ?  279 THR   A N   1 1 
ATOM   2181 C CA  . THR   A 1 299 ? 112.09  10.21  -11.997 1    27.28 ?  279 THR   A CA  1 1 
ATOM   2182 C C   . THR   A 1 299 ? 110.765 9.599  -11.525 1    26.16 ?  279 THR   A C   1 1 
ATOM   2183 O O   . THR   A 1 299 ? 110.395 9.781  -10.368 1    25.78 ?  279 THR   A O   1 1 
ATOM   2184 C CB  . THR   A 1 299 ? 111.889 11.458 -12.825 1    30.41 ?  279 THR   A CB  1 1 
ATOM   2185 O OG1 . THR   A 1 299 ? 113.195 12.015 -12.988 1    33.05 ?  279 THR   A OG1 1 1 
ATOM   2186 C CG2 . THR   A 1 299 ? 110.961 12.456 -12.153 1    31.08 ?  279 THR   A CG2 1 1 
ATOM   2187 N N   . ASN   A 1 300 ? 110.079 8.836  -12.385 1    26.68 ?  280 ASN   A N   1 1 
ATOM   2188 C CA  . ASN   A 1 300 ? 108.823 8.186  -11.964 1    28.3  ?  280 ASN   A CA  1 1 
ATOM   2189 C C   . ASN   A 1 300 ? 109.069 7.223  -10.806 1    27.44 ?  280 ASN   A C   1 1 
ATOM   2190 O O   . ASN   A 1 300 ? 108.265 7.184  -9.878  1    27.89 ?  280 ASN   A O   1 1 
ATOM   2191 C CB  . ASN   A 1 300 ? 108.128 7.491  -13.113 1    30.04 ?  280 ASN   A CB  1 1 
ATOM   2192 C CG  . ASN   A 1 300 ? 107.665 8.454  -14.179 1    35.71 ?  280 ASN   A CG  1 1 
ATOM   2193 O OD1 . ASN   A 1 300 ? 107.568 9.673  -13.971 1    37.31 ?  280 ASN   A OD1 1 1 
ATOM   2194 N ND2 . ASN   A 1 300 ? 107.408 7.926  -15.368 1    39.8  ?  280 ASN   A ND2 1 1 
ATOM   2195 N N   . SER   A 1 301 ? 110.18  6.492  -10.851 1    26.29 ?  281 SER   A N   1 1 
ATOM   2196 C CA  . SER   A 1 301 ? 110.516 5.538  -9.769  1    25.57 ?  281 SER   A CA  1 1 
ATOM   2197 C C   . SER   A 1 301 ? 110.841 6.305  -8.488  1    25.92 ?  281 SER   A C   1 1 
ATOM   2198 O O   . SER   A 1 301 ? 110.373 5.954  -7.412  1    26.63 ?  281 SER   A O   1 1 
ATOM   2199 C CB  . SER   A 1 301 ? 111.708 4.682  -10.179 1    26.64 ?  281 SER   A CB  1 1 
ATOM   2200 O OG  . SER   A 1 301 ? 112.156 3.955  -9.048  1    28.37 ?  281 SER   A OG  1 1 
ATOM   2201 N N   . VAL   A 1 302 ? 111.633 7.386  -8.588  1    24.87 ?  282 VAL   A N   1 1 
ATOM   2202 C CA  . VAL   A 1 302 ? 111.971 8.211  -7.426  1    24.19 ?  282 VAL   A CA  1 1 
ATOM   2203 C C   . VAL   A 1 302 ? 110.703 8.718  -6.728  1    24.39 ?  282 VAL   A C   1 1 
ATOM   2204 O O   . VAL   A 1 302 ? 110.588 8.619  -5.506  1    24.64 ?  282 VAL   A O   1 1 
ATOM   2205 C CB  . VAL   A 1 302 ? 112.906 9.373  -7.864  1    24.64 ?  282 VAL   A CB  1 1 
ATOM   2206 C CG1 . VAL   A 1 302 ? 113.022 10.439 -6.771  1    24.64 ?  282 VAL   A CG1 1 1 
ATOM   2207 C CG2 . VAL   A 1 302 ? 114.287 8.837  -8.262  1    26.12 ?  282 VAL   A CG2 1 1 
ATOM   2208 N N   . PHE   A 1 303 ? 109.733 9.257  -7.518  1    24.77 ?  283 PHE   A N   1 1 
ATOM   2209 C CA  . PHE   A 1 303 ? 108.496 9.751  -6.916  1    24.95 ?  283 PHE   A CA  1 1 
ATOM   2210 C C   . PHE   A 1 303 ? 107.715 8.612  -6.249  1    26.19 ?  283 PHE   A C   1 1 
ATOM   2211 O O   . PHE   A 1 303 ? 107.204 8.757  -5.145  1    26.82 ?  283 PHE   A O   1 1 
ATOM   2212 C CB  . PHE   A 1 303 ? 107.634 10.431 -7.987  1    24.41 ?  283 PHE   A CB  1 1 
ATOM   2213 C CG  . PHE   A 1 303 ? 107.943 11.907 -8.204  1    25.93 ?  283 PHE   A CG  1 1 
ATOM   2214 C CD1 . PHE   A 1 303 ? 109.201 12.32  -8.612  1    26.41 ?  283 PHE   A CD1 1 1 
ATOM   2215 C CD2 . PHE   A 1 303 ? 106.95  12.852 -8.092  1    26.28 ?  283 PHE   A CD2 1 1 
ATOM   2216 C CE1 . PHE   A 1 303 ? 109.461 13.691 -8.872  1    27.67 ?  283 PHE   A CE1 1 1 
ATOM   2217 C CE2 . PHE   A 1 303 ? 107.208 14.202 -8.328  1    26.76 ?  283 PHE   A CE2 1 1 
ATOM   2218 C CZ  . PHE   A 1 303 ? 108.457 14.614 -8.706  1    27.29 ?  283 PHE   A CZ  1 1 
ATOM   2219 N N   . HIS   A 1 304 ? 107.622 7.472  -6.952  1    25.35 ?  284 HIS   A N   1 1 
ATOM   2220 C CA  . HIS   A 1 304 ? 106.891 6.324  -6.395  1    27.17 ?  284 HIS   A CA  1 1 
ATOM   2221 C C   . HIS   A 1 304 ? 107.543 5.835  -5.096  1    27.27 ?  284 HIS   A C   1 1 
ATOM   2222 O O   . HIS   A 1 304 ? 106.841 5.536  -4.135  1    27.79 ?  284 HIS   A O   1 1 
ATOM   2223 C CB  . HIS   A 1 304 ? 106.844 5.212  -7.452  1    29.51 ?  284 HIS   A CB  1 1 
ATOM   2224 C CG  . HIS   A 1 304 ? 106.213 3.955  -6.947  1    34.33 ?  284 HIS   A CG  1 1 
ATOM   2225 N ND1 . HIS   A 1 304 ? 104.845 3.871  -6.737  1    37.35 ?  284 HIS   A ND1 1 1 
ATOM   2226 C CD2 . HIS   A 1 304 ? 106.796 2.804  -6.54   1    37.17 ?  284 HIS   A CD2 1 1 
ATOM   2227 C CE1 . HIS   A 1 304 ? 104.63  2.645  -6.271  1    38.12 ?  284 HIS   A CE1 1 1 
ATOM   2228 N NE2 . HIS   A 1 304 ? 105.776 1.972  -6.11   1    38.36 ?  284 HIS   A NE2 1 1 
ATOM   2229 N N   . GLU   A 1 305 ? 108.878 5.761  -5.065  1    26.01 ?  285 GLU   A N   1 1 
ATOM   2230 C CA  . GLU   A 1 305 ? 109.587 5.235  -3.895  1    26.17 ?  285 GLU   A CA  1 1 
ATOM   2231 C C   . GLU   A 1 305 ? 109.464 6.137  -2.69   1    26.16 ?  285 GLU   A C   1 1 
ATOM   2232 O O   . GLU   A 1 305 ? 109.308 5.686  -1.535  1    26.95 ?  285 GLU   A O   1 1 
ATOM   2233 C CB  . GLU   A 1 305 ? 111.048 4.931  -4.237  1    27.9  ?  285 GLU   A CB  1 1 
ATOM   2234 C CG  . GLU   A 1 305 ? 111.192 3.759  -5.211  1    29.18 ?  285 GLU   A CG  1 1 
ATOM   2235 C CD  . GLU   A 1 305 ? 110.631 2.397  -4.795  1    38.18 ?  285 GLU   A CD  1 1 
ATOM   2236 O OE1 . GLU   A 1 305 ? 110.604 2.101  -3.581  1    37.89 ?  285 GLU   A OE1 1 1 
ATOM   2237 O OE2 . GLU   A 1 305 ? 110.226 1.614  -5.692  1    41.51 ?  285 GLU   A OE2 1 1 
ATOM   2238 N N   . ILE   A 1 306 ? 109.475 7.469  -2.956  1    24.58 ?  286 ILE   A N   1 1 
ATOM   2239 C CA  . ILE   A 1 306 ? 109.295 8.41   -1.863  1    24.34 ?  286 ILE   A CA  1 1 
ATOM   2240 C C   . ILE   A 1 306 ? 107.871 8.324  -1.345  1    26.12 ?  286 ILE   A C   1 1 
ATOM   2241 O O   . ILE   A 1 306 ? 107.633 8.386  -0.135  1    27.33 ?  286 ILE   A O   1 1 
ATOM   2242 C CB  . ILE   A 1 306 ? 109.664 9.851  -2.328  1    24.37 ?  286 ILE   A CB  1 1 
ATOM   2243 C CG1 . ILE   A 1 306 ? 111.177 9.856  -2.609  1    24.41 ?  286 ILE   A CG1 1 1 
ATOM   2244 C CG2 . ILE   A 1 306 ? 109.282 10.875 -1.236  1    25.67 ?  286 ILE   A CG2 1 1 
ATOM   2245 C CD1 . ILE   A 1 306 ? 111.698 11.235 -3.26   1    24.96 ?  286 ILE   A CD1 1 1 
ATOM   2246 N N   . ASN   A 1 307 ? 106.897 8.221  -2.271  1    26.96 ?  287 ASN   A N   1 1 
ATOM   2247 C CA  . ASN   A 1 307 ? 105.485 8.114  -1.922  1    28.22 ?  287 ASN   A CA  1 1 
ATOM   2248 C C   . ASN   A 1 307 ? 105.28  6.856  -1.026  1    29.18 ?  287 ASN   A C   1 1 
ATOM   2249 O O   . ASN   A 1 307 ? 104.667 6.974  0.038   1    31.19 ?  287 ASN   A O   1 1 
ATOM   2250 C CB  . ASN   A 1 307 ? 104.694 7.963  -3.222  1    30.55 ?  287 ASN   A CB  1 1 
ATOM   2251 C CG  . ASN   A 1 307 ? 103.198 7.869  -3.052  1    36.7  ?  287 ASN   A CG  1 1 
ATOM   2252 O OD1 . ASN   A 1 307 ? 102.678 7.234  -2.122  1    37.47 ?  287 ASN   A OD1 1 1 
ATOM   2253 N ND2 . ASN   A 1 307 ? 102.474 8.52   -3.964  1    39.51 ?  287 ASN   A ND2 1 1 
ATOM   2254 N N   . MET   A 1 308 ? 105.821 5.696  -1.427  1    29.36 ?  288 MET   A N   1 1 
ATOM   2255 C CA  . MET   A 1 308 ? 105.657 4.479  -0.616  1    29.34 ?  288 MET   A CA  1 1 
ATOM   2256 C C   . MET   A 1 308 ? 106.308 4.65   0.756   1    29.3  ?  288 MET   A C   1 1 
ATOM   2257 O O   . MET   A 1 308 ? 105.729 4.267  1.797   1    30.04 ?  288 MET   A O   1 1 
ATOM   2258 C CB  . MET   A 1 308 ? 106.316 3.288  -1.313  1    30.43 ?  288 MET   A CB  1 1 
ATOM   2259 C CG  . MET   A 1 308 ? 105.787 2.96   -2.663  1    35.31 ?  288 MET   A CG  1 1 
ATOM   2260 S SD  . MET   A 1 308 ? 104.116 2.274  -2.631  1    43.11 ?  288 MET   A SD  1 1 
ATOM   2261 C CE  . MET   A 1 308 ? 103.114 3.797  -2.963  1    37.8  ?  288 MET   A CE  1 1 
ATOM   2262 N N   . TRP   A 1 309 ? 107.543 5.17   0.773   1    27.21 ?  289 TRP   A N   1 1 
ATOM   2263 C CA  . TRP   A 1 309 ? 108.296 5.263  2.015   1    26.95 ?  289 TRP   A CA  1 1 
ATOM   2264 C C   . TRP   A 1 309 ? 107.63  6.183  3.054   1    27.6  ?  289 TRP   A C   1 1 
ATOM   2265 O O   . TRP   A 1 309 ? 107.493 5.812  4.224   1    27.45 ?  289 TRP   A O   1 1 
ATOM   2266 C CB  . TRP   A 1 309 ? 109.728 5.676  1.707   1    25.95 ?  289 TRP   A CB  1 1 
ATOM   2267 C CG  . TRP   A 1 309 ? 110.665 5.491  2.847   1    25.2  ?  289 TRP   A CG  1 1 
ATOM   2268 C CD1 . TRP   A 1 309 ? 111.457 4.406  3.091   1    24.89 ?  289 TRP   A CD1 1 1 
ATOM   2269 C CD2 . TRP   A 1 309 ? 110.96  6.452  3.867   1    24.07 ?  289 TRP   A CD2 1 1 
ATOM   2270 N NE1 . TRP   A 1 309 ? 112.226 4.637  4.207   1    24.53 ?  289 TRP   A NE1 1 1 
ATOM   2271 C CE2 . TRP   A 1 309 ? 111.947 5.888  4.7     1    24.49 ?  289 TRP   A CE2 1 1 
ATOM   2272 C CE3 . TRP   A 1 309 ? 110.516 7.752  4.128   1    23.83 ?  289 TRP   A CE3 1 1 
ATOM   2273 C CZ2 . TRP   A 1 309 ? 112.444 6.548  5.824   1    24.52 ?  289 TRP   A CZ2 1 1 
ATOM   2274 C CZ3 . TRP   A 1 309 ? 111.028 8.417  5.224   1    24.55 ?  289 TRP   A CZ3 1 1 
ATOM   2275 C CH2 . TRP   A 1 309 ? 111.957 7.809  6.081   1    25.48 ?  289 TRP   A CH2 1 1 
ATOM   2276 N N   . VAL   A 1 310 ? 107.195 7.385  2.616   1    27.87 ?  290 VAL   A N   1 1 
ATOM   2277 C CA  . VAL   A 1 310 ? 106.503 8.297  3.523   1    29.45 ?  290 VAL   A CA  1 1 
ATOM   2278 C C   . VAL   A 1 310 ? 105.105 7.755  3.869   1    30.92 ?  290 VAL   A C   1 1 
ATOM   2279 O O   . VAL   A 1 310 ? 104.683 7.885  5.019   1    31.67 ?  290 VAL   A O   1 1 
ATOM   2280 C CB  . VAL   A 1 310 ? 106.451 9.695  2.87    1    29.1  ?  290 VAL   A CB  1 1 
ATOM   2281 C CG1 . VAL   A 1 310 ? 105.551 10.635 3.666   1    30.42 ?  290 VAL   A CG1 1 1 
ATOM   2282 C CG2 . VAL   A 1 310 ? 107.869 10.26  2.77    1    28.95 ?  290 VAL   A CG2 1 1 
ATOM   2283 N N   . SER   A 1 311 ? 104.402 7.13   2.912   1    31.86 ?  291 SER   A N   1 1 
ATOM   2284 C CA  . SER   A 1 311 ? 103.065 6.554  3.181   1    33.83 ?  291 SER   A CA  1 1 
ATOM   2285 C C   . SER   A 1 311 ? 103.136 5.48   4.284   1    34.2  ?  291 SER   A C   1 1 
ATOM   2286 O O   . SER   A 1 311 ? 102.274 5.434  5.164   1    35.87 ?  291 SER   A O   1 1 
ATOM   2287 C CB  . SER   A 1 311 ? 102.482 5.913  1.917   1    35.12 ?  291 SER   A CB  1 1 
ATOM   2288 O OG  . SER   A 1 311 ? 102.109 6.91   0.977   1    39.09 ?  291 SER   A OG  1 1 
ATOM   2289 N N   . GLN   A 1 312 ? 104.156 4.644  4.249   1    33.28 ?  292 GLN   A N   1 1 
ATOM   2290 C CA  . GLN   A 1 312 ? 104.324 3.577  5.23    1    33.82 ?  292 GLN   A CA  1 1 
ATOM   2291 C C   . GLN   A 1 312 ? 104.644 4.147  6.632   1    34.8  ?  292 GLN   A C   1 1 
ATOM   2292 O O   . GLN   A 1 312 ? 104.392 3.477  7.641   1    37.54 ?  292 GLN   A O   1 1 
ATOM   2293 C CB  . GLN   A 1 312 ? 105.47  2.646  4.782   1    33.16 ?  292 GLN   A CB  1 1 
ATOM   2294 C CG  . GLN   A 1 312 ? 105.053 1.698  3.642   1    36.76 ?  292 GLN   A CG  1 1 
ATOM   2295 C CD  . GLN   A 1 312 ? 106.204 1.212  2.763   1    43.1  ?  292 GLN   A CD  1 1 
ATOM   2296 O OE1 . GLN   A 1 312 ? 105.994 0.758  1.624   1    44.51 ?  292 GLN   A OE1 1 1 
ATOM   2297 N NE2 . GLN   A 1 312 ? 107.447 1.321  3.239   1    44.76 ?  292 GLN   A NE2 1 1 
ATOM   2298 N N   . ARG   A 1 313 ? 105.241 5.349  6.695   1    32.5  ?  293 ARG   A N   1 1 
ATOM   2299 C CA  . ARG   A 1 313 ? 105.657 5.945  7.938   1    31.4  ?  293 ARG   A CA  1 1 
ATOM   2300 C C   . ARG   A 1 313 ? 104.752 7.076  8.45    1    34.08 ?  293 ARG   A C   1 1 
ATOM   2301 O O   . ARG   A 1 313 ? 105.088 7.733  9.434   1    33.34 ?  293 ARG   A O   1 1 
ATOM   2302 C CB  . ARG   A 1 313 ? 107.106 6.4    7.833   1    29.75 ?  293 ARG   A CB  1 1 
ATOM   2303 C CG  . ARG   A 1 313 ? 108.017 5.206  7.77    1    30.13 ?  293 ARG   A CG  1 1 
ATOM   2304 C CD  . ARG   A 1 313 ? 109.391 5.502  7.211   1    30.36 ?  293 ARG   A CD  1 1 
ATOM   2305 N NE  . ARG   A 1 313 ? 110.202 4.277  7.124   1    29.57 ?  293 ARG   A NE  1 1 
ATOM   2306 C CZ  . ARG   A 1 313 ? 110.065 3.353  6.171   1    28.04 ?  293 ARG   A CZ  1 1 
ATOM   2307 N NH1 . ARG   A 1 313 ? 109.139 3.489  5.236   1    29.09 ?  293 ARG   A NH1 1 1 
ATOM   2308 N NH2 . ARG   A 1 313 ? 110.829 2.255  6.177   1    29.23 ?  293 ARG   A NH2 1 1 
ATOM   2309 N N   . THR   A 1 314 ? 103.584 7.256  7.817   1    36.61 ?  294 THR   A N   1 1 
ATOM   2310 C CA  . THR   A 1 314 ? 102.58  8.236  8.209   1    39.3  ?  294 THR   A CA  1 1 
ATOM   2311 C C   . THR   A 1 314 ? 101.213 7.546  8.341   1    43.91 ?  294 THR   A C   1 1 
ATOM   2312 O O   . THR   A 1 314 ? 101.02  6.415  7.882   1    44.94 ?  294 THR   A O   1 1 
ATOM   2313 C CB  . THR   A 1 314 ? 102.508 9.407  7.191   1    39.39 ?  294 THR   A CB  1 1 
ATOM   2314 O OG1 . THR   A 1 314 ? 102.307 8.866  5.875   1    39.68 ?  294 THR   A OG1 1 1 
ATOM   2315 C CG2 . THR   A 1 314 ? 103.74  10.272 7.227   1    39.31 ?  294 THR   A CG2 1 1 
ATOM   2316 N N   . ALA   A 1 315 ? 100.273 8.199  9.031   1    46.96 ?  295 ALA   A N   1 1 
ATOM   2317 C CA  . ALA   A 1 315 ? 98.926  7.638  9.244   1    50.36 ?  295 ALA   A CA  1 1 
ATOM   2318 C C   . ALA   A 1 315 ? 98.011  8.718  9.814   1    51.92 ?  295 ALA   A C   1 1 
ATOM   2319 O O   . ALA   A 1 315 ? 98.495  9.686  10.408  1    53.24 ?  295 ALA   A O   1 1 
ATOM   2320 C CB  . ALA   A 1 315 ? 98.971  6.441  10.205  1    51.47 ?  295 ALA   A CB  1 1 
HETATM 2321 N N1  . A1H35 B 2 .   ? 125.439 20.99  -5.261  1    24.86 ?  401 A1H35 A N1  1 1 
HETATM 2322 C C7  . A1H35 B 2 .   ? 127.992 18.744 -4.808  1    31.39 ?  401 A1H35 A C7  1 1 
HETATM 2323 C C8  . A1H35 B 2 .   ? 127.336 20.1   -5.135  1    29.16 ?  401 A1H35 A C8  1 1 
HETATM 2324 N N2  . A1H35 B 2 .   ? 123.358 20.891 -6.128  1    23.9  ?  401 A1H35 A N2  1 1 
HETATM 2325 C C9  . A1H35 B 2 .   ? 128.737 20.665 -5.438  1    32.32 ?  401 A1H35 A C9  1 1 
HETATM 2326 C C1  . A1H35 B 2 .   ? 132.995 20.25  -1.568  1    48.85 ?  401 A1H35 A C1  1 1 
HETATM 2327 C C5  . A1H35 B 2 .   ? 130.671 18.851 -5.04   1    40.31 ?  401 A1H35 A C5  1 1 
HETATM 2328 C C6  . A1H35 B 2 .   ? 129.329 19.496 -4.616  1    34.8  ?  401 A1H35 A C6  1 1 
HETATM 2329 N N3  . A1H35 B 2 .   ? 119.847 21.116 -10.349 1    23.77 ?  401 A1H35 A N3  1 1 
HETATM 2330 C C4  . A1H35 B 2 .   ? 131.737 19.892 -4.944  1    46.55 ?  401 A1H35 A C4  1 1 
HETATM 2331 C C3  . A1H35 B 2 .   ? 132.343 20.159 -3.716  1    48.29 ?  401 A1H35 A C3  1 1 
HETATM 2332 C C2  . A1H35 B 2 .   ? 132.183 19.571 -2.44   1    48.57 ?  401 A1H35 A C2  1 1 
HETATM 2333 N N4  . A1H35 B 2 .   ? 117.768 21.17  -11.03  1    23.04 ?  401 A1H35 A N4  1 1 
HETATM 2334 O O   . A1H35 B 2 .   ? 123.655 21.127 -3.926  1    22.09 ?  401 A1H35 A O   1 1 
HETATM 2335 C C12 . A1H35 B 2 .   ? 124.127 20.929 -5.033  1    23.24 ?  401 A1H35 A C12 1 1 
HETATM 2336 C C23 . A1H35 B 2 .   ? 123.54  21.156 -7.56   1    24.74 ?  401 A1H35 A C23 1 1 
HETATM 2337 C C14 . A1H35 B 2 .   ? 122.004 21.164 -7.714  1    23.46 ?  401 A1H35 A C14 1 1 
HETATM 2338 C C17 . A1H35 B 2 .   ? 121.344 20.106 -8.619  1    23.45 ?  401 A1H35 A C17 1 1 
HETATM 2339 C C16 . A1H35 B 2 .   ? 121.084 21.238 -9.636  1    23.86 ?  401 A1H35 A C16 1 1 
HETATM 2340 N N5  . A1H35 B 2 .   ? 119.857 20.482 -11.534 1    22.18 ?  401 A1H35 A N5  1 1 
HETATM 2341 C C19 . A1H35 B 2 .   ? 118.575 20.52  -11.917 1    22.47 ?  401 A1H35 A C19 1 1 
HETATM 2342 C C20 . A1H35 B 2 .   ? 118.136 19.912 -13.195 1    22.62 ?  401 A1H35 A C20 1 1 
HETATM 2343 C C22 . A1H35 B 2 .   ? 119.138 19.8   -14.32  1    23.5  ?  401 A1H35 A C22 1 1 
HETATM 2344 C C21 . A1H35 B 2 .   ? 118.711 18.579 -13.599 1    22.73 ?  401 A1H35 A C21 1 1 
HETATM 2345 C C18 . A1H35 B 2 .   ? 118.605 21.524 -10.06  1    23.78 ?  401 A1H35 A C18 1 1 
HETATM 2346 C C15 . A1H35 B 2 .   ? 121.249 22.261 -8.5    1    23.02 ?  401 A1H35 A C15 1 1 
HETATM 2347 C C13 . A1H35 B 2 .   ? 121.899 20.99  -6.181  1    23.89 ?  401 A1H35 A C13 1 1 
HETATM 2348 C C10 . A1H35 B 2 .   ? 126.384 20.825 -4.158  1    26.64 ?  401 A1H35 A C10 1 1 
HETATM 2349 C C11 . A1H35 B 2 .   ? 126.214 20.163 -6.192  1    27.02 ?  401 A1H35 A C11 1 1 
HETATM 2350 C C   . A1H35 B 2 .   ? 133.64  21.243 -2.3    1    49.51 ?  401 A1H35 A C   1 1 
HETATM 2351 N N   . A1H35 B 2 .   ? 133.258 21.2   -3.586  1    50.39 1  401 A1H35 A N   1 1 
HETATM 2352 C C24 . A1H35 B 2 .   ? 132.063 20.656 -6.077  1    50.85 ?  401 A1H35 A C24 1 1 
HETATM 2353 N N6  . A1H35 B 2 .   ? 132.97  21.707 -5.983  1    52.73 ?  401 A1H35 A N6  1 1 
HETATM 2354 B B   . A1H35 B 2 .   ? 133.719 22.15  -4.712  1    53.74 -1 401 A1H35 A B   1 1 
HETATM 2355 F F1  . A1H35 B 2 .   ? 133.396 23.457 -4.394  1    55.69 ?  401 A1H35 A F1  1 1 
HETATM 2356 F F   . A1H35 B 2 .   ? 135.087 22.045 -4.902  1    55.8  ?  401 A1H35 A F   1 1 
HETATM 2357 C C27 . A1H35 B 2 .   ? 133.045 22.294 -7.211  1    53.11 ?  401 A1H35 A C27 1 1 
HETATM 2358 C C26 . A1H35 B 2 .   ? 132.228 21.644 -8.097  1    53.13 ?  401 A1H35 A C26 1 1 
HETATM 2359 C C25 . A1H35 B 2 .   ? 131.608 20.6   -7.4    1    52.4  ?  401 A1H35 A C25 1 1 
HETATM 2360 C C1  . EDO   C 3 .   ? 119.453 26.745 16.835  1    54.36 ?  402 EDO   A C1  1 ? 
HETATM 2361 O O1  . EDO   C 3 .   ? 118.073 26.446 16.881  1    54.5  ?  402 EDO   A O1  1 ? 
HETATM 2362 C C2  . EDO   C 3 .   ? 120.038 26.156 15.611  1    54.73 ?  402 EDO   A C2  1 ? 
HETATM 2363 O O2  . EDO   C 3 .   ? 121.352 25.727 15.888  1    55.4  ?  402 EDO   A O2  1 ? 
HETATM 2364 C C1  . EDO   D 3 .   ? 109.807 16.702 -11.023 1    33.62 ?  403 EDO   A C1  1 ? 
HETATM 2365 O O1  . EDO   D 3 .   ? 110.973 16.959 -10.178 1    29.33 ?  403 EDO   A O1  1 ? 
HETATM 2366 C C2  . EDO   D 3 .   ? 110.08  16.395 -12.505 1    36.5  ?  403 EDO   A C2  1 ? 
HETATM 2367 O O2  . EDO   D 3 .   ? 110.399 17.592 -13.245 1    38.61 ?  403 EDO   A O2  1 ? 
HETATM 2368 C C1  . EDO   E 3 .   ? 119.898 34.035 -9.047  1    48.37 ?  404 EDO   A C1  1 ? 
HETATM 2369 O O1  . EDO   E 3 .   ? 121.302 34.239 -9.03   1    49.29 ?  404 EDO   A O1  1 ? 
HETATM 2370 C C2  . EDO   E 3 .   ? 119.378 33.894 -7.647  1    47.47 ?  404 EDO   A C2  1 ? 
HETATM 2371 O O2  . EDO   E 3 .   ? 119.038 35.188 -7.184  1    48.31 ?  404 EDO   A O2  1 ? 
HETATM 2372 O O   . HOH   F 4 .   ? 123.365 34.687 7.713   1    39.42 ?  501 HOH   A O   1 ? 
HETATM 2373 O O   . HOH   F 4 .   ? 115.419 22.33  -12.235 1    26.72 ?  502 HOH   A O   1 ? 
HETATM 2374 O O   . HOH   F 4 .   ? 116.745 43.015 0.399   1    43.63 ?  503 HOH   A O   1 ? 
HETATM 2375 O O   . HOH   F 4 .   ? 110.319 2.169  -8.178  1    38.34 ?  504 HOH   A O   1 ? 
HETATM 2376 O O   . HOH   F 4 .   ? 114.458 27.603 16.39   1    31.72 ?  505 HOH   A O   1 ? 
HETATM 2377 O O   . HOH   F 4 .   ? 109.475 6.96   10.641  1    38.94 ?  506 HOH   A O   1 ? 
HETATM 2378 O O   . HOH   F 4 .   ? 117.61  31.637 12.195  1    23.01 ?  507 HOH   A O   1 ? 
HETATM 2379 O O   . HOH   F 4 .   ? 119.042 4.475  -14.812 1    53.25 ?  508 HOH   A O   1 ? 
HETATM 2380 O O   . HOH   F 4 .   ? 133.249 28.697 8.949   1    49.85 ?  509 HOH   A O   1 ? 
HETATM 2381 O O   . HOH   F 4 .   ? 122.722 10.559 -7.838  1    22.42 ?  510 HOH   A O   1 ? 
HETATM 2382 O O   . HOH   F 4 .   ? 131.462 13.131 4.886   1    38.52 ?  511 HOH   A O   1 ? 
HETATM 2383 O O   . HOH   F 4 .   ? 95.164  22.552 5.525   1    73.66 ?  512 HOH   A O   1 ? 
HETATM 2384 O O   . HOH   F 4 .   ? 117.538 -2.295 12.22   1    34.04 ?  513 HOH   A O   1 ? 
HETATM 2385 O O   . HOH   F 4 .   ? 121.465 12.334 -22.228 1    40.95 ?  514 HOH   A O   1 ? 
HETATM 2386 O O   . HOH   F 4 .   ? 110.579 4.308  10.925  1    35.37 ?  515 HOH   A O   1 ? 
HETATM 2387 O O   . HOH   F 4 .   ? 104.26  19.368 15.174  1    47.76 ?  516 HOH   A O   1 ? 
HETATM 2388 O O   . HOH   F 4 .   ? 148.918 34.254 5.772   1    60.09 ?  517 HOH   A O   1 ? 
HETATM 2389 O O   . HOH   F 4 .   ? 132.186 32.107 4.1     1    43.45 ?  518 HOH   A O   1 ? 
HETATM 2390 O O   . HOH   F 4 .   ? 118.96  37.572 16.358  1    53.07 ?  519 HOH   A O   1 ? 
HETATM 2391 O O   . HOH   F 4 .   ? 110.027 0.999  3.302   1    45.47 ?  520 HOH   A O   1 ? 
HETATM 2392 O O   . HOH   F 4 .   ? 114.299 3.156  5.572   1    20.48 ?  521 HOH   A O   1 ? 
HETATM 2393 O O   . HOH   F 4 .   ? 114.54  24.462 0.533   1    25.99 ?  522 HOH   A O   1 ? 
HETATM 2394 O O   . HOH   F 4 .   ? 107.481 31.599 14.700  1    42.03 ?  523 HOH   A O   1 ? 
HETATM 2395 O O   . HOH   F 4 .   ? 111.455 16.716 -24.067 1    40.12 ?  524 HOH   A O   1 ? 
HETATM 2396 O O   . HOH   F 4 .   ? 126.515 -0.731 9.465   1    33.14 ?  525 HOH   A O   1 ? 
HETATM 2397 O O   . HOH   F 4 .   ? 126.441 12.927 -12.682 1    29.08 ?  526 HOH   A O   1 ? 
HETATM 2398 O O   . HOH   F 4 .   ? 124.348 34.834 1.515   1    29.11 ?  527 HOH   A O   1 ? 
HETATM 2399 O O   . HOH   F 4 .   ? 126.148 0.371  -15.528 1    67.48 ?  528 HOH   A O   1 ? 
HETATM 2400 O O   . HOH   F 4 .   ? 121.105 1.475  16.294  1    46.91 ?  529 HOH   A O   1 ? 
HETATM 2401 O O   . HOH   F 4 .   ? 116.009 20.248 -8.158  1    28.44 ?  530 HOH   A O   1 ? 
HETATM 2402 O O   . HOH   F 4 .   ? 111.561 37.57  -6.039  1    24.65 ?  531 HOH   A O   1 ? 
HETATM 2403 O O   . HOH   F 4 .   ? 125.15  6.56   -17.377 1    33.52 ?  532 HOH   A O   1 ? 
HETATM 2404 O O   . HOH   F 4 .   ? 122.691 15.854 -20.096 1    42.12 ?  533 HOH   A O   1 ? 
HETATM 2405 O O   . HOH   F 4 .   ? 125.048 26.029 -17.284 1    59.95 ?  534 HOH   A O   1 ? 
HETATM 2406 O O   . HOH   F 4 .   ? 105.711 7.843  -9.969  1    45.57 ?  535 HOH   A O   1 ? 
HETATM 2407 O O   . HOH   F 4 .   ? 131.589 33.255 -8.942  1    47.24 ?  536 HOH   A O   1 ? 
HETATM 2408 O O   . HOH   F 4 .   ? 114.548 18.469 -25.049 1    52.58 ?  537 HOH   A O   1 ? 
HETATM 2409 O O   . HOH   F 4 .   ? 104.321 41.978 -5.668  1    56.42 ?  538 HOH   A O   1 ? 
HETATM 2410 O O   . HOH   F 4 .   ? 126.774 2.296  -7.205  1    28.86 ?  539 HOH   A O   1 ? 
HETATM 2411 O O   . HOH   F 4 .   ? 135.818 18.006 4.298   1    40.65 ?  540 HOH   A O   1 ? 
HETATM 2412 O O   . HOH   F 4 .   ? 112.784 9.29   14.887  1    50.98 ?  541 HOH   A O   1 ? 
HETATM 2413 O O   . HOH   F 4 .   ? 108.472 44.253 2.23    1    33.83 ?  542 HOH   A O   1 ? 
HETATM 2414 O O   . HOH   F 4 .   ? 129.116 17.069 13.012  1    33.89 ?  543 HOH   A O   1 ? 
HETATM 2415 O O   . HOH   F 4 .   ? 117.153 27.919 14.857  1    27.94 ?  544 HOH   A O   1 ? 
HETATM 2416 O O   . HOH   F 4 .   ? 108.073 24.754 18.227  1    46.03 ?  545 HOH   A O   1 ? 
HETATM 2417 O O   . HOH   F 4 .   ? 128.631 4.041  -8.568  1    50.22 ?  546 HOH   A O   1 ? 
HETATM 2418 O O   . HOH   F 4 .   ? 127.188 -1.788 -12.033 1    41.58 ?  547 HOH   A O   1 ? 
HETATM 2419 O O   . HOH   F 4 .   ? 119.441 30.501 -6.427  1    21.6  ?  548 HOH   A O   1 ? 
HETATM 2420 O O   . HOH   F 4 .   ? 125.72  25.508 -12.733 1    48.42 ?  549 HOH   A O   1 ? 
HETATM 2421 O O   . HOH   F 4 .   ? 125.534 10.606 -1.601  1    25.79 ?  550 HOH   A O   1 ? 
HETATM 2422 O O   . HOH   F 4 .   ? 115.02  21.045 -14.691 1    22.83 ?  551 HOH   A O   1 ? 
HETATM 2423 O O   . HOH   F 4 .   ? 108.86  19.709 -12.643 1    48.62 ?  552 HOH   A O   1 ? 
HETATM 2424 O O   . HOH   F 4 .   ? 115.808 4.641  12.35   1    25.28 ?  553 HOH   A O   1 ? 
HETATM 2425 O O   . HOH   F 4 .   ? 120.985 24.387 -22.136 1    54.49 ?  554 HOH   A O   1 ? 
HETATM 2426 O O   . HOH   F 4 .   ? 99.46   12.187 12.445  1    60.61 ?  555 HOH   A O   1 ? 
HETATM 2427 O O   . HOH   F 4 .   ? 108.653 14.092 14.446  1    30.66 ?  556 HOH   A O   1 ? 
HETATM 2428 O O   . HOH   F 4 .   ? 98.576  17.172 -4.876  1    44.85 ?  557 HOH   A O   1 ? 
HETATM 2429 O O   . HOH   F 4 .   ? 100.214 12.08  -3.997  1    41.01 ?  558 HOH   A O   1 ? 
HETATM 2430 O O   . HOH   F 4 .   ? 112.423 0.436  4.079   1    62.19 ?  559 HOH   A O   1 ? 
HETATM 2431 O O   . HOH   F 4 .   ? 103.243 16.192 -8.567  1    40.19 ?  560 HOH   A O   1 ? 
HETATM 2432 O O   . HOH   F 4 .   ? 112.431 49.381 -1.612  1    65.32 ?  561 HOH   A O   1 ? 
HETATM 2433 O O   . HOH   F 4 .   ? 109.528 23.065 -10.331 1    33.32 ?  562 HOH   A O   1 ? 
HETATM 2434 O O   . HOH   F 4 .   ? 111.763 20.686 -13.855 1    39.02 ?  563 HOH   A O   1 ? 
HETATM 2435 O O   . HOH   F 4 .   ? 134.24  30.253 3.905   1    40.78 ?  564 HOH   A O   1 ? 
HETATM 2436 O O   . HOH   F 4 .   ? 110.104 2.978  -1.063  1    43.24 ?  565 HOH   A O   1 ? 
HETATM 2437 O O   . HOH   F 4 .   ? 113.616 0.739  -15.927 1    65.37 ?  566 HOH   A O   1 ? 
HETATM 2438 O O   . HOH   F 4 .   ? 102.302 31.161 18.349  1    42.19 ?  567 HOH   A O   1 ? 
HETATM 2439 O O   . HOH   F 4 .   ? 124.418 30.805 0.138   1    26.04 ?  568 HOH   A O   1 ? 
HETATM 2440 O O   . HOH   F 4 .   ? 109.831 3.803  -13.705 1    39.09 ?  569 HOH   A O   1 ? 
HETATM 2441 O O   . HOH   F 4 .   ? 116.915 0.729  -8.404  1    21.84 ?  570 HOH   A O   1 ? 
HETATM 2442 O O   . HOH   F 4 .   ? 103.279 45.896 -1.332  1    50.12 ?  571 HOH   A O   1 ? 
HETATM 2443 O O   . HOH   F 4 .   ? 118.292 27.31  5.548   1    19.05 ?  572 HOH   A O   1 ? 
HETATM 2444 O O   . HOH   F 4 .   ? 118.24  8.998  18.934  1    52.14 ?  573 HOH   A O   1 ? 
HETATM 2445 O O   . HOH   F 4 .   ? 125.939 12.885 -20.742 1    53.44 ?  574 HOH   A O   1 ? 
HETATM 2446 O O   . HOH   F 4 .   ? 108.469 11.91  -15.248 1    68.54 ?  575 HOH   A O   1 ? 
HETATM 2447 O O   . HOH   F 4 .   ? 110.496 1.514  -15.084 1    80.76 ?  576 HOH   A O   1 ? 
HETATM 2448 O O   . HOH   F 4 .   ? 122.276 10.117 18.661  1    53.59 ?  577 HOH   A O   1 ? 
HETATM 2449 O O   . HOH   F 4 .   ? 127.491 26.804 -10.826 1    48.81 ?  578 HOH   A O   1 ? 
HETATM 2450 O O   . HOH   F 4 .   ? 119.478 0.52   -10.613 1    27.98 ?  579 HOH   A O   1 ? 
HETATM 2451 O O   . HOH   F 4 .   ? 115.977 13.509 14.517  1    33.23 ?  580 HOH   A O   1 ? 
HETATM 2452 O O   . HOH   F 4 .   ? 106.972 6.95   11.268  1    39.12 ?  581 HOH   A O   1 ? 
HETATM 2453 O O   . HOH   F 4 .   ? 106.126 32.206 6.537   1    38.09 ?  582 HOH   A O   1 ? 
HETATM 2454 O O   . HOH   F 4 .   ? 124.554 18.634 13.333  1    51.55 ?  583 HOH   A O   1 ? 
HETATM 2455 O O   . HOH   F 4 .   ? 112.085 30.509 -5.11   1    20.04 ?  584 HOH   A O   1 ? 
HETATM 2456 O O   . HOH   F 4 .   ? 115.211 -2.731 14.949  1    62.22 ?  585 HOH   A O   1 ? 
HETATM 2457 O O   . HOH   F 4 .   ? 116.984 43.065 9.311   1    37.63 ?  586 HOH   A O   1 ? 
HETATM 2458 O O   . HOH   F 4 .   ? 127.663 3.343  -13.092 1    55.97 ?  587 HOH   A O   1 ? 
HETATM 2459 O O   . HOH   F 4 .   ? 100.268 5.972  -1.66   1    56    ?  588 HOH   A O   1 ? 
HETATM 2460 O O   . HOH   F 4 .   ? 102.627 38.267 -4.25   1    48.38 ?  589 HOH   A O   1 ? 
HETATM 2461 O O   . HOH   F 4 .   ? 106.971 35.04  9.258   1    52.84 ?  590 HOH   A O   1 ? 
HETATM 2462 O O   . HOH   F 4 .   ? 119.413 29.82  5.284   1    21.5  ?  591 HOH   A O   1 ? 
HETATM 2463 O O   . HOH   F 4 .   ? 111.841 30.528 -11.488 1    52.34 ?  592 HOH   A O   1 ? 
HETATM 2464 O O   . HOH   F 4 .   ? 105.43  31.057 -1.627  1    26.89 ?  593 HOH   A O   1 ? 
HETATM 2465 O O   . HOH   F 4 .   ? 131.781 11.238 -8.341  1    47.47 ?  594 HOH   A O   1 ? 
HETATM 2466 O O   . HOH   F 4 .   ? 135.794 12.689 -1.801  1    57.59 ?  595 HOH   A O   1 ? 
HETATM 2467 O O   . HOH   F 4 .   ? 135.821 33.305 -2.547  1    45.53 ?  596 HOH   A O   1 ? 
HETATM 2468 O O   . HOH   F 4 .   ? 112.469 14.306 -15.034 1    29.64 ?  597 HOH   A O   1 ? 
HETATM 2469 O O   . HOH   F 4 .   ? 100.09  9.128  4.175   1    64.37 ?  598 HOH   A O   1 ? 
HETATM 2470 O O   . HOH   F 4 .   ? 134.444 12.659 4.83    1    56.31 ?  599 HOH   A O   1 ? 
HETATM 2471 O O   . HOH   F 4 .   ? 104.241 9.963  10.871  1    45.05 ?  600 HOH   A O   1 ? 
HETATM 2472 O O   . HOH   F 4 .   ? 107.67  35.339 -6.441  1    34.45 ?  601 HOH   A O   1 ? 
HETATM 2473 O O   . HOH   F 4 .   ? 104.98  27.091 -4.957  1    42.62 ?  602 HOH   A O   1 ? 
HETATM 2474 O O   . HOH   F 4 .   ? 133.164 33.348 7.615   1    64.36 ?  603 HOH   A O   1 ? 
HETATM 2475 O O   . HOH   F 4 .   ? 128.434 31.106 -7.306  1    37.34 ?  604 HOH   A O   1 ? 
HETATM 2476 O O   . HOH   F 4 .   ? 129.075 8.22   -8.307  1    33.01 ?  605 HOH   A O   1 ? 
HETATM 2477 O O   . HOH   F 4 .   ? 127.927 32.278 11.142  1    46.25 ?  606 HOH   A O   1 ? 
HETATM 2478 O O   . HOH   F 4 .   ? 129.579 30.527 -4.767  1    35.11 ?  607 HOH   A O   1 ? 
HETATM 2479 O O   . HOH   F 4 .   ? 124.89  34.956 14.042  1    75.93 ?  608 HOH   A O   1 ? 
HETATM 2480 O O   . HOH   F 4 .   ? 116.825 10.799 15.325  1    43.99 ?  609 HOH   A O   1 ? 
HETATM 2481 O O   . HOH   F 4 .   ? 116.018 38.393 13.681  1    40.26 ?  610 HOH   A O   1 ? 
HETATM 2482 O O   . HOH   F 4 .   ? 109.807 22.21  17.425  1    56.01 ?  611 HOH   A O   1 ? 
HETATM 2483 O O   . HOH   F 4 .   ? 103.402 1.251  0.611   1    55.99 ?  612 HOH   A O   1 ? 
HETATM 2484 O O   . HOH   F 4 .   ? 95.776  16.105 -0.106  1    58.37 ?  613 HOH   A O   1 ? 
HETATM 2485 O O   . HOH   F 4 .   ? 109.864 18.472 -8.059  1    24.03 ?  614 HOH   A O   1 ? 
HETATM 2486 O O   . HOH   F 4 .   ? 125.787 26.862 -8.864  1    45.4  ?  615 HOH   A O   1 ? 
HETATM 2487 O O   . HOH   F 4 .   ? 101.629 10.633 10.53   1    45.28 ?  616 HOH   A O   1 ? 
HETATM 2488 O O   . HOH   F 4 .   ? 113.148 24.878 19.645  1    41.15 ?  617 HOH   A O   1 ? 
HETATM 2489 O O   . HOH   F 4 .   ? 114.759 15.017 -22.861 1    60.85 ?  618 HOH   A O   1 ? 
HETATM 2490 O O   . HOH   F 4 .   ? 122.075 31.934 -5.685  1    36.05 ?  619 HOH   A O   1 ? 
HETATM 2491 O O   . HOH   F 4 .   ? 123.776 24.572 -9.059  1    45.13 ?  620 HOH   A O   1 ? 
HETATM 2492 O O   . HOH   F 4 .   ? 128.11  11.278 -1.613  1    31.49 ?  621 HOH   A O   1 ? 
HETATM 2493 O O   . HOH   F 4 .   ? 120.116 39.873 14.105  1    66.24 ?  622 HOH   A O   1 ? 
HETATM 2494 O O   . HOH   F 4 .   ? 131.783 11.174 15.559  1    57.72 ?  623 HOH   A O   1 ? 
HETATM 2495 O O   . HOH   F 4 .   ? 118.217 37.228 -9.02   1    43.51 ?  624 HOH   A O   1 ? 
HETATM 2496 O O   . HOH   F 4 .   ? 127.385 16.261 14.977  1    75.91 ?  625 HOH   A O   1 ? 
HETATM 2497 O O   . HOH   F 4 .   ? 134.546 24.491 11.036  1    65.13 ?  626 HOH   A O   1 ? 
HETATM 2498 O O   . HOH   F 4 .   ? 150.599 31.766 4.362   1    46.05 ?  627 HOH   A O   1 ? 
HETATM 2499 O O   . HOH   F 4 .   ? 110.298 41.896 -10.326 1    64.44 ?  628 HOH   A O   1 ? 
HETATM 2500 O O   . HOH   F 4 .   ? 119.105 22.644 18.244  1    54.44 ?  629 HOH   A O   1 ? 
HETATM 2501 O O   . HOH   F 4 .   ? 116.668 36.416 -11.162 1    42.62 ?  630 HOH   A O   1 ? 
HETATM 2502 O O   . HOH   F 4 .   ? 107.932 0.286  5.885   1    43.43 ?  631 HOH   A O   1 ? 
HETATM 2503 O O   . HOH   F 4 .   ? 124.658 36.03  3.903   1    31.61 ?  632 HOH   A O   1 ? 
HETATM 2504 O O   . HOH   F 4 .   ? 123.017 5.951  -19.292 1    46.04 ?  633 HOH   A O   1 ? 
HETATM 2505 O O   . HOH   F 4 .   ? 128.643 9.829  -15.285 1    49.76 ?  634 HOH   A O   1 ? 
HETATM 2506 O O   . HOH   F 4 .   ? 117.43  4.285  15.14   1    28.72 ?  635 HOH   A O   1 ? 
HETATM 2507 O O   . HOH   F 4 .   ? 136.966 16.03  2.877   1    75.43 ?  636 HOH   A O   1 ? 
HETATM 2508 O O   . HOH   F 4 .   ? 94.005  18.067 -0.37   1    60.67 ?  637 HOH   A O   1 ? 
HETATM 2509 O O   . HOH   F 4 .   ? 95.197  21.315 -0.995  1    47.3  ?  638 HOH   A O   1 ? 
HETATM 2510 O O   . HOH   F 4 .   ? 135.441 15.028 9.853   1    59.43 ?  639 HOH   A O   1 ? 
HETATM 2511 O O   . HOH   F 4 .   ? 123.974 31.996 14.694  1    52.83 ?  640 HOH   A O   1 ? 
HETATM 2512 O O   . HOH   F 4 .   ? 132.331 17.772 -8.939  1    63.67 ?  641 HOH   A O   1 ? 
HETATM 2513 O O   . HOH   F 4 .   ? 109.048 31.122 -8.223  1    46.04 ?  642 HOH   A O   1 ? 
HETATM 2514 O O   . HOH   F 4 .   ? 103.354 26.746 -2.844  1    39.22 ?  643 HOH   A O   1 ? 
HETATM 2515 O O   . HOH   F 4 .   ? 134.696 14.535 -0.101  1    47.75 ?  644 HOH   A O   1 ? 
HETATM 2516 O O   . HOH   F 4 .   ? 116.389 44.307 -3.92   1    44.34 ?  645 HOH   A O   1 ? 
HETATM 2517 O O   . HOH   F 4 .   ? 119.794 41.288 4.819   1    47.85 ?  646 HOH   A O   1 ? 
HETATM 2518 O O   . HOH   F 4 .   ? 119.831 20.506 -25.292 1    64.3  ?  647 HOH   A O   1 ? 
HETATM 2519 O O   . HOH   F 4 .   ? 109.154 51.43  -2.615  1    86.42 ?  648 HOH   A O   1 ? 
HETATM 2520 O O   . HOH   F 4 .   ? 130.346 1.101  2.75    1    45.58 ?  649 HOH   A O   1 ? 
HETATM 2521 O O   . HOH   F 4 .   ? 124.2   14.7   -28.176 1    88.53 ?  650 HOH   A O   1 ? 
HETATM 2522 O O   . HOH   F 4 .   ? 130.726 31.437 1.692   1    35.71 ?  651 HOH   A O   1 ? 
HETATM 2523 O O   . HOH   F 4 .   ? 92.727  16.391 2.461   1    79.54 ?  652 HOH   A O   1 ? 
HETATM 2524 O O   . HOH   F 4 .   ? 113.232 48.599 5.249   1    59.32 ?  653 HOH   A O   1 ? 
HETATM 2525 O O   . HOH   F 4 .   ? 118.289 26.319 -22.118 1    51.79 ?  654 HOH   A O   1 ? 
HETATM 2526 O O   . HOH   F 4 .   ? 99.417  7.606  1.913   1    62.59 ?  655 HOH   A O   1 ? 
HETATM 2527 O O   . HOH   F 4 .   ? 111.241 15.103 -19.391 1    53.06 ?  656 HOH   A O   1 ? 
HETATM 2528 O O   . HOH   F 4 .   ? 96.605  14.221 11.929  1    59.58 ?  657 HOH   A O   1 ? 
HETATM 2529 O O   . HOH   F 4 .   ? 99.693  9.356  -4.432  1    64.35 ?  658 HOH   A O   1 ? 
HETATM 2530 O O   . HOH   F 4 .   ? 120.302 40.669 -0.028  1    41.3  ?  659 HOH   A O   1 ? 
HETATM 2531 O O   . HOH   F 4 .   ? 115.209 45.939 -0.125  1    43.4  ?  660 HOH   A O   1 ? 
HETATM 2532 O O   . HOH   F 4 .   ? 109.874 46.171 5.058   1    39.79 ?  661 HOH   A O   1 ? 
HETATM 2533 O O   . HOH   F 4 .   ? 96.171  10.081 -0.64   1    59.11 ?  662 HOH   A O   1 ? 
HETATM 2534 O O   . HOH   F 4 .   ? 120.733 41.505 8.088   1    65.91 ?  663 HOH   A O   1 ? 
HETATM 2535 O O   A HOH   F 4 .   ? 124.582 29.439 12.986  0.5  35.43 ?  664 HOH   A O   1 ? 
HETATM 2536 O O   B HOH   F 4 .   ? 126.677 29.912 12.283  0.5  34.89 ?  664 HOH   A O   1 ? 
HETATM 2537 O O   . HOH   F 4 .   ? 109.02  20.478 -9.993  1    27.33 ?  665 HOH   A O   1 ? 
HETATM 2538 O O   . HOH   F 4 .   ? 136.698 21.225 6.851   1    65.35 ?  666 HOH   A O   1 ? 
HETATM 2539 O O   . HOH   F 4 .   ? 122.152 39.909 3.901   1    33.85 ?  667 HOH   A O   1 ? 
HETATM 2540 O O   . HOH   F 4 .   ? 106.243 30.112 -7.834  1    63.1  ?  668 HOH   A O   1 ? 
HETATM 2541 O O   . HOH   F 4 .   ? 126.153 34.742 10.637  1    72.19 ?  669 HOH   A O   1 ? 
HETATM 2542 O O   . HOH   F 4 .   ? 103.447 45.092 5.907   1    71.77 ?  670 HOH   A O   1 ? 
HETATM 2543 O O   . HOH   F 4 .   ? 125.726 34.254 5.836   1    38.37 ?  671 HOH   A O   1 ? 
HETATM 2544 O O   . HOH   F 4 .   ? 107.687 16.177 16.066  1    46.09 ?  672 HOH   A O   1 ? 
HETATM 2545 O O   . HOH   F 4 .   ? 140.817 35.222 1.578   1    56.72 ?  673 HOH   A O   1 ? 
HETATM 2546 O O   . HOH   F 4 .   ? 129.484 26.208 13.259  1    52.15 ?  674 HOH   A O   1 ? 
HETATM 2547 O O   . HOH   F 4 .   ? 107.382 32.846 -6.071  1    42.01 ?  675 HOH   A O   1 ? 
HETATM 2548 O O   . HOH   F 4 .   ? 106.892 26.908 -8.72   1    55.67 ?  676 HOH   A O   1 ? 
HETATM 2549 O O   . HOH   F 4 .   ? 125.505 38.78  -4.836  1    43.19 ?  677 HOH   A O   1 ? 
HETATM 2550 O O   . HOH   F 4 .   ? 104.889 35.545 5.91    1    41.57 ?  678 HOH   A O   1 ? 
HETATM 2551 O O   . HOH   F 4 .   ? 130.607 -2.313 9.021   1    60.49 ?  679 HOH   A O   1 ? 
HETATM 2552 O O   . HOH   F 4 .   ? 106.693 9.522  -17.867 1    72.14 ?  680 HOH   A O   1 ? 
HETATM 2553 O O   . HOH   F 4 .   ? 113.522 -1.135 11.437  1    50.39 ?  681 HOH   A O   1 ? 
HETATM 2554 O O   . HOH   F 4 .   ? 104.057 49.618 1.551   1    51    ?  682 HOH   A O   1 ? 
HETATM 2555 O O   . HOH   F 4 .   ? 125.49  38.383 2.643   1    43.05 ?  683 HOH   A O   1 ? 
HETATM 2556 O O   . HOH   F 4 .   ? 107.874 4.875  -15.604 1    44.23 ?  684 HOH   A O   1 ? 
HETATM 2557 O O   A HOH   F 4 .   ? 124.761 8.439  -19.913 0.5  42.26 ?  685 HOH   A O   1 ? 
HETATM 2558 O O   B HOH   F 4 .   ? 126.523 8.292  -19.274 0.5  34.17 ?  685 HOH   A O   1 ? 
HETATM 2559 O O   . HOH   F 4 .   ? 120.653 19.782 -22.453 1    37.69 ?  686 HOH   A O   1 ? 
HETATM 2560 O O   . HOH   F 4 .   ? 127.885 33.682 -6.871  1    50.22 ?  687 HOH   A O   1 ? 
HETATM 2561 O O   . HOH   F 4 .   ? 115.547 43.16  -10.071 1    76.34 ?  688 HOH   A O   1 ? 
HETATM 2562 O O   . HOH   F 4 .   ? 135.622 27.706 8.246   1    60.04 ?  689 HOH   A O   1 ? 
HETATM 2563 O O   . HOH   F 4 .   ? 130.851 3.403  -4.936  1    63.69 ?  690 HOH   A O   1 ? 
HETATM 2564 O O   . HOH   F 4 .   ? 101.635 2.013  7.736   1    76.21 ?  691 HOH   A O   1 ? 
HETATM 2565 O O   . HOH   F 4 .   ? 105.976 29.579 9.863   1    59.15 ?  692 HOH   A O   1 ? 
HETATM 2566 O O   . HOH   F 4 .   ? 132.973 22.188 13.219  1    73.05 ?  693 HOH   A O   1 ? 
HETATM 2567 O O   . HOH   F 4 .   ? 140.735 38.365 -4.847  1    63.56 ?  694 HOH   A O   1 ? 
HETATM 2568 O O   . HOH   F 4 .   ? 127.166 28.264 -16.359 1    69.54 ?  695 HOH   A O   1 ? 
HETATM 2569 O O   . HOH   F 4 .   ? 130.52  21.728 13.958  1    60.31 ?  696 HOH   A O   1 ? 
HETATM 2570 O O   . HOH   F 4 .   ? 110.552 48.876 5.774   1    59.08 ?  697 HOH   A O   1 ? 
HETATM 2571 O O   . HOH   F 4 .   ? 113.071 27.431 -16.843 1    57.18 ?  698 HOH   A O   1 ? 
HETATM 2572 O O   . HOH   F 4 .   ? 98.176  19.455 -6.363  1    60.09 ?  699 HOH   A O   1 ? 
HETATM 2573 O O   . HOH   F 4 .   ? 119.378 11.592 14.451  1    40.05 ?  700 HOH   A O   1 ? 
HETATM 2574 O O   . HOH   F 4 .   ? 111.982 0.535  -9.421  1    62.34 ?  701 HOH   A O   1 ? 
HETATM 2575 O O   . HOH   F 4 .   ? 103.76  9.015  -6.828  1    60.28 ?  702 HOH   A O   1 ? 
HETATM 2576 O O   . HOH   F 4 .   ? 102.558 6.097  -6.555  1    63.42 ?  703 HOH   A O   1 ? 
HETATM 2577 O O   . HOH   F 4 .   ? 123.918 28.767 15.613  1    73.18 ?  704 HOH   A O   1 ? 
HETATM 2578 O O   . HOH   F 4 .   ? 134.172 21.813 10.669  1    56.6  ?  705 HOH   A O   1 ? 
HETATM 2579 O O   . HOH   F 4 .   ? 141.759 22.331 1.962   1    69.37 ?  706 HOH   A O   1 ? 
HETATM 2580 O O   . HOH   F 4 .   ? 106.423 46.717 -6.262  1    62.86 ?  707 HOH   A O   1 ? 
HETATM 2581 O O   . HOH   F 4 .   ? 110.65  7.743  13.911  1    61.08 ?  708 HOH   A O   1 ? 
HETATM 2582 O O   . HOH   F 4 .   ? 146.665 36.27  4.823   1    64.11 ?  709 HOH   A O   1 ? 
HETATM 2583 O O   . HOH   F 4 .   ? 138.307 34.063 -9.925  1    68.79 ?  710 HOH   A O   1 ? 
HETATM 2584 O O   . HOH   F 4 .   ? 100.208 12.575 14.912  1    67.82 ?  711 HOH   A O   1 ? 
HETATM 2585 O O   . HOH   F 4 .   ? 121.537 22.399 -25.293 1    49.88 ?  712 HOH   A O   1 ? 
HETATM 2586 O O   . HOH   F 4 .   ? 105.144 19.151 18.315  1    69.26 ?  713 HOH   A O   1 ? 
HETATM 2587 O O   . HOH   F 4 .   ? 126.683 22.701 10.624  1    33.89 ?  714 HOH   A O   1 ? 
HETATM 2588 O O   . HOH   F 4 .   ? 121.756 39.958 -3.28   1    60.73 ?  715 HOH   A O   1 ? 
HETATM 2589 O O   . HOH   F 4 .   ? 136.67  15.635 5.595   1    74.53 ?  716 HOH   A O   1 ? 
HETATM 2590 O O   . HOH   F 4 .   ? 120.358 38.051 -8.384  1    62.4  ?  717 HOH   A O   1 ? 
HETATM 2591 O O   . HOH   F 4 .   ? 130.934 33.435 -12.912 1    71.61 ?  718 HOH   A O   1 ? 
HETATM 2592 O O   . HOH   F 4 .   ? 114.299 3.193  -12.733 1    48.73 ?  719 HOH   A O   1 ? 
HETATM 2593 O O   . HOH   F 4 .   ? 129.97  5.34   -13.198 1    57.62 ?  720 HOH   A O   1 ? 
HETATM 2594 O O   . HOH   F 4 .   ? 104.752 0.81   -9.233  1    60.86 ?  721 HOH   A O   1 ? 
HETATM 2595 O O   . HOH   F 4 .   ? 106.844 12.352 -11.796 1    54.05 ?  722 HOH   A O   1 ? 
HETATM 2596 O O   . HOH   F 4 .   ? 114.856 8.051  15.869  1    61.36 ?  723 HOH   A O   1 ? 
HETATM 2597 O O   . HOH   F 4 .   ? 110.613 17.823 -18.229 1    59.49 ?  724 HOH   A O   1 ? 
HETATM 2598 O O   . HOH   F 4 .   ? 144.797 18.467 -7.882  1    75.91 ?  725 HOH   A O   1 ? 
HETATM 2599 O O   . HOH   F 4 .   ? 96.921  25.665 -6.532  1    66.56 ?  726 HOH   A O   1 ? 
HETATM 2600 O O   . HOH   F 4 .   ? 125.149 17.762 15.965  1    66.66 ?  727 HOH   A O   1 ? 
HETATM 2601 O O   . HOH   F 4 .   ? 128.399 23.547 13.368  1    51.44 ?  728 HOH   A O   1 ? 
HETATM 2602 O O   . HOH   F 4 .   ? 118.16  41.541 -1.551  1    44.83 ?  729 HOH   A O   1 ? 
HETATM 2603 O O   . HOH   F 4 .   ? 115.451 24.602 20.708  1    48.12 ?  730 HOH   A O   1 ? 
HETATM 2604 O O   . HOH   F 4 .   ? 117.655 40.782 13.509  1    54.16 ?  731 HOH   A O   1 ? 
HETATM 2605 O O   . HOH   F 4 .   ? 131.61  9.085  -11.539 1    75.61 ?  732 HOH   A O   1 ? 
HETATM 2606 O O   . HOH   F 4 .   ? 150.618 26.885 6.619   1    51.85 ?  733 HOH   A O   1 ? 
HETATM 2607 O O   . HOH   F 4 .   ? 134.367 8.13   9.487   1    67.82 ?  734 HOH   A O   1 ? 
HETATM 2608 O O   . HOH   F 4 .   ? 124.718 13.672 -25.269 1    73    ?  735 HOH   A O   1 ? 
HETATM 2609 O O   . HOH   F 4 .   ? 111.94  27.013 19.717  1    46.45 ?  736 HOH   A O   1 ? 
HETATM 2610 O O   . HOH   F 4 .   ? 131.053 6.826  -9.169  1    69.88 ?  737 HOH   A O   1 ? 
HETATM 2611 O O   . HOH   F 4 .   ? 100.907 15.189 -7.732  1    67.45 ?  738 HOH   A O   1 ? 
HETATM 2612 O O   . HOH   F 4 .   ? 107.858 3.702  -11.27  1    59.59 ?  739 HOH   A O   1 ? 
HETATM 2613 O O   . HOH   F 4 .   ? 130.848 24.437 -17.542 1    54.78 ?  740 HOH   A O   1 ? 
HETATM 2614 O O   . HOH   F 4 .   ? 104.898 12.911 16.586  1    74    ?  741 HOH   A O   1 ? 
HETATM 2615 O O   . HOH   F 4 .   ? 95.511  26.521 7.165   1    67.2  ?  742 HOH   A O   1 ? 
HETATM 2616 O O   . HOH   F 4 .   ? 121.557 29.319 16.992  1    74.46 ?  743 HOH   A O   1 ? 
HETATM 2617 O O   . HOH   F 4 .   ? 107.324 1.138  8.038   1    56.65 ?  744 HOH   A O   1 ? 
HETATM 2618 O O   . HOH   F 4 .   ? 131.975 25.653 14.006  1    70.94 ?  745 HOH   A O   1 ? 
HETATM 2619 O O   . HOH   F 4 .   ? 127.878 28.053 14.227  1    71.4  ?  746 HOH   A O   1 ? 
HETATM 2620 O O   . HOH   F 4 .   ? 111.198 23.277 20.047  1    56.87 ?  747 HOH   A O   1 ? 
HETATM 2621 O O   . HOH   F 4 .   ? 113.818 4.39   -22.327 1    66.09 ?  748 HOH   A O   1 ? 
HETATM 2622 O O   . HOH   F 4 .   ? 122.793 41.282 0.681   1    72.97 ?  749 HOH   A O   1 ? 
HETATM 2623 O O   . HOH   F 4 .   ? 118.472 18.848 -26.505 1    49.73 ?  750 HOH   A O   1 ? 
HETATM 2624 O O   . HOH   F 4 .   ? 128.891 36.316 4.832   1    62.63 ?  751 HOH   A O   1 ? 
HETATM 2625 O O   . HOH   F 4 .   ? 110.728 37.009 -8.702  1    49.12 ?  752 HOH   A O   1 ? 
HETATM 2626 O O   . HOH   F 4 .   ? 128.136 14.182 -19.657 1    80.54 ?  753 HOH   A O   1 ? 
HETATM 2627 O O   . HOH   F 4 .   ? 119.156 3.812  17.231  1    50.52 ?  754 HOH   A O   1 ? 
HETATM 2628 O O   . HOH   F 4 .   ? 130.522 8.308  -13.865 1    62.01 ?  755 HOH   A O   1 ? 
HETATM 2629 O O   . HOH   F 4 .   ? 136.22  5.174  3.238   1    78.16 ?  756 HOH   A O   1 ? 
HETATM 2630 O O   . HOH   F 4 .   ? 110.048 29.03  -9.592  1    45.2  ?  757 HOH   A O   1 ? 
HETATM 2631 O O   . HOH   F 4 .   ? 109.76  22.003 -14.716 1    48.71 ?  758 HOH   A O   1 ? 
HETATM 2632 O O   . HOH   F 4 .   ? 129.129 0.187  15.436  1    82.88 ?  759 HOH   A O   1 ? 
HETATM 2633 O O   . HOH   F 4 .   ? 114.434 34.275 15.763  1    50.72 ?  760 HOH   A O   1 ? 
HETATM 2634 O O   . HOH   F 4 .   ? 110.515 13.173 -16.295 1    48.51 ?  761 HOH   A O   1 ? 
HETATM 2635 O O   . HOH   F 4 .   ? 103.997 14.13  -10.432 1    75.62 ?  762 HOH   A O   1 ? 
HETATM 2636 O O   . HOH   F 4 .   ? 128.362 19.71  13.188  1    52.91 ?  763 HOH   A O   1 ? 
HETATM 2637 O O   . HOH   F 4 .   ? 125.669 37.619 7.309   1    57.5  ?  764 HOH   A O   1 ? 
HETATM 2638 O O   . HOH   F 4 .   ? 128.794 -1.565 10.955  1    63.06 ?  765 HOH   A O   1 ? 
HETATM 2639 O O   . HOH   F 4 .   ? 108.244 11.546 15.365  1    52.15 ?  766 HOH   A O   1 ? 
HETATM 2640 O O   . HOH   F 4 .   ? 149.154 30.557 -6.063  1    66.54 ?  767 HOH   A O   1 ? 
HETATM 2641 O O   . HOH   F 4 .   ? 96.272  16.918 -3.598  1    63.52 ?  768 HOH   A O   1 ? 
HETATM 2642 O O   . HOH   F 4 .   ? 117.372 30.671 14.904  1    26.24 ?  769 HOH   A O   1 ? 
HETATM 2643 O O   . HOH   F 4 .   ? 105.192 10.599 -10.721 1    63.78 ?  770 HOH   A O   1 ? 
HETATM 2644 O O   . HOH   F 4 .   ? 105.66  9.179  13.293  1    51    ?  771 HOH   A O   1 ? 
HETATM 2645 O O   . HOH   F 4 .   ? 113.795 3.769  13.822  1    43.87 ?  772 HOH   A O   1 ? 
HETATM 2646 O O   . HOH   F 4 .   ? 115.173 31.857 15.944  1    42.65 ?  773 HOH   A O   1 ? 
HETATM 2647 O O   . HOH   F 4 .   ? 106.306 23.289 19.899  1    68.96 ?  774 HOH   A O   1 ? 
HETATM 2648 O O   . HOH   F 4 .   ? 139.449 37.589 2.545   1    74.68 ?  775 HOH   A O   1 ? 
HETATM 2649 O O   . HOH   F 4 .   ? 116.493 38.534 16.128  1    64.72 ?  776 HOH   A O   1 ? 
HETATM 2650 O O   . HOH   F 4 .   ? 127.083 37.234 10.078  1    72.76 ?  777 HOH   A O   1 ? 
HETATM 2651 O O   . HOH   F 4 .   ? 120.423 9.447  20.102  1    48.62 ?  778 HOH   A O   1 ? 
HETATM 2652 O O   . HOH   F 4 .   ? 126.892 35.548 -8.569  1    51.91 ?  779 HOH   A O   1 ? 
HETATM 2653 O O   . HOH   F 4 .   ? 123.709 13.8   -21.576 1    50    ?  780 HOH   A O   1 ? 
HETATM 2654 O O   . HOH   F 4 .   ? 133.879 20.754 -11.72  1    69.02 ?  781 HOH   A O   1 ? 
HETATM 2655 O O   . HOH   F 4 .   ? 115.629 47.739 2.352   1    59.08 ?  782 HOH   A O   1 ? 
HETATM 2656 O O   . HOH   F 4 .   ? 106.049 43.575 -7.034  1    61.85 ?  783 HOH   A O   1 ? 
HETATM 2657 O O   . HOH   F 4 .   ? 114.075 28.944 19.255  1    62.37 ?  784 HOH   A O   1 ? 
HETATM 2658 O O   . HOH   F 4 .   ? 119.041 43.036 -3.469  1    52.58 ?  785 HOH   A O   1 ? 
HETATM 2659 O O   . HOH   F 4 .   ? 107.439 23.735 -11.77  1    57.34 ?  786 HOH   A O   1 ? 
HETATM 2660 O O   . HOH   F 4 .   ? 112.465 0.729  13.088  1    47.1  ?  787 HOH   A O   1 ? 
HETATM 2661 O O   . HOH   F 4 .   ? 104.226 39.009 -5.947  1    54.09 ?  788 HOH   A O   1 ? 
HETATM 2662 O O   . HOH   F 4 .   ? 117.56  43.424 11.715  1    56.72 ?  789 HOH   A O   1 ? 
HETATM 2663 O O   . HOH   F 4 .   ? 117.529 5.674  19.399  1    63.53 ?  790 HOH   A O   1 ? 
HETATM 2664 O O   . HOH   F 4 .   ? 98.176  7.929  -2.183  1    68.05 ?  791 HOH   A O   1 ? 
HETATM 2665 O O   . HOH   F 4 .   ? 126.192 20.4   12.605  1    52.78 ?  792 HOH   A O   1 ? 
HETATM 2666 O O   . HOH   F 4 .   ? 113.524 7.682  -21.382 1    61.06 ?  793 HOH   A O   1 ? 
HETATM 2667 O O   . HOH   F 4 .   ? 135.71  13.604 2.484   1    54.35 ?  794 HOH   A O   1 ? 
HETATM 2668 O O   . HOH   F 4 .   ? 124.714 19.82  18.592  1    71.96 ?  795 HOH   A O   1 ? 
HETATM 2669 O O   . HOH   F 4 .   ? 101.688 29.011 7.208   1    55.05 ?  796 HOH   A O   1 ? 
HETATM 2670 O O   . HOH   F 4 .   ? 136.771 31.131 4.251   1    66.52 ?  797 HOH   A O   1 ? 
HETATM 2671 O O   . HOH   F 4 .   ? 121.964 9.098  -21.832 1    58.25 ?  798 HOH   A O   1 ? 
HETATM 2672 O O   . HOH   F 4 .   ? 115.066 3.507  16.473  1    59.67 ?  799 HOH   A O   1 ? 
HETATM 2673 O O   . HOH   F 4 .   ? 122.754 18.357 -21.522 1    36.81 ?  800 HOH   A O   1 ? 
HETATM 2674 O O   . HOH   F 4 .   ? 119.296 31.367 16.723  1    35.41 ?  801 HOH   A O   1 ? 
HETATM 2675 O O   . HOH   F 4 .   ? 129.311 36.137 -9.802  1    69.14 ?  802 HOH   A O   1 ? 
HETATM 2676 O O   . HOH   F 4 .   ? 113.964 10.113 -22.345 1    52.08 ?  803 HOH   A O   1 ? 
HETATM 2677 O O   . HOH   F 4 .   ? 103.467 11.144 -8.282  1    58.57 ?  804 HOH   A O   1 ? 
HETATM 2678 O O   . HOH   F 4 .   ? 132.571 35.254 2.103   1    75.71 ?  805 HOH   A O   1 ? 
HETATM 2679 O O   . HOH   F 4 .   ? 139.605 23.446 3.683   1    74.87 ?  806 HOH   A O   1 ? 
HETATM 2680 O O   . HOH   F 4 .   ? 117.87  33.859 17.994  1    66.99 ?  807 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  ? 0.8818 0.5563 0.5592 0.0406  -0.0297 0.001   6   SER   A N   
2    C CA  . SER   A 26  ? 0.878  0.5655 0.5681 0.0394  -0.0273 0.0004  6   SER   A CA  
3    C C   . SER   A 26  ? 0.8435 0.5384 0.5425 0.0383  -0.0252 0.0004  6   SER   A C   
4    O O   . SER   A 26  ? 0.8498 0.5418 0.5483 0.0362  -0.0274 0.0007  6   SER   A O   
5    C CB  . SER   A 26  ? 0.9159 0.6055 0.6101 0.0354  -0.0298 0.0001  6   SER   A CB  
6    O OG  . SER   A 26  ? 0.9673 0.6658 0.6693 0.0353  -0.0276 -0.0005 6   SER   A OG  
7    N N   . PRO   A 27  ? 0.8049 0.5086 0.5119 0.0401  -0.0214 0       7   PRO   A N   
8    C CA  . PRO   A 27  ? 0.7606 0.4712 0.4761 0.0393  -0.019  0       7   PRO   A CA  
9    C C   . PRO   A 27  ? 0.6925 0.4075 0.4142 0.0347  -0.0214 -0.0001 7   PRO   A C   
10   O O   . PRO   A 27  ? 0.689  0.4062 0.4136 0.0322  -0.0233 -0.0004 7   PRO   A O   
11   C CB  . PRO   A 27  ? 0.7794 0.4991 0.5046 0.0412  -0.0162 -0.0006 7   PRO   A CB  
12   C CG  . PRO   A 27  ? 0.809  0.5241 0.5285 0.0447  -0.016  -0.0007 7   PRO   A CG  
13   C CD  . PRO   A 27  ? 0.8003 0.5076 0.5099 0.0429  -0.02   -0.0006 7   PRO   A CD  
14   N N   . ARG   A 28  ? 0.6464 0.3613 0.3696 0.034   -0.0208 0.0002  8   ARG   A N   
15   C CA  . ARG   A 28  ? 0.6144 0.334  0.3449 0.03    -0.0228 0.0001  8   ARG   A CA  
16   C C   . ARG   A 28  ? 0.564  0.2945 0.305  0.0291  -0.0204 -0.0005 8   ARG   A C   
17   O O   . ARG   A 28  ? 0.5506 0.2852 0.2948 0.0314  -0.0173 -0.0007 8   ARG   A O   
18   C CB  . ARG   A 28  ? 0.6437 0.3597 0.3723 0.0298  -0.0234 0.0004  8   ARG   A CB  
19   C CG  . ARG   A 28  ? 0.6807 0.3943 0.4114 0.0262  -0.0285 0.0005  8   ARG   A CG  
20   C CD  . ARG   A 28  ? 0.6313 0.3323 0.3519 0.0269  -0.0331 0.0008  8   ARG   A CD  
21   N NE  . ARG   A 28  ? 0.6501 0.3533 0.377  0.0247  -0.0353 0.0007  8   ARG   A NE  
22   C CZ  . ARG   A 28  ? 0.6401 0.3336 0.3598 0.0255  -0.0392 0.0007  8   ARG   A CZ  
23   N NH1 . ARG   A 28  ? 0.6488 0.328  0.3532 0.0285  -0.0415 0.0009  8   ARG   A NH1 
24   N NH2 . ARG   A 28  ? 0.6282 0.3246 0.3548 0.0236  -0.0412 0.0005  8   ARG   A NH2 
25   N N   . ARG   A 29  ? 0.5334 0.2672 0.2794 0.026   -0.0217 -0.0006 9   ARG   A N   
26   C CA  . ARG   A 29  ? 0.5193 0.2605 0.2723 0.0252  -0.02   -0.0011 9   ARG   A CA  
27   C C   . ARG   A 29  ? 0.5088 0.2545 0.269  0.0222  -0.0196 -0.0009 9   ARG   A C   
28   O O   . ARG   A 29  ? 0.533  0.2761 0.2943 0.02    -0.0213 -0.0003 9   ARG   A O   
29   C CB  . ARG   A 29  ? 0.5358 0.2746 0.2859 0.0249  -0.0207 -0.0014 9   ARG   A CB  
30   C CG  . ARG   A 29  ? 0.5961 0.3307 0.3393 0.0282  -0.0213 -0.0017 9   ARG   A CG  
31   C CD  . ARG   A 29  ? 0.6571 0.3876 0.3956 0.028   -0.0221 -0.002  9   ARG   A CD  
32   N NE  . ARG   A 29  ? 0.7132 0.4393 0.4449 0.0313  -0.0232 -0.0024 9   ARG   A NE  
33   C CZ  . ARG   A 29  ? 0.7667 0.4944 0.4988 0.0343  -0.0237 -0.0034 9   ARG   A CZ  
34   N NH1 . ARG   A 29  ? 0.7372 0.4698 0.475  0.0342  -0.0239 -0.0042 9   ARG   A NH1 
35   N NH2 . ARG   A 29  ? 0.7887 0.5122 0.5152 0.0374  -0.0247 -0.0037 9   ARG   A NH2 
36   N N   . THR   A 30  ? 0.4787 0.2304 0.2443 0.0221  -0.0179 -0.0014 10  THR   A N   
37   C CA  . THR   A 30  ? 0.4739 0.2294 0.2457 0.0195  -0.0171 -0.0011 10  THR   A CA  
38   C C   . THR   A 30  ? 0.4995 0.2521 0.2714 0.0173  -0.0168 -0.0006 10  THR   A C   
39   O O   . THR   A 30  ? 0.4979 0.2458 0.2644 0.018   -0.0172 -0.0006 10  THR   A O   
40   C CB  . THR   A 30  ? 0.4758 0.2367 0.2517 0.0201  -0.0158 -0.0019 10  THR   A CB  
41   O OG1 . THR   A 30  ? 0.5054 0.2639 0.2777 0.0211  -0.0163 -0.0025 10  THR   A OG1 
42   C CG2 . THR   A 30  ? 0.4641 0.2284 0.2424 0.0223  -0.0151 -0.0024 10  THR   A CG2 
43   N N   . PRO   A 31  ? 0.5022 0.2571 0.2804 0.0148  -0.0154 0       11  PRO   A N   
44   C CA  . PRO   A 31  ? 0.5031 0.2546 0.2825 0.013   -0.0134 0.0008  11  PRO   A CA  
45   C C   . PRO   A 31  ? 0.518  0.2662 0.2909 0.0144  -0.0113 0.0004  11  PRO   A C   
46   O O   . PRO   A 31  ? 0.5559 0.2985 0.3262 0.0137  -0.0089 0.0011  11  PRO   A O   
47   C CB  . PRO   A 31  ? 0.5176 0.2728 0.3063 0.0106  -0.0118 0.0016  11  PRO   A CB  
48   C CG  . PRO   A 31  ? 0.5186 0.2773 0.3096 0.0109  -0.0148 0.0011  11  PRO   A CG  
49   C CD  . PRO   A 31  ? 0.4993 0.2587 0.2838 0.0137  -0.0153 0.0001  11  PRO   A CD  
50   N N   . GLN   A 32  ? 0.4821 0.2324 0.252  0.0167  -0.0125 -0.0008 12  GLN   A N   
51   C CA  . GLN   A 32  ? 0.4955 0.241  0.2579 0.0187  -0.0126 -0.0017 12  GLN   A CA  
52   C C   . GLN   A 32  ? 0.5296 0.2722 0.2859 0.0213  -0.0155 -0.0025 12  GLN   A C   
53   O O   . GLN   A 32  ? 0.541  0.2801 0.2918 0.0236  -0.0174 -0.0036 12  GLN   A O   
54   C CB  . GLN   A 32  ? 0.4883 0.2371 0.2526 0.0195  -0.0133 -0.0026 12  GLN   A CB  
55   C CG  . GLN   A 32  ? 0.4749 0.2261 0.2443 0.0172  -0.0102 -0.0017 12  GLN   A CG  
56   C CD  . GLN   A 32  ? 0.4916 0.2505 0.2702 0.0157  -0.0104 -0.0013 12  GLN   A CD  
57   O OE1 . GLN   A 32  ? 0.4972 0.26   0.2778 0.0167  -0.0125 -0.0019 12  GLN   A OE1 
58   N NE2 . GLN   A 32  ? 0.4947 0.2548 0.2786 0.0134  -0.0078 -0.0002 12  GLN   A NE2 
59   N N   . SER   A 33  ? 0.5308 0.2737 0.2876 0.0212  -0.0163 -0.0021 13  SER   A N   
60   C CA  A SER   A 33  ? 0.5443 0.2841 0.2956 0.0234  -0.0184 -0.0025 13  SER   A CA  
61   C CA  B SER   A 33  ? 0.539  0.2784 0.2899 0.0235  -0.0184 -0.0025 13  SER   A CA  
62   C C   . SER   A 33  ? 0.5514 0.295  0.3044 0.0266  -0.0203 -0.0036 13  SER   A C   
63   O O   . SER   A 33  ? 0.5945 0.3347 0.3427 0.0292  -0.022  -0.0042 13  SER   A O   
64   C CB  A SER   A 33  ? 0.5708 0.3021 0.3134 0.0239  -0.0182 -0.0024 13  SER   A CB  
65   C CB  B SER   A 33  ? 0.5539 0.2848 0.2958 0.0243  -0.0182 -0.0027 13  SER   A CB  
66   O OG  A SER   A 33  ? 0.5907 0.3186 0.3286 0.0255  -0.0186 -0.0033 13  SER   A OG  
67   O OG  B SER   A 33  ? 0.5607 0.2876 0.3026 0.0214  -0.0152 -0.0014 13  SER   A OG  
68   N N   . ILE   A 34  ? 0.5237 0.2742 0.2844 0.0265  -0.0197 -0.0038 14  ILE   A N   
69   C CA  . ILE   A 34  ? 0.5145 0.269  0.2798 0.0292  -0.0205 -0.0045 14  ILE   A CA  
70   C C   . ILE   A 34  ? 0.5167 0.2712 0.282  0.03    -0.0187 -0.0037 14  ILE   A C   
71   O O   . ILE   A 34  ? 0.5139 0.2691 0.2801 0.028   -0.0173 -0.0029 14  ILE   A O   
72   C CB  . ILE   A 34  ? 0.5152 0.2761 0.2891 0.0288  -0.0204 -0.0051 14  ILE   A CB  
73   C CG1 . ILE   A 34  ? 0.5412 0.299  0.3121 0.0285  -0.0228 -0.006  14  ILE   A CG1 
74   C CG2 . ILE   A 34  ? 0.5073 0.2728 0.2891 0.0315  -0.0204 -0.0056 14  ILE   A CG2 
75   C CD1 . ILE   A 34  ? 0.5908 0.3532 0.3692 0.0287  -0.0246 -0.007  14  ILE   A CD1 
76   N N   . PRO   A 35  ? 0.521  0.2737 0.2845 0.033   -0.0185 -0.0038 15  PRO   A N   
77   C CA  . PRO   A 35  ? 0.5087 0.2586 0.2693 0.0342  -0.0161 -0.0028 15  PRO   A CA  
78   C C   . PRO   A 35  ? 0.4955 0.25   0.263  0.0338  -0.013  -0.0024 15  PRO   A C   
79   O O   . PRO   A 35  ? 0.5048 0.2655 0.2816 0.0346  -0.012  -0.003  15  PRO   A O   
80   C CB  . PRO   A 35  ? 0.5283 0.2759 0.2874 0.0381  -0.0155 -0.003  15  PRO   A CB  
81   C CG  . PRO   A 35  ? 0.5425 0.2895 0.3002 0.0385  -0.0193 -0.0041 15  PRO   A CG  
82   C CD  . PRO   A 35  ? 0.5201 0.2717 0.2831 0.036   -0.0206 -0.0047 15  PRO   A CD  
83   N N   . TYR   A 36  ? 0.4891 0.2395 0.2518 0.0328  -0.0118 -0.0016 16  TYR   A N   
84   C CA  . TYR   A 36  ? 0.4972 0.2497 0.264  0.033   -0.0084 -0.0012 16  TYR   A CA  
85   C C   . TYR   A 36  ? 0.5137 0.2661 0.2836 0.0366  -0.0038 -0.0008 16  TYR   A C   
86   O O   . TYR   A 36  ? 0.5179 0.2746 0.2955 0.0367  -0.0003 -0.0007 16  TYR   A O   
87   C CB  . TYR   A 36  ? 0.4887 0.2343 0.2478 0.0319  -0.0089 -0.0005 16  TYR   A CB  
88   C CG  . TYR   A 36  ? 0.4643 0.2127 0.2262 0.0281  -0.0121 -0.0007 16  TYR   A CG  
89   C CD1 . TYR   A 36  ? 0.4518 0.2071 0.2218 0.0264  -0.011  -0.0009 16  TYR   A CD1 
90   C CD2 . TYR   A 36  ? 0.4641 0.2083 0.2219 0.0263  -0.016  -0.0005 16  TYR   A CD2 
91   C CE1 . TYR   A 36  ? 0.4445 0.2022 0.2177 0.0232  -0.0132 -0.001  16  TYR   A CE1 
92   C CE2 . TYR   A 36  ? 0.4611 0.208  0.2238 0.023   -0.018  -0.0005 16  TYR   A CE2 
93   C CZ  . TYR   A 36  ? 0.4493 0.2032 0.2197 0.0216  -0.0164 -0.0007 16  TYR   A CZ  
94   O OH  . TYR   A 36  ? 0.4631 0.2193 0.2386 0.0187  -0.0176 -0.0005 16  TYR   A OH  
95   N N   . GLN   A 37  ? 0.5151 0.2628 0.2802 0.0396  -0.0033 -0.0006 17  GLN   A N   
96   C CA  . GLN   A 37  ? 0.5345 0.2827 0.3052 0.0434  0.0023  -0.0001 17  GLN   A CA  
97   C C   . GLN   A 37  ? 0.5387 0.2976 0.326  0.0435  0.0022  -0.0009 17  GLN   A C   
98   O O   . GLN   A 37  ? 0.5616 0.323  0.3585 0.0459  0.0074  -0.0004 17  GLN   A O   
99   C CB  . GLN   A 37  ? 0.5594 0.3    0.3217 0.0469  0.0032  0.0004  17  GLN   A CB  
100  C CG  . GLN   A 37  ? 0.6202 0.3637 0.3837 0.0468  -0.0021 -0.0007 17  GLN   A CG  
101  C CD  . GLN   A 37  ? 0.746  0.4812 0.4999 0.0501  -0.0016 -0.0002 17  GLN   A CD  
102  O OE1 . GLN   A 37  ? 0.7956 0.5223 0.5412 0.0527  0.0028  0.001   17  GLN   A OE1 
103  N NE2 . GLN   A 37  ? 0.7618 0.4979 0.5149 0.0503  -0.0061 -0.0012 17  GLN   A NE2 
104  N N   . ASP   A 38  ? 0.5157 0.2801 0.307  0.041   -0.0034 -0.0022 18  ASP   A N   
105  C CA  . ASP   A 38  ? 0.5147 0.2875 0.3207 0.0411  -0.0052 -0.0033 18  ASP   A CA  
106  C C   . ASP   A 38  ? 0.5106 0.2887 0.3235 0.0382  -0.0045 -0.0034 18  ASP   A C   
107  O O   . ASP   A 38  ? 0.517  0.3013 0.3414 0.0378  -0.007  -0.0044 18  ASP   A O   
108  C CB  . ASP   A 38  ? 0.5431 0.3157 0.3464 0.0406  -0.012  -0.0047 18  ASP   A CB  
109  C CG  . ASP   A 38  ? 0.6614 0.4292 0.459  0.0435  -0.0137 -0.0049 18  ASP   A CG  
110  O OD1 . ASP   A 38  ? 0.6538 0.4192 0.451  0.0463  -0.0095 -0.004  18  ASP   A OD1 
111  O OD2 . ASP   A 38  ? 0.7198 0.4851 0.5121 0.0432  -0.0189 -0.006  18  ASP   A OD2 
112  N N   . LEU   A 39  ? 0.4953 0.2704 0.301  0.0363  -0.0021 -0.0026 19  LEU   A N   
113  C CA  . LEU   A 39  ? 0.5008 0.2802 0.3115 0.0335  -0.0018 -0.0027 19  LEU   A CA  
114  C C   . LEU   A 39  ? 0.5077 0.2841 0.3165 0.0339  0.0042  -0.0015 19  LEU   A C   
115  O O   . LEU   A 39  ? 0.5104 0.2785 0.3084 0.0354  0.0066  -0.0006 19  LEU   A O   
116  C CB  . LEU   A 39  ? 0.5042 0.2817 0.3065 0.0305  -0.0058 -0.003  19  LEU   A CB  
117  C CG  . LEU   A 39  ? 0.5182 0.296  0.3189 0.03    -0.0109 -0.0041 19  LEU   A CG  
118  C CD1 . LEU   A 39  ? 0.5297 0.3044 0.3228 0.0273  -0.0127 -0.0038 19  LEU   A CD1 
119  C CD2 . LEU   A 39  ? 0.5205 0.3036 0.3309 0.0299  -0.0135 -0.0052 19  LEU   A CD2 
120  N N   . PRO   A 40  ? 0.4934 0.2745 0.3107 0.0325  0.0063  -0.0016 20  PRO   A N   
121  C CA  . PRO   A 40  ? 0.4794 0.2557 0.292  0.0326  0.0118  -0.0004 20  PRO   A CA  
122  C C   . PRO   A 40  ? 0.4626 0.2325 0.2615 0.0309  0.0085  -0.0003 20  PRO   A C   
123  O O   . PRO   A 40  ? 0.4537 0.2273 0.253  0.0282  0.0034  -0.0011 20  PRO   A O   
124  C CB  . PRO   A 40  ? 0.4953 0.2788 0.3201 0.0307  0.0132  -0.0008 20  PRO   A CB  
125  C CG  . PRO   A 40  ? 0.5115 0.3031 0.3488 0.0302  0.0088  -0.002  20  PRO   A CG  
126  C CD  . PRO   A 40  ? 0.4944 0.2838 0.3237 0.0306  0.0031  -0.0027 20  PRO   A CD  
127  N N   . HIS   A 41  ? 0.4673 0.2269 0.2543 0.0326  0.0111  0.0006  21  HIS   A N   
128  C CA  . HIS   A 41  ? 0.471  0.224  0.2465 0.0312  0.0066  0.0006  21  HIS   A CA  
129  C C   . HIS   A 41  ? 0.4933 0.2341 0.2565 0.0331  0.0095  0.0015  21  HIS   A C   
130  O O   . HIS   A 41  ? 0.5293 0.2653 0.2909 0.0359  0.0163  0.0023  21  HIS   A O   
131  C CB  . HIS   A 41  ? 0.4621 0.2122 0.2317 0.0313  0.0018  0.0004  21  HIS   A CB  
132  C CG  . HIS   A 41  ? 0.4929 0.2347 0.2544 0.0349  0.0045  0.0011  21  HIS   A CG  
133  N ND1 . HIS   A 41  ? 0.5275 0.2737 0.296  0.037   0.0074  0.001   21  HIS   A ND1 
134  C CD2 . HIS   A 41  ? 0.5524 0.2808 0.2991 0.0371  0.0049  0.0018  21  HIS   A CD2 
135  C CE1 . HIS   A 41  ? 0.5519 0.2881 0.3101 0.0404  0.0099  0.0019  21  HIS   A CE1 
136  N NE2 . HIS   A 41  ? 0.5766 0.3011 0.3206 0.0406  0.0088  0.0024  21  HIS   A NE2 
137  N N   . LEU   A 42  ? 0.4897 0.2244 0.2444 0.0317  0.0044  0.0013  22  LEU   A N   
138  C CA  . LEU   A 42  ? 0.5177 0.2377 0.2575 0.0336  0.0047  0.0018  22  LEU   A CA  
139  C C   . LEU   A 42  ? 0.5415 0.2551 0.2736 0.0325  -0.0037 0.0014  22  LEU   A C   
140  O O   . LEU   A 42  ? 0.572  0.2943 0.3128 0.0294  -0.0084 0.0008  22  LEU   A O   
141  C CB  . LEU   A 42  ? 0.5419 0.2641 0.285  0.032   0.0057  0.0016  22  LEU   A CB  
142  C CG  . LEU   A 42  ? 0.6452 0.3526 0.3741 0.0342  0.0071  0.0021  22  LEU   A CG  
143  C CD1 . LEU   A 42  ? 0.6632 0.3617 0.3851 0.0382  0.0167  0.0033  22  LEU   A CD1 
144  C CD2 . LEU   A 42  ? 0.649  0.3619 0.3842 0.0319  0.0069  0.0016  22  LEU   A CD2 
145  N N   . VAL   A 43  ? 0.4919 0.1892 0.2075 0.0352  -0.0055 0.0018  23  VAL   A N   
146  C CA  . VAL   A 43  ? 0.5059 0.1964 0.2156 0.0339  -0.0146 0.0013  23  VAL   A CA  
147  C C   . VAL   A 43  ? 0.5243 0.2049 0.2263 0.0339  -0.0191 0.0009  23  VAL   A C   
148  O O   . VAL   A 43  ? 0.5451 0.2124 0.2334 0.0371  -0.0158 0.0013  23  VAL   A O   
149  C CB  . VAL   A 43  ? 0.5274 0.2049 0.223  0.037   -0.0157 0.0017  23  VAL   A CB  
150  C CG1 . VAL   A 43  ? 0.5381 0.2099 0.2307 0.035   -0.0258 0.0011  23  VAL   A CG1 
151  C CG2 . VAL   A 43  ? 0.5259 0.2124 0.2286 0.0376  -0.0109 0.002   23  VAL   A CG2 
152  N N   . ASN   A 44  ? 0.5148 0.2011 0.2259 0.0305  -0.0262 0.0003  24  ASN   A N   
153  C CA  . ASN   A 44  ? 0.5139 0.1922 0.2204 0.0303  -0.0314 -0.0002 24  ASN   A CA  
154  C C   . ASN   A 44  ? 0.5548 0.213  0.2444 0.0325  -0.0398 -0.0006 24  ASN   A C   
155  O O   . ASN   A 44  ? 0.5702 0.2206 0.2511 0.0341  -0.0412 -0.0003 24  ASN   A O   
156  C CB  . ASN   A 44  ? 0.5194 0.212  0.244  0.0262  -0.0348 -0.0007 24  ASN   A CB  
157  C CG  . ASN   A 44  ? 0.5242 0.2196 0.2575 0.0235  -0.0424 -0.001  24  ASN   A CG  
158  O OD1 . ASN   A 44  ? 0.5251 0.2119 0.2512 0.0243  -0.0465 -0.0009 24  ASN   A OD1 
159  N ND2 . ASN   A 44  ? 0.4985 0.2061 0.2484 0.02    -0.0437 -0.0011 24  ASN   A ND2 
160  N N   . ALA   A 45  ? 0.5779 0.2268 0.2622 0.0328  -0.0461 -0.0012 25  ALA   A N   
161  C CA  . ALA   A 45  ? 0.617  0.2444 0.2841 0.0352  -0.0558 -0.0018 25  ALA   A CA  
162  C C   . ALA   A 45  ? 0.6398 0.2684 0.3145 0.0328  -0.0653 -0.0022 25  ALA   A C   
163  O O   . ALA   A 45  ? 0.6838 0.2939 0.3429 0.035   -0.0727 -0.0026 25  ALA   A O   
164  C CB  . ALA   A 45  ? 0.6221 0.2396 0.2833 0.036   -0.0615 -0.0026 25  ALA   A CB  
165  N N   . ASP   A 46  ? 0.6177 0.2656 0.3148 0.0285  -0.065  -0.0021 26  ASP   A N   
166  C CA  . ASP   A 46  ? 0.6224 0.2733 0.3296 0.0257  -0.0721 -0.0022 26  ASP   A CA  
167  C C   . ASP   A 46  ? 0.6189 0.2738 0.3247 0.0259  -0.0668 -0.0016 26  ASP   A C   
168  O O   . ASP   A 46  ? 0.6286 0.2881 0.3444 0.0232  -0.0707 -0.0015 26  ASP   A O   
169  C CB  . ASP   A 46  ? 0.6347 0.3027 0.3666 0.0212  -0.0735 -0.0023 26  ASP   A CB  
170  C CG  . ASP   A 46  ? 0.7321 0.3949 0.4672 0.0209  -0.0813 -0.0031 26  ASP   A CG  
171  O OD1 . ASP   A 46  ? 0.7961 0.4409 0.5181 0.0231  -0.0908 -0.0038 26  ASP   A OD1 
172  O OD2 . ASP   A 46  ? 0.7108 0.3864 0.4605 0.0189  -0.0783 -0.0029 26  ASP   A OD2 
173  N N   . GLY   A 47  ? 0.5973 0.2515 0.293  0.0288  -0.0576 -0.001  27  GLY   A N   
174  C CA  . GLY   A 47  ? 0.5784 0.2365 0.2731 0.0294  -0.0525 -0.0004 27  GLY   A CA  
175  C C   . GLY   A 47  ? 0.5647 0.2429 0.278  0.0262  -0.0472 -0.0002 27  GLY   A C   
176  O O   . GLY   A 47  ? 0.5705 0.2523 0.2849 0.0262  -0.0448 0.0001  27  GLY   A O   
177  N N   . GLN   A 48  ? 0.5301 0.2202 0.2568 0.0238  -0.0453 -0.0003 28  GLN   A N   
178  C CA  . GLN   A 48  ? 0.5203 0.2272 0.2624 0.0212  -0.0403 -0.0001 28  GLN   A CA  
179  C C   . GLN   A 48  ? 0.5036 0.217  0.2452 0.023   -0.0318 0.0001  28  GLN   A C   
180  O O   . GLN   A 48  ? 0.4967 0.2073 0.2338 0.0246  -0.0291 0       28  GLN   A O   
181  C CB  . GLN   A 48  ? 0.5262 0.242  0.2834 0.0178  -0.0425 -0.0002 28  GLN   A CB  
182  C CG  . GLN   A 48  ? 0.5513 0.2627 0.3145 0.0156  -0.0508 -0.0003 28  GLN   A CG  
183  C CD  . GLN   A 48  ? 0.5616 0.2793 0.3388 0.0131  -0.053  -0.0003 28  GLN   A CD  
184  O OE1 . GLN   A 48  ? 0.5476 0.2629 0.322  0.0141  -0.0539 -0.0007 28  GLN   A OE1 
185  N NE2 . GLN   A 48  ? 0.5804 0.3057 0.373  0.01    -0.0532 0.0002  28  GLN   A NE2 
186  N N   . TYR   A 49  ? 0.4859 0.2075 0.2326 0.0227  -0.0279 0.0002  29  TYR   A N   
187  C CA  . TYR   A 49  ? 0.4678 0.1966 0.2173 0.0241  -0.021  0.0002  29  TYR   A CA  
188  C C   . TYR   A 49  ? 0.468  0.208  0.2294 0.0217  -0.0191 -0.0001 29  TYR   A C   
189  O O   . TYR   A 49  ? 0.4704 0.2165 0.24   0.0191  -0.0209 -0.0001 29  TYR   A O   
190  C CB  . TYR   A 49  ? 0.4601 0.1926 0.2108 0.0249  -0.0191 0.0002  29  TYR   A CB  
191  C CG  . TYR   A 49  ? 0.4961 0.2187 0.2351 0.0284  -0.0181 0.0005  29  TYR   A CG  
192  C CD1 . TYR   A 49  ? 0.5258 0.2371 0.2547 0.0288  -0.023  0.0007  29  TYR   A CD1 
193  C CD2 . TYR   A 49  ? 0.5036 0.2276 0.2421 0.0314  -0.0123 0.0008  29  TYR   A CD2 
194  C CE1 . TYR   A 49  ? 0.5283 0.2291 0.2447 0.0323  -0.022  0.0011  29  TYR   A CE1 
195  C CE2 . TYR   A 49  ? 0.5156 0.2302 0.2436 0.0349  -0.0105 0.0013  29  TYR   A CE2 
196  C CZ  . TYR   A 49  ? 0.5337 0.2364 0.2497 0.0354  -0.0152 0.0014  29  TYR   A CZ  
197  O OH  . TYR   A 49  ? 0.5536 0.2452 0.2571 0.0392  -0.0132 0.002   29  TYR   A OH  
198  N N   . LEU   A 50  ? 0.4513 0.193  0.2131 0.0229  -0.015  -0.0001 30  LEU   A N   
199  C CA  . LEU   A 50  ? 0.4402 0.1917 0.2121 0.0209  -0.013  -0.0003 30  LEU   A CA  
200  C C   . LEU   A 50  ? 0.4461 0.2042 0.223  0.022   -0.0085 -0.0005 30  LEU   A C   
201  O O   . LEU   A 50  ? 0.4522 0.2072 0.226  0.0246  -0.0047 -0.0003 30  LEU   A O   
202  C CB  . LEU   A 50  ? 0.4445 0.1925 0.2139 0.0212  -0.0122 -0.0003 30  LEU   A CB  
203  C CG  . LEU   A 50  ? 0.4876 0.2271 0.2515 0.0207  -0.0179 -0.0003 30  LEU   A CG  
204  C CD1 . LEU   A 50  ? 0.5101 0.2469 0.2721 0.021   -0.0171 -0.0004 30  LEU   A CD1 
205  C CD2 . LEU   A 50  ? 0.5038 0.2485 0.2768 0.0177  -0.0224 -0.0004 30  LEU   A CD2 
206  N N   . PHE   A 51  ? 0.4235 0.19   0.2088 0.0202  -0.0087 -0.001  31  PHE   A N   
207  C CA  . PHE   A 51  ? 0.4353 0.2077 0.2266 0.0211  -0.0062 -0.0014 31  PHE   A CA  
208  C C   . PHE   A 51  ? 0.4306 0.2065 0.2271 0.0209  -0.003  -0.0014 31  PHE   A C   
209  O O   . PHE   A 51  ? 0.4277 0.2049 0.2255 0.0189  -0.0038 -0.0015 31  PHE   A O   
210  C CB  . PHE   A 51  ? 0.4218 0.199  0.2174 0.0195  -0.0084 -0.0019 31  PHE   A CB  
211  C CG  . PHE   A 51  ? 0.4266 0.2093 0.229  0.02    -0.0076 -0.0027 31  PHE   A CG  
212  C CD1 . PHE   A 51  ? 0.4511 0.2343 0.2552 0.0223  -0.0077 -0.0031 31  PHE   A CD1 
213  C CD2 . PHE   A 51  ? 0.4389 0.2258 0.2466 0.0185  -0.0075 -0.0031 31  PHE   A CD2 
214  C CE1 . PHE   A 51  ? 0.4651 0.253  0.2773 0.0228  -0.0085 -0.004  31  PHE   A CE1 
215  C CE2 . PHE   A 51  ? 0.4553 0.2462 0.2696 0.019   -0.0081 -0.0039 31  PHE   A CE2 
216  C CZ  . PHE   A 51  ? 0.4591 0.2505 0.2762 0.0211  -0.0089 -0.0044 31  PHE   A CZ  
217  N N   . CYS   A 52  ? 0.4217 0.199  0.2222 0.0228  0.0008  -0.0014 32  CYS   A N   
218  C CA  . CYS   A 52  ? 0.4306 0.2105 0.2368 0.0226  0.0047  -0.0013 32  CYS   A CA  
219  C C   . CYS   A 52  ? 0.4321 0.2201 0.2507 0.0222  0.0048  -0.002  32  CYS   A C   
220  O O   . CYS   A 52  ? 0.4331 0.2234 0.2556 0.0233  0.0032  -0.0024 32  CYS   A O   
221  C CB  . CYS   A 52  ? 0.4516 0.2242 0.2528 0.0253  0.0102  -0.0003 32  CYS   A CB  
222  S SG  . CYS   A 52  ? 0.4831 0.2424 0.267  0.0263  0.0089  0.0003  32  CYS   A SG  
223  N N   . ARG   A 53  ? 0.4213 0.2128 0.2462 0.0209  0.0066  -0.0021 33  ARG   A N   
224  C CA  . ARG   A 53  ? 0.4246 0.2229 0.2624 0.0204  0.0063  -0.0028 33  ARG   A CA  
225  C C   . ARG   A 53  ? 0.4396 0.2385 0.2841 0.0206  0.0123  -0.0021 33  ARG   A C   
226  O O   . ARG   A 53  ? 0.4413 0.2357 0.2788 0.0202  0.0153  -0.0015 33  ARG   A O   
227  C CB  . ARG   A 53  ? 0.4459 0.2476 0.2851 0.018   0.0017  -0.0037 33  ARG   A CB  
228  C CG  . ARG   A 53  ? 0.462  0.2624 0.2954 0.0177  -0.0031 -0.0042 33  ARG   A CG  
229  C CD  . ARG   A 53  ? 0.4641 0.2662 0.2991 0.0159  -0.0066 -0.0051 33  ARG   A CD  
230  N NE  . ARG   A 53  ? 0.443  0.2414 0.27   0.0159  -0.0096 -0.0052 33  ARG   A NE  
231  C CZ  . ARG   A 53  ? 0.4614 0.258  0.2872 0.0171  -0.0133 -0.0061 33  ARG   A CZ  
232  N NH1 . ARG   A 53  ? 0.4662 0.2652 0.3    0.0182  -0.0157 -0.007  33  ARG   A NH1 
233  N NH2 . ARG   A 53  ? 0.4575 0.2493 0.2747 0.0171  -0.0147 -0.006  33  ARG   A NH2 
234  N N   . TYR   A 54  ? 0.4562 0.26   0.3148 0.0214  0.0141  -0.0023 34  TYR   A N   
235  C CA  . TYR   A 54  ? 0.4642 0.2687 0.3321 0.0215  0.0208  -0.0015 34  TYR   A CA  
236  C C   . TYR   A 54  ? 0.4722 0.2848 0.3578 0.0201  0.0178  -0.0025 34  TYR   A C   
237  O O   . TYR   A 54  ? 0.4789 0.2953 0.3714 0.0206  0.0122  -0.0036 34  TYR   A O   
238  C CB  . TYR   A 54  ? 0.4659 0.2661 0.3352 0.0247  0.0285  -0.0002 34  TYR   A CB  
239  C CG  . TYR   A 54  ? 0.4658 0.2557 0.316  0.0265  0.0306  0.0007  34  TYR   A CG  
240  C CD1 . TYR   A 54  ? 0.4723 0.2538 0.3109 0.0266  0.0349  0.0016  34  TYR   A CD1 
241  C CD2 . TYR   A 54  ? 0.475  0.2625 0.3178 0.028   0.0271  0.0005  34  TYR   A CD2 
242  C CE1 . TYR   A 54  ? 0.4778 0.2484 0.2981 0.0282  0.0345  0.0021  34  TYR   A CE1 
243  C CE2 . TYR   A 54  ? 0.4921 0.2695 0.3174 0.0293  0.0274  0.0012  34  TYR   A CE2 
244  C CZ  . TYR   A 54  ? 0.4938 0.2627 0.308  0.0294  0.0305  0.0019  34  TYR   A CZ  
245  O OH  . TYR   A 54  ? 0.5128 0.2703 0.3095 0.0308  0.0292  0.0023  34  TYR   A OH  
246  N N   . TRP   A 55  ? 0.4579 0.2721 0.35   0.0184  0.0207  -0.0023 35  TRP   A N   
247  C CA  . TRP   A 55  ? 0.4636 0.2846 0.3736 0.0169  0.0179  -0.0032 35  TRP   A CA  
248  C C   . TRP   A 55  ? 0.482  0.3027 0.4022 0.0169  0.0274  -0.0018 35  TRP   A C   
249  O O   . TRP   A 55  ? 0.4994 0.3168 0.4131 0.0156  0.0312  -0.0012 35  TRP   A O   
250  C CB  . TRP   A 55  ? 0.4545 0.2765 0.3602 0.0142  0.011   -0.0044 35  TRP   A CB  
251  C CG  . TRP   A 55  ? 0.4531 0.2734 0.347  0.0141  0.0033  -0.0055 35  TRP   A CG  
252  C CD1 . TRP   A 55  ? 0.4708 0.2923 0.3682 0.014   -0.0049 -0.007  35  TRP   A CD1 
253  C CD2 . TRP   A 55  ? 0.4313 0.2469 0.3079 0.0139  0.0031  -0.0051 35  TRP   A CD2 
254  N NE1 . TRP   A 55  ? 0.47   0.2873 0.3523 0.0138  -0.0089 -0.0074 35  TRP   A NE1 
255  C CE2 . TRP   A 55  ? 0.4477 0.2623 0.3189 0.0136  -0.004  -0.0062 35  TRP   A CE2 
256  C CE3 . TRP   A 55  ? 0.4193 0.2306 0.285  0.0141  0.0079  -0.004  35  TRP   A CE3 
257  C CZ2 . TRP   A 55  ? 0.4293 0.2399 0.2867 0.0132  -0.0051 -0.006  35  TRP   A CZ2 
258  C CZ3 . TRP   A 55  ? 0.413  0.221  0.2661 0.0136  0.0051  -0.004  35  TRP   A CZ3 
259  C CH2 . TRP   A 55  ? 0.4189 0.2273 0.2691 0.013   -0.0007 -0.0049 35  TRP   A CH2 
260  N N   . ALA   A 56  ? 0.4933 0.3165 0.4289 0.0187  0.0321  -0.0011 36  ALA   A N   
261  C CA  . ALA   A 56  ? 0.5218 0.3433 0.4675 0.0192  0.0433  0.0006  36  ALA   A CA  
262  C C   . ALA   A 56  ? 0.5512 0.3811 0.5235 0.0176  0.0423  0.0002  36  ALA   A C   
263  O O   . ALA   A 56  ? 0.5506 0.3868 0.5368 0.0177  0.0347  -0.0011 36  ALA   A O   
264  C CB  . ALA   A 56  ? 0.5366 0.3527 0.4797 0.023   0.0521  0.0023  36  ALA   A CB  
265  N N   . PRO   A 57  ? 0.5691 0.3984 0.549  0.0159  0.0492  0.0011  37  PRO   A N   
266  C CA  . PRO   A 57  ? 0.5921 0.4293 0.6002 0.014   0.0483  0.0008  37  PRO   A CA  
267  C C   . PRO   A 57  ? 0.6506 0.4909 0.6804 0.0165  0.0555  0.0021  37  PRO   A C   
268  O O   . PRO   A 57  ? 0.6564 0.491  0.6773 0.0197  0.0639  0.0037  37  PRO   A O   
269  C CB  . PRO   A 57  ? 0.5884 0.4222 0.5953 0.0119  0.0555  0.0017  37  PRO   A CB  
270  C CG  . PRO   A 57  ? 0.5882 0.4109 0.5709 0.014   0.0646  0.0033  37  PRO   A CG  
271  C CD  . PRO   A 57  ? 0.5724 0.3927 0.5361 0.0159  0.0582  0.0025  37  PRO   A CD  
272  N N   . THR   A 58  ? 0.683  0.5319 0.7422 0.0151  0.0521  0.0015  38  THR   A N   
273  C CA  . THR   A 58  ? 0.712  0.5651 0.7966 0.0173  0.0591  0.0028  38  THR   A CA  
274  C C   . THR   A 58  ? 0.7432 0.5907 0.8321 0.0185  0.0775  0.0059  38  THR   A C   
275  O O   . THR   A 58  ? 0.7512 0.5971 0.8489 0.0218  0.0874  0.0077  38  THR   A O   
276  C CB  . THR   A 58  ? 0.7218 0.5853 0.8381 0.0155  0.0488  0.0011  38  THR   A CB  
277  O OG1 . THR   A 58  ? 0.7426 0.608  0.8681 0.0117  0.0474  0.0007  38  THR   A OG1 
278  C CG2 . THR   A 58  ? 0.7275 0.5934 0.8374 0.0158  0.0317  -0.0018 38  THR   A CG2 
279  N N   . GLY   A 59  ? 0.7604 0.6034 0.8419 0.0161  0.0824  0.0065  39  GLY   A N   
280  C CA  . GLY   A 59  ? 0.7758 0.6109 0.8583 0.0173  0.1002  0.0094  39  GLY   A CA  
281  C C   . GLY   A 59  ? 0.7933 0.6136 0.8406 0.0198  0.1082  0.0107  39  GLY   A C   
282  O O   . GLY   A 59  ? 0.8101 0.6269 0.8347 0.0213  0.1015  0.0097  39  GLY   A O   
283  N N   . THR   A 60  ? 0.7814 0.5917 0.824  0.0203  0.1226  0.013   40  THR   A N   
284  C CA  . THR   A 60  ? 0.7802 0.574  0.7883 0.0229  0.1296  0.0141  40  THR   A CA  
285  C C   . THR   A 60  ? 0.7401 0.5335 0.7292 0.0198  0.1186  0.012   40  THR   A C   
286  O O   . THR   A 60  ? 0.736  0.5353 0.737  0.0161  0.1156  0.0113  40  THR   A O   
287  C CB  . THR   A 60  ? 0.8171 0.5982 0.8255 0.0249  0.1488  0.0172  40  THR   A CB  
288  O OG1 . THR   A 60  ? 0.8436 0.6223 0.8633 0.0289  0.1594  0.0193  40  THR   A OG1 
289  C CG2 . THR   A 60  ? 0.84   0.6021 0.8116 0.0269  0.1541  0.0179  40  THR   A CG2 
290  N N   . PRO   A 61  ? 0.711  0.4984 0.6729 0.0211  0.1117  0.011   41  PRO   A N   
291  C CA  . PRO   A 61  ? 0.6917 0.4795 0.6378 0.0184  0.1014  0.0092  41  PRO   A CA  
292  C C   . PRO   A 61  ? 0.677  0.453  0.6085 0.0182  0.1092  0.0102  41  PRO   A C   
293  O O   . PRO   A 61  ? 0.6991 0.4611 0.6189 0.0213  0.1215  0.0122  41  PRO   A O   
294  C CB  . PRO   A 61  ? 0.7086 0.4927 0.6326 0.0203  0.0935  0.0082  41  PRO   A CB  
295  C CG  . PRO   A 61  ? 0.7305 0.5059 0.6492 0.0247  0.1027  0.01    41  PRO   A CG  
296  C CD  . PRO   A 61  ? 0.7079 0.488  0.6534 0.0252  0.1129  0.0116  41  PRO   A CD  
297  N N   . LYS   A 62  ? 0.6396 0.42   0.5716 0.0146  0.1026  0.0088  42  LYS   A N   
298  C CA  . LYS   A 62  ? 0.627  0.3965 0.5443 0.0143  0.1085  0.0095  42  LYS   A CA  
299  C C   . LYS   A 62  ? 0.6037 0.3613 0.4894 0.0164  0.1046  0.009   42  LYS   A C   
300  O O   . LYS   A 62  ? 0.6097 0.3528 0.4774 0.018   0.1113  0.01    42  LYS   A O   
301  C CB  . LYS   A 62  ? 0.6621 0.4406 0.5901 0.0098  0.1014  0.0081  42  LYS   A CB  
302  C CG  . LYS   A 62  ? 0.7353 0.5246 0.6951 0.0071  0.1035  0.0083  42  LYS   A CG  
303  C CD  . LYS   A 62  ? 0.8256 0.6218 0.7911 0.0029  0.0943  0.0066  42  LYS   A CD  
304  C CE  . LYS   A 62  ? 0.8823 0.6886 0.8792 -0.0002 0.0939  0.0064  42  LYS   A CE  
305  N NZ  . LYS   A 62  ? 0.9102 0.7234 0.9104 -0.0039 0.0809  0.0042  42  LYS   A NZ  
306  N N   . ALA   A 63  ? 0.5618 0.3253 0.4411 0.0163  0.0928  0.0074  43  ALA   A N   
307  C CA  . ALA   A 63  ? 0.5427 0.2967 0.3961 0.0179  0.0875  0.0068  43  ALA   A CA  
308  C C   . ALA   A 63  ? 0.516  0.2768 0.3684 0.0183  0.0778  0.0057  43  ALA   A C   
309  O O   . ALA   A 63  ? 0.5007 0.2737 0.3711 0.017   0.0743  0.0051  43  ALA   A O   
310  C CB  . ALA   A 63  ? 0.5409 0.2962 0.3885 0.0152  0.0813  0.0056  43  ALA   A CB  
311  N N   . LEU   A 64  ? 0.5149 0.2672 0.3467 0.02    0.0735  0.0053  44  LEU   A N   
312  C CA  . LEU   A 64  ? 0.504  0.2613 0.3327 0.0201  0.0643  0.0043  44  LEU   A CA  
313  C C   . LEU   A 64  ? 0.4844 0.2458 0.3079 0.0177  0.0546  0.0028  44  LEU   A C   
314  O O   . LEU   A 64  ? 0.4918 0.2466 0.3056 0.0175  0.0551  0.0028  44  LEU   A O   
315  C CB  . LEU   A 64  ? 0.5317 0.2747 0.3407 0.0239  0.0662  0.005   44  LEU   A CB  
316  C CG  . LEU   A 64  ? 0.5829 0.3166 0.391  0.0274  0.0777  0.0069  44  LEU   A CG  
317  C CD1 . LEU   A 64  ? 0.614  0.3306 0.3979 0.0313  0.0779  0.0074  44  LEU   A CD1 
318  C CD2 . LEU   A 64  ? 0.5919 0.3385 0.4217 0.0269  0.0789  0.007   44  LEU   A CD2 
319  N N   . ILE   A 65  ? 0.4601 0.2311 0.2889 0.0164  0.0461  0.0017  45  ILE   A N   
320  C CA  . ILE   A 65  ? 0.455  0.2288 0.2787 0.0145  0.0381  0.0006  45  ILE   A CA  
321  C C   . ILE   A 65  ? 0.4493 0.2255 0.2697 0.0149  0.0314  0.0001  45  ILE   A C   
322  O O   . ILE   A 65  ? 0.4346 0.2179 0.2644 0.0147  0.0298  -0.0002 45  ILE   A O   
323  C CB  . ILE   A 65  ? 0.4566 0.2396 0.2921 0.0114  0.0356  -0.0002 45  ILE   A CB  
324  C CG1 . ILE   A 65  ? 0.4615 0.2456 0.2904 0.01    0.0289  -0.001  45  ILE   A CG1 
325  C CG2 . ILE   A 65  ? 0.4557 0.2489 0.3074 0.0102  0.0333  -0.0007 45  ILE   A CG2 
326  C CD1 . ILE   A 65  ? 0.4399 0.229  0.2757 0.0074  0.0277  -0.0016 45  ILE   A CD1 
327  N N   . PHE   A 66  ? 0.4333 0.2037 0.2415 0.0154  0.0272  -0.0001 46  PHE   A N   
328  C CA  . PHE   A 66  ? 0.427  0.1994 0.2329 0.0154  0.021   -0.0005 46  PHE   A CA  
329  C C   . PHE   A 66  ? 0.4191 0.1992 0.2302 0.0129  0.0155  -0.0013 46  PHE   A C   
330  O O   . PHE   A 66  ? 0.4247 0.2033 0.2331 0.012   0.0146  -0.0014 46  PHE   A O   
331  C CB  . PHE   A 66  ? 0.4211 0.1817 0.2119 0.0175  0.0189  -0.0003 46  PHE   A CB  
332  C CG  . PHE   A 66  ? 0.4237 0.1863 0.2137 0.0172  0.0127  -0.0006 46  PHE   A CG  
333  C CD1 . PHE   A 66  ? 0.4327 0.1936 0.221  0.0188  0.0132  -0.0003 46  PHE   A CD1 
334  C CD2 . PHE   A 66  ? 0.4428 0.208  0.2339 0.0156  0.0068  -0.0011 46  PHE   A CD2 
335  C CE1 . PHE   A 66  ? 0.4387 0.2011 0.2266 0.0184  0.0078  -0.0006 46  PHE   A CE1 
336  C CE2 . PHE   A 66  ? 0.4503 0.2177 0.2427 0.0151  0.0021  -0.0012 46  PHE   A CE2 
337  C CZ  . PHE   A 66  ? 0.4339 0.1992 0.2238 0.0165  0.0024  -0.001  46  PHE   A CZ  
338  N N   . VAL   A 67  ? 0.4042 0.1908 0.221  0.0121  0.0121  -0.0017 47  VAL   A N   
339  C CA  . VAL   A 67  ? 0.4035 0.1951 0.2233 0.0103  0.008   -0.0022 47  VAL   A CA  
340  C C   . VAL   A 67  ? 0.4071 0.1965 0.2221 0.0105  0.0041  -0.002  47  VAL   A C   
341  O O   . VAL   A 67  ? 0.4204 0.2088 0.2339 0.0115  0.0031  -0.0019 47  VAL   A O   
342  C CB  . VAL   A 67  ? 0.4265 0.2244 0.2545 0.0095  0.0068  -0.0027 47  VAL   A CB  
343  C CG1 . VAL   A 67  ? 0.4573 0.2574 0.2852 0.0082  0.0032  -0.0031 47  VAL   A CG1 
344  C CG2 . VAL   A 67  ? 0.4365 0.237  0.272  0.0089  0.0097  -0.003  47  VAL   A CG2 
345  N N   . SER   A 68  ? 0.4033 0.1917 0.217  0.0097  0.0021  -0.0019 48  SER   A N   
346  C CA  . SER   A 68  ? 0.3972 0.1835 0.2091 0.0096  -0.0016 -0.0017 48  SER   A CA  
347  C C   . SER   A 68  ? 0.3998 0.191  0.2173 0.0081  -0.0024 -0.0016 48  SER   A C   
348  O O   . SER   A 68  ? 0.3973 0.1901 0.2171 0.0073  -0.0019 -0.0015 48  SER   A O   
349  C CB  . SER   A 68  ? 0.4349 0.2149 0.242  0.0103  -0.0033 -0.0016 48  SER   A CB  
350  O OG  . SER   A 68  ? 0.4585 0.2371 0.2671 0.01    -0.0077 -0.0014 48  SER   A OG  
351  N N   . HIS   A 69  ? 0.391  0.1834 0.2096 0.0081  -0.0034 -0.0014 49  HIS   A N   
352  C CA  . HIS   A 69  ? 0.3786 0.173  0.2002 0.0072  -0.0031 -0.0011 49  HIS   A CA  
353  C C   . HIS   A 69  ? 0.3839 0.1774 0.2091 0.0065  -0.0041 -0.0004 49  HIS   A C   
354  O O   . HIS   A 69  ? 0.394  0.1848 0.2191 0.0068  -0.0067 -0.0003 49  HIS   A O   
355  C CB  . HIS   A 69  ? 0.3789 0.1733 0.1991 0.0076  -0.0033 -0.0013 49  HIS   A CB  
356  C CG  . HIS   A 69  ? 0.3743 0.1664 0.1935 0.0079  -0.0049 -0.0009 49  HIS   A CG  
357  N ND1 . HIS   A 69  ? 0.393  0.1841 0.2153 0.0071  -0.0051 -0.0001 49  HIS   A ND1 
358  C CD2 . HIS   A 69  ? 0.3824 0.1727 0.1984 0.009   -0.006  -0.0011 49  HIS   A CD2 
359  C CE1 . HIS   A 69  ? 0.3927 0.1814 0.2137 0.0074  -0.0071 0       49  HIS   A CE1 
360  N NE2 . HIS   A 69  ? 0.3789 0.1667 0.1951 0.0087  -0.0078 -0.0006 49  HIS   A NE2 
361  N N   . GLY   A 70  ? 0.3959 0.1902 0.224  0.0058  -0.0022 0.0002  50  GLY   A N   
362  C CA  . GLY   A 70  ? 0.3944 0.1884 0.2291 0.0052  -0.002  0.0012  50  GLY   A CA  
363  C C   . GLY   A 70  ? 0.4024 0.1951 0.2403 0.0048  -0.0017 0.002   50  GLY   A C   
364  O O   . GLY   A 70  ? 0.401  0.1926 0.2346 0.0052  -0.0021 0.0017  50  GLY   A O   
365  N N   . ALA   A 71  ? 0.4042 0.1972 0.251  0.0041  -0.0006 0.0031  51  ALA   A N   
366  C CA  . ALA   A 71  ? 0.4074 0.1991 0.2598 0.0035  0.0004  0.0041  51  ALA   A CA  
367  C C   . ALA   A 71  ? 0.422  0.2108 0.2685 0.0038  0.0054  0.0046  51  ALA   A C   
368  O O   . ALA   A 71  ? 0.4346 0.2219 0.2768 0.0044  0.0092  0.0047  51  ALA   A O   
369  C CB  . ALA   A 71  ? 0.4294 0.2223 0.2953 0.0027  0.0015  0.0053  51  ALA   A CB  
370  N N   . GLY   A 72  ? 0.4284 0.2151 0.2736 0.0037  0.0049  0.0047  52  GLY   A N   
371  C CA  . GLY   A 72  ? 0.449  0.2309 0.2872 0.0043  0.009   0.0051  52  GLY   A CA  
372  C C   . GLY   A 72  ? 0.4559 0.2362 0.2821 0.0057  0.0074  0.0038  52  GLY   A C   
373  O O   . GLY   A 72  ? 0.4942 0.2698 0.3135 0.0064  0.0084  0.0037  52  GLY   A O   
374  N N   . GLU   A 73  ? 0.419  0.2026 0.2432 0.006   0.0048  0.0026  53  GLU   A N   
375  C CA  . GLU   A 73  ? 0.4039 0.1865 0.2199 0.0072  0.0031  0.0014  53  GLU   A CA  
376  C C   . GLU   A 73  ? 0.4001 0.1856 0.2157 0.0076  -0.0008 0.0004  53  GLU   A C   
377  O O   . GLU   A 73  ? 0.4257 0.2109 0.2434 0.0073  -0.002  0.0008  53  GLU   A O   
378  C CB  . GLU   A 73  ? 0.4143 0.1975 0.2285 0.0074  0.0037  0.0009  53  GLU   A CB  
379  C CG  . GLU   A 73  ? 0.3967 0.1852 0.2168 0.0066  0.0024  0.0007  53  GLU   A CG  
380  C CD  . GLU   A 73  ? 0.4256 0.2154 0.2441 0.0066  0.0021  -0.0001 53  GLU   A CD  
381  O OE1 . GLU   A 73  ? 0.4581 0.2446 0.2712 0.0073  0.002   -0.0006 53  GLU   A OE1 
382  O OE2 . GLU   A 73  ? 0.4391 0.2321 0.261  0.0061  0.0014  -0.0002 53  GLU   A OE2 
383  N N   . HIS   A 74  ? 0.4002 0.1872 0.2132 0.0084  -0.0025 -0.0007 54  HIS   A N   
384  C CA  . HIS   A 74  ? 0.397  0.1856 0.2095 0.0093  -0.0048 -0.0014 54  HIS   A CA  
385  C C   . HIS   A 74  ? 0.3998 0.1913 0.2137 0.0098  -0.0054 -0.0023 54  HIS   A C   
386  O O   . HIS   A 74  ? 0.3962 0.188  0.2104 0.0094  -0.005  -0.0026 54  HIS   A O   
387  C CB  . HIS   A 74  ? 0.3999 0.1852 0.2081 0.0104  -0.0058 -0.0016 54  HIS   A CB  
388  C CG  . HIS   A 74  ? 0.4063 0.1886 0.21   0.0114  -0.0065 -0.0023 54  HIS   A CG  
389  N ND1 . HIS   A 74  ? 0.4397 0.2233 0.2436 0.0127  -0.0092 -0.0035 54  HIS   A ND1 
390  C CD2 . HIS   A 74  ? 0.4217 0.1983 0.2203 0.0115  -0.005  -0.002  54  HIS   A CD2 
391  C CE1 . HIS   A 74  ? 0.4517 0.23   0.2502 0.0135  -0.0107 -0.0041 54  HIS   A CE1 
392  N NE2 . HIS   A 74  ? 0.4508 0.2239 0.2444 0.013   -0.0079 -0.0032 54  HIS   A NE2 
393  N N   . SER   A 75  ? 0.3944 0.1875 0.2094 0.0107  -0.006  -0.0027 55  SER   A N   
394  C CA  . SER   A 75  ? 0.4003 0.1964 0.2192 0.0111  -0.0055 -0.0033 55  SER   A CA  
395  C C   . SER   A 75  ? 0.4212 0.2181 0.2422 0.0115  -0.0075 -0.0043 55  SER   A C   
396  O O   . SER   A 75  ? 0.4271 0.2266 0.2531 0.0111  -0.0075 -0.0048 55  SER   A O   
397  C CB  . SER   A 75  ? 0.4117 0.2077 0.2311 0.0124  -0.0043 -0.0032 55  SER   A CB  
398  O OG  . SER   A 75  ? 0.4333 0.2283 0.2514 0.0138  -0.0056 -0.0034 55  SER   A OG  
399  N N   . GLY   A 76  ? 0.4209 0.2145 0.2378 0.0123  -0.0097 -0.0046 56  GLY   A N   
400  C CA  . GLY   A 76  ? 0.434  0.2261 0.2513 0.0131  -0.0132 -0.0058 56  GLY   A CA  
401  C C   . GLY   A 76  ? 0.4619 0.2515 0.277  0.0123  -0.014  -0.0061 56  GLY   A C   
402  O O   . GLY   A 76  ? 0.486  0.2742 0.3025 0.0128  -0.0178 -0.0072 56  GLY   A O   
403  N N   . ARG   A 77  ? 0.4223 0.2111 0.2346 0.0111  -0.0108 -0.0051 57  ARG   A N   
404  C CA  . ARG   A 77  ? 0.4408 0.2266 0.2503 0.0104  -0.0107 -0.0051 57  ARG   A CA  
405  C C   . ARG   A 77  ? 0.4423 0.2328 0.2588 0.0095  -0.0112 -0.0057 57  ARG   A C   
406  O O   . ARG   A 77  ? 0.451  0.2388 0.2654 0.009   -0.012  -0.006  57  ARG   A O   
407  C CB  . ARG   A 77  ? 0.4701 0.2548 0.2774 0.0095  -0.0064 -0.0037 57  ARG   A CB  
408  C CG  . ARG   A 77  ? 0.5526 0.3322 0.3546 0.01    -0.0043 -0.0028 57  ARG   A CG  
409  C CD  . ARG   A 77  ? 0.642  0.4134 0.4351 0.0117  -0.0063 -0.0034 57  ARG   A CD  
410  N NE  . ARG   A 77  ? 0.6486 0.413  0.4347 0.0124  -0.0078 -0.004  57  ARG   A NE  
411  C CZ  . ARG   A 77  ? 0.7297 0.4878 0.5096 0.014   -0.0127 -0.0054 57  ARG   A CZ  
412  N NH1 . ARG   A 77  ? 0.6599 0.4096 0.4319 0.0149  -0.0148 -0.006  57  ARG   A NH1 
413  N NH2 . ARG   A 77  ? 0.8005 0.5594 0.5814 0.0151  -0.0162 -0.0062 57  ARG   A NH2 
414  N N   . TYR   A 78  ? 0.4236 0.22   0.2478 0.0093  -0.0103 -0.0057 58  TYR   A N   
415  C CA  . TYR   A 78  ? 0.4274 0.2278 0.2587 0.0083  -0.0093 -0.0059 58  TYR   A CA  
416  C C   . TYR   A 78  ? 0.4317 0.2347 0.2718 0.0088  -0.012  -0.007  58  TYR   A C   
417  O O   . TYR   A 78  ? 0.4265 0.2332 0.2747 0.008   -0.0101 -0.007  58  TYR   A O   
418  C CB  . TYR   A 78  ? 0.4202 0.2231 0.2528 0.008   -0.005  -0.005  58  TYR   A CB  
419  C CG  . TYR   A 78  ? 0.4276 0.2283 0.2546 0.0073  -0.0035 -0.0042 58  TYR   A CG  
420  C CD1 . TYR   A 78  ? 0.4333 0.2318 0.256  0.0077  -0.0035 -0.0035 58  TYR   A CD1 
421  C CD2 . TYR   A 78  ? 0.4427 0.2434 0.2697 0.0062  -0.0023 -0.004  58  TYR   A CD2 
422  C CE1 . TYR   A 78  ? 0.4331 0.23   0.2538 0.0071  -0.0022 -0.0027 58  TYR   A CE1 
423  C CE2 . TYR   A 78  ? 0.4474 0.2464 0.2711 0.0059  -0.0011 -0.0032 58  TYR   A CE2 
424  C CZ  . TYR   A 78  ? 0.4487 0.246  0.2703 0.0063  -0.001  -0.0026 58  TYR   A CZ  
425  O OH  . TYR   A 78  ? 0.448  0.244  0.2693 0.0059  0.0004  -0.0017 58  TYR   A OH  
426  N N   . GLU   A 79  ? 0.4525 0.2529 0.2916 0.01    -0.0166 -0.0079 59  GLU   A N   
427  C CA  . GLU   A 79  ? 0.4705 0.2734 0.3202 0.0107  -0.0203 -0.009  59  GLU   A CA  
428  C C   . GLU   A 79  ? 0.4768 0.2816 0.3352 0.0093  -0.0222 -0.0097 59  GLU   A C   
429  O O   . GLU   A 79  ? 0.4825 0.2927 0.3541 0.0089  -0.0204 -0.0096 59  GLU   A O   
430  C CB  . GLU   A 79  ? 0.5093 0.3068 0.354  0.0125  -0.0265 -0.0101 59  GLU   A CB  
431  C CG  . GLU   A 79  ? 0.5739 0.3746 0.4316 0.0135  -0.0309 -0.0112 59  GLU   A CG  
432  C CD  . GLU   A 79  ? 0.6432 0.4496 0.5081 0.0145  -0.0262 -0.0104 59  GLU   A CD  
433  O OE1 . GLU   A 79  ? 0.6838 0.4887 0.5396 0.015   -0.0226 -0.0094 59  GLU   A OE1 
434  O OE2 . GLU   A 79  ? 0.6684 0.48   0.5484 0.0149  -0.0262 -0.0106 59  GLU   A OE2 
435  N N   . GLU   A 80  ? 0.4561 0.2552 0.3068 0.0086  -0.0253 -0.0102 60  GLU   A N   
436  C CA  . GLU   A 80  ? 0.4521 0.2517 0.3098 0.0072  -0.0281 -0.0109 60  GLU   A CA  
437  C C   . GLU   A 80  ? 0.4487 0.2539 0.3128 0.0054  -0.0216 -0.0099 60  GLU   A C   
438  O O   . GLU   A 80  ? 0.462  0.2711 0.3392 0.0044  -0.0218 -0.0102 60  GLU   A O   
439  C CB  . GLU   A 80  ? 0.5171 0.3072 0.3624 0.0073  -0.0327 -0.0116 60  GLU   A CB  
440  C CG  . GLU   A 80  ? 0.6585 0.4408 0.4993 0.0093  -0.0412 -0.0132 60  GLU   A CG  
441  C CD  . GLU   A 80  ? 0.8816 0.6518 0.7097 0.0098  -0.0468 -0.0141 60  GLU   A CD  
442  O OE1 . GLU   A 80  ? 0.9421 0.7119 0.7696 0.0082  -0.0452 -0.0138 60  GLU   A OE1 
443  O OE2 . GLU   A 80  ? 0.9403 0.7    0.7576 0.012   -0.0527 -0.0151 60  GLU   A OE2 
444  N N   . LEU   A 81  ? 0.4377 0.2425 0.2932 0.0051  -0.0161 -0.0086 61  LEU   A N   
445  C CA  A LEU   A 81  ? 0.4356 0.2438 0.2949 0.0038  -0.0103 -0.0077 61  LEU   A CA  
446  C CA  B LEU   A 81  ? 0.4435 0.2516 0.3027 0.0038  -0.0104 -0.0078 61  LEU   A CA  
447  C C   . LEU   A 81  ? 0.429  0.2418 0.2986 0.0043  -0.0061 -0.0072 61  LEU   A C   
448  O O   . LEU   A 81  ? 0.4361 0.2512 0.3142 0.0033  -0.0027 -0.007  61  LEU   A O   
449  C CB  A LEU   A 81  ? 0.4478 0.2541 0.2965 0.0039  -0.0062 -0.0066 61  LEU   A CB  
450  C CB  B LEU   A 81  ? 0.4696 0.2755 0.3178 0.0039  -0.0068 -0.0067 61  LEU   A CB  
451  C CG  A LEU   A 81  ? 0.4581 0.2606 0.2989 0.0032  -0.0067 -0.0065 61  LEU   A CG  
452  C CG  B LEU   A 81  ? 0.4994 0.3056 0.3466 0.0029  -0.0026 -0.006  61  LEU   A CG  
453  C CD1 A LEU   A 81  ? 0.4441 0.2454 0.2777 0.0036  -0.0035 -0.0054 61  LEU   A CD1 
454  C CD1 B LEU   A 81  ? 0.5106 0.3157 0.3601 0.0014  -0.0044 -0.0066 61  LEU   A CD1 
455  C CD2 A LEU   A 81  ? 0.4672 0.2705 0.3123 0.0016  -0.0055 -0.0066 61  LEU   A CD2 
456  C CD2 B LEU   A 81  ? 0.5214 0.3251 0.3592 0.0033  -0.0009 -0.0052 61  LEU   A CD2 
457  N N   . ALA   A 82  ? 0.4273 0.2406 0.2956 0.0059  -0.0056 -0.007  62  ALA   A N   
458  C CA  . ALA   A 82  ? 0.4321 0.2481 0.3082 0.0069  -0.0008 -0.0063 62  ALA   A CA  
459  C C   . ALA   A 82  ? 0.4389 0.2589 0.3319 0.0067  -0.0023 -0.0069 62  ALA   A C   
460  O O   . ALA   A 82  ? 0.4503 0.2724 0.3525 0.0065  0.0037  -0.0061 62  ALA   A O   
461  C CB  . ALA   A 82  ? 0.4406 0.2553 0.311  0.0089  -0.0011 -0.006  62  ALA   A CB  
462  N N   . ARG   A 83  ? 0.444  0.2642 0.3413 0.0066  -0.01   -0.0083 63  ARG   A N   
463  C CA  . ARG   A 83  ? 0.4612 0.2852 0.377  0.0063  -0.0131 -0.0092 63  ARG   A CA  
464  C C   . ARG   A 83  ? 0.4742 0.2997 0.3987 0.004   -0.0115 -0.0091 63  ARG   A C   
465  O O   . ARG   A 83  ? 0.4949 0.3248 0.4367 0.0035  -0.008  -0.0087 63  ARG   A O   
466  C CB  . ARG   A 83  ? 0.4913 0.3129 0.4074 0.0072  -0.0233 -0.0109 63  ARG   A CB  
467  C CG  . ARG   A 83  ? 0.5507 0.3719 0.4632 0.0097  -0.0239 -0.0109 63  ARG   A CG  
468  C CD  . ARG   A 83  ? 0.6267 0.4445 0.5404 0.0111  -0.0342 -0.0127 63  ARG   A CD  
469  N NE  . ARG   A 83  ? 0.6891 0.507  0.6008 0.0135  -0.0338 -0.0125 63  ARG   A NE  
470  C CZ  . ARG   A 83  ? 0.7332 0.5562 0.6608 0.0149  -0.0331 -0.0125 63  ARG   A CZ  
471  N NH1 . ARG   A 83  ? 0.722  0.5507 0.6706 0.0141  -0.033  -0.0127 63  ARG   A NH1 
472  N NH2 . ARG   A 83  ? 0.7471 0.5694 0.6706 0.0173  -0.0325 -0.0123 63  ARG   A NH2 
473  N N   . MET   A 84  ? 0.4787 0.3004 0.3915 0.0026  -0.0127 -0.0093 64  MET   A N   
474  C CA  . MET   A 84  ? 0.4712 0.2935 0.3897 0.0003  -0.0105 -0.0091 64  MET   A CA  
475  C C   . MET   A 84  ? 0.4735 0.2977 0.3955 0.0002  0.0003  -0.0074 64  MET   A C   
476  O O   . MET   A 84  ? 0.4869 0.3137 0.4235 -0.001  0.0039  -0.007  64  MET   A O   
477  C CB  . MET   A 84  ? 0.4721 0.289  0.3745 -0.0005 -0.0127 -0.0093 64  MET   A CB  
478  C CG  . MET   A 84  ? 0.5043 0.321  0.4105 -0.0028 -0.0103 -0.0091 64  MET   A CG  
479  S SD  . MET   A 84  ? 0.5736 0.3899 0.4727 -0.003  0.0008  -0.0073 64  MET   A SD  
480  C CE  . MET   A 84  ? 0.5362 0.3475 0.4146 -0.0021 -0.0009 -0.0072 64  MET   A CE  
481  N N   . LEU   A 85  ? 0.4517 0.2734 0.3604 0.0017  0.0053  -0.0063 65  LEU   A N   
482  C CA  . LEU   A 85  ? 0.455  0.275  0.3626 0.0022  0.0151  -0.0048 65  LEU   A CA  
483  C C   . LEU   A 85  ? 0.4834 0.3063 0.4063 0.0033  0.0203  -0.0041 65  LEU   A C   
484  O O   . LEU   A 85  ? 0.4926 0.3147 0.4232 0.003   0.0281  -0.003  65  LEU   A O   
485  C CB  . LEU   A 85  ? 0.4457 0.2609 0.3354 0.0037  0.0173  -0.0041 65  LEU   A CB  
486  C CG  . LEU   A 85  ? 0.4628 0.2751 0.3397 0.0027  0.0144  -0.0044 65  LEU   A CG  
487  C CD1 . LEU   A 85  ? 0.4836 0.2926 0.3468 0.0042  0.0136  -0.004  65  LEU   A CD1 
488  C CD2 . LEU   A 85  ? 0.4953 0.3045 0.3704 0.0017  0.0196  -0.0038 65  LEU   A CD2 
489  N N   . MET   A 86  ? 0.4878 0.3134 0.4157 0.0048  0.0164  -0.0046 66  MET   A N   
490  C CA  A MET   A 86  ? 0.4984 0.3272 0.4426 0.0062  0.0209  -0.0039 66  MET   A CA  
491  C CA  B MET   A 86  ? 0.4974 0.3262 0.4416 0.0062  0.0208  -0.0039 66  MET   A CA  
492  C C   . MET   A 86  ? 0.5032 0.3371 0.4703 0.0042  0.0203  -0.0043 66  MET   A C   
493  O O   . MET   A 86  ? 0.5102 0.3457 0.4922 0.0047  0.0284  -0.003  66  MET   A O   
494  C CB  A MET   A 86  ? 0.5013 0.3319 0.4457 0.0082  0.0153  -0.0047 66  MET   A CB  
495  C CB  B MET   A 86  ? 0.4976 0.3283 0.4421 0.0082  0.0149  -0.0047 66  MET   A CB  
496  C CG  A MET   A 86  ? 0.5293 0.3628 0.4894 0.0102  0.0206  -0.0038 66  MET   A CG  
497  C CG  B MET   A 86  ? 0.5191 0.3539 0.4828 0.0098  0.0183  -0.0042 66  MET   A CG  
498  S SD  A MET   A 86  ? 0.5816 0.423  0.5714 0.0091  0.0145  -0.005  66  MET   A SD  
499  S SD  B MET   A 86  ? 0.5605 0.3967 0.5234 0.0123  0.0106  -0.0053 66  MET   A SD  
500  C CE  A MET   A 86  ? 0.5784 0.4196 0.5614 0.0102  0.0006  -0.0072 66  MET   A CE  
501  C CE  B MET   A 86  ? 0.482  0.3186 0.4438 0.0105  -0.0034 -0.0077 66  MET   A CE  
502  N N   . GLY   A 87  ? 0.5134 0.3486 0.4828 0.0021  0.011   -0.0059 67  GLY   A N   
503  C CA  . GLY   A 87  ? 0.5269 0.366  0.5173 -0.0002 0.0086  -0.0065 67  GLY   A CA  
504  C C   . GLY   A 87  ? 0.5415 0.3792 0.5353 -0.0019 0.0182  -0.0051 67  GLY   A C   
505  O O   . GLY   A 87  ? 0.5477 0.3889 0.5625 -0.0037 0.0196  -0.0049 67  GLY   A O   
506  N N   . LEU   A 88  ? 0.541  0.373  0.5146 -0.0014 0.0247  -0.004  68  LEU   A N   
507  C CA  . LEU   A 88  ? 0.5419 0.37   0.5146 -0.0023 0.0348  -0.0025 68  LEU   A CA  
508  C C   . LEU   A 88  ? 0.5495 0.3746 0.5247 0       0.0473  -0.0005 68  LEU   A C   
509  O O   . LEU   A 88  ? 0.5625 0.3814 0.5316 0.0001  0.0569  0.0009  68  LEU   A O   
510  C CB  . LEU   A 88  ? 0.5514 0.3732 0.5006 -0.0026 0.0349  -0.0025 68  LEU   A CB  
511  C CG  . LEU   A 88  ? 0.5766 0.3991 0.5181 -0.0042 0.0242  -0.0042 68  LEU   A CG  
512  C CD1 . LEU   A 88  ? 0.5912 0.4076 0.5117 -0.0041 0.0258  -0.0039 68  LEU   A CD1 
513  C CD2 . LEU   A 88  ? 0.5862 0.412  0.5442 -0.0069 0.0189  -0.0053 68  LEU   A CD2 
514  N N   . ASP   A 89  ? 0.5383 0.3663 0.5206 0.0023  0.0475  -0.0003 69  ASP   A N   
515  C CA  . ASP   A 89  ? 0.543  0.3672 0.5269 0.0052  0.059   0.0017  69  ASP   A CA  
516  C C   . ASP   A 89  ? 0.5409 0.3549 0.4975 0.0077  0.0637  0.0026  69  ASP   A C   
517  O O   . ASP   A 89  ? 0.5572 0.3633 0.5091 0.0099  0.075   0.0045  69  ASP   A O   
518  C CB  . ASP   A 89  ? 0.5918 0.4155 0.5947 0.0044  0.0705  0.0034  69  ASP   A CB  
519  C CG  . ASP   A 89  ? 0.6897 0.5239 0.7247 0.0027  0.0665  0.0028  69  ASP   A CG  
520  O OD1 . ASP   A 89  ? 0.7195 0.5552 0.7725 0.0006  0.0718  0.0035  69  ASP   A OD1 
521  O OD2 . ASP   A 89  ? 0.7227 0.5629 0.765  0.0035  0.0573  0.0015  69  ASP   A OD2 
522  N N   . LEU   A 90  ? 0.5234 0.3364 0.4622 0.0075  0.0549  0.0013  70  LEU   A N   
523  C CA  . LEU   A 90  ? 0.5134 0.3172 0.4284 0.01    0.0572  0.0019  70  LEU   A CA  
524  C C   . LEU   A 90  ? 0.4931 0.299  0.4065 0.0121  0.0532  0.0016  70  LEU   A C   
525  O O   . LEU   A 90  ? 0.4945 0.3087 0.4197 0.0113  0.0456  0.0004  70  LEU   A O   
526  C CB  . LEU   A 90  ? 0.5278 0.3292 0.4258 0.0086  0.0505  0.0009  70  LEU   A CB  
527  C CG  . LEU   A 90  ? 0.5665 0.3615 0.4572 0.0076  0.0555  0.0015  70  LEU   A CG  
528  C CD1 . LEU   A 90  ? 0.5813 0.3831 0.4869 0.0044  0.0528  0.0007  70  LEU   A CD1 
529  C CD2 . LEU   A 90  ? 0.5735 0.3628 0.4436 0.0079  0.0509  0.0009  70  LEU   A CD2 
530  N N   . LEU   A 91  ? 0.4871 0.2841 0.3853 0.015   0.0581  0.0027  71  LEU   A N   
531  C CA  . LEU   A 91  ? 0.4821 0.2794 0.3757 0.0171  0.0545  0.0025  71  LEU   A CA  
532  C C   . LEU   A 91  ? 0.4747 0.2696 0.3503 0.0164  0.0465  0.0014  71  LEU   A C   
533  O O   . LEU   A 91  ? 0.4891 0.275  0.3485 0.0171  0.0486  0.0019  71  LEU   A O   
534  C CB  . LEU   A 91  ? 0.5044 0.2916 0.3901 0.0209  0.0642  0.0043  71  LEU   A CB  
535  C CG  . LEU   A 91  ? 0.5495 0.3388 0.4369 0.0231  0.0618  0.0042  71  LEU   A CG  
536  C CD1 . LEU   A 91  ? 0.5723 0.3517 0.4558 0.027   0.0731  0.0062  71  LEU   A CD1 
537  C CD2 . LEU   A 91  ? 0.5613 0.3484 0.4317 0.0232  0.0532  0.0031  71  LEU   A CD2 
538  N N   . VAL   A 92  ? 0.4552 0.2574 0.3345 0.0151  0.0374  0       72  VAL   A N   
539  C CA  . VAL   A 92  ? 0.443  0.2443 0.3093 0.0142  0.0302  -0.0008 72  VAL   A CA  
540  C C   . VAL   A 92  ? 0.435  0.233  0.2921 0.0163  0.0282  -0.0007 72  VAL   A C   
541  O O   . VAL   A 92  ? 0.4355 0.2366 0.3003 0.0176  0.028   -0.0007 72  VAL   A O   
542  C CB  . VAL   A 92  ? 0.4376 0.2464 0.3113 0.0118  0.0223  -0.0023 72  VAL   A CB  
543  C CG1 . VAL   A 92  ? 0.4447 0.2514 0.3054 0.0109  0.0171  -0.0028 72  VAL   A CG1 
544  C CG2 . VAL   A 92  ? 0.4296 0.2418 0.315  0.0097  0.0236  -0.0025 72  VAL   A CG2 
545  N N   . PHE   A 93  ? 0.4116 0.203  0.2532 0.0167  0.0267  -0.0005 73  PHE   A N   
546  C CA  . PHE   A 93  ? 0.4221 0.2101 0.2552 0.0184  0.0239  -0.0004 73  PHE   A CA  
547  C C   . PHE   A 93  ? 0.4208 0.2076 0.2448 0.017   0.0178  -0.001  73  PHE   A C   
548  O O   . PHE   A 93  ? 0.4218 0.2081 0.2435 0.0156  0.0169  -0.0011 73  PHE   A O   
549  C CB  . PHE   A 93  ? 0.4378 0.2156 0.2618 0.0214  0.0302  0.0008  73  PHE   A CB  
550  C CG  . PHE   A 93  ? 0.4614 0.2283 0.2716 0.0222  0.0329  0.0014  73  PHE   A CG  
551  C CD1 . PHE   A 93  ? 0.4728 0.2379 0.2854 0.0217  0.0383  0.0018  73  PHE   A CD1 
552  C CD2 . PHE   A 93  ? 0.4817 0.238  0.2759 0.0239  0.0304  0.0016  73  PHE   A CD2 
553  C CE1 . PHE   A 93  ? 0.4897 0.2426 0.2875 0.0229  0.0406  0.0023  73  PHE   A CE1 
554  C CE2 . PHE   A 93  ? 0.4996 0.2436 0.2797 0.0252  0.032   0.002   73  PHE   A CE2 
555  C CZ  . PHE   A 93  ? 0.4962 0.2383 0.2775 0.0248  0.0371  0.0023  73  PHE   A CZ  
556  N N   . ALA   A 94  ? 0.4218 0.2083 0.242  0.0175  0.0138  -0.0012 74  ALA   A N   
557  C CA  . ALA   A 94  ? 0.4131 0.1991 0.2278 0.0161  0.0085  -0.0015 74  ALA   A CA  
558  C C   . ALA   A 94  ? 0.4184 0.2009 0.2273 0.0174  0.0061  -0.0014 74  ALA   A C   
559  O O   . ALA   A 94  ? 0.421  0.203  0.2308 0.0192  0.0078  -0.0012 74  ALA   A O   
560  C CB  . ALA   A 94  ? 0.4104 0.204  0.2326 0.0141  0.0052  -0.0023 74  ALA   A CB  
561  N N   . HIS   A 95  ? 0.4167 0.197  0.2208 0.0164  0.002   -0.0014 75  HIS   A N   
562  C CA  . HIS   A 95  ? 0.416  0.1943 0.2167 0.0168  -0.0011 -0.0013 75  HIS   A CA  
563  C C   . HIS   A 95  ? 0.4052 0.1861 0.2083 0.0146  -0.0046 -0.0014 75  HIS   A C   
564  O O   . HIS   A 95  ? 0.4151 0.1979 0.2208 0.0132  -0.0049 -0.0015 75  HIS   A O   
565  C CB  . HIS   A 95  ? 0.4154 0.1838 0.2058 0.0188  -0.0016 -0.0008 75  HIS   A CB  
566  C CG  . HIS   A 95  ? 0.4314 0.1929 0.2155 0.0186  -0.0039 -0.0007 75  HIS   A CG  
567  N ND1 . HIS   A 95  ? 0.4506 0.2034 0.2263 0.0206  -0.001  -0.0004 75  HIS   A ND1 
568  C CD2 . HIS   A 95  ? 0.4495 0.2107 0.2348 0.0169  -0.0086 -0.0008 75  HIS   A CD2 
569  C CE1 . HIS   A 95  ? 0.4694 0.216  0.2399 0.0203  -0.0054 -0.0006 75  HIS   A CE1 
570  N NE2 . HIS   A 95  ? 0.4626 0.215  0.2403 0.0179  -0.0102 -0.0008 75  HIS   A NE2 
571  N N   . ASP   A 96  ? 0.3938 0.1747 0.1964 0.0145  -0.0068 -0.0014 76  ASP   A N   
572  C CA  . ASP   A 96  ? 0.3884 0.1702 0.1934 0.0126  -0.0089 -0.0012 76  ASP   A CA  
573  C C   . ASP   A 96  ? 0.3955 0.1719 0.1978 0.0124  -0.0118 -0.0008 76  ASP   A C   
574  O O   . ASP   A 96  ? 0.4111 0.1815 0.2072 0.0138  -0.0134 -0.0007 76  ASP   A O   
575  C CB  . ASP   A 96  ? 0.3908 0.173  0.1956 0.0126  -0.0095 -0.0012 76  ASP   A CB  
576  C CG  . ASP   A 96  ? 0.4364 0.2222 0.2431 0.013   -0.0083 -0.0018 76  ASP   A CG  
577  O OD1 . ASP   A 96  ? 0.4257 0.2146 0.2357 0.0126  -0.0071 -0.0022 76  ASP   A OD1 
578  O OD2 . ASP   A 96  ? 0.4313 0.2159 0.2361 0.0136  -0.009  -0.0021 76  ASP   A OD2 
579  N N   . HIS   A 97  ? 0.3993 0.1769 0.2062 0.0109  -0.0129 -0.0005 77  HIS   A N   
580  C CA  . HIS   A 97  ? 0.4072 0.1793 0.2133 0.0107  -0.0172 -0.0003 77  HIS   A CA  
581  C C   . HIS   A 97  ? 0.4295 0.1993 0.2367 0.0101  -0.0199 0       77  HIS   A C   
582  O O   . HIS   A 97  ? 0.4223 0.1956 0.2326 0.0093  -0.0177 0.0003  77  HIS   A O   
583  C CB  . HIS   A 97  ? 0.4071 0.1819 0.2208 0.0091  -0.018  -0.0001 77  HIS   A CB  
584  C CG  . HIS   A 97  ? 0.406  0.1826 0.2185 0.0095  -0.0157 -0.0005 77  HIS   A CG  
585  N ND1 . HIS   A 97  ? 0.4286 0.1993 0.2327 0.0112  -0.0159 -0.0009 77  HIS   A ND1 
586  C CD2 . HIS   A 97  ? 0.4131 0.1952 0.2307 0.0085  -0.0127 -0.0004 77  HIS   A CD2 
587  C CE1 . HIS   A 97  ? 0.4213 0.1952 0.227  0.011   -0.013  -0.001  77  HIS   A CE1 
588  N NE2 . HIS   A 97  ? 0.405  0.1859 0.2188 0.0093  -0.0115 -0.0008 77  HIS   A NE2 
589  N N   . VAL   A 98  ? 0.4443 0.207  0.2487 0.0104  -0.0251 0       78  VAL   A N   
590  C CA  A VAL   A 98  ? 0.4512 0.2113 0.258  0.0095  -0.0283 0.0004  78  VAL   A CA  
591  C CA  B VAL   A 98  ? 0.4453 0.2051 0.2522 0.0095  -0.0285 0.0004  78  VAL   A CA  
592  C C   . VAL   A 98  ? 0.4475 0.2141 0.267  0.007   -0.0262 0.0011  78  VAL   A C   
593  O O   . VAL   A 98  ? 0.438  0.2087 0.2651 0.006   -0.0248 0.0014  78  VAL   A O   
594  C CB  A VAL   A 98  ? 0.4812 0.2315 0.2841 0.0101  -0.0358 0.0001  78  VAL   A CB  
595  C CB  B VAL   A 98  ? 0.4562 0.2072 0.261  0.0099  -0.036  0.0001  78  VAL   A CB  
596  C CG1 A VAL   A 98  ? 0.4763 0.2268 0.2877 0.009   -0.0397 0       78  VAL   A CG1 
597  C CG1 B VAL   A 98  ? 0.4633 0.2135 0.2779 0.0078  -0.0406 0.0005  78  VAL   A CG1 
598  C CG2 A VAL   A 98  ? 0.4939 0.2412 0.2992 0.0091  -0.0391 0.0005  78  VAL   A CG2 
599  C CG2 B VAL   A 98  ? 0.4616 0.2024 0.2507 0.0127  -0.0377 -0.0004 78  VAL   A CG2 
600  N N   . GLY   A 99  ? 0.4332 0.1998 0.2536 0.0064  -0.0248 0.0016  79  GLY   A N   
601  C CA  . GLY   A 99  ? 0.4401 0.2104 0.2706 0.0044  -0.0213 0.0025  79  GLY   A CA  
602  C C   . GLY   A 99  ? 0.4246 0.1993 0.2541 0.0046  -0.0151 0.0027  79  GLY   A C   
603  O O   . GLY   A 99  ? 0.4439 0.22   0.2798 0.0035  -0.011  0.0036  79  GLY   A O   
604  N N   . HIS   A 100 ? 0.4137 0.1896 0.2349 0.0063  -0.0141 0.0018  80  HIS   A N   
605  C CA  . HIS   A 100 ? 0.397  0.176  0.2167 0.0067  -0.0098 0.0016  80  HIS   A CA  
606  C C   . HIS   A 100 ? 0.3944 0.1727 0.2061 0.0085  -0.0094 0.0008  80  HIS   A C   
607  O O   . HIS   A 100 ? 0.417  0.1938 0.2243 0.0097  -0.0116 0.0003  80  HIS   A O   
608  C CB  . HIS   A 100 ? 0.404  0.1863 0.2255 0.0068  -0.0096 0.0012  80  HIS   A CB  
609  C CG  . HIS   A 100 ? 0.4052 0.1888 0.2355 0.0054  -0.0094 0.002   80  HIS   A CG  
610  N ND1 . HIS   A 100 ? 0.4119 0.1937 0.247  0.0048  -0.0137 0.0021  80  HIS   A ND1 
611  C CD2 . HIS   A 100 ? 0.4069 0.1925 0.242  0.0047  -0.0057 0.0026  80  HIS   A CD2 
612  C CE1 . HIS   A 100 ? 0.4244 0.2084 0.2691 0.0036  -0.0126 0.0029  80  HIS   A CE1 
613  N NE2 . HIS   A 100 ? 0.4307 0.2171 0.2756 0.0036  -0.0071 0.0033  80  HIS   A NE2 
614  N N   . GLY   A 101 ? 0.3971 0.1755 0.2064 0.0089  -0.0068 0.0006  81  GLY   A N   
615  C CA  . GLY   A 101 ? 0.4054 0.1834 0.2089 0.0107  -0.0074 -0.0004 81  GLY   A CA  
616  C C   . GLY   A 101 ? 0.4128 0.188  0.2119 0.0119  -0.0093 -0.0006 81  GLY   A C   
617  O O   . GLY   A 101 ? 0.4266 0.1981 0.2244 0.0113  -0.0091 0       81  GLY   A O   
618  N N   . GLN   A 102 ? 0.3994 0.1761 0.1971 0.0135  -0.0106 -0.0013 82  GLN   A N   
619  C CA  . GLN   A 102 ? 0.41   0.184  0.2032 0.0152  -0.012  -0.0016 82  GLN   A CA  
620  C C   . GLN   A 102 ? 0.4208 0.1924 0.2124 0.0154  -0.0131 -0.0011 82  GLN   A C   
621  O O   . GLN   A 102 ? 0.4142 0.1827 0.2011 0.0171  -0.0139 -0.0012 82  GLN   A O   
622  C CB  . GLN   A 102 ? 0.4159 0.1923 0.2096 0.0173  -0.0122 -0.0025 82  GLN   A CB  
623  C CG  . GLN   A 102 ? 0.4362 0.2128 0.2299 0.0174  -0.0128 -0.0033 82  GLN   A CG  
624  C CD  . GLN   A 102 ? 0.4392 0.218  0.2355 0.0195  -0.0145 -0.0044 82  GLN   A CD  
625  O OE1 . GLN   A 102 ? 0.4597 0.2365 0.2538 0.0215  -0.0159 -0.0047 82  GLN   A OE1 
626  N NE2 . GLN   A 102 ? 0.4385 0.221  0.2403 0.0192  -0.0148 -0.0049 82  GLN   A NE2 
627  N N   . SER   A 103 ? 0.4155 0.1871 0.2099 0.0139  -0.0137 -0.0006 83  SER   A N   
628  C CA  . SER   A 103 ? 0.4245 0.1909 0.2154 0.0143  -0.0162 -0.0003 83  SER   A CA  
629  C C   . SER   A 103 ? 0.4414 0.204  0.2329 0.0129  -0.0188 0.0002  83  SER   A C   
630  O O   . SER   A 103 ? 0.4423 0.2068 0.2386 0.0112  -0.0176 0.0006  83  SER   A O   
631  C CB  . SER   A 103 ? 0.4205 0.1873 0.2137 0.0137  -0.0166 -0.0003 83  SER   A CB  
632  O OG  . SER   A 103 ? 0.4277 0.1964 0.2193 0.0153  -0.0137 -0.0007 83  SER   A OG  
633  N N   . GLU   A 104 ? 0.4486 0.2044 0.2348 0.0136  -0.0223 0.0003  84  GLU   A N   
634  C CA  . GLU   A 104 ? 0.4651 0.2166 0.2529 0.0121  -0.0258 0.0007  84  GLU   A CA  
635  C C   . GLU   A 104 ? 0.4934 0.2462 0.2911 0.0096  -0.0283 0.0011  84  GLU   A C   
636  O O   . GLU   A 104 ? 0.4774 0.2333 0.2783 0.0095  -0.0278 0.001   84  GLU   A O   
637  C CB  . GLU   A 104 ? 0.4675 0.2095 0.2451 0.014   -0.0298 0.0006  84  GLU   A CB  
638  C CG  . GLU   A 104 ? 0.4736 0.2142 0.2436 0.0162  -0.0274 0.0004  84  GLU   A CG  
639  C CD  . GLU   A 104 ? 0.521  0.2509 0.2798 0.0182  -0.0309 0.0005  84  GLU   A CD  
640  O OE1 . GLU   A 104 ? 0.5104 0.2331 0.2638 0.0191  -0.034  0.0004  84  GLU   A OE1 
641  O OE2 . GLU   A 104 ? 0.5502 0.2775 0.3046 0.019   -0.0307 0.0005  84  GLU   A OE2 
642  N N   . GLY   A 105 ? 0.5152 0.2657 0.3188 0.0077  -0.0309 0.0017  85  GLY   A N   
643  C CA  . GLY   A 105 ? 0.5234 0.2747 0.339  0.0054  -0.034  0.0022  85  GLY   A CA  
644  C C   . GLY   A 105 ? 0.5317 0.2879 0.3592 0.003   -0.0295 0.0032  85  GLY   A C   
645  O O   . GLY   A 105 ? 0.5441 0.3039 0.3696 0.0034  -0.0233 0.0034  85  GLY   A O   
646  N N   . GLU   A 106 ? 0.5304 0.2859 0.3711 0.0007  -0.0323 0.004   86  GLU   A N   
647  C CA  . GLU   A 106 ? 0.5302 0.2896 0.3841 -0.0015 -0.0264 0.0054  86  GLU   A CA  
648  C C   . GLU   A 106 ? 0.5178 0.2832 0.3743 -0.0011 -0.0209 0.0055  86  GLU   A C   
649  O O   . GLU   A 106 ? 0.5086 0.2757 0.3645 -0.0003 -0.024  0.0048  86  GLU   A O   
650  C CB  . GLU   A 106 ? 0.5945 0.3532 0.4659 -0.004  -0.0312 0.0061  86  GLU   A CB  
651  C CG  . GLU   A 106 ? 0.7315 0.4925 0.6177 -0.0063 -0.0241 0.0079  86  GLU   A CG  
652  C CD  . GLU   A 106 ? 0.8811 0.6427 0.7893 -0.009  -0.0281 0.0088  86  GLU   A CD  
653  O OE1 . GLU   A 106 ? 0.8995 0.6572 0.8094 -0.0093 -0.0383 0.0079  86  GLU   A OE1 
654  O OE2 . GLU   A 106 ? 0.9189 0.6841 0.8427 -0.0105 -0.021  0.0105  86  GLU   A OE2 
655  N N   . ARG   A 107 ? 0.5197 0.2866 0.3757 -0.0012 -0.0129 0.0064  87  ARG   A N   
656  C CA  . ARG   A 107 ? 0.5255 0.2961 0.3807 -0.0004 -0.008  0.0064  87  ARG   A CA  
657  C C   . ARG   A 107 ? 0.5205 0.295  0.3894 -0.0015 -0.0084 0.007   87  ARG   A C   
658  O O   . ARG   A 107 ? 0.5267 0.3015 0.4103 -0.0033 -0.0068 0.0084  87  ARG   A O   
659  C CB  . ARG   A 107 ? 0.5365 0.3047 0.3874 0       0.0002  0.0073  87  ARG   A CB  
660  C CG  . ARG   A 107 ? 0.5758 0.3392 0.4127 0.0014  0.0004  0.0067  87  ARG   A CG  
661  C CD  . ARG   A 107 ? 0.5784 0.3435 0.4032 0.0036  -0.0026 0.005   87  ARG   A CD  
662  N NE  . ARG   A 107 ? 0.5329 0.299  0.3561 0.0041  -0.0091 0.004   87  ARG   A NE  
663  C CZ  . ARG   A 107 ? 0.523  0.2902 0.338  0.006   -0.0113 0.0028  87  ARG   A CZ  
664  N NH1 . ARG   A 107 ? 0.5019 0.2707 0.3115 0.0074  -0.0087 0.0022  87  ARG   A NH1 
665  N NH2 . ARG   A 107 ? 0.5012 0.267  0.3134 0.0067  -0.016  0.0023  87  ARG   A NH2 
666  N N   . MET   A 108 ? 0.5055 0.2828 0.3706 -0.0004 -0.0102 0.0061  88  MET   A N   
667  C CA  A MET   A 108 ? 0.5015 0.2824 0.378  -0.0011 -0.0105 0.0065  88  MET   A CA  
668  C CA  B MET   A 108 ? 0.5136 0.2944 0.3907 -0.0012 -0.0101 0.0066  88  MET   A CA  
669  C C   . MET   A 108 ? 0.5138 0.2943 0.4052 -0.0026 -0.0165 0.0068  88  MET   A C   
670  O O   . MET   A 108 ? 0.5263 0.3094 0.4342 -0.0039 -0.0143 0.0081  88  MET   A O   
671  C CB  A MET   A 108 ? 0.4878 0.2705 0.3686 -0.0012 -0.0017 0.0078  88  MET   A CB  
672  C CB  B MET   A 108 ? 0.5287 0.3108 0.4114 -0.0015 -0.0009 0.0081  88  MET   A CB  
673  C CG  A MET   A 108 ? 0.4761 0.2582 0.3421 0.0005  0.0018  0.007   88  MET   A CG  
674  C CG  B MET   A 108 ? 0.5741 0.3545 0.4422 0       0.0041  0.0077  88  MET   A CG  
675  S SD  A MET   A 108 ? 0.4522 0.2331 0.3193 0.0009  0.0114  0.0085  88  MET   A SD  
676  S SD  B MET   A 108 ? 0.6968 0.4802 0.5552 0.0015  0.0003  0.006   88  MET   A SD  
677  C CE  A MET   A 108 ? 0.4494 0.2357 0.3273 0.0006  0.0091  0.0084  88  MET   A CE  
678  C CE  B MET   A 108 ? 0.688  0.4752 0.5598 0.0008  0.001   0.0067  88  MET   A CE  
679  N N   A VAL   A 109 ? 0.5105 0.287  0.3962 -0.0022 -0.0245 0.0057  89  VAL   A N   
680  N N   B VAL   A 109 ? 0.5157 0.2919 0.4009 -0.0022 -0.0244 0.0057  89  VAL   A N   
681  C CA  A VAL   A 109 ? 0.5102 0.2842 0.4065 -0.003  -0.0332 0.0054  89  VAL   A CA  
682  C CA  B VAL   A 109 ? 0.5236 0.2967 0.4182 -0.0031 -0.0334 0.0054  89  VAL   A CA  
683  C C   A VAL   A 109 ? 0.5151 0.2834 0.3962 -0.0009 -0.0406 0.0037  89  VAL   A C   
684  C C   B VAL   A 109 ? 0.5222 0.2901 0.4027 -0.0009 -0.0408 0.0037  89  VAL   A C   
685  O O   A VAL   A 109 ? 0.5247 0.2908 0.3895 0.0007  -0.0387 0.0031  89  VAL   A O   
686  O O   B VAL   A 109 ? 0.5323 0.2979 0.3963 0.0008  -0.0391 0.003   89  VAL   A O   
687  C CB  A VAL   A 109 ? 0.5154 0.2868 0.4232 -0.005  -0.0363 0.0062  89  VAL   A CB  
688  C CB  B VAL   A 109 ? 0.5402 0.309  0.4367 -0.0043 -0.0357 0.0058  89  VAL   A CB  
689  C CG1 A VAL   A 109 ? 0.5118 0.2877 0.4369 -0.007  -0.0279 0.0082  89  VAL   A CG1 
690  C CG1 B VAL   A 109 ? 0.5443 0.3071 0.4455 -0.0047 -0.0473 0.005   89  VAL   A CG1 
691  C CG2 A VAL   A 109 ? 0.5213 0.2872 0.4142 -0.0044 -0.0376 0.0057  89  VAL   A CG2 
692  C CG2 B VAL   A 109 ? 0.5409 0.3131 0.4525 -0.0064 -0.0281 0.0077  89  VAL   A CG2 
693  N N   . VAL   A 110 ? 0.5137 0.2786 0.4002 -0.0008 -0.0487 0.0031  90  VAL   A N   
694  C CA  . VAL   A 110 ? 0.5225 0.2791 0.3934 0.0016  -0.0556 0.0016  90  VAL   A CA  
695  C C   . VAL   A 110 ? 0.5388 0.2886 0.4182 0.0013  -0.0671 0.001   90  VAL   A C   
696  O O   . VAL   A 110 ? 0.5448 0.2994 0.4438 -0.0003 -0.0688 0.0015  90  VAL   A O   
697  C CB  . VAL   A 110 ? 0.5274 0.286  0.3886 0.0034  -0.0516 0.0011  90  VAL   A CB  
698  C CG1 . VAL   A 110 ? 0.5246 0.2868 0.3986 0.0029  -0.0531 0.0011  90  VAL   A CG1 
699  C CG2 . VAL   A 110 ? 0.5373 0.2857 0.3781 0.0061  -0.0553 -0.0002 90  VAL   A CG2 
700  N N   . SER   A 111 ? 0.5423 0.28   0.4076 0.0029  -0.0753 -0.0001 91  SER   A N   
701  C CA  . SER   A 111 ? 0.5612 0.2898 0.4329 0.0029  -0.0882 -0.0009 91  SER   A CA  
702  C C   . SER   A 111 ? 0.5674 0.2943 0.4427 0.004   -0.0933 -0.0017 91  SER   A C   
703  O O   . SER   A 111 ? 0.5735 0.3007 0.4671 0.0028  -0.1009 -0.0018 91  SER   A O   
704  C CB  . SER   A 111 ? 0.5897 0.3029 0.4412 0.005   -0.0959 -0.002  91  SER   A CB  
705  O OG  . SER   A 111 ? 0.6364 0.3427 0.4648 0.0083  -0.093  -0.0027 91  SER   A OG  
706  N N   . ASP   A 112 ? 0.5532 0.2783 0.4121 0.0063  -0.0888 -0.0022 92  ASP   A N   
707  C CA  . ASP   A 112 ? 0.5463 0.2701 0.4062 0.0076  -0.0917 -0.0029 92  ASP   A CA  
708  C C   . ASP   A 112 ? 0.5352 0.2645 0.3837 0.0086  -0.0807 -0.0026 92  ASP   A C   
709  O O   . ASP   A 112 ? 0.5336 0.2597 0.3654 0.0099  -0.0757 -0.0026 92  ASP   A O   
710  C CB  . ASP   A 112 ? 0.577  0.2826 0.4218 0.0105  -0.1043 -0.0046 92  ASP   A CB  
711  C CG  . ASP   A 112 ? 0.6248 0.3283 0.4706 0.012   -0.1076 -0.0054 92  ASP   A CG  
712  O OD1 . ASP   A 112 ? 0.6317 0.3379 0.4975 0.0109  -0.115  -0.0056 92  ASP   A OD1 
713  O OD2 . ASP   A 112 ? 0.6292 0.3286 0.4569 0.0143  -0.1023 -0.0057 92  ASP   A OD2 
714  N N   . PHE   A 113 ? 0.5133 0.2499 0.3706 0.0083  -0.0773 -0.0024 93  PHE   A N   
715  C CA  . PHE   A 113 ? 0.5004 0.2425 0.3488 0.009   -0.0674 -0.0021 93  PHE   A CA  
716  C C   . PHE   A 113 ? 0.5199 0.2504 0.3439 0.0119  -0.0674 -0.0031 93  PHE   A C   
717  O O   . PHE   A 113 ? 0.5317 0.266  0.3473 0.0123  -0.0587 -0.0027 93  PHE   A O   
718  C CB  . PHE   A 113 ? 0.4797 0.2277 0.3392 0.0086  -0.0662 -0.002  93  PHE   A CB  
719  C CG  . PHE   A 113 ? 0.4788 0.2355 0.3347 0.0083  -0.0551 -0.0014 93  PHE   A CG  
720  C CD1 . PHE   A 113 ? 0.4647 0.2322 0.3307 0.0063  -0.0469 -0.0001 93  PHE   A CD1 
721  C CD2 . PHE   A 113 ? 0.4885 0.2407 0.3297 0.0101  -0.053  -0.0021 93  PHE   A CD2 
722  C CE1 . PHE   A 113 ? 0.4688 0.2424 0.3304 0.0062  -0.0381 0.0003  93  PHE   A CE1 
723  C CE2 . PHE   A 113 ? 0.4859 0.2458 0.325  0.0096  -0.0437 -0.0016 93  PHE   A CE2 
724  C CZ  . PHE   A 113 ? 0.4724 0.2428 0.3217 0.0077  -0.037  -0.0005 93  PHE   A CZ  
725  N N   . HIS   A 114 ? 0.5201 0.2351 0.3324 0.0142  -0.077  -0.0042 94  HIS   A N   
726  C CA  . HIS   A 114 ? 0.5373 0.2384 0.3248 0.0175  -0.076  -0.0048 94  HIS   A CA  
727  C C   . HIS   A 114 ? 0.5148 0.2152 0.2918 0.018   -0.0697 -0.0043 94  HIS   A C   
728  O O   . HIS   A 114 ? 0.5286 0.2231 0.2896 0.0202  -0.0638 -0.0042 94  HIS   A O   
729  C CB  . HIS   A 114 ? 0.59   0.2711 0.364  0.0205  -0.088  -0.0062 94  HIS   A CB  
730  C CG  . HIS   A 114 ? 0.6592 0.3246 0.407  0.0242  -0.0851 -0.0066 94  HIS   A CG  
731  N ND1 . HIS   A 114 ? 0.7047 0.3555 0.4326 0.0268  -0.0853 -0.0066 94  HIS   A ND1 
732  C CD2 . HIS   A 114 ? 0.6896 0.3524 0.4288 0.0257  -0.0802 -0.0067 94  HIS   A CD2 
733  C CE1 . HIS   A 114 ? 0.7175 0.3565 0.4256 0.03    -0.0803 -0.0067 94  HIS   A CE1 
734  N NE2 . HIS   A 114 ? 0.7242 0.37   0.4384 0.0293  -0.0771 -0.0068 94  HIS   A NE2 
735  N N   . VAL   A 115 ? 0.4941 0.201  0.2808 0.016   -0.0699 -0.0037 95  VAL   A N   
736  C CA  . VAL   A 115 ? 0.4953 0.2023 0.2728 0.0166  -0.0637 -0.0032 95  VAL   A CA  
737  C C   . VAL   A 115 ? 0.4895 0.206  0.2657 0.0166  -0.0524 -0.0026 95  VAL   A C   
738  O O   . VAL   A 115 ? 0.5003 0.2116 0.2631 0.0187  -0.0474 -0.0025 95  VAL   A O   
739  C CB  . VAL   A 115 ? 0.5113 0.2259 0.3021 0.014   -0.0648 -0.0026 95  VAL   A CB  
740  C CG1 . VAL   A 115 ? 0.5159 0.2342 0.3005 0.0143  -0.0571 -0.002  95  VAL   A CG1 
741  C CG2 . VAL   A 115 ? 0.5288 0.2314 0.3184 0.0144  -0.0765 -0.0032 95  VAL   A CG2 
742  N N   . PHE   A 116 ? 0.4724 0.2018 0.2627 0.0144  -0.0486 -0.0023 96  PHE   A N   
743  C CA  . PHE   A 116 ? 0.4614 0.1996 0.2517 0.0142  -0.0392 -0.0019 96  PHE   A CA  
744  C C   . PHE   A 116 ? 0.4744 0.2042 0.2508 0.0166  -0.0367 -0.0023 96  PHE   A C   
745  O O   . PHE   A 116 ? 0.4864 0.2171 0.2568 0.0176  -0.0299 -0.002  96  PHE   A O   
746  C CB  . PHE   A 116 ? 0.4527 0.2033 0.2584 0.0117  -0.0364 -0.0015 96  PHE   A CB  
747  C CG  . PHE   A 116 ? 0.4401 0.1985 0.2594 0.0094  -0.0363 -0.0008 96  PHE   A CG  
748  C CD1 . PHE   A 116 ? 0.4504 0.2103 0.2679 0.0091  -0.034  -0.0005 96  PHE   A CD1 
749  C CD2 . PHE   A 116 ? 0.4435 0.2077 0.2774 0.0077  -0.0371 -0.0003 96  PHE   A CD2 
750  C CE1 . PHE   A 116 ? 0.4557 0.2217 0.2846 0.0071  -0.0326 0.0003  96  PHE   A CE1 
751  C CE2 . PHE   A 116 ? 0.4462 0.2167 0.2922 0.0058  -0.0347 0.0006  96  PHE   A CE2 
752  C CZ  . PHE   A 116 ? 0.4427 0.2136 0.2856 0.0054  -0.0326 0.0009  96  PHE   A CZ  
753  N N   . VAL   A 117 ? 0.4656 0.1866 0.2374 0.0178  -0.0422 -0.0029 97  VAL   A N   
754  C CA  . VAL   A 117 ? 0.4871 0.1977 0.2441 0.0203  -0.0397 -0.0032 97  VAL   A CA  
755  C C   . VAL   A 117 ? 0.5063 0.2017 0.2442 0.0236  -0.0385 -0.0031 97  VAL   A C   
756  O O   . VAL   A 117 ? 0.5159 0.2086 0.2452 0.0251  -0.0304 -0.0027 97  VAL   A O   
757  C CB  . VAL   A 117 ? 0.5088 0.2118 0.2647 0.0211  -0.0474 -0.004  97  VAL   A CB  
758  C CG1 . VAL   A 117 ? 0.5367 0.2256 0.2743 0.0241  -0.045  -0.0044 97  VAL   A CG1 
759  C CG2 . VAL   A 117 ? 0.4922 0.21   0.2669 0.0182  -0.0468 -0.0038 97  VAL   A CG2 
760  N N   . ARG   A 118 ? 0.5074 0.1928 0.2394 0.0246  -0.0463 -0.0035 98  ARG   A N   
761  C CA  . ARG   A 118 ? 0.5241 0.194  0.2373 0.0279  -0.0455 -0.0033 98  ARG   A CA  
762  C C   . ARG   A 118 ? 0.5137 0.1919 0.2287 0.0278  -0.0354 -0.0023 98  ARG   A C   
763  O O   . ARG   A 118 ? 0.5446 0.2131 0.2457 0.0307  -0.0288 -0.0018 98  ARG   A O   
764  C CB  . ARG   A 118 ? 0.5656 0.2278 0.2777 0.0278  -0.0562 -0.0038 98  ARG   A CB  
765  C CG  . ARG   A 118 ? 0.5932 0.2373 0.2845 0.0314  -0.0569 -0.0037 98  ARG   A CG  
766  C CD  . ARG   A 118 ? 0.597  0.2394 0.293  0.0302  -0.0663 -0.004  98  ARG   A CD  
767  N NE  . ARG   A 118 ? 0.5928 0.2537 0.3054 0.0271  -0.061  -0.0033 98  ARG   A NE  
768  C CZ  . ARG   A 118 ? 0.5984 0.2634 0.3207 0.025   -0.0665 -0.0033 98  ARG   A CZ  
769  N NH1 . ARG   A 118 ? 0.6309 0.2835 0.3497 0.0253  -0.0781 -0.004  98  ARG   A NH1 
770  N NH2 . ARG   A 118 ? 0.5728 0.2528 0.3075 0.0226  -0.0607 -0.0026 98  ARG   A NH2 
771  N N   . ASP   A 119 ? 0.4963 0.1923 0.2291 0.0245  -0.0337 -0.002  99  ASP   A N   
772  C CA  . ASP   A 119 ? 0.489  0.1927 0.2244 0.0246  -0.0259 -0.0014 99  ASP   A CA  
773  C C   . ASP   A 119 ? 0.4802 0.1903 0.2184 0.0247  -0.017  -0.001  99  ASP   A C   
774  O O   . ASP   A 119 ? 0.4953 0.2037 0.2292 0.0265  -0.01   -0.0004 99  ASP   A O   
775  C CB  . ASP   A 119 ? 0.4726 0.1898 0.2228 0.0216  -0.0274 -0.0013 99  ASP   A CB  
776  C CG  . ASP   A 119 ? 0.4913 0.2016 0.2387 0.0216  -0.0349 -0.0014 99  ASP   A CG  
777  O OD1 . ASP   A 119 ? 0.5301 0.2237 0.2623 0.0242  -0.0398 -0.0017 99  ASP   A OD1 
778  O OD2 . ASP   A 119 ? 0.493  0.2129 0.2523 0.0191  -0.0362 -0.0012 99  ASP   A OD2 
779  N N   . VAL   A 120 ? 0.4662 0.1832 0.2124 0.0228  -0.017  -0.0013 100 VAL   A N   
780  C CA  . VAL   A 120 ? 0.4613 0.1826 0.2095 0.0229  -0.009  -0.001  100 VAL   A CA  
781  C C   . VAL   A 120 ? 0.4897 0.1947 0.2209 0.0265  -0.0046 -0.0006 100 VAL   A C   
782  O O   . VAL   A 120 ? 0.4959 0.2014 0.2268 0.0276  0.0037  0.0001  100 VAL   A O   
783  C CB  . VAL   A 120 ? 0.4581 0.1869 0.215  0.0207  -0.0104 -0.0014 100 VAL   A CB  
784  C CG1 . VAL   A 120 ? 0.4634 0.1935 0.2202 0.0209  -0.0029 -0.0011 100 VAL   A CG1 
785  C CG2 . VAL   A 120 ? 0.4544 0.1981 0.227  0.0176  -0.012  -0.0015 100 VAL   A CG2 
786  N N   . LEU   A 121 ? 0.4933 0.1828 0.2105 0.0285  -0.0104 -0.001  101 LEU   A N   
787  C CA  . LEU   A 121 ? 0.5277 0.1977 0.2248 0.0325  -0.0063 -0.0006 101 LEU   A CA  
788  C C   . LEU   A 121 ? 0.5345 0.1965 0.2224 0.0353  -0.0009 0.0003  101 LEU   A C   
789  O O   . LEU   A 121 ? 0.5472 0.2017 0.2275 0.0377  0.0088  0.0013  101 LEU   A O   
790  C CB  . LEU   A 121 ? 0.5506 0.2034 0.2328 0.0344  -0.0153 -0.0015 101 LEU   A CB  
791  C CG  . LEU   A 121 ? 0.5802 0.2373 0.2684 0.0328  -0.0184 -0.0022 101 LEU   A CG  
792  C CD1 . LEU   A 121 ? 0.6107 0.2527 0.2881 0.0344  -0.0301 -0.0033 101 LEU   A CD1 
793  C CD2 . LEU   A 121 ? 0.5784 0.2326 0.2616 0.0337  -0.0084 -0.0016 101 LEU   A CD2 
794  N N   . GLN   A 122 ? 0.5224 0.1871 0.2128 0.0348  -0.006  0.0002  102 GLN   A N   
795  C CA  . GLN   A 122 ? 0.5221 0.18   0.2046 0.0374  -0.001  0.001   102 GLN   A CA  
796  C C   . GLN   A 122 ? 0.5296 0.2012 0.2255 0.0367  0.0096  0.0019  102 GLN   A C   
797  O O   . GLN   A 122 ? 0.5579 0.221  0.2463 0.0398  0.0184  0.003   102 GLN   A O   
798  C CB  . GLN   A 122 ? 0.5261 0.1864 0.211  0.0364  -0.009  0.0006  102 GLN   A CB  
799  C CG  . GLN   A 122 ? 0.5368 0.1906 0.2138 0.0393  -0.0039 0.0015  102 GLN   A CG  
800  C CD  . GLN   A 122 ? 0.5628 0.2232 0.2462 0.0377  -0.01   0.0012  102 GLN   A CD  
801  O OE1 . GLN   A 122 ? 0.5929 0.2603 0.2852 0.0346  -0.0185 0.0003  102 GLN   A OE1 
802  N NE2 . GLN   A 122 ? 0.585  0.2431 0.2647 0.0398  -0.005  0.0019  102 GLN   A NE2 
803  N N   . HIS   A 123 ? 0.5031 0.195  0.2194 0.0328  0.0088  0.0015  103 HIS   A N   
804  C CA  . HIS   A 123 ? 0.5041 0.2088 0.2344 0.0321  0.0166  0.002   103 HIS   A CA  
805  C C   . HIS   A 123 ? 0.5129 0.2145 0.2429 0.033   0.0252  0.0027  103 HIS   A C   
806  O O   . HIS   A 123 ? 0.5295 0.2309 0.2629 0.0347  0.0341  0.0037  103 HIS   A O   
807  C CB  . HIS   A 123 ? 0.476  0.1996 0.2247 0.028   0.0123  0.0012  103 HIS   A CB  
808  C CG  . HIS   A 123 ? 0.4716 0.2073 0.234  0.0274  0.0167  0.0014  103 HIS   A CG  
809  N ND1 . HIS   A 123 ? 0.4609 0.2103 0.2362 0.0246  0.0127  0.0006  103 HIS   A ND1 
810  C CD2 . HIS   A 123 ? 0.4748 0.2095 0.2396 0.0296  0.0242  0.0022  103 HIS   A CD2 
811  C CE1 . HIS   A 123 ? 0.4663 0.2223 0.251  0.0251  0.0168  0.0008  103 HIS   A CE1 
812  N NE2 . HIS   A 123 ? 0.4694 0.2177 0.2495 0.0281  0.0237  0.0018  103 HIS   A NE2 
813  N N   . VAL   A 124 ? 0.5073 0.2057 0.2336 0.032   0.023   0.0022  104 VAL   A N   
814  C CA  . VAL   A 124 ? 0.5172 0.2112 0.2419 0.0329  0.0313  0.0029  104 VAL   A CA  
815  C C   . VAL   A 124 ? 0.5441 0.2174 0.2499 0.0376  0.0391  0.0042  104 VAL   A C   
816  O O   . VAL   A 124 ? 0.5613 0.2334 0.2708 0.039   0.05    0.0054  104 VAL   A O   
817  C CB  . VAL   A 124 ? 0.5356 0.2267 0.2559 0.0316  0.0265  0.002   104 VAL   A CB  
818  C CG1 . VAL   A 124 ? 0.5637 0.2441 0.2759 0.0333  0.0351  0.0028  104 VAL   A CG1 
819  C CG2 . VAL   A 124 ? 0.5238 0.2342 0.2627 0.0273  0.0218  0.0011  104 VAL   A CG2 
820  N N   . ASP   A 125 ? 0.5638 0.2208 0.2506 0.0403  0.0335  0.0039  105 ASP   A N   
821  C CA  . ASP   A 125 ? 0.6009 0.2347 0.2657 0.0454  0.0403  0.0051  105 ASP   A CA  
822  C C   . ASP   A 125 ? 0.6138 0.2506 0.2847 0.0471  0.0493  0.0065  105 ASP   A C   
823  O O   . ASP   A 125 ? 0.6504 0.2761 0.3147 0.0503  0.061   0.0081  105 ASP   A O   
824  C CB  . ASP   A 125 ? 0.6387 0.2531 0.2811 0.0479  0.0305  0.0044  105 ASP   A CB  
825  C CG  . ASP   A 125 ? 0.6957 0.3017 0.3289 0.0475  0.023   0.0032  105 ASP   A CG  
826  O OD1 . ASP   A 125 ? 0.7018 0.3112 0.3396 0.0465  0.0281  0.0034  105 ASP   A OD1 
827  O OD2 . ASP   A 125 ? 0.7061 0.3014 0.3277 0.0484  0.0116  0.0021  105 ASP   A OD2 
828  N N   . SER   A 126 ? 0.5852 0.237  0.2698 0.0451  0.0443  0.006   106 SER   A N   
829  C CA  A SER   A 126 ? 0.592  0.2485 0.2847 0.0466  0.0515  0.0071  106 SER   A CA  
830  C CA  C SER   A 126 ? 0.5954 0.2519 0.2881 0.0466  0.0515  0.0071  106 SER   A CA  
831  C C   . SER   A 126 ? 0.6095 0.2785 0.322  0.0454  0.0616  0.0079  106 SER   A C   
832  O O   . SER   A 126 ? 0.6358 0.2985 0.3482 0.0485  0.0727  0.0096  106 SER   A O   
833  C CB  A SER   A 126 ? 0.5853 0.256  0.2892 0.0442  0.043   0.0061  106 SER   A CB  
834  C CB  C SER   A 126 ? 0.5981 0.2684 0.3015 0.0443  0.0429  0.0061  106 SER   A CB  
835  O OG  A SER   A 126 ? 0.5909 0.2627 0.2989 0.0465  0.049   0.0071  106 SER   A OG  
836  O OG  C SER   A 126 ? 0.6306 0.2871 0.3158 0.0457  0.0348  0.0055  106 SER   A OG  
837  N N   . MET   A 127 ? 0.5939 0.2799 0.3238 0.0411  0.0581  0.0069  107 MET   A N   
838  C CA  . MET   A 127 ? 0.6089 0.3067 0.3588 0.0397  0.0661  0.0075  107 MET   A CA  
839  C C   . MET   A 127 ? 0.6467 0.3314 0.3893 0.0419  0.0777  0.009   107 MET   A C   
840  O O   . MET   A 127 ? 0.6586 0.347  0.415  0.0426  0.088   0.0103  107 MET   A O   
841  C CB  . MET   A 127 ? 0.5967 0.3127 0.3633 0.0348  0.0588  0.006   107 MET   A CB  
842  C CG  . MET   A 127 ? 0.615  0.3447 0.3923 0.0328  0.0507  0.0049  107 MET   A CG  
843  S SD  . MET   A 127 ? 0.6876 0.4267 0.4836 0.034   0.0567  0.0056  107 MET   A SD  
844  C CE  . MET   A 127 ? 0.6319 0.3851 0.4502 0.0308  0.0586  0.0052  107 MET   A CE  
845  N N   . GLN   A 128 ? 0.6526 0.3216 0.3747 0.0432  0.076   0.0089  108 GLN   A N   
846  C CA  . GLN   A 128 ? 0.7041 0.3573 0.4154 0.0457  0.0871  0.0103  108 GLN   A CA  
847  C C   . GLN   A 128 ? 0.7684 0.4038 0.4672 0.051   0.0989  0.0124  108 GLN   A C   
848  O O   . GLN   A 128 ? 0.7979 0.4247 0.4964 0.0529  0.1121  0.0142  108 GLN   A O   
849  C CB  . GLN   A 128 ? 0.7202 0.3597 0.4112 0.046   0.0809  0.0094  108 GLN   A CB  
850  C CG  . GLN   A 128 ? 0.7516 0.409  0.4586 0.041   0.0739  0.0079  108 GLN   A CG  
851  C CD  . GLN   A 128 ? 0.8371 0.4807 0.5278 0.0417  0.0727  0.0075  108 GLN   A CD  
852  O OE1 . GLN   A 128 ? 0.8771 0.5132 0.554  0.0421  0.0623  0.0062  108 GLN   A OE1 
853  N NE2 . GLN   A 128 ? 0.8475 0.4872 0.5402 0.0419  0.0831  0.0086  108 GLN   A NE2 
854  N N   . LYS   A 129 ? 0.8087 0.4386 0.4981 0.0533  0.0951  0.0124  109 LYS   A N   
855  C CA  . LYS   A 129 ? 0.8451 0.4588 0.5234 0.0586  0.1065  0.0145  109 LYS   A CA  
856  C C   . LYS   A 129 ? 0.8546 0.485  0.5613 0.0578  0.1163  0.0158  109 LYS   A C   
857  O O   . LYS   A 129 ? 0.8735 0.4938 0.5801 0.0611  0.1311  0.0181  109 LYS   A O   
858  C CB  . LYS   A 129 ? 0.8848 0.4902 0.5475 0.0608  0.0982  0.0139  109 LYS   A CB  
859  C CG  . LYS   A 129 ? 0.9643 0.5455 0.5951 0.0634  0.0912  0.0133  109 LYS   A CG  
860  C CD  . LYS   A 129 ? 1.0349 0.6109 0.6547 0.0648  0.0818  0.0126  109 LYS   A CD  
861  C CE  . LYS   A 129 ? 1.083  0.6455 0.6932 0.0699  0.0924  0.0146  109 LYS   A CE  
862  N NZ  . LYS   A 129 ? 1.0992 0.6793 0.7264 0.0683  0.0882  0.0141  109 LYS   A NZ  
863  N N   . ASP   A 130 ? 0.8445 0.4993 0.5755 0.0537  0.1081  0.0144  110 ASP   A N   
864  C CA  . ASP   A 130 ? 0.8472 0.5186 0.6068 0.0528  0.1146  0.0151  110 ASP   A CA  
865  C C   . ASP   A 130 ? 0.8459 0.5261 0.6253 0.0503  0.1219  0.0157  110 ASP   A C   
866  O O   . ASP   A 130 ? 0.8478 0.5361 0.6494 0.0506  0.1308  0.017   110 ASP   A O   
867  C CB  . ASP   A 130 ? 0.8693 0.5613 0.6455 0.0495  0.1023  0.0132  110 ASP   A CB  
868  C CG  . ASP   A 130 ? 0.9762 0.662  0.7376 0.0516  0.0956  0.0128  110 ASP   A CG  
869  O OD1 . ASP   A 130 ? 1.0143 0.679  0.751  0.0558  0.0995  0.0138  110 ASP   A OD1 
870  O OD2 . ASP   A 130 ? 1.0077 0.7083 0.7809 0.0493  0.0865  0.0113  110 ASP   A OD2 
871  N N   . TYR   A 131 ? 0.8387 0.5181 0.6121 0.0476  0.1177  0.0147  111 TYR   A N   
872  C CA  . TYR   A 131 ? 0.826  0.513  0.6165 0.0449  0.1236  0.0151  111 TYR   A CA  
873  C C   . TYR   A 131 ? 0.8421 0.5102 0.6093 0.0462  0.1276  0.0156  111 TYR   A C   
874  O O   . TYR   A 131 ? 0.8545 0.5267 0.6186 0.0431  0.1192  0.014   111 TYR   A O   
875  C CB  . TYR   A 131 ? 0.8062 0.5163 0.6178 0.0393  0.1115  0.0128  111 TYR   A CB  
876  C CG  . TYR   A 131 ? 0.8043 0.5313 0.6366 0.0382  0.106   0.0121  111 TYR   A CG  
877  C CD1 . TYR   A 131 ? 0.8177 0.547  0.6414 0.0384  0.0956  0.0108  111 TYR   A CD1 
878  C CD2 . TYR   A 131 ? 0.8051 0.5444 0.6657 0.0373  0.1113  0.0127  111 TYR   A CD2 
879  C CE1 . TYR   A 131 ? 0.8262 0.5687 0.6664 0.0379  0.0908  0.0101  111 TYR   A CE1 
880  C CE2 . TYR   A 131 ? 0.8073 0.5603 0.6857 0.0368  0.1055  0.0118  111 TYR   A CE2 
881  C CZ  . TYR   A 131 ? 0.8303 0.5843 0.6972 0.0373  0.0954  0.0105  111 TYR   A CZ  
882  O OH  . TYR   A 131 ? 0.8546 0.6206 0.7368 0.037   0.0893  0.0096  111 TYR   A OH  
883  N N   . PRO   A 132 ? 0.8434 0.4886 0.5917 0.0512  0.1404  0.0178  112 PRO   A N   
884  C CA  . PRO   A 132 ? 0.8462 0.4698 0.5683 0.0531  0.1438  0.0181  112 PRO   A CA  
885  C C   . PRO   A 132 ? 0.8324 0.4601 0.5672 0.0505  0.151   0.0187  112 PRO   A C   
886  O O   . PRO   A 132 ? 0.8277 0.4698 0.5905 0.0484  0.1584  0.0196  112 PRO   A O   
887  C CB  . PRO   A 132 ? 0.8742 0.4711 0.5734 0.0597  0.1568  0.0206  112 PRO   A CB  
888  C CG  . PRO   A 132 ? 0.872  0.4804 0.5958 0.0603  0.1664  0.0222  112 PRO   A CG  
889  C CD  . PRO   A 132 ? 0.8385 0.4743 0.5861 0.0558  0.1524  0.02    112 PRO   A CD  
890  N N   . GLY   A 133 ? 0.8262 0.4403 0.5401 0.0507  0.1484  0.018   113 GLY   A N   
891  C CA  . GLY   A 133 ? 0.8149 0.4297 0.536  0.0485  0.1548  0.0184  113 GLY   A CA  
892  C C   . GLY   A 133 ? 0.7804 0.4207 0.5262 0.0423  0.1446  0.0165  113 GLY   A C   
893  O O   . GLY   A 133 ? 0.7874 0.4291 0.5397 0.04    0.1488  0.0167  113 GLY   A O   
894  N N   . LEU   A 134 ? 0.743  0.4022 0.5016 0.0396  0.1316  0.0146  114 LEU   A N   
895  C CA  . LEU   A 134 ? 0.7098 0.391  0.4896 0.0341  0.1221  0.0128  114 LEU   A CA  
896  C C   . LEU   A 134 ? 0.6869 0.3668 0.4518 0.0326  0.1096  0.0109  114 LEU   A C   
897  O O   . LEU   A 134 ? 0.7012 0.3729 0.4478 0.0346  0.1021  0.0101  114 LEU   A O   
898  C CB  . LEU   A 134 ? 0.6992 0.4014 0.5024 0.0318  0.1152  0.012   114 LEU   A CB  
899  C CG  . LEU   A 134 ? 0.7226 0.4323 0.5496 0.0323  0.1251  0.0135  114 LEU   A CG  
900  C CD1 . LEU   A 134 ? 0.7214 0.4508 0.5688 0.03    0.1153  0.0121  114 LEU   A CD1 
901  C CD2 . LEU   A 134 ? 0.7248 0.4377 0.5696 0.0301  0.1345  0.0146  114 LEU   A CD2 
902  N N   . PRO   A 135 ? 0.6523 0.3413 0.4268 0.029   0.1067  0.01    115 PRO   A N   
903  C CA  . PRO   A 135 ? 0.6257 0.316  0.3898 0.0273  0.0946  0.0081  115 PRO   A CA  
904  C C   . PRO   A 135 ? 0.5764 0.2814 0.3482 0.0255  0.0822  0.0066  115 PRO   A C   
905  O O   . PRO   A 135 ? 0.5722 0.2907 0.3625 0.0241  0.0821  0.0066  115 PRO   A O   
906  C CB  . PRO   A 135 ? 0.642  0.3422 0.4205 0.0235  0.0953  0.0077  115 PRO   A CB  
907  C CG  . PRO   A 135 ? 0.6577 0.3551 0.4477 0.0239  0.1095  0.0096  115 PRO   A CG  
908  C CD  . PRO   A 135 ? 0.6474 0.3461 0.4442 0.0261  0.114   0.0107  115 PRO   A CD  
909  N N   . VAL   A 136 ? 0.5328 0.2338 0.2905 0.0258  0.0722  0.0053  116 VAL   A N   
910  C CA  A VAL   A 136 ? 0.5181 0.2321 0.2831 0.0241  0.0615  0.004   116 VAL   A CA  
911  C CA  B VAL   A 136 ? 0.5126 0.226  0.2768 0.0242  0.0613  0.004   116 VAL   A CA  
912  C C   . VAL   A 136 ? 0.5025 0.2236 0.2692 0.0213  0.0526  0.0026  116 VAL   A C   
913  O O   . VAL   A 136 ? 0.535  0.2458 0.288  0.0223  0.0505  0.0023  116 VAL   A O   
914  C CB  A VAL   A 136 ? 0.5547 0.2599 0.3064 0.027   0.0579  0.0041  116 VAL   A CB  
915  C CB  B VAL   A 136 ? 0.5356 0.2376 0.2831 0.0273  0.0572  0.004   116 VAL   A CB  
916  C CG1 A VAL   A 136 ? 0.5878 0.2742 0.3157 0.0297  0.0543  0.0038  116 VAL   A CG1 
917  C CG1 B VAL   A 136 ? 0.5302 0.245  0.2857 0.0254  0.0469  0.0028  116 VAL   A CG1 
918  C CG2 A VAL   A 136 ? 0.5395 0.2591 0.3017 0.0249  0.0486  0.003   116 VAL   A CG2 
919  C CG2 B VAL   A 136 ? 0.5388 0.2315 0.2819 0.0306  0.0665  0.0055  116 VAL   A CG2 
920  N N   . PHE   A 137 ? 0.4707 0.2086 0.2541 0.0182  0.0476  0.0018  117 PHE   A N   
921  C CA  . PHE   A 137 ? 0.4592 0.2046 0.2458 0.0157  0.0402  0.0007  117 PHE   A CA  
922  C C   . PHE   A 137 ? 0.4536 0.2049 0.2412 0.0154  0.0318  0       117 PHE   A C   
923  O O   . PHE   A 137 ? 0.4517 0.2044 0.2412 0.0163  0.0319  0.0003  117 PHE   A O   
924  C CB  . PHE   A 137 ? 0.4469 0.2057 0.2512 0.0125  0.041   0.0004  117 PHE   A CB  
925  C CG  . PHE   A 137 ? 0.4758 0.2304 0.2818 0.012   0.0483  0.001   117 PHE   A CG  
926  C CD1 . PHE   A 137 ? 0.5044 0.2559 0.3157 0.013   0.0574  0.0022  117 PHE   A CD1 
927  C CD2 . PHE   A 137 ? 0.4892 0.2442 0.2938 0.0103  0.0466  0.0005  117 PHE   A CD2 
928  C CE1 . PHE   A 137 ? 0.5183 0.2657 0.3325 0.0123  0.0651  0.0029  117 PHE   A CE1 
929  C CE2 . PHE   A 137 ? 0.5039 0.2545 0.31   0.0097  0.0537  0.0011  117 PHE   A CE2 
930  C CZ  . PHE   A 137 ? 0.5142 0.261  0.3251 0.0107  0.063   0.0023  117 PHE   A CZ  
931  N N   . LEU   A 138 ? 0.4519 0.2064 0.239  0.014   0.0253  -0.0007 118 LEU   A N   
932  C CA  . LEU   A 138 ? 0.4494 0.2103 0.2399 0.0132  0.0183  -0.0012 118 LEU   A CA  
933  C C   . LEU   A 138 ? 0.4359 0.2077 0.2371 0.0106  0.0161  -0.0017 118 LEU   A C   
934  O O   . LEU   A 138 ? 0.4371 0.2092 0.2391 0.0096  0.0173  -0.0018 118 LEU   A O   
935  C CB  . LEU   A 138 ? 0.4584 0.2115 0.2391 0.0144  0.0127  -0.0015 118 LEU   A CB  
936  C CG  . LEU   A 138 ? 0.5062 0.2444 0.2722 0.0176  0.0132  -0.0012 118 LEU   A CG  
937  C CD1 . LEU   A 138 ? 0.5437 0.2722 0.2997 0.0189  0.0066  -0.0017 118 LEU   A CD1 
938  C CD2 . LEU   A 138 ? 0.5235 0.2627 0.2902 0.0184  0.0129  -0.0009 118 LEU   A CD2 
939  N N   . LEU   A 139 ? 0.4077 0.1868 0.2154 0.0096  0.0129  -0.0019 119 LEU   A N   
940  C CA  . LEU   A 139 ? 0.4096 0.1962 0.2241 0.0077  0.0104  -0.0023 119 LEU   A CA  
941  C C   . LEU   A 139 ? 0.4055 0.1933 0.2197 0.0077  0.0061  -0.0022 119 LEU   A C   
942  O O   . LEU   A 139 ? 0.4067 0.1947 0.2208 0.0084  0.0053  -0.0021 119 LEU   A O   
943  C CB  . LEU   A 139 ? 0.4277 0.2205 0.2509 0.0066  0.0116  -0.0026 119 LEU   A CB  
944  C CG  . LEU   A 139 ? 0.4576 0.255  0.2849 0.0049  0.0089  -0.0031 119 LEU   A CG  
945  C CD1 . LEU   A 139 ? 0.4667 0.2672 0.3014 0.0038  0.0099  -0.0036 119 LEU   A CD1 
946  C CD2 . LEU   A 139 ? 0.4479 0.2474 0.2755 0.0051  0.0056  -0.0032 119 LEU   A CD2 
947  N N   . GLY   A 140 ? 0.401  0.1897 0.2159 0.007   0.004   -0.0022 120 GLY   A N   
948  C CA  . GLY   A 140 ? 0.3968 0.1868 0.2137 0.0069  0.0009  -0.0019 120 GLY   A CA  
949  C C   . GLY   A 140 ? 0.395  0.1884 0.2162 0.0059  0.0009  -0.0017 120 GLY   A C   
950  O O   . GLY   A 140 ? 0.3993 0.1925 0.2202 0.0055  0.0019  -0.0017 120 GLY   A O   
951  N N   . HIS   A 141 ? 0.3758 0.1711 0.1998 0.0056  0.0004  -0.0013 121 HIS   A N   
952  C CA  . HIS   A 141 ? 0.3768 0.1731 0.2035 0.0051  0.0016  -0.0007 121 HIS   A CA  
953  C C   . HIS   A 141 ? 0.3727 0.1686 0.2041 0.0052  0.0006  0.0001  121 HIS   A C   
954  O O   . HIS   A 141 ? 0.3825 0.1782 0.2149 0.0053  -0.0008 0.0002  121 HIS   A O   
955  C CB  . HIS   A 141 ? 0.4007 0.1974 0.2257 0.0049  0.0026  -0.0009 121 HIS   A CB  
956  C CG  . HIS   A 141 ? 0.3869 0.1817 0.2119 0.005   0.0047  -0.0001 121 HIS   A CG  
957  N ND1 . HIS   A 141 ? 0.3896 0.1833 0.2148 0.0049  0.0066  0.0004  121 HIS   A ND1 
958  C CD2 . HIS   A 141 ? 0.4026 0.1951 0.2263 0.0053  0.0058  0.0004  121 HIS   A CD2 
959  C CE1 . HIS   A 141 ? 0.4025 0.1928 0.2263 0.0054  0.0094  0.0013  121 HIS   A CE1 
960  N NE2 . HIS   A 141 ? 0.4226 0.2118 0.2453 0.0057  0.0092  0.0014  121 HIS   A NE2 
961  N N   . SER   A 142 ? 0.3738 0.1699 0.2096 0.0051  0.0016  0.0008  122 SER   A N   
962  C CA  . SER   A 142 ? 0.3803 0.1767 0.2243 0.0051  0.0016  0.0018  122 SER   A CA  
963  C C   . SER   A 142 ? 0.3841 0.1793 0.2313 0.0053  -0.0035 0.0015  122 SER   A C   
964  O O   . SER   A 142 ? 0.3883 0.1812 0.2324 0.0059  -0.0068 0.0008  122 SER   A O   
965  C CB  . SER   A 142 ? 0.4138 0.2097 0.2581 0.0049  0.0054  0.0026  122 SER   A CB  
966  O OG  . SER   A 142 ? 0.4294 0.2254 0.2832 0.0048  0.0077  0.004   122 SER   A OG  
967  N N   . MET   A 143 ? 0.372  0.1674 0.2234 0.0049  -0.0043 0.002   123 MET   A N   
968  C CA  . MET   A 143 ? 0.3853 0.1779 0.2377 0.0052  -0.0102 0.0016  123 MET   A CA  
969  C C   . MET   A 143 ? 0.392  0.181  0.2327 0.0061  -0.0122 0.0005  123 MET   A C   
970  O O   . MET   A 143 ? 0.4168 0.2006 0.2541 0.007   -0.0169 -0.0001 123 MET   A O   
971  C CB  . MET   A 143 ? 0.3975 0.1903 0.2544 0.0045  -0.0104 0.0022  123 MET   A CB  
972  C CG  . MET   A 143 ? 0.4192 0.2079 0.2767 0.0048  -0.0172 0.0017  123 MET   A CG  
973  S SD  . MET   A 143 ? 0.4381 0.2267 0.2995 0.0038  -0.017  0.0025  123 MET   A SD  
974  C CE  . MET   A 143 ? 0.417  0.2038 0.2626 0.0049  -0.0155 0.0015  123 MET   A CE  
975  N N   . GLY   A 144 ? 0.3779 0.1685 0.2125 0.0061  -0.0086 0.0002  124 GLY   A N   
976  C CA  . GLY   A 144 ? 0.3855 0.1733 0.2112 0.0071  -0.0086 -0.0006 124 GLY   A CA  
977  C C   . GLY   A 144 ? 0.3984 0.1832 0.2201 0.0077  -0.0087 -0.001  124 GLY   A C   
978  O O   . GLY   A 144 ? 0.4146 0.194  0.2286 0.0089  -0.0091 -0.0015 124 GLY   A O   
979  N N   . GLY   A 145 ? 0.4042 0.1915 0.2299 0.0071  -0.0075 -0.0009 125 GLY   A N   
980  C CA  . GLY   A 145 ? 0.405  0.1892 0.2271 0.0076  -0.0076 -0.0013 125 GLY   A CA  
981  C C   . GLY   A 145 ? 0.4145 0.1925 0.2357 0.0088  -0.0131 -0.0015 125 GLY   A C   
982  O O   . GLY   A 145 ? 0.4386 0.2094 0.251  0.0101  -0.0144 -0.0021 125 GLY   A O   
983  N N   . ALA   A 146 ? 0.4267 0.2062 0.2567 0.0085  -0.0166 -0.0011 126 ALA   A N   
984  C CA  . ALA   A 146 ? 0.4444 0.2172 0.2749 0.0096  -0.0238 -0.0015 126 ALA   A CA  
985  C C   . ALA   A 146 ? 0.4456 0.2097 0.2641 0.011   -0.0267 -0.0021 126 ALA   A C   
986  O O   . ALA   A 146 ? 0.4698 0.2238 0.2788 0.0129  -0.0309 -0.0028 126 ALA   A O   
987  C CB  . ALA   A 146 ? 0.4394 0.2161 0.2844 0.0087  -0.0267 -0.0008 126 ALA   A CB  
988  N N   . ILE   A 147 ? 0.4327 0.1993 0.2496 0.0105  -0.0239 -0.0018 127 ILE   A N   
989  C CA  . ILE   A 147 ? 0.4365 0.1946 0.2414 0.0121  -0.0252 -0.0022 127 ILE   A CA  
990  C C   . ILE   A 147 ? 0.4512 0.2029 0.2439 0.0137  -0.0216 -0.0025 127 ILE   A C   
991  O O   . ILE   A 147 ? 0.4685 0.2078 0.249  0.0159  -0.0246 -0.003  127 ILE   A O   
992  C CB  . ILE   A 147 ? 0.4397 0.2028 0.2463 0.0114  -0.0221 -0.0017 127 ILE   A CB  
993  C CG1 . ILE   A 147 ? 0.4307 0.1972 0.2476 0.01    -0.0257 -0.0013 127 ILE   A CG1 
994  C CG2 . ILE   A 147 ? 0.4502 0.2048 0.244  0.0133  -0.0214 -0.002  127 ILE   A CG2 
995  C CD1 . ILE   A 147 ? 0.4291 0.2017 0.249  0.009   -0.0218 -0.0008 127 ILE   A CD1 
996  N N   . ALA   A 148 ? 0.4315 0.19   0.2268 0.0126  -0.0153 -0.0023 128 ALA   A N   
997  C CA  . ALA   A 148 ? 0.4477 0.2006 0.2335 0.0138  -0.0109 -0.0025 128 ALA   A CA  
998  C C   . ALA   A 148 ? 0.4738 0.217  0.252  0.0153  -0.0142 -0.003  128 ALA   A C   
999  O O   . ALA   A 148 ? 0.4805 0.2116 0.2451 0.0175  -0.013  -0.0032 128 ALA   A O   
1000 C CB  . ALA   A 148 ? 0.4395 0.2019 0.232  0.012   -0.005  -0.0023 128 ALA   A CB  
1001 N N   . ILE   A 149 ? 0.461  0.2081 0.2472 0.0145  -0.0181 -0.0032 129 ILE   A N   
1002 C CA  . ILE   A 149 ? 0.469  0.2063 0.2484 0.0162  -0.0225 -0.0038 129 ILE   A CA  
1003 C C   . ILE   A 149 ? 0.4872 0.2101 0.2555 0.0187  -0.0296 -0.0044 129 ILE   A C   
1004 O O   . ILE   A 149 ? 0.5041 0.2128 0.2571 0.0212  -0.0307 -0.0049 129 ILE   A O   
1005 C CB  . ILE   A 149 ? 0.476  0.2209 0.269  0.015   -0.026  -0.0038 129 ILE   A CB  
1006 C CG1 . ILE   A 149 ? 0.4852 0.24   0.2843 0.0132  -0.0192 -0.0033 129 ILE   A CG1 
1007 C CG2 . ILE   A 149 ? 0.4957 0.2299 0.284  0.0171  -0.0336 -0.0046 129 ILE   A CG2 
1008 C CD1 . ILE   A 149 ? 0.479  0.2419 0.2919 0.0121  -0.0205 -0.0028 129 ILE   A CD1 
1009 N N   . LEU   A 150 ? 0.4862 0.2111 0.261  0.0182  -0.0347 -0.0043 130 LEU   A N   
1010 C CA  . LEU   A 150 ? 0.5078 0.2179 0.2719 0.0206  -0.0429 -0.005  130 LEU   A CA  
1011 C C   . LEU   A 150 ? 0.5351 0.2333 0.2808 0.0229  -0.0388 -0.0049 130 LEU   A C   
1012 O O   . LEU   A 150 ? 0.5935 0.2737 0.3224 0.026   -0.0435 -0.0056 130 LEU   A O   
1013 C CB  . LEU   A 150 ? 0.4905 0.2065 0.2684 0.0191  -0.0492 -0.0049 130 LEU   A CB  
1014 C CG  . LEU   A 150 ? 0.5169 0.2429 0.3139 0.0174  -0.0526 -0.0048 130 LEU   A CG  
1015 C CD1 . LEU   A 150 ? 0.5124 0.2449 0.3248 0.0156  -0.0565 -0.0044 130 LEU   A CD1 
1016 C CD2 . LEU   A 150 ? 0.5417 0.2577 0.3352 0.0194  -0.0604 -0.0058 130 LEU   A CD2 
1017 N N   . THR   A 151 ? 0.5117 0.2182 0.2596 0.0218  -0.0298 -0.0041 131 THR   A N   
1018 C CA  . THR   A 151 ? 0.5284 0.2243 0.2611 0.024   -0.0243 -0.0037 131 THR   A CA  
1019 C C   . THR   A 151 ? 0.5476 0.2318 0.2665 0.0262  -0.0199 -0.0038 131 THR   A C   
1020 O O   . THR   A 151 ? 0.5659 0.2311 0.2655 0.0296  -0.0206 -0.0039 131 THR   A O   
1021 C CB  . THR   A 151 ? 0.5222 0.2323 0.2652 0.022   -0.0163 -0.0029 131 THR   A CB  
1022 O OG1 . THR   A 151 ? 0.5164 0.2345 0.2694 0.0205  -0.0206 -0.0028 131 THR   A OG1 
1023 C CG2 . THR   A 151 ? 0.5552 0.2567 0.2864 0.0243  -0.009  -0.0022 131 THR   A CG2 
1024 N N   . ALA   A 152 ? 0.5291 0.2224 0.256  0.0244  -0.0159 -0.0037 132 ALA   A N   
1025 C CA  . ALA   A 152 ? 0.5679 0.2501 0.2821 0.0262  -0.0112 -0.0037 132 ALA   A CA  
1026 C C   . ALA   A 152 ? 0.6255 0.2904 0.3255 0.029   -0.0197 -0.0047 132 ALA   A C   
1027 O O   . ALA   A 152 ? 0.6759 0.3224 0.3564 0.0322  -0.0171 -0.0047 132 ALA   A O   
1028 C CB  . ALA   A 152 ? 0.5466 0.2424 0.2732 0.0234  -0.0062 -0.0035 132 ALA   A CB  
1029 N N   . ALA   A 153 ? 0.6263 0.2955 0.3357 0.0282  -0.0299 -0.0055 133 ALA   A N   
1030 C CA  . ALA   A 153 ? 0.6672 0.3198 0.3649 0.031   -0.0399 -0.0067 133 ALA   A CA  
1031 C C   . ALA   A 153 ? 0.6928 0.3242 0.3705 0.0347  -0.0452 -0.0072 133 ALA   A C   
1032 O O   . ALA   A 153 ? 0.7233 0.3339 0.3823 0.0382  -0.0511 -0.0081 133 ALA   A O   
1033 C CB  . ALA   A 153 ? 0.6666 0.3297 0.3827 0.0292  -0.0495 -0.0074 133 ALA   A CB  
1034 N N   . GLU   A 154 ? 0.673  0.3082 0.3534 0.0341  -0.0439 -0.0066 134 GLU   A N   
1035 C CA  . GLU   A 154 ? 0.7018 0.3169 0.3628 0.0375  -0.0483 -0.0068 134 GLU   A CA  
1036 C C   . GLU   A 154 ? 0.7317 0.3287 0.3688 0.041   -0.0383 -0.0061 134 GLU   A C   
1037 O O   . GLU   A 154 ? 0.7746 0.3476 0.3884 0.0452  -0.0419 -0.0064 134 GLU   A O   
1038 C CB  . GLU   A 154 ? 0.7278 0.3541 0.4002 0.0355  -0.0485 -0.0063 134 GLU   A CB  
1039 C CG  . GLU   A 154 ? 0.8076 0.4132 0.4612 0.0389  -0.0553 -0.0067 134 GLU   A CG  
1040 C CD  . GLU   A 154 ? 0.868  0.483  0.5342 0.0368  -0.0601 -0.0066 134 GLU   A CD  
1041 O OE1 . GLU   A 154 ? 0.8551 0.4883 0.5444 0.0332  -0.0641 -0.0067 134 GLU   A OE1 
1042 O OE2 . GLU   A 154 ? 0.9343 0.5374 0.5868 0.039   -0.0598 -0.0063 134 GLU   A OE2 
1043 N N   . ARG   A 155 ? 0.6977 0.3049 0.3405 0.0396  -0.0254 -0.0049 135 ARG   A N   
1044 C CA  . ARG   A 155 ? 0.7011 0.2936 0.3259 0.0425  -0.0138 -0.0039 135 ARG   A CA  
1045 C C   . ARG   A 155 ? 0.7176 0.3113 0.3425 0.0419  -0.0068 -0.0036 135 ARG   A C   
1046 O O   . ARG   A 155 ? 0.697  0.3025 0.3323 0.0399  0.0043  -0.0025 135 ARG   A O   
1047 C CB  . ARG   A 155 ? 0.6869 0.2897 0.3198 0.0414  -0.0036 -0.0024 135 ARG   A CB  
1048 C CG  . ARG   A 155 ? 0.6699 0.2727 0.3032 0.0418  -0.0092 -0.0025 135 ARG   A CG  
1049 C CD  . ARG   A 155 ? 0.7458 0.3246 0.3544 0.0466  -0.0052 -0.0017 135 ARG   A CD  
1050 N NE  . ARG   A 155 ? 0.7257 0.3058 0.3358 0.0467  -0.0102 -0.0017 135 ARG   A NE  
1051 C CZ  . ARG   A 155 ? 0.7261 0.3136 0.342  0.0465  -0.0021 -0.0005 135 ARG   A CZ  
1052 N NH1 . ARG   A 155 ? 0.7019 0.2988 0.3266 0.0456  0.0109  0.0008  135 ARG   A NH1 
1053 N NH2 . ARG   A 155 ? 0.689  0.2762 0.3047 0.0467  -0.0075 -0.0006 135 ARG   A NH2 
1054 N N   . PRO   A 156 ? 0.761  0.342  0.3749 0.0437  -0.014  -0.0048 136 PRO   A N   
1055 C CA  . PRO   A 156 ? 0.7683 0.349  0.3808 0.0433  -0.0075 -0.0047 136 PRO   A CA  
1056 C C   . PRO   A 156 ? 0.7666 0.3348 0.365  0.0454  0.0072  -0.0031 136 PRO   A C   
1057 O O   . PRO   A 156 ? 0.774  0.3201 0.3503 0.0495  0.0101  -0.0026 136 PRO   A O   
1058 C CB  . PRO   A 156 ? 0.798  0.361  0.3955 0.0462  -0.0191 -0.0063 136 PRO   A CB  
1059 C CG  . PRO   A 156 ? 0.8189 0.3667 0.404  0.0491  -0.0298 -0.0071 136 PRO   A CG  
1060 C CD  . PRO   A 156 ? 0.7862 0.3509 0.3878 0.0464  -0.0287 -0.0064 136 PRO   A CD  
1061 N N   . GLY   A 157 ? 0.7453 0.3289 0.3587 0.0422  0.0167  -0.0023 137 GLY   A N   
1062 C CA  . GLY   A 157 ? 0.7479 0.3249 0.3557 0.043   0.0318  -0.0007 137 GLY   A CA  
1063 C C   . GLY   A 157 ? 0.743  0.3287 0.361  0.0422  0.0413  0.0009  137 GLY   A C   
1064 O O   . GLY   A 157 ? 0.7716 0.3549 0.3904 0.0424  0.0545  0.0024  137 GLY   A O   
1065 N N   . HIS   A 158 ? 0.7068 0.3034 0.3346 0.0412  0.035   0.0006  138 HIS   A N   
1066 C CA  A HIS   A 158 ? 0.6979 0.302  0.3347 0.0408  0.0423  0.0018  138 HIS   A CA  
1067 C CA  B HIS   A 158 ? 0.7041 0.3072 0.3402 0.0409  0.0433  0.0019  138 HIS   A CA  
1068 C C   . HIS   A 158 ? 0.6826 0.3137 0.3481 0.036   0.0464  0.0022  138 HIS   A C   
1069 O O   . HIS   A 158 ? 0.709  0.3453 0.3834 0.0358  0.056   0.0035  138 HIS   A O   
1070 C CB  A HIS   A 158 ? 0.7043 0.3068 0.3375 0.0419  0.0327  0.0012  138 HIS   A CB  
1071 C CB  B HIS   A 158 ? 0.7282 0.3238 0.3551 0.0432  0.0363  0.0016  138 HIS   A CB  
1072 C CG  A HIS   A 158 ? 0.7299 0.3381 0.3699 0.0421  0.0389  0.0023  138 HIS   A CG  
1073 C CG  B HIS   A 158 ? 0.7935 0.3577 0.3888 0.0489  0.036   0.0017  138 HIS   A CG  
1074 N ND1 A HIS   A 158 ? 0.7751 0.3627 0.3958 0.0467  0.0463  0.0036  138 HIS   A ND1 
1075 N ND1 B HIS   A 158 ? 0.8284 0.378  0.4079 0.0508  0.0233  0.0001  138 HIS   A ND1 
1076 C CD2 A HIS   A 158 ? 0.7288 0.3592 0.3911 0.0388  0.0381  0.0024  138 HIS   A CD2 
1077 C CD2 B HIS   A 158 ? 0.8333 0.3771 0.41   0.0531  0.047   0.0033  138 HIS   A CD2 
1078 C CE1 A HIS   A 158 ? 0.7734 0.3726 0.4069 0.0458  0.0498  0.0044  138 HIS   A CE1 
1079 C CE1 B HIS   A 158 ? 0.8611 0.3811 0.4112 0.0563  0.0258  0.0006  138 HIS   A CE1 
1080 N NE2 A HIS   A 158 ? 0.7448 0.3697 0.4032 0.0411  0.0448  0.0036  138 HIS   A NE2 
1081 N NE2 B HIS   A 158 ? 0.8664 0.3813 0.4129 0.0579  0.0406  0.0026  138 HIS   A NE2 
1082 N N   . PHE   A 159 ? 0.6279 0.2757 0.3082 0.0324  0.0382  0.001   139 PHE   A N   
1083 C CA  . PHE   A 159 ? 0.5883 0.2598 0.2936 0.0282  0.0403  0.0011  139 PHE   A CA  
1084 C C   . PHE   A 159 ? 0.5789 0.2548 0.2911 0.0262  0.0466  0.0014  139 PHE   A C   
1085 O O   . PHE   A 159 ? 0.5925 0.2596 0.2946 0.0268  0.0447  0.0009  139 PHE   A O   
1086 C CB  . PHE   A 159 ? 0.5659 0.2524 0.2831 0.0255  0.0293  -0.0001 139 PHE   A CB  
1087 C CG  . PHE   A 159 ? 0.5572 0.2431 0.2728 0.0267  0.0247  -0.0001 139 PHE   A CG  
1088 C CD1 . PHE   A 159 ? 0.544  0.2408 0.2715 0.0256  0.0283  0.0005  139 PHE   A CD1 
1089 C CD2 . PHE   A 159 ? 0.56   0.2337 0.2623 0.0289  0.0161  -0.0008 139 PHE   A CD2 
1090 C CE1 . PHE   A 159 ? 0.5494 0.2445 0.2741 0.0268  0.0245  0.0005  139 PHE   A CE1 
1091 C CE2 . PHE   A 159 ? 0.5605 0.233  0.2611 0.0298  0.0118  -0.0009 139 PHE   A CE2 
1092 C CZ  . PHE   A 159 ? 0.5515 0.2347 0.2628 0.0287  0.0164  -0.0002 139 PHE   A CZ  
1093 N N   . ALA   A 160 ? 0.5637 0.252  0.293  0.0239  0.0537  0.0021  140 ALA   A N   
1094 C CA  . ALA   A 160 ? 0.5541 0.2468 0.292  0.0217  0.0597  0.0024  140 ALA   A CA  
1095 C C   . ALA   A 160 ? 0.5427 0.2493 0.2912 0.0183  0.0519  0.0012  140 ALA   A C   
1096 O O   . ALA   A 160 ? 0.5601 0.2664 0.3099 0.0169  0.0543  0.0011  140 ALA   A O   
1097 C CB  . ALA   A 160 ? 0.5608 0.2631 0.3165 0.0202  0.0683  0.0035  140 ALA   A CB  
1098 N N   . GLY   A 161 ? 0.5063 0.2246 0.263  0.0169  0.0436  0.0004  141 GLY   A N   
1099 C CA  . GLY   A 161 ? 0.4914 0.2216 0.2576 0.0141  0.0373  -0.0005 141 GLY   A CA  
1100 C C   . GLY   A 161 ? 0.4745 0.215  0.2481 0.0132  0.0299  -0.0011 141 GLY   A C   
1101 O O   . GLY   A 161 ? 0.4793 0.2204 0.2537 0.0142  0.0299  -0.0008 141 GLY   A O   
1102 N N   . MET   A 162 ? 0.4758 0.2232 0.254  0.0116  0.0243  -0.0017 142 MET   A N   
1103 C CA  A MET   A 162 ? 0.4627 0.2186 0.2475 0.0108  0.0181  -0.0021 142 MET   A CA  
1104 C CA  B MET   A 162 ? 0.467  0.2235 0.2524 0.0107  0.0183  -0.0021 142 MET   A CA  
1105 C C   . MET   A 162 ? 0.4393 0.2061 0.2348 0.0082  0.017   -0.0023 142 MET   A C   
1106 O O   . MET   A 162 ? 0.4329 0.1983 0.2268 0.0076  0.0173  -0.0025 142 MET   A O   
1107 C CB  A MET   A 162 ? 0.484  0.2329 0.2605 0.0124  0.012   -0.0024 142 MET   A CB  
1108 C CB  B MET   A 162 ? 0.5005 0.2524 0.2799 0.012   0.0116  -0.0024 142 MET   A CB  
1109 C CG  A MET   A 162 ? 0.4828 0.2376 0.2651 0.012   0.0062  -0.0026 142 MET   A CG  
1110 C CG  B MET   A 162 ? 0.5569 0.2959 0.3236 0.0148  0.0102  -0.0024 142 MET   A CG  
1111 S SD  A MET   A 162 ? 0.4816 0.2264 0.2561 0.0141  -0.0016 -0.003  142 MET   A SD  
1112 S SD  B MET   A 162 ? 0.6279 0.3674 0.3964 0.0152  0.0004  -0.0029 142 MET   A SD  
1113 C CE  A MET   A 162 ? 0.4826 0.2261 0.2564 0.0139  -0.0019 -0.0034 142 MET   A CE  
1114 C CE  B MET   A 162 ? 0.5278 0.2669 0.2972 0.0149  -0.0026 -0.0034 142 MET   A CE  
1115 N N   . VAL   A 163 ? 0.413  0.1885 0.2171 0.007   0.0153  -0.0024 143 VAL   A N   
1116 C CA  . VAL   A 163 ? 0.4057 0.1887 0.2171 0.0051  0.0136  -0.0027 143 VAL   A CA  
1117 C C   . VAL   A 163 ? 0.3978 0.1832 0.2099 0.0054  0.0093  -0.0026 143 VAL   A C   
1118 O O   . VAL   A 163 ? 0.4054 0.1917 0.2182 0.006   0.0079  -0.0025 143 VAL   A O   
1119 C CB  . VAL   A 163 ? 0.4176 0.2066 0.2376 0.0038  0.0149  -0.0029 143 VAL   A CB  
1120 C CG1 . VAL   A 163 ? 0.4257 0.2195 0.2499 0.0024  0.0118  -0.0033 143 VAL   A CG1 
1121 C CG2 . VAL   A 163 ? 0.45   0.2372 0.2728 0.0032  0.0198  -0.0028 143 VAL   A CG2 
1122 N N   . LEU   A 164 ? 0.3968 0.1826 0.209  0.0051  0.0076  -0.0026 144 LEU   A N   
1123 C CA  . LEU   A 164 ? 0.3849 0.1727 0.1998 0.0053  0.0047  -0.0022 144 LEU   A CA  
1124 C C   . LEU   A 164 ? 0.3925 0.1841 0.211  0.0043  0.0053  -0.002  144 LEU   A C   
1125 O O   . LEU   A 164 ? 0.3951 0.1861 0.2128 0.0039  0.0064  -0.0021 144 LEU   A O   
1126 C CB  . LEU   A 164 ? 0.3996 0.1831 0.2124 0.0064  0.0023  -0.0021 144 LEU   A CB  
1127 C CG  . LEU   A 164 ? 0.4263 0.2023 0.2321 0.008   0.0006  -0.0024 144 LEU   A CG  
1128 C CD1 . LEU   A 164 ? 0.4668 0.2371 0.2696 0.0093  -0.0028 -0.0027 144 LEU   A CD1 
1129 C CD2 . LEU   A 164 ? 0.4316 0.207  0.2376 0.0086  -0.0016 -0.0023 144 LEU   A CD2 
1130 N N   . ILE   A 165 ? 0.3917 0.1858 0.213  0.0042  0.0047  -0.0017 145 ILE   A N   
1131 C CA  . ILE   A 165 ? 0.3901 0.1847 0.2119 0.0039  0.0057  -0.0014 145 ILE   A CA  
1132 C C   . ILE   A 165 ? 0.387  0.1815 0.212  0.0045  0.0059  -0.0005 145 ILE   A C   
1133 O O   . ILE   A 165 ? 0.3891 0.1843 0.2164 0.0047  0.005   -0.0002 145 ILE   A O   
1134 C CB  . ILE   A 165 ? 0.4026 0.198  0.2239 0.0036  0.0051  -0.0018 145 ILE   A CB  
1135 C CG1 . ILE   A 165 ? 0.4308 0.2274 0.2529 0.003   0.0048  -0.0027 145 ILE   A CG1 
1136 C CG2 . ILE   A 165 ? 0.421  0.2135 0.2393 0.0037  0.0058  -0.0016 145 ILE   A CG2 
1137 C CD1 . ILE   A 165 ? 0.4492 0.2469 0.2728 0.0029  0.0031  -0.0033 145 ILE   A CD1 
1138 N N   . SER   A 166 ? 0.3899 0.1833 0.216  0.0048  0.0074  0.0001  146 SER   A N   
1139 C CA  A SER   A 166 ? 0.3897 0.1832 0.222  0.0055  0.0084  0.0012  146 SER   A CA  
1140 C CA  B SER   A 166 ? 0.4014 0.1949 0.2336 0.0055  0.0085  0.0012  146 SER   A CA  
1141 C C   . SER   A 166 ? 0.4026 0.1975 0.2405 0.0056  0.0053  0.0013  146 SER   A C   
1142 O O   . SER   A 166 ? 0.4016 0.1973 0.244  0.0056  0.0058  0.002   146 SER   A O   
1143 C CB  A SER   A 166 ? 0.3854 0.1769 0.2171 0.0058  0.0122  0.0022  146 SER   A CB  
1144 C CB  B SER   A 166 ? 0.4304 0.222  0.2616 0.0057  0.012   0.0022  146 SER   A CB  
1145 O OG  A SER   A 166 ? 0.3679 0.1586 0.1948 0.0055  0.0116  0.0017  146 SER   A OG  
1146 O OG  B SER   A 166 ? 0.46   0.2483 0.2833 0.0057  0.0132  0.0017  146 SER   A OG  
1147 N N   . PRO   A 167 ? 0.3956 0.1893 0.2321 0.006   0.0019  0.0006  147 PRO   A N   
1148 C CA  . PRO   A 167 ? 0.4109 0.2035 0.2504 0.0064  -0.0023 0.0004  147 PRO   A CA  
1149 C C   . PRO   A 167 ? 0.4145 0.2082 0.2651 0.0067  -0.0037 0.0013  147 PRO   A C   
1150 O O   . PRO   A 167 ? 0.423  0.2174 0.2784 0.007   -0.0019 0.0018  147 PRO   A O   
1151 C CB  . PRO   A 167 ? 0.4024 0.1903 0.2348 0.0072  -0.0052 -0.0006 147 PRO   A CB  
1152 C CG  . PRO   A 167 ? 0.4021 0.1899 0.2332 0.0073  -0.003  -0.0006 147 PRO   A CG  
1153 C CD  . PRO   A 167 ? 0.3969 0.1883 0.2278 0.0062  0.0016  -0.0002 147 PRO   A CD  
1154 N N   . LEU   A 168 ? 0.4257 0.2193 0.2814 0.0065  -0.0067 0.0015  148 LEU   A N   
1155 C CA  . LEU   A 168 ? 0.4348 0.2297 0.3042 0.0066  -0.0087 0.0023  148 LEU   A CA  
1156 C C   . LEU   A 168 ? 0.4481 0.2392 0.3185 0.0078  -0.0154 0.0014  148 LEU   A C   
1157 O O   . LEU   A 168 ? 0.4635 0.2494 0.3285 0.0084  -0.0216 0.0004  148 LEU   A O   
1158 C CB  . LEU   A 168 ? 0.4542 0.2495 0.3285 0.0059  -0.0105 0.0027  148 LEU   A CB  
1159 C CG  . LEU   A 168 ? 0.4913 0.2877 0.3822 0.0057  -0.0138 0.0035  148 LEU   A CG  
1160 C CD1 . LEU   A 168 ? 0.4995 0.2996 0.4023 0.0056  -0.0072 0.0051  148 LEU   A CD1 
1161 C CD2 . LEU   A 168 ? 0.5172 0.3134 0.4118 0.0048  -0.0156 0.0037  148 LEU   A CD2 
1162 N N   . VAL   A 169 ? 0.4666 0.2586 0.3421 0.0084  -0.0142 0.0018  149 VAL   A N   
1163 C CA  . VAL   A 169 ? 0.4886 0.2763 0.3654 0.0098  -0.0207 0.0009  149 VAL   A CA  
1164 C C   . VAL   A 169 ? 0.5255 0.3166 0.4216 0.01    -0.022  0.0019  149 VAL   A C   
1165 O O   . VAL   A 169 ? 0.5342 0.3225 0.4382 0.0108  -0.03   0.0013  149 VAL   A O   
1166 C CB  . VAL   A 169 ? 0.5092 0.2941 0.3746 0.0106  -0.0187 0.0002  149 VAL   A CB  
1167 C CG1 . VAL   A 169 ? 0.5266 0.3061 0.3934 0.0124  -0.0256 -0.0006 149 VAL   A CG1 
1168 C CG2 . VAL   A 169 ? 0.5256 0.3069 0.3749 0.0103  -0.0175 -0.0007 149 VAL   A CG2 
1169 N N   . LEU   A 170 ? 0.5465 0.3427 0.4503 0.0096  -0.0141 0.0034  150 LEU   A N   
1170 C CA  . LEU   A 170 ? 0.5691 0.3691 0.4931 0.0099  -0.0125 0.0049  150 LEU   A CA  
1171 C C   . LEU   A 170 ? 0.5974 0.4006 0.5249 0.0089  -0.003  0.0067  150 LEU   A C   
1172 O O   . LEU   A 170 ? 0.5918 0.3942 0.507  0.0088  0.0037  0.007   150 LEU   A O   
1173 C CB  . LEU   A 170 ? 0.5712 0.3712 0.4979 0.0114  -0.0104 0.0052  150 LEU   A CB  
1174 C CG  . LEU   A 170 ? 0.6062 0.4018 0.5306 0.0129  -0.0194 0.0036  150 LEU   A CG  
1175 C CD1 . LEU   A 170 ? 0.6155 0.4115 0.5424 0.0144  -0.016  0.0041  150 LEU   A CD1 
1176 C CD2 . LEU   A 170 ? 0.6145 0.4094 0.5551 0.0134  -0.0288 0.0032  150 LEU   A CD2 
1177 N N   . ALA   A 171 ? 0.6193 0.425  0.5627 0.0081  -0.0026 0.0079  151 ALA   A N   
1178 C CA  . ALA   A 171 ? 0.6552 0.462  0.6016 0.0074  0.0072  0.0098  151 ALA   A CA  
1179 C C   . ALA   A 171 ? 0.6972 0.5043 0.6515 0.0087  0.0164  0.0118  151 ALA   A C   
1180 O O   . ALA   A 171 ? 0.6892 0.4975 0.6517 0.0099  0.0142  0.0117  151 ALA   A O   
1181 C CB  . ALA   A 171 ? 0.6501 0.4588 0.6124 0.0062  0.0054  0.0106  151 ALA   A CB  
1182 N N   . ASN   A 172 ? 0.7377 0.5424 0.6886 0.0089  0.0269  0.0136  152 ASN   A N   
1183 C CA  . ASN   A 172 ? 0.785  0.5878 0.7422 0.0105  0.0372  0.0158  152 ASN   A CA  
1184 C C   . ASN   A 172 ? 0.8137 0.6212 0.7991 0.0107  0.037   0.0173  152 ASN   A C   
1185 O O   . ASN   A 172 ? 0.8079 0.618  0.8077 0.0094  0.0351  0.0178  152 ASN   A O   
1186 C CB  . ASN   A 172 ? 0.8239 0.6208 0.7726 0.0107  0.0477  0.0176  152 ASN   A CB  
1187 C CG  . ASN   A 172 ? 0.9008 0.6928 0.8538 0.0128  0.06    0.0202  152 ASN   A CG  
1188 O OD1 . ASN   A 172 ? 0.9175 0.7122 0.8928 0.0133  0.0644  0.0222  152 ASN   A OD1 
1189 N ND2 . ASN   A 172 ? 0.9272 0.711  0.8592 0.0142  0.0656  0.0204  152 ASN   A ND2 
1190 N N   . PRO   A 173 ? 0.838  0.6466 0.8318 0.0124  0.0379  0.0177  153 PRO   A N   
1191 C CA  . PRO   A 173 ? 0.8498 0.6635 0.8729 0.0128  0.0362  0.0189  153 PRO   A CA  
1192 C C   . PRO   A 173 ? 0.8764 0.691  0.9197 0.0123  0.0457  0.0217  153 PRO   A C   
1193 O O   . PRO   A 173 ? 0.8762 0.6956 0.9425 0.0111  0.0402  0.0219  153 PRO   A O   
1194 C CB  . PRO   A 173 ? 0.8532 0.6663 0.8779 0.0152  0.0388  0.0193  153 PRO   A CB  
1195 C CG  . PRO   A 173 ? 0.8645 0.6736 0.8609 0.0154  0.0356  0.0172  153 PRO   A CG  
1196 C CD  . PRO   A 173 ? 0.8454 0.6507 0.8234 0.014   0.0395  0.0171  153 PRO   A CD  
1197 N N   . GLU   A 174 ? 0.8962 0.7048 0.9303 0.0134  0.0596  0.024   154 GLU   A N   
1198 C CA  . GLU   A 174 ? 0.9119 0.7191 0.9628 0.0133  0.0709  0.027   154 GLU   A CA  
1199 C C   . GLU   A 174 ? 0.9203 0.7288 0.9727 0.0106  0.0667  0.0264  154 GLU   A C   
1200 O O   . GLU   A 174 ? 0.917  0.7289 0.9942 0.0095  0.0686  0.028   154 GLU   A O   
1201 C CB  . GLU   A 174 ? 0.9607 0.7577 0.9967 0.0157  0.0872  0.0295  154 GLU   A CB  
1202 C CG  . GLU   A 174 ? 1.0482 0.8366 1.0684 0.0153  0.0956  0.0306  154 GLU   A CG  
1203 C CD  . GLU   A 174 ? 1.1685 0.9468 1.1538 0.0166  0.0974  0.0295  154 GLU   A CD  
1204 O OE1 . GLU   A 174 ? 1.1946 0.9681 1.1695 0.0189  0.1013  0.0298  154 GLU   A OE1 
1205 O OE2 . GLU   A 174 ? 1.2086 0.9837 1.1775 0.0153  0.0942  0.0282  154 GLU   A OE2 
1206 N N   . SER   A 175 ? 0.9266 0.7324 0.954  0.0096  0.0607  0.0242  155 SER   A N   
1207 C CA  . SER   A 175 ? 0.9344 0.7406 0.9603 0.0074  0.0566  0.0235  155 SER   A CA  
1208 C C   . SER   A 175 ? 0.9312 0.7445 0.974  0.0056  0.0427  0.0218  155 SER   A C   
1209 O O   . SER   A 175 ? 0.9315 0.7462 0.9865 0.0038  0.041   0.0222  155 SER   A O   
1210 C CB  . SER   A 175 ? 0.9652 0.7666 0.9605 0.0073  0.0543  0.0216  155 SER   A CB  
1211 O OG  . SER   A 175 ? 1.0051 0.7979 0.9834 0.0091  0.0657  0.023   155 SER   A OG  
1212 N N   . ALA   A 176 ? 0.9253 0.7414 0.9669 0.0062  0.0323  0.0197  156 ALA   A N   
1213 C CA  . ALA   A 176 ? 0.9225 0.7421 0.9758 0.0051  0.0177  0.0178  156 ALA   A CA  
1214 C C   . ALA   A 176 ? 0.9069 0.7312 0.9949 0.0046  0.0168  0.0194  156 ALA   A C   
1215 O O   . ALA   A 176 ? 0.9034 0.7289 1.0037 0.0028  0.0088  0.0188  156 ALA   A O   
1216 C CB  . ALA   A 176 ? 0.9286 0.7475 0.9702 0.0065  0.0083  0.0154  156 ALA   A CB  
1217 N N   . THR   A 177 ? 0.8929 0.7192 0.9973 0.0062  0.0251  0.0214  157 THR   A N   
1218 C CA  . THR   A 177 ? 0.8797 0.7112 1.0207 0.0059  0.0251  0.0232  157 THR   A CA  
1219 C C   . THR   A 177 ? 0.8701 0.7018 1.0258 0.0038  0.0327  0.0254  157 THR   A C   
1220 O O   . THR   A 177 ? 0.8651 0.7007 1.0466 0.0021  0.0255  0.0254  157 THR   A O   
1221 C CB  . THR   A 177 ? 0.8919 0.725  1.0459 0.0084  0.0341  0.0251  157 THR   A CB  
1222 O OG1 . THR   A 177 ? 0.9086 0.7407 1.0474 0.0101  0.0258  0.0228  157 THR   A OG1 
1223 C CG2 . THR   A 177 ? 0.8836 0.7227 1.0789 0.0082  0.034   0.027   157 THR   A CG2 
1224 N N   . THR   A 178 ? 0.8659 0.6924 1.004  0.0039  0.0464  0.027   158 THR   A N   
1225 C CA  . THR   A 178 ? 0.8608 0.6855 1.0083 0.0022  0.0553  0.0292  158 THR   A CA  
1226 C C   . THR   A 178 ? 0.8544 0.6798 0.9982 -0.0004 0.0429  0.0271  158 THR   A C   
1227 O O   . THR   A 178 ? 0.8433 0.6711 1.0107 -0.0025 0.0416  0.0281  158 THR   A O   
1228 C CB  . THR   A 178 ? 0.8879 0.7039 1.0111 0.0037  0.0712  0.031   158 THR   A CB  
1229 O OG1 . THR   A 178 ? 0.9037 0.7176 1.0343 0.0062  0.0838  0.0336  158 THR   A OG1 
1230 C CG2 . THR   A 178 ? 0.89   0.7017 1.0153 0.0021  0.0795  0.0329  158 THR   A CG2 
1231 N N   . PHE   A 179 ? 0.8583 0.6812 0.9732 -0.0003 0.0341  0.0242  159 PHE   A N   
1232 C CA  . PHE   A 179 ? 0.8589 0.681  0.9666 -0.0023 0.0229  0.0222  159 PHE   A CA  
1233 C C   . PHE   A 179 ? 0.8641 0.6898 0.9938 -0.0033 0.0074  0.0207  159 PHE   A C   
1234 O O   . PHE   A 179 ? 0.861  0.6866 1.0012 -0.0054 0.0019  0.0206  159 PHE   A O   
1235 C CB  . PHE   A 179 ? 0.8562 0.6742 0.9289 -0.0015 0.0182  0.0197  159 PHE   A CB  
1236 C CG  . PHE   A 179 ? 0.8505 0.6667 0.9162 -0.0033 0.0083  0.018   159 PHE   A CG  
1237 C CD1 . PHE   A 179 ? 0.8566 0.6702 0.919  -0.0047 0.0143  0.0191  159 PHE   A CD1 
1238 C CD2 . PHE   A 179 ? 0.851  0.6668 0.9142 -0.0033 -0.007  0.0154  159 PHE   A CD2 
1239 C CE1 . PHE   A 179 ? 0.8606 0.6723 0.9175 -0.0061 0.0053  0.0176  159 PHE   A CE1 
1240 C CE2 . PHE   A 179 ? 0.858  0.6707 0.9151 -0.0046 -0.0158 0.014   159 PHE   A CE2 
1241 C CZ  . PHE   A 179 ? 0.8569 0.6681 0.9115 -0.0061 -0.0096 0.0151  159 PHE   A CZ  
1242 N N   . LYS   A 180 ? 0.8701 0.6981 1.0067 -0.0017 0.0001  0.0196  160 LYS   A N   
1243 C CA  . LYS   A 180 ? 0.8806 0.71   1.0364 -0.0022 -0.0162 0.0179  160 LYS   A CA  
1244 C C   . LYS   A 180 ? 0.8787 0.7126 1.0731 -0.0041 -0.0158 0.0199  160 LYS   A C   
1245 O O   . LYS   A 180 ? 0.8774 0.7107 1.0859 -0.0053 -0.0303 0.0184  160 LYS   A O   
1246 C CB  . LYS   A 180 ? 0.9073 0.7371 1.0624 0.0003  -0.0228 0.0165  160 LYS   A CB  
1247 C CG  . LYS   A 180 ? 0.9671 0.791  1.0879 0.0016  -0.0307 0.0136  160 LYS   A CG  
1248 C CD  . LYS   A 180 ? 1.0229 0.8462 1.14   0.0042  -0.0344 0.0125  160 LYS   A CD  
1249 C CE  . LYS   A 180 ? 1.0826 0.8993 1.1659 0.0054  -0.0404 0.0099  160 LYS   A CE  
1250 N NZ  . LYS   A 180 ? 1.113  0.9286 1.1905 0.0078  -0.042  0.0091  160 LYS   A NZ  
1251 N N   . VAL   A 181 ? 0.8748 0.7118 1.0852 -0.0043 0.001   0.0233  161 VAL   A N   
1252 C CA  . VAL   A 181 ? 0.8663 0.7074 1.1141 -0.0062 0.0047  0.0258  161 VAL   A CA  
1253 C C   . VAL   A 181 ? 0.8655 0.7037 1.1081 -0.009  0.0045  0.0258  161 VAL   A C   
1254 O O   . VAL   A 181 ? 0.8642 0.7037 1.1291 -0.0112 -0.0056 0.0254  161 VAL   A O   
1255 C CB  . VAL   A 181 ? 0.8776 0.7211 1.1418 -0.0051 0.025   0.0297  161 VAL   A CB  
1256 C CG1 . VAL   A 181 ? 0.874  0.7206 1.1749 -0.0073 0.0323  0.0327  161 VAL   A CG1 
1257 C CG2 . VAL   A 181 ? 0.8785 0.7254 1.1528 -0.0023 0.0241  0.0297  161 VAL   A CG2 
1258 N N   . LEU   A 182 ? 0.8649 0.698  1.0774 -0.0088 0.0146  0.0262  162 LEU   A N   
1259 C CA  . LEU   A 182 ? 0.8642 0.6934 1.0667 -0.011  0.0155  0.0263  162 LEU   A CA  
1260 C C   . LEU   A 182 ? 0.8535 0.6806 1.0465 -0.0121 -0.0039 0.0229  162 LEU   A C   
1261 O O   . LEU   A 182 ? 0.852  0.6776 1.0532 -0.0145 -0.0083 0.0229  162 LEU   A O   
1262 C CB  . LEU   A 182 ? 0.8827 0.7062 1.0513 -0.0096 0.0279  0.0267  162 LEU   A CB  
1263 C CG  . LEU   A 182 ? 0.909  0.7276 1.068  -0.0113 0.0338  0.0276  162 LEU   A CG  
1264 C CD1 . LEU   A 182 ? 0.9072 0.7264 1.0955 -0.0129 0.0459  0.0311  162 LEU   A CD1 
1265 C CD2 . LEU   A 182 ? 0.9345 0.7466 1.0582 -0.0094 0.0433  0.0275  162 LEU   A CD2 
1266 N N   . ALA   A 183 ? 0.842  0.6678 1.017  -0.0102 -0.015  0.0201  163 ALA   A N   
1267 C CA  . ALA   A 183 ? 0.8425 0.6636 1.0046 -0.0103 -0.033  0.0169  163 ALA   A CA  
1268 C C   . ALA   A 183 ? 0.8263 0.6484 1.0196 -0.0117 -0.0469 0.0164  163 ALA   A C   
1269 O O   . ALA   A 183 ? 0.8258 0.6428 1.0154 -0.0129 -0.0591 0.0147  163 ALA   A O   
1270 C CB  . ALA   A 183 ? 0.8526 0.6709 0.9902 -0.0076 -0.039  0.0146  163 ALA   A CB  
1271 N N   . ALA   A 184 ? 0.8094 0.6374 1.0337 -0.0115 -0.0452 0.0178  164 ALA   A N   
1272 C CA  . ALA   A 184 ? 0.7985 0.628  1.057  -0.0128 -0.0587 0.0173  164 ALA   A CA  
1273 C C   . ALA   A 184 ? 0.7836 0.6143 1.0636 -0.0163 -0.0559 0.0191  164 ALA   A C   
1274 O O   . ALA   A 184 ? 0.787  0.6146 1.0805 -0.0179 -0.0714 0.0176  164 ALA   A O   
1275 C CB  . ALA   A 184 ? 0.7905 0.627  1.0788 -0.0116 -0.0552 0.0188  164 ALA   A CB  
1276 N N   . LYS   A 185 ? 0.764  0.5972 1.0439 -0.0173 -0.0367 0.0221  165 LYS   A N   
1277 C CA  . LYS   A 185 ? 0.7467 0.5799 1.0431 -0.0205 -0.0314 0.024   165 LYS   A CA  
1278 C C   . LYS   A 185 ? 0.7295 0.5551 1.0009 -0.0217 -0.0433 0.0215  165 LYS   A C   
1279 O O   . LYS   A 185 ? 0.7224 0.5462 1.0118 -0.0242 -0.0538 0.021   165 LYS   A O   
1280 C CB  . LYS   A 185 ? 0.7825 0.6166 1.0738 -0.0204 -0.0075 0.0275  165 LYS   A CB  
1281 C CG  . LYS   A 185 ? 0.8451 0.6805 1.1655 -0.0234 0.0033  0.0307  165 LYS   A CG  
1282 C CD  . LYS   A 185 ? 0.921  0.7535 1.2289 -0.0224 0.0272  0.034   165 LYS   A CD  
1283 C CE  . LYS   A 185 ? 0.9773 0.8121 1.2858 -0.0193 0.0392  0.0356  165 LYS   A CE  
1284 N NZ  . LYS   A 185 ? 1.0182 0.8466 1.3087 -0.0178 0.0612  0.0384  165 LYS   A NZ  
1285 N N   . VAL   A 186 ? 0.7182 0.5388 0.9492 -0.0198 -0.0423 0.0198  166 VAL   A N   
1286 C CA  . VAL   A 186 ? 0.7144 0.5274 0.9201 -0.0203 -0.0521 0.0176  166 VAL   A CA  
1287 C C   . VAL   A 186 ? 0.6944 0.5017 0.8999 -0.0197 -0.0743 0.0145  166 VAL   A C   
1288 O O   . VAL   A 186 ? 0.697  0.4982 0.9008 -0.0212 -0.0849 0.0133  166 VAL   A O   
1289 C CB  . VAL   A 186 ? 0.7394 0.549  0.9048 -0.0183 -0.0436 0.017   166 VAL   A CB  
1290 C CG1 . VAL   A 186 ? 0.7593 0.5607 0.8953 -0.0173 -0.0568 0.014   166 VAL   A CG1 
1291 C CG2 . VAL   A 186 ? 0.7489 0.5589 0.9114 -0.0195 -0.0265 0.0196  166 VAL   A CG2 
1292 N N   . LEU   A 187 ? 0.6725 0.4804 0.8789 -0.0173 -0.0816 0.0131  167 LEU   A N   
1293 C CA  . LEU   A 187 ? 0.6695 0.4693 0.8735 -0.0162 -0.103  0.01    167 LEU   A CA  
1294 C C   . LEU   A 187 ? 0.6537 0.4536 0.895  -0.0185 -0.1154 0.0101  167 LEU   A C   
1295 O O   . LEU   A 187 ? 0.6746 0.4645 0.9103 -0.0184 -0.1333 0.0077  167 LEU   A O   
1296 C CB  . LEU   A 187 ? 0.6758 0.475  0.8707 -0.0128 -0.1072 0.0086  167 LEU   A CB  
1297 C CG  . LEU   A 187 ? 0.7156 0.5116 0.8708 -0.0104 -0.1001 0.0077  167 LEU   A CG  
1298 C CD1 . LEU   A 187 ? 0.7235 0.5204 0.8747 -0.0076 -0.1014 0.0068  167 LEU   A CD1 
1299 C CD2 . LEU   A 187 ? 0.7406 0.5248 0.8642 -0.0096 -0.1096 0.0054  167 LEU   A CD2 
1300 N N   . ASN   A 188 ? 0.6109 0.4211 0.8901 -0.0206 -0.1059 0.0129  168 ASN   A N   
1301 C CA  . ASN   A 188 ? 0.5771 0.3889 0.897  -0.0231 -0.1168 0.0132  168 ASN   A CA  
1302 C C   . ASN   A 188 ? 0.5627 0.3741 0.8944 -0.0269 -0.1134 0.0147  168 ASN   A C   
1303 O O   . ASN   A 188 ? 0.5604 0.3701 0.9203 -0.0291 -0.1266 0.0143  168 ASN   A O   
1304 C CB  . ASN   A 188 ? 0.5661 0.3892 0.9256 -0.0233 -0.108  0.0158  168 ASN   A CB  
1305 C CG  . ASN   A 188 ? 0.5891 0.4118 0.9535 -0.0203 -0.1199 0.0138  168 ASN   A CG  
1306 O OD1 . ASN   A 188 ? 0.5976 0.4177 0.9863 -0.0205 -0.1382 0.0122  168 ASN   A OD1 
1307 N ND2 . ASN   A 188 ? 0.5964 0.421  0.9387 -0.0174 -0.1101 0.0139  168 ASN   A ND2 
1308 N N   . SER   A 189 ? 0.5544 0.3668 0.8664 -0.0275 -0.0964 0.0165  169 SER   A N   
1309 C CA  A SER   A 189 ? 0.5488 0.3604 0.8719 -0.0311 -0.0918 0.0181  169 SER   A CA  
1310 C CA  B SER   A 189 ? 0.5508 0.3625 0.8729 -0.031  -0.0912 0.0182  169 SER   A CA  
1311 C C   . SER   A 189 ? 0.5718 0.3752 0.8528 -0.0306 -0.0902 0.0169  169 SER   A C   
1312 O O   . SER   A 189 ? 0.6031 0.4016 0.8489 -0.0276 -0.0935 0.0148  169 SER   A O   
1313 C CB  A SER   A 189 ? 0.5348 0.356  0.889  -0.033  -0.0712 0.0223  169 SER   A CB  
1314 C CB  B SER   A 189 ? 0.544  0.3647 0.893  -0.0328 -0.0693 0.0224  169 SER   A CB  
1315 O OG  A SER   A 189 ? 0.4848 0.3119 0.8867 -0.0348 -0.0769 0.0234  169 SER   A OG  
1316 O OG  B SER   A 189 ? 0.5382 0.3639 0.8786 -0.0302 -0.0536 0.0239  169 SER   A OG  
1317 N N   . VAL   A 190 ? 0.5597 0.3608 0.8453 -0.0336 -0.0864 0.0181  170 VAL   A N   
1318 C CA  . VAL   A 190 ? 0.5733 0.3667 0.8212 -0.033  -0.085  0.0171  170 VAL   A CA  
1319 C C   . VAL   A 190 ? 0.5794 0.3772 0.8203 -0.0331 -0.0621 0.02    170 VAL   A C   
1320 O O   . VAL   A 190 ? 0.5684 0.3682 0.8302 -0.0359 -0.0523 0.0225  170 VAL   A O   
1321 C CB  . VAL   A 190 ? 0.5794 0.365  0.8309 -0.0356 -0.0976 0.0161  170 VAL   A CB  
1322 C CG1 . VAL   A 190 ? 0.5913 0.3689 0.8028 -0.0345 -0.0953 0.0151  170 VAL   A CG1 
1323 C CG2 . VAL   A 190 ? 0.5901 0.3692 0.8507 -0.0352 -0.1214 0.0133  170 VAL   A CG2 
1324 N N   . LEU   A 191 ? 0.5946 0.3934 0.8081 -0.0301 -0.0531 0.0197  171 LEU   A N   
1325 C CA  . LEU   A 191 ? 0.6126 0.4133 0.8158 -0.0296 -0.0322 0.0222  171 LEU   A CA  
1326 C C   . LEU   A 191 ? 0.6663 0.462  0.8262 -0.0269 -0.031  0.0204  171 LEU   A C   
1327 O O   . LEU   A 191 ? 0.6661 0.4638 0.8107 -0.0242 -0.0266 0.0199  171 LEU   A O   
1328 C CB  . LEU   A 191 ? 0.5895 0.3973 0.811  -0.0285 -0.0203 0.0243  171 LEU   A CB  
1329 C CG  . LEU   A 191 ? 0.5815 0.395  0.8493 -0.0311 -0.0173 0.0269  171 LEU   A CG  
1330 C CD1 . LEU   A 191 ? 0.5808 0.4009 0.8655 -0.0293 -0.0083 0.0285  171 LEU   A CD1 
1331 C CD2 . LEU   A 191 ? 0.5827 0.394  0.8612 -0.0337 -0.0029 0.0299  171 LEU   A CD2 
1332 N N   . PRO   A 192 ? 0.7051 0.4942 0.8463 -0.0275 -0.0353 0.0193  172 PRO   A N   
1333 C CA  . PRO   A 192 ? 0.7451 0.5296 0.8476 -0.0248 -0.0359 0.0175  172 PRO   A CA  
1334 C C   . PRO   A 192 ? 0.7856 0.5708 0.8684 -0.0229 -0.0197 0.0186  172 PRO   A C   
1335 O O   . PRO   A 192 ? 0.8001 0.5841 0.8567 -0.0203 -0.0209 0.017   172 PRO   A O   
1336 C CB  . PRO   A 192 ? 0.7495 0.5267 0.8421 -0.0261 -0.0431 0.0166  172 PRO   A CB  
1337 C CG  . PRO   A 192 ? 0.7411 0.5195 0.8642 -0.0297 -0.0397 0.0187  172 PRO   A CG  
1338 C CD  . PRO   A 192 ? 0.6972 0.4825 0.8527 -0.0306 -0.0417 0.0196  172 PRO   A CD  
1339 N N   . ASN   A 193 ? 0.7991 0.5847 0.8927 -0.0241 -0.0048 0.0214  173 ASN   A N   
1340 C CA  . ASN   A 193 ? 0.831  0.614  0.9026 -0.022  0.0094  0.0224  173 ASN   A CA  
1341 C C   . ASN   A 193 ? 0.8337 0.6204 0.9083 -0.0201 0.0189  0.0235  173 ASN   A C   
1342 O O   . ASN   A 193 ? 0.8498 0.6329 0.9039 -0.018  0.0291  0.024   173 ASN   A O   
1343 C CB  . ASN   A 193 ? 0.8632 0.6407 0.9366 -0.0234 0.0209  0.0246  173 ASN   A CB  
1344 C CG  . ASN   A 193 ? 0.9386 0.7112 1.0034 -0.0248 0.0125  0.0233  173 ASN   A CG  
1345 O OD1 . ASN   A 193 ? 0.9704 0.7414 1.0145 -0.0235 0.0016  0.0207  173 ASN   A OD1 
1346 N ND2 . ASN   A 193 ? 0.9394 0.709  1.02   -0.0274 0.0179  0.0253  173 ASN   A ND2 
1347 N N   . LEU   A 194 ? 0.8152 0.6081 0.914  -0.0206 0.0149  0.0238  174 LEU   A N   
1348 C CA  . LEU   A 194 ? 0.8131 0.6093 0.917  -0.0189 0.0242  0.0252  174 LEU   A CA  
1349 C C   . LEU   A 194 ? 0.8239 0.6187 0.897  -0.0158 0.0252  0.0235  174 LEU   A C   
1350 O O   . LEU   A 194 ? 0.8252 0.6203 0.8822 -0.015  0.0135  0.0208  174 LEU   A O   
1351 C CB  . LEU   A 194 ? 0.8049 0.6082 0.9392 -0.0196 0.0171  0.0253  174 LEU   A CB  
1352 C CG  . LEU   A 194 ? 0.8216 0.628  0.9815 -0.0196 0.0312  0.0285  174 LEU   A CG  
1353 C CD1 . LEU   A 194 ? 0.8252 0.6301 1.0091 -0.0223 0.0393  0.0313  174 LEU   A CD1 
1354 C CD2 . LEU   A 194 ? 0.8209 0.6344 1.0041 -0.0192 0.0234  0.0281  174 LEU   A CD2 
1355 N N   . SER   A 195 ? 0.8306 0.6222 0.8946 -0.0141 0.0396  0.0253  175 SER   A N   
1356 C CA  . SER   A 195 ? 0.8427 0.6321 0.8799 -0.0112 0.0423  0.0242  175 SER   A CA  
1357 C C   . SER   A 195 ? 0.8355 0.6248 0.8803 -0.0097 0.054   0.0263  175 SER   A C   
1358 O O   . SER   A 195 ? 0.8393 0.6262 0.9005 -0.0101 0.0659  0.0292  175 SER   A O   
1359 C CB  . SER   A 195 ? 0.8754 0.6563 0.8858 -0.0101 0.0484  0.0241  175 SER   A CB  
1360 O OG  . SER   A 195 ? 0.922  0.7016 0.924  -0.0113 0.0397  0.0224  175 SER   A OG  
1361 N N   . SER   A 196 ? 0.8277 0.6186 0.8593 -0.0076 0.0518  0.025   176 SER   A N   
1362 C CA  . SER   A 196 ? 0.8218 0.6109 0.8544 -0.0056 0.063   0.0268  176 SER   A CA  
1363 C C   . SER   A 196 ? 0.8117 0.5902 0.8143 -0.0034 0.0724  0.0271  176 SER   A C   
1364 O O   . SER   A 196 ? 0.8105 0.584  0.7978 -0.0037 0.0711  0.0263  176 SER   A O   
1365 C CB  . SER   A 196 ? 0.8438 0.6392 0.8775 -0.0046 0.055   0.0251  176 SER   A CB  
1366 O OG  . SER   A 196 ? 0.897  0.6923 0.9068 -0.004  0.0453  0.0222  176 SER   A OG  
1367 N N   . GLY   A 197 ? 0.8018 0.5755 0.7959 -0.0009 0.0815  0.0282  177 GLY   A N   
1368 C CA  . GLY   A 197 ? 0.8089 0.5707 0.774  0.0015  0.0888  0.0282  177 GLY   A CA  
1369 C C   . GLY   A 197 ? 0.8022 0.5653 0.7439 0.0022  0.0779  0.025   177 GLY   A C   
1370 O O   . GLY   A 197 ? 0.7982 0.5707 0.7449 0.0012  0.0668  0.0229  177 GLY   A O   
1371 N N   A PRO   A 198 ? 0.8088 0.5615 0.7248 0.004   0.0809  0.0244  178 PRO   A N   
1372 N N   B PRO   A 198 ? 0.8088 0.5615 0.7248 0.004   0.0809  0.0244  178 PRO   A N   
1373 C CA  A PRO   A 198 ? 0.8154 0.5696 0.7115 0.0046  0.071   0.0214  178 PRO   A CA  
1374 C CA  B PRO   A 198 ? 0.8154 0.5696 0.7115 0.0046  0.071   0.0214  178 PRO   A CA  
1375 C C   A PRO   A 198 ? 0.8219 0.5778 0.7121 0.006   0.0696  0.0206  178 PRO   A C   
1376 C C   B PRO   A 198 ? 0.8219 0.5778 0.7121 0.006   0.0696  0.0206  178 PRO   A C   
1377 O O   A PRO   A 198 ? 0.8242 0.5762 0.7184 0.0073  0.0781  0.0225  178 PRO   A O   
1378 O O   B PRO   A 198 ? 0.8242 0.5762 0.7184 0.0073  0.0781  0.0225  178 PRO   A O   
1379 C CB  A PRO   A 198 ? 0.8342 0.5753 0.707  0.0064  0.0752  0.0213  178 PRO   A CB  
1380 C CB  B PRO   A 198 ? 0.8342 0.5753 0.707  0.0064  0.0752  0.0213  178 PRO   A CB  
1381 C CG  A PRO   A 198 ? 0.8436 0.5733 0.7174 0.0078  0.0896  0.0244  178 PRO   A CG  
1382 C CG  B PRO   A 198 ? 0.8436 0.5733 0.7174 0.0078  0.0896  0.0244  178 PRO   A CG  
1383 C CD  A PRO   A 198 ? 0.8107 0.5488 0.7145 0.0057  0.0932  0.0265  178 PRO   A CD  
1384 C CD  B PRO   A 198 ? 0.8107 0.5488 0.7145 0.0057  0.0932  0.0265  178 PRO   A CD  
1385 N N   . ILE   A 199 ? 0.8207 0.5816 0.7009 0.0059  0.0594  0.0179  179 ILE   A N   
1386 C CA  . ILE   A 199 ? 0.8199 0.5821 0.6934 0.007   0.0575  0.017   179 ILE   A CA  
1387 C C   . ILE   A 199 ? 0.8219 0.5704 0.6749 0.0096  0.065   0.0176  179 ILE   A C   
1388 O O   . ILE   A 199 ? 0.8347 0.5761 0.6718 0.0104  0.0635  0.0167  179 ILE   A O   
1389 C CB  . ILE   A 199 ? 0.8244 0.5934 0.6911 0.0062  0.046   0.0141  179 ILE   A CB  
1390 C CG1 . ILE   A 199 ? 0.8213 0.6007 0.7048 0.0043  0.0384  0.0134  179 ILE   A CG1 
1391 C CG2 . ILE   A 199 ? 0.8363 0.6042 0.6917 0.0074  0.0445  0.013   179 ILE   A CG2 
1392 C CD1 . ILE   A 199 ? 0.8357 0.6189 0.7117 0.0037  0.0289  0.0111  179 ILE   A CD1 
1393 N N   . ASP   A 200 ? 0.8059 0.5486 0.6596 0.0113  0.0736  0.0195  180 ASP   A N   
1394 C CA  . ASP   A 200 ? 0.7957 0.5219 0.6281 0.0143  0.0814  0.0204  180 ASP   A CA  
1395 C C   . ASP   A 200 ? 0.7413 0.4637 0.5527 0.0152  0.0733  0.0177  180 ASP   A C   
1396 O O   . ASP   A 200 ? 0.7387 0.4678 0.5518 0.0148  0.068   0.0165  180 ASP   A O   
1397 C CB  . ASP   A 200 ? 0.8572 0.5782 0.6949 0.016   0.0919  0.0229  180 ASP   A CB  
1398 C CG  . ASP   A 200 ? 0.9918 0.6924 0.8066 0.0196  0.1015  0.0243  180 ASP   A CG  
1399 O OD1 . ASP   A 200 ? 1.0287 0.718  0.8258 0.0207  0.1017  0.0238  180 ASP   A OD1 
1400 O OD2 . ASP   A 200 ? 1.0556 0.7501 0.8689 0.0216  0.1089  0.0259  180 ASP   A OD2 
1401 N N   . SER   A 201 ? 0.683  0.3942 0.4755 0.0166  0.0724  0.0169  181 SER   A N   
1402 C CA  A SER   A 201 ? 0.6544 0.3629 0.4304 0.0173  0.0634  0.0142  181 SER   A CA  
1403 C CA  B SER   A 201 ? 0.6675 0.3752 0.4427 0.0174  0.0637  0.0143  181 SER   A CA  
1404 C C   . SER   A 201 ? 0.6402 0.3394 0.4027 0.0194  0.0645  0.0141  181 SER   A C   
1405 O O   . SER   A 201 ? 0.6059 0.3093 0.3641 0.0188  0.0558  0.0118  181 SER   A O   
1406 C CB  A SER   A 201 ? 0.6494 0.3481 0.4098 0.0184  0.0608  0.0132  181 SER   A CB  
1407 C CB  B SER   A 201 ? 0.6999 0.3956 0.4582 0.0189  0.0625  0.0136  181 SER   A CB  
1408 O OG  A SER   A 201 ? 0.6459 0.3253 0.3904 0.0214  0.07    0.015   181 SER   A OG  
1409 O OG  B SER   A 201 ? 0.7358 0.4411 0.5052 0.0168  0.0593  0.0132  181 SER   A OG  
1410 N N   . SER   A 202 ? 0.6383 0.3246 0.3944 0.0217  0.0752  0.0164  182 SER   A N   
1411 C CA  . SER   A 202 ? 0.6585 0.3343 0.3999 0.024   0.0762  0.0163  182 SER   A CA  
1412 C C   . SER   A 202 ? 0.6235 0.3137 0.3786 0.0222  0.0718  0.0156  182 SER   A C   
1413 O O   . SER   A 202 ? 0.6422 0.3272 0.3855 0.0231  0.0682  0.0145  182 SER   A O   
1414 C CB  . SER   A 202 ? 0.7301 0.3874 0.4607 0.0274  0.0898  0.0193  182 SER   A CB  
1415 O OG  . SER   A 202 ? 0.7763 0.4417 0.5286 0.0265  0.0992  0.022   182 SER   A OG  
1416 N N   . VAL   A 203 ? 0.5814 0.2881 0.3603 0.0197  0.0721  0.0163  183 VAL   A N   
1417 C CA  . VAL   A 203 ? 0.5656 0.2846 0.3562 0.0183  0.0676  0.0155  183 VAL   A CA  
1418 C C   . VAL   A 203 ? 0.5239 0.2541 0.3161 0.016   0.0557  0.0126  183 VAL   A C   
1419 O O   . VAL   A 203 ? 0.5077 0.2467 0.3072 0.0149  0.0517  0.0117  183 VAL   A O   
1420 C CB  . VAL   A 203 ? 0.5988 0.3285 0.4133 0.0172  0.0722  0.0173  183 VAL   A CB  
1421 C CG1 . VAL   A 203 ? 0.625  0.3444 0.4416 0.0193  0.0854  0.0205  183 VAL   A CG1 
1422 C CG2 . VAL   A 203 ? 0.6121 0.355  0.4428 0.0144  0.0661  0.0165  183 VAL   A CG2 
1423 N N   . LEU   A 204 ? 0.5004 0.2296 0.2856 0.0155  0.0505  0.0111  184 LEU   A N   
1424 C CA  . LEU   A 204 ? 0.477  0.2162 0.2648 0.0136  0.0405  0.0087  184 LEU   A CA  
1425 C C   . LEU   A 204 ? 0.4807 0.2161 0.2572 0.0141  0.0354  0.007   184 LEU   A C   
1426 O O   . LEU   A 204 ? 0.4654 0.2102 0.2481 0.0124  0.0297  0.0056  184 LEU   A O   
1427 C CB  . LEU   A 204 ? 0.4649 0.2044 0.2504 0.0132  0.037   0.0078  184 LEU   A CB  
1428 C CG  . LEU   A 204 ? 0.4636 0.2092 0.2629 0.0121  0.04    0.0091  184 LEU   A CG  
1429 C CD1 . LEU   A 204 ? 0.4648 0.2073 0.258  0.0122  0.0376  0.0084  184 LEU   A CD1 
1430 C CD2 . LEU   A 204 ? 0.4689 0.2287 0.2841 0.0099  0.0352  0.0085  184 LEU   A CD2 
1431 N N   . SER   A 205 ? 0.4752 0.1954 0.2343 0.0164  0.0372  0.0071  185 SER   A N   
1432 C CA  . SER   A 205 ? 0.472  0.1869 0.22   0.0168  0.031   0.0053  185 SER   A CA  
1433 C C   . SER   A 205 ? 0.5004 0.1956 0.2289 0.0199  0.0353  0.0062  185 SER   A C   
1434 O O   . SER   A 205 ? 0.531  0.2146 0.2503 0.022   0.0409  0.0075  185 SER   A O   
1435 C CB  . SER   A 205 ? 0.4825 0.1991 0.2279 0.0161  0.0225  0.0031  185 SER   A CB  
1436 O OG  . SER   A 205 ? 0.5106 0.2214 0.2468 0.0165  0.0156  0.0013  185 SER   A OG  
1437 N N   . ARG   A 206 ? 0.5141 0.204  0.2347 0.0204  0.0324  0.0054  186 ARG   A N   
1438 C CA  . ARG   A 206 ? 0.5309 0.1993 0.2292 0.0237  0.0348  0.0059  186 ARG   A CA  
1439 C C   . ARG   A 206 ? 0.5567 0.2133 0.2397 0.025   0.0263  0.0038  186 ARG   A C   
1440 O O   . ARG   A 206 ? 0.5821 0.217  0.2429 0.0283  0.0275  0.004   186 ARG   A O   
1441 C CB  . ARG   A 206 ? 0.5481 0.2143 0.2428 0.0237  0.0332  0.0055  186 ARG   A CB  
1442 C CG  . ARG   A 206 ? 0.5587 0.2321 0.265  0.0235  0.0421  0.0077  186 ARG   A CG  
1443 C CD  . ARG   A 206 ? 0.5655 0.2379 0.2689 0.0233  0.0399  0.0072  186 ARG   A CD  
1444 N NE  . ARG   A 206 ? 0.5676 0.253  0.2803 0.0202  0.0299  0.0048  186 ARG   A NE  
1445 C CZ  . ARG   A 206 ? 0.5549 0.2414 0.2667 0.0192  0.0257  0.0037  186 ARG   A CZ  
1446 N NH1 . ARG   A 206 ? 0.5758 0.2502 0.2758 0.0212  0.0296  0.0047  186 ARG   A NH1 
1447 N NH2 . ARG   A 206 ? 0.5515 0.2492 0.2727 0.0163  0.0177  0.0017  186 ARG   A NH2 
1448 N N   . ASN   A 207 ? 0.5262 0.1952 0.2197 0.0227  0.0176  0.0017  187 ASN   A N   
1449 C CA  . ASN   A 207 ? 0.5329 0.1923 0.215  0.0238  0.0086  -0.0004 187 ASN   A CA  
1450 C C   . ASN   A 207 ? 0.5462 0.1978 0.2212 0.0257  0.013   0.0006  187 ASN   A C   
1451 O O   . ASN   A 207 ? 0.5319 0.1969 0.2209 0.0239  0.0138  0.0008  187 ASN   A O   
1452 C CB  . ASN   A 207 ? 0.5203 0.1964 0.2187 0.0208  -0.0009 -0.0026 187 ASN   A CB  
1453 C CG  . ASN   A 207 ? 0.5777 0.2456 0.2683 0.0219  -0.0115 -0.005  187 ASN   A CG  
1454 O OD1 . ASN   A 207 ? 0.5914 0.2449 0.2673 0.0246  -0.0123 -0.0051 187 ASN   A OD1 
1455 N ND2 . ASN   A 207 ? 0.5592 0.2361 0.2606 0.0198  -0.0198 -0.0068 187 ASN   A ND2 
1456 N N   . LYS   A 208 ? 0.5798 0.2081 0.2316 0.0294  0.0157  0.0012  188 LYS   A N   
1457 C CA  . LYS   A 208 ? 0.5859 0.2037 0.2282 0.0315  0.021   0.0023  188 LYS   A CA  
1458 C C   . LYS   A 208 ? 0.5836 0.2058 0.2287 0.031   0.012   0.0001  188 LYS   A C   
1459 O O   . LYS   A 208 ? 0.5978 0.2215 0.2453 0.0311  0.0163  0.0011  188 LYS   A O   
1460 C CB  . LYS   A 208 ? 0.6368 0.2249 0.2499 0.0363  0.0261  0.0033  188 LYS   A CB  
1461 C CG  . LYS   A 208 ? 0.7155 0.2982 0.3262 0.0373  0.0378  0.006   188 LYS   A CG  
1462 C CD  . LYS   A 208 ? 0.839  0.3896 0.418  0.0426  0.0429  0.007   188 LYS   A CD  
1463 C CE  . LYS   A 208 ? 0.9263 0.4693 0.5019 0.0443  0.0565  0.0101  188 LYS   A CE  
1464 N NZ  . LYS   A 208 ? 1.0022 0.5111 0.5447 0.0499  0.0635  0.0115  188 LYS   A NZ  
1465 N N   . THR   A 209 ? 0.5809 0.204  0.2255 0.0306  -0.0007 -0.0027 189 THR   A N   
1466 C CA  . THR   A 209 ? 0.5779 0.2053 0.2265 0.0303  -0.0096 -0.0047 189 THR   A CA  
1467 C C   . THR   A 209 ? 0.5417 0.1945 0.2158 0.0267  -0.0072 -0.0042 189 THR   A C   
1468 O O   . THR   A 209 ? 0.546  0.2016 0.2227 0.0268  -0.0067 -0.0041 189 THR   A O   
1469 C CB  . THR   A 209 ? 0.6388 0.2652 0.2878 0.0302  -0.0234 -0.0076 189 THR   A CB  
1470 O OG1 . THR   A 209 ? 0.7373 0.3392 0.3619 0.0335  -0.0263 -0.0081 189 THR   A OG1 
1471 C CG2 . THR   A 209 ? 0.6494 0.2786 0.3026 0.0305  -0.0327 -0.0097 189 THR   A CG2 
1472 N N   . GLU   A 210 ? 0.5213 0.1906 0.2123 0.0238  -0.0051 -0.0037 190 GLU   A N   
1473 C CA  . GLU   A 210 ? 0.4968 0.1868 0.2087 0.0208  -0.003  -0.0032 190 GLU   A CA  
1474 C C   . GLU   A 210 ? 0.4856 0.1759 0.199  0.0209  0.0067  -0.0009 190 GLU   A C   
1475 O O   . GLU   A 210 ? 0.4887 0.1885 0.2118 0.0198  0.0065  -0.0009 190 GLU   A O   
1476 C CB  . GLU   A 210 ? 0.5035 0.2082 0.2305 0.0181  -0.0026 -0.0031 190 GLU   A CB  
1477 C CG  . GLU   A 210 ? 0.5407 0.247  0.2699 0.0174  -0.012  -0.0053 190 GLU   A CG  
1478 C CD  . GLU   A 210 ? 0.6345 0.3534 0.3777 0.016   -0.0182 -0.0069 190 GLU   A CD  
1479 O OE1 . GLU   A 210 ? 0.5853 0.3084 0.3321 0.0161  -0.0169 -0.0066 190 GLU   A OE1 
1480 O OE2 . GLU   A 210 ? 0.697  0.4222 0.4491 0.0145  -0.0234 -0.0081 190 GLU   A OE2 
1481 N N   . VAL   A 211 ? 0.5111 0.1909 0.2159 0.0224  0.0153  0.0011  191 VAL   A N   
1482 C CA  . VAL   A 211 ? 0.5222 0.2017 0.2306 0.0224  0.0251  0.0035  191 VAL   A CA  
1483 C C   . VAL   A 211 ? 0.5273 0.1962 0.2245 0.0243  0.0245  0.0032  191 VAL   A C   
1484 O O   . VAL   A 211 ? 0.5275 0.2037 0.2341 0.023   0.0272  0.004   191 VAL   A O   
1485 C CB  . VAL   A 211 ? 0.5561 0.2252 0.2582 0.024   0.0354  0.0059  191 VAL   A CB  
1486 C CG1 . VAL   A 211 ? 0.5703 0.2384 0.2781 0.0241  0.0457  0.0084  191 VAL   A CG1 
1487 C CG2 . VAL   A 211 ? 0.5572 0.2385 0.2726 0.0221  0.036   0.0062  191 VAL   A CG2 
1488 N N   . ASP   A 212 ? 0.5479 0.1988 0.2245 0.0272  0.0199  0.0019  192 ASP   A N   
1489 C CA  . ASP   A 212 ? 0.5637 0.2022 0.227  0.0294  0.0181  0.0014  192 ASP   A CA  
1490 C C   . ASP   A 212 ? 0.5583 0.2119 0.2349 0.0275  0.0103  -0.0004 192 ASP   A C   
1491 O O   . ASP   A 212 ? 0.5638 0.2175 0.2411 0.0276  0.0128  0.0002  192 ASP   A O   
1492 C CB  . ASP   A 212 ? 0.5975 0.2127 0.2354 0.0332  0.0123  -0.0001 192 ASP   A CB  
1493 C CG  . ASP   A 212 ? 0.6895 0.2831 0.3077 0.0363  0.0224  0.002   192 ASP   A CG  
1494 O OD1 . ASP   A 212 ? 0.7514 0.3453 0.3741 0.036   0.0349  0.0048  192 ASP   A OD1 
1495 O OD2 . ASP   A 212 ? 0.678  0.253  0.2761 0.0392  0.0178  0.001   192 ASP   A OD2 
1496 N N   . ILE   A 213 ? 0.5394 0.2066 0.2281 0.0257  0.0019  -0.0022 193 ILE   A N   
1497 C CA  . ILE   A 213 ? 0.521  0.2032 0.2239 0.024   -0.0044 -0.0036 193 ILE   A CA  
1498 C C   . ILE   A 213 ? 0.5203 0.2175 0.2394 0.0215  0.0021  -0.0019 193 ILE   A C   
1499 O O   . ILE   A 213 ? 0.5127 0.2134 0.2351 0.0213  0.0013  -0.0021 193 ILE   A O   
1500 C CB  . ILE   A 213 ? 0.5287 0.2211 0.2419 0.0227  -0.013  -0.0056 193 ILE   A CB  
1501 C CG1 . ILE   A 213 ? 0.5547 0.2324 0.254  0.0253  -0.0223 -0.0078 193 ILE   A CG1 
1502 C CG2 . ILE   A 213 ? 0.5278 0.2378 0.2589 0.0207  -0.0162 -0.0063 193 ILE   A CG2 
1503 C CD1 . ILE   A 213 ? 0.5845 0.2694 0.2935 0.0239  -0.03   -0.0095 193 ILE   A CD1 
1504 N N   . TYR   A 214 ? 0.5081 0.2127 0.2366 0.0197  0.008   -0.0004 194 TYR   A N   
1505 C CA  . TYR   A 214 ? 0.4877 0.2049 0.2315 0.0174  0.013   0.0011  194 TYR   A CA  
1506 C C   . TYR   A 214 ? 0.5088 0.2184 0.248  0.0181  0.0191  0.0026  194 TYR   A C   
1507 O O   . TYR   A 214 ? 0.5057 0.2229 0.2537 0.0169  0.0187  0.0028  194 TYR   A O   
1508 C CB  . TYR   A 214 ? 0.4767 0.1993 0.2289 0.016   0.018   0.0024  194 TYR   A CB  
1509 C CG  . TYR   A 214 ? 0.4699 0.2016 0.2366 0.0142  0.0234  0.0042  194 TYR   A CG  
1510 C CD1 . TYR   A 214 ? 0.485  0.2312 0.2663 0.012   0.0199  0.0037  194 TYR   A CD1 
1511 C CD2 . TYR   A 214 ? 0.507  0.2317 0.2733 0.0147  0.0322  0.0065  194 TYR   A CD2 
1512 C CE1 . TYR   A 214 ? 0.4888 0.2416 0.283  0.0104  0.0231  0.0051  194 TYR   A CE1 
1513 C CE2 . TYR   A 214 ? 0.5242 0.2573 0.3065 0.0129  0.0362  0.008   194 TYR   A CE2 
1514 C CZ  . TYR   A 214 ? 0.5207 0.2678 0.3167 0.0107  0.0308  0.0072  194 TYR   A CZ  
1515 O OH  . TYR   A 214 ? 0.5619 0.3158 0.3735 0.0091  0.0332  0.0086  194 TYR   A OH  
1516 N N   . ASN   A 215 ? 0.5159 0.2085 0.2399 0.0205  0.0249  0.0038  195 ASN   A N   
1517 C CA  . ASN   A 215 ? 0.5329 0.2157 0.2512 0.0215  0.0323  0.0055  195 ASN   A CA  
1518 C C   . ASN   A 215 ? 0.5531 0.2293 0.2613 0.0229  0.0274  0.0041  195 ASN   A C   
1519 O O   . ASN   A 215 ? 0.5794 0.2492 0.2847 0.0233  0.0332  0.0055  195 ASN   A O   
1520 C CB  . ASN   A 215 ? 0.5731 0.2377 0.2768 0.0239  0.0413  0.0073  195 ASN   A CB  
1521 C CG  . ASN   A 215 ? 0.6271 0.2985 0.3444 0.0225  0.0494  0.0095  195 ASN   A CG  
1522 O OD1 . ASN   A 215 ? 0.6282 0.3155 0.3661 0.0196  0.0503  0.0103  195 ASN   A OD1 
1523 N ND2 . ASN   A 215 ? 0.6592 0.3177 0.3652 0.0247  0.0552  0.0106  195 ASN   A ND2 
1524 N N   . SER   A 216 ? 0.5302 0.208  0.2344 0.0236  0.0171  0.0016  196 SER   A N   
1525 C CA  . SER   A 216 ? 0.5528 0.2238 0.2473 0.0255  0.0111  0       196 SER   A CA  
1526 C C   . SER   A 216 ? 0.5452 0.2329 0.2549 0.0236  0.0053  -0.0012 196 SER   A C   
1527 O O   . SER   A 216 ? 0.5543 0.238  0.2583 0.025   0.0013  -0.0022 196 SER   A O   
1528 C CB  . SER   A 216 ? 0.5822 0.2419 0.2624 0.0281  0.0023  -0.0023 196 SER   A CB  
1529 O OG  . SER   A 216 ? 0.6028 0.2436 0.2649 0.0306  0.0066  -0.0015 196 SER   A OG  
1530 N N   . ASP   A 217 ? 0.5184 0.2233 0.2458 0.0208  0.0047  -0.001  197 ASP   A N   
1531 C CA  . ASP   A 217 ? 0.4993 0.218  0.2391 0.0195  -0.0003 -0.002  197 ASP   A CA  
1532 C C   . ASP   A 217 ? 0.5052 0.2275 0.2507 0.0182  0.0041  -0.0006 197 ASP   A C   
1533 O O   . ASP   A 217 ? 0.4922 0.2193 0.2465 0.0163  0.0096  0.0011  197 ASP   A O   
1534 C CB  . ASP   A 217 ? 0.4856 0.2183 0.2394 0.0174  -0.0021 -0.0023 197 ASP   A CB  
1535 C CG  . ASP   A 217 ? 0.5419 0.2871 0.3073 0.0164  -0.0061 -0.0031 197 ASP   A CG  
1536 O OD1 . ASP   A 217 ? 0.5444 0.2893 0.3089 0.017   -0.0071 -0.0033 197 ASP   A OD1 
1537 O OD2 . ASP   A 217 ? 0.5531 0.3073 0.3275 0.0153  -0.0078 -0.0036 197 ASP   A OD2 
1538 N N   . PRO   A 218 ? 0.5294 0.249  0.2707 0.0193  0.0013  -0.0013 198 PRO   A N   
1539 C CA  . PRO   A 218 ? 0.5258 0.2477 0.272  0.018   0.0051  0.0001  198 PRO   A CA  
1540 C C   . PRO   A 218 ? 0.5068 0.2432 0.2687 0.0155  0.0041  0.0004  198 PRO   A C   
1541 O O   . PRO   A 218 ? 0.5264 0.2645 0.2939 0.0141  0.0069  0.0016  198 PRO   A O   
1542 C CB  . PRO   A 218 ? 0.5521 0.267  0.2885 0.0201  0.0013  -0.0011 198 PRO   A CB  
1543 C CG  . PRO   A 218 ? 0.5765 0.2869 0.305  0.0226  -0.0054 -0.0031 198 PRO   A CG  
1544 C CD  . PRO   A 218 ? 0.5435 0.258  0.2765 0.0218  -0.006  -0.0034 198 PRO   A CD  
1545 N N   . LEU   A 219 ? 0.489  0.2343 0.2574 0.0152  -0.0002 -0.0007 199 LEU   A N   
1546 C CA  . LEU   A 219 ? 0.4788 0.2351 0.2593 0.0134  -0.001  -0.0004 199 LEU   A CA  
1547 C C   . LEU   A 219 ? 0.4838 0.2439 0.2722 0.0115  0.0025  0.0008  199 LEU   A C   
1548 O O   . LEU   A 219 ? 0.4992 0.2663 0.2962 0.0101  0.0014  0.001   199 LEU   A O   
1549 C CB  . LEU   A 219 ? 0.4822 0.2452 0.2662 0.014   -0.0057 -0.0019 199 LEU   A CB  
1550 C CG  . LEU   A 219 ? 0.5051 0.2672 0.2858 0.0159  -0.0096 -0.003  199 LEU   A CG  
1551 C CD1 . LEU   A 219 ? 0.5002 0.2691 0.2871 0.0165  -0.0129 -0.0042 199 LEU   A CD1 
1552 C CD2 . LEU   A 219 ? 0.5033 0.2655 0.2845 0.0155  -0.009  -0.0023 199 LEU   A CD2 
1553 N N   . ILE   A 220 ? 0.4719 0.2265 0.2567 0.0117  0.0065  0.0015  200 ILE   A N   
1554 C CA  . ILE   A 220 ? 0.4727 0.2306 0.2656 0.0101  0.0102  0.0027  200 ILE   A CA  
1555 C C   . ILE   A 220 ? 0.5018 0.2563 0.2991 0.0092  0.0156  0.0046  200 ILE   A C   
1556 O O   . ILE   A 220 ? 0.5396 0.2845 0.3286 0.0102  0.0194  0.0053  200 ILE   A O   
1557 C CB  . ILE   A 220 ? 0.4758 0.2287 0.2622 0.0112  0.0121  0.0026  200 ILE   A CB  
1558 C CG1 . ILE   A 220 ? 0.5007 0.2586 0.2866 0.0116  0.0062  0.0008  200 ILE   A CG1 
1559 C CG2 . ILE   A 220 ? 0.4845 0.2399 0.2795 0.0099  0.0171  0.0042  200 ILE   A CG2 
1560 C CD1 . ILE   A 220 ? 0.5131 0.2672 0.2941 0.0122  0.0066  0.0004  200 ILE   A CD1 
1561 N N   . CYS   A 221 ? 0.5021 0.2634 0.3127 0.0073  0.0159  0.0055  201 CYS   A N   
1562 C CA  . CYS   A 221 ? 0.5196 0.279  0.3389 0.006   0.0208  0.0074  201 CYS   A CA  
1563 C C   . CYS   A 221 ? 0.5472 0.3047 0.3709 0.006   0.0272  0.0088  201 CYS   A C   
1564 O O   . CYS   A 221 ? 0.5541 0.3179 0.3852 0.0054  0.0256  0.0087  201 CYS   A O   
1565 C CB  . CYS   A 221 ? 0.5268 0.2935 0.3589 0.0041  0.0163  0.0074  201 CYS   A CB  
1566 S SG  . CYS   A 221 ? 0.5574 0.3225 0.4045 0.0021  0.021   0.0097  201 CYS   A SG  
1567 N N   . ARG   A 222 ? 0.567  0.3148 0.3852 0.0069  0.0348  0.0103  202 ARG   A N   
1568 C CA  . ARG   A 222 ? 0.5985 0.3424 0.4199 0.0074  0.0426  0.012   202 ARG   A CA  
1569 C C   . ARG   A 222 ? 0.6369 0.3799 0.4732 0.006   0.05    0.0146  202 ARG   A C   
1570 O O   . ARG   A 222 ? 0.6604 0.3974 0.4985 0.0068  0.059   0.0165  202 ARG   A O   
1571 C CB  . ARG   A 222 ? 0.6075 0.3381 0.4091 0.0102  0.0467  0.012   202 ARG   A CB  
1572 C CG  . ARG   A 222 ? 0.605  0.3372 0.3956 0.0113  0.0389  0.0095  202 ARG   A CG  
1573 C CD  . ARG   A 222 ? 0.6106 0.3276 0.3802 0.0142  0.0405  0.0091  202 ARG   A CD  
1574 N NE  . ARG   A 222 ? 0.6293 0.3369 0.389  0.0153  0.0416  0.0091  202 ARG   A NE  
1575 C CZ  . ARG   A 222 ? 0.6515 0.3592 0.404  0.016   0.0342  0.0072  202 ARG   A CZ  
1576 N NH1 . ARG   A 222 ? 0.5747 0.2902 0.3281 0.0159  0.0258  0.005   202 ARG   A NH1 
1577 N NH2 . ARG   A 222 ? 0.6625 0.3619 0.407  0.0169  0.0355  0.0074  202 ARG   A NH2 
1578 N N   . ALA   A 223 ? 0.6358 0.3846 0.484  0.004   0.0463  0.0146  203 ALA   A N   
1579 C CA  . ALA   A 223 ? 0.6519 0.4009 0.5176 0.0023  0.0521  0.0168  203 ALA   A CA  
1580 C C   . ALA   A 223 ? 0.6536 0.411  0.5391 0.0011  0.0521  0.0177  203 ALA   A C   
1581 O O   . ALA   A 223 ? 0.6537 0.4174 0.5385 0.0013  0.0459  0.0162  203 ALA   A O   
1582 C CB  . ALA   A 223 ? 0.6517 0.4038 0.5231 0.0004  0.0461  0.0163  203 ALA   A CB  
1583 N N   . GLY   A 224 ? 0.6521 0.4095 0.5564 -0.0002 0.0589  0.0201  204 GLY   A N   
1584 C CA  . GLY   A 224 ? 0.6441 0.4096 0.5701 -0.0012 0.0582  0.0209  204 GLY   A CA  
1585 C C   . GLY   A 224 ? 0.6333 0.4085 0.5683 -0.0029 0.0448  0.0188  204 GLY   A C   
1586 O O   . GLY   A 224 ? 0.6301 0.4056 0.5616 -0.0039 0.0384  0.0177  204 GLY   A O   
1587 N N   . LEU   A 225 ? 0.6248 0.4063 0.5682 -0.0028 0.0405  0.0182  205 LEU   A N   
1588 C CA  . LEU   A 225 ? 0.6294 0.4174 0.5785 -0.0038 0.0278  0.0163  205 LEU   A CA  
1589 C C   . LEU   A 225 ? 0.6025 0.393  0.5739 -0.006  0.0241  0.0171  205 LEU   A C   
1590 O O   . LEU   A 225 ? 0.5887 0.381  0.5808 -0.0068 0.0295  0.0191  205 LEU   A O   
1591 C CB  . LEU   A 225 ? 0.6464 0.439  0.5995 -0.003  0.0249  0.0157  205 LEU   A CB  
1592 C CG  . LEU   A 225 ? 0.6934 0.4865 0.6274 -0.0017 0.0184  0.0133  205 LEU   A CG  
1593 C CD1 . LEU   A 225 ? 0.7192 0.5073 0.6319 -0.0004 0.024   0.013   205 LEU   A CD1 
1594 C CD2 . LEU   A 225 ? 0.7031 0.4996 0.6413 -0.0009 0.017   0.0129  205 LEU   A CD2 
1595 N N   . LYS   A 226 ? 0.5873 0.3776 0.5556 -0.007  0.0146  0.0156  206 LYS   A N   
1596 C CA  . LYS   A 226 ? 0.5734 0.3652 0.5626 -0.0092 0.0087  0.0161  206 LYS   A CA  
1597 C C   . LYS   A 226 ? 0.5546 0.3512 0.5601 -0.0093 0.001   0.0155  206 LYS   A C   
1598 O O   . LYS   A 226 ? 0.5466 0.3441 0.5406 -0.0077 -0.0037 0.0139  206 LYS   A O   
1599 C CB  . LYS   A 226 ? 0.6072 0.3958 0.5854 -0.0098 -0.0003 0.0144  206 LYS   A CB  
1600 C CG  . LYS   A 226 ? 0.6872 0.4708 0.6553 -0.0101 0.0067  0.0153  206 LYS   A CG  
1601 C CD  . LYS   A 226 ? 0.7815 0.5616 0.7272 -0.009  0.0004  0.0132  206 LYS   A CD  
1602 C CE  . LYS   A 226 ? 0.8613 0.6359 0.7962 -0.009  0.0063  0.0139  206 LYS   A CE  
1603 N NZ  . LYS   A 226 ? 0.9012 0.6731 0.8148 -0.0075 0.0005  0.0119  206 LYS   A NZ  
1604 N N   . VAL   A 227 ? 0.5442 0.3435 0.5772 -0.011  0.0004  0.0169  207 VAL   A N   
1605 C CA  . VAL   A 227 ? 0.5382 0.3416 0.5888 -0.0109 -0.0078 0.0163  207 VAL   A CA  
1606 C C   . VAL   A 227 ? 0.5251 0.3255 0.564  -0.0102 -0.0237 0.0134  207 VAL   A C   
1607 O O   . VAL   A 227 ? 0.5133 0.3145 0.5493 -0.0087 -0.0291 0.0121  207 VAL   A O   
1608 C CB  . VAL   A 227 ? 0.5562 0.363  0.6415 -0.0129 -0.0063 0.0183  207 VAL   A CB  
1609 C CG1 . VAL   A 227 ? 0.5538 0.3643 0.6581 -0.0126 -0.0164 0.0175  207 VAL   A CG1 
1610 C CG2 . VAL   A 227 ? 0.5679 0.3756 0.6622 -0.0129 0.0114  0.0215  207 VAL   A CG2 
1611 N N   . CYS   A 228 ? 0.5253 0.3209 0.554  -0.011  -0.0302 0.0123  208 CYS   A N   
1612 C CA  . CYS   A 228 ? 0.5421 0.3321 0.5563 -0.0098 -0.0441 0.0097  208 CYS   A CA  
1613 C C   . CYS   A 228 ? 0.5381 0.3269 0.5267 -0.0072 -0.0424 0.0083  208 CYS   A C   
1614 O O   . CYS   A 228 ? 0.5557 0.341  0.537  -0.0057 -0.0513 0.0066  208 CYS   A O   
1615 C CB  . CYS   A 228 ? 0.579  0.363  0.5857 -0.0108 -0.0497 0.0091  208 CYS   A CB  
1616 S SG  . CYS   A 228 ? 0.7044 0.4871 0.6878 -0.0103 -0.0387 0.0096  208 CYS   A SG  
1617 N N   . PHE   A 229 ? 0.5168 0.3075 0.4922 -0.0067 -0.0313 0.0091  209 PHE   A N   
1618 C CA  . PHE   A 229 ? 0.5136 0.3037 0.4675 -0.0046 -0.0292 0.0079  209 PHE   A CA  
1619 C C   . PHE   A 229 ? 0.5191 0.3132 0.4796 -0.0037 -0.0269 0.0082  209 PHE   A C   
1620 O O   . PHE   A 229 ? 0.5228 0.3151 0.4719 -0.0022 -0.0316 0.0067  209 PHE   A O   
1621 C CB  . PHE   A 229 ? 0.5017 0.292  0.4412 -0.0043 -0.0195 0.0085  209 PHE   A CB  
1622 C CG  . PHE   A 229 ? 0.5055 0.2948 0.4239 -0.0024 -0.0191 0.0071  209 PHE   A CG  
1623 C CD1 . PHE   A 229 ? 0.5253 0.3104 0.4286 -0.0014 -0.0252 0.0056  209 PHE   A CD1 
1624 C CD2 . PHE   A 229 ? 0.517  0.3092 0.4313 -0.0016 -0.012  0.0075  209 PHE   A CD2 
1625 C CE1 . PHE   A 229 ? 0.5466 0.3311 0.4331 0.0003  -0.0237 0.0045  209 PHE   A CE1 
1626 C CE2 . PHE   A 229 ? 0.5253 0.3168 0.4225 -0.0001 -0.0118 0.0063  209 PHE   A CE2 
1627 C CZ  . PHE   A 229 ? 0.5183 0.3066 0.403  0.0007  -0.0174 0.0048  209 PHE   A CZ  
1628 N N   . GLY   A 230 ? 0.5029 0.3014 0.4819 -0.0046 -0.0197 0.0101  210 GLY   A N   
1629 C CA  . GLY   A 230 ? 0.4943 0.2963 0.4817 -0.0036 -0.0174 0.0105  210 GLY   A CA  
1630 C C   . GLY   A 230 ? 0.5007 0.3017 0.4968 -0.0031 -0.0297 0.0091  210 GLY   A C   
1631 O O   . GLY   A 230 ? 0.4924 0.2934 0.4828 -0.0016 -0.0317 0.0082  210 GLY   A O   
1632 N N   . ILE   A 231 ? 0.5075 0.306  0.5154 -0.0043 -0.0391 0.0086  211 ILE   A N   
1633 C CA  . ILE   A 231 ? 0.5121 0.3066 0.5256 -0.0035 -0.0531 0.0069  211 ILE   A CA  
1634 C C   . ILE   A 231 ? 0.4952 0.2823 0.4806 -0.0013 -0.0592 0.0047  211 ILE   A C   
1635 O O   . ILE   A 231 ? 0.5055 0.2893 0.4881 0.0004  -0.0659 0.0034  211 ILE   A O   
1636 C CB  . ILE   A 231 ? 0.5367 0.3285 0.567  -0.0053 -0.0623 0.0069  211 ILE   A CB  
1637 C CG1 . ILE   A 231 ? 0.5429 0.3422 0.6068 -0.0072 -0.0571 0.0092  211 ILE   A CG1 
1638 C CG2 . ILE   A 231 ? 0.5553 0.3384 0.5823 -0.004  -0.079  0.0046  211 ILE   A CG2 
1639 C CD1 . ILE   A 231 ? 0.5515 0.3495 0.6344 -0.0097 -0.063  0.0097  211 ILE   A CD1 
1640 N N   . GLN   A 232 ? 0.4868 0.2709 0.4517 -0.0012 -0.0562 0.0043  212 GLN   A N   
1641 C CA  . GLN   A 232 ? 0.481  0.2581 0.4203 0.001   -0.0596 0.0025  212 GLN   A CA  
1642 C C   . GLN   A 232 ? 0.4893 0.2699 0.4198 0.0022  -0.0525 0.0025  212 GLN   A C   
1643 O O   . GLN   A 232 ? 0.5074 0.2822 0.4241 0.0041  -0.0568 0.0011  212 GLN   A O   
1644 C CB  . GLN   A 232 ? 0.473  0.2463 0.3951 0.001   -0.0578 0.0022  212 GLN   A CB  
1645 C CG  . GLN   A 232 ? 0.4913 0.2584 0.4182 0.0001  -0.0668 0.0019  212 GLN   A CG  
1646 C CD  . GLN   A 232 ? 0.5304 0.2871 0.4542 0.0017  -0.0805 0.0002  212 GLN   A CD  
1647 O OE1 . GLN   A 232 ? 0.5488 0.299  0.4561 0.0042  -0.083  -0.001  212 GLN   A OE1 
1648 N NE2 . GLN   A 232 ? 0.56   0.313  0.4987 0.0006  -0.0901 0.0001  212 GLN   A NE2 
1649 N N   . LEU   A 233 ? 0.4781 0.2667 0.4159 0.0012  -0.0415 0.0041  213 LEU   A N   
1650 C CA  . LEU   A 233 ? 0.4897 0.2811 0.4206 0.0023  -0.0355 0.0041  213 LEU   A CA  
1651 C C   . LEU   A 233 ? 0.5044 0.2958 0.4468 0.0032  -0.0407 0.0038  213 LEU   A C   
1652 O O   . LEU   A 233 ? 0.5173 0.3063 0.4487 0.0047  -0.0417 0.0029  213 LEU   A O   
1653 C CB  . LEU   A 233 ? 0.4896 0.2868 0.4243 0.0015  -0.0236 0.0059  213 LEU   A CB  
1654 C CG  . LEU   A 233 ? 0.4977 0.2943 0.4192 0.0011  -0.018  0.0061  213 LEU   A CG  
1655 C CD1 . LEU   A 233 ? 0.4933 0.2927 0.4172 0.0008  -0.0069 0.0078  213 LEU   A CD1 
1656 C CD2 . LEU   A 233 ? 0.5203 0.3138 0.4212 0.0022  -0.0198 0.0045  213 LEU   A CD2 
1657 N N   . LEU   A 234 ? 0.5066 0.3001 0.4719 0.0023  -0.0445 0.0046  214 LEU   A N   
1658 C CA  . LEU   A 234 ? 0.5263 0.3194 0.5046 0.0034  -0.0512 0.0041  214 LEU   A CA  
1659 C C   . LEU   A 234 ? 0.5368 0.3194 0.5002 0.0052  -0.0641 0.0017  214 LEU   A C   
1660 O O   . LEU   A 234 ? 0.5538 0.3333 0.5134 0.0069  -0.0679 0.0008  214 LEU   A O   
1661 C CB  . LEU   A 234 ? 0.5357 0.3331 0.5441 0.002   -0.0535 0.0054  214 LEU   A CB  
1662 C CG  . LEU   A 234 ? 0.568  0.3738 0.594  0.0008  -0.0402 0.0081  214 LEU   A CG  
1663 C CD1 . LEU   A 234 ? 0.5741 0.3835 0.6323 -0.0006 -0.0431 0.0094  214 LEU   A CD1 
1664 C CD2 . LEU   A 234 ? 0.5812 0.3899 0.605  0.0024  -0.0328 0.0087  214 LEU   A CD2 
1665 N N   . ASN   A 235 ? 0.5325 0.3081 0.485  0.005   -0.0702 0.0008  215 ASN   A N   
1666 C CA  . ASN   A 235 ? 0.5391 0.3016 0.4729 0.0073  -0.0811 -0.0013 215 ASN   A CA  
1667 C C   . ASN   A 235 ? 0.5402 0.2997 0.4503 0.009   -0.0753 -0.0019 215 ASN   A C   
1668 O O   . ASN   A 235 ? 0.5569 0.3079 0.4562 0.0112  -0.081  -0.0033 215 ASN   A O   
1669 C CB  . ASN   A 235 ? 0.5556 0.3101 0.4803 0.007   -0.0873 -0.002  215 ASN   A CB  
1670 C CG  . ASN   A 235 ? 0.5972 0.3513 0.5438 0.0056  -0.0964 -0.0018 215 ASN   A CG  
1671 O OD1 . ASN   A 235 ? 0.6148 0.371  0.5812 0.0056  -0.1021 -0.0019 215 ASN   A OD1 
1672 N ND2 . ASN   A 235 ? 0.6082 0.3599 0.5533 0.0043  -0.0979 -0.0016 215 ASN   A ND2 
1673 N N   . ALA   A 236 ? 0.5181 0.2842 0.421  0.0079  -0.064  -0.001  216 ALA   A N   
1674 C CA  . ALA   A 236 ? 0.512  0.2763 0.3956 0.0092  -0.0581 -0.0015 216 ALA   A CA  
1675 C C   . ALA   A 236 ? 0.5149 0.2815 0.4023 0.01    -0.0567 -0.0015 216 ALA   A C   
1676 O O   . ALA   A 236 ? 0.5301 0.2895 0.4025 0.0118  -0.0585 -0.0026 216 ALA   A O   
1677 C CB  . ALA   A 236 ? 0.5095 0.2814 0.3894 0.0078  -0.0474 -0.0004 216 ALA   A CB  
1678 N N   . VAL   A 237 ? 0.5035 0.279  0.4107 0.0088  -0.0532 -0.0003 217 VAL   A N   
1679 C CA  . VAL   A 237 ? 0.5178 0.2955 0.4297 0.0098  -0.0516 -0.0002 217 VAL   A CA  
1680 C C   . VAL   A 237 ? 0.533  0.3013 0.4441 0.0119  -0.0636 -0.0018 217 VAL   A C   
1681 O O   . VAL   A 237 ? 0.5437 0.3074 0.4438 0.0136  -0.0642 -0.0026 217 VAL   A O   
1682 C CB  . VAL   A 237 ? 0.5287 0.3166 0.4625 0.0084  -0.0447 0.0018  217 VAL   A CB  
1683 C CG1 . VAL   A 237 ? 0.5429 0.3323 0.4857 0.0097  -0.0449 0.0019  217 VAL   A CG1 
1684 C CG2 . VAL   A 237 ? 0.533  0.3265 0.4608 0.0072  -0.0327 0.003   217 VAL   A CG2 
1685 N N   . SER   A 238 ? 0.5388 0.303  0.4603 0.0119  -0.0737 -0.0023 218 SER   A N   
1686 C CA  A SER   A 238 ? 0.5545 0.3075 0.4745 0.0143  -0.0871 -0.004  218 SER   A CA  
1687 C CA  B SER   A 238 ? 0.5499 0.303  0.4698 0.0143  -0.087  -0.004  218 SER   A CA  
1688 C C   . SER   A 238 ? 0.5555 0.2939 0.4456 0.0166  -0.0906 -0.0057 218 SER   A C   
1689 O O   . SER   A 238 ? 0.5686 0.2979 0.4491 0.0191  -0.0959 -0.0069 218 SER   A O   
1690 C CB  A SER   A 238 ? 0.5926 0.3429 0.5289 0.0137  -0.0981 -0.0043 218 SER   A CB  
1691 C CB  B SER   A 238 ? 0.5745 0.3252 0.5116 0.0137  -0.0979 -0.0043 218 SER   A CB  
1692 O OG  A SER   A 238 ? 0.6325 0.3955 0.5984 0.0115  -0.0942 -0.0026 218 SER   A OG  
1693 O OG  B SER   A 238 ? 0.6103 0.3483 0.5446 0.0162  -0.1123 -0.0062 218 SER   A OG  
1694 N N   . ARG   A 239 ? 0.5335 0.2689 0.409  0.0161  -0.0873 -0.0056 219 ARG   A N   
1695 C CA  . ARG   A 239 ? 0.541  0.2618 0.3885 0.0185  -0.0887 -0.0068 219 ARG   A CA  
1696 C C   . ARG   A 239 ? 0.5421 0.2644 0.3768 0.0191  -0.0793 -0.0066 219 ARG   A C   
1697 O O   . ARG   A 239 ? 0.5533 0.2621 0.3688 0.0217  -0.0819 -0.0077 219 ARG   A O   
1698 C CB  . ARG   A 239 ? 0.549  0.2664 0.3862 0.0181  -0.0872 -0.0066 219 ARG   A CB  
1699 C CG  . ARG   A 239 ? 0.5667 0.2795 0.414  0.0177  -0.0983 -0.007  219 ARG   A CG  
1700 C CD  . ARG   A 239 ? 0.5791 0.291  0.4198 0.0168  -0.096  -0.0066 219 ARG   A CD  
1701 N NE  . ARG   A 239 ? 0.587  0.2976 0.4428 0.0157  -0.1057 -0.0067 219 ARG   A NE  
1702 C CZ  . ARG   A 239 ? 0.5968 0.3065 0.4512 0.0146  -0.106  -0.0063 219 ARG   A CZ  
1703 N NH1 . ARG   A 239 ? 0.5935 0.3032 0.4318 0.0148  -0.0973 -0.0058 219 ARG   A NH1 
1704 N NH2 . ARG   A 239 ? 0.5798 0.2884 0.4496 0.0134  -0.1152 -0.0065 219 ARG   A NH2 
1705 N N   . VAL   A 240 ? 0.5224 0.2594 0.3667 0.0168  -0.0683 -0.0052 220 VAL   A N   
1706 C CA  . VAL   A 240 ? 0.5293 0.2685 0.3639 0.017   -0.0599 -0.0051 220 VAL   A CA  
1707 C C   . VAL   A 240 ? 0.5407 0.2753 0.376  0.0187  -0.0643 -0.0058 220 VAL   A C   
1708 O O   . VAL   A 240 ? 0.5387 0.2642 0.3568 0.0205  -0.0633 -0.0066 220 VAL   A O   
1709 C CB  . VAL   A 240 ? 0.5313 0.2856 0.3761 0.0144  -0.0489 -0.0036 220 VAL   A CB  
1710 C CG1 . VAL   A 240 ? 0.5342 0.2911 0.3738 0.0145  -0.0422 -0.0034 220 VAL   A CG1 
1711 C CG2 . VAL   A 240 ? 0.5438 0.3001 0.3817 0.0133  -0.0439 -0.0031 220 VAL   A CG2 
1712 N N   . GLU   A 241 ? 0.5504 0.2902 0.4057 0.0185  -0.0693 -0.0056 221 GLU   A N   
1713 C CA  . GLU   A 241 ? 0.5914 0.3273 0.4501 0.0204  -0.0746 -0.0063 221 GLU   A CA  
1714 C C   . GLU   A 241 ? 0.6258 0.3426 0.4652 0.0236  -0.085  -0.0082 221 GLU   A C   
1715 O O   . GLU   A 241 ? 0.6436 0.353  0.4706 0.0256  -0.0849 -0.009  221 GLU   A O   
1716 C CB  . GLU   A 241 ? 0.6478 0.3921 0.5342 0.0197  -0.0791 -0.0057 221 GLU   A CB  
1717 C CG  . GLU   A 241 ? 0.7817 0.523  0.6753 0.0218  -0.0851 -0.0064 221 GLU   A CG  
1718 C CD  . GLU   A 241 ? 0.9358 0.6828 0.8582 0.0216  -0.0922 -0.006  221 GLU   A CD  
1719 O OE1 . GLU   A 241 ? 0.9697 0.7275 0.91   0.0191  -0.0873 -0.0044 221 GLU   A OE1 
1720 O OE2 . GLU   A 241 ? 0.9853 0.7255 0.9131 0.0239  -0.1027 -0.0072 221 GLU   A OE2 
1721 N N   . ARG   A 242 ? 0.6312 0.3384 0.4654 0.0244  -0.0934 -0.009  222 ARG   A N   
1722 C CA  . ARG   A 242 ? 0.656  0.3415 0.4681 0.0281  -0.1035 -0.0109 222 ARG   A CA  
1723 C C   . ARG   A 242 ? 0.6609 0.336  0.4449 0.0294  -0.0956 -0.011  222 ARG   A C   
1724 O O   . ARG   A 242 ? 0.6929 0.3499 0.4561 0.0328  -0.0999 -0.0122 222 ARG   A O   
1725 C CB  . ARG   A 242 ? 0.6984 0.3746 0.5122 0.0288  -0.1157 -0.0118 222 ARG   A CB  
1726 C CG  . ARG   A 242 ? 0.7779 0.46   0.6192 0.0283  -0.1263 -0.012  222 ARG   A CG  
1727 C CD  . ARG   A 242 ? 0.8712 0.5426 0.7154 0.029   -0.1405 -0.0131 222 ARG   A CD  
1728 N NE  . ARG   A 242 ? 0.9709 0.6354 0.7978 0.0287  -0.1382 -0.013  222 ARG   A NE  
1729 C CZ  . ARG   A 242 ? 1.0219 0.6975 0.862  0.0257  -0.1344 -0.0118 222 ARG   A CZ  
1730 N NH1 . ARG   A 242 ? 1.0106 0.7044 0.8813 0.0226  -0.1317 -0.0105 222 ARG   A NH1 
1731 N NH2 . ARG   A 242 ? 1.0366 0.7042 0.859  0.026   -0.1327 -0.0117 222 ARG   A NH2 
1732 N N   . ALA   A 243 ? 0.6222 0.308  0.4059 0.027   -0.0837 -0.0096 223 ALA   A N   
1733 C CA  . ALA   A 243 ? 0.6427 0.3202 0.4038 0.0281  -0.0754 -0.0095 223 ALA   A CA  
1734 C C   . ALA   A 243 ? 0.6704 0.3501 0.4263 0.028   -0.0673 -0.0092 223 ALA   A C   
1735 O O   . ALA   A 243 ? 0.69   0.357  0.4251 0.0299  -0.0631 -0.0094 223 ALA   A O   
1736 C CB  . ALA   A 243 ? 0.6331 0.3209 0.3976 0.0257  -0.067  -0.0083 223 ALA   A CB  
1737 N N   . LEU   A 244 ? 0.6781 0.3724 0.4516 0.0261  -0.0646 -0.0087 224 LEU   A N   
1738 C CA  . LEU   A 244 ? 0.7267 0.4237 0.4955 0.0257  -0.0567 -0.0084 224 LEU   A CA  
1739 C C   . LEU   A 244 ? 0.7929 0.4715 0.5411 0.0291  -0.0594 -0.0095 224 LEU   A C   
1740 O O   . LEU   A 244 ? 0.8028 0.4767 0.5369 0.0292  -0.051  -0.0092 224 LEU   A O   
1741 C CB  . LEU   A 244 ? 0.7187 0.4309 0.5077 0.0239  -0.0547 -0.0077 224 LEU   A CB  
1742 C CG  . LEU   A 244 ? 0.7267 0.4557 0.534  0.0208  -0.0497 -0.0063 224 LEU   A CG  
1743 C CD1 . LEU   A 244 ? 0.7278 0.4687 0.5509 0.0195  -0.0459 -0.0054 224 LEU   A CD1 
1744 C CD2 . LEU   A 244 ? 0.7404 0.4735 0.5405 0.0191  -0.0409 -0.0056 224 LEU   A CD2 
1745 N N   . PRO   A 245 ? 0.8351 0.5011 0.5796 0.032   -0.0711 -0.0109 225 PRO   A N   
1746 C CA  . PRO   A 245 ? 0.8715 0.5172 0.5927 0.0356  -0.0734 -0.012  225 PRO   A CA  
1747 C C   . PRO   A 245 ? 0.9024 0.5294 0.5972 0.0378  -0.0701 -0.0121 225 PRO   A C   
1748 O O   . PRO   A 245 ? 0.9422 0.5505 0.615  0.0409  -0.0697 -0.0128 225 PRO   A O   
1749 C CB  . PRO   A 245 ? 0.8885 0.5247 0.6135 0.0383  -0.0885 -0.0136 225 PRO   A CB  
1750 C CG  . PRO   A 245 ? 0.8715 0.5281 0.6274 0.0354  -0.0913 -0.0129 225 PRO   A CG  
1751 C CD  . PRO   A 245 ? 0.8368 0.5057 0.5987 0.0323  -0.0828 -0.0115 225 PRO   A CD  
1752 N N   . LYS   A 246 ? 0.8811 0.5118 0.5772 0.0366  -0.0672 -0.0114 226 LYS   A N   
1753 C CA  . LYS   A 246 ? 0.8847 0.499  0.5577 0.0387  -0.0625 -0.0112 226 LYS   A CA  
1754 C C   . LYS   A 246 ? 0.8387 0.465  0.5147 0.036   -0.0476 -0.0096 226 LYS   A C   
1755 O O   . LYS   A 246 ? 0.8688 0.4834 0.5284 0.0376  -0.0413 -0.009  226 LYS   A O   
1756 C CB  . LYS   A 246 ? 0.9447 0.5527 0.616  0.0397  -0.0704 -0.0115 226 LYS   A CB  
1757 C CG  . LYS   A 246 ? 1.0168 0.6222 0.6982 0.0406  -0.0864 -0.0129 226 LYS   A CG  
1758 C CD  . LYS   A 246 ? 1.0815 0.6832 0.763  0.0407  -0.0924 -0.013  226 LYS   A CD  
1759 C CE  . LYS   A 246 ? 1.142  0.7391 0.8337 0.0416  -0.1091 -0.0144 226 LYS   A CE  
1760 N NZ  . LYS   A 246 ? 1.1847 0.7776 0.8763 0.0416  -0.1152 -0.0145 226 LYS   A NZ  
1761 N N   . LEU   A 247 ? 0.7609 0.4103 0.459  0.032   -0.0425 -0.0087 227 LEU   A N   
1762 C CA  . LEU   A 247 ? 0.7093 0.3706 0.4128 0.0293  -0.0307 -0.0075 227 LEU   A CA  
1763 C C   . LEU   A 247 ? 0.667  0.3226 0.3603 0.0297  -0.0222 -0.0072 227 LEU   A C   
1764 O O   . LEU   A 247 ? 0.6829 0.3404 0.3789 0.0294  -0.0233 -0.0076 227 LEU   A O   
1765 C CB  . LEU   A 247 ? 0.6932 0.3776 0.4213 0.0255  -0.03   -0.0069 227 LEU   A CB  
1766 C CG  . LEU   A 247 ? 0.6929 0.3911 0.4301 0.0227  -0.0212 -0.0058 227 LEU   A CG  
1767 C CD1 . LEU   A 247 ? 0.6959 0.3907 0.4293 0.0233  -0.0218 -0.0055 227 LEU   A CD1 
1768 C CD2 . LEU   A 247 ? 0.662  0.379  0.4195 0.0196  -0.0207 -0.0053 227 LEU   A CD2 
1769 N N   . THR   A 248 ? 0.63   0.2779 0.3117 0.0305  -0.0135 -0.0064 228 THR   A N   
1770 C CA  . THR   A 248 ? 0.6277 0.2697 0.3007 0.0306  -0.0037 -0.0058 228 THR   A CA  
1771 C C   . THR   A 248 ? 0.5936 0.2482 0.2773 0.0277  0.0074  -0.0045 228 THR   A C   
1772 O O   . THR   A 248 ? 0.6042 0.2571 0.2856 0.0271  0.0159  -0.0039 228 THR   A O   
1773 C CB  . THR   A 248 ? 0.6745 0.2892 0.3201 0.0352  -0.0023 -0.006  228 THR   A CB  
1774 O OG1 . THR   A 248 ? 0.7018 0.3106 0.3412 0.0366  -0.0002 -0.0053 228 THR   A OG1 
1775 C CG2 . THR   A 248 ? 0.7011 0.2999 0.3336 0.0386  -0.0143 -0.0075 228 THR   A CG2 
1776 N N   . VAL   A 249 ? 0.5675 0.2348 0.2638 0.026   0.007   -0.0041 229 VAL   A N   
1777 C CA  . VAL   A 249 ? 0.5432 0.2218 0.2504 0.0236  0.0161  -0.0031 229 VAL   A CA  
1778 C C   . VAL   A 249 ? 0.523  0.2171 0.2455 0.02    0.0191  -0.003  229 VAL   A C   
1779 O O   . VAL   A 249 ? 0.5178 0.2202 0.2481 0.0187  0.0132  -0.0036 229 VAL   A O   
1780 C CB  . VAL   A 249 ? 0.5325 0.2213 0.2498 0.0227  0.0131  -0.0029 229 VAL   A CB  
1781 C CG1 . VAL   A 249 ? 0.5352 0.2393 0.268  0.0203  0.0057  -0.0035 229 VAL   A CG1 
1782 C CG2 . VAL   A 249 ? 0.5391 0.2364 0.2655 0.0211  0.0218  -0.0019 229 VAL   A CG2 
1783 N N   . PRO   A 250 ? 0.5134 0.2109 0.2407 0.0185  0.0281  -0.0022 230 PRO   A N   
1784 C CA  . PRO   A 250 ? 0.4807 0.1925 0.2229 0.015   0.0298  -0.0022 230 PRO   A CA  
1785 C C   . PRO   A 250 ? 0.4651 0.1932 0.2225 0.0128  0.0247  -0.0025 230 PRO   A C   
1786 O O   . PRO   A 250 ? 0.4875 0.2182 0.2477 0.0132  0.0239  -0.0022 230 PRO   A O   
1787 C CB  . PRO   A 250 ? 0.5061 0.2185 0.2532 0.0139  0.0396  -0.0012 230 PRO   A CB  
1788 C CG  . PRO   A 250 ? 0.5301 0.2227 0.2586 0.0175  0.0452  -0.0006 230 PRO   A CG  
1789 C CD  . PRO   A 250 ? 0.5257 0.213  0.2455 0.02    0.0375  -0.0011 230 PRO   A CD  
1790 N N   . PHE   A 251 ? 0.4544 0.1916 0.22   0.0108  0.0216  -0.0028 231 PHE   A N   
1791 C CA  . PHE   A 251 ? 0.4399 0.1899 0.2176 0.0091  0.018   -0.0029 231 PHE   A CA  
1792 C C   . PHE   A 251 ? 0.4167 0.1753 0.203  0.0067  0.0183  -0.003  231 PHE   A C   
1793 O O   . PHE   A 251 ? 0.4112 0.1668 0.1944 0.0064  0.0193  -0.0032 231 PHE   A O   
1794 C CB  . PHE   A 251 ? 0.4487 0.199  0.2262 0.0103  0.0111  -0.0032 231 PHE   A CB  
1795 C CG  . PHE   A 251 ? 0.4646 0.2121 0.2399 0.0111  0.0067  -0.0036 231 PHE   A CG  
1796 C CD1 . PHE   A 251 ? 0.4585 0.2147 0.2427 0.0097  0.0055  -0.0035 231 PHE   A CD1 
1797 C CD2 . PHE   A 251 ? 0.4878 0.2231 0.2519 0.0137  0.0034  -0.004  231 PHE   A CD2 
1798 C CE1 . PHE   A 251 ? 0.4682 0.2221 0.2519 0.0107  0.0019  -0.0037 231 PHE   A CE1 
1799 C CE2 . PHE   A 251 ? 0.4857 0.2188 0.2496 0.0147  -0.0016 -0.0044 231 PHE   A CE2 
1800 C CZ  . PHE   A 251 ? 0.475  0.2181 0.2498 0.0131  -0.0021 -0.0042 231 PHE   A CZ  
1801 N N   . LEU   A 252 ? 0.4151 0.1832 0.2112 0.0051  0.0174  -0.003  232 LEU   A N   
1802 C CA  . LEU   A 252 ? 0.4073 0.1824 0.2101 0.0032  0.0164  -0.0031 232 LEU   A CA  
1803 C C   . LEU   A 252 ? 0.391  0.1702 0.1966 0.0037  0.0122  -0.003  232 LEU   A C   
1804 O O   . LEU   A 252 ? 0.4063 0.1872 0.2136 0.0042  0.0109  -0.0029 232 LEU   A O   
1805 C CB  . LEU   A 252 ? 0.4247 0.205  0.2356 0.0015  0.0182  -0.0032 232 LEU   A CB  
1806 C CG  . LEU   A 252 ? 0.4288 0.2141 0.2447 0       0.0157  -0.0035 232 LEU   A CG  
1807 C CD1 . LEU   A 252 ? 0.4339 0.2163 0.2466 -0.0008 0.0164  -0.0037 232 LEU   A CD1 
1808 C CD2 . LEU   A 252 ? 0.4523 0.2419 0.2767 -0.0014 0.0156  -0.0039 232 LEU   A CD2 
1809 N N   . LEU   A 253 ? 0.3851 0.1649 0.1907 0.0037  0.0108  -0.0029 233 LEU   A N   
1810 C CA  . LEU   A 253 ? 0.3923 0.1751 0.2015 0.0042  0.0084  -0.0025 233 LEU   A CA  
1811 C C   . LEU   A 253 ? 0.3958 0.1813 0.2072 0.0033  0.0092  -0.0023 233 LEU   A C   
1812 O O   . LEU   A 253 ? 0.3933 0.177  0.2024 0.0029  0.0102  -0.0024 233 LEU   A O   
1813 C CB  . LEU   A 253 ? 0.4219 0.201  0.2293 0.0058  0.0064  -0.0024 233 LEU   A CB  
1814 C CG  . LEU   A 253 ? 0.4511 0.2327 0.2645 0.0065  0.0046  -0.0018 233 LEU   A CG  
1815 C CD1 . LEU   A 253 ? 0.4666 0.2511 0.2848 0.0065  0.003   -0.0014 233 LEU   A CD1 
1816 C CD2 . LEU   A 253 ? 0.4673 0.2445 0.2799 0.0081  0.0016  -0.0019 233 LEU   A CD2 
1817 N N   . LEU   A 254 ? 0.392  0.1804 0.2064 0.0031  0.0087  -0.0021 234 LEU   A N   
1818 C CA  . LEU   A 254 ? 0.3947 0.1828 0.2082 0.0026  0.0092  -0.0019 234 LEU   A CA  
1819 C C   . LEU   A 254 ? 0.3975 0.1855 0.2127 0.0038  0.0099  -0.0009 234 LEU   A C   
1820 O O   . LEU   A 254 ? 0.4075 0.1975 0.2263 0.0042  0.0092  -0.0006 234 LEU   A O   
1821 C CB  . LEU   A 254 ? 0.4107 0.2001 0.2251 0.0018  0.008   -0.0025 234 LEU   A CB  
1822 C CG  . LEU   A 254 ? 0.4415 0.2321 0.2581 0.0006  0.008   -0.0033 234 LEU   A CG  
1823 C CD1 . LEU   A 254 ? 0.4611 0.2535 0.2812 0       0.006   -0.0039 234 LEU   A CD1 
1824 C CD2 . LEU   A 254 ? 0.4528 0.241  0.2677 -0.0004 0.0088  -0.0036 234 LEU   A CD2 
1825 N N   . GLN   A 255 ? 0.3876 0.1727 0.2008 0.0044  0.0119  -0.0003 235 GLN   A N   
1826 C CA  . GLN   A 255 ? 0.3851 0.1696 0.2017 0.0057  0.0142  0.001   235 GLN   A CA  
1827 C C   . GLN   A 255 ? 0.4006 0.1794 0.2114 0.0066  0.0174  0.0018  235 GLN   A C   
1828 O O   . GLN   A 255 ? 0.4057 0.1811 0.2111 0.0065  0.0177  0.0014  235 GLN   A O   
1829 C CB  . GLN   A 255 ? 0.3996 0.1854 0.2216 0.0066  0.0139  0.0014  235 GLN   A CB  
1830 C CG  . GLN   A 255 ? 0.3986 0.1844 0.228  0.0079  0.0167  0.0029  235 GLN   A CG  
1831 C CD  . GLN   A 255 ? 0.4445 0.2331 0.281  0.0078  0.0161  0.0034  235 GLN   A CD  
1832 O OE1 . GLN   A 255 ? 0.4464 0.2375 0.2851 0.0073  0.012   0.0026  235 GLN   A OE1 
1833 N NE2 . GLN   A 255 ? 0.4713 0.2582 0.3104 0.0085  0.0206  0.0048  235 GLN   A NE2 
1834 N N   . GLY   A 256 ? 0.4164 0.1926 0.2271 0.0076  0.0203  0.0028  236 GLY   A N   
1835 C CA  . GLY   A 256 ? 0.4311 0.199  0.2341 0.009   0.0244  0.0038  236 GLY   A CA  
1836 C C   . GLY   A 256 ? 0.4398 0.207  0.2484 0.0106  0.0293  0.0054  236 GLY   A C   
1837 O O   . GLY   A 256 ? 0.45   0.2228 0.2704 0.0107  0.0298  0.0061  236 GLY   A O   
1838 N N   . SER   A 257 ? 0.4465 0.2063 0.2473 0.0119  0.0327  0.0061  237 SER   A N   
1839 C CA  . SER   A 257 ? 0.4582 0.2174 0.2654 0.0137  0.0378  0.0077  237 SER   A CA  
1840 C C   . SER   A 257 ? 0.4942 0.2499 0.3058 0.0154  0.0448  0.0098  237 SER   A C   
1841 O O   . SER   A 257 ? 0.522  0.2798 0.3449 0.0167  0.0491  0.0114  237 SER   A O   
1842 C CB  . SER   A 257 ? 0.4696 0.2213 0.2666 0.0148  0.0397  0.0078  237 SER   A CB  
1843 O OG  . SER   A 257 ? 0.5212 0.261  0.3043 0.0163  0.0433  0.0085  237 SER   A OG  
1844 N N   . ALA   A 258 ? 0.4905 0.2399 0.2935 0.0157  0.0463  0.01    238 ALA   A N   
1845 C CA  . ALA   A 258 ? 0.5052 0.2491 0.3105 0.0175  0.0543  0.0122  238 ALA   A CA  
1846 C C   . ALA   A 258 ? 0.5046 0.2552 0.3194 0.016   0.0524  0.0121  238 ALA   A C   
1847 O O   . ALA   A 258 ? 0.5387 0.283  0.3498 0.0169  0.057   0.0132  238 ALA   A O   
1848 C CB  . ALA   A 258 ? 0.53   0.2579 0.3151 0.0195  0.0583  0.0127  238 ALA   A CB  
1849 N N   . ASP   A 259 ? 0.4697 0.2318 0.2956 0.0139  0.0456  0.0108  239 ASP   A N   
1850 C CA  . ASP   A 259 ? 0.4722 0.2404 0.3068 0.0125  0.0428  0.0105  239 ASP   A CA  
1851 C C   . ASP   A 259 ? 0.4905 0.2611 0.3415 0.0131  0.0482  0.0126  239 ASP   A C   
1852 O O   . ASP   A 259 ? 0.5112 0.2871 0.3754 0.0133  0.0476  0.013   239 ASP   A O   
1853 C CB  . ASP   A 259 ? 0.445  0.2219 0.2835 0.0107  0.0343  0.0085  239 ASP   A CB  
1854 C CG  . ASP   A 259 ? 0.4548 0.2363 0.2975 0.0093  0.0302  0.0078  239 ASP   A CG  
1855 O OD1 . ASP   A 259 ? 0.4444 0.2253 0.2936 0.0095  0.0336  0.009   239 ASP   A OD1 
1856 O OD2 . ASP   A 259 ? 0.4639 0.2488 0.3036 0.0082  0.0243  0.0061  239 ASP   A OD2 
1857 N N   . ARG   A 260 ? 0.4944 0.2606 0.3452 0.0135  0.0532  0.0139  240 ARG   A N   
1858 C CA  . ARG   A 260 ? 0.5102 0.2787 0.3787 0.0138  0.0588  0.016   240 ARG   A CA  
1859 C C   . ARG   A 260 ? 0.5122 0.2896 0.3939 0.0116  0.0525  0.0152  240 ARG   A C   
1860 O O   . ARG   A 260 ? 0.5356 0.3157 0.4344 0.0114  0.0558  0.0168  240 ARG   A O   
1861 C CB  . ARG   A 260 ? 0.5547 0.3118 0.4162 0.0156  0.0694  0.0182  240 ARG   A CB  
1862 C CG  . ARG   A 260 ? 0.6641 0.4091 0.5089 0.0181  0.0757  0.019   240 ARG   A CG  
1863 C CD  . ARG   A 260 ? 0.7756 0.515  0.6293 0.0204  0.0877  0.0221  240 ARG   A CD  
1864 N NE  . ARG   A 260 ? 0.874  0.6048 0.7266 0.0214  0.0967  0.0242  240 ARG   A NE  
1865 C CZ  . ARG   A 260 ? 0.952  0.6658 0.7827 0.0239  0.1036  0.0251  240 ARG   A CZ  
1866 N NH1 . ARG   A 260 ? 0.9585 0.6638 0.7882 0.0248  0.1123  0.0271  240 ARG   A NH1 
1867 N NH2 . ARG   A 260 ? 0.9711 0.675  0.7798 0.0255  0.1015  0.024   240 ARG   A NH2 
1868 N N   . LEU   A 261 ? 0.4846 0.2658 0.3593 0.0102  0.0438  0.0129  241 LEU   A N   
1869 C CA  . LEU   A 261 ? 0.4869 0.2745 0.3708 0.0085  0.0373  0.0121  241 LEU   A CA  
1870 C C   . LEU   A 261 ? 0.4986 0.2925 0.3899 0.0079  0.0293  0.0107  241 LEU   A C   
1871 O O   . LEU   A 261 ? 0.5111 0.309  0.4183 0.0074  0.0263  0.0111  241 LEU   A O   
1872 C CB  . LEU   A 261 ? 0.4973 0.2828 0.3676 0.0078  0.0343  0.0108  241 LEU   A CB  
1873 C CG  . LEU   A 261 ? 0.5355 0.3133 0.3998 0.0086  0.0416  0.0122  241 LEU   A CG  
1874 C CD1 . LEU   A 261 ? 0.564  0.3396 0.4151 0.0082  0.0377  0.0107  241 LEU   A CD1 
1875 C CD2 . LEU   A 261 ? 0.5533 0.3331 0.4343 0.0079  0.045   0.014   241 LEU   A CD2 
1876 N N   . CYS   A 262 ? 0.4878 0.2815 0.3677 0.008   0.0255  0.0091  242 CYS   A N   
1877 C CA  . CYS   A 262 ? 0.4935 0.2904 0.3762 0.0079  0.0188  0.0078  242 CYS   A CA  
1878 C C   . CYS   A 262 ? 0.5316 0.327  0.4131 0.009   0.0217  0.0082  242 CYS   A C   
1879 O O   . CYS   A 262 ? 0.5286 0.3208 0.397  0.0092  0.0235  0.0077  242 CYS   A O   
1880 C CB  . CYS   A 262 ? 0.4898 0.2866 0.3604 0.0071  0.0133  0.0058  242 CYS   A CB  
1881 S SG  . CYS   A 262 ? 0.4639 0.262  0.3362 0.0061  0.0092  0.0054  242 CYS   A SG  
1882 N N   . ASP   A 263 ? 0.5284 0.3259 0.4243 0.0098  0.0216  0.0091  243 ASP   A N   
1883 C CA  . ASP   A 263 ? 0.5323 0.3283 0.4286 0.0113  0.025   0.0097  243 ASP   A CA  
1884 C C   . ASP   A 263 ? 0.5184 0.3131 0.4021 0.0112  0.0204  0.0078  243 ASP   A C   
1885 O O   . ASP   A 263 ? 0.5075 0.3034 0.3898 0.0107  0.0132  0.0063  243 ASP   A O   
1886 C CB  . ASP   A 263 ? 0.5639 0.3631 0.4806 0.0122  0.0247  0.0108  243 ASP   A CB  
1887 C CG  . ASP   A 263 ? 0.6321 0.429  0.5509 0.0141  0.0315  0.0122  243 ASP   A CG  
1888 O OD1 . ASP   A 263 ? 0.6489 0.4427 0.5698 0.0149  0.041   0.0143  243 ASP   A OD1 
1889 O OD2 . ASP   A 263 ? 0.6125 0.4092 0.5287 0.0149  0.0279  0.0113  243 ASP   A OD2 
1890 N N   . SER   A 264 ? 0.5149 0.3058 0.3881 0.0119  0.0248  0.0081  244 SER   A N   
1891 C CA  . SER   A 264 ? 0.5258 0.315  0.3874 0.0116  0.0214  0.0065  244 SER   A CA  
1892 C C   . SER   A 264 ? 0.519  0.3095 0.3865 0.0124  0.0161  0.0057  244 SER   A C   
1893 O O   . SER   A 264 ? 0.5035 0.2924 0.3621 0.012   0.012   0.0042  244 SER   A O   
1894 C CB  . SER   A 264 ? 0.5575 0.3415 0.4082 0.0123  0.0267  0.007   244 SER   A CB  
1895 O OG  . SER   A 264 ? 0.5807 0.3633 0.4388 0.0142  0.0313  0.0085  244 SER   A OG  
1896 N N   . LYS   A 265 ? 0.5109 0.3035 0.394  0.0136  0.016   0.0067  245 LYS   A N   
1897 C CA  . LYS   A 265 ? 0.5195 0.3123 0.409  0.0147  0.0093  0.0058  245 LYS   A CA  
1898 C C   . LYS   A 265 ? 0.5022 0.2939 0.3869 0.0139  0.0009  0.004   245 LYS   A C   
1899 O O   . LYS   A 265 ? 0.522  0.3099 0.4006 0.0148  -0.0046 0.0026  245 LYS   A O   
1900 C CB  . LYS   A 265 ? 0.5649 0.3609 0.4757 0.016   0.0099  0.0073  245 LYS   A CB  
1901 C CG  . LYS   A 265 ? 0.676  0.4716 0.5961 0.0174  0.0012  0.0062  245 LYS   A CG  
1902 C CD  . LYS   A 265 ? 0.7755 0.5756 0.7211 0.0181  0.0009  0.0077  245 LYS   A CD  
1903 C CE  . LYS   A 265 ? 0.8518 0.6511 0.8086 0.0192  -0.0107 0.0063  245 LYS   A CE  
1904 N NZ  . LYS   A 265 ? 0.8982 0.7017 0.8774 0.0186  -0.0135 0.0072  245 LYS   A NZ  
1905 N N   . GLY   A 266 ? 0.4659 0.2593 0.3509 0.0126  0.0004  0.004   246 GLY   A N   
1906 C CA  . GLY   A 266 ? 0.4674 0.2583 0.3458 0.0121  -0.0065 0.0025  246 GLY   A CA  
1907 C C   . GLY   A 266 ? 0.4613 0.2483 0.3221 0.0117  -0.0063 0.0012  246 GLY   A C   
1908 O O   . GLY   A 266 ? 0.4677 0.2495 0.3212 0.0124  -0.0117 -0.0001 246 GLY   A O   
1909 N N   . ALA   A 267 ? 0.4521 0.2402 0.3056 0.0108  -0.0003 0.0016  247 ALA   A N   
1910 C CA  . ALA   A 267 ? 0.4601 0.245  0.2999 0.0101  0.0002  0.0005  247 ALA   A CA  
1911 C C   . ALA   A 267 ? 0.4677 0.2482 0.3029 0.0113  -0.0014 -0.0001 247 ALA   A C   
1912 O O   . ALA   A 267 ? 0.479  0.2546 0.3046 0.0115  -0.0036 -0.0012 247 ALA   A O   
1913 C CB  . ALA   A 267 ? 0.466  0.2526 0.3012 0.0089  0.0058  0.001   247 ALA   A CB  
1914 N N   . TYR   A 268 ? 0.4748 0.2561 0.3163 0.0124  0       0.0006  248 TYR   A N   
1915 C CA  . TYR   A 268 ? 0.491  0.2677 0.3282 0.0138  -0.0019 0       248 TYR   A CA  
1916 C C   . TYR   A 268 ? 0.4995 0.2716 0.3375 0.0153  -0.0097 -0.0011 248 TYR   A C   
1917 O O   . TYR   A 268 ? 0.5052 0.2701 0.3324 0.0162  -0.0122 -0.0022 248 TYR   A O   
1918 C CB  . TYR   A 268 ? 0.4938 0.2723 0.3389 0.015   0.0015  0.0012  248 TYR   A CB  
1919 C CG  . TYR   A 268 ? 0.5047 0.2839 0.3445 0.014   0.0086  0.0021  248 TYR   A CG  
1920 C CD1 . TYR   A 268 ? 0.5226 0.2981 0.3498 0.0133  0.0101  0.0014  248 TYR   A CD1 
1921 C CD2 . TYR   A 268 ? 0.5319 0.3138 0.3786 0.0141  0.0136  0.0036  248 TYR   A CD2 
1922 C CE1 . TYR   A 268 ? 0.5255 0.3    0.347  0.0125  0.0151  0.002   248 TYR   A CE1 
1923 C CE2 . TYR   A 268 ? 0.532  0.3115 0.3709 0.0138  0.0193  0.0043  248 TYR   A CE2 
1924 C CZ  . TYR   A 268 ? 0.5372 0.3129 0.3637 0.013   0.0194  0.0034  248 TYR   A CZ  
1925 O OH  . TYR   A 268 ? 0.5556 0.3274 0.3735 0.0127  0.0235  0.0039  248 TYR   A OH  
1926 N N   . LEU   A 269 ? 0.4967 0.2712 0.3464 0.0157  -0.0137 -0.0008 249 LEU   A N   
1927 C CA  . LEU   A 269 ? 0.5237 0.2923 0.3742 0.0173  -0.0226 -0.0019 249 LEU   A CA  
1928 C C   . LEU   A 269 ? 0.5119 0.2732 0.3462 0.0171  -0.0247 -0.0031 249 LEU   A C   
1929 O O   . LEU   A 269 ? 0.5239 0.2752 0.3482 0.019   -0.0301 -0.0043 249 LEU   A O   
1930 C CB  . LEU   A 269 ? 0.5634 0.3367 0.4312 0.0172  -0.0263 -0.0012 249 LEU   A CB  
1931 C CG  . LEU   A 269 ? 0.6556 0.429  0.5389 0.0191  -0.0317 -0.0011 249 LEU   A CG  
1932 C CD1 . LEU   A 269 ? 0.6834 0.4618 0.5742 0.0195  -0.0245 0.0002  249 LEU   A CD1 
1933 C CD2 . LEU   A 269 ? 0.6751 0.4526 0.5771 0.0187  -0.0361 -0.0006 249 LEU   A CD2 
1934 N N   . LEU   A 270 ? 0.4992 0.2641 0.33   0.0152  -0.0201 -0.0027 250 LEU   A N   
1935 C CA  . LEU   A 270 ? 0.5044 0.2627 0.3209 0.0152  -0.0204 -0.0035 250 LEU   A CA  
1936 C C   . LEU   A 270 ? 0.4992 0.2512 0.3022 0.0156  -0.0172 -0.0041 250 LEU   A C   
1937 O O   . LEU   A 270 ? 0.5029 0.2442 0.2933 0.0171  -0.0197 -0.005  250 LEU   A O   
1938 C CB  . LEU   A 270 ? 0.5139 0.279  0.3322 0.0131  -0.0155 -0.0029 250 LEU   A CB  
1939 C CG  . LEU   A 270 ? 0.5489 0.3094 0.3551 0.0128  -0.0134 -0.0033 250 LEU   A CG  
1940 C CD1 . LEU   A 270 ? 0.5629 0.3126 0.3603 0.0149  -0.0192 -0.0042 250 LEU   A CD1 
1941 C CD2 . LEU   A 270 ? 0.5516 0.3197 0.363  0.011   -0.01   -0.0027 250 LEU   A CD2 
1942 N N   . MET   A 271 ? 0.4883 0.2454 0.2931 0.0144  -0.0117 -0.0035 251 MET   A N   
1943 C CA  . MET   A 271 ? 0.505  0.2562 0.2983 0.0145  -0.0088 -0.004  251 MET   A CA  
1944 C C   . MET   A 271 ? 0.5217 0.2633 0.309  0.0171  -0.0139 -0.0049 251 MET   A C   
1945 O O   . MET   A 271 ? 0.5362 0.2681 0.3098 0.0179  -0.0129 -0.0055 251 MET   A O   
1946 C CB  . MET   A 271 ? 0.5101 0.2674 0.3067 0.0129  -0.0034 -0.0034 251 MET   A CB  
1947 C CG  . MET   A 271 ? 0.5285 0.2918 0.3268 0.0106  0.0012  -0.0029 251 MET   A CG  
1948 S SD  . MET   A 271 ? 0.5238 0.2821 0.3119 0.0096  0.0042  -0.0035 251 MET   A SD  
1949 C CE  . MET   A 271 ? 0.5275 0.281  0.3082 0.009   0.0078  -0.0038 251 MET   A CE  
1950 N N   . GLU   A 272 ? 0.4948 0.2384 0.2924 0.0185  -0.0189 -0.0048 252 GLU   A N   
1951 C CA  . GLU   A 272 ? 0.503  0.2371 0.2959 0.0213  -0.0251 -0.0058 252 GLU   A CA  
1952 C C   . GLU   A 272 ? 0.5324 0.2545 0.3164 0.0235  -0.0329 -0.0069 252 GLU   A C   
1953 O O   . GLU   A 272 ? 0.5628 0.2713 0.3313 0.0257  -0.0356 -0.008  252 GLU   A O   
1954 C CB  . GLU   A 272 ? 0.5139 0.2547 0.3237 0.0221  -0.0278 -0.0052 252 GLU   A CB  
1955 C CG  . GLU   A 272 ? 0.6251 0.3568 0.4313 0.0251  -0.0343 -0.0062 252 GLU   A CG  
1956 C CD  . GLU   A 272 ? 0.8096 0.5467 0.6353 0.0266  -0.039  -0.0058 252 GLU   A CD  
1957 O OE1 . GLU   A 272 ? 0.83   0.5786 0.6717 0.0251  -0.0344 -0.0043 252 GLU   A OE1 
1958 O OE2 . GLU   A 272 ? 0.8895 0.6185 0.7147 0.0294  -0.0472 -0.0069 252 GLU   A OE2 
1959 N N   . LEU   A 273 ? 0.5111 0.2363 0.3026 0.0231  -0.0365 -0.0068 253 LEU   A N   
1960 C CA  . LEU   A 273 ? 0.5371 0.2495 0.3204 0.0255  -0.0456 -0.008  253 LEU   A CA  
1961 C C   . LEU   A 273 ? 0.5667 0.2687 0.3315 0.0259  -0.0433 -0.0083 253 LEU   A C   
1962 O O   . LEU   A 273 ? 0.6138 0.2994 0.3639 0.0289  -0.0497 -0.0095 253 LEU   A O   
1963 C CB  . LEU   A 273 ? 0.5539 0.2725 0.3552 0.0254  -0.0525 -0.0078 253 LEU   A CB  
1964 C CG  . LEU   A 273 ? 0.6081 0.3352 0.4295 0.0256  -0.055  -0.0073 253 LEU   A CG  
1965 C CD1 . LEU   A 273 ? 0.6328 0.3679 0.4748 0.0248  -0.0593 -0.0067 253 LEU   A CD1 
1966 C CD2 . LEU   A 273 ? 0.6432 0.3588 0.459  0.0289  -0.0632 -0.0087 253 LEU   A CD2 
1967 N N   . ALA   A 274 ? 0.5441 0.2535 0.3083 0.0234  -0.0342 -0.0074 254 ALA   A N   
1968 C CA  . ALA   A 274 ? 0.5693 0.2688 0.3173 0.024   -0.0307 -0.0075 254 ALA   A CA  
1969 C C   . ALA   A 274 ? 0.5989 0.2828 0.3275 0.0262  -0.0285 -0.0081 254 ALA   A C   
1970 O O   . ALA   A 274 ? 0.603  0.2894 0.3325 0.0256  -0.0254 -0.008  254 ALA   A O   
1971 C CB  . ALA   A 274 ? 0.565  0.2762 0.3186 0.021   -0.0214 -0.0064 254 ALA   A CB  
1972 N N   . LYS   A 275 ? 0.6174 0.2844 0.3276 0.0287  -0.0294 -0.0085 255 LYS   A N   
1973 C CA  A LYS   A 275 ? 0.6434 0.293  0.333  0.0311  -0.026  -0.0089 255 LYS   A CA  
1974 C CA  B LYS   A 275 ? 0.6432 0.2927 0.3327 0.0311  -0.026  -0.0089 255 LYS   A CA  
1975 C C   . LYS   A 275 ? 0.6312 0.2823 0.3162 0.0293  -0.0133 -0.0078 255 LYS   A C   
1976 O O   . LYS   A 275 ? 0.643  0.2808 0.3127 0.0307  -0.0083 -0.0078 255 LYS   A O   
1977 C CB  A LYS   A 275 ? 0.6967 0.3225 0.365  0.0356  -0.0334 -0.01   255 LYS   A CB  
1978 C CB  B LYS   A 275 ? 0.695  0.321  0.3635 0.0355  -0.0335 -0.01   255 LYS   A CB  
1979 C CG  A LYS   A 275 ? 0.7624 0.3841 0.4349 0.0377  -0.0475 -0.0114 255 LYS   A CG  
1980 C CG  B LYS   A 275 ? 0.756  0.3806 0.4317 0.0372  -0.0477 -0.0112 255 LYS   A CG  
1981 C CD  A LYS   A 275 ? 0.8271 0.4502 0.503  0.0381  -0.0495 -0.012  255 LYS   A CD  
1982 C CD  B LYS   A 275 ? 0.8037 0.4331 0.4888 0.0374  -0.0525 -0.0119 255 LYS   A CD  
1983 C CE  A LYS   A 275 ? 0.8829 0.4992 0.5623 0.0409  -0.064  -0.0135 255 LYS   A CE  
1984 C CE  B LYS   A 275 ? 0.851  0.4807 0.5479 0.0388  -0.0663 -0.0129 255 LYS   A CE  
1985 N NZ  A LYS   A 275 ? 0.9375 0.5266 0.5915 0.0456  -0.072  -0.0148 255 LYS   A NZ  
1986 N NZ  B LYS   A 275 ? 0.8559 0.5064 0.5791 0.0363  -0.0665 -0.0123 255 LYS   A NZ  
1987 N N   . SER   A 276 ? 0.5822 0.249  0.2813 0.0261  -0.0081 -0.0068 256 SER   A N   
1988 C CA  A SER   A 276 ? 0.5624 0.2324 0.2615 0.0243  0.003   -0.0058 256 SER   A CA  
1989 C CA  B SER   A 276 ? 0.5663 0.2367 0.2658 0.0242  0.0031  -0.0058 256 SER   A CA  
1990 C C   . SER   A 276 ? 0.5573 0.2262 0.254  0.0232  0.0093  -0.0056 256 SER   A C   
1991 O O   . SER   A 276 ? 0.5647 0.243  0.2707 0.0217  0.007   -0.0058 256 SER   A O   
1992 C CB  A SER   A 276 ? 0.5406 0.2304 0.259  0.0208  0.0052  -0.0051 256 SER   A CB  
1993 C CB  B SER   A 276 ? 0.556  0.2465 0.2751 0.0207  0.005   -0.0051 256 SER   A CB  
1994 O OG  A SER   A 276 ? 0.5592 0.2508 0.2809 0.0215  -0.0006 -0.0052 256 SER   A OG  
1995 O OG  B SER   A 276 ? 0.5648 0.2596 0.2871 0.0187  0.0145  -0.0042 256 SER   A OG  
1996 N N   . GLN   A 277 ? 0.5497 0.2075 0.2349 0.0239  0.0179  -0.005  257 GLN   A N   
1997 C CA  . GLN   A 277 ? 0.569  0.2254 0.2527 0.0226  0.0249  -0.0046 257 GLN   A CA  
1998 C C   . GLN   A 277 ? 0.5504 0.2258 0.2538 0.0181  0.0304  -0.0039 257 GLN   A C   
1999 O O   . GLN   A 277 ? 0.5633 0.2417 0.2701 0.0162  0.0337  -0.0038 257 GLN   A O   
2000 C CB  . GLN   A 277 ? 0.6279 0.2638 0.2922 0.0251  0.033   -0.0041 257 GLN   A CB  
2001 C CG  . GLN   A 277 ? 0.7076 0.3218 0.3494 0.0298  0.0266  -0.0051 257 GLN   A CG  
2002 C CD  . GLN   A 277 ? 0.81   0.421  0.4478 0.0301  0.0229  -0.006  257 GLN   A CD  
2003 O OE1 . GLN   A 277 ? 0.8705 0.4735 0.5005 0.0329  0.0128  -0.0072 257 GLN   A OE1 
2004 N NE2 . GLN   A 277 ? 0.7824 0.3988 0.4257 0.0275  0.0305  -0.0054 257 GLN   A NE2 
2005 N N   . ASP   A 278 ? 0.5327 0.2203 0.2488 0.0165  0.0301  -0.0035 258 ASP   A N   
2006 C CA  . ASP   A 278 ? 0.5137 0.2172 0.2471 0.0127  0.0337  -0.003  258 ASP   A CA  
2007 C C   . ASP   A 278 ? 0.476  0.1936 0.2218 0.0115  0.0267  -0.0034 258 ASP   A C   
2008 O O   . ASP   A 278 ? 0.4742 0.1952 0.2235 0.0118  0.0252  -0.0032 258 ASP   A O   
2009 C CB  . ASP   A 278 ? 0.5368 0.2392 0.273  0.0122  0.0417  -0.0021 258 ASP   A CB  
2010 C CG  . ASP   A 278 ? 0.5598 0.2777 0.315  0.0086  0.0445  -0.0017 258 ASP   A CG  
2011 O OD1 . ASP   A 278 ? 0.5394 0.2673 0.3036 0.0062  0.0408  -0.0022 258 ASP   A OD1 
2012 O OD2 . ASP   A 278 ? 0.5834 0.3025 0.3443 0.0083  0.0498  -0.001  258 ASP   A OD2 
2013 N N   . LYS   A 279 ? 0.4638 0.1877 0.2147 0.0104  0.0228  -0.0038 259 LYS   A N   
2014 C CA  . LYS   A 279 ? 0.4618 0.1974 0.2235 0.0096  0.0174  -0.0039 259 LYS   A CA  
2015 C C   . LYS   A 279 ? 0.4486 0.1933 0.219  0.0071  0.0181  -0.0039 259 LYS   A C   
2016 O O   . LYS   A 279 ? 0.4541 0.1953 0.2207 0.007   0.0191  -0.004  259 LYS   A O   
2017 C CB  . LYS   A 279 ? 0.4942 0.2261 0.2528 0.012   0.0103  -0.0044 259 LYS   A CB  
2018 C CG  . LYS   A 279 ? 0.5405 0.2623 0.2894 0.014   0.008   -0.0049 259 LYS   A CG  
2019 C CD  . LYS   A 279 ? 0.5668 0.2846 0.3147 0.0165  -0.0003 -0.0055 259 LYS   A CD  
2020 C CE  . LYS   A 279 ? 0.5568 0.2639 0.2951 0.0187  -0.0032 -0.0062 259 LYS   A CE  
2021 N NZ  . LYS   A 279 ? 0.5564 0.2611 0.2977 0.0211  -0.0125 -0.0068 259 LYS   A NZ  
2022 N N   . THR   A 280 ? 0.4268 0.1817 0.2075 0.0055  0.0173  -0.0036 260 THR   A N   
2023 C CA  . THR   A 280 ? 0.4276 0.1889 0.2145 0.0035  0.0176  -0.0036 260 THR   A CA  
2024 C C   . THR   A 280 ? 0.4153 0.1834 0.2084 0.0036  0.0143  -0.0034 260 THR   A C   
2025 O O   . THR   A 280 ? 0.4218 0.1928 0.2182 0.0038  0.0132  -0.0033 260 THR   A O   
2026 C CB  . THR   A 280 ? 0.4759 0.2405 0.2685 0.0012  0.021   -0.0036 260 THR   A CB  
2027 O OG1 . THR   A 280 ? 0.5209 0.2787 0.309  0.0011  0.0257  -0.0035 260 THR   A OG1 
2028 C CG2 . THR   A 280 ? 0.4969 0.266  0.2946 -0.0009 0.0201  -0.0038 260 THR   A CG2 
2029 N N   . LEU   A 281 ? 0.4026 0.1724 0.197  0.0034  0.0135  -0.0032 261 LEU   A N   
2030 C CA  . LEU   A 281 ? 0.4065 0.1809 0.2058 0.0037  0.012   -0.0027 261 LEU   A CA  
2031 C C   . LEU   A 281 ? 0.4101 0.1857 0.2098 0.0023  0.013   -0.0027 261 LEU   A C   
2032 O O   . LEU   A 281 ? 0.4024 0.1748 0.1984 0.0018  0.0139  -0.0029 261 LEU   A O   
2033 C CB  . LEU   A 281 ? 0.4289 0.2018 0.2286 0.0056  0.0105  -0.0023 261 LEU   A CB  
2034 C CG  . LEU   A 281 ? 0.4433 0.2193 0.2482 0.0062  0.0111  -0.0014 261 LEU   A CG  
2035 C CD1 . LEU   A 281 ? 0.4559 0.236  0.2664 0.0061  0.0103  -0.001  261 LEU   A CD1 
2036 C CD2 . LEU   A 281 ? 0.4752 0.2498 0.2829 0.0081  0.0102  -0.0009 261 LEU   A CD2 
2037 N N   . LYS   A 282 ? 0.4093 0.1879 0.2121 0.0018  0.0123  -0.0025 262 LYS   A N   
2038 C CA  . LYS   A 282 ? 0.4194 0.1965 0.2203 0.0011  0.0121  -0.0026 262 LYS   A CA  
2039 C C   . LYS   A 282 ? 0.4246 0.2013 0.2253 0.0026  0.0125  -0.0017 262 LYS   A C   
2040 O O   . LYS   A 282 ? 0.4067 0.1865 0.2113 0.0031  0.0121  -0.0014 262 LYS   A O   
2041 C CB  . LYS   A 282 ? 0.4286 0.2072 0.2321 -0.0006 0.0105  -0.0034 262 LYS   A CB  
2042 C CG  . LYS   A 282 ? 0.502  0.2766 0.3019 -0.0012 0.0086  -0.0037 262 LYS   A CG  
2043 C CD  . LYS   A 282 ? 0.557  0.3329 0.362  -0.0032 0.0061  -0.0047 262 LYS   A CD  
2044 C CE  . LYS   A 282 ? 0.6064 0.3771 0.4078 -0.0035 0.0021  -0.0053 262 LYS   A CE  
2045 N NZ  . LYS   A 282 ? 0.6169 0.3826 0.4142 -0.0044 0.0017  -0.0055 262 LYS   A NZ  
2046 N N   . ILE   A 283 ? 0.4293 0.2018 0.2257 0.0036  0.0141  -0.0011 263 ILE   A N   
2047 C CA  . ILE   A 283 ? 0.4295 0.1997 0.2252 0.0053  0.0164  0.0001  263 ILE   A CA  
2048 C C   . ILE   A 283 ? 0.4487 0.2128 0.2368 0.0053  0.0159  -0.0001 263 ILE   A C   
2049 O O   . ILE   A 283 ? 0.4667 0.226  0.2487 0.0046  0.0145  -0.0007 263 ILE   A O   
2050 C CB  . ILE   A 283 ? 0.453  0.2207 0.2485 0.0071  0.0194  0.0011  263 ILE   A CB  
2051 C CG1 . ILE   A 283 ? 0.4542 0.2267 0.2576 0.0076  0.0184  0.0012  263 ILE   A CG1 
2052 C CG2 . ILE   A 283 ? 0.4631 0.2262 0.257  0.0091  0.0236  0.0027  263 ILE   A CG2 
2053 C CD1 . ILE   A 283 ? 0.4805 0.2571 0.2929 0.0084  0.0186  0.002   263 ILE   A CD1 
2054 N N   . TYR   A 284 ? 0.4292 0.1918 0.2167 0.0062  0.0168  0.0005  264 TYR   A N   
2055 C CA  . TYR   A 284 ? 0.4497 0.2034 0.2273 0.0069  0.016   0.0004  264 TYR   A CA  
2056 C C   . TYR   A 284 ? 0.462  0.2079 0.2336 0.0095  0.0216  0.0021  264 TYR   A C   
2057 O O   . TYR   A 284 ? 0.4676 0.2147 0.2434 0.0107  0.0254  0.0034  264 TYR   A O   
2058 C CB  . TYR   A 284 ? 0.4532 0.2089 0.2325 0.0064  0.0131  -0.0003 264 TYR   A CB  
2059 C CG  . TYR   A 284 ? 0.4433 0.2048 0.2281 0.0042  0.0082  -0.0019 264 TYR   A CG  
2060 C CD1 . TYR   A 284 ? 0.4719 0.2287 0.2525 0.0033  0.0037  -0.0031 264 TYR   A CD1 
2061 C CD2 . TYR   A 284 ? 0.4482 0.2188 0.2424 0.0031  0.0084  -0.002  264 TYR   A CD2 
2062 C CE1 . TYR   A 284 ? 0.4765 0.239  0.2651 0.0012  0.0001  -0.0044 264 TYR   A CE1 
2063 C CE2 . TYR   A 284 ? 0.4502 0.225  0.2496 0.0013  0.0056  -0.0032 264 TYR   A CE2 
2064 C CZ  . TYR   A 284 ? 0.4672 0.2388 0.2652 0.0003  0.0019  -0.0043 264 TYR   A CZ  
2065 O OH  . TYR   A 284 ? 0.4885 0.2648 0.2945 -0.0015 -0.0002 -0.0052 264 TYR   A OH  
2066 N N   . GLU   A 285 ? 0.4676 0.2047 0.2295 0.0105  0.0227  0.0023  265 GLU   A N   
2067 C CA  . GLU   A 285 ? 0.4848 0.2134 0.2407 0.0133  0.0293  0.0042  265 GLU   A CA  
2068 C C   . GLU   A 285 ? 0.5141 0.2326 0.2607 0.0153  0.0319  0.005   265 GLU   A C   
2069 O O   . GLU   A 285 ? 0.5446 0.2542 0.2794 0.0153  0.0275  0.0039  265 GLU   A O   
2070 C CB  . GLU   A 285 ? 0.5188 0.2387 0.2641 0.014   0.029   0.004   265 GLU   A CB  
2071 C CG  . GLU   A 285 ? 0.5717 0.2841 0.3127 0.017   0.0368  0.0061  265 GLU   A CG  
2072 C CD  . GLU   A 285 ? 0.6435 0.3662 0.4001 0.0175  0.0411  0.0073  265 GLU   A CD  
2073 O OE1 . GLU   A 285 ? 0.579  0.3136 0.3472 0.0154  0.0371  0.0063  265 GLU   A OE1 
2074 O OE2 . GLU   A 285 ? 0.6896 0.4071 0.4463 0.0202  0.0486  0.0094  265 GLU   A OE2 
2075 N N   . GLY   A 286 ? 0.5073 0.2261 0.2591 0.017   0.0389  0.0069  266 GLY   A N   
2076 C CA  . GLY   A 286 ? 0.5098 0.2179 0.2528 0.0191  0.0433  0.0081  266 GLY   A CA  
2077 C C   . GLY   A 286 ? 0.4964 0.21   0.2444 0.0178  0.0401  0.0074  266 GLY   A C   
2078 O O   . GLY   A 286 ? 0.51   0.215  0.2515 0.0196  0.0444  0.0085  266 GLY   A O   
2079 N N   . ALA   A 287 ? 0.4874 0.2136 0.2452 0.015   0.0331  0.0056  267 ALA   A N   
2080 C CA  . ALA   A 287 ? 0.4793 0.2102 0.2409 0.0139  0.0298  0.0048  267 ALA   A CA  
2081 C C   . ALA   A 287 ? 0.4744 0.2125 0.2485 0.0138  0.0341  0.0062  267 ALA   A C   
2082 O O   . ALA   A 287 ? 0.4636 0.2085 0.2492 0.0137  0.0372  0.0072  267 ALA   A O   
2083 C CB  . ALA   A 287 ? 0.4667 0.2067 0.2339 0.0113  0.0219  0.0026  267 ALA   A CB  
2084 N N   . TYR   A 288 ? 0.4675 0.2038 0.2397 0.014   0.0337  0.0061  268 TYR   A N   
2085 C CA  . TYR   A 288 ? 0.4644 0.2068 0.2484 0.0137  0.0372  0.0073  268 TYR   A CA  
2086 C C   . TYR   A 288 ? 0.4619 0.2175 0.2576 0.0113  0.0311  0.006   268 TYR   A C   
2087 O O   . TYR   A 288 ? 0.4747 0.2354 0.2715 0.0101  0.0262  0.0046  268 TYR   A O   
2088 C CB  . TYR   A 288 ? 0.4855 0.2174 0.2599 0.0153  0.0408  0.0081  268 TYR   A CB  
2089 C CG  . TYR   A 288 ? 0.5036 0.2206 0.2669 0.0183  0.0494  0.0102  268 TYR   A CG  
2090 C CD1 . TYR   A 288 ? 0.5222 0.2349 0.2827 0.0195  0.0531  0.011   268 TYR   A CD1 
2091 C CD2 . TYR   A 288 ? 0.5332 0.239  0.2878 0.0201  0.0546  0.0113  268 TYR   A CD2 
2092 C CE1 . TYR   A 288 ? 0.5465 0.2433 0.2947 0.0227  0.062   0.013   268 TYR   A CE1 
2093 C CE2 . TYR   A 288 ? 0.5704 0.2599 0.3125 0.0232  0.0638  0.0134  268 TYR   A CE2 
2094 C CZ  . TYR   A 288 ? 0.589  0.274  0.3281 0.0246  0.0676  0.0143  268 TYR   A CZ  
2095 O OH  . TYR   A 288 ? 0.6366 0.3032 0.3613 0.0282  0.0776  0.0165  268 TYR   A OH  
2096 N N   . HIS   A 289 ? 0.4409 0.2009 0.245  0.0109  0.032   0.0066  269 HIS   A N   
2097 C CA  . HIS   A 289 ? 0.4166 0.1873 0.2309 0.0091  0.0268  0.0056  269 HIS   A CA  
2098 C C   . HIS   A 289 ? 0.4132 0.1861 0.2226 0.0081  0.0206  0.0036  269 HIS   A C   
2099 O O   . HIS   A 289 ? 0.4133 0.1929 0.2274 0.0069  0.0168  0.0026  269 HIS   A O   
2100 C CB  . HIS   A 289 ? 0.4173 0.1899 0.2401 0.009   0.0292  0.0067  269 HIS   A CB  
2101 C CG  . HIS   A 289 ? 0.4054 0.1868 0.2384 0.0075  0.0242  0.006   269 HIS   A CG  
2102 N ND1 . HIS   A 289 ? 0.4203 0.2071 0.2605 0.007   0.0213  0.0056  269 HIS   A ND1 
2103 C CD2 . HIS   A 289 ? 0.4047 0.1885 0.2403 0.0069  0.0217  0.0057  269 HIS   A CD2 
2104 C CE1 . HIS   A 289 ? 0.4145 0.2057 0.2604 0.0062  0.0169  0.005   269 HIS   A CE1 
2105 N NE2 . HIS   A 289 ? 0.3999 0.1898 0.2435 0.006   0.0171  0.0051  269 HIS   A NE2 
2106 N N   . VAL   A 290 ? 0.401  0.168  0.2017 0.0087  0.0198  0.0032  270 VAL   A N   
2107 C CA  . VAL   A 290 ? 0.404  0.1744 0.2039 0.0079  0.014   0.0015  270 VAL   A CA  
2108 C C   . VAL   A 290 ? 0.4266 0.1944 0.2206 0.0077  0.0104  0.0001  270 VAL   A C   
2109 O O   . VAL   A 290 ? 0.4412 0.2012 0.2261 0.0086  0.0081  -0.0006 270 VAL   A O   
2110 C CB  . VAL   A 290 ? 0.4071 0.1732 0.2027 0.0087  0.014   0.0016  270 VAL   A CB  
2111 C CG1 . VAL   A 290 ? 0.4136 0.1849 0.2115 0.008   0.0084  0       270 VAL   A CG1 
2112 C CG2 . VAL   A 290 ? 0.4008 0.1689 0.2035 0.0087  0.0183  0.0032  270 VAL   A CG2 
2113 N N   . LEU   A 291 ? 0.4124 0.1858 0.2116 0.0065  0.0092  -0.0004 271 LEU   A N   
2114 C CA  . LEU   A 291 ? 0.4194 0.1902 0.2146 0.006   0.0064  -0.0014 271 LEU   A CA  
2115 C C   . LEU   A 291 ? 0.4321 0.2031 0.2273 0.0055  0.001   -0.003  271 LEU   A C   
2116 O O   . LEU   A 291 ? 0.4454 0.2106 0.2353 0.0056  -0.0023 -0.0039 271 LEU   A O   
2117 C CB  . LEU   A 291 ? 0.414  0.1909 0.2155 0.0048  0.0069  -0.0015 271 LEU   A CB  
2118 C CG  . LEU   A 291 ? 0.4314 0.2082 0.2343 0.0054  0.011   -0.0002 271 LEU   A CG  
2119 C CD1 . LEU   A 291 ? 0.4288 0.2103 0.2363 0.0044  0.0105  -0.0006 271 LEU   A CD1 
2120 C CD2 . LEU   A 291 ? 0.4534 0.2214 0.2478 0.0067  0.0137  0.0005  271 LEU   A CD2 
2121 N N   . HIS   A 292 ? 0.4206 0.1975 0.2219 0.0052  -0.0002 -0.0033 272 HIS   A N   
2122 C CA  . HIS   A 292 ? 0.4181 0.1958 0.2218 0.0049  -0.0052 -0.0047 272 HIS   A CA  
2123 C C   . HIS   A 292 ? 0.4419 0.2113 0.2371 0.0066  -0.008  -0.0052 272 HIS   A C   
2124 O O   . HIS   A 292 ? 0.4551 0.2243 0.2522 0.0068  -0.0129 -0.0064 272 HIS   A O   
2125 C CB  . HIS   A 292 ? 0.4093 0.1955 0.2223 0.0043  -0.0049 -0.0049 272 HIS   A CB  
2126 C CG  . HIS   A 292 ? 0.4078 0.1955 0.2205 0.0049  -0.0023 -0.0039 272 HIS   A CG  
2127 N ND1 . HIS   A 292 ? 0.4119 0.2001 0.2246 0.0049  0.0013  -0.0027 272 HIS   A ND1 
2128 C CD2 . HIS   A 292 ? 0.4411 0.2294 0.2542 0.0056  -0.0033 -0.004  272 HIS   A CD2 
2129 C CE1 . HIS   A 292 ? 0.4356 0.2248 0.2494 0.0053  0.0021  -0.0021 272 HIS   A CE1 
2130 N NE2 . HIS   A 292 ? 0.4579 0.2471 0.2713 0.0058  -0.0004 -0.0028 272 HIS   A NE2 
2131 N N   . LYS   A 293 ? 0.4263 0.1881 0.2123 0.0079  -0.0045 -0.004  273 LYS   A N   
2132 C CA  . LYS   A 293 ? 0.4361 0.1865 0.2103 0.01    -0.0059 -0.0042 273 LYS   A CA  
2133 C C   . LYS   A 293 ? 0.4613 0.1995 0.2228 0.0115  -0.0023 -0.0032 273 LYS   A C   
2134 O O   . LYS   A 293 ? 0.4924 0.2214 0.2445 0.0133  0.0017  -0.0021 273 LYS   A O   
2135 C CB  . LYS   A 293 ? 0.451  0.2031 0.2264 0.0105  -0.0031 -0.0034 273 LYS   A CB  
2136 C CG  . LYS   A 293 ? 0.4875 0.2492 0.2729 0.0096  -0.007  -0.0045 273 LYS   A CG  
2137 C CD  . LYS   A 293 ? 0.5648 0.3261 0.3494 0.0104  -0.007  -0.0043 273 LYS   A CD  
2138 C CE  . LYS   A 293 ? 0.5246 0.2957 0.3197 0.0096  -0.0097 -0.0051 273 LYS   A CE  
2139 N NZ  . LYS   A 293 ? 0.5084 0.2782 0.3047 0.0102  -0.0162 -0.0068 273 LYS   A NZ  
2140 N N   . GLU   A 294 ? 0.4579 0.1955 0.2189 0.0108  -0.003  -0.0035 274 GLU   A N   
2141 C CA  . GLU   A 294 ? 0.4655 0.1919 0.215  0.0123  0.0008  -0.0025 274 GLU   A CA  
2142 C C   . GLU   A 294 ? 0.5065 0.2189 0.2422 0.0137  -0.0057 -0.0039 274 GLU   A C   
2143 O O   . GLU   A 294 ? 0.5229 0.2327 0.2572 0.014   -0.0126 -0.0055 274 GLU   A O   
2144 C CB  . GLU   A 294 ? 0.4785 0.2136 0.2369 0.0108  0.0042  -0.0018 274 GLU   A CB  
2145 C CG  . GLU   A 294 ? 0.4894 0.2238 0.2485 0.0118  0.0127  0.0005  274 GLU   A CG  
2146 C CD  . GLU   A 294 ? 0.5149 0.2345 0.2597 0.0142  0.0171  0.0016  274 GLU   A CD  
2147 O OE1 . GLU   A 294 ? 0.5298 0.2404 0.264  0.0147  0.0127  0.0005  274 GLU   A OE1 
2148 O OE2 . GLU   A 294 ? 0.5446 0.2606 0.2887 0.0156  0.0249  0.0036  274 GLU   A OE2 
2149 N N   . LEU   A 295 ? 0.5241 0.2263 0.2494 0.0147  -0.0041 -0.0035 275 LEU   A N   
2150 C CA  . LEU   A 295 ? 0.5421 0.229  0.2529 0.0162  -0.0115 -0.005  275 LEU   A CA  
2151 C C   . LEU   A 295 ? 0.5628 0.2595 0.2866 0.0135  -0.0205 -0.0071 275 LEU   A C   
2152 O O   . LEU   A 295 ? 0.5534 0.2659 0.2935 0.0108  -0.0187 -0.007  275 LEU   A O   
2153 C CB  . LEU   A 295 ? 0.5574 0.2324 0.2554 0.0176  -0.0075 -0.004  275 LEU   A CB  
2154 C CG  . LEU   A 295 ? 0.59   0.2547 0.2767 0.0205  0.003   -0.0015 275 LEU   A CG  
2155 C CD1 . LEU   A 295 ? 0.6198 0.2724 0.2942 0.0222  0.0069  -0.0005 275 LEU   A CD1 
2156 C CD2 . LEU   A 295 ? 0.6078 0.2553 0.2772 0.0236  0.0023  -0.0016 275 LEU   A CD2 
2157 N N   . PRO   A 296 ? 0.5985 0.2858 0.3162 0.0143  -0.0301 -0.0091 276 PRO   A N   
2158 C CA  . PRO   A 296 ? 0.612  0.3087 0.345  0.0118  -0.0385 -0.011  276 PRO   A CA  
2159 C C   . PRO   A 296 ? 0.6175 0.3231 0.3611 0.009   -0.0373 -0.0109 276 PRO   A C   
2160 O O   . PRO   A 296 ? 0.626  0.3464 0.3879 0.0065  -0.0378 -0.0113 276 PRO   A O   
2161 C CB  . PRO   A 296 ? 0.6468 0.3262 0.367  0.0137  -0.0497 -0.013  276 PRO   A CB  
2162 C CG  . PRO   A 296 ? 0.6669 0.332  0.3684 0.0173  -0.0469 -0.0123 276 PRO   A CG  
2163 C CD  . PRO   A 296 ? 0.6266 0.2927 0.3229 0.0178  -0.0342 -0.0097 276 PRO   A CD  
2164 N N   . GLU   A 297 ? 0.6021 0.2983 0.3341 0.0097  -0.0351 -0.0103 277 GLU   A N   
2165 C CA  . GLU   A 297 ? 0.613  0.317  0.3542 0.0071  -0.0338 -0.0102 277 GLU   A CA  
2166 C C   . GLU   A 297 ? 0.5956 0.3165 0.3508 0.0054  -0.0254 -0.0088 277 GLU   A C   
2167 O O   . GLU   A 297 ? 0.6118 0.3429 0.3802 0.0029  -0.0255 -0.0091 277 GLU   A O   
2168 C CB  . GLU   A 297 ? 0.685  0.3744 0.4092 0.0087  -0.0325 -0.0096 277 GLU   A CB  
2169 C CG  . GLU   A 297 ? 0.8409 0.5129 0.5523 0.0098  -0.043  -0.0114 277 GLU   A CG  
2170 C CD  . GLU   A 297 ? 1.0342 0.6945 0.7337 0.0102  -0.044  -0.0114 277 GLU   A CD  
2171 O OE1 . GLU   A 297 ? 1.0697 0.7405 0.7804 0.0076  -0.0413 -0.0111 277 GLU   A OE1 
2172 O OE2 . GLU   A 297 ? 1.1099 0.7491 0.7876 0.0133  -0.0475 -0.0117 277 GLU   A OE2 
2173 N N   . VAL   A 298 ? 0.5664 0.2889 0.3186 0.0069  -0.0183 -0.0072 278 VAL   A N   
2174 C CA  . VAL   A 298 ? 0.5335 0.27   0.2976 0.0057  -0.0116 -0.006  278 VAL   A CA  
2175 C C   . VAL   A 298 ? 0.5013 0.2493 0.2793 0.0042  -0.0139 -0.0068 278 VAL   A C   
2176 O O   . VAL   A 298 ? 0.5032 0.2612 0.2929 0.0022  -0.0129 -0.0069 278 VAL   A O   
2177 C CB  . VAL   A 298 ? 0.5322 0.2664 0.2907 0.0076  -0.004  -0.0041 278 VAL   A CB  
2178 C CG1 . VAL   A 298 ? 0.5185 0.2664 0.2902 0.0065  0.0004  -0.0032 278 VAL   A CG1 
2179 C CG2 . VAL   A 298 ? 0.544  0.268  0.2911 0.0092  0       -0.003  278 VAL   A CG2 
2180 N N   . THR   A 299 ? 0.4927 0.2378 0.2684 0.0054  -0.0169 -0.0073 279 THR   A N   
2181 C CA  . THR   A 299 ? 0.4977 0.2528 0.286  0.0043  -0.0189 -0.008  279 THR   A CA  
2182 C C   . THR   A 299 ? 0.4776 0.2381 0.2781 0.0022  -0.0237 -0.0093 279 THR   A C   
2183 O O   . THR   A 299 ? 0.4651 0.2362 0.2781 0.0008  -0.0212 -0.0091 279 THR   A O   
2184 C CB  . THR   A 299 ? 0.5416 0.2905 0.3235 0.0062  -0.022  -0.0084 279 THR   A CB  
2185 O OG1 . THR   A 299 ? 0.5785 0.3247 0.3528 0.0077  -0.0155 -0.0068 279 THR   A OG1 
2186 C CG2 . THR   A 299 ? 0.5427 0.3009 0.3372 0.0056  -0.0245 -0.0091 279 THR   A CG2 
2187 N N   . ASN   A 300 ? 0.4882 0.2406 0.285  0.0021  -0.0303 -0.0106 280 ASN   A N   
2188 C CA  . ASN   A 300 ? 0.5021 0.2599 0.3132 -0.0002 -0.0348 -0.0117 280 ASN   A CA  
2189 C C   . ASN   A 300 ? 0.4861 0.2517 0.3047 -0.0023 -0.0286 -0.0108 280 ASN   A C   
2190 O O   . ASN   A 300 ? 0.4839 0.2584 0.3175 -0.004  -0.0274 -0.011  280 ASN   A O   
2191 C CB  . ASN   A 300 ? 0.5298 0.2761 0.3354 0       -0.044  -0.0133 280 ASN   A CB  
2192 C CG  . ASN   A 300 ? 0.6069 0.3442 0.4057 0.0022  -0.0516 -0.0146 280 ASN   A CG  
2193 O OD1 . ASN   A 300 ? 0.6244 0.3664 0.4269 0.0032  -0.0507 -0.0145 280 ASN   A OD1 
2194 N ND2 . ASN   A 300 ? 0.6678 0.3901 0.4543 0.0034  -0.0597 -0.0158 280 ASN   A ND2 
2195 N N   . SER   A 301 ? 0.4764 0.2381 0.2845 -0.0018 -0.0241 -0.0098 281 SER   A N   
2196 C CA  . SER   A 301 ? 0.4636 0.2311 0.2766 -0.0034 -0.0185 -0.009  281 SER   A CA  
2197 C C   . SER   A 301 ? 0.4626 0.2396 0.2827 -0.0034 -0.0126 -0.0081 281 SER   A C   
2198 O O   . SER   A 301 ? 0.4665 0.2494 0.2957 -0.0049 -0.0097 -0.0079 281 SER   A O   
2199 C CB  . SER   A 301 ? 0.484  0.2444 0.2839 -0.0023 -0.0155 -0.0081 281 SER   A CB  
2200 O OG  . SER   A 301 ? 0.5026 0.2686 0.3065 -0.0034 -0.0101 -0.0074 281 SER   A OG  
2201 N N   . VAL   A 302 ? 0.4509 0.2281 0.2661 -0.0017 -0.0106 -0.0074 282 VAL   A N   
2202 C CA  . VAL   A 302 ? 0.4381 0.2226 0.2585 -0.0015 -0.0062 -0.0066 282 VAL   A CA  
2203 C C   . VAL   A 302 ? 0.4346 0.2252 0.267  -0.0025 -0.007  -0.0072 282 VAL   A C   
2204 O O   . VAL   A 302 ? 0.4345 0.2294 0.2721 -0.003  -0.0028 -0.0066 282 VAL   A O   
2205 C CB  . VAL   A 302 ? 0.4464 0.2292 0.2606 0.0004  -0.0052 -0.0059 282 VAL   A CB  
2206 C CG1 . VAL   A 302 ? 0.4423 0.2316 0.2622 0.0006  -0.0027 -0.0054 282 VAL   A CG1 
2207 C CG2 . VAL   A 302 ? 0.4696 0.2477 0.2752 0.0014  -0.0021 -0.0048 282 VAL   A CG2 
2208 N N   . PHE   A 303 ? 0.4385 0.2281 0.2748 -0.0023 -0.0124 -0.0082 283 PHE   A N   
2209 C CA  . PHE   A 303 ? 0.4342 0.2298 0.2842 -0.003  -0.0128 -0.0086 283 PHE   A CA  
2210 C C   . PHE   A 303 ? 0.4456 0.2439 0.3058 -0.0051 -0.0109 -0.0087 283 PHE   A C   
2211 O O   . PHE   A 303 ? 0.4489 0.252  0.318  -0.0056 -0.006  -0.0082 283 PHE   A O   
2212 C CB  . PHE   A 303 ? 0.4271 0.2204 0.28   -0.0024 -0.0202 -0.0099 283 PHE   A CB  
2213 C CG  . PHE   A 303 ? 0.4479 0.2411 0.2963 -0.0004 -0.0206 -0.0098 283 PHE   A CG  
2214 C CD1 . PHE   A 303 ? 0.46   0.2487 0.2949 0.001   -0.0188 -0.009  283 PHE   A CD1 
2215 C CD2 . PHE   A 303 ? 0.4477 0.2447 0.306  0.0001  -0.023  -0.0103 283 PHE   A CD2 
2216 C CE1 . PHE   A 303 ? 0.4776 0.2654 0.3085 0.0026  -0.0191 -0.0089 283 PHE   A CE1 
2217 C CE2 . PHE   A 303 ? 0.4557 0.252  0.3091 0.002   -0.0236 -0.0103 283 PHE   A CE2 
2218 C CZ  . PHE   A 303 ? 0.4686 0.2602 0.3081 0.0031  -0.0217 -0.0095 283 PHE   A CZ  
2219 N N   . HIS   A 304 ? 0.4372 0.2309 0.2951 -0.0063 -0.0144 -0.0094 284 HIS   A N   
2220 C CA  . HIS   A 304 ? 0.4563 0.2518 0.3241 -0.0085 -0.0127 -0.0094 284 HIS   A CA  
2221 C C   . HIS   A 304 ? 0.458  0.2552 0.3227 -0.0087 -0.0043 -0.0082 284 HIS   A C   
2222 O O   . HIS   A 304 ? 0.4604 0.2607 0.3349 -0.0098 0.0004  -0.0077 284 HIS   A O   
2223 C CB  . HIS   A 304 ? 0.4899 0.2785 0.3529 -0.0095 -0.0187 -0.0104 284 HIS   A CB  
2224 C CG  . HIS   A 304 ? 0.5476 0.3372 0.4197 -0.012  -0.017  -0.0104 284 HIS   A CG  
2225 N ND1 . HIS   A 304 ? 0.578  0.372  0.469  -0.0139 -0.0187 -0.011  284 HIS   A ND1 
2226 C CD2 . HIS   A 304 ? 0.5865 0.3735 0.4523 -0.0129 -0.013  -0.0098 284 HIS   A CD2 
2227 C CE1 . HIS   A 304 ? 0.5865 0.3799 0.4819 -0.016  -0.0157 -0.0107 284 HIS   A CE1 
2228 N NE2 . HIS   A 304 ? 0.5963 0.3854 0.4759 -0.0154 -0.0122 -0.01   284 HIS   A NE2 
2229 N N   . GLU   A 305 ? 0.4476 0.2418 0.2988 -0.0074 -0.0023 -0.0075 285 GLU   A N   
2230 C CA  . GLU   A 305 ? 0.4512 0.2451 0.2979 -0.0072 0.004   -0.0065 285 GLU   A CA  
2231 C C   . GLU   A 305 ? 0.4491 0.246  0.2987 -0.0062 0.0088  -0.0058 285 GLU   A C   
2232 O O   . GLU   A 305 ? 0.4593 0.2551 0.3096 -0.0064 0.0143  -0.0052 285 GLU   A O   
2233 C CB  . GLU   A 305 ? 0.4787 0.2687 0.3125 -0.0059 0.004   -0.0061 285 GLU   A CB  
2234 C CG  . GLU   A 305 ? 0.4983 0.2832 0.3271 -0.0067 0.001   -0.0066 285 GLU   A CG  
2235 C CD  . GLU   A 305 ? 0.6117 0.3952 0.4438 -0.0086 0.0024  -0.0068 285 GLU   A CD  
2236 O OE1 . GLU   A 305 ? 0.6069 0.3917 0.441  -0.0089 0.0076  -0.0062 285 GLU   A OE1 
2237 O OE2 . GLU   A 305 ? 0.6554 0.4349 0.4869 -0.0097 -0.0018 -0.0075 285 GLU   A OE2 
2238 N N   . ILE   A 306 ? 0.4282 0.2274 0.2785 -0.005  0.0069  -0.0059 286 ILE   A N   
2239 C CA  . ILE   A 306 ? 0.4239 0.2248 0.2761 -0.0038 0.011   -0.0052 286 ILE   A CA  
2240 C C   . ILE   A 306 ? 0.4413 0.2446 0.3064 -0.0047 0.0142  -0.0052 286 ILE   A C   
2241 O O   . ILE   A 306 ? 0.4571 0.2588 0.3224 -0.0041 0.0205  -0.0043 286 ILE   A O   
2242 C CB  . ILE   A 306 ? 0.4246 0.227  0.2743 -0.0023 0.0081  -0.0053 286 ILE   A CB  
2243 C CG1 . ILE   A 306 ? 0.4297 0.2294 0.2685 -0.0014 0.007   -0.0049 286 ILE   A CG1 
2244 C CG2 . ILE   A 306 ? 0.44   0.2435 0.292  -0.001  0.012   -0.0047 286 ILE   A CG2 
2245 C CD1 . ILE   A 306 ? 0.4373 0.2377 0.2732 -0.0001 0.0043  -0.0049 286 ILE   A CD1 
2246 N N   . ASN   A 307 ? 0.4474 0.2537 0.3234 -0.006  0.0097  -0.006  287 ASN   A N   
2247 C CA  . ASN   A 307 ? 0.4567 0.2663 0.3492 -0.0071 0.012   -0.006  287 ASN   A CA  
2248 C C   . ASN   A 307 ? 0.4691 0.2761 0.3635 -0.0085 0.0186  -0.0053 287 ASN   A C   
2249 O O   . ASN   A 307 ? 0.4927 0.2994 0.3931 -0.0082 0.0262  -0.0042 287 ASN   A O   
2250 C CB  . ASN   A 307 ? 0.4822 0.2937 0.3848 -0.0085 0.0037  -0.0074 287 ASN   A CB  
2251 C CG  . ASN   A 307 ? 0.5516 0.3675 0.4755 -0.0098 0.0044  -0.0075 287 ASN   A CG  
2252 O OD1 . ASN   A 307 ? 0.5583 0.3748 0.4906 -0.0109 0.0118  -0.0066 287 ASN   A OD1 
2253 N ND2 . ASN   A 307 ? 0.5831 0.4014 0.5166 -0.0096 -0.0032 -0.0087 287 ASN   A ND2 
2254 N N   . MET   A 308 ? 0.4746 0.2784 0.3625 -0.0098 0.0165  -0.0056 288 MET   A N   
2255 C CA  . MET   A 308 ? 0.4752 0.2758 0.3638 -0.0111 0.0226  -0.005  288 MET   A CA  
2256 C C   . MET   A 308 ? 0.4802 0.2759 0.3572 -0.0092 0.0303  -0.0038 288 MET   A C   
2257 O O   . MET   A 308 ? 0.4895 0.2819 0.3698 -0.0093 0.0382  -0.0029 288 MET   A O   
2258 C CB  . MET   A 308 ? 0.4929 0.2901 0.3734 -0.0124 0.0185  -0.0056 288 MET   A CB  
2259 C CG  . MET   A 308 ? 0.552  0.3503 0.4395 -0.014  0.0101  -0.0069 288 MET   A CG  
2260 S SD  . MET   A 308 ? 0.6421 0.4434 0.5526 -0.0171 0.0104  -0.0072 288 MET   A SD  
2261 C CE  . MET   A 308 ? 0.5674 0.3754 0.4934 -0.0161 0.007   -0.0076 288 MET   A CE  
2262 N N   . TRP   A 309 ? 0.4591 0.2528 0.322  -0.0072 0.028   -0.0038 289 TRP   A N   
2263 C CA  . TRP   A 309 ? 0.4622 0.2494 0.3125 -0.0051 0.033   -0.003  289 TRP   A CA  
2264 C C   . TRP   A 309 ? 0.4703 0.2554 0.3228 -0.0035 0.0392  -0.0021 289 TRP   A C   
2265 O O   . TRP   A 309 ? 0.473  0.2505 0.3196 -0.0025 0.0463  -0.0012 289 TRP   A O   
2266 C CB  . TRP   A 309 ? 0.4538 0.2401 0.2922 -0.0036 0.0281  -0.0033 289 TRP   A CB  
2267 C CG  . TRP   A 309 ? 0.4513 0.2298 0.2764 -0.0017 0.0308  -0.0028 289 TRP   A CG  
2268 C CD1 . TRP   A 309 ? 0.4518 0.2254 0.2686 -0.0015 0.0307  -0.0029 289 TRP   A CD1 
2269 C CD2 . TRP   A 309 ? 0.441  0.2146 0.2589 0.0008  0.0327  -0.0023 289 TRP   A CD2 
2270 N NE1 . TRP   A 309 ? 0.4537 0.2195 0.2589 0.0009  0.0318  -0.0026 289 TRP   A NE1 
2271 C CE2 . TRP   A 309 ? 0.4535 0.2187 0.2585 0.0024  0.0328  -0.0023 289 TRP   A CE2 
2272 C CE3 . TRP   A 309 ? 0.4367 0.2116 0.2571 0.002   0.0336  -0.002  289 TRP   A CE3 
2273 C CZ2 . TRP   A 309 ? 0.4603 0.2169 0.2543 0.0051  0.0335  -0.002  289 TRP   A CZ2 
2274 C CZ3 . TRP   A 309 ? 0.4523 0.2191 0.2614 0.0046  0.0348  -0.0016 289 TRP   A CZ3 
2275 C CH2 . TRP   A 309 ? 0.4718 0.2289 0.2675 0.0062  0.0346  -0.0016 289 TRP   A CH2 
2276 N N   . VAL   A 310 ? 0.4696 0.2602 0.3293 -0.0029 0.0368  -0.0023 290 VAL   A N   
2277 C CA  . VAL   A 310 ? 0.4894 0.2778 0.3516 -0.0012 0.0428  -0.0013 290 VAL   A CA  
2278 C C   . VAL   A 310 ? 0.5027 0.292  0.3801 -0.0024 0.0499  -0.0006 290 VAL   A C   
2279 O O   . VAL   A 310 ? 0.5153 0.2978 0.3901 -0.0008 0.0588  0.0007  290 VAL   A O   
2280 C CB  . VAL   A 310 ? 0.4817 0.276  0.3478 -0.0002 0.0378  -0.0018 290 VAL   A CB  
2281 C CG1 . VAL   A 310 ? 0.4972 0.2901 0.3685 0.0016  0.0441  -0.0008 290 VAL   A CG1 
2282 C CG2 . VAL   A 310 ? 0.4855 0.2775 0.337  0.0011  0.0329  -0.0021 290 VAL   A CG2 
2283 N N   . SER   A 311 ? 0.5073 0.3034 0.4    -0.0052 0.0462  -0.0013 291 SER   A N   
2284 C CA  . SER   A 311 ? 0.5256 0.3233 0.4364 -0.0068 0.0524  -0.0006 291 SER   A CA  
2285 C C   . SER   A 311 ? 0.5358 0.3244 0.4391 -0.0069 0.0617  0.0005  291 SER   A C   
2286 O O   . SER   A 311 ? 0.5558 0.3407 0.4664 -0.0063 0.0718  0.002   291 SER   A O   
2287 C CB  . SER   A 311 ? 0.5344 0.3392 0.4608 -0.0099 0.0446  -0.0019 291 SER   A CB  
2288 O OG  . SER   A 311 ? 0.5794 0.391  0.5149 -0.0096 0.037   -0.0029 291 SER   A OG  
2289 N N   . GLN   A 312 ? 0.5307 0.3147 0.4192 -0.0072 0.0589  0       292 GLN   A N   
2290 C CA  . GLN   A 312 ? 0.544  0.3181 0.4229 -0.0071 0.0666  0.0009  292 GLN   A CA  
2291 C C   . GLN   A 312 ? 0.5656 0.3282 0.4284 -0.0034 0.0745  0.0021  292 GLN   A C   
2292 O O   . GLN   A 312 ? 0.6059 0.358  0.4625 -0.0027 0.0838  0.0032  292 GLN   A O   
2293 C CB  . GLN   A 312 ? 0.5406 0.3127 0.4065 -0.0078 0.0603  -0.0002 292 GLN   A CB  
2294 C CG  . GLN   A 312 ? 0.5798 0.3584 0.4584 -0.0113 0.0548  -0.0011 292 GLN   A CG  
2295 C CD  . GLN   A 312 ? 0.6636 0.4428 0.5312 -0.0116 0.0462  -0.0023 292 GLN   A CD  
2296 O OE1 . GLN   A 312 ? 0.6774 0.4612 0.5525 -0.0138 0.0396  -0.0033 292 GLN   A OE1 
2297 N NE2 . GLN   A 312 ? 0.6923 0.4661 0.5422 -0.0093 0.0457  -0.0022 292 GLN   A NE2 
2298 N N   . ARG   A 313 ? 0.5394 0.3019 0.3934 -0.001  0.0707  0.0019  293 ARG   A N   
2299 C CA  . ARG   A 313 ? 0.5355 0.2856 0.3719 0.0027  0.0759  0.0028  293 ARG   A CA  
2300 C C   . ARG   A 313 ? 0.5678 0.3168 0.4103 0.0047  0.0825  0.004   293 ARG   A C   
2301 O O   . ARG   A 313 ? 0.5676 0.3052 0.394  0.0082  0.0861  0.0047  293 ARG   A O   
2302 C CB  . ARG   A 313 ? 0.5207 0.2689 0.3409 0.0043  0.0671  0.0017  293 ARG   A CB  
2303 C CG  . ARG   A 313 ? 0.5298 0.2743 0.3405 0.0035  0.0638  0.001   293 ARG   A CG  
2304 C CD  . ARG   A 313 ? 0.5342 0.2819 0.3373 0.004   0.0538  -0.0001 293 ARG   A CD  
2305 N NE  . ARG   A 313 ? 0.5277 0.2723 0.3236 0.0033  0.0512  -0.0007 293 ARG   A NE  
2306 C CZ  . ARG   A 313 ? 0.503  0.2546 0.3077 0.0006  0.049   -0.0012 293 ARG   A CZ  
2307 N NH1 . ARG   A 313 ? 0.5076 0.2692 0.3285 -0.0019 0.0483  -0.0013 293 ARG   A NH1 
2308 N NH2 . ARG   A 313 ? 0.522  0.2697 0.3189 0.0004  0.0472  -0.0016 293 ARG   A NH2 
2309 N N   . THR   A 314 ? 0.5886 0.3482 0.4541 0.0027  0.084   0.0042  294 THR   A N   
2310 C CA  . THR   A 314 ? 0.6192 0.3792 0.4948 0.0045  0.0909  0.0054  294 THR   A CA  
2311 C C   . THR   A 314 ? 0.6698 0.432  0.5667 0.0026  0.1003  0.0067  294 THR   A C   
2312 O O   . THR   A 314 ? 0.6783 0.4445 0.5847 -0.0005 0.099   0.0062  294 THR   A O   
2313 C CB  . THR   A 314 ? 0.6129 0.3851 0.4987 0.0042  0.0818  0.0044  294 THR   A CB  
2314 O OG1 . THR   A 314 ? 0.6072 0.3915 0.5088 0.0006  0.0733  0.0029  294 THR   A OG1 
2315 C CG2 . THR   A 314 ? 0.6194 0.3883 0.4859 0.0063  0.0749  0.0036  294 THR   A CG2 
2316 N N   . ALA   A 315 ? 0.7069 0.4656 0.6116 0.0048  0.1107  0.0084  295 ALA   A N   
2317 C CA  . ALA   A 315 ? 0.7416 0.5022 0.6695 0.0033  0.1213  0.01    295 ALA   A CA  
2318 C C   . ALA   A 315 ? 0.759  0.5177 0.696  0.0063  0.1309  0.0118  295 ALA   A C   
2319 O O   . ALA   A 315 ? 0.7848 0.535  0.7029 0.0101  0.1322  0.0122  295 ALA   A O   
2320 C CB  . ALA   A 315 ? 0.764  0.5108 0.681  0.0034  0.1321  0.0113  295 ALA   A CB  
2321 N N1  . A1H35 B .   ? 0.4279 0.2222 0.2945 0.0039  0.011   0.0063  401 A1H35 A N1  
2322 C C7  . A1H35 B .   ? 0.5005 0.2992 0.3929 0.0044  0.0131  0.0081  401 A1H35 A C7  
2323 C C8  . A1H35 B .   ? 0.475  0.2718 0.361  0.0038  0.0133  0.0079  401 A1H35 A C8  
2324 N N2  . A1H35 B .   ? 0.4237 0.2146 0.2696 0.0048  0.0118  0.0048  401 A1H35 A N2  
2325 C C9  . A1H35 B .   ? 0.5089 0.3066 0.4123 0.0033  0.0165  0.0098  401 A1H35 A C9  
2326 C C1  . A1H35 B .   ? 0.6932 0.4998 0.6632 0.0023  -0.0109 0.0092  401 A1H35 A C1  
2327 C C5  . A1H35 B .   ? 0.6006 0.4027 0.5284 0.0042  0.0175  0.0112  401 A1H35 A C5  
2328 C C6  . A1H35 B .   ? 0.5368 0.3374 0.4479 0.0037  0.0126  0.0094  401 A1H35 A C6  
2329 N N3  . A1H35 B .   ? 0.4443 0.2125 0.2464 0.0088  0.0146  0.0026  401 A1H35 A N3  
2330 C C4  . A1H35 B .   ? 0.6728 0.4766 0.6194 0.0031  0.0172  0.0124  401 A1H35 A C4  
2331 C C3  . A1H35 B .   ? 0.6898 0.4962 0.6488 0.0024  0.0074  0.0115  401 A1H35 A C3  
2332 C C2  . A1H35 B .   ? 0.6946 0.5009 0.65   0.003   -0.0026 0.0095  401 A1H35 A C2  
2333 N N4  . A1H35 B .   ? 0.4406 0.2042 0.2308 0.01    0.0074  0.0001  401 A1H35 A N4  
2334 O O   . A1H35 B .   ? 0.3969 0.1921 0.2502 0.0042  0.0034  0.0037  401 A1H35 A O   
2335 C C12 . A1H35 B .   ? 0.4112 0.2053 0.2664 0.0042  0.0085  0.0048  401 A1H35 A C12 
2336 C C23 . A1H35 B .   ? 0.4377 0.2231 0.2793 0.0055  0.0176  0.0058  401 A1H35 A C23 
2337 C C14 . A1H35 B .   ? 0.4257 0.2099 0.2557 0.006   0.0144  0.0042  401 A1H35 A C14 
2338 C C17 . A1H35 B .   ? 0.4301 0.21   0.2508 0.0069  0.0157  0.0037  401 A1H35 A C17 
2339 C C16 . A1H35 B .   ? 0.4401 0.2132 0.2533 0.0078  0.0173  0.004   401 A1H35 A C16 
2340 N N5  . A1H35 B .   ? 0.4305 0.1895 0.2228 0.0101  0.0172  0.0029  401 A1H35 A N5  
2341 C C19 . A1H35 B .   ? 0.4378 0.1937 0.2222 0.0108  0.012   0.0013  401 A1H35 A C19 
2342 C C20 . A1H35 B .   ? 0.4483 0.1923 0.219  0.0126  0.0115  0.0008  401 A1H35 A C20 
2343 C C22 . A1H35 B .   ? 0.4669 0.1983 0.2278 0.0144  0.0185  0.0025  401 A1H35 A C22 
2344 C C21 . A1H35 B .   ? 0.4523 0.1918 0.2196 0.013   0.0149  0.0016  401 A1H35 A C21 
2345 C C18 . A1H35 B .   ? 0.4445 0.2149 0.2443 0.0088  0.0094  0.0011  401 A1H35 A C18 
2346 C C15 . A1H35 B .   ? 0.4246 0.2039 0.2461 0.0067  0.0144  0.0038  401 A1H35 A C15 
2347 C C13 . A1H35 B .   ? 0.4273 0.2175 0.2629 0.0052  0.0095  0.0034  401 A1H35 A C13 
2348 C C10 . A1H35 B .   ? 0.4457 0.2427 0.3239 0.0035  0.0064  0.0063  401 A1H35 A C10 
2349 C C11 . A1H35 B .   ? 0.4543 0.2472 0.3251 0.0044  0.0174  0.0077  401 A1H35 A C11 
2350 C C   . A1H35 B .   ? 0.6962 0.5045 0.6804 0.0009  -0.0058 0.011   401 A1H35 A C   
2351 N N   . A1H35 B .   ? 0.7099 0.5176 0.687  0.0011  0.0057  0.0124  401 A1H35 A N   
2352 C C24 . A1H35 B .   ? 0.7267 0.5281 0.6771 0.0028  0.0262  0.0144  401 A1H35 A C24 
2353 N N6  . A1H35 B .   ? 0.7441 0.5469 0.7124 0.0014  0.0261  0.0156  401 A1H35 A N6  
2354 B B   . A1H35 B .   ? 0.7496 0.5566 0.7356 0.0001  0.0153  0.0147  401 A1H35 A B   
2355 F F1  . A1H35 B .   ? 0.7757 0.5813 0.7589 -0.0012 0.011   0.0141  401 A1H35 A F1  
2356 F F   . A1H35 B .   ? 0.7663 0.5762 0.7776 -0.0002 0.0186  0.0166  401 A1H35 A F   
2357 C C27 . A1H35 B .   ? 0.7511 0.5496 0.7174 0.0015  0.0367  0.0175  401 A1H35 A C27 
2358 C C26 . A1H35 B .   ? 0.7597 0.5529 0.7063 0.0031  0.0427  0.0174  401 A1H35 A C26 
2359 C C25 . A1H35 B .   ? 0.7525 0.5482 0.6902 0.0038  0.036   0.0155  401 A1H35 A C25 
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