data_9F8C
# 
_entry.id   9F8C 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.401 
_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   9F8C         pdb_00009f8c 10.2210/pdb9f8c/pdb 
WWPDB D_1292138404 ?            ?                   
# 
_pdbx_audit_revision_history.ordinal             1 
_pdbx_audit_revision_history.data_content_type   'Structure model' 
_pdbx_audit_revision_history.major_revision      1 
_pdbx_audit_revision_history.minor_revision      0 
_pdbx_audit_revision_history.revision_date       2025-01-22 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        9F8C 
_pdbx_database_status.recvd_initial_deposition_date   2024-05-06 
_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 
'Kuhn, B.'        1  ? 
'Ritter, M.'      2  ? 
'Hornsperger, B.' 3  ? 
'Bell, C.'        4  ? 
'Kocer, B.'       5  ? 
'Rombach, D.'     6  ? 
'Richter, H.'     7  ? 
'Grether, U.'     8  ? 
'Gobbi, L.'       9  ? 
'Kuratli, M.'     10 ? 
'Collin, L.'      11 ? 
'Benz, J.'        12 ? 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   US 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            J.Med.Chem. 
_citation.journal_id_ASTM           JMCMAR 
_citation.journal_id_CSD            0151 
_citation.journal_id_ISSN           0022-2623 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            67 
_citation.language                  ? 
_citation.page_first                18448 
_citation.page_last                 18464 
_citation.title                     
'Structure-Guided Discovery of cis -Hexahydro-pyrido-oxazinones as Reversible, Drug-like Monoacylglycerol Lipase Inhibitors.' 
_citation.year                      2024 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1021/acs.jmedchem.4c01769 
_citation.pdbx_database_id_PubMed   39360636 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Kuhn, B.'          1  0000-0002-4301-562X 
primary 'Ritter, M.'        2  ?                   
primary 'Hornsperger, B.'   3  ?                   
primary 'Bell, C.'          4  ?                   
primary 'Kocer, B.'         5  ?                   
primary 'Rombach, D.'       6  ?                   
primary 'Lutz, M.D.R.'      7  0000-0003-3842-2295 
primary 'Gobbi, L.'         8  0000-0002-0563-2491 
primary 'Kuratli, M.'       9  ?                   
primary 'Bartelmus, C.'     10 0000-0002-1527-4325 
primary 'Burkler, M.'       11 ?                   
primary 'Koller, R.'        12 ?                   
primary 'Tosatti, P.'       13 ?                   
primary 'Ruf, I.'           14 ?                   
primary 'Guerard, M.'       15 ?                   
primary 'Pavlovic, A.'      16 0009-0002-9395-6740 
primary 'Stephanus, J.'     17 ?                   
primary 
;O'Hara, F.
;
18 ?                   
primary 'Wetzl, D.'         19 ?                   
primary 'Saal, W.'          20 ?                   
primary 'Stihle, M.'        21 ?                   
primary 'Roth, D.'          22 ?                   
primary 'Hug, M.'           23 ?                   
primary 'Huber, S.'         24 ?                   
primary 'Heer, D.'          25 0009-0003-2089-4339 
primary 'Kroll, C.'         26 0009-0005-8255-326X 
primary 'Topp, A.'          27 ?                   
primary 'Schneider, M.'     28 ?                   
primary 'Gertsch, J.'       29 0000-0003-0978-1555 
primary 'Glasmacher, S.'    30 ?                   
primary 'van der Stelt, M.' 31 0000-0002-1029-5717 
primary 'Martella, A.'      32 ?                   
primary 'Wittwer, M.B.'     33 0000-0003-1359-4795 
primary 'Collin, L.'        34 ?                   
primary 'Benz, J.'          35 ?                   
primary 'Richter, H.'       36 ?                   
primary 'Grether, U.'       37 0000-0002-3164-9270 
# 
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 
;(4~{a}~{R},8~{a}~{R})-6-[4-[[4-(trifluoromethyl)phenyl]methyl]piperidin-1-yl]carbonyl-4,4~{a},5,7,8,8~{a}-hexahydropyrido[4,3-b][1,4]oxazin-3-one
;
425.445   1   ?        ? ? ? 
3 non-polymer syn 'SODIUM ION' 22.990    2   ?        ? ? ? 
4 non-polymer syn 1,2-ETHANEDIOL 62.068    2   ?        ? ? ? 
5 water       nat water 18.015    360 ?        ? ? ? 
# 
_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 
;(4~{a}~{R},8~{a}~{R})-6-[4-[[4-(trifluoromethyl)phenyl]methyl]piperidin-1-yl]carbonyl-4,4~{a},5,7,8,8~{a}-hexahydropyrido[4,3-b][1,4]oxazin-3-one
;
A1IA2 
3 'SODIUM ION' NA    
4 1,2-ETHANEDIOL EDO   
5 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 
A1IA2 non-polymer         . 
;(4~{a}~{R},8~{a}~{R})-6-[4-[[4-(trifluoromethyl)phenyl]methyl]piperidin-1-yl]carbonyl-4,4~{a},5,7,8,8~{a}-hexahydropyrido[4,3-b][1,4]oxazin-3-one
;
?                 'C21 H26 F3 N3 O3' 425.445 
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 
NA    non-polymer         . 'SODIUM ION' ?                 'Na 1'             22.990  
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   1   MET MET A . n 
A 1 22  PRO 22  2   2   PRO PRO A . n 
A 1 23  GLU 23  3   3   GLU GLU A . n 
A 1 24  GLU 24  4   4   GLU GLU A . n 
A 1 25  SER 25  5   5   SER SER 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        A1IA2 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1IA2 
_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 A1IA2 1   401 1   A1IA2 XXX A . 
C 3 NA    1   402 2   NA    NA  A . 
D 3 NA    1   403 3   NA    NA  A . 
E 4 EDO   1   404 1   EDO   EDO A . 
F 4 EDO   1   405 2   EDO   EDO A . 
G 5 HOH   1   501 411 HOH   HOH A . 
G 5 HOH   2   502 425 HOH   HOH A . 
G 5 HOH   3   503 3   HOH   HOH A . 
G 5 HOH   4   504 412 HOH   HOH A . 
G 5 HOH   5   505 216 HOH   HOH A . 
G 5 HOH   6   506 217 HOH   HOH A . 
G 5 HOH   7   507 362 HOH   HOH A . 
G 5 HOH   8   508 269 HOH   HOH A . 
G 5 HOH   9   509 255 HOH   HOH A . 
G 5 HOH   10  510 155 HOH   HOH A . 
G 5 HOH   11  511 141 HOH   HOH A . 
G 5 HOH   12  512 205 HOH   HOH A . 
G 5 HOH   13  513 132 HOH   HOH A . 
G 5 HOH   14  514 272 HOH   HOH A . 
G 5 HOH   15  515 226 HOH   HOH A . 
G 5 HOH   16  516 146 HOH   HOH A . 
G 5 HOH   17  517 203 HOH   HOH A . 
G 5 HOH   18  518 185 HOH   HOH A . 
G 5 HOH   19  519 157 HOH   HOH A . 
G 5 HOH   20  520 303 HOH   HOH A . 
G 5 HOH   21  521 9   HOH   HOH A . 
G 5 HOH   22  522 6   HOH   HOH A . 
G 5 HOH   23  523 149 HOH   HOH A . 
G 5 HOH   24  524 414 HOH   HOH A . 
G 5 HOH   25  525 250 HOH   HOH A . 
G 5 HOH   26  526 417 HOH   HOH A . 
G 5 HOH   27  527 147 HOH   HOH A . 
G 5 HOH   28  528 190 HOH   HOH A . 
G 5 HOH   29  529 188 HOH   HOH A . 
G 5 HOH   30  530 382 HOH   HOH A . 
G 5 HOH   31  531 88  HOH   HOH A . 
G 5 HOH   32  532 176 HOH   HOH A . 
G 5 HOH   33  533 128 HOH   HOH A . 
G 5 HOH   34  534 345 HOH   HOH A . 
G 5 HOH   35  535 160 HOH   HOH A . 
G 5 HOH   36  536 5   HOH   HOH A . 
G 5 HOH   37  537 156 HOH   HOH A . 
G 5 HOH   38  538 127 HOH   HOH A . 
G 5 HOH   39  539 158 HOH   HOH A . 
G 5 HOH   40  540 46  HOH   HOH A . 
G 5 HOH   41  541 150 HOH   HOH A . 
G 5 HOH   42  542 257 HOH   HOH A . 
G 5 HOH   43  543 135 HOH   HOH A . 
G 5 HOH   44  544 13  HOH   HOH A . 
G 5 HOH   45  545 308 HOH   HOH A . 
G 5 HOH   46  546 238 HOH   HOH A . 
G 5 HOH   47  547 174 HOH   HOH A . 
G 5 HOH   48  548 144 HOH   HOH A . 
G 5 HOH   49  549 304 HOH   HOH A . 
G 5 HOH   50  550 23  HOH   HOH A . 
G 5 HOH   51  551 84  HOH   HOH A . 
G 5 HOH   52  552 266 HOH   HOH A . 
G 5 HOH   53  553 397 HOH   HOH A . 
G 5 HOH   54  554 2   HOH   HOH A . 
G 5 HOH   55  555 136 HOH   HOH A . 
G 5 HOH   56  556 218 HOH   HOH A . 
G 5 HOH   57  557 305 HOH   HOH A . 
G 5 HOH   58  558 212 HOH   HOH A . 
G 5 HOH   59  559 422 HOH   HOH A . 
G 5 HOH   60  560 234 HOH   HOH A . 
G 5 HOH   61  561 296 HOH   HOH A . 
G 5 HOH   62  562 126 HOH   HOH A . 
G 5 HOH   63  563 24  HOH   HOH A . 
G 5 HOH   64  564 129 HOH   HOH A . 
G 5 HOH   65  565 210 HOH   HOH A . 
G 5 HOH   66  566 193 HOH   HOH A . 
G 5 HOH   67  567 287 HOH   HOH A . 
G 5 HOH   68  568 213 HOH   HOH A . 
G 5 HOH   69  569 192 HOH   HOH A . 
G 5 HOH   70  570 202 HOH   HOH A . 
G 5 HOH   71  571 143 HOH   HOH A . 
G 5 HOH   72  572 49  HOH   HOH A . 
G 5 HOH   73  573 222 HOH   HOH A . 
G 5 HOH   74  574 294 HOH   HOH A . 
G 5 HOH   75  575 153 HOH   HOH A . 
G 5 HOH   76  576 196 HOH   HOH A . 
G 5 HOH   77  577 74  HOH   HOH A . 
G 5 HOH   78  578 145 HOH   HOH A . 
G 5 HOH   79  579 134 HOH   HOH A . 
G 5 HOH   80  580 307 HOH   HOH A . 
G 5 HOH   81  581 431 HOH   HOH A . 
G 5 HOH   82  582 276 HOH   HOH A . 
G 5 HOH   83  583 403 HOH   HOH A . 
G 5 HOH   84  584 140 HOH   HOH A . 
G 5 HOH   85  585 223 HOH   HOH A . 
G 5 HOH   86  586 233 HOH   HOH A . 
G 5 HOH   87  587 194 HOH   HOH A . 
G 5 HOH   88  588 186 HOH   HOH A . 
G 5 HOH   89  589 56  HOH   HOH A . 
G 5 HOH   90  590 1   HOH   HOH A . 
G 5 HOH   91  591 426 HOH   HOH A . 
G 5 HOH   92  592 130 HOH   HOH A . 
G 5 HOH   93  593 191 HOH   HOH A . 
G 5 HOH   94  594 368 HOH   HOH A . 
G 5 HOH   95  595 200 HOH   HOH A . 
G 5 HOH   96  596 243 HOH   HOH A . 
G 5 HOH   97  597 182 HOH   HOH A . 
G 5 HOH   98  598 70  HOH   HOH A . 
G 5 HOH   99  599 69  HOH   HOH A . 
G 5 HOH   100 600 370 HOH   HOH A . 
G 5 HOH   101 601 312 HOH   HOH A . 
G 5 HOH   102 602 169 HOH   HOH A . 
G 5 HOH   103 603 207 HOH   HOH A . 
G 5 HOH   104 604 85  HOH   HOH A . 
G 5 HOH   105 605 103 HOH   HOH A . 
G 5 HOH   106 606 246 HOH   HOH A . 
G 5 HOH   107 607 63  HOH   HOH A . 
G 5 HOH   108 608 302 HOH   HOH A . 
G 5 HOH   109 609 281 HOH   HOH A . 
G 5 HOH   110 610 177 HOH   HOH A . 
G 5 HOH   111 611 291 HOH   HOH A . 
G 5 HOH   112 612 95  HOH   HOH A . 
G 5 HOH   113 613 168 HOH   HOH A . 
G 5 HOH   114 614 90  HOH   HOH A . 
G 5 HOH   115 615 235 HOH   HOH A . 
G 5 HOH   116 616 316 HOH   HOH A . 
G 5 HOH   117 617 51  HOH   HOH A . 
G 5 HOH   118 618 421 HOH   HOH A . 
G 5 HOH   119 619 259 HOH   HOH A . 
G 5 HOH   120 620 66  HOH   HOH A . 
G 5 HOH   121 621 245 HOH   HOH A . 
G 5 HOH   122 622 152 HOH   HOH A . 
G 5 HOH   123 623 317 HOH   HOH A . 
G 5 HOH   124 624 289 HOH   HOH A . 
G 5 HOH   125 625 8   HOH   HOH A . 
G 5 HOH   126 626 263 HOH   HOH A . 
G 5 HOH   127 627 179 HOH   HOH A . 
G 5 HOH   128 628 242 HOH   HOH A . 
G 5 HOH   129 629 265 HOH   HOH A . 
G 5 HOH   130 630 404 HOH   HOH A . 
G 5 HOH   131 631 240 HOH   HOH A . 
G 5 HOH   132 632 10  HOH   HOH A . 
G 5 HOH   133 633 401 HOH   HOH A . 
G 5 HOH   134 634 197 HOH   HOH A . 
G 5 HOH   135 635 427 HOH   HOH A . 
G 5 HOH   136 636 346 HOH   HOH A . 
G 5 HOH   137 637 254 HOH   HOH A . 
G 5 HOH   138 638 309 HOH   HOH A . 
G 5 HOH   139 639 55  HOH   HOH A . 
G 5 HOH   140 640 409 HOH   HOH A . 
G 5 HOH   141 641 159 HOH   HOH A . 
G 5 HOH   142 642 167 HOH   HOH A . 
G 5 HOH   143 643 224 HOH   HOH A . 
G 5 HOH   144 644 148 HOH   HOH A . 
G 5 HOH   145 645 413 HOH   HOH A . 
G 5 HOH   146 646 38  HOH   HOH A . 
G 5 HOH   147 647 232 HOH   HOH A . 
G 5 HOH   148 648 249 HOH   HOH A . 
G 5 HOH   149 649 237 HOH   HOH A . 
G 5 HOH   150 650 247 HOH   HOH A . 
G 5 HOH   151 651 274 HOH   HOH A . 
G 5 HOH   152 652 131 HOH   HOH A . 
G 5 HOH   153 653 189 HOH   HOH A . 
G 5 HOH   154 654 329 HOH   HOH A . 
G 5 HOH   155 655 22  HOH   HOH A . 
G 5 HOH   156 656 139 HOH   HOH A . 
G 5 HOH   157 657 7   HOH   HOH A . 
G 5 HOH   158 658 301 HOH   HOH A . 
G 5 HOH   159 659 295 HOH   HOH A . 
G 5 HOH   160 660 284 HOH   HOH A . 
G 5 HOH   161 661 330 HOH   HOH A . 
G 5 HOH   162 662 377 HOH   HOH A . 
G 5 HOH   163 663 11  HOH   HOH A . 
G 5 HOH   164 664 311 HOH   HOH A . 
G 5 HOH   165 665 418 HOH   HOH A . 
G 5 HOH   166 666 282 HOH   HOH A . 
G 5 HOH   167 667 318 HOH   HOH A . 
G 5 HOH   168 668 151 HOH   HOH A . 
G 5 HOH   169 669 25  HOH   HOH A . 
G 5 HOH   170 670 199 HOH   HOH A . 
G 5 HOH   171 671 292 HOH   HOH A . 
G 5 HOH   172 672 16  HOH   HOH A . 
G 5 HOH   173 673 142 HOH   HOH A . 
G 5 HOH   174 674 372 HOH   HOH A . 
G 5 HOH   175 675 40  HOH   HOH A . 
G 5 HOH   176 676 91  HOH   HOH A . 
G 5 HOH   177 677 21  HOH   HOH A . 
G 5 HOH   178 678 119 HOH   HOH A . 
G 5 HOH   179 679 278 HOH   HOH A . 
G 5 HOH   180 680 187 HOH   HOH A . 
G 5 HOH   181 681 410 HOH   HOH A . 
G 5 HOH   182 682 394 HOH   HOH A . 
G 5 HOH   183 683 61  HOH   HOH A . 
G 5 HOH   184 684 47  HOH   HOH A . 
G 5 HOH   185 685 181 HOH   HOH A . 
G 5 HOH   186 686 204 HOH   HOH A . 
G 5 HOH   187 687 271 HOH   HOH A . 
G 5 HOH   188 688 172 HOH   HOH A . 
G 5 HOH   189 689 67  HOH   HOH A . 
G 5 HOH   190 690 262 HOH   HOH A . 
G 5 HOH   191 691 154 HOH   HOH A . 
G 5 HOH   192 692 112 HOH   HOH A . 
G 5 HOH   193 693 244 HOH   HOH A . 
G 5 HOH   194 694 211 HOH   HOH A . 
G 5 HOH   195 695 297 HOH   HOH A . 
G 5 HOH   196 696 428 HOH   HOH A . 
G 5 HOH   197 697 175 HOH   HOH A . 
G 5 HOH   198 698 201 HOH   HOH A . 
G 5 HOH   199 699 285 HOH   HOH A . 
G 5 HOH   200 700 342 HOH   HOH A . 
G 5 HOH   201 701 268 HOH   HOH A . 
G 5 HOH   202 702 260 HOH   HOH A . 
G 5 HOH   203 703 350 HOH   HOH A . 
G 5 HOH   204 704 267 HOH   HOH A . 
G 5 HOH   205 705 220 HOH   HOH A . 
G 5 HOH   206 706 319 HOH   HOH A . 
G 5 HOH   207 707 369 HOH   HOH A . 
G 5 HOH   208 708 124 HOH   HOH A . 
G 5 HOH   209 709 87  HOH   HOH A . 
G 5 HOH   210 710 273 HOH   HOH A . 
G 5 HOH   211 711 229 HOH   HOH A . 
G 5 HOH   212 712 373 HOH   HOH A . 
G 5 HOH   213 713 383 HOH   HOH A . 
G 5 HOH   214 714 432 HOH   HOH A . 
G 5 HOH   215 715 164 HOH   HOH A . 
G 5 HOH   216 716 26  HOH   HOH A . 
G 5 HOH   217 717 183 HOH   HOH A . 
G 5 HOH   218 718 264 HOH   HOH A . 
G 5 HOH   219 719 50  HOH   HOH A . 
G 5 HOH   220 720 37  HOH   HOH A . 
G 5 HOH   221 721 331 HOH   HOH A . 
G 5 HOH   222 722 18  HOH   HOH A . 
G 5 HOH   223 723 219 HOH   HOH A . 
G 5 HOH   224 724 288 HOH   HOH A . 
G 5 HOH   225 725 75  HOH   HOH A . 
G 5 HOH   226 726 338 HOH   HOH A . 
G 5 HOH   227 727 73  HOH   HOH A . 
G 5 HOH   228 728 58  HOH   HOH A . 
G 5 HOH   229 729 390 HOH   HOH A . 
G 5 HOH   230 730 14  HOH   HOH A . 
G 5 HOH   231 731 236 HOH   HOH A . 
G 5 HOH   232 732 398 HOH   HOH A . 
G 5 HOH   233 733 399 HOH   HOH A . 
G 5 HOH   234 734 125 HOH   HOH A . 
G 5 HOH   235 735 99  HOH   HOH A . 
G 5 HOH   236 736 391 HOH   HOH A . 
G 5 HOH   237 737 12  HOH   HOH A . 
G 5 HOH   238 738 15  HOH   HOH A . 
G 5 HOH   239 739 101 HOH   HOH A . 
G 5 HOH   240 740 343 HOH   HOH A . 
G 5 HOH   241 741 113 HOH   HOH A . 
G 5 HOH   242 742 314 HOH   HOH A . 
G 5 HOH   243 743 313 HOH   HOH A . 
G 5 HOH   244 744 59  HOH   HOH A . 
G 5 HOH   245 745 334 HOH   HOH A . 
G 5 HOH   246 746 118 HOH   HOH A . 
G 5 HOH   247 747 80  HOH   HOH A . 
G 5 HOH   248 748 225 HOH   HOH A . 
G 5 HOH   249 749 430 HOH   HOH A . 
G 5 HOH   250 750 253 HOH   HOH A . 
G 5 HOH   251 751 27  HOH   HOH A . 
G 5 HOH   252 752 114 HOH   HOH A . 
G 5 HOH   253 753 325 HOH   HOH A . 
G 5 HOH   254 754 93  HOH   HOH A . 
G 5 HOH   255 755 64  HOH   HOH A . 
G 5 HOH   256 756 29  HOH   HOH A . 
G 5 HOH   257 757 344 HOH   HOH A . 
G 5 HOH   258 758 121 HOH   HOH A . 
G 5 HOH   259 759 251 HOH   HOH A . 
G 5 HOH   260 760 387 HOH   HOH A . 
G 5 HOH   261 761 117 HOH   HOH A . 
G 5 HOH   262 762 221 HOH   HOH A . 
G 5 HOH   263 763 326 HOH   HOH A . 
G 5 HOH   264 764 376 HOH   HOH A . 
G 5 HOH   265 765 275 HOH   HOH A . 
G 5 HOH   266 766 97  HOH   HOH A . 
G 5 HOH   267 767 378 HOH   HOH A . 
G 5 HOH   268 768 315 HOH   HOH A . 
G 5 HOH   269 769 100 HOH   HOH A . 
G 5 HOH   270 770 355 HOH   HOH A . 
G 5 HOH   271 771 337 HOH   HOH A . 
G 5 HOH   272 772 405 HOH   HOH A . 
G 5 HOH   273 773 52  HOH   HOH A . 
G 5 HOH   274 774 17  HOH   HOH A . 
G 5 HOH   275 775 111 HOH   HOH A . 
G 5 HOH   276 776 89  HOH   HOH A . 
G 5 HOH   277 777 300 HOH   HOH A . 
G 5 HOH   278 778 35  HOH   HOH A . 
G 5 HOH   279 779 241 HOH   HOH A . 
G 5 HOH   280 780 102 HOH   HOH A . 
G 5 HOH   281 781 359 HOH   HOH A . 
G 5 HOH   282 782 123 HOH   HOH A . 
G 5 HOH   283 783 86  HOH   HOH A . 
G 5 HOH   284 784 380 HOH   HOH A . 
G 5 HOH   285 785 34  HOH   HOH A . 
G 5 HOH   286 786 62  HOH   HOH A . 
G 5 HOH   287 787 65  HOH   HOH A . 
G 5 HOH   288 788 230 HOH   HOH A . 
G 5 HOH   289 789 41  HOH   HOH A . 
G 5 HOH   290 790 28  HOH   HOH A . 
G 5 HOH   291 791 106 HOH   HOH A . 
G 5 HOH   292 792 120 HOH   HOH A . 
G 5 HOH   293 793 60  HOH   HOH A . 
G 5 HOH   294 794 270 HOH   HOH A . 
G 5 HOH   295 795 32  HOH   HOH A . 
G 5 HOH   296 796 306 HOH   HOH A . 
G 5 HOH   297 797 214 HOH   HOH A . 
G 5 HOH   298 798 423 HOH   HOH A . 
G 5 HOH   299 799 171 HOH   HOH A . 
G 5 HOH   300 800 45  HOH   HOH A . 
G 5 HOH   301 801 104 HOH   HOH A . 
G 5 HOH   302 802 321 HOH   HOH A . 
G 5 HOH   303 803 54  HOH   HOH A . 
G 5 HOH   304 804 363 HOH   HOH A . 
G 5 HOH   305 805 83  HOH   HOH A . 
G 5 HOH   306 806 339 HOH   HOH A . 
G 5 HOH   307 807 333 HOH   HOH A . 
G 5 HOH   308 808 53  HOH   HOH A . 
G 5 HOH   309 809 279 HOH   HOH A . 
G 5 HOH   310 810 19  HOH   HOH A . 
G 5 HOH   311 811 92  HOH   HOH A . 
G 5 HOH   312 812 77  HOH   HOH A . 
G 5 HOH   313 813 198 HOH   HOH A . 
G 5 HOH   314 814 20  HOH   HOH A . 
G 5 HOH   315 815 361 HOH   HOH A . 
G 5 HOH   316 816 385 HOH   HOH A . 
G 5 HOH   317 817 341 HOH   HOH A . 
G 5 HOH   318 818 107 HOH   HOH A . 
G 5 HOH   319 819 98  HOH   HOH A . 
G 5 HOH   320 820 39  HOH   HOH A . 
G 5 HOH   321 821 356 HOH   HOH A . 
G 5 HOH   322 822 81  HOH   HOH A . 
G 5 HOH   323 823 393 HOH   HOH A . 
G 5 HOH   324 824 43  HOH   HOH A . 
G 5 HOH   325 825 375 HOH   HOH A . 
G 5 HOH   326 826 371 HOH   HOH A . 
G 5 HOH   327 827 72  HOH   HOH A . 
G 5 HOH   328 828 429 HOH   HOH A . 
G 5 HOH   329 829 239 HOH   HOH A . 
G 5 HOH   330 830 248 HOH   HOH A . 
G 5 HOH   331 831 78  HOH   HOH A . 
G 5 HOH   332 832 424 HOH   HOH A . 
G 5 HOH   333 833 310 HOH   HOH A . 
G 5 HOH   334 834 335 HOH   HOH A . 
G 5 HOH   335 835 258 HOH   HOH A . 
G 5 HOH   336 836 298 HOH   HOH A . 
G 5 HOH   337 837 347 HOH   HOH A . 
G 5 HOH   338 838 386 HOH   HOH A . 
G 5 HOH   339 839 48  HOH   HOH A . 
G 5 HOH   340 840 76  HOH   HOH A . 
G 5 HOH   341 841 105 HOH   HOH A . 
G 5 HOH   342 842 36  HOH   HOH A . 
G 5 HOH   343 843 358 HOH   HOH A . 
G 5 HOH   344 844 79  HOH   HOH A . 
G 5 HOH   345 845 360 HOH   HOH A . 
G 5 HOH   346 846 166 HOH   HOH A . 
G 5 HOH   347 847 115 HOH   HOH A . 
G 5 HOH   348 848 384 HOH   HOH A . 
G 5 HOH   349 849 416 HOH   HOH A . 
G 5 HOH   350 850 42  HOH   HOH A . 
G 5 HOH   351 851 31  HOH   HOH A . 
G 5 HOH   352 852 122 HOH   HOH A . 
G 5 HOH   353 853 116 HOH   HOH A . 
G 5 HOH   354 854 108 HOH   HOH A . 
G 5 HOH   355 855 389 HOH   HOH A . 
G 5 HOH   356 856 96  HOH   HOH A . 
G 5 HOH   357 857 71  HOH   HOH A . 
G 5 HOH   358 858 68  HOH   HOH A . 
G 5 HOH   359 859 94  HOH   HOH A . 
G 5 HOH   360 860 44  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 ? ? ? '2.11.7 (19-MAR-2020)' 1 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? SADABS ? ? ? .                      2 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? XDS    ? ? ? .                      3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHASER ? ? ? .                      4 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.00 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9F8C 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     89.991 
_cell.length_a_esd                 ? 
_cell.length_b                     127.429 
_cell.length_b_esd                 ? 
_cell.length_c                     62.593 
_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                         9F8C 
_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                   9F8C 
_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             2.53 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          51.38 
_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    
;0.1 M MES pH 6.5 
6 %w/v PEG MME 5K 
12 %v/v iso-propanol
;
_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 PILATUS 6M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2017-10-14 
_diffrn_detector.pdbx_frequency               ? 
_diffrn_detector.id                           ? 
_diffrn_detector.number_of_axes               ? 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.99996 
_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        0.99996 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   X10SA 
_diffrn_source.pdbx_synchrotron_site       SLS 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       9F8C 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.52 
_reflns.d_resolution_low                               73.51 
_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                                     55359 
_reflns.observed_criterion                             ? 
_reflns.observed_criterion_F_max                       ? 
_reflns.observed_criterion_F_min                       ? 
_reflns.observed_criterion_I_max                       ? 
_reflns.observed_criterion_I_min                       ? 
_reflns.observed_criterion_sigma_F                     ? 
_reflns.observed_criterion_sigma_I                     ? 
_reflns.percent_possible_obs                           99.4 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                7.31 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          9.46 
_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                                   0.999 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.08 
_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                                    1.52 
_reflns_shell.d_res_low                                     1.62 
_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                             9371 
_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                                  0.603 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          ? 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  0.89 
_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]                            -7.52050 
_refine.aniso_B[1][2]                            0.00000 
_refine.aniso_B[1][3]                            0.00000 
_refine.aniso_B[2][2]                            5.34110 
_refine.aniso_B[2][3]                            0.00000 
_refine.aniso_B[3][3]                            2.17940 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               33.86 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               0.961 
_refine.correlation_coeff_Fo_to_Fc_free          0.953 
_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                                 9F8C 
_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                            1.520 
_refine.ls_d_res_low                             73.51 
_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                     55316 
_refine.ls_number_reflns_R_free                  2748 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.4 
_refine.ls_percent_reflns_R_free                 4.970 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1802 
_refine.ls_R_factor_R_free                       0.1957 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1793 
_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                          0.000 
_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   0.066 
_refine.pdbx_overall_SU_R_free_Blow_DPI          0.070 
_refine.pdbx_overall_SU_R_Blow_DPI               0.073 
_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             0.068 
_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                        9F8C 
_refine_analyze.pdbx_refine_id                  'X-RAY DIFFRACTION' 
_refine_analyze.Luzzati_coordinate_error_free   ? 
_refine_analyze.Luzzati_coordinate_error_obs    0.22 
_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                         1 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       1.520 
_refine_hist.d_res_low                        73.51 
_refine_hist.number_atoms_solvent             360 
_refine_hist.number_atoms_total               2683 
_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        2283 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         40 
_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' ? 0.008 ? 2449 ? t_bond_d                  2.00  HARMONIC     
'X-RAY DIFFRACTION' ? 0.93  ? 3349 ? t_angle_deg               2.00  HARMONIC     
'X-RAY DIFFRACTION' ? ?     ? 866  ? t_dihedral_angle_d        2.00  SINUSOIDAL   
'X-RAY DIFFRACTION' ? ?     ? ?    ? t_incorr_chiral_ct        ?     ?            
'X-RAY DIFFRACTION' ? ?     ? ?    ? t_pseud_angle             ?     ?            
'X-RAY DIFFRACTION' ? ?     ? ?    ? t_trig_c_planes           ?     ?            
'X-RAY DIFFRACTION' ? ?     ? 431  ? t_gen_planes              5.00  HARMONIC     
'X-RAY DIFFRACTION' ? ?     ? 2449 ? t_it                      10.00 HARMONIC     
'X-RAY DIFFRACTION' ? ?     ? ?    ? t_nbd                     ?     ?            
'X-RAY DIFFRACTION' ? 3.34  ? ?    ? t_omega_torsion           ?     ?            
'X-RAY DIFFRACTION' ? 14.87 ? ?    ? t_other_torsion           ?     ?            
'X-RAY DIFFRACTION' ? ?     ? ?    ? t_improper_torsion        ?     ?            
'X-RAY DIFFRACTION' ? ?     ? 312  ? t_chiral_improper_torsion 5.00  SEMIHARMONIC 
'X-RAY DIFFRACTION' ? ?     ? ?    ? t_sum_occupancies         ?     ?            
'X-RAY DIFFRACTION' ? ?     ? ?    ? t_utility_distance        ?     ?            
'X-RAY DIFFRACTION' ? ?     ? ?    ? t_utility_angle           ?     ?            
'X-RAY DIFFRACTION' ? ?     ? ?    ? t_utility_torsion         ?     ?            
'X-RAY DIFFRACTION' ? ?     ? 2559 ? t_ideal_dist_contact      4.00  SEMIHARMONIC 
# 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.d_res_high                       1.52 
_refine_ls_shell.d_res_low                        1.53 
_refine_ls_shell.number_reflns_all                1107 
_refine_ls_shell.number_reflns_obs                ? 
_refine_ls_shell.number_reflns_R_free             ? 
_refine_ls_shell.number_reflns_R_work             1059 
_refine_ls_shell.percent_reflns_obs               91.35 
_refine_ls_shell.percent_reflns_R_free            4.34 
_refine_ls_shell.R_factor_all                     0.2769 
_refine_ls_shell.R_factor_obs                     ? 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.R_factor_R_work                  0.2772 
_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   51 
_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                  0.2711 
# 
_struct.entry_id                     9F8C 
_struct.title                        'Crystal structure of human monoacylglycerol lipase in complex with compound 7m' 
_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        9F8C 
_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 4 ? 
F N N 4 ? 
G N N 5 ? 
# 
_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              9F8C 
_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 9F8C MET A 1   ? UNP Q99685 ?   ?   'initiating methionine' -19 1  
1 9F8C GLY A 2   ? UNP Q99685 ?   ?   'expression tag'        -18 2  
1 9F8C SER A 3   ? UNP Q99685 ?   ?   'expression tag'        -17 3  
1 9F8C SER A 4   ? UNP Q99685 ?   ?   'expression tag'        -16 4  
1 9F8C HIS A 5   ? UNP Q99685 ?   ?   'expression tag'        -15 5  
1 9F8C HIS A 6   ? UNP Q99685 ?   ?   'expression tag'        -14 6  
1 9F8C HIS A 7   ? UNP Q99685 ?   ?   'expression tag'        -13 7  
1 9F8C HIS A 8   ? UNP Q99685 ?   ?   'expression tag'        -12 8  
1 9F8C HIS A 9   ? UNP Q99685 ?   ?   'expression tag'        -11 9  
1 9F8C HIS A 10  ? UNP Q99685 ?   ?   'expression tag'        -10 10 
1 9F8C SER A 11  ? UNP Q99685 ?   ?   'expression tag'        -9  11 
1 9F8C SER A 12  ? UNP Q99685 ?   ?   'expression tag'        -8  12 
1 9F8C GLY A 13  ? UNP Q99685 ?   ?   'expression tag'        -7  13 
1 9F8C GLU A 14  ? UNP Q99685 ?   ?   'expression tag'        -6  14 
1 9F8C ASN A 15  ? UNP Q99685 ?   ?   'expression tag'        -5  15 
1 9F8C LEU A 16  ? UNP Q99685 ?   ?   'expression tag'        -4  16 
1 9F8C TYR A 17  ? UNP Q99685 ?   ?   'expression tag'        -3  17 
1 9F8C PHE A 18  ? UNP Q99685 ?   ?   'expression tag'        -2  18 
1 9F8C GLN A 19  ? UNP Q99685 ?   ?   'expression tag'        -1  19 
1 9F8C GLY A 20  ? UNP Q99685 ?   ?   'expression tag'        0   20 
1 9F8C ALA A 56  ? UNP Q99685 LYS 36  'engineered mutation'   36  21 
1 9F8C SER A 189 ? UNP Q99685 LEU 169 'engineered mutation'   169 22 
1 9F8C SER A 196 ? UNP Q99685 LEU 176 'engineered mutation'   176 23 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_defined_assembly 
_pdbx_struct_assembly.method_details       ? 
_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,G 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   'gel filtration' 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 PRO A 35  ? LEU A 39  ? PRO A 15  LEU A 19  5 ? 5  
HELX_P HELX_P2  AA2 HIS A 74  ? ARG A 77  ? HIS A 54  ARG A 57  5 ? 4  
HELX_P HELX_P3  AA3 TYR A 78  ? LEU A 88  ? TYR A 58  LEU A 68  1 ? 11 
HELX_P HELX_P4  AA4 PHE A 113 ? TYR A 131 ? PHE A 93  TYR A 111 1 ? 19 
HELX_P HELX_P5  AA5 SER A 142 ? ARG A 155 ? SER A 122 ARG A 135 1 ? 14 
HELX_P HELX_P6  AA6 ASN A 172 ? SER A 189 ? ASN A 152 SER A 169 1 ? 18 
HELX_P HELX_P7  AA7 ASP A 200 ? LEU A 204 ? ASP A 180 LEU A 184 5 ? 5  
HELX_P HELX_P8  AA8 ASN A 207 ? ASP A 217 ? ASN A 187 ASP A 197 1 ? 11 
HELX_P HELX_P9  AA9 LYS A 226 ? LEU A 244 ? LYS A 206 LEU A 224 1 ? 19 
HELX_P HELX_P10 AB1 PRO A 245 ? LEU A 247 ? PRO A 225 LEU A 227 5 ? 3  
HELX_P HELX_P11 AB2 ASP A 263 ? ALA A 274 ? ASP A 243 ALA A 254 1 ? 12 
HELX_P HELX_P12 AB3 VAL A 290 ? GLU A 294 ? VAL A 270 GLU A 274 5 ? 5  
HELX_P HELX_P13 AB4 LEU A 295 ? 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   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
metalc1 metalc ? ? A PRO 132 O  ? ? ? 1_555 D NA  . NA ? ? A PRO 112 A NA  403 1_555 ? ? ? ? ? ? ? 2.239 ? ? 
metalc2 metalc ? ? C NA  .   NA ? ? ? 1_555 G HOH . O  ? ? A NA  402 A HOH 633 1_555 ? ? ? ? ? ? ? 2.391 ? ? 
metalc3 metalc ? ? C NA  .   NA ? ? ? 1_555 G HOH . O  ? ? A NA  402 A HOH 650 1_555 ? ? ? ? ? ? ? 2.339 ? ? 
# 
_struct_conn_type.id          metalc 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
_pdbx_struct_conn_angle.id                    1 
_pdbx_struct_conn_angle.ptnr1_label_atom_id   O 
_pdbx_struct_conn_angle.ptnr1_label_alt_id    ? 
_pdbx_struct_conn_angle.ptnr1_label_asym_id   G 
_pdbx_struct_conn_angle.ptnr1_label_comp_id   HOH 
_pdbx_struct_conn_angle.ptnr1_label_seq_id    . 
_pdbx_struct_conn_angle.ptnr1_auth_atom_id    ? 
_pdbx_struct_conn_angle.ptnr1_auth_asym_id    A 
_pdbx_struct_conn_angle.ptnr1_auth_comp_id    HOH 
_pdbx_struct_conn_angle.ptnr1_auth_seq_id     633 
_pdbx_struct_conn_angle.ptnr1_PDB_ins_code    ? 
_pdbx_struct_conn_angle.ptnr1_symmetry        1_555 
_pdbx_struct_conn_angle.ptnr2_label_atom_id   NA 
_pdbx_struct_conn_angle.ptnr2_label_alt_id    ? 
_pdbx_struct_conn_angle.ptnr2_label_asym_id   C 
_pdbx_struct_conn_angle.ptnr2_label_comp_id   NA 
_pdbx_struct_conn_angle.ptnr2_label_seq_id    . 
_pdbx_struct_conn_angle.ptnr2_auth_atom_id    ? 
_pdbx_struct_conn_angle.ptnr2_auth_asym_id    A 
_pdbx_struct_conn_angle.ptnr2_auth_comp_id    NA 
_pdbx_struct_conn_angle.ptnr2_auth_seq_id     402 
_pdbx_struct_conn_angle.ptnr2_PDB_ins_code    ? 
_pdbx_struct_conn_angle.ptnr2_symmetry        1_555 
_pdbx_struct_conn_angle.ptnr3_label_atom_id   O 
_pdbx_struct_conn_angle.ptnr3_label_alt_id    ? 
_pdbx_struct_conn_angle.ptnr3_label_asym_id   G 
_pdbx_struct_conn_angle.ptnr3_label_comp_id   HOH 
_pdbx_struct_conn_angle.ptnr3_label_seq_id    . 
_pdbx_struct_conn_angle.ptnr3_auth_atom_id    ? 
_pdbx_struct_conn_angle.ptnr3_auth_asym_id    A 
_pdbx_struct_conn_angle.ptnr3_auth_comp_id    HOH 
_pdbx_struct_conn_angle.ptnr3_auth_seq_id     650 
_pdbx_struct_conn_angle.ptnr3_PDB_ins_code    ? 
_pdbx_struct_conn_angle.ptnr3_symmetry        1_555 
_pdbx_struct_conn_angle.value                 114.8 
_pdbx_struct_conn_angle.value_esd             ? 
# 
_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                   9F8C 
_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 
# 
_pdbx_validate_close_contact.id               1 
_pdbx_validate_close_contact.PDB_model_num    1 
_pdbx_validate_close_contact.auth_atom_id_1   O 
_pdbx_validate_close_contact.auth_asym_id_1   A 
_pdbx_validate_close_contact.auth_comp_id_1   HOH 
_pdbx_validate_close_contact.auth_seq_id_1    650 
_pdbx_validate_close_contact.PDB_ins_code_1   ? 
_pdbx_validate_close_contact.label_alt_id_1   ? 
_pdbx_validate_close_contact.auth_atom_id_2   O 
_pdbx_validate_close_contact.auth_asym_id_2   A 
_pdbx_validate_close_contact.auth_comp_id_2   HOH 
_pdbx_validate_close_contact.auth_seq_id_2    705 
_pdbx_validate_close_contact.PDB_ins_code_2   ? 
_pdbx_validate_close_contact.label_alt_id_2   ? 
_pdbx_validate_close_contact.dist             2.17 
# 
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  ? ? -102.77 -154.21 
2 1 SER A 122 ? ? 60.22   -122.25 
3 1 TYR A 268 ? ? -88.78  -151.89 
# 
_pdbx_refine_tls.id               1 
_pdbx_refine_tls.pdbx_refine_id   'X-RAY DIFFRACTION' 
_pdbx_refine_tls.details          ? 
_pdbx_refine_tls.method           refined 
_pdbx_refine_tls.origin_x         117.7940 
_pdbx_refine_tls.origin_y         21.1028 
_pdbx_refine_tls.origin_z         0.2615 
_pdbx_refine_tls.T[1][1]          -0.0331 
_pdbx_refine_tls.T[1][1]_esd      ? 
_pdbx_refine_tls.T[1][2]          -0.0050 
_pdbx_refine_tls.T[1][2]_esd      ? 
_pdbx_refine_tls.T[1][3]          -0.0021 
_pdbx_refine_tls.T[1][3]_esd      ? 
_pdbx_refine_tls.T[2][2]          -0.0862 
_pdbx_refine_tls.T[2][2]_esd      ? 
_pdbx_refine_tls.T[2][3]          -0.0019 
_pdbx_refine_tls.T[2][3]_esd      ? 
_pdbx_refine_tls.T[3][3]          -0.0615 
_pdbx_refine_tls.T[3][3]_esd      ? 
_pdbx_refine_tls.L[1][1]          0.1790 
_pdbx_refine_tls.L[1][1]_esd      ? 
_pdbx_refine_tls.L[1][2]          -0.3292 
_pdbx_refine_tls.L[1][2]_esd      ? 
_pdbx_refine_tls.L[1][3]          0.0224 
_pdbx_refine_tls.L[1][3]_esd      ? 
_pdbx_refine_tls.L[2][2]          2.4260 
_pdbx_refine_tls.L[2][2]_esd      ? 
_pdbx_refine_tls.L[2][3]          0.0946 
_pdbx_refine_tls.L[2][3]_esd      ? 
_pdbx_refine_tls.L[3][3]          0.7925 
_pdbx_refine_tls.L[3][3]_esd      ? 
_pdbx_refine_tls.S[1][1]          -0.0206 
_pdbx_refine_tls.S[1][1]_esd      ? 
_pdbx_refine_tls.S[1][2]          -0.0108 
_pdbx_refine_tls.S[1][2]_esd      ? 
_pdbx_refine_tls.S[1][3]          0.0261 
_pdbx_refine_tls.S[1][3]_esd      ? 
_pdbx_refine_tls.S[2][1]          0.0987 
_pdbx_refine_tls.S[2][1]_esd      ? 
_pdbx_refine_tls.S[2][2]          -0.0040 
_pdbx_refine_tls.S[2][2]_esd      ? 
_pdbx_refine_tls.S[2][3]          -0.0614 
_pdbx_refine_tls.S[2][3]_esd      ? 
_pdbx_refine_tls.S[3][1]          -0.0441 
_pdbx_refine_tls.S[3][1]_esd      ? 
_pdbx_refine_tls.S[3][2]          0.0069 
_pdbx_refine_tls.S[3][2]_esd      ? 
_pdbx_refine_tls.S[3][3]          0.0245 
_pdbx_refine_tls.S[3][3]_esd      ? 
# 
_pdbx_refine_tls_group.id                  1 
_pdbx_refine_tls_group.pdbx_refine_id      'X-RAY DIFFRACTION' 
_pdbx_refine_tls_group.refine_tls_id       1 
_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   '{ A|* }' 
# 
loop_
_pdbx_distant_solvent_atoms.id 
_pdbx_distant_solvent_atoms.PDB_model_num 
_pdbx_distant_solvent_atoms.auth_atom_id 
_pdbx_distant_solvent_atoms.label_alt_id 
_pdbx_distant_solvent_atoms.auth_asym_id 
_pdbx_distant_solvent_atoms.auth_comp_id 
_pdbx_distant_solvent_atoms.auth_seq_id 
_pdbx_distant_solvent_atoms.PDB_ins_code 
_pdbx_distant_solvent_atoms.neighbor_macromolecule_distance 
_pdbx_distant_solvent_atoms.neighbor_ligand_distance 
1 1 O ? A HOH 856 ? 5.86 . 
2 1 O ? A HOH 857 ? 5.95 . 
3 1 O ? A HOH 858 ? 6.17 . 
4 1 O ? A HOH 859 ? 6.37 . 
5 1 O ? A HOH 860 ? 6.45 . 
# 
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 THR 296 ? A THR 316 
22 1 Y 1 A ALA 297 ? A ALA 317 
23 1 Y 1 A GLY 298 ? A GLY 318 
24 1 Y 1 A THR 299 ? A THR 319 
25 1 Y 1 A ALA 300 ? A ALA 320 
26 1 Y 1 A SER 301 ? A SER 321 
27 1 Y 1 A PRO 302 ? A PRO 322 
28 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 
A1IA2 C8   C  N N 1   
A1IA2 C9   C  N N 2   
A1IA2 C1   C  N R 3   
A1IA2 C6   C  N N 4   
A1IA2 C4   C  N N 5   
A1IA2 C3   C  N N 6   
A1IA2 C2   C  N R 7   
A1IA2 N5   N  N N 8   
A1IA2 N7   N  N N 9   
A1IA2 O10  O  N N 10  
A1IA2 O13  O  N N 11  
A1IA2 C14  C  N N 12  
A1IA2 N15  N  N N 13  
A1IA2 O16  O  N N 14  
A1IA2 C17  C  N N 15  
A1IA2 C18  C  N N 16  
A1IA2 C19  C  N N 17  
A1IA2 C20  C  N N 18  
A1IA2 C21  C  N N 19  
A1IA2 C22  C  N N 20  
A1IA2 C23  C  Y N 21  
A1IA2 C24  C  Y N 22  
A1IA2 C25  C  Y N 23  
A1IA2 C26  C  Y N 24  
A1IA2 C27  C  Y N 25  
A1IA2 C28  C  Y N 26  
A1IA2 C29  C  N N 27  
A1IA2 F30  F  N N 28  
A1IA2 F31  F  N N 29  
A1IA2 F32  F  N N 30  
A1IA2 H1   H  N N 31  
A1IA2 H2   H  N N 32  
A1IA2 H3   H  N N 33  
A1IA2 H4   H  N N 34  
A1IA2 H5   H  N N 35  
A1IA2 H6   H  N N 36  
A1IA2 H7   H  N N 37  
A1IA2 H8   H  N N 38  
A1IA2 H9   H  N N 39  
A1IA2 H10  H  N N 40  
A1IA2 H11  H  N N 41  
A1IA2 H12  H  N N 42  
A1IA2 H13  H  N N 43  
A1IA2 H14  H  N N 44  
A1IA2 H15  H  N N 45  
A1IA2 H16  H  N N 46  
A1IA2 H17  H  N N 47  
A1IA2 H18  H  N N 48  
A1IA2 H19  H  N N 49  
A1IA2 H20  H  N N 50  
A1IA2 H21  H  N N 51  
A1IA2 H22  H  N N 52  
A1IA2 H23  H  N N 53  
A1IA2 H24  H  N N 54  
A1IA2 H25  H  N N 55  
A1IA2 H26  H  N N 56  
ALA   N    N  N N 57  
ALA   CA   C  N S 58  
ALA   C    C  N N 59  
ALA   O    O  N N 60  
ALA   CB   C  N N 61  
ALA   OXT  O  N N 62  
ALA   H    H  N N 63  
ALA   H2   H  N N 64  
ALA   HA   H  N N 65  
ALA   HB1  H  N N 66  
ALA   HB2  H  N N 67  
ALA   HB3  H  N N 68  
ALA   HXT  H  N N 69  
ARG   N    N  N N 70  
ARG   CA   C  N S 71  
ARG   C    C  N N 72  
ARG   O    O  N N 73  
ARG   CB   C  N N 74  
ARG   CG   C  N N 75  
ARG   CD   C  N N 76  
ARG   NE   N  N N 77  
ARG   CZ   C  N N 78  
ARG   NH1  N  N N 79  
ARG   NH2  N  N N 80  
ARG   OXT  O  N N 81  
ARG   H    H  N N 82  
ARG   H2   H  N N 83  
ARG   HA   H  N N 84  
ARG   HB2  H  N N 85  
ARG   HB3  H  N N 86  
ARG   HG2  H  N N 87  
ARG   HG3  H  N N 88  
ARG   HD2  H  N N 89  
ARG   HD3  H  N N 90  
ARG   HE   H  N N 91  
ARG   HH11 H  N N 92  
ARG   HH12 H  N N 93  
ARG   HH21 H  N N 94  
ARG   HH22 H  N N 95  
ARG   HXT  H  N N 96  
ASN   N    N  N N 97  
ASN   CA   C  N S 98  
ASN   C    C  N N 99  
ASN   O    O  N N 100 
ASN   CB   C  N N 101 
ASN   CG   C  N N 102 
ASN   OD1  O  N N 103 
ASN   ND2  N  N N 104 
ASN   OXT  O  N N 105 
ASN   H    H  N N 106 
ASN   H2   H  N N 107 
ASN   HA   H  N N 108 
ASN   HB2  H  N N 109 
ASN   HB3  H  N N 110 
ASN   HD21 H  N N 111 
ASN   HD22 H  N N 112 
ASN   HXT  H  N N 113 
ASP   N    N  N N 114 
ASP   CA   C  N S 115 
ASP   C    C  N N 116 
ASP   O    O  N N 117 
ASP   CB   C  N N 118 
ASP   CG   C  N N 119 
ASP   OD1  O  N N 120 
ASP   OD2  O  N N 121 
ASP   OXT  O  N N 122 
ASP   H    H  N N 123 
ASP   H2   H  N N 124 
ASP   HA   H  N N 125 
ASP   HB2  H  N N 126 
ASP   HB3  H  N N 127 
ASP   HD2  H  N N 128 
ASP   HXT  H  N N 129 
CYS   N    N  N N 130 
CYS   CA   C  N R 131 
CYS   C    C  N N 132 
CYS   O    O  N N 133 
CYS   CB   C  N N 134 
CYS   SG   S  N N 135 
CYS   OXT  O  N N 136 
CYS   H    H  N N 137 
CYS   H2   H  N N 138 
CYS   HA   H  N N 139 
CYS   HB2  H  N N 140 
CYS   HB3  H  N N 141 
CYS   HG   H  N N 142 
CYS   HXT  H  N N 143 
EDO   C1   C  N N 144 
EDO   O1   O  N N 145 
EDO   C2   C  N N 146 
EDO   O2   O  N N 147 
EDO   H11  H  N N 148 
EDO   H12  H  N N 149 
EDO   HO1  H  N N 150 
EDO   H21  H  N N 151 
EDO   H22  H  N N 152 
EDO   HO2  H  N N 153 
GLN   N    N  N N 154 
GLN   CA   C  N S 155 
GLN   C    C  N N 156 
GLN   O    O  N N 157 
GLN   CB   C  N N 158 
GLN   CG   C  N N 159 
GLN   CD   C  N N 160 
GLN   OE1  O  N N 161 
GLN   NE2  N  N N 162 
GLN   OXT  O  N N 163 
GLN   H    H  N N 164 
GLN   H2   H  N N 165 
GLN   HA   H  N N 166 
GLN   HB2  H  N N 167 
GLN   HB3  H  N N 168 
GLN   HG2  H  N N 169 
GLN   HG3  H  N N 170 
GLN   HE21 H  N N 171 
GLN   HE22 H  N N 172 
GLN   HXT  H  N N 173 
GLU   N    N  N N 174 
GLU   CA   C  N S 175 
GLU   C    C  N N 176 
GLU   O    O  N N 177 
GLU   CB   C  N N 178 
GLU   CG   C  N N 179 
GLU   CD   C  N N 180 
GLU   OE1  O  N N 181 
GLU   OE2  O  N N 182 
GLU   OXT  O  N N 183 
GLU   H    H  N N 184 
GLU   H2   H  N N 185 
GLU   HA   H  N N 186 
GLU   HB2  H  N N 187 
GLU   HB3  H  N N 188 
GLU   HG2  H  N N 189 
GLU   HG3  H  N N 190 
GLU   HE2  H  N N 191 
GLU   HXT  H  N N 192 
GLY   N    N  N N 193 
GLY   CA   C  N N 194 
GLY   C    C  N N 195 
GLY   O    O  N N 196 
GLY   OXT  O  N N 197 
GLY   H    H  N N 198 
GLY   H2   H  N N 199 
GLY   HA2  H  N N 200 
GLY   HA3  H  N N 201 
GLY   HXT  H  N N 202 
HIS   N    N  N N 203 
HIS   CA   C  N S 204 
HIS   C    C  N N 205 
HIS   O    O  N N 206 
HIS   CB   C  N N 207 
HIS   CG   C  Y N 208 
HIS   ND1  N  Y N 209 
HIS   CD2  C  Y N 210 
HIS   CE1  C  Y N 211 
HIS   NE2  N  Y N 212 
HIS   OXT  O  N N 213 
HIS   H    H  N N 214 
HIS   H2   H  N N 215 
HIS   HA   H  N N 216 
HIS   HB2  H  N N 217 
HIS   HB3  H  N N 218 
HIS   HD1  H  N N 219 
HIS   HD2  H  N N 220 
HIS   HE1  H  N N 221 
HIS   HE2  H  N N 222 
HIS   HXT  H  N N 223 
HOH   O    O  N N 224 
HOH   H1   H  N N 225 
HOH   H2   H  N N 226 
ILE   N    N  N N 227 
ILE   CA   C  N S 228 
ILE   C    C  N N 229 
ILE   O    O  N N 230 
ILE   CB   C  N S 231 
ILE   CG1  C  N N 232 
ILE   CG2  C  N N 233 
ILE   CD1  C  N N 234 
ILE   OXT  O  N N 235 
ILE   H    H  N N 236 
ILE   H2   H  N N 237 
ILE   HA   H  N N 238 
ILE   HB   H  N N 239 
ILE   HG12 H  N N 240 
ILE   HG13 H  N N 241 
ILE   HG21 H  N N 242 
ILE   HG22 H  N N 243 
ILE   HG23 H  N N 244 
ILE   HD11 H  N N 245 
ILE   HD12 H  N N 246 
ILE   HD13 H  N N 247 
ILE   HXT  H  N N 248 
LEU   N    N  N N 249 
LEU   CA   C  N S 250 
LEU   C    C  N N 251 
LEU   O    O  N N 252 
LEU   CB   C  N N 253 
LEU   CG   C  N N 254 
LEU   CD1  C  N N 255 
LEU   CD2  C  N N 256 
LEU   OXT  O  N N 257 
LEU   H    H  N N 258 
LEU   H2   H  N N 259 
LEU   HA   H  N N 260 
LEU   HB2  H  N N 261 
LEU   HB3  H  N N 262 
LEU   HG   H  N N 263 
LEU   HD11 H  N N 264 
LEU   HD12 H  N N 265 
LEU   HD13 H  N N 266 
LEU   HD21 H  N N 267 
LEU   HD22 H  N N 268 
LEU   HD23 H  N N 269 
LEU   HXT  H  N N 270 
LYS   N    N  N N 271 
LYS   CA   C  N S 272 
LYS   C    C  N N 273 
LYS   O    O  N N 274 
LYS   CB   C  N N 275 
LYS   CG   C  N N 276 
LYS   CD   C  N N 277 
LYS   CE   C  N N 278 
LYS   NZ   N  N N 279 
LYS   OXT  O  N N 280 
LYS   H    H  N N 281 
LYS   H2   H  N N 282 
LYS   HA   H  N N 283 
LYS   HB2  H  N N 284 
LYS   HB3  H  N N 285 
LYS   HG2  H  N N 286 
LYS   HG3  H  N N 287 
LYS   HD2  H  N N 288 
LYS   HD3  H  N N 289 
LYS   HE2  H  N N 290 
LYS   HE3  H  N N 291 
LYS   HZ1  H  N N 292 
LYS   HZ2  H  N N 293 
LYS   HZ3  H  N N 294 
LYS   HXT  H  N N 295 
MET   N    N  N N 296 
MET   CA   C  N S 297 
MET   C    C  N N 298 
MET   O    O  N N 299 
MET   CB   C  N N 300 
MET   CG   C  N N 301 
MET   SD   S  N N 302 
MET   CE   C  N N 303 
MET   OXT  O  N N 304 
MET   H    H  N N 305 
MET   H2   H  N N 306 
MET   HA   H  N N 307 
MET   HB2  H  N N 308 
MET   HB3  H  N N 309 
MET   HG2  H  N N 310 
MET   HG3  H  N N 311 
MET   HE1  H  N N 312 
MET   HE2  H  N N 313 
MET   HE3  H  N N 314 
MET   HXT  H  N N 315 
NA    NA   NA N N 316 
PHE   N    N  N N 317 
PHE   CA   C  N S 318 
PHE   C    C  N N 319 
PHE   O    O  N N 320 
PHE   CB   C  N N 321 
PHE   CG   C  Y N 322 
PHE   CD1  C  Y N 323 
PHE   CD2  C  Y N 324 
PHE   CE1  C  Y N 325 
PHE   CE2  C  Y N 326 
PHE   CZ   C  Y N 327 
PHE   OXT  O  N N 328 
PHE   H    H  N N 329 
PHE   H2   H  N N 330 
PHE   HA   H  N N 331 
PHE   HB2  H  N N 332 
PHE   HB3  H  N N 333 
PHE   HD1  H  N N 334 
PHE   HD2  H  N N 335 
PHE   HE1  H  N N 336 
PHE   HE2  H  N N 337 
PHE   HZ   H  N N 338 
PHE   HXT  H  N N 339 
PRO   N    N  N N 340 
PRO   CA   C  N S 341 
PRO   C    C  N N 342 
PRO   O    O  N N 343 
PRO   CB   C  N N 344 
PRO   CG   C  N N 345 
PRO   CD   C  N N 346 
PRO   OXT  O  N N 347 
PRO   H    H  N N 348 
PRO   HA   H  N N 349 
PRO   HB2  H  N N 350 
PRO   HB3  H  N N 351 
PRO   HG2  H  N N 352 
PRO   HG3  H  N N 353 
PRO   HD2  H  N N 354 
PRO   HD3  H  N N 355 
PRO   HXT  H  N N 356 
SER   N    N  N N 357 
SER   CA   C  N S 358 
SER   C    C  N N 359 
SER   O    O  N N 360 
SER   CB   C  N N 361 
SER   OG   O  N N 362 
SER   OXT  O  N N 363 
SER   H    H  N N 364 
SER   H2   H  N N 365 
SER   HA   H  N N 366 
SER   HB2  H  N N 367 
SER   HB3  H  N N 368 
SER   HG   H  N N 369 
SER   HXT  H  N N 370 
THR   N    N  N N 371 
THR   CA   C  N S 372 
THR   C    C  N N 373 
THR   O    O  N N 374 
THR   CB   C  N R 375 
THR   OG1  O  N N 376 
THR   CG2  C  N N 377 
THR   OXT  O  N N 378 
THR   H    H  N N 379 
THR   H2   H  N N 380 
THR   HA   H  N N 381 
THR   HB   H  N N 382 
THR   HG1  H  N N 383 
THR   HG21 H  N N 384 
THR   HG22 H  N N 385 
THR   HG23 H  N N 386 
THR   HXT  H  N N 387 
TRP   N    N  N N 388 
TRP   CA   C  N S 389 
TRP   C    C  N N 390 
TRP   O    O  N N 391 
TRP   CB   C  N N 392 
TRP   CG   C  Y N 393 
TRP   CD1  C  Y N 394 
TRP   CD2  C  Y N 395 
TRP   NE1  N  Y N 396 
TRP   CE2  C  Y N 397 
TRP   CE3  C  Y N 398 
TRP   CZ2  C  Y N 399 
TRP   CZ3  C  Y N 400 
TRP   CH2  C  Y N 401 
TRP   OXT  O  N N 402 
TRP   H    H  N N 403 
TRP   H2   H  N N 404 
TRP   HA   H  N N 405 
TRP   HB2  H  N N 406 
TRP   HB3  H  N N 407 
TRP   HD1  H  N N 408 
TRP   HE1  H  N N 409 
TRP   HE3  H  N N 410 
TRP   HZ2  H  N N 411 
TRP   HZ3  H  N N 412 
TRP   HH2  H  N N 413 
TRP   HXT  H  N N 414 
TYR   N    N  N N 415 
TYR   CA   C  N S 416 
TYR   C    C  N N 417 
TYR   O    O  N N 418 
TYR   CB   C  N N 419 
TYR   CG   C  Y N 420 
TYR   CD1  C  Y N 421 
TYR   CD2  C  Y N 422 
TYR   CE1  C  Y N 423 
TYR   CE2  C  Y N 424 
TYR   CZ   C  Y N 425 
TYR   OH   O  N N 426 
TYR   OXT  O  N N 427 
TYR   H    H  N N 428 
TYR   H2   H  N N 429 
TYR   HA   H  N N 430 
TYR   HB2  H  N N 431 
TYR   HB3  H  N N 432 
TYR   HD1  H  N N 433 
TYR   HD2  H  N N 434 
TYR   HE1  H  N N 435 
TYR   HE2  H  N N 436 
TYR   HH   H  N N 437 
TYR   HXT  H  N N 438 
VAL   N    N  N N 439 
VAL   CA   C  N S 440 
VAL   C    C  N N 441 
VAL   O    O  N N 442 
VAL   CB   C  N N 443 
VAL   CG1  C  N N 444 
VAL   CG2  C  N N 445 
VAL   OXT  O  N N 446 
VAL   H    H  N N 447 
VAL   H2   H  N N 448 
VAL   HA   H  N N 449 
VAL   HB   H  N N 450 
VAL   HG11 H  N N 451 
VAL   HG12 H  N N 452 
VAL   HG13 H  N N 453 
VAL   HG21 H  N N 454 
VAL   HG22 H  N N 455 
VAL   HG23 H  N N 456 
VAL   HXT  H  N N 457 
# 
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 
A1IA2 O10 C9   sing N N 1   
A1IA2 O10 C2   sing N N 2   
A1IA2 C9  C8   sing N N 3   
A1IA2 O13 C8   doub N N 4   
A1IA2 C8  N7   sing N N 5   
A1IA2 C3  C2   sing N N 6   
A1IA2 C3  C4   sing N N 7   
A1IA2 C2  C1   sing N N 8   
A1IA2 N7  C1   sing N N 9   
A1IA2 C1  C6   sing N N 10  
A1IA2 C4  N5   sing N N 11  
A1IA2 C20 C21  sing N N 12  
A1IA2 C20 C19  sing N N 13  
A1IA2 C6  N5   sing N N 14  
A1IA2 N5  C14  sing N N 15  
A1IA2 C21 N15  sing N N 16  
A1IA2 C22 C19  sing N N 17  
A1IA2 C22 C23  sing N N 18  
A1IA2 C19 C18  sing N N 19  
A1IA2 N15 C14  sing N N 20  
A1IA2 N15 C17  sing N N 21  
A1IA2 C14 O16  doub N N 22  
A1IA2 C23 C28  doub Y N 23  
A1IA2 C23 C24  sing Y N 24  
A1IA2 C28 C27  sing Y N 25  
A1IA2 C18 C17  sing N N 26  
A1IA2 C24 C25  doub Y N 27  
A1IA2 C27 C26  doub Y N 28  
A1IA2 C25 C26  sing Y N 29  
A1IA2 C26 C29  sing N N 30  
A1IA2 F30 C29  sing N N 31  
A1IA2 C29 F31  sing N N 32  
A1IA2 C29 F32  sing N N 33  
A1IA2 C9  H1   sing N N 34  
A1IA2 C9  H2   sing N N 35  
A1IA2 C1  H3   sing N N 36  
A1IA2 C6  H4   sing N N 37  
A1IA2 C6  H5   sing N N 38  
A1IA2 C4  H6   sing N N 39  
A1IA2 C4  H7   sing N N 40  
A1IA2 C3  H8   sing N N 41  
A1IA2 C3  H9   sing N N 42  
A1IA2 C2  H10  sing N N 43  
A1IA2 N7  H11  sing N N 44  
A1IA2 C17 H12  sing N N 45  
A1IA2 C17 H13  sing N N 46  
A1IA2 C18 H14  sing N N 47  
A1IA2 C18 H15  sing N N 48  
A1IA2 C19 H16  sing N N 49  
A1IA2 C20 H17  sing N N 50  
A1IA2 C20 H18  sing N N 51  
A1IA2 C21 H19  sing N N 52  
A1IA2 C21 H20  sing N N 53  
A1IA2 C22 H21  sing N N 54  
A1IA2 C22 H22  sing N N 55  
A1IA2 C24 H23  sing N N 56  
A1IA2 C25 H24  sing N N 57  
A1IA2 C27 H25  sing N N 58  
A1IA2 C28 H26  sing N N 59  
ALA   N   CA   sing N N 60  
ALA   N   H    sing N N 61  
ALA   N   H2   sing N N 62  
ALA   CA  C    sing N N 63  
ALA   CA  CB   sing N N 64  
ALA   CA  HA   sing N N 65  
ALA   C   O    doub N N 66  
ALA   C   OXT  sing N N 67  
ALA   CB  HB1  sing N N 68  
ALA   CB  HB2  sing N N 69  
ALA   CB  HB3  sing N N 70  
ALA   OXT HXT  sing N N 71  
ARG   N   CA   sing N N 72  
ARG   N   H    sing N N 73  
ARG   N   H2   sing N N 74  
ARG   CA  C    sing N N 75  
ARG   CA  CB   sing N N 76  
ARG   CA  HA   sing N N 77  
ARG   C   O    doub N N 78  
ARG   C   OXT  sing N N 79  
ARG   CB  CG   sing N N 80  
ARG   CB  HB2  sing N N 81  
ARG   CB  HB3  sing N N 82  
ARG   CG  CD   sing N N 83  
ARG   CG  HG2  sing N N 84  
ARG   CG  HG3  sing N N 85  
ARG   CD  NE   sing N N 86  
ARG   CD  HD2  sing N N 87  
ARG   CD  HD3  sing N N 88  
ARG   NE  CZ   sing N N 89  
ARG   NE  HE   sing N N 90  
ARG   CZ  NH1  sing N N 91  
ARG   CZ  NH2  doub N N 92  
ARG   NH1 HH11 sing N N 93  
ARG   NH1 HH12 sing N N 94  
ARG   NH2 HH21 sing N N 95  
ARG   NH2 HH22 sing N N 96  
ARG   OXT HXT  sing N N 97  
ASN   N   CA   sing N N 98  
ASN   N   H    sing N N 99  
ASN   N   H2   sing N N 100 
ASN   CA  C    sing N N 101 
ASN   CA  CB   sing N N 102 
ASN   CA  HA   sing N N 103 
ASN   C   O    doub N N 104 
ASN   C   OXT  sing N N 105 
ASN   CB  CG   sing N N 106 
ASN   CB  HB2  sing N N 107 
ASN   CB  HB3  sing N N 108 
ASN   CG  OD1  doub N N 109 
ASN   CG  ND2  sing N N 110 
ASN   ND2 HD21 sing N N 111 
ASN   ND2 HD22 sing N N 112 
ASN   OXT HXT  sing N N 113 
ASP   N   CA   sing N N 114 
ASP   N   H    sing N N 115 
ASP   N   H2   sing N N 116 
ASP   CA  C    sing N N 117 
ASP   CA  CB   sing N N 118 
ASP   CA  HA   sing N N 119 
ASP   C   O    doub N N 120 
ASP   C   OXT  sing N N 121 
ASP   CB  CG   sing N N 122 
ASP   CB  HB2  sing N N 123 
ASP   CB  HB3  sing N N 124 
ASP   CG  OD1  doub N N 125 
ASP   CG  OD2  sing N N 126 
ASP   OD2 HD2  sing N N 127 
ASP   OXT HXT  sing N N 128 
CYS   N   CA   sing N N 129 
CYS   N   H    sing N N 130 
CYS   N   H2   sing N N 131 
CYS   CA  C    sing N N 132 
CYS   CA  CB   sing N N 133 
CYS   CA  HA   sing N N 134 
CYS   C   O    doub N N 135 
CYS   C   OXT  sing N N 136 
CYS   CB  SG   sing N N 137 
CYS   CB  HB2  sing N N 138 
CYS   CB  HB3  sing N N 139 
CYS   SG  HG   sing N N 140 
CYS   OXT HXT  sing N N 141 
EDO   C1  O1   sing N N 142 
EDO   C1  C2   sing N N 143 
EDO   C1  H11  sing N N 144 
EDO   C1  H12  sing N N 145 
EDO   O1  HO1  sing N N 146 
EDO   C2  O2   sing N N 147 
EDO   C2  H21  sing N N 148 
EDO   C2  H22  sing N N 149 
EDO   O2  HO2  sing N N 150 
GLN   N   CA   sing N N 151 
GLN   N   H    sing N N 152 
GLN   N   H2   sing N N 153 
GLN   CA  C    sing N N 154 
GLN   CA  CB   sing N N 155 
GLN   CA  HA   sing N N 156 
GLN   C   O    doub N N 157 
GLN   C   OXT  sing N N 158 
GLN   CB  CG   sing N N 159 
GLN   CB  HB2  sing N N 160 
GLN   CB  HB3  sing N N 161 
GLN   CG  CD   sing N N 162 
GLN   CG  HG2  sing N N 163 
GLN   CG  HG3  sing N N 164 
GLN   CD  OE1  doub N N 165 
GLN   CD  NE2  sing N N 166 
GLN   NE2 HE21 sing N N 167 
GLN   NE2 HE22 sing N N 168 
GLN   OXT HXT  sing N N 169 
GLU   N   CA   sing N N 170 
GLU   N   H    sing N N 171 
GLU   N   H2   sing N N 172 
GLU   CA  C    sing N N 173 
GLU   CA  CB   sing N N 174 
GLU   CA  HA   sing N N 175 
GLU   C   O    doub N N 176 
GLU   C   OXT  sing N N 177 
GLU   CB  CG   sing N N 178 
GLU   CB  HB2  sing N N 179 
GLU   CB  HB3  sing N N 180 
GLU   CG  CD   sing N N 181 
GLU   CG  HG2  sing N N 182 
GLU   CG  HG3  sing N N 183 
GLU   CD  OE1  doub N N 184 
GLU   CD  OE2  sing N N 185 
GLU   OE2 HE2  sing N N 186 
GLU   OXT HXT  sing N N 187 
GLY   N   CA   sing N N 188 
GLY   N   H    sing N N 189 
GLY   N   H2   sing N N 190 
GLY   CA  C    sing N N 191 
GLY   CA  HA2  sing N N 192 
GLY   CA  HA3  sing N N 193 
GLY   C   O    doub N N 194 
GLY   C   OXT  sing N N 195 
GLY   OXT HXT  sing N N 196 
HIS   N   CA   sing N N 197 
HIS   N   H    sing N N 198 
HIS   N   H2   sing N N 199 
HIS   CA  C    sing N N 200 
HIS   CA  CB   sing N N 201 
HIS   CA  HA   sing N N 202 
HIS   C   O    doub N N 203 
HIS   C   OXT  sing N N 204 
HIS   CB  CG   sing N N 205 
HIS   CB  HB2  sing N N 206 
HIS   CB  HB3  sing N N 207 
HIS   CG  ND1  sing Y N 208 
HIS   CG  CD2  doub Y N 209 
HIS   ND1 CE1  doub Y N 210 
HIS   ND1 HD1  sing N N 211 
HIS   CD2 NE2  sing Y N 212 
HIS   CD2 HD2  sing N N 213 
HIS   CE1 NE2  sing Y N 214 
HIS   CE1 HE1  sing N N 215 
HIS   NE2 HE2  sing N N 216 
HIS   OXT HXT  sing N N 217 
HOH   O   H1   sing N N 218 
HOH   O   H2   sing N N 219 
ILE   N   CA   sing N N 220 
ILE   N   H    sing N N 221 
ILE   N   H2   sing N N 222 
ILE   CA  C    sing N N 223 
ILE   CA  CB   sing N N 224 
ILE   CA  HA   sing N N 225 
ILE   C   O    doub N N 226 
ILE   C   OXT  sing N N 227 
ILE   CB  CG1  sing N N 228 
ILE   CB  CG2  sing N N 229 
ILE   CB  HB   sing N N 230 
ILE   CG1 CD1  sing N N 231 
ILE   CG1 HG12 sing N N 232 
ILE   CG1 HG13 sing N N 233 
ILE   CG2 HG21 sing N N 234 
ILE   CG2 HG22 sing N N 235 
ILE   CG2 HG23 sing N N 236 
ILE   CD1 HD11 sing N N 237 
ILE   CD1 HD12 sing N N 238 
ILE   CD1 HD13 sing N N 239 
ILE   OXT HXT  sing N N 240 
LEU   N   CA   sing N N 241 
LEU   N   H    sing N N 242 
LEU   N   H2   sing N N 243 
LEU   CA  C    sing N N 244 
LEU   CA  CB   sing N N 245 
LEU   CA  HA   sing N N 246 
LEU   C   O    doub N N 247 
LEU   C   OXT  sing N N 248 
LEU   CB  CG   sing N N 249 
LEU   CB  HB2  sing N N 250 
LEU   CB  HB3  sing N N 251 
LEU   CG  CD1  sing N N 252 
LEU   CG  CD2  sing N N 253 
LEU   CG  HG   sing N N 254 
LEU   CD1 HD11 sing N N 255 
LEU   CD1 HD12 sing N N 256 
LEU   CD1 HD13 sing N N 257 
LEU   CD2 HD21 sing N N 258 
LEU   CD2 HD22 sing N N 259 
LEU   CD2 HD23 sing N N 260 
LEU   OXT HXT  sing N N 261 
LYS   N   CA   sing N N 262 
LYS   N   H    sing N N 263 
LYS   N   H2   sing N N 264 
LYS   CA  C    sing N N 265 
LYS   CA  CB   sing N N 266 
LYS   CA  HA   sing N N 267 
LYS   C   O    doub N N 268 
LYS   C   OXT  sing N N 269 
LYS   CB  CG   sing N N 270 
LYS   CB  HB2  sing N N 271 
LYS   CB  HB3  sing N N 272 
LYS   CG  CD   sing N N 273 
LYS   CG  HG2  sing N N 274 
LYS   CG  HG3  sing N N 275 
LYS   CD  CE   sing N N 276 
LYS   CD  HD2  sing N N 277 
LYS   CD  HD3  sing N N 278 
LYS   CE  NZ   sing N N 279 
LYS   CE  HE2  sing N N 280 
LYS   CE  HE3  sing N N 281 
LYS   NZ  HZ1  sing N N 282 
LYS   NZ  HZ2  sing N N 283 
LYS   NZ  HZ3  sing N N 284 
LYS   OXT HXT  sing N N 285 
MET   N   CA   sing N N 286 
MET   N   H    sing N N 287 
MET   N   H2   sing N N 288 
MET   CA  C    sing N N 289 
MET   CA  CB   sing N N 290 
MET   CA  HA   sing N N 291 
MET   C   O    doub N N 292 
MET   C   OXT  sing N N 293 
MET   CB  CG   sing N N 294 
MET   CB  HB2  sing N N 295 
MET   CB  HB3  sing N N 296 
MET   CG  SD   sing N N 297 
MET   CG  HG2  sing N N 298 
MET   CG  HG3  sing N N 299 
MET   SD  CE   sing N N 300 
MET   CE  HE1  sing N N 301 
MET   CE  HE2  sing N N 302 
MET   CE  HE3  sing N N 303 
MET   OXT HXT  sing N N 304 
PHE   N   CA   sing N N 305 
PHE   N   H    sing N N 306 
PHE   N   H2   sing N N 307 
PHE   CA  C    sing N N 308 
PHE   CA  CB   sing N N 309 
PHE   CA  HA   sing N N 310 
PHE   C   O    doub N N 311 
PHE   C   OXT  sing N N 312 
PHE   CB  CG   sing N N 313 
PHE   CB  HB2  sing N N 314 
PHE   CB  HB3  sing N N 315 
PHE   CG  CD1  doub Y N 316 
PHE   CG  CD2  sing Y N 317 
PHE   CD1 CE1  sing Y N 318 
PHE   CD1 HD1  sing N N 319 
PHE   CD2 CE2  doub Y N 320 
PHE   CD2 HD2  sing N N 321 
PHE   CE1 CZ   doub Y N 322 
PHE   CE1 HE1  sing N N 323 
PHE   CE2 CZ   sing Y N 324 
PHE   CE2 HE2  sing N N 325 
PHE   CZ  HZ   sing N N 326 
PHE   OXT HXT  sing N N 327 
PRO   N   CA   sing N N 328 
PRO   N   CD   sing N N 329 
PRO   N   H    sing N N 330 
PRO   CA  C    sing N N 331 
PRO   CA  CB   sing N N 332 
PRO   CA  HA   sing N N 333 
PRO   C   O    doub N N 334 
PRO   C   OXT  sing N N 335 
PRO   CB  CG   sing N N 336 
PRO   CB  HB2  sing N N 337 
PRO   CB  HB3  sing N N 338 
PRO   CG  CD   sing N N 339 
PRO   CG  HG2  sing N N 340 
PRO   CG  HG3  sing N N 341 
PRO   CD  HD2  sing N N 342 
PRO   CD  HD3  sing N N 343 
PRO   OXT HXT  sing N N 344 
SER   N   CA   sing N N 345 
SER   N   H    sing N N 346 
SER   N   H2   sing N N 347 
SER   CA  C    sing N N 348 
SER   CA  CB   sing N N 349 
SER   CA  HA   sing N N 350 
SER   C   O    doub N N 351 
SER   C   OXT  sing N N 352 
SER   CB  OG   sing N N 353 
SER   CB  HB2  sing N N 354 
SER   CB  HB3  sing N N 355 
SER   OG  HG   sing N N 356 
SER   OXT HXT  sing N N 357 
THR   N   CA   sing N N 358 
THR   N   H    sing N N 359 
THR   N   H2   sing N N 360 
THR   CA  C    sing N N 361 
THR   CA  CB   sing N N 362 
THR   CA  HA   sing N N 363 
THR   C   O    doub N N 364 
THR   C   OXT  sing N N 365 
THR   CB  OG1  sing N N 366 
THR   CB  CG2  sing N N 367 
THR   CB  HB   sing N N 368 
THR   OG1 HG1  sing N N 369 
THR   CG2 HG21 sing N N 370 
THR   CG2 HG22 sing N N 371 
THR   CG2 HG23 sing N N 372 
THR   OXT HXT  sing N N 373 
TRP   N   CA   sing N N 374 
TRP   N   H    sing N N 375 
TRP   N   H2   sing N N 376 
TRP   CA  C    sing N N 377 
TRP   CA  CB   sing N N 378 
TRP   CA  HA   sing N N 379 
TRP   C   O    doub N N 380 
TRP   C   OXT  sing N N 381 
TRP   CB  CG   sing N N 382 
TRP   CB  HB2  sing N N 383 
TRP   CB  HB3  sing N N 384 
TRP   CG  CD1  doub Y N 385 
TRP   CG  CD2  sing Y N 386 
TRP   CD1 NE1  sing Y N 387 
TRP   CD1 HD1  sing N N 388 
TRP   CD2 CE2  doub Y N 389 
TRP   CD2 CE3  sing Y N 390 
TRP   NE1 CE2  sing Y N 391 
TRP   NE1 HE1  sing N N 392 
TRP   CE2 CZ2  sing Y N 393 
TRP   CE3 CZ3  doub Y N 394 
TRP   CE3 HE3  sing N N 395 
TRP   CZ2 CH2  doub Y N 396 
TRP   CZ2 HZ2  sing N N 397 
TRP   CZ3 CH2  sing Y N 398 
TRP   CZ3 HZ3  sing N N 399 
TRP   CH2 HH2  sing N N 400 
TRP   OXT HXT  sing N N 401 
TYR   N   CA   sing N N 402 
TYR   N   H    sing N N 403 
TYR   N   H2   sing N N 404 
TYR   CA  C    sing N N 405 
TYR   CA  CB   sing N N 406 
TYR   CA  HA   sing N N 407 
TYR   C   O    doub N N 408 
TYR   C   OXT  sing N N 409 
TYR   CB  CG   sing N N 410 
TYR   CB  HB2  sing N N 411 
TYR   CB  HB3  sing N N 412 
TYR   CG  CD1  doub Y N 413 
TYR   CG  CD2  sing Y N 414 
TYR   CD1 CE1  sing Y N 415 
TYR   CD1 HD1  sing N N 416 
TYR   CD2 CE2  doub Y N 417 
TYR   CD2 HD2  sing N N 418 
TYR   CE1 CZ   doub Y N 419 
TYR   CE1 HE1  sing N N 420 
TYR   CE2 CZ   sing Y N 421 
TYR   CE2 HE2  sing N N 422 
TYR   CZ  OH   sing N N 423 
TYR   OH  HH   sing N N 424 
TYR   OXT HXT  sing N N 425 
VAL   N   CA   sing N N 426 
VAL   N   H    sing N N 427 
VAL   N   H2   sing N N 428 
VAL   CA  C    sing N N 429 
VAL   CA  CB   sing N N 430 
VAL   CA  HA   sing N N 431 
VAL   C   O    doub N N 432 
VAL   C   OXT  sing N N 433 
VAL   CB  CG1  sing N N 434 
VAL   CB  CG2  sing N N 435 
VAL   CB  HB   sing N N 436 
VAL   CG1 HG11 sing N N 437 
VAL   CG1 HG12 sing N N 438 
VAL   CG1 HG13 sing N N 439 
VAL   CG2 HG21 sing N N 440 
VAL   CG2 HG22 sing N N 441 
VAL   CG2 HG23 sing N N 442 
VAL   OXT HXT  sing N N 443 
# 
_pdbx_audit_support.funding_organization   'Not funded' 
_pdbx_audit_support.country                Switzerland 
_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                    9F8C 
_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]   0.011112 
_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]   0.007848 
_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]   0.015976 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
C  
F  
N  
NA 
O  
S  
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N  N   . MET   A 1 21  ? 107.446 64.419 11.891  1.00 61.37  ? 1   MET   A N   1 
ATOM   2    C  CA  . MET   A 1 21  ? 107.030 63.039 12.134  1.00 61.89  ? 1   MET   A CA  1 
ATOM   3    C  C   . MET   A 1 21  ? 107.909 62.049 11.360  1.00 61.99  ? 1   MET   A C   1 
ATOM   4    O  O   . MET   A 1 21  ? 108.048 62.161 10.139  1.00 62.17  ? 1   MET   A O   1 
ATOM   5    C  CB  . MET   A 1 21  ? 105.538 62.849 11.773  1.00 62.60  ? 1   MET   A CB  1 
ATOM   6    C  CG  . MET   A 1 21  ? 105.048 61.401 11.860  1.00 64.68  ? 1   MET   A CG  1 
ATOM   7    S  SD  . MET   A 1 21  ? 104.787 60.786 13.548  1.00 66.40  ? 1   MET   A SD  1 
ATOM   8    C  CE  . MET   A 1 21  ? 103.451 61.866 14.079  1.00 64.07  ? 1   MET   A CE  1 
ATOM   9    N  N   . PRO   A 1 22  ? 108.506 61.066 12.058  1.00 61.40  ? 2   PRO   A N   1 
ATOM   10   C  CA  . PRO   A 1 22  ? 109.313 60.063 11.352  1.00 61.25  ? 2   PRO   A CA  1 
ATOM   11   C  C   . PRO   A 1 22  ? 108.441 59.167 10.476  1.00 61.17  ? 2   PRO   A C   1 
ATOM   12   O  O   . PRO   A 1 22  ? 107.251 58.975 10.749  1.00 61.26  ? 2   PRO   A O   1 
ATOM   13   C  CB  . PRO   A 1 22  ? 109.973 59.274 12.489  1.00 61.74  ? 2   PRO   A CB  1 
ATOM   14   C  CG  . PRO   A 1 22  ? 109.042 59.415 13.630  1.00 62.19  ? 2   PRO   A CG  1 
ATOM   15   C  CD  . PRO   A 1 22  ? 108.431 60.781 13.502  1.00 60.80  ? 2   PRO   A CD  1 
ATOM   16   N  N   . GLU   A 1 23  ? 109.023 58.653 9.392   1.00 60.59  ? 3   GLU   A N   1 
ATOM   17   C  CA  . GLU   A 1 23  ? 108.285 57.812 8.459   1.00 60.62  ? 3   GLU   A CA  1 
ATOM   18   C  C   . GLU   A 1 23  ? 108.935 56.456 8.319   1.00 59.72  ? 3   GLU   A C   1 
ATOM   19   O  O   . GLU   A 1 23  ? 110.152 56.332 8.480   1.00 59.72  ? 3   GLU   A O   1 
ATOM   20   C  CB  . GLU   A 1 23  ? 108.190 58.483 7.078   1.00 63.70  ? 3   GLU   A CB  1 
ATOM   21   C  CG  . GLU   A 1 23  ? 107.659 59.904 7.125   1.00 70.18  ? 3   GLU   A CG  1 
ATOM   22   C  CD  . GLU   A 1 23  ? 107.546 60.563 5.766   1.00 78.69  ? 3   GLU   A CD  1 
ATOM   23   O  OE1 . GLU   A 1 23  ? 107.406 59.828 4.761   1.00 80.31  ? 3   GLU   A OE1 1 
ATOM   24   O  OE2 . GLU   A 1 23  ? 107.593 61.813 5.706   1.00 81.64  ? 3   GLU   A OE2 1 
ATOM   25   N  N   . GLU   A 1 24  ? 108.131 55.438 8.004   1.00 58.83  ? 4   GLU   A N   1 
ATOM   26   C  CA  . GLU   A 1 24  ? 108.661 54.096 7.821   1.00 58.38  ? 4   GLU   A CA  1 
ATOM   27   C  C   . GLU   A 1 24  ? 109.429 54.010 6.504   1.00 58.25  ? 4   GLU   A C   1 
ATOM   28   O  O   . GLU   A 1 24  ? 108.964 54.520 5.483   1.00 58.52  ? 4   GLU   A O   1 
ATOM   29   C  CB  . GLU   A 1 24  ? 107.537 53.044 7.918   1.00 59.64  ? 4   GLU   A CB  1 
ATOM   30   C  CG  . GLU   A 1 24  ? 107.899 51.644 7.448   1.00 61.77  ? 4   GLU   A CG  1 
ATOM   31   C  CD  . GLU   A 1 24  ? 108.857 50.836 8.306   1.00 63.96  ? 4   GLU   A CD  1 
ATOM   32   O  OE1 . GLU   A 1 24  ? 109.718 51.435 8.988   1.00 67.10  ? 4   GLU   A OE1 1 
ATOM   33   O  OE2 . GLU   A 1 24  ? 108.771 49.592 8.268   1.00 59.65  ? 4   GLU   A OE2 1 
ATOM   34   N  N   . SER   A 1 25  ? 110.631 53.410 6.544   1.00 57.45  ? 5   SER   A N   1 
ATOM   35   C  CA  . SER   A 1 25  ? 111.480 53.214 5.375   1.00 57.09  ? 5   SER   A CA  1 
ATOM   36   C  C   . SER   A 1 25  ? 110.779 52.328 4.340   1.00 55.83  ? 5   SER   A C   1 
ATOM   37   O  O   . SER   A 1 25  ? 109.893 51.541 4.692   1.00 55.78  ? 5   SER   A O   1 
ATOM   38   C  CB  . SER   A 1 25  ? 112.795 52.557 5.786   1.00 58.87  ? 5   SER   A CB  1 
ATOM   39   O  OG  . SER   A 1 25  ? 112.571 51.255 6.305   1.00 61.15  ? 5   SER   A OG  1 
ATOM   40   N  N   . SER   A 1 26  ? 111.206 52.439 3.057   1.00 54.28  ? 6   SER   A N   1 
ATOM   41   C  CA  . SER   A 1 26  ? 110.690 51.677 1.913   1.00 52.96  ? 6   SER   A CA  1 
ATOM   42   C  C   . SER   A 1 26  ? 110.611 50.184 2.238   1.00 50.12  ? 6   SER   A C   1 
ATOM   43   O  O   . SER   A 1 26  ? 111.498 49.663 2.913   1.00 50.36  ? 6   SER   A O   1 
ATOM   44   C  CB  . SER   A 1 26  ? 111.582 51.902 0.694   1.00 55.18  ? 6   SER   A CB  1 
ATOM   45   O  OG  . SER   A 1 26  ? 111.035 51.305 -0.470  1.00 58.87  ? 6   SER   A OG  1 
ATOM   46   N  N   . PRO   A 1 27  ? 109.510 49.513 1.854   1.00 47.17  ? 7   PRO   A N   1 
ATOM   47   C  CA  . PRO   A 1 27  ? 109.357 48.086 2.198   1.00 44.35  ? 7   PRO   A CA  1 
ATOM   48   C  C   . PRO   A 1 27  ? 110.543 47.207 1.803   1.00 39.58  ? 7   PRO   A C   1 
ATOM   49   O  O   . PRO   A 1 27  ? 111.163 47.450 0.769   1.00 39.78  ? 7   PRO   A O   1 
ATOM   50   C  CB  . PRO   A 1 27  ? 108.086 47.659 1.451   1.00 46.02  ? 7   PRO   A CB  1 
ATOM   51   C  CG  . PRO   A 1 27  ? 107.377 48.902 1.112   1.00 47.55  ? 7   PRO   A CG  1 
ATOM   52   C  CD  . PRO   A 1 27  ? 108.364 50.022 1.075   1.00 46.41  ? 7   PRO   A CD  1 
ATOM   53   N  N   . ARG   A 1 28  ? 110.885 46.214 2.641   1.00 35.84  ? 8   ARG   A N   1 
ATOM   54   C  CA  . ARG   A 1 28  ? 111.978 45.288 2.340   1.00 33.06  ? 8   ARG   A CA  1 
ATOM   55   C  C   . ARG   A 1 28  ? 111.536 44.442 1.142   1.00 30.48  ? 8   ARG   A C   1 
ATOM   56   O  O   . ARG   A 1 28  ? 110.380 44.022 1.074   1.00 30.32  ? 8   ARG   A O   1 
ATOM   57   C  CB  . ARG   A 1 28  ? 112.285 44.367 3.536   1.00 32.65  ? 8   ARG   A CB  1 
ATOM   58   C  CG  . ARG   A 1 28  ? 112.972 45.057 4.734   1.00 34.21  ? 8   ARG   A CG  1 
ATOM   59   C  CD  . ARG   A 1 28  ? 114.486 45.149 4.594   1.00 34.31  ? 8   ARG   A CD  1 
ATOM   60   N  NE  . ARG   A 1 28  ? 115.163 43.886 4.898   1.00 35.10  ? 8   ARG   A NE  1 
ATOM   61   C  CZ  . ARG   A 1 28  ? 115.573 43.526 6.110   1.00 33.23  ? 8   ARG   A CZ  1 
ATOM   62   N  NH1 . ARG   A 1 28  ? 115.379 44.334 7.155   1.00 31.04  ? 8   ARG   A NH1 1 
ATOM   63   N  NH2 . ARG   A 1 28  ? 116.190 42.366 6.289   1.00 31.98  ? 8   ARG   A NH2 1 
ATOM   64   N  N   . ARG   A 1 29  ? 112.422 44.280 0.166   1.00 28.47  ? 9   ARG   A N   1 
ATOM   65   C  CA  . ARG   A 1 29  ? 112.079 43.549 -1.058  1.00 27.14  ? 9   ARG   A CA  1 
ATOM   66   C  C   . ARG   A 1 29  ? 113.007 42.382 -1.296  1.00 25.22  ? 9   ARG   A C   1 
ATOM   67   O  O   . ARG   A 1 29  ? 114.163 42.406 -0.876  1.00 25.75  ? 9   ARG   A O   1 
ATOM   68   C  CB  . ARG   A 1 29  ? 112.182 44.487 -2.270  1.00 28.24  ? 9   ARG   A CB  1 
ATOM   69   C  CG  . ARG   A 1 29  ? 111.183 45.637 -2.268  1.00 31.22  ? 9   ARG   A CG  1 
ATOM   70   C  CD  . ARG   A 1 29  ? 111.420 46.570 -3.441  1.00 34.40  ? 9   ARG   A CD  1 
ATOM   71   N  NE  . ARG   A 1 29  ? 110.543 47.735 -3.355  1.00 38.92  ? 9   ARG   A NE  1 
ATOM   72   C  CZ  . ARG   A 1 29  ? 109.395 47.861 -4.014  1.00 42.53  ? 9   ARG   A CZ  1 
ATOM   73   N  NH1 . ARG   A 1 29  ? 109.001 46.919 -4.864  1.00 41.67  ? 9   ARG   A NH1 1 
ATOM   74   N  NH2 . ARG   A 1 29  ? 108.657 48.959 -3.871  1.00 43.14  ? 9   ARG   A NH2 1 
ATOM   75   N  N   . THR   A 1 30  ? 112.541 41.408 -2.082  1.00 23.20  ? 10  THR   A N   1 
ATOM   76   C  CA  . THR   A 1 30  ? 113.382 40.281 -2.470  1.00 23.44  ? 10  THR   A CA  1 
ATOM   77   C  C   . THR   A 1 30  ? 114.517 40.786 -3.370  1.00 24.33  ? 10  THR   A C   1 
ATOM   78   O  O   . THR   A 1 30  ? 114.452 41.933 -3.876  1.00 24.96  ? 10  THR   A O   1 
ATOM   79   C  CB  . THR   A 1 30  ? 112.539 39.265 -3.275  1.00 23.67  ? 10  THR   A CB  1 
ATOM   80   O  OG1 . THR   A 1 30  ? 112.123 39.856 -4.523  1.00 24.90  ? 10  THR   A OG1 1 
ATOM   81   C  CG2 . THR   A 1 30  ? 111.323 38.810 -2.518  1.00 24.13  ? 10  THR   A CG2 1 
ATOM   82   N  N   . PRO   A 1 31  ? 115.503 39.918 -3.685  1.00 24.78  ? 11  PRO   A N   1 
ATOM   83   C  CA  . PRO   A 1 31  ? 116.538 40.335 -4.647  1.00 25.58  ? 11  PRO   A CA  1 
ATOM   84   C  C   . PRO   A 1 31  ? 115.943 40.615 -6.038  1.00 26.16  ? 11  PRO   A C   1 
ATOM   85   O  O   . PRO   A 1 31  ? 116.585 41.302 -6.832  1.00 28.10  ? 11  PRO   A O   1 
ATOM   86   C  CB  . PRO   A 1 31  ? 117.514 39.160 -4.664  1.00 26.14  ? 11  PRO   A CB  1 
ATOM   87   C  CG  . PRO   A 1 31  ? 117.287 38.478 -3.323  1.00 26.49  ? 11  PRO   A CG  1 
ATOM   88   C  CD  . PRO   A 1 31  ? 115.802 38.584 -3.121  1.00 24.53  ? 11  PRO   A CD  1 
ATOM   89   N  N   . GLN   A 1 32  ? 114.707 40.144 -6.316  1.00 24.98  ? 12  GLN   A N   1 
ATOM   90   C  CA  . GLN   A 1 32  ? 114.005 40.396 -7.583  1.00 25.47  ? 12  GLN   A CA  1 
ATOM   91   C  C   . GLN   A 1 32  ? 113.040 41.617 -7.491  1.00 27.38  ? 12  GLN   A C   1 
ATOM   92   O  O   . GLN   A 1 32  ? 112.207 41.804 -8.376  1.00 28.20  ? 12  GLN   A O   1 
ATOM   93   C  CB  . GLN   A 1 32  ? 113.287 39.116 -8.088  1.00 25.42  ? 12  GLN   A CB  1 
ATOM   94   C  CG  . GLN   A 1 32  ? 114.201 37.878 -8.219  1.00 25.94  ? 12  GLN   A CG  1 
ATOM   95   C  CD  . GLN   A 1 32  ? 114.568 37.239 -6.889  1.00 24.82  ? 12  GLN   A CD  1 
ATOM   96   O  OE1 . GLN   A 1 32  ? 113.788 37.253 -5.930  1.00 25.27  ? 12  GLN   A OE1 1 
ATOM   97   N  NE2 . GLN   A 1 32  ? 115.778 36.684 -6.805  1.00 24.20  ? 12  GLN   A NE2 1 
ATOM   98   N  N   . SER   A 1 33  ? 113.176 42.412 -6.411  1.00 27.67  ? 13  SER   A N   1 
ATOM   99   C  CA  A SER   A 1 33  ? 112.451 43.646 -6.104  0.44 28.53  ? 13  SER   A CA  1 
ATOM   100  C  CA  B SER   A 1 33  ? 112.436 43.644 -6.145  0.56 27.97  ? 13  SER   A CA  1 
ATOM   101  C  C   . SER   A 1 33  ? 110.954 43.473 -5.798  1.00 28.57  ? 13  SER   A C   1 
ATOM   102  O  O   . SER   A 1 33  ? 110.195 44.431 -5.932  1.00 29.68  ? 13  SER   A O   1 
ATOM   103  C  CB  A SER   A 1 33  ? 112.654 44.703 -7.190  0.44 31.19  ? 13  SER   A CB  1 
ATOM   104  C  CB  B SER   A 1 33  ? 112.585 44.631 -7.301  0.56 29.15  ? 13  SER   A CB  1 
ATOM   105  O  OG  A SER   A 1 33  ? 111.869 44.432 -8.337  0.44 35.16  ? 13  SER   A OG  1 
ATOM   106  O  OG  B SER   A 1 33  ? 113.954 44.825 -7.610  0.56 30.70  ? 13  SER   A OG  1 
ATOM   107  N  N   . ILE   A 1 34  ? 110.541 42.306 -5.286  1.00 26.85  ? 14  ILE   A N   1 
ATOM   108  C  CA  . ILE   A 1 34  ? 109.139 42.120 -4.884  1.00 27.07  ? 14  ILE   A CA  1 
ATOM   109  C  C   . ILE   A 1 34  ? 109.043 42.400 -3.391  1.00 27.20  ? 14  ILE   A C   1 
ATOM   110  O  O   . ILE   A 1 34  ? 109.806 41.791 -2.639  1.00 26.94  ? 14  ILE   A O   1 
ATOM   111  C  CB  . ILE   A 1 34  ? 108.626 40.692 -5.177  1.00 28.41  ? 14  ILE   A CB  1 
ATOM   112  C  CG1 . ILE   A 1 34  ? 108.751 40.381 -6.680  1.00 30.11  ? 14  ILE   A CG1 1 
ATOM   113  C  CG2 . ILE   A 1 34  ? 107.178 40.550 -4.660  1.00 28.79  ? 14  ILE   A CG2 1 
ATOM   114  C  CD1 . ILE   A 1 34  ? 108.115 39.103 -7.152  1.00 32.47  ? 14  ILE   A CD1 1 
ATOM   115  N  N   . PRO   A 1 35  ? 108.121 43.264 -2.909  1.00 27.17  ? 15  PRO   A N   1 
ATOM   116  C  CA  . PRO   A 1 35  ? 108.017 43.472 -1.452  1.00 26.53  ? 15  PRO   A CA  1 
ATOM   117  C  C   . PRO   A 1 35  ? 107.716 42.170 -0.693  1.00 26.39  ? 15  PRO   A C   1 
ATOM   118  O  O   . PRO   A 1 35  ? 106.827 41.411 -1.091  1.00 27.05  ? 15  PRO   A O   1 
ATOM   119  C  CB  . PRO   A 1 35  ? 106.837 44.455 -1.314  1.00 27.56  ? 15  PRO   A CB  1 
ATOM   120  C  CG  . PRO   A 1 35  ? 106.752 45.152 -2.664  1.00 28.78  ? 15  PRO   A CG  1 
ATOM   121  C  CD  . PRO   A 1 35  ? 107.134 44.079 -3.655  1.00 27.38  ? 15  PRO   A CD  1 
ATOM   122  N  N   . TYR   A 1 36  ? 108.463 41.894 0.400   1.00 25.30  ? 16  TYR   A N   1 
ATOM   123  C  CA  . TYR   A 1 36  ? 108.170 40.710 1.220   1.00 25.26  ? 16  TYR   A CA  1 
ATOM   124  C  C   . TYR   A 1 36  ? 106.755 40.774 1.811   1.00 26.31  ? 16  TYR   A C   1 
ATOM   125  O  O   . TYR   A 1 36  ? 106.160 39.717 2.047   1.00 26.50  ? 16  TYR   A O   1 
ATOM   126  C  CB  . TYR   A 1 36  ? 109.211 40.499 2.322   1.00 24.59  ? 16  TYR   A CB  1 
ATOM   127  C  CG  . TYR   A 1 36  ? 110.489 39.882 1.802   1.00 23.39  ? 16  TYR   A CG  1 
ATOM   128  C  CD1 . TYR   A 1 36  ? 110.526 38.558 1.388   1.00 22.44  ? 16  TYR   A CD1 1 
ATOM   129  C  CD2 . TYR   A 1 36  ? 111.640 40.646 1.647   1.00 22.99  ? 16  TYR   A CD2 1 
ATOM   130  C  CE1 . TYR   A 1 36  ? 111.702 37.975 0.928   1.00 22.30  ? 16  TYR   A CE1 1 
ATOM   131  C  CE2 . TYR   A 1 36  ? 112.813 40.086 1.157   1.00 22.89  ? 16  TYR   A CE2 1 
ATOM   132  C  CZ  . TYR   A 1 36  ? 112.831 38.756 0.766   1.00 22.41  ? 16  TYR   A CZ  1 
ATOM   133  O  OH  . TYR   A 1 36  ? 113.968 38.212 0.250   1.00 22.10  ? 16  TYR   A OH  1 
ATOM   134  N  N   . GLN   A 1 37  ? 106.177 41.998 1.989   1.00 26.89  ? 17  GLN   A N   1 
ATOM   135  C  CA  . GLN   A 1 37  ? 104.803 42.090 2.509   1.00 28.61  ? 17  GLN   A CA  1 
ATOM   136  C  C   . GLN   A 1 37  ? 103.763 41.429 1.575   1.00 29.59  ? 17  GLN   A C   1 
ATOM   137  O  O   . GLN   A 1 37  ? 102.676 41.073 2.025   1.00 30.98  ? 17  GLN   A O   1 
ATOM   138  C  CB  . GLN   A 1 37  ? 104.409 43.533 2.845   1.00 30.92  ? 17  GLN   A CB  1 
ATOM   139  C  CG  . GLN   A 1 37  ? 104.393 44.471 1.649   1.00 36.13  ? 17  GLN   A CG  1 
ATOM   140  C  CD  . GLN   A 1 37  ? 104.138 45.911 2.065   1.00 44.06  ? 17  GLN   A CD  1 
ATOM   141  O  OE1 . GLN   A 1 37  ? 104.240 46.293 3.242   1.00 46.72  ? 17  GLN   A OE1 1 
ATOM   142  N  NE2 . GLN   A 1 37  ? 103.816 46.747 1.099   1.00 45.60  ? 17  GLN   A NE2 1 
ATOM   143  N  N   . ASP   A 1 38  ? 104.113 41.222 0.294   1.00 28.52  ? 18  ASP   A N   1 
ATOM   144  C  CA  . ASP   A 1 38  ? 103.222 40.572 -0.668  1.00 28.79  ? 18  ASP   A CA  1 
ATOM   145  C  C   . ASP   A 1 38  ? 103.508 39.072 -0.816  1.00 27.97  ? 18  ASP   A C   1 
ATOM   146  O  O   . ASP   A 1 38  ? 102.987 38.457 -1.740  1.00 28.44  ? 18  ASP   A O   1 
ATOM   147  C  CB  . ASP   A 1 38  ? 103.409 41.218 -2.054  1.00 30.76  ? 18  ASP   A CB  1 
ATOM   148  C  CG  . ASP   A 1 38  ? 103.115 42.708 -2.087  1.00 38.30  ? 18  ASP   A CG  1 
ATOM   149  O  OD1 . ASP   A 1 38  ? 102.437 43.196 -1.167  1.00 38.31  ? 18  ASP   A OD1 1 
ATOM   150  O  OD2 . ASP   A 1 38  ? 103.562 43.379 -3.043  1.00 42.85  ? 18  ASP   A OD2 1 
ATOM   151  N  N   . LEU   A 1 39  ? 104.399 38.494 0.005   1.00 26.29  ? 19  LEU   A N   1 
ATOM   152  C  CA  . LEU   A 1 39  ? 104.778 37.091 -0.143  1.00 26.18  ? 19  LEU   A CA  1 
ATOM   153  C  C   . LEU   A 1 39  ? 104.811 36.408 1.215   1.00 25.93  ? 19  LEU   A C   1 
ATOM   154  O  O   . LEU   A 1 39  ? 105.140 37.049 2.222   1.00 26.47  ? 19  LEU   A O   1 
ATOM   155  C  CB  . LEU   A 1 39  ? 106.210 37.028 -0.711  1.00 27.11  ? 19  LEU   A CB  1 
ATOM   156  C  CG  . LEU   A 1 39  ? 106.451 37.664 -2.068  1.00 29.83  ? 19  LEU   A CG  1 
ATOM   157  C  CD1 . LEU   A 1 39  ? 107.927 37.693 -2.376  1.00 30.79  ? 19  LEU   A CD1 1 
ATOM   158  C  CD2 . LEU   A 1 39  ? 105.703 36.933 -3.161  1.00 31.08  ? 19  LEU   A CD2 1 
ATOM   159  N  N   . PRO   A 1 40  ? 104.601 35.078 1.260   1.00 24.92  ? 20  PRO   A N   1 
ATOM   160  C  CA  . PRO   A 1 40  ? 104.809 34.360 2.529   1.00 24.04  ? 20  PRO   A CA  1 
ATOM   161  C  C   . PRO   A 1 40  ? 106.296 34.452 2.880   1.00 22.51  ? 20  PRO   A C   1 
ATOM   162  O  O   . PRO   A 1 40  ? 107.162 34.293 2.006   1.00 22.68  ? 20  PRO   A O   1 
ATOM   163  C  CB  . PRO   A 1 40  ? 104.415 32.905 2.212   1.00 25.29  ? 20  PRO   A CB  1 
ATOM   164  C  CG  . PRO   A 1 40  ? 103.679 32.963 0.925   1.00 26.35  ? 20  PRO   A CG  1 
ATOM   165  C  CD  . PRO   A 1 40  ? 104.260 34.146 0.168   1.00 25.10  ? 20  PRO   A CD  1 
ATOM   166  N  N   . HIS   A 1 41  ? 106.581 34.768 4.142   1.00 22.00  ? 21  HIS   A N   1 
ATOM   167  C  CA  . HIS   A 1 41  ? 107.966 34.943 4.553   1.00 22.30  ? 21  HIS   A CA  1 
ATOM   168  C  C   . HIS   A 1 41  ? 108.179 34.664 6.015   1.00 22.87  ? 21  HIS   A C   1 
ATOM   169  O  O   . HIS   A 1 41  ? 107.221 34.481 6.785   1.00 25.20  ? 21  HIS   A O   1 
ATOM   170  C  CB  . HIS   A 1 41  ? 108.447 36.374 4.221   1.00 22.51  ? 21  HIS   A CB  1 
ATOM   171  C  CG  . HIS   A 1 41  ? 107.683 37.435 4.959   1.00 24.70  ? 21  HIS   A CG  1 
ATOM   172  N  ND1 . HIS   A 1 41  ? 106.543 37.998 4.424   1.00 26.82  ? 21  HIS   A ND1 1 
ATOM   173  C  CD2 . HIS   A 1 41  ? 107.896 37.970 6.188   1.00 27.37  ? 21  HIS   A CD2 1 
ATOM   174  C  CE1 . HIS   A 1 41  ? 106.121 38.895 5.308   1.00 28.36  ? 21  HIS   A CE1 1 
ATOM   175  N  NE2 . HIS   A 1 41  ? 106.887 38.895 6.400   1.00 28.81  ? 21  HIS   A NE2 1 
ATOM   176  N  N   . LEU   A 1 42  ? 109.442 34.638 6.389   1.00 22.34  ? 22  LEU   A N   1 
ATOM   177  C  CA  A LEU   A 1 42  ? 109.903 34.407 7.751   0.50 24.02  ? 22  LEU   A CA  1 
ATOM   178  C  CA  B LEU   A 1 42  ? 109.857 34.509 7.775   0.50 24.06  ? 22  LEU   A CA  1 
ATOM   179  C  C   . LEU   A 1 42  ? 111.178 35.250 7.940   1.00 25.36  ? 22  LEU   A C   1 
ATOM   180  O  O   . LEU   A 1 42  ? 111.969 35.345 6.997   1.00 27.13  ? 22  LEU   A O   1 
ATOM   181  C  CB  A LEU   A 1 42  ? 110.241 32.909 7.877   0.50 24.53  ? 22  LEU   A CB  1 
ATOM   182  C  CB  B LEU   A 1 42  ? 109.926 33.046 8.247   0.50 24.66  ? 22  LEU   A CB  1 
ATOM   183  C  CG  A LEU   A 1 42  ? 110.453 32.372 9.279   0.50 27.01  ? 22  LEU   A CG  1 
ATOM   184  C  CG  B LEU   A 1 42  ? 111.155 32.223 7.899   0.50 26.83  ? 22  LEU   A CG  1 
ATOM   185  C  CD1 A LEU   A 1 42  ? 109.162 32.428 10.075  0.50 27.60  ? 22  LEU   A CD1 1 
ATOM   186  C  CD1 B LEU   A 1 42  ? 112.293 32.487 8.875   0.50 28.36  ? 22  LEU   A CD1 1 
ATOM   187  C  CD2 A LEU   A 1 42  ? 110.963 30.943 9.223   0.50 27.46  ? 22  LEU   A CD2 1 
ATOM   188  C  CD2 B LEU   A 1 42  ? 110.836 30.747 8.026   0.50 27.56  ? 22  LEU   A CD2 1 
ATOM   189  N  N   . VAL   A 1 43  ? 111.400 35.845 9.115   1.00 22.92  ? 23  VAL   A N   1 
ATOM   190  C  CA  . VAL   A 1 43  ? 112.648 36.591 9.345   1.00 22.74  ? 23  VAL   A CA  1 
ATOM   191  C  C   . VAL   A 1 43  ? 113.530 35.685 10.201  1.00 23.17  ? 23  VAL   A C   1 
ATOM   192  O  O   . VAL   A 1 43  ? 113.094 35.265 11.271  1.00 23.35  ? 23  VAL   A O   1 
ATOM   193  C  CB  . VAL   A 1 43  ? 112.435 37.956 10.008  1.00 23.61  ? 23  VAL   A CB  1 
ATOM   194  C  CG1 . VAL   A 1 43  ? 113.765 38.670 10.160  1.00 23.83  ? 23  VAL   A CG1 1 
ATOM   195  C  CG2 . VAL   A 1 43  ? 111.470 38.815 9.193   1.00 23.26  ? 23  VAL   A CG2 1 
ATOM   196  N  N   . ASN   A 1 44  ? 114.740 35.387 9.741   1.00 22.61  ? 24  ASN   A N   1 
ATOM   197  C  CA  . ASN   A 1 44  ? 115.612 34.486 10.488  1.00 22.57  ? 24  ASN   A CA  1 
ATOM   198  C  C   . ASN   A 1 44  ? 116.319 35.206 11.681  1.00 23.45  ? 24  ASN   A C   1 
ATOM   199  O  O   . ASN   A 1 44  ? 116.114 36.412 11.923  1.00 23.92  ? 24  ASN   A O   1 
ATOM   200  C  CB  . ASN   A 1 44  ? 116.576 33.747 9.563   1.00 23.19  ? 24  ASN   A CB  1 
ATOM   201  C  CG  . ASN   A 1 44  ? 117.737 34.567 9.082   1.00 24.03  ? 24  ASN   A CG  1 
ATOM   202  O  OD1 . ASN   A 1 44  ? 117.945 35.714 9.492   1.00 24.02  ? 24  ASN   A OD1 1 
ATOM   203  N  ND2 . ASN   A 1 44  ? 118.539 33.965 8.212   1.00 23.08  ? 24  ASN   A ND2 1 
ATOM   204  N  N   . ALA   A 1 45  ? 117.135 34.451 12.436  1.00 24.51  ? 25  ALA   A N   1 
ATOM   205  C  CA  . ALA   A 1 45  ? 117.833 34.984 13.617  1.00 26.01  ? 25  ALA   A CA  1 
ATOM   206  C  C   . ALA   A 1 45  ? 118.823 36.109 13.304  1.00 27.30  ? 25  ALA   A C   1 
ATOM   207  O  O   . ALA   A 1 45  ? 119.178 36.887 14.195  1.00 28.87  ? 25  ALA   A O   1 
ATOM   208  C  CB  . ALA   A 1 45  ? 118.533 33.859 14.349  1.00 26.38  ? 25  ALA   A CB  1 
ATOM   209  N  N   . ASP   A 1 46  ? 119.286 36.175 12.049  1.00 26.97  ? 26  ASP   A N   1 
ATOM   210  C  CA  . ASP   A 1 46  ? 120.176 37.231 11.591  1.00 27.43  ? 26  ASP   A CA  1 
ATOM   211  C  C   . ASP   A 1 46  ? 119.423 38.442 11.006  1.00 28.15  ? 26  ASP   A C   1 
ATOM   212  O  O   . ASP   A 1 46  ? 120.065 39.357 10.498  1.00 29.59  ? 26  ASP   A O   1 
ATOM   213  C  CB  . ASP   A 1 46  ? 121.192 36.684 10.582  1.00 29.00  ? 26  ASP   A CB  1 
ATOM   214  C  CG  . ASP   A 1 46  ? 122.134 35.687 11.214  1.00 33.75  ? 26  ASP   A CG  1 
ATOM   215  O  OD1 . ASP   A 1 46  ? 122.525 35.901 12.376  1.00 37.49  ? 26  ASP   A OD1 1 
ATOM   216  O  OD2 . ASP   A 1 46  ? 122.480 34.688 10.545  1.00 34.62  ? 26  ASP   A OD2 1 
ATOM   217  N  N   . GLY   A 1 47  ? 118.094 38.472 11.119  1.00 26.86  ? 27  GLY   A N   1 
ATOM   218  C  CA  . GLY   A 1 47  ? 117.287 39.571 10.595  1.00 26.72  ? 27  GLY   A CA  1 
ATOM   219  C  C   . GLY   A 1 47  ? 117.094 39.532 9.090   1.00 26.29  ? 27  GLY   A C   1 
ATOM   220  O  O   . GLY   A 1 47  ? 116.717 40.543 8.497   1.00 27.12  ? 27  GLY   A O   1 
ATOM   221  N  N   . GLN   A 1 48  ? 117.333 38.358 8.457   1.00 24.79  ? 28  GLN   A N   1 
ATOM   222  C  CA  . GLN   A 1 48  ? 117.199 38.205 7.001   1.00 23.76  ? 28  GLN   A CA  1 
ATOM   223  C  C   . GLN   A 1 48  ? 115.855 37.604 6.649   1.00 23.23  ? 28  GLN   A C   1 
ATOM   224  O  O   . GLN   A 1 48  ? 115.417 36.669 7.306   1.00 23.33  ? 28  GLN   A O   1 
ATOM   225  C  CB  . GLN   A 1 48  ? 118.294 37.292 6.428   1.00 24.82  ? 28  GLN   A CB  1 
ATOM   226  C  CG  . GLN   A 1 48  ? 119.689 37.850 6.627   1.00 25.81  ? 28  GLN   A CG  1 
ATOM   227  C  CD  . GLN   A 1 48  ? 120.745 36.813 6.337   1.00 26.74  ? 28  GLN   A CD  1 
ATOM   228  O  OE1 . GLN   A 1 48  ? 120.751 35.728 6.932   1.00 26.75  ? 28  GLN   A OE1 1 
ATOM   229  N  NE2 . GLN   A 1 48  ? 121.664 37.146 5.437   1.00 26.60  ? 28  GLN   A NE2 1 
ATOM   230  N  N   . TYR   A 1 49  ? 115.207 38.128 5.608   1.00 22.67  ? 29  TYR   A N   1 
ATOM   231  C  CA  . TYR   A 1 49  ? 113.926 37.590 5.169   1.00 21.58  ? 29  TYR   A CA  1 
ATOM   232  C  C   . TYR   A 1 49  ? 114.136 36.364 4.324   1.00 21.58  ? 29  TYR   A C   1 
ATOM   233  O  O   . TYR   A 1 49  ? 114.920 36.386 3.374   1.00 21.83  ? 29  TYR   A O   1 
ATOM   234  C  CB  . TYR   A 1 49  ? 113.163 38.613 4.337   1.00 21.53  ? 29  TYR   A CB  1 
ATOM   235  C  CG  . TYR   A 1 49  ? 112.443 39.661 5.153   1.00 22.35  ? 29  TYR   A CG  1 
ATOM   236  C  CD1 . TYR   A 1 49  ? 113.144 40.661 5.813   1.00 23.11  ? 29  TYR   A CD1 1 
ATOM   237  C  CD2 . TYR   A 1 49  ? 111.060 39.670 5.244   1.00 23.23  ? 29  TYR   A CD2 1 
ATOM   238  C  CE1 . TYR   A 1 49  ? 112.484 41.644 6.541   1.00 23.74  ? 29  TYR   A CE1 1 
ATOM   239  C  CE2 . TYR   A 1 49  ? 110.386 40.676 5.930   1.00 23.63  ? 29  TYR   A CE2 1 
ATOM   240  C  CZ  . TYR   A 1 49  ? 111.102 41.668 6.571   1.00 24.40  ? 29  TYR   A CZ  1 
ATOM   241  O  OH  . TYR   A 1 49  ? 110.445 42.638 7.307   1.00 25.45  ? 29  TYR   A OH  1 
ATOM   242  N  N   . LEU   A 1 50  ? 113.395 35.305 4.657   1.00 20.51  ? 30  LEU   A N   1 
ATOM   243  C  CA  . LEU   A 1 50  ? 113.381 34.088 3.853   1.00 20.24  ? 30  LEU   A CA  1 
ATOM   244  C  C   . LEU   A 1 50  ? 112.032 33.975 3.187   1.00 20.67  ? 30  LEU   A C   1 
ATOM   245  O  O   . LEU   A 1 50  ? 111.006 34.143 3.839   1.00 21.88  ? 30  LEU   A O   1 
ATOM   246  C  CB  . LEU   A 1 50  ? 113.584 32.813 4.704   1.00 20.47  ? 30  LEU   A CB  1 
ATOM   247  C  CG  . LEU   A 1 50  ? 114.836 32.791 5.571   1.00 22.78  ? 30  LEU   A CG  1 
ATOM   248  C  CD1 . LEU   A 1 50  ? 114.998 31.451 6.262   1.00 24.00  ? 30  LEU   A CD1 1 
ATOM   249  C  CD2 . LEU   A 1 50  ? 116.095 33.114 4.758   1.00 23.43  ? 30  LEU   A CD2 1 
ATOM   250  N  N   . PHE   A 1 51  ? 112.022 33.698 1.890   1.00 19.36  ? 31  PHE   A N   1 
ATOM   251  C  CA  . PHE   A 1 51  ? 110.776 33.510 1.155   1.00 19.49  ? 31  PHE   A CA  1 
ATOM   252  C  C   . PHE   A 1 51  ? 110.286 32.088 1.481   1.00 19.05  ? 31  PHE   A C   1 
ATOM   253  O  O   . PHE   A 1 51  ? 111.078 31.147 1.388   1.00 19.40  ? 31  PHE   A O   1 
ATOM   254  C  CB  . PHE   A 1 51  ? 111.063 33.630 -0.346  1.00 19.65  ? 31  PHE   A CB  1 
ATOM   255  C  CG  . PHE   A 1 51  ? 109.938 33.116 -1.204  1.00 20.80  ? 31  PHE   A CG  1 
ATOM   256  C  CD1 . PHE   A 1 51  ? 108.822 33.896 -1.448  1.00 22.44  ? 31  PHE   A CD1 1 
ATOM   257  C  CD2 . PHE   A 1 51  ? 110.003 31.857 -1.770  1.00 21.68  ? 31  PHE   A CD2 1 
ATOM   258  C  CE1 . PHE   A 1 51  ? 107.776 33.411 -2.223  1.00 23.87  ? 31  PHE   A CE1 1 
ATOM   259  C  CE2 . PHE   A 1 51  ? 108.951 31.369 -2.532  1.00 22.86  ? 31  PHE   A CE2 1 
ATOM   260  C  CZ  . PHE   A 1 51  ? 107.846 32.147 -2.744  1.00 23.31  ? 31  PHE   A CZ  1 
ATOM   261  N  N   . CYS   A 1 52  ? 108.983 31.948 1.751   1.00 18.73  ? 32  CYS   A N   1 
ATOM   262  C  CA  . CYS   A 1 52  ? 108.353 30.677 2.121   1.00 19.39  ? 32  CYS   A CA  1 
ATOM   263  C  C   . CYS   A 1 52  ? 107.318 30.210 1.116   1.00 20.72  ? 32  CYS   A C   1 
ATOM   264  O  O   . CYS   A 1 52  ? 106.650 31.026 0.465   1.00 21.45  ? 32  CYS   A O   1 
ATOM   265  C  CB  . CYS   A 1 52  ? 107.721 30.781 3.505   1.00 20.24  ? 32  CYS   A CB  1 
ATOM   266  S  SG  . CYS   A 1 52  ? 108.894 31.196 4.810   1.00 23.26  ? 32  CYS   A SG  1 
ATOM   267  N  N   . ARG   A 1 53  ? 107.103 28.890 1.099   1.00 20.09  ? 33  ARG   A N   1 
ATOM   268  C  CA  . ARG   A 1 53  ? 106.076 28.235 0.286   1.00 20.64  ? 33  ARG   A CA  1 
ATOM   269  C  C   . ARG   A 1 53  ? 105.314 27.230 1.125   1.00 22.14  ? 33  ARG   A C   1 
ATOM   270  O  O   . ARG   A 1 53  ? 105.906 26.569 1.988   1.00 21.57  ? 33  ARG   A O   1 
ATOM   271  C  CB  . ARG   A 1 53  ? 106.674 27.457 -0.886  1.00 21.44  ? 33  ARG   A CB  1 
ATOM   272  C  CG  . ARG   A 1 53  ? 107.195 28.339 -1.959  1.00 24.18  ? 33  ARG   A CG  1 
ATOM   273  C  CD  . ARG   A 1 53  ? 107.538 27.469 -3.161  1.00 24.84  ? 33  ARG   A CD  1 
ATOM   274  N  NE  . ARG   A 1 53  ? 108.402 28.234 -4.037  1.00 25.65  ? 33  ARG   A NE  1 
ATOM   275  C  CZ  . ARG   A 1 53  ? 107.960 28.986 -5.040  1.00 27.35  ? 33  ARG   A CZ  1 
ATOM   276  N  NH1 . ARG   A 1 53  ? 106.667 28.982 -5.367  1.00 27.46  ? 33  ARG   A NH1 1 
ATOM   277  N  NH2 . ARG   A 1 53  ? 108.812 29.712 -5.757  1.00 26.54  ? 33  ARG   A NH2 1 
ATOM   278  N  N   . TYR   A 1 54  ? 104.000 27.116 0.869   1.00 22.57  ? 34  TYR   A N   1 
ATOM   279  C  CA  . TYR   A 1 54  ? 103.112 26.205 1.574   1.00 24.09  ? 34  TYR   A CA  1 
ATOM   280  C  C   . TYR   A 1 54  ? 102.181 25.517 0.598   1.00 25.60  ? 34  TYR   A C   1 
ATOM   281  O  O   . TYR   A 1 54  ? 101.676 26.156 -0.326  1.00 26.25  ? 34  TYR   A O   1 
ATOM   282  C  CB  . TYR   A 1 54  ? 102.252 26.967 2.604   1.00 23.81  ? 34  TYR   A CB  1 
ATOM   283  C  CG  . TYR   A 1 54  ? 103.112 27.684 3.616   1.00 23.47  ? 34  TYR   A CG  1 
ATOM   284  C  CD1 . TYR   A 1 54  ? 103.685 26.996 4.677   1.00 23.64  ? 34  TYR   A CD1 1 
ATOM   285  C  CD2 . TYR   A 1 54  ? 103.450 29.023 3.450   1.00 24.18  ? 34  TYR   A CD2 1 
ATOM   286  C  CE1 . TYR   A 1 54  ? 104.555 27.620 5.559   1.00 24.37  ? 34  TYR   A CE1 1 
ATOM   287  C  CE2 . TYR   A 1 54  ? 104.319 29.660 4.328   1.00 24.99  ? 34  TYR   A CE2 1 
ATOM   288  C  CZ  . TYR   A 1 54  ? 104.884 28.947 5.371   1.00 25.26  ? 34  TYR   A CZ  1 
ATOM   289  O  OH  . TYR   A 1 54  ? 105.753 29.562 6.245   1.00 26.19  ? 34  TYR   A OH  1 
ATOM   290  N  N   . TRP   A 1 55  ? 101.972 24.207 0.796   1.00 25.11  ? 35  TRP   A N   1 
ATOM   291  C  CA  . TRP   A 1 55  ? 101.024 23.411 0.033   1.00 26.35  ? 35  TRP   A CA  1 
ATOM   292  C  C   . TRP   A 1 55  ? 100.225 22.623 1.079   1.00 28.16  ? 35  TRP   A C   1 
ATOM   293  O  O   . TRP   A 1 55  ? 100.700 21.620 1.613   1.00 28.64  ? 35  TRP   A O   1 
ATOM   294  C  CB  . TRP   A 1 55  ? 101.729 22.471 -0.927  1.00 25.82  ? 35  TRP   A CB  1 
ATOM   295  C  CG  . TRP   A 1 55  ? 102.604 23.112 -1.967  1.00 25.43  ? 35  TRP   A CG  1 
ATOM   296  C  CD1 . TRP   A 1 55  ? 102.301 23.279 -3.286  1.00 26.85  ? 35  TRP   A CD1 1 
ATOM   297  C  CD2 . TRP   A 1 55  ? 104.008 23.390 -1.842  1.00 24.45  ? 35  TRP   A CD2 1 
ATOM   298  N  NE1 . TRP   A 1 55  ? 103.416 23.688 -3.982  1.00 26.67  ? 35  TRP   A NE1 1 
ATOM   299  C  CE2 . TRP   A 1 55  ? 104.479 23.759 -3.117  1.00 25.22  ? 35  TRP   A CE2 1 
ATOM   300  C  CE3 . TRP   A 1 55  ? 104.916 23.346 -0.774  1.00 23.85  ? 35  TRP   A CE3 1 
ATOM   301  C  CZ2 . TRP   A 1 55  ? 105.812 24.105 -3.350  1.00 24.90  ? 35  TRP   A CZ2 1 
ATOM   302  C  CZ3 . TRP   A 1 55  ? 106.233 23.691 -1.006  1.00 23.56  ? 35  TRP   A CZ3 1 
ATOM   303  C  CH2 . TRP   A 1 55  ? 106.678 24.027 -2.288  1.00 24.31  ? 35  TRP   A CH2 1 
ATOM   304  N  N   . ALA   A 1 56  ? 99.033  23.106 1.417   1.00 29.09  ? 36  ALA   A N   1 
ATOM   305  C  CA  . ALA   A 1 56  ? 98.218  22.501 2.465   1.00 31.83  ? 36  ALA   A CA  1 
ATOM   306  C  C   . ALA   A 1 56  ? 97.000  21.804 1.900   1.00 34.47  ? 36  ALA   A C   1 
ATOM   307  O  O   . ALA   A 1 56  ? 96.372  22.322 0.983   1.00 35.48  ? 36  ALA   A O   1 
ATOM   308  C  CB  . ALA   A 1 56  ? 97.794  23.568 3.478   1.00 31.97  ? 36  ALA   A CB  1 
ATOM   309  N  N   . PRO   A 1 57  ? 96.644  20.625 2.441   1.00 35.77  ? 37  PRO   A N   1 
ATOM   310  C  CA  . PRO   A 1 57  ? 95.430  19.941 1.970   1.00 37.33  ? 37  PRO   A CA  1 
ATOM   311  C  C   . PRO   A 1 57  ? 94.146  20.622 2.473   1.00 40.08  ? 37  PRO   A C   1 
ATOM   312  O  O   . PRO   A 1 57  ? 94.203  21.478 3.360   1.00 39.84  ? 37  PRO   A O   1 
ATOM   313  C  CB  . PRO   A 1 57  ? 95.580  18.535 2.560   1.00 37.86  ? 37  PRO   A CB  1 
ATOM   314  C  CG  . PRO   A 1 57  ? 96.321  18.752 3.841   1.00 37.58  ? 37  PRO   A CG  1 
ATOM   315  C  CD  . PRO   A 1 57  ? 97.290  19.891 3.549   1.00 35.61  ? 37  PRO   A CD  1 
ATOM   316  N  N   . THR   A 1 58  ? 92.980  20.230 1.925   1.00 42.73  ? 38  THR   A N   1 
ATOM   317  C  CA  . THR   A 1 58  ? 91.710  20.820 2.357   1.00 45.88  ? 38  THR   A CA  1 
ATOM   318  C  C   . THR   A 1 58  ? 91.269  20.315 3.742   1.00 48.37  ? 38  THR   A C   1 
ATOM   319  O  O   . THR   A 1 58  ? 90.588  21.035 4.462   1.00 49.55  ? 38  THR   A O   1 
ATOM   320  C  CB  . THR   A 1 58  ? 90.620  20.655 1.289   1.00 47.68  ? 38  THR   A CB  1 
ATOM   321  O  OG1 . THR   A 1 58  ? 90.424  19.265 1.017   1.00 49.32  ? 38  THR   A OG1 1 
ATOM   322  C  CG2 . THR   A 1 58  ? 90.962  21.391 0.002   1.00 48.20  ? 38  THR   A CG2 1 
ATOM   323  N  N   . GLY   A 1 59  ? 91.666  19.103 4.109   1.00 49.50  ? 39  GLY   A N   1 
ATOM   324  C  CA  . GLY   A 1 59  ? 91.310  18.543 5.408   1.00 50.57  ? 39  GLY   A CA  1 
ATOM   325  C  C   . GLY   A 1 59  ? 92.385  18.749 6.457   1.00 50.80  ? 39  GLY   A C   1 
ATOM   326  O  O   . GLY   A 1 59  ? 93.367  19.461 6.218   1.00 51.73  ? 39  GLY   A O   1 
ATOM   327  N  N   . THR   A 1 60  ? 92.211  18.129 7.632   1.00 49.40  ? 40  THR   A N   1 
ATOM   328  C  CA  . THR   A 1 60  ? 93.198  18.219 8.705   1.00 48.28  ? 40  THR   A CA  1 
ATOM   329  C  C   . THR   A 1 60  ? 94.431  17.437 8.258   1.00 45.47  ? 40  THR   A C   1 
ATOM   330  O  O   . THR   A 1 60  ? 94.294  16.300 7.795   1.00 45.37  ? 40  THR   A O   1 
ATOM   331  C  CB  . THR   A 1 60  ? 92.619  17.620 9.991   1.00 50.77  ? 40  THR   A CB  1 
ATOM   332  O  OG1 . THR   A 1 60  ? 91.424  18.328 10.341  1.00 52.05  ? 40  THR   A OG1 1 
ATOM   333  C  CG2 . THR   A 1 60  ? 93.614  17.645 11.147  1.00 51.49  ? 40  THR   A CG2 1 
ATOM   334  N  N   . PRO   A 1 61  ? 95.628  18.038 8.311   1.00 43.09  ? 41  PRO   A N   1 
ATOM   335  C  CA  . PRO   A 1 61  ? 96.814  17.306 7.847   1.00 41.47  ? 41  PRO   A CA  1 
ATOM   336  C  C   . PRO   A 1 61  ? 97.131  16.118 8.737   1.00 39.86  ? 41  PRO   A C   1 
ATOM   337  O  O   . PRO   A 1 61  ? 96.902  16.157 9.943   1.00 40.30  ? 41  PRO   A O   1 
ATOM   338  C  CB  . PRO   A 1 61  ? 97.942  18.347 7.876   1.00 42.31  ? 41  PRO   A CB  1 
ATOM   339  C  CG  . PRO   A 1 61  ? 97.279  19.673 8.167   1.00 43.05  ? 41  PRO   A CG  1 
ATOM   340  C  CD  . PRO   A 1 61  ? 95.962  19.386 8.805   1.00 42.00  ? 41  PRO   A CD  1 
ATOM   341  N  N   . LYS   A 1 62  ? 97.617  15.053 8.128   1.00 37.47  ? 42  LYS   A N   1 
ATOM   342  C  CA  . LYS   A 1 62  ? 98.068  13.863 8.841   1.00 36.14  ? 42  LYS   A CA  1 
ATOM   343  C  C   . LYS   A 1 62  ? 99.470  14.102 9.421   1.00 33.81  ? 42  LYS   A C   1 
ATOM   344  O  O   . LYS   A 1 62  ? 99.840  13.480 10.411  1.00 34.31  ? 42  LYS   A O   1 
ATOM   345  C  CB  . LYS   A 1 62  ? 98.190  12.684 7.870   1.00 38.91  ? 42  LYS   A CB  1 
ATOM   346  C  CG  . LYS   A 1 62  ? 96.874  12.154 7.344   1.00 44.56  ? 42  LYS   A CG  1 
ATOM   347  C  CD  . LYS   A 1 62  ? 97.144  10.903 6.520   1.00 50.83  ? 42  LYS   A CD  1 
ATOM   348  C  CE  . LYS   A 1 62  ? 95.898  10.282 5.933   1.00 56.09  ? 42  LYS   A CE  1 
ATOM   349  N  NZ  . LYS   A 1 62  ? 96.210  9.542  4.675   1.00 59.06  ? 42  LYS   A NZ  1 
ATOM   350  N  N   . ALA   A 1 63  ? 100.285 14.940 8.748   1.00 30.67  ? 43  ALA   A N   1 
ATOM   351  C  CA  . ALA   A 1 63  ? 101.659 15.202 9.135   1.00 28.72  ? 43  ALA   A CA  1 
ATOM   352  C  C   . ALA   A 1 63  ? 102.154 16.470 8.423   1.00 28.01  ? 43  ALA   A C   1 
ATOM   353  O  O   . ALA   A 1 63  ? 101.513 16.950 7.486   1.00 28.21  ? 43  ALA   A O   1 
ATOM   354  C  CB  . ALA   A 1 63  ? 102.542 14.004 8.723   1.00 28.12  ? 43  ALA   A CB  1 
ATOM   355  N  N   . LEU   A 1 64  ? 103.296 17.004 8.861   1.00 26.81  ? 44  LEU   A N   1 
ATOM   356  C  CA  . LEU   A 1 64  ? 103.951 18.136 8.217   1.00 25.83  ? 44  LEU   A CA  1 
ATOM   357  C  C   . LEU   A 1 64  ? 105.206 17.605 7.523   1.00 23.88  ? 44  LEU   A C   1 
ATOM   358  O  O   . LEU   A 1 64  ? 105.814 16.660 8.015   1.00 23.98  ? 44  LEU   A O   1 
ATOM   359  C  CB  . LEU   A 1 64  ? 104.433 19.125 9.272   1.00 27.42  ? 44  LEU   A CB  1 
ATOM   360  C  CG  . LEU   A 1 64  ? 103.353 19.690 10.174  1.00 30.49  ? 44  LEU   A CG  1 
ATOM   361  C  CD1 . LEU   A 1 64  ? 103.967 20.546 11.284  1.00 31.32  ? 44  LEU   A CD1 1 
ATOM   362  C  CD2 . LEU   A 1 64  ? 102.373 20.508 9.377   1.00 32.14  ? 44  LEU   A CD2 1 
ATOM   363  N  N   . ILE   A 1 65  ? 105.649 18.279 6.452   1.00 22.49  ? 45  ILE   A N   1 
ATOM   364  C  CA  . ILE   A 1 65  ? 106.893 17.873 5.794   1.00 21.77  ? 45  ILE   A CA  1 
ATOM   365  C  C   . ILE   A 1 65  ? 107.611 19.086 5.244   1.00 21.71  ? 45  ILE   A C   1 
ATOM   366  O  O   . ILE   A 1 65  ? 107.032 19.841 4.476   1.00 21.67  ? 45  ILE   A O   1 
ATOM   367  C  CB  . ILE   A 1 65  ? 106.723 16.732 4.755   1.00 22.01  ? 45  ILE   A CB  1 
ATOM   368  C  CG1 . ILE   A 1 65  ? 108.093 16.302 4.155   1.00 23.06  ? 45  ILE   A CG1 1 
ATOM   369  C  CG2 . ILE   A 1 65  ? 105.718 17.092 3.663   1.00 22.51  ? 45  ILE   A CG2 1 
ATOM   370  C  CD1 . ILE   A 1 65  ? 108.017 14.942 3.423   1.00 23.46  ? 45  ILE   A CD1 1 
ATOM   371  N  N   . PHE   A 1 66  ? 108.855 19.294 5.683   1.00 20.93  ? 46  PHE   A N   1 
ATOM   372  C  CA  . PHE   A 1 66  ? 109.667 20.407 5.193   1.00 20.39  ? 46  PHE   A CA  1 
ATOM   373  C  C   . PHE   A 1 66  ? 110.509 19.939 4.018   1.00 20.01  ? 46  PHE   A C   1 
ATOM   374  O  O   . PHE   A 1 66  ? 111.166 18.894 4.111   1.00 20.01  ? 46  PHE   A O   1 
ATOM   375  C  CB  . PHE   A 1 66  ? 110.606 20.936 6.291   1.00 20.20  ? 46  PHE   A CB  1 
ATOM   376  C  CG  . PHE   A 1 66  ? 111.434 22.113 5.808   1.00 20.37  ? 46  PHE   A CG  1 
ATOM   377  C  CD1 . PHE   A 1 66  ? 110.936 23.411 5.870   1.00 21.13  ? 46  PHE   A CD1 1 
ATOM   378  C  CD2 . PHE   A 1 66  ? 112.715 21.924 5.307   1.00 21.24  ? 46  PHE   A CD2 1 
ATOM   379  C  CE1 . PHE   A 1 66  ? 111.697 24.490 5.401   1.00 21.35  ? 46  PHE   A CE1 1 
ATOM   380  C  CE2 . PHE   A 1 66  ? 113.463 23.006 4.830   1.00 21.63  ? 46  PHE   A CE2 1 
ATOM   381  C  CZ  . PHE   A 1 66  ? 112.956 24.279 4.909   1.00 20.93  ? 46  PHE   A CZ  1 
ATOM   382  N  N   . VAL   A 1 67  ? 110.505 20.712 2.933   1.00 19.35  ? 47  VAL   A N   1 
ATOM   383  C  CA  . VAL   A 1 67  ? 111.293 20.415 1.746   1.00 20.13  ? 47  VAL   A CA  1 
ATOM   384  C  C   . VAL   A 1 67  ? 112.514 21.351 1.717   1.00 20.35  ? 47  VAL   A C   1 
ATOM   385  O  O   . VAL   A 1 67  ? 112.365 22.583 1.738   1.00 20.12  ? 47  VAL   A O   1 
ATOM   386  C  CB  . VAL   A 1 67  ? 110.440 20.554 0.473   1.00 22.13  ? 47  VAL   A CB  1 
ATOM   387  C  CG1 . VAL   A 1 67  ? 111.328 20.463 -0.776  1.00 23.85  ? 47  VAL   A CG1 1 
ATOM   388  C  CG2 . VAL   A 1 67  ? 109.348 19.488 0.439   1.00 22.79  ? 47  VAL   A CG2 1 
ATOM   389  N  N   . SER   A 1 68  ? 113.713 20.756 1.654   1.00 19.26  ? 48  SER   A N   1 
ATOM   390  C  CA  . SER   A 1 68  ? 115.004 21.421 1.696   1.00 18.58  ? 48  SER   A CA  1 
ATOM   391  C  C   . SER   A 1 68  ? 115.723 21.319 0.351   1.00 18.62  ? 48  SER   A C   1 
ATOM   392  O  O   . SER   A 1 68  ? 116.164 20.232 -0.050  1.00 18.73  ? 48  SER   A O   1 
ATOM   393  C  CB  . SER   A 1 68  ? 115.847 20.813 2.813   1.00 20.40  ? 48  SER   A CB  1 
ATOM   394  O  OG  . SER   A 1 68  ? 117.103 21.454 2.931   1.00 21.65  ? 48  SER   A OG  1 
ATOM   395  N  N   . HIS   A 1 69  ? 115.745 22.430 -0.406  1.00 18.08  ? 49  HIS   A N   1 
ATOM   396  C  CA  . HIS   A 1 69  ? 116.348 22.473 -1.742  1.00 17.21  ? 49  HIS   A CA  1 
ATOM   397  C  C   . HIS   A 1 69  ? 117.885 22.481 -1.708  1.00 17.94  ? 49  HIS   A C   1 
ATOM   398  O  O   . HIS   A 1 69  ? 118.493 22.645 -0.652  1.00 18.85  ? 49  HIS   A O   1 
ATOM   399  C  CB  . HIS   A 1 69  ? 115.782 23.672 -2.550  1.00 17.20  ? 49  HIS   A CB  1 
ATOM   400  C  CG  . HIS   A 1 69  ? 116.302 25.005 -2.120  1.00 17.67  ? 49  HIS   A CG  1 
ATOM   401  N  ND1 . HIS   A 1 69  ? 117.585 25.411 -2.451  1.00 18.49  ? 49  HIS   A ND1 1 
ATOM   402  C  CD2 . HIS   A 1 69  ? 115.679 26.003 -1.436  1.00 18.23  ? 49  HIS   A CD2 1 
ATOM   403  C  CE1 . HIS   A 1 69  ? 117.698 26.658 -1.992  1.00 19.49  ? 49  HIS   A CE1 1 
ATOM   404  N  NE2 . HIS   A 1 69  ? 116.573 27.058 -1.368  1.00 18.49  ? 49  HIS   A NE2 1 
ATOM   405  N  N   . GLY   A 1 70  ? 118.500 22.277 -2.867  1.00 19.13  ? 50  GLY   A N   1 
ATOM   406  C  CA  . GLY   A 1 70  ? 119.946 22.210 -2.972  1.00 20.10  ? 50  GLY   A CA  1 
ATOM   407  C  C   . GLY   A 1 70  ? 120.628 23.515 -3.339  1.00 19.96  ? 50  GLY   A C   1 
ATOM   408  O  O   . GLY   A 1 70  ? 119.999 24.579 -3.456  1.00 19.61  ? 50  GLY   A O   1 
ATOM   409  N  N   . ALA   A 1 71  ? 121.949 23.436 -3.510  1.00 20.19  ? 51  ALA   A N   1 
ATOM   410  C  CA  . ALA   A 1 71  ? 122.775 24.608 -3.793  1.00 20.84  ? 51  ALA   A CA  1 
ATOM   411  C  C   . ALA   A 1 71  ? 122.428 25.232 -5.130  1.00 21.49  ? 51  ALA   A C   1 
ATOM   412  O  O   . ALA   A 1 71  ? 122.146 24.532 -6.096  1.00 21.92  ? 51  ALA   A O   1 
ATOM   413  C  CB  . ALA   A 1 71  ? 124.249 24.244 -3.778  1.00 21.44  ? 51  ALA   A CB  1 
ATOM   414  N  N   . GLY   A 1 72  ? 122.358 26.549 -5.129  1.00 20.82  ? 52  GLY   A N   1 
ATOM   415  C  CA  . GLY   A 1 72  ? 122.078 27.321 -6.325  1.00 21.58  ? 52  GLY   A CA  1 
ATOM   416  C  C   . GLY   A 1 72  ? 120.648 27.316 -6.789  1.00 21.97  ? 52  GLY   A C   1 
ATOM   417  O  O   . GLY   A 1 72  ? 120.298 28.171 -7.604  1.00 24.16  ? 52  GLY   A O   1 
ATOM   418  N  N   . GLU   A 1 73  ? 119.808 26.400 -6.287  1.00 20.33  ? 53  GLU   A N   1 
ATOM   419  C  CA  . GLU   A 1 73  ? 118.423 26.362 -6.772  1.00 19.83  ? 53  GLU   A CA  1 
ATOM   420  C  C   . GLU   A 1 73  ? 117.476 27.010 -5.733  1.00 19.63  ? 53  GLU   A C   1 
ATOM   421  O  O   . GLU   A 1 73  ? 117.898 27.951 -5.036  1.00 20.25  ? 53  GLU   A O   1 
ATOM   422  C  CB  . GLU   A 1 73  ? 118.006 24.942 -7.252  1.00 20.31  ? 53  GLU   A CB  1 
ATOM   423  C  CG  . GLU   A 1 73  ? 118.093 23.912 -6.141  1.00 20.97  ? 53  GLU   A CG  1 
ATOM   424  C  CD  . GLU   A 1 73  ? 117.197 22.693 -6.271  1.00 25.15  ? 53  GLU   A CD  1 
ATOM   425  O  OE1 . GLU   A 1 73  ? 116.433 22.601 -7.258  1.00 26.41  ? 53  GLU   A OE1 1 
ATOM   426  O  OE2 . GLU   A 1 73  ? 117.255 21.828 -5.368  1.00 22.91  ? 53  GLU   A OE2 1 
ATOM   427  N  N   . HIS   A 1 74  ? 116.192 26.629 -5.715  1.00 19.73  ? 54  HIS   A N   1 
ATOM   428  C  CA  . HIS   A 1 74  ? 115.221 27.277 -4.852  1.00 19.97  ? 54  HIS   A CA  1 
ATOM   429  C  C   . HIS   A 1 74  ? 114.002 26.364 -4.722  1.00 19.98  ? 54  HIS   A C   1 
ATOM   430  O  O   . HIS   A 1 74  ? 113.886 25.339 -5.411  1.00 19.78  ? 54  HIS   A O   1 
ATOM   431  C  CB  . HIS   A 1 74  ? 114.845 28.649 -5.468  1.00 19.41  ? 54  HIS   A CB  1 
ATOM   432  C  CG  . HIS   A 1 74  ? 114.179 28.538 -6.807  1.00 19.62  ? 54  HIS   A CG  1 
ATOM   433  N  ND1 . HIS   A 1 74  ? 112.801 28.522 -6.933  1.00 21.45  ? 54  HIS   A ND1 1 
ATOM   434  C  CD2 . HIS   A 1 74  ? 114.731 28.384 -8.040  1.00 20.19  ? 54  HIS   A CD2 1 
ATOM   435  C  CE1 . HIS   A 1 74  ? 112.559 28.388 -8.235  1.00 21.82  ? 54  HIS   A CE1 1 
ATOM   436  N  NE2 . HIS   A 1 74  ? 113.686 28.292 -8.940  1.00 21.25  ? 54  HIS   A NE2 1 
ATOM   437  N  N   . SER   A 1 75  ? 113.098 26.718 -3.801  1.00 19.46  ? 55  SER   A N   1 
ATOM   438  C  CA  . SER   A 1 75  ? 111.930 25.904 -3.469  1.00 19.31  ? 55  SER   A CA  1 
ATOM   439  C  C   . SER   A 1 75  ? 110.894 25.723 -4.584  1.00 20.17  ? 55  SER   A C   1 
ATOM   440  O  O   . SER   A 1 75  ? 110.127 24.757 -4.545  1.00 21.06  ? 55  SER   A O   1 
ATOM   441  C  CB  . SER   A 1 75  ? 111.233 26.448 -2.228  1.00 20.52  ? 55  SER   A CB  1 
ATOM   442  O  OG  . SER   A 1 75  ? 110.733 27.756 -2.456  1.00 21.15  ? 55  SER   A OG  1 
ATOM   443  N  N   . GLY   A 1 76  ? 110.878 26.632 -5.551  1.00 19.97  ? 56  GLY   A N   1 
ATOM   444  C  CA  . GLY   A 1 76  ? 109.909 26.547 -6.653  1.00 21.22  ? 56  GLY   A CA  1 
ATOM   445  C  C   . GLY   A 1 76  ? 110.078 25.309 -7.522  1.00 22.34  ? 56  GLY   A C   1 
ATOM   446  O  O   . GLY   A 1 76  ? 109.122 24.845 -8.167  1.00 23.91  ? 56  GLY   A O   1 
ATOM   447  N  N   . ARG   A 1 77  ? 111.262 24.701 -7.460  1.00 20.87  ? 57  ARG   A N   1 
ATOM   448  C  CA  . ARG   A 1 77  ? 111.547 23.499 -8.244  1.00 21.51  ? 57  ARG   A CA  1 
ATOM   449  C  C   . ARG   A 1 77  ? 110.928 22.210 -7.656  1.00 22.03  ? 57  ARG   A C   1 
ATOM   450  O  O   . ARG   A 1 77  ? 111.019 21.127 -8.261  1.00 22.37  ? 57  ARG   A O   1 
ATOM   451  C  CB  . ARG   A 1 77  ? 113.057 23.398 -8.426  1.00 22.93  ? 57  ARG   A CB  1 
ATOM   452  C  CG  . ARG   A 1 77  ? 113.478 24.387 -9.541  1.00 25.00  ? 57  ARG   A CG  1 
ATOM   453  C  CD  . ARG   A 1 77  ? 114.969 24.522 -9.721  1.00 25.69  ? 57  ARG   A CD  1 
ATOM   454  N  NE  . ARG   A 1 77  ? 115.624 23.243 -10.002 1.00 23.86  ? 57  ARG   A NE  1 
ATOM   455  C  CZ  . ARG   A 1 77  ? 115.652 22.658 -11.198 1.00 24.63  ? 57  ARG   A CZ  1 
ATOM   456  N  NH1 . ARG   A 1 77  ? 116.322 21.521 -11.372 1.00 24.19  ? 57  ARG   A NH1 1 
ATOM   457  N  NH2 . ARG   A 1 77  ? 115.010 23.205 -12.232 1.00 24.24  ? 57  ARG   A NH2 1 
ATOM   458  N  N   . TYR   A 1 78  ? 110.284 22.328 -6.496  1.00 21.40  ? 58  TYR   A N   1 
ATOM   459  C  CA  . TYR   A 1 78  ? 109.656 21.195 -5.811  1.00 21.76  ? 58  TYR   A CA  1 
ATOM   460  C  C   . TYR   A 1 78  ? 108.144 21.189 -5.931  1.00 21.83  ? 58  TYR   A C   1 
ATOM   461  O  O   . TYR   A 1 78  ? 107.492 20.409 -5.232  1.00 21.90  ? 58  TYR   A O   1 
ATOM   462  C  CB  . TYR   A 1 78  ? 110.108 21.174 -4.337  1.00 21.33  ? 58  TYR   A CB  1 
ATOM   463  C  CG  . TYR   A 1 78  ? 111.586 20.858 -4.282  1.00 21.22  ? 58  TYR   A CG  1 
ATOM   464  C  CD1 . TYR   A 1 78  ? 112.533 21.843 -4.547  1.00 21.25  ? 58  TYR   A CD1 1 
ATOM   465  C  CD2 . TYR   A 1 78  ? 112.029 19.544 -4.181  1.00 21.30  ? 58  TYR   A CD2 1 
ATOM   466  C  CE1 . TYR   A 1 78  ? 113.878 21.540 -4.655  1.00 21.37  ? 58  TYR   A CE1 1 
ATOM   467  C  CE2 . TYR   A 1 78  ? 113.381 19.237 -4.231  1.00 22.32  ? 58  TYR   A CE2 1 
ATOM   468  C  CZ  . TYR   A 1 78  ? 114.299 20.242 -4.473  1.00 22.17  ? 58  TYR   A CZ  1 
ATOM   469  O  OH  . TYR   A 1 78  ? 115.619 19.931 -4.598  1.00 22.19  ? 58  TYR   A OH  1 
ATOM   470  N  N   . GLU   A 1 79  ? 107.578 21.980 -6.867  1.00 22.29  ? 59  GLU   A N   1 
ATOM   471  C  CA  . GLU   A 1 79  ? 106.142 22.070 -7.051  1.00 22.81  ? 59  GLU   A CA  1 
ATOM   472  C  C   . GLU   A 1 79  ? 105.456 20.711 -7.223  1.00 23.48  ? 59  GLU   A C   1 
ATOM   473  O  O   . GLU   A 1 79  ? 104.502 20.408 -6.489  1.00 23.99  ? 59  GLU   A O   1 
ATOM   474  C  CB  . GLU   A 1 79  ? 105.824 22.997 -8.232  1.00 25.78  ? 59  GLU   A CB  1 
ATOM   475  C  CG  . GLU   A 1 79  ? 104.357 23.352 -8.303  1.00 32.20  ? 59  GLU   A CG  1 
ATOM   476  C  CD  . GLU   A 1 79  ? 103.912 24.282 -7.189  1.00 36.49  ? 59  GLU   A CD  1 
ATOM   477  O  OE1 . GLU   A 1 79  ? 104.720 25.123 -6.736  1.00 37.14  ? 59  GLU   A OE1 1 
ATOM   478  O  OE2 . GLU   A 1 79  ? 102.734 24.183 -6.787  1.00 41.87  ? 59  GLU   A OE2 1 
ATOM   479  N  N   . GLU   A 1 80  ? 105.930 19.884 -8.182  1.00 23.04  ? 60  GLU   A N   1 
ATOM   480  C  CA  . GLU   A 1 80  ? 105.264 18.603 -8.438  1.00 24.26  ? 60  GLU   A CA  1 
ATOM   481  C  C   . GLU   A 1 80  ? 105.407 17.635 -7.276  1.00 24.17  ? 60  GLU   A C   1 
ATOM   482  O  O   . GLU   A 1 80  ? 104.418 17.013 -6.898  1.00 25.15  ? 60  GLU   A O   1 
ATOM   483  C  CB  . GLU   A 1 80  ? 105.688 17.977 -9.763  1.00 28.62  ? 60  GLU   A CB  1 
ATOM   484  C  CG  . GLU   A 1 80  ? 105.214 18.797 -10.961 1.00 37.55  ? 60  GLU   A CG  1 
ATOM   485  C  CD  . GLU   A 1 80  ? 103.753 19.227 -10.991 1.00 51.17  ? 60  GLU   A CD  1 
ATOM   486  O  OE1 . GLU   A 1 80  ? 102.870 18.346 -10.885 1.00 55.06  ? 60  GLU   A OE1 1 
ATOM   487  O  OE2 . GLU   A 1 80  ? 103.492 20.448 -11.118 1.00 55.16  ? 60  GLU   A OE2 1 
ATOM   488  N  N   . LEU   A 1 81  ? 106.603 17.546 -6.669  1.00 23.05  ? 61  LEU   A N   1 
ATOM   489  C  CA  . LEU   A 1 81  ? 106.786 16.669 -5.504  1.00 24.22  ? 61  LEU   A CA  1 
ATOM   490  C  C   . LEU   A 1 81  ? 105.873 17.104 -4.365  1.00 23.29  ? 61  LEU   A C   1 
ATOM   491  O  O   . LEU   A 1 81  ? 105.234 16.263 -3.749  1.00 23.53  ? 61  LEU   A O   1 
ATOM   492  C  CB  . LEU   A 1 81  ? 108.214 16.706 -4.977  1.00 25.76  ? 61  LEU   A CB  1 
ATOM   493  C  CG  . LEU   A 1 81  ? 109.185 15.698 -5.505  1.00 27.26  ? 61  LEU   A CG  1 
ATOM   494  C  CD1 . LEU   A 1 81  ? 110.594 16.060 -5.057  1.00 27.20  ? 61  LEU   A CD1 1 
ATOM   495  C  CD2 . LEU   A 1 81  ? 108.799 14.245 -5.079  1.00 27.24  ? 61  LEU   A CD2 1 
ATOM   496  N  N   . ALA   A 1 82  ? 105.795 18.427 -4.111  1.00 22.32  ? 62  ALA   A N   1 
ATOM   497  C  CA  . ALA   A 1 82  ? 104.988 18.967 -3.027  1.00 23.48  ? 62  ALA   A CA  1 
ATOM   498  C  C   . ALA   A 1 82  ? 103.527 18.712 -3.271  1.00 24.56  ? 62  ALA   A C   1 
ATOM   499  O  O   . ALA   A 1 82  ? 102.828 18.334 -2.331  1.00 25.50  ? 62  ALA   A O   1 
ATOM   500  C  CB  . ALA   A 1 82  ? 105.241 20.467 -2.880  1.00 24.04  ? 62  ALA   A CB  1 
ATOM   501  N  N   . ARG   A 1 83  ? 103.058 18.852 -4.522  1.00 25.13  ? 63  ARG   A N   1 
ATOM   502  C  CA  . ARG   A 1 83  ? 101.644 18.584 -4.806  1.00 26.65  ? 63  ARG   A CA  1 
ATOM   503  C  C   . ARG   A 1 83  ? 101.296 17.103 -4.584  1.00 27.59  ? 63  ARG   A C   1 
ATOM   504  O  O   . ARG   A 1 83  ? 100.204 16.776 -4.092  1.00 28.21  ? 63  ARG   A O   1 
ATOM   505  C  CB  . ARG   A 1 83  ? 101.248 19.084 -6.192  1.00 28.97  ? 63  ARG   A CB  1 
ATOM   506  C  CG  . ARG   A 1 83  ? 101.138 20.604 -6.178  1.00 34.43  ? 63  ARG   A CG  1 
ATOM   507  C  CD  . ARG   A 1 83  ? 100.660 21.193 -7.479  1.00 39.42  ? 63  ARG   A CD  1 
ATOM   508  N  NE  . ARG   A 1 83  ? 100.494 22.645 -7.360  1.00 44.30  ? 63  ARG   A NE  1 
ATOM   509  C  CZ  . ARG   A 1 83  ? 99.374  23.242 -6.953  1.00 47.18  ? 63  ARG   A CZ  1 
ATOM   510  N  NH1 . ARG   A 1 83  ? 98.309  22.520 -6.619  1.00 46.76  ? 63  ARG   A NH1 1 
ATOM   511  N  NH2 . ARG   A 1 83  ? 99.310  24.566 -6.879  1.00 47.87  ? 63  ARG   A NH2 1 
ATOM   512  N  N   . MET   A 1 84  ? 102.224 16.208 -4.900  1.00 26.88  ? 64  MET   A N   1 
ATOM   513  C  CA  . MET   A 1 84  ? 102.027 14.762 -4.641  1.00 26.82  ? 64  MET   A CA  1 
ATOM   514  C  C   . MET   A 1 84  ? 101.907 14.542 -3.128  1.00 27.31  ? 64  MET   A C   1 
ATOM   515  O  O   . MET   A 1 84  ? 100.995 13.853 -2.670  1.00 28.72  ? 64  MET   A O   1 
ATOM   516  C  CB  . MET   A 1 84  ? 103.215 13.932 -5.189  1.00 27.10  ? 64  MET   A CB  1 
ATOM   517  C  CG  . MET   A 1 84  ? 103.091 12.426 -4.897  1.00 29.01  ? 64  MET   A CG  1 
ATOM   518  S  SD  . MET   A 1 84  ? 103.838 11.959 -3.298  1.00 33.36  ? 64  MET   A SD  1 
ATOM   519  C  CE  . MET   A 1 84  ? 105.558 12.127 -3.662  1.00 30.50  ? 64  MET   A CE  1 
ATOM   520  N  N   . LEU   A 1 85  ? 102.794 15.173 -2.348  1.00 25.94  ? 65  LEU   A N   1 
ATOM   521  C  CA  . LEU   A 1 85  ? 102.772 15.016 -0.893  1.00 25.96  ? 65  LEU   A CA  1 
ATOM   522  C  C   . LEU   A 1 85  ? 101.515 15.592 -0.287  1.00 27.68  ? 65  LEU   A C   1 
ATOM   523  O  O   . LEU   A 1 85  ? 100.920 14.973 0.589   1.00 28.38  ? 65  LEU   A O   1 
ATOM   524  C  CB  . LEU   A 1 85  ? 104.029 15.597 -0.266  1.00 25.05  ? 65  LEU   A CB  1 
ATOM   525  C  CG  . LEU   A 1 85  ? 105.296 14.811 -0.569  1.00 24.41  ? 65  LEU   A CG  1 
ATOM   526  C  CD1 . LEU   A 1 85  ? 106.530 15.680 -0.341  1.00 23.83  ? 65  LEU   A CD1 1 
ATOM   527  C  CD2 . LEU   A 1 85  ? 105.357 13.487 0.267   1.00 25.11  ? 65  LEU   A CD2 1 
ATOM   528  N  N   . MET   A 1 86  ? 101.082 16.759 -0.774  1.00 28.43  ? 66  MET   A N   1 
ATOM   529  C  CA  A MET   A 1 86  ? 99.848  17.379 -0.307  0.50 29.76  ? 66  MET   A CA  1 
ATOM   530  C  CA  B MET   A 1 86  ? 99.845  17.390 -0.324  0.50 29.50  ? 66  MET   A CA  1 
ATOM   531  C  C   . MET   A 1 86  ? 98.643  16.479 -0.639  1.00 30.63  ? 66  MET   A C   1 
ATOM   532  O  O   . MET   A 1 86  ? 97.693  16.406 0.142   1.00 31.26  ? 66  MET   A O   1 
ATOM   533  C  CB  A MET   A 1 86  ? 99.698  18.787 -0.916  0.50 30.67  ? 66  MET   A CB  1 
ATOM   534  C  CB  B MET   A 1 86  ? 99.694  18.765 -1.000  0.50 29.77  ? 66  MET   A CB  1 
ATOM   535  C  CG  A MET   A 1 86  ? 98.504  19.541 -0.400  0.50 33.57  ? 66  MET   A CG  1 
ATOM   536  C  CG  B MET   A 1 86  ? 98.394  19.457 -0.690  0.50 31.42  ? 66  MET   A CG  1 
ATOM   537  S  SD  A MET   A 1 86  ? 97.055  19.273 -1.442  0.50 40.47  ? 66  MET   A SD  1 
ATOM   538  S  SD  B MET   A 1 86  ? 98.228  21.033 -1.549  0.50 33.06  ? 66  MET   A SD  1 
ATOM   539  C  CE  A MET   A 1 86  ? 97.454  20.358 -2.821  0.50 39.07  ? 66  MET   A CE  1 
ATOM   540  C  CE  B MET   A 1 86  ? 98.311  20.517 -3.228  0.50 30.40  ? 66  MET   A CE  1 
ATOM   541  N  N   . GLY   A 1 87  ? 98.712  15.753 -1.763  1.00 31.86  ? 67  GLY   A N   1 
ATOM   542  C  CA  . GLY   A 1 87  ? 97.665  14.809 -2.163  1.00 33.34  ? 67  GLY   A CA  1 
ATOM   543  C  C   . GLY   A 1 87  ? 97.533  13.638 -1.200  1.00 34.05  ? 67  GLY   A C   1 
ATOM   544  O  O   . GLY   A 1 87  ? 96.510  12.958 -1.186  1.00 35.30  ? 67  GLY   A O   1 
ATOM   545  N  N   . LEU   A 1 88  ? 98.574  13.379 -0.388  1.00 33.55  ? 68  LEU   A N   1 
ATOM   546  C  CA  . LEU   A 1 88  ? 98.562  12.353 0.658   1.00 33.99  ? 68  LEU   A CA  1 
ATOM   547  C  C   . LEU   A 1 88  ? 98.085  12.915 2.008   1.00 34.28  ? 68  LEU   A C   1 
ATOM   548  O  O   . LEU   A 1 88  ? 98.227  12.229 3.015   1.00 35.02  ? 68  LEU   A O   1 
ATOM   549  C  CB  . LEU   A 1 88  ? 99.967  11.736 0.847   1.00 34.10  ? 68  LEU   A CB  1 
ATOM   550  C  CG  . LEU   A 1 88  ? 100.576 11.052 -0.377  1.00 35.74  ? 68  LEU   A CG  1 
ATOM   551  C  CD1 . LEU   A 1 88  ? 101.966 10.499 -0.057  1.00 36.32  ? 68  LEU   A CD1 1 
ATOM   552  C  CD2 . LEU   A 1 88  ? 99.659  9.961  -0.920  1.00 36.83  ? 68  LEU   A CD2 1 
ATOM   553  N  N   . ASP   A 1 89  ? 97.586  14.168 2.036   1.00 33.58  ? 69  ASP   A N   1 
ATOM   554  C  CA  . ASP   A 1 89  ? 97.107  14.872 3.222   1.00 33.76  ? 69  ASP   A CA  1 
ATOM   555  C  C   . ASP   A 1 89  ? 98.215  15.342 4.142   1.00 32.64  ? 69  ASP   A C   1 
ATOM   556  O  O   . ASP   A 1 89  ? 97.970  15.549 5.328   1.00 32.96  ? 69  ASP   A O   1 
ATOM   557  C  CB  . ASP   A 1 89  ? 96.046  14.067 3.988   1.00 37.21  ? 69  ASP   A CB  1 
ATOM   558  C  CG  . ASP   A 1 89  ? 94.803  13.837 3.158   1.00 45.13  ? 69  ASP   A CG  1 
ATOM   559  O  OD1 . ASP   A 1 89  ? 94.145  12.785 3.352   1.00 47.14  ? 69  ASP   A OD1 1 
ATOM   560  O  OD2 . ASP   A 1 89  ? 94.488  14.705 2.302   1.00 47.49  ? 69  ASP   A OD2 1 
ATOM   561  N  N   . LEU   A 1 90  ? 99.411  15.580 3.592   1.00 31.05  ? 70  LEU   A N   1 
ATOM   562  C  CA  . LEU   A 1 90  ? 100.492 16.179 4.371   1.00 30.07  ? 70  LEU   A CA  1 
ATOM   563  C  C   . LEU   A 1 90  ? 100.509 17.673 4.063   1.00 29.00  ? 70  LEU   A C   1 
ATOM   564  O  O   . LEU   A 1 90  ? 100.199 18.092 2.938   1.00 28.75  ? 70  LEU   A O   1 
ATOM   565  C  CB  . LEU   A 1 90  ? 101.882 15.596 4.031   1.00 30.45  ? 70  LEU   A CB  1 
ATOM   566  C  CG  . LEU   A 1 90  ? 102.291 14.332 4.828   1.00 32.52  ? 70  LEU   A CG  1 
ATOM   567  C  CD1 . LEU   A 1 90  ? 101.681 13.094 4.235   1.00 33.84  ? 70  LEU   A CD1 1 
ATOM   568  C  CD2 . LEU   A 1 90  ? 103.823 14.162 4.880   1.00 32.90  ? 70  LEU   A CD2 1 
ATOM   569  N  N   . LEU   A 1 91  ? 100.874 18.472 5.062   1.00 27.48  ? 71  LEU   A N   1 
ATOM   570  C  CA  . LEU   A 1 91  ? 101.042 19.903 4.852   1.00 26.96  ? 71  LEU   A CA  1 
ATOM   571  C  C   . LEU   A 1 91  ? 102.529 20.084 4.517   1.00 25.90  ? 71  LEU   A C   1 
ATOM   572  O  O   . LEU   A 1 91  ? 103.390 19.837 5.365   1.00 26.79  ? 71  LEU   A O   1 
ATOM   573  C  CB  . LEU   A 1 91  ? 100.640 20.694 6.103   1.00 27.43  ? 71  LEU   A CB  1 
ATOM   574  C  CG  . LEU   A 1 91  ? 100.377 22.171 5.837   1.00 30.01  ? 71  LEU   A CG  1 
ATOM   575  C  CD1 . LEU   A 1 91  ? 99.615  22.807 6.982   1.00 30.94  ? 71  LEU   A CD1 1 
ATOM   576  C  CD2 . LEU   A 1 91  ? 101.653 22.936 5.556   1.00 31.03  ? 71  LEU   A CD2 1 
ATOM   577  N  N   . VAL   A 1 92  ? 102.823 20.478 3.273   1.00 23.55  ? 72  VAL   A N   1 
ATOM   578  C  CA  . VAL   A 1 92  ? 104.190 20.645 2.802   1.00 22.05  ? 72  VAL   A CA  1 
ATOM   579  C  C   . VAL   A 1 92  ? 104.581 22.104 2.955   1.00 21.55  ? 72  VAL   A C   1 
ATOM   580  O  O   . VAL   A 1 92  ? 103.771 22.996 2.685   1.00 22.23  ? 72  VAL   A O   1 
ATOM   581  C  CB  . VAL   A 1 92  ? 104.339 20.222 1.319   1.00 22.64  ? 72  VAL   A CB  1 
ATOM   582  C  CG1 . VAL   A 1 92  ? 105.810 20.181 0.926   1.00 22.98  ? 72  VAL   A CG1 1 
ATOM   583  C  CG2 . VAL   A 1 92  ? 103.659 18.874 1.051   1.00 23.37  ? 72  VAL   A CG2 1 
ATOM   584  N  N   . PHE   A 1 93  ? 105.791 22.340 3.421   1.00 20.07  ? 73  PHE   A N   1 
ATOM   585  C  CA  . PHE   A 1 93  ? 106.279 23.715 3.604   1.00 20.36  ? 73  PHE   A CA  1 
ATOM   586  C  C   . PHE   A 1 93  ? 107.750 23.781 3.262   1.00 20.44  ? 73  PHE   A C   1 
ATOM   587  O  O   . PHE   A 1 93  ? 108.463 22.773 3.305   1.00 20.86  ? 73  PHE   A O   1 
ATOM   588  C  CB  . PHE   A 1 93  ? 105.937 24.296 5.003   1.00 20.92  ? 73  PHE   A CB  1 
ATOM   589  C  CG  . PHE   A 1 93  ? 106.604 23.637 6.189   1.00 21.71  ? 73  PHE   A CG  1 
ATOM   590  C  CD1 . PHE   A 1 93  ? 106.241 22.360 6.592   1.00 23.18  ? 73  PHE   A CD1 1 
ATOM   591  C  CD2 . PHE   A 1 93  ? 107.558 24.311 6.932   1.00 22.81  ? 73  PHE   A CD2 1 
ATOM   592  C  CE1 . PHE   A 1 93  ? 106.851 21.761 7.686   1.00 24.20  ? 73  PHE   A CE1 1 
ATOM   593  C  CE2 . PHE   A 1 93  ? 108.152 23.717 8.035   1.00 23.76  ? 73  PHE   A CE2 1 
ATOM   594  C  CZ  . PHE   A 1 93  ? 107.803 22.439 8.400   1.00 23.82  ? 73  PHE   A CZ  1 
ATOM   595  N  N   . ALA   A 1 94  ? 108.205 24.959 2.836   1.00 19.14  ? 74  ALA   A N   1 
ATOM   596  C  CA  . ALA   A 1 94  ? 109.583 25.120 2.397   1.00 18.52  ? 74  ALA   A CA  1 
ATOM   597  C  C   . ALA   A 1 94  ? 109.949 26.602 2.527   1.00 18.61  ? 74  ALA   A C   1 
ATOM   598  O  O   . ALA   A 1 94  ? 109.080 27.474 2.685   1.00 19.11  ? 74  ALA   A O   1 
ATOM   599  C  CB  . ALA   A 1 94  ? 109.701 24.684 0.908   1.00 18.80  ? 74  ALA   A CB  1 
ATOM   600  N  N   . HIS   A 1 95  ? 111.241 26.885 2.433   1.00 18.32  ? 75  HIS   A N   1 
ATOM   601  C  CA  . HIS   A 1 95  ? 111.705 28.236 2.251   1.00 18.96  ? 75  HIS   A CA  1 
ATOM   602  C  C   . HIS   A 1 95  ? 112.949 28.173 1.374   1.00 18.76  ? 75  HIS   A C   1 
ATOM   603  O  O   . HIS   A 1 95  ? 113.580 27.121 1.231   1.00 19.88  ? 75  HIS   A O   1 
ATOM   604  C  CB  . HIS   A 1 95  ? 111.961 28.997 3.569   1.00 19.01  ? 75  HIS   A CB  1 
ATOM   605  C  CG  . HIS   A 1 95  ? 112.992 28.388 4.473   1.00 20.18  ? 75  HIS   A CG  1 
ATOM   606  N  ND1 . HIS   A 1 95  ? 112.649 27.918 5.724   1.00 21.43  ? 75  HIS   A ND1 1 
ATOM   607  C  CD2 . HIS   A 1 95  ? 114.336 28.284 4.319   1.00 21.16  ? 75  HIS   A CD2 1 
ATOM   608  C  CE1 . HIS   A 1 95  ? 113.784 27.529 6.292   1.00 22.11  ? 75  HIS   A CE1 1 
ATOM   609  N  NE2 . HIS   A 1 95  ? 114.825 27.710 5.473   1.00 21.43  ? 75  HIS   A NE2 1 
ATOM   610  N  N   . ASP   A 1 96  ? 113.261 29.297 0.716   1.00 18.14  ? 76  ASP   A N   1 
ATOM   611  C  CA  . ASP   A 1 96  ? 114.514 29.395 -0.023  1.00 18.63  ? 76  ASP   A CA  1 
ATOM   612  C  C   . ASP   A 1 96  ? 115.587 29.650 1.034   1.00 19.05  ? 76  ASP   A C   1 
ATOM   613  O  O   . ASP   A 1 96  ? 115.453 30.562 1.867   1.00 19.86  ? 76  ASP   A O   1 
ATOM   614  C  CB  . ASP   A 1 96  ? 114.451 30.541 -1.052  1.00 19.31  ? 76  ASP   A CB  1 
ATOM   615  C  CG  . ASP   A 1 96  ? 113.506 30.215 -2.208  1.00 20.99  ? 76  ASP   A CG  1 
ATOM   616  O  OD1 . ASP   A 1 96  ? 113.068 29.042 -2.313  1.00 19.87  ? 76  ASP   A OD1 1 
ATOM   617  O  OD2 . ASP   A 1 96  ? 113.227 31.111 -3.021  1.00 21.91  ? 76  ASP   A OD2 1 
ATOM   618  N  N   . HIS   A 1 97  ? 116.664 28.843 1.009   1.00 18.76  ? 77  HIS   A N   1 
ATOM   619  C  CA  . HIS   A 1 97  ? 117.748 29.024 1.969   1.00 19.17  ? 77  HIS   A CA  1 
ATOM   620  C  C   . HIS   A 1 97  ? 118.380 30.405 1.768   1.00 19.78  ? 77  HIS   A C   1 
ATOM   621  O  O   . HIS   A 1 97  ? 118.329 30.972 0.662   1.00 19.75  ? 77  HIS   A O   1 
ATOM   622  C  CB  . HIS   A 1 97  ? 118.838 27.950 1.763   1.00 19.47  ? 77  HIS   A CB  1 
ATOM   623  C  CG  . HIS   A 1 97  ? 118.351 26.546 1.949   1.00 20.44  ? 77  HIS   A CG  1 
ATOM   624  N  ND1 . HIS   A 1 97  ? 117.738 26.154 3.124   1.00 22.06  ? 77  HIS   A ND1 1 
ATOM   625  C  CD2 . HIS   A 1 97  ? 118.399 25.480 1.100   1.00 21.29  ? 77  HIS   A CD2 1 
ATOM   626  C  CE1 . HIS   A 1 97  ? 117.435 24.864 2.965   1.00 21.63  ? 77  HIS   A CE1 1 
ATOM   627  N  NE2 . HIS   A 1 97  ? 117.816 24.417 1.765   1.00 22.03  ? 77  HIS   A NE2 1 
ATOM   628  N  N   . VAL   A 1 98  ? 119.012 30.953 2.816   1.00 20.02  ? 78  VAL   A N   1 
ATOM   629  C  CA  A VAL   A 1 98  ? 119.675 32.257 2.700   0.63 20.99  ? 78  VAL   A CA  1 
ATOM   630  C  CA  B VAL   A 1 98  ? 119.723 32.234 2.742   0.37 20.43  ? 78  VAL   A CA  1 
ATOM   631  C  C   . VAL   A 1 98  ? 120.637 32.263 1.489   1.00 20.69  ? 78  VAL   A C   1 
ATOM   632  O  O   . VAL   A 1 98  ? 121.233 31.231 1.157   1.00 19.87  ? 78  VAL   A O   1 
ATOM   633  C  CB  A VAL   A 1 98  ? 120.389 32.663 4.012   0.63 23.06  ? 78  VAL   A CB  1 
ATOM   634  C  CB  B VAL   A 1 98  ? 120.531 32.382 4.062   0.37 21.22  ? 78  VAL   A CB  1 
ATOM   635  C  CG1 A VAL   A 1 98  ? 121.519 31.708 4.348   0.63 23.84  ? 78  VAL   A CG1 1 
ATOM   636  C  CG1 B VAL   A 1 98  ? 121.786 33.226 3.899   0.37 22.10  ? 78  VAL   A CG1 1 
ATOM   637  C  CG2 A VAL   A 1 98  ? 120.912 34.083 3.927   0.63 24.12  ? 78  VAL   A CG2 1 
ATOM   638  C  CG2 B VAL   A 1 98  ? 119.654 32.933 5.168   0.37 21.37  ? 78  VAL   A CG2 1 
ATOM   639  N  N   . GLY   A 1 99  ? 120.692 33.394 0.780   1.00 20.41  ? 79  GLY   A N   1 
ATOM   640  C  CA  . GLY   A 1 99  ? 121.540 33.479 -0.407  1.00 21.13  ? 79  GLY   A CA  1 
ATOM   641  C  C   . GLY   A 1 99  ? 120.995 32.768 -1.636  1.00 21.78  ? 79  GLY   A C   1 
ATOM   642  O  O   . GLY   A 1 99  ? 121.685 32.678 -2.659  1.00 23.24  ? 79  GLY   A O   1 
ATOM   643  N  N   . HIS   A 1 100 ? 119.756 32.268 -1.563  1.00 20.76  ? 80  HIS   A N   1 
ATOM   644  C  CA  . HIS   A 1 100 ? 119.122 31.538 -2.652  1.00 20.51  ? 80  HIS   A CA  1 
ATOM   645  C  C   . HIS   A 1 100 ? 117.761 32.094 -3.034  1.00 20.67  ? 80  HIS   A C   1 
ATOM   646  O  O   . HIS   A 1 100 ? 117.057 32.677 -2.204  1.00 20.82  ? 80  HIS   A O   1 
ATOM   647  C  CB  . HIS   A 1 100 ? 118.934 30.050 -2.249  1.00 20.17  ? 80  HIS   A CB  1 
ATOM   648  C  CG  . HIS   A 1 100 ? 120.230 29.303 -2.202  1.00 20.61  ? 80  HIS   A CG  1 
ATOM   649  N  ND1 . HIS   A 1 100 ? 121.158 29.517 -1.195  1.00 21.87  ? 80  HIS   A ND1 1 
ATOM   650  C  CD2 . HIS   A 1 100 ? 120.711 28.360 -3.047  1.00 22.13  ? 80  HIS   A CD2 1 
ATOM   651  C  CE1 . HIS   A 1 100 ? 122.174 28.701 -1.461  1.00 22.93  ? 80  HIS   A CE1 1 
ATOM   652  N  NE2 . HIS   A 1 100 ? 121.956 27.994 -2.571  1.00 22.52  ? 80  HIS   A NE2 1 
ATOM   653  N  N   . GLY   A 1 101 ? 117.383 31.863 -4.279  1.00 20.24  ? 81  GLY   A N   1 
ATOM   654  C  CA  . GLY   A 1 101 ? 116.065 32.176 -4.806  1.00 19.78  ? 81  GLY   A CA  1 
ATOM   655  C  C   . GLY   A 1 101 ? 115.557 33.558 -4.442  1.00 20.36  ? 81  GLY   A C   1 
ATOM   656  O  O   . GLY   A 1 101 ? 116.221 34.573 -4.723  1.00 20.78  ? 81  GLY   A O   1 
ATOM   657  N  N   . GLN   A 1 102 ? 114.389 33.586 -3.778  1.00 19.58  ? 82  GLN   A N   1 
ATOM   658  C  CA  . GLN   A 1 102 ? 113.726 34.829 -3.392  1.00 20.07  ? 82  GLN   A CA  1 
ATOM   659  C  C   . GLN   A 1 102 ? 114.027 35.283 -1.971  1.00 19.78  ? 82  GLN   A C   1 
ATOM   660  O  O   . GLN   A 1 102 ? 113.434 36.274 -1.512  1.00 19.61  ? 82  GLN   A O   1 
ATOM   661  C  CB  . GLN   A 1 102 ? 112.218 34.690 -3.605  1.00 21.00  ? 82  GLN   A CB  1 
ATOM   662  C  CG  . GLN   A 1 102 ? 111.874 34.350 -5.073  1.00 22.06  ? 82  GLN   A CG  1 
ATOM   663  C  CD  . GLN   A 1 102 ? 110.388 34.301 -5.273  1.00 24.09  ? 82  GLN   A CD  1 
ATOM   664  O  OE1 . GLN   A 1 102 ? 109.701 35.346 -5.267  1.00 23.56  ? 82  GLN   A OE1 1 
ATOM   665  N  NE2 . GLN   A 1 102 ? 109.847 33.091 -5.456  1.00 23.56  ? 82  GLN   A NE2 1 
ATOM   666  N  N   . SER   A 1 103 ? 114.941 34.573 -1.267  1.00 19.23  ? 83  SER   A N   1 
ATOM   667  C  CA  . SER   A 1 103 ? 115.363 34.974 0.065   1.00 19.86  ? 83  SER   A CA  1 
ATOM   668  C  C   . SER   A 1 103 ? 116.480 36.006 -0.014  1.00 21.10  ? 83  SER   A C   1 
ATOM   669  O  O   . SER   A 1 103 ? 117.139 36.163 -1.053  1.00 21.74  ? 83  SER   A O   1 
ATOM   670  C  CB  . SER   A 1 103 ? 115.843 33.759 0.851   1.00 19.88  ? 83  SER   A CB  1 
ATOM   671  O  OG  . SER   A 1 103 ? 114.716 32.946 1.125   1.00 19.94  ? 83  SER   A OG  1 
ATOM   672  N  N   . GLU   A 1 104 ? 116.700 36.712 1.101   1.00 21.11  ? 84  GLU   A N   1 
ATOM   673  C  CA  . GLU   A 1 104 ? 117.769 37.689 1.172   1.00 22.01  ? 84  GLU   A CA  1 
ATOM   674  C  C   . GLU   A 1 104 ? 119.142 36.999 1.312   1.00 23.84  ? 84  GLU   A C   1 
ATOM   675  O  O   . GLU   A 1 104 ? 119.235 35.775 1.491   1.00 24.02  ? 84  GLU   A O   1 
ATOM   676  C  CB  . GLU   A 1 104 ? 117.517 38.643 2.353   1.00 22.34  ? 84  GLU   A CB  1 
ATOM   677  C  CG  . GLU   A 1 104 ? 116.411 39.640 2.078   1.00 23.75  ? 84  GLU   A CG  1 
ATOM   678  C  CD  . GLU   A 1 104 ? 116.281 40.682 3.180   1.00 24.86  ? 84  GLU   A CD  1 
ATOM   679  O  OE1 . GLU   A 1 104 ? 116.521 40.335 4.359   1.00 23.63  ? 84  GLU   A OE1 1 
ATOM   680  O  OE2 . GLU   A 1 104 ? 115.947 41.846 2.862   1.00 28.83  ? 84  GLU   A OE2 1 
ATOM   681  N  N   . GLY   A 1 105 ? 120.188 37.815 1.245   1.00 25.31  ? 85  GLY   A N   1 
ATOM   682  C  CA  . GLY   A 1 105 ? 121.560 37.380 1.423   1.00 26.61  ? 85  GLY   A CA  1 
ATOM   683  C  C   . GLY   A 1 105 ? 122.360 37.454 0.143   1.00 27.94  ? 85  GLY   A C   1 
ATOM   684  O  O   . GLY   A 1 105 ? 121.823 37.236 -0.945  1.00 27.84  ? 85  GLY   A O   1 
ATOM   685  N  N   . GLU   A 1 106 ? 123.692 37.685 0.251   1.00 29.08  ? 86  GLU   A N   1 
ATOM   686  C  CA  . GLU   A 1 106 ? 124.565 37.666 -0.934  1.00 30.34  ? 86  GLU   A CA  1 
ATOM   687  C  C   . GLU   A 1 106 ? 124.447 36.266 -1.587  1.00 29.81  ? 86  GLU   A C   1 
ATOM   688  O  O   . GLU   A 1 106 ? 124.329 35.256 -0.872  1.00 29.00  ? 86  GLU   A O   1 
ATOM   689  C  CB  . GLU   A 1 106 ? 126.021 37.953 -0.535  1.00 34.63  ? 86  GLU   A CB  1 
ATOM   690  C  CG  . GLU   A 1 106 ? 126.962 38.090 -1.720  1.00 43.89  ? 86  GLU   A CG  1 
ATOM   691  C  CD  . GLU   A 1 106 ? 128.393 38.478 -1.395  1.00 53.97  ? 86  GLU   A CD  1 
ATOM   692  O  OE1 . GLU   A 1 106 ? 128.688 38.740 -0.206  1.00 55.25  ? 86  GLU   A OE1 1 
ATOM   693  O  OE2 . GLU   A 1 106 ? 129.224 38.504 -2.333  1.00 57.14  ? 86  GLU   A OE2 1 
ATOM   694  N  N   . ARG   A 1 107 ? 124.333 36.218 -2.919  1.00 29.60  ? 87  ARG   A N   1 
ATOM   695  C  CA  . ARG   A 1 107 ? 124.102 34.956 -3.605  1.00 29.83  ? 87  ARG   A CA  1 
ATOM   696  C  C   . ARG   A 1 107 ? 125.153 33.909 -3.316  1.00 30.31  ? 87  ARG   A C   1 
ATOM   697  O  O   . ARG   A 1 107 ? 126.341 34.172 -3.483  1.00 30.66  ? 87  ARG   A O   1 
ATOM   698  C  CB  . ARG   A 1 107 ? 123.959 35.157 -5.124  1.00 30.46  ? 87  ARG   A CB  1 
ATOM   699  C  CG  . ARG   A 1 107 ? 122.935 36.223 -5.523  1.00 32.06  ? 87  ARG   A CG  1 
ATOM   700  C  CD  . ARG   A 1 107 ? 121.486 35.809 -5.253  1.00 32.74  ? 87  ARG   A CD  1 
ATOM   701  N  NE  . ARG   A 1 107 ? 121.089 36.032 -3.859  1.00 31.12  ? 87  ARG   A NE  1 
ATOM   702  C  CZ  . ARG   A 1 107 ? 119.895 35.724 -3.362  1.00 29.71  ? 87  ARG   A CZ  1 
ATOM   703  N  NH1 . ARG   A 1 107 ? 118.966 35.182 -4.136  1.00 28.31  ? 87  ARG   A NH1 1 
ATOM   704  N  NH2 . ARG   A 1 107 ? 119.621 35.962 -2.086  1.00 28.55  ? 87  ARG   A NH2 1 
ATOM   705  N  N   . MET   A 1 108 ? 124.712 32.748 -2.822  1.00 30.34  ? 88  MET   A N   1 
ATOM   706  C  CA  . MET   A 1 108 ? 125.609 31.624 -2.591  1.00 31.42  ? 88  MET   A CA  1 
ATOM   707  C  C   . MET   A 1 108 ? 126.733 31.913 -1.644  1.00 31.29  ? 88  MET   A C   1 
ATOM   708  O  O   . MET   A 1 108 ? 127.897 31.583 -1.891  1.00 32.67  ? 88  MET   A O   1 
ATOM   709  C  CB  . MET   A 1 108 ? 126.136 31.111 -3.918  1.00 33.74  ? 88  MET   A CB  1 
ATOM   710  C  CG  . MET   A 1 108 ? 125.134 31.231 -4.951  1.00 38.98  ? 88  MET   A CG  1 
ATOM   711  S  SD  . MET   A 1 108 ? 124.216 29.773 -4.769  1.00 46.75  ? 88  MET   A SD  1 
ATOM   712  C  CE  . MET   A 1 108 ? 125.023 28.969 -6.123  1.00 27.85  ? 88  MET   A CE  1 
ATOM   713  N  N   A VAL   A 1 109 ? 126.399 32.584 -0.571  0.44 30.64  ? 89  VAL   A N   1 
ATOM   714  N  N   B VAL   A 1 109 ? 126.386 32.589 -0.564  0.56 30.44  ? 89  VAL   A N   1 
ATOM   715  C  CA  A VAL   A 1 109 ? 127.321 32.820 0.522   0.44 30.98  ? 89  VAL   A CA  1 
ATOM   716  C  CA  B VAL   A 1 109 ? 127.282 32.953 0.528   0.56 30.71  ? 89  VAL   A CA  1 
ATOM   717  C  C   A VAL   A 1 109 ? 126.568 32.470 1.799   0.44 29.98  ? 89  VAL   A C   1 
ATOM   718  C  C   B VAL   A 1 109 ? 126.565 32.558 1.823   0.56 29.96  ? 89  VAL   A C   1 
ATOM   719  O  O   A VAL   A 1 109 ? 125.339 32.591 1.867   0.44 29.70  ? 89  VAL   A O   1 
ATOM   720  O  O   B VAL   A 1 109 ? 125.350 32.739 1.927   0.56 29.83  ? 89  VAL   A O   1 
ATOM   721  C  CB  A VAL   A 1 109 ? 127.993 34.222 0.603   0.44 32.91  ? 89  VAL   A CB  1 
ATOM   722  C  CB  B VAL   A 1 109 ? 127.599 34.480 0.524   0.56 32.19  ? 89  VAL   A CB  1 
ATOM   723  C  CG1 A VAL   A 1 109 ? 128.495 34.711 -0.751  0.44 34.06  ? 89  VAL   A CG1 1 
ATOM   724  C  CG1 B VAL   A 1 109 ? 128.342 34.898 1.791   0.56 32.87  ? 89  VAL   A CG1 1 
ATOM   725  C  CG2 A VAL   A 1 109 ? 127.086 35.250 1.253   0.44 33.59  ? 89  VAL   A CG2 1 
ATOM   726  C  CG2 B VAL   A 1 109 ? 128.405 34.875 -0.707  0.56 33.30  ? 89  VAL   A CG2 1 
ATOM   727  N  N   . VAL   A 1 110 ? 127.297 32.003 2.798   1.00 29.16  ? 90  VAL   A N   1 
ATOM   728  C  CA  . VAL   A 1 110 ? 126.718 31.666 4.082   1.00 28.45  ? 90  VAL   A CA  1 
ATOM   729  C  C   . VAL   A 1 110 ? 127.819 31.825 5.121   1.00 28.83  ? 90  VAL   A C   1 
ATOM   730  O  O   . VAL   A 1 110 ? 128.945 31.387 4.889   1.00 29.68  ? 90  VAL   A O   1 
ATOM   731  C  CB  . VAL   A 1 110 ? 125.987 30.296 4.112   1.00 27.92  ? 90  VAL   A CB  1 
ATOM   732  C  CG1 . VAL   A 1 110 ? 126.964 29.125 4.086   1.00 27.47  ? 90  VAL   A CG1 1 
ATOM   733  C  CG2 . VAL   A 1 110 ? 125.030 30.203 5.292   1.00 28.70  ? 90  VAL   A CG2 1 
ATOM   734  N  N   . SER   A 1 111 ? 127.528 32.516 6.230   1.00 28.03  ? 91  SER   A N   1 
ATOM   735  C  CA  . SER   A 1 111 ? 128.545 32.757 7.258   1.00 28.94  ? 91  SER   A CA  1 
ATOM   736  C  C   . SER   A 1 111 ? 129.070 31.453 7.851   1.00 29.44  ? 91  SER   A C   1 
ATOM   737  O  O   . SER   A 1 111 ? 130.267 31.303 8.092   1.00 30.39  ? 91  SER   A O   1 
ATOM   738  C  CB  . SER   A 1 111 ? 127.995 33.665 8.346   1.00 29.98  ? 91  SER   A CB  1 
ATOM   739  O  OG  . SER   A 1 111 ? 126.905 33.049 9.008   1.00 32.41  ? 91  SER   A OG  1 
ATOM   740  N  N   . ASP   A 1 112 ? 128.174 30.500 8.068   1.00 28.40  ? 92  ASP   A N   1 
ATOM   741  C  CA  . ASP   A 1 112 ? 128.515 29.153 8.517   1.00 27.83  ? 92  ASP   A CA  1 
ATOM   742  C  C   . ASP   A 1 112 ? 127.405 28.256 8.034   1.00 26.17  ? 92  ASP   A C   1 
ATOM   743  O  O   . ASP   A 1 112 ? 126.244 28.664 8.050   1.00 26.08  ? 92  ASP   A O   1 
ATOM   744  C  CB  . ASP   A 1 112 ? 128.667 29.044 10.041  1.00 29.40  ? 92  ASP   A CB  1 
ATOM   745  C  CG  . ASP   A 1 112 ? 129.120 27.655 10.474  1.00 33.81  ? 92  ASP   A CG  1 
ATOM   746  O  OD1 . ASP   A 1 112 ? 130.349 27.422 10.542  1.00 34.64  ? 92  ASP   A OD1 1 
ATOM   747  O  OD2 . ASP   A 1 112 ? 128.248 26.798 10.728  1.00 33.45  ? 92  ASP   A OD2 1 
ATOM   748  N  N   . PHE   A 1 113 ? 127.737 27.024 7.627   1.00 25.06  ? 93  PHE   A N   1 
ATOM   749  C  CA  . PHE   A 1 113 ? 126.730 26.088 7.106   1.00 23.75  ? 93  PHE   A CA  1 
ATOM   750  C  C   . PHE   A 1 113 ? 125.565 25.882 8.090   1.00 24.19  ? 93  PHE   A C   1 
ATOM   751  O  O   . PHE   A 1 113 ? 124.424 25.665 7.662   1.00 23.49  ? 93  PHE   A O   1 
ATOM   752  C  CB  . PHE   A 1 113 ? 127.387 24.730 6.759   1.00 22.84  ? 93  PHE   A CB  1 
ATOM   753  C  CG  . PHE   A 1 113 ? 126.514 23.894 5.849   1.00 23.00  ? 93  PHE   A CG  1 
ATOM   754  C  CD1 . PHE   A 1 113 ? 126.492 24.123 4.479   1.00 23.65  ? 93  PHE   A CD1 1 
ATOM   755  C  CD2 . PHE   A 1 113 ? 125.705 22.896 6.365   1.00 23.87  ? 93  PHE   A CD2 1 
ATOM   756  C  CE1 . PHE   A 1 113 ? 125.679 23.367 3.636   1.00 23.52  ? 93  PHE   A CE1 1 
ATOM   757  C  CE2 . PHE   A 1 113 ? 124.869 22.158 5.528   1.00 23.73  ? 93  PHE   A CE2 1 
ATOM   758  C  CZ  . PHE   A 1 113 ? 124.875 22.389 4.166   1.00 23.72  ? 93  PHE   A CZ  1 
ATOM   759  N  N   . HIS   A 1 114 ? 125.845 26.015 9.420   1.00 25.00  ? 94  HIS   A N   1 
ATOM   760  C  CA  . HIS   A 1 114 ? 124.809 25.834 10.434  1.00 25.39  ? 94  HIS   A CA  1 
ATOM   761  C  C   . HIS   A 1 114 ? 123.669 26.837 10.317  1.00 24.23  ? 94  HIS   A C   1 
ATOM   762  O  O   . HIS   A 1 114 ? 122.560 26.518 10.731  1.00 23.52  ? 94  HIS   A O   1 
ATOM   763  C  CB  . HIS   A 1 114 ? 125.368 25.800 11.869  1.00 26.97  ? 94  HIS   A CB  1 
ATOM   764  C  CG  . HIS   A 1 114 ? 124.329 25.396 12.870  1.00 30.68  ? 94  HIS   A CG  1 
ATOM   765  N  ND1 . HIS   A 1 114 ? 123.635 26.343 13.611  1.00 32.78  ? 94  HIS   A ND1 1 
ATOM   766  C  CD2 . HIS   A 1 114 ? 123.852 24.166 13.177  1.00 32.75  ? 94  HIS   A CD2 1 
ATOM   767  C  CE1 . HIS   A 1 114 ? 122.780 25.659 14.355  1.00 33.28  ? 94  HIS   A CE1 1 
ATOM   768  N  NE2 . HIS   A 1 114 ? 122.881 24.347 14.143  1.00 33.93  ? 94  HIS   A NE2 1 
ATOM   769  N  N   . VAL   A 1 115 ? 123.881 27.992 9.658   1.00 23.01  ? 95  VAL   A N   1 
ATOM   770  C  CA  . VAL   A 1 115 ? 122.776 28.943 9.416   1.00 23.34  ? 95  VAL   A CA  1 
ATOM   771  C  C   . VAL   A 1 115 ? 121.599 28.248 8.710   1.00 22.62  ? 95  VAL   A C   1 
ATOM   772  O  O   . VAL   A 1 115 ? 120.444 28.431 9.091   1.00 23.00  ? 95  VAL   A O   1 
ATOM   773  C  CB  . VAL   A 1 115 ? 123.294 30.125 8.585   1.00 25.64  ? 95  VAL   A CB  1 
ATOM   774  C  CG1 . VAL   A 1 115 ? 122.148 30.925 7.947   1.00 26.84  ? 95  VAL   A CG1 1 
ATOM   775  C  CG2 . VAL   A 1 115 ? 124.193 31.028 9.438   1.00 25.55  ? 95  VAL   A CG2 1 
ATOM   776  N  N   . PHE   A 1 116 ? 121.911 27.390 7.720   1.00 21.52  ? 96  PHE   A N   1 
ATOM   777  C  CA  . PHE   A 1 116 ? 120.839 26.686 7.000   1.00 21.26  ? 96  PHE   A CA  1 
ATOM   778  C  C   . PHE   A 1 116 ? 120.042 25.794 7.946   1.00 21.55  ? 96  PHE   A C   1 
ATOM   779  O  O   . PHE   A 1 116 ? 118.814 25.727 7.849   1.00 21.80  ? 96  PHE   A O   1 
ATOM   780  C  CB  . PHE   A 1 116 ? 121.423 25.839 5.867   1.00 20.63  ? 96  PHE   A CB  1 
ATOM   781  C  CG  . PHE   A 1 116 ? 122.146 26.622 4.797   1.00 20.68  ? 96  PHE   A CG  1 
ATOM   782  C  CD1 . PHE   A 1 116 ? 121.588 27.773 4.253   1.00 21.26  ? 96  PHE   A CD1 1 
ATOM   783  C  CD2 . PHE   A 1 116 ? 123.318 26.139 4.241   1.00 21.41  ? 96  PHE   A CD2 1 
ATOM   784  C  CE1 . PHE   A 1 116 ? 122.220 28.440 3.201   1.00 22.00  ? 96  PHE   A CE1 1 
ATOM   785  C  CE2 . PHE   A 1 116 ? 123.943 26.805 3.201   1.00 22.16  ? 96  PHE   A CE2 1 
ATOM   786  C  CZ  . PHE   A 1 116 ? 123.387 27.945 2.677   1.00 21.99  ? 96  PHE   A CZ  1 
ATOM   787  N  N   . VAL   A 1 117 ? 120.746 25.090 8.835   1.00 21.00  ? 97  VAL   A N   1 
ATOM   788  C  CA  . VAL   A 1 117 ? 120.116 24.164 9.778   1.00 21.97  ? 97  VAL   A CA  1 
ATOM   789  C  C   . VAL   A 1 117 ? 119.273 24.933 10.796  1.00 22.16  ? 97  VAL   A C   1 
ATOM   790  O  O   . VAL   A 1 117 ? 118.108 24.608 11.041  1.00 22.71  ? 97  VAL   A O   1 
ATOM   791  C  CB  . VAL   A 1 117 ? 121.207 23.311 10.454  1.00 23.66  ? 97  VAL   A CB  1 
ATOM   792  C  CG1 . VAL   A 1 117 ? 120.600 22.420 11.531  1.00 24.83  ? 97  VAL   A CG1 1 
ATOM   793  C  CG2 . VAL   A 1 117 ? 121.954 22.476 9.414   1.00 23.74  ? 97  VAL   A CG2 1 
ATOM   794  N  N   . ARG   A 1 118 ? 119.846 26.006 11.339  1.00 21.22  ? 98  ARG   A N   1 
ATOM   795  C  CA  . ARG   A 1 118 ? 119.176 26.884 12.290  1.00 21.99  ? 98  ARG   A CA  1 
ATOM   796  C  C   . ARG   A 1 118 ? 117.849 27.410 11.693  1.00 22.11  ? 98  ARG   A C   1 
ATOM   797  O  O   . ARG   A 1 118 ? 116.806 27.378 12.361  1.00 23.25  ? 98  ARG   A O   1 
ATOM   798  C  CB  . ARG   A 1 118 ? 120.113 28.056 12.583  1.00 23.44  ? 98  ARG   A CB  1 
ATOM   799  C  CG  . ARG   A 1 118 ? 119.551 29.068 13.587  1.00 25.32  ? 98  ARG   A CG  1 
ATOM   800  C  CD  . ARG   A 1 118 ? 120.324 30.355 13.494  1.00 26.00  ? 98  ARG   A CD  1 
ATOM   801  N  NE  . ARG   A 1 118 ? 120.057 31.037 12.234  1.00 26.09  ? 98  ARG   A NE  1 
ATOM   802  C  CZ  . ARG   A 1 118 ? 120.745 32.079 11.784  1.00 28.10  ? 98  ARG   A CZ  1 
ATOM   803  N  NH1 . ARG   A 1 118 ? 121.782 32.548 12.474  1.00 27.79  ? 98  ARG   A NH1 1 
ATOM   804  N  NH2 . ARG   A 1 118 ? 120.420 32.647 10.626  1.00 26.16  ? 98  ARG   A NH2 1 
ATOM   805  N  N   . ASP   A 1 119 ? 117.894 27.835 10.413  1.00 21.44  ? 99  ASP   A N   1 
ATOM   806  C  CA  . ASP   A 1 119 ? 116.718 28.409 9.764   1.00 20.63  ? 99  ASP   A CA  1 
ATOM   807  C  C   . ASP   A 1 119 ? 115.638 27.359 9.494   1.00 20.88  ? 99  ASP   A C   1 
ATOM   808  O  O   . ASP   A 1 119 ? 114.454 27.652 9.680   1.00 21.22  ? 99  ASP   A O   1 
ATOM   809  C  CB  . ASP   A 1 119 ? 117.122 29.173 8.499   1.00 20.62  ? 99  ASP   A CB  1 
ATOM   810  C  CG  . ASP   A 1 119 ? 117.926 30.448 8.777   1.00 23.15  ? 99  ASP   A CG  1 
ATOM   811  O  OD1 . ASP   A 1 119 ? 118.094 30.815 9.984   1.00 23.46  ? 99  ASP   A OD1 1 
ATOM   812  O  OD2 . ASP   A 1 119 ? 118.366 31.097 7.801   1.00 22.52  ? 99  ASP   A OD2 1 
ATOM   813  N  N   . VAL   A 1 120 ? 116.029 26.113 9.114   1.00 20.16  ? 100 VAL   A N   1 
ATOM   814  C  CA  . VAL   A 1 120 ? 115.047 25.020 8.939   1.00 19.57  ? 100 VAL   A CA  1 
ATOM   815  C  C   . VAL   A 1 120 ? 114.365 24.766 10.293  1.00 20.59  ? 100 VAL   A C   1 
ATOM   816  O  O   . VAL   A 1 120 ? 113.144 24.717 10.363  1.00 21.50  ? 100 VAL   A O   1 
ATOM   817  C  CB  . VAL   A 1 120 ? 115.715 23.728 8.415   1.00 19.89  ? 100 VAL   A CB  1 
ATOM   818  C  CG1 . VAL   A 1 120 ? 114.748 22.552 8.507   1.00 20.81  ? 100 VAL   A CG1 1 
ATOM   819  C  CG2 . VAL   A 1 120 ? 116.204 23.922 6.973   1.00 19.50  ? 100 VAL   A CG2 1 
ATOM   820  N  N   . LEU   A 1 121 ? 115.155 24.714 11.377  1.00 21.15  ? 101 LEU   A N   1 
ATOM   821  C  CA  . LEU   A 1 121 ? 114.593 24.486 12.706  1.00 22.34  ? 101 LEU   A CA  1 
ATOM   822  C  C   . LEU   A 1 121 ? 113.645 25.585 13.139  1.00 22.56  ? 101 LEU   A C   1 
ATOM   823  O  O   . LEU   A 1 121 ? 112.602 25.292 13.719  1.00 24.04  ? 101 LEU   A O   1 
ATOM   824  C  CB  . LEU   A 1 121 ? 115.695 24.284 13.725  1.00 23.06  ? 101 LEU   A CB  1 
ATOM   825  C  CG  . LEU   A 1 121 ? 116.436 22.954 13.519  1.00 25.82  ? 101 LEU   A CG  1 
ATOM   826  C  CD1 . LEU   A 1 121 ? 117.639 22.922 14.366  1.00 27.30  ? 101 LEU   A CD1 1 
ATOM   827  C  CD2 . LEU   A 1 121 ? 115.522 21.753 13.815  1.00 26.93  ? 101 LEU   A CD2 1 
ATOM   828  N  N   . GLN   A 1 122 ? 113.946 26.861 12.792  1.00 21.83  ? 102 GLN   A N   1 
ATOM   829  C  CA  . GLN   A 1 122 ? 113.044 27.947 13.147  1.00 21.34  ? 102 GLN   A CA  1 
ATOM   830  C  C   . GLN   A 1 122 ? 111.706 27.756 12.424  1.00 22.31  ? 102 GLN   A C   1 
ATOM   831  O  O   . GLN   A 1 122 ? 110.654 27.890 13.039  1.00 23.44  ? 102 GLN   A O   1 
ATOM   832  C  CB  . GLN   A 1 122 ? 113.678 29.292 12.785  1.00 21.28  ? 102 GLN   A CB  1 
ATOM   833  C  CG  . GLN   A 1 122 ? 112.741 30.453 13.088  1.00 23.24  ? 102 GLN   A CG  1 
ATOM   834  C  CD  . GLN   A 1 122 ? 113.174 31.745 12.446  1.00 25.36  ? 102 GLN   A CD  1 
ATOM   835  O  OE1 . GLN   A 1 122 ? 114.280 31.862 11.882  1.00 27.27  ? 102 GLN   A OE1 1 
ATOM   836  N  NE2 . GLN   A 1 122 ? 112.295 32.754 12.516  1.00 24.78  ? 102 GLN   A NE2 1 
ATOM   837  N  N   . HIS   A 1 123 ? 111.755 27.427 11.126  1.00 21.37  ? 103 HIS   A N   1 
ATOM   838  C  CA  . HIS   A 1 123 ? 110.533 27.260 10.356  1.00 21.78  ? 103 HIS   A CA  1 
ATOM   839  C  C   . HIS   A 1 123 ? 109.727 26.045 10.843  1.00 22.09  ? 103 HIS   A C   1 
ATOM   840  O  O   . HIS   A 1 123 ? 108.518 26.170 11.067  1.00 22.99  ? 103 HIS   A O   1 
ATOM   841  C  CB  . HIS   A 1 123 ? 110.875 27.161 8.869   1.00 21.06  ? 103 HIS   A CB  1 
ATOM   842  C  CG  . HIS   A 1 123 ? 109.750 27.497 7.944   1.00 20.86  ? 103 HIS   A CG  1 
ATOM   843  N  ND1 . HIS   A 1 123 ? 109.961 27.584 6.582   1.00 22.42  ? 103 HIS   A ND1 1 
ATOM   844  C  CD2 . HIS   A 1 123 ? 108.436 27.719 8.199   1.00 21.74  ? 103 HIS   A CD2 1 
ATOM   845  C  CE1 . HIS   A 1 123 ? 108.787 27.904 6.051   1.00 22.67  ? 103 HIS   A CE1 1 
ATOM   846  N  NE2 . HIS   A 1 123 ? 107.832 27.968 6.986   1.00 22.42  ? 103 HIS   A NE2 1 
ATOM   847  N  N   . VAL   A 1 124 ? 110.407 24.929 11.154  1.00 21.93  ? 104 VAL   A N   1 
ATOM   848  C  CA  . VAL   A 1 124 ? 109.732 23.738 11.671  1.00 22.96  ? 104 VAL   A CA  1 
ATOM   849  C  C   . VAL   A 1 124 ? 109.057 24.084 13.022  1.00 24.46  ? 104 VAL   A C   1 
ATOM   850  O  O   . VAL   A 1 124 ? 107.883 23.783 13.234  1.00 25.58  ? 104 VAL   A O   1 
ATOM   851  C  CB  . VAL   A 1 124 ? 110.747 22.587 11.823  1.00 23.39  ? 104 VAL   A CB  1 
ATOM   852  C  CG1 . VAL   A 1 124 ? 110.187 21.479 12.726  1.00 24.34  ? 104 VAL   A CG1 1 
ATOM   853  C  CG2 . VAL   A 1 124 ? 111.133 22.037 10.448  1.00 22.28  ? 104 VAL   A CG2 1 
ATOM   854  N  N   . ASP   A 1 125 ? 109.794 24.764 13.907  1.00 24.43  ? 105 ASP   A N   1 
ATOM   855  C  CA  . ASP   A 1 125 ? 109.258 25.141 15.220  1.00 25.28  ? 105 ASP   A CA  1 
ATOM   856  C  C   . ASP   A 1 125 ? 108.046 26.040 15.096  1.00 26.84  ? 105 ASP   A C   1 
ATOM   857  O  O   . ASP   A 1 125 ? 107.080 25.869 15.838  1.00 28.58  ? 105 ASP   A O   1 
ATOM   858  C  CB  . ASP   A 1 125 ? 110.347 25.802 16.066  1.00 26.48  ? 105 ASP   A CB  1 
ATOM   859  C  CG  . ASP   A 1 125 ? 111.418 24.823 16.541  1.00 29.57  ? 105 ASP   A CG  1 
ATOM   860  O  OD1 . ASP   A 1 125 ? 111.186 23.591 16.454  1.00 30.38  ? 105 ASP   A OD1 1 
ATOM   861  O  OD2 . ASP   A 1 125 ? 112.480 25.284 17.005  1.00 30.43  ? 105 ASP   A OD2 1 
ATOM   862  N  N   . SER   A 1 126 ? 108.076 26.968 14.133  1.00 26.14  ? 106 SER   A N   1 
ATOM   863  C  CA  A SER   A 1 126 ? 106.967 27.889 13.903  0.50 26.74  ? 106 SER   A CA  1 
ATOM   864  C  CA  C SER   A 1 126 ? 106.957 27.874 13.927  0.49 27.06  ? 106 SER   A CA  1 
ATOM   865  C  C   . SER   A 1 126 ? 105.737 27.113 13.417  1.00 28.31  ? 106 SER   A C   1 
ATOM   866  O  O   . SER   A 1 126 ? 104.623 27.369 13.867  1.00 30.38  ? 106 SER   A O   1 
ATOM   867  C  CB  A SER   A 1 126 ? 107.366 28.932 12.862  0.50 27.01  ? 106 SER   A CB  1 
ATOM   868  C  CB  C SER   A 1 126 ? 107.353 28.974 12.953  0.49 28.26  ? 106 SER   A CB  1 
ATOM   869  O  OG  A SER   A 1 126 ? 106.396 29.962 12.756  0.50 27.74  ? 106 SER   A OG  1 
ATOM   870  O  OG  C SER   A 1 126 ? 108.345 29.787 13.558  0.49 30.37  ? 106 SER   A OG  1 
ATOM   871  N  N   . MET   A 1 127 ? 105.941 26.168 12.495  1.00 28.30  ? 107 MET   A N   1 
ATOM   872  C  CA  . MET   A 1 127 ? 104.831 25.380 11.965  1.00 29.84  ? 107 MET   A CA  1 
ATOM   873  C  C   . MET   A 1 127 ? 104.228 24.443 12.994  1.00 31.92  ? 107 MET   A C   1 
ATOM   874  O  O   . MET   A 1 127 ? 103.009 24.240 13.006  1.00 33.09  ? 107 MET   A O   1 
ATOM   875  C  CB  . MET   A 1 127 ? 105.274 24.626 10.709  1.00 29.97  ? 107 MET   A CB  1 
ATOM   876  C  CG  . MET   A 1 127 ? 105.489 25.566 9.565   1.00 32.44  ? 107 MET   A CG  1 
ATOM   877  S  SD  . MET   A 1 127 ? 103.910 26.265 9.012   1.00 37.47  ? 107 MET   A SD  1 
ATOM   878  C  CE  . MET   A 1 127 ? 103.220 24.869 8.245   1.00 35.92  ? 107 MET   A CE  1 
ATOM   879  N  N   . GLN   A 1 128 ? 105.062 23.900 13.877  1.00 32.39  ? 108 GLN   A N   1 
ATOM   880  C  CA  . GLN   A 1 128 ? 104.572 23.000 14.923  1.00 34.30  ? 108 GLN   A CA  1 
ATOM   881  C  C   . GLN   A 1 128 ? 103.728 23.743 15.972  1.00 36.74  ? 108 GLN   A C   1 
ATOM   882  O  O   . GLN   A 1 128 ? 102.899 23.133 16.630  1.00 37.44  ? 108 GLN   A O   1 
ATOM   883  C  CB  . GLN   A 1 128 ? 105.714 22.214 15.552  1.00 35.17  ? 108 GLN   A CB  1 
ATOM   884  C  CG  . GLN   A 1 128 ? 106.278 21.194 14.578  1.00 37.38  ? 108 GLN   A CG  1 
ATOM   885  C  CD  . GLN   A 1 128 ? 107.041 20.135 15.320  1.00 41.90  ? 108 GLN   A CD  1 
ATOM   886  O  OE1 . GLN   A 1 128 ? 108.226 20.293 15.604  1.00 43.32  ? 108 GLN   A OE1 1 
ATOM   887  N  NE2 . GLN   A 1 128 ? 106.369 19.037 15.675  1.00 43.23  ? 108 GLN   A NE2 1 
ATOM   888  N  N   . LYS   A 1 129 ? 103.904 25.057 16.090  1.00 38.84  ? 109 LYS   A N   1 
ATOM   889  C  CA  . LYS   A 1 129 ? 103.086 25.878 16.971  1.00 40.66  ? 109 LYS   A CA  1 
ATOM   890  C  C   . LYS   A 1 129 ? 101.679 25.986 16.351  1.00 42.21  ? 109 LYS   A C   1 
ATOM   891  O  O   . LYS   A 1 129 ? 100.688 25.863 17.059  1.00 42.74  ? 109 LYS   A O   1 
ATOM   892  C  CB  . LYS   A 1 129 ? 103.714 27.275 17.096  1.00 42.85  ? 109 LYS   A CB  1 
ATOM   893  C  CG  . LYS   A 1 129 ? 104.953 27.312 17.973  1.00 48.03  ? 109 LYS   A CG  1 
ATOM   894  C  CD  . LYS   A 1 129 ? 104.611 27.591 19.431  1.00 54.77  ? 109 LYS   A CD  1 
ATOM   895  C  CE  . LYS   A 1 129 ? 103.868 28.895 19.615  1.00 59.06  ? 109 LYS   A CE  1 
ATOM   896  N  NZ  . LYS   A 1 129 ? 104.554 30.029 18.944  1.00 61.05  ? 109 LYS   A NZ  1 
ATOM   897  N  N   . ASP   A 1 130 ? 101.594 26.206 15.032  1.00 42.96  ? 110 ASP   A N   1 
ATOM   898  C  CA  . ASP   A 1 130 ? 100.311 26.339 14.344  1.00 44.66  ? 110 ASP   A CA  1 
ATOM   899  C  C   . ASP   A 1 130 ? 99.593  25.002 14.158  1.00 45.54  ? 110 ASP   A C   1 
ATOM   900  O  O   . ASP   A 1 130 ? 98.368  24.965 14.096  1.00 46.31  ? 110 ASP   A O   1 
ATOM   901  C  CB  . ASP   A 1 130 ? 100.492 27.045 12.991  1.00 47.20  ? 110 ASP   A CB  1 
ATOM   902  C  CG  . ASP   A 1 130 ? 100.990 28.476 13.077  1.00 53.32  ? 110 ASP   A CG  1 
ATOM   903  O  OD1 . ASP   A 1 130 ? 101.040 29.025 14.201  1.00 54.06  ? 110 ASP   A OD1 1 
ATOM   904  O  OD2 . ASP   A 1 130 ? 101.345 29.044 12.022  1.00 56.90  ? 110 ASP   A OD2 1 
ATOM   905  N  N   . TYR   A 1 131 ? 100.343 23.904 14.061  1.00 45.39  ? 111 TYR   A N   1 
ATOM   906  C  CA  . TYR   A 1 131 ? 99.762  22.577 13.878  1.00 45.70  ? 111 TYR   A CA  1 
ATOM   907  C  C   . TYR   A 1 131 ? 100.365 21.652 14.918  1.00 45.94  ? 111 TYR   A C   1 
ATOM   908  O  O   . TYR   A 1 131 ? 101.256 20.867 14.603  1.00 46.45  ? 111 TYR   A O   1 
ATOM   909  C  CB  . TYR   A 1 131 ? 100.048 22.074 12.447  1.00 45.66  ? 111 TYR   A CB  1 
ATOM   910  C  CG  . TYR   A 1 131 ? 99.512  23.008 11.384  1.00 46.34  ? 111 TYR   A CG  1 
ATOM   911  C  CD1 . TYR   A 1 131 ? 100.288 24.044 10.884  1.00 46.87  ? 111 TYR   A CD1 1 
ATOM   912  C  CD2 . TYR   A 1 131 ? 98.206  22.895 10.926  1.00 47.37  ? 111 TYR   A CD2 1 
ATOM   913  C  CE1 . TYR   A 1 131 ? 99.784  24.938 9.949   1.00 48.16  ? 111 TYR   A CE1 1 
ATOM   914  C  CE2 . TYR   A 1 131 ? 97.694  23.775 9.979   1.00 48.24  ? 111 TYR   A CE2 1 
ATOM   915  C  CZ  . TYR   A 1 131 ? 98.481  24.807 9.506   1.00 49.44  ? 111 TYR   A CZ  1 
ATOM   916  O  OH  . TYR   A 1 131 ? 97.994  25.675 8.555   1.00 51.47  ? 111 TYR   A OH  1 
ATOM   917  N  N   . PRO   A 1 132 ? 99.952  21.785 16.191  1.00 45.61  ? 112 PRO   A N   1 
ATOM   918  C  CA  . PRO   A 1 132 ? 100.556 20.953 17.240  1.00 45.45  ? 112 PRO   A CA  1 
ATOM   919  C  C   . PRO   A 1 132 ? 100.133 19.497 17.184  1.00 45.64  ? 112 PRO   A C   1 
ATOM   920  O  O   . PRO   A 1 132 ? 99.080  19.173 16.641  1.00 46.71  ? 112 PRO   A O   1 
ATOM   921  C  CB  . PRO   A 1 132 ? 100.090 21.620 18.531  1.00 46.29  ? 112 PRO   A CB  1 
ATOM   922  C  CG  . PRO   A 1 132 ? 98.807  22.272 18.172  1.00 46.85  ? 112 PRO   A CG  1 
ATOM   923  C  CD  . PRO   A 1 132 ? 98.921  22.691 16.738  1.00 45.15  ? 112 PRO   A CD  1 
ATOM   924  N  N   . GLY   A 1 133 ? 100.972 18.632 17.736  1.00 44.68  ? 113 GLY   A N   1 
ATOM   925  C  CA  . GLY   A 1 133 ? 100.712 17.200 17.801  1.00 43.92  ? 113 GLY   A CA  1 
ATOM   926  C  C   . GLY   A 1 133 ? 100.893 16.425 16.512  1.00 42.74  ? 113 GLY   A C   1 
ATOM   927  O  O   . GLY   A 1 133 ? 100.636 15.217 16.484  1.00 43.41  ? 113 GLY   A O   1 
ATOM   928  N  N   . LEU   A 1 134 ? 101.329 17.092 15.436  1.00 40.42  ? 114 LEU   A N   1 
ATOM   929  C  CA  . LEU   A 1 134 ? 101.517 16.412 14.160  1.00 38.54  ? 114 LEU   A CA  1 
ATOM   930  C  C   . LEU   A 1 134 ? 102.938 15.925 13.995  1.00 36.05  ? 114 LEU   A C   1 
ATOM   931  O  O   . LEU   A 1 134 ? 103.880 16.656 14.301  1.00 36.05  ? 114 LEU   A O   1 
ATOM   932  C  CB  . LEU   A 1 134 ? 101.184 17.333 12.975  1.00 39.05  ? 114 LEU   A CB  1 
ATOM   933  C  CG  . LEU   A 1 134 ? 99.717  17.672 12.718  1.00 41.55  ? 114 LEU   A CG  1 
ATOM   934  C  CD1 . LEU   A 1 134 ? 99.576  18.467 11.418  1.00 42.29  ? 114 LEU   A CD1 1 
ATOM   935  C  CD2 . LEU   A 1 134 ? 98.844  16.407 12.669  1.00 42.40  ? 114 LEU   A CD2 1 
ATOM   936  N  N   . PRO   A 1 135 ? 103.115 14.734 13.411  1.00 33.73  ? 115 PRO   A N   1 
ATOM   937  C  CA  . PRO   A 1 135 ? 104.476 14.280 13.088  1.00 31.62  ? 115 PRO   A CA  1 
ATOM   938  C  C   . PRO   A 1 135 ? 105.091 15.182 12.019  1.00 29.44  ? 115 PRO   A C   1 
ATOM   939  O  O   . PRO   A 1 135 ? 104.372 15.760 11.197  1.00 29.58  ? 115 PRO   A O   1 
ATOM   940  C  CB  . PRO   A 1 135 ? 104.257 12.869 12.520  1.00 32.62  ? 115 PRO   A CB  1 
ATOM   941  C  CG  . PRO   A 1 135 ? 102.858 12.480 12.992  1.00 34.30  ? 115 PRO   A CG  1 
ATOM   942  C  CD  . PRO   A 1 135 ? 102.100 13.761 12.971  1.00 33.11  ? 115 PRO   A CD  1 
ATOM   943  N  N   . VAL   A 1 136 ? 106.412 15.331 12.050  1.00 26.71  ? 116 VAL   A N   1 
ATOM   944  C  CA  A VAL   A 1 136 ? 107.104 16.165 11.070  0.56 26.21  ? 116 VAL   A CA  1 
ATOM   945  C  CA  B VAL   A 1 136 ? 107.112 16.166 11.076  0.44 25.69  ? 116 VAL   A CA  1 
ATOM   946  C  C   . VAL   A 1 136 ? 108.186 15.388 10.346  1.00 25.33  ? 116 VAL   A C   1 
ATOM   947  O  O   . VAL   A 1 136 ? 109.019 14.752 10.982  1.00 25.71  ? 116 VAL   A O   1 
ATOM   948  C  CB  A VAL   A 1 136 ? 107.637 17.484 11.671  0.56 28.00  ? 116 VAL   A CB  1 
ATOM   949  C  CB  B VAL   A 1 136 ? 107.706 17.419 11.737  0.44 26.23  ? 116 VAL   A CB  1 
ATOM   950  C  CG1 A VAL   A 1 136 ? 108.526 17.231 12.881  0.56 29.49  ? 116 VAL   A CG1 1 
ATOM   951  C  CG1 B VAL   A 1 136 ? 108.434 18.284 10.717  0.44 26.75  ? 116 VAL   A CG1 1 
ATOM   952  C  CG2 A VAL   A 1 136 ? 108.358 18.323 10.623  0.56 28.36  ? 116 VAL   A CG2 1 
ATOM   953  C  CG2 B VAL   A 1 136 ? 106.617 18.216 12.436  0.44 26.32  ? 116 VAL   A CG2 1 
ATOM   954  N  N   . PHE   A 1 137 ? 108.165 15.437 9.011   1.00 23.59  ? 117 PHE   A N   1 
ATOM   955  C  CA  . PHE   A 1 137 ? 109.149 14.772 8.159   1.00 22.56  ? 117 PHE   A CA  1 
ATOM   956  C  C   . PHE   A 1 137 ? 110.042 15.826 7.495   1.00 21.32  ? 117 PHE   A C   1 
ATOM   957  O  O   . PHE   A 1 137 ? 109.670 16.995 7.401   1.00 21.11  ? 117 PHE   A O   1 
ATOM   958  C  CB  . PHE   A 1 137 ? 108.437 14.018 7.011   1.00 22.97  ? 117 PHE   A CB  1 
ATOM   959  C  CG  . PHE   A 1 137 ? 107.667 12.816 7.474   1.00 24.33  ? 117 PHE   A CG  1 
ATOM   960  C  CD1 . PHE   A 1 137 ? 106.420 12.955 8.050   1.00 25.85  ? 117 PHE   A CD1 1 
ATOM   961  C  CD2 . PHE   A 1 137 ? 108.184 11.540 7.317   1.00 25.37  ? 117 PHE   A CD2 1 
ATOM   962  C  CE1 . PHE   A 1 137 ? 105.717 11.841 8.506   1.00 26.99  ? 117 PHE   A CE1 1 
ATOM   963  C  CE2 . PHE   A 1 137 ? 107.486 10.426 7.783   1.00 25.61  ? 117 PHE   A CE2 1 
ATOM   964  C  CZ  . PHE   A 1 137 ? 106.256 10.585 8.367   1.00 26.43  ? 117 PHE   A CZ  1 
ATOM   965  N  N   . LEU   A 1 138 ? 111.178 15.379 6.984   1.00 20.44  ? 118 LEU   A N   1 
ATOM   966  C  CA  . LEU   A 1 138 ? 112.084 16.202 6.192   1.00 20.70  ? 118 LEU   A CA  1 
ATOM   967  C  C   . LEU   A 1 138 ? 112.279 15.567 4.845   1.00 20.82  ? 118 LEU   A C   1 
ATOM   968  O  O   . LEU   A 1 138 ? 112.379 14.349 4.756   1.00 21.02  ? 118 LEU   A O   1 
ATOM   969  C  CB  . LEU   A 1 138 ? 113.456 16.315 6.842   1.00 21.05  ? 118 LEU   A CB  1 
ATOM   970  C  CG  . LEU   A 1 138 ? 113.465 16.978 8.208   1.00 23.01  ? 118 LEU   A CG  1 
ATOM   971  C  CD1 . LEU   A 1 138 ? 114.754 16.701 8.945   1.00 24.46  ? 118 LEU   A CD1 1 
ATOM   972  C  CD2 . LEU   A 1 138 ? 113.212 18.481 8.081   1.00 23.87  ? 118 LEU   A CD2 1 
ATOM   973  N  N   . LEU   A 1 139 ? 112.402 16.376 3.803   1.00 19.84  ? 119 LEU   A N   1 
ATOM   974  C  CA  . LEU   A 1 139 ? 112.755 15.891 2.477   1.00 19.78  ? 119 LEU   A CA  1 
ATOM   975  C  C   . LEU   A 1 139 ? 113.864 16.783 1.997   1.00 19.83  ? 119 LEU   A C   1 
ATOM   976  O  O   . LEU   A 1 139 ? 113.666 17.994 1.963   1.00 19.81  ? 119 LEU   A O   1 
ATOM   977  C  CB  . LEU   A 1 139 ? 111.575 15.914 1.505   1.00 19.89  ? 119 LEU   A CB  1 
ATOM   978  C  CG  . LEU   A 1 139 ? 111.878 15.291 0.129   1.00 21.60  ? 119 LEU   A CG  1 
ATOM   979  C  CD1 . LEU   A 1 139 ? 110.649 14.595 -0.425  1.00 22.08  ? 119 LEU   A CD1 1 
ATOM   980  C  CD2 . LEU   A 1 139 ? 112.411 16.355 -0.843  1.00 21.15  ? 119 LEU   A CD2 1 
ATOM   981  N  N   . GLY   A 1 140 ? 115.010 16.227 1.646   1.00 18.45  ? 120 GLY   A N   1 
ATOM   982  C  CA  . GLY   A 1 140 ? 116.119 17.053 1.173   1.00 18.04  ? 120 GLY   A CA  1 
ATOM   983  C  C   . GLY   A 1 140 ? 116.794 16.468 -0.036  1.00 18.99  ? 120 GLY   A C   1 
ATOM   984  O  O   . GLY   A 1 140 ? 116.977 15.250 -0.110  1.00 19.82  ? 120 GLY   A O   1 
ATOM   985  N  N   . HIS   A 1 141 ? 117.216 17.331 -0.957  1.00 17.81  ? 121 HIS   A N   1 
ATOM   986  C  CA  . HIS   A 1 141 ? 117.973 16.917 -2.138  1.00 18.90  ? 121 HIS   A CA  1 
ATOM   987  C  C   . HIS   A 1 141 ? 119.363 17.567 -2.124  1.00 19.87  ? 121 HIS   A C   1 
ATOM   988  O  O   . HIS   A 1 141 ? 119.456 18.758 -1.871  1.00 19.78  ? 121 HIS   A O   1 
ATOM   989  C  CB  . HIS   A 1 141 ? 117.233 17.374 -3.408  1.00 19.48  ? 121 HIS   A CB  1 
ATOM   990  C  CG  . HIS   A 1 141 ? 118.062 17.333 -4.665  1.00 20.34  ? 121 HIS   A CG  1 
ATOM   991  N  ND1 . HIS   A 1 141 ? 118.724 16.176 -5.076  1.00 20.51  ? 121 HIS   A ND1 1 
ATOM   992  C  CD2 . HIS   A 1 141 ? 118.293 18.316 -5.569  1.00 20.76  ? 121 HIS   A CD2 1 
ATOM   993  C  CE1 . HIS   A 1 141 ? 119.337 16.494 -6.212  1.00 20.86  ? 121 HIS   A CE1 1 
ATOM   994  N  NE2 . HIS   A 1 141 ? 119.116 17.776 -6.547  1.00 21.42  ? 121 HIS   A NE2 1 
ATOM   995  N  N   . SER   A 1 142 ? 120.429 16.780 -2.345  1.00 20.28  ? 122 SER   A N   1 
ATOM   996  C  CA  . SER   A 1 142 ? 121.783 17.306 -2.528  1.00 20.43  ? 122 SER   A CA  1 
ATOM   997  C  C   . SER   A 1 142 ? 122.285 18.102 -1.301  1.00 19.56  ? 122 SER   A C   1 
ATOM   998  O  O   . SER   A 1 142 ? 122.251 17.542 -0.196  1.00 18.11  ? 122 SER   A O   1 
ATOM   999  C  CB  . SER   A 1 142 ? 121.830 18.084 -3.840  1.00 23.41  ? 122 SER   A CB  1 
ATOM   1000 O  OG  . SER   A 1 142 ? 123.169 18.283 -4.260  1.00 25.46  ? 122 SER   A OG  1 
ATOM   1001 N  N   . MET   A 1 143 ? 122.676 19.397 -1.428  1.00 19.78  ? 123 MET   A N   1 
ATOM   1002 C  CA  . MET   A 1 143 ? 123.032 20.194 -0.245  1.00 19.62  ? 123 MET   A CA  1 
ATOM   1003 C  C   . MET   A 1 143 ? 121.866 20.221 0.763   1.00 18.90  ? 123 MET   A C   1 
ATOM   1004 O  O   . MET   A 1 143 ? 122.103 20.174 1.981   1.00 19.92  ? 123 MET   A O   1 
ATOM   1005 C  CB  . MET   A 1 143 ? 123.403 21.630 -0.645  1.00 20.08  ? 123 MET   A CB  1 
ATOM   1006 C  CG  . MET   A 1 143 ? 123.772 22.490 0.538   1.00 21.67  ? 123 MET   A CG  1 
ATOM   1007 S  SD  . MET   A 1 143 ? 123.986 24.221 0.057   1.00 23.94  ? 123 MET   A SD  1 
ATOM   1008 C  CE  . MET   A 1 143 ? 122.306 24.772 0.066   1.00 22.72  ? 123 MET   A CE  1 
ATOM   1009 N  N   . GLY   A 1 144 ? 120.631 20.228 0.253   1.00 18.30  ? 124 GLY   A N   1 
ATOM   1010 C  CA  . GLY   A 1 144 ? 119.439 20.212 1.098   1.00 18.23  ? 124 GLY   A CA  1 
ATOM   1011 C  C   . GLY   A 1 144 ? 119.309 18.911 1.888   1.00 18.39  ? 124 GLY   A C   1 
ATOM   1012 O  O   . GLY   A 1 144 ? 118.705 18.894 2.959   1.00 19.48  ? 124 GLY   A O   1 
ATOM   1013 N  N   . GLY   A 1 145 ? 119.883 17.823 1.372   1.00 18.00  ? 125 GLY   A N   1 
ATOM   1014 C  CA  . GLY   A 1 145 ? 119.925 16.517 2.041   1.00 19.00  ? 125 GLY   A CA  1 
ATOM   1015 C  C   . GLY   A 1 145 ? 120.938 16.566 3.174   1.00 19.69  ? 125 GLY   A C   1 
ATOM   1016 O  O   . GLY   A 1 145 ? 120.707 15.982 4.240   1.00 19.75  ? 125 GLY   A O   1 
ATOM   1017 N  N   . ALA   A 1 146 ? 122.085 17.243 2.970   1.00 19.85  ? 126 ALA   A N   1 
ATOM   1018 C  CA  . ALA   A 1 146 ? 123.071 17.408 4.058   1.00 20.47  ? 126 ALA   A CA  1 
ATOM   1019 C  C   . ALA   A 1 146 ? 122.429 18.263 5.172   1.00 20.58  ? 126 ALA   A C   1 
ATOM   1020 O  O   . ALA   A 1 146 ? 122.537 17.949 6.359   1.00 21.71  ? 126 ALA   A O   1 
ATOM   1021 C  CB  . ALA   A 1 146 ? 124.343 18.084 3.553   1.00 20.66  ? 126 ALA   A CB  1 
ATOM   1022 N  N   . ILE   A 1 147 ? 121.693 19.317 4.776   1.00 19.94  ? 127 ILE   A N   1 
ATOM   1023 C  CA  . ILE   A 1 147 ? 120.960 20.127 5.752   1.00 19.70  ? 127 ILE   A CA  1 
ATOM   1024 C  C   . ILE   A 1 147 ? 119.930 19.275 6.516   1.00 20.29  ? 127 ILE   A C   1 
ATOM   1025 O  O   . ILE   A 1 147 ? 119.880 19.350 7.752   1.00 21.38  ? 127 ILE   A O   1 
ATOM   1026 C  CB  . ILE   A 1 147 ? 120.295 21.304 5.021   1.00 19.89  ? 127 ILE   A CB  1 
ATOM   1027 C  CG1 . ILE   A 1 147 ? 121.390 22.244 4.479   1.00 19.13  ? 127 ILE   A CG1 1 
ATOM   1028 C  CG2 . ILE   A 1 147 ? 119.358 22.064 5.975   1.00 21.33  ? 127 ILE   A CG2 1 
ATOM   1029 C  CD1 . ILE   A 1 147 ? 120.824 23.334 3.474   1.00 19.81  ? 127 ILE   A CD1 1 
ATOM   1030 N  N   . ALA   A 1 148 ? 119.162 18.406 5.805   1.00 20.04  ? 128 ALA   A N   1 
ATOM   1031 C  CA  . ALA   A 1 148 ? 118.164 17.556 6.467   1.00 20.81  ? 128 ALA   A CA  1 
ATOM   1032 C  C   . ALA   A 1 148 ? 118.836 16.594 7.461   1.00 21.48  ? 128 ALA   A C   1 
ATOM   1033 O  O   . ALA   A 1 148 ? 118.374 16.464 8.600   1.00 22.52  ? 128 ALA   A O   1 
ATOM   1034 C  CB  . ALA   A 1 148 ? 117.349 16.763 5.433   1.00 20.44  ? 128 ALA   A CB  1 
ATOM   1035 N  N   . ILE   A 1 149 ? 119.974 15.987 7.070   1.00 20.73  ? 129 ILE   A N   1 
ATOM   1036 C  CA  . ILE   A 1 149 ? 120.695 15.079 7.978   1.00 21.14  ? 129 ILE   A CA  1 
ATOM   1037 C  C   . ILE   A 1 149 ? 121.149 15.816 9.237   1.00 21.79  ? 129 ILE   A C   1 
ATOM   1038 O  O   . ILE   A 1 149 ? 120.944 15.322 10.351  1.00 22.73  ? 129 ILE   A O   1 
ATOM   1039 C  CB  . ILE   A 1 149 ? 121.904 14.458 7.254   1.00 21.82  ? 129 ILE   A CB  1 
ATOM   1040 C  CG1 . ILE   A 1 149 ? 121.418 13.478 6.177   1.00 22.21  ? 129 ILE   A CG1 1 
ATOM   1041 C  CG2 . ILE   A 1 149 ? 122.889 13.768 8.242   1.00 22.62  ? 129 ILE   A CG2 1 
ATOM   1042 C  CD1 . ILE   A 1 149 ? 122.537 13.087 5.239   1.00 23.02  ? 129 ILE   A CD1 1 
ATOM   1043 N  N   . LEU   A 1 150 ? 121.766 16.991 9.057   1.00 21.37  ? 130 LEU   A N   1 
ATOM   1044 C  CA  . LEU   A 1 150 ? 122.258 17.750 10.223  1.00 22.27  ? 130 LEU   A CA  1 
ATOM   1045 C  C   . LEU   A 1 150 ? 121.105 18.230 11.113  1.00 23.22  ? 130 LEU   A C   1 
ATOM   1046 O  O   . LEU   A 1 150 ? 121.263 18.328 12.336  1.00 25.68  ? 130 LEU   A O   1 
ATOM   1047 C  CB  . LEU   A 1 150 ? 123.182 18.896 9.785   1.00 22.51  ? 130 LEU   A CB  1 
ATOM   1048 C  CG  . LEU   A 1 150 ? 124.449 18.410 9.073   1.00 23.91  ? 130 LEU   A CG  1 
ATOM   1049 C  CD1 . LEU   A 1 150 ? 125.251 19.580 8.548   1.00 23.64  ? 130 LEU   A CD1 1 
ATOM   1050 C  CD2 . LEU   A 1 150 ? 125.315 17.559 9.997   1.00 25.69  ? 130 LEU   A CD2 1 
ATOM   1051 N  N   . THR   A 1 151 ? 119.945 18.528 10.505  1.00 22.08  ? 131 THR   A N   1 
ATOM   1052 C  CA  . THR   A 1 151 ? 118.757 18.983 11.238  1.00 23.19  ? 131 THR   A CA  1 
ATOM   1053 C  C   . THR   A 1 151 ? 118.221 17.833 12.094  1.00 24.24  ? 131 THR   A C   1 
ATOM   1054 O  O   . THR   A 1 151 ? 117.950 18.014 13.297  1.00 24.56  ? 131 THR   A O   1 
ATOM   1055 C  CB  . THR   A 1 151 ? 117.687 19.454 10.241  1.00 24.40  ? 131 THR   A CB  1 
ATOM   1056 O  OG1 . THR   A 1 151 ? 118.191 20.599 9.539   1.00 23.66  ? 131 THR   A OG1 1 
ATOM   1057 C  CG2 . THR   A 1 151 ? 116.388 19.818 10.936  1.00 25.46  ? 131 THR   A CG2 1 
ATOM   1058 N  N   . ALA   A 1 152 ? 118.124 16.629 11.488  1.00 24.22  ? 132 ALA   A N   1 
ATOM   1059 C  CA  . ALA   A 1 152 ? 117.633 15.472 12.248  1.00 26.27  ? 132 ALA   A CA  1 
ATOM   1060 C  C   . ALA   A 1 152 ? 118.631 15.069 13.323  1.00 29.75  ? 132 ALA   A C   1 
ATOM   1061 O  O   . ALA   A 1 152 ? 118.215 14.670 14.416  1.00 32.13  ? 132 ALA   A O   1 
ATOM   1062 C  CB  . ALA   A 1 152 ? 117.357 14.302 11.320  1.00 25.89  ? 132 ALA   A CB  1 
ATOM   1063 N  N   . ALA   A 1 153 ? 119.942 15.194 13.047  1.00 30.21  ? 133 ALA   A N   1 
ATOM   1064 C  CA  . ALA   A 1 153 ? 120.955 14.811 14.040  1.00 31.75  ? 133 ALA   A CA  1 
ATOM   1065 C  C   . ALA   A 1 153 ? 120.986 15.750 15.237  1.00 32.54  ? 133 ALA   A C   1 
ATOM   1066 O  O   . ALA   A 1 153 ? 121.377 15.328 16.326  1.00 33.65  ? 133 ALA   A O   1 
ATOM   1067 C  CB  . ALA   A 1 153 ? 122.332 14.735 13.412  1.00 32.40  ? 133 ALA   A CB  1 
ATOM   1068 N  N   . GLU   A 1 154 ? 120.612 17.008 15.042  1.00 31.81  ? 134 GLU   A N   1 
ATOM   1069 C  CA  . GLU   A 1 154 ? 120.563 18.000 16.120  1.00 32.68  ? 134 GLU   A CA  1 
ATOM   1070 C  C   . GLU   A 1 154 ? 119.365 17.722 17.062  1.00 33.42  ? 134 GLU   A C   1 
ATOM   1071 O  O   . GLU   A 1 154 ? 119.424 18.044 18.256  1.00 34.58  ? 134 GLU   A O   1 
ATOM   1072 C  CB  . GLU   A 1 154 ? 120.462 19.419 15.518  1.00 34.79  ? 134 GLU   A CB  1 
ATOM   1073 C  CG  . GLU   A 1 154 ? 120.428 20.512 16.561  1.00 38.08  ? 134 GLU   A CG  1 
ATOM   1074 C  CD  . GLU   A 1 154 ? 120.736 21.883 16.006  1.00 40.16  ? 134 GLU   A CD  1 
ATOM   1075 O  OE1 . GLU   A 1 154 ? 121.562 21.966 15.070  1.00 39.14  ? 134 GLU   A OE1 1 
ATOM   1076 O  OE2 . GLU   A 1 154 ? 120.175 22.875 16.520  1.00 42.92  ? 134 GLU   A OE2 1 
ATOM   1077 N  N   . ARG   A 1 155 ? 118.274 17.123 16.532  1.00 32.66  ? 135 ARG   A N   1 
ATOM   1078 C  CA  . ARG   A 1 155 ? 117.090 16.854 17.343  1.00 32.77  ? 135 ARG   A CA  1 
ATOM   1079 C  C   . ARG   A 1 155 ? 116.728 15.364 17.292  1.00 33.79  ? 135 ARG   A C   1 
ATOM   1080 O  O   . ARG   A 1 155 ? 115.720 14.988 16.693  1.00 33.29  ? 135 ARG   A O   1 
ATOM   1081 C  CB  . ARG   A 1 155 ? 115.902 17.709 16.866  1.00 32.89  ? 135 ARG   A CB  1 
ATOM   1082 C  CG  . ARG   A 1 155 ? 116.176 19.216 16.791  1.00 34.23  ? 135 ARG   A CG  1 
ATOM   1083 C  CD  . ARG   A 1 155 ? 115.257 19.940 17.723  1.00 34.91  ? 135 ARG   A CD  1 
ATOM   1084 N  NE  . ARG   A 1 155 ? 115.435 21.397 17.678  1.00 34.39  ? 135 ARG   A NE  1 
ATOM   1085 C  CZ  . ARG   A 1 155 ? 114.467 22.254 17.381  1.00 34.04  ? 135 ARG   A CZ  1 
ATOM   1086 N  NH1 . ARG   A 1 155 ? 113.256 21.814 17.053  1.00 32.17  ? 135 ARG   A NH1 1 
ATOM   1087 N  NH2 . ARG   A 1 155 ? 114.707 23.559 17.378  1.00 31.89  ? 135 ARG   A NH2 1 
ATOM   1088 N  N   . PRO   A 1 156 ? 117.544 14.480 17.892  1.00 35.39  ? 136 PRO   A N   1 
ATOM   1089 C  CA  . PRO   A 1 156 ? 117.212 13.045 17.848  1.00 36.17  ? 136 PRO   A CA  1 
ATOM   1090 C  C   . PRO   A 1 156 ? 115.839 12.749 18.447  1.00 35.88  ? 136 PRO   A C   1 
ATOM   1091 O  O   . PRO   A 1 156 ? 115.455 13.326 19.473  1.00 35.87  ? 136 PRO   A O   1 
ATOM   1092 C  CB  . PRO   A 1 156 ? 118.355 12.379 18.623  1.00 37.72  ? 136 PRO   A CB  1 
ATOM   1093 C  CG  . PRO   A 1 156 ? 118.963 13.464 19.436  1.00 38.79  ? 136 PRO   A CG  1 
ATOM   1094 C  CD  . PRO   A 1 156 ? 118.778 14.733 18.657  1.00 36.44  ? 136 PRO   A CD  1 
ATOM   1095 N  N   . GLY   A 1 157 ? 115.072 11.940 17.733  1.00 34.55  ? 137 GLY   A N   1 
ATOM   1096 C  CA  . GLY   A 1 157 ? 113.731 11.538 18.134  1.00 34.63  ? 137 GLY   A CA  1 
ATOM   1097 C  C   . GLY   A 1 157 ? 112.616 12.496 17.780  1.00 34.77  ? 137 GLY   A C   1 
ATOM   1098 O  O   . GLY   A 1 157 ? 111.449 12.171 17.985  1.00 36.49  ? 137 GLY   A O   1 
ATOM   1099 N  N   . HIS   A 1 158 ? 112.945 13.674 17.258  1.00 32.72  ? 138 HIS   A N   1 
ATOM   1100 C  CA  . HIS   A 1 158 ? 111.950 14.701 16.967  1.00 32.83  ? 138 HIS   A CA  1 
ATOM   1101 C  C   . HIS   A 1 158 ? 111.237 14.489 15.631  1.00 32.06  ? 138 HIS   A C   1 
ATOM   1102 O  O   . HIS   A 1 158 ? 110.055 14.829 15.494  1.00 33.94  ? 138 HIS   A O   1 
ATOM   1103 C  CB  . HIS   A 1 158 ? 112.657 16.067 16.954  1.00 35.26  ? 138 HIS   A CB  1 
ATOM   1104 C  CG  . HIS   A 1 158 ? 111.771 17.256 16.769  1.00 40.98  ? 138 HIS   A CG  1 
ATOM   1105 N  ND1 . HIS   A 1 158 ? 111.337 18.004 17.856  1.00 44.10  ? 138 HIS   A ND1 1 
ATOM   1106 C  CD2 . HIS   A 1 158 ? 111.340 17.851 15.630  1.00 42.46  ? 138 HIS   A CD2 1 
ATOM   1107 C  CE1 . HIS   A 1 158 ? 110.636 19.006 17.345  1.00 44.66  ? 138 HIS   A CE1 1 
ATOM   1108 N  NE2 . HIS   A 1 158 ? 110.595 18.942 16.009  1.00 44.09  ? 138 HIS   A NE2 1 
ATOM   1109 N  N   . PHE   A 1 159 ? 111.976 14.033 14.627  1.00 28.88  ? 139 PHE   A N   1 
ATOM   1110 C  CA  . PHE   A 1 159 ? 111.410 13.891 13.290  1.00 26.90  ? 139 PHE   A CA  1 
ATOM   1111 C  C   . PHE   A 1 159 ? 110.899 12.482 13.059  1.00 26.87  ? 139 PHE   A C   1 
ATOM   1112 O  O   . PHE   A 1 159 ? 111.522 11.519 13.505  1.00 26.83  ? 139 PHE   A O   1 
ATOM   1113 C  CB  . PHE   A 1 159 ? 112.431 14.286 12.223  1.00 25.75  ? 139 PHE   A CB  1 
ATOM   1114 C  CG  . PHE   A 1 159 ? 112.739 15.763 12.277  1.00 25.84  ? 139 PHE   A CG  1 
ATOM   1115 C  CD1 . PHE   A 1 159 ? 111.906 16.681 11.665  1.00 25.89  ? 139 PHE   A CD1 1 
ATOM   1116 C  CD2 . PHE   A 1 159 ? 113.842 16.232 12.969  1.00 25.88  ? 139 PHE   A CD2 1 
ATOM   1117 C  CE1 . PHE   A 1 159 ? 112.187 18.046 11.726  1.00 26.30  ? 139 PHE   A CE1 1 
ATOM   1118 C  CE2 . PHE   A 1 159 ? 114.113 17.591 13.041  1.00 25.89  ? 139 PHE   A CE2 1 
ATOM   1119 C  CZ  . PHE   A 1 159 ? 113.278 18.492 12.421  1.00 26.01  ? 139 PHE   A CZ  1 
ATOM   1120 N  N   . ALA   A 1 160 ? 109.770 12.362 12.346  1.00 26.38  ? 140 ALA   A N   1 
ATOM   1121 C  CA  . ALA   A 1 160 ? 109.164 11.067 12.050  1.00 27.15  ? 140 ALA   A CA  1 
ATOM   1122 C  C   . ALA   A 1 160 ? 109.904 10.310 10.942  1.00 26.28  ? 140 ALA   A C   1 
ATOM   1123 O  O   . ALA   A 1 160 ? 109.798 9.079  10.853  1.00 27.45  ? 140 ALA   A O   1 
ATOM   1124 C  CB  . ALA   A 1 160 ? 107.711 11.259 11.649  1.00 28.00  ? 140 ALA   A CB  1 
ATOM   1125 N  N   . GLY   A 1 161 ? 110.578 11.040 10.068  1.00 24.28  ? 141 GLY   A N   1 
ATOM   1126 C  CA  . GLY   A 1 161 ? 111.281 10.418 8.959   1.00 23.08  ? 141 GLY   A CA  1 
ATOM   1127 C  C   . GLY   A 1 161 ? 111.946 11.440 8.081   1.00 22.79  ? 141 GLY   A C   1 
ATOM   1128 O  O   . GLY   A 1 161 ? 111.665 12.646 8.172   1.00 22.63  ? 141 GLY   A O   1 
ATOM   1129 N  N   . MET   A 1 162 ? 112.823 10.959 7.227   1.00 21.64  ? 142 MET   A N   1 
ATOM   1130 C  CA  A MET   A 1 162 ? 113.555 11.809 6.326   0.50 21.28  ? 142 MET   A CA  1 
ATOM   1131 C  CA  B MET   A 1 162 ? 113.573 11.794 6.290   0.50 21.48  ? 142 MET   A CA  1 
ATOM   1132 C  C   . MET   A 1 162 ? 113.623 11.116 4.952   1.00 20.57  ? 142 MET   A C   1 
ATOM   1133 O  O   . MET   A 1 162 ? 113.911 9.923  4.893   1.00 20.43  ? 142 MET   A O   1 
ATOM   1134 C  CB  A MET   A 1 162 ? 114.943 12.016 6.964   0.50 22.27  ? 142 MET   A CB  1 
ATOM   1135 C  CB  B MET   A 1 162 ? 115.049 11.914 6.688   0.50 22.94  ? 142 MET   A CB  1 
ATOM   1136 C  CG  A MET   A 1 162 ? 115.921 12.832 6.195   0.50 23.57  ? 142 MET   A CG  1 
ATOM   1137 C  CG  B MET   A 1 162 ? 115.348 12.786 7.852   0.50 25.17  ? 142 MET   A CG  1 
ATOM   1138 S  SD  A MET   A 1 162 ? 117.454 13.020 7.178   0.50 24.15  ? 142 MET   A SD  1 
ATOM   1139 S  SD  B MET   A 1 162 ? 117.067 13.362 7.723   0.50 28.21  ? 142 MET   A SD  1 
ATOM   1140 C  CE  A MET   A 1 162 ? 117.995 11.312 7.322   0.50 24.97  ? 142 MET   A CE  1 
ATOM   1141 C  CE  B MET   A 1 162 ? 117.981 11.848 7.600   0.50 26.76  ? 142 MET   A CE  1 
ATOM   1142 N  N   . VAL   A 1 163 ? 113.391 11.862 3.887   1.00 19.25  ? 143 VAL   A N   1 
ATOM   1143 C  CA  . VAL   A 1 163 ? 113.485 11.373 2.519   1.00 19.52  ? 143 VAL   A CA  1 
ATOM   1144 C  C   . VAL   A 1 163 ? 114.669 12.122 1.905   1.00 19.15  ? 143 VAL   A C   1 
ATOM   1145 O  O   . VAL   A 1 163 ? 114.681 13.361 1.922   1.00 19.18  ? 143 VAL   A O   1 
ATOM   1146 C  CB  . VAL   A 1 163 ? 112.188 11.621 1.732   1.00 20.85  ? 143 VAL   A CB  1 
ATOM   1147 C  CG1 . VAL   A 1 163 ? 112.372 11.287 0.247   1.00 21.19  ? 143 VAL   A CG1 1 
ATOM   1148 C  CG2 . VAL   A 1 163 ? 111.031 10.842 2.343   1.00 21.87  ? 143 VAL   A CG2 1 
ATOM   1149 N  N   . LEU   A 1 164 ? 115.711 11.401 1.449   1.00 17.93  ? 144 LEU   A N   1 
ATOM   1150 C  CA  . LEU   A 1 164 ? 116.920 12.023 0.914   1.00 17.98  ? 144 LEU   A CA  1 
ATOM   1151 C  C   . LEU   A 1 164 ? 117.081 11.655 -0.548  1.00 17.83  ? 144 LEU   A C   1 
ATOM   1152 O  O   . LEU   A 1 164 ? 117.163 10.457 -0.896  1.00 18.21  ? 144 LEU   A O   1 
ATOM   1153 C  CB  . LEU   A 1 164 ? 118.140 11.527 1.704   1.00 18.73  ? 144 LEU   A CB  1 
ATOM   1154 C  CG  . LEU   A 1 164 ? 118.113 11.866 3.197   1.00 20.92  ? 144 LEU   A CG  1 
ATOM   1155 C  CD1 . LEU   A 1 164 ? 119.295 11.223 3.926   1.00 23.02  ? 144 LEU   A CD1 1 
ATOM   1156 C  CD2 . LEU   A 1 164 ? 118.112 13.377 3.400   1.00 21.29  ? 144 LEU   A CD2 1 
ATOM   1157 N  N   . ILE   A 1 165 ? 117.151 12.662 -1.393  1.00 17.28  ? 145 ILE   A N   1 
ATOM   1158 C  CA  . ILE   A 1 165 ? 117.344 12.436 -2.825  1.00 17.06  ? 145 ILE   A CA  1 
ATOM   1159 C  C   . ILE   A 1 165 ? 118.736 12.890 -3.158  1.00 17.64  ? 145 ILE   A C   1 
ATOM   1160 O  O   . ILE   A 1 165 ? 119.010 14.093 -3.100  1.00 19.06  ? 145 ILE   A O   1 
ATOM   1161 C  CB  . ILE   A 1 165 ? 116.321 13.222 -3.643  1.00 18.69  ? 145 ILE   A CB  1 
ATOM   1162 C  CG1 . ILE   A 1 165 ? 114.890 12.892 -3.186  1.00 19.90  ? 145 ILE   A CG1 1 
ATOM   1163 C  CG2 . ILE   A 1 165 ? 116.535 12.946 -5.144  1.00 19.23  ? 145 ILE   A CG2 1 
ATOM   1164 C  CD1 . ILE   A 1 165 ? 113.809 13.737 -3.939  1.00 20.59  ? 145 ILE   A CD1 1 
ATOM   1165 N  N   . SER   A 1 166 ? 119.660 11.941 -3.452  1.00 17.77  ? 146 SER   A N   1 
ATOM   1166 C  CA  A SER   A 1 166 ? 121.072 12.221 -3.749  0.37 17.48  ? 146 SER   A CA  1 
ATOM   1167 C  CA  B SER   A 1 166 ? 121.063 12.244 -3.782  0.63 18.64  ? 146 SER   A CA  1 
ATOM   1168 C  C   . SER   A 1 166 ? 121.673 13.227 -2.778  1.00 18.87  ? 146 SER   A C   1 
ATOM   1169 O  O   . SER   A 1 166 ? 122.144 14.290 -3.176  1.00 19.35  ? 146 SER   A O   1 
ATOM   1170 C  CB  A SER   A 1 166 ? 121.271 12.657 -5.199  0.37 16.57  ? 146 SER   A CB  1 
ATOM   1171 C  CB  B SER   A 1 166 ? 121.199 12.778 -5.213  0.63 21.38  ? 146 SER   A CB  1 
ATOM   1172 O  OG  A SER   A 1 166 ? 120.301 13.601 -5.614  0.37 14.59  ? 146 SER   A OG  1 
ATOM   1173 O  OG  B SER   A 1 166 ? 120.305 12.154 -6.115  0.63 25.98  ? 146 SER   A OG  1 
ATOM   1174 N  N   . PRO   A 1 167 ? 121.621 12.920 -1.460  1.00 18.51  ? 147 PRO   A N   1 
ATOM   1175 C  CA  . PRO   A 1 167 ? 122.146 13.878 -0.482  1.00 18.98  ? 147 PRO   A CA  1 
ATOM   1176 C  C   . PRO   A 1 167 ? 123.646 14.050 -0.580  1.00 20.33  ? 147 PRO   A C   1 
ATOM   1177 O  O   . PRO   A 1 167 ? 124.366 13.139 -0.998  1.00 20.94  ? 147 PRO   A O   1 
ATOM   1178 C  CB  . PRO   A 1 167 ? 121.743 13.258 0.875   1.00 18.88  ? 147 PRO   A CB  1 
ATOM   1179 C  CG  . PRO   A 1 167 ? 121.746 11.775 0.582   1.00 19.34  ? 147 PRO   A CG  1 
ATOM   1180 C  CD  . PRO   A 1 167 ? 121.094 11.706 -0.799  1.00 18.82  ? 147 PRO   A CD  1 
ATOM   1181 N  N   . LEU   A 1 168 ? 124.115 15.233 -0.180  1.00 20.76  ? 148 LEU   A N   1 
ATOM   1182 C  CA  . LEU   A 1 168 ? 125.549 15.501 -0.174  1.00 21.99  ? 148 LEU   A CA  1 
ATOM   1183 C  C   . LEU   A 1 168 ? 126.147 14.859 1.071   1.00 23.19  ? 148 LEU   A C   1 
ATOM   1184 O  O   . LEU   A 1 168 ? 125.995 15.379 2.181   1.00 23.40  ? 148 LEU   A O   1 
ATOM   1185 C  CB  . LEU   A 1 168 ? 125.820 17.017 -0.181  1.00 22.66  ? 148 LEU   A CB  1 
ATOM   1186 C  CG  . LEU   A 1 168 ? 127.291 17.429 -0.036  1.00 25.63  ? 148 LEU   A CG  1 
ATOM   1187 C  CD1 . LEU   A 1 168 ? 128.174 16.775 -1.123  1.00 26.84  ? 148 LEU   A CD1 1 
ATOM   1188 C  CD2 . LEU   A 1 168 ? 127.423 18.962 -0.014  1.00 27.17  ? 148 LEU   A CD2 1 
ATOM   1189 N  N   . VAL   A 1 169 ? 126.730 13.660 0.896   1.00 23.56  ? 149 VAL   A N   1 
ATOM   1190 C  CA  . VAL   A 1 169 ? 127.374 12.936 1.989   1.00 25.12  ? 149 VAL   A CA  1 
ATOM   1191 C  C   . VAL   A 1 169 ? 128.850 12.899 1.664   1.00 26.96  ? 149 VAL   A C   1 
ATOM   1192 O  O   . VAL   A 1 169 ? 129.670 13.258 2.500   1.00 28.01  ? 149 VAL   A O   1 
ATOM   1193 C  CB  . VAL   A 1 169 ? 126.783 11.521 2.186   1.00 25.87  ? 149 VAL   A CB  1 
ATOM   1194 C  CG1 . VAL   A 1 169 ? 127.544 10.772 3.281   1.00 26.81  ? 149 VAL   A CG1 1 
ATOM   1195 C  CG2 . VAL   A 1 169 ? 125.294 11.604 2.508   1.00 26.31  ? 149 VAL   A CG2 1 
ATOM   1196 N  N   . LEU   A 1 170 ? 129.197 12.470 0.431   1.00 27.79  ? 150 LEU   A N   1 
ATOM   1197 C  CA  . LEU   A 1 170 ? 130.571 12.514 -0.039  1.00 29.67  ? 150 LEU   A CA  1 
ATOM   1198 C  C   . LEU   A 1 170 ? 130.538 13.237 -1.378  1.00 30.94  ? 150 LEU   A C   1 
ATOM   1199 O  O   . LEU   A 1 170 ? 129.703 12.927 -2.229  1.00 31.12  ? 150 LEU   A O   1 
ATOM   1200 C  CB  . LEU   A 1 170 ? 131.153 11.116 -0.244  1.00 30.23  ? 150 LEU   A CB  1 
ATOM   1201 C  CG  . LEU   A 1 170 ? 131.394 10.279 1.003   1.00 32.91  ? 150 LEU   A CG  1 
ATOM   1202 C  CD1 . LEU   A 1 170 ? 131.935 8.928  0.609   1.00 33.36  ? 150 LEU   A CD1 1 
ATOM   1203 C  CD2 . LEU   A 1 170 ? 132.394 10.954 1.924   1.00 34.16  ? 150 LEU   A CD2 1 
ATOM   1204 N  N   . ALA   A 1 171 ? 131.409 14.215 -1.552  1.00 31.95  ? 151 ALA   A N   1 
ATOM   1205 C  CA  . ALA   A 1 171 ? 131.493 14.940 -2.819  1.00 34.28  ? 151 ALA   A CA  1 
ATOM   1206 C  C   . ALA   A 1 171 ? 132.206 14.050 -3.851  1.00 36.14  ? 151 ALA   A C   1 
ATOM   1207 O  O   . ALA   A 1 171 ? 132.886 13.100 -3.473  1.00 36.51  ? 151 ALA   A O   1 
ATOM   1208 C  CB  . ALA   A 1 171 ? 132.301 16.210 -2.606  1.00 34.98  ? 151 ALA   A CB  1 
ATOM   1209 N  N   . ASN   A 1 172 ? 132.129 14.385 -5.156  1.00 37.80  ? 152 ASN   A N   1 
ATOM   1210 C  CA  . ASN   A 1 172 ? 132.895 13.681 -6.192  1.00 40.60  ? 152 ASN   A CA  1 
ATOM   1211 C  C   . ASN   A 1 172 ? 134.395 13.825 -5.836  1.00 42.53  ? 152 ASN   A C   1 
ATOM   1212 O  O   . ASN   A 1 172 ? 134.821 14.906 -5.440  1.00 42.28  ? 152 ASN   A O   1 
ATOM   1213 C  CB  . ASN   A 1 172 ? 132.620 14.302 -7.565  1.00 43.14  ? 152 ASN   A CB  1 
ATOM   1214 C  CG  . ASN   A 1 172 ? 133.447 13.710 -8.691  1.00 47.88  ? 152 ASN   A CG  1 
ATOM   1215 O  OD1 . ASN   A 1 172 ? 134.647 13.994 -8.839  1.00 49.04  ? 152 ASN   A OD1 1 
ATOM   1216 N  ND2 . ASN   A 1 172 ? 132.820 12.872 -9.509  1.00 48.99  ? 152 ASN   A ND2 1 
ATOM   1217 N  N   . PRO   A 1 173 ? 135.139 12.716 -5.796  1.00 44.32  ? 153 PRO   A N   1 
ATOM   1218 C  CA  . PRO   A 1 173 ? 136.542 12.777 -5.349  1.00 46.20  ? 153 PRO   A CA  1 
ATOM   1219 C  C   . PRO   A 1 173 ? 137.405 13.868 -5.978  1.00 48.95  ? 153 PRO   A C   1 
ATOM   1220 O  O   . PRO   A 1 173 ? 138.226 14.464 -5.281  1.00 49.15  ? 153 PRO   A O   1 
ATOM   1221 C  CB  . PRO   A 1 173 ? 137.079 11.380 -5.672  1.00 46.41  ? 153 PRO   A CB  1 
ATOM   1222 C  CG  . PRO   A 1 173 ? 135.885 10.506 -5.657  1.00 46.58  ? 153 PRO   A CG  1 
ATOM   1223 C  CD  . PRO   A 1 173 ? 134.729 11.341 -6.139  1.00 44.30  ? 153 PRO   A CD  1 
ATOM   1224 N  N   . GLU   A 1 174 ? 137.226 14.139 -7.278  1.00 50.75  ? 154 GLU   A N   1 
ATOM   1225 C  CA  . GLU   A 1 174 ? 138.006 15.183 -7.949  1.00 52.63  ? 154 GLU   A CA  1 
ATOM   1226 C  C   . GLU   A 1 174 ? 137.622 16.567 -7.435  1.00 53.50  ? 154 GLU   A C   1 
ATOM   1227 O  O   . GLU   A 1 174 ? 138.492 17.420 -7.233  1.00 54.10  ? 154 GLU   A O   1 
ATOM   1228 C  CB  . GLU   A 1 174 ? 137.838 15.095 -9.471  1.00 56.36  ? 154 GLU   A CB  1 
ATOM   1229 C  CG  . GLU   A 1 174 ? 138.550 13.892 -10.065 1.00 63.84  ? 154 GLU   A CG  1 
ATOM   1230 C  CD  . GLU   A 1 174 ? 137.662 12.914 -10.808 1.00 73.48  ? 154 GLU   A CD  1 
ATOM   1231 O  OE1 . GLU   A 1 174 ? 138.212 12.044 -11.522 1.00 75.47  ? 154 GLU   A OE1 1 
ATOM   1232 O  OE2 . GLU   A 1 174 ? 136.419 13.017 -10.680 1.00 76.56  ? 154 GLU   A OE2 1 
ATOM   1233 N  N   . SER   A 1 175 ? 136.324 16.783 -7.207  1.00 53.18  ? 155 SER   A N   1 
ATOM   1234 C  CA  A SER   A 1 175 ? 135.838 18.060 -6.702  0.50 53.58  ? 155 SER   A CA  1 
ATOM   1235 C  CA  B SER   A 1 175 ? 135.800 18.045 -6.693  0.50 53.63  ? 155 SER   A CA  1 
ATOM   1236 C  C   . SER   A 1 175 ? 136.233 18.279 -5.243  1.00 53.72  ? 155 SER   A C   1 
ATOM   1237 O  O   . SER   A 1 175 ? 136.434 19.419 -4.837  1.00 54.01  ? 155 SER   A O   1 
ATOM   1238 C  CB  A SER   A 1 175 ? 134.327 18.164 -6.868  0.50 54.88  ? 155 SER   A CB  1 
ATOM   1239 C  CB  B SER   A 1 175 ? 134.278 18.055 -6.788  0.50 55.07  ? 155 SER   A CB  1 
ATOM   1240 O  OG  A SER   A 1 175 ? 133.963 18.021 -8.232  0.50 56.93  ? 155 SER   A OG  1 
ATOM   1241 O  OG  B SER   A 1 175 ? 133.698 19.192 -6.171  0.50 57.33  ? 155 SER   A OG  1 
ATOM   1242 N  N   . ALA   A 1 176 ? 136.349 17.203 -4.456  1.00 53.15  ? 156 ALA   A N   1 
ATOM   1243 C  CA  . ALA   A 1 176 ? 136.767 17.314 -3.062  1.00 53.39  ? 156 ALA   A CA  1 
ATOM   1244 C  C   . ALA   A 1 176 ? 138.236 17.786 -3.010  1.00 53.79  ? 156 ALA   A C   1 
ATOM   1245 O  O   . ALA   A 1 176 ? 138.583 18.616 -2.172  1.00 53.79  ? 156 ALA   A O   1 
ATOM   1246 C  CB  . ALA   A 1 176 ? 136.619 15.970 -2.363  1.00 53.36  ? 156 ALA   A CB  1 
ATOM   1247 N  N   . THR   A 1 177 ? 139.080 17.295 -3.935  1.00 53.85  ? 157 THR   A N   1 
ATOM   1248 C  CA  . THR   A 1 177 ? 140.481 17.694 -4.014  1.00 54.59  ? 157 THR   A CA  1 
ATOM   1249 C  C   . THR   A 1 177 ? 140.592 19.165 -4.423  1.00 55.54  ? 157 THR   A C   1 
ATOM   1250 O  O   . THR   A 1 177 ? 141.328 19.924 -3.793  1.00 55.89  ? 157 THR   A O   1 
ATOM   1251 C  CB  . THR   A 1 177 ? 141.234 16.779 -4.982  1.00 55.79  ? 157 THR   A CB  1 
ATOM   1252 O  OG1 . THR   A 1 177 ? 141.050 15.424 -4.576  1.00 56.44  ? 157 THR   A OG1 1 
ATOM   1253 C  CG2 . THR   A 1 177 ? 142.723 17.104 -5.050  1.00 56.44  ? 157 THR   A CG2 1 
ATOM   1254 N  N   . THR   A 1 178 ? 139.825 19.572 -5.444  1.00 55.85  ? 158 THR   A N   1 
ATOM   1255 C  CA  . THR   A 1 178 ? 139.789 20.942 -5.959  1.00 56.69  ? 158 THR   A CA  1 
ATOM   1256 C  C   . THR   A 1 178 ? 139.457 21.963 -4.865  1.00 56.71  ? 158 THR   A C   1 
ATOM   1257 O  O   . THR   A 1 178 ? 140.154 22.975 -4.727  1.00 56.56  ? 158 THR   A O   1 
ATOM   1258 C  CB  . THR   A 1 178 ? 138.794 21.017 -7.127  1.00 58.53  ? 158 THR   A CB  1 
ATOM   1259 O  OG1 . THR   A 1 178 ? 139.302 20.239 -8.215  1.00 59.91  ? 158 THR   A OG1 1 
ATOM   1260 C  CG2 . THR   A 1 178 ? 138.518 22.448 -7.576  1.00 58.90  ? 158 THR   A CG2 1 
ATOM   1261 N  N   . PHE   A 1 179 ? 138.414 21.685 -4.068  1.00 56.49  ? 159 PHE   A N   1 
ATOM   1262 C  CA  . PHE   A 1 179 ? 138.018 22.597 -3.004  1.00 56.82  ? 159 PHE   A CA  1 
ATOM   1263 C  C   . PHE   A 1 179 ? 138.925 22.545 -1.776  1.00 56.36  ? 159 PHE   A C   1 
ATOM   1264 O  O   . PHE   A 1 179 ? 139.044 23.557 -1.092  1.00 56.07  ? 159 PHE   A O   1 
ATOM   1265 C  CB  . PHE   A 1 179 ? 136.558 22.412 -2.621  1.00 57.15  ? 159 PHE   A CB  1 
ATOM   1266 C  CG  . PHE   A 1 179 ? 135.655 23.145 -3.575  1.00 58.47  ? 159 PHE   A CG  1 
ATOM   1267 C  CD1 . PHE   A 1 179 ? 135.026 22.477 -4.610  1.00 59.40  ? 159 PHE   A CD1 1 
ATOM   1268 C  CD2 . PHE   A 1 179 ? 135.492 24.518 -3.482  1.00 59.56  ? 159 PHE   A CD2 1 
ATOM   1269 C  CE1 . PHE   A 1 179 ? 134.192 23.154 -5.490  1.00 60.19  ? 159 PHE   A CE1 1 
ATOM   1270 C  CE2 . PHE   A 1 179 ? 134.663 25.195 -4.367  1.00 60.33  ? 159 PHE   A CE2 1 
ATOM   1271 C  CZ  . PHE   A 1 179 ? 134.007 24.504 -5.353  1.00 60.10  ? 159 PHE   A CZ  1 
ATOM   1272 N  N   . LYS   A 1 180 ? 139.578 21.402 -1.500  1.00 55.97  ? 160 LYS   A N   1 
ATOM   1273 C  CA  . LYS   A 1 180 ? 140.519 21.330 -0.378  1.00 56.43  ? 160 LYS   A CA  1 
ATOM   1274 C  C   . LYS   A 1 180 ? 141.762 22.192 -0.673  1.00 56.44  ? 160 LYS   A C   1 
ATOM   1275 O  O   . LYS   A 1 180 ? 142.294 22.841 0.229   1.00 56.31  ? 160 LYS   A O   1 
ATOM   1276 C  CB  . LYS   A 1 180 ? 140.916 19.877 -0.073  1.00 58.36  ? 160 LYS   A CB  1 
ATOM   1277 C  CG  . LYS   A 1 180 ? 139.880 19.133 0.760   1.00 62.59  ? 160 LYS   A CG  1 
ATOM   1278 C  CD  . LYS   A 1 180 ? 140.224 17.658 0.881   1.00 67.62  ? 160 LYS   A CD  1 
ATOM   1279 C  CE  . LYS   A 1 180 ? 139.030 16.820 1.267   1.00 71.68  ? 160 LYS   A CE  1 
ATOM   1280 N  NZ  . LYS   A 1 180 ? 139.336 15.367 1.181   1.00 73.88  ? 160 LYS   A NZ  1 
ATOM   1281 N  N   . VAL   A 1 181 ? 142.192 22.226 -1.946  1.00 56.37  ? 161 VAL   A N   1 
ATOM   1282 C  CA  . VAL   A 1 181 ? 143.324 23.029 -2.386  1.00 56.98  ? 161 VAL   A CA  1 
ATOM   1283 C  C   . VAL   A 1 181 ? 142.942 24.514 -2.367  1.00 57.15  ? 161 VAL   A C   1 
ATOM   1284 O  O   . VAL   A 1 181 ? 143.702 25.342 -1.853  1.00 56.94  ? 161 VAL   A O   1 
ATOM   1285 C  CB  . VAL   A 1 181 ? 143.811 22.554 -3.781  1.00 58.05  ? 161 VAL   A CB  1 
ATOM   1286 C  CG1 . VAL   A 1 181 ? 144.697 23.593 -4.456  1.00 58.87  ? 161 VAL   A CG1 1 
ATOM   1287 C  CG2 . VAL   A 1 181 ? 144.537 21.215 -3.677  1.00 58.54  ? 161 VAL   A CG2 1 
ATOM   1288 N  N   . LEU   A 1 182 ? 141.756 24.848 -2.897  1.00 57.20  ? 162 LEU   A N   1 
ATOM   1289 C  CA  . LEU   A 1 182 ? 141.306 26.235 -2.922  1.00 57.91  ? 162 LEU   A CA  1 
ATOM   1290 C  C   . LEU   A 1 182 ? 141.094 26.787 -1.519  1.00 58.57  ? 162 LEU   A C   1 
ATOM   1291 O  O   . LEU   A 1 182 ? 141.515 27.912 -1.241  1.00 58.74  ? 162 LEU   A O   1 
ATOM   1292 C  CB  . LEU   A 1 182 ? 140.049 26.396 -3.777  1.00 58.26  ? 162 LEU   A CB  1 
ATOM   1293 C  CG  . LEU   A 1 182 ? 140.273 26.324 -5.281  1.00 59.97  ? 162 LEU   A CG  1 
ATOM   1294 C  CD1 . LEU   A 1 182 ? 138.955 26.344 -6.024  1.00 60.84  ? 162 LEU   A CD1 1 
ATOM   1295 C  CD2 . LEU   A 1 182 ? 141.161 27.458 -5.759  1.00 60.59  ? 162 LEU   A CD2 1 
ATOM   1296 N  N   . ALA   A 1 183 ? 140.513 25.979 -0.617  1.00 58.80  ? 163 ALA   A N   1 
ATOM   1297 C  CA  . ALA   A 1 183 ? 140.294 26.373 0.780   1.00 59.81  ? 163 ALA   A CA  1 
ATOM   1298 C  C   . ALA   A 1 183 ? 141.615 26.661 1.478   1.00 60.52  ? 163 ALA   A C   1 
ATOM   1299 O  O   . ALA   A 1 183 ? 141.679 27.553 2.314   1.00 60.48  ? 163 ALA   A O   1 
ATOM   1300 C  CB  . ALA   A 1 183 ? 139.558 25.276 1.533   1.00 60.10  ? 163 ALA   A CB  1 
ATOM   1301 N  N   . ALA   A 1 184 ? 142.661 25.899 1.153   1.00 60.87  ? 164 ALA   A N   1 
ATOM   1302 C  CA  . ALA   A 1 184 ? 143.982 26.103 1.731   1.00 61.72  ? 164 ALA   A CA  1 
ATOM   1303 C  C   . ALA   A 1 184 ? 144.646 27.389 1.189   1.00 62.63  ? 164 ALA   A C   1 
ATOM   1304 O  O   . ALA   A 1 184 ? 145.433 28.004 1.897   1.00 62.90  ? 164 ALA   A O   1 
ATOM   1305 C  CB  . ALA   A 1 184 ? 144.852 24.889 1.471   1.00 61.75  ? 164 ALA   A CB  1 
ATOM   1306 N  N   . LYS   A 1 185 ? 144.297 27.823 -0.036  1.00 63.02  ? 165 LYS   A N   1 
ATOM   1307 C  CA  . LYS   A 1 185 ? 144.833 29.064 -0.597  1.00 63.84  ? 165 LYS   A CA  1 
ATOM   1308 C  C   . LYS   A 1 185 ? 144.160 30.285 0.056   1.00 64.61  ? 165 LYS   A C   1 
ATOM   1309 O  O   . LYS   A 1 185 ? 144.839 31.262 0.362   1.00 64.56  ? 165 LYS   A O   1 
ATOM   1310 C  CB  . LYS   A 1 185 ? 144.641 29.124 -2.127  1.00 65.59  ? 165 LYS   A CB  1 
ATOM   1311 C  CG  . LYS   A 1 185 ? 145.111 27.892 -2.894  1.00 69.42  ? 165 LYS   A CG  1 
ATOM   1312 C  CD  . LYS   A 1 185 ? 146.585 27.571 -2.678  1.00 73.49  ? 165 LYS   A CD  1 
ATOM   1313 C  CE  . LYS   A 1 185 ? 146.997 26.242 -3.273  1.00 76.68  ? 165 LYS   A CE  1 
ATOM   1314 N  NZ  . LYS   A 1 185 ? 147.189 26.316 -4.746  1.00 78.18  ? 165 LYS   A NZ  1 
ATOM   1315 N  N   . VAL   A 1 186 ? 142.827 30.240 0.255   1.00 65.08  ? 166 VAL   A N   1 
ATOM   1316 C  CA  . VAL   A 1 186 ? 142.124 31.359 0.889   1.00 65.97  ? 166 VAL   A CA  1 
ATOM   1317 C  C   . VAL   A 1 186 ? 142.321 31.363 2.412   1.00 66.40  ? 166 VAL   A C   1 
ATOM   1318 O  O   . VAL   A 1 186 ? 142.324 32.433 3.018   1.00 66.66  ? 166 VAL   A O   1 
ATOM   1319 C  CB  . VAL   A 1 186 ? 140.642 31.457 0.489   1.00 67.18  ? 166 VAL   A CB  1 
ATOM   1320 C  CG1 . VAL   A 1 186 ? 140.490 31.450 -1.026  1.00 67.94  ? 166 VAL   A CG1 1 
ATOM   1321 C  CG2 . VAL   A 1 186 ? 139.836 30.336 1.118   1.00 67.64  ? 166 VAL   A CG2 1 
ATOM   1322 N  N   . LEU   A 1 187 ? 142.529 30.182 3.026   1.00 66.15  ? 167 LEU   A N   1 
ATOM   1323 C  CA  . LEU   A 1 187 ? 142.822 30.077 4.462   1.00 66.02  ? 167 LEU   A CA  1 
ATOM   1324 C  C   . LEU   A 1 187 ? 144.174 30.731 4.770   1.00 64.31  ? 167 LEU   A C   1 
ATOM   1325 O  O   . LEU   A 1 187 ? 144.359 31.283 5.851   1.00 65.12  ? 167 LEU   A O   1 
ATOM   1326 C  CB  . LEU   A 1 187 ? 142.851 28.596 4.901   1.00 67.23  ? 167 LEU   A CB  1 
ATOM   1327 C  CG  . LEU   A 1 187 ? 143.135 28.310 6.381   1.00 69.79  ? 167 LEU   A CG  1 
ATOM   1328 C  CD1 . LEU   A 1 187 ? 141.996 28.803 7.266   1.00 70.68  ? 167 LEU   A CD1 1 
ATOM   1329 C  CD2 . LEU   A 1 187 ? 143.391 26.828 6.615   1.00 70.67  ? 167 LEU   A CD2 1 
ATOM   1330 N  N   . ASN   A 1 188 ? 145.112 30.690 3.813   1.00 61.99  ? 168 ASN   A N   1 
ATOM   1331 C  CA  . ASN   A 1 188 ? 146.440 31.260 3.961   1.00 59.79  ? 168 ASN   A CA  1 
ATOM   1332 C  C   . ASN   A 1 188 ? 146.575 32.694 3.445   1.00 57.16  ? 168 ASN   A C   1 
ATOM   1333 O  O   . ASN   A 1 188 ? 147.495 33.398 3.851   1.00 57.86  ? 168 ASN   A O   1 
ATOM   1334 C  CB  . ASN   A 1 188 ? 147.453 30.352 3.278   1.00 61.17  ? 168 ASN   A CB  1 
ATOM   1335 C  CG  . ASN   A 1 188 ? 147.882 29.208 4.157   1.00 64.78  ? 168 ASN   A CG  1 
ATOM   1336 O  OD1 . ASN   A 1 188 ? 148.934 29.261 4.803   1.00 66.41  ? 168 ASN   A OD1 1 
ATOM   1337 N  ND2 . ASN   A 1 188 ? 147.070 28.165 4.222   1.00 65.33  ? 168 ASN   A ND2 1 
ATOM   1338 N  N   . SER   A 1 189 ? 145.701 33.118 2.530   1.00 54.26  ? 169 SER   A N   1 
ATOM   1339 C  CA  . SER   A 1 189 ? 145.774 34.472 1.963   1.00 51.65  ? 169 SER   A CA  1 
ATOM   1340 C  C   . SER   A 1 189 ? 144.387 35.187 1.941   1.00 49.82  ? 169 SER   A C   1 
ATOM   1341 O  O   . SER   A 1 189 ? 143.414 34.620 2.419   1.00 49.66  ? 169 SER   A O   1 
ATOM   1342 C  CB  . SER   A 1 189 ? 146.427 34.426 0.577   1.00 51.25  ? 169 SER   A CB  1 
ATOM   1343 O  OG  . SER   A 1 189 ? 147.845 34.326 0.638   1.00 50.26  ? 169 SER   A OG  1 
ATOM   1344 N  N   . VAL   A 1 190 ? 144.303 36.445 1.461   1.00 48.38  ? 170 VAL   A N   1 
ATOM   1345 C  CA  . VAL   A 1 190 ? 143.030 37.164 1.406   1.00 47.53  ? 170 VAL   A CA  1 
ATOM   1346 C  C   . VAL   A 1 190 ? 142.596 37.252 -0.046  1.00 46.29  ? 170 VAL   A C   1 
ATOM   1347 O  O   . VAL   A 1 190 ? 143.141 38.058 -0.785  1.00 45.81  ? 170 VAL   A O   1 
ATOM   1348 C  CB  . VAL   A 1 190 ? 143.119 38.572 2.042   1.00 48.34  ? 170 VAL   A CB  1 
ATOM   1349 C  CG1 . VAL   A 1 190 ? 141.759 39.271 2.023   1.00 49.04  ? 170 VAL   A CG1 1 
ATOM   1350 C  CG2 . VAL   A 1 190 ? 143.677 38.504 3.458   1.00 48.96  ? 170 VAL   A CG2 1 
ATOM   1351 N  N   . LEU   A 1 191 ? 141.688 36.377 -0.485  1.00 45.46  ? 171 LEU   A N   1 
ATOM   1352 C  CA  . LEU   A 1 191 ? 141.208 36.375 -1.867  1.00 45.45  ? 171 LEU   A CA  1 
ATOM   1353 C  C   . LEU   A 1 191 ? 139.678 36.245 -1.857  1.00 46.84  ? 171 LEU   A C   1 
ATOM   1354 O  O   . LEU   A 1 191 ? 139.149 35.148 -2.003  1.00 46.60  ? 171 LEU   A O   1 
ATOM   1355 C  CB  . LEU   A 1 191 ? 141.854 35.221 -2.656  1.00 44.72  ? 171 LEU   A CB  1 
ATOM   1356 C  CG  . LEU   A 1 191 ? 143.378 35.340 -2.844  1.00 45.71  ? 171 LEU   A CG  1 
ATOM   1357 C  CD1 . LEU   A 1 191 ? 143.995 33.999 -3.240  1.00 46.40  ? 171 LEU   A CD1 1 
ATOM   1358 C  CD2 . LEU   A 1 191 ? 143.720 36.426 -3.845  1.00 45.98  ? 171 LEU   A CD2 1 
ATOM   1359 N  N   . PRO   A 1 192 ? 138.961 37.370 -1.675  1.00 47.88  ? 172 PRO   A N   1 
ATOM   1360 C  CA  . PRO   A 1 192 ? 137.493 37.301 -1.551  1.00 48.66  ? 172 PRO   A CA  1 
ATOM   1361 C  C   . PRO   A 1 192 ? 136.707 36.905 -2.803  1.00 49.73  ? 172 PRO   A C   1 
ATOM   1362 O  O   . PRO   A 1 192 ? 135.591 36.399 -2.675  1.00 50.30  ? 172 PRO   A O   1 
ATOM   1363 C  CB  . PRO   A 1 192 ? 137.110 38.713 -1.084  1.00 49.24  ? 172 PRO   A CB  1 
ATOM   1364 C  CG  . PRO   A 1 192 ? 138.233 39.586 -1.527  1.00 49.41  ? 172 PRO   A CG  1 
ATOM   1365 C  CD  . PRO   A 1 192 ? 139.468 38.739 -1.444  1.00 47.55  ? 172 PRO   A CD  1 
ATOM   1366 N  N   . ASN   A 1 193 ? 137.259 37.137 -3.998  1.00 49.99  ? 173 ASN   A N   1 
ATOM   1367 C  CA  . ASN   A 1 193 ? 136.542 36.817 -5.233  1.00 50.81  ? 173 ASN   A CA  1 
ATOM   1368 C  C   . ASN   A 1 193 ? 136.877 35.443 -5.826  1.00 50.04  ? 173 ASN   A C   1 
ATOM   1369 O  O   . ASN   A 1 193 ? 136.310 35.087 -6.855  1.00 50.61  ? 173 ASN   A O   1 
ATOM   1370 C  CB  . ASN   A 1 193 ? 136.749 37.922 -6.266  1.00 53.06  ? 173 ASN   A CB  1 
ATOM   1371 C  CG  . ASN   A 1 193 ? 136.234 39.263 -5.792  1.00 58.21  ? 173 ASN   A CG  1 
ATOM   1372 O  OD1 . ASN   A 1 193 ? 135.107 39.377 -5.285  1.00 60.09  ? 173 ASN   A OD1 1 
ATOM   1373 N  ND2 . ASN   A 1 193 ? 137.051 40.308 -5.931  1.00 58.91  ? 173 ASN   A ND2 1 
ATOM   1374 N  N   . LEU   A 1 194 ? 137.788 34.679 -5.200  1.00 48.58  ? 174 LEU   A N   1 
ATOM   1375 C  CA  . LEU   A 1 194 ? 138.199 33.382 -5.725  1.00 47.97  ? 174 LEU   A CA  1 
ATOM   1376 C  C   . LEU   A 1 194 ? 137.025 32.420 -5.838  1.00 46.88  ? 174 LEU   A C   1 
ATOM   1377 O  O   . LEU   A 1 194 ? 136.247 32.270 -4.900  1.00 46.17  ? 174 LEU   A O   1 
ATOM   1378 C  CB  . LEU   A 1 194 ? 139.332 32.770 -4.891  1.00 48.58  ? 174 LEU   A CB  1 
ATOM   1379 C  CG  . LEU   A 1 194 ? 140.093 31.618 -5.558  1.00 51.03  ? 174 LEU   A CG  1 
ATOM   1380 C  CD1 . LEU   A 1 194 ? 140.786 32.080 -6.830  1.00 52.17  ? 174 LEU   A CD1 1 
ATOM   1381 C  CD2 . LEU   A 1 194 ? 141.108 31.004 -4.607  1.00 51.40  ? 174 LEU   A CD2 1 
ATOM   1382 N  N   . SER   A 1 195 ? 136.882 31.803 -7.008  1.00 46.49  ? 175 SER   A N   1 
ATOM   1383 C  CA  . SER   A 1 195 ? 135.790 30.870 -7.264  1.00 46.59  ? 175 SER   A CA  1 
ATOM   1384 C  C   . SER   A 1 195 ? 136.251 29.728 -8.152  1.00 46.14  ? 175 SER   A C   1 
ATOM   1385 O  O   . SER   A 1 195 ? 137.187 29.880 -8.932  1.00 46.41  ? 175 SER   A O   1 
ATOM   1386 C  CB  . SER   A 1 195 ? 134.643 31.584 -7.979  1.00 48.40  ? 175 SER   A CB  1 
ATOM   1387 O  OG  . SER   A 1 195 ? 134.149 32.702 -7.264  1.00 51.96  ? 175 SER   A OG  1 
ATOM   1388 N  N   . SER   A 1 196 ? 135.562 28.593 -8.065  1.00 45.61  ? 176 SER   A N   1 
ATOM   1389 C  CA  . SER   A 1 196 ? 135.821 27.474 -8.959  1.00 45.41  ? 176 SER   A CA  1 
ATOM   1390 C  C   . SER   A 1 196 ? 134.921 27.695 -10.217 1.00 44.12  ? 176 SER   A C   1 
ATOM   1391 O  O   . SER   A 1 196 ? 134.261 28.737 -10.348 1.00 43.42  ? 176 SER   A O   1 
ATOM   1392 C  CB  . SER   A 1 196 ? 135.477 26.164 -8.255  1.00 47.70  ? 176 SER   A CB  1 
ATOM   1393 O  OG  . SER   A 1 196 ? 134.067 26.026 -8.152  1.00 51.88  ? 176 SER   A OG  1 
ATOM   1394 N  N   . GLY   A 1 197 ? 134.920 26.737 -11.135 1.00 43.36  ? 177 GLY   A N   1 
ATOM   1395 C  CA  . GLY   A 1 197 ? 134.060 26.813 -12.307 1.00 43.37  ? 177 GLY   A CA  1 
ATOM   1396 C  C   . GLY   A 1 197 ? 132.632 26.457 -11.929 1.00 42.99  ? 177 GLY   A C   1 
ATOM   1397 O  O   . GLY   A 1 197 ? 132.380 25.889 -10.858 1.00 42.65  ? 177 GLY   A O   1 
ATOM   1398 N  N   A PRO   A 1 198 ? 131.661 26.794 -12.789 0.50 43.09  ? 178 PRO   A N   1 
ATOM   1399 N  N   B PRO   A 1 198 ? 131.661 26.794 -12.789 0.50 43.09  ? 178 PRO   A N   1 
ATOM   1400 C  CA  A PRO   A 1 198 ? 130.261 26.463 -12.473 0.50 43.42  ? 178 PRO   A CA  1 
ATOM   1401 C  CA  B PRO   A 1 198 ? 130.261 26.463 -12.473 0.50 43.42  ? 178 PRO   A CA  1 
ATOM   1402 C  C   A PRO   A 1 198 ? 129.957 24.967 -12.563 0.50 44.07  ? 178 PRO   A C   1 
ATOM   1403 C  C   B PRO   A 1 198 ? 129.957 24.967 -12.563 0.50 44.07  ? 178 PRO   A C   1 
ATOM   1404 O  O   A PRO   A 1 198 ? 130.721 24.207 -13.157 0.50 44.53  ? 178 PRO   A O   1 
ATOM   1405 O  O   B PRO   A 1 198 ? 130.721 24.207 -13.157 0.50 44.53  ? 178 PRO   A O   1 
ATOM   1406 C  CB  A PRO   A 1 198 ? 129.471 27.245 -13.523 0.50 44.15  ? 178 PRO   A CB  1 
ATOM   1407 C  CB  B PRO   A 1 198 ? 129.471 27.245 -13.523 0.50 44.15  ? 178 PRO   A CB  1 
ATOM   1408 C  CG  A PRO   A 1 198 ? 130.405 27.380 -14.672 0.50 44.58  ? 178 PRO   A CG  1 
ATOM   1409 C  CG  B PRO   A 1 198 ? 130.405 27.380 -14.672 0.50 44.58  ? 178 PRO   A CG  1 
ATOM   1410 C  CD  A PRO   A 1 198 ? 131.787 27.484 -14.088 0.50 42.79  ? 178 PRO   A CD  1 
ATOM   1411 C  CD  B PRO   A 1 198 ? 131.787 27.484 -14.088 0.50 42.79  ? 178 PRO   A CD  1 
ATOM   1412 N  N   . ILE   A 1 199 ? 128.831 24.543 -11.981 1.00 44.12  ? 179 ILE   A N   1 
ATOM   1413 C  CA  . ILE   A 1 199 ? 128.412 23.139 -12.035 1.00 44.76  ? 179 ILE   A CA  1 
ATOM   1414 C  C   . ILE   A 1 199 ? 128.007 22.843 -13.481 1.00 44.50  ? 179 ILE   A C   1 
ATOM   1415 O  O   . ILE   A 1 199 ? 127.248 23.622 -14.064 1.00 45.49  ? 179 ILE   A O   1 
ATOM   1416 C  CB  . ILE   A 1 199 ? 127.239 22.923 -11.045 1.00 45.88  ? 179 ILE   A CB  1 
ATOM   1417 C  CG1 . ILE   A 1 199 ? 127.745 22.967 -9.588  1.00 47.16  ? 179 ILE   A CG1 1 
ATOM   1418 C  CG2 . ILE   A 1 199 ? 126.483 21.618 -11.331 1.00 46.37  ? 179 ILE   A CG2 1 
ATOM   1419 C  CD1 . ILE   A 1 199 ? 126.750 23.477 -8.598  1.00 48.60  ? 179 ILE   A CD1 1 
ATOM   1420 N  N   . ASP   A 1 200 ? 128.603 21.798 -14.094 1.00 42.71  ? 180 ASP   A N   1 
ATOM   1421 C  CA  . ASP   A 1 200 ? 128.322 21.400 -15.478 1.00 40.91  ? 180 ASP   A CA  1 
ATOM   1422 C  C   . ASP   A 1 200 ? 126.862 20.911 -15.513 1.00 38.02  ? 180 ASP   A C   1 
ATOM   1423 O  O   . ASP   A 1 200 ? 126.565 19.865 -14.954 1.00 38.35  ? 180 ASP   A O   1 
ATOM   1424 C  CB  . ASP   A 1 200 ? 129.298 20.285 -15.882 1.00 43.39  ? 180 ASP   A CB  1 
ATOM   1425 C  CG  . ASP   A 1 200 ? 129.163 19.747 -17.292 1.00 49.29  ? 180 ASP   A CG  1 
ATOM   1426 O  OD1 . ASP   A 1 200 ? 128.359 20.307 -18.070 1.00 50.87  ? 180 ASP   A OD1 1 
ATOM   1427 O  OD2 . ASP   A 1 200 ? 129.859 18.757 -17.617 1.00 51.55  ? 180 ASP   A OD2 1 
ATOM   1428 N  N   . SER   A 1 201 ? 125.956 21.677 -16.148 1.00 34.52  ? 181 SER   A N   1 
ATOM   1429 C  CA  A SER   A 1 201 ? 124.535 21.334 -16.183 0.50 32.71  ? 181 SER   A CA  1 
ATOM   1430 C  CA  B SER   A 1 201 ? 124.530 21.342 -16.207 0.50 33.59  ? 181 SER   A CA  1 
ATOM   1431 C  C   . SER   A 1 201 ? 124.242 19.985 -16.846 1.00 31.74  ? 181 SER   A C   1 
ATOM   1432 O  O   . SER   A 1 201 ? 123.253 19.350 -16.491 1.00 30.18  ? 181 SER   A O   1 
ATOM   1433 C  CB  A SER   A 1 201 ? 123.732 22.439 -16.862 0.50 32.32  ? 181 SER   A CB  1 
ATOM   1434 C  CB  B SER   A 1 201 ? 123.758 22.423 -16.955 0.50 35.74  ? 181 SER   A CB  1 
ATOM   1435 O  OG  A SER   A 1 201 ? 124.150 22.593 -18.207 0.50 31.90  ? 181 SER   A OG  1 
ATOM   1436 O  OG  B SER   A 1 201 ? 124.036 23.704 -16.420 0.50 39.60  ? 181 SER   A OG  1 
ATOM   1437 N  N   . SER   A 1 202 ? 125.087 19.546 -17.793 1.00 31.02  ? 182 SER   A N   1 
ATOM   1438 C  CA  . SER   A 1 202 ? 124.852 18.261 -18.471 1.00 31.25  ? 182 SER   A CA  1 
ATOM   1439 C  C   . SER   A 1 202 ? 124.891 17.044 -17.544 1.00 29.97  ? 182 SER   A C   1 
ATOM   1440 O  O   . SER   A 1 202 ? 124.280 16.015 -17.865 1.00 30.68  ? 182 SER   A O   1 
ATOM   1441 C  CB  . SER   A 1 202 ? 125.800 18.064 -19.650 1.00 34.61  ? 182 SER   A CB  1 
ATOM   1442 O  OG  . SER   A 1 202 ? 127.131 17.854 -19.206 1.00 39.55  ? 182 SER   A OG  1 
ATOM   1443 N  N   . VAL   A 1 203 ? 125.579 17.149 -16.387 1.00 28.09  ? 183 VAL   A N   1 
ATOM   1444 C  CA  . VAL   A 1 203 ? 125.629 16.016 -15.444 1.00 27.04  ? 183 VAL   A CA  1 
ATOM   1445 C  C   . VAL   A 1 203 ? 124.457 15.998 -14.463 1.00 25.01  ? 183 VAL   A C   1 
ATOM   1446 O  O   . VAL   A 1 203 ? 124.390 15.099 -13.616 1.00 25.30  ? 183 VAL   A O   1 
ATOM   1447 C  CB  . VAL   A 1 203 ? 126.986 15.904 -14.692 1.00 28.46  ? 183 VAL   A CB  1 
ATOM   1448 C  CG1 . VAL   A 1 203 ? 128.147 15.991 -15.676 1.00 29.76  ? 183 VAL   A CG1 1 
ATOM   1449 C  CG2 . VAL   A 1 203 ? 127.117 16.985 -13.625 1.00 29.20  ? 183 VAL   A CG2 1 
ATOM   1450 N  N   . LEU   A 1 204 ? 123.534 16.976 -14.551 1.00 23.02  ? 184 LEU   A N   1 
ATOM   1451 C  CA  . LEU   A 1 204 ? 122.407 17.015 -13.636 1.00 22.51  ? 184 LEU   A CA  1 
ATOM   1452 C  C   . LEU   A 1 204 ? 121.402 15.919 -13.883 1.00 22.31  ? 184 LEU   A C   1 
ATOM   1453 O  O   . LEU   A 1 204 ? 120.833 15.387 -12.932 1.00 21.74  ? 184 LEU   A O   1 
ATOM   1454 C  CB  . LEU   A 1 204 ? 121.698 18.363 -13.714 1.00 22.05  ? 184 LEU   A CB  1 
ATOM   1455 C  CG  . LEU   A 1 204 ? 122.540 19.528 -13.196 1.00 24.28  ? 184 LEU   A CG  1 
ATOM   1456 C  CD1 . LEU   A 1 204 ? 121.832 20.852 -13.446 1.00 25.94  ? 184 LEU   A CD1 1 
ATOM   1457 C  CD2 . LEU   A 1 204 ? 122.778 19.385 -11.691 1.00 25.15  ? 184 LEU   A CD2 1 
ATOM   1458 N  N   . SER   A 1 205 ? 121.118 15.639 -15.157 1.00 21.87  ? 185 SER   A N   1 
ATOM   1459 C  CA  . SER   A 1 205 ? 120.068 14.712 -15.494 1.00 22.02  ? 185 SER   A CA  1 
ATOM   1460 C  C   . SER   A 1 205 ? 120.215 14.257 -16.923 1.00 22.94  ? 185 SER   A C   1 
ATOM   1461 O  O   . SER   A 1 205 ? 120.625 15.043 -17.785 1.00 23.63  ? 185 SER   A O   1 
ATOM   1462 C  CB  . SER   A 1 205 ? 118.724 15.422 -15.360 1.00 22.18  ? 185 SER   A CB  1 
ATOM   1463 O  OG  . SER   A 1 205 ? 117.655 14.616 -15.821 1.00 23.48  ? 185 SER   A OG  1 
ATOM   1464 N  N   . ARG   A 1 206 ? 119.848 13.005 -17.184 1.00 23.05  ? 186 ARG   A N   1 
ATOM   1465 C  CA  . ARG   A 1 206 ? 119.824 12.511 -18.566 1.00 23.34  ? 186 ARG   A CA  1 
ATOM   1466 C  C   . ARG   A 1 206 ? 118.638 13.120 -19.349 1.00 24.90  ? 186 ARG   A C   1 
ATOM   1467 O  O   . ARG   A 1 206 ? 118.624 13.051 -20.592 1.00 25.94  ? 186 ARG   A O   1 
ATOM   1468 C  CB  . ARG   A 1 206 ? 119.728 10.982 -18.571 1.00 23.34  ? 186 ARG   A CB  1 
ATOM   1469 C  CG  . ARG   A 1 206 ? 121.018 10.305 -18.107 1.00 25.43  ? 186 ARG   A CG  1 
ATOM   1470 C  CD  . ARG   A 1 206 ? 120.840 8.786  -17.969 1.00 24.89  ? 186 ARG   A CD  1 
ATOM   1471 N  NE  . ARG   A 1 206 ? 119.791 8.489  -16.990 1.00 25.09  ? 186 ARG   A NE  1 
ATOM   1472 C  CZ  . ARG   A 1 206 ? 119.271 7.286  -16.785 1.00 24.52  ? 186 ARG   A CZ  1 
ATOM   1473 N  NH1 . ARG   A 1 206 ? 119.721 6.233  -17.466 1.00 25.01  ? 186 ARG   A NH1 1 
ATOM   1474 N  NH2 . ARG   A 1 206 ? 118.301 7.122  -15.896 1.00 24.10  ? 186 ARG   A NH2 1 
ATOM   1475 N  N   . ASN   A 1 207 ? 117.655 13.698 -18.636 1.00 24.44  ? 187 ASN   A N   1 
ATOM   1476 C  CA  . ASN   A 1 207 ? 116.503 14.348 -19.219 1.00 24.06  ? 187 ASN   A CA  1 
ATOM   1477 C  C   . ASN   A 1 207 ? 116.955 15.730 -19.704 1.00 24.54  ? 187 ASN   A C   1 
ATOM   1478 O  O   . ASN   A 1 207 ? 117.121 16.671 -18.919 1.00 24.83  ? 187 ASN   A O   1 
ATOM   1479 C  CB  . ASN   A 1 207 ? 115.370 14.417 -18.214 1.00 25.41  ? 187 ASN   A CB  1 
ATOM   1480 C  CG  . ASN   A 1 207 ? 114.079 14.957 -18.775 1.00 27.86  ? 187 ASN   A CG  1 
ATOM   1481 O  OD1 . ASN   A 1 207 ? 114.064 15.834 -19.642 1.00 29.47  ? 187 ASN   A OD1 1 
ATOM   1482 N  ND2 . ASN   A 1 207 ? 112.972 14.481 -18.241 1.00 28.32  ? 187 ASN   A ND2 1 
ATOM   1483 N  N   . LYS   A 1 208 ? 117.199 15.823 -21.017 1.00 24.93  ? 188 LYS   A N   1 
ATOM   1484 C  CA  . LYS   A 1 208 ? 117.670 17.073 -21.613 1.00 25.60  ? 188 LYS   A CA  1 
ATOM   1485 C  C   . LYS   A 1 208 ? 116.726 18.244 -21.411 1.00 26.08  ? 188 LYS   A C   1 
ATOM   1486 O  O   . LYS   A 1 208 ? 117.201 19.373 -21.275 1.00 26.94  ? 188 LYS   A O   1 
ATOM   1487 C  CB  . LYS   A 1 208 ? 118.003 16.894 -23.100 1.00 28.29  ? 188 LYS   A CB  1 
ATOM   1488 C  CG  . LYS   A 1 208 ? 119.089 15.848 -23.347 1.00 33.68  ? 188 LYS   A CG  1 
ATOM   1489 C  CD  . LYS   A 1 208 ? 119.539 15.840 -24.798 1.00 42.74  ? 188 LYS   A CD  1 
ATOM   1490 C  CE  . LYS   A 1 208 ? 120.705 14.905 -25.024 1.00 48.52  ? 188 LYS   A CE  1 
ATOM   1491 N  NZ  . LYS   A 1 208 ? 121.109 14.877 -26.456 1.00 52.64  ? 188 LYS   A NZ  1 
ATOM   1492 N  N   . THR   A 1 209 ? 115.406 17.999 -21.372 1.00 25.59  ? 189 THR   A N   1 
ATOM   1493 C  CA  . THR   A 1 209 ? 114.457 19.103 -21.152 1.00 25.90  ? 189 THR   A CA  1 
ATOM   1494 C  C   . THR   A 1 209 ? 114.681 19.717 -19.742 1.00 23.74  ? 189 THR   A C   1 
ATOM   1495 O  O   . THR   A 1 209 ? 114.700 20.925 -19.582 1.00 23.32  ? 189 THR   A O   1 
ATOM   1496 C  CB  . THR   A 1 209 ? 113.019 18.612 -21.314 1.00 29.28  ? 189 THR   A CB  1 
ATOM   1497 O  OG1 . THR   A 1 209 ? 112.890 18.051 -22.618 1.00 33.28  ? 189 THR   A OG1 1 
ATOM   1498 C  CG2 . THR   A 1 209 ? 111.999 19.733 -21.169 1.00 29.51  ? 189 THR   A CG2 1 
ATOM   1499 N  N   . GLU   A 1 210 ? 114.901 18.864 -18.730 1.00 23.11  ? 190 GLU   A N   1 
ATOM   1500 C  CA  . GLU   A 1 210 ? 115.146 19.337 -17.375 1.00 22.10  ? 190 GLU   A CA  1 
ATOM   1501 C  C   . GLU   A 1 210 ? 116.472 20.091 -17.287 1.00 22.04  ? 190 GLU   A C   1 
ATOM   1502 O  O   . GLU   A 1 210 ? 116.555 21.080 -16.558 1.00 22.64  ? 190 GLU   A O   1 
ATOM   1503 C  CB  . GLU   A 1 210 ? 115.061 18.155 -16.393 1.00 23.30  ? 190 GLU   A CB  1 
ATOM   1504 C  CG  . GLU   A 1 210 ? 113.639 17.619 -16.300 1.00 25.33  ? 190 GLU   A CG  1 
ATOM   1505 C  CD  . GLU   A 1 210 ? 112.634 18.554 -15.644 1.00 31.45  ? 190 GLU   A CD  1 
ATOM   1506 O  OE1 . GLU   A 1 210 ? 113.054 19.546 -15.011 1.00 29.12  ? 190 GLU   A OE1 1 
ATOM   1507 O  OE2 . GLU   A 1 210 ? 111.416 18.288 -15.764 1.00 38.72  ? 190 GLU   A OE2 1 
ATOM   1508 N  N   . VAL   A 1 211 ? 117.497 19.670 -18.062 1.00 22.90  ? 191 VAL   A N   1 
ATOM   1509 C  CA  . VAL   A 1 211 ? 118.756 20.435 -18.103 1.00 23.62  ? 191 VAL   A CA  1 
ATOM   1510 C  C   . VAL   A 1 211 ? 118.488 21.836 -18.694 1.00 23.97  ? 191 VAL   A C   1 
ATOM   1511 O  O   . VAL   A 1 211 ? 118.941 22.864 -18.160 1.00 24.90  ? 191 VAL   A O   1 
ATOM   1512 C  CB  . VAL   A 1 211 ? 119.870 19.705 -18.872 1.00 24.34  ? 191 VAL   A CB  1 
ATOM   1513 C  CG1 . VAL   A 1 211 ? 121.106 20.605 -19.002 1.00 26.16  ? 191 VAL   A CG1 1 
ATOM   1514 C  CG2 . VAL   A 1 211 ? 120.233 18.395 -18.157 1.00 23.67  ? 191 VAL   A CG2 1 
ATOM   1515 N  N   . ASP   A 1 212 ? 117.717 21.867 -19.778 1.00 23.83  ? 192 ASP   A N   1 
ATOM   1516 C  CA  . ASP   A 1 212 ? 117.350 23.149 -20.410 1.00 23.72  ? 192 ASP   A CA  1 
ATOM   1517 C  C   . ASP   A 1 212 ? 116.524 24.073 -19.480 1.00 23.64  ? 192 ASP   A C   1 
ATOM   1518 O  O   . ASP   A 1 212 ? 116.729 25.288 -19.469 1.00 25.32  ? 192 ASP   A O   1 
ATOM   1519 C  CB  . ASP   A 1 212 ? 116.615 22.893 -21.722 1.00 25.45  ? 192 ASP   A CB  1 
ATOM   1520 C  CG  . ASP   A 1 212 ? 117.534 22.349 -22.802 1.00 31.98  ? 192 ASP   A CG  1 
ATOM   1521 O  OD1 . ASP   A 1 212 ? 118.729 22.700 -22.792 1.00 35.86  ? 192 ASP   A OD1 1 
ATOM   1522 O  OD2 . ASP   A 1 212 ? 117.047 21.617 -23.687 1.00 31.72  ? 192 ASP   A OD2 1 
ATOM   1523 N  N   . ILE   A 1 213 ? 115.611 23.493 -18.704 1.00 22.68  ? 193 ILE   A N   1 
ATOM   1524 C  CA  . ILE   A 1 213 ? 114.795 24.229 -17.745 1.00 22.95  ? 193 ILE   A CA  1 
ATOM   1525 C  C   . ILE   A 1 213 ? 115.689 24.822 -16.672 1.00 22.42  ? 193 ILE   A C   1 
ATOM   1526 O  O   . ILE   A 1 213 ? 115.558 25.998 -16.347 1.00 23.00  ? 193 ILE   A O   1 
ATOM   1527 C  CB  . ILE   A 1 213 ? 113.684 23.322 -17.162 1.00 23.62  ? 193 ILE   A CB  1 
ATOM   1528 C  CG1 . ILE   A 1 213 ? 112.578 23.100 -18.201 1.00 24.64  ? 193 ILE   A CG1 1 
ATOM   1529 C  CG2 . ILE   A 1 213 ? 113.078 23.921 -15.873 1.00 23.78  ? 193 ILE   A CG2 1 
ATOM   1530 C  CD1 . ILE   A 1 213 ? 111.581 22.011 -17.813 1.00 26.60  ? 193 ILE   A CD1 1 
ATOM   1531 N  N   . TYR   A 1 214 ? 116.648 24.025 -16.150 1.00 22.24  ? 194 TYR   A N   1 
ATOM   1532 C  CA  . TYR   A 1 214 ? 117.605 24.516 -15.151 1.00 23.35  ? 194 TYR   A CA  1 
ATOM   1533 C  C   . TYR   A 1 214 ? 118.395 25.702 -15.717 1.00 24.34  ? 194 TYR   A C   1 
ATOM   1534 O  O   . TYR   A 1 214 ? 118.579 26.703 -15.024 1.00 24.30  ? 194 TYR   A O   1 
ATOM   1535 C  CB  . TYR   A 1 214 ? 118.587 23.371 -14.775 1.00 23.73  ? 194 TYR   A CB  1 
ATOM   1536 C  CG  . TYR   A 1 214 ? 119.787 23.815 -13.957 1.00 25.61  ? 194 TYR   A CG  1 
ATOM   1537 C  CD1 . TYR   A 1 214 ? 119.753 23.795 -12.572 1.00 26.81  ? 194 TYR   A CD1 1 
ATOM   1538 C  CD2 . TYR   A 1 214 ? 120.990 24.139 -14.570 1.00 27.71  ? 194 TYR   A CD2 1 
ATOM   1539 C  CE1 . TYR   A 1 214 ? 120.855 24.181 -11.816 1.00 27.29  ? 194 TYR   A CE1 1 
ATOM   1540 C  CE2 . TYR   A 1 214 ? 122.108 24.492 -13.823 1.00 28.94  ? 194 TYR   A CE2 1 
ATOM   1541 C  CZ  . TYR   A 1 214 ? 122.035 24.508 -12.446 1.00 29.29  ? 194 TYR   A CZ  1 
ATOM   1542 O  OH  . TYR   A 1 214 ? 123.138 24.874 -11.711 1.00 32.54  ? 194 TYR   A OH  1 
ATOM   1543 N  N   . ASN   A 1 215 ? 118.831 25.599 -16.978 1.00 24.00  ? 195 ASN   A N   1 
ATOM   1544 C  CA  . ASN   A 1 215 ? 119.587 26.670 -17.609 1.00 24.44  ? 195 ASN   A CA  1 
ATOM   1545 C  C   . ASN   A 1 215 ? 118.749 27.908 -17.943 1.00 24.83  ? 195 ASN   A C   1 
ATOM   1546 O  O   . ASN   A 1 215 ? 119.327 28.934 -18.291 1.00 26.84  ? 195 ASN   A O   1 
ATOM   1547 C  CB  . ASN   A 1 215 ? 120.319 26.154 -18.853 1.00 27.26  ? 195 ASN   A CB  1 
ATOM   1548 C  CG  . ASN   A 1 215 ? 121.506 25.287 -18.501 1.00 30.94  ? 195 ASN   A CG  1 
ATOM   1549 O  OD1 . ASN   A 1 215 ? 122.181 25.513 -17.482 1.00 33.12  ? 195 ASN   A OD1 1 
ATOM   1550 N  ND2 . ASN   A 1 215 ? 121.827 24.349 -19.356 1.00 31.07  ? 195 ASN   A ND2 1 
ATOM   1551 N  N   . SER   A 1 216 ? 117.421 27.822 -17.857 1.00 23.30  ? 196 SER   A N   1 
ATOM   1552 C  CA  . SER   A 1 216 ? 116.532 28.946 -18.212 1.00 25.09  ? 196 SER   A CA  1 
ATOM   1553 C  C   . SER   A 1 216 ? 115.931 29.656 -17.008 1.00 25.76  ? 196 SER   A C   1 
ATOM   1554 O  O   . SER   A 1 216 ? 115.305 30.695 -17.190 1.00 26.65  ? 196 SER   A O   1 
ATOM   1555 C  CB  . SER   A 1 216 ? 115.354 28.421 -19.046 1.00 27.19  ? 196 SER   A CB  1 
ATOM   1556 O  OG  . SER   A 1 216 ? 115.783 27.760 -20.210 1.00 29.41  ? 196 SER   A OG  1 
ATOM   1557 N  N   . ASP   A 1 217 ? 116.015 29.059 -15.821 1.00 24.27  ? 197 ASP   A N   1 
ATOM   1558 C  CA  . ASP   A 1 217 ? 115.372 29.609 -14.634 1.00 23.67  ? 197 ASP   A CA  1 
ATOM   1559 C  C   . ASP   A 1 217 ? 116.182 30.792 -14.094 1.00 24.70  ? 197 ASP   A C   1 
ATOM   1560 O  O   . ASP   A 1 217 ? 117.283 30.602 -13.579 1.00 24.71  ? 197 ASP   A O   1 
ATOM   1561 C  CB  . ASP   A 1 217 ? 115.269 28.490 -13.576 1.00 23.06  ? 197 ASP   A CB  1 
ATOM   1562 C  CG  . ASP   A 1 217 ? 114.460 28.854 -12.337 1.00 25.56  ? 197 ASP   A CG  1 
ATOM   1563 O  OD1 . ASP   A 1 217 ? 114.219 30.080 -12.115 1.00 25.93  ? 197 ASP   A OD1 1 
ATOM   1564 O  OD2 . ASP   A 1 217 ? 114.065 27.922 -11.595 1.00 25.85  ? 197 ASP   A OD2 1 
ATOM   1565 N  N   . PRO   A 1 218 ? 115.610 31.998 -14.103 1.00 25.63  ? 198 PRO   A N   1 
ATOM   1566 C  CA  . PRO   A 1 218 ? 116.369 33.157 -13.582 1.00 25.20  ? 198 PRO   A CA  1 
ATOM   1567 C  C   . PRO   A 1 218 ? 116.588 33.117 -12.065 1.00 24.71  ? 198 PRO   A C   1 
ATOM   1568 O  O   . PRO   A 1 218 ? 117.406 33.889 -11.557 1.00 26.51  ? 198 PRO   A O   1 
ATOM   1569 C  CB  . PRO   A 1 218 ? 115.559 34.387 -14.025 1.00 26.95  ? 198 PRO   A CB  1 
ATOM   1570 C  CG  . PRO   A 1 218 ? 114.225 33.861 -14.414 1.00 28.03  ? 198 PRO   A CG  1 
ATOM   1571 C  CD  . PRO   A 1 218 ? 114.278 32.376 -14.608 1.00 26.19  ? 198 PRO   A CD  1 
ATOM   1572 N  N   . LEU   A 1 219 ? 115.837 32.278 -11.340 1.00 23.74  ? 199 LEU   A N   1 
ATOM   1573 C  CA  . LEU   A 1 219 ? 116.044 32.171 -9.880  1.00 24.21  ? 199 LEU   A CA  1 
ATOM   1574 C  C   . LEU   A 1 219 ? 117.177 31.231 -9.495  1.00 25.66  ? 199 LEU   A C   1 
ATOM   1575 O  O   . LEU   A 1 219 ? 117.444 31.058 -8.304  1.00 26.79  ? 199 LEU   A O   1 
ATOM   1576 C  CB  . LEU   A 1 219 ? 114.755 31.745 -9.178  1.00 24.69  ? 199 LEU   A CB  1 
ATOM   1577 C  CG  . LEU   A 1 219 ? 113.653 32.806 -9.106  1.00 26.79  ? 199 LEU   A CG  1 
ATOM   1578 C  CD1 . LEU   A 1 219 ? 112.407 32.235 -8.401  1.00 27.93  ? 199 LEU   A CD1 1 
ATOM   1579 C  CD2 . LEU   A 1 219 ? 114.140 34.068 -8.394  1.00 27.10  ? 199 LEU   A CD2 1 
ATOM   1580 N  N   . ILE   A 1 220 ? 117.789 30.538 -10.480 1.00 24.52  ? 200 ILE   A N   1 
ATOM   1581 C  CA  . ILE   A 1 220 ? 118.881 29.634 -10.190 1.00 24.44  ? 200 ILE   A CA  1 
ATOM   1582 C  C   . ILE   A 1 220 ? 120.187 30.369 -10.384 1.00 26.20  ? 200 ILE   A C   1 
ATOM   1583 O  O   . ILE   A 1 220 ? 120.367 31.077 -11.388 1.00 27.77  ? 200 ILE   A O   1 
ATOM   1584 C  CB  . ILE   A 1 220 ? 118.811 28.396 -11.122 1.00 23.83  ? 200 ILE   A CB  1 
ATOM   1585 C  CG1 . ILE   A 1 220 ? 117.596 27.515 -10.763 1.00 24.87  ? 200 ILE   A CG1 1 
ATOM   1586 C  CG2 . ILE   A 1 220 ? 120.100 27.561 -11.009 1.00 24.36  ? 200 ILE   A CG2 1 
ATOM   1587 C  CD1 . ILE   A 1 220 ? 117.373 26.346 -11.707 1.00 25.41  ? 200 ILE   A CD1 1 
ATOM   1588 N  N   . CYS   A 1 221 ? 121.110 30.202 -9.438  1.00 26.80  ? 201 CYS   A N   1 
ATOM   1589 C  CA  . CYS   A 1 221 ? 122.432 30.779 -9.564  1.00 28.87  ? 201 CYS   A CA  1 
ATOM   1590 C  C   . CYS   A 1 221 ? 123.321 29.760 -10.233 1.00 30.94  ? 201 CYS   A C   1 
ATOM   1591 O  O   . CYS   A 1 221 ? 123.570 28.682 -9.672  1.00 31.48  ? 201 CYS   A O   1 
ATOM   1592 C  CB  . CYS   A 1 221 ? 123.002 31.184 -8.214  1.00 30.35  ? 201 CYS   A CB  1 
ATOM   1593 S  SG  . CYS   A 1 221 ? 124.648 31.940 -8.327  1.00 36.41  ? 201 CYS   A SG  1 
ATOM   1594 N  N   . ARG   A 1 222 ? 123.767 30.076 -11.437 1.00 31.76  ? 202 ARG   A N   1 
ATOM   1595 C  CA  . ARG   A 1 222 ? 124.633 29.180 -12.184 1.00 33.94  ? 202 ARG   A CA  1 
ATOM   1596 C  C   . ARG   A 1 222 ? 126.079 29.701 -12.286 1.00 36.79  ? 202 ARG   A C   1 
ATOM   1597 O  O   . ARG   A 1 222 ? 126.832 29.257 -13.149 1.00 38.04  ? 202 ARG   A O   1 
ATOM   1598 C  CB  . ARG   A 1 222 ? 124.045 28.901 -13.573 1.00 33.83  ? 202 ARG   A CB  1 
ATOM   1599 C  CG  . ARG   A 1 222 ? 122.751 28.077 -13.526 1.00 33.70  ? 202 ARG   A CG  1 
ATOM   1600 C  CD  . ARG   A 1 222 ? 122.104 27.920 -14.903 1.00 34.65  ? 202 ARG   A CD  1 
ATOM   1601 N  NE  . ARG   A 1 222 ? 121.864 29.230 -15.508 1.00 35.79  ? 202 ARG   A NE  1 
ATOM   1602 C  CZ  . ARG   A 1 222 ? 120.732 29.915 -15.399 1.00 36.44  ? 202 ARG   A CZ  1 
ATOM   1603 N  NH1 . ARG   A 1 222 ? 119.678 29.383 -14.784 1.00 31.52  ? 202 ARG   A NH1 1 
ATOM   1604 N  NH2 . ARG   A 1 222 ? 120.631 31.124 -15.932 1.00 37.85  ? 202 ARG   A NH2 1 
ATOM   1605 N  N   . ALA   A 1 223 ? 126.466 30.622 -11.404 1.00 37.45  ? 203 ALA   A N   1 
ATOM   1606 C  CA  . ALA   A 1 223 ? 127.823 31.144 -11.366 1.00 38.27  ? 203 ALA   A CA  1 
ATOM   1607 C  C   . ALA   A 1 223 ? 128.751 30.074 -10.744 1.00 38.42  ? 203 ALA   A C   1 
ATOM   1608 O  O   . ALA   A 1 223 ? 128.278 29.116 -10.111 1.00 37.91  ? 203 ALA   A O   1 
ATOM   1609 C  CB  . ALA   A 1 223 ? 127.841 32.421 -10.525 1.00 38.95  ? 203 ALA   A CB  1 
ATOM   1610 N  N   . GLY   A 1 224 ? 130.067 30.251 -10.888 1.00 38.71  ? 204 GLY   A N   1 
ATOM   1611 C  CA  . GLY   A 1 224 ? 131.020 29.352 -10.252 1.00 38.69  ? 204 GLY   A CA  1 
ATOM   1612 C  C   . GLY   A 1 224 ? 130.910 29.446 -8.741  1.00 38.04  ? 204 GLY   A C   1 
ATOM   1613 O  O   . GLY   A 1 224 ? 130.525 30.499 -8.206  1.00 37.41  ? 204 GLY   A O   1 
ATOM   1614 N  N   . LEU   A 1 225 ? 131.173 28.347 -8.054  1.00 37.81  ? 205 LEU   A N   1 
ATOM   1615 C  CA  . LEU   A 1 225 ? 131.058 28.322 -6.601  1.00 38.40  ? 205 LEU   A CA  1 
ATOM   1616 C  C   . LEU   A 1 225 ? 132.182 29.119 -5.983  1.00 37.58  ? 205 LEU   A C   1 
ATOM   1617 O  O   . LEU   A 1 225 ? 133.343 28.853 -6.270  1.00 37.13  ? 205 LEU   A O   1 
ATOM   1618 C  CB  . LEU   A 1 225 ? 131.070 26.875 -6.079  1.00 39.95  ? 205 LEU   A CB  1 
ATOM   1619 C  CG  . LEU   A 1 225 ? 129.710 26.276 -5.723  1.00 43.25  ? 205 LEU   A CG  1 
ATOM   1620 C  CD1 . LEU   A 1 225 ? 128.718 26.380 -6.898  1.00 44.44  ? 205 LEU   A CD1 1 
ATOM   1621 C  CD2 . LEU   A 1 225 ? 129.858 24.820 -5.305  1.00 44.68  ? 205 LEU   A CD2 1 
ATOM   1622 N  N   . LYS   A 1 226 ? 131.849 30.116 -5.147  1.00 37.17  ? 206 LYS   A N   1 
ATOM   1623 C  CA  . LYS   A 1 226 ? 132.866 30.910 -4.458  1.00 37.34  ? 206 LYS   A CA  1 
ATOM   1624 C  C   . LYS   A 1 226 ? 133.629 29.990 -3.491  1.00 37.07  ? 206 LYS   A C   1 
ATOM   1625 O  O   . LYS   A 1 226 ? 133.040 29.043 -2.960  1.00 36.55  ? 206 LYS   A O   1 
ATOM   1626 C  CB  . LYS   A 1 226 ? 132.212 32.057 -3.683  1.00 39.89  ? 206 LYS   A CB  1 
ATOM   1627 C  CG  . LYS   A 1 226 ? 131.699 33.190 -4.568  1.00 45.49  ? 206 LYS   A CG  1 
ATOM   1628 C  CD  . LYS   A 1 226 ? 130.668 34.038 -3.811  1.00 51.99  ? 206 LYS   A CD  1 
ATOM   1629 C  CE  . LYS   A 1 226 ? 130.099 35.164 -4.643  1.00 57.80  ? 206 LYS   A CE  1 
ATOM   1630 N  NZ  . LYS   A 1 226 ? 128.717 35.543 -4.206  1.00 60.46  ? 206 LYS   A NZ  1 
ATOM   1631 N  N   . VAL   A 1 227 ? 134.931 30.225 -3.305  1.00 37.41  ? 207 VAL   A N   1 
ATOM   1632 C  CA  . VAL   A 1 227 ? 135.724 29.358 -2.434  1.00 38.09  ? 207 VAL   A CA  1 
ATOM   1633 C  C   . VAL   A 1 227 ? 135.210 29.396 -0.981  1.00 36.28  ? 207 VAL   A C   1 
ATOM   1634 O  O   . VAL   A 1 227 ? 135.185 28.345 -0.338  1.00 36.85  ? 207 VAL   A O   1 
ATOM   1635 C  CB  . VAL   A 1 227 ? 137.239 29.599 -2.566  1.00 40.49  ? 207 VAL   A CB  1 
ATOM   1636 C  CG1 . VAL   A 1 227 ? 138.012 28.753 -1.562  1.00 41.43  ? 207 VAL   A CG1 1 
ATOM   1637 C  CG2 . VAL   A 1 227 ? 137.687 29.260 -3.985  1.00 41.58  ? 207 VAL   A CG2 1 
ATOM   1638 N  N   . CYS   A 1 228 ? 134.717 30.555 -0.491  1.00 34.15  ? 208 CYS   A N   1 
ATOM   1639 C  CA  A CYS   A 1 228 ? 134.169 30.618 0.865   0.50 33.67  ? 208 CYS   A CA  1 
ATOM   1640 C  CA  B CYS   A 1 228 ? 134.142 30.644 0.855   0.50 34.18  ? 208 CYS   A CA  1 
ATOM   1641 C  C   . CYS   A 1 228 ? 132.943 29.691 0.987   1.00 33.10  ? 208 CYS   A C   1 
ATOM   1642 O  O   . CYS   A 1 228 ? 132.759 29.056 2.024   1.00 33.21  ? 208 CYS   A O   1 
ATOM   1643 C  CB  A CYS   A 1 228 ? 133.823 32.053 1.246   0.50 33.92  ? 208 CYS   A CB  1 
ATOM   1644 C  CB  B CYS   A 1 228 ? 133.737 32.080 1.180   0.50 35.67  ? 208 CYS   A CB  1 
ATOM   1645 S  SG  A CYS   A 1 228 ? 132.534 32.789 0.215   0.50 35.75  ? 208 CYS   A SG  1 
ATOM   1646 S  SG  B CYS   A 1 228 ? 135.105 33.136 1.714   0.50 41.62  ? 208 CYS   A SG  1 
ATOM   1647 N  N   . PHE   A 1 229 ? 132.116 29.597 -0.072  1.00 31.49  ? 209 PHE   A N   1 
ATOM   1648 C  CA  . PHE   A 1 229 ? 130.953 28.699 -0.047  1.00 30.47  ? 209 PHE   A CA  1 
ATOM   1649 C  C   . PHE   A 1 229 ? 131.420 27.233 -0.122  1.00 31.05  ? 209 PHE   A C   1 
ATOM   1650 O  O   . PHE   A 1 229 ? 130.890 26.384 0.592   1.00 30.74  ? 209 PHE   A O   1 
ATOM   1651 C  CB  . PHE   A 1 229 ? 129.983 29.020 -1.189  1.00 29.10  ? 209 PHE   A CB  1 
ATOM   1652 C  CG  . PHE   A 1 229 ? 128.619 28.401 -0.977  1.00 28.50  ? 209 PHE   A CG  1 
ATOM   1653 C  CD1 . PHE   A 1 229 ? 127.798 28.829 0.052   1.00 28.75  ? 209 PHE   A CD1 1 
ATOM   1654 C  CD2 . PHE   A 1 229 ? 128.178 27.369 -1.779  1.00 28.77  ? 209 PHE   A CD2 1 
ATOM   1655 C  CE1 . PHE   A 1 229 ? 126.552 28.249 0.259   1.00 29.28  ? 209 PHE   A CE1 1 
ATOM   1656 C  CE2 . PHE   A 1 229 ? 126.916 26.812 -1.589  1.00 29.24  ? 209 PHE   A CE2 1 
ATOM   1657 C  CZ  . PHE   A 1 229 ? 126.123 27.243 -0.564  1.00 28.80  ? 209 PHE   A CZ  1 
ATOM   1658 N  N   . GLY   A 1 230 ? 132.447 26.967 -0.929  1.00 31.56  ? 210 GLY   A N   1 
ATOM   1659 C  CA  . GLY   A 1 230 ? 133.064 25.645 -1.038  1.00 32.24  ? 210 GLY   A CA  1 
ATOM   1660 C  C   . GLY   A 1 230 ? 133.565 25.123 0.298   1.00 32.26  ? 210 GLY   A C   1 
ATOM   1661 O  O   . GLY   A 1 230 ? 133.391 23.930 0.607   1.00 31.48  ? 210 GLY   A O   1 
ATOM   1662 N  N   . ILE   A 1 231 ? 134.135 26.032 1.128   1.00 32.42  ? 211 ILE   A N   1 
ATOM   1663 C  CA  . ILE   A 1 231 ? 134.606 25.760 2.492   1.00 33.05  ? 211 ILE   A CA  1 
ATOM   1664 C  C   . ILE   A 1 231 ? 133.430 25.315 3.357   1.00 31.47  ? 211 ILE   A C   1 
ATOM   1665 O  O   . ILE   A 1 231 ? 133.573 24.368 4.138   1.00 31.98  ? 211 ILE   A O   1 
ATOM   1666 C  CB  . ILE   A 1 231 ? 135.312 26.999 3.096   1.00 34.94  ? 211 ILE   A CB  1 
ATOM   1667 C  CG1 . ILE   A 1 231 ? 136.718 27.154 2.499   1.00 37.15  ? 211 ILE   A CG1 1 
ATOM   1668 C  CG2 . ILE   A 1 231 ? 135.387 26.942 4.647   1.00 35.40  ? 211 ILE   A CG2 1 
ATOM   1669 C  CD1 . ILE   A 1 231 ? 137.405 28.436 2.875   1.00 39.25  ? 211 ILE   A CD1 1 
ATOM   1670 N  N   . GLN   A 1 232 ? 132.278 26.000 3.233   1.00 29.33  ? 212 GLN   A N   1 
ATOM   1671 C  CA  . GLN   A 1 232 ? 131.103 25.600 3.991   1.00 28.18  ? 212 GLN   A CA  1 
ATOM   1672 C  C   . GLN   A 1 232 ? 130.554 24.257 3.529   1.00 27.77  ? 212 GLN   A C   1 
ATOM   1673 O  O   . GLN   A 1 232 ? 130.011 23.524 4.349   1.00 27.88  ? 212 GLN   A O   1 
ATOM   1674 C  CB  . GLN   A 1 232 ? 130.019 26.693 4.016   1.00 27.98  ? 212 GLN   A CB  1 
ATOM   1675 C  CG  . GLN   A 1 232 ? 130.478 27.998 4.706   1.00 30.13  ? 212 GLN   A CG  1 
ATOM   1676 C  CD  . GLN   A 1 232 ? 130.991 27.763 6.113   1.00 31.60  ? 212 GLN   A CD  1 
ATOM   1677 O  OE1 . GLN   A 1 232 ? 130.489 26.906 6.862   1.00 30.93  ? 212 GLN   A OE1 1 
ATOM   1678 N  NE2 . GLN   A 1 232 ? 132.018 28.508 6.506   1.00 32.89  ? 212 GLN   A NE2 1 
ATOM   1679 N  N   . LEU   A 1 233 ? 130.731 23.902 2.249   1.00 27.10  ? 213 LEU   A N   1 
ATOM   1680 C  CA  . LEU   A 1 233 ? 130.296 22.590 1.762   1.00 27.96  ? 213 LEU   A CA  1 
ATOM   1681 C  C   . LEU   A 1 233 ? 131.249 21.516 2.304   1.00 29.27  ? 213 LEU   A C   1 
ATOM   1682 O  O   . LEU   A 1 233 ? 130.801 20.422 2.652   1.00 29.55  ? 213 LEU   A O   1 
ATOM   1683 C  CB  . LEU   A 1 233 ? 130.192 22.552 0.238   1.00 28.25  ? 213 LEU   A CB  1 
ATOM   1684 C  CG  . LEU   A 1 233 ? 129.089 23.441 -0.373  1.00 29.62  ? 213 LEU   A CG  1 
ATOM   1685 C  CD1 . LEU   A 1 233 ? 129.157 23.409 -1.896  1.00 29.96  ? 213 LEU   A CD1 1 
ATOM   1686 C  CD2 . LEU   A 1 233 ? 127.702 23.007 0.076   1.00 30.87  ? 213 LEU   A CD2 1 
ATOM   1687 N  N   . LEU   A 1 234 ? 132.557 21.836 2.440   1.00 30.04  ? 214 LEU   A N   1 
ATOM   1688 C  CA  . LEU   A 1 234 ? 133.520 20.918 3.059   1.00 31.67  ? 214 LEU   A CA  1 
ATOM   1689 C  C   . LEU   A 1 234 ? 133.139 20.753 4.539   1.00 31.84  ? 214 LEU   A C   1 
ATOM   1690 O  O   . LEU   A 1 234 ? 133.195 19.646 5.066   1.00 31.96  ? 214 LEU   A O   1 
ATOM   1691 C  CB  . LEU   A 1 234 ? 134.955 21.473 2.983   1.00 33.05  ? 214 LEU   A CB  1 
ATOM   1692 C  CG  . LEU   A 1 234 ? 135.631 21.427 1.618   1.00 35.53  ? 214 LEU   A CG  1 
ATOM   1693 C  CD1 . LEU   A 1 234 ? 136.965 22.187 1.659   1.00 36.16  ? 214 LEU   A CD1 1 
ATOM   1694 C  CD2 . LEU   A 1 234 ? 135.820 19.986 1.132   1.00 36.80  ? 214 LEU   A CD2 1 
ATOM   1695 N  N   . ASN   A 1 235 ? 132.702 21.839 5.202   1.00 31.06  ? 215 ASN   A N   1 
ATOM   1696 C  CA  . ASN   A 1 235 ? 132.240 21.771 6.583   1.00 31.31  ? 215 ASN   A CA  1 
ATOM   1697 C  C   . ASN   A 1 235 ? 131.027 20.869 6.674   1.00 30.59  ? 215 ASN   A C   1 
ATOM   1698 O  O   . ASN   A 1 235 ? 131.002 20.003 7.531   1.00 31.40  ? 215 ASN   A O   1 
ATOM   1699 C  CB  . ASN   A 1 235 ? 131.886 23.159 7.130   1.00 32.92  ? 215 ASN   A CB  1 
ATOM   1700 C  CG  . ASN   A 1 235 ? 133.086 24.000 7.469   1.00 37.41  ? 215 ASN   A CG  1 
ATOM   1701 O  OD1 . ASN   A 1 235 ? 134.229 23.518 7.493   1.00 39.42  ? 215 ASN   A OD1 1 
ATOM   1702 N  ND2 . ASN   A 1 235 ? 132.849 25.279 7.747   1.00 37.51  ? 215 ASN   A ND2 1 
ATOM   1703 N  N   . ALA   A 1 236 ? 130.077 21.003 5.739   1.00 29.21  ? 216 ALA   A N   1 
ATOM   1704 C  CA  . ALA   A 1 236 ? 128.876 20.182 5.715   1.00 28.50  ? 216 ALA   A CA  1 
ATOM   1705 C  C   . ALA   A 1 236 ? 129.243 18.694 5.614   1.00 28.30  ? 216 ALA   A C   1 
ATOM   1706 O  O   . ALA   A 1 236 ? 128.745 17.908 6.408   1.00 27.58  ? 216 ALA   A O   1 
ATOM   1707 C  CB  . ALA   A 1 236 ? 127.978 20.596 4.557   1.00 28.52  ? 216 ALA   A CB  1 
ATOM   1708 N  N   . VAL   A 1 237 ? 130.142 18.327 4.688   1.00 28.02  ? 217 VAL   A N   1 
ATOM   1709 C  CA  . VAL   A 1 237 ? 130.558 16.933 4.513   1.00 28.22  ? 217 VAL   A CA  1 
ATOM   1710 C  C   . VAL   A 1 237 ? 131.208 16.378 5.805   1.00 28.28  ? 217 VAL   A C   1 
ATOM   1711 O  O   . VAL   A 1 237 ? 130.922 15.243 6.212   1.00 28.05  ? 217 VAL   A O   1 
ATOM   1712 C  CB  . VAL   A 1 237 ? 131.487 16.832 3.273   1.00 29.31  ? 217 VAL   A CB  1 
ATOM   1713 C  CG1 . VAL   A 1 237 ? 132.284 15.528 3.261   1.00 30.55  ? 217 VAL   A CG1 1 
ATOM   1714 C  CG2 . VAL   A 1 237 ? 130.678 16.990 1.981   1.00 29.25  ? 217 VAL   A CG2 1 
ATOM   1715 N  N   . SER   A 1 238 ? 132.051 17.191 6.454   1.00 29.21  ? 218 SER   A N   1 
ATOM   1716 C  CA  A SER   A 1 238 ? 132.723 16.767 7.681   0.50 30.28  ? 218 SER   A CA  1 
ATOM   1717 C  CA  B SER   A 1 238 ? 132.724 16.772 7.679   0.50 29.85  ? 218 SER   A CA  1 
ATOM   1718 C  C   . SER   A 1 238 ? 131.718 16.581 8.809   1.00 29.72  ? 218 SER   A C   1 
ATOM   1719 O  O   . SER   A 1 238 ? 131.788 15.586 9.539   1.00 30.26  ? 218 SER   A O   1 
ATOM   1720 C  CB  A SER   A 1 238 ? 133.784 17.786 8.088   0.50 33.70  ? 218 SER   A CB  1 
ATOM   1721 C  CB  B SER   A 1 238 ? 133.772 17.804 8.084   0.50 31.98  ? 218 SER   A CB  1 
ATOM   1722 O  OG  A SER   A 1 238 ? 134.813 17.856 7.115   0.50 38.56  ? 218 SER   A OG  1 
ATOM   1723 O  OG  B SER   A 1 238 ? 134.523 17.335 9.189   0.50 34.66  ? 218 SER   A OG  1 
ATOM   1724 N  N   . ARG   A 1 239 ? 130.775 17.527 8.942   1.00 28.50  ? 219 ARG   A N   1 
ATOM   1725 C  CA  . ARG   A 1 239 ? 129.741 17.488 9.965   1.00 27.68  ? 219 ARG   A CA  1 
ATOM   1726 C  C   . ARG   A 1 239 ? 128.776 16.340 9.735   1.00 26.40  ? 219 ARG   A C   1 
ATOM   1727 O  O   . ARG   A 1 239 ? 128.345 15.705 10.695  1.00 26.91  ? 219 ARG   A O   1 
ATOM   1728 C  CB  . ARG   A 1 239 ? 129.005 18.826 10.032  1.00 28.20  ? 219 ARG   A CB  1 
ATOM   1729 C  CG  . ARG   A 1 239 ? 129.880 19.911 10.632  1.00 30.22  ? 219 ARG   A CG  1 
ATOM   1730 C  CD  . ARG   A 1 239 ? 129.267 21.275 10.416  1.00 31.63  ? 219 ARG   A CD  1 
ATOM   1731 N  NE  . ARG   A 1 239 ? 130.257 22.346 10.592  1.00 33.00  ? 219 ARG   A NE  1 
ATOM   1732 C  CZ  . ARG   A 1 239 ? 129.965 23.644 10.549  1.00 32.82  ? 219 ARG   A CZ  1 
ATOM   1733 N  NH1 . ARG   A 1 239 ? 128.709 24.044 10.371  1.00 30.27  ? 219 ARG   A NH1 1 
ATOM   1734 N  NH2 . ARG   A 1 239 ? 130.924 24.551 10.686  1.00 32.09  ? 219 ARG   A NH2 1 
ATOM   1735 N  N   . VAL   A 1 240 ? 128.446 16.035 8.463   1.00 25.44  ? 220 VAL   A N   1 
ATOM   1736 C  CA  . VAL   A 1 240 ? 127.552 14.915 8.158   1.00 25.53  ? 220 VAL   A CA  1 
ATOM   1737 C  C   . VAL   A 1 240 ? 128.224 13.615 8.606   1.00 26.91  ? 220 VAL   A C   1 
ATOM   1738 O  O   . VAL   A 1 240 ? 127.597 12.812 9.278   1.00 26.71  ? 220 VAL   A O   1 
ATOM   1739 C  CB  . VAL   A 1 240 ? 127.162 14.887 6.652   1.00 25.98  ? 220 VAL   A CB  1 
ATOM   1740 C  CG1 . VAL   A 1 240 ? 126.642 13.506 6.227   1.00 26.18  ? 220 VAL   A CG1 1 
ATOM   1741 C  CG2 . VAL   A 1 240 ? 126.127 15.974 6.355   1.00 25.85  ? 220 VAL   A CG2 1 
ATOM   1742 N  N   . GLU   A 1 241 ? 129.517 13.457 8.308   1.00 28.72  ? 221 GLU   A N   1 
ATOM   1743 C  CA  . GLU   A 1 241 ? 130.255 12.252 8.708   1.00 31.29  ? 221 GLU   A CA  1 
ATOM   1744 C  C   . GLU   A 1 241 ? 130.222 12.056 10.234  1.00 32.65  ? 221 GLU   A C   1 
ATOM   1745 O  O   . GLU   A 1 241 ? 129.938 10.954 10.706  1.00 33.46  ? 221 GLU   A O   1 
ATOM   1746 C  CB  . GLU   A 1 241 ? 131.711 12.343 8.229   1.00 35.66  ? 221 GLU   A CB  1 
ATOM   1747 C  CG  . GLU   A 1 241 ? 132.523 11.091 8.519   1.00 44.25  ? 221 GLU   A CG  1 
ATOM   1748 C  CD  . GLU   A 1 241 ? 134.017 11.351 8.562   1.00 56.05  ? 221 GLU   A CD  1 
ATOM   1749 O  OE1 . GLU   A 1 241 ? 134.476 12.304 7.889   1.00 58.49  ? 221 GLU   A OE1 1 
ATOM   1750 O  OE2 . GLU   A 1 241 ? 134.726 10.607 9.279   1.00 59.90  ? 221 GLU   A OE2 1 
ATOM   1751 N  N   . ARG   A 1 242 ? 130.456 13.139 10.999  1.00 32.53  ? 222 ARG   A N   1 
ATOM   1752 C  CA  . ARG   A 1 242 ? 130.414 13.055 12.454  1.00 33.63  ? 222 ARG   A CA  1 
ATOM   1753 C  C   . ARG   A 1 242 ? 129.000 12.825 12.986  1.00 33.20  ? 222 ARG   A C   1 
ATOM   1754 O  O   . ARG   A 1 242 ? 128.856 12.292 14.082  1.00 34.22  ? 222 ARG   A O   1 
ATOM   1755 C  CB  . ARG   A 1 242 ? 131.013 14.321 13.093  1.00 36.99  ? 222 ARG   A CB  1 
ATOM   1756 C  CG  . ARG   A 1 242 ? 132.532 14.368 13.035  1.00 43.07  ? 222 ARG   A CG  1 
ATOM   1757 C  CD  . ARG   A 1 242 ? 133.073 15.558 13.810  1.00 49.27  ? 222 ARG   A CD  1 
ATOM   1758 N  NE  . ARG   A 1 242 ? 132.685 16.833 13.198  1.00 54.74  ? 222 ARG   A NE  1 
ATOM   1759 C  CZ  . ARG   A 1 242 ? 133.459 17.537 12.375  1.00 58.02  ? 222 ARG   A CZ  1 
ATOM   1760 N  NH1 . ARG   A 1 242 ? 134.675 17.102 12.060  1.00 58.87  ? 222 ARG   A NH1 1 
ATOM   1761 N  NH2 . ARG   A 1 242 ? 133.026 18.682 11.863  1.00 57.02  ? 222 ARG   A NH2 1 
ATOM   1762 N  N   . ALA   A 1 243 ? 127.967 13.233 12.240  1.00 31.72  ? 223 ALA   A N   1 
ATOM   1763 C  CA  . ALA   A 1 243 ? 126.592 13.088 12.695  1.00 32.04  ? 223 ALA   A CA  1 
ATOM   1764 C  C   . ALA   A 1 243 ? 126.033 11.688 12.496  1.00 33.07  ? 223 ALA   A C   1 
ATOM   1765 O  O   . ALA   A 1 243 ? 125.078 11.341 13.178  1.00 33.88  ? 223 ALA   A O   1 
ATOM   1766 C  CB  . ALA   A 1 243 ? 125.688 14.083 11.972  1.00 31.81  ? 223 ALA   A CB  1 
ATOM   1767 N  N   . LEU   A 1 244 ? 126.553 10.926 11.540  1.00 33.16  ? 224 LEU   A N   1 
ATOM   1768 C  CA  . LEU   A 1 244 ? 125.964 9.622  11.195  1.00 35.20  ? 224 LEU   A CA  1 
ATOM   1769 C  C   . LEU   A 1 244 ? 125.767 8.658  12.384  1.00 37.83  ? 224 LEU   A C   1 
ATOM   1770 O  O   . LEU   A 1 244 ? 124.644 8.155  12.524  1.00 37.44  ? 224 LEU   A O   1 
ATOM   1771 C  CB  . LEU   A 1 244 ? 126.710 8.947  10.050  1.00 35.06  ? 224 LEU   A CB  1 
ATOM   1772 C  CG  . LEU   A 1 244 ? 126.767 9.739  8.744   1.00 36.24  ? 224 LEU   A CG  1 
ATOM   1773 C  CD1 . LEU   A 1 244 ? 127.345 8.902  7.625   1.00 36.75  ? 224 LEU   A CD1 1 
ATOM   1774 C  CD2 . LEU   A 1 244 ? 125.384 10.290 8.324   1.00 37.11  ? 224 LEU   A CD2 1 
ATOM   1775 N  N   . PRO   A 1 245 ? 126.728 8.478  13.320  1.00 39.75  ? 225 PRO   A N   1 
ATOM   1776 C  CA  . PRO   A 1 245 ? 126.447 7.615  14.490  1.00 41.24  ? 225 PRO   A CA  1 
ATOM   1777 C  C   . PRO   A 1 245 ? 125.377 8.181  15.444  1.00 42.54  ? 225 PRO   A C   1 
ATOM   1778 O  O   . PRO   A 1 245 ? 124.864 7.457  16.290  1.00 44.58  ? 225 PRO   A O   1 
ATOM   1779 C  CB  . PRO   A 1 245 ? 127.817 7.472  15.168  1.00 42.38  ? 225 PRO   A CB  1 
ATOM   1780 C  CG  . PRO   A 1 245 ? 128.833 7.933  14.128  1.00 42.67  ? 225 PRO   A CG  1 
ATOM   1781 C  CD  . PRO   A 1 245 ? 128.114 8.986  13.354  1.00 40.32  ? 225 PRO   A CD  1 
ATOM   1782 N  N   . LYS   A 1 246 ? 125.030 9.451  15.313  1.00 41.98  ? 226 LYS   A N   1 
ATOM   1783 C  CA  . LYS   A 1 246 ? 123.968 10.080 16.103  1.00 41.82  ? 226 LYS   A CA  1 
ATOM   1784 C  C   . LYS   A 1 246 ? 122.604 10.010 15.380  1.00 40.08  ? 226 LYS   A C   1 
ATOM   1785 O  O   . LYS   A 1 246 ? 121.583 10.400 15.963  1.00 41.55  ? 226 LYS   A O   1 
ATOM   1786 C  CB  . LYS   A 1 246 ? 124.290 11.575 16.351  1.00 44.75  ? 226 LYS   A CB  1 
ATOM   1787 C  CG  . LYS   A 1 246 ? 125.728 11.843 16.787  1.00 50.67  ? 226 LYS   A CG  1 
ATOM   1788 C  CD  . LYS   A 1 246 ? 126.056 13.333 16.847  1.00 56.34  ? 226 LYS   A CD  1 
ATOM   1789 C  CE  . LYS   A 1 246 ? 127.496 13.547 17.250  1.00 61.28  ? 226 LYS   A CE  1 
ATOM   1790 N  NZ  . LYS   A 1 246 ? 127.820 14.988 17.441  1.00 64.31  ? 226 LYS   A NZ  1 
ATOM   1791 N  N   . LEU   A 1 247 ? 122.598 9.665  14.078  1.00 36.28  ? 227 LEU   A N   1 
ATOM   1792 C  CA  . LEU   A 1 247 ? 121.390 9.669  13.295  1.00 32.88  ? 227 LEU   A CA  1 
ATOM   1793 C  C   . LEU   A 1 247 ? 120.594 8.399  13.577  1.00 30.52  ? 227 LEU   A C   1 
ATOM   1794 O  O   . LEU   A 1 247 ? 121.085 7.284  13.382  1.00 30.68  ? 227 LEU   A O   1 
ATOM   1795 C  CB  . LEU   A 1 247 ? 121.745 9.795  11.804  1.00 32.38  ? 227 LEU   A CB  1 
ATOM   1796 C  CG  . LEU   A 1 247 ? 120.635 10.208 10.870  1.00 32.85  ? 227 LEU   A CG  1 
ATOM   1797 C  CD1 . LEU   A 1 247 ? 120.232 11.660 11.116  1.00 33.07  ? 227 LEU   A CD1 1 
ATOM   1798 C  CD2 . LEU   A 1 247 ? 121.066 10.008 9.424   1.00 31.89  ? 227 LEU   A CD2 1 
ATOM   1799 N  N   . THR   A 1 248 ? 119.385 8.578  14.087  1.00 28.50  ? 228 THR   A N   1 
ATOM   1800 C  CA  . THR   A 1 248 ? 118.473 7.472  14.379  1.00 27.99  ? 228 THR   A CA  1 
ATOM   1801 C  C   . THR   A 1 248 ? 117.143 7.610  13.637  1.00 25.64  ? 228 THR   A C   1 
ATOM   1802 O  O   . THR   A 1 248 ? 116.317 6.705  13.718  1.00 25.87  ? 228 THR   A O   1 
ATOM   1803 C  CB  . THR   A 1 248 ? 118.201 7.403  15.897  1.00 30.24  ? 228 THR   A CB  1 
ATOM   1804 O  OG1 . THR   A 1 248 ? 117.600 8.648  16.316  1.00 31.45  ? 228 THR   A OG1 1 
ATOM   1805 C  CG2 . THR   A 1 248 ? 119.467 7.123  16.695  1.00 31.62  ? 228 THR   A CG2 1 
ATOM   1806 N  N   . VAL   A 1 249 ? 116.903 8.740  12.953  1.00 24.75  ? 229 VAL   A N   1 
ATOM   1807 C  CA  . VAL   A 1 249 ? 115.638 8.971  12.288  1.00 24.22  ? 229 VAL   A CA  1 
ATOM   1808 C  C   . VAL   A 1 249 ? 115.397 7.962  11.173  1.00 23.18  ? 229 VAL   A C   1 
ATOM   1809 O  O   . VAL   A 1 249 ? 116.335 7.614  10.465  1.00 22.88  ? 229 VAL   A O   1 
ATOM   1810 C  CB  . VAL   A 1 249 ? 115.616 10.436 11.732  1.00 24.29  ? 229 VAL   A CB  1 
ATOM   1811 C  CG1 . VAL   A 1 249 ? 116.626 10.603 10.607  1.00 24.00  ? 229 VAL   A CG1 1 
ATOM   1812 C  CG2 . VAL   A 1 249 ? 114.223 10.843 11.259  1.00 24.94  ? 229 VAL   A CG2 1 
ATOM   1813 N  N   . PRO   A 1 250 ? 114.160 7.489  10.990  1.00 23.31  ? 230 PRO   A N   1 
ATOM   1814 C  CA  . PRO   A 1 250 ? 113.864 6.644  9.824   1.00 23.02  ? 230 PRO   A CA  1 
ATOM   1815 C  C   . PRO   A 1 250 ? 114.175 7.399  8.520   1.00 21.51  ? 230 PRO   A C   1 
ATOM   1816 O  O   . PRO   A 1 250 ? 113.940 8.614  8.446   1.00 21.68  ? 230 PRO   A O   1 
ATOM   1817 C  CB  . PRO   A 1 250 ? 112.355 6.414  9.931   1.00 24.36  ? 230 PRO   A CB  1 
ATOM   1818 C  CG  . PRO   A 1 250 ? 112.046 6.580  11.423  1.00 24.79  ? 230 PRO   A CG  1 
ATOM   1819 C  CD  . PRO   A 1 250 ? 112.964 7.690  11.842  1.00 23.54  ? 230 PRO   A CD  1 
ATOM   1820 N  N   . PHE   A 1 251 ? 114.735 6.703  7.512   1.00 20.13  ? 231 PHE   A N   1 
ATOM   1821 C  CA  . PHE   A 1 251 ? 114.978 7.404  6.250   1.00 19.19  ? 231 PHE   A CA  1 
ATOM   1822 C  C   . PHE   A 1 251 ? 114.875 6.511  5.051   1.00 18.83  ? 231 PHE   A C   1 
ATOM   1823 O  O   . PHE   A 1 251 ? 115.099 5.292  5.138   1.00 18.59  ? 231 PHE   A O   1 
ATOM   1824 C  CB  . PHE   A 1 251 ? 116.300 8.201  6.229   1.00 19.95  ? 231 PHE   A CB  1 
ATOM   1825 C  CG  . PHE   A 1 251 ? 117.568 7.383  6.328   1.00 20.84  ? 231 PHE   A CG  1 
ATOM   1826 C  CD1 . PHE   A 1 251 ? 118.181 6.879  5.188   1.00 21.39  ? 231 PHE   A CD1 1 
ATOM   1827 C  CD2 . PHE   A 1 251 ? 118.201 7.204  7.549   1.00 22.19  ? 231 PHE   A CD2 1 
ATOM   1828 C  CE1 . PHE   A 1 251 ? 119.377 6.170  5.274   1.00 22.29  ? 231 PHE   A CE1 1 
ATOM   1829 C  CE2 . PHE   A 1 251 ? 119.394 6.489  7.632   1.00 22.88  ? 231 PHE   A CE2 1 
ATOM   1830 C  CZ  . PHE   A 1 251 ? 119.985 5.989  6.487   1.00 22.03  ? 231 PHE   A CZ  1 
ATOM   1831 N  N   . LEU   A 1 252 ? 114.548 7.158  3.931   1.00 18.87  ? 232 LEU   A N   1 
ATOM   1832 C  CA  . LEU   A 1 252 ? 114.522 6.592  2.582   1.00 18.74  ? 232 LEU   A CA  1 
ATOM   1833 C  C   . LEU   A 1 252 ? 115.592 7.350  1.821   1.00 19.08  ? 232 LEU   A C   1 
ATOM   1834 O  O   . LEU   A 1 252 ? 115.587 8.583  1.815   1.00 18.85  ? 232 LEU   A O   1 
ATOM   1835 C  CB  . LEU   A 1 252 ? 113.170 6.814  1.891   1.00 19.07  ? 232 LEU   A CB  1 
ATOM   1836 C  CG  . LEU   A 1 252 ? 113.101 6.416  0.420   1.00 20.17  ? 232 LEU   A CG  1 
ATOM   1837 C  CD1 . LEU   A 1 252 ? 113.351 4.903  0.253   1.00 20.29  ? 232 LEU   A CD1 1 
ATOM   1838 C  CD2 . LEU   A 1 252 ? 111.737 6.804  -0.192  1.00 20.70  ? 232 LEU   A CD2 1 
ATOM   1839 N  N   . LEU   A 1 253 ? 116.522 6.635  1.204   1.00 18.34  ? 233 LEU   A N   1 
ATOM   1840 C  CA  . LEU   A 1 253 ? 117.649 7.228  0.504   1.00 18.72  ? 233 LEU   A CA  1 
ATOM   1841 C  C   . LEU   A 1 253 ? 117.581 6.791  -0.958  1.00 18.40  ? 233 LEU   A C   1 
ATOM   1842 O  O   . LEU   A 1 253 ? 117.501 5.594  -1.240  1.00 18.54  ? 233 LEU   A O   1 
ATOM   1843 C  CB  . LEU   A 1 253 ? 118.914 6.708  1.181   1.00 19.94  ? 233 LEU   A CB  1 
ATOM   1844 C  CG  . LEU   A 1 253 ? 120.272 7.015  0.602   1.00 22.48  ? 233 LEU   A CG  1 
ATOM   1845 C  CD1 . LEU   A 1 253 ? 120.518 8.493  0.450   1.00 21.75  ? 233 LEU   A CD1 1 
ATOM   1846 C  CD2 . LEU   A 1 253 ? 121.369 6.411  1.480   1.00 24.47  ? 233 LEU   A CD2 1 
ATOM   1847 N  N   . LEU   A 1 254 ? 117.521 7.759  -1.868  1.00 17.63  ? 234 LEU   A N   1 
ATOM   1848 C  CA  . LEU   A 1 254 ? 117.414 7.477  -3.304  1.00 17.84  ? 234 LEU   A CA  1 
ATOM   1849 C  C   . LEU   A 1 254 ? 118.694 8.028  -3.942  1.00 17.97  ? 234 LEU   A C   1 
ATOM   1850 O  O   . LEU   A 1 254 ? 119.039 9.195  -3.719  1.00 18.99  ? 234 LEU   A O   1 
ATOM   1851 C  CB  . LEU   A 1 254 ? 116.192 8.187  -3.890  1.00 18.71  ? 234 LEU   A CB  1 
ATOM   1852 C  CG  . LEU   A 1 254 ? 114.861 7.940  -3.177  1.00 21.13  ? 234 LEU   A CG  1 
ATOM   1853 C  CD1 . LEU   A 1 254 ? 113.735 8.702  -3.860  1.00 21.96  ? 234 LEU   A CD1 1 
ATOM   1854 C  CD2 . LEU   A 1 254 ? 114.505 6.438  -3.159  1.00 21.94  ? 234 LEU   A CD2 1 
ATOM   1855 N  N   . GLN   A 1 255 ? 119.372 7.222  -4.769  1.00 17.77  ? 235 GLN   A N   1 
ATOM   1856 C  CA  . GLN   A 1 255 ? 120.666 7.636  -5.309  1.00 17.68  ? 235 GLN   A CA  1 
ATOM   1857 C  C   . GLN   A 1 255 ? 120.874 7.058  -6.710  1.00 18.44  ? 235 GLN   A C   1 
ATOM   1858 O  O   . GLN   A 1 255 ? 120.563 5.892  -6.938  1.00 18.49  ? 235 GLN   A O   1 
ATOM   1859 C  CB  . GLN   A 1 255 ? 121.764 7.079  -4.365  1.00 18.71  ? 235 GLN   A CB  1 
ATOM   1860 C  CG  . GLN   A 1 255 ? 123.207 7.282  -4.858  1.00 21.48  ? 235 GLN   A CG  1 
ATOM   1861 C  CD  . GLN   A 1 255 ? 123.601 8.740  -4.803  1.00 23.05  ? 235 GLN   A CD  1 
ATOM   1862 O  OE1 . GLN   A 1 255 ? 123.310 9.449  -3.824  1.00 21.92  ? 235 GLN   A OE1 1 
ATOM   1863 N  NE2 . GLN   A 1 255 ? 124.223 9.244  -5.872  1.00 22.93  ? 235 GLN   A NE2 1 
ATOM   1864 N  N   . GLY   A 1 256 ? 121.376 7.883  -7.625  1.00 18.39  ? 236 GLY   A N   1 
ATOM   1865 C  CA  . GLY   A 1 256 ? 121.698 7.439  -8.979  1.00 20.58  ? 236 GLY   A CA  1 
ATOM   1866 C  C   . GLY   A 1 256 ? 123.110 6.887  -8.994  1.00 21.46  ? 236 GLY   A C   1 
ATOM   1867 O  O   . GLY   A 1 256 ? 124.000 7.425  -8.330  1.00 22.02  ? 236 GLY   A O   1 
ATOM   1868 N  N   . SER   A 1 257 ? 123.336 5.813  -9.773  1.00 21.36  ? 237 SER   A N   1 
ATOM   1869 C  CA  . SER   A 1 257 ? 124.647 5.197  -9.801  1.00 22.28  ? 237 SER   A CA  1 
ATOM   1870 C  C   . SER   A 1 257 ? 125.675 6.005  -10.599 1.00 23.78  ? 237 SER   A C   1 
ATOM   1871 O  O   . SER   A 1 257 ? 126.871 5.774  -10.436 1.00 25.48  ? 237 SER   A O   1 
ATOM   1872 C  CB  . SER   A 1 257 ? 124.552 3.764  -10.318 1.00 23.93  ? 237 SER   A CB  1 
ATOM   1873 O  OG  . SER   A 1 257 ? 124.413 3.772  -11.728 1.00 24.72  ? 237 SER   A OG  1 
ATOM   1874 N  N   . ALA   A 1 258 ? 125.218 6.898  -11.490 1.00 22.88  ? 238 ALA   A N   1 
ATOM   1875 C  CA  . ALA   A 1 258 ? 126.129 7.680  -12.319 1.00 22.95  ? 238 ALA   A CA  1 
ATOM   1876 C  C   . ALA   A 1 258 ? 126.113 9.156  -11.906 1.00 23.94  ? 238 ALA   A C   1 
ATOM   1877 O  O   . ALA   A 1 258 ? 126.218 10.047 -12.746 1.00 25.52  ? 238 ALA   A O   1 
ATOM   1878 C  CB  . ALA   A 1 258 ? 125.743 7.530  -13.788 1.00 24.40  ? 238 ALA   A CB  1 
ATOM   1879 N  N   . ASP   A 1 259 ? 125.971 9.414  -10.606 1.00 22.68  ? 239 ASP   A N   1 
ATOM   1880 C  CA  . ASP   A 1 259 ? 125.914 10.769 -10.085 1.00 22.25  ? 239 ASP   A CA  1 
ATOM   1881 C  C   . ASP   A 1 259 ? 127.340 11.328 -9.992  1.00 24.32  ? 239 ASP   A C   1 
ATOM   1882 O  O   . ASP   A 1 259 ? 128.159 10.812 -9.220  1.00 25.13  ? 239 ASP   A O   1 
ATOM   1883 C  CB  . ASP   A 1 259 ? 125.221 10.730 -8.714  1.00 21.90  ? 239 ASP   A CB  1 
ATOM   1884 C  CG  . ASP   A 1 259 ? 124.884 12.092 -8.143  1.00 22.63  ? 239 ASP   A CG  1 
ATOM   1885 O  OD1 . ASP   A 1 259 ? 125.585 13.084 -8.499  1.00 23.59  ? 239 ASP   A OD1 1 
ATOM   1886 O  OD2 . ASP   A 1 259 ? 123.928 12.177 -7.330  1.00 23.01  ? 239 ASP   A OD2 1 
ATOM   1887 N  N   . ARG   A 1 260 ? 127.633 12.380 -10.777 1.00 24.44  ? 240 ARG   A N   1 
ATOM   1888 C  CA  . ARG   A 1 260 ? 128.941 13.015 -10.787 1.00 26.57  ? 240 ARG   A CA  1 
ATOM   1889 C  C   . ARG   A 1 260 ? 129.065 14.170 -9.784  1.00 27.44  ? 240 ARG   A C   1 
ATOM   1890 O  O   . ARG   A 1 260 ? 130.121 14.820 -9.751  1.00 28.26  ? 240 ARG   A O   1 
ATOM   1891 C  CB  . ARG   A 1 260 ? 129.273 13.539 -12.191 1.00 28.92  ? 240 ARG   A CB  1 
ATOM   1892 C  CG  . ARG   A 1 260 ? 129.351 12.423 -13.225 1.00 35.49  ? 240 ARG   A CG  1 
ATOM   1893 C  CD  . ARG   A 1 260 ? 130.576 12.584 -14.096 1.00 43.08  ? 240 ARG   A CD  1 
ATOM   1894 N  NE  . ARG   A 1 260 ? 130.214 12.624 -15.508 1.00 49.93  ? 240 ARG   A NE  1 
ATOM   1895 C  CZ  . ARG   A 1 260 ? 130.707 13.492 -16.387 1.00 53.10  ? 240 ARG   A CZ  1 
ATOM   1896 N  NH1 . ARG   A 1 260 ? 131.584 14.413 -16.003 1.00 52.92  ? 240 ARG   A NH1 1 
ATOM   1897 N  NH2 . ARG   A 1 260 ? 130.304 13.467 -17.649 1.00 53.84  ? 240 ARG   A NH2 1 
ATOM   1898 N  N   . LEU   A 1 261 ? 127.996 14.472 -9.027  1.00 26.60  ? 241 LEU   A N   1 
ATOM   1899 C  CA  . LEU   A 1 261 ? 127.989 15.578 -8.068  1.00 27.25  ? 241 LEU   A CA  1 
ATOM   1900 C  C   . LEU   A 1 261 ? 128.027 15.099 -6.624  1.00 28.05  ? 241 LEU   A C   1 
ATOM   1901 O  O   . LEU   A 1 261 ? 128.793 15.639 -5.826  1.00 30.18  ? 241 LEU   A O   1 
ATOM   1902 C  CB  . LEU   A 1 261 ? 126.798 16.502 -8.337  1.00 26.78  ? 241 LEU   A CB  1 
ATOM   1903 C  CG  . LEU   A 1 261 ? 126.815 17.108 -9.746  1.00 28.07  ? 241 LEU   A CG  1 
ATOM   1904 C  CD1 . LEU   A 1 261 ? 125.582 17.941 -9.993  1.00 27.98  ? 241 LEU   A CD1 1 
ATOM   1905 C  CD2 . LEU   A 1 261 ? 128.064 17.975 -9.962  1.00 28.89  ? 241 LEU   A CD2 1 
ATOM   1906 N  N   . CYS   A 1 262 ? 127.192 14.121 -6.275  1.00 26.43  ? 242 CYS   A N   1 
ATOM   1907 C  CA  . CYS   A 1 262 ? 127.173 13.492 -4.958  1.00 26.74  ? 242 CYS   A CA  1 
ATOM   1908 C  C   . CYS   A 1 262 ? 127.485 12.060 -5.201  1.00 27.54  ? 242 CYS   A C   1 
ATOM   1909 O  O   . CYS   A 1 262 ? 126.647 11.302 -5.715  1.00 27.52  ? 242 CYS   A O   1 
ATOM   1910 C  CB  . CYS   A 1 262 ? 125.827 13.662 -4.273  1.00 27.36  ? 242 CYS   A CB  1 
ATOM   1911 S  SG  . CYS   A 1 262 ? 125.491 15.373 -3.797  1.00 28.27  ? 242 CYS   A SG  1 
ATOM   1912 N  N   . ASP   A 1 263 ? 128.727 11.698 -4.892  1.00 27.15  ? 243 ASP   A N   1 
ATOM   1913 C  CA  . ASP   A 1 263 ? 129.232 10.361 -5.139  1.00 27.58  ? 243 ASP   A CA  1 
ATOM   1914 C  C   . ASP   A 1 263 ? 128.396 9.285  -4.493  1.00 26.31  ? 243 ASP   A C   1 
ATOM   1915 O  O   . ASP   A 1 263 ? 128.078 9.385  -3.312  1.00 25.49  ? 243 ASP   A O   1 
ATOM   1916 C  CB  . ASP   A 1 263 ? 130.682 10.239 -4.720  1.00 29.80  ? 243 ASP   A CB  1 
ATOM   1917 C  CG  . ASP   A 1 263 ? 131.308 9.111  -5.502  1.00 36.45  ? 243 ASP   A CG  1 
ATOM   1918 O  OD1 . ASP   A 1 263 ? 131.798 9.369  -6.629  1.00 39.51  ? 243 ASP   A OD1 1 
ATOM   1919 O  OD2 . ASP   A 1 263 ? 131.229 7.967  -5.042  1.00 36.26  ? 243 ASP   A OD2 1 
ATOM   1920 N  N   . SER   A 1 264 ? 128.011 8.275  -5.277  1.00 26.04  ? 244 SER   A N   1 
ATOM   1921 C  CA  . SER   A 1 264 ? 127.164 7.193  -4.783  1.00 26.59  ? 244 SER   A CA  1 
ATOM   1922 C  C   . SER   A 1 264 ? 127.778 6.472  -3.575  1.00 26.25  ? 244 SER   A C   1 
ATOM   1923 O  O   . SER   A 1 264 ? 127.035 5.912  -2.776  1.00 25.87  ? 244 SER   A O   1 
ATOM   1924 C  CB  . SER   A 1 264 ? 126.869 6.195  -5.894  1.00 28.78  ? 244 SER   A CB  1 
ATOM   1925 O  OG  . SER   A 1 264 ? 128.055 5.482  -6.204  1.00 29.98  ? 244 SER   A OG  1 
ATOM   1926 N  N   . LYS   A 1 265 ? 129.114 6.515  -3.423  1.00 25.97  ? 245 LYS   A N   1 
ATOM   1927 C  CA  . LYS   A 1 265 ? 129.799 5.936  -2.254  1.00 26.35  ? 245 LYS   A CA  1 
ATOM   1928 C  C   . LYS   A 1 265 ? 129.267 6.569  -0.940  1.00 25.38  ? 245 LYS   A C   1 
ATOM   1929 O  O   . LYS   A 1 265 ? 129.221 5.900  0.104   1.00 25.53  ? 245 LYS   A O   1 
ATOM   1930 C  CB  . LYS   A 1 265 ? 131.315 6.165  -2.364  1.00 30.28  ? 245 LYS   A CB  1 
ATOM   1931 C  CG  . LYS   A 1 265 ? 132.123 5.576  -1.220  1.00 38.75  ? 245 LYS   A CG  1 
ATOM   1932 C  CD  . LYS   A 1 265 ? 133.620 5.894  -1.362  1.00 46.85  ? 245 LYS   A CD  1 
ATOM   1933 C  CE  . LYS   A 1 265 ? 134.439 5.226  -0.280  1.00 53.13  ? 245 LYS   A CE  1 
ATOM   1934 N  NZ  . LYS   A 1 265 ? 133.915 5.531  1.084   1.00 56.76  ? 245 LYS   A NZ  1 
ATOM   1935 N  N   . GLY   A 1 266 ? 128.850 7.834  -1.011  1.00 24.23  ? 246 GLY   A N   1 
ATOM   1936 C  CA  . GLY   A 1 266 ? 128.274 8.527  0.137   1.00 24.14  ? 246 GLY   A CA  1 
ATOM   1937 C  C   . GLY   A 1 266 ? 126.970 7.897  0.569   1.00 23.19  ? 246 GLY   A C   1 
ATOM   1938 O  O   . GLY   A 1 266 ? 126.715 7.776  1.769   1.00 23.14  ? 246 GLY   A O   1 
ATOM   1939 N  N   . ALA   A 1 267 ? 126.132 7.476  -0.396  1.00 22.27  ? 247 ALA   A N   1 
ATOM   1940 C  CA  . ALA   A 1 267 ? 124.860 6.834  -0.064  1.00 22.56  ? 247 ALA   A CA  1 
ATOM   1941 C  C   . ALA   A 1 267 ? 125.124 5.497  0.654   1.00 22.88  ? 247 ALA   A C   1 
ATOM   1942 O  O   . ALA   A 1 267 ? 124.467 5.192  1.652   1.00 22.63  ? 247 ALA   A O   1 
ATOM   1943 C  CB  . ALA   A 1 267 ? 124.038 6.592  -1.325  1.00 23.28  ? 247 ALA   A CB  1 
ATOM   1944 N  N   . TYR   A 1 268 ? 126.121 4.721  0.180   1.00 23.27  ? 248 TYR   A N   1 
ATOM   1945 C  CA  . TYR   A 1 268 ? 126.453 3.445  0.832   1.00 23.48  ? 248 TYR   A CA  1 
ATOM   1946 C  C   . TYR   A 1 268 ? 127.035 3.706  2.243   1.00 24.66  ? 248 TYR   A C   1 
ATOM   1947 O  O   . TYR   A 1 268 ? 126.735 2.975  3.180   1.00 24.77  ? 248 TYR   A O   1 
ATOM   1948 C  CB  . TYR   A 1 268 ? 127.429 2.628  -0.027  1.00 23.13  ? 248 TYR   A CB  1 
ATOM   1949 C  CG  . TYR   A 1 268 ? 126.827 2.188  -1.347  1.00 24.25  ? 248 TYR   A CG  1 
ATOM   1950 C  CD1 . TYR   A 1 268 ? 125.851 1.206  -1.396  1.00 26.07  ? 248 TYR   A CD1 1 
ATOM   1951 C  CD2 . TYR   A 1 268 ? 127.254 2.732  -2.545  1.00 25.44  ? 248 TYR   A CD2 1 
ATOM   1952 C  CE1 . TYR   A 1 268 ? 125.307 0.785  -2.607  1.00 26.61  ? 248 TYR   A CE1 1 
ATOM   1953 C  CE2 . TYR   A 1 268 ? 126.716 2.320  -3.764  1.00 26.11  ? 248 TYR   A CE2 1 
ATOM   1954 C  CZ  . TYR   A 1 268 ? 125.759 1.327  -3.791  1.00 26.83  ? 248 TYR   A CZ  1 
ATOM   1955 O  OH  . TYR   A 1 268 ? 125.223 0.900  -4.983  1.00 27.72  ? 248 TYR   A OH  1 
ATOM   1956 N  N   . LEU   A 1 269 ? 127.809 4.792  2.405   1.00 25.14  ? 249 LEU   A N   1 
ATOM   1957 C  CA  . LEU   A 1 269 ? 128.379 5.144  3.707   1.00 26.10  ? 249 LEU   A CA  1 
ATOM   1958 C  C   . LEU   A 1 269 ? 127.269 5.510  4.691   1.00 24.65  ? 249 LEU   A C   1 
ATOM   1959 O  O   . LEU   A 1 269 ? 127.315 5.109  5.858   1.00 25.04  ? 249 LEU   A O   1 
ATOM   1960 C  CB  . LEU   A 1 269 ? 129.345 6.326  3.545   1.00 28.63  ? 249 LEU   A CB  1 
ATOM   1961 C  CG  . LEU   A 1 269 ? 130.089 6.787  4.805   1.00 33.08  ? 249 LEU   A CG  1 
ATOM   1962 C  CD1 . LEU   A 1 269 ? 131.290 5.899  5.058   1.00 34.70  ? 249 LEU   A CD1 1 
ATOM   1963 C  CD2 . LEU   A 1 269 ? 130.551 8.254  4.674   1.00 34.81  ? 249 LEU   A CD2 1 
ATOM   1964 N  N   . LEU   A 1 270 ? 126.254 6.246  4.217   1.00 23.56  ? 250 LEU   A N   1 
ATOM   1965 C  CA  . LEU   A 1 270 ? 125.135 6.646  5.059   1.00 23.68  ? 250 LEU   A CA  1 
ATOM   1966 C  C   . LEU   A 1 270 ? 124.360 5.400  5.502   1.00 23.45  ? 250 LEU   A C   1 
ATOM   1967 O  O   . LEU   A 1 270 ? 124.051 5.259  6.691   1.00 24.32  ? 250 LEU   A O   1 
ATOM   1968 C  CB  . LEU   A 1 270 ? 124.252 7.619  4.269   1.00 24.25  ? 250 LEU   A CB  1 
ATOM   1969 C  CG  . LEU   A 1 270 ? 122.907 8.004  4.863   1.00 26.53  ? 250 LEU   A CG  1 
ATOM   1970 C  CD1 . LEU   A 1 270 ? 123.041 8.575  6.257   1.00 27.60  ? 250 LEU   A CD1 1 
ATOM   1971 C  CD2 . LEU   A 1 270 ? 122.237 9.016  3.953   1.00 26.13  ? 250 LEU   A CD2 1 
ATOM   1972 N  N   . MET   A 1 271 ? 124.095 4.456  4.575   1.00 22.98  ? 251 MET   A N   1 
ATOM   1973 C  CA  . MET   A 1 271 ? 123.407 3.205  4.957   1.00 23.42  ? 251 MET   A CA  1 
ATOM   1974 C  C   . MET   A 1 271 ? 124.182 2.431  5.994   1.00 24.97  ? 251 MET   A C   1 
ATOM   1975 O  O   . MET   A 1 271 ? 123.583 1.813  6.879   1.00 25.78  ? 251 MET   A O   1 
ATOM   1976 C  CB  . MET   A 1 271 ? 123.192 2.267  3.744   1.00 24.08  ? 251 MET   A CB  1 
ATOM   1977 C  CG  . MET   A 1 271 ? 122.116 2.733  2.817   1.00 26.29  ? 251 MET   A CG  1 
ATOM   1978 S  SD  . MET   A 1 271 ? 120.506 2.833  3.627   1.00 25.50  ? 251 MET   A SD  1 
ATOM   1979 C  CE  . MET   A 1 271 ? 120.004 1.106  3.707   1.00 25.47  ? 251 MET   A CE  1 
ATOM   1980 N  N   . GLU   A 1 272 ? 125.509 2.413  5.869   1.00 24.10  ? 252 GLU   A N   1 
ATOM   1981 C  CA  . GLU   A 1 272 ? 126.339 1.661  6.776   1.00 25.16  ? 252 GLU   A CA  1 
ATOM   1982 C  C   . GLU   A 1 272 ? 126.512 2.314  8.143   1.00 25.79  ? 252 GLU   A C   1 
ATOM   1983 O  O   . GLU   A 1 272 ? 126.455 1.618  9.162   1.00 27.00  ? 252 GLU   A O   1 
ATOM   1984 C  CB  . GLU   A 1 272 ? 127.714 1.425  6.152   1.00 27.14  ? 252 GLU   A CB  1 
ATOM   1985 C  CG  . GLU   A 1 272 ? 128.569 0.458  6.962   1.00 34.74  ? 252 GLU   A CG  1 
ATOM   1986 C  CD  . GLU   A 1 272 ? 130.031 0.392  6.563   1.00 45.46  ? 252 GLU   A CD  1 
ATOM   1987 O  OE1 . GLU   A 1 272 ? 130.446 1.162  5.665   1.00 47.30  ? 252 GLU   A OE1 1 
ATOM   1988 O  OE2 . GLU   A 1 272 ? 130.769 -0.423 7.165   1.00 49.21  ? 252 GLU   A OE2 1 
ATOM   1989 N  N   . LEU   A 1 273 ? 126.758 3.638  8.177   1.00 25.52  ? 253 LEU   A N   1 
ATOM   1990 C  CA  . LEU   A 1 273 ? 127.110 4.280  9.444   1.00 26.85  ? 253 LEU   A CA  1 
ATOM   1991 C  C   . LEU   A 1 273 ? 125.949 4.848  10.252  1.00 27.04  ? 253 LEU   A C   1 
ATOM   1992 O  O   . LEU   A 1 273 ? 126.120 5.023  11.460  1.00 28.41  ? 253 LEU   A O   1 
ATOM   1993 C  CB  . LEU   A 1 273 ? 128.179 5.364  9.216   1.00 28.72  ? 253 LEU   A CB  1 
ATOM   1994 C  CG  . LEU   A 1 273 ? 129.531 4.869  8.656   1.00 32.41  ? 253 LEU   A CG  1 
ATOM   1995 C  CD1 . LEU   A 1 273 ? 130.523 6.011  8.594   1.00 34.39  ? 253 LEU   A CD1 1 
ATOM   1996 C  CD2 . LEU   A 1 273 ? 130.130 3.744  9.511   1.00 33.88  ? 253 LEU   A CD2 1 
ATOM   1997 N  N   . ALA   A 1 274 ? 124.787 5.153  9.632   1.00 26.01  ? 254 ALA   A N   1 
ATOM   1998 C  CA  . ALA   A 1 274 ? 123.651 5.660  10.417  1.00 26.37  ? 254 ALA   A CA  1 
ATOM   1999 C  C   . ALA   A 1 274 ? 123.177 4.598  11.407  1.00 27.36  ? 254 ALA   A C   1 
ATOM   2000 O  O   . ALA   A 1 274 ? 123.207 3.408  11.093  1.00 27.52  ? 254 ALA   A O   1 
ATOM   2001 C  CB  . ALA   A 1 274 ? 122.494 6.051  9.511   1.00 26.01  ? 254 ALA   A CB  1 
ATOM   2002 N  N   . LYS   A 1 275 ? 122.729 5.026  12.588  1.00 27.67  ? 255 LYS   A N   1 
ATOM   2003 C  CA  . LYS   A 1 275 ? 122.238 4.068  13.578  1.00 29.11  ? 255 LYS   A CA  1 
ATOM   2004 C  C   . LYS   A 1 275 ? 120.748 3.736  13.420  1.00 27.84  ? 255 LYS   A C   1 
ATOM   2005 O  O   . LYS   A 1 275 ? 120.257 2.812  14.075  1.00 28.06  ? 255 LYS   A O   1 
ATOM   2006 C  CB  . LYS   A 1 275 ? 122.570 4.534  14.990  1.00 33.99  ? 255 LYS   A CB  1 
ATOM   2007 C  CG  . LYS   A 1 275 ? 124.074 4.652  15.197  1.00 41.56  ? 255 LYS   A CG  1 
ATOM   2008 C  CD  . LYS   A 1 275 ? 124.810 3.320  15.171  1.00 47.71  ? 255 LYS   A CD  1 
ATOM   2009 C  CE  . LYS   A 1 275 ? 126.315 3.499  15.210  1.00 52.49  ? 255 LYS   A CE  1 
ATOM   2010 N  NZ  . LYS   A 1 275 ? 126.874 3.793  13.853  1.00 54.94  ? 255 LYS   A NZ  1 
ATOM   2011 N  N   . SER   A 1 276 ? 120.053 4.437  12.508  1.00 25.87  ? 256 SER   A N   1 
ATOM   2012 C  CA  . SER   A 1 276 ? 118.628 4.289  12.249  1.00 24.93  ? 256 SER   A CA  1 
ATOM   2013 C  C   . SER   A 1 276 ? 118.175 2.833  12.133  1.00 24.75  ? 256 SER   A C   1 
ATOM   2014 O  O   . SER   A 1 276 ? 118.752 2.072  11.355  1.00 25.89  ? 256 SER   A O   1 
ATOM   2015 C  CB  . SER   A 1 276 ? 118.269 5.000  10.948  1.00 24.55  ? 256 SER   A CB  1 
ATOM   2016 O  OG  . SER   A 1 276 ? 118.701 6.359  11.000  1.00 27.14  ? 256 SER   A OG  1 
ATOM   2017 N  N   . GLN   A 1 277 ? 117.153 2.458  12.899  1.00 23.97  ? 257 GLN   A N   1 
ATOM   2018 C  CA  . GLN   A 1 277 ? 116.581 1.119  12.780  1.00 25.34  ? 257 GLN   A CA  1 
ATOM   2019 C  C   . GLN   A 1 277 ? 115.732 0.953  11.503  1.00 25.60  ? 257 GLN   A C   1 
ATOM   2020 O  O   . GLN   A 1 277 ? 115.466 -0.178 11.100  1.00 26.29  ? 257 GLN   A O   1 
ATOM   2021 C  CB  . GLN   A 1 277 ? 115.735 0.799  14.008  1.00 27.22  ? 257 GLN   A CB  1 
ATOM   2022 C  CG  . GLN   A 1 277 ? 116.589 0.499  15.222  1.00 31.63  ? 257 GLN   A CG  1 
ATOM   2023 C  CD  . GLN   A 1 277 ? 117.384 -0.787 15.076  1.00 37.88  ? 257 GLN   A CD  1 
ATOM   2024 O  OE1 . GLN   A 1 277 ? 116.866 -1.852 14.690  1.00 39.37  ? 257 GLN   A OE1 1 
ATOM   2025 N  NE2 . GLN   A 1 277 ? 118.664 -0.728 15.401  1.00 39.47  ? 257 GLN   A NE2 1 
ATOM   2026 N  N   . ASP   A 1 278 ? 115.316 2.073  10.862  1.00 24.63  ? 258 ASP   A N   1 
ATOM   2027 C  CA  . ASP   A 1 278 ? 114.490 2.007  9.668   1.00 23.49  ? 258 ASP   A CA  1 
ATOM   2028 C  C   . ASP   A 1 278 ? 115.194 2.761  8.542   1.00 21.95  ? 258 ASP   A C   1 
ATOM   2029 O  O   . ASP   A 1 278 ? 115.050 3.978  8.430   1.00 22.06  ? 258 ASP   A O   1 
ATOM   2030 C  CB  . ASP   A 1 278 ? 113.127 2.636  9.998   1.00 25.63  ? 258 ASP   A CB  1 
ATOM   2031 C  CG  . ASP   A 1 278 ? 112.145 2.689  8.848   1.00 27.86  ? 258 ASP   A CG  1 
ATOM   2032 O  OD1 . ASP   A 1 278 ? 112.424 2.063  7.794   1.00 27.61  ? 258 ASP   A OD1 1 
ATOM   2033 O  OD2 . ASP   A 1 278 ? 111.086 3.329  9.010   1.00 30.45  ? 258 ASP   A OD2 1 
ATOM   2034 N  N   . LYS   A 1 279 ? 115.984 2.049  7.747   1.00 20.98  ? 259 LYS   A N   1 
ATOM   2035 C  CA  . LYS   A 1 279 ? 116.739 2.680  6.669   1.00 21.45  ? 259 LYS   A CA  1 
ATOM   2036 C  C   . LYS   A 1 279 ? 116.644 1.855  5.410   1.00 20.01  ? 259 LYS   A C   1 
ATOM   2037 O  O   . LYS   A 1 279 ? 116.815 0.631  5.430   1.00 19.88  ? 259 LYS   A O   1 
ATOM   2038 C  CB  . LYS   A 1 279 ? 118.198 2.968  7.061   1.00 24.09  ? 259 LYS   A CB  1 
ATOM   2039 C  CG  . LYS   A 1 279 ? 118.912 1.859  7.812   1.00 26.58  ? 259 LYS   A CG  1 
ATOM   2040 C  CD  . LYS   A 1 279 ? 120.323 2.301  8.239   1.00 27.52  ? 259 LYS   A CD  1 
ATOM   2041 C  CE  . LYS   A 1 279 ? 120.985 1.213  9.033   1.00 26.88  ? 259 LYS   A CE  1 
ATOM   2042 N  NZ  . LYS   A 1 279 ? 122.413 1.488  9.319   1.00 25.15  ? 259 LYS   A NZ  1 
ATOM   2043 N  N   . THR   A 1 280 ? 116.365 2.539  4.299   1.00 19.86  ? 260 THR   A N   1 
ATOM   2044 C  CA  . THR   A 1 280 ? 116.172 1.900  2.999   1.00 19.88  ? 260 THR   A CA  1 
ATOM   2045 C  C   . THR   A 1 280 ? 116.917 2.669  1.947   1.00 19.60  ? 260 THR   A C   1 
ATOM   2046 O  O   . THR   A 1 280 ? 116.846 3.894  1.941   1.00 19.90  ? 260 THR   A O   1 
ATOM   2047 C  CB  . THR   A 1 280 ? 114.685 1.923  2.667   1.00 22.67  ? 260 THR   A CB  1 
ATOM   2048 O  OG1 . THR   A 1 280 ? 113.968 1.266  3.709   1.00 24.08  ? 260 THR   A OG1 1 
ATOM   2049 C  CG2 . THR   A 1 280 ? 114.358 1.239  1.319   1.00 24.55  ? 260 THR   A CG2 1 
ATOM   2050 N  N   . LEU   A 1 281 ? 117.595 1.964  1.040   1.00 18.09  ? 261 LEU   A N   1 
ATOM   2051 C  CA  . LEU   A 1 281 ? 118.327 2.567  -0.079  1.00 18.38  ? 261 LEU   A CA  1 
ATOM   2052 C  C   . LEU   A 1 281 ? 117.755 2.043  -1.376  1.00 19.23  ? 261 LEU   A C   1 
ATOM   2053 O  O   . LEU   A 1 281 ? 117.618 0.831  -1.543  1.00 19.26  ? 261 LEU   A O   1 
ATOM   2054 C  CB  . LEU   A 1 281 ? 119.808 2.161  -0.026  1.00 19.58  ? 261 LEU   A CB  1 
ATOM   2055 C  CG  . LEU   A 1 281 ? 120.668 2.485  -1.264  1.00 21.11  ? 261 LEU   A CG  1 
ATOM   2056 C  CD1 . LEU   A 1 281 ? 120.746 4.015  -1.478  1.00 22.33  ? 261 LEU   A CD1 1 
ATOM   2057 C  CD2 . LEU   A 1 281 ? 122.072 1.891  -1.139  1.00 22.76  ? 261 LEU   A CD2 1 
ATOM   2058 N  N   . LYS   A 1 282 ? 117.509 2.934  -2.338  1.00 19.16  ? 262 LYS   A N   1 
ATOM   2059 C  CA  . LYS   A 1 282 ? 117.138 2.508  -3.679  1.00 19.99  ? 262 LYS   A CA  1 
ATOM   2060 C  C   . LYS   A 1 282 ? 118.138 3.146  -4.632  1.00 20.06  ? 262 LYS   A C   1 
ATOM   2061 O  O   . LYS   A 1 282 ? 118.364 4.360  -4.559  1.00 19.56  ? 262 LYS   A O   1 
ATOM   2062 C  CB  . LYS   A 1 282 ? 115.699 2.872  -4.015  1.00 22.17  ? 262 LYS   A CB  1 
ATOM   2063 C  CG  . LYS   A 1 282 ? 115.246 2.328  -5.346  1.00 28.05  ? 262 LYS   A CG  1 
ATOM   2064 C  CD  . LYS   A 1 282 ? 113.724 2.453  -5.484  1.00 32.73  ? 262 LYS   A CD  1 
ATOM   2065 C  CE  . LYS   A 1 282 ? 113.266 2.032  -6.851  1.00 35.94  ? 262 LYS   A CE  1 
ATOM   2066 N  NZ  . LYS   A 1 282 ? 113.242 0.552  -6.952  1.00 37.17  ? 262 LYS   A NZ  1 
ATOM   2067 N  N   . ILE   A 1 283 ? 118.814 2.316  -5.430  1.00 19.80  ? 263 ILE   A N   1 
ATOM   2068 C  CA  . ILE   A 1 283 ? 119.802 2.763  -6.405  1.00 20.04  ? 263 ILE   A CA  1 
ATOM   2069 C  C   . ILE   A 1 283 ? 119.131 2.774  -7.782  1.00 20.83  ? 263 ILE   A C   1 
ATOM   2070 O  O   . ILE   A 1 283 ? 118.468 1.798  -8.160  1.00 20.81  ? 263 ILE   A O   1 
ATOM   2071 C  CB  . ILE   A 1 283 ? 121.047 1.837  -6.419  1.00 20.74  ? 263 ILE   A CB  1 
ATOM   2072 C  CG1 . ILE   A 1 283 ? 121.846 1.940  -5.095  1.00 21.49  ? 263 ILE   A CG1 1 
ATOM   2073 C  CG2 . ILE   A 1 283 ? 121.957 2.113  -7.675  1.00 20.80  ? 263 ILE   A CG2 1 
ATOM   2074 C  CD1 . ILE   A 1 283 ? 122.666 3.284  -4.969  1.00 23.10  ? 263 ILE   A CD1 1 
ATOM   2075 N  N   . TYR   A 1 284 ? 119.337 3.858  -8.537  1.00 20.27  ? 264 TYR   A N   1 
ATOM   2076 C  CA  . TYR   A 1 284 ? 118.814 3.987  -9.902  1.00 20.39  ? 264 TYR   A CA  1 
ATOM   2077 C  C   . TYR   A 1 284 ? 119.984 3.850  -10.866 1.00 20.98  ? 264 TYR   A C   1 
ATOM   2078 O  O   . TYR   A 1 284 ? 120.842 4.739  -10.983 1.00 21.17  ? 264 TYR   A O   1 
ATOM   2079 C  CB  . TYR   A 1 284 ? 118.097 5.333  -10.078 1.00 20.34  ? 264 TYR   A CB  1 
ATOM   2080 C  CG  . TYR   A 1 284 ? 116.769 5.348  -9.360  1.00 20.77  ? 264 TYR   A CG  1 
ATOM   2081 C  CD1 . TYR   A 1 284 ? 115.631 4.819  -9.955  1.00 22.28  ? 264 TYR   A CD1 1 
ATOM   2082 C  CD2 . TYR   A 1 284 ? 116.674 5.772  -8.040  1.00 21.25  ? 264 TYR   A CD2 1 
ATOM   2083 C  CE1 . TYR   A 1 284 ? 114.411 4.804  -9.290  1.00 23.38  ? 264 TYR   A CE1 1 
ATOM   2084 C  CE2 . TYR   A 1 284 ? 115.462 5.757  -7.362  1.00 21.53  ? 264 TYR   A CE2 1 
ATOM   2085 C  CZ  . TYR   A 1 284 ? 114.329 5.286  -7.996  1.00 23.66  ? 264 TYR   A CZ  1 
ATOM   2086 O  OH  . TYR   A 1 284 ? 113.130 5.279  -7.329  1.00 25.29  ? 264 TYR   A OH  1 
ATOM   2087 N  N   . GLU   A 1 285 ? 120.052 2.683  -11.510 1.00 21.49  ? 265 GLU   A N   1 
ATOM   2088 C  CA  . GLU   A 1 285 ? 121.155 2.307  -12.363 1.00 22.41  ? 265 GLU   A CA  1 
ATOM   2089 C  C   . GLU   A 1 285 ? 121.260 3.221  -13.568 1.00 23.38  ? 265 GLU   A C   1 
ATOM   2090 O  O   . GLU   A 1 285 ? 120.326 3.306  -14.367 1.00 24.91  ? 265 GLU   A O   1 
ATOM   2091 C  CB  . GLU   A 1 285 ? 121.045 0.831  -12.774 1.00 25.45  ? 265 GLU   A CB  1 
ATOM   2092 C  CG  . GLU   A 1 285 ? 122.329 0.299  -13.377 1.00 28.74  ? 265 GLU   A CG  1 
ATOM   2093 C  CD  . GLU   A 1 285 ? 123.531 0.258  -12.451 1.00 32.69  ? 265 GLU   A CD  1 
ATOM   2094 O  OE1 . GLU   A 1 285 ? 123.373 0.352  -11.207 1.00 29.37  ? 265 GLU   A OE1 1 
ATOM   2095 O  OE2 . GLU   A 1 285 ? 124.653 0.129  -12.990 1.00 36.76  ? 265 GLU   A OE2 1 
ATOM   2096 N  N   . GLY   A 1 286 ? 122.393 3.905  -13.660 1.00 22.38  ? 266 GLY   A N   1 
ATOM   2097 C  CA  . GLY   A 1 286 ? 122.694 4.805  -14.763 1.00 22.65  ? 266 GLY   A CA  1 
ATOM   2098 C  C   . GLY   A 1 286 ? 122.161 6.225  -14.612 1.00 22.82  ? 266 GLY   A C   1 
ATOM   2099 O  O   . GLY   A 1 286 ? 122.440 7.084  -15.456 1.00 23.50  ? 266 GLY   A O   1 
ATOM   2100 N  N   . ALA   A 1 287 ? 121.361 6.474  -13.559 1.00 21.20  ? 267 ALA   A N   1 
ATOM   2101 C  CA  . ALA   A 1 287 ? 120.765 7.795  -13.370 1.00 21.12  ? 267 ALA   A CA  1 
ATOM   2102 C  C   . ALA   A 1 287 ? 121.758 8.819  -12.887 1.00 20.99  ? 267 ALA   A C   1 
ATOM   2103 O  O   . ALA   A 1 287 ? 122.750 8.489  -12.213 1.00 20.55  ? 267 ALA   A O   1 
ATOM   2104 C  CB  . ALA   A 1 287 ? 119.575 7.700  -12.435 1.00 20.49  ? 267 ALA   A CB  1 
ATOM   2105 N  N   . TYR   A 1 288 ? 121.495 10.086 -13.232 1.00 20.72  ? 268 TYR   A N   1 
ATOM   2106 C  CA  . TYR   A 1 288 ? 122.367 11.172 -12.847 1.00 20.92  ? 268 TYR   A CA  1 
ATOM   2107 C  C   . TYR   A 1 288 ? 121.966 11.744 -11.468 1.00 21.68  ? 268 TYR   A C   1 
ATOM   2108 O  O   . TYR   A 1 288 ? 121.443 11.006 -10.640 1.00 23.32  ? 268 TYR   A O   1 
ATOM   2109 C  CB  . TYR   A 1 288 ? 122.403 12.251 -13.953 1.00 21.32  ? 268 TYR   A CB  1 
ATOM   2110 C  CG  . TYR   A 1 288 ? 123.145 11.870 -15.221 1.00 22.79  ? 268 TYR   A CG  1 
ATOM   2111 C  CD1 . TYR   A 1 288 ? 123.653 10.583 -15.405 1.00 24.23  ? 268 TYR   A CD1 1 
ATOM   2112 C  CD2 . TYR   A 1 288 ? 123.330 12.793 -16.236 1.00 24.48  ? 268 TYR   A CD2 1 
ATOM   2113 C  CE1 . TYR   A 1 288 ? 124.309 10.229 -16.584 1.00 25.58  ? 268 TYR   A CE1 1 
ATOM   2114 C  CE2 . TYR   A 1 288 ? 123.973 12.449 -17.418 1.00 25.82  ? 268 TYR   A CE2 1 
ATOM   2115 C  CZ  . TYR   A 1 288 ? 124.471 11.172 -17.585 1.00 27.25  ? 268 TYR   A CZ  1 
ATOM   2116 O  OH  . TYR   A 1 288 ? 125.117 10.852 -18.764 1.00 30.19  ? 268 TYR   A OH  1 
ATOM   2117 N  N   . HIS   A 1 289 ? 122.232 13.012 -11.211 1.00 20.21  ? 269 HIS   A N   1 
ATOM   2118 C  CA  . HIS   A 1 289 ? 122.016 13.603 -9.886  1.00 19.83  ? 269 HIS   A CA  1 
ATOM   2119 C  C   . HIS   A 1 289 ? 120.587 13.950 -9.501  1.00 19.79  ? 269 HIS   A C   1 
ATOM   2120 O  O   . HIS   A 1 289 ? 120.167 13.656 -8.366  1.00 21.30  ? 269 HIS   A O   1 
ATOM   2121 C  CB  . HIS   A 1 289 ? 122.887 14.863 -9.814  1.00 20.77  ? 269 HIS   A CB  1 
ATOM   2122 C  CG  . HIS   A 1 289 ? 122.860 15.528 -8.481  1.00 20.54  ? 269 HIS   A CG  1 
ATOM   2123 N  ND1 . HIS   A 1 289 ? 123.234 14.845 -7.334  1.00 21.65  ? 269 HIS   A ND1 1 
ATOM   2124 C  CD2 . HIS   A 1 289 ? 122.574 16.815 -8.160  1.00 21.84  ? 269 HIS   A CD2 1 
ATOM   2125 C  CE1 . HIS   A 1 289 ? 123.146 15.736 -6.348  1.00 23.38  ? 269 HIS   A CE1 1 
ATOM   2126 N  NE2 . HIS   A 1 289 ? 122.757 16.925 -6.799  1.00 23.12  ? 269 HIS   A NE2 1 
ATOM   2127 N  N   . VAL   A 1 290 ? 119.860 14.644 -10.370 1.00 19.12  ? 270 VAL   A N   1 
ATOM   2128 C  CA  . VAL   A 1 290 ? 118.551 15.169 -9.994  1.00 19.55  ? 270 VAL   A CA  1 
ATOM   2129 C  C   . VAL   A 1 290 ? 117.483 14.129 -10.277 1.00 19.60  ? 270 VAL   A C   1 
ATOM   2130 O  O   . VAL   A 1 290 ? 116.786 14.203 -11.290 1.00 19.94  ? 270 VAL   A O   1 
ATOM   2131 C  CB  . VAL   A 1 290 ? 118.285 16.528 -10.681 1.00 19.99  ? 270 VAL   A CB  1 
ATOM   2132 C  CG1 . VAL   A 1 290 ? 117.021 17.165 -10.110 1.00 20.76  ? 270 VAL   A CG1 1 
ATOM   2133 C  CG2 . VAL   A 1 290 ? 119.481 17.485 -10.504 1.00 20.63  ? 270 VAL   A CG2 1 
ATOM   2134 N  N   . LEU   A 1 291 ? 117.343 13.154 -9.363  1.00 19.40  ? 271 LEU   A N   1 
ATOM   2135 C  CA  . LEU   A 1 291 ? 116.464 12.008 -9.600  1.00 19.64  ? 271 LEU   A CA  1 
ATOM   2136 C  C   . LEU   A 1 291 ? 115.002 12.337 -9.791  1.00 19.96  ? 271 LEU   A C   1 
ATOM   2137 O  O   . LEU   A 1 291 ? 114.312 11.628 -10.549 1.00 21.04  ? 271 LEU   A O   1 
ATOM   2138 C  CB  . LEU   A 1 291 ? 116.615 10.957 -8.490  1.00 19.63  ? 271 LEU   A CB  1 
ATOM   2139 C  CG  . LEU   A 1 291 ? 118.026 10.437 -8.305  1.00 20.21  ? 271 LEU   A CG  1 
ATOM   2140 C  CD1 . LEU   A 1 291 ? 118.074 9.517  -7.103  1.00 20.57  ? 271 LEU   A CD1 1 
ATOM   2141 C  CD2 . LEU   A 1 291 ? 118.478 9.596  -9.520  1.00 20.96  ? 271 LEU   A CD2 1 
ATOM   2142 N  N   . HIS   A 1 292 ? 114.528 13.419 -9.149  1.00 19.45  ? 272 HIS   A N   1 
ATOM   2143 C  CA  . HIS   A 1 292 ? 113.136 13.793 -9.294  1.00 19.45  ? 272 HIS   A CA  1 
ATOM   2144 C  C   . HIS   A 1 292 ? 112.889 14.621 -10.584 1.00 20.47  ? 272 HIS   A C   1 
ATOM   2145 O  O   . HIS   A 1 292 ? 111.770 15.081 -10.815 1.00 22.28  ? 272 HIS   A O   1 
ATOM   2146 C  CB  . HIS   A 1 292 ? 112.644 14.519 -8.041  1.00 19.55  ? 272 HIS   A CB  1 
ATOM   2147 C  CG  . HIS   A 1 292 ? 113.506 15.695 -7.682  1.00 20.75  ? 272 HIS   A CG  1 
ATOM   2148 N  ND1 . HIS   A 1 292 ? 114.815 15.522 -7.260  1.00 21.90  ? 272 HIS   A ND1 1 
ATOM   2149 C  CD2 . HIS   A 1 292 ? 113.217 17.020 -7.680  1.00 21.95  ? 272 HIS   A CD2 1 
ATOM   2150 C  CE1 . HIS   A 1 292 ? 115.286 16.739 -7.033  1.00 22.20  ? 272 HIS   A CE1 1 
ATOM   2151 N  NE2 . HIS   A 1 292 ? 114.358 17.674 -7.256  1.00 22.85  ? 272 HIS   A NE2 1 
ATOM   2152 N  N   . LYS   A 1 293 ? 113.931 14.813 -11.410 1.00 19.97  ? 273 LYS   A N   1 
ATOM   2153 C  CA  . LYS   A 1 293 ? 113.847 15.506 -12.711 1.00 20.37  ? 273 LYS   A CA  1 
ATOM   2154 C  C   . LYS   A 1 293 ? 114.701 14.740 -13.738 1.00 21.44  ? 273 LYS   A C   1 
ATOM   2155 O  O   . LYS   A 1 293 ? 115.416 15.341 -14.537 1.00 22.52  ? 273 LYS   A O   1 
ATOM   2156 C  CB  . LYS   A 1 293 ? 114.309 16.952 -12.576 1.00 21.13  ? 273 LYS   A CB  1 
ATOM   2157 C  CG  . LYS   A 1 293 ? 113.406 17.735 -11.635 1.00 20.66  ? 273 LYS   A CG  1 
ATOM   2158 C  CD  . LYS   A 1 293 ? 113.734 19.192 -11.609 1.00 24.09  ? 273 LYS   A CD  1 
ATOM   2159 C  CE  . LYS   A 1 293 ? 112.940 19.928 -10.548 1.00 26.13  ? 273 LYS   A CE  1 
ATOM   2160 N  NZ  . LYS   A 1 293 ? 111.471 19.874 -10.793 1.00 25.75  ? 273 LYS   A NZ  1 
ATOM   2161 N  N   . GLU   A 1 294 ? 114.661 13.407 -13.654 1.00 21.24  ? 274 GLU   A N   1 
ATOM   2162 C  CA  . GLU   A 1 294 ? 115.434 12.530 -14.507 1.00 21.64  ? 274 GLU   A CA  1 
ATOM   2163 C  C   . GLU   A 1 294 ? 114.550 12.011 -15.638 1.00 23.16  ? 274 GLU   A C   1 
ATOM   2164 O  O   . GLU   A 1 294 ? 113.506 12.601 -15.939 1.00 24.08  ? 274 GLU   A O   1 
ATOM   2165 C  CB  . GLU   A 1 294 ? 115.994 11.393 -13.625 1.00 22.10  ? 274 GLU   A CB  1 
ATOM   2166 C  CG  . GLU   A 1 294 ? 117.515 11.394 -13.564 1.00 23.09  ? 274 GLU   A CG  1 
ATOM   2167 C  CD  . GLU   A 1 294 ? 118.169 10.693 -14.740 1.00 25.04  ? 274 GLU   A CD  1 
ATOM   2168 O  OE1 . GLU   A 1 294 ? 117.481 9.898  -15.424 1.00 25.75  ? 274 GLU   A OE1 1 
ATOM   2169 O  OE2 . GLU   A 1 294 ? 119.368 10.951 -14.990 1.00 25.02  ? 274 GLU   A OE2 1 
ATOM   2170 N  N   . LEU   A 1 295 ? 114.952 10.923 -16.313 1.00 23.42  ? 275 LEU   A N   1 
ATOM   2171 C  CA  . LEU   A 1 295 ? 114.122 10.325 -17.361 1.00 24.90  ? 275 LEU   A CA  1 
ATOM   2172 C  C   . LEU   A 1 295 ? 112.773 9.900  -16.737 1.00 26.88  ? 275 LEU   A C   1 
ATOM   2173 O  O   . LEU   A 1 295 ? 112.734 9.552  -15.554 1.00 25.70  ? 275 LEU   A O   1 
ATOM   2174 C  CB  . LEU   A 1 295 ? 114.841 9.094  -17.920 1.00 25.58  ? 275 LEU   A CB  1 
ATOM   2175 C  CG  . LEU   A 1 295 ? 116.190 9.330  -18.589 1.00 27.50  ? 275 LEU   A CG  1 
ATOM   2176 C  CD1 . LEU   A 1 295 ? 116.735 8.008  -19.164 1.00 28.47  ? 275 LEU   A CD1 1 
ATOM   2177 C  CD2 . LEU   A 1 295 ? 116.093 10.345 -19.726 1.00 28.42  ? 275 LEU   A CD2 1 
ATOM   2178 N  N   . PRO   A 1 296 ? 111.659 9.996  -17.476 1.00 29.95  ? 276 PRO   A N   1 
ATOM   2179 C  CA  . PRO   A 1 296 ? 110.350 9.650  -16.889 1.00 31.27  ? 276 PRO   A CA  1 
ATOM   2180 C  C   . PRO   A 1 296 ? 110.274 8.340  -16.129 1.00 31.83  ? 276 PRO   A C   1 
ATOM   2181 O  O   . PRO   A 1 296 ? 109.657 8.312  -15.072 1.00 32.59  ? 276 PRO   A O   1 
ATOM   2182 C  CB  . PRO   A 1 296 ? 109.398 9.642  -18.094 1.00 32.97  ? 276 PRO   A CB  1 
ATOM   2183 C  CG  . PRO   A 1 296 ? 110.279 9.784  -19.308 1.00 33.72  ? 276 PRO   A CG  1 
ATOM   2184 C  CD  . PRO   A 1 296 ? 111.524 10.452 -18.878 1.00 30.94  ? 276 PRO   A CD  1 
ATOM   2185 N  N   . GLU   A 1 297 ? 110.945 7.280  -16.595 1.00 30.63  ? 277 GLU   A N   1 
ATOM   2186 C  CA  . GLU   A 1 297 ? 110.923 5.994  -15.898 1.00 30.59  ? 277 GLU   A CA  1 
ATOM   2187 C  C   . GLU   A 1 297 ? 111.511 6.135  -14.476 1.00 29.43  ? 277 GLU   A C   1 
ATOM   2188 O  O   . GLU   A 1 297 ? 110.999 5.542  -13.525 1.00 30.85  ? 277 GLU   A O   1 
ATOM   2189 C  CB  . GLU   A 1 297 ? 111.675 4.938  -16.715 1.00 34.21  ? 277 GLU   A CB  1 
ATOM   2190 C  CG  . GLU   A 1 297 ? 111.036 4.711  -18.081 1.00 41.86  ? 277 GLU   A CG  1 
ATOM   2191 C  CD  . GLU   A 1 297 ? 111.561 5.531  -19.253 1.00 49.07  ? 277 GLU   A CD  1 
ATOM   2192 O  OE1 . GLU   A 1 297 ? 112.118 6.637  -19.043 1.00 44.82  ? 277 GLU   A OE1 1 
ATOM   2193 O  OE2 . GLU   A 1 297 ? 111.395 5.058  -20.402 1.00 54.17  ? 277 GLU   A OE2 1 
ATOM   2194 N  N   . VAL   A 1 298 ? 112.571 6.930  -14.341 1.00 26.48  ? 278 VAL   A N   1 
ATOM   2195 C  CA  . VAL   A 1 298 ? 113.195 7.164  -13.052 1.00 25.76  ? 278 VAL   A CA  1 
ATOM   2196 C  C   . VAL   A 1 298 ? 112.320 8.088  -12.204 1.00 25.12  ? 278 VAL   A C   1 
ATOM   2197 O  O   . VAL   A 1 298 ? 111.995 7.744  -11.070 1.00 24.97  ? 278 VAL   A O   1 
ATOM   2198 C  CB  . VAL   A 1 298 ? 114.623 7.725  -13.222 1.00 25.56  ? 278 VAL   A CB  1 
ATOM   2199 C  CG1 . VAL   A 1 298 ? 115.193 8.189  -11.880 1.00 25.02  ? 278 VAL   A CG1 1 
ATOM   2200 C  CG2 . VAL   A 1 298 ? 115.527 6.682  -13.871 1.00 26.15  ? 278 VAL   A CG2 1 
ATOM   2201 N  N   . THR   A 1 299 ? 111.914 9.242  -12.751 1.00 24.68  ? 279 THR   A N   1 
ATOM   2202 C  CA  . THR   A 1 299 ? 111.114 10.202 -11.998 1.00 25.20  ? 279 THR   A CA  1 
ATOM   2203 C  C   . THR   A 1 299 ? 109.800 9.600  -11.513 1.00 24.82  ? 279 THR   A C   1 
ATOM   2204 O  O   . THR   A 1 299 ? 109.461 9.760  -10.345 1.00 24.58  ? 279 THR   A O   1 
ATOM   2205 C  CB  . THR   A 1 299 ? 110.896 11.444 -12.832 1.00 27.93  ? 279 THR   A CB  1 
ATOM   2206 O  OG1 . THR   A 1 299 ? 112.187 11.972 -13.121 1.00 30.25  ? 279 THR   A OG1 1 
ATOM   2207 C  CG2 . THR   A 1 299 ? 110.029 12.469 -12.130 1.00 28.46  ? 279 THR   A CG2 1 
ATOM   2208 N  N   . ASN   A 1 300 ? 109.110 8.834  -12.366 1.00 24.99  ? 280 ASN   A N   1 
ATOM   2209 C  CA  . ASN   A 1 300 ? 107.857 8.190  -11.945 1.00 25.64  ? 280 ASN   A CA  1 
ATOM   2210 C  C   . ASN   A 1 300 ? 108.085 7.236  -10.767 1.00 24.65  ? 280 ASN   A C   1 
ATOM   2211 O  O   . ASN   A 1 300 ? 107.299 7.230  -9.819  1.00 25.31  ? 280 ASN   A O   1 
ATOM   2212 C  CB  . ASN   A 1 300 ? 107.176 7.466  -13.106 1.00 27.41  ? 280 ASN   A CB  1 
ATOM   2213 C  CG  . ASN   A 1 300 ? 106.709 8.397  -14.196 1.00 32.00  ? 280 ASN   A CG  1 
ATOM   2214 O  OD1 . ASN   A 1 300 ? 106.601 9.614  -14.008 1.00 33.20  ? 280 ASN   A OD1 1 
ATOM   2215 N  ND2 . ASN   A 1 300 ? 106.457 7.839  -15.380 1.00 34.16  ? 280 ASN   A ND2 1 
ATOM   2216 N  N   . SER   A 1 301 ? 109.193 6.495  -10.798 1.00 23.38  ? 281 SER   A N   1 
ATOM   2217 C  CA  . SER   A 1 301 ? 109.546 5.573  -9.719  1.00 23.44  ? 281 SER   A CA  1 
ATOM   2218 C  C   . SER   A 1 301 ? 109.882 6.351  -8.452  1.00 23.21  ? 281 SER   A C   1 
ATOM   2219 O  O   . SER   A 1 301 ? 109.439 5.989  -7.378  1.00 23.18  ? 281 SER   A O   1 
ATOM   2220 C  CB  . SER   A 1 301 ? 110.733 4.701  -10.122 1.00 24.36  ? 281 SER   A CB  1 
ATOM   2221 O  OG  . SER   A 1 301 ? 111.205 3.978  -8.993  1.00 25.69  ? 281 SER   A OG  1 
ATOM   2222 N  N   . VAL   A 1 302 ? 110.653 7.427  -8.563  1.00 22.52  ? 282 VAL   A N   1 
ATOM   2223 C  CA  . VAL   A 1 302 ? 111.019 8.263  -7.416  1.00 22.28  ? 282 VAL   A CA  1 
ATOM   2224 C  C   . VAL   A 1 302 ? 109.766 8.782  -6.715  1.00 22.65  ? 282 VAL   A C   1 
ATOM   2225 O  O   . VAL   A 1 302 ? 109.663 8.660  -5.492  1.00 23.00  ? 282 VAL   A O   1 
ATOM   2226 C  CB  . VAL   A 1 302 ? 111.955 9.412  -7.852  1.00 22.19  ? 282 VAL   A CB  1 
ATOM   2227 C  CG1 . VAL   A 1 302 ? 112.049 10.500 -6.767  1.00 22.30  ? 282 VAL   A CG1 1 
ATOM   2228 C  CG2 . VAL   A 1 302 ? 113.336 8.862  -8.212  1.00 22.11  ? 282 VAL   A CG2 1 
ATOM   2229 N  N   . PHE   A 1 303 ? 108.794 9.309  -7.494  1.00 22.18  ? 283 PHE   A N   1 
ATOM   2230 C  CA  . PHE   A 1 303 ? 107.557 9.828  -6.899  1.00 22.38  ? 283 PHE   A CA  1 
ATOM   2231 C  C   . PHE   A 1 303 ? 106.779 8.685  -6.248  1.00 23.08  ? 283 PHE   A C   1 
ATOM   2232 O  O   . PHE   A 1 303 ? 106.289 8.857  -5.139  1.00 23.93  ? 283 PHE   A O   1 
ATOM   2233 C  CB  . PHE   A 1 303 ? 106.655 10.512 -7.943  1.00 22.47  ? 283 PHE   A CB  1 
ATOM   2234 C  CG  . PHE   A 1 303 ? 106.979 11.971 -8.186  1.00 23.24  ? 283 PHE   A CG  1 
ATOM   2235 C  CD1 . PHE   A 1 303 ? 108.234 12.355 -8.621  1.00 23.99  ? 283 PHE   A CD1 1 
ATOM   2236 C  CD2 . PHE   A 1 303 ? 106.015 12.950 -8.011  1.00 23.97  ? 283 PHE   A CD2 1 
ATOM   2237 C  CE1 . PHE   A 1 303 ? 108.516 13.706 -8.897  1.00 24.55  ? 283 PHE   A CE1 1 
ATOM   2238 C  CE2 . PHE   A 1 303 ? 106.297 14.290 -8.267  1.00 24.70  ? 283 PHE   A CE2 1 
ATOM   2239 C  CZ  . PHE   A 1 303 ? 107.545 14.665 -8.699  1.00 24.14  ? 283 PHE   A CZ  1 
ATOM   2240 N  N   . HIS   A 1 304 ? 106.687 7.526  -6.925  1.00 22.20  ? 284 HIS   A N   1 
ATOM   2241 C  CA  . HIS   A 1 304 ? 105.953 6.378  -6.383  1.00 23.04  ? 284 HIS   A CA  1 
ATOM   2242 C  C   . HIS   A 1 304 ? 106.570 5.886  -5.063  1.00 23.55  ? 284 HIS   A C   1 
ATOM   2243 O  O   . HIS   A 1 304 ? 105.837 5.613  -4.112  1.00 24.76  ? 284 HIS   A O   1 
ATOM   2244 C  CB  . HIS   A 1 304 ? 105.938 5.237  -7.413  1.00 24.63  ? 284 HIS   A CB  1 
ATOM   2245 C  CG  . HIS   A 1 304 ? 105.257 4.000  -6.909  1.00 29.79  ? 284 HIS   A CG  1 
ATOM   2246 N  ND1 . HIS   A 1 304 ? 103.897 3.984  -6.648  1.00 33.25  ? 284 HIS   A ND1 1 
ATOM   2247 C  CD2 . HIS   A 1 304 ? 105.773 2.778  -6.634  1.00 32.32  ? 284 HIS   A CD2 1 
ATOM   2248 C  CE1 . HIS   A 1 304 ? 103.619 2.751  -6.246  1.00 34.28  ? 284 HIS   A CE1 1 
ATOM   2249 N  NE2 . HIS   A 1 304 ? 104.718 1.983  -6.223  1.00 34.13  ? 284 HIS   A NE2 1 
ATOM   2250 N  N   . GLU   A 1 305 ? 107.904 5.765  -5.007  1.00 23.09  ? 285 GLU   A N   1 
ATOM   2251 C  CA  . GLU   A 1 305 ? 108.600 5.264  -3.826  1.00 23.73  ? 285 GLU   A CA  1 
ATOM   2252 C  C   . GLU   A 1 305 ? 108.462 6.191  -2.633  1.00 23.27  ? 285 GLU   A C   1 
ATOM   2253 O  O   . GLU   A 1 305 ? 108.221 5.730  -1.515  1.00 23.49  ? 285 GLU   A O   1 
ATOM   2254 C  CB  . GLU   A 1 305 ? 110.069 4.930  -4.134  1.00 25.43  ? 285 GLU   A CB  1 
ATOM   2255 C  CG  . GLU   A 1 305 ? 110.212 3.818  -5.168  1.00 28.60  ? 285 GLU   A CG  1 
ATOM   2256 C  CD  . GLU   A 1 305 ? 109.633 2.476  -4.734  1.00 36.52  ? 285 GLU   A CD  1 
ATOM   2257 O  OE1 . GLU   A 1 305 ? 109.580 2.222  -3.509  1.00 36.63  ? 285 GLU   A OE1 1 
ATOM   2258 O  OE2 . GLU   A 1 305 ? 109.228 1.680  -5.615  1.00 38.21  ? 285 GLU   A OE2 1 
ATOM   2259 N  N   . ILE   A 1 306 ? 108.553 7.506  -2.873  1.00 21.89  ? 286 ILE   A N   1 
ATOM   2260 C  CA  . ILE   A 1 306 ? 108.373 8.460  -1.789  1.00 22.38  ? 286 ILE   A CA  1 
ATOM   2261 C  C   . ILE   A 1 306 ? 106.920 8.428  -1.310  1.00 23.25  ? 286 ILE   A C   1 
ATOM   2262 O  O   . ILE   A 1 306 ? 106.661 8.432  -0.104  1.00 24.29  ? 286 ILE   A O   1 
ATOM   2263 C  CB  . ILE   A 1 306 ? 108.781 9.865  -2.260  1.00 22.83  ? 286 ILE   A CB  1 
ATOM   2264 C  CG1 . ILE   A 1 306 ? 110.278 9.899  -2.575  1.00 22.54  ? 286 ILE   A CG1 1 
ATOM   2265 C  CG2 . ILE   A 1 306 ? 108.407 10.896 -1.190  1.00 23.95  ? 286 ILE   A CG2 1 
ATOM   2266 C  CD1 . ILE   A 1 306 ? 110.657 11.270 -3.304  1.00 23.78  ? 286 ILE   A CD1 1 
ATOM   2267 N  N   . ASN   A 1 307 ? 105.963 8.333  -2.247  1.00 23.57  ? 287 ASN   A N   1 
ATOM   2268 C  CA  . ASN   A 1 307 ? 104.544 8.240  -1.897  1.00 25.06  ? 287 ASN   A CA  1 
ATOM   2269 C  C   . ASN   A 1 307 ? 104.305 7.013  -0.979  1.00 25.91  ? 287 ASN   A C   1 
ATOM   2270 O  O   . ASN   A 1 307 ? 103.707 7.170  0.085   1.00 27.17  ? 287 ASN   A O   1 
ATOM   2271 C  CB  . ASN   A 1 307 ? 103.713 8.107  -3.184  1.00 27.08  ? 287 ASN   A CB  1 
ATOM   2272 C  CG  . ASN   A 1 307 ? 102.208 8.008  -2.995  1.00 31.96  ? 287 ASN   A CG  1 
ATOM   2273 O  OD1 . ASN   A 1 307 ? 101.701 7.353  -2.091  1.00 32.61  ? 287 ASN   A OD1 1 
ATOM   2274 N  ND2 . ASN   A 1 307 ? 101.469 8.634  -3.900  1.00 33.73  ? 287 ASN   A ND2 1 
ATOM   2275 N  N   . MET   A 1 308 ? 104.810 5.829  -1.370  1.00 25.78  ? 288 MET   A N   1 
ATOM   2276 C  CA  . MET   A 1 308 ? 104.620 4.608  -0.573  1.00 26.56  ? 288 MET   A CA  1 
ATOM   2277 C  C   . MET   A 1 308 ? 105.284 4.716  0.791   1.00 26.92  ? 288 MET   A C   1 
ATOM   2278 O  O   . MET   A 1 308 ? 104.686 4.327  1.802   1.00 28.14  ? 288 MET   A O   1 
ATOM   2279 C  CB  . MET   A 1 308 ? 105.200 3.381  -1.294  1.00 27.65  ? 288 MET   A CB  1 
ATOM   2280 C  CG  . MET   A 1 308 ? 104.619 3.135  -2.645  1.00 31.87  ? 288 MET   A CG  1 
ATOM   2281 S  SD  . MET   A 1 308 ? 102.994 2.385  -2.592  1.00 43.68  ? 288 MET   A SD  1 
ATOM   2282 C  CE  . MET   A 1 308 ? 101.948 3.824  -2.905  1.00 40.97  ? 288 MET   A CE  1 
ATOM   2283 N  N   . TRP   A 1 309 ? 106.522 5.249  0.822   1.00 25.61  ? 289 TRP   A N   1 
ATOM   2284 C  CA  . TRP   A 1 309 ? 107.292 5.325  2.057   1.00 24.87  ? 289 TRP   A CA  1 
ATOM   2285 C  C   . TRP   A 1 309 ? 106.644 6.259  3.080   1.00 25.30  ? 289 TRP   A C   1 
ATOM   2286 O  O   . TRP   A 1 309 ? 106.528 5.911  4.256   1.00 25.63  ? 289 TRP   A O   1 
ATOM   2287 C  CB  . TRP   A 1 309 ? 108.736 5.737  1.734   1.00 23.49  ? 289 TRP   A CB  1 
ATOM   2288 C  CG  . TRP   A 1 309 ? 109.697 5.543  2.861   1.00 22.22  ? 289 TRP   A CG  1 
ATOM   2289 C  CD1 . TRP   A 1 309 ? 110.454 4.435  3.114   1.00 22.83  ? 289 TRP   A CD1 1 
ATOM   2290 C  CD2 . TRP   A 1 309 ? 109.993 6.486  3.905   1.00 21.51  ? 289 TRP   A CD2 1 
ATOM   2291 N  NE1 . TRP   A 1 309 ? 111.209 4.628  4.244   1.00 23.24  ? 289 TRP   A NE1 1 
ATOM   2292 C  CE2 . TRP   A 1 309 ? 110.966 5.892  4.737   1.00 22.59  ? 289 TRP   A CE2 1 
ATOM   2293 C  CE3 . TRP   A 1 309 ? 109.558 7.791  4.193   1.00 21.60  ? 289 TRP   A CE3 1 
ATOM   2294 C  CZ2 . TRP   A 1 309 ? 111.464 6.529  5.874   1.00 22.72  ? 289 TRP   A CZ2 1 
ATOM   2295 C  CZ3 . TRP   A 1 309 ? 110.086 8.438  5.298   1.00 21.84  ? 289 TRP   A CZ3 1 
ATOM   2296 C  CH2 . TRP   A 1 309 ? 111.006 7.798  6.141   1.00 22.51  ? 289 TRP   A CH2 1 
ATOM   2297 N  N   . VAL   A 1 310 ? 106.207 7.442  2.632   1.00 25.11  ? 290 VAL   A N   1 
ATOM   2298 C  CA  . VAL   A 1 310 ? 105.533 8.389  3.522   1.00 26.32  ? 290 VAL   A CA  1 
ATOM   2299 C  C   . VAL   A 1 310 ? 104.127 7.886  3.882   1.00 28.38  ? 290 VAL   A C   1 
ATOM   2300 O  O   . VAL   A 1 310 ? 103.737 7.972  5.049   1.00 28.95  ? 290 VAL   A O   1 
ATOM   2301 C  CB  . VAL   A 1 310 ? 105.517 9.800  2.882   1.00 26.48  ? 290 VAL   A CB  1 
ATOM   2302 C  CG1 . VAL   A 1 310 ? 104.667 10.767 3.707   1.00 27.64  ? 290 VAL   A CG1 1 
ATOM   2303 C  CG2 . VAL   A 1 310 ? 106.942 10.327 2.713   1.00 26.09  ? 290 VAL   A CG2 1 
ATOM   2304 N  N   . SER   A 1 311 ? 103.409 7.260  2.929   1.00 29.44  ? 291 SER   A N   1 
ATOM   2305 C  CA  . SER   A 1 311 ? 102.070 6.729  3.211   1.00 31.20  ? 291 SER   A CA  1 
ATOM   2306 C  C   . SER   A 1 311 ? 102.139 5.642  4.296   1.00 32.30  ? 291 SER   A C   1 
ATOM   2307 O  O   . SER   A 1 311 ? 101.304 5.624  5.200   1.00 33.57  ? 291 SER   A O   1 
ATOM   2308 C  CB  . SER   A 1 311 ? 101.426 6.153  1.950   1.00 33.96  ? 291 SER   A CB  1 
ATOM   2309 O  OG  . SER   A 1 311 ? 101.200 7.174  0.990   1.00 37.80  ? 291 SER   A OG  1 
ATOM   2310 N  N   . GLN   A 1 312 ? 103.153 4.777  4.234   1.00 31.92  ? 292 GLN   A N   1 
ATOM   2311 C  CA  . GLN   A 1 312 ? 103.326 3.716  5.226   1.00 32.02  ? 292 GLN   A CA  1 
ATOM   2312 C  C   . GLN   A 1 312 ? 103.636 4.280  6.623   1.00 32.68  ? 292 GLN   A C   1 
ATOM   2313 O  O   . GLN   A 1 312 ? 103.298 3.656  7.621   1.00 35.17  ? 292 GLN   A O   1 
ATOM   2314 C  CB  . GLN   A 1 312 ? 104.439 2.734  4.795   1.00 33.41  ? 292 GLN   A CB  1 
ATOM   2315 C  CG  . GLN   A 1 312 ? 104.045 1.806  3.630   1.00 37.54  ? 292 GLN   A CG  1 
ATOM   2316 C  CD  . GLN   A 1 312 ? 105.242 1.211  2.902   1.00 45.22  ? 292 GLN   A CD  1 
ATOM   2317 O  OE1 . GLN   A 1 312 ? 106.358 1.129  3.435   1.00 49.52  ? 292 GLN   A OE1 1 
ATOM   2318 N  NE2 . GLN   A 1 312 ? 105.048 0.797  1.652   1.00 45.44  ? 292 GLN   A NE2 1 
ATOM   2319 N  N   . ARG   A 1 313 ? 104.268 5.447  6.696   1.00 30.54  ? 293 ARG   A N   1 
ATOM   2320 C  CA  . ARG   A 1 313 ? 104.674 6.041  7.956   1.00 30.24  ? 293 ARG   A CA  1 
ATOM   2321 C  C   . ARG   A 1 313 ? 103.764 7.179  8.451   1.00 33.03  ? 293 ARG   A C   1 
ATOM   2322 O  O   . ARG   A 1 313 ? 104.109 7.853  9.413   1.00 32.72  ? 293 ARG   A O   1 
ATOM   2323 C  CB  . ARG   A 1 313 ? 106.134 6.492  7.839   1.00 28.86  ? 293 ARG   A CB  1 
ATOM   2324 C  CG  . ARG   A 1 313 ? 107.033 5.262  7.807   1.00 28.35  ? 293 ARG   A CG  1 
ATOM   2325 C  CD  . ARG   A 1 313 ? 108.406 5.523  7.237   1.00 28.76  ? 293 ARG   A CD  1 
ATOM   2326 N  NE  . ARG   A 1 313 ? 109.204 4.290  7.132   1.00 27.99  ? 293 ARG   A NE  1 
ATOM   2327 C  CZ  . ARG   A 1 313 ? 109.062 3.380  6.171   1.00 27.35  ? 293 ARG   A CZ  1 
ATOM   2328 N  NH1 . ARG   A 1 313 ? 108.146 3.543  5.221   1.00 27.13  ? 293 ARG   A NH1 1 
ATOM   2329 N  NH2 . ARG   A 1 313 ? 109.824 2.285  6.162   1.00 25.82  ? 293 ARG   A NH2 1 
ATOM   2330 N  N   . THR   A 1 314 ? 102.601 7.372  7.800   1.00 35.52  ? 294 THR   A N   1 
ATOM   2331 C  CA  . THR   A 1 314 ? 101.581 8.367  8.170   1.00 38.61  ? 294 THR   A CA  1 
ATOM   2332 C  C   . THR   A 1 314 ? 100.190 7.731  8.377   1.00 43.12  ? 294 THR   A C   1 
ATOM   2333 O  O   . THR   A 1 314 ? 99.276  8.414  8.860   1.00 44.84  ? 294 THR   A O   1 
ATOM   2334 C  CB  . THR   A 1 314 ? 101.523 9.519  7.144   1.00 38.65  ? 294 THR   A CB  1 
ATOM   2335 O  OG1 . THR   A 1 314 ? 101.429 8.974  5.824   1.00 39.24  ? 294 THR   A OG1 1 
ATOM   2336 C  CG2 . THR   A 1 314 ? 102.726 10.427 7.226   1.00 38.11  ? 294 THR   A CG2 1 
ATOM   2337 N  N   . ALA   A 1 315 ? 100.028 6.439  8.032   1.00 45.21  ? 295 ALA   A N   1 
ATOM   2338 C  CA  . ALA   A 1 315 ? 98.790  5.673  8.195   1.00 47.79  ? 295 ALA   A CA  1 
ATOM   2339 C  C   . ALA   A 1 315 ? 98.403  5.546  9.676   1.00 49.84  ? 295 ALA   A C   1 
ATOM   2340 O  O   . ALA   A 1 315 ? 97.914  6.509  10.273  1.00 50.90  ? 295 ALA   A O   1 
ATOM   2341 C  CB  . ALA   A 1 315 ? 98.957  4.283  7.584   1.00 48.23  ? 295 ALA   A CB  1 
HETATM 2342 C  C8  . A1IA2 B 2 .   ? 118.922 20.763 -8.918  1.00 29.94  ? 401 A1IA2 A C8  1 
HETATM 2343 C  C9  . A1IA2 B 2 .   ? 119.631 21.674 -9.884  1.00 31.45  ? 401 A1IA2 A C9  1 
HETATM 2344 C  C1  . A1IA2 B 2 .   ? 121.136 20.421 -7.757  1.00 30.92  ? 401 A1IA2 A C1  1 
HETATM 2345 C  C6  . A1IA2 B 2 .   ? 121.618 20.735 -6.337  1.00 30.85  ? 401 A1IA2 A C6  1 
HETATM 2346 C  C4  . A1IA2 B 2 .   ? 123.708 21.768 -7.212  1.00 31.37  ? 401 A1IA2 A C4  1 
HETATM 2347 C  C3  . A1IA2 B 2 .   ? 123.163 21.610 -8.631  1.00 31.67  ? 401 A1IA2 A C3  1 
HETATM 2348 C  C2  . A1IA2 B 2 .   ? 121.647 21.568 -8.630  1.00 31.72  ? 401 A1IA2 A C2  1 
HETATM 2349 N  N5  . A1IA2 B 2 .   ? 123.084 20.809 -6.279  1.00 30.39  ? 401 A1IA2 A N5  1 
HETATM 2350 N  N7  . A1IA2 B 2 .   ? 119.684 20.257 -7.944  1.00 30.02  ? 401 A1IA2 A N7  1 
HETATM 2351 O  O10 . A1IA2 B 2 .   ? 121.052 21.477 -9.929  1.00 32.57  ? 401 A1IA2 A O10 1 
HETATM 2352 O  O13 . A1IA2 B 2 .   ? 117.738 20.469 -9.063  1.00 28.36  ? 401 A1IA2 A O13 1 
HETATM 2353 C  C14 . A1IA2 B 2 .   ? 123.682 20.711 -5.028  1.00 29.06  ? 401 A1IA2 A C14 1 
HETATM 2354 N  N15 . A1IA2 B 2 .   ? 124.980 20.292 -5.052  1.00 29.98  ? 401 A1IA2 A N15 1 
HETATM 2355 O  O16 . A1IA2 B 2 .   ? 123.103 20.926 -3.970  1.00 26.33  ? 401 A1IA2 A O16 1 
HETATM 2356 C  C17 . A1IA2 B 2 .   ? 125.793 20.451 -3.839  1.00 30.55  ? 401 A1IA2 A C17 1 
HETATM 2357 C  C18 . A1IA2 B 2 .   ? 127.222 20.851 -4.188  1.00 31.01  ? 401 A1IA2 A C18 1 
HETATM 2358 C  C19 . A1IA2 B 2 .   ? 127.865 19.869 -5.170  1.00 32.19  ? 401 A1IA2 A C19 1 
HETATM 2359 C  C20 . A1IA2 B 2 .   ? 126.959 19.692 -6.385  1.00 31.47  ? 401 A1IA2 A C20 1 
HETATM 2360 C  C21 . A1IA2 B 2 .   ? 125.548 19.290 -5.966  1.00 30.63  ? 401 A1IA2 A C21 1 
HETATM 2361 C  C22 . A1IA2 B 2 .   ? 129.277 20.308 -5.574  1.00 34.26  ? 401 A1IA2 A C22 1 
HETATM 2362 C  C23 . A1IA2 B 2 .   ? 130.277 20.269 -4.447  1.00 36.33  ? 401 A1IA2 A C23 1 
HETATM 2363 C  C24 . A1IA2 B 2 .   ? 130.194 19.301 -3.457  1.00 37.45  ? 401 A1IA2 A C24 1 
HETATM 2364 C  C25 . A1IA2 B 2 .   ? 131.061 19.308 -2.383  1.00 38.55  ? 401 A1IA2 A C25 1 
HETATM 2365 C  C26 . A1IA2 B 2 .   ? 132.061 20.263 -2.288  1.00 39.66  ? 401 A1IA2 A C26 1 
HETATM 2366 C  C27 . A1IA2 B 2 .   ? 132.136 21.240 -3.269  1.00 38.45  ? 401 A1IA2 A C27 1 
HETATM 2367 C  C28 . A1IA2 B 2 .   ? 131.261 21.236 -4.337  1.00 37.51  ? 401 A1IA2 A C28 1 
HETATM 2368 C  C29 . A1IA2 B 2 .   ? 133.121 20.152 -1.247  1.00 41.98  ? 401 A1IA2 A C29 1 
HETATM 2369 F  F30 . A1IA2 B 2 .   ? 134.129 19.359 -1.635  1.00 42.67  ? 401 A1IA2 A F30 1 
HETATM 2370 F  F31 . A1IA2 B 2 .   ? 133.652 21.333 -0.939  1.00 43.24  ? 401 A1IA2 A F31 1 
HETATM 2371 F  F32 . A1IA2 B 2 .   ? 132.668 19.636 -0.114  1.00 41.92  ? 401 A1IA2 A F32 1 
HETATM 2372 NA NA  . NA    C 3 .   ? 115.806 38.330 16.111  1.00 55.19  1 402 NA    A NA  1 
HETATM 2373 NA NA  . NA    D 3 .   ? 97.449  19.879 15.280  1.00 73.85  1 403 NA    A NA  1 
HETATM 2374 C  C1  . EDO   E 4 .   ? 109.547 28.584 -10.141 1.00 73.06  ? 404 EDO   A C1  1 
HETATM 2375 O  O1  . EDO   E 4 .   ? 108.713 28.755 -9.016  1.00 73.01  ? 404 EDO   A O1  1 
HETATM 2376 C  C2  . EDO   E 4 .   ? 109.548 27.109 -10.572 1.00 73.18  ? 404 EDO   A C2  1 
HETATM 2377 O  O2  . EDO   E 4 .   ? 110.520 26.924 -11.583 1.00 73.31  ? 404 EDO   A O2  1 
HETATM 2378 C  C1  . EDO   F 4 .   ? 118.810 33.875 -7.325  1.00 46.69  ? 405 EDO   A C1  1 
HETATM 2379 O  O1  . EDO   F 4 .   ? 118.685 35.255 -7.056  1.00 46.59  ? 405 EDO   A O1  1 
HETATM 2380 C  C2  . EDO   F 4 .   ? 119.624 33.677 -8.620  1.00 47.28  ? 405 EDO   A C2  1 
HETATM 2381 O  O2  . EDO   F 4 .   ? 120.927 34.199 -8.463  1.00 47.60  ? 405 EDO   A O2  1 
HETATM 2382 O  O   . HOH   G 5 .   ? 111.922 55.984 9.962   1.00 46.55  ? 501 HOH   A O   1 
HETATM 2383 O  O   . HOH   G 5 .   ? 111.754 51.034 10.173  1.00 55.39  ? 502 HOH   A O   1 
HETATM 2384 O  O   . HOH   G 5 .   ? 130.885 16.857 -5.902  1.00 38.65  ? 503 HOH   A O   1 
HETATM 2385 O  O   . HOH   G 5 .   ? 103.250 19.586 15.145  1.00 44.05  ? 504 HOH   A O   1 
HETATM 2386 O  O   . HOH   G 5 .   ? 116.624 -2.402 12.238  1.00 35.56  ? 505 HOH   A O   1 
HETATM 2387 O  O   . HOH   G 5 .   ? 108.446 6.944  10.565  1.00 36.06  ? 506 HOH   A O   1 
HETATM 2388 O  O   . HOH   G 5 .   ? 116.273 43.022 0.630   1.00 39.23  ? 507 HOH   A O   1 
HETATM 2389 O  O   . HOH   G 5 .   ? 111.815 30.626 -11.466 1.00 40.39  ? 508 HOH   A O   1 
HETATM 2390 O  O   . HOH   G 5 .   ? 99.480  6.170  -1.632  1.00 59.31  ? 509 HOH   A O   1 
HETATM 2391 O  O   . HOH   G 5 .   ? 125.394 -0.703 9.451   1.00 28.82  ? 510 HOH   A O   1 
HETATM 2392 O  O   . HOH   G 5 .   ? 123.760 34.755 1.769   1.00 27.52  ? 511 HOH   A O   1 
HETATM 2393 O  O   . HOH   G 5 .   ? 120.111 1.444  16.258  1.00 37.00  ? 512 HOH   A O   1 
HETATM 2394 O  O   . HOH   G 5 .   ? 116.796 31.507 12.335  1.00 21.09  ? 513 HOH   A O   1 
HETATM 2395 O  O   . HOH   G 5 .   ? 120.492 12.204 -22.163 1.00 38.56  ? 514 HOH   A O   1 
HETATM 2396 O  O   . HOH   G 5 .   ? 120.660 24.176 -21.900 1.00 42.94  ? 515 HOH   A O   1 
HETATM 2397 O  O   . HOH   G 5 .   ? 125.625 13.017 -12.678 1.00 25.49  ? 516 HOH   A O   1 
HETATM 2398 O  O   . HOH   G 5 .   ? 131.469 31.881 4.527   1.00 42.72  ? 517 HOH   A O   1 
HETATM 2399 O  O   . HOH   G 5 .   ? 106.926 0.257  5.815   1.00 40.34  ? 518 HOH   A O   1 
HETATM 2400 O  O   . HOH   G 5 .   ? 109.464 2.104  -8.171  1.00 33.70  ? 519 HOH   A O   1 
HETATM 2401 O  O   . HOH   G 5 .   ? 97.787  17.399 -4.827  1.00 42.99  ? 520 HOH   A O   1 
HETATM 2402 O  O   . HOH   G 5 .   ? 118.279 32.114 -16.447 1.00 39.06  ? 521 HOH   A O   1 
HETATM 2403 O  O   . HOH   G 5 .   ? 122.899 34.593 7.977   1.00 36.15  ? 522 HOH   A O   1 
HETATM 2404 O  O   . HOH   G 5 .   ? 115.364 20.246 -8.016  1.00 30.93  ? 523 HOH   A O   1 
HETATM 2405 O  O   . HOH   G 5 .   ? 97.244  9.550  10.049  1.00 57.19  ? 524 HOH   A O   1 
HETATM 2406 O  O   . HOH   G 5 .   ? 118.015 4.482  -14.757 1.00 42.57  ? 525 HOH   A O   1 
HETATM 2407 O  O   . HOH   G 5 .   ? 114.404 -2.759 14.844  1.00 50.53  ? 526 HOH   A O   1 
HETATM 2408 O  O   . HOH   G 5 .   ? 107.743 14.173 14.424  1.00 30.28  ? 527 HOH   A O   1 
HETATM 2409 O  O   . HOH   G 5 .   ? 109.506 4.281  10.889  1.00 35.29  ? 528 HOH   A O   1 
HETATM 2410 O  O   . HOH   G 5 .   ? 122.154 15.666 -19.838 1.00 35.35  ? 529 HOH   A O   1 
HETATM 2411 O  O   . HOH   G 5 .   ? 100.564 18.341 -9.605  1.00 73.07  ? 530 HOH   A O   1 
HETATM 2412 O  O   . HOH   G 5 .   ? 125.199 12.587 -20.751 1.00 45.42  ? 531 HOH   A O   1 
HETATM 2413 O  O   . HOH   G 5 .   ? 124.165 6.523  -17.379 1.00 30.56  ? 532 HOH   A O   1 
HETATM 2414 O  O   . HOH   G 5 .   ? 116.030 0.794  -8.367  1.00 22.09  ? 533 HOH   A O   1 
HETATM 2415 O  O   . HOH   G 5 .   ? 131.366 32.974 -8.622  1.00 50.03  ? 534 HOH   A O   1 
HETATM 2416 O  O   . HOH   G 5 .   ? 128.096 8.361  -8.209  1.00 31.33  ? 535 HOH   A O   1 
HETATM 2417 O  O   . HOH   G 5 .   ? 132.457 28.625 9.471   1.00 40.26  ? 536 HOH   A O   1 
HETATM 2418 O  O   . HOH   G 5 .   ? 130.517 12.890 5.044   1.00 35.59  ? 537 HOH   A O   1 
HETATM 2419 O  O   . HOH   G 5 .   ? 113.346 3.151  5.549   1.00 21.59  ? 538 HOH   A O   1 
HETATM 2420 O  O   . HOH   G 5 .   ? 130.846 11.354 -8.127  1.00 38.79  ? 539 HOH   A O   1 
HETATM 2421 O  O   . HOH   G 5 .   ? 130.814 38.095 1.266   1.00 69.09  ? 540 HOH   A O   1 
HETATM 2422 O  O   . HOH   G 5 .   ? 111.540 14.216 -15.136 1.00 36.36  ? 541 HOH   A O   1 
HETATM 2423 O  O   . HOH   G 5 .   ? 102.459 16.222 -8.531  1.00 36.69  ? 542 HOH   A O   1 
HETATM 2424 O  O   . HOH   G 5 .   ? 113.864 24.481 0.605   1.00 26.05  ? 543 HOH   A O   1 
HETATM 2425 O  O   . HOH   G 5 .   ? 116.017 43.365 -8.486  1.00 49.05  ? 544 HOH   A O   1 
HETATM 2426 O  O   . HOH   G 5 .   ? 124.986 26.140 -17.009 1.00 53.17  ? 545 HOH   A O   1 
HETATM 2427 O  O   . HOH   G 5 .   ? 126.523 -1.520 -12.005 1.00 36.62  ? 546 HOH   A O   1 
HETATM 2428 O  O   . HOH   G 5 .   ? 125.706 2.309  -7.213  1.00 27.76  ? 547 HOH   A O   1 
HETATM 2429 O  O   . HOH   G 5 .   ? 121.733 10.629 -7.801  1.00 22.63  ? 548 HOH   A O   1 
HETATM 2430 O  O   . HOH   G 5 .   ? 103.452 10.038 10.831  1.00 40.07  ? 549 HOH   A O   1 
HETATM 2431 O  O   . HOH   G 5 .   ? 123.872 20.642 15.441  1.00 63.23  ? 550 HOH   A O   1 
HETATM 2432 O  O   . HOH   G 5 .   ? 109.014 22.081 17.455  1.00 43.70  ? 551 HOH   A O   1 
HETATM 2433 O  O   . HOH   G 5 .   ? 148.538 34.133 6.221   1.00 76.26  ? 552 HOH   A O   1 
HETATM 2434 O  O   . HOH   G 5 .   ? 103.935 42.337 -5.499  1.00 58.52  ? 553 HOH   A O   1 
HETATM 2435 O  O   . HOH   G 5 .   ? 113.524 25.545 -12.743 1.00 25.24  ? 554 HOH   A O   1 
HETATM 2436 O  O   . HOH   G 5 .   ? 118.976 30.466 -6.166  1.00 22.46  ? 555 HOH   A O   1 
HETATM 2437 O  O   . HOH   G 5 .   ? 116.488 43.022 9.532   1.00 32.08  ? 556 HOH   A O   1 
HETATM 2438 O  O   . HOH   G 5 .   ? 125.366 34.763 10.409  1.00 56.16  ? 557 HOH   A O   1 
HETATM 2439 O  O   . HOH   G 5 .   ? 117.272 8.849  18.989  1.00 47.66  ? 558 HOH   A O   1 
HETATM 2440 O  O   . HOH   G 5 .   ? 131.267 18.014 -8.412  1.00 53.71  ? 559 HOH   A O   1 
HETATM 2441 O  O   . HOH   G 5 .   ? 105.808 35.350 8.919   1.00 57.37  ? 560 HOH   A O   1 
HETATM 2442 O  O   . HOH   G 5 .   ? 122.817 25.132 -9.036  1.00 66.86  ? 561 HOH   A O   1 
HETATM 2443 O  O   . HOH   G 5 .   ? 117.554 27.155 5.636   1.00 19.34  ? 562 HOH   A O   1 
HETATM 2444 O  O   . HOH   G 5 .   ? 131.382 5.649  -6.440  1.00 64.80  ? 563 HOH   A O   1 
HETATM 2445 O  O   . HOH   G 5 .   ? 124.511 10.479 -1.537  1.00 22.89  ? 564 HOH   A O   1 
HETATM 2446 O  O   . HOH   G 5 .   ? 108.552 31.325 -8.141  1.00 52.78  ? 565 HOH   A O   1 
HETATM 2447 O  O   . HOH   G 5 .   ? 113.800 27.585 16.401  1.00 29.11  ? 566 HOH   A O   1 
HETATM 2448 O  O   . HOH   G 5 .   ? 126.753 3.599  -13.108 1.00 51.41  ? 567 HOH   A O   1 
HETATM 2449 O  O   . HOH   G 5 .   ? 127.715 4.000  -8.462  1.00 36.09  ? 568 HOH   A O   1 
HETATM 2450 O  O   . HOH   G 5 .   ? 110.726 16.810 -23.710 1.00 42.95  ? 569 HOH   A O   1 
HETATM 2451 O  O   . HOH   G 5 .   ? 127.244 32.142 11.553  1.00 48.23  ? 570 HOH   A O   1 
HETATM 2452 O  O   . HOH   G 5 .   ? 123.820 30.757 0.434   1.00 26.14  ? 571 HOH   A O   1 
HETATM 2453 O  O   . HOH   G 5 .   ? 92.923  15.391 5.619   1.00 77.04  ? 572 HOH   A O   1 
HETATM 2454 O  O   . HOH   G 5 .   ? 107.160 35.332 -6.260  1.00 36.85  ? 573 HOH   A O   1 
HETATM 2455 O  O   . HOH   G 5 .   ? 115.270 21.101 -14.151 1.00 22.59  ? 574 HOH   A O   1 
HETATM 2456 O  O   . HOH   G 5 .   ? 118.499 0.576  -10.602 1.00 29.84  ? 575 HOH   A O   1 
HETATM 2457 O  O   . HOH   G 5 .   ? 108.868 3.834  -13.614 1.00 34.46  ? 576 HOH   A O   1 
HETATM 2458 O  O   . HOH   G 5 .   ? 133.954 8.078  -7.703  1.00 63.45  ? 577 HOH   A O   1 
HETATM 2459 O  O   . HOH   G 5 .   ? 116.277 27.794 15.011  1.00 26.24  ? 578 HOH   A O   1 
HETATM 2460 O  O   . HOH   G 5 .   ? 111.525 30.500 -5.074  1.00 20.69  ? 579 HOH   A O   1 
HETATM 2461 O  O   . HOH   G 5 .   ? 104.653 7.881  -10.092 1.00 38.78  ? 580 HOH   A O   1 
HETATM 2462 O  O   . HOH   G 5 .   ? 149.958 31.798 4.680   1.00 48.74  ? 581 HOH   A O   1 
HETATM 2463 O  O   . HOH   G 5 .   ? 110.180 41.401 -10.173 1.00 62.74  ? 582 HOH   A O   1 
HETATM 2464 O  O   . HOH   G 5 .   ? 95.803  14.634 11.937  1.00 48.74  ? 583 HOH   A O   1 
HETATM 2465 O  O   . HOH   G 5 .   ? 111.062 37.642 -5.884  1.00 24.48  ? 584 HOH   A O   1 
HETATM 2466 O  O   . HOH   G 5 .   ? 107.348 24.642 18.277  1.00 38.37  ? 585 HOH   A O   1 
HETATM 2467 O  O   . HOH   G 5 .   ? 121.470 9.986  18.675  1.00 45.19  ? 586 HOH   A O   1 
HETATM 2468 O  O   . HOH   G 5 .   ? 117.770 37.132 -8.839  1.00 42.22  ? 587 HOH   A O   1 
HETATM 2469 O  O   . HOH   G 5 .   ? 111.581 -0.288 -4.929  1.00 43.52  ? 588 HOH   A O   1 
HETATM 2470 O  O   . HOH   G 5 .   ? 123.343 38.262 13.526  1.00 63.97  ? 589 HOH   A O   1 
HETATM 2471 O  O   . HOH   G 5 .   ? 110.071 17.141 -10.144 1.00 25.85  ? 590 HOH   A O   1 
HETATM 2472 O  O   . HOH   G 5 .   ? 103.579 30.054 14.484  1.00 48.85  ? 591 HOH   A O   1 
HETATM 2473 O  O   . HOH   G 5 .   ? 118.722 29.710 5.442   1.00 20.91  ? 592 HOH   A O   1 
HETATM 2474 O  O   . HOH   G 5 .   ? 108.760 23.219 -10.370 1.00 31.95  ? 593 HOH   A O   1 
HETATM 2475 O  O   . HOH   G 5 .   ? 134.915 12.512 -1.690  1.00 52.02  ? 594 HOH   A O   1 
HETATM 2476 O  O   . HOH   G 5 .   ? 135.056 17.764 4.266   1.00 39.51  ? 595 HOH   A O   1 
HETATM 2477 O  O   . HOH   G 5 .   ? 102.844 46.153 -1.422  1.00 49.98  ? 596 HOH   A O   1 
HETATM 2478 O  O   . HOH   G 5 .   ? 107.939 44.281 2.351   1.00 32.99  ? 597 HOH   A O   1 
HETATM 2479 O  O   . HOH   G 5 .   ? 132.297 33.154 7.737   1.00 66.51  ? 598 HOH   A O   1 
HETATM 2480 O  O   . HOH   G 5 .   ? 141.271 12.992 -5.885  1.00 75.24  ? 599 HOH   A O   1 
HETATM 2481 O  O   . HOH   G 5 .   ? 125.513 25.747 -12.846 1.00 46.05  ? 600 HOH   A O   1 
HETATM 2482 O  O   . HOH   G 5 .   ? 124.181 8.427  -19.731 1.00 48.43  ? 601 HOH   A O   1 
HETATM 2483 O  O   . HOH   G 5 .   ? 99.223  12.291 -4.131  1.00 35.96  ? 602 HOH   A O   1 
HETATM 2484 O  O   . HOH   G 5 .   ? 128.084 16.812 13.229  1.00 31.98  ? 603 HOH   A O   1 
HETATM 2485 O  O   . HOH   G 5 .   ? 107.310 11.918 -15.390 1.00 54.92  ? 604 HOH   A O   1 
HETATM 2486 O  O   . HOH   G 5 .   ? 126.806 28.835 -15.897 1.00 67.71  ? 605 HOH   A O   1 
HETATM 2487 O  O   . HOH   G 5 .   ? 108.973 3.079  -0.933  1.00 35.87  ? 606 HOH   A O   1 
HETATM 2488 O  O   . HOH   G 5 .   ? 137.971 33.924 0.202   1.00 101.59 ? 607 HOH   A O   1 
HETATM 2489 O  O   . HOH   G 5 .   ? 123.825 18.387 13.429  1.00 43.36  ? 608 HOH   A O   1 
HETATM 2490 O  O   . HOH   G 5 .   ? 123.814 29.113 13.367  1.00 50.16  ? 609 HOH   A O   1 
HETATM 2491 O  O   . HOH   G 5 .   ? 115.618 10.650 15.322  1.00 37.07  ? 610 HOH   A O   1 
HETATM 2492 O  O   . HOH   G 5 .   ? 110.166 18.070 -18.249 1.00 47.38  ? 611 HOH   A O   1 
HETATM 2493 O  O   . HOH   G 5 .   ? 100.852 31.294 15.818  1.00 56.09  ? 612 HOH   A O   1 
HETATM 2494 O  O   . HOH   G 5 .   ? 115.002 13.371 14.529  1.00 31.35  ? 613 HOH   A O   1 
HETATM 2495 O  O   . HOH   G 5 .   ? 102.221 6.221  -6.728  1.00 51.08  ? 614 HOH   A O   1 
HETATM 2496 O  O   . HOH   G 5 .   ? 112.387 24.802 19.760  1.00 41.03  ? 615 HOH   A O   1 
HETATM 2497 O  O   . HOH   G 5 .   ? 100.773 10.845 10.550  1.00 46.28  ? 616 HOH   A O   1 
HETATM 2498 O  O   . HOH   G 5 .   ? 138.580 19.081 -10.660 1.00 81.54  ? 617 HOH   A O   1 
HETATM 2499 O  O   . HOH   G 5 .   ? 135.348 33.005 -2.352  1.00 49.36  ? 618 HOH   A O   1 
HETATM 2500 O  O   . HOH   G 5 .   ? 105.342 32.334 6.368   1.00 35.59  ? 619 HOH   A O   1 
HETATM 2501 O  O   . HOH   G 5 .   ? 132.145 16.506 -10.718 1.00 72.66  ? 620 HOH   A O   1 
HETATM 2502 O  O   . HOH   G 5 .   ? 102.749 38.526 -4.536  1.00 58.27  ? 621 HOH   A O   1 
HETATM 2503 O  O   . HOH   G 5 .   ? 149.743 32.539 1.692   1.00 28.01  ? 622 HOH   A O   1 
HETATM 2504 O  O   . HOH   G 5 .   ? 113.676 15.351 -22.711 1.00 56.34  ? 623 HOH   A O   1 
HETATM 2505 O  O   . HOH   G 5 .   ? 105.987 7.024  11.345  1.00 42.05  ? 624 HOH   A O   1 
HETATM 2506 O  O   . HOH   G 5 .   ? 127.118 26.600 -10.667 1.00 49.12  ? 625 HOH   A O   1 
HETATM 2507 O  O   . HOH   G 5 .   ? 128.168 31.001 -6.728  1.00 40.70  ? 626 HOH   A O   1 
HETATM 2508 O  O   . HOH   G 5 .   ? 121.534 31.872 -5.367  1.00 35.36  ? 627 HOH   A O   1 
HETATM 2509 O  O   . HOH   G 5 .   ? 118.041 22.391 18.316  1.00 43.87  ? 628 HOH   A O   1 
HETATM 2510 O  O   . HOH   G 5 .   ? 94.897  16.318 -0.294  1.00 45.75  ? 629 HOH   A O   1 
HETATM 2511 O  O   . HOH   G 5 .   ? 130.552 18.481 14.087  1.00 56.01  ? 630 HOH   A O   1 
HETATM 2512 O  O   . HOH   G 5 .   ? 119.145 41.185 5.043   1.00 38.05  ? 631 HOH   A O   1 
HETATM 2513 O  O   . HOH   G 5 .   ? 126.590 24.048 -18.130 1.00 41.86  ? 632 HOH   A O   1 
HETATM 2514 O  O   . HOH   G 5 .   ? 117.835 37.201 16.682  1.00 54.01  ? 633 HOH   A O   1 
HETATM 2515 O  O   . HOH   G 5 .   ? 133.458 30.129 4.564   1.00 36.09  ? 634 HOH   A O   1 
HETATM 2516 O  O   . HOH   G 5 .   ? 111.092 21.006 -13.557 1.00 39.16  ? 635 HOH   A O   1 
HETATM 2517 O  O   . HOH   G 5 .   ? 125.358 26.706 -8.671  1.00 48.52  ? 636 HOH   A O   1 
HETATM 2518 O  O   . HOH   G 5 .   ? 116.416 36.523 -11.120 1.00 45.06  ? 637 HOH   A O   1 
HETATM 2519 O  O   . HOH   G 5 .   ? 98.972  9.617  3.872   1.00 53.00  ? 638 HOH   A O   1 
HETATM 2520 O  O   . HOH   G 5 .   ? 122.767 40.259 10.565  1.00 65.45  ? 639 HOH   A O   1 
HETATM 2521 O  O   . HOH   G 5 .   ? 107.236 -0.445 0.309   0.50 32.31  ? 640 HOH   A O   1 
HETATM 2522 O  O   . HOH   G 5 .   ? 104.331 27.243 -4.868  1.00 39.50  ? 641 HOH   A O   1 
HETATM 2523 O  O   . HOH   G 5 .   ? 129.133 30.364 -4.308  1.00 38.65  ? 642 HOH   A O   1 
HETATM 2524 O  O   . HOH   G 5 .   ? 117.600 26.393 -21.952 1.00 41.20  ? 643 HOH   A O   1 
HETATM 2525 O  O   . HOH   G 5 .   ? 116.375 4.251  15.175  1.00 24.41  ? 644 HOH   A O   1 
HETATM 2526 O  O   . HOH   G 5 .   ? 119.683 25.622 15.882  1.00 40.67  ? 645 HOH   A O   1 
HETATM 2527 O  O   . HOH   G 5 .   ? 129.915 -2.386 9.066   1.00 58.11  ? 646 HOH   A O   1 
HETATM 2528 O  O   . HOH   G 5 .   ? 122.912 31.959 15.040  1.00 44.13  ? 647 HOH   A O   1 
HETATM 2529 O  O   . HOH   G 5 .   ? 124.254 21.336 -20.783 1.00 50.86  ? 648 HOH   A O   1 
HETATM 2530 O  O   . HOH   G 5 .   ? 106.527 16.194 16.086  1.00 51.13  ? 649 HOH   A O   1 
HETATM 2531 O  O   . HOH   G 5 .   ? 115.360 38.443 13.818  1.00 36.04  ? 650 HOH   A O   1 
HETATM 2532 O  O   . HOH   G 5 .   ? 128.469 25.842 13.435  1.00 45.34  ? 651 HOH   A O   1 
HETATM 2533 O  O   . HOH   G 5 .   ? 127.042 11.321 -1.448  1.00 25.63  ? 652 HOH   A O   1 
HETATM 2534 O  O   . HOH   G 5 .   ? 109.451 46.260 5.140   1.00 42.49  ? 653 HOH   A O   1 
HETATM 2535 O  O   . HOH   G 5 .   ? 127.691 9.969  -15.223 1.00 45.11  ? 654 HOH   A O   1 
HETATM 2536 O  O   . HOH   G 5 .   ? 97.406  19.777 -6.574  1.00 56.53  ? 655 HOH   A O   1 
HETATM 2537 O  O   . HOH   G 5 .   ? 114.916 4.566  12.374  1.00 25.98  ? 656 HOH   A O   1 
HETATM 2538 O  O   . HOH   G 5 .   ? 123.321 32.576 -12.816 1.00 42.82  ? 657 HOH   A O   1 
HETATM 2539 O  O   . HOH   G 5 .   ? 121.956 5.720  -19.231 1.00 38.42  ? 658 HOH   A O   1 
HETATM 2540 O  O   . HOH   G 5 .   ? 109.243 0.887  3.389   1.00 45.90  ? 659 HOH   A O   1 
HETATM 2541 O  O   . HOH   G 5 .   ? 114.852 45.853 0.036   1.00 53.46  ? 660 HOH   A O   1 
HETATM 2542 O  O   . HOH   G 5 .   ? 113.035 9.603  15.075  1.00 46.40  ? 661 HOH   A O   1 
HETATM 2543 O  O   . HOH   G 5 .   ? 98.140  12.239 12.415  1.00 57.79  ? 662 HOH   A O   1 
HETATM 2544 O  O   . HOH   G 5 .   ? 139.962 35.190 1.532   1.00 51.44  ? 663 HOH   A O   1 
HETATM 2545 O  O   . HOH   G 5 .   ? 106.563 26.854 -8.535  1.00 44.68  ? 664 HOH   A O   1 
HETATM 2546 O  O   . HOH   G 5 .   ? 149.238 28.063 -5.866  1.00 34.50  ? 665 HOH   A O   1 
HETATM 2547 O  O   . HOH   G 5 .   ? 94.542  21.689 -1.198  1.00 45.80  ? 666 HOH   A O   1 
HETATM 2548 O  O   . HOH   G 5 .   ? 110.487 15.674 -19.197 1.00 46.82  ? 667 HOH   A O   1 
HETATM 2549 O  O   . HOH   G 5 .   ? 124.014 35.892 4.235   1.00 30.33  ? 668 HOH   A O   1 
HETATM 2550 O  O   . HOH   G 5 .   ? 92.028  16.681 2.512   1.00 57.65  ? 669 HOH   A O   1 
HETATM 2551 O  O   . HOH   G 5 .   ? 124.901 38.362 2.826   1.00 33.97  ? 670 HOH   A O   1 
HETATM 2552 O  O   . HOH   G 5 .   ? 112.081 53.499 9.082   1.00 47.24  ? 671 HOH   A O   1 
HETATM 2553 O  O   . HOH   G 5 .   ? 141.982 22.630 3.130   1.00 59.61  ? 672 HOH   A O   1 
HETATM 2554 O  O   . HOH   G 5 .   ? 109.024 18.544 -7.975  1.00 23.20  ? 673 HOH   A O   1 
HETATM 2555 O  O   . HOH   G 5 .   ? 106.005 30.170 -7.959  1.00 53.56  ? 674 HOH   A O   1 
HETATM 2556 O  O   . HOH   G 5 .   ? 133.658 40.505 -3.004  1.00 66.70  ? 675 HOH   A O   1 
HETATM 2557 O  O   . HOH   G 5 .   ? 113.173 4.026  -22.498 1.00 68.78  ? 676 HOH   A O   1 
HETATM 2558 O  O   . HOH   G 5 .   ? 95.226  22.243 6.005   1.00 68.82  ? 677 HOH   A O   1 
HETATM 2559 O  O   . HOH   G 5 .   ? 136.937 24.597 -11.102 1.00 85.31  ? 678 HOH   A O   1 
HETATM 2560 O  O   . HOH   G 5 .   ? 115.927 44.465 -3.588  1.00 49.72  ? 679 HOH   A O   1 
HETATM 2561 O  O   . HOH   G 5 .   ? 130.063 31.305 2.068   1.00 30.33  ? 680 HOH   A O   1 
HETATM 2562 O  O   . HOH   G 5 .   ? 112.739 -1.218 11.492  1.00 44.91  ? 681 HOH   A O   1 
HETATM 2563 O  O   . HOH   G 5 .   ? 138.385 32.804 -9.335  1.00 55.77  ? 682 HOH   A O   1 
HETATM 2564 O  O   . HOH   G 5 .   ? 136.913 24.033 6.390   1.00 71.40  ? 683 HOH   A O   1 
HETATM 2565 O  O   . HOH   G 5 .   ? 131.656 17.607 -15.574 1.00 82.67  ? 684 HOH   A O   1 
HETATM 2566 O  O   . HOH   G 5 .   ? 133.869 14.282 0.082   1.00 41.26  ? 685 HOH   A O   1 
HETATM 2567 O  O   . HOH   G 5 .   ? 121.509 39.810 4.162   1.00 34.89  ? 686 HOH   A O   1 
HETATM 2568 O  O   . HOH   G 5 .   ? 93.270  18.570 -0.507  1.00 47.57  ? 687 HOH   A O   1 
HETATM 2569 O  O   . HOH   G 5 .   ? 124.958 38.695 -4.420  1.00 43.60  ? 688 HOH   A O   1 
HETATM 2570 O  O   . HOH   G 5 .   ? 135.344 20.313 -9.525  1.00 69.00  ? 689 HOH   A O   1 
HETATM 2571 O  O   . HOH   G 5 .   ? 129.423 1.248  2.873   1.00 50.30  ? 690 HOH   A O   1 
HETATM 2572 O  O   . HOH   G 5 .   ? 108.249 20.543 -9.925  1.00 26.76  ? 691 HOH   A O   1 
HETATM 2573 O  O   . HOH   G 5 .   ? 133.532 23.710 -14.012 1.00 64.57  ? 692 HOH   A O   1 
HETATM 2574 O  O   . HOH   G 5 .   ? 134.839 27.157 8.946   1.00 47.70  ? 693 HOH   A O   1 
HETATM 2575 O  O   . HOH   G 5 .   ? 124.993 34.116 6.227   1.00 34.05  ? 694 HOH   A O   1 
HETATM 2576 O  O   . HOH   G 5 .   ? 107.024 32.614 -6.353  1.00 44.66  ? 695 HOH   A O   1 
HETATM 2577 O  O   . HOH   G 5 .   ? 102.760 26.789 -3.058  1.00 45.12  ? 696 HOH   A O   1 
HETATM 2578 O  O   . HOH   G 5 .   ? 119.650 40.622 0.283   1.00 41.27  ? 697 HOH   A O   1 
HETATM 2579 O  O   . HOH   G 5 .   ? 133.352 21.604 11.192  1.00 51.38  ? 698 HOH   A O   1 
HETATM 2580 O  O   . HOH   G 5 .   ? 140.061 37.672 -4.981  1.00 51.67  ? 699 HOH   A O   1 
HETATM 2581 O  O   . HOH   G 5 .   ? 105.550 9.598  -17.683 1.00 56.93  ? 700 HOH   A O   1 
HETATM 2582 O  O   . HOH   G 5 .   ? 107.065 4.855  -15.567 1.00 42.80  ? 701 HOH   A O   1 
HETATM 2583 O  O   . HOH   G 5 .   ? 111.037 22.742 -11.741 1.00 39.16  ? 702 HOH   A O   1 
HETATM 2584 O  O   . HOH   G 5 .   ? 98.358  7.900  1.886   1.00 59.19  ? 703 HOH   A O   1 
HETATM 2585 O  O   . HOH   G 5 .   ? 119.615 20.926 -25.216 1.00 60.13  ? 704 HOH   A O   1 
HETATM 2586 O  O   . HOH   G 5 .   ? 113.707 37.039 13.719  1.00 38.19  ? 705 HOH   A O   1 
HETATM 2587 O  O   . HOH   G 5 .   ? 133.264 12.376 5.067   1.00 70.11  ? 706 HOH   A O   1 
HETATM 2588 O  O   . HOH   G 5 .   ? 102.203 1.343  0.619   1.00 68.52  ? 707 HOH   A O   1 
HETATM 2589 O  O   . HOH   G 5 .   ? 144.525 26.594 -6.263  1.00 74.49  ? 708 HOH   A O   1 
HETATM 2590 O  O   . HOH   G 5 .   ? 102.694 0.670  7.128   1.00 78.15  ? 709 HOH   A O   1 
HETATM 2591 O  O   . HOH   G 5 .   ? 127.658 38.441 2.693   1.00 62.17  ? 710 HOH   A O   1 
HETATM 2592 O  O   . HOH   G 5 .   ? 120.059 19.710 -22.407 1.00 37.78  ? 711 HOH   A O   1 
HETATM 2593 O  O   . HOH   G 5 .   ? 130.048 3.379  -5.106  1.00 49.86  ? 712 HOH   A O   1 
HETATM 2594 O  O   . HOH   G 5 .   ? 103.436 22.335 19.584  1.00 72.30  ? 713 HOH   A O   1 
HETATM 2595 O  O   . HOH   G 5 .   ? 112.967 27.707 -16.558 1.00 47.57  ? 714 HOH   A O   1 
HETATM 2596 O  O   . HOH   G 5 .   ? 126.033 22.488 10.787  1.00 26.61  ? 715 HOH   A O   1 
HETATM 2597 O  O   . HOH   G 5 .   ? 135.330 15.176 5.593   1.00 52.09  ? 716 HOH   A O   1 
HETATM 2598 O  O   . HOH   G 5 .   ? 118.524 11.538 14.629  1.00 31.64  ? 717 HOH   A O   1 
HETATM 2599 O  O   . HOH   G 5 .   ? 113.110 3.362  -12.719 1.00 37.63  ? 718 HOH   A O   1 
HETATM 2600 O  O   . HOH   G 5 .   ? 98.977  12.881 15.152  1.00 59.30  ? 719 HOH   A O   1 
HETATM 2601 O  O   . HOH   G 5 .   ? 109.078 44.317 -9.815  1.00 69.11  ? 720 HOH   A O   1 
HETATM 2602 O  O   . HOH   G 5 .   ? 102.817 9.064  -6.739  1.00 51.79  ? 721 HOH   A O   1 
HETATM 2603 O  O   . HOH   G 5 .   ? 130.458 20.087 -12.145 1.00 52.90  ? 722 HOH   A O   1 
HETATM 2604 O  O   . HOH   G 5 .   ? 111.324 0.544  -9.503  1.00 43.96  ? 723 HOH   A O   1 
HETATM 2605 O  O   . HOH   G 5 .   ? 121.883 39.137 -3.894  1.00 46.11  ? 724 HOH   A O   1 
HETATM 2606 O  O   . HOH   G 5 .   ? 99.826  44.615 0.063   1.00 66.53  ? 725 HOH   A O   1 
HETATM 2607 O  O   . HOH   G 5 .   ? 127.678 33.647 -6.613  1.00 49.56  ? 726 HOH   A O   1 
HETATM 2608 O  O   . HOH   G 5 .   ? 112.765 12.982 21.238  1.00 71.37  ? 727 HOH   A O   1 
HETATM 2609 O  O   . HOH   G 5 .   ? 134.164 23.197 -10.564 1.00 85.03  ? 728 HOH   A O   1 
HETATM 2610 O  O   . HOH   G 5 .   ? 106.227 46.513 -6.495  1.00 54.13  ? 729 HOH   A O   1 
HETATM 2611 O  O   . HOH   G 5 .   ? 148.097 23.250 -5.354  1.00 58.39  ? 730 HOH   A O   1 
HETATM 2612 O  O   . HOH   G 5 .   ? 105.217 29.482 9.756   1.00 48.78  ? 731 HOH   A O   1 
HETATM 2613 O  O   . HOH   G 5 .   ? 103.784 0.881  -9.152  1.00 56.58  ? 732 HOH   A O   1 
HETATM 2614 O  O   . HOH   G 5 .   ? 101.344 22.855 -10.546 1.00 76.81  ? 733 HOH   A O   1 
HETATM 2615 O  O   . HOH   G 5 .   ? 104.994 66.086 10.447  1.00 65.99  ? 734 HOH   A O   1 
HETATM 2616 O  O   . HOH   G 5 .   ? 136.292 20.813 6.974   1.00 60.70  ? 735 HOH   A O   1 
HETATM 2617 O  O   . HOH   G 5 .   ? 129.012 5.315  -12.932 1.00 47.11  ? 736 HOH   A O   1 
HETATM 2618 O  O   . HOH   G 5 .   ? 120.375 37.727 -8.561  1.00 59.79  ? 737 HOH   A O   1 
HETATM 2619 O  O   . HOH   G 5 .   ? 113.217 16.734 20.385  1.00 59.74  ? 738 HOH   A O   1 
HETATM 2620 O  O   . HOH   G 5 .   ? 139.632 31.962 5.044   1.00 78.20  ? 739 HOH   A O   1 
HETATM 2621 O  O   . HOH   G 5 .   ? 120.052 41.641 7.960   1.00 52.25  ? 740 HOH   A O   1 
HETATM 2622 O  O   . HOH   G 5 .   ? 134.571 7.406  -4.532  1.00 91.34  ? 741 HOH   A O   1 
HETATM 2623 O  O   . HOH   G 5 .   ? 127.627 23.230 13.540  1.00 47.35  ? 742 HOH   A O   1 
HETATM 2624 O  O   . HOH   G 5 .   ? 132.030 23.069 -8.887  1.00 75.07  ? 743 HOH   A O   1 
HETATM 2625 O  O   . HOH   G 5 .   ? 96.706  26.334 16.814  1.00 65.23  ? 744 HOH   A O   1 
HETATM 2626 O  O   . HOH   G 5 .   ? 114.269 7.526  16.427  1.00 74.24  ? 745 HOH   A O   1 
HETATM 2627 O  O   . HOH   G 5 .   ? 101.938 45.084 5.615   1.00 74.73  ? 746 HOH   A O   1 
HETATM 2628 O  O   . HOH   G 5 .   ? 128.195 42.157 -0.939  1.00 71.27  ? 747 HOH   A O   1 
HETATM 2629 O  O   . HOH   G 5 .   ? 117.652 41.426 -1.312  1.00 53.82  ? 748 HOH   A O   1 
HETATM 2630 O  O   . HOH   G 5 .   ? 122.075 21.584 -22.381 1.00 52.22  ? 749 HOH   A O   1 
HETATM 2631 O  O   . HOH   G 5 .   ? 111.537 27.199 19.871  1.00 50.65  ? 750 HOH   A O   1 
HETATM 2632 O  O   . HOH   G 5 .   ? 127.527 14.343 -19.828 1.00 63.94  ? 751 HOH   A O   1 
HETATM 2633 O  O   . HOH   G 5 .   ? 133.236 2.761  7.280   1.00 71.13  ? 752 HOH   A O   1 
HETATM 2634 O  O   . HOH   G 5 .   ? 114.679 47.988 2.463   1.00 61.84  ? 753 HOH   A O   1 
HETATM 2635 O  O   . HOH   G 5 .   ? 124.529 17.004 15.694  1.00 63.64  ? 754 HOH   A O   1 
HETATM 2636 O  O   . HOH   G 5 .   ? 137.376 19.062 4.850   1.00 74.80  ? 755 HOH   A O   1 
HETATM 2637 O  O   . HOH   G 5 .   ? 130.180 6.893  -8.784  1.00 53.47  ? 756 HOH   A O   1 
HETATM 2638 O  O   . HOH   G 5 .   ? 109.587 7.623  14.175  1.00 59.46  ? 757 HOH   A O   1 
HETATM 2639 O  O   . HOH   G 5 .   ? 128.094 36.024 5.467   1.00 68.88  ? 758 HOH   A O   1 
HETATM 2640 O  O   . HOH   G 5 .   ? 117.653 19.038 -26.181 1.00 45.79  ? 759 HOH   A O   1 
HETATM 2641 O  O   . HOH   G 5 .   ? 102.025 6.394  12.042  1.00 65.95  ? 760 HOH   A O   1 
HETATM 2642 O  O   . HOH   G 5 .   ? 134.729 15.783 -12.442 1.00 75.72  ? 761 HOH   A O   1 
HETATM 2643 O  O   . HOH   G 5 .   ? 108.210 19.485 -12.513 1.00 38.10  ? 762 HOH   A O   1 
HETATM 2644 O  O   . HOH   G 5 .   ? 114.776 42.925 -10.805 1.00 70.72  ? 763 HOH   A O   1 
HETATM 2645 O  O   . HOH   G 5 .   ? 116.849 40.753 13.770  1.00 49.02  ? 764 HOH   A O   1 
HETATM 2646 O  O   . HOH   G 5 .   ? 106.691 67.344 14.056  1.00 47.44  ? 765 HOH   A O   1 
HETATM 2647 O  O   . HOH   G 5 .   ? 130.540 29.741 13.441  1.00 66.68  ? 766 HOH   A O   1 
HETATM 2648 O  O   . HOH   G 5 .   ? 130.344 8.744  -11.416 1.00 67.32  ? 767 HOH   A O   1 
HETATM 2649 O  O   . HOH   G 5 .   ? 105.619 12.539 -11.880 1.00 57.07  ? 768 HOH   A O   1 
HETATM 2650 O  O   . HOH   G 5 .   ? 111.179 48.499 -7.488  1.00 64.32  ? 769 HOH   A O   1 
HETATM 2651 O  O   . HOH   G 5 .   ? 110.305 23.372 20.118  1.00 53.86  ? 770 HOH   A O   1 
HETATM 2652 O  O   . HOH   G 5 .   ? 122.669 28.911 16.204  1.00 54.45  ? 771 HOH   A O   1 
HETATM 2653 O  O   . HOH   G 5 .   ? 125.708 22.519 15.944  1.00 54.40  ? 772 HOH   A O   1 
HETATM 2654 O  O   . HOH   G 5 .   ? 119.539 42.606 12.437  1.00 67.99  ? 773 HOH   A O   1 
HETATM 2655 O  O   . HOH   G 5 .   ? 108.438 16.594 -12.020 1.00 45.07  ? 774 HOH   A O   1 
HETATM 2656 O  O   . HOH   G 5 .   ? 107.011 3.321  -10.901 1.00 68.00  ? 775 HOH   A O   1 
HETATM 2657 O  O   . HOH   G 5 .   ? 110.476 37.073 -8.632  1.00 44.16  ? 776 HOH   A O   1 
HETATM 2658 O  O   . HOH   G 5 .   ? 109.658 13.071 -16.117 1.00 54.48  ? 777 HOH   A O   1 
HETATM 2659 O  O   . HOH   G 5 .   ? 135.004 36.667 1.166   1.00 64.33  ? 778 HOH   A O   1 
HETATM 2660 O  O   . HOH   G 5 .   ? 106.388 1.354  8.220   1.00 54.86  ? 779 HOH   A O   1 
HETATM 2661 O  O   . HOH   G 5 .   ? 104.792 4.756  -11.528 1.00 66.38  ? 780 HOH   A O   1 
HETATM 2662 O  O   . HOH   G 5 .   ? 99.891  3.593  0.056   1.00 60.77  ? 781 HOH   A O   1 
HETATM 2663 O  O   . HOH   G 5 .   ? 94.092  13.278 10.294  1.00 69.42  ? 782 HOH   A O   1 
HETATM 2664 O  O   . HOH   G 5 .   ? 123.598 39.155 8.204   1.00 65.92  ? 783 HOH   A O   1 
HETATM 2665 O  O   . HOH   G 5 .   ? 129.507 21.392 14.334  1.00 54.68  ? 784 HOH   A O   1 
HETATM 2666 O  O   . HOH   G 5 .   ? 141.692 15.381 -8.475  1.00 59.42  ? 785 HOH   A O   1 
HETATM 2667 O  O   . HOH   G 5 .   ? 133.012 20.992 -12.712 1.00 70.85  ? 786 HOH   A O   1 
HETATM 2668 O  O   . HOH   G 5 .   ? 104.359 12.976 16.750  1.00 61.86  ? 787 HOH   A O   1 
HETATM 2669 O  O   . HOH   G 5 .   ? 107.373 11.650 15.441  1.00 46.57  ? 788 HOH   A O   1 
HETATM 2670 O  O   . HOH   G 5 .   ? 135.459 16.244 1.601   1.00 61.71  ? 789 HOH   A O   1 
HETATM 2671 O  O   . HOH   G 5 .   ? 130.260 32.047 12.020  1.00 58.08  ? 790 HOH   A O   1 
HETATM 2672 O  O   . HOH   G 5 .   ? 101.095 0.592  -5.260  1.00 76.46  ? 791 HOH   A O   1 
HETATM 2673 O  O   . HOH   G 5 .   ? 100.189 2.348  3.085   1.00 67.27  ? 792 HOH   A O   1 
HETATM 2674 O  O   . HOH   G 5 .   ? 134.741 8.220  3.945   1.00 71.87  ? 793 HOH   A O   1 
HETATM 2675 O  O   . HOH   G 5 .   ? 114.215 34.254 15.711  1.00 51.72  ? 794 HOH   A O   1 
HETATM 2676 O  O   . HOH   G 5 .   ? 131.424 34.629 4.760   1.00 58.28  ? 795 HOH   A O   1 
HETATM 2677 O  O   . HOH   G 5 .   ? 107.436 2.310  10.538  1.00 46.72  ? 796 HOH   A O   1 
HETATM 2678 O  O   . HOH   G 5 .   ? 114.174 31.773 16.022  1.00 42.17  ? 797 HOH   A O   1 
HETATM 2679 O  O   . HOH   G 5 .   ? 103.147 33.449 5.982   1.00 42.47  ? 798 HOH   A O   1 
HETATM 2680 O  O   . HOH   G 5 .   ? 116.614 30.561 15.012  1.00 25.78  ? 799 HOH   A O   1 
HETATM 2681 O  O   . HOH   G 5 .   ? 101.399 24.082 20.717  1.00 65.56  ? 800 HOH   A O   1 
HETATM 2682 O  O   . HOH   G 5 .   ? 134.432 9.367  -2.589  1.00 66.05  ? 801 HOH   A O   1 
HETATM 2683 O  O   . HOH   G 5 .   ? 128.026 -1.692 11.105  1.00 52.11  ? 802 HOH   A O   1 
HETATM 2684 O  O   . HOH   G 5 .   ? 138.297 28.233 -13.083 1.00 75.22  ? 803 HOH   A O   1 
HETATM 2685 O  O   . HOH   G 5 .   ? 110.443 1.337  0.499   1.00 54.98  ? 804 HOH   A O   1 
HETATM 2686 O  O   . HOH   G 5 .   ? 130.726 20.464 -9.424  1.00 58.26  ? 805 HOH   A O   1 
HETATM 2687 O  O   . HOH   G 5 .   ? 111.894 0.797  13.165  1.00 44.40  ? 806 HOH   A O   1 
HETATM 2688 O  O   . HOH   G 5 .   ? 104.618 9.384  13.387  1.00 54.30  ? 807 HOH   A O   1 
HETATM 2689 O  O   . HOH   G 5 .   ? 126.148 3.668  -15.759 1.00 62.14  ? 808 HOH   A O   1 
HETATM 2690 O  O   . HOH   G 5 .   ? 112.639 3.692  13.837  1.00 36.33  ? 809 HOH   A O   1 
HETATM 2691 O  O   . HOH   G 5 .   ? 130.956 17.604 -12.957 1.00 57.02  ? 810 HOH   A O   1 
HETATM 2692 O  O   . HOH   G 5 .   ? 107.535 30.266 -12.907 1.00 62.33  ? 811 HOH   A O   1 
HETATM 2693 O  O   . HOH   G 5 .   ? 119.516 9.275  20.159  1.00 51.53  ? 812 HOH   A O   1 
HETATM 2694 O  O   . HOH   G 5 .   ? 117.763 26.584 16.789  1.00 42.95  ? 813 HOH   A O   1 
HETATM 2695 O  O   . HOH   G 5 .   ? 139.155 26.068 -9.623  1.00 54.48  ? 814 HOH   A O   1 
HETATM 2696 O  O   . HOH   G 5 .   ? 128.241 0.015  15.510  1.00 64.62  ? 815 HOH   A O   1 
HETATM 2697 O  O   . HOH   G 5 .   ? 95.213  17.446 -3.722  1.00 61.77  ? 816 HOH   A O   1 
HETATM 2698 O  O   . HOH   G 5 .   ? 106.671 23.969 -11.718 1.00 47.72  ? 817 HOH   A O   1 
HETATM 2699 O  O   . HOH   G 5 .   ? 116.323 5.879  19.499  1.00 61.11  ? 818 HOH   A O   1 
HETATM 2700 O  O   . HOH   G 5 .   ? 99.691  2.675  -6.271  1.00 67.28  ? 819 HOH   A O   1 
HETATM 2701 O  O   . HOH   G 5 .   ? 124.569 14.997 -23.656 1.00 52.99  ? 820 HOH   A O   1 
HETATM 2702 O  O   . HOH   G 5 .   ? 105.528 4.100  11.453  1.00 63.69  ? 821 HOH   A O   1 
HETATM 2703 O  O   . HOH   G 5 .   ? 139.830 21.227 3.610   1.00 77.03  ? 822 HOH   A O   1 
HETATM 2704 O  O   . HOH   G 5 .   ? 129.565 25.070 -17.626 1.00 52.90  ? 823 HOH   A O   1 
HETATM 2705 O  O   . HOH   G 5 .   ? 105.747 43.663 -6.956  1.00 60.57  ? 824 HOH   A O   1 
HETATM 2706 O  O   . HOH   G 5 .   ? 113.251 29.184 19.154  1.00 50.52  ? 825 HOH   A O   1 
HETATM 2707 O  O   . HOH   G 5 .   ? 122.994 13.915 -21.674 1.00 46.40  ? 826 HOH   A O   1 
HETATM 2708 O  O   . HOH   G 5 .   ? 138.919 37.196 3.041   1.00 69.83  ? 827 HOH   A O   1 
HETATM 2709 O  O   . HOH   G 5 .   ? 116.312 43.340 12.112  1.00 46.60  ? 828 HOH   A O   1 
HETATM 2710 O  O   . HOH   G 5 .   ? 125.753 37.577 7.492   1.00 70.88  ? 829 HOH   A O   1 
HETATM 2711 O  O   . HOH   G 5 .   ? 101.253 29.105 7.127   1.00 53.34  ? 830 HOH   A O   1 
HETATM 2712 O  O   . HOH   G 5 .   ? 97.133  7.919  -2.500  1.00 71.82  ? 831 HOH   A O   1 
HETATM 2713 O  O   . HOH   G 5 .   ? 127.808 19.341 13.492  1.00 53.01  ? 832 HOH   A O   1 
HETATM 2714 O  O   . HOH   G 5 .   ? 118.885 43.075 -3.239  1.00 50.35  ? 833 HOH   A O   1 
HETATM 2715 O  O   . HOH   G 5 .   ? 124.684 18.047 -23.126 1.00 64.06  ? 834 HOH   A O   1 
HETATM 2716 O  O   . HOH   G 5 .   ? 122.107 17.934 -21.500 1.00 40.89  ? 835 HOH   A O   1 
HETATM 2717 O  O   . HOH   G 5 .   ? 125.495 20.220 12.738  1.00 41.76  ? 836 HOH   A O   1 
HETATM 2718 O  O   . HOH   G 5 .   ? 136.008 31.314 4.491   1.00 90.32  ? 837 HOH   A O   1 
HETATM 2719 O  O   . HOH   G 5 .   ? 122.822 1.379  17.713  1.00 87.17  ? 838 HOH   A O   1 
HETATM 2720 O  O   . HOH   G 5 .   ? 114.047 3.542  16.350  1.00 53.01  ? 839 HOH   A O   1 
HETATM 2721 O  O   . HOH   G 5 .   ? 136.678 28.574 7.555   1.00 74.60  ? 840 HOH   A O   1 
HETATM 2722 O  O   . HOH   G 5 .   ? 109.611 1.363  -15.568 1.00 73.50  ? 841 HOH   A O   1 
HETATM 2723 O  O   . HOH   G 5 .   ? 93.317  23.655 -2.581  1.00 63.72  ? 842 HOH   A O   1 
HETATM 2724 O  O   . HOH   G 5 .   ? 125.738 35.346 -8.540  1.00 68.56  ? 843 HOH   A O   1 
HETATM 2725 O  O   . HOH   G 5 .   ? 121.818 4.661  19.030  1.00 56.58  ? 844 HOH   A O   1 
HETATM 2726 O  O   . HOH   G 5 .   ? 131.925 35.661 1.997   1.00 60.09  ? 845 HOH   A O   1 
HETATM 2727 O  O   . HOH   G 5 .   ? 118.366 31.284 16.926  1.00 38.99  ? 846 HOH   A O   1 
HETATM 2728 O  O   . HOH   G 5 .   ? 93.961  19.739 -2.978  1.00 75.03  ? 847 HOH   A O   1 
HETATM 2729 O  O   . HOH   G 5 .   ? 94.297  10.095 10.357  1.00 68.78  ? 848 HOH   A O   1 
HETATM 2730 O  O   . HOH   G 5 .   ? 134.895 13.286 2.628   1.00 45.66  ? 849 HOH   A O   1 
HETATM 2731 O  O   . HOH   G 5 .   ? 102.350 11.344 -8.188  1.00 51.53  ? 850 HOH   A O   1 
HETATM 2732 O  O   . HOH   G 5 .   ? 138.835 23.606 4.625   1.00 65.81  ? 851 HOH   A O   1 
HETATM 2733 O  O   . HOH   G 5 .   ? 140.241 17.980 5.823   1.00 88.21  ? 852 HOH   A O   1 
HETATM 2734 O  O   . HOH   G 5 .   ? 120.156 28.795 17.275  1.00 69.75  ? 853 HOH   A O   1 
HETATM 2735 O  O   . HOH   G 5 .   ? 102.008 9.285  14.327  1.00 83.45  ? 854 HOH   A O   1 
HETATM 2736 O  O   . HOH   G 5 .   ? 97.961  10.234 -8.006  1.00 76.22  ? 855 HOH   A O   1 
HETATM 2737 O  O   . HOH   G 5 .   ? 117.156 28.744 18.582  1.00 66.67  ? 856 HOH   A O   1 
HETATM 2738 O  O   . HOH   G 5 .   ? 107.752 12.069 -21.451 1.00 71.59  ? 857 HOH   A O   1 
HETATM 2739 O  O   . HOH   G 5 .   ? 143.691 30.142 -8.101  1.00 78.77  ? 858 HOH   A O   1 
HETATM 2740 O  O   . HOH   G 5 .   ? 98.854  1.702  -2.846  1.00 78.52  ? 859 HOH   A O   1 
HETATM 2741 O  O   . HOH   G 5 .   ? 134.261 35.022 4.528   1.00 77.55  ? 860 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   . MET A 21  ? 1.1763 0.5293 0.6261 0.1229  -0.0181 -0.0421 1   MET A N   
2    C CA  . MET A 21  ? 1.1662 0.5469 0.6384 0.1245  -0.0098 -0.0414 1   MET A CA  
3    C C   . MET A 21  ? 1.1488 0.5584 0.6481 0.1109  -0.0168 -0.0390 1   MET A C   
4    O O   . MET A 21  ? 1.1401 0.5650 0.6572 0.1068  -0.0208 -0.0370 1   MET A O   
5    C CB  . MET A 21  ? 1.1627 0.5615 0.6546 0.1388  0.0033  -0.0410 1   MET A CB  
6    C CG  . MET A 21  ? 1.1690 0.5993 0.6891 0.1397  0.0122  -0.0400 1   MET A CG  
7    S SD  . MET A 21  ? 1.2027 0.6172 0.7029 0.1450  0.0241  -0.0418 1   MET A SD  
8    C CE  . MET A 21  ? 1.1866 0.5779 0.6698 0.1636  0.0375  -0.0438 1   MET A CE  
9    N N   . PRO A 22  ? 1.1388 0.5544 0.6398 0.1044  -0.0181 -0.0392 2   PRO A N   
10   C CA  . PRO A 22  ? 1.1185 0.5622 0.6464 0.0924  -0.0237 -0.0370 2   PRO A CA  
11   C C   . PRO A 22  ? 1.0952 0.5735 0.6554 0.0969  -0.0154 -0.0350 2   PRO A C   
12   O O   . PRO A 22  ? 1.0931 0.5767 0.6578 0.1086  -0.0044 -0.0356 2   PRO A O   
13   C CB  . PRO A 22  ? 1.1301 0.5677 0.6482 0.0875  -0.0264 -0.0382 2   PRO A CB  
14   C CG  . PRO A 22  ? 1.1501 0.5677 0.6452 0.1000  -0.0161 -0.0403 2   PRO A CG  
15   C CD  . PRO A 22  ? 1.1455 0.5414 0.6232 0.1086  -0.0139 -0.0414 2   PRO A CD  
16   N N   . GLU A 23  ? 1.0727 0.5736 0.6559 0.0878  -0.0206 -0.0327 3   GLU A N   
17   C CA  . GLU A 23  ? 1.0530 0.5848 0.6655 0.0911  -0.0152 -0.0309 3   GLU A CA  
18   C C   . GLU A 23  ? 1.0269 0.5827 0.6596 0.0819  -0.0166 -0.0294 3   GLU A C   
19   O O   . GLU A 23  ? 1.0297 0.5810 0.6584 0.0710  -0.0243 -0.0291 3   GLU A O   
20   C CB  . GLU A 23  ? 1.0887 0.6235 0.7081 0.0911  -0.0193 -0.0293 3   GLU A CB  
21   C CG  . GLU A 23  ? 1.1864 0.6955 0.7845 0.0996  -0.0194 -0.0306 3   GLU A CG  
22   C CD  . GLU A 23  ? 1.2932 0.8019 0.8946 0.1003  -0.0238 -0.0290 3   GLU A CD  
23   O OE1 . GLU A 23  ? 1.2987 0.8305 0.9221 0.0987  -0.0242 -0.0271 3   GLU A OE1 
24   O OE2 . GLU A 23  ? 1.3462 0.8295 0.9263 0.1027  -0.0269 -0.0295 3   GLU A OE2 
25   N N   . GLU A 24  ? 0.9995 0.5806 0.6552 0.0863  -0.0097 -0.0287 4   GLU A N   
26   C CA  . GLU A 24  ? 0.9796 0.5838 0.6548 0.0785  -0.0105 -0.0273 4   GLU A CA  
27   C C   . GLU A 24  ? 0.9694 0.5858 0.6580 0.0696  -0.0176 -0.0250 4   GLU A C   
28   O O   . GLU A 24  ? 0.9705 0.5890 0.6638 0.0731  -0.0183 -0.0242 4   GLU A O   
29   C CB  . GLU A 24  ? 0.9816 0.6075 0.6769 0.0857  -0.0006 -0.0273 4   GLU A CB  
30   C CG  . GLU A 24  ? 0.9922 0.6443 0.7105 0.0786  -0.0013 -0.0256 4   GLU A CG  
31   C CD  . GLU A 24  ? 1.0223 0.6729 0.7348 0.0708  -0.0032 -0.0256 4   GLU A CD  
32   O OE1 . GLU A 24  ? 1.0763 0.7055 0.7675 0.0667  -0.0092 -0.0266 4   GLU A OE1 
33   O OE2 . GLU A 24  ? 0.9555 0.6258 0.6850 0.0688  0.0000  -0.0247 4   GLU A OE2 
34   N N   . SER A 25  ? 0.9559 0.5777 0.6492 0.0584  -0.0228 -0.0241 5   SER A N   
35   C CA  . SER A 25  ? 0.9433 0.5762 0.6497 0.0492  -0.0274 -0.0217 5   SER A CA  
36   C C   . SER A 25  ? 0.9120 0.5694 0.6401 0.0524  -0.0235 -0.0201 5   SER A C   
37   O O   . SER A 25  ? 0.9035 0.5742 0.6418 0.0587  -0.0181 -0.0209 5   SER A O   
38   C CB  . SER A 25  ? 0.9627 0.5997 0.6742 0.0381  -0.0324 -0.0214 5   SER A CB  
39   O OG  . SER A 25  ? 0.9823 0.6360 0.7051 0.0392  -0.0290 -0.0216 5   SER A OG  
40   N N   . SER A 26  ? 0.8887 0.5505 0.6233 0.0478  -0.0262 -0.0180 6   SER A N   
41   C CA  . SER A 26  ? 0.8601 0.5408 0.6115 0.0500  -0.0247 -0.0165 6   SER A CA  
42   C C   . SER A 26  ? 0.8104 0.5138 0.5801 0.0484  -0.0218 -0.0165 6   SER A C   
43   O O   . SER A 26  ? 0.8123 0.5180 0.5833 0.0413  -0.0226 -0.0165 6   SER A O   
44   C CB  . SER A 26  ? 0.8894 0.5670 0.6403 0.0424  -0.0274 -0.0139 6   SER A CB  
45   O OG  . SER A 26  ? 0.9285 0.6186 0.6898 0.0457  -0.0270 -0.0126 6   SER A OG  
46   N N   . PRO A 27  ? 0.7631 0.4822 0.5470 0.0554  -0.0190 -0.0169 7   PRO A N   
47   C CA  . PRO A 27  ? 0.7149 0.4543 0.5159 0.0540  -0.0155 -0.0169 7   PRO A CA  
48   C C   . PRO A 27  ? 0.6488 0.3980 0.4572 0.0438  -0.0177 -0.0150 7   PRO A C   
49   O O   . PRO A 27  ? 0.6525 0.3993 0.4598 0.0393  -0.0206 -0.0133 7   PRO A O   
50   C CB  . PRO A 27  ? 0.7260 0.4795 0.5429 0.0619  -0.0144 -0.0173 7   PRO A CB  
51   C CG  . PRO A 27  ? 0.7533 0.4928 0.5607 0.0698  -0.0164 -0.0182 7   PRO A CG  
52   C CD  . PRO A 27  ? 0.7531 0.4712 0.5391 0.0649  -0.0197 -0.0174 7   PRO A CD  
53   N N   . ARG A 28  ? 0.5963 0.3546 0.4110 0.0404  -0.0156 -0.0153 8   ARG A N   
54   C CA  . ARG A 28  ? 0.5544 0.3233 0.3784 0.0316  -0.0175 -0.0138 8   ARG A CA  
55   C C   . ARG A 28  ? 0.5113 0.2967 0.3502 0.0326  -0.0165 -0.0125 8   ARG A C   
56   O O   . ARG A 28  ? 0.5034 0.2978 0.3508 0.0392  -0.0141 -0.0135 8   ARG A O   
57   C CB  . ARG A 28  ? 0.5469 0.3206 0.3729 0.0294  -0.0161 -0.0146 8   ARG A CB  
58   C CG  . ARG A 28  ? 0.5786 0.3336 0.3876 0.0271  -0.0195 -0.0160 8   ARG A CG  
59   C CD  . ARG A 28  ? 0.5803 0.3324 0.3909 0.0173  -0.0260 -0.0152 8   ARG A CD  
60   N NE  . ARG A 28  ? 0.5823 0.3471 0.4042 0.0126  -0.0273 -0.0148 8   ARG A NE  
61   C CZ  . ARG A 28  ? 0.5633 0.3213 0.3779 0.0117  -0.0306 -0.0162 8   ARG A CZ  
62   N NH1 . ARG A 28  ? 0.5492 0.2866 0.3436 0.0150  -0.0326 -0.0183 8   ARG A NH1 
63   N NH2 . ARG A 28  ? 0.5402 0.3096 0.3653 0.0079  -0.0323 -0.0158 8   ARG A NH2 
64   N N   . ARG A 29  ? 0.4843 0.2716 0.3259 0.0264  -0.0184 -0.0105 9   ARG A N   
65   C CA  . ARG A 29  ? 0.4606 0.2588 0.3117 0.0275  -0.0182 -0.0093 9   ARG A CA  
66   C C   . ARG A 29  ? 0.4288 0.2391 0.2903 0.0205  -0.0171 -0.0079 9   ARG A C   
67   O O   . ARG A 29  ? 0.4363 0.2442 0.2977 0.0137  -0.0173 -0.0072 9   ARG A O   
68   C CB  . ARG A 29  ? 0.4827 0.2676 0.3229 0.0281  -0.0202 -0.0080 9   ARG A CB  
69   C CG  . ARG A 29  ? 0.5281 0.3004 0.3578 0.0363  -0.0222 -0.0093 9   ARG A CG  
70   C CD  . ARG A 29  ? 0.5787 0.3343 0.3941 0.0364  -0.0243 -0.0077 9   ARG A CD  
71   N NE  . ARG A 29  ? 0.6443 0.3861 0.4484 0.0444  -0.0268 -0.0091 9   ARG A NE  
72   C CZ  . ARG A 29  ? 0.6900 0.4314 0.4947 0.0534  -0.0305 -0.0101 9   ARG A CZ  
73   N NH1 . ARG A 29  ? 0.6723 0.4245 0.4865 0.0550  -0.0329 -0.0099 9   ARG A NH1 
74   N NH2 . ARG A 29  ? 0.7052 0.4336 0.5003 0.0610  -0.0328 -0.0115 9   ARG A NH2 
75   N N   . THR A 30  ? 0.3962 0.2182 0.2670 0.0223  -0.0167 -0.0075 10  THR A N   
76   C CA  . THR A 30  ? 0.3928 0.2251 0.2725 0.0165  -0.0152 -0.0060 10  THR A CA  
77   C C   . THR A 30  ? 0.4094 0.2321 0.2828 0.0109  -0.0142 -0.0036 10  THR A C   
78   O O   . THR A 30  ? 0.4265 0.2342 0.2877 0.0122  -0.0148 -0.0031 10  THR A O   
79   C CB  . THR A 30  ? 0.3896 0.2326 0.2773 0.0202  -0.0158 -0.0061 10  THR A CB  
80   O OG1 . THR A 30  ? 0.4115 0.2444 0.2903 0.0239  -0.0185 -0.0056 10  THR A OG1 
81   C CG2 . THR A 30  ? 0.3891 0.2417 0.2861 0.0257  -0.0157 -0.0083 10  THR A CG2 
82   N N   . PRO A 31  ? 0.4099 0.2401 0.2917 0.0051  -0.0116 -0.0021 11  PRO A N   
83   C CA  . PRO A 31  ? 0.4244 0.2455 0.3021 0.0000  -0.0081 0.0004  11  PRO A CA  
84   C C   . PRO A 31  ? 0.4396 0.2498 0.3044 0.0045  -0.0074 0.0015  11  PRO A C   
85   O O   . PRO A 31  ? 0.4721 0.2684 0.3273 0.0017  -0.0037 0.0037  11  PRO A O   
86   C CB  . PRO A 31  ? 0.4226 0.2563 0.3143 -0.0053 -0.0050 0.0015  11  PRO A CB  
87   C CG  . PRO A 31  ? 0.4199 0.2657 0.3208 -0.0047 -0.0084 -0.0007 11  PRO A CG  
88   C CD  . PRO A 31  ? 0.3971 0.2428 0.2920 0.0028  -0.0109 -0.0025 11  PRO A CD  
89   N N   . GLN A 32  ? 0.4235 0.2382 0.2875 0.0115  -0.0113 0.0001  12  GLN A N   
90   C CA  . GLN A 32  ? 0.4381 0.2408 0.2887 0.0170  -0.0138 0.0005  12  GLN A CA  
91   C C   . GLN A 32  ? 0.4698 0.2607 0.3099 0.0235  -0.0187 -0.0010 12  GLN A C   
92   O O   . GLN A 32  ? 0.4862 0.2684 0.3169 0.0299  -0.0235 -0.0014 12  GLN A O   
93   C CB  . GLN A 32  ? 0.4317 0.2451 0.2890 0.0206  -0.0168 -0.0005 12  GLN A CB  
94   C CG  . GLN A 32  ? 0.4320 0.2555 0.2981 0.0150  -0.0119 0.0009  12  GLN A CG  
95   C CD  . GLN A 32  ? 0.4063 0.2471 0.2896 0.0111  -0.0103 0.0000  12  GLN A CD  
96   O OE1 . GLN A 32  ? 0.4071 0.2557 0.2974 0.0139  -0.0132 -0.0021 12  GLN A OE1 
97   N NE2 . GLN A 32  ? 0.3946 0.2403 0.2845 0.0049  -0.0053 0.0016  12  GLN A NE2 
98   N N   . SER A 33  ? 0.4733 0.2632 0.3147 0.0222  -0.0182 -0.0018 13  SER A N   
99   C CA  A SER A 33  ? 0.4914 0.2696 0.3231 0.0277  -0.0215 -0.0032 13  SER A CA  
100  C CA  B SER A 33  ? 0.4845 0.2624 0.3159 0.0278  -0.0216 -0.0031 13  SER A CA  
101  C C   . SER A 33  ? 0.4866 0.2730 0.3258 0.0367  -0.0263 -0.0059 13  SER A C   
102  O O   . SER A 33  ? 0.5071 0.2826 0.3379 0.0433  -0.0298 -0.0070 13  SER A O   
103  C CB  A SER A 33  ? 0.5394 0.2948 0.3508 0.0287  -0.0218 -0.0014 13  SER A CB  
104  C CB  B SER A 33  ? 0.5136 0.2691 0.3248 0.0292  -0.0221 -0.0014 13  SER A CB  
105  O OG  A SER A 33  ? 0.5939 0.3440 0.3980 0.0352  -0.0262 -0.0015 13  SER A OG  
106  O OG  B SER A 33  ? 0.5374 0.2851 0.3439 0.0206  -0.0158 0.0014  13  SER A OG  
107  N N   . ILE A 34  ? 0.4529 0.2581 0.3092 0.0370  -0.0258 -0.0072 14  ILE A N   
108  C CA  . ILE A 34  ? 0.4486 0.2633 0.3167 0.0448  -0.0285 -0.0098 14  ILE A CA  
109  C C   . ILE A 34  ? 0.4477 0.2658 0.3199 0.0449  -0.0241 -0.0111 14  ILE A C   
110  O O   . ILE A 34  ? 0.4411 0.2657 0.3169 0.0388  -0.0203 -0.0105 14  ILE A O   
111  C CB  . ILE A 34  ? 0.4543 0.2860 0.3390 0.0452  -0.0298 -0.0105 14  ILE A CB  
112  C CG1 . ILE A 34  ? 0.4809 0.3057 0.3576 0.0455  -0.0348 -0.0094 14  ILE A CG1 
113  C CG2 . ILE A 34  ? 0.4501 0.2926 0.3514 0.0525  -0.0314 -0.0133 14  ILE A CG2 
114  C CD1 . ILE A 34  ? 0.5018 0.3395 0.3924 0.0469  -0.0385 -0.0106 14  ILE A CD1 
115  N N   . PRO A 35  ? 0.4496 0.2624 0.3203 0.0520  -0.0246 -0.0129 15  PRO A N   
116  C CA  . PRO A 35  ? 0.4412 0.2543 0.3125 0.0527  -0.0193 -0.0141 15  PRO A CA  
117  C C   . PRO A 35  ? 0.4281 0.2585 0.3159 0.0514  -0.0145 -0.0147 15  PRO A C   
118  O O   . PRO A 35  ? 0.4267 0.2703 0.3309 0.0548  -0.0152 -0.0156 15  PRO A O   
119  C CB  . PRO A 35  ? 0.4567 0.2631 0.3271 0.0625  -0.0201 -0.0160 15  PRO A CB  
120  C CG  . PRO A 35  ? 0.4789 0.2745 0.3402 0.0652  -0.0273 -0.0153 15  PRO A CG  
121  C CD  . PRO A 35  ? 0.4561 0.2607 0.3235 0.0606  -0.0301 -0.0140 15  PRO A CD  
122  N N   . TYR A 36  ? 0.4164 0.2454 0.2993 0.0466  -0.0104 -0.0144 16  TYR A N   
123  C CA  . TYR A 36  ? 0.4079 0.2494 0.3024 0.0459  -0.0051 -0.0149 16  TYR A CA  
124  C C   . TYR A 36  ? 0.4166 0.2621 0.3210 0.0540  0.0005  -0.0168 16  TYR A C   
125  O O   . TYR A 36  ? 0.4092 0.2682 0.3294 0.0545  0.0048  -0.0171 16  TYR A O   
126  C CB  . TYR A 36  ? 0.4051 0.2403 0.2889 0.0403  -0.0031 -0.0144 16  TYR A CB  
127  C CG  . TYR A 36  ? 0.3882 0.2276 0.2730 0.0321  -0.0069 -0.0127 16  TYR A CG  
128  C CD1 . TYR A 36  ? 0.3668 0.2212 0.2648 0.0295  -0.0061 -0.0120 16  TYR A CD1 
129  C CD2 . TYR A 36  ? 0.3904 0.2187 0.2644 0.0270  -0.0108 -0.0118 16  TYR A CD2 
130  C CE1 . TYR A 36  ? 0.3633 0.2213 0.2628 0.0227  -0.0086 -0.0104 16  TYR A CE1 
131  C CE2 . TYR A 36  ? 0.3860 0.2192 0.2644 0.0197  -0.0130 -0.0102 16  TYR A CE2 
132  C CZ  . TYR A 36  ? 0.3708 0.2189 0.2617 0.0180  -0.0116 -0.0095 16  TYR A CZ  
133  O OH  . TYR A 36  ? 0.3638 0.2164 0.2595 0.0117  -0.0128 -0.0079 16  TYR A OH  
134  N N   . GLN A 37  ? 0.4302 0.2643 0.3272 0.0605  0.0009  -0.0179 17  GLN A N   
135  C CA  . GLN A 37  ? 0.4464 0.2850 0.3559 0.0690  0.0074  -0.0197 17  GLN A CA  
136  C C   . GLN A 37  ? 0.4441 0.3007 0.3797 0.0724  0.0046  -0.0206 17  GLN A C   
137  O O   . GLN A 37  ? 0.4522 0.3185 0.4064 0.0774  0.0111  -0.0219 17  GLN A O   
138  C CB  . GLN A 37  ? 0.4853 0.3075 0.3818 0.0759  0.0082  -0.0209 17  GLN A CB  
139  C CG  . GLN A 37  ? 0.5552 0.3709 0.4469 0.0784  -0.0011 -0.0208 17  GLN A CG  
140  C CD  . GLN A 37  ? 0.6672 0.4641 0.5427 0.0848  -0.0003 -0.0219 17  GLN A CD  
141  O OE1 . GLN A 37  ? 0.7089 0.4945 0.5718 0.0859  0.0064  -0.0224 17  GLN A OE1 
142  N NE2 . GLN A 37  ? 0.6896 0.4804 0.5626 0.0894  -0.0074 -0.0222 17  GLN A NE2 
143  N N   . ASP A 38  ? 0.4289 0.2889 0.3659 0.0696  -0.0048 -0.0198 18  ASP A N   
144  C CA  . ASP A 38  ? 0.4203 0.2945 0.3792 0.0725  -0.0102 -0.0208 18  ASP A CA  
145  C C   . ASP A 38  ? 0.4013 0.2896 0.3717 0.0659  -0.0095 -0.0200 18  ASP A C   
146  O O   . ASP A 38  ? 0.3993 0.2971 0.3844 0.0668  -0.0160 -0.0208 18  ASP A O   
147  C CB  . ASP A 38  ? 0.4517 0.3167 0.4004 0.0740  -0.0217 -0.0206 18  ASP A CB  
148  C CG  . ASP A 38  ? 0.5566 0.4061 0.4927 0.0808  -0.0240 -0.0213 18  ASP A CG  
149  O OD1 . ASP A 38  ? 0.5550 0.4041 0.4964 0.0863  -0.0176 -0.0227 18  ASP A OD1 
150  O OD2 . ASP A 38  ? 0.6242 0.4602 0.5438 0.0808  -0.0314 -0.0204 18  ASP A OD2 
151  N N   . LEU A 39  ? 0.3831 0.2707 0.3450 0.0595  -0.0033 -0.0186 19  LEU A N   
152  C CA  . LEU A 39  ? 0.3752 0.2741 0.3454 0.0534  -0.0028 -0.0177 19  LEU A CA  
153  C C   . LEU A 39  ? 0.3705 0.2723 0.3425 0.0513  0.0076  -0.0175 19  LEU A C   
154  O O   . LEU A 39  ? 0.3862 0.2762 0.3432 0.0520  0.0127  -0.0173 19  LEU A O   
155  C CB  . LEU A 39  ? 0.3949 0.2869 0.3482 0.0466  -0.0074 -0.0156 19  LEU A CB  
156  C CG  . LEU A 39  ? 0.4348 0.3191 0.3796 0.0475  -0.0160 -0.0152 19  LEU A CG  
157  C CD1 . LEU A 39  ? 0.4547 0.3312 0.3838 0.0405  -0.0167 -0.0129 19  LEU A CD1 
158  C CD2 . LEU A 39  ? 0.4431 0.3362 0.4016 0.0496  -0.0224 -0.0161 19  LEU A CD2 
159  N N   . PRO A 40  ? 0.3488 0.2631 0.3351 0.0481  0.0103  -0.0173 20  PRO A N   
160  C CA  . PRO A 40  ? 0.3391 0.2524 0.3219 0.0455  0.0200  -0.0166 20  PRO A CA  
161  C C   . PRO A 40  ? 0.3310 0.2331 0.2911 0.0401  0.0175  -0.0151 20  PRO A C   
162  O O   . PRO A 40  ? 0.3339 0.2373 0.2904 0.0359  0.0102  -0.0141 20  PRO A O   
163  C CB  . PRO A 40  ? 0.3436 0.2717 0.3455 0.0424  0.0211  -0.0166 20  PRO A CB  
164  C CG  . PRO A 40  ? 0.3482 0.2858 0.3673 0.0449  0.0126  -0.0178 20  PRO A CG  
165  C CD  . PRO A 40  ? 0.3414 0.2682 0.3442 0.0465  0.0040  -0.0176 20  PRO A CD  
166  N N   . HIS A 41  ? 0.3338 0.2236 0.2786 0.0407  0.0235  -0.0150 21  HIS A N   
167  C CA  . HIS A 41  ? 0.3478 0.2263 0.2730 0.0360  0.0194  -0.0141 21  HIS A CA  
168  C C   . HIS A 41  ? 0.3639 0.2305 0.2744 0.0362  0.0257  -0.0141 21  HIS A C   
169  O O   . HIS A 41  ? 0.3936 0.2580 0.3061 0.0405  0.0356  -0.0147 21  HIS A O   
170  C CB  . HIS A 41  ? 0.3585 0.2256 0.2711 0.0369  0.0134  -0.0143 21  HIS A CB  
171  C CG  . HIS A 41  ? 0.3931 0.2482 0.2972 0.0434  0.0183  -0.0157 21  HIS A CG  
172  N ND1 . HIS A 41  ? 0.4145 0.2743 0.3303 0.0496  0.0197  -0.0167 21  HIS A ND1 
173  C CD2 . HIS A 41  ? 0.4390 0.2768 0.3239 0.0451  0.0219  -0.0163 21  HIS A CD2 
174  C CE1 . HIS A 41  ? 0.4424 0.2886 0.3466 0.0549  0.0250  -0.0177 21  HIS A CE1 
175  N NE2 . HIS A 41  ? 0.4596 0.2913 0.3437 0.0525  0.0269  -0.0175 21  HIS A NE2 
176  N N   . LEU A 42  ? 0.3652 0.2228 0.2609 0.0317  0.0201  -0.0136 22  LEU A N   
177  C CA  A LEU A 42  ? 0.3980 0.2399 0.2747 0.0316  0.0225  -0.0138 22  LEU A CA  
178  C CA  B LEU A 42  ? 0.3991 0.2401 0.2750 0.0320  0.0227  -0.0139 22  LEU A CA  
179  C C   . LEU A 42  ? 0.4246 0.2534 0.2855 0.0284  0.0126  -0.0141 22  LEU A C   
180  O O   . LEU A 42  ? 0.4415 0.2786 0.3109 0.0238  0.0051  -0.0134 22  LEU A O   
181  C CB  A LEU A 42  ? 0.3999 0.2499 0.2822 0.0279  0.0235  -0.0127 22  LEU A CB  
182  C CB  B LEU A 42  ? 0.4044 0.2497 0.2827 0.0299  0.0267  -0.0130 22  LEU A CB  
183  C CG  A LEU A 42  ? 0.4432 0.2767 0.3062 0.0288  0.0275  -0.0128 22  LEU A CG  
184  C CG  B LEU A 42  ? 0.4293 0.2804 0.3097 0.0238  0.0184  -0.0121 22  LEU A CG  
185  C CD1 A LEU A 42  ? 0.4546 0.2805 0.3135 0.0347  0.0411  -0.0132 22  LEU A CD1 
186  C CD1 B LEU A 42  ? 0.4617 0.2948 0.3210 0.0222  0.0117  -0.0126 22  LEU A CD1 
187  C CD2 A LEU A 42  ? 0.4444 0.2858 0.3129 0.0248  0.0262  -0.0117 22  LEU A CD2 
188  C CD2 B LEU A 42  ? 0.4330 0.2926 0.3216 0.0227  0.0239  -0.0112 22  LEU A CD2 
189  N N   . VAL A 43  ? 0.4083 0.2158 0.2467 0.0306  0.0124  -0.0152 23  VAL A N   
190  C CA  . VAL A 43  ? 0.4147 0.2093 0.2401 0.0269  0.0014  -0.0158 23  VAL A CA  
191  C C   . VAL A 43  ? 0.4259 0.2131 0.2415 0.0241  -0.0033 -0.0159 23  VAL A C   
192  O O   . VAL A 43  ? 0.4380 0.2118 0.2376 0.0279  0.0024  -0.0163 23  VAL A O   
193  C CB  . VAL A 43  ? 0.4395 0.2128 0.2447 0.0309  0.0010  -0.0174 23  VAL A CB  
194  C CG1 . VAL A 43  ? 0.4494 0.2108 0.2450 0.0258  -0.0117 -0.0182 23  VAL A CG1 
195  C CG2 . VAL A 43  ? 0.4297 0.2096 0.2444 0.0348  0.0058  -0.0173 23  VAL A CG2 
196  N N   . ASN A 44  ? 0.4131 0.2079 0.2379 0.0180  -0.0130 -0.0155 24  ASN A N   
197  C CA  . ASN A 44  ? 0.4169 0.2058 0.2349 0.0159  -0.0191 -0.0157 24  ASN A CA  
198  C C   . ASN A 44  ? 0.4450 0.2076 0.2384 0.0165  -0.0285 -0.0178 24  ASN A C   
199  O O   . ASN A 44  ? 0.4597 0.2084 0.2408 0.0184  -0.0295 -0.0190 24  ASN A O   
200  C CB  . ASN A 44  ? 0.4110 0.2191 0.2510 0.0100  -0.0248 -0.0146 24  ASN A CB  
201  C CG  . ASN A 44  ? 0.4188 0.2277 0.2667 0.0048  -0.0348 -0.0149 24  ASN A CG  
202  O OD1 . ASN A 44  ? 0.4274 0.2214 0.2637 0.0048  -0.0397 -0.0163 24  ASN A OD1 
203  N ND2 . ASN A 44  ? 0.3943 0.2199 0.2626 0.0001  -0.0375 -0.0137 24  ASN A ND2 
204  N N   . ALA A 45  ? 0.4642 0.2181 0.2491 0.0153  -0.0363 -0.0184 25  ALA A N   
205  C CA  . ALA A 45  ? 0.5006 0.2272 0.2605 0.0162  -0.0476 -0.0207 25  ALA A CA  
206  C C   . ALA A 45  ? 0.5153 0.2399 0.2821 0.0113  -0.0603 -0.0221 25  ALA A C   
207  O O   . ALA A 45  ? 0.5507 0.2507 0.2957 0.0123  -0.0692 -0.0244 25  ALA A O   
208  C CB  . ALA A 45  ? 0.5102 0.2297 0.2624 0.0162  -0.0550 -0.0212 25  ALA A CB  
209  N N   . ASP A 46  ? 0.4935 0.2419 0.2894 0.0057  -0.0608 -0.0207 26  ASP A N   
210  C CA  . ASP A 46  ? 0.4957 0.2444 0.3021 0.0002  -0.0699 -0.0215 26  ASP A CA  
211  C C   . ASP A 46  ? 0.5062 0.2533 0.3102 0.0013  -0.0629 -0.0211 26  ASP A C   
212  O O   . ASP A 46  ? 0.5213 0.2688 0.3342 -0.0035 -0.0683 -0.0213 26  ASP A O   
213  C CB  . ASP A 46  ? 0.4973 0.2694 0.3352 -0.0065 -0.0734 -0.0201 26  ASP A CB  
214  C CG  . ASP A 46  ? 0.5565 0.3280 0.3979 -0.0077 -0.0835 -0.0211 26  ASP A CG  
215  O OD1 . ASP A 46  ? 0.6175 0.3672 0.4397 -0.0062 -0.0947 -0.0236 26  ASP A OD1 
216  O OD2 . ASP A 46  ? 0.5540 0.3453 0.4161 -0.0097 -0.0809 -0.0195 26  ASP A OD2 
217  N N   . GLY A 47  ? 0.4946 0.2389 0.2870 0.0078  -0.0511 -0.0206 27  GLY A N   
218  C CA  . GLY A 47  ? 0.4944 0.2367 0.2843 0.0103  -0.0447 -0.0203 27  GLY A CA  
219  C C   . GLY A 47  ? 0.4731 0.2386 0.2872 0.0078  -0.0393 -0.0181 27  GLY A C   
220  O O   . GLY A 47  ? 0.4844 0.2478 0.2982 0.0086  -0.0370 -0.0179 27  GLY A O   
221  N N   . GLN A 48  ? 0.4411 0.2266 0.2741 0.0052  -0.0373 -0.0165 28  GLN A N   
222  C CA  . GLN A 48  ? 0.4150 0.2198 0.2680 0.0031  -0.0326 -0.0145 28  GLN A CA  
223  C C   . GLN A 48  ? 0.4038 0.2187 0.2603 0.0086  -0.0228 -0.0137 28  GLN A C   
224  O O   . GLN A 48  ? 0.4056 0.2218 0.2591 0.0112  -0.0191 -0.0140 28  GLN A O   
225  C CB  . GLN A 48  ? 0.4173 0.2369 0.2890 -0.0029 -0.0361 -0.0132 28  GLN A CB  
226  C CG  . GLN A 48  ? 0.4304 0.2438 0.3064 -0.0091 -0.0459 -0.0139 28  GLN A CG  
227  C CD  . GLN A 48  ? 0.4312 0.2585 0.3262 -0.0137 -0.0492 -0.0131 28  GLN A CD  
228  O OE1 . GLN A 48  ? 0.4310 0.2610 0.3246 -0.0118 -0.0504 -0.0135 28  GLN A OE1 
229  N NE2 . GLN A 48  ? 0.4212 0.2561 0.3335 -0.0195 -0.0500 -0.0119 28  GLN A NE2 
230  N N   . TYR A 49  ? 0.3925 0.2136 0.2554 0.0102  -0.0189 -0.0129 29  TYR A N   
231  C CA  . TYR A 49  ? 0.3726 0.2045 0.2429 0.0153  -0.0114 -0.0126 29  TYR A CA  
232  C C   . TYR A 49  ? 0.3613 0.2108 0.2480 0.0123  -0.0106 -0.0111 29  TYR A C   
233  O O   . TYR A 49  ? 0.3600 0.2150 0.2544 0.0079  -0.0135 -0.0099 29  TYR A O   
234  C CB  . TYR A 49  ? 0.3722 0.2027 0.2430 0.0188  -0.0099 -0.0125 29  TYR A CB  
235  C CG  . TYR A 49  ? 0.3927 0.2077 0.2487 0.0246  -0.0077 -0.0141 29  TYR A CG  
236  C CD1 . TYR A 49  ? 0.4137 0.2107 0.2536 0.0229  -0.0124 -0.0150 29  TYR A CD1 
237  C CD2 . TYR A 49  ? 0.4018 0.2197 0.2611 0.0318  -0.0009 -0.0149 29  TYR A CD2 
238  C CE1 . TYR A 49  ? 0.4325 0.2130 0.2565 0.0287  -0.0101 -0.0165 29  TYR A CE1 
239  C CE2 . TYR A 49  ? 0.4160 0.2193 0.2624 0.0378  0.0023  -0.0163 29  TYR A CE2 
240  C CZ  . TYR A 49  ? 0.4388 0.2225 0.2659 0.0364  -0.0021 -0.0171 29  TYR A CZ  
241  O OH  . TYR A 49  ? 0.4628 0.2297 0.2744 0.0429  0.0014  -0.0186 29  TYR A OH  
242  N N   . LEU A 50  ? 0.3436 0.2007 0.2351 0.0149  -0.0055 -0.0112 30  LEU A N   
243  C CA  . LEU A 50  ? 0.3300 0.2029 0.2362 0.0129  -0.0043 -0.0101 30  LEU A CA  
244  C C   . LEU A 50  ? 0.3295 0.2108 0.2452 0.0173  0.0000  -0.0104 30  LEU A C   
245  O O   . LEU A 50  ? 0.3462 0.2247 0.2605 0.0220  0.0051  -0.0114 30  LEU A O   
246  C CB  . LEU A 50  ? 0.3322 0.2073 0.2381 0.0118  -0.0025 -0.0100 30  LEU A CB  
247  C CG  . LEU A 50  ? 0.3679 0.2334 0.2642 0.0086  -0.0084 -0.0103 30  LEU A CG  
248  C CD1 . LEU A 50  ? 0.3831 0.2502 0.2785 0.0082  -0.0072 -0.0101 30  LEU A CD1 
249  C CD2 . LEU A 50  ? 0.3722 0.2416 0.2763 0.0033  -0.0147 -0.0095 30  LEU A CD2 
250  N N   . PHE A 51  ? 0.3067 0.1970 0.2320 0.0161  -0.0021 -0.0095 31  PHE A N   
251  C CA  . PHE A 51  ? 0.3021 0.2004 0.2380 0.0202  -0.0007 -0.0101 31  PHE A CA  
252  C C   . PHE A 51  ? 0.2895 0.1983 0.2361 0.0197  0.0031  -0.0103 31  PHE A C   
253  O O   . PHE A 51  ? 0.2922 0.2049 0.2399 0.0156  0.0022  -0.0093 31  PHE A O   
254  C CB  . PHE A 51  ? 0.3028 0.2030 0.2408 0.0190  -0.0054 -0.0092 31  PHE A CB  
255  C CG  . PHE A 51  ? 0.3108 0.2192 0.2602 0.0224  -0.0069 -0.0100 31  PHE A CG  
256  C CD1 . PHE A 51  ? 0.3311 0.2378 0.2838 0.0282  -0.0084 -0.0115 31  PHE A CD1 
257  C CD2 . PHE A 51  ? 0.3165 0.2336 0.2738 0.0201  -0.0076 -0.0096 31  PHE A CD2 
258  C CE1 . PHE A 51  ? 0.3423 0.2568 0.3081 0.0314  -0.0117 -0.0126 31  PHE A CE1 
259  C CE2 . PHE A 51  ? 0.3256 0.2492 0.2939 0.0230  -0.0106 -0.0108 31  PHE A CE2 
260  C CZ  . PHE A 51  ? 0.3298 0.2525 0.3032 0.0286  -0.0132 -0.0124 31  PHE A CZ  
261  N N   . CYS A 52  ? 0.2807 0.1941 0.2369 0.0240  0.0075  -0.0115 32  CYS A N   
262  C CA  . CYS A 52  ? 0.2821 0.2046 0.2501 0.0235  0.0126  -0.0117 32  CYS A CA  
263  C C   . CYS A 52  ? 0.2888 0.2230 0.2756 0.0251  0.0104  -0.0126 32  CYS A C   
264  O O   . CYS A 52  ? 0.2961 0.2307 0.2881 0.0291  0.0067  -0.0136 32  CYS A O   
265  C CB  . CYS A 52  ? 0.2959 0.2124 0.2606 0.0264  0.0217  -0.0122 32  CYS A CB  
266  S SG  . CYS A 52  ? 0.3485 0.2473 0.2879 0.0249  0.0225  -0.0117 32  CYS A SG  
267  N N   . ARG A 53  ? 0.2744 0.2172 0.2716 0.0225  0.0125  -0.0124 33  ARG A N   
268  C CA  . ARG A 53  ? 0.2711 0.2250 0.2882 0.0234  0.0099  -0.0136 33  ARG A CA  
269  C C   . ARG A 53  ? 0.2834 0.2437 0.3140 0.0224  0.0187  -0.0139 33  ARG A C   
270  O O   . ARG A 53  ? 0.2809 0.2369 0.3018 0.0195  0.0244  -0.0126 33  ARG A O   
271  C CB  . ARG A 53  ? 0.2807 0.2373 0.2968 0.0200  0.0023  -0.0130 33  ARG A CB  
272  C CG  . ARG A 53  ? 0.3212 0.2710 0.3264 0.0213  -0.0055 -0.0128 33  ARG A CG  
273  C CD  . ARG A 53  ? 0.3294 0.2803 0.3339 0.0190  -0.0116 -0.0125 33  ARG A CD  
274  N NE  . ARG A 53  ? 0.3484 0.2893 0.3370 0.0191  -0.0159 -0.0113 33  ARG A NE  
275  C CZ  . ARG A 53  ? 0.3732 0.3078 0.3581 0.0229  -0.0226 -0.0121 33  ARG A CZ  
276  N NH1 . ARG A 53  ? 0.3686 0.3077 0.3671 0.0269  -0.0278 -0.0144 33  ARG A NH1 
277  N NH2 . ARG A 53  ? 0.3724 0.2954 0.3406 0.0227  -0.0244 -0.0107 33  ARG A NH2 
278  N N   . TYR A 54  ? 0.2781 0.2478 0.3314 0.0249  0.0195  -0.0156 34  TYR A N   
279  C CA  . TYR A 54  ? 0.2892 0.2659 0.3602 0.0239  0.0290  -0.0159 34  TYR A CA  
280  C C   . TYR A 54  ? 0.2954 0.2849 0.3923 0.0231  0.0226  -0.0177 34  TYR A C   
281  O O   . TYR A 54  ? 0.2993 0.2924 0.4057 0.0266  0.0131  -0.0194 34  TYR A O   
282  C CB  . TYR A 54  ? 0.2844 0.2588 0.3615 0.0286  0.0403  -0.0165 34  TYR A CB  
283  C CG  . TYR A 54  ? 0.2946 0.2533 0.3438 0.0297  0.0456  -0.0151 34  TYR A CG  
284  C CD1 . TYR A 54  ? 0.3051 0.2546 0.3386 0.0269  0.0537  -0.0135 34  TYR A CD1 
285  C CD2 . TYR A 54  ? 0.3104 0.2615 0.3468 0.0333  0.0406  -0.0155 34  TYR A CD2 
286  C CE1 . TYR A 54  ? 0.3287 0.2619 0.3352 0.0278  0.0555  -0.0126 34  TYR A CE1 
287  C CE2 . TYR A 54  ? 0.3345 0.2701 0.3450 0.0337  0.0432  -0.0145 34  TYR A CE2 
288  C CZ  . TYR A 54  ? 0.3458 0.2725 0.3416 0.0309  0.0499  -0.0132 34  TYR A CZ  
289  O OH  . TYR A 54  ? 0.3719 0.2816 0.3415 0.0315  0.0504  -0.0126 34  TYR A OH  
290  N N   . TRP A 55  ? 0.2841 0.2788 0.3912 0.0187  0.0268  -0.0174 35  TRP A N   
291  C CA  . TRP A 55  ? 0.2869 0.2933 0.4209 0.0171  0.0213  -0.0193 35  TRP A CA  
292  C C   . TRP A 55  ? 0.3021 0.3137 0.4542 0.0147  0.0358  -0.0190 35  TRP A C   
293  O O   . TRP A 55  ? 0.3126 0.3200 0.4554 0.0102  0.0423  -0.0173 35  TRP A O   
294  C CB  . TRP A 55  ? 0.2836 0.2887 0.4089 0.0129  0.0112  -0.0190 35  TRP A CB  
295  C CG  . TRP A 55  ? 0.2878 0.2854 0.3930 0.0147  -0.0006 -0.0188 35  TRP A CG  
296  C CD1 . TRP A 55  ? 0.3045 0.3021 0.4137 0.0166  -0.0141 -0.0206 35  TRP A CD1 
297  C CD2 . TRP A 55  ? 0.2880 0.2754 0.3655 0.0136  0.0003  -0.0166 35  TRP A CD2 
298  N NE1 . TRP A 55  ? 0.3141 0.3011 0.3980 0.0170  -0.0199 -0.0193 35  TRP A NE1 
299  C CE2 . TRP A 55  ? 0.3032 0.2853 0.3699 0.0149  -0.0110 -0.0169 35  TRP A CE2 
300  C CE3 . TRP A 55  ? 0.2880 0.2693 0.3491 0.0118  0.0090  -0.0144 35  TRP A CE3 
301  C CZ2 . TRP A 55  ? 0.3100 0.2828 0.3534 0.0140  -0.0119 -0.0149 35  TRP A CZ2 
302  C CZ3 . TRP A 55  ? 0.2941 0.2672 0.3338 0.0110  0.0058  -0.0129 35  TRP A CZ3 
303  C CH2 . TRP A 55  ? 0.3069 0.2770 0.3396 0.0118  -0.0037 -0.0130 35  TRP A CH2 
304  N N   . ALA A 56  ? 0.3030 0.3223 0.4802 0.0182  0.0421  -0.0205 36  ALA A N   
305  C CA  . ALA A 56  ? 0.3305 0.3532 0.5256 0.0165  0.0590  -0.0200 36  ALA A CA  
306  C C   . ALA A 56  ? 0.3451 0.3838 0.5807 0.0143  0.0561  -0.0223 36  ALA A C   
307  O O   . ALA A 56  ? 0.3481 0.3960 0.6038 0.0175  0.0437  -0.0250 36  ALA A O   
308  C CB  . ALA A 56  ? 0.3344 0.3522 0.5279 0.0222  0.0723  -0.0196 36  ALA A CB  
309  N N   . PRO A 57  ? 0.3567 0.3978 0.6048 0.0087  0.0669  -0.0215 37  PRO A N   
310  C CA  . PRO A 57  ? 0.3568 0.4137 0.6477 0.0058  0.0647  -0.0239 37  PRO A CA  
311  C C   . PRO A 57  ? 0.3766 0.4440 0.7021 0.0102  0.0758  -0.0253 37  PRO A C   
312  O O   . PRO A 57  ? 0.3805 0.4404 0.6931 0.0151  0.0886  -0.0240 37  PRO A O   
313  C CB  . PRO A 57  ? 0.3658 0.4185 0.6541 -0.0016 0.0757  -0.0219 37  PRO A CB  
314  C CG  . PRO A 57  ? 0.3791 0.4152 0.6337 -0.0003 0.0920  -0.0186 37  PRO A CG  
315  C CD  . PRO A 57  ? 0.3669 0.3951 0.5912 0.0050  0.0816  -0.0183 37  PRO A CD  
316  N N   . THR A 58  ? 0.3897 0.4738 0.7600 0.0086  0.0709  -0.0282 38  THR A N   
317  C CA  . THR A 58  ? 0.4124 0.5089 0.8220 0.0128  0.0815  -0.0298 38  THR A CA  
318  C C   . THR A 58  ? 0.4421 0.5356 0.8603 0.0101  0.1096  -0.0273 38  THR A C   
319  O O   . THR A 58  ? 0.4513 0.5469 0.8844 0.0152  0.1249  -0.0272 38  THR A O   
320  C CB  . THR A 58  ? 0.4128 0.5285 0.8703 0.0127  0.0650  -0.0342 38  THR A CB  
321  O OG1 . THR A 58  ? 0.4264 0.5470 0.9004 0.0039  0.0626  -0.0346 38  THR A OG1 
322  C CG2 . THR A 58  ? 0.4240 0.5384 0.8692 0.0177  0.0388  -0.0367 38  THR A CG2 
323  N N   . GLY A 59  ? 0.4626 0.5491 0.8691 0.0024  0.1170  -0.0251 39  GLY A N   
324  C CA  . GLY A 59  ? 0.4777 0.5571 0.8869 -0.0005 0.1440  -0.0223 39  GLY A CA  
325  C C   . GLY A 59  ? 0.5063 0.5613 0.8625 0.0015  0.1564  -0.0185 39  GLY A C   
326  O O   . GLY A 59  ? 0.5328 0.5785 0.8542 0.0054  0.1446  -0.0183 39  GLY A O   
327  N N   . THR A 60  ? 0.4951 0.5377 0.8442 -0.0013 0.1801  -0.0157 40  THR A N   
328  C CA  . THR A 60  ? 0.5070 0.5232 0.8043 0.0006  0.1915  -0.0122 40  THR A CA  
329  C C   . THR A 60  ? 0.4848 0.4927 0.7501 -0.0041 0.1759  -0.0113 40  THR A C   
330  O O   . THR A 60  ? 0.4761 0.4909 0.7568 -0.0110 0.1717  -0.0115 40  THR A O   
331  C CB  . THR A 60  ? 0.5426 0.5456 0.8407 -0.0013 0.2205  -0.0095 40  THR A CB  
332  O OG1 . THR A 60  ? 0.5442 0.5566 0.8768 0.0033  0.2361  -0.0105 40  THR A OG1 
333  C CG2 . THR A 60  ? 0.5812 0.5527 0.8225 0.0011  0.2313  -0.0061 40  THR A CG2 
334  N N   . PRO A 61  ? 0.4729 0.4675 0.6969 -0.0004 0.1662  -0.0105 41  PRO A N   
335  C CA  . PRO A 61  ? 0.4634 0.4517 0.6607 -0.0044 0.1516  -0.0097 41  PRO A CA  
336  C C   . PRO A 61  ? 0.4552 0.4266 0.6325 -0.0090 0.1648  -0.0068 41  PRO A C   
337  O O   . PRO A 61  ? 0.4710 0.4261 0.6343 -0.0072 0.1846  -0.0048 41  PRO A O   
338  C CB  . PRO A 61  ? 0.4896 0.4670 0.6509 0.0010  0.1415  -0.0094 41  PRO A CB  
339  C CG  . PRO A 61  ? 0.4950 0.4747 0.6660 0.0077  0.1478  -0.0105 41  PRO A CG  
340  C CD  . PRO A 61  ? 0.4703 0.4545 0.6712 0.0073  0.1681  -0.0103 41  PRO A CD  
341  N N   . LYS A 62  ? 0.4250 0.3987 0.6001 -0.0146 0.1544  -0.0068 42  LYS A N   
342  C CA  . LYS A 62  ? 0.4213 0.3779 0.5741 -0.0188 0.1635  -0.0041 42  LYS A CA  
343  C C   . LYS A 62  ? 0.4150 0.3506 0.5192 -0.0152 0.1590  -0.0023 42  LYS A C   
344  O O   . LYS A 62  ? 0.4374 0.3518 0.5145 -0.0158 0.1700  0.0001  42  LYS A O   
345  C CB  . LYS A 62  ? 0.4488 0.4149 0.6148 -0.0254 0.1511  -0.0050 42  LYS A CB  
346  C CG  . LYS A 62  ? 0.4986 0.4828 0.7118 -0.0306 0.1541  -0.0069 42  LYS A CG  
347  C CD  . LYS A 62  ? 0.5754 0.5629 0.7929 -0.0371 0.1421  -0.0075 42  LYS A CD  
348  C CE  . LYS A 62  ? 0.6207 0.6252 0.8853 -0.0431 0.1421  -0.0097 42  LYS A CE  
349  N NZ  . LYS A 62  ? 0.6544 0.6656 0.9239 -0.0470 0.1213  -0.0119 42  LYS A NZ  
350  N N   . ALA A 63  ? 0.3770 0.3177 0.4706 -0.0117 0.1418  -0.0037 43  ALA A N   
351  C CA  . ALA A 63  ? 0.3710 0.2953 0.4249 -0.0088 0.1344  -0.0025 43  ALA A CA  
352  C C   . ALA A 63  ? 0.3595 0.2925 0.4122 -0.0047 0.1199  -0.0042 43  ALA A C   
353  O O   . ALA A 63  ? 0.3468 0.2980 0.4272 -0.0045 0.1133  -0.0063 43  ALA A O   
354  C CB  . ALA A 63  ? 0.3683 0.2898 0.4104 -0.0130 0.1249  -0.0018 43  ALA A CB  
355  N N   . LEU A 64  ? 0.3596 0.2787 0.3805 -0.0016 0.1142  -0.0035 44  LEU A N   
356  C CA  . LEU A 64  ? 0.3467 0.2714 0.3632 0.0015  0.1005  -0.0048 44  LEU A CA  
357  C C   . LEU A 64  ? 0.3255 0.2515 0.3305 -0.0009 0.0859  -0.0045 44  LEU A C   
358  O O   . LEU A 64  ? 0.3358 0.2509 0.3245 -0.0027 0.0873  -0.0031 44  LEU A O   
359  C CB  . LEU A 64  ? 0.3824 0.2886 0.3710 0.0063  0.1044  -0.0042 44  LEU A CB  
360  C CG  . LEU A 64  ? 0.4226 0.3215 0.4144 0.0099  0.1211  -0.0041 44  LEU A CG  
361  C CD1 . LEU A 64  ? 0.4526 0.3278 0.4095 0.0148  0.1239  -0.0035 44  LEU A CD1 
362  C CD2 . LEU A 64  ? 0.4265 0.3447 0.4499 0.0117  0.1199  -0.0060 44  LEU A CD2 
363  N N   . ILE A 65  ? 0.3023 0.2391 0.3133 -0.0002 0.0727  -0.0058 45  ILE A N   
364  C CA  . ILE A 65  ? 0.2965 0.2338 0.2970 -0.0019 0.0606  -0.0054 45  ILE A CA  
365  C C   . ILE A 65  ? 0.2969 0.2363 0.2918 0.0006  0.0508  -0.0061 45  ILE A C   
366  O O   . ILE A 65  ? 0.2884 0.2374 0.2978 0.0019  0.0474  -0.0073 45  ILE A O   
367  C CB  . ILE A 65  ? 0.2908 0.2387 0.3066 -0.0058 0.0556  -0.0058 45  ILE A CB  
368  C CG1 . ILE A 65  ? 0.3090 0.2552 0.3117 -0.0067 0.0452  -0.0052 45  ILE A CG1 
369  C CG2 . ILE A 65  ? 0.2836 0.2465 0.3252 -0.0060 0.0513  -0.0077 45  ILE A CG2 
370  C CD1 . ILE A 65  ? 0.3100 0.2607 0.3208 -0.0103 0.0425  -0.0052 45  ILE A CD1 
371  N N   . PHE A 66  ? 0.2972 0.2265 0.2715 0.0013  0.0462  -0.0053 46  PHE A N   
372  C CA  . PHE A 66  ? 0.2916 0.2220 0.2609 0.0027  0.0373  -0.0057 46  PHE A CA  
373  C C   . PHE A 66  ? 0.2827 0.2210 0.2565 0.0004  0.0283  -0.0055 46  PHE A C   
374  O O   . PHE A 66  ? 0.2852 0.2212 0.2537 -0.0013 0.0271  -0.0047 46  PHE A O   
375  C CB  . PHE A 66  ? 0.3018 0.2168 0.2488 0.0044  0.0362  -0.0053 46  PHE A CB  
376  C CG  . PHE A 66  ? 0.3046 0.2207 0.2488 0.0051  0.0275  -0.0058 46  PHE A CG  
377  C CD1 . PHE A 66  ? 0.3147 0.2290 0.2589 0.0076  0.0286  -0.0066 46  PHE A CD1 
378  C CD2 . PHE A 66  ? 0.3155 0.2337 0.2579 0.0032  0.0190  -0.0053 46  PHE A CD2 
379  C CE1 . PHE A 66  ? 0.3186 0.2326 0.2599 0.0077  0.0210  -0.0069 46  PHE A CE1 
380  C CE2 . PHE A 66  ? 0.3202 0.2393 0.2622 0.0030  0.0125  -0.0056 46  PHE A CE2 
381  C CZ  . PHE A 66  ? 0.3129 0.2291 0.2533 0.0050  0.0134  -0.0064 46  PHE A CZ  
382  N N   . VAL A 67  ? 0.2694 0.2150 0.2509 0.0009  0.0225  -0.0062 47  VAL A N   
383  C CA  . VAL A 67  ? 0.2770 0.2274 0.2603 -0.0006 0.0155  -0.0058 47  VAL A CA  
384  C C   . VAL A 67  ? 0.2843 0.2305 0.2582 -0.0002 0.0109  -0.0053 47  VAL A C   
385  O O   . VAL A 67  ? 0.2828 0.2268 0.2550 0.0014  0.0100  -0.0058 47  VAL A O   
386  C CB  . VAL A 67  ? 0.2955 0.2538 0.2917 -0.0002 0.0121  -0.0069 47  VAL A CB  
387  C CG1 . VAL A 67  ? 0.3183 0.2770 0.3109 -0.0009 0.0058  -0.0064 47  VAL A CG1 
388  C CG2 . VAL A 67  ? 0.2979 0.2613 0.3067 -0.0015 0.0151  -0.0077 47  VAL A CG2 
389  N N   . SER A 68  ? 0.2726 0.2174 0.2419 -0.0017 0.0080  -0.0044 48  SER A N   
390  C CA  . SER A 68  ? 0.2665 0.2084 0.2310 -0.0021 0.0038  -0.0039 48  SER A CA  
391  C C   . SER A 68  ? 0.2636 0.2104 0.2334 -0.0033 0.0014  -0.0031 48  SER A C   
392  O O   . SER A 68  ? 0.2636 0.2128 0.2353 -0.0040 0.0014  -0.0025 48  SER A O   
393  C CB  . SER A 68  ? 0.2943 0.2298 0.2511 -0.0023 0.0026  -0.0035 48  SER A CB  
394  O OG  . SER A 68  ? 0.3112 0.2445 0.2670 -0.0030 -0.0027 -0.0034 48  SER A OG  
395  N N   . HIS A 69  ? 0.2566 0.2032 0.2271 -0.0030 0.0001  -0.0031 49  HIS A N   
396  C CA  . HIS A 69  ? 0.2447 0.1924 0.2169 -0.0037 -0.0004 -0.0022 49  HIS A CA  
397  C C   . HIS A 69  ? 0.2532 0.2007 0.2275 -0.0054 -0.0008 -0.0010 49  HIS A C   
398  O O   . HIS A 69  ? 0.2650 0.2114 0.2397 -0.0062 -0.0029 -0.0013 49  HIS A O   
399  C CB  . HIS A 69  ? 0.2463 0.1909 0.2162 -0.0024 -0.0013 -0.0024 49  HIS A CB  
400  C CG  . HIS A 69  ? 0.2547 0.1950 0.2218 -0.0030 -0.0020 -0.0022 49  HIS A CG  
401  N ND1 . HIS A 69  ? 0.2654 0.2038 0.2335 -0.0052 -0.0016 -0.0010 49  HIS A ND1 
402  C CD2 . HIS A 69  ? 0.2640 0.2008 0.2279 -0.0016 -0.0027 -0.0032 49  HIS A CD2 
403  C CE1 . HIS A 69  ? 0.2805 0.2141 0.2458 -0.0057 -0.0030 -0.0013 49  HIS A CE1 
404  N NE2 . HIS A 69  ? 0.2698 0.2016 0.2312 -0.0032 -0.0038 -0.0027 49  HIS A NE2 
405  N N   . GLY A 70  ? 0.2677 0.2154 0.2436 -0.0059 0.0012  0.0001  50  GLY A N   
406  C CA  . GLY A 70  ? 0.2774 0.2266 0.2598 -0.0074 0.0024  0.0012  50  GLY A CA  
407  C C   . GLY A 70  ? 0.2758 0.2220 0.2605 -0.0092 0.0036  0.0020  50  GLY A C   
408  O O   . GLY A 70  ? 0.2749 0.2166 0.2538 -0.0090 0.0029  0.0017  50  GLY A O   
409  N N   . ALA A 71  ? 0.2746 0.2233 0.2693 -0.0110 0.0057  0.0031  51  ALA A N   
410  C CA  . ALA A 71  ? 0.2817 0.2280 0.2823 -0.0136 0.0077  0.0040  51  ALA A CA  
411  C C   . ALA A 71  ? 0.2956 0.2340 0.2869 -0.0132 0.0136  0.0053  51  ALA A C   
412  O O   . ALA A 71  ? 0.3044 0.2397 0.2887 -0.0111 0.0175  0.0060  51  ALA A O   
413  C CB  . ALA A 71  ? 0.2817 0.2338 0.2993 -0.0156 0.0097  0.0048  51  ALA A CB  
414  N N   . GLY A 72  ? 0.2900 0.2228 0.2782 -0.0147 0.0132  0.0054  52  GLY A N   
415  C CA  . GLY A 72  ? 0.3071 0.2291 0.2839 -0.0141 0.0182  0.0068  52  GLY A CA  
416  C C   . GLY A 72  ? 0.3191 0.2351 0.2803 -0.0101 0.0152  0.0059  52  GLY A C   
417  O O   . GLY A 72  ? 0.3545 0.2594 0.3041 -0.0090 0.0168  0.0065  52  GLY A O   
418  N N   . GLU A 73  ? 0.2962 0.2185 0.2576 -0.0079 0.0107  0.0043  53  GLU A N   
419  C CA  . GLU A 73  ? 0.2948 0.2129 0.2458 -0.0043 0.0071  0.0031  53  GLU A CA  
420  C C   . GLU A 73  ? 0.2908 0.2118 0.2432 -0.0033 0.0021  0.0013  53  GLU A C   
421  O O   . GLU A 73  ? 0.2983 0.2183 0.2526 -0.0050 0.0018  0.0013  53  GLU A O   
422  C CB  . GLU A 73  ? 0.3006 0.2209 0.2502 -0.0025 0.0066  0.0026  53  GLU A CB  
423  C CG  . GLU A 73  ? 0.3019 0.2332 0.2618 -0.0037 0.0053  0.0018  53  GLU A CG  
424  C CD  . GLU A 73  ? 0.3541 0.2880 0.3134 -0.0020 0.0028  0.0006  53  GLU A CD  
425  O OE1 . GLU A 73  ? 0.3746 0.3023 0.3264 0.0001  0.0007  0.0001  53  GLU A OE1 
426  O OE2 . GLU A 73  ? 0.3213 0.2622 0.2871 -0.0029 0.0025  0.0002  53  GLU A OE2 
427  N N   . HIS A 74  ? 0.2918 0.2149 0.2432 -0.0004 -0.0015 -0.0003 54  HIS A N   
428  C CA  . HIS A 74  ? 0.2935 0.2185 0.2468 0.0014  -0.0043 -0.0019 54  HIS A CA  
429  C C   . HIS A 74  ? 0.2897 0.2209 0.2487 0.0035  -0.0064 -0.0035 54  HIS A C   
430  O O   . HIS A 74  ? 0.2865 0.2190 0.2461 0.0036  -0.0072 -0.0035 54  HIS A O   
431  C CB  . HIS A 74  ? 0.2924 0.2077 0.2373 0.0036  -0.0060 -0.0019 54  HIS A CB  
432  C CG  . HIS A 74  ? 0.2998 0.2083 0.2373 0.0067  -0.0089 -0.0021 54  HIS A CG  
433  N ND1 . HIS A 74  ? 0.3215 0.2316 0.2619 0.0107  -0.0142 -0.0042 54  HIS A ND1 
434  C CD2 . HIS A 74  ? 0.3137 0.2126 0.2409 0.0067  -0.0074 -0.0007 54  HIS A CD2 
435  C CE1 . HIS A 74  ? 0.3325 0.2332 0.2633 0.0130  -0.0178 -0.0041 54  HIS A CE1 
436  N NE2 . HIS A 74  ? 0.3315 0.2238 0.2520 0.0109  -0.0133 -0.0020 54  HIS A NE2 
437  N N   . SER A 75  ? 0.2805 0.2149 0.2441 0.0052  -0.0068 -0.0049 55  SER A N   
438  C CA  . SER A 75  ? 0.2731 0.2145 0.2462 0.0066  -0.0071 -0.0064 55  SER A CA  
439  C C   . SER A 75  ? 0.2826 0.2241 0.2594 0.0092  -0.0121 -0.0077 55  SER A C   
440  O O   . SER A 75  ? 0.2885 0.2363 0.2752 0.0091  -0.0129 -0.0088 55  SER A O   
441  C CB  . SER A 75  ? 0.2867 0.2296 0.2635 0.0082  -0.0042 -0.0074 55  SER A CB  
442  O OG  . SER A 75  ? 0.2970 0.2353 0.2713 0.0114  -0.0062 -0.0081 55  SER A OG  
443  N N   . GLY A 76  ? 0.2858 0.2189 0.2542 0.0116  -0.0161 -0.0077 56  GLY A N   
444  C CA  . GLY A 76  ? 0.3023 0.2323 0.2717 0.0149  -0.0233 -0.0092 56  GLY A CA  
445  C C   . GLY A 76  ? 0.3179 0.2462 0.2846 0.0136  -0.0259 -0.0092 56  GLY A C   
446  O O   . GLY A 76  ? 0.3361 0.2643 0.3080 0.0157  -0.0329 -0.0111 56  GLY A O   
447  N N   . ARG A 77  ? 0.3015 0.2291 0.2622 0.0103  -0.0206 -0.0072 57  ARG A N   
448  C CA  . ARG A 77  ? 0.3123 0.2366 0.2684 0.0094  -0.0218 -0.0070 57  ARG A CA  
449  C C   . ARG A 77  ? 0.3108 0.2455 0.2805 0.0075  -0.0221 -0.0083 57  ARG A C   
450  O O   . ARG A 77  ? 0.3171 0.2490 0.2837 0.0068  -0.0239 -0.0085 57  ARG A O   
451  C CB  . ARG A 77  ? 0.3351 0.2547 0.2815 0.0071  -0.0152 -0.0045 57  ARG A CB  
452  C CG  . ARG A 77  ? 0.3717 0.2763 0.3018 0.0092  -0.0152 -0.0033 57  ARG A CG  
453  C CD  . ARG A 77  ? 0.3840 0.2841 0.3080 0.0068  -0.0070 -0.0007 57  ARG A CD  
454  N NE  . ARG A 77  ? 0.3607 0.2617 0.2843 0.0056  -0.0034 0.0001  57  ARG A NE  
455  C CZ  . ARG A 77  ? 0.3793 0.2677 0.2890 0.0077  -0.0038 0.0003  57  ARG A CZ  
456  N NH1 . ARG A 77  ? 0.3736 0.2625 0.2830 0.0069  0.0004  0.0011  57  ARG A NH1 
457  N NH2 . ARG A 77  ? 0.3845 0.2578 0.2788 0.0112  -0.0088 -0.0003 57  ARG A NH2 
458  N N   . TYR A 78  ? 0.2950 0.2398 0.2784 0.0069  -0.0198 -0.0091 58  TYR A N   
459  C CA  . TYR A 78  ? 0.2923 0.2457 0.2888 0.0048  -0.0181 -0.0100 58  TYR A CA  
460  C C   . TYR A 78  ? 0.2861 0.2449 0.2986 0.0064  -0.0230 -0.0125 58  TYR A C   
461  O O   . TYR A 78  ? 0.2796 0.2462 0.3062 0.0044  -0.0199 -0.0133 58  TYR A O   
462  C CB  . TYR A 78  ? 0.2844 0.2428 0.2833 0.0029  -0.0100 -0.0089 58  TYR A CB  
463  C CG  . TYR A 78  ? 0.2880 0.2425 0.2756 0.0011  -0.0072 -0.0069 58  TYR A CG  
464  C CD1 . TYR A 78  ? 0.2931 0.2424 0.2718 0.0016  -0.0069 -0.0056 58  TYR A CD1 
465  C CD2 . TYR A 78  ? 0.2889 0.2444 0.2761 -0.0010 -0.0055 -0.0063 58  TYR A CD2 
466  C CE1 . TYR A 78  ? 0.2974 0.2445 0.2702 0.0000  -0.0045 -0.0040 58  TYR A CE1 
467  C CE2 . TYR A 78  ? 0.3052 0.2580 0.2850 -0.0020 -0.0035 -0.0046 58  TYR A CE2 
468  C CZ  . TYR A 78  ? 0.3063 0.2557 0.2805 -0.0015 -0.0028 -0.0035 58  TYR A CZ  
469  O OH  . TYR A 78  ? 0.3081 0.2560 0.2791 -0.0025 -0.0005 -0.0020 58  TYR A OH  
470  N N   . GLU A 79  ? 0.2941 0.2479 0.3051 0.0100  -0.0310 -0.0139 59  GLU A N   
471  C CA  . GLU A 79  ? 0.2927 0.2520 0.3218 0.0123  -0.0375 -0.0167 59  GLU A CA  
472  C C   . GLU A 79  ? 0.2947 0.2594 0.3381 0.0096  -0.0409 -0.0183 59  GLU A C   
473  O O   . GLU A 79  ? 0.2899 0.2658 0.3557 0.0084  -0.0379 -0.0196 59  GLU A O   
474  C CB  . GLU A 79  ? 0.3366 0.2857 0.3571 0.0171  -0.0480 -0.0179 59  GLU A CB  
475  C CG  . GLU A 79  ? 0.4085 0.3645 0.4506 0.0205  -0.0555 -0.0210 59  GLU A CG  
476  C CD  . GLU A 79  ? 0.4556 0.4204 0.5105 0.0222  -0.0481 -0.0210 59  GLU A CD  
477  O OE1 . GLU A 79  ? 0.4704 0.4303 0.5105 0.0226  -0.0416 -0.0189 59  GLU A OE1 
478  O OE2 . GLU A 79  ? 0.5116 0.4875 0.5918 0.0233  -0.0487 -0.0231 59  GLU A OE2 
479  N N   . GLU A 80  ? 0.2964 0.2522 0.3270 0.0085  -0.0463 -0.0183 60  GLU A N   
480  C CA  . GLU A 80  ? 0.3068 0.2655 0.3495 0.0058  -0.0511 -0.0201 60  GLU A CA  
481  C C   . GLU A 80  ? 0.2993 0.2672 0.3518 0.0010  -0.0404 -0.0189 60  GLU A C   
482  O O   . GLU A 80  ? 0.3017 0.2780 0.3757 -0.0013 -0.0404 -0.0205 60  GLU A O   
483  C CB  . GLU A 80  ? 0.3733 0.3172 0.3971 0.0065  -0.0598 -0.0206 60  GLU A CB  
484  C CG  . GLU A 80  ? 0.4933 0.4254 0.5082 0.0116  -0.0727 -0.0225 60  GLU A CG  
485  C CD  . GLU A 80  ? 0.6549 0.5949 0.6943 0.0139  -0.0825 -0.0259 60  GLU A CD  
486  O OE1 . GLU A 80  ? 0.6942 0.6423 0.7554 0.0112  -0.0871 -0.0282 60  GLU A OE1 
487  O OE2 . GLU A 80  ? 0.7065 0.6447 0.7447 0.0183  -0.0855 -0.0263 60  GLU A OE2 
488  N N   . LEU A 81  ? 0.2908 0.2564 0.3287 -0.0003 -0.0313 -0.0161 61  LEU A N   
489  C CA  . LEU A 81  ? 0.3020 0.2731 0.3452 -0.0041 -0.0216 -0.0148 61  LEU A CA  
490  C C   . LEU A 81  ? 0.2811 0.2616 0.3424 -0.0043 -0.0148 -0.0153 61  LEU A C   
491  O O   . LEU A 81  ? 0.2778 0.2633 0.3530 -0.0073 -0.0099 -0.0156 61  LEU A O   
492  C CB  . LEU A 81  ? 0.3288 0.2956 0.3544 -0.0044 -0.0148 -0.0121 61  LEU A CB  
493  C CG  . LEU A 81  ? 0.3544 0.3145 0.3667 -0.0056 -0.0155 -0.0110 61  LEU A CG  
494  C CD1 . LEU A 81  ? 0.3590 0.3163 0.3582 -0.0050 -0.0101 -0.0087 61  LEU A CD1 
495  C CD2 . LEU A 81  ? 0.3512 0.3130 0.3707 -0.0092 -0.0132 -0.0114 61  LEU A CD2 
496  N N   . ALA A 82  ? 0.2686 0.2500 0.3293 -0.0009 -0.0137 -0.0152 62  ALA A N   
497  C CA  . ALA A 82  ? 0.2763 0.2644 0.3514 -0.0001 -0.0059 -0.0155 62  ALA A CA  
498  C C   . ALA A 82  ? 0.2781 0.2750 0.3802 -0.0002 -0.0089 -0.0181 62  ALA A C   
499  O O   . ALA A 82  ? 0.2826 0.2856 0.4007 -0.0020 0.0004  -0.0181 62  ALA A O   
500  C CB  . ALA A 82  ? 0.2872 0.2724 0.3539 0.0041  -0.0057 -0.0151 62  ALA A CB  
501  N N   . ARG A 83  ? 0.2835 0.2801 0.3913 0.0017  -0.0220 -0.0203 63  ARG A N   
502  C CA  . ARG A 83  ? 0.2897 0.2956 0.4272 0.0015  -0.0275 -0.0233 63  ARG A CA  
503  C C   . ARG A 83  ? 0.2960 0.3057 0.4466 -0.0043 -0.0245 -0.0236 63  ARG A C   
504  O O   . ARG A 83  ? 0.2910 0.3109 0.4702 -0.0063 -0.0201 -0.0250 63  ARG A O   
505  C CB  . ARG A 83  ? 0.3204 0.3221 0.4583 0.0054  -0.0443 -0.0259 63  ARG A CB  
506  C CG  . ARG A 83  ? 0.3910 0.3916 0.5255 0.0113  -0.0454 -0.0260 63  ARG A CG  
507  C CD  . ARG A 83  ? 0.4565 0.4509 0.5904 0.0162  -0.0623 -0.0286 63  ARG A CD  
508  N NE  . ARG A 83  ? 0.5195 0.5127 0.6511 0.0220  -0.0623 -0.0287 63  ARG A NE  
509  C CZ  . ARG A 83  ? 0.5435 0.5473 0.7018 0.0253  -0.0621 -0.0307 63  ARG A CZ  
510  N NH1 . ARG A 83  ? 0.5224 0.5399 0.7142 0.0231  -0.0611 -0.0328 63  ARG A NH1 
511  N NH2 . ARG A 83  ? 0.5553 0.5557 0.7080 0.0310  -0.0623 -0.0307 63  ARG A NH2 
512  N N   . MET A 84  ? 0.2964 0.2978 0.4272 -0.0071 -0.0257 -0.0223 64  MET A N   
513  C CA  . MET A 84  ? 0.2925 0.2949 0.4315 -0.0128 -0.0223 -0.0222 64  MET A CA  
514  C C   . MET A 84  ? 0.2951 0.3019 0.4407 -0.0152 -0.0052 -0.0202 64  MET A C   
515  O O   . MET A 84  ? 0.3033 0.3164 0.4716 -0.0190 0.0003  -0.0210 64  MET A O   
516  C CB  . MET A 84  ? 0.3088 0.2996 0.4212 -0.0141 -0.0254 -0.0208 64  MET A CB  
517  C CG  . MET A 84  ? 0.3317 0.3215 0.4492 -0.0197 -0.0217 -0.0206 64  MET A CG  
518  S SD  . MET A 84  ? 0.3912 0.3791 0.4973 -0.0220 -0.0039 -0.0170 64  MET A SD  
519  C CE  . MET A 84  ? 0.3695 0.3468 0.4423 -0.0189 -0.0061 -0.0148 64  MET A CE  
520  N N   . LEU A 85  ? 0.2860 0.2879 0.4116 -0.0130 0.0031  -0.0177 65  LEU A N   
521  C CA  . LEU A 85  ? 0.2869 0.2878 0.4117 -0.0144 0.0187  -0.0157 65  LEU A CA  
522  C C   . LEU A 85  ? 0.2972 0.3069 0.4474 -0.0133 0.0264  -0.0168 65  LEU A C   
523  O O   . LEU A 85  ? 0.3017 0.3125 0.4639 -0.0163 0.0385  -0.0161 65  LEU A O   
524  C CB  . LEU A 85  ? 0.2877 0.2796 0.3846 -0.0119 0.0229  -0.0133 65  LEU A CB  
525  C CG  . LEU A 85  ? 0.2894 0.2733 0.3646 -0.0134 0.0191  -0.0118 65  LEU A CG  
526  C CD1 . LEU A 85  ? 0.2915 0.2692 0.3449 -0.0103 0.0185  -0.0103 65  LEU A CD1 
527  C CD2 . LEU A 85  ? 0.3010 0.2800 0.3732 -0.0173 0.0277  -0.0105 65  LEU A CD2 
528  N N   . MET A 86  ? 0.3021 0.3170 0.4611 -0.0088 0.0200  -0.0185 66  MET A N   
529  C CA  A MET A 86  ? 0.3068 0.3310 0.4930 -0.0066 0.0265  -0.0198 66  MET A CA  
530  C CA  B MET A 86  ? 0.3035 0.3277 0.4897 -0.0066 0.0263  -0.0199 66  MET A CA  
531  C C   . MET A 86  ? 0.3026 0.3376 0.5237 -0.0107 0.0248  -0.0221 66  MET A C   
532  O O   . MET A 86  ? 0.3002 0.3420 0.5455 -0.0117 0.0371  -0.0222 66  MET A O   
533  C CB  A MET A 86  ? 0.3173 0.3437 0.5042 -0.0004 0.0174  -0.0214 66  MET A CB  
534  C CB  B MET A 86  ? 0.3059 0.3324 0.4931 -0.0005 0.0163  -0.0215 66  MET A CB  
535  C CG  A MET A 86  ? 0.3421 0.3776 0.5560 0.0030  0.0244  -0.0228 66  MET A CG  
536  C CG  B MET A 86  ? 0.3130 0.3501 0.5308 0.0028  0.0208  -0.0234 66  MET A CG  
537  S SD  A MET A 86  ? 0.4099 0.4606 0.6670 0.0029  0.0116  -0.0269 66  MET A SD  
538  S SD  B MET A 86  ? 0.3340 0.3715 0.5507 0.0106  0.0075  -0.0254 66  MET A SD  
539  C CE  A MET A 86  ? 0.3995 0.4446 0.6404 0.0090  -0.0093 -0.0287 66  MET A CE  
540  C CE  B MET A 86  ? 0.3010 0.3372 0.5171 0.0095  -0.0144 -0.0277 66  MET A CE  
541  N N   . GLY A 87  ? 0.3175 0.3526 0.5404 -0.0133 0.0103  -0.0237 67  GLY A N   
542  C CA  . GLY A 87  ? 0.3228 0.3664 0.5776 -0.0179 0.0060  -0.0262 67  GLY A CA  
543  C C   . GLY A 87  ? 0.3304 0.3728 0.5906 -0.0242 0.0213  -0.0243 67  GLY A C   
544  O O   . GLY A 87  ? 0.3326 0.3835 0.6250 -0.0287 0.0232  -0.0259 67  GLY A O   
545  N N   . LEU A 88  ? 0.3383 0.3690 0.5674 -0.0248 0.0320  -0.0209 68  LEU A N   
546  C CA  . LEU A 88  ? 0.3464 0.3715 0.5734 -0.0298 0.0479  -0.0186 68  LEU A CA  
547  C C   . LEU A 88  ? 0.3486 0.3731 0.5809 -0.0280 0.0675  -0.0168 68  LEU A C   
548  O O   . LEU A 88  ? 0.3646 0.3796 0.5865 -0.0309 0.0824  -0.0143 68  LEU A O   
549  C CB  . LEU A 88  ? 0.3655 0.3758 0.5542 -0.0305 0.0479  -0.0159 68  LEU A CB  
550  C CG  . LEU A 88  ? 0.3909 0.3982 0.5691 -0.0320 0.0317  -0.0171 68  LEU A CG  
551  C CD1 . LEU A 88  ? 0.4143 0.4081 0.5577 -0.0319 0.0339  -0.0144 68  LEU A CD1 
552  C CD2 . LEU A 88  ? 0.3944 0.4066 0.5983 -0.0379 0.0270  -0.0192 68  LEU A CD2 
553  N N   . ASP A 89  ? 0.3332 0.3651 0.5777 -0.0227 0.0678  -0.0180 69  ASP A N   
554  C CA  . ASP A 89  ? 0.3348 0.3649 0.5831 -0.0196 0.0859  -0.0167 69  ASP A CA  
555  C C   . ASP A 89  ? 0.3399 0.3530 0.5471 -0.0161 0.0935  -0.0138 69  ASP A C   
556  O O   . ASP A 89  ? 0.3488 0.3535 0.5501 -0.0147 0.1111  -0.0120 69  ASP A O   
557  C CB  . ASP A 89  ? 0.3683 0.4016 0.6441 -0.0243 0.1036  -0.0161 69  ASP A CB  
558  C CG  . ASP A 89  ? 0.4462 0.4986 0.7699 -0.0271 0.0960  -0.0196 69  ASP A CG  
559  O OD1 . ASP A 89  ? 0.4628 0.5186 0.8096 -0.0337 0.1037  -0.0196 69  ASP A OD1 
560  O OD2 . ASP A 89  ? 0.4676 0.5307 0.8061 -0.0227 0.0814  -0.0224 69  ASP A OD2 
561  N N   . LEU A 90  ? 0.3310 0.3382 0.5104 -0.0145 0.0802  -0.0134 70  LEU A N   
562  C CA  . LEU A 90  ? 0.3355 0.3278 0.4791 -0.0109 0.0841  -0.0113 70  LEU A CA  
563  C C   . LEU A 90  ? 0.3211 0.3170 0.4638 -0.0050 0.0778  -0.0125 70  LEU A C   
564  O O   . LEU A 90  ? 0.3090 0.3159 0.4675 -0.0038 0.0648  -0.0147 70  LEU A O   
565  C CB  . LEU A 90  ? 0.3526 0.3363 0.4680 -0.0126 0.0744  -0.0100 70  LEU A CB  
566  C CG  . LEU A 90  ? 0.3882 0.3596 0.4880 -0.0164 0.0832  -0.0078 70  LEU A CG  
567  C CD1 . LEU A 90  ? 0.3955 0.3741 0.5162 -0.0221 0.0815  -0.0087 70  LEU A CD1 
568  C CD2 . LEU A 90  ? 0.4076 0.3676 0.4748 -0.0154 0.0759  -0.0064 70  LEU A CD2 
569  N N   . LEU A 91  ? 0.3127 0.2968 0.4346 -0.0011 0.0865  -0.0111 71  LEU A N   
570  C CA  . LEU A 91  ? 0.3081 0.2924 0.4240 0.0044  0.0808  -0.0120 71  LEU A CA  
571  C C   . LEU A 91  ? 0.3072 0.2832 0.3936 0.0043  0.0694  -0.0111 71  LEU A C   
572  O O   . LEU A 91  ? 0.3316 0.2938 0.3926 0.0038  0.0738  -0.0093 71  LEU A O   
573  C CB  . LEU A 91  ? 0.3198 0.2941 0.4283 0.0088  0.0961  -0.0113 71  LEU A CB  
574  C CG  . LEU A 91  ? 0.3503 0.3276 0.4623 0.0148  0.0918  -0.0128 71  LEU A CG  
575  C CD1 . LEU A 91  ? 0.3642 0.3340 0.4774 0.0193  0.1090  -0.0124 71  LEU A CD1 
576  C CD2 . LEU A 91  ? 0.3757 0.3443 0.4591 0.0163  0.0799  -0.0124 71  LEU A CD2 
577  N N   . VAL A 92  ? 0.2737 0.2570 0.3639 0.0049  0.0548  -0.0124 72  VAL A N   
578  C CA  . VAL A 92  ? 0.2645 0.2416 0.3316 0.0044  0.0449  -0.0115 72  VAL A CA  
579  C C   . VAL A 92  ? 0.2644 0.2359 0.3187 0.0088  0.0427  -0.0116 72  VAL A C   
580  O O   . VAL A 92  ? 0.2670 0.2434 0.3342 0.0124  0.0419  -0.0130 72  VAL A O   
581  C CB  . VAL A 92  ? 0.2669 0.2515 0.3417 0.0026  0.0316  -0.0126 72  VAL A CB  
582  C CG1 . VAL A 92  ? 0.2811 0.2587 0.3332 0.0017  0.0249  -0.0112 72  VAL A CG1 
583  C CG2 . VAL A 92  ? 0.2681 0.2593 0.3606 -0.0015 0.0325  -0.0132 72  VAL A CG2 
584  N N   . PHE A 93  ? 0.2573 0.2180 0.2875 0.0086  0.0415  -0.0102 73  PHE A N   
585  C CA  . PHE A 93  ? 0.2677 0.2213 0.2844 0.0119  0.0388  -0.0103 73  PHE A CA  
586  C C   . PHE A 93  ? 0.2761 0.2246 0.2758 0.0099  0.0306  -0.0093 73  PHE A C   
587  O O   . PHE A 93  ? 0.2837 0.2311 0.2779 0.0068  0.0295  -0.0083 73  PHE A O   
588  C CB  . PHE A 93  ? 0.2820 0.2243 0.2885 0.0150  0.0496  -0.0101 73  PHE A CB  
589  C CG  . PHE A 93  ? 0.3034 0.2319 0.2896 0.0136  0.0555  -0.0086 73  PHE A CG  
590  C CD1 . PHE A 93  ? 0.3205 0.2491 0.3110 0.0111  0.0629  -0.0078 73  PHE A CD1 
591  C CD2 . PHE A 93  ? 0.3304 0.2439 0.2923 0.0150  0.0532  -0.0082 73  PHE A CD2 
592  C CE1 . PHE A 93  ? 0.3459 0.2589 0.3146 0.0105  0.0677  -0.0065 73  PHE A CE1 
593  C CE2 . PHE A 93  ? 0.3544 0.2527 0.2958 0.0145  0.0567  -0.0072 73  PHE A CE2 
594  C CZ  . PHE A 93  ? 0.3546 0.2521 0.2983 0.0125  0.0640  -0.0062 73  PHE A CZ  
595  N N   . ALA A 94  ? 0.2627 0.2084 0.2559 0.0116  0.0247  -0.0095 74  ALA A N   
596  C CA  . ALA A 94  ? 0.2600 0.2022 0.2414 0.0095  0.0177  -0.0086 74  ALA A CA  
597  C C   . ALA A 94  ? 0.2670 0.2016 0.2386 0.0116  0.0151  -0.0088 74  ALA A C   
598  O O   . ALA A 94  ? 0.2728 0.2061 0.2474 0.0152  0.0175  -0.0098 74  ALA A O   
599  C CB  . ALA A 94  ? 0.2582 0.2083 0.2480 0.0079  0.0111  -0.0086 74  ALA A CB  
600  N N   . HIS A 95  ? 0.2683 0.1980 0.2299 0.0093  0.0103  -0.0080 75  HIS A N   
601  C CA  . HIS A 95  ? 0.2809 0.2042 0.2352 0.0101  0.0066  -0.0081 75  HIS A CA  
602  C C   . HIS A 95  ? 0.2781 0.2028 0.2317 0.0065  0.0014  -0.0070 75  HIS A C   
603  O O   . HIS A 95  ? 0.2900 0.2190 0.2464 0.0040  0.0009  -0.0062 75  HIS A O   
604  C CB  . HIS A 95  ? 0.2904 0.2011 0.2309 0.0114  0.0081  -0.0086 75  HIS A CB  
605  C CG  . HIS A 95  ? 0.3106 0.2148 0.2415 0.0089  0.0065  -0.0081 75  HIS A CG  
606  N ND1 . HIS A 95  ? 0.3323 0.2280 0.2538 0.0107  0.0113  -0.0085 75  HIS A ND1 
607  C CD2 . HIS A 95  ? 0.3237 0.2273 0.2531 0.0054  0.0003  -0.0075 75  HIS A CD2 
608  C CE1 . HIS A 95  ? 0.3461 0.2352 0.2586 0.0085  0.0063  -0.0082 75  HIS A CE1 
609  N NE2 . HIS A 95  ? 0.3332 0.2284 0.2527 0.0053  -0.0006 -0.0077 75  HIS A NE2 
610  N N   . ASP A 96  ? 0.2728 0.1934 0.2232 0.0066  -0.0016 -0.0068 76  ASP A N   
611  C CA  . ASP A 96  ? 0.2794 0.1994 0.2292 0.0031  -0.0043 -0.0054 76  ASP A CA  
612  C C   . ASP A 96  ? 0.2882 0.2026 0.2331 0.0005  -0.0063 -0.0054 76  ASP A C   
613  O O   . ASP A 96  ? 0.3040 0.2097 0.2410 0.0018  -0.0072 -0.0063 76  ASP A O   
614  C CB  . ASP A 96  ? 0.2908 0.2056 0.2371 0.0039  -0.0058 -0.0051 76  ASP A CB  
615  C CG  . ASP A 96  ? 0.3099 0.2281 0.2595 0.0067  -0.0065 -0.0053 76  ASP A CG  
616  O OD1 . ASP A 96  ? 0.2909 0.2166 0.2474 0.0069  -0.0059 -0.0056 76  ASP A OD1 
617  O OD2 . ASP A 96  ? 0.3253 0.2372 0.2698 0.0087  -0.0083 -0.0052 76  ASP A OD2 
618  N N   . HIS A 97  ? 0.2817 0.1999 0.2313 -0.0026 -0.0076 -0.0046 77  HIS A N   
619  C CA  . HIS A 97  ? 0.2893 0.2024 0.2368 -0.0049 -0.0118 -0.0049 77  HIS A CA  
620  C C   . HIS A 97  ? 0.2996 0.2062 0.2458 -0.0071 -0.0145 -0.0049 77  HIS A C   
621  O O   . HIS A 97  ? 0.2983 0.2056 0.2466 -0.0077 -0.0123 -0.0039 77  HIS A O   
622  C CB  . HIS A 97  ? 0.2877 0.2076 0.2444 -0.0075 -0.0132 -0.0041 77  HIS A CB  
623  C CG  . HIS A 97  ? 0.2982 0.2231 0.2554 -0.0059 -0.0108 -0.0040 77  HIS A CG  
624  N ND1 . HIS A 97  ? 0.3235 0.2428 0.2719 -0.0037 -0.0105 -0.0050 77  HIS A ND1 
625  C CD2 . HIS A 97  ? 0.3040 0.2369 0.2681 -0.0062 -0.0082 -0.0031 77  HIS A CD2 
626  C CE1 . HIS A 97  ? 0.3151 0.2400 0.2666 -0.0033 -0.0077 -0.0045 77  HIS A CE1 
627  N NE2 . HIS A 97  ? 0.3143 0.2475 0.2752 -0.0047 -0.0069 -0.0035 77  HIS A NE2 
628  N N   . VAL A 98  ? 0.3071 0.2052 0.2483 -0.0083 -0.0198 -0.0060 78  VAL A N   
629  C CA  A VAL A 98  ? 0.3219 0.2129 0.2629 -0.0112 -0.0231 -0.0061 78  VAL A CA  
630  C CA  B VAL A 98  ? 0.3148 0.2057 0.2559 -0.0113 -0.0233 -0.0061 78  VAL A CA  
631  C C   . VAL A 98  ? 0.3109 0.2091 0.2661 -0.0155 -0.0209 -0.0043 78  VAL A C   
632  O O   . VAL A 98  ? 0.2939 0.2013 0.2599 -0.0168 -0.0198 -0.0034 78  VAL A O   
633  C CB  A VAL A 98  ? 0.3536 0.2339 0.2886 -0.0125 -0.0312 -0.0078 78  VAL A CB  
634  C CB  B VAL A 98  ? 0.3291 0.2112 0.2661 -0.0128 -0.0317 -0.0078 78  VAL A CB  
635  C CG1 A VAL A 98  ? 0.3579 0.2439 0.3040 -0.0151 -0.0364 -0.0079 78  VAL A CG1 
636  C CG1 B VAL A 98  ? 0.3377 0.2174 0.2845 -0.0181 -0.0371 -0.0079 78  VAL A CG1 
637  C CG2 A VAL A 98  ? 0.3703 0.2418 0.3044 -0.0156 -0.0348 -0.0082 78  VAL A CG2 
638  C CG2 B VAL A 98  ? 0.3422 0.2101 0.2598 -0.0086 -0.0327 -0.0095 78  VAL A CG2 
639  N N   . GLY A 99  ? 0.3098 0.2026 0.2633 -0.0170 -0.0190 -0.0035 79  GLY A N   
640  C CA  . GLY A 99  ? 0.3140 0.2104 0.2784 -0.0208 -0.0146 -0.0015 79  GLY A CA  
641  C C   . GLY A 99  ? 0.3210 0.2224 0.2843 -0.0184 -0.0079 0.0001  79  GLY A C   
642  O O   . GLY A 99  ? 0.3369 0.2395 0.3065 -0.0208 -0.0026 0.0020  79  GLY A O   
643  N N   . HIS A 100 ? 0.3101 0.2133 0.2654 -0.0136 -0.0078 -0.0007 80  HIS A N   
644  C CA  . HIS A 100 ? 0.3064 0.2131 0.2600 -0.0109 -0.0039 0.0002  80  HIS A CA  
645  C C   . HIS A 100 ? 0.3136 0.2150 0.2568 -0.0063 -0.0044 -0.0005 80  HIS A C   
646  O O   . HIS A 100 ? 0.3179 0.2163 0.2567 -0.0040 -0.0069 -0.0020 80  HIS A O   
647  C CB  . HIS A 100 ? 0.2968 0.2133 0.2560 -0.0097 -0.0043 -0.0003 80  HIS A CB  
648  C CG  . HIS A 100 ? 0.2968 0.2192 0.2671 -0.0131 -0.0035 0.0006  80  HIS A CG  
649  N ND1 . HIS A 100 ? 0.3103 0.2331 0.2874 -0.0158 -0.0077 -0.0001 80  HIS A ND1 
650  C CD2 . HIS A 100 ? 0.3126 0.2397 0.2885 -0.0135 0.0005  0.0019  80  HIS A CD2 
651  C CE1 . HIS A 100 ? 0.3175 0.2470 0.3067 -0.0178 -0.0063 0.0008  80  HIS A CE1 
652  N NE2 . HIS A 100 ? 0.3116 0.2439 0.3002 -0.0164 -0.0004 0.0021  80  HIS A NE2 
653  N N   . GLY A 101 ? 0.3102 0.2094 0.2493 -0.0044 -0.0024 0.0004  81  GLY A N   
654  C CA  . GLY A 101 ? 0.3082 0.2034 0.2399 0.0006  -0.0046 -0.0006 81  GLY A CA  
655  C C   . GLY A 101 ? 0.3208 0.2075 0.2453 0.0027  -0.0067 -0.0014 81  GLY A C   
656  O O   . GLY A 101 ? 0.3315 0.2084 0.2499 0.0005  -0.0055 -0.0003 81  GLY A O   
657  N N   . GLN A 102 ? 0.3091 0.1993 0.2355 0.0069  -0.0091 -0.0034 82  GLN A N   
658  C CA  . GLN A 102 ? 0.3202 0.2024 0.2401 0.0104  -0.0108 -0.0045 82  GLN A CA  
659  C C   . GLN A 102 ? 0.3173 0.1978 0.2363 0.0090  -0.0103 -0.0053 82  GLN A C   
660  O O   . GLN A 102 ? 0.3198 0.1929 0.2325 0.0124  -0.0111 -0.0064 82  GLN A O   
661  C CB  . GLN A 102 ? 0.3295 0.2153 0.2531 0.0166  -0.0131 -0.0062 82  GLN A CB  
662  C CG  . GLN A 102 ? 0.3445 0.2280 0.2657 0.0187  -0.0163 -0.0058 82  GLN A CG  
663  C CD  . GLN A 102 ? 0.3667 0.2539 0.2948 0.0249  -0.0207 -0.0079 82  GLN A CD  
664  O OE1 . GLN A 102 ? 0.3633 0.2440 0.2879 0.0296  -0.0233 -0.0090 82  GLN A OE1 
665  N NE2 . GLN A 102 ? 0.3528 0.2504 0.2921 0.0252  -0.0221 -0.0088 82  GLN A NE2 
666  N N   . SER A 103 ? 0.3072 0.1926 0.2309 0.0047  -0.0096 -0.0050 83  SER A N   
667  C CA  . SER A 103 ? 0.3182 0.1985 0.2380 0.0033  -0.0109 -0.0059 83  SER A CA  
668  C C   . SER A 103 ? 0.3382 0.2092 0.2541 -0.0011 -0.0132 -0.0052 83  SER A C   
669  O O   . SER A 103 ? 0.3455 0.2161 0.2643 -0.0042 -0.0119 -0.0036 83  SER A O   
670  C CB  . SER A 103 ? 0.3141 0.2017 0.2396 0.0012  -0.0110 -0.0061 83  SER A CB  
671  O OG  . SER A 103 ? 0.3120 0.2058 0.2401 0.0051  -0.0081 -0.0069 83  SER A OG  
672  N N   . GLU A 104 ? 0.3438 0.2056 0.2525 -0.0015 -0.0162 -0.0066 84  GLU A N   
673  C CA  . GLU A 104 ? 0.3590 0.2114 0.2657 -0.0064 -0.0194 -0.0063 84  GLU A CA  
674  C C   . GLU A 104 ? 0.3757 0.2349 0.2951 -0.0125 -0.0219 -0.0057 84  GLU A C   
675  O O   . GLU A 104 ? 0.3722 0.2416 0.2989 -0.0123 -0.0214 -0.0056 84  GLU A O   
676  C CB  . GLU A 104 ? 0.3724 0.2106 0.2656 -0.0044 -0.0231 -0.0083 84  GLU A CB  
677  C CG  . GLU A 104 ? 0.3968 0.2264 0.2790 0.0011  -0.0208 -0.0087 84  GLU A CG  
678  C CD  . GLU A 104 ? 0.4215 0.2345 0.2886 0.0029  -0.0239 -0.0106 84  GLU A CD  
679  O OE1 . GLU A 104 ? 0.4091 0.2177 0.2711 0.0029  -0.0267 -0.0120 84  GLU A OE1 
680  O OE2 . GLU A 104 ? 0.4784 0.2804 0.3365 0.0049  -0.0239 -0.0107 84  GLU A OE2 
681  N N   . GLY A 105 ? 0.3953 0.2482 0.3184 -0.0179 -0.0245 -0.0053 85  GLY A N   
682  C CA  . GLY A 105 ? 0.4045 0.2632 0.3433 -0.0239 -0.0278 -0.0051 85  GLY A CA  
683  C C   . GLY A 105 ? 0.4154 0.2789 0.3672 -0.0285 -0.0218 -0.0026 85  GLY A C   
684  O O   . GLY A 105 ? 0.4146 0.2803 0.3630 -0.0262 -0.0148 -0.0009 85  GLY A O   
685  N N   . GLU A 106 ? 0.4241 0.2889 0.3919 -0.0351 -0.0243 -0.0024 86  GLU A N   
686  C CA  . GLU A 106 ? 0.4335 0.3030 0.4162 -0.0398 -0.0162 0.0002  86  GLU A CA  
687  C C   . GLU A 106 ? 0.4206 0.3028 0.4091 -0.0370 -0.0102 0.0016  86  GLU A C   
688  O O   . GLU A 106 ? 0.4067 0.2971 0.3981 -0.0346 -0.0149 0.0002  86  GLU A O   
689  C CB  . GLU A 106 ? 0.4796 0.3516 0.4845 -0.0473 -0.0204 -0.0002 86  GLU A CB  
690  C CG  . GLU A 106 ? 0.5902 0.4654 0.6121 -0.0526 -0.0098 0.0027  86  GLU A CG  
691  C CD  . GLU A 106 ? 0.7077 0.5864 0.7566 -0.0606 -0.0131 0.0022  86  GLU A CD  
692  O OE1 . GLU A 106 ? 0.7232 0.6000 0.7761 -0.0622 -0.0262 -0.0007 86  GLU A OE1 
693  O OE2 . GLU A 106 ? 0.7408 0.6232 0.8071 -0.0651 -0.0026 0.0047  86  GLU A OE2 
694  N N   . ARG A 107 ? 0.4194 0.3001 0.4050 -0.0365 -0.0003 0.0041  87  ARG A N   
695  C CA  . ARG A 107 ? 0.4192 0.3085 0.4059 -0.0333 0.0049  0.0052  87  ARG A CA  
696  C C   . ARG A 107 ? 0.4138 0.3162 0.4216 -0.0358 0.0047  0.0052  87  ARG A C   
697  O O   . ARG A 107 ? 0.4115 0.3162 0.4374 -0.0410 0.0075  0.0061  87  ARG A O   
698  C CB  . ARG A 107 ? 0.4331 0.3141 0.4104 -0.0325 0.0153  0.0079  87  ARG A CB  
699  C CG  . ARG A 107 ? 0.4654 0.3317 0.4211 -0.0293 0.0148  0.0080  87  ARG A CG  
700  C CD  . ARG A 107 ? 0.4778 0.3458 0.4205 -0.0224 0.0092  0.0061  87  ARG A CD  
701  N NE  . ARG A 107 ? 0.4558 0.3270 0.3994 -0.0215 0.0010  0.0035  87  ARG A NE  
702  C CZ  . ARG A 107 ? 0.4397 0.3132 0.3758 -0.0161 -0.0029 0.0018  87  ARG A CZ  
703  N NH1 . ARG A 107 ? 0.4237 0.2985 0.3536 -0.0115 -0.0013 0.0020  87  ARG A NH1 
704  N NH2 . ARG A 107 ? 0.4255 0.2989 0.3603 -0.0152 -0.0085 -0.0003 87  ARG A NH2 
705  N N   . MET A 108 ? 0.4118 0.3224 0.4186 -0.0320 0.0009  0.0040  88  MET A N   
706  C CA  . MET A 108 ? 0.4155 0.3379 0.4403 -0.0330 0.0003  0.0040  88  MET A CA  
707  C C   . MET A 108 ? 0.4066 0.3325 0.4499 -0.0373 -0.0073 0.0026  88  MET A C   
708  O O   . MET A 108 ? 0.4140 0.3478 0.4795 -0.0405 -0.0048 0.0033  88  MET A O   
709  C CB  . MET A 108 ? 0.4418 0.3668 0.4735 -0.0335 0.0118  0.0066  88  MET A CB  
710  C CG  . MET A 108 ? 0.5178 0.4340 0.5292 -0.0300 0.0179  0.0079  88  MET A CG  
711  S SD  . MET A 108 ? 0.6165 0.5395 0.6202 -0.0246 0.0148  0.0068  88  MET A SD  
712  C CE  . MET A 108 ? 0.3750 0.2986 0.3845 -0.0246 0.0265  0.0094  88  MET A CE  
713  N N   A VAL A 109 ? 0.4036 0.3226 0.4381 -0.0373 -0.0168 0.0004  89  VAL A N   
714  N N   B VAL A 109 ? 0.4012 0.3201 0.4355 -0.0372 -0.0169 0.0004  89  VAL A N   
715  C CA  A VAL A 109 ? 0.4033 0.3226 0.4510 -0.0405 -0.0278 -0.0018 89  VAL A CA  
716  C CA  B VAL A 109 ? 0.4008 0.3188 0.4473 -0.0407 -0.0279 -0.0018 89  VAL A CA  
717  C C   A VAL A 109 ? 0.3986 0.3120 0.4286 -0.0360 -0.0375 -0.0042 89  VAL A C   
718  C C   B VAL A 109 ? 0.3987 0.3114 0.4282 -0.0362 -0.0378 -0.0043 89  VAL A C   
719  O O   A VAL A 109 ? 0.4042 0.3113 0.4131 -0.0319 -0.0350 -0.0043 89  VAL A O   
720  O O   B VAL A 109 ? 0.4064 0.3122 0.4147 -0.0322 -0.0357 -0.0045 89  VAL A O   
721  C CB  A VAL A 109 ? 0.4277 0.3395 0.4834 -0.0465 -0.0307 -0.0021 89  VAL A CB  
722  C CB  B VAL A 109 ? 0.4226 0.3306 0.4699 -0.0456 -0.0295 -0.0020 89  VAL A CB  
723  C CG1 A VAL A 109 ? 0.4379 0.3511 0.5051 -0.0506 -0.0178 0.0008  89  VAL A CG1 
724  C CG1 B VAL A 109 ? 0.4298 0.3336 0.4854 -0.0486 -0.0439 -0.0049 89  VAL A CG1 
725  C CG2 A VAL A 109 ? 0.4492 0.3460 0.4812 -0.0448 -0.0361 -0.0037 89  VAL A CG2 
726  C CG2 B VAL A 109 ? 0.4297 0.3411 0.4943 -0.0507 -0.0183 0.0007  89  VAL A CG2 
727  N N   . VAL A 110 ? 0.3849 0.2995 0.4234 -0.0364 -0.0481 -0.0062 90  VAL A N   
728  C CA  . VAL A 110 ? 0.3854 0.2907 0.4048 -0.0320 -0.0571 -0.0085 90  VAL A CA  
729  C C   . VAL A 110 ? 0.3884 0.2890 0.4179 -0.0344 -0.0719 -0.0110 90  VAL A C   
730  O O   . VAL A 110 ? 0.3870 0.2984 0.4421 -0.0372 -0.0746 -0.0110 90  VAL A O   
731  C CB  . VAL A 110 ? 0.3801 0.2903 0.3902 -0.0268 -0.0528 -0.0078 90  VAL A CB  
732  C CG1 . VAL A 110 ? 0.3647 0.2857 0.3935 -0.0270 -0.0556 -0.0077 90  VAL A CG1 
733  C CG2 . VAL A 110 ? 0.4031 0.2998 0.3875 -0.0222 -0.0572 -0.0095 90  VAL A CG2 
734  N N   . SER A 111 ? 0.3905 0.2740 0.4007 -0.0332 -0.0817 -0.0134 91  SER A N   
735  C CA  . SER A 111 ? 0.4024 0.2778 0.4193 -0.0352 -0.0983 -0.0164 91  SER A CA  
736  C C   . SER A 111 ? 0.4057 0.2848 0.4281 -0.0321 -0.1063 -0.0174 91  SER A C   
737  O O   . SER A 111 ? 0.4085 0.2924 0.4537 -0.0347 -0.1172 -0.0190 91  SER A O   
738  C CB  . SER A 111 ? 0.4329 0.2851 0.4212 -0.0333 -0.1067 -0.0188 91  SER A CB  
739  O OG  . SER A 111 ? 0.4767 0.3187 0.4362 -0.0265 -0.1037 -0.0189 91  SER A OG  
740  N N   . ASP A 112 ? 0.3997 0.2768 0.4026 -0.0264 -0.1007 -0.0166 92  ASP A N   
741  C CA  . ASP A 112 ? 0.3910 0.2708 0.3956 -0.0228 -0.1057 -0.0171 92  ASP A CA  
742  C C   . ASP A 112 ? 0.3724 0.2576 0.3644 -0.0190 -0.0917 -0.0147 92  ASP A C   
743  O O   . ASP A 112 ? 0.3805 0.2583 0.3521 -0.0172 -0.0840 -0.0141 92  ASP A O   
744  C CB  . ASP A 112 ? 0.4253 0.2834 0.4082 -0.0191 -0.1218 -0.0202 92  ASP A CB  
745  C CG  . ASP A 112 ? 0.4800 0.3397 0.4650 -0.0152 -0.1280 -0.0206 92  ASP A CG  
746  O OD1 . ASP A 112 ? 0.4799 0.3466 0.4896 -0.0168 -0.1396 -0.0220 92  ASP A OD1 
747  O OD2 . ASP A 112 ? 0.4844 0.3385 0.4479 -0.0105 -0.1211 -0.0195 92  ASP A OD2 
748  N N   . PHE A 113 ? 0.3500 0.2474 0.3546 -0.0176 -0.0888 -0.0136 93  PHE A N   
749  C CA  . PHE A 113 ? 0.3350 0.2377 0.3297 -0.0145 -0.0762 -0.0115 93  PHE A CA  
750  C C   . PHE A 113 ? 0.3568 0.2426 0.3198 -0.0101 -0.0754 -0.0121 93  PHE A C   
751  O O   . PHE A 113 ? 0.3503 0.2384 0.3039 -0.0086 -0.0639 -0.0107 93  PHE A O   
752  C CB  . PHE A 113 ? 0.3144 0.2288 0.3246 -0.0131 -0.0759 -0.0107 93  PHE A CB  
753  C CG  . PHE A 113 ? 0.3147 0.2376 0.3215 -0.0116 -0.0622 -0.0084 93  PHE A CG  
754  C CD1 . PHE A 113 ? 0.3140 0.2495 0.3349 -0.0142 -0.0516 -0.0064 93  PHE A CD1 
755  C CD2 . PHE A 113 ? 0.3342 0.2504 0.3222 -0.0077 -0.0600 -0.0082 93  PHE A CD2 
756  C CE1 . PHE A 113 ? 0.3122 0.2533 0.3283 -0.0127 -0.0410 -0.0047 93  PHE A CE1 
757  C CE2 . PHE A 113 ? 0.3307 0.2541 0.3167 -0.0069 -0.0486 -0.0064 93  PHE A CE2 
758  C CZ  . PHE A 113 ? 0.3218 0.2577 0.3219 -0.0093 -0.0401 -0.0048 93  PHE A CZ  
759  N N   . HIS A 114 ? 0.3788 0.2460 0.3249 -0.0078 -0.0876 -0.0144 94  HIS A N   
760  C CA  . HIS A 114 ? 0.4011 0.2486 0.3148 -0.0032 -0.0855 -0.0149 94  HIS A CA  
761  C C   . HIS A 114 ? 0.3926 0.2349 0.2932 -0.0032 -0.0762 -0.0145 94  HIS A C   
762  O O   . HIS A 114 ? 0.3931 0.2266 0.2741 0.0003  -0.0678 -0.0139 94  HIS A O   
763  C CB  . HIS A 114 ? 0.4356 0.2597 0.3294 -0.0002 -0.1008 -0.0175 94  HIS A CB  
764  C CG  . HIS A 114 ? 0.5015 0.3037 0.3603 0.0050  -0.0958 -0.0175 94  HIS A CG  
765  N ND1 . HIS A 114 ? 0.5434 0.3253 0.3768 0.0070  -0.0945 -0.0185 94  HIS A ND1 
766  C CD2 . HIS A 114 ? 0.5335 0.3312 0.3798 0.0085  -0.0901 -0.0163 94  HIS A CD2 
767  C CE1 . HIS A 114 ? 0.5641 0.3297 0.3709 0.0116  -0.0872 -0.0178 94  HIS A CE1 
768  N NE2 . HIS A 114 ? 0.5673 0.3413 0.3806 0.0124  -0.0845 -0.0165 94  HIS A NE2 
769  N N   . VAL A 115 ? 0.3706 0.2196 0.2840 -0.0069 -0.0759 -0.0145 95  VAL A N   
770  C CA  . VAL A 115 ? 0.3797 0.2249 0.2824 -0.0063 -0.0668 -0.0140 95  VAL A CA  
771  C C   . VAL A 115 ? 0.3666 0.2228 0.2700 -0.0044 -0.0527 -0.0120 95  VAL A C   
772  O O   . VAL A 115 ? 0.3795 0.2274 0.2669 -0.0011 -0.0454 -0.0119 95  VAL A O   
773  C CB  . VAL A 115 ? 0.4007 0.2535 0.3200 -0.0111 -0.0680 -0.0139 95  VAL A CB  
774  C CG1 . VAL A 115 ? 0.4174 0.2714 0.3309 -0.0102 -0.0573 -0.0128 95  VAL A CG1 
775  C CG2 . VAL A 115 ? 0.4059 0.2438 0.3210 -0.0130 -0.0821 -0.0164 95  VAL A CG2 
776  N N   . PHE A 116 ? 0.3404 0.2144 0.2630 -0.0062 -0.0490 -0.0104 96  PHE A N   
777  C CA  . PHE A 116 ? 0.3332 0.2171 0.2576 -0.0047 -0.0376 -0.0088 96  PHE A CA  
778  C C   . PHE A 116 ? 0.3459 0.2198 0.2530 -0.0009 -0.0341 -0.0089 96  PHE A C   
779  O O   . PHE A 116 ? 0.3507 0.2250 0.2526 0.0010  -0.0248 -0.0084 96  PHE A O   
780  C CB  . PHE A 116 ? 0.3129 0.2137 0.2573 -0.0069 -0.0354 -0.0073 96  PHE A CB  
781  C CG  . PHE A 116 ? 0.3049 0.2147 0.2661 -0.0107 -0.0354 -0.0066 96  PHE A CG  
782  C CD1 . PHE A 116 ? 0.3135 0.2219 0.2724 -0.0114 -0.0316 -0.0063 96  PHE A CD1 
783  C CD2 . PHE A 116 ? 0.3049 0.2244 0.2843 -0.0130 -0.0374 -0.0059 96  PHE A CD2 
784  C CE1 . PHE A 116 ? 0.3165 0.2310 0.2886 -0.0149 -0.0298 -0.0052 96  PHE A CE1 
785  C CE2 . PHE A 116 ? 0.3069 0.2336 0.3014 -0.0165 -0.0345 -0.0048 96  PHE A CE2 
786  C CZ  . PHE A 116 ? 0.3075 0.2308 0.2972 -0.0176 -0.0305 -0.0044 96  PHE A CZ  
787  N N   . VAL A 117 ? 0.3447 0.2094 0.2440 0.0003  -0.0414 -0.0097 97  VAL A N   
788  C CA  . VAL A 117 ? 0.3675 0.2195 0.2478 0.0038  -0.0378 -0.0096 97  VAL A CA  
789  C C   . VAL A 117 ? 0.3845 0.2166 0.2408 0.0070  -0.0344 -0.0105 97  VAL A C   
790  O O   . VAL A 117 ? 0.3958 0.2240 0.2430 0.0092  -0.0232 -0.0097 97  VAL A O   
791  C CB  . VAL A 117 ? 0.3928 0.2372 0.2689 0.0048  -0.0484 -0.0103 97  VAL A CB  
792  C CG1 . VAL A 117 ? 0.4221 0.2481 0.2733 0.0088  -0.0448 -0.0101 97  VAL A CG1 
793  C CG2 . VAL A 117 ? 0.3790 0.2433 0.2795 0.0025  -0.0494 -0.0092 97  VAL A CG2 
794  N N   . ARG A 118 ? 0.3796 0.1995 0.2274 0.0070  -0.0434 -0.0121 98  ARG A N   
795  C CA  . ARG A 118 ? 0.4046 0.2031 0.2279 0.0103  -0.0411 -0.0132 98  ARG A CA  
796  C C   . ARG A 118 ? 0.4015 0.2087 0.2301 0.0111  -0.0273 -0.0123 98  ARG A C   
797  O O   . ARG A 118 ? 0.4254 0.2204 0.2376 0.0149  -0.0175 -0.0121 98  ARG A O   
798  C CB  . ARG A 118 ? 0.4269 0.2162 0.2476 0.0087  -0.0543 -0.0153 98  ARG A CB  
799  C CG  . ARG A 118 ? 0.4685 0.2324 0.2611 0.0124  -0.0536 -0.0167 98  ARG A CG  
800  C CD  . ARG A 118 ? 0.4769 0.2372 0.2736 0.0095  -0.0648 -0.0185 98  ARG A CD  
801  N NE  . ARG A 118 ? 0.4635 0.2447 0.2832 0.0061  -0.0586 -0.0173 98  ARG A NE  
802  C CZ  . ARG A 118 ? 0.4842 0.2685 0.3151 0.0021  -0.0658 -0.0181 98  ARG A CZ  
803  N NH1 . ARG A 118 ? 0.4869 0.2572 0.3120 0.0004  -0.0806 -0.0203 98  ARG A NH1 
804  N NH2 . ARG A 118 ? 0.4485 0.2489 0.2965 -0.0003 -0.0589 -0.0167 98  ARG A NH2 
805  N N   . ASP A 119 ? 0.3782 0.2061 0.2303 0.0077  -0.0263 -0.0116 99  ASP A N   
806  C CA  . ASP A 119 ? 0.3631 0.1991 0.2217 0.0089  -0.0161 -0.0110 99  ASP A CA  
807  C C   . ASP A 119 ? 0.3609 0.2063 0.2259 0.0102  -0.0049 -0.0097 99  ASP A C   
808  O O   . ASP A 119 ? 0.3673 0.2100 0.2290 0.0132  0.0046  -0.0098 99  ASP A O   
809  C CB  . ASP A 119 ? 0.3517 0.2026 0.2292 0.0054  -0.0193 -0.0106 99  ASP A CB  
810  C CG  . ASP A 119 ? 0.3893 0.2295 0.2609 0.0038  -0.0281 -0.0119 99  ASP A CG  
811  O OD1 . ASP A 119 ? 0.4066 0.2268 0.2579 0.0059  -0.0328 -0.0134 99  ASP A OD1 
812  O OD2 . ASP A 119 ? 0.3734 0.2233 0.2591 0.0005  -0.0303 -0.0115 99  ASP A OD2 
813  N N   . VAL A 120 ? 0.3453 0.2007 0.2200 0.0082  -0.0058 -0.0088 100 VAL A N   
814  C CA  . VAL A 120 ? 0.3337 0.1961 0.2138 0.0089  0.0041  -0.0077 100 VAL A CA  
815  C C   . VAL A 120 ? 0.3602 0.2031 0.2190 0.0125  0.0115  -0.0078 100 VAL A C   
816  O O   . VAL A 120 ? 0.3704 0.2146 0.2319 0.0143  0.0228  -0.0075 100 VAL A O   
817  C CB  . VAL A 120 ? 0.3310 0.2036 0.2213 0.0063  0.0009  -0.0068 100 VAL A CB  
818  C CG1 . VAL A 120 ? 0.3413 0.2162 0.2331 0.0068  0.0104  -0.0059 100 VAL A CG1 
819  C CG2 . VAL A 120 ? 0.3132 0.2039 0.2238 0.0033  -0.0029 -0.0063 100 VAL A CG2 
820  N N   . LEU A 121 ? 0.3810 0.2043 0.2182 0.0140  0.0050  -0.0085 101 LEU A N   
821  C CA  . LEU A 121 ? 0.4128 0.2122 0.2238 0.0180  0.0123  -0.0085 101 LEU A CA  
822  C C   . LEU A 121 ? 0.4221 0.2114 0.2236 0.0214  0.0208  -0.0091 101 LEU A C   
823  O O   . LEU A 121 ? 0.4467 0.2271 0.2398 0.0242  0.0344  -0.0084 101 LEU A O   
824  C CB  . LEU A 121 ? 0.4371 0.2147 0.2243 0.0194  0.0010  -0.0094 101 LEU A CB  
825  C CG  . LEU A 121 ? 0.4679 0.2519 0.2614 0.0176  -0.0046 -0.0086 101 LEU A CG  
826  C CD1 . LEU A 121 ? 0.4989 0.2643 0.2743 0.0191  -0.0193 -0.0099 101 LEU A CD1 
827  C CD2 . LEU A 121 ? 0.4851 0.2652 0.2729 0.0186  0.0087  -0.0069 101 LEU A CD2 
828  N N   . GLN A 122 ? 0.4110 0.2025 0.2160 0.0211  0.0141  -0.0103 102 GLN A N   
829  C CA  . GLN A 122 ? 0.4107 0.1928 0.2072 0.0249  0.0221  -0.0110 102 GLN A CA  
830  C C   . GLN A 122 ? 0.4095 0.2100 0.2283 0.0255  0.0353  -0.0101 102 GLN A C   
831  O O   . GLN A 122 ? 0.4292 0.2204 0.2409 0.0294  0.0482  -0.0099 102 GLN A O   
832  C CB  . GLN A 122 ? 0.4096 0.1916 0.2073 0.0239  0.0115  -0.0123 102 GLN A CB  
833  C CG  . GLN A 122 ? 0.4406 0.2128 0.2297 0.0284  0.0195  -0.0131 102 GLN A CG  
834  C CD  . GLN A 122 ? 0.4638 0.2402 0.2593 0.0269  0.0109  -0.0141 102 GLN A CD  
835  O OE1 . GLN A 122 ? 0.4825 0.2667 0.2870 0.0222  -0.0012 -0.0143 102 GLN A OE1 
836  N NE2 . GLN A 122 ? 0.4597 0.2306 0.2513 0.0310  0.0178  -0.0148 102 GLN A NE2 
837  N N   . HIS A 123 ? 0.3802 0.2057 0.2260 0.0217  0.0320  -0.0095 103 HIS A N   
838  C CA  . HIS A 123 ? 0.3719 0.2150 0.2405 0.0221  0.0412  -0.0091 103 HIS A CA  
839  C C   . HIS A 123 ? 0.3756 0.2178 0.2461 0.0225  0.0531  -0.0081 103 HIS A C   
840  O O   . HIS A 123 ? 0.3844 0.2273 0.2620 0.0252  0.0654  -0.0081 103 HIS A O   
841  C CB  . HIS A 123 ? 0.3477 0.2130 0.2394 0.0183  0.0332  -0.0089 103 HIS A CB  
842  C CG  . HIS A 123 ? 0.3331 0.2136 0.2460 0.0196  0.0375  -0.0093 103 HIS A CG  
843  N ND1 . HIS A 123 ? 0.3423 0.2383 0.2714 0.0172  0.0303  -0.0093 103 HIS A ND1 
844  C CD2 . HIS A 123 ? 0.3413 0.2229 0.2620 0.0232  0.0479  -0.0098 103 HIS A CD2 
845  C CE1 . HIS A 123 ? 0.3373 0.2422 0.2819 0.0197  0.0344  -0.0100 103 HIS A CE1 
846  N NE2 . HIS A 123 ? 0.3368 0.2353 0.2797 0.0233  0.0451  -0.0103 103 HIS A NE2 
847  N N   . VAL A 124 ? 0.3777 0.2154 0.2402 0.0201  0.0504  -0.0072 104 VAL A N   
848  C CA  . VAL A 124 ? 0.3924 0.2262 0.2538 0.0200  0.0618  -0.0060 104 VAL A CA  
849  C C   . VAL A 124 ? 0.4272 0.2368 0.2656 0.0248  0.0747  -0.0059 104 VAL A C   
850  O O   . VAL A 124 ? 0.4378 0.2489 0.2853 0.0259  0.0897  -0.0053 104 VAL A O   
851  C CB  . VAL A 124 ? 0.4024 0.2319 0.2545 0.0173  0.0547  -0.0052 104 VAL A CB  
852  C CG1 . VAL A 124 ? 0.4233 0.2386 0.2630 0.0180  0.0669  -0.0039 104 VAL A CG1 
853  C CG2 . VAL A 124 ? 0.3721 0.2256 0.2490 0.0130  0.0468  -0.0051 104 VAL A CG2 
854  N N   . ASP A 125 ? 0.4441 0.2307 0.2534 0.0276  0.0690  -0.0066 105 ASP A N   
855  C CA  . ASP A 125 ? 0.4736 0.2321 0.2549 0.0329  0.0807  -0.0066 105 ASP A CA  
856  C C   . ASP A 125 ? 0.4872 0.2512 0.2813 0.0363  0.0929  -0.0070 105 ASP A C   
857  O O   . ASP A 125 ? 0.5156 0.2675 0.3029 0.0396  0.1102  -0.0062 105 ASP A O   
858  C CB  . ASP A 125 ? 0.5087 0.2410 0.2564 0.0354  0.0685  -0.0078 105 ASP A CB  
859  C CG  . ASP A 125 ? 0.5580 0.2777 0.2879 0.0339  0.0584  -0.0074 105 ASP A CG  
860  O OD1 . ASP A 125 ? 0.5643 0.2894 0.3007 0.0320  0.0645  -0.0059 105 ASP A OD1 
861  O OD2 . ASP A 125 ? 0.5808 0.2846 0.2907 0.0349  0.0438  -0.0088 105 ASP A OD2 
862  N N   . SER A 126 ? 0.4657 0.2480 0.2794 0.0356  0.0848  -0.0082 106 SER A N   
863  C CA  A SER A 126 ? 0.4663 0.2554 0.2945 0.0393  0.0941  -0.0089 106 SER A CA  
864  C CA  C SER A 126 ? 0.4706 0.2593 0.2984 0.0393  0.0944  -0.0089 106 SER A CA  
865  C C   . SER A 126 ? 0.4691 0.2781 0.3285 0.0382  0.1068  -0.0081 106 SER A C   
866  O O   . SER A 126 ? 0.4946 0.3000 0.3596 0.0423  0.1223  -0.0081 106 SER A O   
867  C CB  A SER A 126 ? 0.4602 0.2642 0.3020 0.0383  0.0807  -0.0102 106 SER A CB  
868  C CB  C SER A 126 ? 0.4774 0.2794 0.3172 0.0387  0.0813  -0.0102 106 SER A CB  
869  O OG  A SER A 126 ? 0.4658 0.2718 0.3164 0.0430  0.0879  -0.0111 106 SER A OG  
870  O OG  C SER A 126 ? 0.5204 0.3015 0.3319 0.0398  0.0715  -0.0111 106 SER A OG  
871  N N   . MET A 127 ? 0.4550 0.2845 0.3358 0.0328  0.1003  -0.0076 107 MET A N   
872  C CA  . MET A 127 ? 0.4577 0.3063 0.3698 0.0310  0.1097  -0.0072 107 MET A CA  
873  C C   . MET A 127 ? 0.4912 0.3262 0.3953 0.0313  0.1270  -0.0057 107 MET A C   
874  O O   . MET A 127 ? 0.4957 0.3392 0.4224 0.0321  0.1411  -0.0056 107 MET A O   
875  C CB  . MET A 127 ? 0.4452 0.3157 0.3779 0.0254  0.0972  -0.0073 107 MET A CB  
876  C CG  . MET A 127 ? 0.4672 0.3522 0.4132 0.0256  0.0844  -0.0086 107 MET A CG  
877  S SD  . MET A 127 ? 0.5151 0.4159 0.4927 0.0294  0.0914  -0.0101 107 MET A SD  
878  C CE  . MET A 127 ? 0.4786 0.3992 0.4870 0.0246  0.0928  -0.0100 107 MET A CE  
879  N N   . GLN A 128 ? 0.5154 0.3280 0.3874 0.0309  0.1263  -0.0046 108 GLN A N   
880  C CA  . GLN A 128 ? 0.5503 0.3446 0.4081 0.0314  0.1432  -0.0028 108 GLN A CA  
881  C C   . GLN A 128 ? 0.5930 0.3668 0.4361 0.0377  0.1613  -0.0026 108 GLN A C   
882  O O   . GLN A 128 ? 0.6050 0.3694 0.4480 0.0384  0.1804  -0.0011 108 GLN A O   
883  C CB  . GLN A 128 ? 0.5791 0.3528 0.4045 0.0301  0.1359  -0.0018 108 GLN A CB  
884  C CG  . GLN A 128 ? 0.5941 0.3882 0.4380 0.0241  0.1241  -0.0015 108 GLN A CG  
885  C CD  . GLN A 128 ? 0.6674 0.4408 0.4836 0.0233  0.1225  -0.0002 108 GLN A CD  
886  O OE1 . GLN A 128 ? 0.6974 0.4582 0.4905 0.0244  0.1086  -0.0007 108 GLN A OE1 
887  N NE2 . GLN A 128 ? 0.6853 0.4538 0.5036 0.0214  0.1367  0.0016  108 GLN A NE2 
888  N N   . LYS A 129 ? 0.6257 0.3925 0.4576 0.0423  0.1563  -0.0041 109 LYS A N   
889  C CA  . LYS A 129 ? 0.6591 0.4074 0.4784 0.0490  0.1731  -0.0042 109 LYS A CA  
890  C C   . LYS A 129 ? 0.6555 0.4294 0.5189 0.0495  0.1859  -0.0045 109 LYS A C   
891  O O   . LYS A 129 ? 0.6645 0.4290 0.5304 0.0527  0.2075  -0.0035 109 LYS A O   
892  C CB  . LYS A 129 ? 0.6979 0.4341 0.4959 0.0533  0.1613  -0.0060 109 LYS A CB  
893  C CG  . LYS A 129 ? 0.7891 0.4942 0.5414 0.0542  0.1507  -0.0060 109 LYS A CG  
894  C CD  . LYS A 129 ? 0.9010 0.5668 0.6132 0.0610  0.1666  -0.0055 109 LYS A CD  
895  C CE  . LYS A 129 ? 0.9571 0.6174 0.6694 0.0674  0.1756  -0.0067 109 LYS A CE  
896  N NZ  . LYS A 129 ? 0.9780 0.6478 0.6938 0.0671  0.1559  -0.0088 109 LYS A NZ  
897  N N   . ASP A 130 ? 0.6429 0.4480 0.5413 0.0466  0.1727  -0.0059 110 ASP A N   
898  C CA  . ASP A 130 ? 0.6413 0.4717 0.5837 0.0473  0.1806  -0.0068 110 ASP A CA  
899  C C   . ASP A 130 ? 0.6384 0.4830 0.6088 0.0422  0.1907  -0.0057 110 ASP A C   
900  O O   . ASP A 130 ? 0.6333 0.4903 0.6359 0.0435  0.2045  -0.0060 110 ASP A O   
901  C CB  . ASP A 130 ? 0.6577 0.5124 0.6233 0.0466  0.1614  -0.0088 110 ASP A CB  
902  C CG  . ASP A 130 ? 0.7461 0.5893 0.6907 0.0516  0.1531  -0.0100 110 ASP A CG  
903  O OD1 . ASP A 130 ? 0.7742 0.5912 0.6887 0.0566  0.1629  -0.0097 110 ASP A OD1 
904  O OD2 . ASP A 130 ? 0.7826 0.6407 0.7386 0.0506  0.1368  -0.0113 110 ASP A OD2 
905  N N   . TYR A 131 ? 0.6405 0.4834 0.6007 0.0363  0.1836  -0.0045 111 TYR A N   
906  C CA  . TYR A 131 ? 0.6329 0.4869 0.6167 0.0308  0.1919  -0.0034 111 TYR A CA  
907  C C   . TYR A 131 ? 0.6570 0.4840 0.6046 0.0292  0.1995  -0.0010 111 TYR A C   
908  O O   . TYR A 131 ? 0.6666 0.4941 0.6042 0.0248  0.1870  -0.0005 111 TYR A O   
909  C CB  . TYR A 131 ? 0.6141 0.4956 0.6252 0.0250  0.1728  -0.0046 111 TYR A CB  
910  C CG  . TYR A 131 ? 0.6047 0.5093 0.6468 0.0272  0.1631  -0.0071 111 TYR A CG  
911  C CD1 . TYR A 131 ? 0.6158 0.5204 0.6444 0.0298  0.1472  -0.0083 111 TYR A CD1 
912  C CD2 . TYR A 131 ? 0.5968 0.5215 0.6816 0.0270  0.1703  -0.0082 111 TYR A CD2 
913  C CE1 . TYR A 131 ? 0.6183 0.5402 0.6714 0.0326  0.1387  -0.0104 111 TYR A CE1 
914  C CE2 . TYR A 131 ? 0.5927 0.5361 0.7042 0.0300  0.1602  -0.0107 111 TYR A CE2 
915  C CZ  . TYR A 131 ? 0.6147 0.5555 0.7083 0.0331  0.1448  -0.0116 111 TYR A CZ  
916  O OH  . TYR A 131 ? 0.6274 0.5840 0.7442 0.0364  0.1344  -0.0139 111 TYR A OH  
917  N N   . PRO A 132 ? 0.6696 0.4698 0.5935 0.0336  0.2197  0.0005  112 PRO A N   
918  C CA  . PRO A 132 ? 0.6915 0.4607 0.5747 0.0331  0.2262  0.0028  112 PRO A CA  
919  C C   . PRO A 132 ? 0.6869 0.4612 0.5858 0.0268  0.2359  0.0046  112 PRO A C   
920  O O   . PRO A 132 ? 0.6786 0.4761 0.6201 0.0236  0.2449  0.0043  112 PRO A O   
921  C CB  . PRO A 132 ? 0.7223 0.4602 0.5763 0.0403  0.2463  0.0037  112 PRO A CB  
922  C CG  . PRO A 132 ? 0.7091 0.4676 0.6034 0.0426  0.2591  0.0027  112 PRO A CG  
923  C CD  . PRO A 132 ? 0.6633 0.4580 0.5943 0.0398  0.2379  0.0002  112 PRO A CD  
924  N N   . GLY A 133 ? 0.6935 0.4458 0.5585 0.0252  0.2329  0.0062  113 GLY A N   
925  C CA  . GLY A 133 ? 0.6818 0.4332 0.5537 0.0194  0.2418  0.0082  113 GLY A CA  
926  C C   . GLY A 133 ? 0.6452 0.4277 0.5509 0.0123  0.2261  0.0072  113 GLY A C   
927  O O   . GLY A 133 ? 0.6508 0.4337 0.5648 0.0070  0.2327  0.0086  113 GLY A O   
928  N N   . LEU A 134 ? 0.6020 0.4084 0.5255 0.0121  0.2057  0.0048  114 LEU A N   
929  C CA  . LEU A 134 ? 0.5596 0.3929 0.5119 0.0061  0.1906  0.0037  114 LEU A CA  
930  C C   . LEU A 134 ? 0.5394 0.3650 0.4652 0.0051  0.1728  0.0039  114 LEU A C   
931  O O   . LEU A 134 ? 0.5525 0.3659 0.4512 0.0091  0.1626  0.0035  114 LEU A O   
932  C CB  . LEU A 134 ? 0.5451 0.4074 0.5313 0.0066  0.1785  0.0010  114 LEU A CB  
933  C CG  . LEU A 134 ? 0.5573 0.4374 0.5840 0.0068  0.1908  0.0000  114 LEU A CG  
934  C CD1 . LEU A 134 ? 0.5481 0.4548 0.6039 0.0074  0.1740  -0.0028 114 LEU A CD1 
935  C CD2 . LEU A 134 ? 0.5568 0.4441 0.6100 0.0006  0.2030  0.0009  114 LEU A CD2 
936  N N   . PRO A 135 ? 0.5035 0.3380 0.4401 -0.0004 0.1676  0.0044  115 PRO A N   
937  C CA  . PRO A 135 ? 0.4844 0.3155 0.4015 -0.0011 0.1498  0.0043  115 PRO A CA  
938  C C   . PRO A 135 ? 0.4462 0.2970 0.3754 -0.0001 0.1312  0.0022  115 PRO A C   
939  O O   . PRO A 135 ? 0.4311 0.3028 0.3901 -0.0008 0.1298  0.0007  115 PRO A O   
940  C CB  . PRO A 135 ? 0.4886 0.3287 0.4223 -0.0073 0.1501  0.0050  115 PRO A CB  
941  C CG  . PRO A 135 ? 0.5042 0.3430 0.4561 -0.0098 0.1716  0.0060  115 PRO A CG  
942  C CD  . PRO A 135 ? 0.4801 0.3287 0.4492 -0.0063 0.1769  0.0047  115 PRO A CD  
943  N N   . VAL A 136 ? 0.4219 0.2647 0.3281 0.0017  0.1171  0.0020  116 VAL A N   
944  C CA  A VAL A 136 ? 0.4071 0.2661 0.3227 0.0023  0.1008  0.0004  116 VAL A CA  
945  C CA  B VAL A 136 ? 0.4006 0.2595 0.3160 0.0023  0.1007  0.0004  116 VAL A CA  
946  C C   . VAL A 136 ? 0.3943 0.2595 0.3088 -0.0002 0.0869  0.0004  116 VAL A C   
947  O O   . VAL A 136 ? 0.4120 0.2612 0.3035 0.0006  0.0843  0.0014  116 VAL A O   
948  C CB  A VAL A 136 ? 0.4406 0.2874 0.3359 0.0072  0.0968  -0.0003 116 VAL A CB  
949  C CB  B VAL A 136 ? 0.4194 0.2646 0.3125 0.0072  0.0967  -0.0002 116 VAL A CB  
950  C CG1 A VAL A 136 ? 0.4812 0.3000 0.3392 0.0099  0.0957  0.0006  116 VAL A CG1 
951  C CG1 B VAL A 136 ? 0.4173 0.2783 0.3207 0.0072  0.0811  -0.0017 116 VAL A CG1 
952  C CG2 A VAL A 136 ? 0.4362 0.2991 0.3422 0.0071  0.0811  -0.0018 116 VAL A CG2 
953  C CG2 B VAL A 136 ? 0.4230 0.2608 0.3162 0.0104  0.1114  -0.0003 116 VAL A CG2 
954  N N   . PHE A 137 ? 0.3570 0.2440 0.2954 -0.0026 0.0782  -0.0008 117 PHE A N   
955  C CA  . PHE A 137 ? 0.3411 0.2352 0.2807 -0.0045 0.0661  -0.0008 117 PHE A CA  
956  C C   . PHE A 137 ? 0.3229 0.2244 0.2629 -0.0028 0.0540  -0.0018 117 PHE A C   
957  O O   . PHE A 137 ? 0.3172 0.2226 0.2623 -0.0010 0.0542  -0.0027 117 PHE A O   
958  C CB  . PHE A 137 ? 0.3324 0.2431 0.2973 -0.0085 0.0654  -0.0014 117 PHE A CB  
959  C CG  . PHE A 137 ? 0.3504 0.2556 0.3185 -0.0116 0.0761  -0.0005 117 PHE A CG  
960  C CD1 . PHE A 137 ? 0.3665 0.2705 0.3453 -0.0122 0.0897  -0.0003 117 PHE A CD1 
961  C CD2 . PHE A 137 ? 0.3672 0.2680 0.3288 -0.0140 0.0734  0.0004  117 PHE A CD2 
962  C CE1 . PHE A 137 ? 0.3817 0.2795 0.3643 -0.0157 0.1011  0.0008  117 PHE A CE1 
963  C CE2 . PHE A 137 ? 0.3721 0.2657 0.3352 -0.0172 0.0838  0.0014  117 PHE A CE2 
964  C CZ  . PHE A 137 ? 0.3793 0.2716 0.3534 -0.0184 0.0978  0.0017  117 PHE A CZ  
965  N N   . LEU A 138 ? 0.3123 0.2159 0.2483 -0.0034 0.0442  -0.0016 118 LEU A N   
966  C CA  . LEU A 138 ? 0.3118 0.2235 0.2514 -0.0027 0.0339  -0.0023 118 LEU A CA  
967  C C   . LEU A 138 ? 0.3044 0.2288 0.2577 -0.0049 0.0288  -0.0024 118 LEU A C   
968  O O   . LEU A 138 ? 0.3077 0.2307 0.2603 -0.0064 0.0295  -0.0019 118 LEU A O   
969  C CB  . LEU A 138 ? 0.3254 0.2264 0.2480 -0.0008 0.0268  -0.0020 118 LEU A CB  
970  C CG  . LEU A 138 ? 0.3624 0.2460 0.2657 0.0020  0.0292  -0.0021 118 LEU A CG  
971  C CD1 . LEU A 138 ? 0.3911 0.2615 0.2770 0.0037  0.0209  -0.0020 118 LEU A CD1 
972  C CD2 . LEU A 138 ? 0.3711 0.2578 0.2779 0.0032  0.0284  -0.0031 118 LEU A CD2 
973  N N   . LEU A 139 ? 0.2855 0.2198 0.2485 -0.0048 0.0235  -0.0031 119 LEU A N   
974  C CA  . LEU A 139 ? 0.2793 0.2219 0.2504 -0.0061 0.0183  -0.0032 119 LEU A CA  
975  C C   . LEU A 139 ? 0.2803 0.2244 0.2489 -0.0050 0.0124  -0.0031 119 LEU A C   
976  O O   . LEU A 139 ? 0.2793 0.2243 0.2490 -0.0040 0.0117  -0.0036 119 LEU A O   
977  C CB  . LEU A 139 ? 0.2729 0.2240 0.2587 -0.0071 0.0185  -0.0043 119 LEU A CB  
978  C CG  . LEU A 139 ? 0.2920 0.2471 0.2815 -0.0080 0.0130  -0.0046 119 LEU A CG  
979  C CD1 . LEU A 139 ? 0.2927 0.2519 0.2945 -0.0099 0.0131  -0.0058 119 LEU A CD1 
980  C CD2 . LEU A 139 ? 0.2859 0.2432 0.2745 -0.0064 0.0078  -0.0047 119 LEU A CD2 
981  N N   . GLY A 140 ? 0.2637 0.2076 0.2298 -0.0051 0.0088  -0.0024 120 GLY A N   
982  C CA  . GLY A 140 ? 0.2576 0.2034 0.2245 -0.0045 0.0046  -0.0021 120 GLY A CA  
983  C C   . GLY A 140 ? 0.2669 0.2167 0.2379 -0.0048 0.0033  -0.0015 120 GLY A C   
984  O O   . GLY A 140 ? 0.2782 0.2270 0.2481 -0.0049 0.0038  -0.0012 120 GLY A O   
985  N N   . HIS A 141 ? 0.2501 0.2023 0.2242 -0.0047 0.0022  -0.0012 121 HIS A N   
986  C CA  . HIS A 141 ? 0.2630 0.2162 0.2389 -0.0045 0.0027  -0.0004 121 HIS A CA  
987  C C   . HIS A 141 ? 0.2735 0.2277 0.2535 -0.0046 0.0023  0.0004  121 HIS A C   
988  O O   . HIS A 141 ? 0.2721 0.2261 0.2532 -0.0053 0.0012  0.0003  121 HIS A O   
989  C CB  . HIS A 141 ? 0.2713 0.2233 0.2456 -0.0041 0.0028  -0.0007 121 HIS A CB  
990  C CG  . HIS A 141 ? 0.2840 0.2329 0.2558 -0.0034 0.0047  0.0003  121 HIS A CG  
991  N ND1 . HIS A 141 ? 0.2870 0.2345 0.2577 -0.0026 0.0067  0.0009  121 HIS A ND1 
992  C CD2 . HIS A 141 ? 0.2917 0.2367 0.2604 -0.0029 0.0059  0.0009  121 HIS A CD2 
993  C CE1 . HIS A 141 ? 0.2941 0.2370 0.2613 -0.0016 0.0099  0.0020  121 HIS A CE1 
994  N NE2 . HIS A 141 ? 0.3026 0.2433 0.2680 -0.0019 0.0098  0.0021  121 HIS A NE2 
995  N N   . SER A 142 ? 0.2770 0.2325 0.2610 -0.0039 0.0031  0.0012  122 SER A N   
996  C CA  . SER A 142 ? 0.2750 0.2331 0.2680 -0.0042 0.0037  0.0021  122 SER A CA  
997  C C   . SER A 142 ? 0.2623 0.2211 0.2597 -0.0052 -0.0015 0.0014  122 SER A C   
998  O O   . SER A 142 ? 0.2458 0.2024 0.2399 -0.0043 -0.0056 0.0006  122 SER A O   
999  C CB  . SER A 142 ? 0.3136 0.2698 0.3060 -0.0047 0.0083  0.0030  122 SER A CB  
1000 O OG  . SER A 142 ? 0.3353 0.2938 0.3382 -0.0050 0.0119  0.0042  122 SER A OG  
1001 N N   . MET A 143 ? 0.2633 0.2226 0.2657 -0.0069 -0.0018 0.0016  123 MET A N   
1002 C CA  . MET A 143 ? 0.2613 0.2187 0.2654 -0.0079 -0.0081 0.0005  123 MET A CA  
1003 C C   . MET A 143 ? 0.2588 0.2101 0.2491 -0.0069 -0.0105 -0.0006 123 MET A C   
1004 O O   . MET A 143 ? 0.2749 0.2210 0.2608 -0.0062 -0.0160 -0.0016 123 MET A O   
1005 C CB  . MET A 143 ? 0.2653 0.2226 0.2749 -0.0104 -0.0073 0.0009  123 MET A CB  
1006 C CG  . MET A 143 ? 0.2866 0.2400 0.2968 -0.0116 -0.0148 -0.0005 123 MET A CG  
1007 S SD  . MET A 143 ? 0.3149 0.2660 0.3288 -0.0149 -0.0135 -0.0001 123 MET A SD  
1008 C CE  . MET A 143 ? 0.3078 0.2523 0.3032 -0.0130 -0.0114 -0.0006 123 MET A CE  
1009 N N   . GLY A 144 ? 0.2537 0.2044 0.2373 -0.0064 -0.0063 -0.0006 124 GLY A N   
1010 C CA  . GLY A 144 ? 0.2577 0.2037 0.2315 -0.0054 -0.0061 -0.0015 124 GLY A CA  
1011 C C   . GLY A 144 ? 0.2623 0.2053 0.2309 -0.0043 -0.0063 -0.0016 124 GLY A C   
1012 O O   . GLY A 144 ? 0.2816 0.2175 0.2409 -0.0034 -0.0061 -0.0022 124 GLY A O   
1013 N N   . GLY A 145 ? 0.2548 0.2013 0.2279 -0.0040 -0.0059 -0.0009 125 GLY A N   
1014 C CA  . GLY A 145 ? 0.2707 0.2131 0.2383 -0.0028 -0.0064 -0.0009 125 GLY A CA  
1015 C C   . GLY A 145 ? 0.2824 0.2188 0.2471 -0.0015 -0.0130 -0.0014 125 GLY A C   
1016 O O   . GLY A 145 ? 0.2902 0.2170 0.2430 -0.0001 -0.0144 -0.0017 125 GLY A O   
1017 N N   . ALA A 146 ? 0.2794 0.2201 0.2548 -0.0020 -0.0174 -0.0015 126 ALA A N   
1018 C CA  . ALA A 146 ? 0.2895 0.2242 0.2643 -0.0009 -0.0264 -0.0025 126 ALA A CA  
1019 C C   . ALA A 146 ? 0.2999 0.2228 0.2594 -0.0006 -0.0289 -0.0035 126 ALA A C   
1020 O O   . ALA A 146 ? 0.3229 0.2332 0.2688 0.0016  -0.0342 -0.0043 126 ALA A O   
1021 C CB  . ALA A 146 ? 0.2828 0.2257 0.2765 -0.0023 -0.0301 -0.0026 126 ALA A CB  
1022 N N   . ILE A 147 ? 0.2911 0.2161 0.2504 -0.0023 -0.0246 -0.0035 127 ILE A N   
1023 C CA  . ILE A 147 ? 0.2971 0.2104 0.2412 -0.0015 -0.0250 -0.0044 127 ILE A CA  
1024 C C   . ILE A 147 ? 0.3130 0.2167 0.2412 0.0006  -0.0199 -0.0042 127 ILE A C   
1025 O O   . ILE A 147 ? 0.3377 0.2258 0.2487 0.0027  -0.0227 -0.0049 127 ILE A O   
1026 C CB  . ILE A 147 ? 0.2962 0.2147 0.2447 -0.0030 -0.0205 -0.0043 127 ILE A CB  
1027 C CG1 . ILE A 147 ? 0.2805 0.2043 0.2419 -0.0054 -0.0252 -0.0044 127 ILE A CG1 
1028 C CG2 . ILE A 147 ? 0.3237 0.2302 0.2565 -0.0014 -0.0187 -0.0052 127 ILE A CG2 
1029 C CD1 . ILE A 147 ? 0.2861 0.2147 0.2517 -0.0069 -0.0202 -0.0039 127 ILE A CD1 
1030 N N   . ALA A 148 ? 0.3058 0.2169 0.2386 0.0000  -0.0125 -0.0033 128 ALA A N   
1031 C CA  . ALA A 148 ? 0.3223 0.2250 0.2433 0.0011  -0.0062 -0.0029 128 ALA A CA  
1032 C C   . ALA A 148 ? 0.3395 0.2295 0.2473 0.0032  -0.0106 -0.0029 128 ALA A C   
1033 O O   . ALA A 148 ? 0.3643 0.2379 0.2534 0.0051  -0.0083 -0.0029 128 ALA A O   
1034 C CB  . ALA A 148 ? 0.3105 0.2240 0.2420 -0.0006 0.0005  -0.0022 128 ALA A CB  
1035 N N   . ILE A 149 ? 0.3255 0.2208 0.2416 0.0035  -0.0171 -0.0027 129 ILE A N   
1036 C CA  . ILE A 149 ? 0.3388 0.2215 0.2430 0.0063  -0.0232 -0.0029 129 ILE A CA  
1037 C C   . ILE A 149 ? 0.3578 0.2238 0.2462 0.0086  -0.0315 -0.0042 129 ILE A C   
1038 O O   . ILE A 149 ? 0.3837 0.2301 0.2497 0.0114  -0.0321 -0.0043 129 ILE A O   
1039 C CB  . ILE A 149 ? 0.3384 0.2319 0.2588 0.0067  -0.0291 -0.0028 129 ILE A CB  
1040 C CG1 . ILE A 149 ? 0.3372 0.2409 0.2658 0.0054  -0.0211 -0.0016 129 ILE A CG1 
1041 C CG2 . ILE A 149 ? 0.3560 0.2367 0.2668 0.0105  -0.0392 -0.0035 129 ILE A CG2 
1042 C CD1 . ILE A 149 ? 0.3377 0.2531 0.2837 0.0059  -0.0242 -0.0014 129 ILE A CD1 
1043 N N   . LEU A 150 ? 0.3474 0.2188 0.2458 0.0075  -0.0379 -0.0052 130 LEU A N   
1044 C CA  . LEU A 150 ? 0.3696 0.2238 0.2529 0.0095  -0.0478 -0.0069 130 LEU A CA  
1045 C C   . LEU A 150 ? 0.3956 0.2322 0.2545 0.0109  -0.0409 -0.0069 130 LEU A C   
1046 O O   . LEU A 150 ? 0.4423 0.2560 0.2773 0.0141  -0.0467 -0.0079 130 LEU A O   
1047 C CB  . LEU A 150 ? 0.3632 0.2274 0.2648 0.0072  -0.0560 -0.0081 130 LEU A CB  
1048 C CG  . LEU A 150 ? 0.3676 0.2469 0.2939 0.0064  -0.0624 -0.0081 130 LEU A CG  
1049 C CD1 . LEU A 150 ? 0.3538 0.2437 0.3007 0.0032  -0.0673 -0.0089 130 LEU A CD1 
1050 C CD2 . LEU A 150 ? 0.3969 0.2640 0.3154 0.0103  -0.0742 -0.0092 130 LEU A CD2 
1051 N N   . THR A 151 ? 0.3762 0.2220 0.2407 0.0090  -0.0286 -0.0059 131 THR A N   
1052 C CA  . THR A 151 ? 0.4010 0.2329 0.2472 0.0104  -0.0194 -0.0058 131 THR A CA  
1053 C C   . THR A 151 ? 0.4267 0.2418 0.2527 0.0128  -0.0129 -0.0049 131 THR A C   
1054 O O   . THR A 151 ? 0.4478 0.2385 0.2470 0.0160  -0.0114 -0.0052 131 THR A O   
1055 C CB  . THR A 151 ? 0.4050 0.2541 0.2680 0.0080  -0.0088 -0.0052 131 THR A CB  
1056 O OG1 . THR A 151 ? 0.3873 0.2474 0.2643 0.0062  -0.0145 -0.0060 131 THR A OG1 
1057 C CG2 . THR A 151 ? 0.4270 0.2643 0.2761 0.0098  0.0024  -0.0050 131 THR A CG2 
1058 N N   . ALA A 152 ? 0.4194 0.2448 0.2559 0.0113  -0.0090 -0.0036 132 ALA A N   
1059 C CA  . ALA A 152 ? 0.4572 0.2661 0.2749 0.0130  -0.0022 -0.0025 132 ALA A CA  
1060 C C   . ALA A 152 ? 0.5166 0.3029 0.3109 0.0170  -0.0133 -0.0031 132 ALA A C   
1061 O O   . ALA A 152 ? 0.5644 0.3255 0.3308 0.0199  -0.0085 -0.0026 132 ALA A O   
1062 C CB  . ALA A 152 ? 0.4417 0.2660 0.2759 0.0103  0.0031  -0.0013 132 ALA A CB  
1063 N N   . ALA A 153 ? 0.5164 0.3098 0.3215 0.0175  -0.0281 -0.0044 133 ALA A N   
1064 C CA  . ALA A 153 ? 0.5494 0.3218 0.3350 0.0219  -0.0416 -0.0055 133 ALA A CA  
1065 C C   . ALA A 153 ? 0.5771 0.3238 0.3357 0.0250  -0.0474 -0.0070 133 ALA A C   
1066 O O   . ALA A 153 ? 0.6094 0.3291 0.3400 0.0295  -0.0550 -0.0076 133 ALA A O   
1067 C CB  . ALA A 153 ? 0.5444 0.3330 0.3536 0.0216  -0.0558 -0.0066 133 ALA A CB  
1068 N N   . GLU A 154 ? 0.5637 0.3165 0.3284 0.0231  -0.0447 -0.0076 134 GLU A N   
1069 C CA  . GLU A 154 ? 0.5919 0.3196 0.3302 0.0261  -0.0492 -0.0092 134 GLU A CA  
1070 C C   . GLU A 154 ? 0.6206 0.3226 0.3266 0.0291  -0.0342 -0.0078 134 GLU A C   
1071 O O   . GLU A 154 ? 0.6573 0.3273 0.3291 0.0335  -0.0381 -0.0088 134 GLU A O   
1072 C CB  . GLU A 154 ? 0.6075 0.3506 0.3637 0.0230  -0.0493 -0.0101 134 GLU A CB  
1073 C CG  . GLU A 154 ? 0.6668 0.3838 0.3961 0.0260  -0.0544 -0.0119 134 GLU A CG  
1074 C CD  . GLU A 154 ? 0.6827 0.4131 0.4301 0.0230  -0.0600 -0.0133 134 GLU A CD  
1075 O OE1 . GLU A 154 ? 0.6517 0.4059 0.4295 0.0192  -0.0675 -0.0136 134 GLU A OE1 
1076 O OE2 . GLU A 154 ? 0.7283 0.4440 0.4586 0.0245  -0.0564 -0.0140 134 GLU A OE2 
1077 N N   . ARG A 155 ? 0.6033 0.3178 0.3199 0.0266  -0.0166 -0.0056 135 ARG A N   
1078 C CA  . ARG A 155 ? 0.6202 0.3131 0.3119 0.0287  0.0003  -0.0041 135 ARG A CA  
1079 C C   . ARG A 155 ? 0.6340 0.3256 0.3242 0.0279  0.0092  -0.0019 135 ARG A C   
1080 O O   . ARG A 155 ? 0.6166 0.3239 0.3244 0.0245  0.0241  -0.0004 135 ARG A O   
1081 C CB  . ARG A 155 ? 0.6118 0.3190 0.3190 0.0265  0.0151  -0.0036 135 ARG A CB  
1082 C CG  . ARG A 155 ? 0.6266 0.3367 0.3372 0.0270  0.0074  -0.0056 135 ARG A CG  
1083 C CD  . ARG A 155 ? 0.6516 0.3380 0.3369 0.0306  0.0194  -0.0055 135 ARG A CD  
1084 N NE  . ARG A 155 ? 0.6444 0.3314 0.3308 0.0313  0.0129  -0.0074 135 ARG A NE  
1085 C CZ  . ARG A 155 ? 0.6339 0.3293 0.3303 0.0312  0.0244  -0.0073 135 ARG A CZ  
1086 N NH1 . ARG A 155 ? 0.6018 0.3085 0.3121 0.0302  0.0422  -0.0056 135 ARG A NH1 
1087 N NH2 . ARG A 155 ? 0.6079 0.3012 0.3027 0.0320  0.0176  -0.0090 135 ARG A NH2 
1088 N N   . PRO A 156 ? 0.6672 0.3401 0.3374 0.0310  -0.0006 -0.0020 136 PRO A N   
1089 C CA  . PRO A 156 ? 0.6791 0.3490 0.3463 0.0302  0.0079  0.0001  136 PRO A CA  
1090 C C   . PRO A 156 ? 0.6868 0.3397 0.3367 0.0300  0.0299  0.0023  136 PRO A C   
1091 O O   . PRO A 156 ? 0.7058 0.3312 0.3261 0.0336  0.0358  0.0023  136 PRO A O   
1092 C CB  . PRO A 156 ? 0.7153 0.3610 0.3570 0.0352  -0.0080 -0.0007 136 PRO A CB  
1093 C CG  . PRO A 156 ? 0.7423 0.3682 0.3633 0.0393  -0.0211 -0.0030 136 PRO A CG  
1094 C CD  . PRO A 156 ? 0.6943 0.3467 0.3437 0.0355  -0.0205 -0.0041 136 PRO A CD  
1095 N N   . GLY A 157 ? 0.6570 0.3277 0.3283 0.0254  0.0425  0.0040  137 GLY A N   
1096 C CA  . GLY A 157 ? 0.6637 0.3239 0.3280 0.0239  0.0646  0.0061  137 GLY A CA  
1097 C C   . GLY A 157 ? 0.6533 0.3296 0.3383 0.0215  0.0778  0.0060  137 GLY A C   
1098 O O   . GLY A 157 ? 0.6755 0.3481 0.3630 0.0196  0.0970  0.0077  137 GLY A O   
1099 N N   . HIS A 158 ? 0.6163 0.3097 0.3171 0.0216  0.0682  0.0041  138 HIS A N   
1100 C CA  . HIS A 158 ? 0.6075 0.3141 0.3258 0.0206  0.0788  0.0037  138 HIS A CA  
1101 C C   . HIS A 158 ? 0.5719 0.3139 0.3325 0.0150  0.0836  0.0038  138 HIS A C   
1102 O O   . HIS A 158 ? 0.5877 0.3379 0.3639 0.0137  0.0977  0.0041  138 HIS A O   
1103 C CB  . HIS A 158 ? 0.6387 0.3467 0.3541 0.0231  0.0652  0.0015  138 HIS A CB  
1104 C CG  . HIS A 158 ? 0.7040 0.4211 0.4319 0.0233  0.0741  0.0009  138 HIS A CG  
1105 N ND1 . HIS A 158 ? 0.7617 0.4521 0.4619 0.0280  0.0826  0.0008  138 HIS A ND1 
1106 C CD2 . HIS A 158 ? 0.7011 0.4486 0.4635 0.0203  0.0740  0.0001  138 HIS A CD2 
1107 C CE1 . HIS A 158 ? 0.7562 0.4633 0.4772 0.0276  0.0880  0.0000  138 HIS A CE1 
1108 N NE2 . HIS A 158 ? 0.7251 0.4665 0.4837 0.0230  0.0828  -0.0004 138 HIS A NE2 
1109 N N   . PHE A 159 ? 0.5184 0.2809 0.2981 0.0122  0.0709  0.0032  139 PHE A N   
1110 C CA  . PHE A 159 ? 0.4708 0.2641 0.2872 0.0075  0.0725  0.0030  139 PHE A CA  
1111 C C   . PHE A 159 ? 0.4671 0.2627 0.2911 0.0039  0.0804  0.0044  139 PHE A C   
1112 O O   . PHE A 159 ? 0.4777 0.2583 0.2833 0.0047  0.0773  0.0053  139 PHE A O   
1113 C CB  . PHE A 159 ? 0.4441 0.2574 0.2767 0.0066  0.0561  0.0016  139 PHE A CB  
1114 C CG  . PHE A 159 ? 0.4453 0.2600 0.2766 0.0088  0.0499  0.0002  139 PHE A CG  
1115 C CD1 . PHE A 159 ? 0.4343 0.2643 0.2850 0.0079  0.0546  -0.0005 139 PHE A CD1 
1116 C CD2 . PHE A 159 ? 0.4580 0.2570 0.2684 0.0120  0.0387  -0.0006 139 PHE A CD2 
1117 C CE1 . PHE A 159 ? 0.4407 0.2700 0.2885 0.0100  0.0492  -0.0018 139 PHE A CE1 
1118 C CE2 . PHE A 159 ? 0.4586 0.2574 0.2675 0.0136  0.0329  -0.0020 139 PHE A CE2 
1119 C CZ  . PHE A 159 ? 0.4493 0.2628 0.2760 0.0125  0.0388  -0.0025 139 PHE A CZ  
1120 N N   . ALA A 160 ? 0.4456 0.2593 0.2972 0.0000  0.0895  0.0044  140 ALA A N   
1121 C CA  . ALA A 160 ? 0.4505 0.2678 0.3134 -0.0044 0.0969  0.0054  140 ALA A CA  
1122 C C   . ALA A 160 ? 0.4304 0.2626 0.3055 -0.0068 0.0841  0.0049  140 ALA A C   
1123 O O   . ALA A 160 ? 0.4466 0.2752 0.3214 -0.0096 0.0870  0.0058  140 ALA A O   
1124 C CB  . ALA A 160 ? 0.4467 0.2789 0.3383 -0.0077 0.1092  0.0051  140 ALA A CB  
1125 N N   . GLY A 161 ? 0.3961 0.2443 0.2821 -0.0060 0.0714  0.0034  141 GLY A N   
1126 C CA  . GLY A 161 ? 0.3728 0.2342 0.2699 -0.0076 0.0607  0.0029  141 GLY A CA  
1127 C C   . GLY A 161 ? 0.3606 0.2371 0.2684 -0.0064 0.0496  0.0016  141 GLY A C   
1128 O O   . GLY A 161 ? 0.3562 0.2362 0.2675 -0.0050 0.0502  0.0008  141 GLY A O   
1129 N N   . MET A 162 ? 0.3418 0.2260 0.2543 -0.0067 0.0405  0.0013  142 MET A N   
1130 C CA  A MET A 162 ? 0.3298 0.2268 0.2519 -0.0058 0.0313  0.0004  142 MET A CA  
1131 C CA  B MET A 162 ? 0.3322 0.2295 0.2546 -0.0058 0.0311  0.0004  142 MET A CA  
1132 C C   . MET A 162 ? 0.3119 0.2214 0.2483 -0.0079 0.0276  0.0001  142 MET A C   
1133 O O   . MET A 162 ? 0.3131 0.2181 0.2451 -0.0085 0.0274  0.0007  142 MET A O   
1134 C CB  A MET A 162 ? 0.3505 0.2382 0.2577 -0.0024 0.0232  0.0005  142 MET A CB  
1135 C CB  B MET A 162 ? 0.3569 0.2476 0.2672 -0.0027 0.0221  0.0005  142 MET A CB  
1136 C CG  A MET A 162 ? 0.3601 0.2587 0.2766 -0.0017 0.0144  -0.0002 142 MET A CG  
1137 C CG  B MET A 162 ? 0.3946 0.2724 0.2894 0.0000  0.0207  0.0003  142 MET A CG  
1138 S SD  A MET A 162 ? 0.3765 0.2628 0.2784 0.0020  0.0045  -0.0004 142 MET A SD  
1139 S SD  B MET A 162 ? 0.4322 0.3123 0.3273 0.0024  0.0068  -0.0005 142 MET A SD  
1140 C CE  A MET A 162 ? 0.3917 0.2708 0.2864 0.0032  0.0029  0.0005  142 MET A CE  
1141 C CE  B MET A 162 ? 0.4156 0.2929 0.3081 0.0035  0.0022  0.0002  142 MET A CE  
1142 N N   . VAL A 163 ? 0.2862 0.2085 0.2366 -0.0086 0.0247  -0.0008 143 VAL A N   
1143 C CA  . VAL A 163 ? 0.2836 0.2145 0.2437 -0.0099 0.0206  -0.0013 143 VAL A CA  
1144 C C   . VAL A 163 ? 0.2775 0.2127 0.2373 -0.0077 0.0142  -0.0013 143 VAL A C   
1145 O O   . VAL A 163 ? 0.2761 0.2144 0.2382 -0.0069 0.0130  -0.0016 143 VAL A O   
1146 C CB  . VAL A 163 ? 0.2926 0.2319 0.2678 -0.0120 0.0219  -0.0025 143 VAL A CB  
1147 C CG1 . VAL A 163 ? 0.2933 0.2379 0.2740 -0.0125 0.0158  -0.0032 143 VAL A CG1 
1148 C CG2 . VAL A 163 ? 0.3049 0.2412 0.2849 -0.0148 0.0293  -0.0025 143 VAL A CG2 
1149 N N   . LEU A 164 ? 0.2632 0.1976 0.2203 -0.0067 0.0108  -0.0007 144 LEU A N   
1150 C CA  . LEU A 164 ? 0.2619 0.2002 0.2212 -0.0049 0.0066  -0.0005 144 LEU A CA  
1151 C C   . LEU A 164 ? 0.2572 0.1995 0.2210 -0.0050 0.0059  -0.0005 144 LEU A C   
1152 O O   . LEU A 164 ? 0.2638 0.2030 0.2249 -0.0049 0.0063  -0.0004 144 LEU A O   
1153 C CB  . LEU A 164 ? 0.2751 0.2081 0.2285 -0.0027 0.0036  0.0001  144 LEU A CB  
1154 C CG  . LEU A 164 ? 0.3091 0.2333 0.2527 -0.0018 0.0029  0.0000  144 LEU A CG  
1155 C CD1 . LEU A 164 ? 0.3404 0.2572 0.2772 0.0010  -0.0023 0.0003  144 LEU A CD1 
1156 C CD2 . LEU A 164 ? 0.3121 0.2388 0.2582 -0.0019 0.0013  -0.0005 144 LEU A CD2 
1157 N N   . ILE A 165 ? 0.2473 0.1939 0.2154 -0.0048 0.0050  -0.0007 145 ILE A N   
1158 C CA  . ILE A 165 ? 0.2445 0.1911 0.2127 -0.0042 0.0047  -0.0007 145 ILE A CA  
1159 C C   . ILE A 165 ? 0.2508 0.1987 0.2209 -0.0025 0.0053  0.0004  145 ILE A C   
1160 O O   . ILE A 165 ? 0.2667 0.2172 0.2401 -0.0028 0.0050  0.0006  145 ILE A O   
1161 C CB  . ILE A 165 ? 0.2643 0.2117 0.2340 -0.0049 0.0034  -0.0016 145 ILE A CB  
1162 C CG1 . ILE A 165 ? 0.2780 0.2265 0.2517 -0.0068 0.0031  -0.0028 145 ILE A CG1 
1163 C CG2 . ILE A 165 ? 0.2746 0.2171 0.2390 -0.0036 0.0027  -0.0016 145 ILE A CG2 
1164 C CD1 . ILE A 165 ? 0.2845 0.2349 0.2629 -0.0068 0.0001  -0.0042 145 ILE A CD1 
1165 N N   . SER A 166 ? 0.2532 0.1992 0.2226 -0.0008 0.0066  0.0011  146 SER A N   
1166 C CA  A SER A 166 ? 0.2468 0.1952 0.2223 0.0009  0.0083  0.0021  146 SER A CA  
1167 C CA  B SER A 166 ? 0.2614 0.2098 0.2369 0.0009  0.0084  0.0021  146 SER A CA  
1168 C C   . SER A 166 ? 0.2601 0.2133 0.2434 0.0002  0.0057  0.0021  146 SER A C   
1169 O O   . SER A 166 ? 0.2635 0.2193 0.2525 -0.0004 0.0070  0.0026  146 SER A O   
1170 C CB  A SER A 166 ? 0.2368 0.1825 0.2103 0.0016  0.0125  0.0028  146 SER A CB  
1171 C CB  B SER A 166 ? 0.2977 0.2435 0.2711 0.0015  0.0124  0.0027  146 SER A CB  
1172 O OG  A SER A 166 ? 0.2136 0.1577 0.1829 0.0002  0.0114  0.0022  146 SER A OG  
1173 O OG  B SER A 166 ? 0.3617 0.3005 0.3248 0.0018  0.0124  0.0021  146 SER A OG  
1174 N N   . PRO A 167 ? 0.2566 0.2085 0.2381 0.0003  0.0017  0.0016  147 PRO A N   
1175 C CA  . PRO A 167 ? 0.2607 0.2140 0.2466 -0.0001 -0.0025 0.0012  147 PRO A CA  
1176 C C   . PRO A 167 ? 0.2718 0.2297 0.2708 0.0011  -0.0042 0.0016  147 PRO A C   
1177 O O   . PRO A 167 ? 0.2774 0.2368 0.2814 0.0032  -0.0026 0.0021  147 PRO A O   
1178 C CB  . PRO A 167 ? 0.2650 0.2114 0.2411 0.0007  -0.0060 0.0006  147 PRO A CB  
1179 C CG  . PRO A 167 ? 0.2728 0.2166 0.2453 0.0021  -0.0042 0.0010  147 PRO A CG  
1180 C CD  . PRO A 167 ? 0.2651 0.2117 0.2384 0.0009  0.0009  0.0013  147 PRO A CD  
1181 N N   . LEU A 168 ? 0.2742 0.2344 0.2802 -0.0003 -0.0074 0.0013  148 LEU A N   
1182 C CA  . LEU A 168 ? 0.2822 0.2480 0.3054 0.0000  -0.0098 0.0014  148 LEU A CA  
1183 C C   . LEU A 168 ? 0.2983 0.2610 0.3220 0.0024  -0.0187 0.0003  148 LEU A C   
1184 O O   . LEU A 168 ? 0.3051 0.2619 0.3221 0.0020  -0.0258 -0.0008 148 LEU A O   
1185 C CB  . LEU A 168 ? 0.2874 0.2555 0.3182 -0.0029 -0.0108 0.0012  148 LEU A CB  
1186 C CG  . LEU A 168 ? 0.3157 0.2901 0.3682 -0.0036 -0.0143 0.0010  148 LEU A CG  
1187 C CD1 . LEU A 168 ? 0.3238 0.3049 0.3912 -0.0022 -0.0065 0.0024  148 LEU A CD1 
1188 C CD2 . LEU A 168 ? 0.3332 0.3078 0.3912 -0.0073 -0.0154 0.0008  148 LEU A CD2 
1189 N N   . VAL A 169 ? 0.3011 0.2649 0.3291 0.0055  -0.0183 0.0006  149 VAL A N   
1190 C CA  . VAL A 169 ? 0.3223 0.2818 0.3503 0.0087  -0.0275 -0.0004 149 VAL A CA  
1191 C C   . VAL A 169 ? 0.3341 0.3030 0.3871 0.0104  -0.0295 -0.0006 149 VAL A C   
1192 O O   . VAL A 169 ? 0.3438 0.3132 0.4074 0.0111  -0.0397 -0.0019 149 VAL A O   
1193 C CB  . VAL A 169 ? 0.3400 0.2914 0.3517 0.0114  -0.0261 -0.0001 149 VAL A CB  
1194 C CG1 . VAL A 169 ? 0.3546 0.2993 0.3648 0.0155  -0.0362 -0.0011 149 VAL A CG1 
1195 C CG2 . VAL A 169 ? 0.3550 0.2983 0.3464 0.0091  -0.0229 0.0000  149 VAL A CG2 
1196 N N   . LEU A 170 ? 0.3390 0.3147 0.4022 0.0112  -0.0197 0.0008  150 LEU A N   
1197 C CA  . LEU A 170 ? 0.3503 0.3362 0.4407 0.0126  -0.0181 0.0010  150 LEU A CA  
1198 C C   . LEU A 170 ? 0.3627 0.3533 0.4594 0.0096  -0.0052 0.0027  150 LEU A C   
1199 O O   . LEU A 170 ? 0.3722 0.3576 0.4524 0.0095  0.0031  0.0038  150 LEU A O   
1200 C CB  . LEU A 170 ? 0.3558 0.3421 0.4507 0.0179  -0.0167 0.0012  150 LEU A CB  
1201 C CG  . LEU A 170 ? 0.3937 0.3737 0.4831 0.0219  -0.0295 -0.0003 150 LEU A CG  
1202 C CD1 . LEU A 170 ? 0.3980 0.3781 0.4916 0.0274  -0.0264 0.0001  150 LEU A CD1 
1203 C CD2 . LEU A 170 ? 0.4015 0.3858 0.5105 0.0221  -0.0422 -0.0021 150 LEU A CD2 
1204 N N   . ALA A 171 ? 0.3655 0.3640 0.4845 0.0072  -0.0042 0.0028  151 ALA A N   
1205 C CA  . ALA A 171 ? 0.3926 0.3931 0.5168 0.0046  0.0091  0.0047  151 ALA A CA  
1206 C C   . ALA A 171 ? 0.4120 0.4149 0.5461 0.0083  0.0207  0.0062  151 ALA A C   
1207 O O   . ALA A 171 ? 0.4116 0.4184 0.5570 0.0124  0.0170  0.0055  151 ALA A O   
1208 C CB  . ALA A 171 ? 0.3915 0.3990 0.5387 0.0005  0.0070  0.0044  151 ALA A CB  
1209 N N   . ASN A 172 ? 0.4358 0.4349 0.5655 0.0074  0.0350  0.0082  152 ASN A N   
1210 C CA  . ASN A 172 ? 0.4683 0.4674 0.6069 0.0112  0.0483  0.0098  152 ASN A CA  
1211 C C   . ASN A 172 ? 0.4752 0.4883 0.6526 0.0116  0.0481  0.0095  152 ASN A C   
1212 O O   . ASN A 172 ? 0.4636 0.4835 0.6592 0.0072  0.0445  0.0091  152 ASN A O   
1213 C CB  . ASN A 172 ? 0.5079 0.4975 0.6339 0.0097  0.0633  0.0120  152 ASN A CB  
1214 C CG  . ASN A 172 ? 0.5667 0.5531 0.6996 0.0137  0.0796  0.0140  152 ASN A CG  
1215 O OD1 . ASN A 172 ? 0.5685 0.5638 0.7310 0.0135  0.0873  0.0148  152 ASN A OD1 
1216 N ND2 . ASN A 172 ? 0.5942 0.5668 0.7003 0.0174  0.0854  0.0146  152 ASN A ND2 
1217 N N   . PRO A 173 ? 0.4919 0.5094 0.6827 0.0171  0.0490  0.0092  153 PRO A N   
1218 C CA  . PRO A 173 ? 0.4973 0.5295 0.7286 0.0181  0.0463  0.0084  153 PRO A CA  
1219 C C   . PRO A 173 ? 0.5202 0.5600 0.7797 0.0139  0.0580  0.0098  153 PRO A C   
1220 O O   . PRO A 173 ? 0.5082 0.5600 0.7993 0.0113  0.0497  0.0084  153 PRO A O   
1221 C CB  . PRO A 173 ? 0.4981 0.5306 0.7345 0.0255  0.0515  0.0086  153 PRO A CB  
1222 C CG  . PRO A 173 ? 0.5178 0.5366 0.7154 0.0278  0.0480  0.0084  153 PRO A CG  
1223 C CD  . PRO A 173 ? 0.5013 0.5102 0.6717 0.0226  0.0517  0.0094  153 PRO A CD  
1224 N N   . GLU A 174 ? 0.5499 0.5809 0.7974 0.0132  0.0768  0.0125  154 GLU A N   
1225 C CA  . GLU A 174 ? 0.5644 0.5996 0.8356 0.0090  0.0906  0.0144  154 GLU A CA  
1226 C C   . GLU A 174 ? 0.5756 0.6114 0.8459 0.0016  0.0821  0.0138  154 GLU A C   
1227 O O   . GLU A 174 ? 0.5688 0.6148 0.8718 -0.0029 0.0828  0.0137  154 GLU A O   
1228 C CB  . GLU A 174 ? 0.6233 0.6436 0.8745 0.0108  0.1131  0.0176  154 GLU A CB  
1229 C CG  . GLU A 174 ? 0.7150 0.7353 0.9753 0.0181  0.1252  0.0185  154 GLU A CG  
1230 C CD  . GLU A 174 ? 0.8571 0.8588 1.0758 0.0234  0.1303  0.0192  154 GLU A CD  
1231 O OE1 . GLU A 174 ? 0.8831 0.8803 1.1040 0.0294  0.1437  0.0204  154 GLU A OE1 
1232 O OE2 . GLU A 174 ? 0.9109 0.9023 1.0958 0.0216  0.1209  0.0185  154 GLU A OE2 
1233 N N   . SER A 175 ? 0.5871 0.6120 0.8217 0.0003  0.0740  0.0132  155 SER A N   
1234 C CA  A SER A 175 ? 0.5943 0.6177 0.8237 -0.0059 0.0658  0.0125  155 SER A CA  
1235 C CA  B SER A 175 ? 0.5954 0.6186 0.8238 -0.0058 0.0655  0.0125  155 SER A CA  
1236 C C   . SER A 175 ? 0.5857 0.6200 0.8354 -0.0076 0.0462  0.0095  155 SER A C   
1237 O O   . SER A 175 ? 0.5847 0.6215 0.8461 -0.0131 0.0411  0.0089  155 SER A O   
1238 C CB  A SER A 175 ? 0.6294 0.6386 0.8172 -0.0058 0.0630  0.0126  155 SER A CB  
1239 C CB  B SER A 175 ? 0.6322 0.6415 0.8188 -0.0054 0.0617  0.0124  155 SER A CB  
1240 O OG  A SER A 175 ? 0.6665 0.6630 0.8336 -0.0040 0.0790  0.0151  155 SER A OG  
1241 O OG  B SER A 175 ? 0.6638 0.6712 0.8432 -0.0102 0.0524  0.0114  155 SER A OG  
1242 N N   . ALA A 176 ? 0.5765 0.6148 0.8282 -0.0029 0.0347  0.0076  156 ALA A N   
1243 C CA  . ALA A 176 ? 0.5720 0.6170 0.8396 -0.0034 0.0150  0.0045  156 ALA A CA  
1244 C C   . ALA A 176 ? 0.5566 0.6161 0.8713 -0.0057 0.0151  0.0040  156 ALA A C   
1245 O O   . ALA A 176 ? 0.5502 0.6133 0.8801 -0.0097 0.0019  0.0020  156 ALA A O   
1246 C CB  . ALA A 176 ? 0.5755 0.6188 0.8330 0.0031  0.0046  0.0030  156 ALA A CB  
1247 N N   . THR A 177 ? 0.5472 0.6140 0.8850 -0.0032 0.0307  0.0058  157 THR A N   
1248 C CA  . THR A 177 ? 0.5350 0.6169 0.9222 -0.0055 0.0340  0.0056  157 THR A CA  
1249 C C   . THR A 177 ? 0.5441 0.6254 0.9408 -0.0138 0.0419  0.0069  157 THR A C   
1250 O O   . THR A 177 ? 0.5349 0.6255 0.9633 -0.0185 0.0319  0.0050  157 THR A O   
1251 C CB  . THR A 177 ? 0.5422 0.6298 0.9480 -0.0002 0.0521  0.0075  157 THR A CB  
1252 O OG1 . THR A 177 ? 0.5551 0.6411 0.9483 0.0076  0.0439  0.0062  157 THR A OG1 
1253 C CG2 . THR A 177 ? 0.5256 0.6309 0.9881 -0.0020 0.0566  0.0072  157 THR A CG2 
1254 N N   . THR A 178 ? 0.5620 0.6306 0.9294 -0.0156 0.0583  0.0099  158 THR A N   
1255 C CA  . THR A 178 ? 0.5739 0.6377 0.9424 -0.0229 0.0677  0.0116  158 THR A CA  
1256 C C   . THR A 178 ? 0.5753 0.6383 0.9412 -0.0283 0.0485  0.0090  158 THR A C   
1257 O O   . THR A 178 ? 0.5623 0.6308 0.9561 -0.0348 0.0478  0.0087  158 THR A O   
1258 C CB  . THR A 178 ? 0.6168 0.6628 0.9441 -0.0218 0.0843  0.0147  158 THR A CB  
1259 O OG1 . THR A 178 ? 0.6330 0.6776 0.9657 -0.0174 0.1041  0.0173  158 THR A OG1 
1260 C CG2 . THR A 178 ? 0.6275 0.6642 0.9463 -0.0287 0.0915  0.0164  158 THR A CG2 
1261 N N   . PHE A 179 ? 0.5861 0.6412 0.9190 -0.0258 0.0332  0.0071  159 PHE A N   
1262 C CA  . PHE A 179 ? 0.5943 0.6453 0.9193 -0.0298 0.0156  0.0047  159 PHE A CA  
1263 C C   . PHE A 179 ? 0.5751 0.6360 0.9305 -0.0302 -0.0044 0.0011  159 PHE A C   
1264 O O   . PHE A 179 ? 0.5699 0.6288 0.9316 -0.0353 -0.0161 -0.0008 159 PHE A O   
1265 C CB  . PHE A 179 ? 0.6182 0.6558 0.8975 -0.0271 0.0087  0.0042  159 PHE A CB  
1266 C CG  . PHE A 179 ? 0.6475 0.6737 0.9003 -0.0294 0.0221  0.0067  159 PHE A CG  
1267 C CD1 . PHE A 179 ? 0.6690 0.6887 0.8994 -0.0256 0.0358  0.0090  159 PHE A CD1 
1268 C CD2 . PHE A 179 ? 0.6639 0.6847 0.9145 -0.0353 0.0207  0.0067  159 PHE A CD2 
1269 C CE1 . PHE A 179 ? 0.6917 0.6989 0.8965 -0.0271 0.0461  0.0111  159 PHE A CE1 
1270 C CE2 . PHE A 179 ? 0.6861 0.6949 0.9113 -0.0367 0.0321  0.0090  159 PHE A CE2 
1271 C CZ  . PHE A 179 ? 0.6930 0.6951 0.8953 -0.0324 0.0440  0.0111  159 PHE A CZ  
1272 N N   . LYS A 180 ? 0.5609 0.6309 0.9347 -0.0247 -0.0093 -0.0001 160 LYS A N   
1273 C CA  . LYS A 180 ? 0.5536 0.6321 0.9583 -0.0243 -0.0298 -0.0037 160 LYS A CA  
1274 C C   . LYS A 180 ? 0.5328 0.6247 0.9871 -0.0307 -0.0258 -0.0038 160 LYS A C   
1275 O O   . LYS A 180 ? 0.5234 0.6179 0.9981 -0.0344 -0.0438 -0.0069 160 LYS A O   
1276 C CB  . LYS A 180 ? 0.5737 0.6579 0.9859 -0.0161 -0.0357 -0.0049 160 LYS A CB  
1277 C CG  . LYS A 180 ? 0.6462 0.7164 1.0154 -0.0108 -0.0484 -0.0062 160 LYS A CG  
1278 C CD  . LYS A 180 ? 0.7073 0.7811 1.0807 -0.0026 -0.0510 -0.0067 160 LYS A CD  
1279 C CE  . LYS A 180 ? 0.7793 0.8380 1.1062 0.0021  -0.0544 -0.0065 160 LYS A CE  
1280 N NZ  . LYS A 180 ? 0.8056 0.8666 1.1348 0.0098  -0.0535 -0.0064 160 LYS A NZ  
1281 N N   . VAL A 181 ? 0.5237 0.6222 0.9959 -0.0322 -0.0018 -0.0004 161 VAL A N   
1282 C CA  . VAL A 181 ? 0.5116 0.6221 1.0312 -0.0388 0.0071  0.0003  161 VAL A CA  
1283 C C   . VAL A 181 ? 0.5203 0.6216 1.0295 -0.0475 0.0069  0.0006  161 VAL A C   
1284 O O   . VAL A 181 ? 0.5042 0.6122 1.0469 -0.0538 -0.0033 -0.0015 161 VAL A O   
1285 C CB  . VAL A 181 ? 0.5180 0.6341 1.0534 -0.0369 0.0357  0.0042  161 VAL A CB  
1286 C CG1 . VAL A 181 ? 0.5133 0.6364 1.0872 -0.0450 0.0515  0.0061  161 VAL A CG1 
1287 C CG2 . VAL A 181 ? 0.5119 0.6406 1.0719 -0.0289 0.0340  0.0032  161 VAL A CG2 
1288 N N   . LEU A 182 ? 0.5416 0.6270 1.0047 -0.0477 0.0167  0.0031  162 LEU A N   
1289 C CA  . LEU A 182 ? 0.5588 0.6335 1.0079 -0.0550 0.0171  0.0036  162 LEU A CA  
1290 C C   . LEU A 182 ? 0.5707 0.6410 1.0136 -0.0570 -0.0095 -0.0006 162 LEU A C   
1291 O O   . LEU A 182 ? 0.5672 0.6369 1.0278 -0.0644 -0.0150 -0.0017 162 LEU A O   
1292 C CB  . LEU A 182 ? 0.5848 0.6429 0.9858 -0.0535 0.0315  0.0067  162 LEU A CB  
1293 C CG  . LEU A 182 ? 0.6066 0.6623 1.0097 -0.0536 0.0592  0.0111  162 LEU A CG  
1294 C CD1 . LEU A 182 ? 0.6407 0.6782 0.9929 -0.0506 0.0687  0.0135  162 LEU A CD1 
1295 C CD2 . LEU A 182 ? 0.6029 0.6611 1.0380 -0.0620 0.0709  0.0127  162 LEU A CD2 
1296 N N   . ALA A 183 ? 0.5832 0.6492 1.0019 -0.0506 -0.0259 -0.0030 163 ALA A N   
1297 C CA  . ALA A 183 ? 0.6024 0.6604 1.0098 -0.0510 -0.0512 -0.0070 163 ALA A CA  
1298 C C   . ALA A 183 ? 0.5921 0.6610 1.0465 -0.0546 -0.0673 -0.0104 163 ALA A C   
1299 O O   . ALA A 183 ? 0.5942 0.6555 1.0482 -0.0588 -0.0839 -0.0132 163 ALA A O   
1300 C CB  . ALA A 183 ? 0.6191 0.6699 0.9944 -0.0428 -0.0627 -0.0085 163 ALA A CB  
1301 N N   . ALA A 184 ? 0.5773 0.6632 1.0723 -0.0525 -0.0632 -0.0103 164 ALA A N   
1302 C CA  . ALA A 184 ? 0.5665 0.6655 1.1133 -0.0556 -0.0782 -0.0136 164 ALA A CA  
1303 C C   . ALA A 184 ? 0.5646 0.6694 1.1456 -0.0660 -0.0687 -0.0126 164 ALA A C   
1304 O O   . ALA A 184 ? 0.5558 0.6649 1.1693 -0.0710 -0.0862 -0.0161 164 ALA A O   
1305 C CB  . ALA A 184 ? 0.5497 0.6657 1.1308 -0.0495 -0.0747 -0.0136 164 ALA A CB  
1306 N N   . LYS A 185 ? 0.5736 0.6760 1.1449 -0.0695 -0.0418 -0.0080 165 LYS A N   
1307 C CA  . LYS A 185 ? 0.5744 0.6788 1.1725 -0.0796 -0.0304 -0.0065 165 LYS A CA  
1308 C C   . LYS A 185 ? 0.5994 0.6865 1.1688 -0.0851 -0.0439 -0.0082 165 LYS A C   
1309 O O   . LYS A 185 ? 0.5882 0.6773 1.1874 -0.0932 -0.0516 -0.0099 165 LYS A O   
1310 C CB  . LYS A 185 ? 0.5996 0.7023 1.1904 -0.0807 0.0030  -0.0008 165 LYS A CB  
1311 C CG  . LYS A 185 ? 0.6382 0.7531 1.2464 -0.0741 0.0198  0.0014  165 LYS A CG  
1312 C CD  . LYS A 185 ? 0.6604 0.7975 1.3344 -0.0754 0.0159  -0.0006 165 LYS A CD  
1313 C CE  . LYS A 185 ? 0.6924 0.8406 1.3806 -0.0672 0.0296  0.0011  165 LYS A CE  
1314 N NZ  . LYS A 185 ? 0.7104 0.8571 1.4031 -0.0686 0.0642  0.0064  165 LYS A NZ  
1315 N N   . VAL A 186 ? 0.6299 0.6999 1.1428 -0.0806 -0.0462 -0.0076 166 VAL A N   
1316 C CA  . VAL A 186 ? 0.6571 0.7095 1.1401 -0.0845 -0.0582 -0.0093 166 VAL A CA  
1317 C C   . VAL A 186 ? 0.6639 0.7115 1.1474 -0.0831 -0.0894 -0.0147 166 VAL A C   
1318 O O   . VAL A 186 ? 0.6719 0.7088 1.1521 -0.0886 -0.1022 -0.0170 166 VAL A O   
1319 C CB  . VAL A 186 ? 0.6967 0.7326 1.1232 -0.0807 -0.0478 -0.0067 166 VAL A CB  
1320 C CG1 . VAL A 186 ? 0.7067 0.7441 1.1306 -0.0815 -0.0190 -0.0016 166 VAL A CG1 
1321 C CG2 . VAL A 186 ? 0.7147 0.7465 1.1086 -0.0713 -0.0577 -0.0080 166 VAL A CG2 
1322 N N   . LEU A 187 ? 0.6577 0.7112 1.1446 -0.0756 -0.1019 -0.0169 167 LEU A N   
1323 C CA  . LEU A 187 ? 0.6582 0.7049 1.1454 -0.0733 -0.1323 -0.0222 167 LEU A CA  
1324 C C   . LEU A 187 ? 0.6148 0.6720 1.1567 -0.0807 -0.1455 -0.0253 167 LEU A C   
1325 O O   . LEU A 187 ? 0.6298 0.6755 1.1692 -0.0825 -0.1702 -0.0296 167 LEU A O   
1326 C CB  . LEU A 187 ? 0.6738 0.7247 1.1557 -0.0634 -0.1405 -0.0233 167 LEU A CB  
1327 C CG  . LEU A 187 ? 0.7115 0.7520 1.1882 -0.0591 -0.1721 -0.0287 167 LEU A CG  
1328 C CD1 . LEU A 187 ? 0.7504 0.7641 1.1709 -0.0573 -0.1831 -0.0301 167 LEU A CD1 
1329 C CD2 . LEU A 187 ? 0.7191 0.7664 1.1998 -0.0499 -0.1773 -0.0293 167 LEU A CD2 
1330 N N   . ASN A 188 ? 0.5621 0.6399 1.1535 -0.0851 -0.1287 -0.0230 168 ASN A N   
1331 C CA  . ASN A 188 ? 0.5097 0.6011 1.1611 -0.0928 -0.1378 -0.0256 168 ASN A CA  
1332 C C   . ASN A 188 ? 0.4735 0.5612 1.1371 -0.1042 -0.1269 -0.0240 168 ASN A C   
1333 O O   . ASN A 188 ? 0.4668 0.5597 1.1719 -0.1118 -0.1405 -0.0271 168 ASN A O   
1334 C CB  . ASN A 188 ? 0.5016 0.6181 1.2046 -0.0906 -0.1253 -0.0242 168 ASN A CB  
1335 C CG  . ASN A 188 ? 0.5418 0.6641 1.2556 -0.0818 -0.1477 -0.0281 168 ASN A CG  
1336 O OD1 . ASN A 188 ? 0.5439 0.6760 1.3035 -0.0836 -0.1683 -0.0324 168 ASN A OD1 
1337 N ND2 . ASN A 188 ? 0.5651 0.6802 1.2369 -0.0720 -0.1452 -0.0269 168 ASN A ND2 
1338 N N   . SER A 189 ? 0.4511 0.5297 1.0808 -0.1057 -0.1029 -0.0193 169 SER A N   
1339 C CA  . SER A 189 ? 0.4178 0.4902 1.0544 -0.1161 -0.0905 -0.0173 169 SER A CA  
1340 C C   . SER A 189 ? 0.4237 0.4718 0.9975 -0.1154 -0.0867 -0.0157 169 SER A C   
1341 O O   . SER A 189 ? 0.4400 0.4778 0.9692 -0.1071 -0.0942 -0.0164 169 SER A O   
1342 C CB  . SER A 189 ? 0.3956 0.4831 1.0685 -0.1203 -0.0595 -0.0125 169 SER A CB  
1343 O OG  . SER A 189 ? 0.3535 0.4619 1.0944 -0.1252 -0.0633 -0.0143 169 SER A OG  
1344 N N   . VAL A 190 ? 0.4094 0.4479 0.9809 -0.1239 -0.0763 -0.0138 170 VAL A N   
1345 C CA  . VAL A 190 ? 0.4248 0.4408 0.9403 -0.1228 -0.0727 -0.0124 170 VAL A CA  
1346 C C   . VAL A 190 ? 0.4143 0.4286 0.9158 -0.1231 -0.0413 -0.0064 170 VAL A C   
1347 O O   . VAL A 190 ? 0.4007 0.4151 0.9249 -0.1314 -0.0262 -0.0040 170 VAL A O   
1348 C CB  . VAL A 190 ? 0.4406 0.4415 0.9545 -0.1310 -0.0871 -0.0151 170 VAL A CB  
1349 C CG1 . VAL A 190 ? 0.4770 0.4544 0.9321 -0.1285 -0.0837 -0.0138 170 VAL A CG1 
1350 C CG2 . VAL A 190 ? 0.4434 0.4437 0.9730 -0.1310 -0.1196 -0.0213 170 VAL A CG2 
1351 N N   . LEU A 191 ? 0.4163 0.4284 0.8825 -0.1141 -0.0312 -0.0041 171 LEU A N   
1352 C CA  . LEU A 191 ? 0.4240 0.4313 0.8715 -0.1130 -0.0033 0.0012  171 LEU A CA  
1353 C C   . LEU A 191 ? 0.4666 0.4579 0.8552 -0.1054 -0.0040 0.0020  171 LEU A C   
1354 O O   . LEU A 191 ? 0.4681 0.4633 0.8391 -0.0973 -0.0013 0.0026  171 LEU A O   
1355 C CB  . LEU A 191 ? 0.4001 0.4244 0.8744 -0.1095 0.0129  0.0037  171 LEU A CB  
1356 C CG  . LEU A 191 ? 0.3859 0.4276 0.9233 -0.1169 0.0182  0.0036  171 LEU A CG  
1357 C CD1 . LEU A 191 ? 0.3797 0.4396 0.9437 -0.1110 0.0273  0.0045  171 LEU A CD1 
1358 C CD2 . LEU A 191 ? 0.3883 0.4223 0.9364 -0.1257 0.0404  0.0074  171 LEU A CD2 
1359 N N   . PRO A 192 ? 0.4955 0.4688 0.8550 -0.1079 -0.0077 0.0017  172 PRO A N   
1360 C CA  . PRO A 192 ? 0.5274 0.4865 0.8348 -0.1006 -0.0101 0.0018  172 PRO A CA  
1361 C C   . PRO A 192 ? 0.5516 0.5058 0.8322 -0.0955 0.0108  0.0061  172 PRO A C   
1362 O O   . PRO A 192 ? 0.5720 0.5208 0.8182 -0.0880 0.0078  0.0058  172 PRO A O   
1363 C CB  . PRO A 192 ? 0.5465 0.4880 0.8363 -0.1052 -0.0185 0.0005  172 PRO A CB  
1364 C CG  . PRO A 192 ? 0.5358 0.4794 0.8621 -0.1156 -0.0110 0.0016  172 PRO A CG  
1365 C CD  . PRO A 192 ? 0.4889 0.4542 0.8635 -0.1175 -0.0122 0.0008  172 PRO A CD  
1366 N N   . ASN A 193 ? 0.5500 0.5042 0.8451 -0.0995 0.0317  0.0099  173 ASN A N   
1367 C CA  . ASN A 193 ? 0.5731 0.5182 0.8393 -0.0946 0.0507  0.0139  173 ASN A CA  
1368 C C   . ASN A 193 ? 0.5554 0.5130 0.8330 -0.0895 0.0614  0.0154  173 ASN A C   
1369 O O   . ASN A 193 ? 0.5739 0.5226 0.8265 -0.0849 0.0761  0.0184  173 ASN A O   
1370 C CB  . ASN A 193 ? 0.6077 0.5379 0.8705 -0.1005 0.0688  0.0175  173 ASN A CB  
1371 C CG  . ASN A 193 ? 0.6844 0.5989 0.9284 -0.1043 0.0593  0.0163  173 ASN A CG  
1372 O OD1 . ASN A 193 ? 0.7223 0.6284 0.9326 -0.0989 0.0476  0.0145  173 ASN A OD1 
1373 N ND2 . ASN A 193 ? 0.6874 0.5974 0.9536 -0.1136 0.0645  0.0172  173 ASN A ND2 
1374 N N   . LEU A 194 ? 0.5185 0.4949 0.8323 -0.0898 0.0534  0.0133  174 LEU A N   
1375 C CA  . LEU A 194 ? 0.5024 0.4907 0.8296 -0.0848 0.0634  0.0146  174 LEU A CA  
1376 C C   . LEU A 194 ? 0.5033 0.4866 0.7915 -0.0756 0.0614  0.0147  174 LEU A C   
1377 O O   . LEU A 194 ? 0.5012 0.4831 0.7698 -0.0722 0.0441  0.0118  174 LEU A O   
1378 C CB  . LEU A 194 ? 0.4880 0.4970 0.8609 -0.0861 0.0515  0.0117  174 LEU A CB  
1379 C CG  . LEU A 194 ? 0.5061 0.5285 0.9042 -0.0825 0.0655  0.0135  174 LEU A CG  
1380 C CD1 . LEU A 194 ? 0.5158 0.5350 0.9313 -0.0872 0.0920  0.0178  174 LEU A CD1 
1381 C CD2 . LEU A 194 ? 0.4897 0.5320 0.9311 -0.0825 0.0499  0.0100  174 LEU A CD2 
1382 N N   . SER A 195 ? 0.5039 0.4827 0.7800 -0.0716 0.0799  0.0179  175 SER A N   
1383 C CA  . SER A 195 ? 0.5188 0.4921 0.7594 -0.0634 0.0792  0.0181  175 SER A CA  
1384 C C   . SER A 195 ? 0.5092 0.4868 0.7571 -0.0590 0.0945  0.0203  175 SER A C   
1385 O O   . SER A 195 ? 0.5050 0.4834 0.7749 -0.0619 0.1117  0.0229  175 SER A O   
1386 C CB  . SER A 195 ? 0.5625 0.5150 0.7615 -0.0620 0.0851  0.0199  175 SER A CB  
1387 O OG  . SER A 195 ? 0.6131 0.5592 0.8021 -0.0654 0.0730  0.0182  175 SER A OG  
1388 N N   . SER A 196 ? 0.5085 0.4874 0.7369 -0.0518 0.0894  0.0194  176 SER A N   
1389 C CA  . SER A 196 ? 0.5064 0.4854 0.7337 -0.0467 0.1035  0.0214  176 SER A CA  
1390 C C   . SER A 196 ? 0.5110 0.4677 0.6975 -0.0439 0.1170  0.0242  176 SER A C   
1391 O O   . SER A 196 ? 0.5135 0.4572 0.6790 -0.0463 0.1154  0.0247  176 SER A O   
1392 C CB  . SER A 196 ? 0.5332 0.5220 0.7571 -0.0406 0.0906  0.0189  176 SER A CB  
1393 O OG  . SER A 196 ? 0.6027 0.5808 0.7876 -0.0370 0.0825  0.0180  176 SER A OG  
1394 N N   . GLY A 197 ? 0.5075 0.4580 0.6820 -0.0385 0.1294  0.0260  177 GLY A N   
1395 C CA  . GLY A 197 ? 0.5292 0.4563 0.6625 -0.0348 0.1396  0.0283  177 GLY A CA  
1396 C C   . GLY A 197 ? 0.5363 0.4591 0.6380 -0.0305 0.1235  0.0259  177 GLY A C   
1397 O O   . GLY A 197 ? 0.5241 0.4616 0.6348 -0.0295 0.1080  0.0230  177 GLY A O   
1398 N N   A PRO A 198 ? 0.5570 0.4587 0.6214 -0.0278 0.1268  0.0271  178 PRO A N   
1399 N N   B PRO A 198 ? 0.5570 0.4587 0.6214 -0.0278 0.1268  0.0271  178 PRO A N   
1400 C CA  A PRO A 198 ? 0.5711 0.4697 0.6091 -0.0238 0.1118  0.0247  178 PRO A CA  
1401 C CA  B PRO A 198 ? 0.5711 0.4697 0.6091 -0.0238 0.1118  0.0247  178 PRO A CA  
1402 C C   A PRO A 198 ? 0.5805 0.4825 0.6115 -0.0182 0.1092  0.0237  178 PRO A C   
1403 C C   B PRO A 198 ? 0.5805 0.4825 0.6115 -0.0182 0.1092  0.0237  178 PRO A C   
1404 O O   A PRO A 198 ? 0.5843 0.4855 0.6222 -0.0161 0.1211  0.0252  178 PRO A O   
1405 O O   B PRO A 198 ? 0.5843 0.4855 0.6222 -0.0161 0.1211  0.0252  178 PRO A O   
1406 C CB  A PRO A 198 ? 0.6003 0.4739 0.6034 -0.0222 0.1170  0.0264  178 PRO A CB  
1407 C CB  B PRO A 198 ? 0.6003 0.4739 0.6034 -0.0222 0.1170  0.0264  178 PRO A CB  
1408 C CG  A PRO A 198 ? 0.6108 0.4703 0.6128 -0.0226 0.1379  0.0299  178 PRO A CG  
1409 C CG  B PRO A 198 ? 0.6108 0.4703 0.6128 -0.0226 0.1379  0.0299  178 PRO A CG  
1410 C CD  A PRO A 198 ? 0.5676 0.4460 0.6121 -0.0280 0.1440  0.0305  178 PRO A CD  
1411 C CD  B PRO A 198 ? 0.5676 0.4460 0.6121 -0.0280 0.1440  0.0305  178 PRO A CD  
1412 N N   . ILE A 199 ? 0.5846 0.4898 0.6021 -0.0158 0.0944  0.0211  179 ILE A N   
1413 C CA  . ILE A 199 ? 0.5948 0.5019 0.6040 -0.0109 0.0908  0.0200  179 ILE A CA  
1414 C C   . ILE A 199 ? 0.6091 0.4937 0.5880 -0.0066 0.1003  0.0216  179 ILE A C   
1415 O O   . ILE A 199 ? 0.6347 0.5033 0.5903 -0.0060 0.0994  0.0220  179 ILE A O   
1416 C CB  . ILE A 199 ? 0.6086 0.5232 0.6113 -0.0103 0.0738  0.0170  179 ILE A CB  
1417 C CG1 . ILE A 199 ? 0.6097 0.5432 0.6388 -0.0134 0.0647  0.0153  179 ILE A CG1 
1418 C CG2 . ILE A 199 ? 0.6214 0.5323 0.6082 -0.0056 0.0701  0.0159  179 ILE A CG2 
1419 C CD1 . ILE A 199 ? 0.6289 0.5656 0.6520 -0.0144 0.0515  0.0131  179 ILE A CD1 
1420 N N   . ASP A 200 ? 0.5877 0.4687 0.5663 -0.0032 0.1100  0.0227  180 ASP A N   
1421 C CA  . ASP A 200 ? 0.5835 0.4399 0.5309 0.0016  0.1194  0.0242  180 ASP A CA  
1422 C C   . ASP A 200 ? 0.5577 0.4071 0.4799 0.0048  0.1047  0.0216  180 ASP A C   
1423 O O   . ASP A 200 ? 0.5563 0.4165 0.4842 0.0061  0.0965  0.0197  180 ASP A O   
1424 C CB  . ASP A 200 ? 0.6117 0.4689 0.5681 0.0047  0.1317  0.0254  180 ASP A CB  
1425 C CG  . ASP A 200 ? 0.7067 0.5363 0.6298 0.0104  0.1429  0.0269  180 ASP A CG  
1426 O OD1 . ASP A 200 ? 0.7448 0.5520 0.6359 0.0119  0.1414  0.0272  180 ASP A OD1 
1427 O OD2 . ASP A 200 ? 0.7341 0.5627 0.6617 0.0138  0.1525  0.0277  180 ASP A OD2 
1428 N N   . SER A 201 ? 0.5281 0.3594 0.4240 0.0059  0.1011  0.0216  181 SER A N   
1429 C CA  A SER A 201 ? 0.5135 0.3393 0.3899 0.0086  0.0861  0.0189  181 SER A CA  
1430 C CA  B SER A 201 ? 0.5251 0.3503 0.4009 0.0086  0.0862  0.0190  181 SER A CA  
1431 C C   . SER A 201 ? 0.5108 0.3255 0.3697 0.0133  0.0854  0.0181  181 SER A C   
1432 O O   . SER A 201 ? 0.4904 0.3100 0.3463 0.0142  0.0722  0.0154  181 SER A O   
1433 C CB  A SER A 201 ? 0.5233 0.3295 0.3751 0.0097  0.0827  0.0191  181 SER A CB  
1434 C CB  B SER A 201 ? 0.5678 0.3723 0.4178 0.0100  0.0834  0.0192  181 SER A CB  
1435 O OG  A SER A 201 ? 0.5360 0.3146 0.3616 0.0130  0.0954  0.0216  181 SER A OG  
1436 O OG  B SER A 201 ? 0.6098 0.4216 0.4733 0.0058  0.0847  0.0201  181 SER A OG  
1437 N N   . SER A 202 ? 0.5106 0.3096 0.3583 0.0162  0.1001  0.0203  182 SER A N   
1438 C CA  . SER A 202 ? 0.5246 0.3098 0.3527 0.0211  0.0998  0.0195  182 SER A CA  
1439 C C   . SER A 202 ? 0.4944 0.3009 0.3433 0.0205  0.0932  0.0176  182 SER A C   
1440 O O   . SER A 202 ? 0.5115 0.3094 0.3448 0.0236  0.0867  0.0159  182 SER A O   
1441 C CB  . SER A 202 ? 0.5808 0.3430 0.3914 0.0249  0.1188  0.0224  182 SER A CB  
1442 O OG  . SER A 202 ? 0.6276 0.4067 0.4683 0.0231  0.1323  0.0243  182 SER A OG  
1443 N N   . VAL A 203 ? 0.4506 0.2833 0.3334 0.0166  0.0937  0.0178  183 VAL A N   
1444 C CA  . VAL A 203 ? 0.4253 0.2761 0.3259 0.0164  0.0869  0.0161  183 VAL A CA  
1445 C C   . VAL A 203 ? 0.3939 0.2572 0.2990 0.0139  0.0701  0.0133  183 VAL A C   
1446 O O   . VAL A 203 ? 0.3892 0.2655 0.3065 0.0135  0.0641  0.0120  183 VAL A O   
1447 C CB  . VAL A 203 ? 0.4261 0.2962 0.3592 0.0148  0.0944  0.0173  183 VAL A CB  
1448 C CG1 . VAL A 203 ? 0.4464 0.3052 0.3790 0.0171  0.1133  0.0201  183 VAL A CG1 
1449 C CG2 . VAL A 203 ? 0.4218 0.3098 0.3779 0.0096  0.0887  0.0169  183 VAL A CG2 
1450 N N   . LEU A 204 ? 0.3736 0.2320 0.2689 0.0125  0.0631  0.0126  184 LEU A N   
1451 C CA  . LEU A 204 ? 0.3614 0.2314 0.2627 0.0104  0.0491  0.0101  184 LEU A CA  
1452 C C   . LEU A 204 ? 0.3651 0.2288 0.2536 0.0124  0.0406  0.0079  184 LEU A C   
1453 O O   . LEU A 204 ? 0.3496 0.2266 0.2497 0.0106  0.0327  0.0062  184 LEU A O   
1454 C CB  . LEU A 204 ? 0.3587 0.2248 0.2542 0.0092  0.0445  0.0098  184 LEU A CB  
1455 C CG  . LEU A 204 ? 0.3788 0.2536 0.2901 0.0059  0.0503  0.0114  184 LEU A CG  
1456 C CD1 . LEU A 204 ? 0.4061 0.2727 0.3069 0.0055  0.0464  0.0113  184 LEU A CD1 
1457 C CD2 . LEU A 204 ? 0.3742 0.2711 0.3104 0.0028  0.0452  0.0104  184 LEU A CD2 
1458 N N   . SER A 205 ? 0.3753 0.2170 0.2387 0.0160  0.0417  0.0079  185 SER A N   
1459 C CA  . SER A 205 ? 0.3843 0.2177 0.2347 0.0175  0.0316  0.0055  185 SER A CA  
1460 C C   . SER A 205 ? 0.4148 0.2209 0.2359 0.0222  0.0357  0.0059  185 SER A C   
1461 O O   . SER A 205 ? 0.4345 0.2239 0.2394 0.0244  0.0432  0.0077  185 SER A O   
1462 C CB  . SER A 205 ? 0.3863 0.2208 0.2356 0.0164  0.0190  0.0033  185 SER A CB  
1463 O OG  . SER A 205 ? 0.4097 0.2346 0.2477 0.0178  0.0081  0.0007  185 SER A OG  
1464 N N   . ARG A 206 ? 0.4216 0.2205 0.2336 0.0238  0.0309  0.0043  186 ARG A N   
1465 C CA  . ARG A 206 ? 0.4462 0.2150 0.2256 0.0288  0.0324  0.0041  186 ARG A CA  
1466 C C   . ARG A 206 ? 0.4792 0.2295 0.2373 0.0305  0.0197  0.0020  186 ARG A C   
1467 O O   . ARG A 206 ? 0.5132 0.2334 0.2389 0.0352  0.0205  0.0021  186 ARG A O   
1468 C CB  . ARG A 206 ? 0.4486 0.2142 0.2242 0.0299  0.0293  0.0026  186 ARG A CB  
1469 C CG  . ARG A 206 ? 0.4667 0.2430 0.2563 0.0304  0.0426  0.0047  186 ARG A CG  
1470 C CD  . ARG A 206 ? 0.4614 0.2358 0.2485 0.0312  0.0383  0.0031  186 ARG A CD  
1471 N NE  . ARG A 206 ? 0.4526 0.2441 0.2566 0.0264  0.0247  0.0006  186 ARG A NE  
1472 C CZ  . ARG A 206 ? 0.4461 0.2364 0.2490 0.0256  0.0176  -0.0013 186 ARG A CZ  
1473 N NH1 . ARG A 206 ? 0.4642 0.2369 0.2490 0.0295  0.0218  -0.0013 186 ARG A NH1 
1474 N NH2 . ARG A 206 ? 0.4303 0.2357 0.2498 0.0209  0.0072  -0.0032 186 ARG A NH2 
1475 N N   . ASN A 207 ? 0.4623 0.2289 0.2375 0.0272  0.0079  0.0002  187 ASN A N   
1476 C CA  . ASN A 207 ? 0.4662 0.2198 0.2280 0.0288  -0.0055 -0.0021 187 ASN A CA  
1477 C C   . ASN A 207 ? 0.4801 0.2226 0.2297 0.0306  0.0018  0.0003  187 ASN A C   
1478 O O   . ASN A 207 ? 0.4711 0.2318 0.2405 0.0277  0.0050  0.0014  187 ASN A O   
1479 C CB  . ASN A 207 ? 0.4668 0.2436 0.2552 0.0248  -0.0181 -0.0047 187 ASN A CB  
1480 C CG  . ASN A 207 ? 0.5044 0.2702 0.2841 0.0268  -0.0340 -0.0076 187 ASN A CG  
1481 O OD1 . ASN A 207 ? 0.5387 0.2844 0.2966 0.0306  -0.0352 -0.0071 187 ASN A OD1 
1482 N ND2 . ASN A 207 ? 0.4994 0.2786 0.2981 0.0242  -0.0463 -0.0107 187 ASN A ND2 
1483 N N   . LYS A 208 ? 0.5076 0.2175 0.2221 0.0357  0.0052  0.0011  188 LYS A N   
1484 C CA  . LYS A 208 ? 0.5270 0.2208 0.2248 0.0378  0.0138  0.0037  188 LYS A CA  
1485 C C   . LYS A 208 ? 0.5304 0.2280 0.2326 0.0374  0.0020  0.0023  188 LYS A C   
1486 O O   . LYS A 208 ? 0.5398 0.2391 0.2447 0.0363  0.0102  0.0046  188 LYS A O   
1487 C CB  . LYS A 208 ? 0.5893 0.2423 0.2434 0.0441  0.0195  0.0048  188 LYS A CB  
1488 C CG  . LYS A 208 ? 0.6610 0.3085 0.3100 0.0453  0.0349  0.0067  188 LYS A CG  
1489 C CD  . LYS A 208 ? 0.8052 0.4099 0.4089 0.0519  0.0446  0.0084  188 LYS A CD  
1490 C CE  . LYS A 208 ? 0.8809 0.4808 0.4817 0.0536  0.0628  0.0107  188 LYS A CE  
1491 N NZ  . LYS A 208 ? 0.9639 0.5187 0.5174 0.0606  0.0737  0.0125  188 LYS A NZ  
1492 N N   . THR A 209 ? 0.5227 0.2220 0.2276 0.0381  -0.0171 -0.0016 189 THR A N   
1493 C CA  . THR A 209 ? 0.5226 0.2268 0.2345 0.0384  -0.0287 -0.0032 189 THR A CA  
1494 C C   . THR A 209 ? 0.4717 0.2101 0.2200 0.0329  -0.0229 -0.0021 189 THR A C   
1495 O O   . THR A 209 ? 0.4656 0.2050 0.2154 0.0328  -0.0210 -0.0010 189 THR A O   
1496 C CB  . THR A 209 ? 0.5651 0.2679 0.2795 0.0399  -0.0500 -0.0078 189 THR A CB  
1497 O OG1 . THR A 209 ? 0.6394 0.3077 0.3175 0.0451  -0.0562 -0.0090 189 THR A OG1 
1498 C CG2 . THR A 209 ? 0.5641 0.2707 0.2863 0.0414  -0.0625 -0.0097 189 THR A CG2 
1499 N N   . GLU A 210 ? 0.4466 0.2101 0.2213 0.0285  -0.0197 -0.0023 190 GLU A N   
1500 C CA  . GLU A 210 ? 0.4141 0.2063 0.2194 0.0238  -0.0147 -0.0014 190 GLU A CA  
1501 C C   . GLU A 210 ? 0.4135 0.2056 0.2182 0.0224  0.0009  0.0023  190 GLU A C   
1502 O O   . GLU A 210 ? 0.4122 0.2169 0.2312 0.0201  0.0027  0.0030  190 GLU A O   
1503 C CB  . GLU A 210 ? 0.4144 0.2283 0.2427 0.0202  -0.0156 -0.0025 190 GLU A CB  
1504 C CG  . GLU A 210 ? 0.4362 0.2541 0.2721 0.0202  -0.0307 -0.0062 190 GLU A CG  
1505 C CD  . GLU A 210 ? 0.5034 0.3346 0.3568 0.0195  -0.0385 -0.0079 190 GLU A CD  
1506 O OE1 . GLU A 210 ? 0.4681 0.3086 0.3298 0.0183  -0.0320 -0.0062 190 GLU A OE1 
1507 O OE2 . GLU A 210 ? 0.5931 0.4252 0.4530 0.0203  -0.0513 -0.0110 190 GLU A OE2 
1508 N N   . VAL A 211 ? 0.4352 0.2116 0.2233 0.0240  0.0126  0.0046  191 VAL A N   
1509 C CA  . VAL A 211 ? 0.4445 0.2192 0.2338 0.0226  0.0283  0.0081  191 VAL A CA  
1510 C C   . VAL A 211 ? 0.4604 0.2179 0.2323 0.0244  0.0276  0.0090  191 VAL A C   
1511 O O   . VAL A 211 ? 0.4649 0.2316 0.2495 0.0213  0.0332  0.0106  191 VAL A O   
1512 C CB  . VAL A 211 ? 0.4628 0.2232 0.2389 0.0245  0.0425  0.0105  191 VAL A CB  
1513 C CG1 . VAL A 211 ? 0.4856 0.2432 0.2650 0.0228  0.0594  0.0142  191 VAL A CG1 
1514 C CG2 . VAL A 211 ? 0.4415 0.2206 0.2374 0.0228  0.0435  0.0098  191 VAL A CG2 
1515 N N   . ASP A 212 ? 0.4773 0.2086 0.2196 0.0294  0.0193  0.0077  192 ASP A N   
1516 C CA  . ASP A 212 ? 0.4896 0.2006 0.2112 0.0322  0.0166  0.0083  192 ASP A CA  
1517 C C   . ASP A 212 ? 0.4751 0.2055 0.2176 0.0302  0.0061  0.0065  192 ASP A C   
1518 O O   . ASP A 212 ? 0.4993 0.2245 0.2381 0.0298  0.0101  0.0081  192 ASP A O   
1519 C CB  . ASP A 212 ? 0.5350 0.2125 0.2193 0.0388  0.0068  0.0067  192 ASP A CB  
1520 C CG  . ASP A 212 ? 0.6370 0.2865 0.2917 0.0418  0.0205  0.0092  192 ASP A CG  
1521 O OD1 . ASP A 212 ? 0.6852 0.3345 0.3428 0.0395  0.0394  0.0129  192 ASP A OD1 
1522 O OD2 . ASP A 212 ? 0.6505 0.2764 0.2784 0.0466  0.0125  0.0074  192 ASP A OD2 
1523 N N   . ILE A 213 ? 0.4490 0.2002 0.2127 0.0291  -0.0061 0.0034  193 ILE A N   
1524 C CA  . ILE A 213 ? 0.4388 0.2093 0.2241 0.0277  -0.0147 0.0016  193 ILE A CA  
1525 C C   . ILE A 213 ? 0.4184 0.2083 0.2250 0.0225  -0.0036 0.0037  193 ILE A C   
1526 O O   . ILE A 213 ? 0.4244 0.2156 0.2339 0.0222  -0.0040 0.0041  193 ILE A O   
1527 C CB  . ILE A 213 ? 0.4351 0.2229 0.2396 0.0273  -0.0274 -0.0020 193 ILE A CB  
1528 C CG1 . ILE A 213 ? 0.4607 0.2288 0.2468 0.0327  -0.0427 -0.0050 193 ILE A CG1 
1529 C CG2 . ILE A 213 ? 0.4195 0.2320 0.2521 0.0248  -0.0310 -0.0033 193 ILE A CG2 
1530 C CD1 . ILE A 213 ? 0.4745 0.2570 0.2794 0.0317  -0.0542 -0.0084 193 ILE A CD1 
1531 N N   . TYR A 214 ? 0.4069 0.2102 0.2277 0.0188  0.0060  0.0051  194 TYR A N   
1532 C CA  . TYR A 214 ? 0.4084 0.2288 0.2497 0.0140  0.0151  0.0070  194 TYR A CA  
1533 C C   . TYR A 214 ? 0.4302 0.2353 0.2592 0.0135  0.0248  0.0098  194 TYR A C   
1534 O O   . TYR A 214 ? 0.4232 0.2364 0.2635 0.0108  0.0259  0.0103  194 TYR A O   
1535 C CB  . TYR A 214 ? 0.4051 0.2371 0.2596 0.0115  0.0231  0.0080  194 TYR A CB  
1536 C CG  . TYR A 214 ? 0.4177 0.2635 0.2919 0.0069  0.0325  0.0099  194 TYR A CG  
1537 C CD1 . TYR A 214 ? 0.4181 0.2855 0.3153 0.0038  0.0283  0.0087  194 TYR A CD1 
1538 C CD2 . TYR A 214 ? 0.4488 0.2850 0.3191 0.0059  0.0457  0.0129  194 TYR A CD2 
1539 C CE1 . TYR A 214 ? 0.4144 0.2929 0.3294 -0.0002 0.0344  0.0101  194 TYR A CE1 
1540 C CE2 . TYR A 214 ? 0.4524 0.3023 0.3448 0.0015  0.0530  0.0143  194 TYR A CE2 
1541 C CZ  . TYR A 214 ? 0.4425 0.3134 0.3570 -0.0015 0.0461  0.0127  194 TYR A CZ  
1542 O OH  . TYR A 214 ? 0.4725 0.3553 0.4084 -0.0057 0.0509  0.0137  194 TYR A OH  
1543 N N   . ASN A 215 ? 0.4423 0.2231 0.2466 0.0163  0.0321  0.0116  195 ASN A N   
1544 C CA  . ASN A 215 ? 0.4585 0.2214 0.2488 0.0158  0.0433  0.0147  195 ASN A CA  
1545 C C   . ASN A 215 ? 0.4741 0.2219 0.2475 0.0185  0.0356  0.0141  195 ASN A C   
1546 O O   . ASN A 215 ? 0.5072 0.2415 0.2710 0.0173  0.0445  0.0166  195 ASN A O   
1547 C CB  . ASN A 215 ? 0.5101 0.2488 0.2767 0.0184  0.0556  0.0171  195 ASN A CB  
1548 C CG  . ASN A 215 ? 0.5450 0.2985 0.3319 0.0152  0.0680  0.0187  195 ASN A CG  
1549 O OD1 . ASN A 215 ? 0.5551 0.3317 0.3718 0.0101  0.0717  0.0192  195 ASN A OD1 
1550 N ND2 . ASN A 215 ? 0.5572 0.2956 0.3276 0.0186  0.0746  0.0195  195 ASN A ND2 
1551 N N   . SER A 216 ? 0.4552 0.2045 0.2257 0.0221  0.0195  0.0108  196 SER A N   
1552 C CA  . SER A 216 ? 0.4880 0.2224 0.2427 0.0260  0.0103  0.0099  196 SER A CA  
1553 C C   . SER A 216 ? 0.4814 0.2377 0.2599 0.0241  0.0030  0.0080  196 SER A C   
1554 O O   . SER A 216 ? 0.4996 0.2452 0.2678 0.0271  -0.0033 0.0074  196 SER A O   
1555 C CB  . SER A 216 ? 0.5263 0.2451 0.2618 0.0325  -0.0045 0.0070  196 SER A CB  
1556 O OG  . SER A 216 ? 0.5718 0.2658 0.2799 0.0354  0.0006  0.0083  196 SER A OG  
1557 N N   . ASP A 217 ? 0.4436 0.2278 0.2509 0.0201  0.0028  0.0070  197 ASP A N   
1558 C CA  . ASP A 217 ? 0.4228 0.2259 0.2506 0.0190  -0.0037 0.0051  197 ASP A CA  
1559 C C   . ASP A 217 ? 0.4339 0.2381 0.2664 0.0151  0.0042  0.0071  197 ASP A C   
1560 O O   . ASP A 217 ? 0.4264 0.2405 0.2719 0.0100  0.0134  0.0088  197 ASP A O   
1561 C CB  . ASP A 217 ? 0.3984 0.2267 0.2510 0.0161  -0.0052 0.0035  197 ASP A CB  
1562 C CG  . ASP A 217 ? 0.4177 0.2638 0.2896 0.0157  -0.0113 0.0013  197 ASP A CG  
1563 O OD1 . ASP A 217 ? 0.4247 0.2666 0.2940 0.0167  -0.0127 0.0013  197 ASP A OD1 
1564 O OD2 . ASP A 217 ? 0.4106 0.2731 0.2987 0.0146  -0.0139 -0.0002 197 ASP A OD2 
1565 N N   . PRO A 218 ? 0.4512 0.2467 0.2759 0.0175  -0.0005 0.0066  198 PRO A N   
1566 C CA  . PRO A 218 ? 0.4448 0.2396 0.2731 0.0135  0.0064  0.0084  198 PRO A CA  
1567 C C   . PRO A 218 ? 0.4220 0.2407 0.2763 0.0091  0.0062  0.0073  198 PRO A C   
1568 O O   . PRO A 218 ? 0.4425 0.2620 0.3026 0.0047  0.0117  0.0086  198 PRO A O   
1569 C CB  . PRO A 218 ? 0.4787 0.2560 0.2894 0.0183  0.0000  0.0078  198 PRO A CB  
1570 C CG  . PRO A 218 ? 0.4941 0.2703 0.3005 0.0248  -0.0126 0.0049  198 PRO A CG  
1571 C CD  . PRO A 218 ? 0.4659 0.2508 0.2785 0.0242  -0.0128 0.0043  198 PRO A CD  
1572 N N   . LEU A 219 ? 0.3993 0.2350 0.2678 0.0104  -0.0003 0.0048  199 LEU A N   
1573 C CA  . LEU A 219 ? 0.3921 0.2467 0.2810 0.0068  -0.0001 0.0039  199 LEU A CA  
1574 C C   . LEU A 219 ? 0.4027 0.2682 0.3041 0.0020  0.0061  0.0051  199 LEU A C   
1575 O O   . LEU A 219 ? 0.4078 0.2864 0.3236 -0.0007 0.0054  0.0043  199 LEU A O   
1576 C CB  . LEU A 219 ? 0.3911 0.2575 0.2896 0.0102  -0.0079 0.0010  199 LEU A CB  
1577 C CG  . LEU A 219 ? 0.4210 0.2818 0.3149 0.0150  -0.0141 -0.0006 199 LEU A CG  
1578 C CD1 . LEU A 219 ? 0.4261 0.3007 0.3343 0.0180  -0.0197 -0.0034 199 LEU A CD1 
1579 C CD2 . LEU A 219 ? 0.4267 0.2837 0.3192 0.0129  -0.0113 0.0000  199 LEU A CD2 
1580 N N   . ILE A 220 ? 0.3926 0.2516 0.2875 0.0017  0.0115  0.0067  200 ILE A N   
1581 C CA  . ILE A 220 ? 0.3839 0.2529 0.2918 -0.0021 0.0177  0.0078  200 ILE A CA  
1582 C C   . ILE A 220 ? 0.4071 0.2707 0.3178 -0.0064 0.0267  0.0103  200 ILE A C   
1583 O O   . ILE A 220 ? 0.4378 0.2841 0.3333 -0.0058 0.0320  0.0121  200 ILE A O   
1584 C CB  . ILE A 220 ? 0.3801 0.2450 0.2803 0.0004  0.0194  0.0081  200 ILE A CB  
1585 C CG1 . ILE A 220 ? 0.3893 0.2629 0.2927 0.0033  0.0102  0.0054  200 ILE A CG1 
1586 C CG2 . ILE A 220 ? 0.3803 0.2528 0.2926 -0.0029 0.0276  0.0097  200 ILE A CG2 
1587 C CD1 . ILE A 220 ? 0.4016 0.2686 0.2953 0.0059  0.0097  0.0053  200 ILE A CD1 
1588 N N   . CYS A 221 ? 0.4036 0.2807 0.3341 -0.0108 0.0284  0.0104  201 CYS A N   
1589 C CA  . CYS A 221 ? 0.4274 0.3023 0.3673 -0.0157 0.0367  0.0125  201 CYS A CA  
1590 C C   . CYS A 221 ? 0.4512 0.3277 0.3969 -0.0161 0.0457  0.0142  201 CYS A C   
1591 O O   . CYS A 221 ? 0.4490 0.3391 0.4078 -0.0161 0.0435  0.0133  201 CYS A O   
1592 C CB  . CYS A 221 ? 0.4356 0.3227 0.3948 -0.0200 0.0321  0.0113  201 CYS A CB  
1593 S SG  . CYS A 221 ? 0.5069 0.3930 0.4837 -0.0269 0.0410  0.0135  201 CYS A SG  
1594 N N   . ARG A 222 ? 0.4706 0.3314 0.4046 -0.0160 0.0563  0.0168  202 ARG A N   
1595 C CA  . ARG A 222 ? 0.4978 0.3569 0.4350 -0.0158 0.0673  0.0187  202 ARG A CA  
1596 C C   . ARG A 222 ? 0.5273 0.3876 0.4831 -0.0212 0.0795  0.0211  202 ARG A C   
1597 O O   . ARG A 222 ? 0.5455 0.3990 0.5010 -0.0208 0.0925  0.0234  202 ARG A O   
1598 C CB  . ARG A 222 ? 0.5135 0.3510 0.4209 -0.0105 0.0716  0.0198  202 ARG A CB  
1599 C CG  . ARG A 222 ? 0.5153 0.3544 0.4106 -0.0055 0.0595  0.0172  202 ARG A CG  
1600 C CD  . ARG A 222 ? 0.5460 0.3608 0.4099 -0.0001 0.0606  0.0177  202 ARG A CD  
1601 N NE  . ARG A 222 ? 0.5733 0.3683 0.4182 0.0006  0.0622  0.0189  202 ARG A NE  
1602 C CZ  . ARG A 222 ? 0.5868 0.3770 0.4209 0.0032  0.0508  0.0171  202 ARG A CZ  
1603 N NH1 . ARG A 222 ? 0.5179 0.3212 0.3586 0.0055  0.0377  0.0140  202 ARG A NH1 
1604 N NH2 . ARG A 222 ? 0.6166 0.3879 0.4335 0.0039  0.0529  0.0184  202 ARG A NH2 
1605 N N   . ALA A 223 ? 0.5273 0.3956 0.5000 -0.0261 0.0756  0.0205  203 ALA A N   
1606 C CA  . ALA A 223 ? 0.5288 0.4006 0.5247 -0.0322 0.0853  0.0223  203 ALA A CA  
1607 C C   . ALA A 223 ? 0.5140 0.4061 0.5396 -0.0334 0.0851  0.0216  203 ALA A C   
1608 O O   . ALA A 223 ? 0.5036 0.4066 0.5302 -0.0302 0.0754  0.0194  203 ALA A O   
1609 C CB  . ALA A 223 ? 0.5343 0.4075 0.5379 -0.0369 0.0780  0.0213  203 ALA A CB  
1610 N N   . GLY A 224 ? 0.5076 0.4046 0.5586 -0.0380 0.0956  0.0233  204 GLY A N   
1611 C CA  . GLY A 224 ? 0.4902 0.4069 0.5730 -0.0391 0.0941  0.0223  204 GLY A CA  
1612 C C   . GLY A 224 ? 0.4722 0.4035 0.5695 -0.0409 0.0759  0.0189  204 GLY A C   
1613 O O   . GLY A 224 ? 0.4675 0.3946 0.5594 -0.0437 0.0682  0.0178  204 GLY A O   
1614 N N   . LEU A 225 ? 0.4597 0.4054 0.5714 -0.0386 0.0688  0.0171  205 LEU A N   
1615 C CA  . LEU A 225 ? 0.4607 0.4168 0.5817 -0.0394 0.0514  0.0139  205 LEU A CA  
1616 C C   . LEU A 225 ? 0.4378 0.4011 0.5891 -0.0457 0.0478  0.0132  205 LEU A C   
1617 O O   . LEU A 225 ? 0.4197 0.3916 0.5994 -0.0479 0.0552  0.0141  205 LEU A O   
1618 C CB  . LEU A 225 ? 0.4752 0.4419 0.6010 -0.0349 0.0452  0.0124  205 LEU A CB  
1619 C CG  . LEU A 225 ? 0.5273 0.4900 0.6259 -0.0301 0.0371  0.0109  205 LEU A CG  
1620 C CD1 . LEU A 225 ? 0.5562 0.5054 0.6270 -0.0274 0.0457  0.0127  205 LEU A CD1 
1621 C CD2 . LEU A 225 ? 0.5407 0.5122 0.6449 -0.0261 0.0331  0.0099  205 LEU A CD2 
1622 N N   . LYS A 226 ? 0.4355 0.3947 0.5819 -0.0486 0.0366  0.0113  206 LYS A N   
1623 C CA  . LYS A 226 ? 0.4266 0.3912 0.6010 -0.0549 0.0301  0.0100  206 LYS A CA  
1624 C C   . LYS A 226 ? 0.4100 0.3893 0.6093 -0.0538 0.0185  0.0075  206 LYS A C   
1625 O O   . LYS A 226 ? 0.4073 0.3885 0.5928 -0.0484 0.0108  0.0061  206 LYS A O   
1626 C CB  . LYS A 226 ? 0.4677 0.4222 0.6258 -0.0570 0.0188  0.0081  206 LYS A CB  
1627 C CG  . LYS A 226 ? 0.5499 0.4894 0.6890 -0.0591 0.0290  0.0104  206 LYS A CG  
1628 C CD  . LYS A 226 ? 0.6441 0.5726 0.7585 -0.0580 0.0176  0.0084  206 LYS A CD  
1629 C CE  . LYS A 226 ? 0.7299 0.6423 0.8238 -0.0591 0.0261  0.0104  206 LYS A CE  
1630 N NZ  . LYS A 226 ? 0.7770 0.6797 0.8407 -0.0543 0.0182  0.0089  206 LYS A NZ  
1631 N N   . VAL A 227 ? 0.3987 0.3877 0.6351 -0.0588 0.0174  0.0070  207 VAL A N   
1632 C CA  . VAL A 227 ? 0.3943 0.3967 0.6563 -0.0571 0.0052  0.0045  207 VAL A CA  
1633 C C   . VAL A 227 ? 0.3782 0.3756 0.6247 -0.0552 -0.0165 0.0007  207 VAL A C   
1634 O O   . VAL A 227 ? 0.3844 0.3862 0.6293 -0.0501 -0.0257 -0.0009 207 VAL A O   
1635 C CB  . VAL A 227 ? 0.4047 0.4196 0.7142 -0.0626 0.0081  0.0045  207 VAL A CB  
1636 C CG1 . VAL A 227 ? 0.4038 0.4313 0.7390 -0.0602 -0.0083 0.0013  207 VAL A CG1 
1637 C CG2 . VAL A 227 ? 0.4135 0.4320 0.7345 -0.0625 0.0319  0.0085  207 VAL A CG2 
1638 N N   . CYS A 228 ? 0.3604 0.3461 0.5911 -0.0583 -0.0237 -0.0004 208 CYS A N   
1639 C CA  A CYS A 228 ? 0.3637 0.3409 0.5749 -0.0558 -0.0424 -0.0038 208 CYS A CA  
1640 C CA  B CYS A 228 ? 0.3705 0.3473 0.5809 -0.0558 -0.0422 -0.0038 208 CYS A CA  
1641 C C   . CYS A 228 ? 0.3690 0.3416 0.5470 -0.0485 -0.0412 -0.0035 208 CYS A C   
1642 O O   . CYS A 228 ? 0.3744 0.3443 0.5430 -0.0445 -0.0539 -0.0058 208 CYS A O   
1643 C CB  A CYS A 228 ? 0.3756 0.3393 0.5738 -0.0601 -0.0478 -0.0048 208 CYS A CB  
1644 C CB  B CYS A 228 ? 0.3988 0.3619 0.5948 -0.0600 -0.0468 -0.0046 208 CYS A CB  
1645 S SG  A CYS A 228 ? 0.4136 0.3657 0.5792 -0.0594 -0.0320 -0.0017 208 CYS A SG  
1646 S SG  B CYS A 228 ? 0.4616 0.4263 0.6934 -0.0686 -0.0582 -0.0069 208 CYS A SG  
1647 N N   . PHE A 229 ? 0.3553 0.3255 0.5156 -0.0466 -0.0262 -0.0007 209 PHE A N   
1648 C CA  . PHE A 229 ? 0.3525 0.3195 0.4856 -0.0404 -0.0247 -0.0004 209 PHE A CA  
1649 C C   . PHE A 229 ? 0.3524 0.3299 0.4974 -0.0366 -0.0237 -0.0002 209 PHE A C   
1650 O O   . PHE A 229 ? 0.3539 0.3295 0.4845 -0.0321 -0.0307 -0.0015 209 PHE A O   
1651 C CB  . PHE A 229 ? 0.3439 0.3048 0.4568 -0.0394 -0.0112 0.0021  209 PHE A CB  
1652 C CG  . PHE A 229 ? 0.3471 0.3032 0.4324 -0.0339 -0.0124 0.0017  209 PHE A CG  
1653 C CD1 . PHE A 229 ? 0.3592 0.3069 0.4263 -0.0324 -0.0216 -0.0003 209 PHE A CD1 
1654 C CD2 . PHE A 229 ? 0.3518 0.3111 0.4304 -0.0303 -0.0042 0.0032  209 PHE A CD2 
1655 C CE1 . PHE A 229 ? 0.3743 0.3185 0.4199 -0.0277 -0.0213 -0.0007 209 PHE A CE1 
1656 C CE2 . PHE A 229 ? 0.3663 0.3218 0.4230 -0.0260 -0.0055 0.0026  209 PHE A CE2 
1657 C CZ  . PHE A 229 ? 0.3677 0.3166 0.4098 -0.0249 -0.0136 0.0008  209 PHE A CZ  
1658 N N   . GLY A 230 ? 0.3468 0.3342 0.5182 -0.0385 -0.0148 0.0014  210 GLY A N   
1659 C CA  . GLY A 230 ? 0.3468 0.3445 0.5335 -0.0348 -0.0134 0.0015  210 GLY A CA  
1660 C C   . GLY A 230 ? 0.3430 0.3436 0.5393 -0.0329 -0.0312 -0.0016 210 GLY A C   
1661 O O   . GLY A 230 ? 0.3350 0.3370 0.5241 -0.0277 -0.0344 -0.0021 210 GLY A O   
1662 N N   . ILE A 231 ? 0.3414 0.3401 0.5505 -0.0368 -0.0438 -0.0039 211 ILE A N   
1663 C CA  . ILE A 231 ? 0.3482 0.3448 0.5626 -0.0351 -0.0637 -0.0074 211 ILE A CA  
1664 C C   . ILE A 231 ? 0.3456 0.3286 0.5216 -0.0301 -0.0709 -0.0085 211 ILE A C   
1665 O O   . ILE A 231 ? 0.3540 0.3350 0.5260 -0.0255 -0.0810 -0.0101 211 ILE A O   
1666 C CB  . ILE A 231 ? 0.3673 0.3612 0.5990 -0.0409 -0.0756 -0.0096 211 ILE A CB  
1667 C CG1 . ILE A 231 ? 0.3745 0.3842 0.6530 -0.0455 -0.0714 -0.0092 211 ILE A CG1 
1668 C CG2 . ILE A 231 ? 0.3806 0.3631 0.6014 -0.0384 -0.0985 -0.0136 211 ILE A CG2 
1669 C CD1 . ILE A 231 ? 0.3947 0.4027 0.6938 -0.0526 -0.0804 -0.0110 211 ILE A CD1 
1670 N N   . GLN A 232 ? 0.3310 0.3038 0.4794 -0.0308 -0.0654 -0.0076 212 GLN A N   
1671 C CA  . GLN A 232 ? 0.3320 0.2924 0.4463 -0.0262 -0.0693 -0.0084 212 GLN A CA  
1672 C C   . GLN A 232 ? 0.3285 0.2932 0.4334 -0.0216 -0.0608 -0.0068 212 GLN A C   
1673 O O   . GLN A 232 ? 0.3391 0.2957 0.4246 -0.0174 -0.0665 -0.0078 212 GLN A O   
1674 C CB  . GLN A 232 ? 0.3411 0.2903 0.4316 -0.0276 -0.0658 -0.0082 212 GLN A CB  
1675 C CG  . GLN A 232 ? 0.3701 0.3106 0.4639 -0.0316 -0.0766 -0.0103 212 GLN A CG  
1676 C CD  . GLN A 232 ? 0.3931 0.3241 0.4836 -0.0295 -0.0951 -0.0135 212 GLN A CD  
1677 O OE1 . GLN A 232 ? 0.3941 0.3169 0.4641 -0.0243 -0.0994 -0.0143 212 GLN A OE1 
1678 N NE2 . GLN A 232 ? 0.4032 0.3333 0.5133 -0.0337 -0.1067 -0.0156 212 GLN A NE2 
1679 N N   . LEU A 233 ? 0.3122 0.2876 0.4298 -0.0223 -0.0473 -0.0044 213 LEU A N   
1680 C CA  . LEU A 233 ? 0.3247 0.3033 0.4343 -0.0181 -0.0399 -0.0030 213 LEU A CA  
1681 C C   . LEU A 233 ? 0.3345 0.3182 0.4595 -0.0149 -0.0480 -0.0042 213 LEU A C   
1682 O O   . LEU A 233 ? 0.3440 0.3241 0.4545 -0.0106 -0.0496 -0.0044 213 LEU A O   
1683 C CB  . LEU A 233 ? 0.3250 0.3093 0.4391 -0.0190 -0.0238 -0.0003 213 LEU A CB  
1684 C CG  . LEU A 233 ? 0.3512 0.3284 0.4459 -0.0207 -0.0165 0.0009  213 LEU A CG  
1685 C CD1 . LEU A 233 ? 0.3537 0.3332 0.4516 -0.0212 -0.0018 0.0035  213 LEU A CD1 
1686 C CD2 . LEU A 233 ? 0.3784 0.3481 0.4463 -0.0175 -0.0185 0.0003  213 LEU A CD2 
1687 N N   . LEU A 234 ? 0.3316 0.3231 0.4866 -0.0170 -0.0540 -0.0052 214 LEU A N   
1688 C CA  . LEU A 234 ? 0.3450 0.3412 0.5172 -0.0135 -0.0646 -0.0068 214 LEU A CA  
1689 C C   . LEU A 234 ? 0.3597 0.3410 0.5090 -0.0105 -0.0813 -0.0095 214 LEU A C   
1690 O O   . LEU A 234 ? 0.3650 0.3426 0.5069 -0.0054 -0.0872 -0.0102 214 LEU A O   
1691 C CB  . LEU A 234 ? 0.3453 0.3529 0.5576 -0.0169 -0.0693 -0.0079 214 LEU A CB  
1692 C CG  . LEU A 234 ? 0.3627 0.3845 0.6026 -0.0189 -0.0522 -0.0053 214 LEU A CG  
1693 C CD1 . LEU A 234 ? 0.3534 0.3858 0.6348 -0.0235 -0.0568 -0.0064 214 LEU A CD1 
1694 C CD2 . LEU A 234 ? 0.3757 0.4034 0.6189 -0.0131 -0.0453 -0.0041 214 LEU A CD2 
1695 N N   . ASN A 235 ? 0.3584 0.3287 0.4930 -0.0132 -0.0881 -0.0108 215 ASN A N   
1696 C CA  . ASN A 235 ? 0.3769 0.3288 0.4840 -0.0100 -0.1019 -0.0131 215 ASN A CA  
1697 C C   . ASN A 235 ? 0.3808 0.3245 0.4571 -0.0060 -0.0942 -0.0117 215 ASN A C   
1698 O O   . ASN A 235 ? 0.3993 0.3327 0.4611 -0.0014 -0.1023 -0.0127 215 ASN A O   
1699 C CB  . ASN A 235 ? 0.4053 0.3455 0.4999 -0.0135 -0.1074 -0.0144 215 ASN A CB  
1700 C CG  . ASN A 235 ? 0.4527 0.3953 0.5733 -0.0172 -0.1207 -0.0167 215 ASN A CG  
1701 O OD1 . ASN A 235 ? 0.4654 0.4178 0.6147 -0.0166 -0.1285 -0.0179 215 ASN A OD1 
1702 N ND2 . ASN A 235 ? 0.4596 0.3932 0.5723 -0.0210 -0.1240 -0.0177 215 ASN A ND2 
1703 N N   . ALA A 236 ? 0.3646 0.3127 0.4327 -0.0076 -0.0787 -0.0093 216 ALA A N   
1704 C CA  . ALA A 236 ? 0.3657 0.3079 0.4091 -0.0047 -0.0707 -0.0081 216 ALA A CA  
1705 C C   . ALA A 236 ? 0.3606 0.3066 0.4082 -0.0007 -0.0705 -0.0076 216 ALA A C   
1706 O O   . ALA A 236 ? 0.3624 0.2966 0.3890 0.0028  -0.0739 -0.0080 216 ALA A O   
1707 C CB  . ALA A 236 ? 0.3647 0.3133 0.4055 -0.0072 -0.0561 -0.0060 216 ALA A CB  
1708 N N   . VAL A 237 ? 0.3434 0.3041 0.4171 -0.0011 -0.0661 -0.0067 217 VAL A N   
1709 C CA  . VAL A 237 ? 0.3430 0.3073 0.4220 0.0030  -0.0653 -0.0062 217 VAL A CA  
1710 C C   . VAL A 237 ? 0.3478 0.3027 0.4239 0.0072  -0.0817 -0.0085 217 VAL A C   
1711 O O   . VAL A 237 ? 0.3528 0.2997 0.4131 0.0115  -0.0831 -0.0084 217 VAL A O   
1712 C CB  . VAL A 237 ? 0.3412 0.3221 0.4504 0.0020  -0.0565 -0.0049 217 VAL A CB  
1713 C CG1 . VAL A 237 ? 0.3514 0.3366 0.4727 0.0070  -0.0588 -0.0050 217 VAL A CG1 
1714 C CG2 . VAL A 237 ? 0.3416 0.3259 0.4437 -0.0002 -0.0402 -0.0025 217 VAL A CG2 
1715 N N   . SER A 238 ? 0.3554 0.3093 0.4451 0.0060  -0.0947 -0.0107 218 SER A N   
1716 C CA  A SER A 238 ? 0.3739 0.3165 0.4603 0.0103  -0.1129 -0.0132 218 SER A CA  
1717 C CA  B SER A 238 ? 0.3683 0.3110 0.4548 0.0103  -0.1129 -0.0132 218 SER A CA  
1718 C C   . SER A 238 ? 0.3883 0.3073 0.4338 0.0130  -0.1177 -0.0139 218 SER A C   
1719 O O   . SER A 238 ? 0.4044 0.3110 0.4345 0.0183  -0.1250 -0.0145 218 SER A O   
1720 C CB  A SER A 238 ? 0.4080 0.3538 0.5185 0.0078  -0.1269 -0.0157 218 SER A CB  
1721 C CB  B SER A 238 ? 0.3863 0.3321 0.4966 0.0077  -0.1267 -0.0157 218 SER A CB  
1722 O OG  A SER A 238 ? 0.4487 0.4161 0.6002 0.0056  -0.1218 -0.0151 218 SER A OG  
1723 O OG  B SER A 238 ? 0.4241 0.3591 0.5338 0.0125  -0.1464 -0.0186 218 SER A OG  
1724 N N   . ARG A 239 ? 0.3814 0.2930 0.4085 0.0098  -0.1125 -0.0135 219 ARG A N   
1725 C CA  . ARG A 239 ? 0.3914 0.2802 0.3802 0.0121  -0.1137 -0.0138 219 ARG A CA  
1726 C C   . ARG A 239 ? 0.3820 0.2681 0.3530 0.0142  -0.1014 -0.0117 219 ARG A C   
1727 O O   . ARG A 239 ? 0.4043 0.2706 0.3476 0.0180  -0.1047 -0.0119 219 ARG A O   
1728 C CB  . ARG A 239 ? 0.4030 0.2871 0.3814 0.0082  -0.1095 -0.0139 219 ARG A CB  
1729 C CG  . ARG A 239 ? 0.4275 0.3062 0.4146 0.0067  -0.1249 -0.0166 219 ARG A CG  
1730 C CD  . ARG A 239 ? 0.4471 0.3250 0.4297 0.0023  -0.1191 -0.0164 219 ARG A CD  
1731 N NE  . ARG A 239 ? 0.4576 0.3370 0.4590 -0.0010 -0.1316 -0.0186 219 ARG A NE  
1732 C CZ  . ARG A 239 ? 0.4576 0.3335 0.4560 -0.0047 -0.1303 -0.0190 219 ARG A CZ  
1733 N NH1 . ARG A 239 ? 0.4340 0.3049 0.4113 -0.0049 -0.1177 -0.0175 219 ARG A NH1 
1734 N NH2 . ARG A 239 ? 0.4414 0.3188 0.4591 -0.0083 -0.1421 -0.0211 219 ARG A NH2 
1735 N N   . VAL A 240 ? 0.3592 0.2629 0.3447 0.0118  -0.0873 -0.0095 220 VAL A N   
1736 C CA  . VAL A 240 ? 0.3656 0.2673 0.3370 0.0133  -0.0765 -0.0077 220 VAL A CA  
1737 C C   . VAL A 240 ? 0.3859 0.2815 0.3550 0.0182  -0.0838 -0.0081 220 VAL A C   
1738 O O   . VAL A 240 ? 0.3969 0.2767 0.3411 0.0209  -0.0827 -0.0077 220 VAL A O   
1739 C CB  . VAL A 240 ? 0.3600 0.2800 0.3471 0.0100  -0.0624 -0.0057 220 VAL A CB  
1740 C CG1 . VAL A 240 ? 0.3652 0.2849 0.3447 0.0119  -0.0545 -0.0043 220 VAL A CG1 
1741 C CG2 . VAL A 240 ? 0.3604 0.2810 0.3407 0.0063  -0.0547 -0.0052 220 VAL A CG2 
1742 N N   . GLU A 241 ? 0.3965 0.3032 0.3916 0.0197  -0.0914 -0.0090 221 GLU A N   
1743 C CA  . GLU A 241 ? 0.4306 0.3322 0.4263 0.0253  -0.0996 -0.0096 221 GLU A CA  
1744 C C   . GLU A 241 ? 0.4659 0.3417 0.4331 0.0295  -0.1134 -0.0113 221 GLU A C   
1745 O O   . GLU A 241 ? 0.4878 0.3494 0.4341 0.0336  -0.1135 -0.0107 221 GLU A O   
1746 C CB  . GLU A 241 ? 0.4678 0.3863 0.5007 0.0262  -0.1067 -0.0107 221 GLU A CB  
1747 C CG  . GLU A 241 ? 0.5759 0.4916 0.6138 0.0327  -0.1149 -0.0114 221 GLU A CG  
1748 C CD  . GLU A 241 ? 0.7097 0.6370 0.7830 0.0346  -0.1278 -0.0135 221 GLU A CD  
1749 O OE1 . GLU A 241 ? 0.7256 0.6697 0.8271 0.0299  -0.1241 -0.0135 221 GLU A OE1 
1750 O OE2 . GLU A 241 ? 0.7612 0.6801 0.8347 0.0407  -0.1419 -0.0152 221 GLU A OE2 
1751 N N   . ARG A 242 ? 0.4687 0.3357 0.4317 0.0286  -0.1243 -0.0133 222 ARG A N   
1752 C CA  . ARG A 242 ? 0.5027 0.3410 0.4341 0.0330  -0.1378 -0.0150 222 ARG A CA  
1753 C C   . ARG A 242 ? 0.5169 0.3351 0.4095 0.0331  -0.1264 -0.0134 222 ARG A C   
1754 O O   . ARG A 242 ? 0.5491 0.3408 0.4105 0.0378  -0.1331 -0.0139 222 ARG A O   
1755 C CB  . ARG A 242 ? 0.5457 0.3780 0.4816 0.0318  -0.1528 -0.0178 222 ARG A CB  
1756 C CG  . ARG A 242 ? 0.6075 0.4514 0.5775 0.0334  -0.1695 -0.0202 222 ARG A CG  
1757 C CD  . ARG A 242 ? 0.6892 0.5229 0.6601 0.0322  -0.1866 -0.0234 222 ARG A CD  
1758 N NE  . ARG A 242 ? 0.7504 0.5966 0.7329 0.0251  -0.1770 -0.0227 222 ARG A NE  
1759 C CZ  . ARG A 242 ? 0.7708 0.6404 0.7933 0.0203  -0.1768 -0.0231 222 ARG A CZ  
1760 N NH1 . ARG A 242 ? 0.7646 0.6497 0.8226 0.0216  -0.1851 -0.0242 222 ARG A NH1 
1761 N NH2 . ARG A 242 ? 0.7540 0.6311 0.7816 0.0143  -0.1677 -0.0223 222 ARG A NH2 
1762 N N   . ALA A 243 ? 0.4938 0.3232 0.3882 0.0282  -0.1096 -0.0114 223 ALA A N   
1763 C CA  . ALA A 243 ? 0.5135 0.3268 0.3772 0.0278  -0.0975 -0.0099 223 ALA A CA  
1764 C C   . ALA A 243 ? 0.5308 0.3412 0.3846 0.0292  -0.0877 -0.0079 223 ALA A C   
1765 O O   . ALA A 243 ? 0.5570 0.3481 0.3824 0.0301  -0.0803 -0.0069 223 ALA A O   
1766 C CB  . ALA A 243 ? 0.5032 0.3302 0.3754 0.0224  -0.0847 -0.0089 223 ALA A CB  
1767 N N   . LEU A 244 ? 0.5182 0.3468 0.3950 0.0291  -0.0860 -0.0072 224 LEU A N   
1768 C CA  . LEU A 244 ? 0.5472 0.3742 0.4161 0.0296  -0.0758 -0.0053 224 LEU A CA  
1769 C C   . LEU A 244 ? 0.6012 0.3994 0.4368 0.0344  -0.0792 -0.0051 224 LEU A C   
1770 O O   . LEU A 244 ? 0.6055 0.3941 0.4230 0.0327  -0.0667 -0.0033 224 LEU A O   
1771 C CB  . LEU A 244 ? 0.5294 0.3771 0.4258 0.0299  -0.0750 -0.0049 224 LEU A CB  
1772 C CG  . LEU A 244 ? 0.5264 0.3994 0.4513 0.0253  -0.0681 -0.0045 224 LEU A CG  
1773 C CD1 . LEU A 244 ? 0.5209 0.4091 0.4662 0.0263  -0.0641 -0.0038 224 LEU A CD1 
1774 C CD2 . LEU A 244 ? 0.5387 0.4146 0.4567 0.0203  -0.0549 -0.0034 224 LEU A CD2 
1775 N N   . PRO A 245 ? 0.6347 0.4161 0.4594 0.0400  -0.0955 -0.0068 225 PRO A N   
1776 C CA  . PRO A 245 ? 0.6771 0.4260 0.4639 0.0448  -0.0979 -0.0064 225 PRO A CA  
1777 C C   . PRO A 245 ? 0.7125 0.4375 0.4662 0.0439  -0.0906 -0.0058 225 PRO A C   
1778 O O   . PRO A 245 ? 0.7587 0.4562 0.4791 0.0467  -0.0865 -0.0046 225 PRO A O   
1779 C CB  . PRO A 245 ? 0.6952 0.4334 0.4817 0.0515  -0.1198 -0.0089 225 PRO A CB  
1780 C CG  . PRO A 245 ? 0.6731 0.4437 0.5047 0.0497  -0.1257 -0.0101 225 PRO A CG  
1781 C CD  . PRO A 245 ? 0.6319 0.4217 0.4785 0.0425  -0.1129 -0.0093 225 PRO A CD  
1782 N N   . LYS A 246 ? 0.7000 0.4336 0.4614 0.0402  -0.0877 -0.0064 226 LYS A N   
1783 C CA  . LYS A 246 ? 0.7140 0.4274 0.4474 0.0394  -0.0786 -0.0058 226 LYS A CA  
1784 C C   . LYS A 246 ? 0.6845 0.4121 0.4261 0.0338  -0.0571 -0.0035 226 LYS A C   
1785 O O   . LYS A 246 ? 0.7148 0.4275 0.4363 0.0330  -0.0460 -0.0026 226 LYS A O   
1786 C CB  . LYS A 246 ? 0.7494 0.4640 0.4871 0.0387  -0.0873 -0.0080 226 LYS A CB  
1787 C CG  . LYS A 246 ? 0.8244 0.5337 0.5670 0.0427  -0.1104 -0.0108 226 LYS A CG  
1788 C CD  . LYS A 246 ? 0.8912 0.6055 0.6438 0.0406  -0.1185 -0.0130 226 LYS A CD  
1789 C CE  . LYS A 246 ? 0.9519 0.6624 0.7140 0.0439  -0.1425 -0.0161 226 LYS A CE  
1790 N NZ  . LYS A 246 ? 0.9880 0.6989 0.7566 0.0417  -0.1517 -0.0184 226 LYS A NZ  
1791 N N   . LEU A 247 ? 0.6163 0.3729 0.3892 0.0300  -0.0518 -0.0027 227 LEU A N   
1792 C CA  . LEU A 247 ? 0.5645 0.3360 0.3489 0.0247  -0.0350 -0.0011 227 LEU A CA  
1793 C C   . LEU A 247 ? 0.5448 0.3024 0.3122 0.0246  -0.0239 0.0008  227 LEU A C   
1794 O O   . LEU A 247 ? 0.5473 0.3036 0.3149 0.0262  -0.0273 0.0013  227 LEU A O   
1795 C CB  . LEU A 247 ? 0.5356 0.3390 0.3557 0.0213  -0.0351 -0.0013 227 LEU A CB  
1796 C CG  . LEU A 247 ? 0.5305 0.3515 0.3662 0.0161  -0.0221 -0.0004 227 LEU A CG  
1797 C CD1 . LEU A 247 ? 0.5332 0.3549 0.3686 0.0149  -0.0210 -0.0012 227 LEU A CD1 
1798 C CD2 . LEU A 247 ? 0.5007 0.3465 0.3644 0.0139  -0.0226 -0.0004 227 LEU A CD2 
1799 N N   . THR A 248 ? 0.5282 0.2740 0.2807 0.0228  -0.0103 0.0020  228 THR A N   
1800 C CA  . THR A 248 ? 0.5309 0.2633 0.2693 0.0214  0.0030  0.0040  228 THR A CA  
1801 C C   . THR A 248 ? 0.4888 0.2387 0.2468 0.0154  0.0189  0.0050  228 THR A C   
1802 O O   . THR A 248 ? 0.4956 0.2386 0.2488 0.0129  0.0307  0.0066  228 THR A O   
1803 C CB  . THR A 248 ? 0.5852 0.2804 0.2834 0.0255  0.0066  0.0048  228 THR A CB  
1804 O OG1 . THR A 248 ? 0.6034 0.2948 0.2966 0.0251  0.0122  0.0043  228 THR A OG1 
1805 C CG2 . THR A 248 ? 0.6176 0.2910 0.2929 0.0321  -0.0108 0.0036  228 THR A CG2 
1806 N N   . VAL A 249 ? 0.4632 0.2341 0.2430 0.0130  0.0190  0.0040  229 VAL A N   
1807 C CA  . VAL A 249 ? 0.4448 0.2315 0.2438 0.0081  0.0319  0.0044  229 VAL A CA  
1808 C C   . VAL A 249 ? 0.4194 0.2228 0.2386 0.0042  0.0342  0.0049  229 VAL A C   
1809 O O   . VAL A 249 ? 0.4090 0.2227 0.2375 0.0051  0.0243  0.0043  229 VAL A O   
1810 C CB  . VAL A 249 ? 0.4339 0.2385 0.2507 0.0074  0.0284  0.0030  229 VAL A CB  
1811 C CG1 . VAL A 249 ? 0.4163 0.2417 0.2539 0.0069  0.0166  0.0020  229 VAL A CG1 
1812 C CG2 . VAL A 249 ? 0.4322 0.2493 0.2660 0.0036  0.0411  0.0032  229 VAL A CG2 
1813 N N   . PRO A 250 ? 0.4176 0.2234 0.2446 0.0001  0.0470  0.0058  230 PRO A N   
1814 C CA  . PRO A 250 ? 0.4017 0.2238 0.2492 -0.0040 0.0477  0.0058  230 PRO A CA  
1815 C C   . PRO A 250 ? 0.3663 0.2131 0.2379 -0.0049 0.0397  0.0043  230 PRO A C   
1816 O O   . PRO A 250 ? 0.3633 0.2180 0.2424 -0.0046 0.0395  0.0035  230 PRO A O   
1817 C CB  . PRO A 250 ? 0.4158 0.2379 0.2719 -0.0086 0.0625  0.0065  230 PRO A CB  
1818 C CG  . PRO A 250 ? 0.4382 0.2352 0.2685 -0.0062 0.0719  0.0078  230 PRO A CG  
1819 C CD  . PRO A 250 ? 0.4277 0.2207 0.2460 -0.0011 0.0620  0.0068  230 PRO A CD  
1820 N N   . PHE A 251 ? 0.3423 0.1989 0.2236 -0.0055 0.0335  0.0039  231 PHE A N   
1821 C CA  . PHE A 251 ? 0.3172 0.1938 0.2181 -0.0062 0.0277  0.0028  231 PHE A CA  
1822 C C   . PHE A 251 ? 0.3061 0.1912 0.2182 -0.0084 0.0264  0.0025  231 PHE A C   
1823 O O   . PHE A 251 ? 0.3085 0.1850 0.2127 -0.0084 0.0268  0.0031  231 PHE A O   
1824 C CB  . PHE A 251 ? 0.3263 0.2060 0.2259 -0.0024 0.0180  0.0022  231 PHE A CB  
1825 C CG  . PHE A 251 ? 0.3418 0.2158 0.2341 0.0010  0.0108  0.0025  231 PHE A CG  
1826 C CD1 . PHE A 251 ? 0.3416 0.2259 0.2452 0.0012  0.0073  0.0023  231 PHE A CD1 
1827 C CD2 . PHE A 251 ? 0.3706 0.2279 0.2445 0.0046  0.0069  0.0028  231 PHE A CD2 
1828 C CE1 . PHE A 251 ? 0.3558 0.2359 0.2555 0.0050  0.0010  0.0025  231 PHE A CE1 
1829 C CE2 . PHE A 251 ? 0.3823 0.2350 0.2520 0.0084  -0.0013 0.0028  231 PHE A CE2 
1830 C CZ  . PHE A 251 ? 0.3624 0.2279 0.2469 0.0086  -0.0038 0.0026  231 PHE A CZ  
1831 N N   . LEU A 252 ? 0.2962 0.1962 0.2246 -0.0100 0.0245  0.0014  232 LEU A N   
1832 C CA  . LEU A 252 ? 0.2889 0.1965 0.2268 -0.0114 0.0214  0.0008  232 LEU A CA  
1833 C C   . LEU A 252 ? 0.2894 0.2048 0.2308 -0.0085 0.0152  0.0005  232 LEU A C   
1834 O O   . LEU A 252 ? 0.2828 0.2043 0.2291 -0.0080 0.0141  0.0001  232 LEU A O   
1835 C CB  . LEU A 252 ? 0.2854 0.2011 0.2381 -0.0153 0.0238  -0.0004 232 LEU A CB  
1836 C CG  . LEU A 252 ? 0.2952 0.2162 0.2551 -0.0162 0.0187  -0.0015 232 LEU A CG  
1837 C CD1 . LEU A 252 ? 0.3022 0.2144 0.2545 -0.0170 0.0186  -0.0011 232 LEU A CD1 
1838 C CD2 . LEU A 252 ? 0.2941 0.2226 0.2697 -0.0195 0.0185  -0.0031 232 LEU A CD2 
1839 N N   . LEU A 253 ? 0.2811 0.1956 0.2202 -0.0064 0.0119  0.0007  233 LEU A N   
1840 C CA  . LEU A 253 ? 0.2824 0.2032 0.2258 -0.0036 0.0080  0.0007  233 LEU A CA  
1841 C C   . LEU A 253 ? 0.2765 0.1997 0.2231 -0.0039 0.0076  0.0003  233 LEU A C   
1842 O O   . LEU A 253 ? 0.2820 0.1990 0.2236 -0.0040 0.0081  0.0003  233 LEU A O   
1843 C CB  . LEU A 253 ? 0.3015 0.2170 0.2390 0.0001  0.0050  0.0014  233 LEU A CB  
1844 C CG  . LEU A 253 ? 0.3294 0.2507 0.2741 0.0034  0.0019  0.0016  233 LEU A CG  
1845 C CD1 . LEU A 253 ? 0.3145 0.2441 0.2679 0.0028  0.0008  0.0014  233 LEU A CD1 
1846 C CD2 . LEU A 253 ? 0.3578 0.2733 0.2985 0.0072  -0.0024 0.0019  233 LEU A CD2 
1847 N N   . LEU A 254 ? 0.2626 0.1921 0.2152 -0.0040 0.0068  -0.0001 234 LEU A N   
1848 C CA  . LEU A 254 ? 0.2661 0.1942 0.2176 -0.0037 0.0062  -0.0006 234 LEU A CA  
1849 C C   . LEU A 254 ? 0.2667 0.1969 0.2193 -0.0004 0.0070  0.0002  234 LEU A C   
1850 O O   . LEU A 254 ? 0.2758 0.2116 0.2340 -0.0003 0.0069  0.0006  234 LEU A O   
1851 C CB  . LEU A 254 ? 0.2747 0.2054 0.2306 -0.0061 0.0045  -0.0019 234 LEU A CB  
1852 C CG  . LEU A 254 ? 0.3034 0.2351 0.2645 -0.0096 0.0050  -0.0028 234 LEU A CG  
1853 C CD1 . LEU A 254 ? 0.3100 0.2456 0.2789 -0.0111 0.0020  -0.0043 234 LEU A CD1 
1854 C CD2 . LEU A 254 ? 0.3172 0.2419 0.2745 -0.0115 0.0054  -0.0030 234 LEU A CD2 
1855 N N   . GLN A 255 ? 0.2675 0.1925 0.2153 0.0021  0.0085  0.0006  235 GLN A N   
1856 C CA  . GLN A 255 ? 0.2645 0.1914 0.2157 0.0053  0.0115  0.0016  235 GLN A CA  
1857 C C   . GLN A 255 ? 0.2801 0.1981 0.2223 0.0077  0.0146  0.0017  235 GLN A C   
1858 O O   . GLN A 255 ? 0.2862 0.1964 0.2201 0.0082  0.0138  0.0012  235 GLN A O   
1859 C CB  . GLN A 255 ? 0.2750 0.2043 0.2315 0.0078  0.0112  0.0023  235 GLN A CB  
1860 C CG  . GLN A 255 ? 0.3062 0.2388 0.2713 0.0114  0.0149  0.0033  235 GLN A CG  
1861 C CD  . GLN A 255 ? 0.3198 0.2604 0.2957 0.0101  0.0154  0.0037  235 GLN A CD  
1862 O OE1 . GLN A 255 ? 0.3029 0.2478 0.2824 0.0079  0.0111  0.0033  235 GLN A OE1 
1863 N NE2 . GLN A 255 ? 0.3171 0.2576 0.2964 0.0113  0.0215  0.0046  235 GLN A NE2 
1864 N N   . GLY A 256 ? 0.2798 0.1969 0.2220 0.0092  0.0185  0.0024  236 GLY A N   
1865 C CA  . GLY A 256 ? 0.3155 0.2206 0.2457 0.0123  0.0231  0.0028  236 GLY A CA  
1866 C C   . GLY A 256 ? 0.3244 0.2305 0.2605 0.0163  0.0295  0.0041  236 GLY A C   
1867 O O   . GLY A 256 ? 0.3226 0.2395 0.2744 0.0166  0.0311  0.0049  236 GLY A O   
1868 N N   . SER A 257 ? 0.3311 0.2253 0.2552 0.0197  0.0329  0.0041  237 SER A N   
1869 C CA  . SER A 257 ? 0.3402 0.2353 0.2712 0.0243  0.0395  0.0052  237 SER A CA  
1870 C C   . SER A 257 ? 0.3571 0.2523 0.2942 0.0269  0.0497  0.0069  237 SER A C   
1871 O O   . SER A 257 ? 0.3718 0.2730 0.3234 0.0302  0.0555  0.0079  237 SER A O   
1872 C CB  . SER A 257 ? 0.3709 0.2520 0.2862 0.0276  0.0403  0.0046  237 SER A CB  
1873 O OG  . SER A 257 ? 0.3926 0.2573 0.2895 0.0298  0.0455  0.0047  237 SER A OG  
1874 N N   . ALA A 258 ? 0.3519 0.2394 0.2782 0.0256  0.0522  0.0072  238 ALA A N   
1875 C CA  . ALA A 258 ? 0.3528 0.2371 0.2821 0.0276  0.0637  0.0091  238 ALA A CA  
1876 C C   . ALA A 258 ? 0.3573 0.2526 0.2997 0.0235  0.0624  0.0096  238 ALA A C   
1877 O O   . ALA A 258 ? 0.3822 0.2696 0.3178 0.0234  0.0691  0.0108  238 ALA A O   
1878 C CB  . ALA A 258 ? 0.3882 0.2492 0.2896 0.0304  0.0690  0.0093  238 ALA A CB  
1879 N N   . ASP A 259 ? 0.3306 0.2417 0.2893 0.0202  0.0539  0.0087  239 ASP A N   
1880 C CA  . ASP A 259 ? 0.3182 0.2388 0.2883 0.0163  0.0514  0.0089  239 ASP A CA  
1881 C C   . ASP A 259 ? 0.3340 0.2638 0.3264 0.0168  0.0591  0.0105  239 ASP A C   
1882 O O   . ASP A 259 ? 0.3348 0.2749 0.3451 0.0181  0.0574  0.0102  239 ASP A O   
1883 C CB  . ASP A 259 ? 0.3085 0.2391 0.2845 0.0134  0.0399  0.0073  239 ASP A CB  
1884 C CG  . ASP A 259 ? 0.3131 0.2508 0.2959 0.0095  0.0359  0.0071  239 ASP A CG  
1885 O OD1 . ASP A 259 ? 0.3218 0.2614 0.3130 0.0088  0.0414  0.0083  239 ASP A OD1 
1886 O OD2 . ASP A 259 ? 0.3180 0.2584 0.2978 0.0073  0.0280  0.0058  239 ASP A OD2 
1887 N N   . ARG A 260 ? 0.3373 0.2625 0.3291 0.0158  0.0673  0.0119  240 ARG A N   
1888 C CA  . ARG A 260 ? 0.3536 0.2871 0.3688 0.0153  0.0759  0.0135  240 ARG A CA  
1889 C C   . ARG A 260 ? 0.3541 0.3008 0.3875 0.0105  0.0688  0.0130  240 ARG A C   
1890 O O   . ARG A 260 ? 0.3547 0.3088 0.4101 0.0090  0.0748  0.0140  240 ARG A O   
1891 C CB  . ARG A 260 ? 0.3920 0.3107 0.3959 0.0165  0.0907  0.0157  240 ARG A CB  
1892 C CG  . ARG A 260 ? 0.4868 0.3897 0.4720 0.0220  0.0993  0.0164  240 ARG A CG  
1893 C CD  . ARG A 260 ? 0.5818 0.4793 0.5757 0.0246  0.1177  0.0189  240 ARG A CD  
1894 N NE  . ARG A 260 ? 0.6881 0.5595 0.6494 0.0276  0.1279  0.0203  240 ARG A NE  
1895 C CZ  . ARG A 260 ? 0.7338 0.5934 0.6904 0.0274  0.1425  0.0227  240 ARG A CZ  
1896 N NH1 . ARG A 260 ? 0.7171 0.5909 0.7029 0.0236  0.1487  0.0241  240 ARG A NH1 
1897 N NH2 . ARG A 260 ? 0.7642 0.5959 0.6855 0.0308  0.1503  0.0238  240 ARG A NH2 
1898 N N   . LEU A 261 ? 0.3460 0.2943 0.3705 0.0080  0.0571  0.0113  241 LEU A N   
1899 C CA  . LEU A 261 ? 0.3470 0.3045 0.3838 0.0039  0.0500  0.0106  241 LEU A CA  
1900 C C   . LEU A 261 ? 0.3506 0.3178 0.3973 0.0037  0.0383  0.0088  241 LEU A C   
1901 O O   . LEU A 261 ? 0.3683 0.3444 0.4341 0.0020  0.0340  0.0084  241 LEU A O   
1902 C CB  . LEU A 261 ? 0.3497 0.2995 0.3684 0.0016  0.0472  0.0104  241 LEU A CB  
1903 C CG  . LEU A 261 ? 0.3745 0.3112 0.3807 0.0021  0.0578  0.0122  241 LEU A CG  
1904 C CD1 . LEU A 261 ? 0.3824 0.3107 0.3702 0.0009  0.0530  0.0116  241 LEU A CD1 
1905 C CD2 . LEU A 261 ? 0.3775 0.3179 0.4025 0.0000  0.0670  0.0140  241 LEU A CD2 
1906 N N   . CYS A 262 ? 0.3360 0.2997 0.3687 0.0054  0.0328  0.0078  242 CYS A N   
1907 C CA  . CYS A 262 ? 0.3370 0.3055 0.3735 0.0060  0.0231  0.0063  242 CYS A CA  
1908 C C   . CYS A 262 ? 0.3487 0.3147 0.3829 0.0100  0.0253  0.0064  242 CYS A C   
1909 O O   . CYS A 262 ? 0.3570 0.3148 0.3739 0.0111  0.0269  0.0063  242 CYS A O   
1910 C CB  . CYS A 262 ? 0.3512 0.3160 0.3724 0.0041  0.0163  0.0051  242 CYS A CB  
1911 S SG  . CYS A 262 ? 0.3612 0.3280 0.3848 0.0002  0.0128  0.0047  242 CYS A SG  
1912 N N   . ASP A 263 ? 0.3352 0.3080 0.3883 0.0125  0.0252  0.0065  243 ASP A N   
1913 C CA  . ASP A 263 ? 0.3412 0.3119 0.3949 0.0172  0.0280  0.0067  243 ASP A CA  
1914 C C   . ASP A 263 ? 0.3330 0.2972 0.3696 0.0184  0.0211  0.0057  243 ASP A C   
1915 O O   . ASP A 263 ? 0.3230 0.2880 0.3576 0.0171  0.0118  0.0046  243 ASP A O   
1916 C CB  . ASP A 263 ? 0.3570 0.3377 0.4376 0.0198  0.0268  0.0066  243 ASP A CB  
1917 C CG  . ASP A 263 ? 0.4413 0.4193 0.5243 0.0251  0.0352  0.0074  243 ASP A CG  
1918 O OD1 . ASP A 263 ? 0.4785 0.4556 0.5671 0.0259  0.0480  0.0089  243 ASP A OD1 
1919 O OD2 . ASP A 263 ? 0.4425 0.4168 0.5184 0.0286  0.0302  0.0066  243 ASP A OD2 
1920 N N   . SER A 264 ? 0.3372 0.2927 0.3594 0.0207  0.0262  0.0060  244 SER A N   
1921 C CA  . SER A 264 ? 0.3522 0.3000 0.3579 0.0212  0.0210  0.0052  244 SER A CA  
1922 C C   . SER A 264 ? 0.3452 0.2949 0.3574 0.0240  0.0134  0.0045  244 SER A C   
1923 O O   . SER A 264 ? 0.3468 0.2903 0.3459 0.0232  0.0077  0.0038  244 SER A O   
1924 C CB  . SER A 264 ? 0.3884 0.3256 0.3795 0.0235  0.0273  0.0055  244 SER A CB  
1925 O OG  . SER A 264 ? 0.4001 0.3380 0.4008 0.0288  0.0321  0.0061  244 SER A OG  
1926 N N   . LYS A 265 ? 0.3322 0.2896 0.3649 0.0274  0.0131  0.0046  245 LYS A N   
1927 C CA  . LYS A 265 ? 0.3342 0.2926 0.3743 0.0309  0.0036  0.0036  245 LYS A CA  
1928 C C   . LYS A 265 ? 0.3246 0.2813 0.3583 0.0277  -0.0069 0.0026  245 LYS A C   
1929 O O   . LYS A 265 ? 0.3319 0.2813 0.3567 0.0299  -0.0151 0.0018  245 LYS A O   
1930 C CB  . LYS A 265 ? 0.3706 0.3401 0.4397 0.0344  0.0042  0.0036  245 LYS A CB  
1931 C CG  . LYS A 265 ? 0.4743 0.4447 0.5533 0.0389  -0.0076 0.0023  245 LYS A CG  
1932 C CD  . LYS A 265 ? 0.5609 0.5446 0.6746 0.0420  -0.0076 0.0020  245 LYS A CD  
1933 C CE  . LYS A 265 ? 0.6371 0.6206 0.7612 0.0476  -0.0212 0.0003  245 LYS A CE  
1934 N NZ  . LYS A 265 ? 0.6910 0.6661 0.7994 0.0457  -0.0359 -0.0011 245 LYS A NZ  
1935 N N   . GLY A 266 ? 0.3080 0.2689 0.3438 0.0230  -0.0060 0.0027  246 GLY A N   
1936 C CA  . GLY A 266 ? 0.3107 0.2683 0.3383 0.0202  -0.0142 0.0017  246 GLY A CA  
1937 C C   . GLY A 266 ? 0.3103 0.2567 0.3139 0.0190  -0.0142 0.0017  246 GLY A C   
1938 O O   . GLY A 266 ? 0.3159 0.2543 0.3088 0.0194  -0.0211 0.0010  246 GLY A O   
1939 N N   . ALA A 267 ? 0.3026 0.2467 0.2970 0.0174  -0.0064 0.0024  247 ALA A N   
1940 C CA  . ALA A 267 ? 0.3156 0.2503 0.2912 0.0155  -0.0057 0.0023  247 ALA A CA  
1941 C C   . ALA A 267 ? 0.3258 0.2510 0.2924 0.0191  -0.0093 0.0022  247 ALA A C   
1942 O O   . ALA A 267 ? 0.3305 0.2462 0.2832 0.0182  -0.0119 0.0021  247 ALA A O   
1943 C CB  . ALA A 267 ? 0.3268 0.2607 0.2971 0.0135  0.0013  0.0027  247 ALA A CB  
1944 N N   . TYR A 268 ? 0.3280 0.2544 0.3018 0.0235  -0.0088 0.0024  248 TYR A N   
1945 C CA  . TYR A 268 ? 0.3370 0.2534 0.3019 0.0277  -0.0129 0.0023  248 TYR A CA  
1946 C C   . TYR A 268 ? 0.3532 0.2657 0.3181 0.0301  -0.0232 0.0016  248 TYR A C   
1947 O O   . TYR A 268 ? 0.3648 0.2636 0.3127 0.0316  -0.0272 0.0015  248 TYR A O   
1948 C CB  . TYR A 268 ? 0.3286 0.2475 0.3028 0.0327  -0.0098 0.0026  248 TYR A CB  
1949 C CG  . TYR A 268 ? 0.3458 0.2624 0.3132 0.0312  -0.0007 0.0032  248 TYR A CG  
1950 C CD1 . TYR A 268 ? 0.3789 0.2838 0.3277 0.0296  0.0007  0.0032  248 TYR A CD1 
1951 C CD2 . TYR A 268 ? 0.3547 0.2788 0.3331 0.0315  0.0062  0.0037  248 TYR A CD2 
1952 C CE1 . TYR A 268 ? 0.3896 0.2904 0.3312 0.0283  0.0069  0.0033  248 TYR A CE1 
1953 C CE2 . TYR A 268 ? 0.3686 0.2868 0.3367 0.0308  0.0134  0.0040  248 TYR A CE2 
1954 C CZ  . TYR A 268 ? 0.3877 0.2942 0.3375 0.0294  0.0127  0.0036  248 TYR A CZ  
1955 O OH  . TYR A 268 ? 0.4054 0.3040 0.3439 0.0288  0.0177  0.0035  248 TYR A OH  
1956 N N   . LEU A 269 ? 0.3502 0.2726 0.3324 0.0302  -0.0277 0.0009  249 LEU A N   
1957 C CA  . LEU A 269 ? 0.3642 0.2814 0.3460 0.0325  -0.0395 -0.0002 249 LEU A CA  
1958 C C   . LEU A 269 ? 0.3576 0.2622 0.3169 0.0293  -0.0409 -0.0003 249 LEU A C   
1959 O O   . LEU A 269 ? 0.3730 0.2624 0.3161 0.0321  -0.0484 -0.0008 249 LEU A O   
1960 C CB  . LEU A 269 ? 0.3832 0.3144 0.3903 0.0319  -0.0434 -0.0010 249 LEU A CB  
1961 C CG  . LEU A 269 ? 0.4400 0.3664 0.4504 0.0343  -0.0581 -0.0028 249 LEU A CG  
1962 C CD1 . LEU A 269 ? 0.4565 0.3827 0.4791 0.0411  -0.0665 -0.0037 249 LEU A CD1 
1963 C CD2 . LEU A 269 ? 0.4512 0.3895 0.4819 0.0308  -0.0604 -0.0035 249 LEU A CD2 
1964 N N   . LEU A 270 ? 0.3431 0.2522 0.3000 0.0239  -0.0331 0.0002  250 LEU A N   
1965 C CA  . LEU A 270 ? 0.3543 0.2528 0.2927 0.0210  -0.0320 0.0003  250 LEU A CA  
1966 C C   . LEU A 270 ? 0.3633 0.2468 0.2809 0.0215  -0.0285 0.0010  250 LEU A C   
1967 O O   . LEU A 270 ? 0.3861 0.2533 0.2846 0.0225  -0.0313 0.0010  250 LEU A O   
1968 C CB  . LEU A 270 ? 0.3560 0.2647 0.3005 0.0159  -0.0243 0.0006  250 LEU A CB  
1969 C CG  . LEU A 270 ? 0.3925 0.2933 0.3221 0.0126  -0.0199 0.0007  250 LEU A CG  
1970 C CD1 . LEU A 270 ? 0.4145 0.3029 0.3315 0.0141  -0.0263 0.0001  250 LEU A CD1 
1971 C CD2 . LEU A 270 ? 0.3801 0.2927 0.3200 0.0086  -0.0143 0.0008  250 LEU A CD2 
1972 N N   . MET A 271 ? 0.3559 0.2422 0.2752 0.0209  -0.0222 0.0018  251 MET A N   
1973 C CA  . MET A 271 ? 0.3725 0.2439 0.2734 0.0209  -0.0188 0.0025  251 MET A CA  
1974 C C   . MET A 271 ? 0.4016 0.2577 0.2895 0.0264  -0.0267 0.0024  251 MET A C   
1975 O O   . MET A 271 ? 0.4249 0.2630 0.2914 0.0264  -0.0252 0.0030  251 MET A O   
1976 C CB  . MET A 271 ? 0.3780 0.2536 0.2831 0.0200  -0.0129 0.0029  251 MET A CB  
1977 C CG  . MET A 271 ? 0.4013 0.2854 0.3121 0.0145  -0.0058 0.0029  251 MET A CG  
1978 S SD  . MET A 271 ? 0.3985 0.2736 0.2969 0.0091  -0.0002 0.0033  251 MET A SD  
1979 C CE  . MET A 271 ? 0.4077 0.2678 0.2920 0.0084  0.0035  0.0040  251 MET A CE  
1980 N N   . GLU A 272 ? 0.3841 0.2464 0.2852 0.0315  -0.0347 0.0016  252 GLU A N   
1981 C CA  . GLU A 272 ? 0.4055 0.2537 0.2966 0.0378  -0.0443 0.0012  252 GLU A CA  
1982 C C   . GLU A 272 ? 0.4223 0.2572 0.3002 0.0396  -0.0538 0.0003  252 GLU A C   
1983 O O   . GLU A 272 ? 0.4530 0.2659 0.3069 0.0430  -0.0582 0.0005  252 GLU A O   
1984 C CB  . GLU A 272 ? 0.4190 0.2796 0.3328 0.0430  -0.0498 0.0004  252 GLU A CB  
1985 C CG  . GLU A 272 ? 0.5230 0.3691 0.4279 0.0505  -0.0604 -0.0002 252 GLU A CG  
1986 C CD  . GLU A 272 ? 0.6454 0.5046 0.5773 0.0564  -0.0677 -0.0014 252 GLU A CD  
1987 O OE1 . GLU A 272 ? 0.6532 0.5328 0.6114 0.0543  -0.0637 -0.0016 252 GLU A OE1 
1988 O OE2 . GLU A 272 ? 0.6981 0.5464 0.6252 0.0634  -0.0774 -0.0022 252 GLU A OE2 
1989 N N   . LEU A 273 ? 0.4109 0.2565 0.3021 0.0377  -0.0574 -0.0007 253 LEU A N   
1990 C CA  . LEU A 273 ? 0.4365 0.2682 0.3156 0.0403  -0.0689 -0.0020 253 LEU A CA  
1991 C C   . LEU A 273 ? 0.4519 0.2687 0.3069 0.0369  -0.0636 -0.0015 253 LEU A C   
1992 O O   . LEU A 273 ? 0.4831 0.2792 0.3170 0.0402  -0.0722 -0.0023 253 LEU A O   
1993 C CB  . LEU A 273 ? 0.4457 0.2938 0.3518 0.0408  -0.0781 -0.0037 253 LEU A CB  
1994 C CG  . LEU A 273 ? 0.4793 0.3405 0.4117 0.0454  -0.0849 -0.0045 253 LEU A CG  
1995 C CD1 . LEU A 273 ? 0.4905 0.3661 0.4502 0.0450  -0.0939 -0.0063 253 LEU A CD1 
1996 C CD2 . LEU A 273 ? 0.5088 0.3517 0.4266 0.0528  -0.0960 -0.0052 253 LEU A CD2 
1997 N N   . ALA A 274 ? 0.4353 0.2605 0.2924 0.0309  -0.0500 -0.0003 254 ALA A N   
1998 C CA  . ALA A 274 ? 0.4514 0.2627 0.2877 0.0282  -0.0433 0.0003  254 ALA A CA  
1999 C C   . ALA A 274 ? 0.4833 0.2675 0.2887 0.0305  -0.0406 0.0014  254 ALA A C   
2000 O O   . ALA A 274 ? 0.4869 0.2685 0.2901 0.0314  -0.0381 0.0023  254 ALA A O   
2001 C CB  . ALA A 274 ? 0.4380 0.2643 0.2858 0.0219  -0.0300 0.0012  254 ALA A CB  
2002 N N   . LYS A 275 ? 0.5030 0.2653 0.2829 0.0315  -0.0402 0.0014  255 LYS A N   
2003 C CA  . LYS A 275 ? 0.5420 0.2749 0.2890 0.0337  -0.0357 0.0028  255 LYS A CA  
2004 C C   . LYS A 275 ? 0.5282 0.2593 0.2704 0.0280  -0.0169 0.0048  255 LYS A C   
2005 O O   . LYS A 275 ? 0.5466 0.2549 0.2647 0.0286  -0.0101 0.0064  255 LYS A O   
2006 C CB  . LYS A 275 ? 0.6235 0.3276 0.3403 0.0388  -0.0447 0.0020  255 LYS A CB  
2007 C CG  . LYS A 275 ? 0.7174 0.4214 0.4402 0.0448  -0.0654 -0.0003 255 LYS A CG  
2008 C CD  . LYS A 275 ? 0.7988 0.4958 0.5180 0.0497  -0.0726 -0.0001 255 LYS A CD  
2009 C CE  . LYS A 275 ? 0.8522 0.5553 0.5870 0.0554  -0.0931 -0.0027 255 LYS A CE  
2010 N NZ  . LYS A 275 ? 0.8563 0.5963 0.6348 0.0525  -0.0928 -0.0033 255 LYS A NZ  
2011 N N   . SER A 276 ? 0.4872 0.2421 0.2536 0.0224  -0.0089 0.0047  256 SER A N   
2012 C CA  . SER A 276 ? 0.4731 0.2311 0.2428 0.0166  0.0074  0.0061  256 SER A CA  
2013 C C   . SER A 276 ? 0.4762 0.2253 0.2388 0.0148  0.0149  0.0077  256 SER A C   
2014 O O   . SER A 276 ? 0.4838 0.2425 0.2575 0.0154  0.0097  0.0074  256 SER A O   
2015 C CB  . SER A 276 ? 0.4475 0.2358 0.2493 0.0120  0.0099  0.0053  256 SER A CB  
2016 O OG  . SER A 276 ? 0.4753 0.2718 0.2841 0.0132  0.0033  0.0040  256 SER A OG  
2017 N N   . GLN A 277 ? 0.4787 0.2088 0.2232 0.0127  0.0278  0.0093  257 GLN A N   
2018 C CA  . GLN A 277 ? 0.5006 0.2220 0.2401 0.0097  0.0366  0.0109  257 GLN A CA  
2019 C C   . GLN A 277 ? 0.4853 0.2320 0.2555 0.0027  0.0436  0.0106  257 GLN A C   
2020 O O   . GLN A 277 ? 0.4942 0.2387 0.2660 0.0001  0.0472  0.0113  257 GLN A O   
2021 C CB  . GLN A 277 ? 0.5437 0.2357 0.2550 0.0092  0.0500  0.0129  257 GLN A CB  
2022 C CG  . GLN A 277 ? 0.6228 0.2823 0.2967 0.0166  0.0423  0.0133  257 GLN A CG  
2023 C CD  . GLN A 277 ? 0.7079 0.3585 0.3729 0.0197  0.0340  0.0136  257 GLN A CD  
2024 O OE1 . GLN A 277 ? 0.7263 0.3757 0.3941 0.0158  0.0423  0.0149  257 GLN A OE1 
2025 N NE2 . GLN A 277 ? 0.7341 0.3774 0.3884 0.0271  0.0170  0.0123  257 GLN A NE2 
2026 N N   . ASP A 278 ? 0.4578 0.2267 0.2511 0.0001  0.0443  0.0094  258 ASP A N   
2027 C CA  . ASP A 278 ? 0.4269 0.2177 0.2479 -0.0059 0.0489  0.0088  258 ASP A CA  
2028 C C   . ASP A 278 ? 0.3928 0.2070 0.2341 -0.0046 0.0382  0.0071  258 ASP A C   
2029 O O   . ASP A 278 ? 0.3873 0.2124 0.2384 -0.0047 0.0373  0.0062  258 ASP A O   
2030 C CB  . ASP A 278 ? 0.4507 0.2434 0.2796 -0.0102 0.0619  0.0092  258 ASP A CB  
2031 C CG  . ASP A 278 ? 0.4617 0.2761 0.3206 -0.0161 0.0654  0.0081  258 ASP A CG  
2032 O OD1 . ASP A 278 ? 0.4514 0.2761 0.3214 -0.0175 0.0589  0.0073  258 ASP A OD1 
2033 O OD2 . ASP A 278 ? 0.4887 0.3086 0.3596 -0.0190 0.0744  0.0080  258 ASP A OD2 
2034 N N   . LYS A 279 ? 0.3773 0.1969 0.2230 -0.0032 0.0309  0.0067  259 LYS A N   
2035 C CA  . LYS A 279 ? 0.3711 0.2100 0.2341 -0.0016 0.0225  0.0054  259 LYS A CA  
2036 C C   . LYS A 279 ? 0.3461 0.1936 0.2204 -0.0038 0.0220  0.0049  259 LYS A C   
2037 O O   . LYS A 279 ? 0.3511 0.1881 0.2162 -0.0033 0.0223  0.0055  259 LYS A O   
2038 C CB  . LYS A 279 ? 0.4076 0.2435 0.2640 0.0045  0.0121  0.0050  259 LYS A CB  
2039 C CG  . LYS A 279 ? 0.4519 0.2690 0.2889 0.0089  0.0082  0.0058  259 LYS A CG  
2040 C CD  . LYS A 279 ? 0.4650 0.2808 0.2998 0.0151  -0.0038 0.0049  259 LYS A CD  
2041 C CE  . LYS A 279 ? 0.4704 0.2657 0.2851 0.0202  -0.0090 0.0054  259 LYS A CE  
2042 N NZ  . LYS A 279 ? 0.4475 0.2433 0.2650 0.0266  -0.0226 0.0042  259 LYS A NZ  
2043 N N   . THR A 280 ? 0.3325 0.1972 0.2249 -0.0059 0.0209  0.0039  260 THR A N   
2044 C CA  . THR A 280 ? 0.3276 0.1988 0.2291 -0.0079 0.0199  0.0031  260 THR A CA  
2045 C C   . THR A 280 ? 0.3161 0.2005 0.2280 -0.0054 0.0145  0.0023  260 THR A C   
2046 O O   . THR A 280 ? 0.3144 0.2076 0.2339 -0.0056 0.0138  0.0019  260 THR A O   
2047 C CB  . THR A 280 ? 0.3579 0.2333 0.2701 -0.0139 0.0252  0.0025  260 THR A CB  
2048 O OG1 . THR A 280 ? 0.3828 0.2454 0.2866 -0.0166 0.0326  0.0035  260 THR A OG1 
2049 C CG2 . THR A 280 ? 0.3780 0.2571 0.2977 -0.0162 0.0224  0.0013  260 THR A CG2 
2050 N N   . LEU A 281 ? 0.2971 0.1814 0.2087 -0.0032 0.0117  0.0021  261 LEU A N   
2051 C CA  . LEU A 281 ? 0.2948 0.1889 0.2147 -0.0008 0.0088  0.0016  261 LEU A CA  
2052 C C   . LEU A 281 ? 0.3054 0.1989 0.2266 -0.0028 0.0091  0.0007  261 LEU A C   
2053 O O   . LEU A 281 ? 0.3112 0.1955 0.2251 -0.0032 0.0095  0.0007  261 LEU A O   
2054 C CB  . LEU A 281 ? 0.3115 0.2036 0.2289 0.0049  0.0060  0.0022  261 LEU A CB  
2055 C CG  . LEU A 281 ? 0.3258 0.2251 0.2510 0.0079  0.0058  0.0020  261 LEU A CG  
2056 C CD1 . LEU A 281 ? 0.3339 0.2445 0.2698 0.0069  0.0055  0.0019  261 LEU A CD1 
2057 C CD2 . LEU A 281 ? 0.3472 0.2446 0.2730 0.0137  0.0040  0.0026  261 LEU A CD2 
2058 N N   . LYS A 282 ? 0.2994 0.2006 0.2279 -0.0035 0.0081  0.0000  262 LYS A N   
2059 C CA  . LYS A 282 ? 0.3119 0.2095 0.2382 -0.0042 0.0067  -0.0011 262 LYS A CA  
2060 C C   . LYS A 282 ? 0.3117 0.2122 0.2381 0.0000  0.0068  -0.0008 262 LYS A C   
2061 O O   . LYS A 282 ? 0.3003 0.2091 0.2337 0.0003  0.0071  -0.0004 262 LYS A O   
2062 C CB  . LYS A 282 ? 0.3363 0.2365 0.2694 -0.0090 0.0049  -0.0026 262 LYS A CB  
2063 C CG  . LYS A 282 ? 0.4147 0.3079 0.3433 -0.0096 0.0010  -0.0041 262 LYS A CG  
2064 C CD  . LYS A 282 ? 0.4697 0.3653 0.4084 -0.0148 -0.0024 -0.0059 262 LYS A CD  
2065 C CE  . LYS A 282 ? 0.5151 0.4020 0.4484 -0.0151 -0.0090 -0.0079 262 LYS A CE  
2066 N NZ  . LYS A 282 ? 0.5374 0.4125 0.4623 -0.0165 -0.0096 -0.0083 262 LYS A NZ  
2067 N N   . ILE A 283 ? 0.3138 0.2065 0.2322 0.0033  0.0077  -0.0006 263 ILE A N   
2068 C CA  . ILE A 283 ? 0.3172 0.2098 0.2345 0.0076  0.0103  -0.0001 263 ILE A CA  
2069 C C   . ILE A 283 ? 0.3332 0.2170 0.2412 0.0070  0.0089  -0.0013 263 ILE A C   
2070 O O   . ILE A 283 ? 0.3393 0.2130 0.2386 0.0056  0.0060  -0.0025 263 ILE A O   
2071 C CB  . ILE A 283 ? 0.3287 0.2167 0.2427 0.0128  0.0135  0.0008  263 ILE A CB  
2072 C CG1 . ILE A 283 ? 0.3325 0.2282 0.2559 0.0144  0.0128  0.0018  263 ILE A CG1 
2073 C CG2 . ILE A 283 ? 0.3314 0.2161 0.2429 0.0173  0.0188  0.0014  263 ILE A CG2 
2074 C CD1 . ILE A 283 ? 0.3442 0.2519 0.2814 0.0155  0.0140  0.0025  263 ILE A CD1 
2075 N N   . TYR A 284 ? 0.3254 0.2110 0.2339 0.0082  0.0103  -0.0010 264 TYR A N   
2076 C CA  . TYR A 284 ? 0.3351 0.2088 0.2309 0.0088  0.0083  -0.0021 264 TYR A CA  
2077 C C   . TYR A 284 ? 0.3492 0.2133 0.2346 0.0144  0.0153  -0.0009 264 TYR A C   
2078 O O   . TYR A 284 ? 0.3480 0.2174 0.2391 0.0164  0.0212  0.0006  264 TYR A O   
2079 C CB  . TYR A 284 ? 0.3309 0.2101 0.2317 0.0066  0.0050  -0.0027 264 TYR A CB  
2080 C CG  . TYR A 284 ? 0.3309 0.2169 0.2413 0.0016  -0.0013 -0.0042 264 TYR A CG  
2081 C CD1 . TYR A 284 ? 0.3543 0.2321 0.2602 -0.0005 -0.0084 -0.0064 264 TYR A CD1 
2082 C CD2 . TYR A 284 ? 0.3279 0.2272 0.2522 -0.0007 0.0001  -0.0036 264 TYR A CD2 
2083 C CE1 . TYR A 284 ? 0.3614 0.2466 0.2804 -0.0053 -0.0129 -0.0078 264 TYR A CE1 
2084 C CE2 . TYR A 284 ? 0.3266 0.2312 0.2601 -0.0050 -0.0032 -0.0048 264 TYR A CE2 
2085 C CZ  . TYR A 284 ? 0.3559 0.2546 0.2887 -0.0074 -0.0092 -0.0068 264 TYR A CZ  
2086 O OH  . TYR A 284 ? 0.3698 0.2750 0.3159 -0.0119 -0.0112 -0.0080 264 TYR A OH  
2087 N N   . GLU A 285 ? 0.3655 0.2147 0.2362 0.0168  0.0155  -0.0015 265 GLU A N   
2088 C CA  . GLU A 285 ? 0.3846 0.2226 0.2443 0.0227  0.0238  -0.0004 265 GLU A CA  
2089 C C   . GLU A 285 ? 0.4044 0.2318 0.2520 0.0250  0.0275  0.0001  265 GLU A C   
2090 O O   . GLU A 285 ? 0.4335 0.2474 0.2655 0.0241  0.0211  -0.0016 265 GLU A O   
2091 C CB  . GLU A 285 ? 0.4338 0.2556 0.2775 0.0247  0.0224  -0.0014 265 GLU A CB  
2092 C CG  . GLU A 285 ? 0.4814 0.2936 0.3171 0.0317  0.0327  0.0000  265 GLU A CG  
2093 C CD  . GLU A 285 ? 0.5194 0.3474 0.3751 0.0342  0.0390  0.0018  265 GLU A CD  
2094 O OE1 . GLU A 285 ? 0.4668 0.3103 0.3388 0.0308  0.0341  0.0018  265 GLU A OE1 
2095 O OE2 . GLU A 285 ? 0.5727 0.3964 0.4278 0.0401  0.0490  0.0031  265 GLU A OE2 
2096 N N   . GLY A 286 ? 0.3874 0.2203 0.2427 0.0279  0.0375  0.0022  266 GLY A N   
2097 C CA  . GLY A 286 ? 0.3986 0.2201 0.2421 0.0303  0.0442  0.0033  266 GLY A CA  
2098 C C   . GLY A 286 ? 0.3955 0.2254 0.2461 0.0267  0.0405  0.0033  266 GLY A C   
2099 O O   . GLY A 286 ? 0.4107 0.2309 0.2515 0.0285  0.0465  0.0045  266 GLY A O   
2100 N N   . ALA A 287 ? 0.3648 0.2104 0.2303 0.0218  0.0313  0.0021  267 ALA A N   
2101 C CA  . ALA A 287 ? 0.3591 0.2122 0.2310 0.0187  0.0273  0.0020  267 ALA A CA  
2102 C C   . ALA A 287 ? 0.3477 0.2138 0.2360 0.0184  0.0348  0.0040  267 ALA A C   
2103 O O   . ALA A 287 ? 0.3337 0.2104 0.2368 0.0191  0.0397  0.0051  267 ALA A O   
2104 C CB  . ALA A 287 ? 0.3440 0.2081 0.2263 0.0140  0.0168  0.0000  267 ALA A CB  
2105 N N   . TYR A 288 ? 0.3455 0.2103 0.2317 0.0173  0.0347  0.0044  268 TYR A N   
2106 C CA  . TYR A 288 ? 0.3394 0.2149 0.2407 0.0163  0.0412  0.0062  268 TYR A CA  
2107 C C   . TYR A 288 ? 0.3365 0.2307 0.2566 0.0121  0.0341  0.0054  268 TYR A C   
2108 O O   . TYR A 288 ? 0.3533 0.2542 0.2786 0.0107  0.0279  0.0042  268 TYR A O   
2109 C CB  . TYR A 288 ? 0.3539 0.2152 0.2408 0.0175  0.0463  0.0074  268 TYR A CB  
2110 C CG  . TYR A 288 ? 0.3853 0.2268 0.2539 0.0221  0.0575  0.0089  268 TYR A CG  
2111 C CD1 . TYR A 288 ? 0.4061 0.2430 0.2713 0.0252  0.0617  0.0090  268 TYR A CD1 
2112 C CD2 . TYR A 288 ? 0.4173 0.2426 0.2702 0.0237  0.0646  0.0104  268 TYR A CD2 
2113 C CE1 . TYR A 288 ? 0.4364 0.2528 0.2827 0.0301  0.0732  0.0104  268 TYR A CE1 
2114 C CE2 . TYR A 288 ? 0.4483 0.2518 0.2809 0.0283  0.0764  0.0120  268 TYR A CE2 
2115 C CZ  . TYR A 288 ? 0.4688 0.2681 0.2985 0.0316  0.0811  0.0120  268 TYR A CZ  
2116 O OH  . TYR A 288 ? 0.5211 0.2969 0.3291 0.0369  0.0943  0.0136  268 TYR A OH  
2117 N N   . HIS A 289 ? 0.3129 0.2134 0.2418 0.0103  0.0358  0.0063  269 HIS A N   
2118 C CA  . HIS A 289 ? 0.2975 0.2133 0.2425 0.0070  0.0302  0.0057  269 HIS A CA  
2119 C C   . HIS A 289 ? 0.2977 0.2149 0.2392 0.0050  0.0214  0.0039  269 HIS A C   
2120 O O   . HIS A 289 ? 0.3109 0.2373 0.2609 0.0032  0.0168  0.0029  269 HIS A O   
2121 C CB  . HIS A 289 ? 0.3045 0.2248 0.2597 0.0058  0.0353  0.0072  269 HIS A CB  
2122 C CG  . HIS A 289 ? 0.2924 0.2257 0.2623 0.0028  0.0298  0.0065  269 HIS A CG  
2123 N ND1 . HIS A 289 ? 0.2996 0.2422 0.2808 0.0025  0.0262  0.0059  269 HIS A ND1 
2124 C CD2 . HIS A 289 ? 0.3072 0.2428 0.2797 0.0006  0.0275  0.0064  269 HIS A CD2 
2125 C CE1 . HIS A 289 ? 0.3167 0.2660 0.3057 0.0002  0.0216  0.0054  269 HIS A CE1 
2126 N NE2 . HIS A 289 ? 0.3159 0.2618 0.3007 -0.0011 0.0225  0.0056  269 HIS A NE2 
2127 N N   . VAL A 290 ? 0.2963 0.2041 0.2261 0.0055  0.0195  0.0034  270 VAL A N   
2128 C CA  . VAL A 290 ? 0.3002 0.2112 0.2313 0.0040  0.0116  0.0017  270 VAL A CA  
2129 C C   . VAL A 290 ? 0.3043 0.2107 0.2296 0.0043  0.0052  -0.0003 270 VAL A C   
2130 O O   . VAL A 290 ? 0.3168 0.2114 0.2296 0.0059  0.0008  -0.0013 270 VAL A O   
2131 C CB  . VAL A 290 ? 0.3108 0.2144 0.2343 0.0048  0.0112  0.0020  270 VAL A CB  
2132 C CG1 . VAL A 290 ? 0.3167 0.2263 0.2459 0.0037  0.0035  0.0002  270 VAL A CG1 
2133 C CG2 . VAL A 290 ? 0.3159 0.2225 0.2455 0.0039  0.0187  0.0041  270 VAL A CG2 
2134 N N   . LEU A 291 ? 0.2964 0.2106 0.2302 0.0026  0.0041  -0.0008 271 LEU A N   
2135 C CA  . LEU A 291 ? 0.3022 0.2119 0.2322 0.0021  -0.0009 -0.0025 271 LEU A CA  
2136 C C   . LEU A 291 ? 0.3055 0.2149 0.2380 0.0010  -0.0090 -0.0047 271 LEU A C   
2137 O O   . LEU A 291 ? 0.3245 0.2249 0.2502 0.0013  -0.0148 -0.0064 271 LEU A O   
2138 C CB  . LEU A 291 ? 0.2968 0.2139 0.2351 0.0003  0.0004  -0.0024 271 LEU A CB  
2139 C CG  . LEU A 291 ? 0.3043 0.2216 0.2420 0.0022  0.0066  -0.0007 271 LEU A CG  
2140 C CD1 . LEU A 291 ? 0.3049 0.2277 0.2489 0.0008  0.0064  -0.0007 271 LEU A CD1 
2141 C CD2 . LEU A 291 ? 0.3229 0.2269 0.2467 0.0051  0.0088  -0.0005 271 LEU A CD2 
2142 N N   . HIS A 292 ? 0.2927 0.2110 0.2352 0.0000  -0.0099 -0.0049 272 HIS A N   
2143 C CA  . HIS A 292 ? 0.2903 0.2099 0.2389 -0.0006 -0.0173 -0.0071 272 HIS A CA  
2144 C C   . HIS A 292 ? 0.3115 0.2189 0.2474 0.0026  -0.0226 -0.0078 272 HIS A C   
2145 O O   . HIS A 292 ? 0.3326 0.2402 0.2737 0.0031  -0.0303 -0.0098 272 HIS A O   
2146 C CB  . HIS A 292 ? 0.2821 0.2147 0.2460 -0.0023 -0.0155 -0.0072 272 HIS A CB  
2147 C CG  . HIS A 292 ? 0.2973 0.2320 0.2591 -0.0013 -0.0109 -0.0055 272 HIS A CG  
2148 N ND1 . HIS A 292 ? 0.3123 0.2481 0.2716 -0.0016 -0.0050 -0.0036 272 HIS A ND1 
2149 C CD2 . HIS A 292 ? 0.3118 0.2475 0.2749 -0.0002 -0.0121 -0.0057 272 HIS A CD2 
2150 C CE1 . HIS A 292 ? 0.3153 0.2528 0.2753 -0.0012 -0.0030 -0.0027 272 HIS A CE1 
2151 N NE2 . HIS A 292 ? 0.3235 0.2603 0.2844 -0.0003 -0.0068 -0.0038 272 HIS A NE2 
2152 N N   . LYS A 293 ? 0.3144 0.2103 0.2339 0.0050  -0.0182 -0.0061 273 LYS A N   
2153 C CA  . LYS A 293 ? 0.3312 0.2101 0.2325 0.0085  -0.0217 -0.0063 273 LYS A CA  
2154 C C   . LYS A 293 ? 0.3573 0.2191 0.2383 0.0109  -0.0174 -0.0052 273 LYS A C   
2155 O O   . LYS A 293 ? 0.3807 0.2292 0.2457 0.0135  -0.0120 -0.0035 273 LYS A O   
2156 C CB  . LYS A 293 ? 0.3405 0.2208 0.2414 0.0092  -0.0171 -0.0046 273 LYS A CB  
2157 C CG  . LYS A 293 ? 0.3242 0.2184 0.2423 0.0078  -0.0213 -0.0059 273 LYS A CG  
2158 C CD  . LYS A 293 ? 0.3692 0.2618 0.2845 0.0088  -0.0185 -0.0046 273 LYS A CD  
2159 C CE  . LYS A 293 ? 0.3850 0.2910 0.3168 0.0077  -0.0211 -0.0058 273 LYS A CE  
2160 N NZ  . LYS A 293 ? 0.3779 0.2845 0.3161 0.0093  -0.0312 -0.0086 273 LYS A NZ  
2161 N N   . GLU A 294 ? 0.3545 0.2163 0.2363 0.0099  -0.0184 -0.0060 274 GLU A N   
2162 C CA  . GLU A 294 ? 0.3709 0.2169 0.2343 0.0125  -0.0138 -0.0051 274 GLU A CA  
2163 C C   . GLU A 294 ? 0.4030 0.2291 0.2479 0.0147  -0.0246 -0.0077 274 GLU A C   
2164 O O   . GLU A 294 ? 0.4156 0.2386 0.2606 0.0151  -0.0352 -0.0098 274 GLU A O   
2165 C CB  . GLU A 294 ? 0.3690 0.2265 0.2442 0.0103  -0.0086 -0.0045 274 GLU A CB  
2166 C CG  . GLU A 294 ? 0.3816 0.2399 0.2558 0.0120  0.0040  -0.0016 274 GLU A CG  
2167 C CD  . GLU A 294 ? 0.4204 0.2583 0.2728 0.0161  0.0092  -0.0009 274 GLU A CD  
2168 O OE1 . GLU A 294 ? 0.4390 0.2626 0.2767 0.0173  0.0021  -0.0028 274 GLU A OE1 
2169 O OE2 . GLU A 294 ? 0.4216 0.2571 0.2719 0.0182  0.0206  0.0015  274 GLU A OE2 
2170 N N   . LEU A 295 ? 0.4170 0.2277 0.2452 0.0167  -0.0230 -0.0078 275 LEU A N   
2171 C CA  . LEU A 295 ? 0.4493 0.2387 0.2582 0.0188  -0.0349 -0.0106 275 LEU A CA  
2172 C C   . LEU A 295 ? 0.4627 0.2656 0.2931 0.0145  -0.0478 -0.0138 275 LEU A C   
2173 O O   . LEU A 295 ? 0.4328 0.2570 0.2867 0.0103  -0.0440 -0.0133 275 LEU A O   
2174 C CB  . LEU A 295 ? 0.4694 0.2427 0.2597 0.0211  -0.0296 -0.0101 275 LEU A CB  
2175 C CG  . LEU A 295 ? 0.5051 0.2639 0.2757 0.0257  -0.0148 -0.0070 275 LEU A CG  
2176 C CD1 . LEU A 295 ? 0.5295 0.2709 0.2814 0.0286  -0.0106 -0.0070 275 LEU A CD1 
2177 C CD2 . LEU A 295 ? 0.5331 0.2687 0.2780 0.0300  -0.0162 -0.0067 275 LEU A CD2 
2178 N N   . PRO A 296 ? 0.5078 0.2985 0.3316 0.0155  -0.0628 -0.0170 276 PRO A N   
2179 C CA  . PRO A 296 ? 0.5111 0.3164 0.3606 0.0111  -0.0743 -0.0201 276 PRO A CA  
2180 C C   . PRO A 296 ? 0.5098 0.3257 0.3740 0.0064  -0.0719 -0.0205 276 PRO A C   
2181 O O   . PRO A 296 ? 0.5032 0.3400 0.3950 0.0018  -0.0715 -0.0209 276 PRO A O   
2182 C CB  . PRO A 296 ? 0.5450 0.3285 0.3791 0.0140  -0.0920 -0.0238 276 PRO A CB  
2183 C CG  . PRO A 296 ? 0.5776 0.3314 0.3722 0.0201  -0.0885 -0.0224 276 PRO A CG  
2184 C CD  . PRO A 296 ? 0.5402 0.3021 0.3333 0.0211  -0.0703 -0.0181 276 PRO A CD  
2185 N N   . GLU A 297 ? 0.5059 0.3067 0.3510 0.0077  -0.0686 -0.0200 277 GLU A N   
2186 C CA  . GLU A 297 ? 0.4993 0.3075 0.3555 0.0035  -0.0661 -0.0202 277 GLU A CA  
2187 C C   . GLU A 297 ? 0.4699 0.3018 0.3466 0.0007  -0.0530 -0.0173 277 GLU A C   
2188 O O   . GLU A 297 ? 0.4769 0.3220 0.3732 -0.0041 -0.0527 -0.0178 277 GLU A O   
2189 C CB  . GLU A 297 ? 0.5619 0.3474 0.3906 0.0067  -0.0638 -0.0199 277 GLU A CB  
2190 C CG  . GLU A 297 ? 0.6756 0.4339 0.4807 0.0095  -0.0783 -0.0232 277 GLU A CG  
2191 C CD  . GLU A 297 ? 0.7850 0.5202 0.5592 0.0164  -0.0774 -0.0224 277 GLU A CD  
2192 O OE1 . GLU A 297 ? 0.7274 0.4712 0.5044 0.0182  -0.0682 -0.0198 277 GLU A OE1 
2193 O OE2 . GLU A 297 ? 0.8689 0.5751 0.6144 0.0200  -0.0860 -0.0244 277 GLU A OE2 
2194 N N   . VAL A 298 ? 0.4331 0.2684 0.3046 0.0037  -0.0426 -0.0144 278 VAL A N   
2195 C CA  . VAL A 298 ? 0.4118 0.2667 0.3001 0.0017  -0.0322 -0.0119 278 VAL A CA  
2196 C C   . VAL A 298 ? 0.3906 0.2629 0.3009 -0.0013 -0.0348 -0.0125 278 VAL A C   
2197 O O   . VAL A 298 ? 0.3785 0.2643 0.3060 -0.0051 -0.0321 -0.0124 278 VAL A O   
2198 C CB  . VAL A 298 ? 0.4135 0.2662 0.2917 0.0056  -0.0213 -0.0089 278 VAL A CB  
2199 C CG1 . VAL A 298 ? 0.3938 0.2663 0.2905 0.0037  -0.0136 -0.0069 278 VAL A CG1 
2200 C CG2 . VAL A 298 ? 0.4319 0.2695 0.2921 0.0089  -0.0163 -0.0081 278 VAL A CG2 
2201 N N   . THR A 299 ? 0.3865 0.2565 0.2948 0.0006  -0.0396 -0.0133 279 THR A N   
2202 C CA  . THR A 299 ? 0.3812 0.2667 0.3096 -0.0013 -0.0415 -0.0139 279 THR A CA  
2203 C C   . THR A 299 ? 0.3668 0.2607 0.3154 -0.0055 -0.0480 -0.0164 279 THR A C   
2204 O O   . THR A 299 ? 0.3524 0.2617 0.3199 -0.0084 -0.0429 -0.0158 279 THR A O   
2205 C CB  . THR A 299 ? 0.4213 0.2992 0.3409 0.0023  -0.0467 -0.0144 279 THR A CB  
2206 O OG1 . THR A 299 ? 0.4579 0.3294 0.3620 0.0052  -0.0377 -0.0116 279 THR A OG1 
2207 C CG2 . THR A 299 ? 0.4162 0.3089 0.3561 0.0012  -0.0490 -0.0152 279 THR A CG2 
2208 N N   . ASN A 300 ? 0.3743 0.2568 0.3186 -0.0060 -0.0584 -0.0190 280 ASN A N   
2209 C CA  . ASN A 300 ? 0.3721 0.2630 0.3391 -0.0107 -0.0646 -0.0216 280 ASN A CA  
2210 C C   . ASN A 300 ? 0.3531 0.2533 0.3303 -0.0152 -0.0545 -0.0200 280 ASN A C   
2211 O O   . ASN A 300 ? 0.3493 0.2631 0.3495 -0.0191 -0.0516 -0.0203 280 ASN A O   
2212 C CB  . ASN A 300 ? 0.4024 0.2773 0.3619 -0.0107 -0.0790 -0.0249 280 ASN A CB  
2213 C CG  . ASN A 300 ? 0.4670 0.3311 0.4176 -0.0062 -0.0914 -0.0271 280 ASN A CG  
2214 O OD1 . ASN A 300 ? 0.4777 0.3496 0.4344 -0.0040 -0.0901 -0.0265 280 ASN A OD1 
2215 N ND2 . ASN A 300 ? 0.5072 0.3504 0.4402 -0.0044 -0.1040 -0.0297 280 ASN A ND2 
2216 N N   . SER A 301 ? 0.3457 0.2375 0.3050 -0.0140 -0.0482 -0.0180 281 SER A N   
2217 C CA  . SER A 301 ? 0.3431 0.2403 0.3074 -0.0171 -0.0393 -0.0163 281 SER A CA  
2218 C C   . SER A 301 ? 0.3321 0.2436 0.3063 -0.0173 -0.0294 -0.0140 281 SER A C   
2219 O O   . SER A 301 ? 0.3247 0.2439 0.3120 -0.0209 -0.0243 -0.0136 281 SER A O   
2220 C CB  . SER A 301 ? 0.3662 0.2506 0.3087 -0.0144 -0.0356 -0.0149 281 SER A CB  
2221 O OG  . SER A 301 ? 0.3803 0.2697 0.3262 -0.0163 -0.0270 -0.0130 281 SER A OG  
2222 N N   . VAL A 302 ? 0.3251 0.2383 0.2921 -0.0135 -0.0267 -0.0125 282 VAL A N   
2223 C CA  . VAL A 302 ? 0.3160 0.2405 0.2903 -0.0133 -0.0190 -0.0107 282 VAL A CA  
2224 C C   . VAL A 302 ? 0.3104 0.2455 0.3047 -0.0161 -0.0192 -0.0119 282 VAL A C   
2225 O O   . VAL A 302 ? 0.3104 0.2515 0.3121 -0.0181 -0.0120 -0.0108 282 VAL A O   
2226 C CB  . VAL A 302 ? 0.3183 0.2417 0.2829 -0.0093 -0.0176 -0.0093 282 VAL A CB  
2227 C CG1 . VAL A 302 ? 0.3132 0.2474 0.2868 -0.0094 -0.0126 -0.0082 282 VAL A CG1 
2228 C CG2 . VAL A 302 ? 0.3250 0.2406 0.2745 -0.0067 -0.0134 -0.0076 282 VAL A CG2 
2229 N N   . PHE A 303 ? 0.3016 0.2373 0.3040 -0.0158 -0.0276 -0.0142 283 PHE A N   
2230 C CA  . PHE A 303 ? 0.2928 0.2397 0.3178 -0.0178 -0.0277 -0.0156 283 PHE A CA  
2231 C C   . PHE A 303 ? 0.2957 0.2458 0.3356 -0.0230 -0.0245 -0.0162 283 PHE A C   
2232 O O   . PHE A 303 ? 0.2991 0.2574 0.3527 -0.0250 -0.0163 -0.0155 283 PHE A O   
2233 C CB  . PHE A 303 ? 0.2917 0.2380 0.3241 -0.0160 -0.0394 -0.0184 283 PHE A CB  
2234 C CG  . PHE A 303 ? 0.3036 0.2503 0.3292 -0.0115 -0.0402 -0.0178 283 PHE A CG  
2235 C CD1 . PHE A 303 ? 0.3233 0.2615 0.3267 -0.0084 -0.0378 -0.0158 283 PHE A CD1 
2236 C CD2 . PHE A 303 ? 0.3043 0.2594 0.3470 -0.0104 -0.0429 -0.0192 283 PHE A CD2 
2237 C CE1 . PHE A 303 ? 0.3329 0.2699 0.3299 -0.0048 -0.0384 -0.0152 283 PHE A CE1 
2238 C CE2 . PHE A 303 ? 0.3166 0.2703 0.3515 -0.0061 -0.0441 -0.0187 283 PHE A CE2 
2239 C CZ  . PHE A 303 ? 0.3204 0.2647 0.3321 -0.0037 -0.0418 -0.0166 283 PHE A CZ  
2240 N N   . HIS A 304 ? 0.2887 0.2304 0.3243 -0.0251 -0.0302 -0.0174 284 HIS A N   
2241 C CA  . HIS A 304 ? 0.2943 0.2373 0.3438 -0.0307 -0.0274 -0.0180 284 HIS A CA  
2242 C C   . HIS A 304 ? 0.3029 0.2458 0.3461 -0.0321 -0.0140 -0.0151 284 HIS A C   
2243 O O   . HIS A 304 ? 0.3114 0.2594 0.3700 -0.0360 -0.0063 -0.0147 284 HIS A O   
2244 C CB  . HIS A 304 ? 0.3216 0.2522 0.3622 -0.0322 -0.0367 -0.0198 284 HIS A CB  
2245 C CG  . HIS A 304 ? 0.3826 0.3128 0.4364 -0.0385 -0.0339 -0.0204 284 HIS A CG  
2246 N ND1 . HIS A 304 ? 0.4134 0.3531 0.4969 -0.0433 -0.0352 -0.0224 284 HIS A ND1 
2247 C CD2 . HIS A 304 ? 0.4218 0.3426 0.4633 -0.0406 -0.0294 -0.0191 284 HIS A CD2 
2248 C CE1 . HIS A 304 ? 0.4261 0.3616 0.5146 -0.0488 -0.0312 -0.0223 284 HIS A CE1 
2249 N NE2 . HIS A 304 ? 0.4371 0.3604 0.4993 -0.0473 -0.0279 -0.0203 284 HIS A NE2 
2250 N N   . GLU A 305 ? 0.3067 0.2427 0.3278 -0.0288 -0.0111 -0.0129 285 GLU A N   
2251 C CA  . GLU A 305 ? 0.3187 0.2519 0.3308 -0.0291 -0.0011 -0.0104 285 GLU A CA  
2252 C C   . GLU A 305 ? 0.3087 0.2489 0.3267 -0.0285 0.0071  -0.0090 285 GLU A C   
2253 O O   . GLU A 305 ? 0.3118 0.2498 0.3310 -0.0308 0.0158  -0.0078 285 GLU A O   
2254 C CB  . GLU A 305 ? 0.3502 0.2753 0.3407 -0.0251 -0.0017 -0.0088 285 GLU A CB  
2255 C CG  . GLU A 305 ? 0.3969 0.3116 0.3783 -0.0255 -0.0077 -0.0099 285 GLU A CG  
2256 C CD  . GLU A 305 ? 0.4979 0.4068 0.4827 -0.0303 -0.0054 -0.0102 285 GLU A CD  
2257 O OE1 . GLU A 305 ? 0.4984 0.4082 0.4853 -0.0321 0.0030  -0.0086 285 GLU A OE1 
2258 O OE2 . GLU A 305 ? 0.5222 0.4238 0.5060 -0.0322 -0.0121 -0.0121 285 GLU A OE2 
2259 N N   . ILE A 306 ? 0.2884 0.2349 0.3085 -0.0253 0.0046  -0.0093 286 ILE A N   
2260 C CA  . ILE A 306 ? 0.2914 0.2430 0.3158 -0.0244 0.0118  -0.0084 286 ILE A CA  
2261 C C   . ILE A 306 ? 0.2933 0.2509 0.3393 -0.0279 0.0166  -0.0095 286 ILE A C   
2262 O O   . ILE A 306 ? 0.3066 0.2627 0.3536 -0.0289 0.0270  -0.0081 286 ILE A O   
2263 C CB  . ILE A 306 ? 0.2966 0.2524 0.3183 -0.0204 0.0074  -0.0086 286 ILE A CB  
2264 C CG1 . ILE A 306 ? 0.3009 0.2513 0.3043 -0.0173 0.0054  -0.0071 286 ILE A CG1 
2265 C CG2 . ILE A 306 ? 0.3076 0.2678 0.3347 -0.0193 0.0142  -0.0080 286 ILE A CG2 
2266 C CD1 . ILE A 306 ? 0.3164 0.2696 0.3175 -0.0140 0.0008  -0.0074 286 ILE A CD1 
2267 N N   . ASN A 307 ? 0.2897 0.2527 0.3531 -0.0298 0.0092  -0.0120 287 ASN A N   
2268 C CA  . ASN A 307 ? 0.2973 0.2678 0.3872 -0.0335 0.0131  -0.0134 287 ASN A CA  
2269 C C   . ASN A 307 ? 0.3095 0.2744 0.4007 -0.0384 0.0236  -0.0120 287 ASN A C   
2270 O O   . ASN A 307 ? 0.3217 0.2883 0.4223 -0.0398 0.0356  -0.0110 287 ASN A O   
2271 C CB  . ASN A 307 ? 0.3157 0.2906 0.4226 -0.0348 -0.0001 -0.0166 287 ASN A CB  
2272 C CG  . ASN A 307 ? 0.3629 0.3479 0.5035 -0.0388 0.0015  -0.0187 287 ASN A CG  
2273 O OD1 . ASN A 307 ? 0.3671 0.3529 0.5192 -0.0431 0.0129  -0.0177 287 ASN A OD1 
2274 N ND2 . ASN A 307 ? 0.3773 0.3692 0.5350 -0.0372 -0.0103 -0.0217 287 ASN A ND2 
2275 N N   . MET A 308 ? 0.3148 0.2708 0.3941 -0.0404 0.0201  -0.0117 288 MET A N   
2276 C CA  . MET A 308 ? 0.3278 0.2758 0.4057 -0.0450 0.0294  -0.0103 288 MET A CA  
2277 C C   . MET A 308 ? 0.3412 0.2811 0.4004 -0.0429 0.0417  -0.0072 288 MET A C   
2278 O O   . MET A 308 ? 0.3566 0.2921 0.4206 -0.0460 0.0540  -0.0060 288 MET A O   
2279 C CB  . MET A 308 ? 0.3494 0.2874 0.4136 -0.0465 0.0223  -0.0106 288 MET A CB  
2280 C CG  . MET A 308 ? 0.3977 0.3387 0.4746 -0.0483 0.0090  -0.0138 288 MET A CG  
2281 S SD  . MET A 308 ? 0.5343 0.4805 0.6449 -0.0566 0.0103  -0.0160 288 MET A SD  
2282 C CE  . MET A 308 ? 0.4845 0.4480 0.6243 -0.0549 0.0055  -0.0185 288 MET A CE  
2283 N N   . TRP A 309 ? 0.3331 0.2693 0.3706 -0.0376 0.0382  -0.0061 289 TRP A N   
2284 C CA  . TRP A 309 ? 0.3339 0.2600 0.3510 -0.0349 0.0464  -0.0036 289 TRP A CA  
2285 C C   . TRP A 309 ? 0.3368 0.2646 0.3597 -0.0341 0.0565  -0.0029 289 TRP A C   
2286 O O   . TRP A 309 ? 0.3481 0.2646 0.3611 -0.0347 0.0677  -0.0011 289 TRP A O   
2287 C CB  . TRP A 309 ? 0.3234 0.2475 0.3217 -0.0296 0.0386  -0.0030 289 TRP A CB  
2288 C CG  . TRP A 309 ? 0.3188 0.2304 0.2950 -0.0267 0.0430  -0.0009 289 TRP A CG  
2289 C CD1 . TRP A 309 ? 0.3357 0.2357 0.2959 -0.0261 0.0425  0.0003  289 TRP A CD1 
2290 C CD2 . TRP A 309 ? 0.3143 0.2220 0.2809 -0.0235 0.0472  0.0001  289 TRP A CD2 
2291 N NE1 . TRP A 309 ? 0.3507 0.2399 0.2924 -0.0226 0.0452  0.0018  289 TRP A NE1 
2292 C CE2 . TRP A 309 ? 0.3403 0.2334 0.2847 -0.0210 0.0477  0.0017  289 TRP A CE2 
2293 C CE3 . TRP A 309 ? 0.3112 0.2250 0.2846 -0.0221 0.0495  -0.0004 289 TRP A CE3 
2294 C CZ2 . TRP A 309 ? 0.3506 0.2338 0.2789 -0.0174 0.0500  0.0027  289 TRP A CZ2 
2295 C CZ3 . TRP A 309 ? 0.3229 0.2271 0.2797 -0.0186 0.0526  0.0007  289 TRP A CZ3 
2296 C CH2 . TRP A 309 ? 0.3442 0.2326 0.2783 -0.0164 0.0525  0.0021  289 TRP A CH2 
2297 N N   . VAL A 310 ? 0.3257 0.2656 0.3629 -0.0324 0.0530  -0.0044 290 VAL A N   
2298 C CA  . VAL A 310 ? 0.3381 0.2798 0.3821 -0.0310 0.0627  -0.0041 290 VAL A CA  
2299 C C   . VAL A 310 ? 0.3554 0.3001 0.4227 -0.0358 0.0734  -0.0044 290 VAL A C   
2300 O O   . VAL A 310 ? 0.3666 0.3033 0.4301 -0.0358 0.0876  -0.0028 290 VAL A O   
2301 C CB  . VAL A 310 ? 0.3338 0.2866 0.3857 -0.0273 0.0551  -0.0056 290 VAL A CB  
2302 C CG1 . VAL A 310 ? 0.3443 0.2997 0.4062 -0.0257 0.0652  -0.0056 290 VAL A CG1 
2303 C CG2 . VAL A 310 ? 0.3377 0.2862 0.3672 -0.0232 0.0474  -0.0049 290 VAL A CG2 
2304 N N   . SER A 311 ? 0.3582 0.3120 0.4482 -0.0402 0.0673  -0.0064 291 SER A N   
2305 C CA  . SER A 311 ? 0.3700 0.3282 0.4874 -0.0456 0.0768  -0.0070 291 SER A CA  
2306 C C   . SER A 311 ? 0.3940 0.3361 0.4972 -0.0489 0.0910  -0.0043 291 SER A C   
2307 O O   . SER A 311 ? 0.4073 0.3468 0.5213 -0.0510 0.1068  -0.0032 291 SER A O   
2308 C CB  . SER A 311 ? 0.3934 0.3618 0.5352 -0.0498 0.0646  -0.0099 291 SER A CB  
2309 O OG  . SER A 311 ? 0.4334 0.4144 0.5883 -0.0465 0.0520  -0.0124 291 SER A OG  
2310 N N   . GLN A 312 ? 0.4016 0.3315 0.4795 -0.0488 0.0863  -0.0031 292 GLN A N   
2311 C CA  . GLN A 312 ? 0.4150 0.3266 0.4749 -0.0512 0.0982  -0.0005 292 GLN A CA  
2312 C C   . GLN A 312 ? 0.4359 0.3332 0.4728 -0.0470 0.1110  0.0021  292 GLN A C   
2313 O O   . GLN A 312 ? 0.4755 0.3574 0.5034 -0.0491 0.1257  0.0042  292 GLN A O   
2314 C CB  . GLN A 312 ? 0.4437 0.3453 0.4806 -0.0506 0.0884  0.0000  292 GLN A CB  
2315 C CG  . GLN A 312 ? 0.4883 0.3961 0.5421 -0.0558 0.0791  -0.0021 292 GLN A CG  
2316 C CD  . GLN A 312 ? 0.5947 0.4963 0.6272 -0.0530 0.0667  -0.0022 292 GLN A CD  
2317 O OE1 . GLN A 312 ? 0.6619 0.5522 0.6674 -0.0484 0.0670  -0.0004 292 GLN A OE1 
2318 N NE2 . GLN A 312 ? 0.5916 0.4994 0.6357 -0.0553 0.0550  -0.0046 292 GLN A NE2 
2319 N N   . ARG A 313 ? 0.4116 0.3116 0.4373 -0.0410 0.1055  0.0018  293 ARG A N   
2320 C CA  . ARG A 313 ? 0.4214 0.3057 0.4218 -0.0363 0.1145  0.0037  293 ARG A CA  
2321 C C   . ARG A 313 ? 0.4503 0.3399 0.4647 -0.0346 0.1250  0.0034  293 ARG A C   
2322 O O   . ARG A 313 ? 0.4583 0.3344 0.4504 -0.0300 0.1309  0.0046  293 ARG A O   
2323 C CB  . ARG A 313 ? 0.4136 0.2938 0.3893 -0.0307 0.1013  0.0038  293 ARG A CB  
2324 C CG  . ARG A 313 ? 0.4175 0.2857 0.3739 -0.0312 0.0961  0.0048  293 ARG A CG  
2325 C CD  . ARG A 313 ? 0.4259 0.2971 0.3700 -0.0269 0.0808  0.0042  293 ARG A CD  
2326 N NE  . ARG A 313 ? 0.4244 0.2854 0.3536 -0.0269 0.0760  0.0050  293 ARG A NE  
2327 C CZ  . ARG A 313 ? 0.4104 0.2777 0.3510 -0.0304 0.0716  0.0042  293 ARG A CZ  
2328 N NH1 . ARG A 313 ? 0.3936 0.2768 0.3604 -0.0344 0.0699  0.0024  293 ARG A NH1 
2329 N NH2 . ARG A 313 ? 0.4001 0.2562 0.3249 -0.0297 0.0680  0.0050  293 ARG A NH2 
2330 N N   . THR A 314 ? 0.4635 0.3717 0.5144 -0.0381 0.1266  0.0016  294 THR A N   
2331 C CA  . THR A 314 ? 0.4934 0.4092 0.5643 -0.0366 0.1371  0.0010  294 THR A CA  
2332 C C   . THR A 314 ? 0.5385 0.4591 0.6407 -0.0425 0.1521  0.0011  294 THR A C   
2333 O O   . THR A 314 ? 0.5530 0.4778 0.6728 -0.0413 0.1649  0.0010  294 THR A O   
2334 C CB  . THR A 314 ? 0.4813 0.4170 0.5704 -0.0336 0.1230  -0.0017 294 THR A CB  
2335 O OG1 . THR A 314 ? 0.4776 0.4274 0.5860 -0.0372 0.1085  -0.0038 294 THR A OG1 
2336 C CG2 . THR A 314 ? 0.4860 0.4155 0.5466 -0.0276 0.1137  -0.0014 294 THR A CG2 
2337 N N   . ALA A 315 ? 0.5626 0.4822 0.6727 -0.0489 0.1513  0.0012  295 ALA A N   
2338 C CA  . ALA A 315 ? 0.5839 0.5072 0.7247 -0.0558 0.1649  0.0013  295 ALA A CA  
2339 C C   . ALA A 315 ? 0.6213 0.5243 0.7479 -0.0556 0.1902  0.0046  295 ALA A C   
2340 O O   . ALA A 315 ? 0.6329 0.5365 0.7646 -0.0517 0.2016  0.0049  295 ALA A O   
2341 C CB  . ALA A 315 ? 0.5895 0.5107 0.7322 -0.0622 0.1573  0.0011  295 ALA A CB  
# 
