data_8RG4
# 
_entry.id   8RG4 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.400 
_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   8RG4         pdb_00008rg4 10.2210/pdb8rg4/pdb 
WWPDB D_1292134759 ?            ?                   
# 
loop_
_pdbx_audit_revision_history.ordinal 
_pdbx_audit_revision_history.data_content_type 
_pdbx_audit_revision_history.major_revision 
_pdbx_audit_revision_history.minor_revision 
_pdbx_audit_revision_history.revision_date 
1 'Structure model' 1 0 2025-01-01 
2 'Structure model' 1 1 2025-01-08 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
_pdbx_audit_revision_group.ordinal             1 
_pdbx_audit_revision_group.revision_ordinal    2 
_pdbx_audit_revision_group.data_content_type   'Structure model' 
_pdbx_audit_revision_group.group               'Database references' 
# 
loop_
_pdbx_audit_revision_category.ordinal 
_pdbx_audit_revision_category.revision_ordinal 
_pdbx_audit_revision_category.data_content_type 
_pdbx_audit_revision_category.category 
1 2 'Structure model' citation        
2 2 'Structure model' citation_author 
# 
loop_
_pdbx_audit_revision_item.ordinal 
_pdbx_audit_revision_item.revision_ordinal 
_pdbx_audit_revision_item.data_content_type 
_pdbx_audit_revision_item.item 
1  2 'Structure model' '_citation.country'                 
2  2 'Structure model' '_citation.journal_abbrev'          
3  2 'Structure model' '_citation.journal_id_CSD'          
4  2 'Structure model' '_citation.journal_id_ISSN'         
5  2 'Structure model' '_citation.journal_volume'          
6  2 'Structure model' '_citation.page_first'              
7  2 'Structure model' '_citation.page_last'               
8  2 'Structure model' '_citation.pdbx_database_id_DOI'    
9  2 'Structure model' '_citation.pdbx_database_id_PubMed' 
10 2 'Structure model' '_citation.title'                   
11 2 'Structure model' '_citation.year'                    
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        8RG4 
_pdbx_database_status.recvd_initial_deposition_date   2023-12-13 
_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           Y 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              beatriz.trastoy@gmail.com 
_pdbx_contact_author.name_first         Beatriz 
_pdbx_contact_author.name_last          Trastoy 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-2178-732X 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Perez-Cruz, C.'       1  0000-0003-2796-5315 
'Moraleda-Montoya, A.' 2  0000-0003-4502-5976 
'Liebana, R.'          3  0000-0002-2196-5632 
'Lorizate, M.'         4  0000-0001-8173-2788 
'Arrizabalaga, U.'     5  ?                   
'Garcia-Alija, M.'     6  0000-0002-8805-1325 
'Terrones, O.'         7  0000-0001-7421-6486 
'Contreras, F.X.'      8  0000-0003-0875-634X 
'Guerin, M.E.'         9  0000-0001-9524-3184 
'Trastoy, B.'          10 0000-0002-2178-732X 
'Alonso-Saez, L.'      11 0000-0003-1757-4767 
# 
_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                   UK 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'Nat Commun' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            ? 
_citation.journal_id_ISSN           2041-1723 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            15 
_citation.language                  ? 
_citation.page_first                10906 
_citation.page_last                 10906 
_citation.title                     'Mechanisms of recalcitrant fucoidan breakdown in marine Planctomycetota.' 
_citation.year                      2024 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1038/s41467-024-55268-w 
_citation.pdbx_database_id_PubMed   39738071 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Perez-Cruz, C.'        1  ?                   
primary 'Moraleda-Montoya, A.'  2  ?                   
primary 'Liebana, R.'           3  ?                   
primary 'Terrones, O.'          4  ?                   
primary 'Arrizabalaga, U.'      5  ?                   
primary 'Garcia-Alija, M.'      6  ?                   
primary 'Lorizate, M.'          7  ?                   
primary 'Martinez Gascuena, A.' 8  ?                   
primary 'Garcia-Alvarez, I.'    9  0000-0002-2273-5046 
primary 'Nieto-Garai, J.A.'     10 0000-0002-8665-099X 
primary 'Olazar-Intxausti, J.'  11 ?                   
primary 'Rodriguez-Colinas, B.' 12 ?                   
primary 'Mann, E.'              13 ?                   
primary 'Chiara, J.L.'          14 0000-0002-8153-1852 
primary 'Contreras, F.X.'       15 0000-0003-0875-634X 
primary 'Guerin, M.E.'          16 0000-0001-9524-3184 
primary 'Trastoy, B.'           17 0000-0002-2178-732X 
primary 'Alonso-Saez, L.'       18 0000-0003-1757-4767 
# 
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 'Glycoside-hydrolase family GH114 TIM-barrel domain-containing protein' 43353.996 1   ? ? ? ? 
2 non-polymer syn 1,2-ETHANEDIOL                                                          62.068    2   ? ? ? ? 
3 water       nat water                                                                   18.015    342 ? ? ? ? 
# 
_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       
;MHHHHHHENLYFQGSGDESHYPEFSWDTVPIAFHFGKSQGLLTKEEAEFVATRSNFICLEKGHATRTHGTTEAGIEAEAR
QLKNLNPKMKVIFYWNTFLDYSMFAAHKEYAKHPQWWLRTTTGELDRKKGQLMRYDLSNAEFRNWWTNVAAKAVVDGTCD
GVFMDAFPQIASQANRKLWGDEKFEAIQQGLQDIIQETRQKIGDDKLIVYNGIRSTPDWSAGFDFAEYTDAAMIEHFGHF
QSASKETMLRDILEMQRAAKAGKIVVLKGWAGFTFIDDQAMRKPLTQKRRVAKDSLKFPLACFLAGAQENCYFIYNWGYR
MENGCLEWYPEFDKPLGKPVGEMVRDGWKLSREYKHASVRVDLESKEAEIRWR
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MHHHHHHENLYFQGSGDESHYPEFSWDTVPIAFHFGKSQGLLTKEEAEFVATRSNFICLEKGHATRTHGTTEAGIEAEAR
QLKNLNPKMKVIFYWNTFLDYSMFAAHKEYAKHPQWWLRTTTGELDRKKGQLMRYDLSNAEFRNWWTNVAAKAVVDGTCD
GVFMDAFPQIASQANRKLWGDEKFEAIQQGLQDIIQETRQKIGDDKLIVYNGIRSTPDWSAGFDFAEYTDAAMIEHFGHF
QSASKETMLRDILEMQRAAKAGKIVVLKGWAGFTFIDDQAMRKPLTQKRRVAKDSLKFPLACFLAGAQENCYFIYNWGYR
MENGCLEWYPEFDKPLGKPVGEMVRDGWKLSREYKHASVRVDLESKEAEIRWR
;
_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 1,2-ETHANEDIOL EDO 
3 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   HIS n 
1 3   HIS n 
1 4   HIS n 
1 5   HIS n 
1 6   HIS n 
1 7   HIS n 
1 8   GLU n 
1 9   ASN n 
1 10  LEU n 
1 11  TYR n 
1 12  PHE n 
1 13  GLN n 
1 14  GLY n 
1 15  SER n 
1 16  GLY n 
1 17  ASP n 
1 18  GLU n 
1 19  SER n 
1 20  HIS n 
1 21  TYR n 
1 22  PRO n 
1 23  GLU n 
1 24  PHE n 
1 25  SER n 
1 26  TRP n 
1 27  ASP n 
1 28  THR n 
1 29  VAL n 
1 30  PRO n 
1 31  ILE n 
1 32  ALA n 
1 33  PHE n 
1 34  HIS n 
1 35  PHE n 
1 36  GLY n 
1 37  LYS n 
1 38  SER n 
1 39  GLN n 
1 40  GLY n 
1 41  LEU n 
1 42  LEU n 
1 43  THR n 
1 44  LYS n 
1 45  GLU n 
1 46  GLU n 
1 47  ALA n 
1 48  GLU n 
1 49  PHE n 
1 50  VAL n 
1 51  ALA n 
1 52  THR n 
1 53  ARG n 
1 54  SER n 
1 55  ASN n 
1 56  PHE n 
1 57  ILE n 
1 58  CYS n 
1 59  LEU n 
1 60  GLU n 
1 61  LYS n 
1 62  GLY n 
1 63  HIS n 
1 64  ALA n 
1 65  THR n 
1 66  ARG n 
1 67  THR n 
1 68  HIS n 
1 69  GLY n 
1 70  THR n 
1 71  THR n 
1 72  GLU n 
1 73  ALA n 
1 74  GLY n 
1 75  ILE n 
1 76  GLU n 
1 77  ALA n 
1 78  GLU n 
1 79  ALA n 
1 80  ARG n 
1 81  GLN n 
1 82  LEU n 
1 83  LYS n 
1 84  ASN n 
1 85  LEU n 
1 86  ASN n 
1 87  PRO n 
1 88  LYS n 
1 89  MET n 
1 90  LYS n 
1 91  VAL n 
1 92  ILE n 
1 93  PHE n 
1 94  TYR n 
1 95  TRP n 
1 96  ASN n 
1 97  THR n 
1 98  PHE n 
1 99  LEU n 
1 100 ASP n 
1 101 TYR n 
1 102 SER n 
1 103 MET n 
1 104 PHE n 
1 105 ALA n 
1 106 ALA n 
1 107 HIS n 
1 108 LYS n 
1 109 GLU n 
1 110 TYR n 
1 111 ALA n 
1 112 LYS n 
1 113 HIS n 
1 114 PRO n 
1 115 GLN n 
1 116 TRP n 
1 117 TRP n 
1 118 LEU n 
1 119 ARG n 
1 120 THR n 
1 121 THR n 
1 122 THR n 
1 123 GLY n 
1 124 GLU n 
1 125 LEU n 
1 126 ASP n 
1 127 ARG n 
1 128 LYS n 
1 129 LYS n 
1 130 GLY n 
1 131 GLN n 
1 132 LEU n 
1 133 MET n 
1 134 ARG n 
1 135 TYR n 
1 136 ASP n 
1 137 LEU n 
1 138 SER n 
1 139 ASN n 
1 140 ALA n 
1 141 GLU n 
1 142 PHE n 
1 143 ARG n 
1 144 ASN n 
1 145 TRP n 
1 146 TRP n 
1 147 THR n 
1 148 ASN n 
1 149 VAL n 
1 150 ALA n 
1 151 ALA n 
1 152 LYS n 
1 153 ALA n 
1 154 VAL n 
1 155 VAL n 
1 156 ASP n 
1 157 GLY n 
1 158 THR n 
1 159 CYS n 
1 160 ASP n 
1 161 GLY n 
1 162 VAL n 
1 163 PHE n 
1 164 MET n 
1 165 ASP n 
1 166 ALA n 
1 167 PHE n 
1 168 PRO n 
1 169 GLN n 
1 170 ILE n 
1 171 ALA n 
1 172 SER n 
1 173 GLN n 
1 174 ALA n 
1 175 ASN n 
1 176 ARG n 
1 177 LYS n 
1 178 LEU n 
1 179 TRP n 
1 180 GLY n 
1 181 ASP n 
1 182 GLU n 
1 183 LYS n 
1 184 PHE n 
1 185 GLU n 
1 186 ALA n 
1 187 ILE n 
1 188 GLN n 
1 189 GLN n 
1 190 GLY n 
1 191 LEU n 
1 192 GLN n 
1 193 ASP n 
1 194 ILE n 
1 195 ILE n 
1 196 GLN n 
1 197 GLU n 
1 198 THR n 
1 199 ARG n 
1 200 GLN n 
1 201 LYS n 
1 202 ILE n 
1 203 GLY n 
1 204 ASP n 
1 205 ASP n 
1 206 LYS n 
1 207 LEU n 
1 208 ILE n 
1 209 VAL n 
1 210 TYR n 
1 211 ASN n 
1 212 GLY n 
1 213 ILE n 
1 214 ARG n 
1 215 SER n 
1 216 THR n 
1 217 PRO n 
1 218 ASP n 
1 219 TRP n 
1 220 SER n 
1 221 ALA n 
1 222 GLY n 
1 223 PHE n 
1 224 ASP n 
1 225 PHE n 
1 226 ALA n 
1 227 GLU n 
1 228 TYR n 
1 229 THR n 
1 230 ASP n 
1 231 ALA n 
1 232 ALA n 
1 233 MET n 
1 234 ILE n 
1 235 GLU n 
1 236 HIS n 
1 237 PHE n 
1 238 GLY n 
1 239 HIS n 
1 240 PHE n 
1 241 GLN n 
1 242 SER n 
1 243 ALA n 
1 244 SER n 
1 245 LYS n 
1 246 GLU n 
1 247 THR n 
1 248 MET n 
1 249 LEU n 
1 250 ARG n 
1 251 ASP n 
1 252 ILE n 
1 253 LEU n 
1 254 GLU n 
1 255 MET n 
1 256 GLN n 
1 257 ARG n 
1 258 ALA n 
1 259 ALA n 
1 260 LYS n 
1 261 ALA n 
1 262 GLY n 
1 263 LYS n 
1 264 ILE n 
1 265 VAL n 
1 266 VAL n 
1 267 LEU n 
1 268 LYS n 
1 269 GLY n 
1 270 TRP n 
1 271 ALA n 
1 272 GLY n 
1 273 PHE n 
1 274 THR n 
1 275 PHE n 
1 276 ILE n 
1 277 ASP n 
1 278 ASP n 
1 279 GLN n 
1 280 ALA n 
1 281 MET n 
1 282 ARG n 
1 283 LYS n 
1 284 PRO n 
1 285 LEU n 
1 286 THR n 
1 287 GLN n 
1 288 LYS n 
1 289 ARG n 
1 290 ARG n 
1 291 VAL n 
1 292 ALA n 
1 293 LYS n 
1 294 ASP n 
1 295 SER n 
1 296 LEU n 
1 297 LYS n 
1 298 PHE n 
1 299 PRO n 
1 300 LEU n 
1 301 ALA n 
1 302 CYS n 
1 303 PHE n 
1 304 LEU n 
1 305 ALA n 
1 306 GLY n 
1 307 ALA n 
1 308 GLN n 
1 309 GLU n 
1 310 ASN n 
1 311 CYS n 
1 312 TYR n 
1 313 PHE n 
1 314 ILE n 
1 315 TYR n 
1 316 ASN n 
1 317 TRP n 
1 318 GLY n 
1 319 TYR n 
1 320 ARG n 
1 321 MET n 
1 322 GLU n 
1 323 ASN n 
1 324 GLY n 
1 325 CYS n 
1 326 LEU n 
1 327 GLU n 
1 328 TRP n 
1 329 TYR n 
1 330 PRO n 
1 331 GLU n 
1 332 PHE n 
1 333 ASP n 
1 334 LYS n 
1 335 PRO n 
1 336 LEU n 
1 337 GLY n 
1 338 LYS n 
1 339 PRO n 
1 340 VAL n 
1 341 GLY n 
1 342 GLU n 
1 343 MET n 
1 344 VAL n 
1 345 ARG n 
1 346 ASP n 
1 347 GLY n 
1 348 TRP n 
1 349 LYS n 
1 350 LEU n 
1 351 SER n 
1 352 ARG n 
1 353 GLU n 
1 354 TYR n 
1 355 LYS n 
1 356 HIS n 
1 357 ALA n 
1 358 SER n 
1 359 VAL n 
1 360 ARG n 
1 361 VAL n 
1 362 ASP n 
1 363 LEU n 
1 364 GLU n 
1 365 SER n 
1 366 LYS n 
1 367 GLU n 
1 368 ALA n 
1 369 GLU n 
1 370 ILE n 
1 371 ARG n 
1 372 TRP n 
1 373 ARG 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                   373 
_entity_src_gen.gene_src_common_name               ? 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 K239x_02140 
_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      'Planctomycetes bacterium K23_9' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     1930275 
_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 BL21(DE3)' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     469008 
_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 
ALA 'L-peptide linking' y ALANINE         ?                 'C3 H7 N O2'     89.093  
ARG 'L-peptide linking' y ARGININE        ?                 'C6 H15 N4 O2 1' 175.209 
ASN 'L-peptide linking' y ASPARAGINE      ?                 'C4 H8 N2 O3'    132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID' ?                 'C4 H7 N O4'     133.103 
CYS 'L-peptide linking' y CYSTEINE        ?                 'C3 H7 N O2 S'   121.158 
EDO non-polymer         . 1,2-ETHANEDIOL  'ETHYLENE GLYCOL' 'C2 H6 O2'       62.068  
GLN 'L-peptide linking' y GLUTAMINE       ?                 'C5 H10 N2 O3'   146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID' ?                 'C5 H9 N O4'     147.129 
GLY 'peptide linking'   y GLYCINE         ?                 'C2 H5 N O2'     75.067  
HIS 'L-peptide linking' y HISTIDINE       ?                 'C6 H10 N3 O2 1' 156.162 
HOH non-polymer         . WATER           ?                 'H2 O'           18.015  
ILE 'L-peptide linking' y ISOLEUCINE      ?                 'C6 H13 N O2'    131.173 
LEU 'L-peptide linking' y LEUCINE         ?                 'C6 H13 N O2'    131.173 
LYS 'L-peptide linking' y LYSINE          ?                 'C6 H15 N2 O2 1' 147.195 
MET 'L-peptide linking' y METHIONINE      ?                 'C5 H11 N O2 S'  149.211 
PHE 'L-peptide linking' y PHENYLALANINE   ?                 'C9 H11 N O2'    165.189 
PRO 'L-peptide linking' y PROLINE         ?                 'C5 H9 N O2'     115.130 
SER 'L-peptide linking' y SERINE          ?                 'C3 H7 N O3'     105.093 
THR 'L-peptide linking' y THREONINE       ?                 'C4 H9 N O3'     119.119 
TRP 'L-peptide linking' y TRYPTOPHAN      ?                 'C11 H12 N2 O2'  204.225 
TYR 'L-peptide linking' y TYROSINE        ?                 'C9 H11 N O3'    181.189 
VAL 'L-peptide linking' y VALINE          ?                 'C5 H11 N O2'    117.146 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   MET 1   20  ?   ?   ?   A . n 
A 1 2   HIS 2   21  ?   ?   ?   A . n 
A 1 3   HIS 3   22  ?   ?   ?   A . n 
A 1 4   HIS 4   23  ?   ?   ?   A . n 
A 1 5   HIS 5   24  ?   ?   ?   A . n 
A 1 6   HIS 6   25  ?   ?   ?   A . n 
A 1 7   HIS 7   26  ?   ?   ?   A . n 
A 1 8   GLU 8   27  ?   ?   ?   A . n 
A 1 9   ASN 9   28  ?   ?   ?   A . n 
A 1 10  LEU 10  29  ?   ?   ?   A . n 
A 1 11  TYR 11  30  ?   ?   ?   A . n 
A 1 12  PHE 12  31  ?   ?   ?   A . n 
A 1 13  GLN 13  32  ?   ?   ?   A . n 
A 1 14  GLY 14  33  ?   ?   ?   A . n 
A 1 15  SER 15  34  ?   ?   ?   A . n 
A 1 16  GLY 16  35  ?   ?   ?   A . n 
A 1 17  ASP 17  36  ?   ?   ?   A . n 
A 1 18  GLU 18  37  37  GLU GLU A . n 
A 1 19  SER 19  38  38  SER SER A . n 
A 1 20  HIS 20  39  39  HIS HIS A . n 
A 1 21  TYR 21  40  40  TYR TYR A . n 
A 1 22  PRO 22  41  41  PRO PRO A . n 
A 1 23  GLU 23  42  42  GLU GLU A . n 
A 1 24  PHE 24  43  43  PHE PHE A . n 
A 1 25  SER 25  44  44  SER SER A . n 
A 1 26  TRP 26  45  45  TRP TRP A . n 
A 1 27  ASP 27  46  46  ASP ASP A . n 
A 1 28  THR 28  47  47  THR THR A . n 
A 1 29  VAL 29  48  48  VAL VAL A . n 
A 1 30  PRO 30  49  49  PRO PRO A . n 
A 1 31  ILE 31  50  50  ILE ILE A . n 
A 1 32  ALA 32  51  51  ALA ALA A . n 
A 1 33  PHE 33  52  52  PHE PHE A . n 
A 1 34  HIS 34  53  53  HIS HIS A . n 
A 1 35  PHE 35  54  54  PHE PHE A . n 
A 1 36  GLY 36  55  55  GLY GLY A . n 
A 1 37  LYS 37  56  56  LYS LYS A . n 
A 1 38  SER 38  57  57  SER SER A . n 
A 1 39  GLN 39  58  58  GLN GLN A . n 
A 1 40  GLY 40  59  59  GLY GLY A . n 
A 1 41  LEU 41  60  60  LEU LEU A . n 
A 1 42  LEU 42  61  61  LEU LEU A . n 
A 1 43  THR 43  62  62  THR THR A . n 
A 1 44  LYS 44  63  63  LYS LYS A . n 
A 1 45  GLU 45  64  64  GLU GLU A . n 
A 1 46  GLU 46  65  65  GLU GLU A . n 
A 1 47  ALA 47  66  66  ALA ALA A . n 
A 1 48  GLU 48  67  67  GLU GLU A . n 
A 1 49  PHE 49  68  68  PHE PHE A . n 
A 1 50  VAL 50  69  69  VAL VAL A . n 
A 1 51  ALA 51  70  70  ALA ALA A . n 
A 1 52  THR 52  71  71  THR THR A . n 
A 1 53  ARG 53  72  72  ARG ARG A . n 
A 1 54  SER 54  73  73  SER SER A . n 
A 1 55  ASN 55  74  74  ASN ASN A . n 
A 1 56  PHE 56  75  75  PHE PHE A . n 
A 1 57  ILE 57  76  76  ILE ILE A . n 
A 1 58  CYS 58  77  77  CYS CYS A . n 
A 1 59  LEU 59  78  78  LEU LEU A . n 
A 1 60  GLU 60  79  79  GLU GLU A . n 
A 1 61  LYS 61  80  80  LYS LYS A . n 
A 1 62  GLY 62  81  81  GLY GLY A . n 
A 1 63  HIS 63  82  82  HIS HIS A . n 
A 1 64  ALA 64  83  83  ALA ALA A . n 
A 1 65  THR 65  84  84  THR THR A . n 
A 1 66  ARG 66  85  85  ARG ARG A . n 
A 1 67  THR 67  86  86  THR THR A . n 
A 1 68  HIS 68  87  87  HIS HIS A . n 
A 1 69  GLY 69  88  88  GLY GLY A . n 
A 1 70  THR 70  89  89  THR THR A . n 
A 1 71  THR 71  90  90  THR THR A . n 
A 1 72  GLU 72  91  91  GLU GLU A . n 
A 1 73  ALA 73  92  92  ALA ALA A . n 
A 1 74  GLY 74  93  93  GLY GLY A . n 
A 1 75  ILE 75  94  94  ILE ILE A . n 
A 1 76  GLU 76  95  95  GLU GLU A . n 
A 1 77  ALA 77  96  96  ALA ALA A . n 
A 1 78  GLU 78  97  97  GLU GLU A . n 
A 1 79  ALA 79  98  98  ALA ALA A . n 
A 1 80  ARG 80  99  99  ARG ARG A . n 
A 1 81  GLN 81  100 100 GLN GLN A . n 
A 1 82  LEU 82  101 101 LEU LEU A . n 
A 1 83  LYS 83  102 102 LYS LYS A . n 
A 1 84  ASN 84  103 103 ASN ASN A . n 
A 1 85  LEU 85  104 104 LEU LEU A . n 
A 1 86  ASN 86  105 105 ASN ASN A . n 
A 1 87  PRO 87  106 106 PRO PRO A . n 
A 1 88  LYS 88  107 107 LYS LYS A . n 
A 1 89  MET 89  108 108 MET MET A . n 
A 1 90  LYS 90  109 109 LYS LYS A . n 
A 1 91  VAL 91  110 110 VAL VAL A . n 
A 1 92  ILE 92  111 111 ILE ILE A . n 
A 1 93  PHE 93  112 112 PHE PHE A . n 
A 1 94  TYR 94  113 113 TYR TYR A . n 
A 1 95  TRP 95  114 114 TRP TRP A . n 
A 1 96  ASN 96  115 115 ASN ASN A . n 
A 1 97  THR 97  116 116 THR THR A . n 
A 1 98  PHE 98  117 117 PHE PHE A . n 
A 1 99  LEU 99  118 118 LEU LEU A . n 
A 1 100 ASP 100 119 119 ASP ASP A . n 
A 1 101 TYR 101 120 120 TYR TYR A . n 
A 1 102 SER 102 121 121 SER SER A . n 
A 1 103 MET 103 122 122 MET MET A . n 
A 1 104 PHE 104 123 123 PHE PHE A . n 
A 1 105 ALA 105 124 124 ALA ALA A . n 
A 1 106 ALA 106 125 125 ALA ALA A . n 
A 1 107 HIS 107 126 126 HIS HIS A . n 
A 1 108 LYS 108 127 127 LYS LYS A . n 
A 1 109 GLU 109 128 128 GLU GLU A . n 
A 1 110 TYR 110 129 129 TYR TYR A . n 
A 1 111 ALA 111 130 130 ALA ALA A . n 
A 1 112 LYS 112 131 131 LYS LYS A . n 
A 1 113 HIS 113 132 132 HIS HIS A . n 
A 1 114 PRO 114 133 133 PRO PRO A . n 
A 1 115 GLN 115 134 134 GLN GLN A . n 
A 1 116 TRP 116 135 135 TRP TRP A . n 
A 1 117 TRP 117 136 136 TRP TRP A . n 
A 1 118 LEU 118 137 137 LEU LEU A . n 
A 1 119 ARG 119 138 138 ARG ARG A . n 
A 1 120 THR 120 139 139 THR THR A . n 
A 1 121 THR 121 140 140 THR THR A . n 
A 1 122 THR 122 141 141 THR THR A . n 
A 1 123 GLY 123 142 142 GLY GLY A . n 
A 1 124 GLU 124 143 143 GLU GLU A . n 
A 1 125 LEU 125 144 144 LEU LEU A . n 
A 1 126 ASP 126 145 145 ASP ASP A . n 
A 1 127 ARG 127 146 146 ARG ARG A . n 
A 1 128 LYS 128 147 147 LYS LYS A . n 
A 1 129 LYS 129 148 148 LYS LYS A . n 
A 1 130 GLY 130 149 149 GLY GLY A . n 
A 1 131 GLN 131 150 150 GLN GLN A . n 
A 1 132 LEU 132 151 151 LEU LEU A . n 
A 1 133 MET 133 152 152 MET MET A . n 
A 1 134 ARG 134 153 153 ARG ARG A . n 
A 1 135 TYR 135 154 154 TYR TYR A . n 
A 1 136 ASP 136 155 155 ASP ASP A . n 
A 1 137 LEU 137 156 156 LEU LEU A . n 
A 1 138 SER 138 157 157 SER SER A . n 
A 1 139 ASN 139 158 158 ASN ASN A . n 
A 1 140 ALA 140 159 159 ALA ALA A . n 
A 1 141 GLU 141 160 160 GLU GLU A . n 
A 1 142 PHE 142 161 161 PHE PHE A . n 
A 1 143 ARG 143 162 162 ARG ARG A . n 
A 1 144 ASN 144 163 163 ASN ASN A . n 
A 1 145 TRP 145 164 164 TRP TRP A . n 
A 1 146 TRP 146 165 165 TRP TRP A . n 
A 1 147 THR 147 166 166 THR THR A . n 
A 1 148 ASN 148 167 167 ASN ASN A . n 
A 1 149 VAL 149 168 168 VAL VAL A . n 
A 1 150 ALA 150 169 169 ALA ALA A . n 
A 1 151 ALA 151 170 170 ALA ALA A . n 
A 1 152 LYS 152 171 171 LYS LYS A . n 
A 1 153 ALA 153 172 172 ALA ALA A . n 
A 1 154 VAL 154 173 173 VAL VAL A . n 
A 1 155 VAL 155 174 174 VAL VAL A . n 
A 1 156 ASP 156 175 175 ASP ASP A . n 
A 1 157 GLY 157 176 176 GLY GLY A . n 
A 1 158 THR 158 177 177 THR THR A . n 
A 1 159 CYS 159 178 178 CYS CYS A . n 
A 1 160 ASP 160 179 179 ASP ASP A . n 
A 1 161 GLY 161 180 180 GLY GLY A . n 
A 1 162 VAL 162 181 181 VAL VAL A . n 
A 1 163 PHE 163 182 182 PHE PHE A . n 
A 1 164 MET 164 183 183 MET MET A . n 
A 1 165 ASP 165 184 184 ASP ASP A . n 
A 1 166 ALA 166 185 185 ALA ALA A . n 
A 1 167 PHE 167 186 186 PHE PHE A . n 
A 1 168 PRO 168 187 187 PRO PRO A . n 
A 1 169 GLN 169 188 188 GLN GLN A . n 
A 1 170 ILE 170 189 189 ILE ILE A . n 
A 1 171 ALA 171 190 190 ALA ALA A . n 
A 1 172 SER 172 191 191 SER SER A . n 
A 1 173 GLN 173 192 192 GLN GLN A . n 
A 1 174 ALA 174 193 193 ALA ALA A . n 
A 1 175 ASN 175 194 194 ASN ASN A . n 
A 1 176 ARG 176 195 195 ARG ARG A . n 
A 1 177 LYS 177 196 196 LYS LYS A . n 
A 1 178 LEU 178 197 197 LEU LEU A . n 
A 1 179 TRP 179 198 198 TRP TRP A . n 
A 1 180 GLY 180 199 199 GLY GLY A . n 
A 1 181 ASP 181 200 200 ASP ASP A . n 
A 1 182 GLU 182 201 201 GLU GLU A . n 
A 1 183 LYS 183 202 202 LYS LYS A . n 
A 1 184 PHE 184 203 203 PHE PHE A . n 
A 1 185 GLU 185 204 204 GLU GLU A . n 
A 1 186 ALA 186 205 205 ALA ALA A . n 
A 1 187 ILE 187 206 206 ILE ILE A . n 
A 1 188 GLN 188 207 207 GLN GLN A . n 
A 1 189 GLN 189 208 208 GLN GLN A . n 
A 1 190 GLY 190 209 209 GLY GLY A . n 
A 1 191 LEU 191 210 210 LEU LEU A . n 
A 1 192 GLN 192 211 211 GLN GLN A . n 
A 1 193 ASP 193 212 212 ASP ASP A . n 
A 1 194 ILE 194 213 213 ILE ILE A . n 
A 1 195 ILE 195 214 214 ILE ILE A . n 
A 1 196 GLN 196 215 215 GLN GLN A . n 
A 1 197 GLU 197 216 216 GLU GLU A . n 
A 1 198 THR 198 217 217 THR THR A . n 
A 1 199 ARG 199 218 218 ARG ARG A . n 
A 1 200 GLN 200 219 219 GLN GLN A . n 
A 1 201 LYS 201 220 220 LYS LYS A . n 
A 1 202 ILE 202 221 221 ILE ILE A . n 
A 1 203 GLY 203 222 222 GLY GLY A . n 
A 1 204 ASP 204 223 223 ASP ASP A . n 
A 1 205 ASP 205 224 224 ASP ASP A . n 
A 1 206 LYS 206 225 225 LYS LYS A . n 
A 1 207 LEU 207 226 226 LEU LEU A . n 
A 1 208 ILE 208 227 227 ILE ILE A . n 
A 1 209 VAL 209 228 228 VAL VAL A . n 
A 1 210 TYR 210 229 229 TYR TYR A . n 
A 1 211 ASN 211 230 230 ASN ASN A . n 
A 1 212 GLY 212 231 231 GLY GLY A . n 
A 1 213 ILE 213 232 232 ILE ILE A . n 
A 1 214 ARG 214 233 233 ARG ARG A . n 
A 1 215 SER 215 234 234 SER SER A . n 
A 1 216 THR 216 235 235 THR THR A . n 
A 1 217 PRO 217 236 236 PRO PRO A . n 
A 1 218 ASP 218 237 237 ASP ASP A . n 
A 1 219 TRP 219 238 238 TRP TRP A . n 
A 1 220 SER 220 239 239 SER SER A . n 
A 1 221 ALA 221 240 240 ALA ALA A . n 
A 1 222 GLY 222 241 241 GLY GLY A . n 
A 1 223 PHE 223 242 242 PHE PHE A . n 
A 1 224 ASP 224 243 243 ASP ASP A . n 
A 1 225 PHE 225 244 244 PHE PHE A . n 
A 1 226 ALA 226 245 245 ALA ALA A . n 
A 1 227 GLU 227 246 246 GLU GLU A . n 
A 1 228 TYR 228 247 247 TYR TYR A . n 
A 1 229 THR 229 248 248 THR THR A . n 
A 1 230 ASP 230 249 249 ASP ASP A . n 
A 1 231 ALA 231 250 250 ALA ALA A . n 
A 1 232 ALA 232 251 251 ALA ALA A . n 
A 1 233 MET 233 252 252 MET MET A . n 
A 1 234 ILE 234 253 253 ILE ILE A . n 
A 1 235 GLU 235 254 254 GLU GLU A . n 
A 1 236 HIS 236 255 255 HIS HIS A . n 
A 1 237 PHE 237 256 256 PHE PHE A . n 
A 1 238 GLY 238 257 257 GLY GLY A . n 
A 1 239 HIS 239 258 258 HIS HIS A . n 
A 1 240 PHE 240 259 259 PHE PHE A . n 
A 1 241 GLN 241 260 260 GLN GLN A . n 
A 1 242 SER 242 261 261 SER SER A . n 
A 1 243 ALA 243 262 262 ALA ALA A . n 
A 1 244 SER 244 263 263 SER SER A . n 
A 1 245 LYS 245 264 264 LYS LYS A . n 
A 1 246 GLU 246 265 265 GLU GLU A . n 
A 1 247 THR 247 266 266 THR THR A . n 
A 1 248 MET 248 267 267 MET MET A . n 
A 1 249 LEU 249 268 268 LEU LEU A . n 
A 1 250 ARG 250 269 269 ARG ARG A . n 
A 1 251 ASP 251 270 270 ASP ASP A . n 
A 1 252 ILE 252 271 271 ILE ILE A . n 
A 1 253 LEU 253 272 272 LEU LEU A . n 
A 1 254 GLU 254 273 273 GLU GLU A . n 
A 1 255 MET 255 274 274 MET MET A . n 
A 1 256 GLN 256 275 275 GLN GLN A . n 
A 1 257 ARG 257 276 276 ARG ARG A . n 
A 1 258 ALA 258 277 277 ALA ALA A . n 
A 1 259 ALA 259 278 278 ALA ALA A . n 
A 1 260 LYS 260 279 279 LYS LYS A . n 
A 1 261 ALA 261 280 280 ALA ALA A . n 
A 1 262 GLY 262 281 281 GLY GLY A . n 
A 1 263 LYS 263 282 282 LYS LYS A . n 
A 1 264 ILE 264 283 283 ILE ILE A . n 
A 1 265 VAL 265 284 284 VAL VAL A . n 
A 1 266 VAL 266 285 285 VAL VAL A . n 
A 1 267 LEU 267 286 286 LEU LEU A . n 
A 1 268 LYS 268 287 287 LYS LYS A . n 
A 1 269 GLY 269 288 288 GLY GLY A . n 
A 1 270 TRP 270 289 289 TRP TRP A . n 
A 1 271 ALA 271 290 290 ALA ALA A . n 
A 1 272 GLY 272 291 291 GLY GLY A . n 
A 1 273 PHE 273 292 292 PHE PHE A . n 
A 1 274 THR 274 293 293 THR THR A . n 
A 1 275 PHE 275 294 294 PHE PHE A . n 
A 1 276 ILE 276 295 295 ILE ILE A . n 
A 1 277 ASP 277 296 296 ASP ASP A . n 
A 1 278 ASP 278 297 297 ASP ASP A . n 
A 1 279 GLN 279 298 298 GLN GLN A . n 
A 1 280 ALA 280 299 299 ALA ALA A . n 
A 1 281 MET 281 300 300 MET MET A . n 
A 1 282 ARG 282 301 301 ARG ARG A . n 
A 1 283 LYS 283 302 302 LYS LYS A . n 
A 1 284 PRO 284 303 303 PRO PRO A . n 
A 1 285 LEU 285 304 304 LEU LEU A . n 
A 1 286 THR 286 305 305 THR THR A . n 
A 1 287 GLN 287 306 306 GLN GLN A . n 
A 1 288 LYS 288 307 307 LYS LYS A . n 
A 1 289 ARG 289 308 308 ARG ARG A . n 
A 1 290 ARG 290 309 309 ARG ARG A . n 
A 1 291 VAL 291 310 310 VAL VAL A . n 
A 1 292 ALA 292 311 311 ALA ALA A . n 
A 1 293 LYS 293 312 312 LYS LYS A . n 
A 1 294 ASP 294 313 313 ASP ASP A . n 
A 1 295 SER 295 314 314 SER SER A . n 
A 1 296 LEU 296 315 315 LEU LEU A . n 
A 1 297 LYS 297 316 316 LYS LYS A . n 
A 1 298 PHE 298 317 317 PHE PHE A . n 
A 1 299 PRO 299 318 318 PRO PRO A . n 
A 1 300 LEU 300 319 319 LEU LEU A . n 
A 1 301 ALA 301 320 320 ALA ALA A . n 
A 1 302 CYS 302 321 321 CYS CYS A . n 
A 1 303 PHE 303 322 322 PHE PHE A . n 
A 1 304 LEU 304 323 323 LEU LEU A . n 
A 1 305 ALA 305 324 324 ALA ALA A . n 
A 1 306 GLY 306 325 325 GLY GLY A . n 
A 1 307 ALA 307 326 326 ALA ALA A . n 
A 1 308 GLN 308 327 327 GLN GLN A . n 
A 1 309 GLU 309 328 328 GLU GLU A . n 
A 1 310 ASN 310 329 329 ASN ASN A . n 
A 1 311 CYS 311 330 330 CYS CYS A . n 
A 1 312 TYR 312 331 331 TYR TYR A . n 
A 1 313 PHE 313 332 332 PHE PHE A . n 
A 1 314 ILE 314 333 333 ILE ILE A . n 
A 1 315 TYR 315 334 334 TYR TYR A . n 
A 1 316 ASN 316 335 335 ASN ASN A . n 
A 1 317 TRP 317 336 336 TRP TRP A . n 
A 1 318 GLY 318 337 337 GLY GLY A . n 
A 1 319 TYR 319 338 338 TYR TYR A . n 
A 1 320 ARG 320 339 339 ARG ARG A . n 
A 1 321 MET 321 340 340 MET MET A . n 
A 1 322 GLU 322 341 341 GLU GLU A . n 
A 1 323 ASN 323 342 342 ASN ASN A . n 
A 1 324 GLY 324 343 343 GLY GLY A . n 
A 1 325 CYS 325 344 344 CYS CYS A . n 
A 1 326 LEU 326 345 345 LEU LEU A . n 
A 1 327 GLU 327 346 346 GLU GLU A . n 
A 1 328 TRP 328 347 347 TRP TRP A . n 
A 1 329 TYR 329 348 348 TYR TYR A . n 
A 1 330 PRO 330 349 349 PRO PRO A . n 
A 1 331 GLU 331 350 350 GLU GLU A . n 
A 1 332 PHE 332 351 351 PHE PHE A . n 
A 1 333 ASP 333 352 352 ASP ASP A . n 
A 1 334 LYS 334 353 353 LYS LYS A . n 
A 1 335 PRO 335 354 354 PRO PRO A . n 
A 1 336 LEU 336 355 355 LEU LEU A . n 
A 1 337 GLY 337 356 356 GLY GLY A . n 
A 1 338 LYS 338 357 357 LYS LYS A . n 
A 1 339 PRO 339 358 358 PRO PRO A . n 
A 1 340 VAL 340 359 359 VAL VAL A . n 
A 1 341 GLY 341 360 360 GLY GLY A . n 
A 1 342 GLU 342 361 361 GLU GLU A . n 
A 1 343 MET 343 362 362 MET MET A . n 
A 1 344 VAL 344 363 363 VAL VAL A . n 
A 1 345 ARG 345 364 364 ARG ARG A . n 
A 1 346 ASP 346 365 365 ASP ASP A . n 
A 1 347 GLY 347 366 366 GLY GLY A . n 
A 1 348 TRP 348 367 367 TRP TRP A . n 
A 1 349 LYS 349 368 368 LYS LYS A . n 
A 1 350 LEU 350 369 369 LEU LEU A . n 
A 1 351 SER 351 370 370 SER SER A . n 
A 1 352 ARG 352 371 371 ARG ARG A . n 
A 1 353 GLU 353 372 372 GLU GLU A . n 
A 1 354 TYR 354 373 373 TYR TYR A . n 
A 1 355 LYS 355 374 374 LYS LYS A . n 
A 1 356 HIS 356 375 375 HIS HIS A . n 
A 1 357 ALA 357 376 376 ALA ALA A . n 
A 1 358 SER 358 377 377 SER SER A . n 
A 1 359 VAL 359 378 378 VAL VAL A . n 
A 1 360 ARG 360 379 379 ARG ARG A . n 
A 1 361 VAL 361 380 380 VAL VAL A . n 
A 1 362 ASP 362 381 381 ASP ASP A . n 
A 1 363 LEU 363 382 382 LEU LEU A . n 
A 1 364 GLU 364 383 383 GLU GLU A . n 
A 1 365 SER 365 384 384 SER SER A . n 
A 1 366 LYS 366 385 385 LYS LYS A . n 
A 1 367 GLU 367 386 386 GLU GLU A . n 
A 1 368 ALA 368 387 387 ALA ALA A . n 
A 1 369 GLU 369 388 388 GLU GLU A . n 
A 1 370 ILE 370 389 389 ILE ILE A . n 
A 1 371 ARG 371 390 390 ARG ARG A . n 
A 1 372 TRP 372 391 391 TRP TRP A . n 
A 1 373 ARG 373 392 392 ARG ARG A . n 
# 
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 EDO 1   401 0   EDO EDO A . 
C 2 EDO 1   402 1   EDO EDO A . 
D 3 HOH 1   501 7   HOH HOH A . 
D 3 HOH 2   502 211 HOH HOH A . 
D 3 HOH 3   503 228 HOH HOH A . 
D 3 HOH 4   504 255 HOH HOH A . 
D 3 HOH 5   505 116 HOH HOH A . 
D 3 HOH 6   506 170 HOH HOH A . 
D 3 HOH 7   507 149 HOH HOH A . 
D 3 HOH 8   508 279 HOH HOH A . 
D 3 HOH 9   509 100 HOH HOH A . 
D 3 HOH 10  510 157 HOH HOH A . 
D 3 HOH 11  511 240 HOH HOH A . 
D 3 HOH 12  512 110 HOH HOH A . 
D 3 HOH 13  513 60  HOH HOH A . 
D 3 HOH 14  514 34  HOH HOH A . 
D 3 HOH 15  515 119 HOH HOH A . 
D 3 HOH 16  516 186 HOH HOH A . 
D 3 HOH 17  517 111 HOH HOH A . 
D 3 HOH 18  518 167 HOH HOH A . 
D 3 HOH 19  519 79  HOH HOH A . 
D 3 HOH 20  520 30  HOH HOH A . 
D 3 HOH 21  521 263 HOH HOH A . 
D 3 HOH 22  522 253 HOH HOH A . 
D 3 HOH 23  523 147 HOH HOH A . 
D 3 HOH 24  524 58  HOH HOH A . 
D 3 HOH 25  525 139 HOH HOH A . 
D 3 HOH 26  526 115 HOH HOH A . 
D 3 HOH 27  527 230 HOH HOH A . 
D 3 HOH 28  528 166 HOH HOH A . 
D 3 HOH 29  529 243 HOH HOH A . 
D 3 HOH 30  530 4   HOH HOH A . 
D 3 HOH 31  531 2   HOH HOH A . 
D 3 HOH 32  532 247 HOH HOH A . 
D 3 HOH 33  533 241 HOH HOH A . 
D 3 HOH 34  534 112 HOH HOH A . 
D 3 HOH 35  535 236 HOH HOH A . 
D 3 HOH 36  536 1   HOH HOH A . 
D 3 HOH 37  537 130 HOH HOH A . 
D 3 HOH 38  538 165 HOH HOH A . 
D 3 HOH 39  539 68  HOH HOH A . 
D 3 HOH 40  540 212 HOH HOH A . 
D 3 HOH 41  541 182 HOH HOH A . 
D 3 HOH 42  542 28  HOH HOH A . 
D 3 HOH 43  543 185 HOH HOH A . 
D 3 HOH 44  544 75  HOH HOH A . 
D 3 HOH 45  545 153 HOH HOH A . 
D 3 HOH 46  546 26  HOH HOH A . 
D 3 HOH 47  547 304 HOH HOH A . 
D 3 HOH 48  548 14  HOH HOH A . 
D 3 HOH 49  549 114 HOH HOH A . 
D 3 HOH 50  550 76  HOH HOH A . 
D 3 HOH 51  551 71  HOH HOH A . 
D 3 HOH 52  552 320 HOH HOH A . 
D 3 HOH 53  553 61  HOH HOH A . 
D 3 HOH 54  554 122 HOH HOH A . 
D 3 HOH 55  555 20  HOH HOH A . 
D 3 HOH 56  556 6   HOH HOH A . 
D 3 HOH 57  557 249 HOH HOH A . 
D 3 HOH 58  558 95  HOH HOH A . 
D 3 HOH 59  559 125 HOH HOH A . 
D 3 HOH 60  560 12  HOH HOH A . 
D 3 HOH 61  561 66  HOH HOH A . 
D 3 HOH 62  562 45  HOH HOH A . 
D 3 HOH 63  563 190 HOH HOH A . 
D 3 HOH 64  564 220 HOH HOH A . 
D 3 HOH 65  565 89  HOH HOH A . 
D 3 HOH 66  566 289 HOH HOH A . 
D 3 HOH 67  567 288 HOH HOH A . 
D 3 HOH 68  568 221 HOH HOH A . 
D 3 HOH 69  569 16  HOH HOH A . 
D 3 HOH 70  570 177 HOH HOH A . 
D 3 HOH 71  571 104 HOH HOH A . 
D 3 HOH 72  572 78  HOH HOH A . 
D 3 HOH 73  573 5   HOH HOH A . 
D 3 HOH 74  574 232 HOH HOH A . 
D 3 HOH 75  575 128 HOH HOH A . 
D 3 HOH 76  576 67  HOH HOH A . 
D 3 HOH 77  577 19  HOH HOH A . 
D 3 HOH 78  578 150 HOH HOH A . 
D 3 HOH 79  579 265 HOH HOH A . 
D 3 HOH 80  580 52  HOH HOH A . 
D 3 HOH 81  581 127 HOH HOH A . 
D 3 HOH 82  582 65  HOH HOH A . 
D 3 HOH 83  583 96  HOH HOH A . 
D 3 HOH 84  584 148 HOH HOH A . 
D 3 HOH 85  585 97  HOH HOH A . 
D 3 HOH 86  586 142 HOH HOH A . 
D 3 HOH 87  587 63  HOH HOH A . 
D 3 HOH 88  588 88  HOH HOH A . 
D 3 HOH 89  589 117 HOH HOH A . 
D 3 HOH 90  590 33  HOH HOH A . 
D 3 HOH 91  591 179 HOH HOH A . 
D 3 HOH 92  592 214 HOH HOH A . 
D 3 HOH 93  593 306 HOH HOH A . 
D 3 HOH 94  594 204 HOH HOH A . 
D 3 HOH 95  595 231 HOH HOH A . 
D 3 HOH 96  596 250 HOH HOH A . 
D 3 HOH 97  597 24  HOH HOH A . 
D 3 HOH 98  598 257 HOH HOH A . 
D 3 HOH 99  599 64  HOH HOH A . 
D 3 HOH 100 600 93  HOH HOH A . 
D 3 HOH 101 601 291 HOH HOH A . 
D 3 HOH 102 602 77  HOH HOH A . 
D 3 HOH 103 603 109 HOH HOH A . 
D 3 HOH 104 604 296 HOH HOH A . 
D 3 HOH 105 605 32  HOH HOH A . 
D 3 HOH 106 606 151 HOH HOH A . 
D 3 HOH 107 607 290 HOH HOH A . 
D 3 HOH 108 608 55  HOH HOH A . 
D 3 HOH 109 609 39  HOH HOH A . 
D 3 HOH 110 610 176 HOH HOH A . 
D 3 HOH 111 611 178 HOH HOH A . 
D 3 HOH 112 612 126 HOH HOH A . 
D 3 HOH 113 613 13  HOH HOH A . 
D 3 HOH 114 614 42  HOH HOH A . 
D 3 HOH 115 615 196 HOH HOH A . 
D 3 HOH 116 616 234 HOH HOH A . 
D 3 HOH 117 617 70  HOH HOH A . 
D 3 HOH 118 618 174 HOH HOH A . 
D 3 HOH 119 619 207 HOH HOH A . 
D 3 HOH 120 620 168 HOH HOH A . 
D 3 HOH 121 621 10  HOH HOH A . 
D 3 HOH 122 622 144 HOH HOH A . 
D 3 HOH 123 623 252 HOH HOH A . 
D 3 HOH 124 624 27  HOH HOH A . 
D 3 HOH 125 625 83  HOH HOH A . 
D 3 HOH 126 626 29  HOH HOH A . 
D 3 HOH 127 627 160 HOH HOH A . 
D 3 HOH 128 628 99  HOH HOH A . 
D 3 HOH 129 629 8   HOH HOH A . 
D 3 HOH 130 630 38  HOH HOH A . 
D 3 HOH 131 631 342 HOH HOH A . 
D 3 HOH 132 632 44  HOH HOH A . 
D 3 HOH 133 633 298 HOH HOH A . 
D 3 HOH 134 634 261 HOH HOH A . 
D 3 HOH 135 635 87  HOH HOH A . 
D 3 HOH 136 636 41  HOH HOH A . 
D 3 HOH 137 637 22  HOH HOH A . 
D 3 HOH 138 638 141 HOH HOH A . 
D 3 HOH 139 639 239 HOH HOH A . 
D 3 HOH 140 640 31  HOH HOH A . 
D 3 HOH 141 641 295 HOH HOH A . 
D 3 HOH 142 642 237 HOH HOH A . 
D 3 HOH 143 643 238 HOH HOH A . 
D 3 HOH 144 644 264 HOH HOH A . 
D 3 HOH 145 645 101 HOH HOH A . 
D 3 HOH 146 646 18  HOH HOH A . 
D 3 HOH 147 647 136 HOH HOH A . 
D 3 HOH 148 648 273 HOH HOH A . 
D 3 HOH 149 649 286 HOH HOH A . 
D 3 HOH 150 650 180 HOH HOH A . 
D 3 HOH 151 651 159 HOH HOH A . 
D 3 HOH 152 652 50  HOH HOH A . 
D 3 HOH 153 653 21  HOH HOH A . 
D 3 HOH 154 654 74  HOH HOH A . 
D 3 HOH 155 655 73  HOH HOH A . 
D 3 HOH 156 656 54  HOH HOH A . 
D 3 HOH 157 657 53  HOH HOH A . 
D 3 HOH 158 658 246 HOH HOH A . 
D 3 HOH 159 659 120 HOH HOH A . 
D 3 HOH 160 660 82  HOH HOH A . 
D 3 HOH 161 661 244 HOH HOH A . 
D 3 HOH 162 662 47  HOH HOH A . 
D 3 HOH 163 663 62  HOH HOH A . 
D 3 HOH 164 664 56  HOH HOH A . 
D 3 HOH 165 665 51  HOH HOH A . 
D 3 HOH 166 666 85  HOH HOH A . 
D 3 HOH 167 667 143 HOH HOH A . 
D 3 HOH 168 668 25  HOH HOH A . 
D 3 HOH 169 669 40  HOH HOH A . 
D 3 HOH 170 670 195 HOH HOH A . 
D 3 HOH 171 671 23  HOH HOH A . 
D 3 HOH 172 672 103 HOH HOH A . 
D 3 HOH 173 673 123 HOH HOH A . 
D 3 HOH 174 674 322 HOH HOH A . 
D 3 HOH 175 675 3   HOH HOH A . 
D 3 HOH 176 676 248 HOH HOH A . 
D 3 HOH 177 677 138 HOH HOH A . 
D 3 HOH 178 678 81  HOH HOH A . 
D 3 HOH 179 679 197 HOH HOH A . 
D 3 HOH 180 680 341 HOH HOH A . 
D 3 HOH 181 681 225 HOH HOH A . 
D 3 HOH 182 682 210 HOH HOH A . 
D 3 HOH 183 683 223 HOH HOH A . 
D 3 HOH 184 684 162 HOH HOH A . 
D 3 HOH 185 685 217 HOH HOH A . 
D 3 HOH 186 686 146 HOH HOH A . 
D 3 HOH 187 687 11  HOH HOH A . 
D 3 HOH 188 688 332 HOH HOH A . 
D 3 HOH 189 689 49  HOH HOH A . 
D 3 HOH 190 690 321 HOH HOH A . 
D 3 HOH 191 691 205 HOH HOH A . 
D 3 HOH 192 692 208 HOH HOH A . 
D 3 HOH 193 693 326 HOH HOH A . 
D 3 HOH 194 694 181 HOH HOH A . 
D 3 HOH 195 695 36  HOH HOH A . 
D 3 HOH 196 696 102 HOH HOH A . 
D 3 HOH 197 697 86  HOH HOH A . 
D 3 HOH 198 698 189 HOH HOH A . 
D 3 HOH 199 699 107 HOH HOH A . 
D 3 HOH 200 700 37  HOH HOH A . 
D 3 HOH 201 701 281 HOH HOH A . 
D 3 HOH 202 702 43  HOH HOH A . 
D 3 HOH 203 703 284 HOH HOH A . 
D 3 HOH 204 704 72  HOH HOH A . 
D 3 HOH 205 705 275 HOH HOH A . 
D 3 HOH 206 706 48  HOH HOH A . 
D 3 HOH 207 707 131 HOH HOH A . 
D 3 HOH 208 708 307 HOH HOH A . 
D 3 HOH 209 709 80  HOH HOH A . 
D 3 HOH 210 710 161 HOH HOH A . 
D 3 HOH 211 711 140 HOH HOH A . 
D 3 HOH 212 712 145 HOH HOH A . 
D 3 HOH 213 713 262 HOH HOH A . 
D 3 HOH 214 714 222 HOH HOH A . 
D 3 HOH 215 715 191 HOH HOH A . 
D 3 HOH 216 716 91  HOH HOH A . 
D 3 HOH 217 717 15  HOH HOH A . 
D 3 HOH 218 718 277 HOH HOH A . 
D 3 HOH 219 719 137 HOH HOH A . 
D 3 HOH 220 720 219 HOH HOH A . 
D 3 HOH 221 721 57  HOH HOH A . 
D 3 HOH 222 722 283 HOH HOH A . 
D 3 HOH 223 723 227 HOH HOH A . 
D 3 HOH 224 724 17  HOH HOH A . 
D 3 HOH 225 725 339 HOH HOH A . 
D 3 HOH 226 726 215 HOH HOH A . 
D 3 HOH 227 727 35  HOH HOH A . 
D 3 HOH 228 728 323 HOH HOH A . 
D 3 HOH 229 729 90  HOH HOH A . 
D 3 HOH 230 730 224 HOH HOH A . 
D 3 HOH 231 731 235 HOH HOH A . 
D 3 HOH 232 732 163 HOH HOH A . 
D 3 HOH 233 733 184 HOH HOH A . 
D 3 HOH 234 734 218 HOH HOH A . 
D 3 HOH 235 735 152 HOH HOH A . 
D 3 HOH 236 736 46  HOH HOH A . 
D 3 HOH 237 737 155 HOH HOH A . 
D 3 HOH 238 738 188 HOH HOH A . 
D 3 HOH 239 739 129 HOH HOH A . 
D 3 HOH 240 740 9   HOH HOH A . 
D 3 HOH 241 741 192 HOH HOH A . 
D 3 HOH 242 742 133 HOH HOH A . 
D 3 HOH 243 743 203 HOH HOH A . 
D 3 HOH 244 744 317 HOH HOH A . 
D 3 HOH 245 745 266 HOH HOH A . 
D 3 HOH 246 746 294 HOH HOH A . 
D 3 HOH 247 747 251 HOH HOH A . 
D 3 HOH 248 748 300 HOH HOH A . 
D 3 HOH 249 749 292 HOH HOH A . 
D 3 HOH 250 750 226 HOH HOH A . 
D 3 HOH 251 751 213 HOH HOH A . 
D 3 HOH 252 752 164 HOH HOH A . 
D 3 HOH 253 753 171 HOH HOH A . 
D 3 HOH 254 754 302 HOH HOH A . 
D 3 HOH 255 755 335 HOH HOH A . 
D 3 HOH 256 756 301 HOH HOH A . 
D 3 HOH 257 757 278 HOH HOH A . 
D 3 HOH 258 758 285 HOH HOH A . 
D 3 HOH 259 759 316 HOH HOH A . 
D 3 HOH 260 760 309 HOH HOH A . 
D 3 HOH 261 761 183 HOH HOH A . 
D 3 HOH 262 762 194 HOH HOH A . 
D 3 HOH 263 763 198 HOH HOH A . 
D 3 HOH 264 764 337 HOH HOH A . 
D 3 HOH 265 765 274 HOH HOH A . 
D 3 HOH 266 766 297 HOH HOH A . 
D 3 HOH 267 767 324 HOH HOH A . 
D 3 HOH 268 768 169 HOH HOH A . 
D 3 HOH 269 769 327 HOH HOH A . 
D 3 HOH 270 770 271 HOH HOH A . 
D 3 HOH 271 771 135 HOH HOH A . 
D 3 HOH 272 772 312 HOH HOH A . 
D 3 HOH 273 773 334 HOH HOH A . 
D 3 HOH 274 774 259 HOH HOH A . 
D 3 HOH 275 775 331 HOH HOH A . 
D 3 HOH 276 776 328 HOH HOH A . 
D 3 HOH 277 777 118 HOH HOH A . 
D 3 HOH 278 778 108 HOH HOH A . 
D 3 HOH 279 779 158 HOH HOH A . 
D 3 HOH 280 780 201 HOH HOH A . 
D 3 HOH 281 781 313 HOH HOH A . 
D 3 HOH 282 782 330 HOH HOH A . 
D 3 HOH 283 783 314 HOH HOH A . 
D 3 HOH 284 784 318 HOH HOH A . 
D 3 HOH 285 785 315 HOH HOH A . 
D 3 HOH 286 786 94  HOH HOH A . 
D 3 HOH 287 787 199 HOH HOH A . 
D 3 HOH 288 788 308 HOH HOH A . 
D 3 HOH 289 789 272 HOH HOH A . 
D 3 HOH 290 790 325 HOH HOH A . 
D 3 HOH 291 791 229 HOH HOH A . 
D 3 HOH 292 792 319 HOH HOH A . 
D 3 HOH 293 793 280 HOH HOH A . 
D 3 HOH 294 794 69  HOH HOH A . 
D 3 HOH 295 795 336 HOH HOH A . 
D 3 HOH 296 796 84  HOH HOH A . 
D 3 HOH 297 797 258 HOH HOH A . 
D 3 HOH 298 798 98  HOH HOH A . 
D 3 HOH 299 799 311 HOH HOH A . 
D 3 HOH 300 800 245 HOH HOH A . 
D 3 HOH 301 801 254 HOH HOH A . 
D 3 HOH 302 802 338 HOH HOH A . 
D 3 HOH 303 803 154 HOH HOH A . 
D 3 HOH 304 804 303 HOH HOH A . 
D 3 HOH 305 805 310 HOH HOH A . 
D 3 HOH 306 806 216 HOH HOH A . 
D 3 HOH 307 807 267 HOH HOH A . 
D 3 HOH 308 808 59  HOH HOH A . 
D 3 HOH 309 809 287 HOH HOH A . 
D 3 HOH 310 810 124 HOH HOH A . 
D 3 HOH 311 811 193 HOH HOH A . 
D 3 HOH 312 812 260 HOH HOH A . 
D 3 HOH 313 813 305 HOH HOH A . 
D 3 HOH 314 814 209 HOH HOH A . 
D 3 HOH 315 815 242 HOH HOH A . 
D 3 HOH 316 816 156 HOH HOH A . 
D 3 HOH 317 817 92  HOH HOH A . 
D 3 HOH 318 818 113 HOH HOH A . 
D 3 HOH 319 819 343 HOH HOH A . 
D 3 HOH 320 820 329 HOH HOH A . 
D 3 HOH 321 821 206 HOH HOH A . 
D 3 HOH 322 822 134 HOH HOH A . 
D 3 HOH 323 823 299 HOH HOH A . 
D 3 HOH 324 824 172 HOH HOH A . 
D 3 HOH 325 825 282 HOH HOH A . 
D 3 HOH 326 826 340 HOH HOH A . 
D 3 HOH 327 827 270 HOH HOH A . 
D 3 HOH 328 828 105 HOH HOH A . 
D 3 HOH 329 829 173 HOH HOH A . 
D 3 HOH 330 830 200 HOH HOH A . 
D 3 HOH 331 831 132 HOH HOH A . 
D 3 HOH 332 832 175 HOH HOH A . 
D 3 HOH 333 833 233 HOH HOH A . 
D 3 HOH 334 834 333 HOH HOH A . 
D 3 HOH 335 835 121 HOH HOH A . 
D 3 HOH 336 836 268 HOH HOH A . 
D 3 HOH 337 837 106 HOH HOH A . 
D 3 HOH 338 838 269 HOH HOH A . 
D 3 HOH 339 839 187 HOH HOH A . 
D 3 HOH 340 840 202 HOH HOH A . 
D 3 HOH 341 841 256 HOH HOH A . 
D 3 HOH 342 842 293 HOH HOH A . 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement       ? ? ? ? ? ? ? ? ? ? ? PHENIX ? ? ? '(1.20.1_4487: ???)' 1 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? XDS    ? ? ? .                    2 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? XDS    ? ? ? .                    3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHENIX ? ? ? .                    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                     8RG4 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     50.983 
_cell.length_a_esd                 ? 
_cell.length_b                     84.868 
_cell.length_b_esd                 ? 
_cell.length_c                     90.344 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        4 
_cell.reciprocal_angle_alpha       ? 
_cell.reciprocal_angle_beta        ? 
_cell.reciprocal_angle_gamma       ? 
_cell.reciprocal_angle_alpha_esd   ? 
_cell.reciprocal_angle_beta_esd    ? 
_cell.reciprocal_angle_gamma_esd   ? 
_cell.reciprocal_length_a          ? 
_cell.reciprocal_length_b          ? 
_cell.reciprocal_length_c          ? 
_cell.reciprocal_length_a_esd      ? 
_cell.reciprocal_length_b_esd      ? 
_cell.reciprocal_length_c_esd      ? 
_cell.pdbx_unique_axis             ? 
_cell.pdbx_esd_method              ? 
# 
_symmetry.entry_id                         8RG4 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                19 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 21 21 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                   8RG4 
_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             2.37 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          48.04 
_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    
;Microseeding of PbFucA-1
0.12 M ethylene glycols, 0.1 M buffer system 2 pH 7.5, 30% v/v precipitant mix 2
;
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            293 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS EIGER2 XE 16M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2022-02-26 
_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   0.9686 
_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                        'DIAMOND BEAMLINE I04' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.9686 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   I04 
_diffrn_source.pdbx_synchrotron_site       Diamond 
# 
_reflns.B_iso_Wilson_estimate                          14.30 
_reflns.entry_id                                       8RG4 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.404 
_reflns.d_resolution_low                               9.989 
_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                                     76431 
_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                           99.02 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                13.2 
_reflns.pdbx_netI_over_av_sigmaI                       19.63 
_reflns.pdbx_netI_over_sigmaI                          19.63 
_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                                0.08231 
_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                                   1.0 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.07903 
_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                                    1.404 
_reflns_shell.d_res_low                                     1.454 
_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                             76431 
_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                               13.2 
_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                                  0.999 
_reflns_shell.pdbx_CC_star                                  1.0 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          99.02 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  0.07903 
_reflns_shell.pdbx_Rsym_value                               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal             ? 
_reflns_shell.pdbx_percent_possible_spherical               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous   ? 
_reflns_shell.pdbx_percent_possible_spherical_anomalous     ? 
_reflns_shell.pdbx_redundancy_anomalous                     ? 
_reflns_shell.pdbx_CC_half_anomalous                        ? 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous             ? 
_reflns_shell.pdbx_percent_possible_anomalous               ? 
# 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               14.30 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.details                                  ? 
_refine.diff_density_max                         ? 
_refine.diff_density_max_esd                     ? 
_refine.diff_density_min                         ? 
_refine.diff_density_min_esd                     ? 
_refine.diff_density_rms                         ? 
_refine.diff_density_rms_esd                     ? 
_refine.entry_id                                 8RG4 
_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                            1.404 
_refine.ls_d_res_low                             9.989 
_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                     76417 
_refine.ls_number_reflns_R_free                  3837 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.36 
_refine.ls_percent_reflns_R_free                 5.02 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1440 
_refine.ls_R_factor_R_free                       0.1641 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1429 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    'FLAT BULK SOLVENT MODEL' 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          1.34 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               'FREE R-VALUE' 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       ML 
_refine.pdbx_R_Free_selection_details            0.1635 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             1.10 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.90 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 14.83 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_diffrn_id                           1 
_refine.overall_SU_B                             ? 
_refine.overall_SU_ML                            0.10 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       1.404 
_refine_hist.d_res_low                        9.989 
_refine_hist.number_atoms_solvent             343 
_refine_hist.number_atoms_total               3261 
_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        2910 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         8 
_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 ? 305 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 1.005 ? 412 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 5.705 ? 403 ? f_dihedral_angle_d ? ? 
'X-RAY DIFFRACTION' ? 0.082 ? 413 ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.009 ? 535 ? f_plane_restr      ? ? 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_obs 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.redundancy_reflns_all 
_refine_ls_shell.redundancy_reflns_obs 
_refine_ls_shell.wR_factor_all 
_refine_ls_shell.wR_factor_obs 
_refine_ls_shell.wR_factor_R_free 
_refine_ls_shell.wR_factor_R_work 
_refine_ls_shell.pdbx_R_complete 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.pdbx_phase_error 
_refine_ls_shell.pdbx_fsc_work 
_refine_ls_shell.pdbx_fsc_free 
_refine_ls_shell.R_factor_R_free 
'X-RAY DIFFRACTION' 1.404 1.42  . . 109 2257 83.00  . . . . 0.1998 . . . . . . . . . . . 0.2619 
'X-RAY DIFFRACTION' 1.42  1.44  . . 138 2661 100.00 . . . . 0.1539 . . . . . . . . . . . 0.2082 
'X-RAY DIFFRACTION' 1.44  1.46  . . 123 2696 100.00 . . . . 0.1474 . . . . . . . . . . . 0.1751 
'X-RAY DIFFRACTION' 1.46  1.48  . . 152 2635 100.00 . . . . 0.1412 . . . . . . . . . . . 0.1883 
'X-RAY DIFFRACTION' 1.48  1.50  . . 130 2722 100.00 . . . . 0.1377 . . . . . . . . . . . 0.1806 
'X-RAY DIFFRACTION' 1.50  1.53  . . 142 2657 100.00 . . . . 0.1258 . . . . . . . . . . . 0.1916 
'X-RAY DIFFRACTION' 1.53  1.55  . . 149 2652 100.00 . . . . 0.1180 . . . . . . . . . . . 0.1548 
'X-RAY DIFFRACTION' 1.55  1.58  . . 147 2670 100.00 . . . . 0.1121 . . . . . . . . . . . 0.1380 
'X-RAY DIFFRACTION' 1.58  1.61  . . 138 2662 100.00 . . . . 0.1153 . . . . . . . . . . . 0.1584 
'X-RAY DIFFRACTION' 1.61  1.64  . . 135 2716 100.00 . . . . 0.1185 . . . . . . . . . . . 0.1659 
'X-RAY DIFFRACTION' 1.64  1.67  . . 160 2656 100.00 . . . . 0.1178 . . . . . . . . . . . 0.1406 
'X-RAY DIFFRACTION' 1.67  1.71  . . 154 2684 100.00 . . . . 0.1195 . . . . . . . . . . . 0.1468 
'X-RAY DIFFRACTION' 1.71  1.75  . . 131 2689 100.00 . . . . 0.1208 . . . . . . . . . . . 0.1699 
'X-RAY DIFFRACTION' 1.75  1.79  . . 153 2668 100.00 . . . . 0.1268 . . . . . . . . . . . 0.1639 
'X-RAY DIFFRACTION' 1.79  1.84  . . 135 2714 100.00 . . . . 0.1267 . . . . . . . . . . . 0.1501 
'X-RAY DIFFRACTION' 1.84  1.89  . . 148 2705 100.00 . . . . 0.1323 . . . . . . . . . . . 0.1600 
'X-RAY DIFFRACTION' 1.89  1.95  . . 151 2666 100.00 . . . . 0.1334 . . . . . . . . . . . 0.1590 
'X-RAY DIFFRACTION' 1.95  2.02  . . 149 2690 100.00 . . . . 0.1353 . . . . . . . . . . . 0.1754 
'X-RAY DIFFRACTION' 2.02  2.10  . . 149 2695 100.00 . . . . 0.1372 . . . . . . . . . . . 0.1622 
'X-RAY DIFFRACTION' 2.10  2.20  . . 146 2715 100.00 . . . . 0.1353 . . . . . . . . . . . 0.1537 
'X-RAY DIFFRACTION' 2.20  2.31  . . 150 2726 100.00 . . . . 0.1384 . . . . . . . . . . . 0.1757 
'X-RAY DIFFRACTION' 2.31  2.45  . . 141 2704 100.00 . . . . 0.1347 . . . . . . . . . . . 0.1463 
'X-RAY DIFFRACTION' 2.45  2.64  . . 129 2733 100.00 . . . . 0.146  . . . . . . . . . . . 0.146  
'X-RAY DIFFRACTION' 2.64  2.90  . . 143 2757 100.00 . . . . 0.1481 . . . . . . . . . . . 0.1837 
'X-RAY DIFFRACTION' 2.90  3.31  . . 128 2768 100.00 . . . . 0.163  . . . . . . . . . . . 0.163  
'X-RAY DIFFRACTION' 3.31  4.12  . . 148 2796 100.00 . . . . 0.1512 . . . . . . . . . . . 0.1673 
'X-RAY DIFFRACTION' 4.12  9.989 . . 159 2886 100.00 . . . . 0.1640 . . . . . . . . . . . 0.1643 
# 
_struct.entry_id                     8RG4 
_struct.title                        'Crystal structure of PbFucA from Planctomycetes bacterium K23_9 in P 21 21 21' 
_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        8RG4 
_struct_keywords.text            'Fucoidan, endofucoidanase, endofuconase, GH168, glycosyl hydrolase, HYDROLASE' 
_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 2 ? 
D N N 3 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    A0A517NMB4_9BACT 
_struct_ref.pdbx_db_accession          A0A517NMB4 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;DESHYPEFSWDTVPIAFHFGKSQGLLTKEEAEFVATRSNFICLEKGHATRTHGTTEAGIEAEARQLKNLNPKMKVIFYWN
TFLDYSMFAAHKEYAKHPQWWLRTTTGELDRKKGQLMRYDLSNAEFRNWWTNVAAKAVVDGTCDGVFMDAFPQIASQANR
KLWGDEKFEAIQQGLQDIIQETRQKIGDDKLIVYNGIRSTPDWSAGFDFAEYTDAAMIEHFGHFQSASKETMLRDILEMQ
RAAKAGKIVVLKGWAGFTFIDDQAMRKPLTQKRRVAKDSLKFPLACFLAGAQENCYFIYNWGYRMENGCLEWYPEFDKPL
GKPVGEMVRDGWKLSREYKHASVRVDLESKEAEIRWR
;
_struct_ref.pdbx_align_begin           36 
# 
_struct_ref_seq.align_id                      1 
_struct_ref_seq.ref_id                        1 
_struct_ref_seq.pdbx_PDB_id_code              8RG4 
_struct_ref_seq.pdbx_strand_id                A 
_struct_ref_seq.seq_align_beg                 17 
_struct_ref_seq.pdbx_seq_align_beg_ins_code   ? 
_struct_ref_seq.seq_align_end                 373 
_struct_ref_seq.pdbx_seq_align_end_ins_code   ? 
_struct_ref_seq.pdbx_db_accession             A0A517NMB4 
_struct_ref_seq.db_align_beg                  36 
_struct_ref_seq.pdbx_db_align_beg_ins_code    ? 
_struct_ref_seq.db_align_end                  392 
_struct_ref_seq.pdbx_db_align_end_ins_code    ? 
_struct_ref_seq.pdbx_auth_seq_align_beg       36 
_struct_ref_seq.pdbx_auth_seq_align_end       392 
# 
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 8RG4 MET A 1  ? UNP A0A517NMB4 ? ? 'initiating methionine' 20 1  
1 8RG4 HIS A 2  ? UNP A0A517NMB4 ? ? 'expression tag'        21 2  
1 8RG4 HIS A 3  ? UNP A0A517NMB4 ? ? 'expression tag'        22 3  
1 8RG4 HIS A 4  ? UNP A0A517NMB4 ? ? 'expression tag'        23 4  
1 8RG4 HIS A 5  ? UNP A0A517NMB4 ? ? 'expression tag'        24 5  
1 8RG4 HIS A 6  ? UNP A0A517NMB4 ? ? 'expression tag'        25 6  
1 8RG4 HIS A 7  ? UNP A0A517NMB4 ? ? 'expression tag'        26 7  
1 8RG4 GLU A 8  ? UNP A0A517NMB4 ? ? 'expression tag'        27 8  
1 8RG4 ASN A 9  ? UNP A0A517NMB4 ? ? 'expression tag'        28 9  
1 8RG4 LEU A 10 ? UNP A0A517NMB4 ? ? 'expression tag'        29 10 
1 8RG4 TYR A 11 ? UNP A0A517NMB4 ? ? 'expression tag'        30 11 
1 8RG4 PHE A 12 ? UNP A0A517NMB4 ? ? 'expression tag'        31 12 
1 8RG4 GLN A 13 ? UNP A0A517NMB4 ? ? 'expression tag'        32 13 
1 8RG4 GLY A 14 ? UNP A0A517NMB4 ? ? 'expression tag'        33 14 
1 8RG4 SER A 15 ? UNP A0A517NMB4 ? ? 'expression tag'        34 15 
1 8RG4 GLY A 16 ? UNP A0A517NMB4 ? ? 'expression tag'        35 16 
# 
_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 
# 
loop_
_pdbx_struct_assembly_prop.biol_id 
_pdbx_struct_assembly_prop.type 
_pdbx_struct_assembly_prop.value 
_pdbx_struct_assembly_prop.details 
1 'ABSA (A^2)' 440   ? 
1 MORE         7     ? 
1 'SSA (A^2)'  15450 ? 
# 
_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 
# 
_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 THR A 43  ? SER A 54  ? THR A 62  SER A 73  1 ? 12 
HELX_P HELX_P2  AA2 ALA A 64  ? GLY A 69  ? ALA A 83  GLY A 88  1 ? 6  
HELX_P HELX_P3  AA3 THR A 70  ? ASN A 86  ? THR A 89  ASN A 105 1 ? 17 
HELX_P HELX_P4  AA4 PHE A 104 ? ALA A 111 ? PHE A 123 ALA A 130 1 ? 8  
HELX_P HELX_P5  AA5 LYS A 112 ? TRP A 117 ? LYS A 131 TRP A 136 5 ? 6  
HELX_P HELX_P6  AA6 ASN A 139 ? VAL A 155 ? ASN A 158 VAL A 174 1 ? 17 
HELX_P HELX_P7  AA7 ALA A 166 ? SER A 172 ? ALA A 185 SER A 191 1 ? 7  
HELX_P HELX_P8  AA8 ALA A 174 ? GLY A 180 ? ALA A 193 GLY A 199 1 ? 7  
HELX_P HELX_P9  AA9 GLY A 180 ? GLY A 203 ? GLY A 199 GLY A 222 1 ? 24 
HELX_P HELX_P10 AB1 SER A 244 ? ALA A 261 ? SER A 263 ALA A 280 1 ? 18 
HELX_P HELX_P11 AB2 ASP A 277 ? ARG A 282 ? ASP A 296 ARG A 301 1 ? 6  
HELX_P HELX_P12 AB3 PRO A 284 ? LEU A 296 ? PRO A 303 LEU A 315 1 ? 13 
HELX_P HELX_P13 AB4 LEU A 296 ? ALA A 307 ? LEU A 315 ALA A 326 1 ? 12 
HELX_P HELX_P14 AB5 TYR A 329 ? ASP A 333 ? TYR A 348 ASP A 352 5 ? 5  
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
_struct_mon_prot_cis.pdbx_id                1 
_struct_mon_prot_cis.label_comp_id          ASN 
_struct_mon_prot_cis.label_seq_id           211 
_struct_mon_prot_cis.label_asym_id          A 
_struct_mon_prot_cis.label_alt_id           . 
_struct_mon_prot_cis.pdbx_PDB_ins_code      ? 
_struct_mon_prot_cis.auth_comp_id           ASN 
_struct_mon_prot_cis.auth_seq_id            230 
_struct_mon_prot_cis.auth_asym_id           A 
_struct_mon_prot_cis.pdbx_label_comp_id_2   GLY 
_struct_mon_prot_cis.pdbx_label_seq_id_2    212 
_struct_mon_prot_cis.pdbx_label_asym_id_2   A 
_struct_mon_prot_cis.pdbx_PDB_ins_code_2    ? 
_struct_mon_prot_cis.pdbx_auth_comp_id_2    GLY 
_struct_mon_prot_cis.pdbx_auth_seq_id_2     231 
_struct_mon_prot_cis.pdbx_auth_asym_id_2    A 
_struct_mon_prot_cis.pdbx_PDB_model_num     1 
_struct_mon_prot_cis.pdbx_omega_angle       -0.30 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 6 ? 
AA2 ? 8 ? 
AA3 ? 2 ? 
AA4 ? 4 ? 
# 
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 ? parallel      
AA1 2 3 ? parallel      
AA1 3 4 ? parallel      
AA1 4 5 ? parallel      
AA1 5 6 ? anti-parallel 
AA2 1 2 ? parallel      
AA2 2 3 ? parallel      
AA2 3 4 ? parallel      
AA2 4 5 ? parallel      
AA2 5 6 ? parallel      
AA2 6 7 ? parallel      
AA2 7 8 ? parallel      
AA3 1 2 ? anti-parallel 
AA4 1 2 ? anti-parallel 
AA4 2 3 ? anti-parallel 
AA4 3 4 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 PHE A 33  ? PHE A 35  ? PHE A 52  PHE A 54  
AA1 2 PHE A 56  ? LEU A 59  ? PHE A 75  LEU A 78  
AA1 3 LYS A 90  ? TYR A 94  ? LYS A 109 TYR A 113 
AA1 4 GLY A 161 ? MET A 164 ? GLY A 180 MET A 183 
AA1 5 LEU A 207 ? SER A 215 ? LEU A 226 SER A 234 
AA1 6 SER A 220 ? ALA A 221 ? SER A 239 ALA A 240 
AA2 1 PHE A 33  ? PHE A 35  ? PHE A 52  PHE A 54  
AA2 2 PHE A 56  ? LEU A 59  ? PHE A 75  LEU A 78  
AA2 3 LYS A 90  ? TYR A 94  ? LYS A 109 TYR A 113 
AA2 4 GLY A 161 ? MET A 164 ? GLY A 180 MET A 183 
AA2 5 LEU A 207 ? SER A 215 ? LEU A 226 SER A 234 
AA2 6 ALA A 231 ? ILE A 234 ? ALA A 250 ILE A 253 
AA2 7 ILE A 264 ? TRP A 270 ? ILE A 283 TRP A 289 
AA2 8 CYS A 311 ? ASN A 316 ? CYS A 330 ASN A 335 
AA3 1 ARG A 127 ? LYS A 128 ? ARG A 146 LYS A 147 
AA3 2 LEU A 132 ? MET A 133 ? LEU A 151 MET A 152 
AA4 1 VAL A 344 ? ASP A 346 ? VAL A 363 ASP A 365 
AA4 2 LYS A 349 ? TYR A 354 ? LYS A 368 TYR A 373 
AA4 3 ALA A 357 ? ASP A 362 ? ALA A 376 ASP A 381 
AA4 4 GLU A 367 ? TRP A 372 ? GLU A 386 TRP A 391 
# 
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 PHE A 33  ? N PHE A 52  O CYS A 58  ? O CYS A 77  
AA1 2 3 N ILE A 57  ? N ILE A 76  O ILE A 92  ? O ILE A 111 
AA1 3 4 N PHE A 93  ? N PHE A 112 O GLY A 161 ? O GLY A 180 
AA1 4 5 N MET A 164 ? N MET A 183 O VAL A 209 ? O VAL A 228 
AA1 5 6 N ARG A 214 ? N ARG A 233 O ALA A 221 ? O ALA A 240 
AA2 1 2 N PHE A 33  ? N PHE A 52  O CYS A 58  ? O CYS A 77  
AA2 2 3 N ILE A 57  ? N ILE A 76  O ILE A 92  ? O ILE A 111 
AA2 3 4 N PHE A 93  ? N PHE A 112 O GLY A 161 ? O GLY A 180 
AA2 4 5 N MET A 164 ? N MET A 183 O VAL A 209 ? O VAL A 228 
AA2 5 6 N TYR A 210 ? N TYR A 229 O MET A 233 ? O MET A 252 
AA2 6 7 N ILE A 234 ? N ILE A 253 O VAL A 266 ? O VAL A 285 
AA2 7 8 N GLY A 269 ? N GLY A 288 O ILE A 314 ? O ILE A 333 
AA3 1 2 N LYS A 128 ? N LYS A 147 O LEU A 132 ? O LEU A 151 
AA4 1 2 N ASP A 346 ? N ASP A 365 O LYS A 349 ? O LYS A 368 
AA4 2 3 N TYR A 354 ? N TYR A 373 O ALA A 357 ? O ALA A 376 
AA4 3 4 N ASP A 362 ? N ASP A 381 O GLU A 367 ? O GLU A 386 
# 
_pdbx_entry_details.entry_id                   8RG4 
_pdbx_entry_details.has_ligand_of_interest     N 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 ALA A 83  ? ? 59.93   19.38   
2 1 MET A 122 ? ? -90.94  32.11   
3 1 ALA A 185 ? ? 82.95   20.24   
4 1 PHE A 259 ? ? 57.46   -123.63 
5 1 ALA A 290 ? ? -84.04  45.80   
6 1 ASN A 335 ? ? -177.30 -169.44 
7 1 ASN A 342 ? ? -83.13  46.97   
# 
loop_
_space_group_symop.id 
_space_group_symop.operation_xyz 
1 x,y,z           
2 x+1/2,-y+1/2,-z 
3 -x,y+1/2,-z+1/2 
4 -x+1/2,-y,z+1/2 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1  1 Y 1 A MET 20 ? A MET 1  
2  1 Y 1 A HIS 21 ? A HIS 2  
3  1 Y 1 A HIS 22 ? A HIS 3  
4  1 Y 1 A HIS 23 ? A HIS 4  
5  1 Y 1 A HIS 24 ? A HIS 5  
6  1 Y 1 A HIS 25 ? A HIS 6  
7  1 Y 1 A HIS 26 ? A HIS 7  
8  1 Y 1 A GLU 27 ? A GLU 8  
9  1 Y 1 A ASN 28 ? A ASN 9  
10 1 Y 1 A LEU 29 ? A LEU 10 
11 1 Y 1 A TYR 30 ? A TYR 11 
12 1 Y 1 A PHE 31 ? A PHE 12 
13 1 Y 1 A GLN 32 ? A GLN 13 
14 1 Y 1 A GLY 33 ? A GLY 14 
15 1 Y 1 A SER 34 ? A SER 15 
16 1 Y 1 A GLY 35 ? A GLY 16 
17 1 Y 1 A ASP 36 ? A ASP 17 
# 
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 
ALA N    N N N 1   
ALA CA   C N S 2   
ALA C    C N N 3   
ALA O    O N N 4   
ALA CB   C N N 5   
ALA OXT  O N N 6   
ALA H    H N N 7   
ALA H2   H N N 8   
ALA HA   H N N 9   
ALA HB1  H N N 10  
ALA HB2  H N N 11  
ALA HB3  H N N 12  
ALA HXT  H N N 13  
ARG N    N N N 14  
ARG CA   C N S 15  
ARG C    C N N 16  
ARG O    O N N 17  
ARG CB   C N N 18  
ARG CG   C N N 19  
ARG CD   C N N 20  
ARG NE   N N N 21  
ARG CZ   C N N 22  
ARG NH1  N N N 23  
ARG NH2  N N N 24  
ARG OXT  O N N 25  
ARG H    H N N 26  
ARG H2   H N N 27  
ARG HA   H N N 28  
ARG HB2  H N N 29  
ARG HB3  H N N 30  
ARG HG2  H N N 31  
ARG HG3  H N N 32  
ARG HD2  H N N 33  
ARG HD3  H N N 34  
ARG HE   H N N 35  
ARG HH11 H N N 36  
ARG HH12 H N N 37  
ARG HH21 H N N 38  
ARG HH22 H N N 39  
ARG HXT  H N N 40  
ASN N    N N N 41  
ASN CA   C N S 42  
ASN C    C N N 43  
ASN O    O N N 44  
ASN CB   C N N 45  
ASN CG   C N N 46  
ASN OD1  O N N 47  
ASN ND2  N N N 48  
ASN OXT  O N N 49  
ASN H    H N N 50  
ASN H2   H N N 51  
ASN HA   H N N 52  
ASN HB2  H N N 53  
ASN HB3  H N N 54  
ASN HD21 H N N 55  
ASN HD22 H N N 56  
ASN HXT  H N N 57  
ASP N    N N N 58  
ASP CA   C N S 59  
ASP C    C N N 60  
ASP O    O N N 61  
ASP CB   C N N 62  
ASP CG   C N N 63  
ASP OD1  O N N 64  
ASP OD2  O N N 65  
ASP OXT  O N N 66  
ASP H    H N N 67  
ASP H2   H N N 68  
ASP HA   H N N 69  
ASP HB2  H N N 70  
ASP HB3  H N N 71  
ASP HD2  H N N 72  
ASP HXT  H N N 73  
CYS N    N N N 74  
CYS CA   C N R 75  
CYS C    C N N 76  
CYS O    O N N 77  
CYS CB   C N N 78  
CYS SG   S N N 79  
CYS OXT  O N N 80  
CYS H    H N N 81  
CYS H2   H N N 82  
CYS HA   H N N 83  
CYS HB2  H N N 84  
CYS HB3  H N N 85  
CYS HG   H N N 86  
CYS HXT  H N N 87  
EDO C1   C N N 88  
EDO O1   O N N 89  
EDO C2   C N N 90  
EDO O2   O N N 91  
EDO H11  H N N 92  
EDO H12  H N N 93  
EDO HO1  H N N 94  
EDO H21  H N N 95  
EDO H22  H N N 96  
EDO HO2  H N N 97  
GLN N    N N N 98  
GLN CA   C N S 99  
GLN C    C N N 100 
GLN O    O N N 101 
GLN CB   C N N 102 
GLN CG   C N N 103 
GLN CD   C N N 104 
GLN OE1  O N N 105 
GLN NE2  N N N 106 
GLN OXT  O N N 107 
GLN H    H N N 108 
GLN H2   H N N 109 
GLN HA   H N N 110 
GLN HB2  H N N 111 
GLN HB3  H N N 112 
GLN HG2  H N N 113 
GLN HG3  H N N 114 
GLN HE21 H N N 115 
GLN HE22 H N N 116 
GLN HXT  H N N 117 
GLU N    N N N 118 
GLU CA   C N S 119 
GLU C    C N N 120 
GLU O    O N N 121 
GLU CB   C N N 122 
GLU CG   C N N 123 
GLU CD   C N N 124 
GLU OE1  O N N 125 
GLU OE2  O N N 126 
GLU OXT  O N N 127 
GLU H    H N N 128 
GLU H2   H N N 129 
GLU HA   H N N 130 
GLU HB2  H N N 131 
GLU HB3  H N N 132 
GLU HG2  H N N 133 
GLU HG3  H N N 134 
GLU HE2  H N N 135 
GLU HXT  H N N 136 
GLY N    N N N 137 
GLY CA   C N N 138 
GLY C    C N N 139 
GLY O    O N N 140 
GLY OXT  O N N 141 
GLY H    H N N 142 
GLY H2   H N N 143 
GLY HA2  H N N 144 
GLY HA3  H N N 145 
GLY HXT  H N N 146 
HIS N    N N N 147 
HIS CA   C N S 148 
HIS C    C N N 149 
HIS O    O N N 150 
HIS CB   C N N 151 
HIS CG   C Y N 152 
HIS ND1  N Y N 153 
HIS CD2  C Y N 154 
HIS CE1  C Y N 155 
HIS NE2  N Y N 156 
HIS OXT  O N N 157 
HIS H    H N N 158 
HIS H2   H N N 159 
HIS HA   H N N 160 
HIS HB2  H N N 161 
HIS HB3  H N N 162 
HIS HD1  H N N 163 
HIS HD2  H N N 164 
HIS HE1  H N N 165 
HIS HE2  H N N 166 
HIS HXT  H N N 167 
HOH O    O N N 168 
HOH H1   H N N 169 
HOH H2   H N N 170 
ILE N    N N N 171 
ILE CA   C N S 172 
ILE C    C N N 173 
ILE O    O N N 174 
ILE CB   C N S 175 
ILE CG1  C N N 176 
ILE CG2  C N N 177 
ILE CD1  C N N 178 
ILE OXT  O N N 179 
ILE H    H N N 180 
ILE H2   H N N 181 
ILE HA   H N N 182 
ILE HB   H N N 183 
ILE HG12 H N N 184 
ILE HG13 H N N 185 
ILE HG21 H N N 186 
ILE HG22 H N N 187 
ILE HG23 H N N 188 
ILE HD11 H N N 189 
ILE HD12 H N N 190 
ILE HD13 H N N 191 
ILE HXT  H N N 192 
LEU N    N N N 193 
LEU CA   C N S 194 
LEU C    C N N 195 
LEU O    O N N 196 
LEU CB   C N N 197 
LEU CG   C N N 198 
LEU CD1  C N N 199 
LEU CD2  C N N 200 
LEU OXT  O N N 201 
LEU H    H N N 202 
LEU H2   H N N 203 
LEU HA   H N N 204 
LEU HB2  H N N 205 
LEU HB3  H N N 206 
LEU HG   H N N 207 
LEU HD11 H N N 208 
LEU HD12 H N N 209 
LEU HD13 H N N 210 
LEU HD21 H N N 211 
LEU HD22 H N N 212 
LEU HD23 H N N 213 
LEU HXT  H N N 214 
LYS N    N N N 215 
LYS CA   C N S 216 
LYS C    C N N 217 
LYS O    O N N 218 
LYS CB   C N N 219 
LYS CG   C N N 220 
LYS CD   C N N 221 
LYS CE   C N N 222 
LYS NZ   N N N 223 
LYS OXT  O N N 224 
LYS H    H N N 225 
LYS H2   H N N 226 
LYS HA   H N N 227 
LYS HB2  H N N 228 
LYS HB3  H N N 229 
LYS HG2  H N N 230 
LYS HG3  H N N 231 
LYS HD2  H N N 232 
LYS HD3  H N N 233 
LYS HE2  H N N 234 
LYS HE3  H N N 235 
LYS HZ1  H N N 236 
LYS HZ2  H N N 237 
LYS HZ3  H N N 238 
LYS HXT  H N N 239 
MET N    N N N 240 
MET CA   C N S 241 
MET C    C N N 242 
MET O    O N N 243 
MET CB   C N N 244 
MET CG   C N N 245 
MET SD   S N N 246 
MET CE   C N N 247 
MET OXT  O N N 248 
MET H    H N N 249 
MET H2   H N N 250 
MET HA   H N N 251 
MET HB2  H N N 252 
MET HB3  H N N 253 
MET HG2  H N N 254 
MET HG3  H N N 255 
MET HE1  H N N 256 
MET HE2  H N N 257 
MET HE3  H N N 258 
MET HXT  H N N 259 
PHE N    N N N 260 
PHE CA   C N S 261 
PHE C    C N N 262 
PHE O    O N N 263 
PHE CB   C N N 264 
PHE CG   C Y N 265 
PHE CD1  C Y N 266 
PHE CD2  C Y N 267 
PHE CE1  C Y N 268 
PHE CE2  C Y N 269 
PHE CZ   C Y N 270 
PHE OXT  O N N 271 
PHE H    H N N 272 
PHE H2   H N N 273 
PHE HA   H N N 274 
PHE HB2  H N N 275 
PHE HB3  H N N 276 
PHE HD1  H N N 277 
PHE HD2  H N N 278 
PHE HE1  H N N 279 
PHE HE2  H N N 280 
PHE HZ   H N N 281 
PHE HXT  H N N 282 
PRO N    N N N 283 
PRO CA   C N S 284 
PRO C    C N N 285 
PRO O    O N N 286 
PRO CB   C N N 287 
PRO CG   C N N 288 
PRO CD   C N N 289 
PRO OXT  O N N 290 
PRO H    H N N 291 
PRO HA   H N N 292 
PRO HB2  H N N 293 
PRO HB3  H N N 294 
PRO HG2  H N N 295 
PRO HG3  H N N 296 
PRO HD2  H N N 297 
PRO HD3  H N N 298 
PRO HXT  H N N 299 
SER N    N N N 300 
SER CA   C N S 301 
SER C    C N N 302 
SER O    O N N 303 
SER CB   C N N 304 
SER OG   O N N 305 
SER OXT  O N N 306 
SER H    H N N 307 
SER H2   H N N 308 
SER HA   H N N 309 
SER HB2  H N N 310 
SER HB3  H N N 311 
SER HG   H N N 312 
SER HXT  H N N 313 
THR N    N N N 314 
THR CA   C N S 315 
THR C    C N N 316 
THR O    O N N 317 
THR CB   C N R 318 
THR OG1  O N N 319 
THR CG2  C N N 320 
THR OXT  O N N 321 
THR H    H N N 322 
THR H2   H N N 323 
THR HA   H N N 324 
THR HB   H N N 325 
THR HG1  H N N 326 
THR HG21 H N N 327 
THR HG22 H N N 328 
THR HG23 H N N 329 
THR HXT  H N N 330 
TRP N    N N N 331 
TRP CA   C N S 332 
TRP C    C N N 333 
TRP O    O N N 334 
TRP CB   C N N 335 
TRP CG   C Y N 336 
TRP CD1  C Y N 337 
TRP CD2  C Y N 338 
TRP NE1  N Y N 339 
TRP CE2  C Y N 340 
TRP CE3  C Y N 341 
TRP CZ2  C Y N 342 
TRP CZ3  C Y N 343 
TRP CH2  C Y N 344 
TRP OXT  O N N 345 
TRP H    H N N 346 
TRP H2   H N N 347 
TRP HA   H N N 348 
TRP HB2  H N N 349 
TRP HB3  H N N 350 
TRP HD1  H N N 351 
TRP HE1  H N N 352 
TRP HE3  H N N 353 
TRP HZ2  H N N 354 
TRP HZ3  H N N 355 
TRP HH2  H N N 356 
TRP HXT  H N N 357 
TYR N    N N N 358 
TYR CA   C N S 359 
TYR C    C N N 360 
TYR O    O N N 361 
TYR CB   C N N 362 
TYR CG   C Y N 363 
TYR CD1  C Y N 364 
TYR CD2  C Y N 365 
TYR CE1  C Y N 366 
TYR CE2  C Y N 367 
TYR CZ   C Y N 368 
TYR OH   O N N 369 
TYR OXT  O N N 370 
TYR H    H N N 371 
TYR H2   H N N 372 
TYR HA   H N N 373 
TYR HB2  H N N 374 
TYR HB3  H N N 375 
TYR HD1  H N N 376 
TYR HD2  H N N 377 
TYR HE1  H N N 378 
TYR HE2  H N N 379 
TYR HH   H N N 380 
TYR HXT  H N N 381 
VAL N    N N N 382 
VAL CA   C N S 383 
VAL C    C N N 384 
VAL O    O N N 385 
VAL CB   C N N 386 
VAL CG1  C N N 387 
VAL CG2  C N N 388 
VAL OXT  O N N 389 
VAL H    H N N 390 
VAL H2   H N N 391 
VAL HA   H N N 392 
VAL HB   H N N 393 
VAL HG11 H N N 394 
VAL HG12 H N N 395 
VAL HG13 H N N 396 
VAL HG21 H N N 397 
VAL HG22 H N N 398 
VAL HG23 H N N 399 
VAL HXT  H N N 400 
# 
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 
ALA N   CA   sing N N 1   
ALA N   H    sing N N 2   
ALA N   H2   sing N N 3   
ALA CA  C    sing N N 4   
ALA CA  CB   sing N N 5   
ALA CA  HA   sing N N 6   
ALA C   O    doub N N 7   
ALA C   OXT  sing N N 8   
ALA CB  HB1  sing N N 9   
ALA CB  HB2  sing N N 10  
ALA CB  HB3  sing N N 11  
ALA OXT HXT  sing N N 12  
ARG N   CA   sing N N 13  
ARG N   H    sing N N 14  
ARG N   H2   sing N N 15  
ARG CA  C    sing N N 16  
ARG CA  CB   sing N N 17  
ARG CA  HA   sing N N 18  
ARG C   O    doub N N 19  
ARG C   OXT  sing N N 20  
ARG CB  CG   sing N N 21  
ARG CB  HB2  sing N N 22  
ARG CB  HB3  sing N N 23  
ARG CG  CD   sing N N 24  
ARG CG  HG2  sing N N 25  
ARG CG  HG3  sing N N 26  
ARG CD  NE   sing N N 27  
ARG CD  HD2  sing N N 28  
ARG CD  HD3  sing N N 29  
ARG NE  CZ   sing N N 30  
ARG NE  HE   sing N N 31  
ARG CZ  NH1  sing N N 32  
ARG CZ  NH2  doub N N 33  
ARG NH1 HH11 sing N N 34  
ARG NH1 HH12 sing N N 35  
ARG NH2 HH21 sing N N 36  
ARG NH2 HH22 sing N N 37  
ARG OXT HXT  sing N N 38  
ASN N   CA   sing N N 39  
ASN N   H    sing N N 40  
ASN N   H2   sing N N 41  
ASN CA  C    sing N N 42  
ASN CA  CB   sing N N 43  
ASN CA  HA   sing N N 44  
ASN C   O    doub N N 45  
ASN C   OXT  sing N N 46  
ASN CB  CG   sing N N 47  
ASN CB  HB2  sing N N 48  
ASN CB  HB3  sing N N 49  
ASN CG  OD1  doub N N 50  
ASN CG  ND2  sing N N 51  
ASN ND2 HD21 sing N N 52  
ASN ND2 HD22 sing N N 53  
ASN OXT HXT  sing N N 54  
ASP N   CA   sing N N 55  
ASP N   H    sing N N 56  
ASP N   H2   sing N N 57  
ASP CA  C    sing N N 58  
ASP CA  CB   sing N N 59  
ASP CA  HA   sing N N 60  
ASP C   O    doub N N 61  
ASP C   OXT  sing N N 62  
ASP CB  CG   sing N N 63  
ASP CB  HB2  sing N N 64  
ASP CB  HB3  sing N N 65  
ASP CG  OD1  doub N N 66  
ASP CG  OD2  sing N N 67  
ASP OD2 HD2  sing N N 68  
ASP OXT HXT  sing N N 69  
CYS N   CA   sing N N 70  
CYS N   H    sing N N 71  
CYS N   H2   sing N N 72  
CYS CA  C    sing N N 73  
CYS CA  CB   sing N N 74  
CYS CA  HA   sing N N 75  
CYS C   O    doub N N 76  
CYS C   OXT  sing N N 77  
CYS CB  SG   sing N N 78  
CYS CB  HB2  sing N N 79  
CYS CB  HB3  sing N N 80  
CYS SG  HG   sing N N 81  
CYS OXT HXT  sing N N 82  
EDO C1  O1   sing N N 83  
EDO C1  C2   sing N N 84  
EDO C1  H11  sing N N 85  
EDO C1  H12  sing N N 86  
EDO O1  HO1  sing N N 87  
EDO C2  O2   sing N N 88  
EDO C2  H21  sing N N 89  
EDO C2  H22  sing N N 90  
EDO O2  HO2  sing N N 91  
GLN N   CA   sing N N 92  
GLN N   H    sing N N 93  
GLN N   H2   sing N N 94  
GLN CA  C    sing N N 95  
GLN CA  CB   sing N N 96  
GLN CA  HA   sing N N 97  
GLN C   O    doub N N 98  
GLN C   OXT  sing N N 99  
GLN CB  CG   sing N N 100 
GLN CB  HB2  sing N N 101 
GLN CB  HB3  sing N N 102 
GLN CG  CD   sing N N 103 
GLN CG  HG2  sing N N 104 
GLN CG  HG3  sing N N 105 
GLN CD  OE1  doub N N 106 
GLN CD  NE2  sing N N 107 
GLN NE2 HE21 sing N N 108 
GLN NE2 HE22 sing N N 109 
GLN OXT HXT  sing N N 110 
GLU N   CA   sing N N 111 
GLU N   H    sing N N 112 
GLU N   H2   sing N N 113 
GLU CA  C    sing N N 114 
GLU CA  CB   sing N N 115 
GLU CA  HA   sing N N 116 
GLU C   O    doub N N 117 
GLU C   OXT  sing N N 118 
GLU CB  CG   sing N N 119 
GLU CB  HB2  sing N N 120 
GLU CB  HB3  sing N N 121 
GLU CG  CD   sing N N 122 
GLU CG  HG2  sing N N 123 
GLU CG  HG3  sing N N 124 
GLU CD  OE1  doub N N 125 
GLU CD  OE2  sing N N 126 
GLU OE2 HE2  sing N N 127 
GLU OXT HXT  sing N N 128 
GLY N   CA   sing N N 129 
GLY N   H    sing N N 130 
GLY N   H2   sing N N 131 
GLY CA  C    sing N N 132 
GLY CA  HA2  sing N N 133 
GLY CA  HA3  sing N N 134 
GLY C   O    doub N N 135 
GLY C   OXT  sing N N 136 
GLY OXT HXT  sing N N 137 
HIS N   CA   sing N N 138 
HIS N   H    sing N N 139 
HIS N   H2   sing N N 140 
HIS CA  C    sing N N 141 
HIS CA  CB   sing N N 142 
HIS CA  HA   sing N N 143 
HIS C   O    doub N N 144 
HIS C   OXT  sing N N 145 
HIS CB  CG   sing N N 146 
HIS CB  HB2  sing N N 147 
HIS CB  HB3  sing N N 148 
HIS CG  ND1  sing Y N 149 
HIS CG  CD2  doub Y N 150 
HIS ND1 CE1  doub Y N 151 
HIS ND1 HD1  sing N N 152 
HIS CD2 NE2  sing Y N 153 
HIS CD2 HD2  sing N N 154 
HIS CE1 NE2  sing Y N 155 
HIS CE1 HE1  sing N N 156 
HIS NE2 HE2  sing N N 157 
HIS OXT HXT  sing N N 158 
HOH O   H1   sing N N 159 
HOH O   H2   sing N N 160 
ILE N   CA   sing N N 161 
ILE N   H    sing N N 162 
ILE N   H2   sing N N 163 
ILE CA  C    sing N N 164 
ILE CA  CB   sing N N 165 
ILE CA  HA   sing N N 166 
ILE C   O    doub N N 167 
ILE C   OXT  sing N N 168 
ILE CB  CG1  sing N N 169 
ILE CB  CG2  sing N N 170 
ILE CB  HB   sing N N 171 
ILE CG1 CD1  sing N N 172 
ILE CG1 HG12 sing N N 173 
ILE CG1 HG13 sing N N 174 
ILE CG2 HG21 sing N N 175 
ILE CG2 HG22 sing N N 176 
ILE CG2 HG23 sing N N 177 
ILE CD1 HD11 sing N N 178 
ILE CD1 HD12 sing N N 179 
ILE CD1 HD13 sing N N 180 
ILE OXT HXT  sing N N 181 
LEU N   CA   sing N N 182 
LEU N   H    sing N N 183 
LEU N   H2   sing N N 184 
LEU CA  C    sing N N 185 
LEU CA  CB   sing N N 186 
LEU CA  HA   sing N N 187 
LEU C   O    doub N N 188 
LEU C   OXT  sing N N 189 
LEU CB  CG   sing N N 190 
LEU CB  HB2  sing N N 191 
LEU CB  HB3  sing N N 192 
LEU CG  CD1  sing N N 193 
LEU CG  CD2  sing N N 194 
LEU CG  HG   sing N N 195 
LEU CD1 HD11 sing N N 196 
LEU CD1 HD12 sing N N 197 
LEU CD1 HD13 sing N N 198 
LEU CD2 HD21 sing N N 199 
LEU CD2 HD22 sing N N 200 
LEU CD2 HD23 sing N N 201 
LEU OXT HXT  sing N N 202 
LYS N   CA   sing N N 203 
LYS N   H    sing N N 204 
LYS N   H2   sing N N 205 
LYS CA  C    sing N N 206 
LYS CA  CB   sing N N 207 
LYS CA  HA   sing N N 208 
LYS C   O    doub N N 209 
LYS C   OXT  sing N N 210 
LYS CB  CG   sing N N 211 
LYS CB  HB2  sing N N 212 
LYS CB  HB3  sing N N 213 
LYS CG  CD   sing N N 214 
LYS CG  HG2  sing N N 215 
LYS CG  HG3  sing N N 216 
LYS CD  CE   sing N N 217 
LYS CD  HD2  sing N N 218 
LYS CD  HD3  sing N N 219 
LYS CE  NZ   sing N N 220 
LYS CE  HE2  sing N N 221 
LYS CE  HE3  sing N N 222 
LYS NZ  HZ1  sing N N 223 
LYS NZ  HZ2  sing N N 224 
LYS NZ  HZ3  sing N N 225 
LYS OXT HXT  sing N N 226 
MET N   CA   sing N N 227 
MET N   H    sing N N 228 
MET N   H2   sing N N 229 
MET CA  C    sing N N 230 
MET CA  CB   sing N N 231 
MET CA  HA   sing N N 232 
MET C   O    doub N N 233 
MET C   OXT  sing N N 234 
MET CB  CG   sing N N 235 
MET CB  HB2  sing N N 236 
MET CB  HB3  sing N N 237 
MET CG  SD   sing N N 238 
MET CG  HG2  sing N N 239 
MET CG  HG3  sing N N 240 
MET SD  CE   sing N N 241 
MET CE  HE1  sing N N 242 
MET CE  HE2  sing N N 243 
MET CE  HE3  sing N N 244 
MET OXT HXT  sing N N 245 
PHE N   CA   sing N N 246 
PHE N   H    sing N N 247 
PHE N   H2   sing N N 248 
PHE CA  C    sing N N 249 
PHE CA  CB   sing N N 250 
PHE CA  HA   sing N N 251 
PHE C   O    doub N N 252 
PHE C   OXT  sing N N 253 
PHE CB  CG   sing N N 254 
PHE CB  HB2  sing N N 255 
PHE CB  HB3  sing N N 256 
PHE CG  CD1  doub Y N 257 
PHE CG  CD2  sing Y N 258 
PHE CD1 CE1  sing Y N 259 
PHE CD1 HD1  sing N N 260 
PHE CD2 CE2  doub Y N 261 
PHE CD2 HD2  sing N N 262 
PHE CE1 CZ   doub Y N 263 
PHE CE1 HE1  sing N N 264 
PHE CE2 CZ   sing Y N 265 
PHE CE2 HE2  sing N N 266 
PHE CZ  HZ   sing N N 267 
PHE OXT HXT  sing N N 268 
PRO N   CA   sing N N 269 
PRO N   CD   sing N N 270 
PRO N   H    sing N N 271 
PRO CA  C    sing N N 272 
PRO CA  CB   sing N N 273 
PRO CA  HA   sing N N 274 
PRO C   O    doub N N 275 
PRO C   OXT  sing N N 276 
PRO CB  CG   sing N N 277 
PRO CB  HB2  sing N N 278 
PRO CB  HB3  sing N N 279 
PRO CG  CD   sing N N 280 
PRO CG  HG2  sing N N 281 
PRO CG  HG3  sing N N 282 
PRO CD  HD2  sing N N 283 
PRO CD  HD3  sing N N 284 
PRO OXT HXT  sing N N 285 
SER N   CA   sing N N 286 
SER N   H    sing N N 287 
SER N   H2   sing N N 288 
SER CA  C    sing N N 289 
SER CA  CB   sing N N 290 
SER CA  HA   sing N N 291 
SER C   O    doub N N 292 
SER C   OXT  sing N N 293 
SER CB  OG   sing N N 294 
SER CB  HB2  sing N N 295 
SER CB  HB3  sing N N 296 
SER OG  HG   sing N N 297 
SER OXT HXT  sing N N 298 
THR N   CA   sing N N 299 
THR N   H    sing N N 300 
THR N   H2   sing N N 301 
THR CA  C    sing N N 302 
THR CA  CB   sing N N 303 
THR CA  HA   sing N N 304 
THR C   O    doub N N 305 
THR C   OXT  sing N N 306 
THR CB  OG1  sing N N 307 
THR CB  CG2  sing N N 308 
THR CB  HB   sing N N 309 
THR OG1 HG1  sing N N 310 
THR CG2 HG21 sing N N 311 
THR CG2 HG22 sing N N 312 
THR CG2 HG23 sing N N 313 
THR OXT HXT  sing N N 314 
TRP N   CA   sing N N 315 
TRP N   H    sing N N 316 
TRP N   H2   sing N N 317 
TRP CA  C    sing N N 318 
TRP CA  CB   sing N N 319 
TRP CA  HA   sing N N 320 
TRP C   O    doub N N 321 
TRP C   OXT  sing N N 322 
TRP CB  CG   sing N N 323 
TRP CB  HB2  sing N N 324 
TRP CB  HB3  sing N N 325 
TRP CG  CD1  doub Y N 326 
TRP CG  CD2  sing Y N 327 
TRP CD1 NE1  sing Y N 328 
TRP CD1 HD1  sing N N 329 
TRP CD2 CE2  doub Y N 330 
TRP CD2 CE3  sing Y N 331 
TRP NE1 CE2  sing Y N 332 
TRP NE1 HE1  sing N N 333 
TRP CE2 CZ2  sing Y N 334 
TRP CE3 CZ3  doub Y N 335 
TRP CE3 HE3  sing N N 336 
TRP CZ2 CH2  doub Y N 337 
TRP CZ2 HZ2  sing N N 338 
TRP CZ3 CH2  sing Y N 339 
TRP CZ3 HZ3  sing N N 340 
TRP CH2 HH2  sing N N 341 
TRP OXT HXT  sing N N 342 
TYR N   CA   sing N N 343 
TYR N   H    sing N N 344 
TYR N   H2   sing N N 345 
TYR CA  C    sing N N 346 
TYR CA  CB   sing N N 347 
TYR CA  HA   sing N N 348 
TYR C   O    doub N N 349 
TYR C   OXT  sing N N 350 
TYR CB  CG   sing N N 351 
TYR CB  HB2  sing N N 352 
TYR CB  HB3  sing N N 353 
TYR CG  CD1  doub Y N 354 
TYR CG  CD2  sing Y N 355 
TYR CD1 CE1  sing Y N 356 
TYR CD1 HD1  sing N N 357 
TYR CD2 CE2  doub Y N 358 
TYR CD2 HD2  sing N N 359 
TYR CE1 CZ   doub Y N 360 
TYR CE1 HE1  sing N N 361 
TYR CE2 CZ   sing Y N 362 
TYR CE2 HE2  sing N N 363 
TYR CZ  OH   sing N N 364 
TYR OH  HH   sing N N 365 
TYR OXT HXT  sing N N 366 
VAL N   CA   sing N N 367 
VAL N   H    sing N N 368 
VAL N   H2   sing N N 369 
VAL CA  C    sing N N 370 
VAL CA  CB   sing N N 371 
VAL CA  HA   sing N N 372 
VAL C   O    doub N N 373 
VAL C   OXT  sing N N 374 
VAL CB  CG1  sing N N 375 
VAL CB  CG2  sing N N 376 
VAL CB  HB   sing N N 377 
VAL CG1 HG11 sing N N 378 
VAL CG1 HG12 sing N N 379 
VAL CG1 HG13 sing N N 380 
VAL CG2 HG21 sing N N 381 
VAL CG2 HG22 sing N N 382 
VAL CG2 HG23 sing N N 383 
VAL OXT HXT  sing N N 384 
# 
_pdbx_audit_support.funding_organization   'Other government' 
_pdbx_audit_support.country                Spain 
_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   8RG3 
_pdbx_initial_refinement_model.details          ? 
# 
_space_group.name_H-M_alt     'P 21 21 21' 
_space_group.name_Hall        'P 2ac 2ab' 
_space_group.IT_number        19 
_space_group.crystal_system   orthorhombic 
_space_group.id               1 
# 
_atom_sites.entry_id                    8RG4 
_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]   0.019614 
_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]   0.011783 
_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]   0.011069 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
_atom_type.scat_dispersion_real 
_atom_type.scat_dispersion_imag 
_atom_type.scat_Cromer_Mann_a1 
_atom_type.scat_Cromer_Mann_a2 
_atom_type.scat_Cromer_Mann_a3 
_atom_type.scat_Cromer_Mann_a4 
_atom_type.scat_Cromer_Mann_b1 
_atom_type.scat_Cromer_Mann_b2 
_atom_type.scat_Cromer_Mann_b3 
_atom_type.scat_Cromer_Mann_b4 
_atom_type.scat_Cromer_Mann_c 
_atom_type.scat_source 
_atom_type.scat_dispersion_source 
C ? ? 3.54356 2.42580 ? ? 25.62398 1.50364  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
H ? ? 0.51345 0.48472 ? ? 24.73122 6.32584  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
N ? ? 4.01032 2.96436 ? ? 19.97189 1.75589  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
O ? ? 4.49882 3.47563 ? ? 15.80542 1.70748  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
S ? ? 9.55732 6.39887 ? ? 1.23737  29.19336 ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N N    . GLU A 1 18  ? 15.235  -9.390  13.126  1.00 39.41 ? 37  GLU A N    1 
ATOM   2    C CA   . GLU A 1 18  ? 15.286  -10.788 13.543  1.00 38.17 ? 37  GLU A CA   1 
ATOM   3    C C    . GLU A 1 18  ? 14.761  -11.029 14.970  1.00 32.44 ? 37  GLU A C    1 
ATOM   4    O O    . GLU A 1 18  ? 13.535  -11.071 15.208  1.00 28.31 ? 37  GLU A O    1 
ATOM   5    C CB   . GLU A 1 18  ? 16.702  -11.357 13.285  1.00 42.01 ? 37  GLU A CB   1 
ATOM   6    C CG   . GLU A 1 18  ? 17.907  -10.402 13.457  1.00 45.69 ? 37  GLU A CG   1 
ATOM   7    C CD   . GLU A 1 18  ? 18.355  -10.187 14.901  1.00 48.36 ? 37  GLU A CD   1 
ATOM   8    O OE1  . GLU A 1 18  ? 18.375  -11.172 15.678  1.00 48.62 ? 37  GLU A OE1  1 
ATOM   9    O OE2  . GLU A 1 18  ? 18.688  -9.035  15.261  1.00 49.81 ? 37  GLU A OE2  1 
ATOM   10   H HA   . GLU A 1 18  ? 14.672  -11.307 13.000  1.00 45.81 ? 37  GLU A HA   1 
ATOM   11   H HB2  . GLU A 1 18  ? 16.842  -12.094 13.900  1.00 50.42 ? 37  GLU A HB2  1 
ATOM   12   H HB3  . GLU A 1 18  ? 16.730  -11.678 12.370  1.00 50.42 ? 37  GLU A HB3  1 
ATOM   13   H HG2  . GLU A 1 18  ? 18.662  -10.767 12.969  1.00 54.84 ? 37  GLU A HG2  1 
ATOM   14   H HG3  . GLU A 1 18  ? 17.667  -9.535  13.095  1.00 54.84 ? 37  GLU A HG3  1 
ATOM   15   N N    . SER A 1 19  ? 15.668  -11.169 15.929  1.00 29.28 ? 38  SER A N    1 
ATOM   16   C CA   . SER A 1 19  ? 15.256  -11.544 17.272  1.00 26.12 ? 38  SER A CA   1 
ATOM   17   C C    . SER A 1 19  ? 14.443  -10.462 17.961  1.00 21.73 ? 38  SER A C    1 
ATOM   18   O O    . SER A 1 19  ? 13.755  -10.765 18.947  1.00 22.00 ? 38  SER A O    1 
ATOM   19   C CB   . SER A 1 19  ? 16.482  -11.889 18.114  1.00 28.08 ? 38  SER A CB   1 
ATOM   20   O OG   . SER A 1 19  ? 17.178  -10.707 18.467  1.00 28.81 ? 38  SER A OG   1 
ATOM   21   H H    . SER A 1 19  ? 16.515  -11.055 15.829  1.00 35.14 ? 38  SER A H    1 
ATOM   22   H HA   . SER A 1 19  ? 14.696  -12.334 17.211  1.00 31.34 ? 38  SER A HA   1 
ATOM   23   H HB2  . SER A 1 19  ? 16.196  -12.344 18.922  1.00 33.71 ? 38  SER A HB2  1 
ATOM   24   H HB3  . SER A 1 19  ? 17.070  -12.464 17.600  1.00 33.71 ? 38  SER A HB3  1 
ATOM   25   H HG   . SER A 1 19  ? 17.230  -10.195 17.804  1.00 34.57 ? 38  SER A HG   1 
ATOM   26   N N    . HIS A 1 20  ? 14.476  -9.222  17.461  1.00 17.89 ? 39  HIS A N    1 
ATOM   27   C CA   . HIS A 1 20  ? 13.698  -8.130  18.057  1.00 15.58 ? 39  HIS A CA   1 
ATOM   28   C C    . HIS A 1 20  ? 12.340  -7.912  17.401  1.00 13.38 ? 39  HIS A C    1 
ATOM   29   O O    . HIS A 1 20  ? 11.603  -7.002  17.796  1.00 13.21 ? 39  HIS A O    1 
ATOM   30   C CB   . HIS A 1 20  ? 14.496  -6.826  18.022  1.00 16.40 ? 39  HIS A CB   1 
ATOM   31   C CG   . HIS A 1 20  ? 14.749  -6.309  16.644  1.00 17.73 ? 39  HIS A CG   1 
ATOM   32   N ND1  . HIS A 1 20  ? 15.454  -7.026  15.701  1.00 19.93 ? 39  HIS A ND1  1 
ATOM   33   C CD2  . HIS A 1 20  ? 14.388  -5.149  16.047  1.00 19.24 ? 39  HIS A CD2  1 
ATOM   34   C CE1  . HIS A 1 20  ? 15.531  -6.325  14.589  1.00 20.33 ? 39  HIS A CE1  1 
ATOM   35   N NE2  . HIS A 1 20  ? 14.895  -5.182  14.771  1.00 19.26 ? 39  HIS A NE2  1 
ATOM   36   H H    . HIS A 1 20  ? 14.942  -8.988  16.777  1.00 21.48 ? 39  HIS A H    1 
ATOM   37   H HA   . HIS A 1 20  ? 13.536  -8.358  18.986  1.00 18.71 ? 39  HIS A HA   1 
ATOM   38   H HB2  . HIS A 1 20  ? 14.003  -6.146  18.507  1.00 19.69 ? 39  HIS A HB2  1 
ATOM   39   H HB3  . HIS A 1 20  ? 15.356  -6.976  18.445  1.00 19.69 ? 39  HIS A HB3  1 
ATOM   40   H HD2  . HIS A 1 20  ? 13.890  -4.462  16.427  1.00 23.09 ? 39  HIS A HD2  1 
ATOM   41   H HE1  . HIS A 1 20  ? 15.960  -6.590  13.808  1.00 24.40 ? 39  HIS A HE1  1 
ATOM   42   H HE2  . HIS A 1 20  ? 14.813  -4.558  14.184  1.00 23.12 ? 39  HIS A HE2  1 
ATOM   43   N N    . TYR A 1 21  ? 11.978  -8.738  16.431  1.00 12.43 ? 40  TYR A N    1 
ATOM   44   C CA   . TYR A 1 21  ? 10.696  -8.631  15.781  1.00 11.97 ? 40  TYR A CA   1 
ATOM   45   C C    . TYR A 1 21  ? 9.603   -9.130  16.721  1.00 12.08 ? 40  TYR A C    1 
ATOM   46   O O    . TYR A 1 21  ? 9.867   -9.937  17.623  1.00 12.89 ? 40  TYR A O    1 
ATOM   47   C CB   . TYR A 1 21  ? 10.684  -9.502  14.527  1.00 12.07 ? 40  TYR A CB   1 
ATOM   48   C CG   . TYR A 1 21  ? 11.388  -8.952  13.302  1.00 11.64 ? 40  TYR A CG   1 
ATOM   49   C CD1  . TYR A 1 21  ? 12.220  -7.840  13.361  1.00 11.83 ? 40  TYR A CD1  1 
ATOM   50   C CD2  . TYR A 1 21  ? 11.162  -9.523  12.054  1.00 12.02 ? 40  TYR A CD2  1 
ATOM   51   C CE1  . TYR A 1 21  ? 12.809  -7.316  12.206  1.00 11.80 ? 40  TYR A CE1  1 
ATOM   52   C CE2  . TYR A 1 21  ? 11.755  -9.014  10.911  1.00 13.06 ? 40  TYR A CE2  1 
ATOM   53   C CZ   . TYR A 1 21  ? 12.578  -7.914  10.983  1.00 11.94 ? 40  TYR A CZ   1 
ATOM   54   O OH   . TYR A 1 21  ? 13.168  -7.403  9.850   1.00 13.68 ? 40  TYR A OH   1 
ATOM   55   H H    . TYR A 1 21  ? 12.469  -9.377  16.130  1.00 14.92 ? 40  TYR A H    1 
ATOM   56   H HA   . TYR A 1 21  ? 10.523  -7.708  15.538  1.00 14.37 ? 40  TYR A HA   1 
ATOM   57   H HB2  . TYR A 1 21  ? 11.112  -10.345 14.744  1.00 14.49 ? 40  TYR A HB2  1 
ATOM   58   H HB3  . TYR A 1 21  ? 9.759   -9.655  14.277  1.00 14.49 ? 40  TYR A HB3  1 
ATOM   59   H HD1  . TYR A 1 21  ? 12.388  -7.437  14.182  1.00 14.20 ? 40  TYR A HD1  1 
ATOM   60   H HD2  . TYR A 1 21  ? 10.601  -10.262 11.986  1.00 14.43 ? 40  TYR A HD2  1 
ATOM   61   H HE1  . TYR A 1 21  ? 13.355  -6.566  12.261  1.00 14.17 ? 40  TYR A HE1  1 
ATOM   62   H HE2  . TYR A 1 21  ? 11.597  -9.419  10.089  1.00 15.68 ? 40  TYR A HE2  1 
ATOM   63   H HH   . TYR A 1 21  ? 12.996  -7.893  9.190   1.00 16.42 ? 40  TYR A HH   1 
ATOM   64   N N    . PRO A 1 22  ? 8.352   -8.682  16.521  1.00 11.52 ? 41  PRO A N    1 
ATOM   65   C CA   . PRO A 1 22  ? 7.233   -9.326  17.235  1.00 11.60 ? 41  PRO A CA   1 
ATOM   66   C C    . PRO A 1 22  ? 7.185   -10.801 16.881  1.00 11.65 ? 41  PRO A C    1 
ATOM   67   O O    . PRO A 1 22  ? 7.511   -11.199 15.765  1.00 12.10 ? 41  PRO A O    1 
ATOM   68   C CB   . PRO A 1 22  ? 5.992   -8.594  16.712  1.00 11.95 ? 41  PRO A CB   1 
ATOM   69   C CG   . PRO A 1 22  ? 6.507   -7.315  16.017  1.00 13.03 ? 41  PRO A CG   1 
ATOM   70   C CD   . PRO A 1 22  ? 7.897   -7.695  15.518  1.00 12.32 ? 41  PRO A CD   1 
ATOM   71   H HA   . PRO A 1 22  ? 7.299   -9.198  18.194  1.00 13.93 ? 41  PRO A HA   1 
ATOM   72   H HB2  . PRO A 1 22  ? 5.522   -9.161  16.080  1.00 14.34 ? 41  PRO A HB2  1 
ATOM   73   H HB3  . PRO A 1 22  ? 5.410   -8.370  17.454  1.00 14.34 ? 41  PRO A HB3  1 
ATOM   74   H HG2  . PRO A 1 22  ? 5.923   -7.078  15.279  1.00 15.64 ? 41  PRO A HG2  1 
ATOM   75   H HG3  . PRO A 1 22  ? 6.552   -6.584  16.653  1.00 15.64 ? 41  PRO A HG3  1 
ATOM   76   H HD2  . PRO A 1 22  ? 7.851   -8.095  14.635  1.00 14.79 ? 41  PRO A HD2  1 
ATOM   77   H HD3  . PRO A 1 22  ? 8.483   -6.922  15.502  1.00 14.79 ? 41  PRO A HD3  1 
ATOM   78   N N    . GLU A 1 23  ? 6.782   -11.619 17.847  1.00 11.38 ? 42  GLU A N    1 
ATOM   79   C CA   . GLU A 1 23  ? 6.667   -13.053 17.612  1.00 11.79 ? 42  GLU A CA   1 
ATOM   80   C C    . GLU A 1 23  ? 5.514   -13.323 16.657  1.00 12.52 ? 42  GLU A C    1 
ATOM   81   O O    . GLU A 1 23  ? 4.357   -13.006 16.961  1.00 13.77 ? 42  GLU A O    1 
ATOM   82   C CB   . GLU A 1 23  ? 6.452   -13.782 18.933  1.00 13.72 ? 42  GLU A CB   1 
ATOM   83   C CG   . GLU A 1 23  ? 6.499   -15.265 18.776  1.00 17.20 ? 42  GLU A CG   1 
ATOM   84   C CD   . GLU A 1 23  ? 6.456   -15.965 20.110  1.00 19.83 ? 42  GLU A CD   1 
ATOM   85   O OE1  . GLU A 1 23  ? 5.395   -16.550 20.433  1.00 24.37 ? 42  GLU A OE1  1 
ATOM   86   O OE2  . GLU A 1 23  ? 7.437   -15.896 20.840  1.00 21.05 ? 42  GLU A OE2  1 
ATOM   87   H H    . GLU A 1 23  ? 6.570   -11.370 18.642  1.00 13.67 ? 42  GLU A H    1 
ATOM   88   H HA   . GLU A 1 23  ? 7.485   -13.385 17.210  1.00 14.15 ? 42  GLU A HA   1 
ATOM   89   H HB2  . GLU A 1 23  ? 7.148   -13.522 19.556  1.00 16.47 ? 42  GLU A HB2  1 
ATOM   90   H HB3  . GLU A 1 23  ? 5.582   -13.544 19.290  1.00 16.47 ? 42  GLU A HB3  1 
ATOM   91   H HG2  . GLU A 1 23  ? 5.735   -15.556 18.253  1.00 20.65 ? 42  GLU A HG2  1 
ATOM   92   H HG3  . GLU A 1 23  ? 7.322   -15.514 18.327  1.00 20.65 ? 42  GLU A HG3  1 
ATOM   93   N N    . PHE A 1 24  ? 5.847   -13.889 15.512  1.00 13.05 ? 43  PHE A N    1 
ATOM   94   C CA   . PHE A 1 24  ? 4.936   -14.112 14.402  1.00 12.38 ? 43  PHE A CA   1 
ATOM   95   C C    . PHE A 1 24  ? 4.425   -15.547 14.414  1.00 13.40 ? 43  PHE A C    1 
ATOM   96   O O    . PHE A 1 24  ? 5.175   -16.478 14.710  1.00 14.85 ? 43  PHE A O    1 
ATOM   97   C CB   . PHE A 1 24  ? 5.683   -13.873 13.079  1.00 12.43 ? 43  PHE A CB   1 
ATOM   98   C CG   . PHE A 1 24  ? 4.830   -14.088 11.860  1.00 11.53 ? 43  PHE A CG   1 
ATOM   99   C CD1  . PHE A 1 24  ? 3.954   -13.103 11.418  1.00 11.62 ? 43  PHE A CD1  1 
ATOM   100  C CD2  . PHE A 1 24  ? 4.863   -15.293 11.194  1.00 13.34 ? 43  PHE A CD2  1 
ATOM   101  C CE1  . PHE A 1 24  ? 3.150   -13.322 10.343  1.00 12.62 ? 43  PHE A CE1  1 
ATOM   102  C CE2  . PHE A 1 24  ? 4.050   -15.504 10.113  1.00 13.24 ? 43  PHE A CE2  1 
ATOM   103  C CZ   . PHE A 1 24  ? 3.199   -14.525 9.686   1.00 13.24 ? 43  PHE A CZ   1 
ATOM   104  H H    . PHE A 1 24  ? 6.642   -14.171 15.342  1.00 15.66 ? 43  PHE A H    1 
ATOM   105  H HA   . PHE A 1 24  ? 4.176   -13.513 14.476  1.00 14.86 ? 43  PHE A HA   1 
ATOM   106  H HB2  . PHE A 1 24  ? 6.001   -12.956 13.061  1.00 14.92 ? 43  PHE A HB2  1 
ATOM   107  H HB3  . PHE A 1 24  ? 6.433   -14.485 13.028  1.00 14.92 ? 43  PHE A HB3  1 
ATOM   108  H HD1  . PHE A 1 24  ? 3.917   -12.286 11.862  1.00 13.95 ? 43  PHE A HD1  1 
ATOM   109  H HD2  . PHE A 1 24  ? 5.439   -15.965 11.480  1.00 16.01 ? 43  PHE A HD2  1 
ATOM   110  H HE1  . PHE A 1 24  ? 2.568   -12.658 10.053  1.00 15.16 ? 43  PHE A HE1  1 
ATOM   111  H HE2  . PHE A 1 24  ? 4.077   -16.319 9.666   1.00 15.90 ? 43  PHE A HE2  1 
ATOM   112  H HZ   . PHE A 1 24  ? 2.652   -14.673 8.949   1.00 15.90 ? 43  PHE A HZ   1 
ATOM   113  N N    . SER A 1 25  ? 3.161   -15.725 14.034  1.00 12.69 ? 44  SER A N    1 
ATOM   114  C CA   . SER A 1 25  ? 2.570   -17.049 13.896  1.00 14.15 ? 44  SER A CA   1 
ATOM   115  C C    . SER A 1 25  ? 1.626   -17.058 12.710  1.00 13.56 ? 44  SER A C    1 
ATOM   116  O O    . SER A 1 25  ? 0.947   -16.064 12.441  1.00 13.63 ? 44  SER A O    1 
ATOM   117  C CB   . SER A 1 25  ? 1.747   -17.385 15.141  1.00 16.71 ? 44  SER A CB   1 
ATOM   118  O OG   . SER A 1 25  ? 1.096   -18.637 15.037  1.00 17.90 ? 44  SER A OG   1 
ATOM   119  H H    . SER A 1 25  ? 2.620   -15.084 13.848  1.00 15.24 ? 44  SER A H    1 
ATOM   120  H HA   . SER A 1 25  ? 3.268   -17.707 13.754  1.00 16.98 ? 44  SER A HA   1 
ATOM   121  H HB2  . SER A 1 25  ? 2.342   -17.408 15.907  1.00 20.06 ? 44  SER A HB2  1 
ATOM   122  H HB3  . SER A 1 25  ? 1.076   -16.696 15.262  1.00 20.06 ? 44  SER A HB3  1 
ATOM   123  H HG   . SER A 1 25  ? 0.609   -18.764 15.709  1.00 21.48 ? 44  SER A HG   1 
ATOM   124  N N    . TRP A 1 26  ? 1.536   -18.217 12.060  1.00 13.94 ? 45  TRP A N    1 
ATOM   125  C CA   . TRP A 1 26  ? 0.568   -18.453 11.004  1.00 14.03 ? 45  TRP A CA   1 
ATOM   126  C C    . TRP A 1 26  ? -0.679  -19.173 11.522  1.00 13.64 ? 45  TRP A C    1 
ATOM   127  O O    . TRP A 1 26  ? -1.537  -19.553 10.717  1.00 14.54 ? 45  TRP A O    1 
ATOM   128  C CB   . TRP A 1 26  ? 1.194   -19.312 9.912   1.00 14.64 ? 45  TRP A CB   1 
ATOM   129  C CG   . TRP A 1 26  ? 2.160   -18.681 8.986   1.00 14.38 ? 45  TRP A CG   1 
ATOM   130  C CD1  . TRP A 1 26  ? 3.463   -19.044 8.832   1.00 15.68 ? 45  TRP A CD1  1 
ATOM   131  C CD2  . TRP A 1 26  ? 1.914   -17.654 8.017   1.00 13.99 ? 45  TRP A CD2  1 
ATOM   132  N NE1  . TRP A 1 26  ? 4.054   -18.285 7.851   1.00 16.15 ? 45  TRP A NE1  1 
ATOM   133  C CE2  . TRP A 1 26  ? 3.124   -17.435 7.327   1.00 15.43 ? 45  TRP A CE2  1 
ATOM   134  C CE3  . TRP A 1 26  ? 0.792   -16.896 7.659   1.00 14.37 ? 45  TRP A CE3  1 
ATOM   135  C CZ2  . TRP A 1 26  ? 3.244   -16.487 6.312   1.00 16.48 ? 45  TRP A CZ2  1 
ATOM   136  C CZ3  . TRP A 1 26  ? 0.926   -15.946 6.642   1.00 15.38 ? 45  TRP A CZ3  1 
ATOM   137  C CH2  . TRP A 1 26  ? 2.131   -15.761 5.987   1.00 16.82 ? 45  TRP A CH2  1 
ATOM   138  H H    . TRP A 1 26  ? 2.039   -18.896 12.221  1.00 16.74 ? 45  TRP A H    1 
ATOM   139  H HA   . TRP A 1 26  ? 0.311   -17.598 10.626  1.00 16.84 ? 45  TRP A HA   1 
ATOM   140  H HB2  . TRP A 1 26  ? 1.664   -20.042 10.345  1.00 17.58 ? 45  TRP A HB2  1 
ATOM   141  H HB3  . TRP A 1 26  ? 0.474   -19.660 9.364   1.00 17.58 ? 45  TRP A HB3  1 
ATOM   142  H HD1  . TRP A 1 26  ? 3.891   -19.709 9.321   1.00 18.82 ? 45  TRP A HD1  1 
ATOM   143  H HE1  . TRP A 1 26  ? 4.877   -18.338 7.607   1.00 19.39 ? 45  TRP A HE1  1 
ATOM   144  H HE3  . TRP A 1 26  ? -0.024  -17.021 8.088   1.00 17.25 ? 45  TRP A HE3  1 
ATOM   145  H HZ2  . TRP A 1 26  ? 4.051   -16.354 5.871   1.00 19.78 ? 45  TRP A HZ2  1 
ATOM   146  H HZ3  . TRP A 1 26  ? 0.192   -15.429 6.401   1.00 18.46 ? 45  TRP A HZ3  1 
ATOM   147  H HH2  . TRP A 1 26  ? 2.186   -15.127 5.309   1.00 20.19 ? 45  TRP A HH2  1 
ATOM   148  N N    . ASP A 1 27  ? -0.785  -19.417 12.832  1.00 14.89 ? 46  ASP A N    1 
ATOM   149  C CA   . ASP A 1 27  ? -1.881  -20.276 13.294  1.00 14.89 ? 46  ASP A CA   1 
ATOM   150  C C    . ASP A 1 27  ? -3.229  -19.742 12.824  1.00 14.89 ? 46  ASP A C    1 
ATOM   151  O O    . ASP A 1 27  ? -4.103  -20.510 12.414  1.00 14.89 ? 46  ASP A O    1 
ATOM   152  C CB   . ASP A 1 27  ? -1.896  -20.387 14.825  1.00 14.89 ? 46  ASP A CB   1 
ATOM   153  C CG   . ASP A 1 27  ? -0.690  -21.107 15.397  1.00 16.98 ? 46  ASP A CG   1 
ATOM   154  O OD1  . ASP A 1 27  ? 0.002   -21.826 14.650  1.00 20.09 ? 46  ASP A OD1  1 
ATOM   155  O OD2  . ASP A 1 27  ? -0.476  -20.937 16.611  1.00 17.75 ? 46  ASP A OD2  1 
ATOM   156  N N    . THR A 1 28  ? -3.417  -18.428 12.927  1.00 13.51 ? 47  THR A N    1 
ATOM   157  C CA   . THR A 1 28  ? -4.590  -17.720 12.466  1.00 12.86 ? 47  THR A CA   1 
ATOM   158  C C    . THR A 1 28  ? -4.072  -16.468 11.754  1.00 12.32 ? 47  THR A C    1 
ATOM   159  O O    . THR A 1 28  ? -2.874  -16.158 11.805  1.00 12.39 ? 47  THR A O    1 
ATOM   160  C CB   . THR A 1 28  ? -5.517  -17.317 13.629  1.00 12.91 ? 47  THR A CB   1 
ATOM   161  O OG1  . THR A 1 28  ? -4.786  -16.551 14.588  1.00 13.57 ? 47  THR A OG1  1 
ATOM   162  C CG2  . THR A 1 28  ? -6.073  -18.540 14.312  1.00 13.71 ? 47  THR A CG2  1 
ATOM   163  H H    . THR A 1 28  ? -2.840  -17.899 13.283  1.00 16.22 ? 47  THR A H    1 
ATOM   164  H HA   . THR A 1 28  ? -5.108  -18.275 11.861  1.00 15.44 ? 47  THR A HA   1 
ATOM   165  H HB   . THR A 1 28  ? -6.253  -16.791 13.279  1.00 15.50 ? 47  THR A HB   1 
ATOM   166  H HG1  . THR A 1 28  ? -5.309  -16.240 15.167  1.00 16.29 ? 47  THR A HG1  1 
ATOM   167  H HG21 . THR A 1 28  ? -6.866  -18.305 14.819  1.00 16.46 ? 47  THR A HG21 1 
ATOM   168  H HG22 . THR A 1 28  ? -6.308  -19.211 13.653  1.00 16.46 ? 47  THR A HG22 1 
ATOM   169  H HG23 . THR A 1 28  ? -5.412  -18.911 14.917  1.00 16.46 ? 47  THR A HG23 1 
ATOM   170  N N    . VAL A 1 29  ? -4.972  -15.717 11.129  1.00 11.83 ? 48  VAL A N    1 
ATOM   171  C CA   . VAL A 1 29  ? -4.558  -14.508 10.412  1.00 11.29 ? 48  VAL A CA   1 
ATOM   172  C C    . VAL A 1 29  ? -3.694  -13.628 11.320  1.00 10.98 ? 48  VAL A C    1 
ATOM   173  O O    . VAL A 1 29  ? -4.123  -13.278 12.435  1.00 11.60 ? 48  VAL A O    1 
ATOM   174  C CB   . VAL A 1 29  ? -5.771  -13.716 9.892   1.00 12.12 ? 48  VAL A CB   1 
ATOM   175  C CG1  . VAL A 1 29  ? -5.342  -12.341 9.354   1.00 13.15 ? 48  VAL A CG1  1 
ATOM   176  C CG2  . VAL A 1 29  ? -6.528  -14.509 8.824   1.00 12.50 ? 48  VAL A CG2  1 
ATOM   177  H H    . VAL A 1 29  ? -5.815  -15.882 11.103  1.00 14.20 ? 48  VAL A H    1 
ATOM   178  H HA   . VAL A 1 29  ? -4.015  -14.785 9.657   1.00 13.55 ? 48  VAL A HA   1 
ATOM   179  H HB   . VAL A 1 29  ? -6.378  -13.567 10.634  1.00 14.55 ? 48  VAL A HB   1 
ATOM   180  H HG11 . VAL A 1 29  ? -6.084  -11.945 8.872   1.00 15.78 ? 48  VAL A HG11 1 
ATOM   181  H HG12 . VAL A 1 29  ? -5.092  -11.774 10.101  1.00 15.78 ? 48  VAL A HG12 1 
ATOM   182  H HG13 . VAL A 1 29  ? -4.585  -12.457 8.759   1.00 15.78 ? 48  VAL A HG13 1 
ATOM   183  H HG21 . VAL A 1 29  ? -7.354  -14.046 8.612   1.00 15.01 ? 48  VAL A HG21 1 
ATOM   184  H HG22 . VAL A 1 29  ? -5.975  -14.578 8.030   1.00 15.01 ? 48  VAL A HG22 1 
ATOM   185  H HG23 . VAL A 1 29  ? -6.725  -15.395 9.168   1.00 15.01 ? 48  VAL A HG23 1 
ATOM   186  N N    . PRO A 1 30  ? -2.503  -13.208 10.884  1.00 10.09 ? 49  PRO A N    1 
ATOM   187  C CA   . PRO A 1 30  ? -1.665  -12.363 11.748  1.00 10.16 ? 49  PRO A CA   1 
ATOM   188  C C    . PRO A 1 30  ? -2.201  -10.937 11.791  1.00 11.35 ? 49  PRO A C    1 
ATOM   189  O O    . PRO A 1 30  ? -2.346  -10.284 10.755  1.00 11.97 ? 49  PRO A O    1 
ATOM   190  C CB   . PRO A 1 30  ? -0.290  -12.426 11.084  1.00 11.91 ? 49  PRO A CB   1 
ATOM   191  C CG   . PRO A 1 30  ? -0.493  -12.951 9.713   1.00 13.93 ? 49  PRO A CG   1 
ATOM   192  C CD   . PRO A 1 30  ? -1.802  -13.672 9.672   1.00 11.59 ? 49  PRO A CD   1 
ATOM   193  H HA   . PRO A 1 30  ? -1.620  -12.725 12.646  1.00 12.19 ? 49  PRO A HA   1 
ATOM   194  H HB2  . PRO A 1 30  ? 0.095   -11.536 11.053  1.00 14.30 ? 49  PRO A HB2  1 
ATOM   195  H HB3  . PRO A 1 30  ? 0.286   -13.019 11.592  1.00 14.30 ? 49  PRO A HB3  1 
ATOM   196  H HG2  . PRO A 1 30  ? -0.500  -12.209 9.089   1.00 16.73 ? 49  PRO A HG2  1 
ATOM   197  H HG3  . PRO A 1 30  ? 0.231   -13.560 9.497   1.00 16.73 ? 49  PRO A HG3  1 
ATOM   198  H HD2  . PRO A 1 30  ? -2.300  -13.433 8.875   1.00 13.91 ? 49  PRO A HD2  1 
ATOM   199  H HD3  . PRO A 1 30  ? -1.666  -14.632 9.701   1.00 13.91 ? 49  PRO A HD3  1 
ATOM   200  N N    . ILE A 1 31  ? -2.471  -10.442 12.993  1.00 12.48 ? 50  ILE A N    1 
ATOM   201  C CA   . ILE A 1 31  ? -3.152  -9.167  13.224  1.00 13.80 ? 50  ILE A CA   1 
ATOM   202  C C    . ILE A 1 31  ? -2.225  -8.234  13.991  1.00 12.85 ? 50  ILE A C    1 
ATOM   203  O O    . ILE A 1 31  ? -1.511  -8.665  14.905  1.00 13.63 ? 50  ILE A O    1 
ATOM   204  C CB   . ILE A 1 31  ? -4.461  -9.391  14.034  1.00 15.58 ? 50  ILE A CB   1 
ATOM   205  C CG1  . ILE A 1 31  ? -5.470  -10.229 13.252  1.00 16.68 ? 50  ILE A CG1  1 
ATOM   206  C CG2  . ILE A 1 31  ? -5.070  -8.069  14.541  1.00 16.87 ? 50  ILE A CG2  1 
ATOM   207  C CD1  . ILE A 1 31  ? -5.996  -9.595  12.036  1.00 17.06 ? 50  ILE A CD1  1 
ATOM   208  H H    . ILE A 1 31  ? -2.262  -10.843 13.725  1.00 14.99 ? 50  ILE A H    1 
ATOM   209  H HA   . ILE A 1 31  ? -3.357  -8.754  12.371  1.00 16.57 ? 50  ILE A HA   1 
ATOM   210  H HB   . ILE A 1 31  ? -4.218  -9.900  14.823  1.00 18.70 ? 50  ILE A HB   1 
ATOM   211  H HG12 . ILE A 1 31  ? -5.040  -11.057 12.984  1.00 20.03 ? 50  ILE A HG12 1 
ATOM   212  H HG13 . ILE A 1 31  ? -6.225  -10.420 13.830  1.00 20.03 ? 50  ILE A HG13 1 
ATOM   213  H HG21 . ILE A 1 31  ? -5.994  -8.224  14.795  1.00 20.26 ? 50  ILE A HG21 1 
ATOM   214  H HG22 . ILE A 1 31  ? -4.563  -7.761  15.308  1.00 20.26 ? 50  ILE A HG22 1 
ATOM   215  H HG23 . ILE A 1 31  ? -5.029  -7.410  13.831  1.00 20.26 ? 50  ILE A HG23 1 
ATOM   216  H HD11 . ILE A 1 31  ? -6.654  -10.183 11.632  1.00 20.48 ? 50  ILE A HD11 1 
ATOM   217  H HD12 . ILE A 1 31  ? -6.410  -8.750  12.274  1.00 20.48 ? 50  ILE A HD12 1 
ATOM   218  H HD13 . ILE A 1 31  ? -5.265  -9.442  11.417  1.00 20.48 ? 50  ILE A HD13 1 
ATOM   219  N N    . ALA A 1 32  ? -2.309  -6.942  13.671  1.00 11.04 ? 51  ALA A N    1 
ATOM   220  C CA   . ALA A 1 32  ? -1.698  -5.879  14.447  1.00 11.42 ? 51  ALA A CA   1 
ATOM   221  C C    . ALA A 1 32  ? -2.760  -4.824  14.719  1.00 11.34 ? 51  ALA A C    1 
ATOM   222  O O    . ALA A 1 32  ? -3.853  -4.858  14.147  1.00 11.64 ? 51  ALA A O    1 
ATOM   223  C CB   . ALA A 1 32  ? -0.500  -5.267  13.715  1.00 11.84 ? 51  ALA A CB   1 
ATOM   224  H H    . ALA A 1 32  ? -2.733  -6.652  12.981  1.00 13.25 ? 51  ALA A H    1 
ATOM   225  H HA   . ALA A 1 32  ? -1.376  -6.225  15.293  1.00 13.71 ? 51  ALA A HA   1 
ATOM   226  H HB1  . ALA A 1 32  ? -0.140  -4.541  14.250  1.00 14.21 ? 51  ALA A HB1  1 
ATOM   227  H HB2  . ALA A 1 32  ? 0.176   -5.951  13.589  1.00 14.21 ? 51  ALA A HB2  1 
ATOM   228  H HB3  . ALA A 1 32  ? -0.794  -4.929  12.854  1.00 14.21 ? 51  ALA A HB3  1 
ATOM   229  N N    . PHE A 1 33  ? -2.436  -3.898  15.614  1.00 10.17 ? 52  PHE A N    1 
ATOM   230  C CA   . PHE A 1 33  ? -3.299  -2.775  15.960  1.00 9.60  ? 52  PHE A CA   1 
ATOM   231  C C    . PHE A 1 33  ? -2.543  -1.472  15.747  1.00 9.97  ? 52  PHE A C    1 
ATOM   232  O O    . PHE A 1 33  ? -1.319  -1.417  15.902  1.00 10.46 ? 52  PHE A O    1 
ATOM   233  C CB   . PHE A 1 33  ? -3.756  -2.858  17.426  1.00 10.84 ? 52  PHE A CB   1 
ATOM   234  C CG   . PHE A 1 33  ? -4.705  -3.992  17.711  1.00 10.97 ? 52  PHE A CG   1 
ATOM   235  C CD1  . PHE A 1 33  ? -6.033  -3.890  17.379  1.00 11.01 ? 52  PHE A CD1  1 
ATOM   236  C CD2  . PHE A 1 33  ? -4.259  -5.163  18.306  1.00 11.29 ? 52  PHE A CD2  1 
ATOM   237  C CE1  . PHE A 1 33  ? -6.914  -4.909  17.624  1.00 12.03 ? 52  PHE A CE1  1 
ATOM   238  C CE2  . PHE A 1 33  ? -5.150  -6.204  18.546  1.00 11.87 ? 52  PHE A CE2  1 
ATOM   239  C CZ   . PHE A 1 33  ? -6.482  -6.061  18.218  1.00 12.47 ? 52  PHE A CZ   1 
ATOM   240  H H    . PHE A 1 33  ? -1.695  -3.898  16.050  1.00 12.21 ? 52  PHE A H    1 
ATOM   241  H HA   . PHE A 1 33  ? -4.082  -2.779  15.388  1.00 11.53 ? 52  PHE A HA   1 
ATOM   242  H HB2  . PHE A 1 33  ? -2.975  -2.978  17.988  1.00 13.02 ? 52  PHE A HB2  1 
ATOM   243  H HB3  . PHE A 1 33  ? -4.207  -2.031  17.657  1.00 13.02 ? 52  PHE A HB3  1 
ATOM   244  H HD1  . PHE A 1 33  ? -6.342  -3.110  16.979  1.00 13.22 ? 52  PHE A HD1  1 
ATOM   245  H HD2  . PHE A 1 33  ? -3.365  -5.252  18.544  1.00 13.55 ? 52  PHE A HD2  1 
ATOM   246  H HE1  . PHE A 1 33  ? -7.808  -4.816  17.385  1.00 14.44 ? 52  PHE A HE1  1 
ATOM   247  H HE2  . PHE A 1 33  ? -4.847  -6.996  18.927  1.00 14.25 ? 52  PHE A HE2  1 
ATOM   248  H HZ   . PHE A 1 33  ? -7.084  -6.746  18.401  1.00 14.97 ? 52  PHE A HZ   1 
ATOM   249  N N    . HIS A 1 34  ? -3.291  -0.421  15.410  1.00 10.47 ? 53  HIS A N    1 
ATOM   250  C CA   . HIS A 1 34  ? -2.727  0.915   15.243  1.00 10.91 ? 53  HIS A CA   1 
ATOM   251  C C    . HIS A 1 34  ? -3.857  1.894   15.546  1.00 10.46 ? 53  HIS A C    1 
ATOM   252  O O    . HIS A 1 34  ? -4.684  2.191   14.673  1.00 11.22 ? 53  HIS A O    1 
ATOM   253  C CB   . HIS A 1 34  ? -2.170  1.133   13.849  1.00 11.41 ? 53  HIS A CB   1 
ATOM   254  C CG   . HIS A 1 34  ? -1.513  2.460   13.678  1.00 12.48 ? 53  HIS A CG   1 
ATOM   255  N ND1  . HIS A 1 34  ? -0.171  2.603   13.428  1.00 14.92 ? 53  HIS A ND1  1 
ATOM   256  C CD2  . HIS A 1 34  ? -2.010  3.712   13.789  1.00 13.63 ? 53  HIS A CD2  1 
ATOM   257  C CE1  . HIS A 1 34  ? 0.126   3.888   13.334  1.00 14.60 ? 53  HIS A CE1  1 
ATOM   258  N NE2  . HIS A 1 34  ? -0.976  4.583   13.547  1.00 13.95 ? 53  HIS A NE2  1 
ATOM   259  H H    . HIS A 1 34  ? -4.138  -0.458  15.270  1.00 12.58 ? 53  HIS A H    1 
ATOM   260  H HA   . HIS A 1 34  ? -2.000  1.039   15.873  1.00 13.10 ? 53  HIS A HA   1 
ATOM   261  H HB2  . HIS A 1 34  ? -1.509  0.447   13.664  1.00 13.69 ? 53  HIS A HB2  1 
ATOM   262  H HB3  . HIS A 1 34  ? -2.896  1.075   13.208  1.00 13.69 ? 53  HIS A HB3  1 
ATOM   263  H HD1  . HIS A 1 34  ? 0.389   1.956   13.344  1.00 17.92 ? 53  HIS A HD1  1 
ATOM   264  H HD2  . HIS A 1 34  ? -2.889  3.941   13.991  1.00 16.37 ? 53  HIS A HD2  1 
ATOM   265  H HE1  . HIS A 1 34  ? 0.966   4.241   13.150  1.00 17.52 ? 53  HIS A HE1  1 
ATOM   266  H HE2  . HIS A 1 34  ? -1.036  5.441   13.537  1.00 16.75 ? 53  HIS A HE2  1 
ATOM   267  N N    . PHE A 1 35  ? -3.882  2.407   16.769  1.00 10.04 ? 54  PHE A N    1 
ATOM   268  C CA   . PHE A 1 35  ? -4.965  3.315   17.136  1.00 10.23 ? 54  PHE A CA   1 
ATOM   269  C C    . PHE A 1 35  ? -4.601  4.059   18.410  1.00 10.32 ? 54  PHE A C    1 
ATOM   270  O O    . PHE A 1 35  ? -3.609  3.746   19.068  1.00 10.60 ? 54  PHE A O    1 
ATOM   271  C CB   . PHE A 1 35  ? -6.314  2.577   17.284  1.00 9.84  ? 54  PHE A CB   1 
ATOM   272  C CG   . PHE A 1 35  ? -6.410  1.694   18.517  1.00 10.06 ? 54  PHE A CG   1 
ATOM   273  C CD1  . PHE A 1 35  ? -6.877  2.199   19.725  1.00 12.90 ? 54  PHE A CD1  1 
ATOM   274  C CD2  . PHE A 1 35  ? -6.076  0.363   18.461  1.00 10.16 ? 54  PHE A CD2  1 
ATOM   275  C CE1  . PHE A 1 35  ? -6.962  1.414   20.828  1.00 14.00 ? 54  PHE A CE1  1 
ATOM   276  C CE2  . PHE A 1 35  ? -6.167  -0.446  19.568  1.00 11.13 ? 54  PHE A CE2  1 
ATOM   277  C CZ   . PHE A 1 35  ? -6.600  0.093   20.770  1.00 13.07 ? 54  PHE A CZ   1 
ATOM   278  H H    . PHE A 1 35  ? -3.304  2.251   17.386  1.00 12.05 ? 54  PHE A H    1 
ATOM   279  H HA   . PHE A 1 35  ? -5.057  3.973   16.430  1.00 12.29 ? 54  PHE A HA   1 
ATOM   280  H HB2  . PHE A 1 35  ? -7.024  3.236   17.338  1.00 11.81 ? 54  PHE A HB2  1 
ATOM   281  H HB3  . PHE A 1 35  ? -6.445  2.011   16.506  1.00 11.81 ? 54  PHE A HB3  1 
ATOM   282  H HD1  . PHE A 1 35  ? -7.137  3.090   19.777  1.00 15.48 ? 54  PHE A HD1  1 
ATOM   283  H HD2  . PHE A 1 35  ? -5.781  0.002   17.656  1.00 12.20 ? 54  PHE A HD2  1 
ATOM   284  H HE1  . PHE A 1 35  ? -7.267  1.775   21.629  1.00 16.81 ? 54  PHE A HE1  1 
ATOM   285  H HE2  . PHE A 1 35  ? -5.941  -1.347  19.512  1.00 13.37 ? 54  PHE A HE2  1 
ATOM   286  H HZ   . PHE A 1 35  ? -6.645  -0.438  21.532  1.00 15.69 ? 54  PHE A HZ   1 
ATOM   287  N N    . GLY A 1 36  ? -5.426  5.046   18.739  1.00 10.79 ? 55  GLY A N    1 
ATOM   288  C CA   . GLY A 1 36  ? -5.345  5.716   20.021  1.00 11.01 ? 55  GLY A CA   1 
ATOM   289  C C    . GLY A 1 36  ? -6.722  5.879   20.627  1.00 11.03 ? 55  GLY A C    1 
ATOM   290  O O    . GLY A 1 36  ? -7.716  6.018   19.919  1.00 11.69 ? 55  GLY A O    1 
ATOM   291  H H    . GLY A 1 36  ? -6.048  5.348   18.227  1.00 12.95 ? 55  GLY A H    1 
ATOM   292  H HA2  . GLY A 1 36  ? -4.796  5.195   20.629  1.00 13.22 ? 55  GLY A HA2  1 
ATOM   293  H HA3  . GLY A 1 36  ? -4.947  6.593   19.909  1.00 13.22 ? 55  GLY A HA3  1 
ATOM   294  N N    . LYS A 1 37  ? -6.757  5.931   21.952  1.00 11.67 ? 56  LYS A N    1 
ATOM   295  C CA   . LYS A 1 37  ? -7.977  6.185   22.727  1.00 11.33 ? 56  LYS A CA   1 
ATOM   296  C C    . LYS A 1 37  ? -7.683  7.462   23.507  1.00 12.23 ? 56  LYS A C    1 
ATOM   297  O O    . LYS A 1 37  ? -7.051  7.417   24.563  1.00 12.84 ? 56  LYS A O    1 
ATOM   298  C CB   . LYS A 1 37  ? -8.261  5.011   23.659  1.00 11.53 ? 56  LYS A CB   1 
ATOM   299  C CG   . LYS A 1 37  ? -9.513  5.234   24.510  1.00 12.06 ? 56  LYS A CG   1 
ATOM   300  C CD   . LYS A 1 37  ? -9.643  4.140   25.550  1.00 13.00 ? 56  LYS A CD   1 
ATOM   301  C CE   . LYS A 1 37  ? -10.782 4.373   26.518  1.00 12.84 ? 56  LYS A CE   1 
ATOM   302  N NZ   . LYS A 1 37  ? -10.882 3.282   27.520  1.00 13.40 ? 56  LYS A NZ   1 
ATOM   303  H H    . LYS A 1 37  ? -6.063  5.820   22.448  1.00 14.01 ? 56  LYS A H    1 
ATOM   304  H HA   . LYS A 1 37  ? -8.752  6.310   22.158  1.00 13.60 ? 56  LYS A HA   1 
ATOM   305  H HB2  . LYS A 1 37  ? -8.395  4.210   23.128  1.00 13.84 ? 56  LYS A HB2  1 
ATOM   306  H HB3  . LYS A 1 37  ? -7.506  4.891   24.257  1.00 13.84 ? 56  LYS A HB3  1 
ATOM   307  H HG2  . LYS A 1 37  ? -9.450  6.089   24.965  1.00 14.48 ? 56  LYS A HG2  1 
ATOM   308  H HG3  . LYS A 1 37  ? -10.300 5.218   23.943  1.00 14.48 ? 56  LYS A HG3  1 
ATOM   309  H HD2  . LYS A 1 37  ? -9.802  3.295   25.100  1.00 15.60 ? 56  LYS A HD2  1 
ATOM   310  H HD3  . LYS A 1 37  ? -8.821  4.093   26.063  1.00 15.60 ? 56  LYS A HD3  1 
ATOM   311  H HE2  . LYS A 1 37  ? -10.635 5.208   26.990  1.00 15.41 ? 56  LYS A HE2  1 
ATOM   312  H HE3  . LYS A 1 37  ? -11.617 4.412   26.026  1.00 15.41 ? 56  LYS A HE3  1 
ATOM   313  H HZ1  . LYS A 1 37  ? -11.541 3.455   28.094  1.00 16.09 ? 56  LYS A HZ1  1 
ATOM   314  H HZ2  . LYS A 1 37  ? -11.050 2.509   27.113  1.00 16.09 ? 56  LYS A HZ2  1 
ATOM   315  H HZ3  . LYS A 1 37  ? -10.118 3.211   27.971  1.00 16.09 ? 56  LYS A HZ3  1 
ATOM   316  N N    A SER A 1 38  ? -8.147  8.606   22.996  0.54 13.18 ? 57  SER A N    1 
ATOM   317  N N    B SER A 1 38  ? -8.130  8.610   22.998  0.46 12.58 ? 57  SER A N    1 
ATOM   318  C CA   A SER A 1 38  ? -7.763  9.874   23.611  0.54 15.13 ? 57  SER A CA   1 
ATOM   319  C CA   B SER A 1 38  ? -7.744  9.870   23.627  0.46 13.65 ? 57  SER A CA   1 
ATOM   320  C C    A SER A 1 38  ? -8.336  10.028  25.017  0.54 14.88 ? 57  SER A C    1 
ATOM   321  C C    B SER A 1 38  ? -8.350  10.048  25.014  0.46 14.17 ? 57  SER A C    1 
ATOM   322  O O    A SER A 1 38  ? -7.748  10.728  25.849  0.54 15.42 ? 57  SER A O    1 
ATOM   323  O O    B SER A 1 38  ? -7.782  10.778  25.833  0.46 14.68 ? 57  SER A O    1 
ATOM   324  C CB   A SER A 1 38  ? -8.219  11.053  22.749  0.54 17.03 ? 57  SER A CB   1 
ATOM   325  C CB   B SER A 1 38  ? -8.131  11.059  22.741  0.46 13.80 ? 57  SER A CB   1 
ATOM   326  O OG   A SER A 1 38  ? -9.630  11.120  22.691  0.54 19.06 ? 57  SER A OG   1 
ATOM   327  O OG   B SER A 1 38  ? -7.364  11.066  21.551  0.46 13.69 ? 57  SER A OG   1 
ATOM   328  H H    A SER A 1 38  ? -8.668  8.671   22.315  0.54 15.83 ? 57  SER A H    1 
ATOM   329  H H    B SER A 1 38  ? -8.642  8.684   22.310  0.46 15.10 ? 57  SER A H    1 
ATOM   330  H HA   A SER A 1 38  ? -6.795  9.890   23.669  0.54 18.16 ? 57  SER A HA   1 
ATOM   331  H HA   B SER A 1 38  ? -6.779  9.869   23.721  0.46 16.39 ? 57  SER A HA   1 
ATOM   332  H HB2  A SER A 1 38  ? -7.879  11.876  23.135  0.54 20.44 ? 57  SER A HB2  1 
ATOM   333  H HB2  B SER A 1 38  ? -9.071  10.990  22.511  0.46 16.57 ? 57  SER A HB2  1 
ATOM   334  H HB3  A SER A 1 38  ? -7.871  10.940  21.850  0.54 20.44 ? 57  SER A HB3  1 
ATOM   335  H HB3  B SER A 1 38  ? -7.968  11.882  23.227  0.46 16.57 ? 57  SER A HB3  1 
ATOM   336  H HG   A SER A 1 38  ? -9.868  11.716  22.149  0.54 22.88 ? 57  SER A HG   1 
ATOM   337  H HG   B SER A 1 38  ? -7.620  11.689  21.048  0.46 16.44 ? 57  SER A HG   1 
ATOM   338  N N    . GLN A 1 39  ? -9.471  9.394   25.303  1.00 14.14 ? 58  GLN A N    1 
ATOM   339  C CA   . GLN A 1 39  ? -10.198 9.688   26.537  1.00 16.04 ? 58  GLN A CA   1 
ATOM   340  C C    . GLN A 1 39  ? -9.625  8.995   27.760  1.00 14.87 ? 58  GLN A C    1 
ATOM   341  O O    . GLN A 1 39  ? -10.017 9.353   28.878  1.00 16.27 ? 58  GLN A O    1 
ATOM   342  C CB   . GLN A 1 39  ? -11.670 9.339   26.345  1.00 19.72 ? 58  GLN A CB   1 
ATOM   343  C CG   . GLN A 1 39  ? -11.875 7.904   26.088  1.00 22.91 ? 58  GLN A CG   1 
ATOM   344  C CD   . GLN A 1 39  ? -12.169 7.636   24.643  1.00 23.60 ? 58  GLN A CD   1 
ATOM   345  O OE1  . GLN A 1 39  ? -11.538 8.237   23.752  1.00 21.32 ? 58  GLN A OE1  1 
ATOM   346  N NE2  . GLN A 1 39  ? -13.099 6.696   24.390  1.00 25.45 ? 58  GLN A NE2  1 
ATOM   347  H H    . GLN A 1 39  ? -9.836  8.796   24.805  1.00 16.97 ? 58  GLN A H    1 
ATOM   348  H HA   . GLN A 1 39  ? -10.145 10.638  26.723  1.00 19.25 ? 58  GLN A HA   1 
ATOM   349  H HB2  . GLN A 1 39  ? -12.160 9.575   27.148  1.00 23.66 ? 58  GLN A HB2  1 
ATOM   350  H HB3  . GLN A 1 39  ? -12.017 9.835   25.587  1.00 23.66 ? 58  GLN A HB3  1 
ATOM   351  H HG2  . GLN A 1 39  ? -11.071 7.418   26.330  1.00 27.49 ? 58  GLN A HG2  1 
ATOM   352  H HG3  . GLN A 1 39  ? -12.626 7.589   26.615  1.00 27.49 ? 58  GLN A HG3  1 
ATOM   353  H HE21 . GLN A 1 39  ? -13.487 6.288   25.040  1.00 30.54 ? 58  GLN A HE21 1 
ATOM   354  H HE22 . GLN A 1 39  ? -13.305 6.503   23.577  1.00 30.54 ? 58  GLN A HE22 1 
ATOM   355  N N    . GLY A 1 40  ? -8.716  8.046   27.594  1.00 14.22 ? 59  GLY A N    1 
ATOM   356  C CA   . GLY A 1 40  ? -8.091  7.404   28.733  1.00 13.94 ? 59  GLY A CA   1 
ATOM   357  C C    . GLY A 1 40  ? -7.371  6.144   28.314  1.00 12.26 ? 59  GLY A C    1 
ATOM   358  O O    . GLY A 1 40  ? -7.351  5.771   27.144  1.00 12.89 ? 59  GLY A O    1 
ATOM   359  H H    . GLY A 1 40  ? -8.445  7.757   26.830  1.00 17.07 ? 59  GLY A H    1 
ATOM   360  H HA2  . GLY A 1 40  ? -7.450  8.009   29.139  1.00 16.73 ? 59  GLY A HA2  1 
ATOM   361  H HA3  . GLY A 1 40  ? -8.767  7.173   29.389  1.00 16.73 ? 59  GLY A HA3  1 
ATOM   362  N N    . LEU A 1 41  ? -6.781  5.483   29.307  1.00 12.53 ? 60  LEU A N    1 
ATOM   363  C CA   . LEU A 1 41  ? -6.169  4.195   29.036  1.00 12.35 ? 60  LEU A CA   1 
ATOM   364  C C    . LEU A 1 41  ? -7.238  3.193   28.617  1.00 12.60 ? 60  LEU A C    1 
ATOM   365  O O    . LEU A 1 41  ? -8.423  3.352   28.907  1.00 13.17 ? 60  LEU A O    1 
ATOM   366  C CB   . LEU A 1 41  ? -5.490  3.647   30.291  1.00 13.39 ? 60  LEU A CB   1 
ATOM   367  C CG   . LEU A 1 41  ? -4.315  4.446   30.842  1.00 13.98 ? 60  LEU A CG   1 
ATOM   368  C CD1  . LEU A 1 41  ? -3.863  3.830   32.172  1.00 15.23 ? 60  LEU A CD1  1 
ATOM   369  C CD2  . LEU A 1 41  ? -3.158  4.509   29.856  1.00 14.12 ? 60  LEU A CD2  1 
ATOM   370  H H    . LEU A 1 41  ? -6.725  5.754   30.121  1.00 15.04 ? 60  LEU A H    1 
ATOM   371  H HA   . LEU A 1 41  ? -5.510  4.301   28.332  1.00 14.82 ? 60  LEU A HA   1 
ATOM   372  H HB2  . LEU A 1 41  ? -6.155  3.599   30.995  1.00 16.08 ? 60  LEU A HB2  1 
ATOM   373  H HB3  . LEU A 1 41  ? -5.158  2.758   30.088  1.00 16.08 ? 60  LEU A HB3  1 
ATOM   374  H HG   . LEU A 1 41  ? -4.598  5.361   30.992  1.00 16.78 ? 60  LEU A HG   1 
ATOM   375  H HD11 . LEU A 1 41  ? -3.160  4.380   32.552  1.00 18.28 ? 60  LEU A HD11 1 
ATOM   376  H HD12 . LEU A 1 41  ? -4.621  3.797   32.778  1.00 18.28 ? 60  LEU A HD12 1 
ATOM   377  H HD13 . LEU A 1 41  ? -3.531  2.934   32.009  1.00 18.28 ? 60  LEU A HD13 1 
ATOM   378  H HD21 . LEU A 1 41  ? -2.438  5.029   30.246  1.00 16.95 ? 60  LEU A HD21 1 
ATOM   379  H HD22 . LEU A 1 41  ? -2.852  3.608   29.669  1.00 16.95 ? 60  LEU A HD22 1 
ATOM   380  H HD23 . LEU A 1 41  ? -3.463  4.930   29.037  1.00 16.95 ? 60  LEU A HD23 1 
ATOM   381  N N    . LEU A 1 42  ? -6.813  2.154   27.908  1.00 11.46 ? 61  LEU A N    1 
ATOM   382  C CA   . LEU A 1 42  ? -7.722  1.056   27.637  1.00 11.94 ? 61  LEU A CA   1 
ATOM   383  C C    . LEU A 1 42  ? -8.305  0.547   28.943  1.00 12.61 ? 61  LEU A C    1 
ATOM   384  O O    . LEU A 1 42  ? -7.605  0.452   29.955  1.00 12.83 ? 61  LEU A O    1 
ATOM   385  C CB   . LEU A 1 42  ? -6.968  -0.072  26.936  1.00 12.08 ? 61  LEU A CB   1 
ATOM   386  C CG   . LEU A 1 42  ? -6.360  0.299   25.573  1.00 13.11 ? 61  LEU A CG   1 
ATOM   387  C CD1  . LEU A 1 42  ? -5.695  -0.925  24.938  1.00 13.63 ? 61  LEU A CD1  1 
ATOM   388  C CD2  . LEU A 1 42  ? -7.397  0.895   24.633  1.00 14.57 ? 61  LEU A CD2  1 
ATOM   389  H H    . LEU A 1 42  ? -6.023  2.066   27.582  1.00 13.76 ? 61  LEU A H    1 
ATOM   390  H HA   . LEU A 1 42  ? -8.443  1.350   27.058  1.00 14.33 ? 61  LEU A HA   1 
ATOM   391  H HB2  . LEU A 1 42  ? -6.241  -0.358  27.511  1.00 14.50 ? 61  LEU A HB2  1 
ATOM   392  H HB3  . LEU A 1 42  ? -7.584  -0.808  26.790  1.00 14.50 ? 61  LEU A HB3  1 
ATOM   393  H HG   . LEU A 1 42  ? -5.684  0.980   25.716  1.00 15.74 ? 61  LEU A HG   1 
ATOM   394  H HD11 . LEU A 1 42  ? -5.333  -0.674  24.073  1.00 16.36 ? 61  LEU A HD11 1 
ATOM   395  H HD12 . LEU A 1 42  ? -4.981  -1.233  25.518  1.00 16.36 ? 61  LEU A HD12 1 
ATOM   396  H HD13 . LEU A 1 42  ? -6.358  -1.624  24.829  1.00 16.36 ? 61  LEU A HD13 1 
ATOM   397  H HD21 . LEU A 1 42  ? -7.034  0.915   23.734  1.00 17.50 ? 61  LEU A HD21 1 
ATOM   398  H HD22 . LEU A 1 42  ? -8.196  0.346   24.655  1.00 17.50 ? 61  LEU A HD22 1 
ATOM   399  H HD23 . LEU A 1 42  ? -7.606  1.796   24.926  1.00 17.50 ? 61  LEU A HD23 1 
ATOM   400  N N    . THR A 1 43  ? -9.596  0.223   28.919  1.00 12.44 ? 62  THR A N    1 
ATOM   401  C CA   . THR A 1 43  ? -10.187 -0.458  30.055  1.00 12.28 ? 62  THR A CA   1 
ATOM   402  C C    . THR A 1 43  ? -9.573  -1.852  30.186  1.00 13.06 ? 62  THR A C    1 
ATOM   403  O O    . THR A 1 43  ? -8.886  -2.348  29.296  1.00 13.10 ? 62  THR A O    1 
ATOM   404  C CB   . THR A 1 43  ? -11.692 -0.643  29.872  1.00 13.43 ? 62  THR A CB   1 
ATOM   405  O OG1  . THR A 1 43  ? -11.922 -1.525  28.767  1.00 14.26 ? 62  THR A OG1  1 
ATOM   406  C CG2  . THR A 1 43  ? -12.394 0.666   29.664  1.00 13.68 ? 62  THR A CG2  1 
ATOM   407  H H    . THR A 1 43  ? -10.135 0.384   28.268  1.00 14.94 ? 62  THR A H    1 
ATOM   408  H HA   . THR A 1 43  ? -10.023 0.077   30.848  1.00 14.74 ? 62  THR A HA   1 
ATOM   409  H HB   . THR A 1 43  ? -12.071 -1.030  30.677  1.00 16.12 ? 62  THR A HB   1 
ATOM   410  H HG1  . THR A 1 43  ? -12.432 -2.150  28.999  1.00 17.12 ? 62  THR A HG1  1 
ATOM   411  H HG21 . THR A 1 43  ? -13.344 0.563   29.831  1.00 16.42 ? 62  THR A HG21 1 
ATOM   412  H HG22 . THR A 1 43  ? -12.038 1.334   30.271  1.00 16.42 ? 62  THR A HG22 1 
ATOM   413  H HG23 . THR A 1 43  ? -12.266 0.969   28.752  1.00 16.42 ? 62  THR A HG23 1 
ATOM   414  N N    . LYS A 1 44  ? -9.841  -2.498  31.319  1.00 13.84 ? 63  LYS A N    1 
ATOM   415  C CA   . LYS A 1 44  ? -9.353  -3.857  31.515  1.00 16.93 ? 63  LYS A CA   1 
ATOM   416  C C    . LYS A 1 44  ? -9.778  -4.742  30.346  1.00 15.54 ? 63  LYS A C    1 
ATOM   417  O O    . LYS A 1 44  ? -8.976  -5.519  29.805  1.00 15.78 ? 63  LYS A O    1 
ATOM   418  C CB   . LYS A 1 44  ? -9.903  -4.366  32.851  1.00 22.49 ? 63  LYS A CB   1 
ATOM   419  C CG   . LYS A 1 44  ? -9.562  -5.771  33.175  1.00 26.45 ? 63  LYS A CG   1 
ATOM   420  C CD   . LYS A 1 44  ? -10.177 -6.237  34.503  1.00 28.98 ? 63  LYS A CD   1 
ATOM   421  C CE   . LYS A 1 44  ? -11.706 -6.271  34.496  1.00 30.55 ? 63  LYS A CE   1 
ATOM   422  N NZ   . LYS A 1 44  ? -12.228 -6.682  35.833  1.00 32.24 ? 63  LYS A NZ   1 
ATOM   423  H H    . LYS A 1 44  ? -10.294 -2.178  31.976  1.00 16.61 ? 63  LYS A H    1 
ATOM   424  H HA   . LYS A 1 44  ? -8.384  -3.886  31.557  1.00 20.33 ? 63  LYS A HA   1 
ATOM   425  H HB2  . LYS A 1 44  ? -9.548  -3.809  33.561  1.00 26.99 ? 63  LYS A HB2  1 
ATOM   426  H HB3  . LYS A 1 44  ? -10.871 -4.300  32.829  1.00 26.99 ? 63  LYS A HB3  1 
ATOM   427  H HG2  . LYS A 1 44  ? -9.895  -6.349  32.471  1.00 31.74 ? 63  LYS A HG2  1 
ATOM   428  H HG3  . LYS A 1 44  ? -8.598  -5.855  33.244  1.00 31.74 ? 63  LYS A HG3  1 
ATOM   429  H HD2  . LYS A 1 44  ? -9.862  -7.134  34.696  1.00 34.78 ? 63  LYS A HD2  1 
ATOM   430  H HD3  . LYS A 1 44  ? -9.898  -5.630  35.206  1.00 34.78 ? 63  LYS A HD3  1 
ATOM   431  H HE2  . LYS A 1 44  ? -12.049 -5.388  34.289  1.00 36.67 ? 63  LYS A HE2  1 
ATOM   432  H HE3  . LYS A 1 44  ? -12.013 -6.911  33.835  1.00 36.67 ? 63  LYS A HE3  1 
ATOM   433  H HZ1  . LYS A 1 44  ? -13.118 -6.675  35.827  1.00 38.70 ? 63  LYS A HZ1  1 
ATOM   434  H HZ2  . LYS A 1 44  ? -11.947 -7.503  36.030  1.00 38.70 ? 63  LYS A HZ2  1 
ATOM   435  H HZ3  . LYS A 1 44  ? -11.939 -6.120  36.459  1.00 38.70 ? 63  LYS A HZ3  1 
ATOM   436  N N    . GLU A 1 45  ? -11.038 -4.623  29.932  1.00 15.23 ? 64  GLU A N    1 
ATOM   437  C CA   . GLU A 1 45  ? -11.552 -5.472  28.863  1.00 16.19 ? 64  GLU A CA   1 
ATOM   438  C C    . GLU A 1 45  ? -10.889 -5.146  27.530  1.00 13.73 ? 64  GLU A C    1 
ATOM   439  O O    . GLU A 1 45  ? -10.534 -6.052  26.761  1.00 14.07 ? 64  GLU A O    1 
ATOM   440  C CB   . GLU A 1 45  ? -13.071 -5.312  28.754  1.00 18.75 ? 64  GLU A CB   1 
ATOM   441  C CG   . GLU A 1 45  ? -13.881 -5.843  29.938  1.00 21.48 ? 64  GLU A CG   1 
ATOM   442  C CD   . GLU A 1 45  ? -13.924 -4.909  31.144  1.00 24.50 ? 64  GLU A CD   1 
ATOM   443  O OE1  . GLU A 1 45  ? -13.510 -3.727  31.050  1.00 24.90 ? 64  GLU A OE1  1 
ATOM   444  O OE2  . GLU A 1 45  ? -14.421 -5.364  32.201  1.00 27.47 ? 64  GLU A OE2  1 
ATOM   445  H H    . GLU A 1 45  ? -11.610 -4.065  30.250  1.00 18.28 ? 64  GLU A H    1 
ATOM   446  H HA   . GLU A 1 45  ? -11.357 -6.397  29.080  1.00 19.43 ? 64  GLU A HA   1 
ATOM   447  H HB2  . GLU A 1 45  ? -13.272 -4.367  28.668  1.00 22.51 ? 64  GLU A HB2  1 
ATOM   448  H HB3  . GLU A 1 45  ? -13.371 -5.788  27.963  1.00 22.51 ? 64  GLU A HB3  1 
ATOM   449  H HG2  . GLU A 1 45  ? -14.795 -5.989  29.647  1.00 25.79 ? 64  GLU A HG2  1 
ATOM   450  H HG3  . GLU A 1 45  ? -13.489 -6.681  30.230  1.00 25.79 ? 64  GLU A HG3  1 
ATOM   451  N N    . GLU A 1 46  ? -10.685 -3.852  27.259  1.00 12.57 ? 65  GLU A N    1 
ATOM   452  C CA   . GLU A 1 46  ? -10.055 -3.447  26.007  1.00 12.60 ? 65  GLU A CA   1 
ATOM   453  C C    . GLU A 1 46  ? -8.592  -3.876  25.971  1.00 13.31 ? 65  GLU A C    1 
ATOM   454  O O    . GLU A 1 46  ? -8.104  -4.346  24.938  1.00 12.89 ? 65  GLU A O    1 
ATOM   455  C CB   . GLU A 1 46  ? -10.190 -1.930  25.835  1.00 12.03 ? 65  GLU A CB   1 
ATOM   456  C CG   . GLU A 1 46  ? -11.610 -1.467  25.591  1.00 12.85 ? 65  GLU A CG   1 
ATOM   457  C CD   . GLU A 1 46  ? -11.877 -0.002  25.921  1.00 13.69 ? 65  GLU A CD   1 
ATOM   458  O OE1  . GLU A 1 46  ? -10.970 0.701   26.396  1.00 12.82 ? 65  GLU A OE1  1 
ATOM   459  O OE2  . GLU A 1 46  ? -13.025 0.439   25.678  1.00 15.00 ? 65  GLU A OE2  1 
ATOM   460  H H    . GLU A 1 46  ? -10.900 -3.200  27.777  1.00 15.09 ? 65  GLU A H    1 
ATOM   461  H HA   . GLU A 1 46  ? -10.507 -3.873  25.262  1.00 15.12 ? 65  GLU A HA   1 
ATOM   462  H HB2  . GLU A 1 46  ? -9.871  -1.495  26.642  1.00 14.45 ? 65  GLU A HB2  1 
ATOM   463  H HB3  . GLU A 1 46  ? -9.653  -1.654  25.076  1.00 14.45 ? 65  GLU A HB3  1 
ATOM   464  H HG2  . GLU A 1 46  ? -11.818 -1.595  24.652  1.00 15.43 ? 65  GLU A HG2  1 
ATOM   465  H HG3  . GLU A 1 46  ? -12.206 -2.001  26.138  1.00 15.43 ? 65  GLU A HG3  1 
ATOM   466  N N    . ALA A 1 47  ? -7.880  -3.725  27.095  1.00 12.92 ? 66  ALA A N    1 
ATOM   467  C CA   . ALA A 1 47  ? -6.471  -4.110  27.157  1.00 12.55 ? 66  ALA A CA   1 
ATOM   468  C C    . ALA A 1 47  ? -6.313  -5.619  27.049  1.00 12.99 ? 66  ALA A C    1 
ATOM   469  O O    . ALA A 1 47  ? -5.431  -6.110  26.336  1.00 12.93 ? 66  ALA A O    1 
ATOM   470  C CB   . ALA A 1 47  ? -5.868  -3.620  28.473  1.00 13.21 ? 66  ALA A CB   1 
ATOM   471  H H    . ALA A 1 47  ? -8.190  -3.404  27.831  1.00 15.51 ? 66  ALA A H    1 
ATOM   472  H HA   . ALA A 1 47  ? -5.995  -3.697  26.419  1.00 15.06 ? 66  ALA A HA   1 
ATOM   473  H HB1  . ALA A 1 47  ? -4.923  -3.837  28.488  1.00 15.86 ? 66  ALA A HB1  1 
ATOM   474  H HB2  . ALA A 1 47  ? -5.988  -2.660  28.537  1.00 15.86 ? 66  ALA A HB2  1 
ATOM   475  H HB3  . ALA A 1 47  ? -6.320  -4.060  29.210  1.00 15.86 ? 66  ALA A HB3  1 
ATOM   476  N N    . GLU A 1 48  ? -7.165  -6.369  27.753  1.00 12.78 ? 67  GLU A N    1 
ATOM   477  C CA   . GLU A 1 48  ? -7.140  -7.822  27.634  1.00 13.10 ? 67  GLU A CA   1 
ATOM   478  C C    . GLU A 1 48  ? -7.385  -8.247  26.189  1.00 13.34 ? 67  GLU A C    1 
ATOM   479  O O    . GLU A 1 48  ? -6.686  -9.126  25.671  1.00 14.09 ? 67  GLU A O    1 
ATOM   480  C CB   . GLU A 1 48  ? -8.146  -8.441  28.611  1.00 13.46 ? 67  GLU A CB   1 
ATOM   481  C CG   . GLU A 1 48  ? -7.699  -8.332  30.046  1.00 14.25 ? 67  GLU A CG   1 
ATOM   482  C CD   . GLU A 1 48  ? -8.707  -8.823  31.051  1.00 14.65 ? 67  GLU A CD   1 
ATOM   483  O OE1  . GLU A 1 48  ? -9.755  -9.344  30.634  1.00 15.86 ? 67  GLU A OE1  1 
ATOM   484  O OE2  . GLU A 1 48  ? -8.436  -8.693  32.265  1.00 14.64 ? 67  GLU A OE2  1 
ATOM   485  H H    . GLU A 1 48  ? -7.757  -6.064  28.298  1.00 15.35 ? 67  GLU A H    1 
ATOM   486  H HA   . GLU A 1 48  ? -6.267  -8.163  27.885  1.00 15.73 ? 67  GLU A HA   1 
ATOM   487  H HB2  . GLU A 1 48  ? -8.996  -7.980  28.525  1.00 16.16 ? 67  GLU A HB2  1 
ATOM   488  H HB3  . GLU A 1 48  ? -8.255  -9.381  28.400  1.00 16.16 ? 67  GLU A HB3  1 
ATOM   489  H HG2  . GLU A 1 48  ? -6.892  -8.858  30.159  1.00 17.11 ? 67  GLU A HG2  1 
ATOM   490  H HG3  . GLU A 1 48  ? -7.518  -7.400  30.244  1.00 17.11 ? 67  GLU A HG3  1 
ATOM   491  N N    . PHE A 1 49  ? -8.332  -7.600  25.505  1.00 13.44 ? 68  PHE A N    1 
ATOM   492  C CA   . PHE A 1 49  ? -8.640  -7.950  24.115  1.00 12.47 ? 68  PHE A CA   1 
ATOM   493  C C    . PHE A 1 49  ? -7.417  -7.744  23.226  1.00 12.45 ? 68  PHE A C    1 
ATOM   494  O O    . PHE A 1 49  ? -7.006  -8.648  22.485  1.00 13.81 ? 68  PHE A O    1 
ATOM   495  C CB   . PHE A 1 49  ? -9.808  -7.069  23.664  1.00 13.32 ? 68  PHE A CB   1 
ATOM   496  C CG   . PHE A 1 49  ? -10.265 -7.273  22.243  1.00 12.81 ? 68  PHE A CG   1 
ATOM   497  C CD1  . PHE A 1 49  ? -9.616  -6.620  21.195  1.00 12.77 ? 68  PHE A CD1  1 
ATOM   498  C CD2  . PHE A 1 49  ? -11.366 -8.050  21.950  1.00 13.21 ? 68  PHE A CD2  1 
ATOM   499  C CE1  . PHE A 1 49  ? -10.048 -6.755  19.890  1.00 13.56 ? 68  PHE A CE1  1 
ATOM   500  C CE2  . PHE A 1 49  ? -11.799 -8.200  20.641  1.00 14.19 ? 68  PHE A CE2  1 
ATOM   501  C CZ   . PHE A 1 49  ? -11.148 -7.550  19.619  1.00 12.56 ? 68  PHE A CZ   1 
ATOM   502  H H    . PHE A 1 49  ? -8.810  -6.957  25.819  1.00 16.14 ? 68  PHE A H    1 
ATOM   503  H HA   . PHE A 1 49  ? -8.894  -8.883  24.042  1.00 14.97 ? 68  PHE A HA   1 
ATOM   504  H HB2  . PHE A 1 49  ? -10.567 -7.252  24.240  1.00 15.99 ? 68  PHE A HB2  1 
ATOM   505  H HB3  . PHE A 1 49  ? -9.542  -6.141  23.751  1.00 15.99 ? 68  PHE A HB3  1 
ATOM   506  H HD1  . PHE A 1 49  ? -8.879  -6.084  21.379  1.00 15.33 ? 68  PHE A HD1  1 
ATOM   507  H HD2  . PHE A 1 49  ? -11.822 -8.478  22.638  1.00 15.86 ? 68  PHE A HD2  1 
ATOM   508  H HE1  . PHE A 1 49  ? -9.604  -6.315  19.201  1.00 16.28 ? 68  PHE A HE1  1 
ATOM   509  H HE2  . PHE A 1 49  ? -12.533 -8.740  20.454  1.00 17.04 ? 68  PHE A HE2  1 
ATOM   510  H HZ   . PHE A 1 49  ? -11.447 -7.646  18.744  1.00 15.08 ? 68  PHE A HZ   1 
ATOM   511  N N    . VAL A 1 50  ? -6.810  -6.562  23.304  1.00 13.05 ? 69  VAL A N    1 
ATOM   512  C CA   . VAL A 1 50  ? -5.675  -6.240  22.448  1.00 14.33 ? 69  VAL A CA   1 
ATOM   513  C C    . VAL A 1 50  ? -4.491  -7.140  22.755  1.00 13.99 ? 69  VAL A C    1 
ATOM   514  O O    . VAL A 1 50  ? -3.850  -7.688  21.844  1.00 14.33 ? 69  VAL A O    1 
ATOM   515  C CB   . VAL A 1 50  ? -5.325  -4.752  22.619  1.00 17.29 ? 69  VAL A CB   1 
ATOM   516  C CG1  . VAL A 1 50  ? -3.995  -4.417  22.103  1.00 20.65 ? 69  VAL A CG1  1 
ATOM   517  C CG2  . VAL A 1 50  ? -6.383  -3.926  21.928  1.00 17.32 ? 69  VAL A CG2  1 
ATOM   518  H H    . VAL A 1 50  ? -7.035  -5.931  23.843  1.00 15.66 ? 69  VAL A H    1 
ATOM   519  H HA   . VAL A 1 50  ? -5.917  -6.403  21.522  1.00 17.20 ? 69  VAL A HA   1 
ATOM   520  H HB   . VAL A 1 50  ? -5.302  -4.548  23.567  1.00 20.76 ? 69  VAL A HB   1 
ATOM   521  H HG11 . VAL A 1 50  ? -3.944  -3.459  21.958  1.00 24.79 ? 69  VAL A HG11 1 
ATOM   522  H HG12 . VAL A 1 50  ? -3.326  -4.689  22.751  1.00 24.79 ? 69  VAL A HG12 1 
ATOM   523  H HG13 . VAL A 1 50  ? -3.854  -4.886  21.266  1.00 24.79 ? 69  VAL A HG13 1 
ATOM   524  H HG21 . VAL A 1 50  ? -6.182  -2.985  22.055  1.00 20.80 ? 69  VAL A HG21 1 
ATOM   525  H HG22 . VAL A 1 50  ? -6.381  -4.139  20.981  1.00 20.80 ? 69  VAL A HG22 1 
ATOM   526  H HG23 . VAL A 1 50  ? -7.248  -4.135  22.313  1.00 20.80 ? 69  VAL A HG23 1 
ATOM   527  N N    . ALA A 1 51  ? -4.161  -7.286  24.044  1.00 13.32 ? 70  ALA A N    1 
ATOM   528  C CA   . ALA A 1 51  ? -2.951  -8.014  24.412  1.00 12.87 ? 70  ALA A CA   1 
ATOM   529  C C    . ALA A 1 51  ? -3.054  -9.502  24.100  1.00 12.87 ? 70  ALA A C    1 
ATOM   530  O O    . ALA A 1 51  ? -2.033  -10.163 23.870  1.00 13.40 ? 70  ALA A O    1 
ATOM   531  C CB   . ALA A 1 51  ? -2.691  -7.834  25.904  1.00 14.55 ? 70  ALA A CB   1 
ATOM   532  H H    . ALA A 1 51  ? -4.613  -6.978  24.708  1.00 15.99 ? 70  ALA A H    1 
ATOM   533  H HA   . ALA A 1 51  ? -2.209  -7.651  23.904  1.00 15.45 ? 70  ALA A HA   1 
ATOM   534  H HB1  . ALA A 1 51  ? -1.916  -8.361  26.155  1.00 17.47 ? 70  ALA A HB1  1 
ATOM   535  H HB2  . ALA A 1 51  ? -2.526  -6.896  26.085  1.00 17.47 ? 70  ALA A HB2  1 
ATOM   536  H HB3  . ALA A 1 51  ? -3.470  -8.135  26.399  1.00 17.47 ? 70  ALA A HB3  1 
ATOM   537  N N    . THR A 1 52  ? -4.258  -10.041 24.103  1.00 13.34 ? 71  THR A N    1 
ATOM   538  C CA   . THR A 1 52  ? -4.455  -11.460 23.873  1.00 14.26 ? 71  THR A CA   1 
ATOM   539  C C    . THR A 1 52  ? -4.472  -11.798 22.394  1.00 14.09 ? 71  THR A C    1 
ATOM   540  O O    . THR A 1 52  ? -4.179  -12.936 22.036  1.00 17.03 ? 71  THR A O    1 
ATOM   541  C CB   . THR A 1 52  ? -5.802  -11.872 24.498  1.00 16.13 ? 71  THR A CB   1 
ATOM   542  O OG1  . THR A 1 52  ? -5.780  -11.570 25.899  1.00 17.15 ? 71  THR A OG1  1 
ATOM   543  C CG2  . THR A 1 52  ? -6.078  -13.331 24.295  1.00 18.39 ? 71  THR A CG2  1 
ATOM   544  H H    . THR A 1 52  ? -4.986  -9.603  24.238  1.00 16.01 ? 71  THR A H    1 
ATOM   545  H HA   . THR A 1 52  ? -3.740  -11.966 24.290  1.00 17.11 ? 71  THR A HA   1 
ATOM   546  H HB   . THR A 1 52  ? -6.520  -11.381 24.069  1.00 19.36 ? 71  THR A HB   1 
ATOM   547  H HG1  . THR A 1 52  ? -6.557  -11.609 26.214  1.00 20.59 ? 71  THR A HG1  1 
ATOM   548  H HG21 . THR A 1 52  ? -6.835  -13.604 24.837  1.00 22.08 ? 71  THR A HG21 1 
ATOM   549  H HG22 . THR A 1 52  ? -6.279  -13.504 23.362  1.00 22.08 ? 71  THR A HG22 1 
ATOM   550  H HG23 . THR A 1 52  ? -5.302  -13.854 24.552  1.00 22.08 ? 71  THR A HG23 1 
ATOM   551  N N    . ARG A 1 53  ? -4.842  -10.849 21.537  1.00 12.98 ? 72  ARG A N    1 
ATOM   552  C CA   . ARG A 1 53  ? -5.119  -11.127 20.133  1.00 13.02 ? 72  ARG A CA   1 
ATOM   553  C C    . ARG A 1 53  ? -4.024  -10.643 19.195  1.00 13.01 ? 72  ARG A C    1 
ATOM   554  O O    . ARG A 1 53  ? -4.121  -10.879 17.985  1.00 13.77 ? 72  ARG A O    1 
ATOM   555  C CB   . ARG A 1 53  ? -6.489  -10.556 19.751  1.00 13.53 ? 72  ARG A CB   1 
ATOM   556  C CG   . ARG A 1 53  ? -7.603  -11.227 20.534  1.00 13.97 ? 72  ARG A CG   1 
ATOM   557  C CD   . ARG A 1 53  ? -8.987  -10.735 20.159  1.00 14.31 ? 72  ARG A CD   1 
ATOM   558  N NE   . ARG A 1 53  ? -9.938  -11.206 21.162  1.00 14.36 ? 72  ARG A NE   1 
ATOM   559  C CZ   . ARG A 1 53  ? -11.197 -11.539 20.932  1.00 14.79 ? 72  ARG A CZ   1 
ATOM   560  N NH1  . ARG A 1 53  ? -11.709 -11.512 19.716  1.00 15.88 ? 72  ARG A NH1  1 
ATOM   561  N NH2  . ARG A 1 53  ? -11.958 -11.918 21.954  1.00 16.04 ? 72  ARG A NH2  1 
ATOM   562  H H    . ARG A 1 53  ? -4.942  -10.022 21.750  1.00 15.58 ? 72  ARG A H    1 
ATOM   563  H HA   . ARG A 1 53  ? -5.171  -12.087 20.001  1.00 15.63 ? 72  ARG A HA   1 
ATOM   564  H HB2  . ARG A 1 53  ? -6.506  -9.606  19.946  1.00 16.24 ? 72  ARG A HB2  1 
ATOM   565  H HB3  . ARG A 1 53  ? -6.646  -10.705 18.806  1.00 16.24 ? 72  ARG A HB3  1 
ATOM   566  H HG2  . ARG A 1 53  ? -7.573  -12.182 20.367  1.00 16.77 ? 72  ARG A HG2  1 
ATOM   567  H HG3  . ARG A 1 53  ? -7.472  -11.051 21.479  1.00 16.77 ? 72  ARG A HG3  1 
ATOM   568  H HD2  . ARG A 1 53  ? -9.000  -9.765  20.141  1.00 17.17 ? 72  ARG A HD2  1 
ATOM   569  H HD3  . ARG A 1 53  ? -9.240  -11.087 19.292  1.00 17.17 ? 72  ARG A HD3  1 
ATOM   570  H HE   . ARG A 1 53  ? -9.655  -11.272 21.972  1.00 17.24 ? 72  ARG A HE   1 
ATOM   571  H HH11 . ARG A 1 53  ? -11.221 -11.273 19.050  1.00 19.06 ? 72  ARG A HH11 1 
ATOM   572  H HH12 . ARG A 1 53  ? -12.530 -11.733 19.590  1.00 19.06 ? 72  ARG A HH12 1 
ATOM   573  H HH21 . ARG A 1 53  ? -11.630 -11.943 22.749  1.00 19.25 ? 72  ARG A HH21 1 
ATOM   574  H HH22 . ARG A 1 53  ? -12.779 -12.138 21.821  1.00 19.25 ? 72  ARG A HH22 1 
ATOM   575  N N    . SER A 1 54  ? -2.969  -10.024 19.717  1.00 11.26 ? 73  SER A N    1 
ATOM   576  C CA   . SER A 1 54  ? -1.870  -9.568  18.871  1.00 11.38 ? 73  SER A CA   1 
ATOM   577  C C    . SER A 1 54  ? -0.619  -9.442  19.704  1.00 11.61 ? 73  SER A C    1 
ATOM   578  O O    . SER A 1 54  ? -0.697  -9.239  20.912  1.00 12.82 ? 73  SER A O    1 
ATOM   579  C CB   . SER A 1 54  ? -2.211  -8.228  18.229  1.00 11.91 ? 73  SER A CB   1 
ATOM   580  O OG   . SER A 1 54  ? -1.163  -7.733  17.418  1.00 12.52 ? 73  SER A OG   1 
ATOM   581  H H    . SER A 1 54  ? -2.865  -9.858  20.554  1.00 13.52 ? 73  SER A H    1 
ATOM   582  H HA   . SER A 1 54  ? -1.702  -10.224 18.177  1.00 13.67 ? 73  SER A HA   1 
ATOM   583  H HB2  . SER A 1 54  ? -3.002  -8.341  17.678  1.00 14.30 ? 73  SER A HB2  1 
ATOM   584  H HB3  . SER A 1 54  ? -2.387  -7.584  18.933  1.00 14.30 ? 73  SER A HB3  1 
ATOM   585  H HG   . SER A 1 54  ? -1.321  -6.938  17.198  1.00 15.03 ? 73  SER A HG   1 
ATOM   586  N N    . ASN A 1 55  ? 0.532   -9.525  19.028  1.00 11.53 ? 74  ASN A N    1 
ATOM   587  C CA   . ASN A 1 55  ? 1.805   -9.158  19.631  1.00 10.85 ? 74  ASN A CA   1 
ATOM   588  C C    . ASN A 1 55  ? 2.355   -7.828  19.115  1.00 11.17 ? 74  ASN A C    1 
ATOM   589  O O    . ASN A 1 55  ? 3.542   -7.557  19.314  1.00 11.92 ? 74  ASN A O    1 
ATOM   590  C CB   . ASN A 1 55  ? 2.851   -10.250 19.378  1.00 10.85 ? 74  ASN A CB   1 
ATOM   591  C CG   . ASN A 1 55  ? 2.569   -11.524 20.109  1.00 11.81 ? 74  ASN A CG   1 
ATOM   592  O OD1  . ASN A 1 55  ? 1.971   -11.517 21.184  1.00 14.11 ? 74  ASN A OD1  1 
ATOM   593  N ND2  . ASN A 1 55  ? 3.015   -12.637 19.539  1.00 13.61 ? 74  ASN A ND2  1 
ATOM   594  H H    . ASN A 1 55  ? 0.595   -9.794  18.214  1.00 13.85 ? 74  ASN A H    1 
ATOM   595  H HA   . ASN A 1 55  ? 1.652   -9.073  20.585  1.00 13.03 ? 74  ASN A HA   1 
ATOM   596  H HB2  . ASN A 1 55  ? 2.872   -10.450 18.429  1.00 13.03 ? 74  ASN A HB2  1 
ATOM   597  H HB3  . ASN A 1 55  ? 3.718   -9.926  19.668  1.00 13.03 ? 74  ASN A HB3  1 
ATOM   598  H HD21 . ASN A 1 55  ? 3.439   -12.598 18.791  1.00 16.34 ? 74  ASN A HD21 1 
ATOM   599  H HD22 . ASN A 1 55  ? 2.880   -13.398 19.917  1.00 16.34 ? 74  ASN A HD22 1 
ATOM   600  N N    . PHE A 1 56  ? 1.543   -6.980  18.481  1.00 10.81 ? 75  PHE A N    1 
ATOM   601  C CA   . PHE A 1 56  ? 2.108   -5.821  17.767  1.00 9.70  ? 75  PHE A CA   1 
ATOM   602  C C    . PHE A 1 56  ? 1.088   -4.690  17.727  1.00 10.12 ? 75  PHE A C    1 
ATOM   603  O O    . PHE A 1 56  ? 0.074   -4.806  17.024  1.00 11.17 ? 75  PHE A O    1 
ATOM   604  C CB   . PHE A 1 56  ? 2.470   -6.269  16.351  1.00 10.88 ? 75  PHE A CB   1 
ATOM   605  C CG   . PHE A 1 56  ? 3.416   -5.367  15.578  1.00 10.74 ? 75  PHE A CG   1 
ATOM   606  C CD1  . PHE A 1 56  ? 4.243   -4.422  16.173  1.00 11.37 ? 75  PHE A CD1  1 
ATOM   607  C CD2  . PHE A 1 56  ? 3.519   -5.562  14.209  1.00 11.57 ? 75  PHE A CD2  1 
ATOM   608  C CE1  . PHE A 1 56  ? 5.114   -3.679  15.403  1.00 11.86 ? 75  PHE A CE1  1 
ATOM   609  C CE2  . PHE A 1 56  ? 4.395   -4.846  13.447  1.00 12.01 ? 75  PHE A CE2  1 
ATOM   610  C CZ   . PHE A 1 56  ? 5.204   -3.896  14.053  1.00 12.16 ? 75  PHE A CZ   1 
ATOM   611  H H    . PHE A 1 56  ? 0.686   -7.047  18.448  1.00 12.97 ? 75  PHE A H    1 
ATOM   612  H HA   . PHE A 1 56  ? 2.881   -5.479  18.243  1.00 11.65 ? 75  PHE A HA   1 
ATOM   613  H HB2  . PHE A 1 56  ? 2.891   -7.141  16.409  1.00 13.06 ? 75  PHE A HB2  1 
ATOM   614  H HB3  . PHE A 1 56  ? 1.650   -6.330  15.836  1.00 13.06 ? 75  PHE A HB3  1 
ATOM   615  H HD1  . PHE A 1 56  ? 4.209   -4.290  17.093  1.00 13.65 ? 75  PHE A HD1  1 
ATOM   616  H HD2  . PHE A 1 56  ? 2.976   -6.196  13.799  1.00 13.89 ? 75  PHE A HD2  1 
ATOM   617  H HE1  . PHE A 1 56  ? 5.643   -3.026  15.803  1.00 14.24 ? 75  PHE A HE1  1 
ATOM   618  H HE2  . PHE A 1 56  ? 4.449   -4.994  12.530  1.00 14.42 ? 75  PHE A HE2  1 
ATOM   619  H HZ   . PHE A 1 56  ? 5.808   -3.406  13.543  1.00 14.60 ? 75  PHE A HZ   1 
ATOM   620  N N    . ILE A 1 57  ? 1.352   -3.592  18.445  1.00 10.33 ? 76  ILE A N    1 
ATOM   621  C CA   . ILE A 1 57  ? 0.437   -2.446  18.466  1.00 9.90  ? 76  ILE A CA   1 
ATOM   622  C C    . ILE A 1 57  ? 1.241   -1.157  18.400  1.00 10.04 ? 76  ILE A C    1 
ATOM   623  O O    . ILE A 1 57  ? 2.249   -1.004  19.098  1.00 11.03 ? 76  ILE A O    1 
ATOM   624  C CB   . ILE A 1 57  ? -0.460  -2.421  19.726  1.00 10.20 ? 76  ILE A CB   1 
ATOM   625  C CG1  . ILE A 1 57  ? -1.405  -1.230  19.691  1.00 10.72 ? 76  ILE A CG1  1 
ATOM   626  C CG2  . ILE A 1 57  ? 0.362   -2.447  21.027  1.00 10.51 ? 76  ILE A CG2  1 
ATOM   627  C CD1  . ILE A 1 57  ? -2.570  -1.329  20.634  1.00 11.56 ? 76  ILE A CD1  1 
ATOM   628  H H    . ILE A 1 57  ? 2.055   -3.488  18.928  1.00 12.40 ? 76  ILE A H    1 
ATOM   629  H HA   . ILE A 1 57  ? -0.128  -2.507  17.680  1.00 11.89 ? 76  ILE A HA   1 
ATOM   630  H HB   . ILE A 1 57  ? -0.992  -3.232  19.714  1.00 12.24 ? 76  ILE A HB   1 
ATOM   631  H HG12 . ILE A 1 57  ? -0.906  -0.432  19.926  1.00 12.87 ? 76  ILE A HG12 1 
ATOM   632  H HG13 . ILE A 1 57  ? -1.763  -1.145  18.793  1.00 12.87 ? 76  ILE A HG13 1 
ATOM   633  H HG21 . ILE A 1 57  ? -0.234  -2.615  21.773  1.00 12.62 ? 76  ILE A HG21 1 
ATOM   634  H HG22 . ILE A 1 57  ? 1.025   -3.152  20.968  1.00 12.62 ? 76  ILE A HG22 1 
ATOM   635  H HG23 . ILE A 1 57  ? 0.800   -1.589  21.140  1.00 12.62 ? 76  ILE A HG23 1 
ATOM   636  H HD11 . ILE A 1 57  ? -3.130  -0.545  20.527  1.00 13.88 ? 76  ILE A HD11 1 
ATOM   637  H HD12 . ILE A 1 57  ? -3.077  -2.129  20.427  1.00 13.88 ? 76  ILE A HD12 1 
ATOM   638  H HD13 . ILE A 1 57  ? -2.236  -1.375  21.544  1.00 13.88 ? 76  ILE A HD13 1 
ATOM   639  N N    A CYS A 1 58  ? 0.775   -0.215  17.581  0.70 10.67 ? 77  CYS A N    1 
ATOM   640  N N    B CYS A 1 58  ? 0.815   -0.237  17.541  0.30 9.87  ? 77  CYS A N    1 
ATOM   641  C CA   A CYS A 1 58  ? 1.273   1.160   17.585  0.70 10.77 ? 77  CYS A CA   1 
ATOM   642  C CA   B CYS A 1 58  ? 1.264   1.146   17.612  0.30 9.45  ? 77  CYS A CA   1 
ATOM   643  C C    A CYS A 1 58  ? 0.206   2.045   18.215  0.70 11.18 ? 77  CYS A C    1 
ATOM   644  C C    B CYS A 1 58  ? 0.179   1.949   18.313  0.30 10.45 ? 77  CYS A C    1 
ATOM   645  O O    A CYS A 1 58  ? -0.950  2.024   17.779  0.70 11.21 ? 77  CYS A O    1 
ATOM   646  O O    B CYS A 1 58  ? -1.010  1.793   18.011  0.30 10.08 ? 77  CYS A O    1 
ATOM   647  C CB   A CYS A 1 58  ? 1.598   1.618   16.165  0.70 12.07 ? 77  CYS A CB   1 
ATOM   648  C CB   B CYS A 1 58  ? 1.535   1.750   16.237  0.30 9.14  ? 77  CYS A CB   1 
ATOM   649  S SG   A CYS A 1 58  ? 2.798   0.582   15.280  0.70 15.28 ? 77  CYS A SG   1 
ATOM   650  S SG   B CYS A 1 58  ? 1.911   3.554   16.317  0.30 9.46  ? 77  CYS A SG   1 
ATOM   651  H H    A CYS A 1 58  ? 0.156   -0.351  17.001  0.70 12.81 ? 77  CYS A H    1 
ATOM   652  H H    B CYS A 1 58  ? 0.260   -0.393  16.903  0.30 11.86 ? 77  CYS A H    1 
ATOM   653  H HA   A CYS A 1 58  ? 2.082   1.226   18.116  0.70 12.93 ? 77  CYS A HA   1 
ATOM   654  H HA   B CYS A 1 58  ? 2.097   1.186   18.107  0.30 11.35 ? 77  CYS A HA   1 
ATOM   655  H HB2  A CYS A 1 58  ? 0.777   1.619   15.647  0.70 14.49 ? 77  CYS A HB2  1 
ATOM   656  H HB2  B CYS A 1 58  ? 2.298   1.301   15.839  0.30 10.98 ? 77  CYS A HB2  1 
ATOM   657  H HB3  A CYS A 1 58  ? 1.964   2.515   16.208  0.70 14.49 ? 77  CYS A HB3  1 
ATOM   658  H HB3  B CYS A 1 58  ? 0.751   1.630   15.678  0.30 10.98 ? 77  CYS A HB3  1 
ATOM   659  H HG   B CYS A 1 58  ? 0.964   4.130   16.777  0.30 11.36 ? 77  CYS A HG   1 
ATOM   660  N N    . LEU A 1 59  ? 0.584   2.784   19.257  1.00 11.65 ? 78  LEU A N    1 
ATOM   661  C CA   . LEU A 1 59  ? -0.337  3.680   19.949  1.00 11.17 ? 78  LEU A CA   1 
ATOM   662  C C    . LEU A 1 59  ? -0.203  5.087   19.379  1.00 10.81 ? 78  LEU A C    1 
ATOM   663  O O    . LEU A 1 59  ? 0.909   5.621   19.268  1.00 11.72 ? 78  LEU A O    1 
ATOM   664  C CB   . LEU A 1 59  ? -0.084  3.670   21.460  1.00 11.53 ? 78  LEU A CB   1 
ATOM   665  C CG   . LEU A 1 59  ? -0.489  2.352   22.130  1.00 12.02 ? 78  LEU A CG   1 
ATOM   666  C CD1  . LEU A 1 59  ? 0.126   2.270   23.508  1.00 11.83 ? 78  LEU A CD1  1 
ATOM   667  C CD2  . LEU A 1 59  ? -1.989  2.177   22.199  1.00 12.27 ? 78  LEU A CD2  1 
ATOM   668  H HA   . LEU A 1 59  ? -1.250  3.384   19.805  1.00 13.41 ? 78  LEU A HA   1 
ATOM   669  H HB2  . LEU A 1 59  ? 0.863   3.808   21.620  1.00 13.84 ? 78  LEU A HB2  1 
ATOM   670  H HB3  . LEU A 1 59  ? -0.598  4.384   21.869  1.00 13.84 ? 78  LEU A HB3  1 
ATOM   671  H HG   . LEU A 1 59  ? -0.155  1.620   21.590  1.00 14.43 ? 78  LEU A HG   1 
ATOM   672  H HD11 . LEU A 1 59  ? -0.073  1.402   23.892  1.00 14.21 ? 78  LEU A HD11 1 
ATOM   673  H HD12 . LEU A 1 59  ? 1.087   2.385   23.433  1.00 14.21 ? 78  LEU A HD12 1 
ATOM   674  H HD13 . LEU A 1 59  ? -0.248  2.972   24.064  1.00 14.21 ? 78  LEU A HD13 1 
ATOM   675  H HD21 . LEU A 1 59  ? -2.189  1.334   22.635  1.00 14.73 ? 78  LEU A HD21 1 
ATOM   676  H HD22 . LEU A 1 59  ? -2.369  2.911   22.707  1.00 14.73 ? 78  LEU A HD22 1 
ATOM   677  H HD23 . LEU A 1 59  ? -2.348  2.178   21.298  1.00 14.73 ? 78  LEU A HD23 1 
ATOM   678  N N    . GLU A 1 60  ? -1.340  5.681   19.034  1.00 10.85 ? 79  GLU A N    1 
ATOM   679  C CA   . GLU A 1 60  ? -1.386  6.929   18.280  1.00 10.66 ? 79  GLU A CA   1 
ATOM   680  C C    . GLU A 1 60  ? -1.204  8.175   19.160  1.00 11.37 ? 79  GLU A C    1 
ATOM   681  O O    . GLU A 1 60  ? -1.311  8.147   20.396  1.00 12.05 ? 79  GLU A O    1 
ATOM   682  C CB   . GLU A 1 60  ? -2.732  7.075   17.562  1.00 11.38 ? 79  GLU A CB   1 
ATOM   683  C CG   . GLU A 1 60  ? -2.688  6.604   16.134  1.00 13.81 ? 79  GLU A CG   1 
ATOM   684  C CD   . GLU A 1 60  ? -2.013  7.603   15.203  1.00 15.67 ? 79  GLU A CD   1 
ATOM   685  O OE1  . GLU A 1 60  ? -1.738  8.760   15.620  1.00 15.72 ? 79  GLU A OE1  1 
ATOM   686  O OE2  . GLU A 1 60  ? -1.736  7.244   14.061  1.00 18.15 ? 79  GLU A OE2  1 
ATOM   687  H H    . GLU A 1 60  ? -2.119  5.373   19.229  1.00 13.02 ? 79  GLU A H    1 
ATOM   688  H HA   . GLU A 1 60  ? -0.655  6.896   17.644  1.00 12.80 ? 79  GLU A HA   1 
ATOM   689  H HB2  . GLU A 1 60  ? -3.398  6.547   18.031  1.00 13.67 ? 79  GLU A HB2  1 
ATOM   690  H HB3  . GLU A 1 60  ? -2.990  8.010   17.562  1.00 13.67 ? 79  GLU A HB3  1 
ATOM   691  H HG2  . GLU A 1 60  ? -2.193  5.772   16.091  1.00 16.58 ? 79  GLU A HG2  1 
ATOM   692  H HG3  . GLU A 1 60  ? -3.595  6.467   15.818  1.00 16.58 ? 79  GLU A HG3  1 
ATOM   693  N N    . LYS A 1 61  ? -0.906  9.279   18.482  1.00 11.56 ? 80  LYS A N    1 
ATOM   694  C CA   . LYS A 1 61  ? -0.955  10.590  19.111  1.00 11.99 ? 80  LYS A CA   1 
ATOM   695  C C    . LYS A 1 61  ? -2.255  10.746  19.885  1.00 12.72 ? 80  LYS A C    1 
ATOM   696  O O    . LYS A 1 61  ? -3.323  10.295  19.448  1.00 12.90 ? 80  LYS A O    1 
ATOM   697  C CB   . LYS A 1 61  ? -0.845  11.686  18.054  1.00 14.32 ? 80  LYS A CB   1 
ATOM   698  C CG   . LYS A 1 61  ? -2.048  11.793  17.113  1.00 16.85 ? 80  LYS A CG   1 
ATOM   699  C CD   . LYS A 1 61  ? -1.850  12.852  16.027  1.00 18.26 ? 80  LYS A CD   1 
ATOM   700  C CE   . LYS A 1 61  ? -1.208  12.293  14.774  1.00 20.50 ? 80  LYS A CE   1 
ATOM   701  N NZ   . LYS A 1 61  ? -1.823  11.100  14.127  1.00 22.30 ? 80  LYS A NZ   1 
ATOM   702  H H    . LYS A 1 61  ? -0.672  9.294   17.655  1.00 13.88 ? 80  LYS A H    1 
ATOM   703  H HA   . LYS A 1 61  ? -0.209  10.685  19.724  1.00 14.39 ? 80  LYS A HA   1 
ATOM   704  H HB2  . LYS A 1 61  ? -0.750  12.540  18.505  1.00 17.19 ? 80  LYS A HB2  1 
ATOM   705  H HB3  . LYS A 1 61  ? -0.062  11.510  17.508  1.00 17.19 ? 80  LYS A HB3  1 
ATOM   706  H HG2  . LYS A 1 61  ? -2.186  10.937  16.677  1.00 20.23 ? 80  LYS A HG2  1 
ATOM   707  H HG3  . LYS A 1 61  ? -2.834  12.033  17.629  1.00 20.23 ? 80  LYS A HG3  1 
ATOM   708  H HD2  . LYS A 1 61  ? -2.714  13.220  15.783  1.00 21.92 ? 80  LYS A HD2  1 
ATOM   709  H HD3  . LYS A 1 61  ? -1.275  13.554  16.371  1.00 21.92 ? 80  LYS A HD3  1 
ATOM   710  H HE2  . LYS A 1 61  ? -1.207  12.996  14.106  1.00 24.61 ? 80  LYS A HE2  1 
ATOM   711  H HE3  . LYS A 1 61  ? -0.297  12.045  14.997  1.00 24.61 ? 80  LYS A HE3  1 
ATOM   712  H HZ1  . LYS A 1 61  ? -1.774  10.399  14.673  1.00 26.77 ? 80  LYS A HZ1  1 
ATOM   713  H HZ2  . LYS A 1 61  ? -1.394  10.909  13.371  1.00 26.77 ? 80  LYS A HZ2  1 
ATOM   714  H HZ3  . LYS A 1 61  ? -2.678  11.262  13.940  1.00 26.77 ? 80  LYS A HZ3  1 
ATOM   715  N N    . GLY A 1 62  ? -2.159  11.381  21.049  1.00 12.16 ? 81  GLY A N    1 
ATOM   716  C CA   . GLY A 1 62  ? -3.312  11.638  21.872  1.00 12.03 ? 81  GLY A CA   1 
ATOM   717  C C    . GLY A 1 62  ? -3.698  10.551  22.841  1.00 11.74 ? 81  GLY A C    1 
ATOM   718  O O    . GLY A 1 62  ? -4.589  10.779  23.674  1.00 12.84 ? 81  GLY A O    1 
ATOM   719  H H    . GLY A 1 62  ? -1.421  11.674  21.380  1.00 14.60 ? 81  GLY A H    1 
ATOM   720  H HA2  . GLY A 1 62  ? -3.144  12.440  22.390  1.00 14.44 ? 81  GLY A HA2  1 
ATOM   721  H HA3  . GLY A 1 62  ? -4.073  11.790  21.291  1.00 14.44 ? 81  GLY A HA3  1 
ATOM   722  N N    . HIS A 1 63  ? -3.069  9.385   22.772  1.00 12.28 ? 82  HIS A N    1 
ATOM   723  C CA   . HIS A 1 63  ? -3.541  8.267   23.571  1.00 11.52 ? 82  HIS A CA   1 
ATOM   724  C C    . HIS A 1 63  ? -3.543  8.592   25.064  1.00 11.76 ? 82  HIS A C    1 
ATOM   725  O O    . HIS A 1 63  ? -2.520  8.982   25.636  1.00 12.30 ? 82  HIS A O    1 
ATOM   726  C CB   . HIS A 1 63  ? -2.682  7.041   23.333  1.00 11.52 ? 82  HIS A CB   1 
ATOM   727  C CG   . HIS A 1 63  ? -3.235  5.831   24.006  1.00 10.99 ? 82  HIS A CG   1 
ATOM   728  N ND1  . HIS A 1 63  ? -4.383  5.206   23.571  1.00 11.52 ? 82  HIS A ND1  1 
ATOM   729  C CD2  . HIS A 1 63  ? -2.862  5.189   25.141  1.00 10.99 ? 82  HIS A CD2  1 
ATOM   730  C CE1  . HIS A 1 63  ? -4.675  4.216   24.393  1.00 11.91 ? 82  HIS A CE1  1 
ATOM   731  N NE2  . HIS A 1 63  ? -3.766  4.183   25.354  1.00 11.04 ? 82  HIS A NE2  1 
ATOM   732  H H    . HIS A 1 63  ? -2.382  9.220   22.281  1.00 14.74 ? 82  HIS A H    1 
ATOM   733  H HA   . HIS A 1 63  ? -4.453  8.081   23.296  1.00 13.83 ? 82  HIS A HA   1 
ATOM   734  H HB2  . HIS A 1 63  ? -2.636  6.864   22.380  1.00 13.83 ? 82  HIS A HB2  1 
ATOM   735  H HB3  . HIS A 1 63  ? -1.792  7.203   23.684  1.00 13.83 ? 82  HIS A HB3  1 
ATOM   736  H HD2  . HIS A 1 63  ? -2.129  5.394   25.676  1.00 13.20 ? 82  HIS A HD2  1 
ATOM   737  H HE1  . HIS A 1 63  ? -5.399  3.639   24.310  1.00 14.30 ? 82  HIS A HE1  1 
ATOM   738  H HE2  . HIS A 1 63  ? -3.746  3.621   26.005  1.00 13.26 ? 82  HIS A HE2  1 
ATOM   739  N N    . ALA A 1 64  ? -4.710  8.428   25.681  1.00 12.52 ? 83  ALA A N    1 
ATOM   740  C CA   . ALA A 1 64  ? -4.958  8.621   27.109  1.00 12.04 ? 83  ALA A CA   1 
ATOM   741  C C    . ALA A 1 64  ? -4.655  10.042  27.577  1.00 13.29 ? 83  ALA A C    1 
ATOM   742  O O    . ALA A 1 64  ? -4.517  10.282  28.784  1.00 14.68 ? 83  ALA A O    1 
ATOM   743  C CB   . ALA A 1 64  ? -4.201  7.590   27.963  1.00 12.81 ? 83  ALA A CB   1 
ATOM   744  H H    . ALA A 1 64  ? -5.424  8.189   25.265  1.00 15.02 ? 83  ALA A H    1 
ATOM   745  H HA   . ALA A 1 64  ? -5.905  8.479   27.261  1.00 14.45 ? 83  ALA A HA   1 
ATOM   746  H HB1  . ALA A 1 64  ? -4.436  7.719   28.895  1.00 15.38 ? 83  ALA A HB1  1 
ATOM   747  H HB2  . ALA A 1 64  ? -4.453  6.698   27.679  1.00 15.38 ? 83  ALA A HB2  1 
ATOM   748  H HB3  . ALA A 1 64  ? -3.247  7.719   27.842  1.00 15.38 ? 83  ALA A HB3  1 
ATOM   749  N N    . THR A 1 65  ? -4.600  11.011  26.664  1.00 13.08 ? 84  THR A N    1 
ATOM   750  C CA   . THR A 1 65  ? -4.272  12.372  27.097  1.00 13.00 ? 84  THR A CA   1 
ATOM   751  C C    . THR A 1 65  ? -5.335  12.988  28.008  1.00 14.22 ? 84  THR A C    1 
ATOM   752  O O    . THR A 1 65  ? -5.007  13.867  28.805  1.00 15.19 ? 84  THR A O    1 
ATOM   753  C CB   . THR A 1 65  ? -4.031  13.317  25.916  1.00 14.08 ? 84  THR A CB   1 
ATOM   754  O OG1  . THR A 1 65  ? -5.095  13.171  24.963  1.00 14.30 ? 84  THR A OG1  1 
ATOM   755  C CG2  . THR A 1 65  ? -2.699  13.029  25.266  1.00 13.82 ? 84  THR A CG2  1 
ATOM   756  H H    . THR A 1 65  ? -4.742  10.913  25.821  1.00 15.70 ? 84  THR A H    1 
ATOM   757  H HA   . THR A 1 65  ? -3.443  12.291  27.594  1.00 15.61 ? 84  THR A HA   1 
ATOM   758  H HB   . THR A 1 65  ? -4.012  14.236  26.227  1.00 16.90 ? 84  THR A HB   1 
ATOM   759  H HG1  . THR A 1 65  ? -4.955  13.664  24.298  1.00 17.16 ? 84  THR A HG1  1 
ATOM   760  H HG21 . THR A 1 65  ? -2.635  13.497  24.419  1.00 16.60 ? 84  THR A HG21 1 
ATOM   761  H HG22 . THR A 1 65  ? -1.978  13.325  25.844  1.00 16.60 ? 84  THR A HG22 1 
ATOM   762  H HG23 . THR A 1 65  ? -2.606  12.077  25.108  1.00 16.60 ? 84  THR A HG23 1 
ATOM   763  N N    . ARG A 1 66  ? -6.602  12.570  27.906  1.00 15.22 ? 85  ARG A N    1 
ATOM   764  C CA   . ARG A 1 66  ? -7.624  13.201  28.739  1.00 16.41 ? 85  ARG A CA   1 
ATOM   765  C C    . ARG A 1 66  ? -7.303  13.007  30.214  1.00 16.49 ? 85  ARG A C    1 
ATOM   766  O O    . ARG A 1 66  ? -7.547  13.901  31.034  1.00 18.73 ? 85  ARG A O    1 
ATOM   767  C CB   . ARG A 1 66  ? -9.009  12.651  28.404  1.00 18.21 ? 85  ARG A CB   1 
ATOM   768  C CG   . ARG A 1 66  ? -10.164 13.420  29.041  1.00 20.61 ? 85  ARG A CG   1 
ATOM   769  C CD   . ARG A 1 66  ? -11.524 12.740  28.769  1.00 22.33 ? 85  ARG A CD   1 
ATOM   770  N NE   . ARG A 1 66  ? -11.738 11.548  29.588  1.00 25.12 ? 85  ARG A NE   1 
ATOM   771  C CZ   . ARG A 1 66  ? -12.473 11.519  30.691  1.00 28.23 ? 85  ARG A CZ   1 
ATOM   772  N NH1  . ARG A 1 66  ? -13.130 12.582  31.106  1.00 29.97 ? 85  ARG A NH1  1 
ATOM   773  N NH2  . ARG A 1 66  ? -12.547 10.394  31.397  1.00 29.00 ? 85  ARG A NH2  1 
ATOM   774  H H    . ARG A 1 66  ? -6.882  11.949  27.383  1.00 18.27 ? 85  ARG A H    1 
ATOM   775  H HA   . ARG A 1 66  ? -7.643  14.152  28.551  1.00 19.70 ? 85  ARG A HA   1 
ATOM   776  H HB2  . ARG A 1 66  ? -9.130  12.684  27.442  1.00 21.86 ? 85  ARG A HB2  1 
ATOM   777  H HB3  . ARG A 1 66  ? -9.061  11.733  28.714  1.00 21.86 ? 85  ARG A HB3  1 
ATOM   778  H HG2  . ARG A 1 66  ? -10.031 13.460  30.001  1.00 24.74 ? 85  ARG A HG2  1 
ATOM   779  H HG3  . ARG A 1 66  ? -10.194 14.316  28.672  1.00 24.74 ? 85  ARG A HG3  1 
ATOM   780  H HD2  . ARG A 1 66  ? -12.236 13.369  28.964  1.00 26.80 ? 85  ARG A HD2  1 
ATOM   781  H HD3  . ARG A 1 66  ? -11.562 12.473  27.837  1.00 26.80 ? 85  ARG A HD3  1 
ATOM   782  H HE   . ARG A 1 66  ? -11.363 10.816  29.338  1.00 30.16 ? 85  ARG A HE   1 
ATOM   783  H HH11 . ARG A 1 66  ? -13.088 13.316  30.659  1.00 35.97 ? 85  ARG A HH11 1 
ATOM   784  H HH12 . ARG A 1 66  ? -13.601 12.544  31.825  1.00 35.97 ? 85  ARG A HH12 1 
ATOM   785  H HH21 . ARG A 1 66  ? -12.121 9.694   31.136  1.00 34.80 ? 85  ARG A HH21 1 
ATOM   786  H HH22 . ARG A 1 66  ? -13.021 10.367  32.114  1.00 34.80 ? 85  ARG A HH22 1 
ATOM   787  N N    . THR A 1 67  ? -6.764  11.837  30.574  1.00 14.54 ? 86  THR A N    1 
ATOM   788  C CA   . THR A 1 67  ? -6.427  11.531  31.960  1.00 14.75 ? 86  THR A CA   1 
ATOM   789  C C    . THR A 1 67  ? -4.949  11.681  32.271  1.00 15.25 ? 86  THR A C    1 
ATOM   790  O O    . THR A 1 67  ? -4.604  11.954  33.424  1.00 17.11 ? 86  THR A O    1 
ATOM   791  C CB   . THR A 1 67  ? -6.847  10.093  32.327  1.00 15.43 ? 86  THR A CB   1 
ATOM   792  O OG1  . THR A 1 67  ? -6.254  9.164   31.417  1.00 15.17 ? 86  THR A OG1  1 
ATOM   793  C CG2  . THR A 1 67  ? -8.348  9.916   32.293  1.00 16.27 ? 86  THR A CG2  1 
ATOM   794  H H    . THR A 1 67  ? -6.583  11.201  30.025  1.00 17.45 ? 86  THR A H    1 
ATOM   795  H HA   . THR A 1 67  ? -6.926  12.142  32.525  1.00 17.71 ? 86  THR A HA   1 
ATOM   796  H HB   . THR A 1 67  ? -6.545  9.914   33.231  1.00 18.52 ? 86  THR A HB   1 
ATOM   797  H HG1  . THR A 1 67  ? -6.455  8.378   31.637  1.00 18.21 ? 86  THR A HG1  1 
ATOM   798  H HG21 . THR A 1 67  ? -8.586  9.040   32.635  1.00 19.53 ? 86  THR A HG21 1 
ATOM   799  H HG22 . THR A 1 67  ? -8.775  10.594  32.839  1.00 19.53 ? 86  THR A HG22 1 
ATOM   800  H HG23 . THR A 1 67  ? -8.671  9.997   31.382  1.00 19.53 ? 86  THR A HG23 1 
ATOM   801  N N    . HIS A 1 68  ? -4.068  11.511  31.282  1.00 14.01 ? 87  HIS A N    1 
ATOM   802  C CA   . HIS A 1 68  ? -2.630  11.499  31.523  1.00 13.98 ? 87  HIS A CA   1 
ATOM   803  C C    . HIS A 1 68  ? -1.900  12.735  31.012  1.00 14.96 ? 87  HIS A C    1 
ATOM   804  O O    . HIS A 1 68  ? -0.689  12.868  31.249  1.00 15.58 ? 87  HIS A O    1 
ATOM   805  C CB   . HIS A 1 68  ? -2.034  10.228  30.919  1.00 13.88 ? 87  HIS A CB   1 
ATOM   806  C CG   . HIS A 1 68  ? -2.338  9.009   31.730  1.00 13.81 ? 87  HIS A CG   1 
ATOM   807  N ND1  . HIS A 1 68  ? -3.627  8.579   31.995  1.00 14.48 ? 87  HIS A ND1  1 
ATOM   808  C CD2  . HIS A 1 68  ? -1.512  8.160   32.387  1.00 14.61 ? 87  HIS A CD2  1 
ATOM   809  C CE1  . HIS A 1 68  ? -3.571  7.514   32.780  1.00 14.79 ? 87  HIS A CE1  1 
ATOM   810  N NE2  . HIS A 1 68  ? -2.301  7.227   33.010  1.00 15.13 ? 87  HIS A NE2  1 
ATOM   811  H H    . HIS A 1 68  ? -4.284  11.400  30.457  1.00 16.82 ? 87  HIS A H    1 
ATOM   812  H HA   . HIS A 1 68  ? -2.465  11.478  32.478  1.00 16.78 ? 87  HIS A HA   1 
ATOM   813  H HB2  . HIS A 1 68  ? -2.400  10.098  30.030  1.00 16.66 ? 87  HIS A HB2  1 
ATOM   814  H HB3  . HIS A 1 68  ? -1.070  10.324  30.869  1.00 16.66 ? 87  HIS A HB3  1 
ATOM   815  H HD2  . HIS A 1 68  ? -0.583  8.202   32.412  1.00 17.54 ? 87  HIS A HD2  1 
ATOM   816  H HE1  . HIS A 1 68  ? -4.303  7.047   33.114  1.00 17.76 ? 87  HIS A HE1  1 
ATOM   817  H HE2  . HIS A 1 68  ? -2.016  6.562   33.475  1.00 18.16 ? 87  HIS A HE2  1 
ATOM   818  N N    . GLY A 1 69  ? -2.596  13.645  30.348  1.00 15.02 ? 88  GLY A N    1 
ATOM   819  C CA   . GLY A 1 69  ? -2.034  14.935  30.019  1.00 15.12 ? 88  GLY A CA   1 
ATOM   820  C C    . GLY A 1 69  ? -1.296  14.948  28.701  1.00 16.09 ? 88  GLY A C    1 
ATOM   821  O O    . GLY A 1 69  ? -1.674  15.685  27.776  1.00 19.81 ? 88  GLY A O    1 
ATOM   822  H H    . GLY A 1 69  ? -3.404  13.535  30.075  1.00 18.03 ? 88  GLY A H    1 
ATOM   823  H HA2  . GLY A 1 69  ? -2.748  15.589  29.971  1.00 18.15 ? 88  GLY A HA2  1 
ATOM   824  H HA3  . GLY A 1 69  ? -1.412  15.196  30.715  1.00 18.15 ? 88  GLY A HA3  1 
ATOM   825  N N    . THR A 1 70  ? -0.243  14.137  28.592  1.00 13.84 ? 89  THR A N    1 
ATOM   826  C CA   . THR A 1 70  ? 0.629   14.116  27.417  1.00 12.92 ? 89  THR A CA   1 
ATOM   827  C C    . THR A 1 70  ? 0.534   12.741  26.774  1.00 12.39 ? 89  THR A C    1 
ATOM   828  O O    . THR A 1 70  ? 0.276   11.742  27.455  1.00 12.81 ? 89  THR A O    1 
ATOM   829  C CB   . THR A 1 70  ? 2.091   14.388  27.797  1.00 15.07 ? 89  THR A CB   1 
ATOM   830  O OG1  . THR A 1 70  ? 2.528   13.310  28.631  1.00 15.28 ? 89  THR A OG1  1 
ATOM   831  C CG2  . THR A 1 70  ? 2.234   15.718  28.513  1.00 15.94 ? 89  THR A CG2  1 
ATOM   832  H H    . THR A 1 70  ? -0.008  13.577  29.200  1.00 16.61 ? 89  THR A H    1 
ATOM   833  H HA   . THR A 1 70  ? 0.349   14.796  26.785  1.00 15.50 ? 89  THR A HA   1 
ATOM   834  H HB   . THR A 1 70  ? 2.650   14.445  27.006  1.00 18.10 ? 89  THR A HB   1 
ATOM   835  H HG1  . THR A 1 70  ? 3.334   13.418  28.841  1.00 18.34 ? 89  THR A HG1  1 
ATOM   836  H HG21 . THR A 1 70  ? 2.003   16.445  27.913  1.00 19.13 ? 89  THR A HG21 1 
ATOM   837  H HG22 . THR A 1 70  ? 1.643   15.746  29.283  1.00 19.13 ? 89  THR A HG22 1 
ATOM   838  H HG23 . THR A 1 70  ? 3.148   15.837  28.814  1.00 19.13 ? 89  THR A HG23 1 
ATOM   839  N N    . THR A 1 71  ? 0.771   12.688  25.461  1.00 11.65 ? 90  THR A N    1 
ATOM   840  C CA   . THR A 1 71  ? 0.813   11.385  24.800  1.00 11.65 ? 90  THR A CA   1 
ATOM   841  C C    . THR A 1 71  ? 1.933   10.521  25.371  1.00 12.45 ? 90  THR A C    1 
ATOM   842  O O    . THR A 1 71  ? 1.778   9.302   25.500  1.00 12.63 ? 90  THR A O    1 
ATOM   843  C CB   . THR A 1 71  ? 0.973   11.555  23.287  1.00 12.08 ? 90  THR A CB   1 
ATOM   844  O OG1  . THR A 1 71  ? -0.148  12.282  22.778  1.00 11.98 ? 90  THR A OG1  1 
ATOM   845  C CG2  . THR A 1 71  ? 1.064   10.213  22.592  1.00 12.48 ? 90  THR A CG2  1 
ATOM   846  H H    . THR A 1 71  ? 0.905   13.366  24.950  1.00 13.99 ? 90  THR A H    1 
ATOM   847  H HA   . THR A 1 71  ? -0.030  10.929  24.952  1.00 13.98 ? 90  THR A HA   1 
ATOM   848  H HB   . THR A 1 71  ? 1.793   12.039  23.100  1.00 14.50 ? 90  THR A HB   1 
ATOM   849  H HG1  . THR A 1 71  ? -0.199  13.031  23.154  1.00 14.38 ? 90  THR A HG1  1 
ATOM   850  H HG21 . THR A 1 71  ? 1.096   10.338  21.630  1.00 14.99 ? 90  THR A HG21 1 
ATOM   851  H HG22 . THR A 1 71  ? 1.866   9.746   22.875  1.00 14.99 ? 90  THR A HG22 1 
ATOM   852  H HG23 . THR A 1 71  ? 0.291   9.671   22.813  1.00 14.99 ? 90  THR A HG23 1 
ATOM   853  N N    . GLU A 1 72  ? 3.073   11.125  25.719  1.00 11.94 ? 91  GLU A N    1 
ATOM   854  C CA   . GLU A 1 72  ? 4.162   10.310  26.253  1.00 11.83 ? 91  GLU A CA   1 
ATOM   855  C C    . GLU A 1 72  ? 3.746   9.593   27.535  1.00 12.05 ? 91  GLU A C    1 
ATOM   856  O O    . GLU A 1 72  ? 4.006   8.393   27.701  1.00 12.47 ? 91  GLU A O    1 
ATOM   857  C CB   . GLU A 1 72  ? 5.409   11.163  26.493  1.00 13.17 ? 91  GLU A CB   1 
ATOM   858  C CG   . GLU A 1 72  ? 5.953   11.837  25.220  1.00 14.29 ? 91  GLU A CG   1 
ATOM   859  C CD   . GLU A 1 72  ? 5.528   13.274  25.069  1.00 12.68 ? 91  GLU A CD   1 
ATOM   860  O OE1  . GLU A 1 72  ? 4.368   13.606  25.379  1.00 12.64 ? 91  GLU A OE1  1 
ATOM   861  O OE2  . GLU A 1 72  ? 6.359   14.074  24.615  1.00 13.03 ? 91  GLU A OE2  1 
ATOM   862  H H    . GLU A 1 72  ? 3.233   11.968  25.658  1.00 14.34 ? 91  GLU A H    1 
ATOM   863  H HA   . GLU A 1 72  ? 4.389   9.638   25.593  1.00 14.20 ? 91  GLU A HA   1 
ATOM   864  H HB2  . GLU A 1 72  ? 5.191   11.863  27.128  1.00 15.81 ? 91  GLU A HB2  1 
ATOM   865  H HB3  . GLU A 1 72  ? 6.110   10.597  26.851  1.00 15.81 ? 91  GLU A HB3  1 
ATOM   866  H HG2  . GLU A 1 72  ? 6.923   11.816  25.245  1.00 17.15 ? 91  GLU A HG2  1 
ATOM   867  H HG3  . GLU A 1 72  ? 5.631   11.349  24.446  1.00 17.15 ? 91  GLU A HG3  1 
ATOM   868  N N    . ALA A 1 73  ? 3.070   10.301  28.437  1.00 13.00 ? 92  ALA A N    1 
ATOM   869  C CA   . ALA A 1 73  ? 2.644   9.670   29.681  1.00 12.67 ? 92  ALA A CA   1 
ATOM   870  C C    . ALA A 1 73  ? 1.550   8.638   29.437  1.00 12.02 ? 92  ALA A C    1 
ATOM   871  O O    . ALA A 1 73  ? 1.552   7.567   30.053  1.00 12.77 ? 92  ALA A O    1 
ATOM   872  C CB   . ALA A 1 73  ? 2.169   10.735  30.666  1.00 13.59 ? 92  ALA A CB   1 
ATOM   873  H H    . ALA A 1 73  ? 2.850   11.128  28.355  1.00 15.60 ? 92  ALA A H    1 
ATOM   874  H HA   . ALA A 1 73  ? 3.402   9.210   30.073  1.00 15.21 ? 92  ALA A HA   1 
ATOM   875  H HB1  . ALA A 1 73  ? 1.851   10.300  31.473  1.00 16.32 ? 92  ALA A HB1  1 
ATOM   876  H HB2  . ALA A 1 73  ? 2.911   11.323  30.877  1.00 16.32 ? 92  ALA A HB2  1 
ATOM   877  H HB3  . ALA A 1 73  ? 1.449   11.243  30.259  1.00 16.32 ? 92  ALA A HB3  1 
ATOM   878  N N    . GLY A 1 74  ? 0.627   8.930   28.519  1.00 11.95 ? 93  GLY A N    1 
ATOM   879  C CA   . GLY A 1 74  ? -0.440  7.988   28.240  1.00 12.37 ? 93  GLY A CA   1 
ATOM   880  C C    . GLY A 1 74  ? 0.073   6.716   27.595  1.00 11.79 ? 93  GLY A C    1 
ATOM   881  O O    . GLY A 1 74  ? -0.337  5.609   27.961  1.00 12.18 ? 93  GLY A O    1 
ATOM   882  H H    . GLY A 1 74  ? 0.602   9.653   28.055  1.00 14.35 ? 93  GLY A H    1 
ATOM   883  H HA2  . GLY A 1 74  ? -0.887  7.753   29.068  1.00 14.85 ? 93  GLY A HA2  1 
ATOM   884  H HA3  . GLY A 1 74  ? -1.082  8.399   27.640  1.00 14.85 ? 93  GLY A HA3  1 
ATOM   885  N N    . ILE A 1 75  ? 0.969   6.854   26.615  1.00 11.29 ? 94  ILE A N    1 
ATOM   886  C CA   . ILE A 1 75  ? 1.530   5.679   25.959  1.00 11.35 ? 94  ILE A CA   1 
ATOM   887  C C    . ILE A 1 75  ? 2.380   4.864   26.936  1.00 11.77 ? 94  ILE A C    1 
ATOM   888  O O    . ILE A 1 75  ? 2.340   3.628   26.925  1.00 12.08 ? 94  ILE A O    1 
ATOM   889  C CB   . ILE A 1 75  ? 2.284   6.069   24.669  1.00 10.91 ? 94  ILE A CB   1 
ATOM   890  C CG1  . ILE A 1 75  ? 1.287   6.491   23.577  1.00 11.34 ? 94  ILE A CG1  1 
ATOM   891  C CG2  . ILE A 1 75  ? 3.163   4.895   24.193  1.00 11.75 ? 94  ILE A CG2  1 
ATOM   892  C CD1  . ILE A 1 75  ? 1.886   6.858   22.248  1.00 11.64 ? 94  ILE A CD1  1 
ATOM   893  H H    . ILE A 1 75  ? 1.262   7.606   26.317  1.00 13.56 ? 94  ILE A H    1 
ATOM   894  H HA   . ILE A 1 75  ? 0.797   5.107   25.682  1.00 13.63 ? 94  ILE A HA   1 
ATOM   895  H HB   . ILE A 1 75  ? 2.862   6.824   24.859  1.00 13.10 ? 94  ILE A HB   1 
ATOM   896  H HG12 . ILE A 1 75  ? 0.676   5.755   23.422  1.00 13.62 ? 94  ILE A HG12 1 
ATOM   897  H HG13 . ILE A 1 75  ? 0.799   7.267   23.895  1.00 13.62 ? 94  ILE A HG13 1 
ATOM   898  H HG21 . ILE A 1 75  ? 3.580   5.133   23.350  1.00 14.10 ? 94  ILE A HG21 1 
ATOM   899  H HG22 . ILE A 1 75  ? 3.845   4.720   24.860  1.00 14.10 ? 94  ILE A HG22 1 
ATOM   900  H HG23 . ILE A 1 75  ? 2.606   4.110   24.076  1.00 14.10 ? 94  ILE A HG23 1 
ATOM   901  H HD11 . ILE A 1 75  ? 1.211   7.301   21.709  1.00 13.98 ? 94  ILE A HD11 1 
ATOM   902  H HD12 . ILE A 1 75  ? 2.637   7.455   22.394  1.00 13.98 ? 94  ILE A HD12 1 
ATOM   903  H HD13 . ILE A 1 75  ? 2.186   6.050   21.803  1.00 13.98 ? 94  ILE A HD13 1 
ATOM   904  N N    . GLU A 1 76  ? 3.176   5.526   27.780  1.00 11.47 ? 95  GLU A N    1 
ATOM   905  C CA   . GLU A 1 76  ? 4.003   4.788   28.729  1.00 11.85 ? 95  GLU A CA   1 
ATOM   906  C C    . GLU A 1 76  ? 3.131   3.949   29.662  1.00 11.45 ? 95  GLU A C    1 
ATOM   907  O O    . GLU A 1 76  ? 3.410   2.767   29.900  1.00 12.36 ? 95  GLU A O    1 
ATOM   908  C CB   . GLU A 1 76  ? 4.894   5.749   29.503  1.00 12.96 ? 95  GLU A CB   1 
ATOM   909  C CG   . GLU A 1 76  ? 5.688   5.123   30.653  1.00 11.97 ? 95  GLU A CG   1 
ATOM   910  C CD   . GLU A 1 76  ? 6.676   4.063   30.207  1.00 13.64 ? 95  GLU A CD   1 
ATOM   911  O OE1  . GLU A 1 76  ? 7.004   4.019   29.011  1.00 14.51 ? 95  GLU A OE1  1 
ATOM   912  O OE2  . GLU A 1 76  ? 7.104   3.278   31.070  1.00 14.68 ? 95  GLU A OE2  1 
ATOM   913  H H    . GLU A 1 76  ? 3.251   6.382   27.821  1.00 13.78 ? 95  GLU A H    1 
ATOM   914  H HA   . GLU A 1 76  ? 4.587   4.182   28.247  1.00 14.23 ? 95  GLU A HA   1 
ATOM   915  H HB2  . GLU A 1 76  ? 5.535   6.136   28.886  1.00 15.56 ? 95  GLU A HB2  1 
ATOM   916  H HB3  . GLU A 1 76  ? 4.336   6.445   29.882  1.00 15.56 ? 95  GLU A HB3  1 
ATOM   917  H HG2  . GLU A 1 76  ? 6.188   5.822   31.103  1.00 14.37 ? 95  GLU A HG2  1 
ATOM   918  H HG3  . GLU A 1 76  ? 5.067   4.708   31.272  1.00 14.37 ? 95  GLU A HG3  1 
ATOM   919  N N    . ALA A 1 77  ? 2.070   4.543   30.205  1.00 11.52 ? 96  ALA A N    1 
ATOM   920  C CA   . ALA A 1 77  ? 1.187   3.799   31.097  1.00 11.76 ? 96  ALA A CA   1 
ATOM   921  C C    . ALA A 1 77  ? 0.484   2.675   30.361  1.00 12.50 ? 96  ALA A C    1 
ATOM   922  O O    . ALA A 1 77  ? 0.286   1.589   30.917  1.00 12.70 ? 96  ALA A O    1 
ATOM   923  C CB   . ALA A 1 77  ? 0.173   4.748   31.723  1.00 12.97 ? 96  ALA A CB   1 
ATOM   924  H H    . ALA A 1 77  ? 1.842   5.362   30.075  1.00 13.84 ? 96  ALA A H    1 
ATOM   925  H HA   . ALA A 1 77  ? 1.714   3.406   31.810  1.00 14.11 ? 96  ALA A HA   1 
ATOM   926  H HB1  . ALA A 1 77  ? -0.443  4.236   32.270  1.00 15.57 ? 96  ALA A HB1  1 
ATOM   927  H HB2  . ALA A 1 77  ? 0.643   5.396   32.271  1.00 15.57 ? 96  ALA A HB2  1 
ATOM   928  H HB3  . ALA A 1 77  ? -0.312  5.203   31.016  1.00 15.57 ? 96  ALA A HB3  1 
ATOM   929  N N    . GLU A 1 78  ? 0.089   2.910   29.108  1.00 11.59 ? 97  GLU A N    1 
ATOM   930  C CA   . GLU A 1 78  ? -0.554  1.848   28.346  1.00 11.86 ? 97  GLU A CA   1 
ATOM   931  C C    . GLU A 1 78  ? 0.417   0.696   28.080  1.00 11.44 ? 97  GLU A C    1 
ATOM   932  O O    . GLU A 1 78  ? 0.046   -0.482  28.182  1.00 12.64 ? 97  GLU A O    1 
ATOM   933  C CB   . GLU A 1 78  ? -1.113  2.395   27.039  1.00 12.18 ? 97  GLU A CB   1 
ATOM   934  C CG   . GLU A 1 78  ? -2.030  1.384   26.350  1.00 11.88 ? 97  GLU A CG   1 
ATOM   935  C CD   . GLU A 1 78  ? -3.305  1.186   27.107  1.00 12.75 ? 97  GLU A CD   1 
ATOM   936  O OE1  . GLU A 1 78  ? -4.072  2.179   27.251  1.00 12.37 ? 97  GLU A OE1  1 
ATOM   937  O OE2  . GLU A 1 78  ? -3.540  0.045   27.556  1.00 14.26 ? 97  GLU A OE2  1 
ATOM   938  H H    . GLU A 1 78  ? 0.180   3.656   28.690  1.00 13.92 ? 97  GLU A H    1 
ATOM   939  H HA   . GLU A 1 78  ? -1.298  1.503   28.864  1.00 14.24 ? 97  GLU A HA   1 
ATOM   940  H HB2  . GLU A 1 78  ? -1.627  3.197   27.222  1.00 14.63 ? 97  GLU A HB2  1 
ATOM   941  H HB3  . GLU A 1 78  ? -0.380  2.600   26.439  1.00 14.63 ? 97  GLU A HB3  1 
ATOM   942  H HG2  . GLU A 1 78  ? -2.250  1.706   25.462  1.00 14.26 ? 97  GLU A HG2  1 
ATOM   943  H HG3  . GLU A 1 78  ? -1.576  0.529   26.290  1.00 14.26 ? 97  GLU A HG3  1 
ATOM   944  N N    . ALA A 1 79  ? 1.638   1.005   27.644  1.00 11.41 ? 98  ALA A N    1 
ATOM   945  C CA   . ALA A 1 79  ? 2.627   -0.038  27.395  1.00 11.55 ? 98  ALA A CA   1 
ATOM   946  C C    . ALA A 1 79  ? 2.790   -0.924  28.616  1.00 11.02 ? 98  ALA A C    1 
ATOM   947  O O    . ALA A 1 79  ? 2.902   -2.144  28.502  1.00 12.43 ? 98  ALA A O    1 
ATOM   948  C CB   . ALA A 1 79  ? 3.964   0.593   27.011  1.00 12.63 ? 98  ALA A CB   1 
ATOM   949  H H    . ALA A 1 79  ? 1.916   1.803   27.487  1.00 13.70 ? 98  ALA A H    1 
ATOM   950  H HA   . ALA A 1 79  ? 2.331   -0.589  26.653  1.00 13.86 ? 98  ALA A HA   1 
ATOM   951  H HB1  . ALA A 1 79  ? 4.613   -0.112  26.858  1.00 15.16 ? 98  ALA A HB1  1 
ATOM   952  H HB2  . ALA A 1 79  ? 3.846   1.115   26.202  1.00 15.16 ? 98  ALA A HB2  1 
ATOM   953  H HB3  . ALA A 1 79  ? 4.262   1.166   27.734  1.00 15.16 ? 98  ALA A HB3  1 
ATOM   954  N N    . ARG A 1 80  ? 2.835   -0.321  29.803  1.00 11.89 ? 99  ARG A N    1 
ATOM   955  C CA   . ARG A 1 80  ? 3.014   -1.111  31.015  1.00 13.06 ? 99  ARG A CA   1 
ATOM   956  C C    . ARG A 1 80  ? 1.820   -2.031  31.234  1.00 13.20 ? 99  ARG A C    1 
ATOM   957  O O    . ARG A 1 80  ? 1.992   -3.206  31.575  1.00 14.45 ? 99  ARG A O    1 
ATOM   958  C CB   . ARG A 1 80  ? 3.168   -0.174  32.214  1.00 14.77 ? 99  ARG A CB   1 
ATOM   959  C CG   . ARG A 1 80  ? 4.593   0.361   32.313  1.00 16.92 ? 99  ARG A CG   1 
ATOM   960  C CD   . ARG A 1 80  ? 4.682   1.412   33.408  1.00 19.08 ? 99  ARG A CD   1 
ATOM   961  N NE   . ARG A 1 80  ? 5.956   2.101   33.313  1.00 22.68 ? 99  ARG A NE   1 
ATOM   962  C CZ   . ARG A 1 80  ? 6.690   2.455   34.353  1.00 28.22 ? 99  ARG A CZ   1 
ATOM   963  N NH1  . ARG A 1 80  ? 6.234   2.345   35.588  1.00 31.05 ? 99  ARG A NH1  1 
ATOM   964  N NH2  . ARG A 1 80  ? 7.912   2.932   34.144  1.00 30.49 ? 99  ARG A NH2  1 
ATOM   965  H H    . ARG A 1 80  ? 2.765   0.526   29.930  1.00 14.27 ? 99  ARG A H    1 
ATOM   966  H HA   . ARG A 1 80  ? 3.816   -1.650  30.933  1.00 15.68 ? 99  ARG A HA   1 
ATOM   967  H HB2  . ARG A 1 80  ? 2.564   0.578   32.115  1.00 17.74 ? 99  ARG A HB2  1 
ATOM   968  H HB3  . ARG A 1 80  ? 2.965   -0.658  33.030  1.00 17.74 ? 99  ARG A HB3  1 
ATOM   969  H HG2  . ARG A 1 80  ? 5.200   -0.364  32.528  1.00 20.31 ? 99  ARG A HG2  1 
ATOM   970  H HG3  . ARG A 1 80  ? 4.847   0.768   31.470  1.00 20.31 ? 99  ARG A HG3  1 
ATOM   971  H HD2  . ARG A 1 80  ? 3.967   2.059   33.303  1.00 22.91 ? 99  ARG A HD2  1 
ATOM   972  H HD3  . ARG A 1 80  ? 4.620   0.987   34.278  1.00 22.91 ? 99  ARG A HD3  1 
ATOM   973  H HE   . ARG A 1 80  ? 6.252   2.291   32.528  1.00 27.22 ? 99  ARG A HE   1 
ATOM   974  H HH11 . ARG A 1 80  ? 5.443   2.038   35.729  1.00 37.27 ? 99  ARG A HH11 1 
ATOM   975  H HH12 . ARG A 1 80  ? 6.727   2.582   36.252  1.00 37.27 ? 99  ARG A HH12 1 
ATOM   976  H HH21 . ARG A 1 80  ? 8.214   3.006   33.342  1.00 36.59 ? 99  ARG A HH21 1 
ATOM   977  H HH22 . ARG A 1 80  ? 8.402   3.167   34.811  1.00 36.59 ? 99  ARG A HH22 1 
ATOM   978  N N    . GLN A 1 81  ? 0.595   -1.533  31.058  1.00 13.03 ? 100 GLN A N    1 
ATOM   979  C CA   . GLN A 1 81  ? -0.520  -2.433  31.336  1.00 13.81 ? 100 GLN A CA   1 
ATOM   980  C C    . GLN A 1 81  ? -0.654  -3.519  30.275  1.00 13.76 ? 100 GLN A C    1 
ATOM   981  O O    . GLN A 1 81  ? -1.007  -4.653  30.600  1.00 14.39 ? 100 GLN A O    1 
ATOM   982  C CB   . GLN A 1 81  ? -1.789  -1.660  31.630  1.00 16.77 ? 100 GLN A CB   1 
ATOM   983  C CG   . GLN A 1 81  ? -2.495  -1.032  30.512  1.00 18.54 ? 100 GLN A CG   1 
ATOM   984  C CD   . GLN A 1 81  ? -3.894  -0.517  30.924  1.00 18.93 ? 100 GLN A CD   1 
ATOM   985  O OE1  . GLN A 1 81  ? -4.238  -0.421  32.115  1.00 21.36 ? 100 GLN A OE1  1 
ATOM   986  N NE2  . GLN A 1 81  ? -4.701  -0.218  29.943  1.00 17.38 ? 100 GLN A NE2  1 
ATOM   987  H H    . GLN A 1 81  ? 0.399   -0.737  30.798  1.00 15.64 ? 100 GLN A H    1 
ATOM   988  H HA   . GLN A 1 81  ? -0.351  -2.916  32.161  1.00 16.58 ? 100 GLN A HA   1 
ATOM   989  H HB2  . GLN A 1 81  ? -2.417  -2.273  32.044  1.00 20.13 ? 100 GLN A HB2  1 
ATOM   990  H HB3  . GLN A 1 81  ? -1.563  -0.949  32.250  1.00 20.13 ? 100 GLN A HB3  1 
ATOM   991  H HG2  . GLN A 1 81  ? -1.977  -0.277  30.192  1.00 22.25 ? 100 GLN A HG2  1 
ATOM   992  H HG3  . GLN A 1 81  ? -2.608  -1.682  29.801  1.00 22.25 ? 100 GLN A HG3  1 
ATOM   993  H HE21 . GLN A 1 81  ? -5.493  0.074   30.111  1.00 20.87 ? 100 GLN A HE21 1 
ATOM   994  H HE22 . GLN A 1 81  ? -4.442  -0.312  29.128  1.00 20.87 ? 100 GLN A HE22 1 
ATOM   995  N N    . LEU A 1 82  ? -0.356  -3.211  29.013  1.00 12.92 ? 101 LEU A N    1 
ATOM   996  C CA   . LEU A 1 82  ? -0.425  -4.234  27.983  1.00 12.94 ? 101 LEU A CA   1 
ATOM   997  C C    . LEU A 1 82  ? 0.641   -5.308  28.193  1.00 12.92 ? 101 LEU A C    1 
ATOM   998  O O    . LEU A 1 82  ? 0.373   -6.494  28.008  1.00 13.12 ? 101 LEU A O    1 
ATOM   999  C CB   . LEU A 1 82  ? -0.252  -3.592  26.616  1.00 12.77 ? 101 LEU A CB   1 
ATOM   1000 C CG   . LEU A 1 82  ? -1.412  -2.721  26.131  1.00 12.92 ? 101 LEU A CG   1 
ATOM   1001 C CD1  . LEU A 1 82  ? -1.068  -2.046  24.806  1.00 14.16 ? 101 LEU A CD1  1 
ATOM   1002 C CD2  . LEU A 1 82  ? -2.668  -3.551  25.987  1.00 14.89 ? 101 LEU A CD2  1 
ATOM   1003 H H    . LEU A 1 82  ? -0.117  -2.432  28.737  1.00 15.51 ? 101 LEU A H    1 
ATOM   1004 H HA   . LEU A 1 82  ? -1.296  -4.660  28.023  1.00 15.53 ? 101 LEU A HA   1 
ATOM   1005 H HB2  . LEU A 1 82  ? 0.537   -3.029  26.645  1.00 15.34 ? 101 LEU A HB2  1 
ATOM   1006 H HB3  . LEU A 1 82  ? -0.132  -4.299  25.964  1.00 15.34 ? 101 LEU A HB3  1 
ATOM   1007 H HG   . LEU A 1 82  ? -1.575  -2.025  26.787  1.00 15.51 ? 101 LEU A HG   1 
ATOM   1008 H HD11 . LEU A 1 82  ? -1.809  -1.479  24.539  1.00 17.00 ? 101 LEU A HD11 1 
ATOM   1009 H HD12 . LEU A 1 82  ? -0.267  -1.512  24.922  1.00 17.00 ? 101 LEU A HD12 1 
ATOM   1010 H HD13 . LEU A 1 82  ? -0.916  -2.729  24.134  1.00 17.00 ? 101 LEU A HD13 1 
ATOM   1011 H HD21 . LEU A 1 82  ? -3.350  -3.019  25.548  1.00 17.87 ? 101 LEU A HD21 1 
ATOM   1012 H HD22 . LEU A 1 82  ? -2.468  -4.337  25.453  1.00 17.87 ? 101 LEU A HD22 1 
ATOM   1013 H HD23 . LEU A 1 82  ? -2.973  -3.819  26.868  1.00 17.87 ? 101 LEU A HD23 1 
ATOM   1014 N N    . LYS A 1 83  ? 1.866   -4.914  28.543  1.00 12.99 ? 102 LYS A N    1 
ATOM   1015 C CA   . LYS A 1 83  ? 2.923   -5.909  28.713  1.00 13.89 ? 102 LYS A CA   1 
ATOM   1016 C C    . LYS A 1 83  ? 2.763   -6.735  29.992  1.00 14.48 ? 102 LYS A C    1 
ATOM   1017 O O    . LYS A 1 83  ? 3.254   -7.871  30.050  1.00 15.65 ? 102 LYS A O    1 
ATOM   1018 C CB   . LYS A 1 83  ? 4.276   -5.219  28.716  1.00 16.17 ? 102 LYS A CB   1 
ATOM   1019 C CG   . LYS A 1 83  ? 4.748   -4.820  27.359  1.00 17.66 ? 102 LYS A CG   1 
ATOM   1020 C CD   . LYS A 1 83  ? 6.244   -4.486  27.464  1.00 21.20 ? 102 LYS A CD   1 
ATOM   1021 C CE   . LYS A 1 83  ? 6.768   -3.996  26.187  1.00 21.42 ? 102 LYS A CE   1 
ATOM   1022 N NZ   . LYS A 1 83  ? 8.168   -3.628  26.347  1.00 19.45 ? 102 LYS A NZ   1 
ATOM   1023 H H    . LYS A 1 83  ? 2.105   -4.100  28.684  1.00 15.60 ? 102 LYS A H    1 
ATOM   1024 H HA   . LYS A 1 83  ? 2.878   -6.523  27.964  1.00 16.67 ? 102 LYS A HA   1 
ATOM   1025 H HB2  . LYS A 1 83  ? 4.216   -4.415  29.257  1.00 19.41 ? 102 LYS A HB2  1 
ATOM   1026 H HB3  . LYS A 1 83  ? 4.934   -5.823  29.093  1.00 19.41 ? 102 LYS A HB3  1 
ATOM   1027 H HG2  . LYS A 1 83  ? 4.627   -5.552  26.733  1.00 21.19 ? 102 LYS A HG2  1 
ATOM   1028 H HG3  . LYS A 1 83  ? 4.265   -4.037  27.052  1.00 21.19 ? 102 LYS A HG3  1 
ATOM   1029 H HD2  . LYS A 1 83  ? 6.374   -3.795  28.133  1.00 25.45 ? 102 LYS A HD2  1 
ATOM   1030 H HD3  . LYS A 1 83  ? 6.737   -5.284  27.711  1.00 25.45 ? 102 LYS A HD3  1 
ATOM   1031 H HE2  . LYS A 1 83  ? 6.702   -4.692  25.515  1.00 25.72 ? 102 LYS A HE2  1 
ATOM   1032 H HE3  . LYS A 1 83  ? 6.268   -3.214  25.904  1.00 25.72 ? 102 LYS A HE3  1 
ATOM   1033 H HZ1  . LYS A 1 83  ? 8.655   -4.351  26.524  1.00 23.34 ? 102 LYS A HZ1  1 
ATOM   1034 H HZ2  . LYS A 1 83  ? 8.472   -3.252  25.599  1.00 23.34 ? 102 LYS A HZ2  1 
ATOM   1035 H HZ3  . LYS A 1 83  ? 8.256   -3.049  27.018  1.00 23.34 ? 102 LYS A HZ3  1 
ATOM   1036 N N    . ASN A 1 84  ? 2.097   -6.204  31.020  1.00 14.35 ? 103 ASN A N    1 
ATOM   1037 C CA   . ASN A 1 84  ? 1.747   -7.059  32.157  1.00 15.30 ? 103 ASN A CA   1 
ATOM   1038 C C    . ASN A 1 84  ? 0.835   -8.205  31.723  1.00 14.34 ? 103 ASN A C    1 
ATOM   1039 O O    . ASN A 1 84  ? 0.915   -9.320  32.262  1.00 15.89 ? 103 ASN A O    1 
ATOM   1040 C CB   . ASN A 1 84  ? 1.090   -6.242  33.269  1.00 18.31 ? 103 ASN A CB   1 
ATOM   1041 C CG   . ASN A 1 84  ? 0.511   -7.125  34.370  1.00 22.90 ? 103 ASN A CG   1 
ATOM   1042 O OD1  . ASN A 1 84  ? 1.244   -7.754  35.130  1.00 25.14 ? 103 ASN A OD1  1 
ATOM   1043 N ND2  . ASN A 1 84  ? -0.809  -7.179  34.450  1.00 24.66 ? 103 ASN A ND2  1 
ATOM   1044 H H    . ASN A 1 84  ? 1.845   -5.384  31.082  1.00 17.23 ? 103 ASN A H    1 
ATOM   1045 H HA   . ASN A 1 84  ? 2.562   -7.437  32.522  1.00 18.37 ? 103 ASN A HA   1 
ATOM   1046 H HB2  . ASN A 1 84  ? 1.753   -5.658  33.669  1.00 21.98 ? 103 ASN A HB2  1 
ATOM   1047 H HB3  . ASN A 1 84  ? 0.368   -5.716  32.893  1.00 21.98 ? 103 ASN A HB3  1 
ATOM   1048 H HD21 . ASN A 1 84  ? -1.292  -6.730  33.898  1.00 29.59 ? 103 ASN A HD21 1 
ATOM   1049 H HD22 . ASN A 1 84  ? -1.184  -7.663  35.054  1.00 29.59 ? 103 ASN A HD22 1 
ATOM   1050 N N    . LEU A 1 85  ? -0.027  -7.955  30.732  1.00 12.61 ? 104 LEU A N    1 
ATOM   1051 C CA   . LEU A 1 85  ? -0.913  -8.992  30.225  1.00 12.44 ? 104 LEU A CA   1 
ATOM   1052 C C    . LEU A 1 85  ? -0.170  -9.914  29.278  1.00 12.75 ? 104 LEU A C    1 
ATOM   1053 O O    . LEU A 1 85  ? -0.264  -11.139 29.394  1.00 14.86 ? 104 LEU A O    1 
ATOM   1054 C CB   . LEU A 1 85  ? -2.109  -8.371  29.502  1.00 12.95 ? 104 LEU A CB   1 
ATOM   1055 C CG   . LEU A 1 85  ? -3.082  -7.697  30.468  1.00 13.72 ? 104 LEU A CG   1 
ATOM   1056 C CD1  . LEU A 1 85  ? -3.961  -6.743  29.700  1.00 13.95 ? 104 LEU A CD1  1 
ATOM   1057 C CD2  . LEU A 1 85  ? -3.925  -8.714  31.183  1.00 14.55 ? 104 LEU A CD2  1 
ATOM   1058 H H    . LEU A 1 85  ? -0.115  -7.194  30.340  1.00 15.14 ? 104 LEU A H    1 
ATOM   1059 H HA   . LEU A 1 85  ? -1.248  -9.506  30.976  1.00 14.94 ? 104 LEU A HA   1 
ATOM   1060 H HB2  . LEU A 1 85  ? -1.790  -7.701  28.878  1.00 15.55 ? 104 LEU A HB2  1 
ATOM   1061 H HB3  . LEU A 1 85  ? -2.588  -9.067  29.026  1.00 15.55 ? 104 LEU A HB3  1 
ATOM   1062 H HG   . LEU A 1 85  ? -2.582  -7.208  31.139  1.00 16.47 ? 104 LEU A HG   1 
ATOM   1063 H HD11 . LEU A 1 85  ? -4.690  -6.456  30.271  1.00 16.75 ? 104 LEU A HD11 1 
ATOM   1064 H HD12 . LEU A 1 85  ? -3.432  -5.976  29.428  1.00 16.75 ? 104 LEU A HD12 1 
ATOM   1065 H HD13 . LEU A 1 85  ? -4.311  -7.196  28.917  1.00 16.75 ? 104 LEU A HD13 1 
ATOM   1066 H HD21 . LEU A 1 85  ? -4.529  -8.254  31.788  1.00 17.47 ? 104 LEU A HD21 1 
ATOM   1067 H HD22 . LEU A 1 85  ? -4.434  -9.219  30.529  1.00 17.47 ? 104 LEU A HD22 1 
ATOM   1068 H HD23 . LEU A 1 85  ? -3.346  -9.309  31.683  1.00 17.47 ? 104 LEU A HD23 1 
ATOM   1069 N N    . ASN A 1 86  ? 0.577   -9.337  28.338  1.00 12.33 ? 105 ASN A N    1 
ATOM   1070 C CA   . ASN A 1 86  ? 1.273   -10.092 27.298  1.00 12.82 ? 105 ASN A CA   1 
ATOM   1071 C C    . ASN A 1 86  ? 2.695   -9.566  27.215  1.00 12.82 ? 105 ASN A C    1 
ATOM   1072 O O    . ASN A 1 86  ? 2.942   -8.548  26.546  1.00 13.42 ? 105 ASN A O    1 
ATOM   1073 C CB   . ASN A 1 86  ? 0.576   -9.936  25.952  1.00 13.42 ? 105 ASN A CB   1 
ATOM   1074 C CG   . ASN A 1 86  ? 1.338   -10.572 24.807  1.00 14.00 ? 105 ASN A CG   1 
ATOM   1075 O OD1  . ASN A 1 86  ? 2.342   -11.255 25.001  1.00 14.37 ? 105 ASN A OD1  1 
ATOM   1076 N ND2  . ASN A 1 86  ? 0.872   -10.319 23.594  1.00 13.25 ? 105 ASN A ND2  1 
ATOM   1077 H H    . ASN A 1 86  ? 0.699   -8.488  28.281  1.00 14.81 ? 105 ASN A H    1 
ATOM   1078 H HA   . ASN A 1 86  ? 1.290   -11.034 27.530  1.00 15.39 ? 105 ASN A HA   1 
ATOM   1079 H HB2  . ASN A 1 86  ? -0.297  -10.356 25.999  1.00 16.11 ? 105 ASN A HB2  1 
ATOM   1080 H HB3  . ASN A 1 86  ? 0.479   -8.991  25.756  1.00 16.11 ? 105 ASN A HB3  1 
ATOM   1081 H HD21 . ASN A 1 86  ? 1.263   -10.653 22.904  1.00 15.91 ? 105 ASN A HD21 1 
ATOM   1082 H HD22 . ASN A 1 86  ? 0.178   -9.820  23.495  1.00 15.91 ? 105 ASN A HD22 1 
ATOM   1083 N N    . PRO A 1 87  ? 3.650   -10.214 27.893  1.00 13.60 ? 106 PRO A N    1 
ATOM   1084 C CA   . PRO A 1 87  ? 5.032   -9.715  27.863  1.00 14.87 ? 106 PRO A CA   1 
ATOM   1085 C C    . PRO A 1 87  ? 5.677   -9.727  26.498  1.00 15.53 ? 106 PRO A C    1 
ATOM   1086 O O    . PRO A 1 87  ? 6.726   -9.100  26.335  1.00 17.48 ? 106 PRO A O    1 
ATOM   1087 C CB   . PRO A 1 87  ? 5.779   -10.625 28.845  1.00 16.49 ? 106 PRO A CB   1 
ATOM   1088 C CG   . PRO A 1 87  ? 4.797   -11.515 29.428  1.00 19.09 ? 106 PRO A CG   1 
ATOM   1089 C CD   . PRO A 1 87  ? 3.463   -11.371 28.783  1.00 15.31 ? 106 PRO A CD   1 
ATOM   1090 H HA   . PRO A 1 87  ? 5.043   -8.807  28.205  1.00 17.85 ? 106 PRO A HA   1 
ATOM   1091 H HB2  . PRO A 1 87  ? 6.454   -11.130 28.366  1.00 19.79 ? 106 PRO A HB2  1 
ATOM   1092 H HB3  . PRO A 1 87  ? 6.196   -10.082 29.533  1.00 19.79 ? 106 PRO A HB3  1 
ATOM   1093 H HG2  . PRO A 1 87  ? 5.111   -12.426 29.315  1.00 22.91 ? 106 PRO A HG2  1 
ATOM   1094 H HG3  . PRO A 1 87  ? 4.722   -11.305 30.372  1.00 22.91 ? 106 PRO A HG3  1 
ATOM   1095 H HD2  . PRO A 1 87  ? 3.236   -12.165 28.276  1.00 18.38 ? 106 PRO A HD2  1 
ATOM   1096 H HD3  . PRO A 1 87  ? 2.777   -11.192 29.444  1.00 18.38 ? 106 PRO A HD3  1 
ATOM   1097 N N    . LYS A 1 88  ? 5.120   -10.447 25.527  1.00 14.96 ? 107 LYS A N    1 
ATOM   1098 C CA   . LYS A 1 88  ? 5.638   -10.477 24.164  1.00 15.10 ? 107 LYS A CA   1 
ATOM   1099 C C    . LYS A 1 88  ? 5.052   -9.368  23.310  1.00 15.38 ? 107 LYS A C    1 
ATOM   1100 O O    . LYS A 1 88  ? 5.420   -9.237  22.146  1.00 15.83 ? 107 LYS A O    1 
ATOM   1101 C CB   . LYS A 1 88  ? 5.330   -11.837 23.534  1.00 18.06 ? 107 LYS A CB   1 
ATOM   1102 C CG   . LYS A 1 88  ? 5.899   -13.021 24.301  1.00 21.72 ? 107 LYS A CG   1 
ATOM   1103 C CD   . LYS A 1 88  ? 6.146   -14.224 23.419  1.00 24.40 ? 107 LYS A CD   1 
ATOM   1104 C CE   . LYS A 1 88  ? 7.068   -15.237 24.088  1.00 27.02 ? 107 LYS A CE   1 
ATOM   1105 N NZ   . LYS A 1 88  ? 6.802   -16.620 23.580  1.00 29.34 ? 107 LYS A NZ   1 
ATOM   1106 H H    . LYS A 1 88  ? 4.424   -10.939 25.637  1.00 17.96 ? 107 LYS A H    1 
ATOM   1107 H HA   . LYS A 1 88  ? 6.602   -10.367 24.177  1.00 18.13 ? 107 LYS A HA   1 
ATOM   1108 H HB2  . LYS A 1 88  ? 4.368   -11.949 23.491  1.00 21.68 ? 107 LYS A HB2  1 
ATOM   1109 H HB3  . LYS A 1 88  ? 5.707   -11.857 22.640  1.00 21.68 ? 107 LYS A HB3  1 
ATOM   1110 H HG2  . LYS A 1 88  ? 6.745   -12.763 24.700  1.00 26.07 ? 107 LYS A HG2  1 
ATOM   1111 H HG3  . LYS A 1 88  ? 5.271   -13.280 24.994  1.00 26.07 ? 107 LYS A HG3  1 
ATOM   1112 H HD2  . LYS A 1 88  ? 5.301   -14.661 23.230  1.00 29.28 ? 107 LYS A HD2  1 
ATOM   1113 H HD3  . LYS A 1 88  ? 6.562   -13.935 22.592  1.00 29.28 ? 107 LYS A HD3  1 
ATOM   1114 H HE2  . LYS A 1 88  ? 7.992   -15.011 23.895  1.00 32.44 ? 107 LYS A HE2  1 
ATOM   1115 H HE3  . LYS A 1 88  ? 6.918   -15.228 25.046  1.00 32.44 ? 107 LYS A HE3  1 
ATOM   1116 H HZ1  . LYS A 1 88  ? 7.002   -16.669 22.714  1.00 35.21 ? 107 LYS A HZ1  1 
ATOM   1117 H HZ2  . LYS A 1 88  ? 7.300   -17.208 24.025  1.00 35.21 ? 107 LYS A HZ2  1 
ATOM   1118 H HZ3  . LYS A 1 88  ? 5.944   -16.825 23.690  1.00 35.21 ? 107 LYS A HZ3  1 
ATOM   1119 N N    . MET A 1 89  ? 4.149   -8.557  23.841  1.00 14.73 ? 108 MET A N    1 
ATOM   1120 C CA   . MET A 1 89  ? 3.551   -7.520  23.002  1.00 14.62 ? 108 MET A CA   1 
ATOM   1121 C C    . MET A 1 89  ? 4.566   -6.425  22.713  1.00 14.24 ? 108 MET A C    1 
ATOM   1122 O O    . MET A 1 89  ? 5.202   -5.889  23.618  1.00 16.66 ? 108 MET A O    1 
ATOM   1123 C CB   . MET A 1 89  ? 2.255   -7.047  23.661  1.00 16.56 ? 108 MET A CB   1 
ATOM   1124 C CG   . MET A 1 89  ? 1.100   -6.741  22.660  1.00 17.69 ? 108 MET A CG   1 
ATOM   1125 S SD   . MET A 1 89  ? -0.174  -5.659  23.143  1.00 18.82 ? 108 MET A SD   1 
ATOM   1126 C CE   . MET A 1 89  ? -1.117  -5.904  21.649  1.00 19.60 ? 108 MET A CE   1 
ATOM   1127 H H    . MET A 1 89  ? 3.873   -8.582  24.655  1.00 17.69 ? 108 MET A H    1 
ATOM   1128 H HA   . MET A 1 89  ? 3.294   -7.861  22.131  1.00 17.55 ? 108 MET A HA   1 
ATOM   1129 H HB2  . MET A 1 89  ? 1.944   -7.740  24.265  1.00 19.88 ? 108 MET A HB2  1 
ATOM   1130 H HB3  . MET A 1 89  ? 2.438   -6.233  24.155  1.00 19.88 ? 108 MET A HB3  1 
ATOM   1131 H HG2  . MET A 1 89  ? 1.498   -6.355  21.864  1.00 21.24 ? 108 MET A HG2  1 
ATOM   1132 H HG3  . MET A 1 89  ? 0.673   -7.585  22.441  1.00 21.24 ? 108 MET A HG3  1 
ATOM   1133 H HE1  . MET A 1 89  ? -1.902  -5.334  21.674  1.00 23.53 ? 108 MET A HE1  1 
ATOM   1134 H HE2  . MET A 1 89  ? -0.565  -5.674  20.886  1.00 23.53 ? 108 MET A HE2  1 
ATOM   1135 H HE3  . MET A 1 89  ? -1.387  -6.834  21.595  1.00 23.53 ? 108 MET A HE3  1 
ATOM   1136 N N    . LYS A 1 90  ? 4.760   -6.134  21.437  1.00 11.41 ? 109 LYS A N    1 
ATOM   1137 C CA   . LYS A 1 90  ? 5.638   -5.042  21.025  1.00 10.87 ? 109 LYS A CA   1 
ATOM   1138 C C    . LYS A 1 90  ? 4.793   -3.785  20.893  1.00 10.72 ? 109 LYS A C    1 
ATOM   1139 O O    . LYS A 1 90  ? 3.863   -3.750  20.089  1.00 11.44 ? 109 LYS A O    1 
ATOM   1140 C CB   . LYS A 1 90  ? 6.314   -5.379  19.697  1.00 11.33 ? 109 LYS A CB   1 
ATOM   1141 C CG   . LYS A 1 90  ? 7.230   -6.605  19.762  1.00 12.15 ? 109 LYS A CG   1 
ATOM   1142 C CD   . LYS A 1 90  ? 8.431   -6.382  20.657  1.00 12.49 ? 109 LYS A CD   1 
ATOM   1143 C CE   . LYS A 1 90  ? 9.401   -7.540  20.546  1.00 13.82 ? 109 LYS A CE   1 
ATOM   1144 N NZ   . LYS A 1 90  ? 10.634  -7.312  21.352  1.00 14.95 ? 109 LYS A NZ   1 
ATOM   1145 H H    . LYS A 1 90  ? 4.394   -6.556  20.783  1.00 13.70 ? 109 LYS A H    1 
ATOM   1146 H HA   . LYS A 1 90  ? 6.330   -4.892  21.687  1.00 13.05 ? 109 LYS A HA   1 
ATOM   1147 H HB2  . LYS A 1 90  ? 5.628   -5.557  19.035  1.00 13.60 ? 109 LYS A HB2  1 
ATOM   1148 H HB3  . LYS A 1 90  ? 6.853   -4.621  19.421  1.00 13.60 ? 109 LYS A HB3  1 
ATOM   1149 H HG2  . LYS A 1 90  ? 6.729   -7.358  20.113  1.00 14.58 ? 109 LYS A HG2  1 
ATOM   1150 H HG3  . LYS A 1 90  ? 7.554   -6.808  18.870  1.00 14.58 ? 109 LYS A HG3  1 
ATOM   1151 H HD2  . LYS A 1 90  ? 8.889   -5.570  20.390  1.00 15.00 ? 109 LYS A HD2  1 
ATOM   1152 H HD3  . LYS A 1 90  ? 8.140   -6.311  21.580  1.00 15.00 ? 109 LYS A HD3  1 
ATOM   1153 H HE2  . LYS A 1 90  ? 8.972   -8.348  20.869  1.00 16.60 ? 109 LYS A HE2  1 
ATOM   1154 H HE3  . LYS A 1 90  ? 9.661   -7.651  19.618  1.00 16.60 ? 109 LYS A HE3  1 
ATOM   1155 H HZ1  . LYS A 1 90  ? 10.880  -6.459  21.296  1.00 17.94 ? 109 LYS A HZ1  1 
ATOM   1156 H HZ2  . LYS A 1 90  ? 10.481  -7.513  22.205  1.00 17.94 ? 109 LYS A HZ2  1 
ATOM   1157 H HZ3  . LYS A 1 90  ? 11.295  -7.824  21.048  1.00 17.94 ? 109 LYS A HZ3  1 
ATOM   1158 N N    . VAL A 1 91  ? 5.088   -2.783  21.714  1.00 10.14 ? 110 VAL A N    1 
ATOM   1159 C CA   . VAL A 1 91  ? 4.285   -1.570  21.815  1.00 10.19 ? 110 VAL A CA   1 
ATOM   1160 C C    . VAL A 1 91  ? 5.093   -0.418  21.228  1.00 10.62 ? 110 VAL A C    1 
ATOM   1161 O O    . VAL A 1 91  ? 6.217   -0.145  21.672  1.00 10.76 ? 110 VAL A O    1 
ATOM   1162 C CB   . VAL A 1 91  ? 3.887   -1.280  23.271  1.00 10.89 ? 110 VAL A CB   1 
ATOM   1163 C CG1  . VAL A 1 91  ? 2.999   -0.030  23.330  1.00 11.98 ? 110 VAL A CG1  1 
ATOM   1164 C CG2  . VAL A 1 91  ? 3.171   -2.476  23.899  1.00 11.82 ? 110 VAL A CG2  1 
ATOM   1165 H H    . VAL A 1 91  ? 5.770   -2.783  22.239  1.00 12.18 ? 110 VAL A H    1 
ATOM   1166 H HA   . VAL A 1 91  ? 3.477   -1.674  21.288  1.00 12.23 ? 110 VAL A HA   1 
ATOM   1167 H HB   . VAL A 1 91  ? 4.692   -1.118  23.788  1.00 13.07 ? 110 VAL A HB   1 
ATOM   1168 H HG11 . VAL A 1 91  ? 2.724   0.119   24.248  1.00 14.39 ? 110 VAL A HG11 1 
ATOM   1169 H HG12 . VAL A 1 91  ? 3.506   0.733   23.009  1.00 14.39 ? 110 VAL A HG12 1 
ATOM   1170 H HG13 . VAL A 1 91  ? 2.220   -0.169  22.769  1.00 14.39 ? 110 VAL A HG13 1 
ATOM   1171 H HG21 . VAL A 1 91  ? 2.970   -2.273  24.826  1.00 14.19 ? 110 VAL A HG21 1 
ATOM   1172 H HG22 . VAL A 1 91  ? 2.349   -2.643  23.412  1.00 14.19 ? 110 VAL A HG22 1 
ATOM   1173 H HG23 . VAL A 1 91  ? 3.749   -3.253  23.848  1.00 14.19 ? 110 VAL A HG23 1 
ATOM   1174 N N    . ILE A 1 92  ? 4.536   0.228   20.210  1.00 10.18 ? 111 ILE A N    1 
ATOM   1175 C CA   . ILE A 1 92  ? 5.266   1.197   19.394  1.00 10.42 ? 111 ILE A CA   1 
ATOM   1176 C C    . ILE A 1 92  ? 4.757   2.608   19.666  1.00 9.90  ? 111 ILE A C    1 
ATOM   1177 O O    . ILE A 1 92  ? 3.546   2.867   19.628  1.00 10.67 ? 111 ILE A O    1 
ATOM   1178 C CB   . ILE A 1 92  ? 5.135   0.846   17.902  1.00 10.59 ? 111 ILE A CB   1 
ATOM   1179 C CG1  . ILE A 1 92  ? 5.511   -0.621  17.634  1.00 10.95 ? 111 ILE A CG1  1 
ATOM   1180 C CG2  . ILE A 1 92  ? 5.946   1.793   17.032  1.00 10.48 ? 111 ILE A CG2  1 
ATOM   1181 C CD1  . ILE A 1 92  ? 6.912   -1.044  18.024  1.00 12.38 ? 111 ILE A CD1  1 
ATOM   1182 H H    . ILE A 1 92  ? 3.719   0.120   19.966  1.00 12.23 ? 111 ILE A H    1 
ATOM   1183 H HA   . ILE A 1 92  ? 6.200   1.184   19.655  1.00 12.51 ? 111 ILE A HA   1 
ATOM   1184 H HB   . ILE A 1 92  ? 4.201   0.957   17.664  1.00 12.72 ? 111 ILE A HB   1 
ATOM   1185 H HG12 . ILE A 1 92  ? 4.896   -1.185  18.129  1.00 13.14 ? 111 ILE A HG12 1 
ATOM   1186 H HG13 . ILE A 1 92  ? 5.420   -0.786  16.682  1.00 13.14 ? 111 ILE A HG13 1 
ATOM   1187 H HG21 . ILE A 1 92  ? 5.897   1.495   16.110  1.00 12.59 ? 111 ILE A HG21 1 
ATOM   1188 H HG22 . ILE A 1 92  ? 5.579   2.687   17.111  1.00 12.59 ? 111 ILE A HG22 1 
ATOM   1189 H HG23 . ILE A 1 92  ? 6.869   1.787   17.333  1.00 12.59 ? 111 ILE A HG23 1 
ATOM   1190 H HD11 . ILE A 1 92  ? 7.029   -1.984  17.811  1.00 14.86 ? 111 ILE A HD11 1 
ATOM   1191 H HD12 . ILE A 1 92  ? 7.553   -0.511  17.529  1.00 14.86 ? 111 ILE A HD12 1 
ATOM   1192 H HD13 . ILE A 1 92  ? 7.031   -0.904  18.976  1.00 14.86 ? 111 ILE A HD13 1 
ATOM   1193 N N    . PHE A 1 93  ? 5.695   3.509   19.937  1.00 10.39 ? 112 PHE A N    1 
ATOM   1194 C CA   . PHE A 1 93  ? 5.436   4.921   20.231  1.00 10.37 ? 112 PHE A CA   1 
ATOM   1195 C C    . PHE A 1 93  ? 5.300   5.725   18.944  1.00 9.22  ? 112 PHE A C    1 
ATOM   1196 O O    . PHE A 1 93  ? 6.226   5.757   18.135  1.00 10.62 ? 112 PHE A O    1 
ATOM   1197 C CB   . PHE A 1 93  ? 6.646   5.426   21.022  1.00 10.82 ? 112 PHE A CB   1 
ATOM   1198 C CG   . PHE A 1 93  ? 6.643   6.909   21.342  1.00 11.07 ? 112 PHE A CG   1 
ATOM   1199 C CD1  . PHE A 1 93  ? 5.775   7.424   22.272  1.00 12.16 ? 112 PHE A CD1  1 
ATOM   1200 C CD2  . PHE A 1 93  ? 7.559   7.776   20.749  1.00 12.44 ? 112 PHE A CD2  1 
ATOM   1201 C CE1  . PHE A 1 93  ? 5.793   8.780   22.591  1.00 12.23 ? 112 PHE A CE1  1 
ATOM   1202 C CE2  . PHE A 1 93  ? 7.582   9.134   21.062  1.00 12.84 ? 112 PHE A CE2  1 
ATOM   1203 C CZ   . PHE A 1 93  ? 6.690   9.632   21.969  1.00 11.77 ? 112 PHE A CZ   1 
ATOM   1204 H H    . PHE A 1 93  ? 6.535   3.322   19.958  1.00 12.48 ? 112 PHE A H    1 
ATOM   1205 H HA   . PHE A 1 93  ? 4.607   5.023   20.724  1.00 12.45 ? 112 PHE A HA   1 
ATOM   1206 H HB2  . PHE A 1 93  ? 6.680   4.949   21.866  1.00 12.99 ? 112 PHE A HB2  1 
ATOM   1207 H HB3  . PHE A 1 93  ? 7.447   5.244   20.506  1.00 12.99 ? 112 PHE A HB3  1 
ATOM   1208 H HD1  . PHE A 1 93  ? 5.168   6.861   22.694  1.00 14.60 ? 112 PHE A HD1  1 
ATOM   1209 H HD2  . PHE A 1 93  ? 8.169   7.441   20.132  1.00 14.94 ? 112 PHE A HD2  1 
ATOM   1210 H HE1  . PHE A 1 93  ? 5.199   9.114   23.224  1.00 14.68 ? 112 PHE A HE1  1 
ATOM   1211 H HE2  . PHE A 1 93  ? 8.201   9.698   20.656  1.00 15.42 ? 112 PHE A HE2  1 
ATOM   1212 H HZ   . PHE A 1 93  ? 6.685   10.541  22.168  1.00 14.13 ? 112 PHE A HZ   1 
ATOM   1213 N N    . TYR A 1 94  ? 4.159   6.403   18.763  1.00 11.11 ? 113 TYR A N    1 
ATOM   1214 C CA   . TYR A 1 94  ? 3.939   7.249   17.583  1.00 10.99 ? 113 TYR A CA   1 
ATOM   1215 C C    . TYR A 1 94  ? 4.721   8.558   17.723  1.00 11.60 ? 113 TYR A C    1 
ATOM   1216 O O    . TYR A 1 94  ? 4.532   9.303   18.689  1.00 12.19 ? 113 TYR A O    1 
ATOM   1217 C CB   . TYR A 1 94  ? 2.442   7.552   17.424  1.00 11.57 ? 113 TYR A CB   1 
ATOM   1218 C CG   . TYR A 1 94  ? 2.133   8.393   16.221  1.00 11.65 ? 113 TYR A CG   1 
ATOM   1219 C CD1  . TYR A 1 94  ? 2.254   9.776   16.282  1.00 11.98 ? 113 TYR A CD1  1 
ATOM   1220 C CD2  . TYR A 1 94  ? 1.746   7.821   15.026  1.00 11.85 ? 113 TYR A CD2  1 
ATOM   1221 C CE1  . TYR A 1 94  ? 1.983   10.567  15.171  1.00 11.77 ? 113 TYR A CE1  1 
ATOM   1222 C CE2  . TYR A 1 94  ? 1.509   8.583   13.911  1.00 11.56 ? 113 TYR A CE2  1 
ATOM   1223 C CZ   . TYR A 1 94  ? 1.610   9.967   13.978  1.00 11.28 ? 113 TYR A CZ   1 
ATOM   1224 O OH   . TYR A 1 94  ? 1.357   10.757  12.890  1.00 11.95 ? 113 TYR A OH   1 
ATOM   1225 H H    . TYR A 1 94  ? 3.496   6.390   19.311  1.00 13.33 ? 113 TYR A H    1 
ATOM   1226 H HA   . TYR A 1 94  ? 4.252   6.778   16.795  1.00 13.19 ? 113 TYR A HA   1 
ATOM   1227 H HB2  . TYR A 1 94  ? 1.960   6.715   17.335  1.00 13.89 ? 113 TYR A HB2  1 
ATOM   1228 H HB3  . TYR A 1 94  ? 2.134   8.031   18.209  1.00 13.89 ? 113 TYR A HB3  1 
ATOM   1229 H HD1  . TYR A 1 94  ? 2.520   10.178  17.077  1.00 14.39 ? 113 TYR A HD1  1 
ATOM   1230 H HD2  . TYR A 1 94  ? 1.644   6.898   14.976  1.00 14.23 ? 113 TYR A HD2  1 
ATOM   1231 H HE1  . TYR A 1 94  ? 2.053   11.493  15.227  1.00 14.12 ? 113 TYR A HE1  1 
ATOM   1232 H HE2  . TYR A 1 94  ? 1.280   8.173   13.108  1.00 13.88 ? 113 TYR A HE2  1 
ATOM   1233 H HH   . TYR A 1 94  ? 1.287   10.283  12.200  1.00 14.35 ? 113 TYR A HH   1 
ATOM   1234 N N    . TRP A 1 95  ? 5.583   8.870   16.745  1.00 10.91 ? 114 TRP A N    1 
ATOM   1235 C CA   . TRP A 1 95  ? 6.410   10.082  16.829  1.00 10.80 ? 114 TRP A CA   1 
ATOM   1236 C C    . TRP A 1 95  ? 6.593   10.589  15.400  1.00 11.38 ? 114 TRP A C    1 
ATOM   1237 O O    . TRP A 1 95  ? 7.369   10.027  14.627  1.00 12.19 ? 114 TRP A O    1 
ATOM   1238 C CB   . TRP A 1 95  ? 7.716   9.775   17.589  1.00 11.82 ? 114 TRP A CB   1 
ATOM   1239 C CG   . TRP A 1 95  ? 8.569   10.983  17.903  1.00 11.44 ? 114 TRP A CG   1 
ATOM   1240 C CD1  . TRP A 1 95  ? 9.907   11.089  17.709  1.00 11.77 ? 114 TRP A CD1  1 
ATOM   1241 C CD2  . TRP A 1 95  ? 8.149   12.250  18.444  1.00 11.47 ? 114 TRP A CD2  1 
ATOM   1242 N NE1  . TRP A 1 95  ? 10.350  12.327  18.062  1.00 11.86 ? 114 TRP A NE1  1 
ATOM   1243 C CE2  . TRP A 1 95  ? 9.295   13.071  18.516  1.00 11.76 ? 114 TRP A CE2  1 
ATOM   1244 C CE3  . TRP A 1 95  ? 6.923   12.764  18.885  1.00 11.79 ? 114 TRP A CE3  1 
ATOM   1245 C CZ2  . TRP A 1 95  ? 9.246   14.395  18.967  1.00 12.13 ? 114 TRP A CZ2  1 
ATOM   1246 C CZ3  . TRP A 1 95  ? 6.869   14.077  19.334  1.00 12.93 ? 114 TRP A CZ3  1 
ATOM   1247 C CH2  . TRP A 1 95  ? 8.026   14.878  19.364  1.00 12.89 ? 114 TRP A CH2  1 
ATOM   1248 H H    . TRP A 1 95  ? 5.705   8.403   16.033  1.00 13.09 ? 114 TRP A H    1 
ATOM   1249 H HA   . TRP A 1 95  ? 5.966   10.796  17.314  1.00 12.97 ? 114 TRP A HA   1 
ATOM   1250 H HB2  . TRP A 1 95  ? 7.489   9.352   18.432  1.00 14.19 ? 114 TRP A HB2  1 
ATOM   1251 H HB3  . TRP A 1 95  ? 8.251   9.173   17.049  1.00 14.19 ? 114 TRP A HB3  1 
ATOM   1252 H HD1  . TRP A 1 95  ? 10.449  10.408  17.380  1.00 14.13 ? 114 TRP A HD1  1 
ATOM   1253 H HE1  . TRP A 1 95  ? 11.164  12.598  18.009  1.00 14.23 ? 114 TRP A HE1  1 
ATOM   1254 H HE3  . TRP A 1 95  ? 6.158   12.235  18.877  1.00 14.15 ? 114 TRP A HE3  1 
ATOM   1255 H HZ2  . TRP A 1 95  ? 10.010  14.926  18.995  1.00 14.57 ? 114 TRP A HZ2  1 
ATOM   1256 H HZ3  . TRP A 1 95  ? 6.058   14.431  19.620  1.00 15.53 ? 114 TRP A HZ3  1 
ATOM   1257 H HH2  . TRP A 1 95  ? 7.961   15.757  19.660  1.00 15.47 ? 114 TRP A HH2  1 
ATOM   1258 N N    . ASN A 1 96  ? 5.839   11.627  15.044  1.00 11.16 ? 115 ASN A N    1 
ATOM   1259 C CA   . ASN A 1 96  ? 5.770   12.060  13.661  1.00 11.05 ? 115 ASN A CA   1 
ATOM   1260 C C    . ASN A 1 96  ? 7.106   12.660  13.248  1.00 10.89 ? 115 ASN A C    1 
ATOM   1261 O O    . ASN A 1 96  ? 7.657   13.517  13.946  1.00 11.26 ? 115 ASN A O    1 
ATOM   1262 C CB   . ASN A 1 96  ? 4.652   13.085  13.500  1.00 10.81 ? 115 ASN A CB   1 
ATOM   1263 C CG   . ASN A 1 96  ? 4.270   13.289  12.057  1.00 11.62 ? 115 ASN A CG   1 
ATOM   1264 O OD1  . ASN A 1 96  ? 5.033   13.862  11.284  1.00 12.00 ? 115 ASN A OD1  1 
ATOM   1265 N ND2  . ASN A 1 96  ? 3.096   12.794  11.674  1.00 12.35 ? 115 ASN A ND2  1 
ATOM   1266 H H    . ASN A 1 96  ? 5.361   12.092  15.586  1.00 13.40 ? 115 ASN A H    1 
ATOM   1267 H HA   . ASN A 1 96  ? 5.579   11.306  13.082  1.00 13.27 ? 115 ASN A HA   1 
ATOM   1268 H HB2  . ASN A 1 96  ? 3.867   12.777  13.979  1.00 12.98 ? 115 ASN A HB2  1 
ATOM   1269 H HB3  . ASN A 1 96  ? 4.946   13.936  13.858  1.00 12.98 ? 115 ASN A HB3  1 
ATOM   1270 H HD21 . ASN A 1 96  ? 2.598   12.382  12.241  1.00 14.82 ? 115 ASN A HD21 1 
ATOM   1271 H HD22 . ASN A 1 96  ? 2.835   12.887  10.860  1.00 14.82 ? 115 ASN A HD22 1 
ATOM   1272 N N    . THR A 1 97  ? 7.611   12.238  12.084  1.00 11.18 ? 116 THR A N    1 
ATOM   1273 C CA   . THR A 1 97  ? 8.945   12.638  11.649  1.00 10.72 ? 116 THR A CA   1 
ATOM   1274 C C    . THR A 1 97  ? 8.969   14.070  11.142  1.00 11.24 ? 116 THR A C    1 
ATOM   1275 O O    . THR A 1 97  ? 10.053  14.650  11.001  1.00 12.12 ? 116 THR A O    1 
ATOM   1276 C CB   . THR A 1 97  ? 9.395   11.739  10.491  1.00 10.86 ? 116 THR A CB   1 
ATOM   1277 O OG1  . THR A 1 97  ? 8.998   10.381  10.725  1.00 11.67 ? 116 THR A OG1  1 
ATOM   1278 C CG2  . THR A 1 97  ? 10.881  11.750  10.313  1.00 12.46 ? 116 THR A CG2  1 
ATOM   1279 H H    . THR A 1 97  ? 7.200   11.722  11.532  1.00 13.43 ? 116 THR A H    1 
ATOM   1280 H HA   . THR A 1 97  ? 9.553   12.546  12.399  1.00 12.87 ? 116 THR A HA   1 
ATOM   1281 H HB   . THR A 1 97  ? 8.980   12.082  9.684   1.00 13.04 ? 116 THR A HB   1 
ATOM   1282 H HG1  . THR A 1 97  ? 8.245   10.238  10.380  1.00 14.01 ? 116 THR A HG1  1 
ATOM   1283 H HG21 . THR A 1 97  ? 11.132  11.168  9.579   1.00 14.95 ? 116 THR A HG21 1 
ATOM   1284 H HG22 . THR A 1 97  ? 11.185  12.651  10.118  1.00 14.95 ? 116 THR A HG22 1 
ATOM   1285 H HG23 . THR A 1 97  ? 11.315  11.440  11.124  1.00 14.95 ? 116 THR A HG23 1 
ATOM   1286 N N    . PHE A 1 98  ? 7.799   14.653  10.861  1.00 11.24 ? 117 PHE A N    1 
ATOM   1287 C CA   . PHE A 1 98  ? 7.739   15.922  10.139  1.00 11.39 ? 117 PHE A CA   1 
ATOM   1288 C C    . PHE A 1 98  ? 6.880   16.985  10.789  1.00 11.84 ? 117 PHE A C    1 
ATOM   1289 O O    . PHE A 1 98  ? 7.067   18.162  10.466  1.00 12.83 ? 117 PHE A O    1 
ATOM   1290 C CB   . PHE A 1 98  ? 7.172   15.649  8.751   1.00 12.56 ? 117 PHE A CB   1 
ATOM   1291 C CG   . PHE A 1 98  ? 7.415   16.713  7.705   1.00 12.30 ? 117 PHE A CG   1 
ATOM   1292 C CD1  . PHE A 1 98  ? 8.530   17.535  7.697   1.00 13.22 ? 117 PHE A CD1  1 
ATOM   1293 C CD2  . PHE A 1 98  ? 6.518   16.804  6.650   1.00 13.65 ? 117 PHE A CD2  1 
ATOM   1294 C CE1  . PHE A 1 98  ? 8.733   18.447  6.649   1.00 13.37 ? 117 PHE A CE1  1 
ATOM   1295 C CE2  . PHE A 1 98  ? 6.708   17.704  5.609   1.00 13.98 ? 117 PHE A CE2  1 
ATOM   1296 C CZ   . PHE A 1 98  ? 7.818   18.528  5.606   1.00 13.63 ? 117 PHE A CZ   1 
ATOM   1297 H H    . PHE A 1 98  ? 7.031   14.332  11.078  1.00 13.50 ? 117 PHE A H    1 
ATOM   1298 H HA   . PHE A 1 98  ? 8.634   16.291  10.069  1.00 13.68 ? 117 PHE A HA   1 
ATOM   1299 H HB2  . PHE A 1 98  ? 7.568   14.828  8.419   1.00 15.08 ? 117 PHE A HB2  1 
ATOM   1300 H HB3  . PHE A 1 98  ? 6.211   15.545  8.833   1.00 15.08 ? 117 PHE A HB3  1 
ATOM   1301 H HD1  . PHE A 1 98  ? 9.147   17.483  8.390   1.00 15.87 ? 117 PHE A HD1  1 
ATOM   1302 H HD2  . PHE A 1 98  ? 5.771   16.250  6.641   1.00 16.39 ? 117 PHE A HD2  1 
ATOM   1303 H HE1  . PHE A 1 98  ? 9.481   18.999  6.653   1.00 16.05 ? 117 PHE A HE1  1 
ATOM   1304 H HE2  . PHE A 1 98  ? 6.090   17.751  4.916   1.00 16.78 ? 117 PHE A HE2  1 
ATOM   1305 H HZ   . PHE A 1 98  ? 7.952   19.132  4.911   1.00 16.36 ? 117 PHE A HZ   1 
ATOM   1306 N N    . LEU A 1 99  ? 5.959   16.624  11.687  1.00 12.76 ? 118 LEU A N    1 
ATOM   1307 C CA   . LEU A 1 99  ? 4.945   17.539  12.165  1.00 12.44 ? 118 LEU A CA   1 
ATOM   1308 C C    . LEU A 1 99  ? 4.975   17.645  13.679  1.00 12.76 ? 118 LEU A C    1 
ATOM   1309 O O    . LEU A 1 99  ? 5.071   16.630  14.395  1.00 12.86 ? 118 LEU A O    1 
ATOM   1310 C CB   . LEU A 1 99  ? 3.556   17.084  11.728  1.00 12.81 ? 118 LEU A CB   1 
ATOM   1311 C CG   . LEU A 1 99  ? 3.394   16.829  10.233  1.00 13.71 ? 118 LEU A CG   1 
ATOM   1312 C CD1  . LEU A 1 99  ? 1.978   16.304  9.955   1.00 15.39 ? 118 LEU A CD1  1 
ATOM   1313 C CD2  . LEU A 1 99  ? 3.676   18.054  9.399   1.00 14.42 ? 118 LEU A CD2  1 
ATOM   1314 H H    . LEU A 1 99  ? 5.909   15.839  12.034  1.00 15.32 ? 118 LEU A H    1 
ATOM   1315 H HA   . LEU A 1 99  ? 5.131   18.420  11.805  1.00 14.93 ? 118 LEU A HA   1 
ATOM   1316 H HB2  . LEU A 1 99  ? 3.347   16.256  12.188  1.00 15.38 ? 118 LEU A HB2  1 
ATOM   1317 H HB3  . LEU A 1 99  ? 2.918   17.772  11.976  1.00 15.38 ? 118 LEU A HB3  1 
ATOM   1318 H HG   . LEU A 1 99  ? 4.047   16.164  9.965   1.00 16.46 ? 118 LEU A HG   1 
ATOM   1319 H HD11 . LEU A 1 99  ? 1.882   16.142  9.004   1.00 18.47 ? 118 LEU A HD11 1 
ATOM   1320 H HD12 . LEU A 1 99  ? 1.846   15.478  10.447  1.00 18.47 ? 118 LEU A HD12 1 
ATOM   1321 H HD13 . LEU A 1 99  ? 1.333   16.968  10.244  1.00 18.47 ? 118 LEU A HD13 1 
ATOM   1322 H HD21 . LEU A 1 99  ? 3.549   17.835  8.463   1.00 17.31 ? 118 LEU A HD21 1 
ATOM   1323 H HD22 . LEU A 1 99  ? 3.065   18.761  9.660   1.00 17.31 ? 118 LEU A HD22 1 
ATOM   1324 H HD23 . LEU A 1 99  ? 4.592   18.335  9.552   1.00 17.31 ? 118 LEU A HD23 1 
ATOM   1325 N N    . ASP A 1 100 ? 4.810   18.888  14.143  1.00 13.18 ? 119 ASP A N    1 
ATOM   1326 C CA   . ASP A 1 100 ? 4.897   19.261  15.560  1.00 12.96 ? 119 ASP A CA   1 
ATOM   1327 C C    . ASP A 1 100 ? 3.498   19.269  16.173  1.00 12.79 ? 119 ASP A C    1 
ATOM   1328 O O    . ASP A 1 100 ? 2.890   20.308  16.377  1.00 14.66 ? 119 ASP A O    1 
ATOM   1329 C CB   . ASP A 1 100 ? 5.546   20.646  15.640  1.00 13.09 ? 119 ASP A CB   1 
ATOM   1330 C CG   . ASP A 1 100 ? 5.433   21.296  17.017  1.00 13.71 ? 119 ASP A CG   1 
ATOM   1331 O OD1  . ASP A 1 100 ? 5.489   20.558  18.023  1.00 13.77 ? 119 ASP A OD1  1 
ATOM   1332 O OD2  . ASP A 1 100 ? 5.310   22.543  17.071  1.00 13.47 ? 119 ASP A OD2  1 
ATOM   1333 H H    . ASP A 1 100 ? 4.638   19.561  13.636  1.00 15.82 ? 119 ASP A H    1 
ATOM   1334 H HA   . ASP A 1 100 ? 5.419   18.602  16.046  1.00 15.56 ? 119 ASP A HA   1 
ATOM   1335 H HB2  . ASP A 1 100 ? 6.489   20.562  15.429  1.00 15.71 ? 119 ASP A HB2  1 
ATOM   1336 H HB3  . ASP A 1 100 ? 5.113   21.231  15.000  1.00 15.71 ? 119 ASP A HB3  1 
ATOM   1337 N N    . TYR A 1 101 ? 2.956   18.082  16.423  1.00 12.71 ? 120 TYR A N    1 
ATOM   1338 C CA   . TYR A 1 101 ? 1.630   17.985  17.029  1.00 12.97 ? 120 TYR A CA   1 
ATOM   1339 C C    . TYR A 1 101 ? 1.622   18.480  18.481  1.00 12.93 ? 120 TYR A C    1 
ATOM   1340 O O    . TYR A 1 101 ? 2.585   18.345  19.232  1.00 13.07 ? 120 TYR A O    1 
ATOM   1341 C CB   . TYR A 1 101 ? 1.150   16.533  16.978  1.00 14.16 ? 120 TYR A CB   1 
ATOM   1342 C CG   . TYR A 1 101 ? 0.617   16.128  15.629  1.00 13.85 ? 120 TYR A CG   1 
ATOM   1343 C CD1  . TYR A 1 101 ? -0.606  16.598  15.186  1.00 15.70 ? 120 TYR A CD1  1 
ATOM   1344 C CD2  . TYR A 1 101 ? 1.309   15.277  14.806  1.00 14.71 ? 120 TYR A CD2  1 
ATOM   1345 C CE1  . TYR A 1 101 ? -1.114  16.233  13.964  1.00 16.44 ? 120 TYR A CE1  1 
ATOM   1346 C CE2  . TYR A 1 101 ? 0.803   14.899  13.576  1.00 15.38 ? 120 TYR A CE2  1 
ATOM   1347 C CZ   . TYR A 1 101 ? -0.405  15.396  13.155  1.00 15.99 ? 120 TYR A CZ   1 
ATOM   1348 O OH   . TYR A 1 101 ? -0.950  15.055  11.937  1.00 18.33 ? 120 TYR A OH   1 
ATOM   1349 H H    . TYR A 1 101 ? 3.330   17.326  16.254  1.00 15.26 ? 120 TYR A H    1 
ATOM   1350 H HA   . TYR A 1 101 ? 1.015   18.547  16.532  1.00 15.57 ? 120 TYR A HA   1 
ATOM   1351 H HB2  . TYR A 1 101 ? 1.894   15.949  17.192  1.00 16.99 ? 120 TYR A HB2  1 
ATOM   1352 H HB3  . TYR A 1 101 ? 0.438   16.415  17.627  1.00 16.99 ? 120 TYR A HB3  1 
ATOM   1353 H HD1  . TYR A 1 101 ? -1.096  17.174  15.728  1.00 18.85 ? 120 TYR A HD1  1 
ATOM   1354 H HD2  . TYR A 1 101 ? 2.135   14.948  15.081  1.00 17.66 ? 120 TYR A HD2  1 
ATOM   1355 H HE1  . TYR A 1 101 ? -1.941  16.556  13.688  1.00 19.73 ? 120 TYR A HE1  1 
ATOM   1356 H HE2  . TYR A 1 101 ? 1.280   14.310  13.036  1.00 18.46 ? 120 TYR A HE2  1 
ATOM   1357 H HH   . TYR A 1 101 ? -0.463  14.488  11.553  1.00 22.00 ? 120 TYR A HH   1 
ATOM   1358 N N    . SER A 1 102 ? 0.496   19.035  18.890  1.00 13.71 ? 121 SER A N    1 
ATOM   1359 C CA   . SER A 1 102 ? 0.441   19.737  20.169  1.00 14.58 ? 121 SER A CA   1 
ATOM   1360 C C    . SER A 1 102 ? 0.328   18.820  21.389  1.00 14.75 ? 121 SER A C    1 
ATOM   1361 O O    . SER A 1 102 ? 0.663   19.238  22.499  1.00 17.13 ? 121 SER A O    1 
ATOM   1362 C CB   . SER A 1 102 ? -0.730  20.720  20.181  1.00 16.50 ? 121 SER A CB   1 
ATOM   1363 O OG   . SER A 1 102 ? -1.951  19.998  20.125  1.00 18.49 ? 121 SER A OG   1 
ATOM   1364 H H    . SER A 1 102 ? -0.245  19.021  18.455  1.00 16.46 ? 121 SER A H    1 
ATOM   1365 H HA   . SER A 1 102 ? 1.270   20.232  20.258  1.00 17.50 ? 121 SER A HA   1 
ATOM   1366 H HB2  . SER A 1 102 ? -0.703  21.243  20.997  1.00 19.80 ? 121 SER A HB2  1 
ATOM   1367 H HB3  . SER A 1 102 ? -0.667  21.305  19.410  1.00 19.80 ? 121 SER A HB3  1 
ATOM   1368 H HG   . SER A 1 102 ? -2.593  20.529  20.020  1.00 22.19 ? 121 SER A HG   1 
ATOM   1369 N N    . MET A 1 103 ? -0.130  17.584  21.231  1.00 13.18 ? 122 MET A N    1 
ATOM   1370 C CA   . MET A 1 103 ? -0.533  16.759  22.373  1.00 13.55 ? 122 MET A CA   1 
ATOM   1371 C C    . MET A 1 103 ? 0.592   15.905  22.935  1.00 13.20 ? 122 MET A C    1 
ATOM   1372 O O    . MET A 1 103 ? 0.325   14.827  23.477  1.00 13.30 ? 122 MET A O    1 
ATOM   1373 C CB   . MET A 1 103 ? -1.786  15.966  21.985  1.00 15.54 ? 122 MET A CB   1 
ATOM   1374 C CG   . MET A 1 103 ? -1.460  14.891  20.986  1.00 17.39 ? 122 MET A CG   1 
ATOM   1375 S SD   . MET A 1 103 ? -1.559  15.452  19.251  1.00 16.98 ? 122 MET A SD   1 
ATOM   1376 C CE   . MET A 1 103 ? -3.046  16.448  19.152  1.00 19.84 ? 122 MET A CE   1 
ATOM   1377 H H    . MET A 1 103 ? -0.219  17.195  20.468  1.00 15.83 ? 122 MET A H    1 
ATOM   1378 H HA   . MET A 1 103 ? -0.792  17.329  23.113  1.00 16.27 ? 122 MET A HA   1 
ATOM   1379 H HB2  . MET A 1 103 ? -2.159  15.547  22.776  1.00 18.66 ? 122 MET A HB2  1 
ATOM   1380 H HB3  . MET A 1 103 ? -2.436  16.566  21.588  1.00 18.66 ? 122 MET A HB3  1 
ATOM   1381 H HG2  . MET A 1 103 ? -0.555  14.580  21.146  1.00 20.88 ? 122 MET A HG2  1 
ATOM   1382 H HG3  . MET A 1 103 ? -2.087  14.160  21.098  1.00 20.88 ? 122 MET A HG3  1 
ATOM   1383 H HE1  . MET A 1 103 ? -3.166  16.746  18.237  1.00 23.81 ? 122 MET A HE1  1 
ATOM   1384 H HE2  . MET A 1 103 ? -3.805  15.910  19.427  1.00 23.81 ? 122 MET A HE2  1 
ATOM   1385 H HE3  . MET A 1 103 ? -2.953  17.214  19.740  1.00 23.81 ? 122 MET A HE3  1 
ATOM   1386 N N    . PHE A 1 104 ? 1.826   16.402  22.860  1.00 12.72 ? 123 PHE A N    1 
ATOM   1387 C CA   . PHE A 1 104 ? 3.004   15.784  23.445  1.00 12.47 ? 123 PHE A CA   1 
ATOM   1388 C C    . PHE A 1 104 ? 3.676   16.813  24.346  1.00 12.35 ? 123 PHE A C    1 
ATOM   1389 O O    . PHE A 1 104 ? 3.691   18.000  24.024  1.00 12.69 ? 123 PHE A O    1 
ATOM   1390 C CB   . PHE A 1 104 ? 4.012   15.381  22.336  1.00 12.48 ? 123 PHE A CB   1 
ATOM   1391 C CG   . PHE A 1 104 ? 3.522   14.277  21.445  1.00 11.83 ? 123 PHE A CG   1 
ATOM   1392 C CD1  . PHE A 1 104 ? 2.548   14.514  20.482  1.00 12.01 ? 123 PHE A CD1  1 
ATOM   1393 C CD2  . PHE A 1 104 ? 4.052   13.012  21.552  1.00 12.46 ? 123 PHE A CD2  1 
ATOM   1394 C CE1  . PHE A 1 104 ? 2.098   13.482  19.667  1.00 12.47 ? 123 PHE A CE1  1 
ATOM   1395 C CE2  . PHE A 1 104 ? 3.599   11.978  20.758  1.00 12.50 ? 123 PHE A CE2  1 
ATOM   1396 C CZ   . PHE A 1 104 ? 2.612   12.205  19.824  1.00 12.53 ? 123 PHE A CZ   1 
ATOM   1397 H H    . PHE A 1 104 ? 2.011   17.136  22.452  1.00 15.27 ? 123 PHE A H    1 
ATOM   1398 H HA   . PHE A 1 104 ? 2.759   14.996  23.956  1.00 14.97 ? 123 PHE A HA   1 
ATOM   1399 H HB2  . PHE A 1 104 ? 4.188   16.156  21.778  1.00 14.98 ? 123 PHE A HB2  1 
ATOM   1400 H HB3  . PHE A 1 104 ? 4.834   15.081  22.755  1.00 14.98 ? 123 PHE A HB3  1 
ATOM   1401 H HD1  . PHE A 1 104 ? 2.196   15.369  20.382  1.00 14.42 ? 123 PHE A HD1  1 
ATOM   1402 H HD2  . PHE A 1 104 ? 4.728   12.851  22.170  1.00 14.96 ? 123 PHE A HD2  1 
ATOM   1403 H HE1  . PHE A 1 104 ? 1.453   13.648  19.018  1.00 14.97 ? 123 PHE A HE1  1 
ATOM   1404 H HE2  . PHE A 1 104 ? 3.960   11.126  20.855  1.00 15.01 ? 123 PHE A HE2  1 
ATOM   1405 H HZ   . PHE A 1 104 ? 2.293   11.505  19.302  1.00 15.05 ? 123 PHE A HZ   1 
ATOM   1406 N N    . ALA A 1 105 ? 4.274   16.354  25.452  1.00 12.62 ? 124 ALA A N    1 
ATOM   1407 C CA   . ALA A 1 105 ? 5.153   17.220  26.229  1.00 13.89 ? 124 ALA A CA   1 
ATOM   1408 C C    . ALA A 1 105 ? 6.230   17.823  25.347  1.00 12.93 ? 124 ALA A C    1 
ATOM   1409 O O    . ALA A 1 105 ? 6.662   18.963  25.567  1.00 13.77 ? 124 ALA A O    1 
ATOM   1410 C CB   . ALA A 1 105 ? 5.831   16.411  27.334  1.00 14.47 ? 124 ALA A CB   1 
ATOM   1411 H H    . ALA A 1 105 ? 4.187   15.557  25.764  1.00 15.15 ? 124 ALA A H    1 
ATOM   1412 H HA   . ALA A 1 105 ? 4.623   17.926  26.631  1.00 16.68 ? 124 ALA A HA   1 
ATOM   1413 H HB1  . ALA A 1 105 ? 6.421   16.994  27.836  1.00 17.36 ? 124 ALA A HB1  1 
ATOM   1414 H HB2  . ALA A 1 105 ? 5.151   16.044  27.920  1.00 17.36 ? 124 ALA A HB2  1 
ATOM   1415 H HB3  . ALA A 1 105 ? 6.341   15.691  26.930  1.00 17.36 ? 124 ALA A HB3  1 
ATOM   1416 N N    . ALA A 1 106 ? 6.681   17.063  24.346  1.00 12.02 ? 125 ALA A N    1 
ATOM   1417 C CA   . ALA A 1 106 ? 7.725   17.519  23.442  1.00 12.61 ? 125 ALA A CA   1 
ATOM   1418 C C    . ALA A 1 106 ? 7.339   18.794  22.716  1.00 12.42 ? 125 ALA A C    1 
ATOM   1419 O O    . ALA A 1 106 ? 8.214   19.588  22.370  1.00 12.94 ? 125 ALA A O    1 
ATOM   1420 C CB   . ALA A 1 106 ? 7.993   16.402  22.433  1.00 13.87 ? 125 ALA A CB   1 
ATOM   1421 H H    . ALA A 1 106 ? 6.394   16.272  24.170  1.00 14.43 ? 125 ALA A H    1 
ATOM   1422 H HA   . ALA A 1 106 ? 8.532   17.712  23.945  1.00 15.14 ? 125 ALA A HA   1 
ATOM   1423 H HB1  . ALA A 1 106 ? 8.721   16.670  21.850  1.00 16.65 ? 125 ALA A HB1  1 
ATOM   1424 H HB2  . ALA A 1 106 ? 8.233   15.594  22.912  1.00 16.65 ? 125 ALA A HB2  1 
ATOM   1425 H HB3  . ALA A 1 106 ? 7.190   16.250  21.910  1.00 16.65 ? 125 ALA A HB3  1 
ATOM   1426 N N    . HIS A 1 107 ? 6.041   19.013  22.485  1.00 12.16 ? 126 HIS A N    1 
ATOM   1427 C CA   . HIS A 1 107 ? 5.602   20.188  21.738  1.00 13.05 ? 126 HIS A CA   1 
ATOM   1428 C C    . HIS A 1 107 ? 6.071   21.479  22.393  1.00 13.50 ? 126 HIS A C    1 
ATOM   1429 O O    . HIS A 1 107 ? 6.554   22.396  21.716  1.00 13.40 ? 126 HIS A O    1 
ATOM   1430 C CB   . HIS A 1 107 ? 4.083   20.151  21.616  1.00 12.59 ? 126 HIS A CB   1 
ATOM   1431 C CG   . HIS A 1 107 ? 3.504   21.366  20.985  1.00 13.25 ? 126 HIS A CG   1 
ATOM   1432 N ND1  . HIS A 1 107 ? 3.719   21.681  19.664  1.00 13.19 ? 126 HIS A ND1  1 
ATOM   1433 C CD2  . HIS A 1 107 ? 2.696   22.333  21.482  1.00 14.38 ? 126 HIS A CD2  1 
ATOM   1434 C CE1  . HIS A 1 107 ? 3.078   22.803  19.375  1.00 13.68 ? 126 HIS A CE1  1 
ATOM   1435 N NE2  . HIS A 1 107 ? 2.420   23.197  20.451  1.00 14.18 ? 126 HIS A NE2  1 
ATOM   1436 H H    . HIS A 1 107 ? 5.403   18.500  22.748  1.00 14.59 ? 126 HIS A H    1 
ATOM   1437 H HA   . HIS A 1 107 ? 5.989   20.169  20.849  1.00 15.67 ? 126 HIS A HA   1 
ATOM   1438 H HB2  . HIS A 1 107 ? 3.833   19.387  21.073  1.00 15.12 ? 126 HIS A HB2  1 
ATOM   1439 H HB3  . HIS A 1 107 ? 3.701   20.067  22.504  1.00 15.12 ? 126 HIS A HB3  1 
ATOM   1440 H HD1  . HIS A 1 107 ? 4.194   21.222  19.113  1.00 15.83 ? 126 HIS A HD1  1 
ATOM   1441 H HD2  . HIS A 1 107 ? 2.386   22.399  22.356  1.00 17.26 ? 126 HIS A HD2  1 
ATOM   1442 H HE1  . HIS A 1 107 ? 3.089   23.240  18.554  1.00 16.42 ? 126 HIS A HE1  1 
ATOM   1443 N N    . LYS A 1 108 ? 5.908   21.593  23.710  1.00 13.11 ? 127 LYS A N    1 
ATOM   1444 C CA   . LYS A 1 108 ? 6.332   22.817  24.386  1.00 13.30 ? 127 LYS A CA   1 
ATOM   1445 C C    . LYS A 1 108 ? 7.835   22.897  24.584  1.00 14.40 ? 127 LYS A C    1 
ATOM   1446 O O    . LYS A 1 108 ? 8.325   23.968  24.965  1.00 15.67 ? 127 LYS A O    1 
ATOM   1447 C CB   . LYS A 1 108 ? 5.540   23.005  25.682  1.00 13.92 ? 127 LYS A CB   1 
ATOM   1448 C CG   . LYS A 1 108 ? 4.121   23.550  25.393  1.00 14.66 ? 127 LYS A CG   1 
ATOM   1449 C CD   . LYS A 1 108 ? 3.222   23.535  26.629  1.00 14.75 ? 127 LYS A CD   1 
ATOM   1450 C CE   . LYS A 1 108 ? 1.868   24.102  26.313  1.00 15.59 ? 127 LYS A CE   1 
ATOM   1451 N NZ   . LYS A 1 108 ? 0.954   24.104  27.487  1.00 16.32 ? 127 LYS A NZ   1 
ATOM   1452 H H    . LYS A 1 108 ? 5.564   20.993  24.220  1.00 15.74 ? 127 LYS A H    1 
ATOM   1453 H HA   . LYS A 1 108 ? 6.109   23.588  23.841  1.00 15.96 ? 127 LYS A HA   1 
ATOM   1454 H HB2  . LYS A 1 108 ? 5.456   22.151  26.134  1.00 16.71 ? 127 LYS A HB2  1 
ATOM   1455 H HB3  . LYS A 1 108 ? 6.003   23.639  26.253  1.00 16.71 ? 127 LYS A HB3  1 
ATOM   1456 H HG2  . LYS A 1 108 ? 4.190   24.467  25.084  1.00 17.60 ? 127 LYS A HG2  1 
ATOM   1457 H HG3  . LYS A 1 108 ? 3.703   23.001  24.711  1.00 17.60 ? 127 LYS A HG3  1 
ATOM   1458 H HD2  . LYS A 1 108 ? 3.109   22.622  26.935  1.00 17.71 ? 127 LYS A HD2  1 
ATOM   1459 H HD3  . LYS A 1 108 ? 3.625   24.072  27.329  1.00 17.71 ? 127 LYS A HD3  1 
ATOM   1460 H HE2  . LYS A 1 108 ? 1.972   25.019  26.013  1.00 18.71 ? 127 LYS A HE2  1 
ATOM   1461 H HE3  . LYS A 1 108 ? 1.457   23.569  25.614  1.00 18.71 ? 127 LYS A HE3  1 
ATOM   1462 H HZ1  . LYS A 1 108 ? 1.315   24.570  28.153  1.00 19.59 ? 127 LYS A HZ1  1 
ATOM   1463 H HZ2  . LYS A 1 108 ? 0.811   23.270  27.763  1.00 19.59 ? 127 LYS A HZ2  1 
ATOM   1464 H HZ3  . LYS A 1 108 ? 0.174   24.472  27.265  1.00 19.59 ? 127 LYS A HZ3  1 
ATOM   1465 N N    . GLU A 1 109 ? 8.570   21.819  24.297  1.00 14.00 ? 128 GLU A N    1 
ATOM   1466 C CA   . GLU A 1 109 ? 10.024  21.912  24.207  1.00 14.05 ? 128 GLU A CA   1 
ATOM   1467 C C    . GLU A 1 109 ? 10.436  22.502  22.860  1.00 13.75 ? 128 GLU A C    1 
ATOM   1468 O O    . GLU A 1 109 ? 11.248  23.432  22.789  1.00 14.56 ? 128 GLU A O    1 
ATOM   1469 C CB   . GLU A 1 109 ? 10.677  20.541  24.360  1.00 14.26 ? 128 GLU A CB   1 
ATOM   1470 C CG   . GLU A 1 109 ? 10.444  19.874  25.697  1.00 14.39 ? 128 GLU A CG   1 
ATOM   1471 C CD   . GLU A 1 109 ? 11.138  18.519  25.842  1.00 18.02 ? 128 GLU A CD   1 
ATOM   1472 O OE1  . GLU A 1 109 ? 12.109  18.243  25.121  1.00 18.96 ? 128 GLU A OE1  1 
ATOM   1473 O OE2  . GLU A 1 109 ? 10.707  17.736  26.711  1.00 20.80 ? 128 GLU A OE2  1 
ATOM   1474 H H    . GLU A 1 109 ? 8.253   21.032  24.153  1.00 16.80 ? 128 GLU A H    1 
ATOM   1475 H HA   . GLU A 1 109 ? 10.334  22.478  24.932  1.00 16.87 ? 128 GLU A HA   1 
ATOM   1476 H HB2  . GLU A 1 109 ? 10.322  19.953  23.675  1.00 17.12 ? 128 GLU A HB2  1 
ATOM   1477 H HB3  . GLU A 1 109 ? 11.635  20.642  24.248  1.00 17.12 ? 128 GLU A HB3  1 
ATOM   1478 H HG2  . GLU A 1 109 ? 10.780  20.454  26.398  1.00 17.28 ? 128 GLU A HG2  1 
ATOM   1479 H HG3  . GLU A 1 109 ? 9.491   19.732  25.813  1.00 17.28 ? 128 GLU A HG3  1 
ATOM   1480 N N    . TYR A 1 110 ? 9.872   21.965  21.772  1.00 12.78 ? 129 TYR A N    1 
ATOM   1481 C CA   . TYR A 1 110 ? 10.172  22.473  20.440  1.00 13.17 ? 129 TYR A CA   1 
ATOM   1482 C C    . TYR A 1 110 ? 9.854   23.950  20.339  1.00 14.22 ? 129 TYR A C    1 
ATOM   1483 O O    . TYR A 1 110 ? 10.549  24.675  19.624  1.00 13.70 ? 129 TYR A O    1 
ATOM   1484 C CB   . TYR A 1 110 ? 9.364   21.659  19.420  1.00 12.17 ? 129 TYR A CB   1 
ATOM   1485 C CG   . TYR A 1 110 ? 9.700   22.003  17.994  1.00 12.81 ? 129 TYR A CG   1 
ATOM   1486 C CD1  . TYR A 1 110 ? 10.884  21.543  17.406  1.00 12.69 ? 129 TYR A CD1  1 
ATOM   1487 C CD2  . TYR A 1 110 ? 8.866   22.798  17.223  1.00 12.22 ? 129 TYR A CD2  1 
ATOM   1488 C CE1  . TYR A 1 110 ? 11.219  21.873  16.099  1.00 13.63 ? 129 TYR A CE1  1 
ATOM   1489 C CE2  . TYR A 1 110 ? 9.189   23.104  15.911  1.00 13.61 ? 129 TYR A CE2  1 
ATOM   1490 C CZ   . TYR A 1 110 ? 10.369  22.652  15.357  1.00 12.79 ? 129 TYR A CZ   1 
ATOM   1491 O OH   . TYR A 1 110 ? 10.724  22.960  14.065  1.00 13.71 ? 129 TYR A OH   1 
ATOM   1492 H H    . TYR A 1 110 ? 9.315   21.309  21.782  1.00 15.34 ? 129 TYR A H    1 
ATOM   1493 H HA   . TYR A 1 110 ? 11.115  22.367  20.238  1.00 15.81 ? 129 TYR A HA   1 
ATOM   1494 H HB2  . TYR A 1 110 ? 9.549   20.716  19.551  1.00 14.61 ? 129 TYR A HB2  1 
ATOM   1495 H HB3  . TYR A 1 110 ? 8.419   21.833  19.555  1.00 14.61 ? 129 TYR A HB3  1 
ATOM   1496 H HD1  . TYR A 1 110 ? 11.458  21.005  17.901  1.00 15.24 ? 129 TYR A HD1  1 
ATOM   1497 H HD2  . TYR A 1 110 ? 8.079   23.131  17.592  1.00 14.67 ? 129 TYR A HD2  1 
ATOM   1498 H HE1  . TYR A 1 110 ? 12.015  21.568  15.729  1.00 16.36 ? 129 TYR A HE1  1 
ATOM   1499 H HE2  . TYR A 1 110 ? 8.606   23.618  15.400  1.00 16.34 ? 129 TYR A HE2  1 
ATOM   1500 H HH   . TYR A 1 110 ? 10.041  23.159  13.619  1.00 16.46 ? 129 TYR A HH   1 
ATOM   1501 N N    . ALA A 1 111 ? 8.826   24.406  21.064  1.00 14.27 ? 130 ALA A N    1 
ATOM   1502 C CA   . ALA A 1 111 ? 8.409   25.798  21.095  1.00 14.11 ? 130 ALA A CA   1 
ATOM   1503 C C    . ALA A 1 111 ? 9.500   26.727  21.580  1.00 14.51 ? 130 ALA A C    1 
ATOM   1504 O O    . ALA A 1 111 ? 9.426   27.932  21.318  1.00 15.39 ? 130 ALA A O    1 
ATOM   1505 C CB   . ALA A 1 111 ? 7.195   25.914  22.019  1.00 14.66 ? 130 ALA A CB   1 
ATOM   1506 H H    . ALA A 1 111 ? 8.338   23.904  21.565  1.00 17.13 ? 130 ALA A H    1 
ATOM   1507 H HA   . ALA A 1 111 ? 8.170   26.081  20.198  1.00 16.94 ? 130 ALA A HA   1 
ATOM   1508 H HB1  . ALA A 1 111 ? 6.929   26.845  22.076  1.00 17.60 ? 130 ALA A HB1  1 
ATOM   1509 H HB2  . ALA A 1 111 ? 6.470   25.383  21.655  1.00 17.60 ? 130 ALA A HB2  1 
ATOM   1510 H HB3  . ALA A 1 111 ? 7.436   25.584  22.899  1.00 17.60 ? 130 ALA A HB3  1 
ATOM   1511 N N    . LYS A 1 112 ? 10.510  26.204  22.276  1.00 14.52 ? 131 LYS A N    1 
ATOM   1512 C CA   . LYS A 1 112 ? 11.553  27.032  22.870  1.00 15.58 ? 131 LYS A CA   1 
ATOM   1513 C C    . LYS A 1 112 ? 12.821  27.085  22.021  1.00 16.41 ? 131 LYS A C    1 
ATOM   1514 O O    . LYS A 1 112 ? 13.838  27.626  22.480  1.00 17.55 ? 131 LYS A O    1 
ATOM   1515 C CB   . LYS A 1 112 ? 11.893  26.542  24.280  1.00 16.05 ? 131 LYS A CB   1 
ATOM   1516 C CG   . LYS A 1 112 ? 10.702  26.227  25.174  1.00 15.72 ? 131 LYS A CG   1 
ATOM   1517 C CD   . LYS A 1 112 ? 9.819   27.440  25.450  1.00 15.96 ? 131 LYS A CD   1 
ATOM   1518 C CE   . LYS A 1 112 ? 8.443   27.015  25.997  1.00 15.69 ? 131 LYS A CE   1 
ATOM   1519 N NZ   . LYS A 1 112 ? 8.519   25.989  27.082  1.00 15.05 ? 131 LYS A NZ   1 
ATOM   1520 H H    . LYS A 1 112 ? 10.612  25.361  22.417  1.00 17.43 ? 131 LYS A H    1 
ATOM   1521 H HA   . LYS A 1 112 ? 11.208  27.935  22.948  1.00 18.71 ? 131 LYS A HA   1 
ATOM   1522 H HB2  . LYS A 1 112 ? 12.417  25.729  24.202  1.00 19.27 ? 131 LYS A HB2  1 
ATOM   1523 H HB3  . LYS A 1 112 ? 12.413  27.230  24.725  1.00 19.27 ? 131 LYS A HB3  1 
ATOM   1524 H HG2  . LYS A 1 112 ? 10.154  25.552  24.743  1.00 18.87 ? 131 LYS A HG2  1 
ATOM   1525 H HG3  . LYS A 1 112 ? 11.026  25.895  26.026  1.00 18.87 ? 131 LYS A HG3  1 
ATOM   1526 H HD2  . LYS A 1 112 ? 10.248  28.008  26.109  1.00 19.16 ? 131 LYS A HD2  1 
ATOM   1527 H HD3  . LYS A 1 112 ? 9.682   27.933  24.626  1.00 19.16 ? 131 LYS A HD3  1 
ATOM   1528 H HE2  . LYS A 1 112 ? 7.996   27.796  26.359  1.00 18.83 ? 131 LYS A HE2  1 
ATOM   1529 H HE3  . LYS A 1 112 ? 7.920   26.641  25.271  1.00 18.83 ? 131 LYS A HE3  1 
ATOM   1530 H HZ1  . LYS A 1 112 ? 9.042   26.280  27.740  1.00 18.07 ? 131 LYS A HZ1  1 
ATOM   1531 H HZ2  . LYS A 1 112 ? 7.706   25.831  27.408  1.00 18.07 ? 131 LYS A HZ2  1 
ATOM   1532 H HZ3  . LYS A 1 112 ? 8.854   25.231  26.760  1.00 18.07 ? 131 LYS A HZ3  1 
ATOM   1533 N N    . HIS A 1 113 ? 12.791  26.538  20.801  1.00 16.48 ? 132 HIS A N    1 
ATOM   1534 C CA   . HIS A 1 113 ? 13.967  26.461  19.934  1.00 16.28 ? 132 HIS A CA   1 
ATOM   1535 C C    . HIS A 1 113 ? 13.672  27.063  18.572  1.00 17.18 ? 132 HIS A C    1 
ATOM   1536 O O    . HIS A 1 113 ? 13.786  26.390  17.538  1.00 15.08 ? 132 HIS A O    1 
ATOM   1537 C CB   . HIS A 1 113 ? 14.407  25.012  19.786  1.00 17.47 ? 132 HIS A CB   1 
ATOM   1538 C CG   . HIS A 1 113 ? 14.906  24.419  21.056  1.00 18.77 ? 132 HIS A CG   1 
ATOM   1539 N ND1  . HIS A 1 113 ? 16.203  24.579  21.493  1.00 20.25 ? 132 HIS A ND1  1 
ATOM   1540 C CD2  . HIS A 1 113 ? 14.269  23.703  22.010  1.00 19.52 ? 132 HIS A CD2  1 
ATOM   1541 C CE1  . HIS A 1 113 ? 16.352  23.949  22.644  1.00 21.51 ? 132 HIS A CE1  1 
ATOM   1542 N NE2  . HIS A 1 113 ? 15.195  23.409  22.980  1.00 21.83 ? 132 HIS A NE2  1 
ATOM   1543 H H    . HIS A 1 113 ? 12.084  26.197  20.449  1.00 19.78 ? 132 HIS A H    1 
ATOM   1544 H HA   . HIS A 1 113 ? 14.681  26.980  20.336  1.00 19.54 ? 132 HIS A HA   1 
ATOM   1545 H HB2  . HIS A 1 113 ? 13.651  24.483  19.487  1.00 20.97 ? 132 HIS A HB2  1 
ATOM   1546 H HB3  . HIS A 1 113 ? 15.123  24.966  19.133  1.00 20.97 ? 132 HIS A HB3  1 
ATOM   1547 H HD2  . HIS A 1 113 ? 13.372  23.457  22.009  1.00 23.43 ? 132 HIS A HD2  1 
ATOM   1548 H HE1  . HIS A 1 113 ? 17.139  23.896  23.136  1.00 25.82 ? 132 HIS A HE1  1 
ATOM   1549 H HE2  . HIS A 1 113 ? 15.046  22.947  23.690  1.00 26.20 ? 132 HIS A HE2  1 
ATOM   1550 N N    . PRO A 1 114 ? 13.326  28.353  18.532  1.00 17.20 ? 133 PRO A N    1 
ATOM   1551 C CA   . PRO A 1 114 ? 12.992  28.982  17.243  1.00 17.98 ? 133 PRO A CA   1 
ATOM   1552 C C    . PRO A 1 114 ? 14.137  28.984  16.256  1.00 17.59 ? 133 PRO A C    1 
ATOM   1553 O O    . PRO A 1 114 ? 13.901  29.099  15.056  1.00 17.08 ? 133 PRO A O    1 
ATOM   1554 C CB   . PRO A 1 114 ? 12.577  30.407  17.641  1.00 19.93 ? 133 PRO A CB   1 
ATOM   1555 C CG   . PRO A 1 114 ? 13.277  30.635  18.970  1.00 20.05 ? 133 PRO A CG   1 
ATOM   1556 C CD   . PRO A 1 114 ? 13.213  29.301  19.660  1.00 18.35 ? 133 PRO A CD   1 
ATOM   1557 H HA   . PRO A 1 114 ? 12.231  28.535  16.841  1.00 21.59 ? 133 PRO A HA   1 
ATOM   1558 H HB2  . PRO A 1 114 ? 12.878  31.042  16.973  1.00 23.92 ? 133 PRO A HB2  1 
ATOM   1559 H HB3  . PRO A 1 114 ? 11.613  30.460  17.739  1.00 23.92 ? 133 PRO A HB3  1 
ATOM   1560 H HG2  . PRO A 1 114 ? 14.196  30.906  18.819  1.00 24.07 ? 133 PRO A HG2  1 
ATOM   1561 H HG3  . PRO A 1 114 ? 12.810  31.315  19.480  1.00 24.07 ? 133 PRO A HG3  1 
ATOM   1562 H HD2  . PRO A 1 114 ? 13.951  29.193  20.280  1.00 22.03 ? 133 PRO A HD2  1 
ATOM   1563 H HD3  . PRO A 1 114 ? 12.369  29.189  20.125  1.00 22.03 ? 133 PRO A HD3  1 
ATOM   1564 N N    . GLN A 1 115 ? 15.373  28.817  16.723  1.00 18.02 ? 134 GLN A N    1 
ATOM   1565 C CA   . GLN A 1 115 ? 16.514  28.710  15.820  1.00 18.71 ? 134 GLN A CA   1 
ATOM   1566 C C    . GLN A 1 115 ? 16.403  27.504  14.901  1.00 17.16 ? 134 GLN A C    1 
ATOM   1567 O O    . GLN A 1 115 ? 17.071  27.469  13.862  1.00 18.78 ? 134 GLN A O    1 
ATOM   1568 C CB   . GLN A 1 115 ? 17.765  28.545  16.688  1.00 22.37 ? 134 GLN A CB   1 
ATOM   1569 C CG   . GLN A 1 115 ? 17.658  27.314  17.622  1.00 26.56 ? 134 GLN A CG   1 
ATOM   1570 C CD   . GLN A 1 115 ? 17.368  27.643  19.083  1.00 27.34 ? 134 GLN A CD   1 
ATOM   1571 O OE1  . GLN A 1 115 ? 16.588  28.541  19.373  1.00 23.93 ? 134 GLN A OE1  1 
ATOM   1572 N NE2  . GLN A 1 115 ? 17.952  26.857  20.012  1.00 28.75 ? 134 GLN A NE2  1 
ATOM   1573 H H    . GLN A 1 115 ? 15.577  28.763  17.556  1.00 21.63 ? 134 GLN A H    1 
ATOM   1574 H HA   . GLN A 1 115 ? 16.579  29.505  15.268  1.00 22.46 ? 134 GLN A HA   1 
ATOM   1575 H HB2  . GLN A 1 115 ? 18.538  28.425  16.114  1.00 26.85 ? 134 GLN A HB2  1 
ATOM   1576 H HB3  . GLN A 1 115 ? 17.879  29.336  17.238  1.00 26.85 ? 134 GLN A HB3  1 
ATOM   1577 H HG2  . GLN A 1 115 ? 16.938  26.747  17.304  1.00 31.88 ? 134 GLN A HG2  1 
ATOM   1578 H HG3  . GLN A 1 115 ? 18.498  26.831  17.594  1.00 31.88 ? 134 GLN A HG3  1 
ATOM   1579 H HE21 . GLN A 1 115 ? 18.459  26.207  19.768  1.00 34.51 ? 134 GLN A HE21 1 
ATOM   1580 H HE22 . GLN A 1 115 ? 17.816  27.007  20.848  1.00 34.51 ? 134 GLN A HE22 1 
ATOM   1581 N N    . TRP A 1 116 ? 15.588  26.506  15.268  1.00 15.08 ? 135 TRP A N    1 
ATOM   1582 C CA   . TRP A 1 116 ? 15.406  25.319  14.454  1.00 15.54 ? 135 TRP A CA   1 
ATOM   1583 C C    . TRP A 1 116 ? 14.279  25.441  13.444  1.00 14.64 ? 135 TRP A C    1 
ATOM   1584 O O    . TRP A 1 116 ? 14.217  24.644  12.504  1.00 14.33 ? 135 TRP A O    1 
ATOM   1585 C CB   . TRP A 1 116 ? 15.056  24.094  15.304  1.00 15.60 ? 135 TRP A CB   1 
ATOM   1586 C CG   . TRP A 1 116 ? 16.037  23.785  16.375  1.00 15.59 ? 135 TRP A CG   1 
ATOM   1587 C CD1  . TRP A 1 116 ? 17.332  24.207  16.451  1.00 15.98 ? 135 TRP A CD1  1 
ATOM   1588 C CD2  . TRP A 1 116 ? 15.836  22.906  17.478  1.00 14.96 ? 135 TRP A CD2  1 
ATOM   1589 N NE1  . TRP A 1 116 ? 17.928  23.683  17.566  1.00 16.12 ? 135 TRP A NE1  1 
ATOM   1590 C CE2  . TRP A 1 116 ? 17.036  22.865  18.205  1.00 15.78 ? 135 TRP A CE2  1 
ATOM   1591 C CE3  . TRP A 1 116 ? 14.752  22.141  17.925  1.00 15.37 ? 135 TRP A CE3  1 
ATOM   1592 C CZ2  . TRP A 1 116 ? 17.171  22.128  19.373  1.00 16.30 ? 135 TRP A CZ2  1 
ATOM   1593 C CZ3  . TRP A 1 116 ? 14.897  21.406  19.067  1.00 16.36 ? 135 TRP A CZ3  1 
ATOM   1594 C CH2  . TRP A 1 116 ? 16.096  21.399  19.775  1.00 16.70 ? 135 TRP A CH2  1 
ATOM   1595 H H    . TRP A 1 116 ? 15.129  26.502  15.995  1.00 18.11 ? 135 TRP A H    1 
ATOM   1596 H HA   . TRP A 1 116 ? 16.253  25.173  14.004  1.00 18.65 ? 135 TRP A HA   1 
ATOM   1597 H HB2  . TRP A 1 116 ? 14.198  24.248  15.729  1.00 18.72 ? 135 TRP A HB2  1 
ATOM   1598 H HB3  . TRP A 1 116 ? 15.004  23.319  14.723  1.00 18.72 ? 135 TRP A HB3  1 
ATOM   1599 H HD1  . TRP A 1 116 ? 17.748  24.768  15.837  1.00 19.18 ? 135 TRP A HD1  1 
ATOM   1600 H HE1  . TRP A 1 116 ? 18.733  23.842  17.824  1.00 19.36 ? 135 TRP A HE1  1 
ATOM   1601 H HE3  . TRP A 1 116 ? 13.950  22.133  17.454  1.00 18.45 ? 135 TRP A HE3  1 
ATOM   1602 H HZ2  . TRP A 1 116 ? 17.964  22.132  19.860  1.00 19.57 ? 135 TRP A HZ2  1 
ATOM   1603 H HZ3  . TRP A 1 116 ? 14.181  20.901  19.378  1.00 19.64 ? 135 TRP A HZ3  1 
ATOM   1604 H HH2  . TRP A 1 116 ? 16.163  20.881  20.544  1.00 20.04 ? 135 TRP A HH2  1 
ATOM   1605 N N    . TRP A 1 117 ? 13.367  26.387  13.632  1.00 14.03 ? 136 TRP A N    1 
ATOM   1606 C CA   . TRP A 1 117 ? 12.089  26.321  12.935  1.00 12.86 ? 136 TRP A CA   1 
ATOM   1607 C C    . TRP A 1 117 ? 12.251  26.513  11.431  1.00 13.82 ? 136 TRP A C    1 
ATOM   1608 O O    . TRP A 1 117 ? 13.036  27.336  10.962  1.00 15.15 ? 136 TRP A O    1 
ATOM   1609 C CB   . TRP A 1 117 ? 11.154  27.391  13.482  1.00 13.22 ? 136 TRP A CB   1 
ATOM   1610 C CG   . TRP A 1 117 ? 10.729  27.190  14.908  1.00 13.65 ? 136 TRP A CG   1 
ATOM   1611 C CD1  . TRP A 1 117 ? 11.012  26.132  15.726  1.00 13.37 ? 136 TRP A CD1  1 
ATOM   1612 C CD2  . TRP A 1 117 ? 9.952   28.096  15.681  1.00 13.50 ? 136 TRP A CD2  1 
ATOM   1613 N NE1  . TRP A 1 117 ? 10.455  26.331  16.978  1.00 14.10 ? 136 TRP A NE1  1 
ATOM   1614 C CE2  . TRP A 1 117 ? 9.786   27.533  16.960  1.00 14.16 ? 136 TRP A CE2  1 
ATOM   1615 C CE3  . TRP A 1 117 ? 9.366   29.334  15.411  1.00 15.23 ? 136 TRP A CE3  1 
ATOM   1616 C CZ2  . TRP A 1 117 ? 9.065   28.189  17.970  1.00 15.94 ? 136 TRP A CZ2  1 
ATOM   1617 C CZ3  . TRP A 1 117 ? 8.649   29.962  16.399  1.00 16.16 ? 136 TRP A CZ3  1 
ATOM   1618 C CH2  . TRP A 1 117 ? 8.496   29.387  17.660  1.00 17.26 ? 136 TRP A CH2  1 
ATOM   1619 H H    . TRP A 1 117 ? 13.462  27.067  14.149  1.00 16.84 ? 136 TRP A H    1 
ATOM   1620 H HA   . TRP A 1 117 ? 11.701  25.443  13.079  1.00 15.43 ? 136 TRP A HA   1 
ATOM   1621 H HB2  . TRP A 1 117 ? 11.605  28.249  13.431  1.00 15.88 ? 136 TRP A HB2  1 
ATOM   1622 H HB3  . TRP A 1 117 ? 10.351  27.405  12.938  1.00 15.88 ? 136 TRP A HB3  1 
ATOM   1623 H HD1  . TRP A 1 117 ? 11.508  25.386  15.478  1.00 16.05 ? 136 TRP A HD1  1 
ATOM   1624 H HE1  . TRP A 1 117 ? 10.517  25.797  17.649  1.00 16.93 ? 136 TRP A HE1  1 
ATOM   1625 H HE3  . TRP A 1 117 ? 9.461   29.728  14.574  1.00 18.28 ? 136 TRP A HE3  1 
ATOM   1626 H HZ2  . TRP A 1 117 ? 8.979   27.819  18.819  1.00 19.13 ? 136 TRP A HZ2  1 
ATOM   1627 H HZ3  . TRP A 1 117 ? 8.257   30.787  16.224  1.00 19.40 ? 136 TRP A HZ3  1 
ATOM   1628 H HH2  . TRP A 1 117 ? 7.995   29.832  18.305  1.00 20.72 ? 136 TRP A HH2  1 
ATOM   1629 N N    . LEU A 1 118 ? 11.456  25.762  10.680  1.00 13.87 ? 137 LEU A N    1 
ATOM   1630 C CA   . LEU A 1 118 ? 11.523  25.768  9.228   1.00 14.62 ? 137 LEU A CA   1 
ATOM   1631 C C    . LEU A 1 118 ? 10.742  26.944  8.667   1.00 14.76 ? 137 LEU A C    1 
ATOM   1632 O O    . LEU A 1 118 ? 9.614   27.237  9.099   1.00 14.02 ? 137 LEU A O    1 
ATOM   1633 C CB   . LEU A 1 118 ? 10.925  24.468  8.696   1.00 14.62 ? 137 LEU A CB   1 
ATOM   1634 C CG   . LEU A 1 118 ? 10.959  24.267  7.182   1.00 15.01 ? 137 LEU A CG   1 
ATOM   1635 C CD1  . LEU A 1 118 ? 12.378  24.297  6.598   1.00 15.97 ? 137 LEU A CD1  1 
ATOM   1636 C CD2  . LEU A 1 118 ? 10.277  22.936  6.869   1.00 15.70 ? 137 LEU A CD2  1 
ATOM   1637 H H    . LEU A 1 118 ? 10.858  25.230  10.994  1.00 16.65 ? 137 LEU A H    1 
ATOM   1638 H HA   . LEU A 1 118 ? 12.446  25.845  8.938   1.00 17.55 ? 137 LEU A HA   1 
ATOM   1639 H HB2  . LEU A 1 118 ? 11.413  23.729  9.092   1.00 17.55 ? 137 LEU A HB2  1 
ATOM   1640 H HB3  . LEU A 1 118 ? 9.994   24.434  8.967   1.00 17.55 ? 137 LEU A HB3  1 
ATOM   1641 H HG   . LEU A 1 118 ? 10.491  25.002  6.756   1.00 18.02 ? 137 LEU A HG   1 
ATOM   1642 H HD11 . LEU A 1 118 ? 12.328  24.171  5.638   1.00 19.17 ? 137 LEU A HD11 1 
ATOM   1643 H HD12 . LEU A 1 118 ? 12.784  25.155  6.799   1.00 19.17 ? 137 LEU A HD12 1 
ATOM   1644 H HD13 . LEU A 1 118 ? 12.899  23.583  6.998   1.00 19.17 ? 137 LEU A HD13 1 
ATOM   1645 H HD21 . LEU A 1 118 ? 10.315  22.779  5.913   1.00 18.85 ? 137 LEU A HD21 1 
ATOM   1646 H HD22 . LEU A 1 118 ? 10.741  22.225  7.339   1.00 18.85 ? 137 LEU A HD22 1 
ATOM   1647 H HD23 . LEU A 1 118 ? 9.353   22.978  7.161   1.00 18.85 ? 137 LEU A HD23 1 
ATOM   1648 N N    . ARG A 1 119 ? 11.348  27.614  7.696   1.00 14.46 ? 138 ARG A N    1 
ATOM   1649 C CA   . ARG A 1 119 ? 10.728  28.735  7.011   1.00 14.58 ? 138 ARG A CA   1 
ATOM   1650 C C    . ARG A 1 119 ? 10.657  28.495  5.509   1.00 14.35 ? 138 ARG A C    1 
ATOM   1651 O O    . ARG A 1 119 ? 11.384  27.676  4.945   1.00 15.44 ? 138 ARG A O    1 
ATOM   1652 C CB   . ARG A 1 119 ? 11.498  30.032  7.286   1.00 16.27 ? 138 ARG A CB   1 
ATOM   1653 C CG   . ARG A 1 119 ? 11.402  30.436  8.755   1.00 16.42 ? 138 ARG A CG   1 
ATOM   1654 C CD   . ARG A 1 119 ? 12.232  31.654  9.111   1.00 17.42 ? 138 ARG A CD   1 
ATOM   1655 N NE   . ARG A 1 119 ? 12.334  31.753  10.565  1.00 17.43 ? 138 ARG A NE   1 
ATOM   1656 C CZ   . ARG A 1 119 ? 11.387  32.237  11.357  1.00 16.91 ? 138 ARG A CZ   1 
ATOM   1657 N NH1  . ARG A 1 119 ? 10.299  32.807  10.871  1.00 16.31 ? 138 ARG A NH1  1 
ATOM   1658 N NH2  . ARG A 1 119 ? 11.526  32.130  12.674  1.00 17.83 ? 138 ARG A NH2  1 
ATOM   1659 H H    . ARG A 1 119 ? 12.139  27.433  7.410   1.00 17.36 ? 138 ARG A H    1 
ATOM   1660 H HA   . ARG A 1 119 ? 9.817   28.827  7.332   1.00 17.50 ? 138 ARG A HA   1 
ATOM   1661 H HB2  . ARG A 1 119 ? 12.433  29.903  7.064   1.00 19.53 ? 138 ARG A HB2  1 
ATOM   1662 H HB3  . ARG A 1 119 ? 11.125  30.747  6.746   1.00 19.53 ? 138 ARG A HB3  1 
ATOM   1663 H HG2  . ARG A 1 119 ? 10.476  30.639  8.964   1.00 19.71 ? 138 ARG A HG2  1 
ATOM   1664 H HG3  . ARG A 1 119 ? 11.711  29.698  9.303   1.00 19.71 ? 138 ARG A HG3  1 
ATOM   1665 H HD2  . ARG A 1 119 ? 13.123  31.567  8.737   1.00 20.91 ? 138 ARG A HD2  1 
ATOM   1666 H HD3  . ARG A 1 119 ? 11.805  32.455  8.769   1.00 20.91 ? 138 ARG A HD3  1 
ATOM   1667 H HE   . ARG A 1 119 ? 13.060  31.478  10.933  1.00 20.92 ? 138 ARG A HE   1 
ATOM   1668 H HH11 . ARG A 1 119 ? 10.191  32.871  10.020  1.00 19.58 ? 138 ARG A HH11 1 
ATOM   1669 H HH12 . ARG A 1 119 ? 9.699   33.113  11.405  1.00 19.58 ? 138 ARG A HH12 1 
ATOM   1670 H HH21 . ARG A 1 119 ? 12.224  31.750  13.003  1.00 21.40 ? 138 ARG A HH21 1 
ATOM   1671 H HH22 . ARG A 1 119 ? 10.918  32.440  13.197  1.00 21.40 ? 138 ARG A HH22 1 
ATOM   1672 N N    . THR A 1 120 ? 9.733   29.202  4.872   1.00 13.98 ? 139 THR A N    1 
ATOM   1673 C CA   . THR A 1 120 ? 9.721   29.232  3.425   1.00 13.40 ? 139 THR A CA   1 
ATOM   1674 C C    . THR A 1 120 ? 10.780  30.220  2.934   1.00 13.42 ? 139 THR A C    1 
ATOM   1675 O O    . THR A 1 120 ? 11.396  30.959  3.710   1.00 14.14 ? 139 THR A O    1 
ATOM   1676 C CB   . THR A 1 120 ? 8.368   29.703  2.902   1.00 15.02 ? 139 THR A CB   1 
ATOM   1677 O OG1  . THR A 1 120 ? 8.248   31.111  3.151   1.00 15.94 ? 139 THR A OG1  1 
ATOM   1678 C CG2  . THR A 1 120 ? 7.218   28.935  3.560   1.00 15.90 ? 139 THR A CG2  1 
ATOM   1679 H H    . THR A 1 120 ? 9.115   29.664  5.252   1.00 16.78 ? 139 THR A H    1 
ATOM   1680 H HA   . THR A 1 120 ? 9.900   28.333  3.107   1.00 16.09 ? 139 THR A HA   1 
ATOM   1681 H HB   . THR A 1 120 ? 8.301   29.536  1.949   1.00 18.03 ? 139 THR A HB   1 
ATOM   1682 H HG1  . THR A 1 120 ? 7.474   31.372  2.954   1.00 19.13 ? 139 THR A HG1  1 
ATOM   1683 H HG21 . THR A 1 120 ? 6.369   29.234  3.198   1.00 19.09 ? 139 THR A HG21 1 
ATOM   1684 H HG22 . THR A 1 120 ? 7.315   27.985  3.392   1.00 19.09 ? 139 THR A HG22 1 
ATOM   1685 H HG23 . THR A 1 120 ? 7.222   29.087  4.518   1.00 19.09 ? 139 THR A HG23 1 
ATOM   1686 N N    . THR A 1 121 ? 10.921  30.310  1.610   1.00 12.94 ? 140 THR A N    1 
ATOM   1687 C CA   . THR A 1 121 ? 11.904  31.222  1.039   1.00 13.38 ? 140 THR A CA   1 
ATOM   1688 C C    . THR A 1 121 ? 11.664  32.672  1.468   1.00 14.20 ? 140 THR A C    1 
ATOM   1689 O O    . THR A 1 121 ? 12.609  33.477  1.463   1.00 16.06 ? 140 THR A O    1 
ATOM   1690 C CB   . THR A 1 121 ? 11.873  31.156  -0.492  1.00 13.11 ? 140 THR A CB   1 
ATOM   1691 O OG1  . THR A 1 121 ? 10.594  31.590  -0.965  1.00 13.37 ? 140 THR A OG1  1 
ATOM   1692 C CG2  . THR A 1 121 ? 12.181  29.791  -1.036  1.00 13.98 ? 140 THR A CG2  1 
ATOM   1693 H H    . THR A 1 121 ? 10.466  29.863  1.033   1.00 15.53 ? 140 THR A H    1 
ATOM   1694 H HA   . THR A 1 121 ? 12.778  30.941  1.353   1.00 16.06 ? 140 THR A HA   1 
ATOM   1695 H HB   . THR A 1 121 ? 12.570  31.741  -0.827  1.00 15.74 ? 140 THR A HB   1 
ATOM   1696 H HG1  . THR A 1 121 ? 10.514  31.411  -1.782  1.00 16.05 ? 140 THR A HG1  1 
ATOM   1697 H HG21 . THR A 1 121 ? 12.171  29.811  -2.005  1.00 16.78 ? 140 THR A HG21 1 
ATOM   1698 H HG22 . THR A 1 121 ? 13.057  29.505  -0.735  1.00 16.78 ? 140 THR A HG22 1 
ATOM   1699 H HG23 . THR A 1 121 ? 11.518  29.154  -0.727  1.00 16.78 ? 140 THR A HG23 1 
ATOM   1700 N N    . THR A 1 122 ? 10.418  33.035  1.812   1.00 14.55 ? 141 THR A N    1 
ATOM   1701 C CA   . THR A 1 122 ? 10.114  34.413  2.186   1.00 17.42 ? 141 THR A CA   1 
ATOM   1702 C C    . THR A 1 122 ? 10.370  34.705  3.664   1.00 17.50 ? 141 THR A C    1 
ATOM   1703 O O    . THR A 1 122 ? 10.247  35.863  4.083   1.00 19.38 ? 141 THR A O    1 
ATOM   1704 C CB   . THR A 1 122 ? 8.642   34.742  1.903   1.00 18.69 ? 141 THR A CB   1 
ATOM   1705 O OG1  . THR A 1 122 ? 7.812   34.048  2.848   1.00 19.11 ? 141 THR A OG1  1 
ATOM   1706 C CG2  . THR A 1 122 ? 8.248   34.393  0.490   1.00 19.65 ? 141 THR A CG2  1 
ATOM   1707 H H    . THR A 1 122 ? 9.743   32.503  1.835   1.00 17.47 ? 141 THR A H    1 
ATOM   1708 H HA   . THR A 1 122 ? 10.676  34.988  1.643   1.00 20.91 ? 141 THR A HA   1 
ATOM   1709 H HB   . THR A 1 122 ? 8.504   35.697  1.997   1.00 22.43 ? 141 THR A HB   1 
ATOM   1710 H HG1  . THR A 1 122 ? 7.927   33.219  2.777   1.00 22.94 ? 141 THR A HG1  1 
ATOM   1711 H HG21 . THR A 1 122 ? 7.344   34.696  0.313   1.00 23.59 ? 141 THR A HG21 1 
ATOM   1712 H HG22 . THR A 1 122 ? 8.852   34.820  -0.138  1.00 23.59 ? 141 THR A HG22 1 
ATOM   1713 H HG23 . THR A 1 122 ? 8.290   33.432  0.362   1.00 23.59 ? 141 THR A HG23 1 
ATOM   1714 N N    . GLY A 1 123 ? 10.691  33.693  4.470   1.00 16.90 ? 142 GLY A N    1 
ATOM   1715 C CA   . GLY A 1 123 ? 10.906  33.877  5.885   1.00 15.84 ? 142 GLY A CA   1 
ATOM   1716 C C    . GLY A 1 123 ? 9.698   33.588  6.735   1.00 15.92 ? 142 GLY A C    1 
ATOM   1717 O O    . GLY A 1 123 ? 9.809   33.610  7.972   1.00 16.95 ? 142 GLY A O    1 
ATOM   1718 H H    . GLY A 1 123 ? 10.788  32.880  4.206   1.00 20.29 ? 142 GLY A H    1 
ATOM   1719 H HA2  . GLY A 1 123 ? 11.621  33.288  6.172   1.00 19.01 ? 142 GLY A HA2  1 
ATOM   1720 H HA3  . GLY A 1 123 ? 11.171  34.796  6.045   1.00 19.01 ? 142 GLY A HA3  1 
ATOM   1721 N N    . GLU A 1 124 ? 8.557   33.318  6.112   1.00 15.40 ? 143 GLU A N    1 
ATOM   1722 C CA   . GLU A 1 124 ? 7.368   32.886  6.829   1.00 16.66 ? 143 GLU A CA   1 
ATOM   1723 C C    . GLU A 1 124 ? 7.598   31.509  7.436   1.00 15.31 ? 143 GLU A C    1 
ATOM   1724 O O    . GLU A 1 124 ? 8.294   30.671  6.870   1.00 16.33 ? 143 GLU A O    1 
ATOM   1725 C CB   . GLU A 1 124 ? 6.167   32.845  5.868   1.00 19.09 ? 143 GLU A CB   1 
ATOM   1726 C CG   . GLU A 1 124 ? 4.846   32.463  6.542   1.00 22.71 ? 143 GLU A CG   1 
ATOM   1727 C CD   . GLU A 1 124 ? 3.629   32.604  5.634   1.00 26.49 ? 143 GLU A CD   1 
ATOM   1728 O OE1  . GLU A 1 124 ? 3.765   32.496  4.393   1.00 27.65 ? 143 GLU A OE1  1 
ATOM   1729 O OE2  . GLU A 1 124 ? 2.524   32.818  6.181   1.00 28.08 ? 143 GLU A OE2  1 
ATOM   1730 H H    . GLU A 1 124 ? 8.445   33.377  5.262   1.00 18.49 ? 143 GLU A H    1 
ATOM   1731 H HA   . GLU A 1 124 ? 7.163   33.507  7.546   1.00 20.00 ? 143 GLU A HA   1 
ATOM   1732 H HB2  . GLU A 1 124 ? 6.054   33.724  5.474   1.00 22.91 ? 143 GLU A HB2  1 
ATOM   1733 H HB3  . GLU A 1 124 ? 6.345   32.191  5.174   1.00 22.91 ? 143 GLU A HB3  1 
ATOM   1734 H HG2  . GLU A 1 124 ? 4.897   31.537  6.826   1.00 27.26 ? 143 GLU A HG2  1 
ATOM   1735 H HG3  . GLU A 1 124 ? 4.710   33.039  7.310   1.00 27.26 ? 143 GLU A HG3  1 
ATOM   1736 N N    . LEU A 1 125 ? 7.003   31.280  8.597   1.00 15.08 ? 144 LEU A N    1 
ATOM   1737 C CA   . LEU A 1 125 ? 7.058   29.956  9.193   1.00 15.15 ? 144 LEU A CA   1 
ATOM   1738 C C    . LEU A 1 125 ? 6.302   28.957  8.326   1.00 14.79 ? 144 LEU A C    1 
ATOM   1739 O O    . LEU A 1 125 ? 5.191   29.227  7.863   1.00 15.57 ? 144 LEU A O    1 
ATOM   1740 C CB   . LEU A 1 125 ? 6.441   29.941  10.581  1.00 15.72 ? 144 LEU A CB   1 
ATOM   1741 C CG   . LEU A 1 125 ? 7.211   30.686  11.666  1.00 16.83 ? 144 LEU A CG   1 
ATOM   1742 C CD1  . LEU A 1 125 ? 6.378   30.716  12.930  1.00 17.24 ? 144 LEU A CD1  1 
ATOM   1743 C CD2  . LEU A 1 125 ? 8.530   30.016  11.904  1.00 18.33 ? 144 LEU A CD2  1 
ATOM   1744 H H    . LEU A 1 125 ? 6.569   31.865  9.054   1.00 18.10 ? 144 LEU A H    1 
ATOM   1745 H HA   . LEU A 1 125 ? 7.991   29.701  9.264   1.00 18.18 ? 144 LEU A HA   1 
ATOM   1746 H HB2  . LEU A 1 125 ? 5.561   30.345  10.525  1.00 18.87 ? 144 LEU A HB2  1 
ATOM   1747 H HB3  . LEU A 1 125 ? 6.364   29.017  10.867  1.00 18.87 ? 144 LEU A HB3  1 
ATOM   1748 H HG   . LEU A 1 125 ? 7.389   31.600  11.394  1.00 20.20 ? 144 LEU A HG   1 
ATOM   1749 H HD11 . LEU A 1 125 ? 6.883   31.157  13.631  1.00 20.70 ? 144 LEU A HD11 1 
ATOM   1750 H HD12 . LEU A 1 125 ? 5.558   31.204  12.756  1.00 20.70 ? 144 LEU A HD12 1 
ATOM   1751 H HD13 . LEU A 1 125 ? 6.172   29.805  13.194  1.00 20.70 ? 144 LEU A HD13 1 
ATOM   1752 H HD21 . LEU A 1 125 ? 8.374   29.095  12.167  1.00 22.00 ? 144 LEU A HD21 1 
ATOM   1753 H HD22 . LEU A 1 125 ? 9.050   30.042  11.086  1.00 22.00 ? 144 LEU A HD22 1 
ATOM   1754 H HD23 . LEU A 1 125 ? 9.001   30.486  12.610  1.00 22.00 ? 144 LEU A HD23 1 
ATOM   1755 N N    . ASP A 1 126 ? 6.918   27.803  8.096   1.00 13.98 ? 145 ASP A N    1 
ATOM   1756 C CA   . ASP A 1 126 ? 6.278   26.707  7.379   1.00 13.85 ? 145 ASP A CA   1 
ATOM   1757 C C    . ASP A 1 126 ? 5.387   25.938  8.348   1.00 14.17 ? 145 ASP A C    1 
ATOM   1758 O O    . ASP A 1 126 ? 5.876   25.223  9.237   1.00 13.84 ? 145 ASP A O    1 
ATOM   1759 C CB   . ASP A 1 126 ? 7.335   25.826  6.735   1.00 14.57 ? 145 ASP A CB   1 
ATOM   1760 C CG   . ASP A 1 126 ? 6.734   24.716  5.906   1.00 16.17 ? 145 ASP A CG   1 
ATOM   1761 O OD1  . ASP A 1 126 ? 5.576   24.303  6.181   1.00 15.96 ? 145 ASP A OD1  1 
ATOM   1762 O OD2  . ASP A 1 126 ? 7.440   24.226  4.998   1.00 17.45 ? 145 ASP A OD2  1 
ATOM   1763 H H    . ASP A 1 126 ? 7.721   27.627  8.350   1.00 16.79 ? 145 ASP A H    1 
ATOM   1764 H HA   . ASP A 1 126 ? 5.709   27.052  6.673   1.00 16.63 ? 145 ASP A HA   1 
ATOM   1765 H HB2  . ASP A 1 126 ? 7.890   26.369  6.153   1.00 17.49 ? 145 ASP A HB2  1 
ATOM   1766 H HB3  . ASP A 1 126 ? 7.878   25.423  7.430   1.00 17.49 ? 145 ASP A HB3  1 
ATOM   1767 N N    . ARG A 1 127 ? 4.076   26.136  8.214   1.00 13.88 ? 146 ARG A N    1 
ATOM   1768 C CA   . ARG A 1 127 ? 3.087   25.510  9.073   1.00 14.61 ? 146 ARG A CA   1 
ATOM   1769 C C    . ARG A 1 127 ? 1.937   25.002  8.221   1.00 16.27 ? 146 ARG A C    1 
ATOM   1770 O O    . ARG A 1 127 ? 1.491   25.684  7.296   1.00 17.56 ? 146 ARG A O    1 
ATOM   1771 C CB   . ARG A 1 127 ? 2.529   26.498  10.108  1.00 14.85 ? 146 ARG A CB   1 
ATOM   1772 C CG   . ARG A 1 127 ? 3.613   27.200  10.905  1.00 14.67 ? 146 ARG A CG   1 
ATOM   1773 C CD   . ARG A 1 127 ? 3.089   27.956  12.118  1.00 15.52 ? 146 ARG A CD   1 
ATOM   1774 N NE   . ARG A 1 127 ? 2.297   29.110  11.721  1.00 16.17 ? 146 ARG A NE   1 
ATOM   1775 C CZ   . ARG A 1 127 ? 1.620   29.888  12.556  1.00 16.41 ? 146 ARG A CZ   1 
ATOM   1776 N NH1  . ARG A 1 127 ? 1.691   29.719  13.866  1.00 16.75 ? 146 ARG A NH1  1 
ATOM   1777 N NH2  . ARG A 1 127 ? 0.852   30.864  12.062  1.00 18.45 ? 146 ARG A NH2  1 
ATOM   1778 H H    . ARG A 1 127 ? 3.730   26.645  7.613   1.00 16.66 ? 146 ARG A H    1 
ATOM   1779 H HA   . ARG A 1 127 ? 3.499   24.765  9.537   1.00 17.54 ? 146 ARG A HA   1 
ATOM   1780 H HB2  . ARG A 1 127 ? 2.009   27.175  9.648   1.00 17.83 ? 146 ARG A HB2  1 
ATOM   1781 H HB3  . ARG A 1 127 ? 1.965   26.014  10.732  1.00 17.83 ? 146 ARG A HB3  1 
ATOM   1782 H HG2  . ARG A 1 127 ? 4.247   26.538  11.220  1.00 17.61 ? 146 ARG A HG2  1 
ATOM   1783 H HG3  . ARG A 1 127 ? 4.060   27.840  10.328  1.00 17.61 ? 146 ARG A HG3  1 
ATOM   1784 H HD2  . ARG A 1 127 ? 2.528   27.367  12.647  1.00 18.63 ? 146 ARG A HD2  1 
ATOM   1785 H HD3  . ARG A 1 127 ? 3.838   28.268  12.650  1.00 18.63 ? 146 ARG A HD3  1 
ATOM   1786 H HE   . ARG A 1 127 ? 2.265   29.303  10.883  1.00 19.41 ? 146 ARG A HE   1 
ATOM   1787 H HH11 . ARG A 1 127 ? 2.185   29.096  14.193  1.00 20.11 ? 146 ARG A HH11 1 
ATOM   1788 H HH12 . ARG A 1 127 ? 1.245   30.234  14.390  1.00 20.11 ? 146 ARG A HH12 1 
ATOM   1789 H HH21 . ARG A 1 127 ? 0.801   30.982  11.212  1.00 22.15 ? 146 ARG A HH21 1 
ATOM   1790 H HH22 . ARG A 1 127 ? 0.409   31.373  12.595  1.00 22.15 ? 146 ARG A HH22 1 
ATOM   1791 N N    . LYS A 1 128 ? 1.440   23.816  8.561   1.00 17.35 ? 147 LYS A N    1 
ATOM   1792 C CA   . LYS A 1 128 ? 0.169   23.372  8.021   1.00 19.71 ? 147 LYS A CA   1 
ATOM   1793 C C    . LYS A 1 128 ? -0.977  24.131  8.689   1.00 21.54 ? 147 LYS A C    1 
ATOM   1794 O O    . LYS A 1 128 ? -0.794  24.830  9.691   1.00 21.85 ? 147 LYS A O    1 
ATOM   1795 C CB   . LYS A 1 128 ? -0.006  21.869  8.232   1.00 21.09 ? 147 LYS A CB   1 
ATOM   1796 C CG   . LYS A 1 128 ? 1.029   21.044  7.509   1.00 22.92 ? 147 LYS A CG   1 
ATOM   1797 C CD   . LYS A 1 128 ? 0.779   19.549  7.700   1.00 24.72 ? 147 LYS A CD   1 
ATOM   1798 C CE   . LYS A 1 128 ? -0.344  19.049  6.808   1.00 26.67 ? 147 LYS A CE   1 
ATOM   1799 N NZ   . LYS A 1 128 ? -0.362  17.564  6.832   1.00 27.47 ? 147 LYS A NZ   1 
ATOM   1800 H H    . LYS A 1 128 ? 1.817   23.260  9.098   1.00 20.83 ? 147 LYS A H    1 
ATOM   1801 H HA   . LYS A 1 128 ? 0.145   23.549  7.067   1.00 23.65 ? 147 LYS A HA   1 
ATOM   1802 H HB2  . LYS A 1 128 ? 0.066   21.675  9.180   1.00 25.31 ? 147 LYS A HB2  1 
ATOM   1803 H HB3  . LYS A 1 128 ? -0.880  21.605  7.905   1.00 25.31 ? 147 LYS A HB3  1 
ATOM   1804 H HG2  . LYS A 1 128 ? 0.993   21.242  6.560   1.00 27.51 ? 147 LYS A HG2  1 
ATOM   1805 H HG3  . LYS A 1 128 ? 1.909   21.254  7.858   1.00 27.51 ? 147 LYS A HG3  1 
ATOM   1806 H HD2  . LYS A 1 128 ? 1.585   19.058  7.476   1.00 29.68 ? 147 LYS A HD2  1 
ATOM   1807 H HD3  . LYS A 1 128 ? 0.533   19.380  8.622   1.00 29.68 ? 147 LYS A HD3  1 
ATOM   1808 H HE2  . LYS A 1 128 ? -1.196  19.379  7.135   1.00 32.01 ? 147 LYS A HE2  1 
ATOM   1809 H HE3  . LYS A 1 128 ? -0.200  19.347  5.897   1.00 32.01 ? 147 LYS A HE3  1 
ATOM   1810 H HZ1  . LYS A 1 128 ? -1.014  17.259  6.307   1.00 32.97 ? 147 LYS A HZ1  1 
ATOM   1811 H HZ2  . LYS A 1 128 ? 0.416   17.246  6.540   1.00 32.97 ? 147 LYS A HZ2  1 
ATOM   1812 H HZ3  . LYS A 1 128 ? -0.500  17.274  7.662   1.00 32.97 ? 147 LYS A HZ3  1 
ATOM   1813 N N    . LYS A 1 129 ? -2.168  24.026  8.098   1.00 23.34 ? 148 LYS A N    1 
ATOM   1814 C CA   . LYS A 1 129 ? -3.342  24.654  8.690   1.00 25.97 ? 148 LYS A CA   1 
ATOM   1815 C C    . LYS A 1 129 ? -3.482  24.217  10.144  1.00 25.96 ? 148 LYS A C    1 
ATOM   1816 O O    . LYS A 1 129 ? -3.180  23.072  10.500  1.00 26.45 ? 148 LYS A O    1 
ATOM   1817 C CB   . LYS A 1 129 ? -4.597  24.249  7.909   1.00 28.82 ? 148 LYS A CB   1 
ATOM   1818 C CG   . LYS A 1 129 ? -4.682  24.803  6.485   1.00 32.44 ? 148 LYS A CG   1 
ATOM   1819 C CD   . LYS A 1 129 ? -4.766  26.341  6.425   1.00 34.97 ? 148 LYS A CD   1 
ATOM   1820 C CE   . LYS A 1 129 ? -4.753  26.834  4.974   1.00 36.66 ? 148 LYS A CE   1 
ATOM   1821 N NZ   . LYS A 1 129 ? -4.433  28.290  4.841   1.00 37.67 ? 148 LYS A NZ   1 
ATOM   1822 H H    . LYS A 1 129 ? -2.318  23.603  7.365   1.00 28.02 ? 148 LYS A H    1 
ATOM   1823 H HA   . LYS A 1 129 ? -3.254  25.620  8.655   1.00 31.17 ? 148 LYS A HA   1 
ATOM   1824 H HB2  . LYS A 1 129 ? -4.620  23.281  7.846   1.00 34.59 ? 148 LYS A HB2  1 
ATOM   1825 H HB3  . LYS A 1 129 ? -5.375  24.568  8.391   1.00 34.59 ? 148 LYS A HB3  1 
ATOM   1826 H HG2  . LYS A 1 129 ? -3.890  24.531  5.995   1.00 38.93 ? 148 LYS A HG2  1 
ATOM   1827 H HG3  . LYS A 1 129 ? -5.475  24.446  6.056   1.00 38.93 ? 148 LYS A HG3  1 
ATOM   1828 H HD2  . LYS A 1 129 ? -5.591  26.636  6.842   1.00 41.97 ? 148 LYS A HD2  1 
ATOM   1829 H HD3  . LYS A 1 129 ? -4.005  26.725  6.886   1.00 41.97 ? 148 LYS A HD3  1 
ATOM   1830 H HE2  . LYS A 1 129 ? -4.083  26.336  4.480   1.00 43.99 ? 148 LYS A HE2  1 
ATOM   1831 H HE3  . LYS A 1 129 ? -5.629  26.686  4.585   1.00 43.99 ? 148 LYS A HE3  1 
ATOM   1832 H HZ1  . LYS A 1 129 ? -4.433  28.524  3.982   1.00 45.21 ? 148 LYS A HZ1  1 
ATOM   1833 H HZ2  . LYS A 1 129 ? -5.040  28.776  5.273   1.00 45.21 ? 148 LYS A HZ2  1 
ATOM   1834 H HZ3  . LYS A 1 129 ? -3.630  28.457  5.186   1.00 45.21 ? 148 LYS A HZ3  1 
ATOM   1835 N N    . GLY A 1 130 ? -3.926  25.138  10.993  1.00 24.52 ? 149 GLY A N    1 
ATOM   1836 C CA   . GLY A 1 130 ? -3.967  24.881  12.416  1.00 23.36 ? 149 GLY A CA   1 
ATOM   1837 C C    . GLY A 1 130 ? -2.674  25.175  13.138  1.00 23.13 ? 149 GLY A C    1 
ATOM   1838 O O    . GLY A 1 130 ? -2.455  24.632  14.228  1.00 23.11 ? 149 GLY A O    1 
ATOM   1839 H H    . GLY A 1 130 ? -4.207  25.918  10.764  1.00 29.43 ? 149 GLY A H    1 
ATOM   1840 H HA2  . GLY A 1 130 ? -4.662  25.430  12.812  1.00 28.04 ? 149 GLY A HA2  1 
ATOM   1841 H HA3  . GLY A 1 130 ? -4.184  23.947  12.559  1.00 28.04 ? 149 GLY A HA3  1 
ATOM   1842 N N    . GLN A 1 131 ? -1.807  26.008  12.559  1.00 21.72 ? 150 GLN A N    1 
ATOM   1843 C CA   . GLN A 1 131 ? -0.542  26.407  13.177  1.00 21.01 ? 150 GLN A CA   1 
ATOM   1844 C C    . GLN A 1 131 ? 0.296   25.189  13.560  1.00 19.77 ? 150 GLN A C    1 
ATOM   1845 O O    . GLN A 1 131 ? 0.841   25.102  14.657  1.00 20.91 ? 150 GLN A O    1 
ATOM   1846 C CB   . GLN A 1 131 ? -0.770  27.340  14.374  1.00 22.18 ? 150 GLN A CB   1 
ATOM   1847 C CG   . GLN A 1 131 ? -1.529  28.630  14.025  1.00 23.10 ? 150 GLN A CG   1 
ATOM   1848 C CD   . GLN A 1 131 ? -3.026  28.449  13.959  1.00 25.45 ? 150 GLN A CD   1 
ATOM   1849 O OE1  . GLN A 1 131 ? -3.626  27.748  14.786  1.00 26.45 ? 150 GLN A OE1  1 
ATOM   1850 N NE2  . GLN A 1 131 ? -3.649  29.093  12.980  1.00 25.58 ? 150 GLN A NE2  1 
ATOM   1851 H H    . GLN A 1 131 ? -1.933  26.366  11.787  1.00 26.07 ? 150 GLN A H    1 
ATOM   1852 H HA   . GLN A 1 131 ? -0.030  26.906  12.521  1.00 25.22 ? 150 GLN A HA   1 
ATOM   1853 H HB2  . GLN A 1 131 ? -1.287  26.865  15.044  1.00 26.63 ? 150 GLN A HB2  1 
ATOM   1854 H HB3  . GLN A 1 131 ? 0.092   27.594  14.739  1.00 26.63 ? 150 GLN A HB3  1 
ATOM   1855 H HG2  . GLN A 1 131 ? -1.340  29.298  14.702  1.00 27.73 ? 150 GLN A HG2  1 
ATOM   1856 H HG3  . GLN A 1 131 ? -1.229  28.945  13.157  1.00 27.73 ? 150 GLN A HG3  1 
ATOM   1857 H HE21 . GLN A 1 131 ? -3.200  29.578  12.430  1.00 30.70 ? 150 GLN A HE21 1 
ATOM   1858 H HE22 . GLN A 1 131 ? -4.503  29.025  12.895  1.00 30.70 ? 150 GLN A HE22 1 
ATOM   1859 N N    . LEU A 1 132 ? 0.405   24.252  12.629  1.00 17.36 ? 151 LEU A N    1 
ATOM   1860 C CA   . LEU A 1 132 ? 1.130   22.997  12.824  1.00 15.62 ? 151 LEU A CA   1 
ATOM   1861 C C    . LEU A 1 132 ? 2.475   23.083  12.103  1.00 13.83 ? 151 LEU A C    1 
ATOM   1862 O O    . LEU A 1 132 ? 2.573   22.879  10.889  1.00 14.89 ? 151 LEU A O    1 
ATOM   1863 C CB   . LEU A 1 132 ? 0.275   21.854  12.296  1.00 16.50 ? 151 LEU A CB   1 
ATOM   1864 C CG   . LEU A 1 132 ? 0.879   20.460  12.335  1.00 17.30 ? 151 LEU A CG   1 
ATOM   1865 C CD1  . LEU A 1 132 ? 1.325   20.107  13.721  1.00 18.64 ? 151 LEU A CD1  1 
ATOM   1866 C CD2  . LEU A 1 132 ? -0.154  19.439  11.813  1.00 17.36 ? 151 LEU A CD2  1 
ATOM   1867 H H    . LEU A 1 132 ? 0.056   24.319  11.846  1.00 20.83 ? 151 LEU A H    1 
ATOM   1868 H HA   . LEU A 1 132 ? 1.321   22.860  13.765  1.00 18.76 ? 151 LEU A HA   1 
ATOM   1869 H HB2  . LEU A 1 132 ? -0.539  21.823  12.823  1.00 19.81 ? 151 LEU A HB2  1 
ATOM   1870 H HB3  . LEU A 1 132 ? 0.063   22.044  11.369  1.00 19.81 ? 151 LEU A HB3  1 
ATOM   1871 H HG   . LEU A 1 132 ? 1.664   20.431  11.765  1.00 20.76 ? 151 LEU A HG   1 
ATOM   1872 H HD11 . LEU A 1 132 ? 1.618   19.182  13.732  1.00 22.37 ? 151 LEU A HD11 1 
ATOM   1873 H HD12 . LEU A 1 132 ? 2.058   20.689  13.975  1.00 22.37 ? 151 LEU A HD12 1 
ATOM   1874 H HD13 . LEU A 1 132 ? 0.581   20.226  14.332  1.00 22.37 ? 151 LEU A HD13 1 
ATOM   1875 H HD21 . LEU A 1 132 ? 0.262   18.564  11.769  1.00 20.84 ? 151 LEU A HD21 1 
ATOM   1876 H HD22 . LEU A 1 132 ? -0.909  19.416  12.421  1.00 20.84 ? 151 LEU A HD22 1 
ATOM   1877 H HD23 . LEU A 1 132 ? -0.448  19.711  10.930  1.00 20.84 ? 151 LEU A HD23 1 
ATOM   1878 N N    . MET A 1 133 ? 3.522   23.391  12.858  1.00 13.47 ? 152 MET A N    1 
ATOM   1879 C CA   . MET A 1 133 ? 4.843   23.589  12.272  1.00 12.26 ? 152 MET A CA   1 
ATOM   1880 C C    . MET A 1 133 ? 5.369   22.271  11.686  1.00 12.89 ? 152 MET A C    1 
ATOM   1881 O O    . MET A 1 133 ? 5.115   21.182  12.214  1.00 13.42 ? 152 MET A O    1 
ATOM   1882 C CB   . MET A 1 133 ? 5.786   24.067  13.379  1.00 14.18 ? 152 MET A CB   1 
ATOM   1883 C CG   . MET A 1 133 ? 5.931   25.609  13.400  1.00 16.07 ? 152 MET A CG   1 
ATOM   1884 S SD   . MET A 1 133 ? 7.092   26.250  14.607  1.00 14.69 ? 152 MET A SD   1 
ATOM   1885 C CE   . MET A 1 133 ? 6.624   25.532  16.159  1.00 15.70 ? 152 MET A CE   1 
ATOM   1886 H H    . MET A 1 133 ? 3.497   23.491  13.712  1.00 16.17 ? 152 MET A H    1 
ATOM   1887 H HA   . MET A 1 133 ? 4.805   24.252  11.564  1.00 14.72 ? 152 MET A HA   1 
ATOM   1888 H HB2  . MET A 1 133 ? 5.437   23.784  14.238  1.00 17.02 ? 152 MET A HB2  1 
ATOM   1889 H HB3  . MET A 1 133 ? 6.665   23.683  13.235  1.00 17.02 ? 152 MET A HB3  1 
ATOM   1890 H HG2  . MET A 1 133 ? 6.232   25.901  12.525  1.00 19.29 ? 152 MET A HG2  1 
ATOM   1891 H HG3  . MET A 1 133 ? 5.064   25.996  13.598  1.00 19.29 ? 152 MET A HG3  1 
ATOM   1892 H HE1  . MET A 1 133 ? 7.221   25.858  16.850  1.00 18.85 ? 152 MET A HE1  1 
ATOM   1893 H HE2  . MET A 1 133 ? 5.711   25.788  16.363  1.00 18.85 ? 152 MET A HE2  1 
ATOM   1894 H HE3  . MET A 1 133 ? 6.690   24.566  16.093  1.00 18.85 ? 152 MET A HE3  1 
ATOM   1895 N N    . ARG A 1 134 ? 6.084   22.383  10.568  1.00 12.23 ? 153 ARG A N    1 
ATOM   1896 C CA   . ARG A 1 134 ? 6.781   21.267  9.941   1.00 12.03 ? 153 ARG A CA   1 
ATOM   1897 C C    . ARG A 1 134 ? 8.259   21.401  10.246  1.00 12.44 ? 153 ARG A C    1 
ATOM   1898 O O    . ARG A 1 134 ? 8.783   22.515  10.281  1.00 13.77 ? 153 ARG A O    1 
ATOM   1899 C CB   . ARG A 1 134 ? 6.530   21.196  8.434   1.00 12.84 ? 153 ARG A CB   1 
ATOM   1900 C CG   . ARG A 1 134 ? 5.025   21.183  8.079   1.00 12.91 ? 153 ARG A CG   1 
ATOM   1901 C CD   . ARG A 1 134 ? 4.719   20.702  6.674   1.00 13.56 ? 153 ARG A CD   1 
ATOM   1902 N NE   . ARG A 1 134 ? 5.340   21.563  5.680   1.00 13.61 ? 153 ARG A NE   1 
ATOM   1903 C CZ   . ARG A 1 134 ? 5.536   21.245  4.405   1.00 14.99 ? 153 ARG A CZ   1 
ATOM   1904 N NH1  . ARG A 1 134 ? 5.101   20.099  3.891   1.00 15.25 ? 153 ARG A NH1  1 
ATOM   1905 N NH2  . ARG A 1 134 ? 6.190   22.096  3.625   1.00 15.35 ? 153 ARG A NH2  1 
ATOM   1906 H H    . ARG A 1 134 ? 6.182   23.122  10.140  1.00 14.69 ? 153 ARG A H    1 
ATOM   1907 H HA   . ARG A 1 134 ? 6.457   20.426  10.300  1.00 14.44 ? 153 ARG A HA   1 
ATOM   1908 H HB2  . ARG A 1 134 ? 6.932   21.970  8.009   1.00 15.42 ? 153 ARG A HB2  1 
ATOM   1909 H HB3  . ARG A 1 134 ? 6.928   20.382  8.085   1.00 15.42 ? 153 ARG A HB3  1 
ATOM   1910 H HG2  . ARG A 1 134 ? 4.566   20.593  8.697   1.00 15.50 ? 153 ARG A HG2  1 
ATOM   1911 H HG3  . ARG A 1 134 ? 4.679   22.085  8.162   1.00 15.50 ? 153 ARG A HG3  1 
ATOM   1912 H HD2  . ARG A 1 134 ? 5.063   19.802  6.558   1.00 16.28 ? 153 ARG A HD2  1 
ATOM   1913 H HD3  . ARG A 1 134 ? 3.760   20.712  6.531   1.00 16.28 ? 153 ARG A HD3  1 
ATOM   1914 H HE   . ARG A 1 134 ? 5.602   22.340  5.939   1.00 16.34 ? 153 ARG A HE   1 
ATOM   1915 H HH11 . ARG A 1 134 ? 4.679   19.538  4.388   1.00 18.31 ? 153 ARG A HH11 1 
ATOM   1916 H HH12 . ARG A 1 134 ? 5.241   19.919  3.062   1.00 18.31 ? 153 ARG A HH12 1 
ATOM   1917 H HH21 . ARG A 1 134 ? 6.480   22.840  3.946   1.00 18.43 ? 153 ARG A HH21 1 
ATOM   1918 H HH22 . ARG A 1 134 ? 6.325   21.905  2.797   1.00 18.43 ? 153 ARG A HH22 1 
ATOM   1919 N N    . TYR A 1 135 ? 8.923   20.267  10.466  1.00 11.97 ? 154 TYR A N    1 
ATOM   1920 C CA   . TYR A 1 135 ? 10.291  20.290  10.958  1.00 12.42 ? 154 TYR A CA   1 
ATOM   1921 C C    . TYR A 1 135 ? 11.325  20.440  9.849   1.00 12.36 ? 154 TYR A C    1 
ATOM   1922 O O    . TYR A 1 135 ? 11.188  19.865  8.764   1.00 13.40 ? 154 TYR A O    1 
ATOM   1923 C CB   . TYR A 1 135 ? 10.637  18.969  11.636  1.00 11.82 ? 154 TYR A CB   1 
ATOM   1924 C CG   . TYR A 1 135 ? 9.854   18.586  12.867  1.00 11.85 ? 154 TYR A CG   1 
ATOM   1925 C CD1  . TYR A 1 135 ? 9.658   19.483  13.911  1.00 12.08 ? 154 TYR A CD1  1 
ATOM   1926 C CD2  . TYR A 1 135 ? 9.352   17.306  13.003  1.00 12.26 ? 154 TYR A CD2  1 
ATOM   1927 C CE1  . TYR A 1 135 ? 8.981   19.089  15.067  1.00 12.42 ? 154 TYR A CE1  1 
ATOM   1928 C CE2  . TYR A 1 135 ? 8.670   16.911  14.127  1.00 12.05 ? 154 TYR A CE2  1 
ATOM   1929 C CZ   . TYR A 1 135 ? 8.485   17.792  15.163  1.00 11.74 ? 154 TYR A CZ   1 
ATOM   1930 O OH   . TYR A 1 135 ? 7.834   17.376  16.292  1.00 12.75 ? 154 TYR A OH   1 
ATOM   1931 H H    . TYR A 1 135 ? 8.602   19.480  10.339  1.00 14.38 ? 154 TYR A H    1 
ATOM   1932 H HA   . TYR A 1 135 ? 10.343  21.046  11.565  1.00 14.91 ? 154 TYR A HA   1 
ATOM   1933 H HB2  . TYR A 1 135 ? 10.502  18.260  10.988  1.00 14.19 ? 154 TYR A HB2  1 
ATOM   1934 H HB3  . TYR A 1 135 ? 11.570  19.006  11.899  1.00 14.19 ? 154 TYR A HB3  1 
ATOM   1935 H HD1  . TYR A 1 135 ? 9.981   20.352  13.839  1.00 14.50 ? 154 TYR A HD1  1 
ATOM   1936 H HD2  . TYR A 1 135 ? 9.479   16.694  12.314  1.00 14.72 ? 154 TYR A HD2  1 
ATOM   1937 H HE1  . TYR A 1 135 ? 8.861   19.689  15.768  1.00 14.91 ? 154 TYR A HE1  1 
ATOM   1938 H HE2  . TYR A 1 135 ? 8.334   16.046  14.187  1.00 14.47 ? 154 TYR A HE2  1 
ATOM   1939 H HH   . TYR A 1 135 ? 7.692   16.549  16.253  1.00 15.31 ? 154 TYR A HH   1 
ATOM   1940 N N    . ASP A 1 136 ? 12.398  21.180  10.160  1.00 12.63 ? 155 ASP A N    1 
ATOM   1941 C CA   . ASP A 1 136 ? 13.543  21.273  9.265   1.00 12.29 ? 155 ASP A CA   1 
ATOM   1942 C C    . ASP A 1 136 ? 14.493  20.128  9.561   1.00 11.72 ? 155 ASP A C    1 
ATOM   1943 O O    . ASP A 1 136 ? 15.368  20.236  10.414  1.00 13.62 ? 155 ASP A O    1 
ATOM   1944 C CB   . ASP A 1 136 ? 14.262  22.604  9.421   1.00 13.22 ? 155 ASP A CB   1 
ATOM   1945 C CG   . ASP A 1 136 ? 15.418  22.738  8.442   1.00 14.68 ? 155 ASP A CG   1 
ATOM   1946 O OD1  . ASP A 1 136 ? 15.658  21.766  7.684   1.00 14.03 ? 155 ASP A OD1  1 
ATOM   1947 O OD2  . ASP A 1 136 ? 16.076  23.802  8.441   1.00 17.00 ? 155 ASP A OD2  1 
ATOM   1948 H H    . ASP A 1 136 ? 12.479  21.635  10.885  1.00 15.17 ? 155 ASP A H    1 
ATOM   1949 H HA   . ASP A 1 136 ? 13.215  21.191  8.356   1.00 14.75 ? 155 ASP A HA   1 
ATOM   1950 H HB2  . ASP A 1 136 ? 13.637  23.326  9.255   1.00 15.87 ? 155 ASP A HB2  1 
ATOM   1951 H HB3  . ASP A 1 136 ? 14.617  22.672  10.322  1.00 15.87 ? 155 ASP A HB3  1 
ATOM   1952 N N    . LEU A 1 137 ? 14.313  19.021  8.832   1.00 11.64 ? 156 LEU A N    1 
ATOM   1953 C CA   . LEU A 1 137 ? 15.115  17.826  9.065   1.00 11.85 ? 156 LEU A CA   1 
ATOM   1954 C C    . LEU A 1 137 ? 16.591  18.049  8.803   1.00 12.50 ? 156 LEU A C    1 
ATOM   1955 O O    . LEU A 1 137 ? 17.419  17.229  9.227   1.00 12.88 ? 156 LEU A O    1 
ATOM   1956 C CB   . LEU A 1 137 ? 14.622  16.688  8.177   1.00 13.25 ? 156 LEU A CB   1 
ATOM   1957 C CG   . LEU A 1 137 ? 13.142  16.313  8.257   1.00 14.90 ? 156 LEU A CG   1 
ATOM   1958 C CD1  . LEU A 1 137 ? 12.864  15.065  7.423   1.00 15.23 ? 156 LEU A CD1  1 
ATOM   1959 C CD2  . LEU A 1 137 ? 12.702  16.100  9.684   1.00 16.39 ? 156 LEU A CD2  1 
ATOM   1960 H H    . LEU A 1 137 ? 13.735  18.940  8.200   1.00 13.98 ? 156 LEU A H    1 
ATOM   1961 H HA   . LEU A 1 137 ? 15.010  17.570  9.994   1.00 14.23 ? 156 LEU A HA   1 
ATOM   1962 H HB2  . LEU A 1 137 ? 14.798  16.935  7.255   1.00 15.91 ? 156 LEU A HB2  1 
ATOM   1963 H HB3  . LEU A 1 137 ? 15.126  15.892  8.409   1.00 15.91 ? 156 LEU A HB3  1 
ATOM   1964 H HG   . LEU A 1 137 ? 12.621  17.048  7.899   1.00 17.89 ? 156 LEU A HG   1 
ATOM   1965 H HD11 . LEU A 1 137 ? 11.913  14.876  7.445   1.00 18.29 ? 156 LEU A HD11 1 
ATOM   1966 H HD12 . LEU A 1 137 ? 13.148  15.226  6.510   1.00 18.29 ? 156 LEU A HD12 1 
ATOM   1967 H HD13 . LEU A 1 137 ? 13.358  14.319  7.797   1.00 18.29 ? 156 LEU A HD13 1 
ATOM   1968 H HD21 . LEU A 1 137 ? 12.821  16.927  10.177  1.00 19.67 ? 156 LEU A HD21 1 
ATOM   1969 H HD22 . LEU A 1 137 ? 11.766  15.843  9.691   1.00 19.67 ? 156 LEU A HD22 1 
ATOM   1970 H HD23 . LEU A 1 137 ? 13.241  15.398  10.080  1.00 19.67 ? 156 LEU A HD23 1 
ATOM   1971 N N    . SER A 1 138 ? 16.944  19.112  8.074   1.00 13.35 ? 157 SER A N    1 
ATOM   1972 C CA   . SER A 1 138 ? 18.351  19.389  7.807   1.00 13.65 ? 157 SER A CA   1 
ATOM   1973 C C    . SER A 1 138 ? 19.090  19.940  9.018   1.00 13.75 ? 157 SER A C    1 
ATOM   1974 O O    . SER A 1 138 ? 20.325  20.006  8.985   1.00 15.22 ? 157 SER A O    1 
ATOM   1975 C CB   . SER A 1 138 ? 18.501  20.347  6.630   1.00 15.24 ? 157 SER A CB   1 
ATOM   1976 O OG   . SER A 1 138 ? 18.181  21.674  6.998   1.00 15.73 ? 157 SER A OG   1 
ATOM   1977 H H    . SER A 1 138 ? 16.394  19.677  7.729   1.00 16.03 ? 157 SER A H    1 
ATOM   1978 H HA   . SER A 1 138 ? 18.776  18.554  7.557   1.00 16.39 ? 157 SER A HA   1 
ATOM   1979 H HB2  . SER A 1 138 ? 19.419  20.321  6.319   1.00 18.29 ? 157 SER A HB2  1 
ATOM   1980 H HB3  . SER A 1 138 ? 17.902  20.067  5.920   1.00 18.29 ? 157 SER A HB3  1 
ATOM   1981 H HG   . SER A 1 138 ? 17.360  21.737  7.161   1.00 18.89 ? 157 SER A HG   1 
ATOM   1982 N N    . ASN A 1 139 ? 18.386  20.334  10.077  1.00 14.21 ? 158 ASN A N    1 
ATOM   1983 C CA   . ASN A 1 139 ? 19.017  20.941  11.247  1.00 14.00 ? 158 ASN A CA   1 
ATOM   1984 C C    . ASN A 1 139 ? 19.449  19.854  12.233  1.00 14.41 ? 158 ASN A C    1 
ATOM   1985 O O    . ASN A 1 139 ? 18.613  19.119  12.767  1.00 14.17 ? 158 ASN A O    1 
ATOM   1986 C CB   . ASN A 1 139 ? 18.034  21.913  11.894  1.00 14.54 ? 158 ASN A CB   1 
ATOM   1987 C CG   . ASN A 1 139 ? 18.632  22.656  13.074  1.00 15.01 ? 158 ASN A CG   1 
ATOM   1988 O OD1  . ASN A 1 139 ? 19.032  22.040  14.072  1.00 15.43 ? 158 ASN A OD1  1 
ATOM   1989 N ND2  . ASN A 1 139 ? 18.697  23.986  12.966  1.00 16.35 ? 158 ASN A ND2  1 
ATOM   1990 H H    . ASN A 1 139 ? 17.532  20.259  10.143  1.00 17.05 ? 158 ASN A H    1 
ATOM   1991 H HA   . ASN A 1 139 ? 19.818  21.421  10.985  1.00 16.81 ? 158 ASN A HA   1 
ATOM   1992 H HB2  . ASN A 1 139 ? 17.759  22.569  11.235  1.00 17.45 ? 158 ASN A HB2  1 
ATOM   1993 H HB3  . ASN A 1 139 ? 17.263  21.418  12.211  1.00 17.45 ? 158 ASN A HB3  1 
ATOM   1994 H HD21 . ASN A 1 139 ? 18.409  24.375  12.255  1.00 19.62 ? 158 ASN A HD21 1 
ATOM   1995 H HD22 . ASN A 1 139 ? 19.027  24.453  13.608  1.00 19.62 ? 158 ASN A HD22 1 
ATOM   1996 N N    . ALA A 1 140 ? 20.765  19.748  12.473  1.00 15.37 ? 159 ALA A N    1 
ATOM   1997 C CA   . ALA A 1 140 ? 21.303  18.651  13.274  1.00 14.43 ? 159 ALA A CA   1 
ATOM   1998 C C    . ALA A 1 140 ? 20.899  18.760  14.741  1.00 14.55 ? 159 ALA A C    1 
ATOM   1999 O O    . ALA A 1 140 ? 20.722  17.737  15.413  1.00 15.17 ? 159 ALA A O    1 
ATOM   2000 C CB   . ALA A 1 140 ? 22.830  18.605  13.161  1.00 14.67 ? 159 ALA A CB   1 
ATOM   2001 H H    . ALA A 1 140 ? 21.360  20.298  12.184  1.00 18.45 ? 159 ALA A H    1 
ATOM   2002 H HA   . ALA A 1 140 ? 20.941  17.824  12.919  1.00 17.32 ? 159 ALA A HA   1 
ATOM   2003 H HB1  . ALA A 1 140 ? 23.159  17.830  13.644  1.00 17.61 ? 159 ALA A HB1  1 
ATOM   2004 H HB2  . ALA A 1 140 ? 23.076  18.540  12.225  1.00 17.61 ? 159 ALA A HB2  1 
ATOM   2005 H HB3  . ALA A 1 140 ? 23.200  19.415  13.545  1.00 17.61 ? 159 ALA A HB3  1 
ATOM   2006 N N    . GLU A 1 141 ? 20.806  19.980  15.281  1.00 15.74 ? 160 GLU A N    1 
ATOM   2007 C CA   . GLU A 1 141 ? 20.355  20.130  16.659  1.00 16.15 ? 160 GLU A CA   1 
ATOM   2008 C C    . GLU A 1 141 ? 18.918  19.656  16.815  1.00 15.41 ? 160 GLU A C    1 
ATOM   2009 O O    . GLU A 1 141 ? 18.592  18.943  17.772  1.00 15.07 ? 160 GLU A O    1 
ATOM   2010 C CB   . GLU A 1 141 ? 20.492  21.577  17.133  1.00 18.70 ? 160 GLU A CB   1 
ATOM   2011 C CG   . GLU A 1 141 ? 21.902  22.032  17.341  1.00 22.72 ? 160 GLU A CG   1 
ATOM   2012 C CD   . GLU A 1 141 ? 21.972  23.461  17.852  1.00 26.65 ? 160 GLU A CD   1 
ATOM   2013 O OE1  . GLU A 1 141 ? 20.905  24.087  18.074  1.00 28.29 ? 160 GLU A OE1  1 
ATOM   2014 O OE2  . GLU A 1 141 ? 23.102  23.955  18.056  1.00 28.45 ? 160 GLU A OE2  1 
ATOM   2015 H H    . GLU A 1 141 ? 20.994  20.716  14.879  1.00 18.90 ? 160 GLU A H    1 
ATOM   2016 H HA   . GLU A 1 141 ? 20.927  19.587  17.224  1.00 19.39 ? 160 GLU A HA   1 
ATOM   2017 H HB2  . GLU A 1 141 ? 20.092  22.159  16.468  1.00 22.44 ? 160 GLU A HB2  1 
ATOM   2018 H HB3  . GLU A 1 141 ? 20.026  21.671  17.979  1.00 22.44 ? 160 GLU A HB3  1 
ATOM   2019 H HG2  . GLU A 1 141 ? 22.329  21.456  17.995  1.00 27.27 ? 160 GLU A HG2  1 
ATOM   2020 H HG3  . GLU A 1 141 ? 22.379  21.988  16.498  1.00 27.27 ? 160 GLU A HG3  1 
ATOM   2021 N N    . PHE A 1 142 ? 18.040  20.048  15.883  1.00 13.72 ? 161 PHE A N    1 
ATOM   2022 C CA   . PHE A 1 142 ? 16.686  19.518  15.883  1.00 13.94 ? 161 PHE A CA   1 
ATOM   2023 C C    . PHE A 1 142 ? 16.699  17.987  15.857  1.00 13.37 ? 161 PHE A C    1 
ATOM   2024 O O    . PHE A 1 142 ? 15.991  17.337  16.628  1.00 14.23 ? 161 PHE A O    1 
ATOM   2025 C CB   . PHE A 1 142 ? 15.864  20.044  14.708  1.00 13.92 ? 161 PHE A CB   1 
ATOM   2026 C CG   . PHE A 1 142 ? 14.775  19.102  14.327  1.00 12.54 ? 161 PHE A CG   1 
ATOM   2027 C CD1  . PHE A 1 142 ? 13.639  18.984  15.108  1.00 13.71 ? 161 PHE A CD1  1 
ATOM   2028 C CD2  . PHE A 1 142 ? 14.933  18.261  13.246  1.00 13.49 ? 161 PHE A CD2  1 
ATOM   2029 C CE1  . PHE A 1 142 ? 12.640  18.077  14.789  1.00 13.38 ? 161 PHE A CE1  1 
ATOM   2030 C CE2  . PHE A 1 142 ? 13.962  17.331  12.936  1.00 13.28 ? 161 PHE A CE2  1 
ATOM   2031 C CZ   . PHE A 1 142 ? 12.800  17.242  13.699  1.00 13.10 ? 161 PHE A CZ   1 
ATOM   2032 H H    . PHE A 1 142 ? 18.207  20.610  15.254  1.00 16.47 ? 161 PHE A H    1 
ATOM   2033 H HA   . PHE A 1 142 ? 16.257  19.827  16.696  1.00 16.73 ? 161 PHE A HA   1 
ATOM   2034 H HB2  . PHE A 1 142 ? 15.460  20.891  14.954  1.00 16.71 ? 161 PHE A HB2  1 
ATOM   2035 H HB3  . PHE A 1 142 ? 16.444  20.164  13.940  1.00 16.71 ? 161 PHE A HB3  1 
ATOM   2036 H HD1  . PHE A 1 142 ? 13.544  19.523  15.860  1.00 16.45 ? 161 PHE A HD1  1 
ATOM   2037 H HD2  . PHE A 1 142 ? 15.699  18.320  12.722  1.00 16.19 ? 161 PHE A HD2  1 
ATOM   2038 H HE1  . PHE A 1 142 ? 11.867  18.031  15.305  1.00 16.07 ? 161 PHE A HE1  1 
ATOM   2039 H HE2  . PHE A 1 142 ? 14.083  16.760  12.212  1.00 15.94 ? 161 PHE A HE2  1 
ATOM   2040 H HZ   . PHE A 1 142 ? 12.139  16.626  13.478  1.00 15.73 ? 161 PHE A HZ   1 
ATOM   2041 N N    . ARG A 1 143 ? 17.511  17.386  14.978  1.00 13.48 ? 162 ARG A N    1 
ATOM   2042 C CA   . ARG A 1 143 ? 17.494  15.929  14.870  1.00 14.18 ? 162 ARG A CA   1 
ATOM   2043 C C    . ARG A 1 143 ? 17.944  15.277  16.174  1.00 14.46 ? 162 ARG A C    1 
ATOM   2044 O O    . ARG A 1 143 ? 17.413  14.236  16.578  1.00 14.08 ? 162 ARG A O    1 
ATOM   2045 C CB   . ARG A 1 143 ? 18.379  15.459  13.710  1.00 13.75 ? 162 ARG A CB   1 
ATOM   2046 C CG   . ARG A 1 143 ? 17.825  15.766  12.331  1.00 14.58 ? 162 ARG A CG   1 
ATOM   2047 C CD   . ARG A 1 143 ? 18.525  14.909  11.283  1.00 14.83 ? 162 ARG A CD   1 
ATOM   2048 N NE   . ARG A 1 143 ? 19.980  14.965  11.350  1.00 15.29 ? 162 ARG A NE   1 
ATOM   2049 C CZ   . ARG A 1 143 ? 20.736  15.839  10.705  1.00 14.90 ? 162 ARG A CZ   1 
ATOM   2050 N NH1  . ARG A 1 143 ? 20.201  16.785  9.957   1.00 16.97 ? 162 ARG A NH1  1 
ATOM   2051 N NH2  . ARG A 1 143 ? 22.064  15.738  10.791  1.00 17.34 ? 162 ARG A NH2  1 
ATOM   2052 H H    . ARG A 1 143 ? 18.061  17.788  14.452  1.00 16.19 ? 162 ARG A H    1 
ATOM   2053 H HA   . ARG A 1 143 ? 16.584  15.649  14.681  1.00 17.03 ? 162 ARG A HA   1 
ATOM   2054 H HB2  . ARG A 1 143 ? 19.242  15.895  13.783  1.00 16.51 ? 162 ARG A HB2  1 
ATOM   2055 H HB3  . ARG A 1 143 ? 18.486  14.497  13.775  1.00 16.51 ? 162 ARG A HB3  1 
ATOM   2056 H HG2  . ARG A 1 143 ? 16.875  15.570  12.309  1.00 17.50 ? 162 ARG A HG2  1 
ATOM   2057 H HG3  . ARG A 1 143 ? 17.976  16.701  12.119  1.00 17.50 ? 162 ARG A HG3  1 
ATOM   2058 H HD2  . ARG A 1 143 ? 18.260  13.985  11.407  1.00 17.80 ? 162 ARG A HD2  1 
ATOM   2059 H HD3  . ARG A 1 143 ? 18.259  15.215  10.401  1.00 17.80 ? 162 ARG A HD3  1 
ATOM   2060 H HE   . ARG A 1 143 ? 20.377  14.386  11.847  1.00 18.35 ? 162 ARG A HE   1 
ATOM   2061 H HH11 . ARG A 1 143 ? 19.346  16.842  9.882   1.00 20.37 ? 162 ARG A HH11 1 
ATOM   2062 H HH12 . ARG A 1 143 ? 20.707  17.345  9.545   1.00 20.37 ? 162 ARG A HH12 1 
ATOM   2063 H HH21 . ARG A 1 143 ? 22.418  15.110  11.260  1.00 20.81 ? 162 ARG A HH21 1 
ATOM   2064 H HH22 . ARG A 1 143 ? 22.565  16.300  10.376  1.00 20.81 ? 162 ARG A HH22 1 
ATOM   2065 N N    . ASN A 1 144 ? 18.936  15.859  16.837  1.00 14.57 ? 163 ASN A N    1 
ATOM   2066 C CA   . ASN A 1 144 ? 19.384  15.299  18.105  1.00 14.76 ? 163 ASN A CA   1 
ATOM   2067 C C    . ASN A 1 144 ? 18.262  15.330  19.132  1.00 14.90 ? 163 ASN A C    1 
ATOM   2068 O O    . ASN A 1 144 ? 18.068  14.367  19.886  1.00 15.21 ? 163 ASN A O    1 
ATOM   2069 C CB   . ASN A 1 144 ? 20.588  16.086  18.609  1.00 15.31 ? 163 ASN A CB   1 
ATOM   2070 C CG   . ASN A 1 144 ? 21.062  15.618  19.961  1.00 17.31 ? 163 ASN A CG   1 
ATOM   2071 O OD1  . ASN A 1 144 ? 21.500  14.484  20.119  1.00 17.94 ? 163 ASN A OD1  1 
ATOM   2072 N ND2  . ASN A 1 144 ? 20.953  16.488  20.952  1.00 19.14 ? 163 ASN A ND2  1 
ATOM   2073 H H    . ASN A 1 144 ? 19.358  16.563  16.581  1.00 17.49 ? 163 ASN A H    1 
ATOM   2074 H HA   . ASN A 1 144 ? 19.652  14.376  17.975  1.00 17.72 ? 163 ASN A HA   1 
ATOM   2075 H HB2  . ASN A 1 144 ? 21.320  15.982  17.982  1.00 18.38 ? 163 ASN A HB2  1 
ATOM   2076 H HB3  . ASN A 1 144 ? 20.346  17.023  18.684  1.00 18.38 ? 163 ASN A HB3  1 
ATOM   2077 H HD21 . ASN A 1 144 ? 20.626  17.269  20.804  1.00 22.98 ? 163 ASN A HD21 1 
ATOM   2078 H HD22 . ASN A 1 144 ? 21.208  16.271  21.744  1.00 22.98 ? 163 ASN A HD22 1 
ATOM   2079 N N    . TRP A 1 145 ? 17.511  16.438  19.174  1.00 13.10 ? 164 TRP A N    1 
ATOM   2080 C CA   . TRP A 1 145 ? 16.369  16.547  20.080  1.00 13.14 ? 164 TRP A CA   1 
ATOM   2081 C C    . TRP A 1 145 ? 15.273  15.537  19.711  1.00 12.79 ? 164 TRP A C    1 
ATOM   2082 O O    . TRP A 1 145 ? 14.700  14.855  20.581  1.00 13.52 ? 164 TRP A O    1 
ATOM   2083 C CB   . TRP A 1 145 ? 15.840  17.988  20.045  1.00 14.10 ? 164 TRP A CB   1 
ATOM   2084 C CG   . TRP A 1 145 ? 14.548  18.149  20.743  1.00 13.93 ? 164 TRP A CG   1 
ATOM   2085 C CD1  . TRP A 1 145 ? 14.355  18.322  22.071  1.00 14.62 ? 164 TRP A CD1  1 
ATOM   2086 C CD2  . TRP A 1 145 ? 13.250  18.103  20.145  1.00 12.81 ? 164 TRP A CD2  1 
ATOM   2087 N NE1  . TRP A 1 145 ? 13.008  18.389  22.351  1.00 14.34 ? 164 TRP A NE1  1 
ATOM   2088 C CE2  . TRP A 1 145 ? 12.309  18.276  21.175  1.00 14.09 ? 164 TRP A CE2  1 
ATOM   2089 C CE3  . TRP A 1 145 ? 12.795  17.959  18.831  1.00 13.58 ? 164 TRP A CE3  1 
ATOM   2090 C CZ2  . TRP A 1 145 ? 10.937  18.284  20.937  1.00 14.63 ? 164 TRP A CZ2  1 
ATOM   2091 C CZ3  . TRP A 1 145 ? 11.415  17.967  18.590  1.00 13.32 ? 164 TRP A CZ3  1 
ATOM   2092 C CH2  . TRP A 1 145 ? 10.505  18.129  19.649  1.00 14.23 ? 164 TRP A CH2  1 
ATOM   2093 H H    . TRP A 1 145 ? 17.643  17.137  18.690  1.00 15.73 ? 164 TRP A H    1 
ATOM   2094 H HA   . TRP A 1 145 ? 16.648  16.347  20.987  1.00 15.77 ? 164 TRP A HA   1 
ATOM   2095 H HB2  . TRP A 1 145 ? 16.486  18.570  20.475  1.00 16.93 ? 164 TRP A HB2  1 
ATOM   2096 H HB3  . TRP A 1 145 ? 15.716  18.255  19.121  1.00 16.93 ? 164 TRP A HB3  1 
ATOM   2097 H HD1  . TRP A 1 145 ? 15.034  18.387  22.704  1.00 17.55 ? 164 TRP A HD1  1 
ATOM   2098 H HE1  . TRP A 1 145 ? 12.663  18.486  23.132  1.00 17.22 ? 164 TRP A HE1  1 
ATOM   2099 H HE3  . TRP A 1 145 ? 13.398  17.860  18.130  1.00 16.30 ? 164 TRP A HE3  1 
ATOM   2100 H HZ2  . TRP A 1 145 ? 10.331  18.392  21.634  1.00 17.57 ? 164 TRP A HZ2  1 
ATOM   2101 H HZ3  . TRP A 1 145 ? 11.098  17.865  17.721  1.00 15.99 ? 164 TRP A HZ3  1 
ATOM   2102 H HH2  . TRP A 1 145 ? 9.592   18.131  19.470  1.00 17.08 ? 164 TRP A HH2  1 
ATOM   2103 N N    . TRP A 1 146 ? 14.936  15.460  18.424  1.00 11.96 ? 165 TRP A N    1 
ATOM   2104 C CA   . TRP A 1 146 ? 13.841  14.593  17.997  1.00 11.96 ? 165 TRP A CA   1 
ATOM   2105 C C    . TRP A 1 146 ? 14.148  13.143  18.335  1.00 12.05 ? 165 TRP A C    1 
ATOM   2106 O O    . TRP A 1 146 ? 13.284  12.399  18.825  1.00 12.23 ? 165 TRP A O    1 
ATOM   2107 C CB   . TRP A 1 146 ? 13.639  14.768  16.480  1.00 12.20 ? 165 TRP A CB   1 
ATOM   2108 C CG   . TRP A 1 146 ? 12.415  14.059  15.917  1.00 11.92 ? 165 TRP A CG   1 
ATOM   2109 C CD1  . TRP A 1 146 ? 11.207  14.621  15.646  1.00 10.81 ? 165 TRP A CD1  1 
ATOM   2110 C CD2  . TRP A 1 146 ? 12.317  12.683  15.533  1.00 11.88 ? 165 TRP A CD2  1 
ATOM   2111 N NE1  . TRP A 1 146 ? 10.354  13.690  15.115  1.00 11.22 ? 165 TRP A NE1  1 
ATOM   2112 C CE2  . TRP A 1 146 ? 11.009  12.489  15.023  1.00 10.99 ? 165 TRP A CE2  1 
ATOM   2113 C CE3  . TRP A 1 146 ? 13.202  11.604  15.558  1.00 12.89 ? 165 TRP A CE3  1 
ATOM   2114 C CZ2  . TRP A 1 146 ? 10.549  11.251  14.590  1.00 11.90 ? 165 TRP A CZ2  1 
ATOM   2115 C CZ3  . TRP A 1 146 ? 12.752  10.377  15.122  1.00 11.97 ? 165 TRP A CZ3  1 
ATOM   2116 C CH2  . TRP A 1 146 ? 11.431  10.208  14.633  1.00 11.79 ? 165 TRP A CH2  1 
ATOM   2117 H H    . TRP A 1 146 ? 15.320  15.892  17.787  1.00 14.36 ? 165 TRP A H    1 
ATOM   2118 H HA   . TRP A 1 146 ? 13.019  14.838  18.450  1.00 14.35 ? 165 TRP A HA   1 
ATOM   2119 H HB2  . TRP A 1 146 ? 13.543  15.714  16.289  1.00 14.65 ? 165 TRP A HB2  1 
ATOM   2120 H HB3  . TRP A 1 146 ? 14.418  14.414  16.022  1.00 14.65 ? 165 TRP A HB3  1 
ATOM   2121 H HD1  . TRP A 1 146 ? 10.989  15.512  15.801  1.00 12.98 ? 165 TRP A HD1  1 
ATOM   2122 H HE1  . TRP A 1 146 ? 9.540   13.836  14.877  1.00 13.47 ? 165 TRP A HE1  1 
ATOM   2123 H HE3  . TRP A 1 146 ? 14.075  11.711  15.861  1.00 15.47 ? 165 TRP A HE3  1 
ATOM   2124 H HZ2  . TRP A 1 146 ? 9.678   11.137  14.285  1.00 14.28 ? 165 TRP A HZ2  1 
ATOM   2125 H HZ3  . TRP A 1 146 ? 13.325  9.645   15.150  1.00 14.37 ? 165 TRP A HZ3  1 
ATOM   2126 H HH2  . TRP A 1 146 ? 11.160  9.369   14.335  1.00 14.16 ? 165 TRP A HH2  1 
ATOM   2127 N N    . THR A 1 147 ? 15.383  12.720  18.071  1.00 12.79 ? 166 THR A N    1 
ATOM   2128 C CA   . THR A 1 147 ? 15.759  11.348  18.382  1.00 13.51 ? 166 THR A CA   1 
ATOM   2129 C C    . THR A 1 147 ? 15.849  11.127  19.886  1.00 13.67 ? 166 THR A C    1 
ATOM   2130 O O    . THR A 1 147 ? 15.613  10.010  20.360  1.00 14.01 ? 166 THR A O    1 
ATOM   2131 C CB   . THR A 1 147 ? 17.057  10.964  17.670  1.00 13.88 ? 166 THR A CB   1 
ATOM   2132 O OG1  . THR A 1 147 ? 18.111  11.861  18.033  1.00 14.13 ? 166 THR A OG1  1 
ATOM   2133 C CG2  . THR A 1 147 ? 16.846  10.994  16.145  1.00 14.26 ? 166 THR A CG2  1 
ATOM   2134 H H    . THR A 1 147 ? 16.006  13.197  17.719  1.00 15.35 ? 166 THR A H    1 
ATOM   2135 H HA   . THR A 1 147 ? 15.077  10.748  18.042  1.00 16.21 ? 166 THR A HA   1 
ATOM   2136 H HB   . THR A 1 147 ? 17.317  10.067  17.931  1.00 16.66 ? 166 THR A HB   1 
ATOM   2137 H HG1  . THR A 1 147 ? 18.701  11.868  17.435  1.00 16.96 ? 166 THR A HG1  1 
ATOM   2138 H HG21 . THR A 1 147 ? 17.660  10.726  15.692  1.00 17.12 ? 166 THR A HG21 1 
ATOM   2139 H HG22 . THR A 1 147 ? 16.132  10.386  15.897  1.00 17.12 ? 166 THR A HG22 1 
ATOM   2140 H HG23 . THR A 1 147 ? 16.608  11.891  15.861  1.00 17.12 ? 166 THR A HG23 1 
ATOM   2141 N N    . ASN A 1 148 ? 16.153  12.177  20.651  1.00 13.23 ? 167 ASN A N    1 
ATOM   2142 C CA   . ASN A 1 148 ? 16.112  12.070  22.108  1.00 14.78 ? 167 ASN A CA   1 
ATOM   2143 C C    . ASN A 1 148 ? 14.698  11.811  22.617  1.00 14.62 ? 167 ASN A C    1 
ATOM   2144 O O    . ASN A 1 148 ? 14.510  11.049  23.574  1.00 15.37 ? 167 ASN A O    1 
ATOM   2145 C CB   . ASN A 1 148 ? 16.657  13.344  22.765  1.00 17.04 ? 167 ASN A CB   1 
ATOM   2146 C CG   . ASN A 1 148 ? 18.163  13.374  22.841  1.00 19.56 ? 167 ASN A CG   1 
ATOM   2147 O OD1  . ASN A 1 148 ? 18.819  12.370  22.612  1.00 19.22 ? 167 ASN A OD1  1 
ATOM   2148 N ND2  . ASN A 1 148 ? 18.721  14.544  23.152  1.00 21.77 ? 167 ASN A ND2  1 
ATOM   2149 H H    . ASN A 1 148 ? 16.383  12.951  20.355  1.00 15.89 ? 167 ASN A H    1 
ATOM   2150 H HA   . ASN A 1 148 ? 16.678  11.323  22.359  1.00 17.74 ? 167 ASN A HA   1 
ATOM   2151 H HB2  . ASN A 1 148 ? 16.370  14.113  22.247  1.00 20.46 ? 167 ASN A HB2  1 
ATOM   2152 H HB3  . ASN A 1 148 ? 16.312  13.405  23.669  1.00 20.46 ? 167 ASN A HB3  1 
ATOM   2153 H HD21 . ASN A 1 148 ? 18.225  15.231  23.298  1.00 26.13 ? 167 ASN A HD21 1 
ATOM   2154 H HD22 . ASN A 1 148 ? 19.576  14.611  23.208  1.00 26.13 ? 167 ASN A HD22 1 
ATOM   2155 N N    . VAL A 1 149 ? 13.688  12.434  21.994  1.00 14.53 ? 168 VAL A N    1 
ATOM   2156 C CA   . VAL A 1 149 ? 12.307  12.162  22.387  1.00 14.20 ? 168 VAL A CA   1 
ATOM   2157 C C    . VAL A 1 149 ? 11.978  10.698  22.138  1.00 13.69 ? 168 VAL A C    1 
ATOM   2158 O O    . VAL A 1 149 ? 11.389  10.014  22.985  1.00 14.20 ? 168 VAL A O    1 
ATOM   2159 C CB   . VAL A 1 149 ? 11.333  13.102  21.653  1.00 13.41 ? 168 VAL A CB   1 
ATOM   2160 C CG1  . VAL A 1 149 ? 9.885   12.703  21.941  1.00 13.69 ? 168 VAL A CG1  1 
ATOM   2161 C CG2  . VAL A 1 149 ? 11.582  14.579  22.031  1.00 14.22 ? 168 VAL A CG2  1 
ATOM   2162 H H    . VAL A 1 149 ? 13.778  13.004  21.357  1.00 17.44 ? 168 VAL A H    1 
ATOM   2163 H HA   . VAL A 1 149 ? 12.214  12.336  23.337  1.00 17.04 ? 168 VAL A HA   1 
ATOM   2164 H HB   . VAL A 1 149 ? 11.488  13.017  20.699  1.00 16.10 ? 168 VAL A HB   1 
ATOM   2165 H HG11 . VAL A 1 149 ? 9.294   13.400  21.615  1.00 16.44 ? 168 VAL A HG11 1 
ATOM   2166 H HG12 . VAL A 1 149 ? 9.691   11.867  21.488  1.00 16.44 ? 168 VAL A HG12 1 
ATOM   2167 H HG13 . VAL A 1 149 ? 9.771   12.594  22.898  1.00 16.44 ? 168 VAL A HG13 1 
ATOM   2168 H HG21 . VAL A 1 149 ? 10.943  15.138  21.562  1.00 17.07 ? 168 VAL A HG21 1 
ATOM   2169 H HG22 . VAL A 1 149 ? 11.472  14.683  22.989  1.00 17.07 ? 168 VAL A HG22 1 
ATOM   2170 H HG23 . VAL A 1 149 ? 12.485  14.823  21.774  1.00 17.07 ? 168 VAL A HG23 1 
ATOM   2171 N N    . ALA A 1 150 ? 12.369  10.185  20.967  1.00 13.35 ? 169 ALA A N    1 
ATOM   2172 C CA   . ALA A 1 150 ? 12.129  8.772   20.685  1.00 13.24 ? 169 ALA A CA   1 
ATOM   2173 C C    . ALA A 1 150 ? 12.855  7.874   21.689  1.00 13.29 ? 169 ALA A C    1 
ATOM   2174 O O    . ALA A 1 150 ? 12.297  6.875   22.166  1.00 13.30 ? 169 ALA A O    1 
ATOM   2175 C CB   . ALA A 1 150 ? 12.601  8.427   19.276  1.00 14.40 ? 169 ALA A CB   1 
ATOM   2176 H H    . ALA A 1 150 ? 12.762  10.622  20.340  1.00 16.03 ? 169 ALA A H    1 
ATOM   2177 H HA   . ALA A 1 150 ? 11.175  8.609   20.747  1.00 15.89 ? 169 ALA A HA   1 
ATOM   2178 H HB1  . ALA A 1 150 ? 12.405  7.494   19.097  1.00 17.29 ? 169 ALA A HB1  1 
ATOM   2179 H HB2  . ALA A 1 150 ? 12.134  8.991   18.640  1.00 17.29 ? 169 ALA A HB2  1 
ATOM   2180 H HB3  . ALA A 1 150 ? 13.557  8.581   19.216  1.00 17.29 ? 169 ALA A HB3  1 
ATOM   2181 N N    . ALA A 1 151 ? 14.109  8.205   22.014  1.00 14.27 ? 170 ALA A N    1 
ATOM   2182 C CA   . ALA A 1 151 ? 14.875  7.379   22.944  1.00 13.93 ? 170 ALA A CA   1 
ATOM   2183 C C    . ALA A 1 151 ? 14.259  7.399   24.340  1.00 13.45 ? 170 ALA A C    1 
ATOM   2184 O O    . ALA A 1 151 ? 14.252  6.382   25.035  1.00 14.51 ? 170 ALA A O    1 
ATOM   2185 C CB   . ALA A 1 151 ? 16.329  7.843   22.970  1.00 14.27 ? 170 ALA A CB   1 
ATOM   2186 H H    . ALA A 1 151 ? 14.531  8.892   21.714  1.00 17.13 ? 170 ALA A H    1 
ATOM   2187 H HA   . ALA A 1 151 ? 14.864  6.458   22.637  1.00 16.72 ? 170 ALA A HA   1 
ATOM   2188 H HB1  . ALA A 1 151 ? 16.813  7.329   23.635  1.00 17.13 ? 170 ALA A HB1  1 
ATOM   2189 H HB2  . ALA A 1 151 ? 16.721  7.702   22.094  1.00 17.13 ? 170 ALA A HB2  1 
ATOM   2190 H HB3  . ALA A 1 151 ? 16.356  8.786   23.196  1.00 17.13 ? 170 ALA A HB3  1 
ATOM   2191 N N    . LYS A 1 152 ? 13.744  8.546   24.784  1.00 14.29 ? 171 LYS A N    1 
ATOM   2192 C CA   . LYS A 1 152 ? 13.086  8.587   26.088  1.00 14.46 ? 171 LYS A CA   1 
ATOM   2193 C C    . LYS A 1 152 ? 11.922  7.603   26.141  1.00 13.51 ? 171 LYS A C    1 
ATOM   2194 O O    . LYS A 1 152 ? 11.733  6.903   27.141  1.00 14.43 ? 171 LYS A O    1 
ATOM   2195 C CB   . LYS A 1 152 ? 12.615  10.008  26.408  1.00 16.62 ? 171 LYS A CB   1 
ATOM   2196 C CG   . LYS A 1 152 ? 11.973  10.122  27.770  1.00 20.38 ? 171 LYS A CG   1 
ATOM   2197 C CD   . LYS A 1 152 ? 11.490  11.543  28.099  1.00 25.00 ? 171 LYS A CD   1 
ATOM   2198 C CE   . LYS A 1 152 ? 12.609  12.551  28.127  1.00 29.26 ? 171 LYS A CE   1 
ATOM   2199 N NZ   . LYS A 1 152 ? 12.131  13.820  28.754  1.00 31.90 ? 171 LYS A NZ   1 
ATOM   2200 H H    . LYS A 1 152 ? 13.763  9.295   24.361  1.00 17.15 ? 171 LYS A H    1 
ATOM   2201 H HA   . LYS A 1 152 ? 13.728  8.335   26.770  1.00 17.36 ? 171 LYS A HA   1 
ATOM   2202 H HB2  . LYS A 1 152 ? 13.378  10.605  26.386  1.00 19.95 ? 171 LYS A HB2  1 
ATOM   2203 H HB3  . LYS A 1 152 ? 11.961  10.280  25.745  1.00 19.95 ? 171 LYS A HB3  1 
ATOM   2204 H HG2  . LYS A 1 152 ? 11.204  9.532   27.805  1.00 24.46 ? 171 LYS A HG2  1 
ATOM   2205 H HG3  . LYS A 1 152 ? 12.620  9.865   28.445  1.00 24.46 ? 171 LYS A HG3  1 
ATOM   2206 H HD2  . LYS A 1 152 ? 10.851  11.824  27.425  1.00 30.00 ? 171 LYS A HD2  1 
ATOM   2207 H HD3  . LYS A 1 152 ? 11.069  11.539  28.973  1.00 30.00 ? 171 LYS A HD3  1 
ATOM   2208 H HE2  . LYS A 1 152 ? 13.350  12.205  28.649  1.00 35.12 ? 171 LYS A HE2  1 
ATOM   2209 H HE3  . LYS A 1 152 ? 12.902  12.742  27.222  1.00 35.12 ? 171 LYS A HE3  1 
ATOM   2210 H HZ1  . LYS A 1 152 ? 11.799  13.653  29.563  1.00 38.28 ? 171 LYS A HZ1  1 
ATOM   2211 H HZ2  . LYS A 1 152 ? 12.807  14.394  28.832  1.00 38.28 ? 171 LYS A HZ2  1 
ATOM   2212 H HZ3  . LYS A 1 152 ? 11.496  14.188  28.251  1.00 38.28 ? 171 LYS A HZ3  1 
ATOM   2213 N N    . ALA A 1 153 ? 11.154  7.504   25.055  1.00 12.79 ? 172 ALA A N    1 
ATOM   2214 C CA   . ALA A 1 153 ? 9.987   6.629   25.040  1.00 13.21 ? 172 ALA A CA   1 
ATOM   2215 C C    . ALA A 1 153 ? 10.353  5.148   24.978  1.00 13.03 ? 172 ALA A C    1 
ATOM   2216 O O    . ALA A 1 153 ? 9.607   4.318   25.517  1.00 13.05 ? 172 ALA A O    1 
ATOM   2217 C CB   . ALA A 1 153 ? 9.107   6.980   23.839  1.00 13.31 ? 172 ALA A CB   1 
ATOM   2218 H H    . ALA A 1 153 ? 11.287  7.930   24.321  1.00 15.36 ? 172 ALA A H    1 
ATOM   2219 H HA   . ALA A 1 153 ? 9.495   6.775   25.863  1.00 15.86 ? 172 ALA A HA   1 
ATOM   2220 H HB1  . ALA A 1 153 ? 8.388   6.332   23.774  1.00 15.98 ? 172 ALA A HB1  1 
ATOM   2221 H HB2  . ALA A 1 153 ? 8.740   7.869   23.965  1.00 15.98 ? 172 ALA A HB2  1 
ATOM   2222 H HB3  . ALA A 1 153 ? 9.647   6.955   23.034  1.00 15.98 ? 172 ALA A HB3  1 
ATOM   2223 N N    . VAL A 1 154 ? 11.458  4.792   24.310  1.00 13.39 ? 173 VAL A N    1 
ATOM   2224 C CA   . VAL A 1 154 ? 11.774  3.393   24.051  1.00 14.64 ? 173 VAL A CA   1 
ATOM   2225 C C    . VAL A 1 154 ? 12.949  2.861   24.863  1.00 15.25 ? 173 VAL A C    1 
ATOM   2226 O O    . VAL A 1 154 ? 12.965  1.666   25.192  1.00 15.97 ? 173 VAL A O    1 
ATOM   2227 C CB   . VAL A 1 154 ? 11.952  3.067   22.556  1.00 17.42 ? 173 VAL A CB   1 
ATOM   2228 C CG1  . VAL A 1 154 ? 10.866  3.720   21.716  1.00 16.06 ? 173 VAL A CG1  1 
ATOM   2229 C CG2  . VAL A 1 154 ? 13.330  3.448   22.073  1.00 19.50 ? 173 VAL A CG2  1 
ATOM   2230 H H    . VAL A 1 154 ? 12.036  5.346   23.999  1.00 16.07 ? 173 VAL A H    1 
ATOM   2231 H HA   . VAL A 1 154 ? 10.997  2.893   24.346  1.00 17.57 ? 173 VAL A HA   1 
ATOM   2232 H HB   . VAL A 1 154 ? 11.863  2.107   22.444  1.00 20.91 ? 173 VAL A HB   1 
ATOM   2233 H HG11 . VAL A 1 154 ? 10.977  3.450   20.791  1.00 19.28 ? 173 VAL A HG11 1 
ATOM   2234 H HG12 . VAL A 1 154 ? 9.999   3.434   22.043  1.00 19.28 ? 173 VAL A HG12 1 
ATOM   2235 H HG13 . VAL A 1 154 ? 10.946  4.684   21.790  1.00 19.28 ? 173 VAL A HG13 1 
ATOM   2236 H HG21 . VAL A 1 154 ? 13.341  3.429   21.104  1.00 23.40 ? 173 VAL A HG21 1 
ATOM   2237 H HG22 . VAL A 1 154 ? 13.539  4.341   22.389  1.00 23.40 ? 173 VAL A HG22 1 
ATOM   2238 H HG23 . VAL A 1 154 ? 13.974  2.814   22.425  1.00 23.40 ? 173 VAL A HG23 1 
ATOM   2239 N N    . VAL A 1 155 ? 13.945  3.684   25.161  1.00 15.19 ? 174 VAL A N    1 
ATOM   2240 C CA   . VAL A 1 155 ? 15.056  3.237   25.987  1.00 16.23 ? 174 VAL A CA   1 
ATOM   2241 C C    . VAL A 1 155 ? 14.695  3.366   27.459  1.00 16.42 ? 174 VAL A C    1 
ATOM   2242 O O    . VAL A 1 155 ? 14.579  2.368   28.183  1.00 18.06 ? 174 VAL A O    1 
ATOM   2243 C CB   . VAL A 1 155 ? 16.340  4.008   25.634  1.00 16.75 ? 174 VAL A CB   1 
ATOM   2244 C CG1  . VAL A 1 155 ? 17.495  3.530   26.536  1.00 17.21 ? 174 VAL A CG1  1 
ATOM   2245 C CG2  . VAL A 1 155 ? 16.706  3.827   24.155  1.00 16.85 ? 174 VAL A CG2  1 
ATOM   2246 H H    . VAL A 1 155 ? 14.001  4.502   24.899  1.00 18.23 ? 174 VAL A H    1 
ATOM   2247 H HA   . VAL A 1 155 ? 15.228  2.300   25.804  1.00 19.49 ? 174 VAL A HA   1 
ATOM   2248 H HB   . VAL A 1 155 ? 16.191  4.955   25.784  1.00 20.11 ? 174 VAL A HB   1 
ATOM   2249 H HG11 . VAL A 1 155 ? 18.331  3.881   26.191  1.00 20.66 ? 174 VAL A HG11 1 
ATOM   2250 H HG12 . VAL A 1 155 ? 17.347  3.856   27.438  1.00 20.66 ? 174 VAL A HG12 1 
ATOM   2251 H HG13 . VAL A 1 155 ? 17.517  2.561   26.534  1.00 20.66 ? 174 VAL A HG13 1 
ATOM   2252 H HG21 . VAL A 1 155 ? 17.512  4.333   23.965  1.00 20.23 ? 174 VAL A HG21 1 
ATOM   2253 H HG22 . VAL A 1 155 ? 16.858  2.886   23.980  1.00 20.23 ? 174 VAL A HG22 1 
ATOM   2254 H HG23 . VAL A 1 155 ? 15.975  4.152   23.607  1.00 20.23 ? 174 VAL A HG23 1 
ATOM   2255 N N    . ASP A 1 156 ? 14.427  4.596   27.906  1.00 16.94 ? 175 ASP A N    1 
ATOM   2256 C CA   . ASP A 1 156 ? 14.051  4.794   29.298  1.00 18.34 ? 175 ASP A CA   1 
ATOM   2257 C C    . ASP A 1 156 ? 12.644  4.295   29.580  1.00 17.13 ? 175 ASP A C    1 
ATOM   2258 O O    . ASP A 1 156 ? 12.359  3.815   30.683  1.00 18.99 ? 175 ASP A O    1 
ATOM   2259 C CB   . ASP A 1 156 ? 14.156  6.270   29.658  1.00 21.42 ? 175 ASP A CB   1 
ATOM   2260 C CG   . ASP A 1 156 ? 15.537  6.831   29.392  1.00 26.80 ? 175 ASP A CG   1 
ATOM   2261 O OD1  . ASP A 1 156 ? 16.526  6.064   29.466  1.00 29.72 ? 175 ASP A OD1  1 
ATOM   2262 O OD2  . ASP A 1 156 ? 15.629  8.037   29.121  1.00 29.23 ? 175 ASP A OD2  1 
ATOM   2263 H H    . ASP A 1 156 ? 14.457  5.312   27.432  1.00 20.33 ? 175 ASP A H    1 
ATOM   2264 H HA   . ASP A 1 156 ? 14.666  4.296   29.859  1.00 22.02 ? 175 ASP A HA   1 
ATOM   2265 H HB2  . ASP A 1 156 ? 13.519  6.773   29.127  1.00 25.72 ? 175 ASP A HB2  1 
ATOM   2266 H HB3  . ASP A 1 156 ? 13.962  6.382   30.602  1.00 25.72 ? 175 ASP A HB3  1 
ATOM   2267 N N    . GLY A 1 157 ? 11.744  4.430   28.619  1.00 15.20 ? 176 GLY A N    1 
ATOM   2268 C CA   . GLY A 1 157 ? 10.377  3.986   28.770  1.00 14.52 ? 176 GLY A CA   1 
ATOM   2269 C C    . GLY A 1 157 ? 10.206  2.537   28.362  1.00 14.16 ? 176 GLY A C    1 
ATOM   2270 O O    . GLY A 1 157 ? 11.163  1.812   28.095  1.00 15.19 ? 176 GLY A O    1 
ATOM   2271 H H    . GLY A 1 157 ? 11.909  4.784   27.852  1.00 18.24 ? 176 GLY A H    1 
ATOM   2272 H HA2  . GLY A 1 157 ? 10.109  4.079   29.698  1.00 17.43 ? 176 GLY A HA2  1 
ATOM   2273 H HA3  . GLY A 1 157 ? 9.797   4.533   28.218  1.00 17.43 ? 176 GLY A HA3  1 
ATOM   2274 N N    . THR A 1 158 ? 8.949   2.135   28.254  1.00 13.25 ? 177 THR A N    1 
ATOM   2275 C CA   . THR A 1 158 ? 8.560   0.737   28.114  1.00 13.36 ? 177 THR A CA   1 
ATOM   2276 C C    . THR A 1 158 ? 8.171   0.368   26.692  1.00 12.88 ? 177 THR A C    1 
ATOM   2277 O O    . THR A 1 158 ? 7.913   -0.805  26.421  1.00 13.64 ? 177 THR A O    1 
ATOM   2278 C CB   . THR A 1 158 ? 7.428   0.467   29.109  1.00 14.14 ? 177 THR A CB   1 
ATOM   2279 O OG1  . THR A 1 158 ? 7.901   0.854   30.406  1.00 16.16 ? 177 THR A OG1  1 
ATOM   2280 C CG2  . THR A 1 158 ? 6.994   -0.996  29.150  1.00 14.32 ? 177 THR A CG2  1 
ATOM   2281 H H    . THR A 1 158 ? 8.277   2.671   28.259  1.00 15.90 ? 177 THR A H    1 
ATOM   2282 H HA   . THR A 1 158 ? 9.298   0.147   28.334  1.00 16.04 ? 177 THR A HA   1 
ATOM   2283 H HB   . THR A 1 158 ? 6.642   0.968   28.841  1.00 16.97 ? 177 THR A HB   1 
ATOM   2284 H HG1  . THR A 1 158 ? 7.332   0.655   30.990  1.00 19.40 ? 177 THR A HG1  1 
ATOM   2285 H HG21 . THR A 1 158 ? 6.415   -1.149  29.913  1.00 17.19 ? 177 THR A HG21 1 
ATOM   2286 H HG22 . THR A 1 158 ? 6.512   -1.222  28.339  1.00 17.19 ? 177 THR A HG22 1 
ATOM   2287 H HG23 . THR A 1 158 ? 7.771   -1.571  29.225  1.00 17.19 ? 177 THR A HG23 1 
ATOM   2288 N N    . CYS A 1 159 ? 8.175   1.314   25.764  1.00 12.83 ? 178 CYS A N    1 
ATOM   2289 C CA   . CYS A 1 159 ? 7.897   0.942   24.385  1.00 11.46 ? 178 CYS A CA   1 
ATOM   2290 C C    . CYS A 1 159 ? 9.069   0.183   23.769  1.00 11.82 ? 178 CYS A C    1 
ATOM   2291 O O    . CYS A 1 159 ? 10.215  0.272   24.220  1.00 13.15 ? 178 CYS A O    1 
ATOM   2292 C CB   . CYS A 1 159 ? 7.560   2.189   23.560  1.00 12.40 ? 178 CYS A CB   1 
ATOM   2293 S SG   . CYS A 1 159 ? 5.900   2.840   23.880  1.00 12.41 ? 178 CYS A SG   1 
ATOM   2294 H H    . CYS A 1 159 ? 8.330   2.149   25.901  1.00 15.40 ? 178 CYS A H    1 
ATOM   2295 H HA   . CYS A 1 159 ? 7.131   0.348   24.359  1.00 13.76 ? 178 CYS A HA   1 
ATOM   2296 H HB2  . CYS A 1 159 ? 8.199   2.887   23.773  1.00 14.89 ? 178 CYS A HB2  1 
ATOM   2297 H HB3  . CYS A 1 159 ? 7.615   1.966   22.618  1.00 14.89 ? 178 CYS A HB3  1 
ATOM   2298 H HG   . CYS A 1 159 ? 5.095   1.976   23.667  1.00 14.89 ? 178 CYS A HG   1 
ATOM   2299 N N    . ASP A 1 160 ? 8.763   -0.536  22.689  1.00 11.53 ? 179 ASP A N    1 
ATOM   2300 C CA   . ASP A 1 160 ? 9.725   -1.397  22.012  1.00 10.74 ? 179 ASP A CA   1 
ATOM   2301 C C    . ASP A 1 160 ? 10.212  -0.808  20.706  1.00 10.91 ? 179 ASP A C    1 
ATOM   2302 O O    . ASP A 1 160 ? 11.042  -1.426  20.039  1.00 11.70 ? 179 ASP A O    1 
ATOM   2303 C CB   . ASP A 1 160 ? 9.129   -2.781  21.769  1.00 11.47 ? 179 ASP A CB   1 
ATOM   2304 C CG   . ASP A 1 160 ? 8.691   -3.404  23.050  1.00 11.87 ? 179 ASP A CG   1 
ATOM   2305 O OD1  . ASP A 1 160 ? 9.569   -3.796  23.847  1.00 13.98 ? 179 ASP A OD1  1 
ATOM   2306 O OD2  . ASP A 1 160 ? 7.464   -3.443  23.301  1.00 12.30 ? 179 ASP A OD2  1 
ATOM   2307 H H    . ASP A 1 160 ? 7.985   -0.541  22.323  1.00 13.84 ? 179 ASP A H    1 
ATOM   2308 H HA   . ASP A 1 160 ? 10.494  -1.515  22.591  1.00 12.89 ? 179 ASP A HA   1 
ATOM   2309 H HB2  . ASP A 1 160 ? 8.358   -2.702  21.186  1.00 13.77 ? 179 ASP A HB2  1 
ATOM   2310 H HB3  . ASP A 1 160 ? 9.797   -3.353  21.361  1.00 13.77 ? 179 ASP A HB3  1 
ATOM   2311 N N    . GLY A 1 161 ? 9.717   0.359   20.329  1.00 11.02 ? 180 GLY A N    1 
ATOM   2312 C CA   . GLY A 1 161 ? 10.091  0.956   19.068  1.00 10.70 ? 180 GLY A CA   1 
ATOM   2313 C C    . GLY A 1 161 ? 9.264   2.195   18.816  1.00 10.33 ? 180 GLY A C    1 
ATOM   2314 O O    . GLY A 1 161 ? 8.468   2.632   19.653  1.00 10.90 ? 180 GLY A O    1 
ATOM   2315 H H    . GLY A 1 161 ? 9.159   0.825   20.790  1.00 13.23 ? 180 GLY A H    1 
ATOM   2316 H HA2  . GLY A 1 161 ? 11.030  1.201   19.084  1.00 12.84 ? 180 GLY A HA2  1 
ATOM   2317 H HA3  . GLY A 1 161 ? 9.942   0.325   18.346  1.00 12.84 ? 180 GLY A HA3  1 
ATOM   2318 N N    . VAL A 1 162 ? 9.482   2.760   17.630  1.00 10.60 ? 181 VAL A N    1 
ATOM   2319 C CA   . VAL A 1 162 ? 8.908   4.040   17.234  1.00 11.09 ? 181 VAL A CA   1 
ATOM   2320 C C    . VAL A 1 162 ? 8.267   3.903   15.859  1.00 10.96 ? 181 VAL A C    1 
ATOM   2321 O O    . VAL A 1 162 ? 8.750   3.161   14.996  1.00 11.57 ? 181 VAL A O    1 
ATOM   2322 C CB   . VAL A 1 162 ? 10.000  5.136   17.255  1.00 11.17 ? 181 VAL A CB   1 
ATOM   2323 C CG1  . VAL A 1 162 ? 11.156  4.810   16.317  1.00 12.30 ? 181 VAL A CG1  1 
ATOM   2324 C CG2  . VAL A 1 162 ? 9.444   6.509   16.960  1.00 11.97 ? 181 VAL A CG2  1 
ATOM   2325 H H    . VAL A 1 162 ? 9.974   2.407   17.019  1.00 12.73 ? 181 VAL A H    1 
ATOM   2326 H HA   . VAL A 1 162 ? 8.196   4.296   17.841  1.00 13.32 ? 181 VAL A HA   1 
ATOM   2327 H HB   . VAL A 1 162 ? 10.351  5.156   18.159  1.00 13.41 ? 181 VAL A HB   1 
ATOM   2328 H HG11 . VAL A 1 162 ? 11.827  5.507   16.388  1.00 14.76 ? 181 VAL A HG11 1 
ATOM   2329 H HG12 . VAL A 1 162 ? 11.539  3.956   16.572  1.00 14.76 ? 181 VAL A HG12 1 
ATOM   2330 H HG13 . VAL A 1 162 ? 10.822  4.764   15.407  1.00 14.76 ? 181 VAL A HG13 1 
ATOM   2331 H HG21 . VAL A 1 162 ? 10.139  7.169   17.108  1.00 14.37 ? 181 VAL A HG21 1 
ATOM   2332 H HG22 . VAL A 1 162 ? 9.149   6.539   16.037  1.00 14.37 ? 181 VAL A HG22 1 
ATOM   2333 H HG23 . VAL A 1 162 ? 8.694   6.679   17.552  1.00 14.37 ? 181 VAL A HG23 1 
ATOM   2334 N N    . PHE A 1 163 ? 7.149   4.616   15.666  1.00 9.71  ? 182 PHE A N    1 
ATOM   2335 C CA   . PHE A 1 163 ? 6.444   4.709   14.387  1.00 9.95  ? 182 PHE A CA   1 
ATOM   2336 C C    . PHE A 1 163 ? 6.742   6.095   13.821  1.00 10.73 ? 182 PHE A C    1 
ATOM   2337 O O    . PHE A 1 163 ? 6.293   7.105   14.374  1.00 11.74 ? 182 PHE A O    1 
ATOM   2338 C CB   . PHE A 1 163 ? 4.930   4.522   14.562  1.00 10.07 ? 182 PHE A CB   1 
ATOM   2339 C CG   . PHE A 1 163 ? 4.146   4.486   13.264  1.00 11.17 ? 182 PHE A CG   1 
ATOM   2340 C CD1  . PHE A 1 163 ? 3.680   5.647   12.675  1.00 12.01 ? 182 PHE A CD1  1 
ATOM   2341 C CD2  . PHE A 1 163 ? 3.828   3.281   12.664  1.00 11.63 ? 182 PHE A CD2  1 
ATOM   2342 C CE1  . PHE A 1 163 ? 2.937   5.595   11.500  1.00 12.34 ? 182 PHE A CE1  1 
ATOM   2343 C CE2  . PHE A 1 163 ? 3.096   3.240   11.490  1.00 13.03 ? 182 PHE A CE2  1 
ATOM   2344 C CZ   . PHE A 1 163 ? 2.660   4.394   10.912  1.00 12.83 ? 182 PHE A CZ   1 
ATOM   2345 H H    . PHE A 1 163 ? 6.768   5.072   16.288  1.00 11.65 ? 182 PHE A H    1 
ATOM   2346 H HA   . PHE A 1 163 ? 6.765   4.019   13.785  1.00 11.94 ? 182 PHE A HA   1 
ATOM   2347 H HB2  . PHE A 1 163 ? 4.774   3.682   15.022  1.00 12.09 ? 182 PHE A HB2  1 
ATOM   2348 H HB3  . PHE A 1 163 ? 4.587   5.259   15.091  1.00 12.09 ? 182 PHE A HB3  1 
ATOM   2349 H HD1  . PHE A 1 163 ? 3.866   6.469   13.067  1.00 14.42 ? 182 PHE A HD1  1 
ATOM   2350 H HD2  . PHE A 1 163 ? 4.111   2.487   13.056  1.00 13.96 ? 182 PHE A HD2  1 
ATOM   2351 H HE1  . PHE A 1 163 ? 2.627   6.382   11.114  1.00 14.82 ? 182 PHE A HE1  1 
ATOM   2352 H HE2  . PHE A 1 163 ? 2.901   2.422   11.094  1.00 15.64 ? 182 PHE A HE2  1 
ATOM   2353 H HZ   . PHE A 1 163 ? 2.176   4.364   10.119  1.00 15.40 ? 182 PHE A HZ   1 
ATOM   2354 N N    . MET A 1 164 ? 7.506   6.130   12.733  1.00 10.55 ? 183 MET A N    1 
ATOM   2355 C CA   . MET A 1 164 ? 7.970   7.347   12.085  1.00 11.27 ? 183 MET A CA   1 
ATOM   2356 C C    . MET A 1 164 ? 7.020   7.643   10.932  1.00 10.24 ? 183 MET A C    1 
ATOM   2357 O O    . MET A 1 164 ? 7.100   7.028   9.868   1.00 11.46 ? 183 MET A O    1 
ATOM   2358 C CB   . MET A 1 164 ? 9.395   7.122   11.582  1.00 10.57 ? 183 MET A CB   1 
ATOM   2359 C CG   . MET A 1 164 ? 10.407  6.863   12.686  1.00 12.64 ? 183 MET A CG   1 
ATOM   2360 S SD   . MET A 1 164 ? 12.097  6.666   12.067  1.00 13.42 ? 183 MET A SD   1 
ATOM   2361 C CE   . MET A 1 164 ? 12.502  8.365   11.670  1.00 13.17 ? 183 MET A CE   1 
ATOM   2362 H H    . MET A 1 164 ? 7.783   5.421   12.333  1.00 12.67 ? 183 MET A H    1 
ATOM   2363 H HA   . MET A 1 164 ? 7.959   8.092   12.706  1.00 13.54 ? 183 MET A HA   1 
ATOM   2364 H HB2  . MET A 1 164 ? 9.398   6.352   10.992  1.00 12.69 ? 183 MET A HB2  1 
ATOM   2365 H HB3  . MET A 1 164 ? 9.682   7.912   11.098  1.00 12.69 ? 183 MET A HB3  1 
ATOM   2366 H HG2  . MET A 1 164 ? 10.400  7.613   13.302  1.00 15.18 ? 183 MET A HG2  1 
ATOM   2367 H HG3  . MET A 1 164 ? 10.163  6.048   13.153  1.00 15.18 ? 183 MET A HG3  1 
ATOM   2368 H HE1  . MET A 1 164 ? 13.400  8.398   11.306  1.00 15.81 ? 183 MET A HE1  1 
ATOM   2369 H HE2  . MET A 1 164 ? 11.867  8.696   11.016  1.00 15.81 ? 183 MET A HE2  1 
ATOM   2370 H HE3  . MET A 1 164 ? 12.453  8.898   12.479  1.00 15.81 ? 183 MET A HE3  1 
ATOM   2371 N N    . ASP A 1 165 ? 6.098   8.572   11.147  1.00 11.28 ? 184 ASP A N    1 
ATOM   2372 C CA   . ASP A 1 165 ? 5.073   8.863   10.157  1.00 11.66 ? 184 ASP A CA   1 
ATOM   2373 C C    . ASP A 1 165 ? 5.563   9.931   9.177   1.00 12.55 ? 184 ASP A C    1 
ATOM   2374 O O    . ASP A 1 165 ? 6.572   10.594  9.398   1.00 13.52 ? 184 ASP A O    1 
ATOM   2375 C CB   . ASP A 1 165 ? 3.801   9.341   10.873  1.00 12.08 ? 184 ASP A CB   1 
ATOM   2376 C CG   . ASP A 1 165 ? 2.534   9.126   10.075  1.00 12.28 ? 184 ASP A CG   1 
ATOM   2377 O OD1  . ASP A 1 165 ? 2.573   8.647   8.919   1.00 13.85 ? 184 ASP A OD1  1 
ATOM   2378 O OD2  . ASP A 1 165 ? 1.446   9.442   10.614  1.00 12.90 ? 184 ASP A OD2  1 
ATOM   2379 H H    . ASP A 1 165 ? 6.045   9.048   11.861  1.00 13.54 ? 184 ASP A H    1 
ATOM   2380 H HA   . ASP A 1 165 ? 4.869   8.063   9.649   1.00 14.00 ? 184 ASP A HA   1 
ATOM   2381 H HB2  . ASP A 1 165 ? 3.711   8.855   11.708  1.00 14.50 ? 184 ASP A HB2  1 
ATOM   2382 H HB3  . ASP A 1 165 ? 3.881   10.292  11.051  1.00 14.50 ? 184 ASP A HB3  1 
ATOM   2383 N N    . ALA A 1 166 ? 4.817   10.094  8.081   1.00 12.49 ? 185 ALA A N    1 
ATOM   2384 C CA   . ALA A 1 166 ? 4.822   11.267  7.210   1.00 12.75 ? 185 ALA A CA   1 
ATOM   2385 C C    . ALA A 1 166 ? 5.926   11.301  6.163   1.00 12.13 ? 185 ALA A C    1 
ATOM   2386 O O    . ALA A 1 166 ? 6.202   12.378  5.608   1.00 12.82 ? 185 ALA A O    1 
ATOM   2387 C CB   . ALA A 1 166 ? 4.801   12.569  8.013   1.00 13.39 ? 185 ALA A CB   1 
ATOM   2388 H H    . ALA A 1 166 ? 4.264   9.496   7.807   1.00 14.99 ? 185 ALA A H    1 
ATOM   2389 H HA   . ALA A 1 166 ? 4.004   11.218  6.690   1.00 15.31 ? 185 ALA A HA   1 
ATOM   2390 H HB1  . ALA A 1 166 ? 4.597   13.305  7.416   1.00 16.07 ? 185 ALA A HB1  1 
ATOM   2391 H HB2  . ALA A 1 166 ? 4.122   12.504  8.702   1.00 16.07 ? 185 ALA A HB2  1 
ATOM   2392 H HB3  . ALA A 1 166 ? 5.672   12.703  8.419   1.00 16.07 ? 185 ALA A HB3  1 
ATOM   2393 N N    . PHE A 1 167 ? 6.533   10.158  5.818   1.00 12.03 ? 186 PHE A N    1 
ATOM   2394 C CA   . PHE A 1 167 ? 7.590   10.201  4.809   1.00 11.89 ? 186 PHE A CA   1 
ATOM   2395 C C    . PHE A 1 167 ? 7.068   10.746  3.473   1.00 13.02 ? 186 PHE A C    1 
ATOM   2396 O O    . PHE A 1 167 ? 7.792   11.525  2.826   1.00 13.66 ? 186 PHE A O    1 
ATOM   2397 C CB   . PHE A 1 167 ? 8.250   8.826   4.621   1.00 12.64 ? 186 PHE A CB   1 
ATOM   2398 C CG   . PHE A 1 167 ? 9.188   8.408   5.727   1.00 12.15 ? 186 PHE A CG   1 
ATOM   2399 C CD1  . PHE A 1 167 ? 9.095   8.901   7.027   1.00 12.31 ? 186 PHE A CD1  1 
ATOM   2400 C CD2  . PHE A 1 167 ? 10.131  7.426   5.463   1.00 13.37 ? 186 PHE A CD2  1 
ATOM   2401 C CE1  . PHE A 1 167 ? 9.955   8.425   8.027   1.00 11.55 ? 186 PHE A CE1  1 
ATOM   2402 C CE2  . PHE A 1 167 ? 10.984  6.951   6.443   1.00 12.96 ? 186 PHE A CE2  1 
ATOM   2403 C CZ   . PHE A 1 167 ? 10.909  7.464   7.726   1.00 12.38 ? 186 PHE A CZ   1 
ATOM   2404 H H    . PHE A 1 167 ? 6.358   9.380   6.140   1.00 14.44 ? 186 PHE A H    1 
ATOM   2405 H HA   . PHE A 1 167 ? 8.287   10.788  5.141   1.00 14.28 ? 186 PHE A HA   1 
ATOM   2406 H HB2  . PHE A 1 167 ? 7.551   8.156   4.565   1.00 15.17 ? 186 PHE A HB2  1 
ATOM   2407 H HB3  . PHE A 1 167 ? 8.762   8.842   3.797   1.00 15.17 ? 186 PHE A HB3  1 
ATOM   2408 H HD1  . PHE A 1 167 ? 8.460   9.549   7.232   1.00 14.78 ? 186 PHE A HD1  1 
ATOM   2409 H HD2  . PHE A 1 167 ? 10.191  7.077   4.604   1.00 16.05 ? 186 PHE A HD2  1 
ATOM   2410 H HE1  . PHE A 1 167 ? 9.885   8.754   8.895   1.00 13.86 ? 186 PHE A HE1  1 
ATOM   2411 H HE2  . PHE A 1 167 ? 11.606  6.290   6.241   1.00 15.56 ? 186 PHE A HE2  1 
ATOM   2412 H HZ   . PHE A 1 167 ? 11.496  7.167   8.383   1.00 14.86 ? 186 PHE A HZ   1 
ATOM   2413 N N    . PRO A 1 168 ? 5.882   10.364  2.983   1.00 13.19 ? 187 PRO A N    1 
ATOM   2414 C CA   . PRO A 1 168 ? 5.423   10.926  1.700   1.00 14.30 ? 187 PRO A CA   1 
ATOM   2415 C C    . PRO A 1 168 ? 5.316   12.443  1.739   1.00 14.60 ? 187 PRO A C    1 
ATOM   2416 O O    . PRO A 1 168 ? 5.561   13.118  0.727   1.00 16.14 ? 187 PRO A O    1 
ATOM   2417 C CB   . PRO A 1 168 ? 4.066   10.229  1.477   1.00 15.34 ? 187 PRO A CB   1 
ATOM   2418 C CG   . PRO A 1 168 ? 4.161   8.949   2.253   1.00 16.00 ? 187 PRO A CG   1 
ATOM   2419 C CD   . PRO A 1 168 ? 4.969   9.313   3.483   1.00 14.86 ? 187 PRO A CD   1 
ATOM   2420 H HA   . PRO A 1 168 ? 6.012   10.670  0.974   1.00 17.17 ? 187 PRO A HA   1 
ATOM   2421 H HB2  . PRO A 1 168 ? 3.348   10.788  1.814   1.00 18.42 ? 187 PRO A HB2  1 
ATOM   2422 H HB3  . PRO A 1 168 ? 3.935   10.055  0.532   1.00 18.42 ? 187 PRO A HB3  1 
ATOM   2423 H HG2  . PRO A 1 168 ? 3.274   8.641   2.497   1.00 19.20 ? 187 PRO A HG2  1 
ATOM   2424 H HG3  . PRO A 1 168 ? 4.614   8.273   1.726   1.00 19.20 ? 187 PRO A HG3  1 
ATOM   2425 H HD2  . PRO A 1 168 ? 4.395   9.658   4.185   1.00 17.84 ? 187 PRO A HD2  1 
ATOM   2426 H HD3  . PRO A 1 168 ? 5.468   8.547   3.808   1.00 17.84 ? 187 PRO A HD3  1 
ATOM   2427 N N    A GLN A 1 169 ? 4.923   13.020  2.881   0.61 14.14 ? 188 GLN A N    1 
ATOM   2428 N N    B GLN A 1 169 ? 4.963   12.998  2.895   0.39 15.02 ? 188 GLN A N    1 
ATOM   2429 C CA   A GLN A 1 169 ? 4.827   14.475  2.972   0.61 13.18 ? 188 GLN A CA   1 
ATOM   2430 C CA   B GLN A 1 169 ? 4.805   14.440  3.024   0.39 15.14 ? 188 GLN A CA   1 
ATOM   2431 C C    A GLN A 1 169 ? 6.200   15.121  2.882   0.61 13.63 ? 188 GLN A C    1 
ATOM   2432 C C    B GLN A 1 169 ? 6.153   15.154  2.998   0.39 14.49 ? 188 GLN A C    1 
ATOM   2433 O O    A GLN A 1 169 ? 6.353   16.179  2.255   0.61 14.17 ? 188 GLN A O    1 
ATOM   2434 O O    B GLN A 1 169 ? 6.242   16.282  2.495   0.39 14.76 ? 188 GLN A O    1 
ATOM   2435 C CB   A GLN A 1 169 ? 4.139   14.862  4.282   0.61 13.08 ? 188 GLN A CB   1 
ATOM   2436 C CB   B GLN A 1 169 ? 3.982   14.694  4.292   0.39 16.34 ? 188 GLN A CB   1 
ATOM   2437 C CG   A GLN A 1 169 ? 2.636   14.681  4.269   0.61 13.43 ? 188 GLN A CG   1 
ATOM   2438 C CG   B GLN A 1 169 ? 2.512   14.163  4.190   0.39 17.64 ? 188 GLN A CG   1 
ATOM   2439 C CD   A GLN A 1 169 ? 2.032   14.986  5.616   0.61 14.32 ? 188 GLN A CD   1 
ATOM   2440 C CD   B GLN A 1 169 ? 2.211   12.854  4.965   0.39 19.86 ? 188 GLN A CD   1 
ATOM   2441 O OE1  A GLN A 1 169 ? 1.917   16.152  6.015   0.61 15.14 ? 188 GLN A OE1  1 
ATOM   2442 O OE1  B GLN A 1 169 ? 2.624   11.744  4.591   0.39 19.06 ? 188 GLN A OE1  1 
ATOM   2443 N NE2  A GLN A 1 169 ? 1.642   13.947  6.330   0.61 15.83 ? 188 GLN A NE2  1 
ATOM   2444 N NE2  B GLN A 1 169 ? 1.448   12.997  6.041   0.39 21.45 ? 188 GLN A NE2  1 
ATOM   2445 H H    A GLN A 1 169 ? 4.712   12.598  3.600   0.61 16.97 ? 188 GLN A H    1 
ATOM   2446 H H    B GLN A 1 169 ? 4.809   12.561  3.619   0.39 18.04 ? 188 GLN A H    1 
ATOM   2447 H HA   A GLN A 1 169 ? 4.290   14.806  2.234   0.61 15.82 ? 188 GLN A HA   1 
ATOM   2448 H HA   B GLN A 1 169 ? 4.314   14.824  2.281   0.39 18.18 ? 188 GLN A HA   1 
ATOM   2449 H HB2  A GLN A 1 169 ? 4.496   14.309  4.995   0.61 15.71 ? 188 GLN A HB2  1 
ATOM   2450 H HB2  B GLN A 1 169 ? 4.410   14.247  5.039   0.39 19.61 ? 188 GLN A HB2  1 
ATOM   2451 H HB3  A GLN A 1 169 ? 4.322   15.797  4.464   0.61 15.71 ? 188 GLN A HB3  1 
ATOM   2452 H HB3  B GLN A 1 169 ? 3.944   15.650  4.455   0.39 19.61 ? 188 GLN A HB3  1 
ATOM   2453 H HG2  A GLN A 1 169 ? 2.246   15.283  3.615   0.61 16.12 ? 188 GLN A HG2  1 
ATOM   2454 H HG2  B GLN A 1 169 ? 1.917   14.845  4.539   0.39 21.17 ? 188 GLN A HG2  1 
ATOM   2455 H HG3  A GLN A 1 169 ? 2.426   13.762  4.040   0.61 16.12 ? 188 GLN A HG3  1 
ATOM   2456 H HG3  B GLN A 1 169 ? 2.314   13.995  3.256   0.39 21.17 ? 188 GLN A HG3  1 
ATOM   2457 H HE21 A GLN A 1 169 ? 1.739   13.151  6.020   0.61 19.00 ? 188 GLN A HE21 1 
ATOM   2458 H HE21 B GLN A 1 169 ? 1.242   12.310  6.516   0.39 25.75 ? 188 GLN A HE21 1 
ATOM   2459 H HE22 A GLN A 1 169 ? 1.290   14.065  7.106   0.61 19.00 ? 188 GLN A HE22 1 
ATOM   2460 H HE22 B GLN A 1 169 ? 1.159   13.776  6.263   0.39 25.75 ? 188 GLN A HE22 1 
ATOM   2461 N N    . ILE A 1 170 ? 7.200   14.519  3.531   1.00 13.34 ? 189 ILE A N    1 
ATOM   2462 C CA   . ILE A 1 170 ? 8.557   15.062  3.457   1.00 13.24 ? 189 ILE A CA   1 
ATOM   2463 C C    . ILE A 1 170 ? 9.054   15.082  2.026   1.00 13.64 ? 189 ILE A C    1 
ATOM   2464 O O    . ILE A 1 170 ? 9.651   16.071  1.572   1.00 14.11 ? 189 ILE A O    1 
ATOM   2465 C CB   . ILE A 1 170 ? 9.494   14.224  4.344   1.00 13.02 ? 189 ILE A CB   1 
ATOM   2466 C CG1  . ILE A 1 170 ? 9.081   14.327  5.803   1.00 13.35 ? 189 ILE A CG1  1 
ATOM   2467 C CG2  . ILE A 1 170 ? 10.937  14.682  4.134   1.00 13.66 ? 189 ILE A CG2  1 
ATOM   2468 C CD1  . ILE A 1 170 ? 9.710   13.248  6.672   1.00 13.89 ? 189 ILE A CD1  1 
ATOM   2469 H H    . ILE A 1 170 ? 7.119   13.809  4.009   1.00 16.01 ? 189 ILE A H    1 
ATOM   2470 H HA   . ILE A 1 170 ? 8.538   15.976  3.782   1.00 15.89 ? 189 ILE A HA   1 
ATOM   2471 H HB   . ILE A 1 170 ? 9.427   13.290  4.090   1.00 15.63 ? 189 ILE A HB   1 
ATOM   2472 H HG12 . ILE A 1 170 ? 9.358   15.190  6.149   1.00 16.03 ? 189 ILE A HG12 1 
ATOM   2473 H HG13 . ILE A 1 170 ? 8.117   14.238  5.865   1.00 16.03 ? 189 ILE A HG13 1 
ATOM   2474 H HG21 . ILE A 1 170 ? 11.486  14.335  4.854   1.00 16.40 ? 189 ILE A HG21 1 
ATOM   2475 H HG22 . ILE A 1 170 ? 11.256  14.343  3.283   1.00 16.40 ? 189 ILE A HG22 1 
ATOM   2476 H HG23 . ILE A 1 170 ? 10.964  15.651  4.135   1.00 16.40 ? 189 ILE A HG23 1 
ATOM   2477 H HD11 . ILE A 1 170 ? 9.496   13.427  7.601   1.00 16.68 ? 189 ILE A HD11 1 
ATOM   2478 H HD12 . ILE A 1 170 ? 9.353   12.385  6.411   1.00 16.68 ? 189 ILE A HD12 1 
ATOM   2479 H HD13 . ILE A 1 170 ? 10.671  13.261  6.545   1.00 16.68 ? 189 ILE A HD13 1 
ATOM   2480 N N    . ALA A 1 171 ? 8.805   13.999  1.298   1.00 14.75 ? 190 ALA A N    1 
ATOM   2481 C CA   . ALA A 1 171 ? 9.346   13.804  -0.033  1.00 16.21 ? 190 ALA A CA   1 
ATOM   2482 C C    . ALA A 1 171 ? 8.585   14.554  -1.111  1.00 16.60 ? 190 ALA A C    1 
ATOM   2483 O O    . ALA A 1 171 ? 9.076   14.625  -2.245  1.00 18.29 ? 190 ALA A O    1 
ATOM   2484 C CB   . ALA A 1 171 ? 9.309   12.306  -0.364  1.00 17.29 ? 190 ALA A CB   1 
ATOM   2485 H H    . ALA A 1 171 ? 8.312   13.347  1.564   1.00 17.70 ? 190 ALA A H    1 
ATOM   2486 H HA   . ALA A 1 171 ? 10.263  14.120  -0.046  1.00 19.46 ? 190 ALA A HA   1 
ATOM   2487 H HB1  . ALA A 1 171 ? 9.707   12.166  -1.237  1.00 20.75 ? 190 ALA A HB1  1 
ATOM   2488 H HB2  . ALA A 1 171 ? 9.810   11.821  0.310   1.00 20.75 ? 190 ALA A HB2  1 
ATOM   2489 H HB3  . ALA A 1 171 ? 8.386   12.007  -0.369  1.00 20.75 ? 190 ALA A HB3  1 
ATOM   2490 N N    . SER A 1 172 ? 7.416   15.101  -0.789  1.00 16.78 ? 191 SER A N    1 
ATOM   2491 C CA   . SER A 1 172 ? 6.567   15.735  -1.787  1.00 17.32 ? 191 SER A CA   1 
ATOM   2492 C C    . SER A 1 172 ? 7.331   16.789  -2.579  1.00 18.30 ? 191 SER A C    1 
ATOM   2493 O O    . SER A 1 172 ? 7.915   17.717  -2.014  1.00 16.32 ? 191 SER A O    1 
ATOM   2494 C CB   . SER A 1 172 ? 5.375   16.389  -1.088  1.00 18.50 ? 191 SER A CB   1 
ATOM   2495 O OG   . SER A 1 172 ? 4.569   17.073  -2.022  1.00 20.83 ? 191 SER A OG   1 
ATOM   2496 H H    . SER A 1 172 ? 7.090   15.118  0.007   1.00 20.15 ? 191 SER A H    1 
ATOM   2497 H HA   . SER A 1 172 ? 6.253   15.061  -2.409  1.00 20.79 ? 191 SER A HA   1 
ATOM   2498 H HB2  . SER A 1 172 ? 4.845   15.702  -0.655  1.00 22.21 ? 191 SER A HB2  1 
ATOM   2499 H HB3  . SER A 1 172 ? 5.702   17.021  -0.428  1.00 22.21 ? 191 SER A HB3  1 
ATOM   2500 H HG   . SER A 1 172 ? 4.338   16.551  -2.638  1.00 25.01 ? 191 SER A HG   1 
ATOM   2501 N N    . GLN A 1 173 ? 7.308   16.646  -3.906  1.00 20.40 ? 192 GLN A N    1 
ATOM   2502 C CA   . GLN A 1 173 ? 8.034   17.570  -4.775  1.00 21.70 ? 192 GLN A CA   1 
ATOM   2503 C C    . GLN A 1 173 ? 7.514   19.001  -4.649  1.00 21.53 ? 192 GLN A C    1 
ATOM   2504 O O    . GLN A 1 173 ? 8.272   19.960  -4.863  1.00 22.01 ? 192 GLN A O    1 
ATOM   2505 C CB   . GLN A 1 173 ? 7.947   17.098  -6.230  1.00 23.18 ? 192 GLN A CB   1 
ATOM   2506 C CG   . GLN A 1 173 ? 8.737   15.810  -6.510  1.00 25.14 ? 192 GLN A CG   1 
ATOM   2507 C CD   . GLN A 1 173 ? 10.239  15.985  -6.335  1.00 25.83 ? 192 GLN A CD   1 
ATOM   2508 O OE1  . GLN A 1 173 ? 10.814  16.981  -6.779  1.00 26.61 ? 192 GLN A OE1  1 
ATOM   2509 N NE2  . GLN A 1 173 ? 10.882  15.019  -5.683  1.00 26.63 ? 192 GLN A NE2  1 
ATOM   2510 H H    . GLN A 1 173 ? 6.883   16.027  -4.325  1.00 24.49 ? 192 GLN A H    1 
ATOM   2511 H HA   . GLN A 1 173 ? 8.968   17.571  -4.512  1.00 26.05 ? 192 GLN A HA   1 
ATOM   2512 H HB2  . GLN A 1 173 ? 7.017   16.928  -6.447  1.00 27.83 ? 192 GLN A HB2  1 
ATOM   2513 H HB3  . GLN A 1 173 ? 8.301   17.794  -6.805  1.00 27.83 ? 192 GLN A HB3  1 
ATOM   2514 H HG2  . GLN A 1 173 ? 8.443   15.119  -5.895  1.00 30.17 ? 192 GLN A HG2  1 
ATOM   2515 H HG3  . GLN A 1 173 ? 8.573   15.532  -7.424  1.00 30.17 ? 192 GLN A HG3  1 
ATOM   2516 H HE21 . GLN A 1 173 ? 10.448  14.339  -5.385  1.00 31.96 ? 192 GLN A HE21 1 
ATOM   2517 H HE22 . GLN A 1 173 ? 11.731  15.075  -5.561  1.00 31.96 ? 192 GLN A HE22 1 
ATOM   2518 N N    . ALA A 1 174 ? 6.245   19.174  -4.268  1.00 21.38 ? 193 ALA A N    1 
ATOM   2519 C CA   . ALA A 1 174 ? 5.715   20.520  -4.046  1.00 20.19 ? 193 ALA A CA   1 
ATOM   2520 C C    . ALA A 1 174 ? 6.469   21.290  -2.956  1.00 18.59 ? 193 ALA A C    1 
ATOM   2521 O O    . ALA A 1 174 ? 6.447   22.526  -2.958  1.00 18.46 ? 193 ALA A O    1 
ATOM   2522 C CB   . ALA A 1 174 ? 4.230   20.443  -3.689  1.00 20.90 ? 193 ALA A CB   1 
ATOM   2523 H H    . ALA A 1 174 ? 5.681   18.540  -4.134  1.00 25.67 ? 193 ALA A H    1 
ATOM   2524 H HA   . ALA A 1 174 ? 5.809   21.020  -4.871  1.00 24.23 ? 193 ALA A HA   1 
ATOM   2525 H HB1  . ALA A 1 174 ? 3.888   21.342  -3.565  1.00 25.08 ? 193 ALA A HB1  1 
ATOM   2526 H HB2  . ALA A 1 174 ? 3.754   20.004  -4.412  1.00 25.08 ? 193 ALA A HB2  1 
ATOM   2527 H HB3  . ALA A 1 174 ? 4.128   19.934  -2.870  1.00 25.08 ? 193 ALA A HB3  1 
ATOM   2528 N N    . ASN A 1 175 ? 7.150   20.600  -2.037  1.00 16.06 ? 194 ASN A N    1 
ATOM   2529 C CA   . ASN A 1 175 ? 7.932   21.310  -1.034  1.00 15.14 ? 194 ASN A CA   1 
ATOM   2530 C C    . ASN A 1 175 ? 9.041   22.137  -1.675  1.00 15.24 ? 194 ASN A C    1 
ATOM   2531 O O    . ASN A 1 175 ? 9.503   23.119  -1.085  1.00 15.91 ? 194 ASN A O    1 
ATOM   2532 C CB   . ASN A 1 175 ? 8.533   20.326  -0.026  1.00 14.54 ? 194 ASN A CB   1 
ATOM   2533 C CG   . ASN A 1 175 ? 7.498   19.682  0.883   1.00 14.67 ? 194 ASN A CG   1 
ATOM   2534 O OD1  . ASN A 1 175 ? 6.501   20.309  1.246   1.00 14.71 ? 194 ASN A OD1  1 
ATOM   2535 N ND2  . ASN A 1 175 ? 7.746   18.434  1.286   1.00 15.15 ? 194 ASN A ND2  1 
ATOM   2536 H H    . ASN A 1 175 ? 7.173   19.743  -1.977  1.00 19.28 ? 194 ASN A H    1 
ATOM   2537 H HA   . ASN A 1 175 ? 7.340   21.908  -0.551  1.00 18.17 ? 194 ASN A HA   1 
ATOM   2538 H HB2  . ASN A 1 175 ? 8.984   19.617  -0.511  1.00 17.46 ? 194 ASN A HB2  1 
ATOM   2539 H HB3  . ASN A 1 175 ? 9.167   20.800  0.535   1.00 17.46 ? 194 ASN A HB3  1 
ATOM   2540 H HD21 . ASN A 1 175 ? 7.188   18.030  1.801   1.00 18.19 ? 194 ASN A HD21 1 
ATOM   2541 H HD22 . ASN A 1 175 ? 8.463   18.034  1.030   1.00 18.19 ? 194 ASN A HD22 1 
ATOM   2542 N N    . ARG A 1 176 ? 9.521   21.734  -2.857  1.00 15.81 ? 195 ARG A N    1 
ATOM   2543 C CA   . ARG A 1 176 ? 10.568  22.511  -3.525  1.00 16.61 ? 195 ARG A CA   1 
ATOM   2544 C C    . ARG A 1 176 ? 10.114  23.947  -3.742  1.00 17.30 ? 195 ARG A C    1 
ATOM   2545 O O    . ARG A 1 176 ? 10.917  24.892  -3.668  1.00 18.66 ? 195 ARG A O    1 
ATOM   2546 C CB   . ARG A 1 176 ? 10.896  21.908  -4.890  1.00 17.82 ? 195 ARG A CB   1 
ATOM   2547 C CG   . ARG A 1 176 ? 11.678  20.641  -4.834  1.00 18.51 ? 195 ARG A CG   1 
ATOM   2548 C CD   . ARG A 1 176 ? 11.952  20.155  -6.255  1.00 20.34 ? 195 ARG A CD   1 
ATOM   2549 N NE   . ARG A 1 176 ? 12.732  18.929  -6.245  1.00 21.56 ? 195 ARG A NE   1 
ATOM   2550 C CZ   . ARG A 1 176 ? 14.049  18.892  -6.124  1.00 21.39 ? 195 ARG A CZ   1 
ATOM   2551 N NH1  . ARG A 1 176 ? 14.757  20.000  -5.998  1.00 20.60 ? 195 ARG A NH1  1 
ATOM   2552 N NH2  . ARG A 1 176 ? 14.663  17.715  -6.104  1.00 21.02 ? 195 ARG A NH2  1 
ATOM   2553 H H    . ARG A 1 176 ? 9.264   21.033  -3.283  1.00 18.98 ? 195 ARG A H    1 
ATOM   2554 H HA   . ARG A 1 176 ? 11.361  22.489  -2.967  1.00 19.93 ? 195 ARG A HA   1 
ATOM   2555 H HB2  . ARG A 1 176 ? 10.065  21.719  -5.353  1.00 21.40 ? 195 ARG A HB2  1 
ATOM   2556 H HB3  . ARG A 1 176 ? 11.418  22.552  -5.395  1.00 21.40 ? 195 ARG A HB3  1 
ATOM   2557 H HG2  . ARG A 1 176 ? 12.524  20.796  -4.386  1.00 22.21 ? 195 ARG A HG2  1 
ATOM   2558 H HG3  . ARG A 1 176 ? 11.171  19.962  -4.362  1.00 22.21 ? 195 ARG A HG3  1 
ATOM   2559 H HD2  . ARG A 1 176 ? 11.111  19.979  -6.705  1.00 24.41 ? 195 ARG A HD2  1 
ATOM   2560 H HD3  . ARG A 1 176 ? 12.451  20.832  -6.738  1.00 24.41 ? 195 ARG A HD3  1 
ATOM   2561 H HE   . ARG A 1 176 ? 12.312  18.183  -6.322  1.00 25.87 ? 195 ARG A HE   1 
ATOM   2562 H HH11 . ARG A 1 176 ? 14.362  20.764  -5.993  1.00 24.73 ? 195 ARG A HH11 1 
ATOM   2563 H HH12 . ARG A 1 176 ? 15.612  19.957  -5.921  1.00 24.73 ? 195 ARG A HH12 1 
ATOM   2564 H HH21 . ARG A 1 176 ? 14.205  16.990  -6.168  1.00 25.23 ? 195 ARG A HH21 1 
ATOM   2565 H HH22 . ARG A 1 176 ? 15.518  17.677  -6.026  1.00 25.23 ? 195 ARG A HH22 1 
ATOM   2566 N N    . LYS A 1 177 ? 8.831   24.130  -4.052  1.00 17.69 ? 196 LYS A N    1 
ATOM   2567 C CA   . LYS A 1 177 ? 8.327   25.481  -4.306  1.00 18.80 ? 196 LYS A CA   1 
ATOM   2568 C C    . LYS A 1 177 ? 8.408   26.337  -3.048  1.00 16.58 ? 196 LYS A C    1 
ATOM   2569 O O    . LYS A 1 177 ? 8.717   27.536  -3.116  1.00 16.29 ? 196 LYS A O    1 
ATOM   2570 C CB   . LYS A 1 177 ? 6.898   25.432  -4.851  1.00 23.33 ? 196 LYS A CB   1 
ATOM   2571 C CG   . LYS A 1 177 ? 6.792   24.792  -6.229  1.00 27.87 ? 196 LYS A CG   1 
ATOM   2572 C CD   . LYS A 1 177 ? 5.517   25.120  -7.018  1.00 31.72 ? 196 LYS A CD   1 
ATOM   2573 C CE   . LYS A 1 177 ? 4.224   25.115  -6.185  1.00 33.39 ? 196 LYS A CE   1 
ATOM   2574 N NZ   . LYS A 1 177 ? 3.210   26.086  -6.772  1.00 33.34 ? 196 LYS A NZ   1 
ATOM   2575 H H    . LYS A 1 177 ? 8.244   23.505  -4.120  1.00 21.24 ? 196 LYS A H    1 
ATOM   2576 H HA   . LYS A 1 177 ? 8.877   25.896  -4.990  1.00 22.57 ? 196 LYS A HA   1 
ATOM   2577 H HB2  . LYS A 1 177 ? 6.349   24.915  -4.240  1.00 28.00 ? 196 LYS A HB2  1 
ATOM   2578 H HB3  . LYS A 1 177 ? 6.557   26.338  -4.917  1.00 28.00 ? 196 LYS A HB3  1 
ATOM   2579 H HG2  . LYS A 1 177 ? 7.545   25.090  -6.763  1.00 33.45 ? 196 LYS A HG2  1 
ATOM   2580 H HG3  . LYS A 1 177 ? 6.822   23.828  -6.122  1.00 33.45 ? 196 LYS A HG3  1 
ATOM   2581 H HD2  . LYS A 1 177 ? 5.611   26.006  -7.403  1.00 38.07 ? 196 LYS A HD2  1 
ATOM   2582 H HD3  . LYS A 1 177 ? 5.411   24.462  -7.723  1.00 38.07 ? 196 LYS A HD3  1 
ATOM   2583 H HE2  . LYS A 1 177 ? 3.838   24.225  -6.188  1.00 40.08 ? 196 LYS A HE2  1 
ATOM   2584 H HE3  . LYS A 1 177 ? 4.422   25.388  -5.275  1.00 40.08 ? 196 LYS A HE3  1 
ATOM   2585 H HZ1  . LYS A 1 177 ? 2.471   26.092  -6.277  1.00 40.02 ? 196 LYS A HZ1  1 
ATOM   2586 H HZ2  . LYS A 1 177 ? 3.552   26.908  -6.791  1.00 40.02 ? 196 LYS A HZ2  1 
ATOM   2587 H HZ3  . LYS A 1 177 ? 3.000   25.842  -7.602  1.00 40.02 ? 196 LYS A HZ3  1 
ATOM   2588 N N    . LEU A 1 178 ? 8.154   25.738  -1.884  1.00 15.70 ? 197 LEU A N    1 
ATOM   2589 C CA   . LEU A 1 178 ? 8.151   26.495  -0.640  1.00 15.88 ? 197 LEU A CA   1 
ATOM   2590 C C    . LEU A 1 178 ? 9.559   26.793  -0.146  1.00 15.23 ? 197 LEU A C    1 
ATOM   2591 O O    . LEU A 1 178 ? 9.801   27.841  0.465   1.00 15.30 ? 197 LEU A O    1 
ATOM   2592 C CB   . LEU A 1 178 ? 7.430   25.698  0.450   1.00 18.33 ? 197 LEU A CB   1 
ATOM   2593 C CG   . LEU A 1 178 ? 5.911   25.653  0.354   1.00 20.91 ? 197 LEU A CG   1 
ATOM   2594 C CD1  . LEU A 1 178 ? 5.341   24.638  1.327   1.00 22.40 ? 197 LEU A CD1  1 
ATOM   2595 C CD2  . LEU A 1 178 ? 5.380   27.054  0.579   1.00 22.32 ? 197 LEU A CD2  1 
ATOM   2596 H H    . LEU A 1 178 ? 7.983   24.901  -1.791  1.00 18.85 ? 197 LEU A H    1 
ATOM   2597 H HA   . LEU A 1 178 ? 7.686   27.330  -0.805  1.00 19.06 ? 197 LEU A HA   1 
ATOM   2598 H HB2  . LEU A 1 178 ? 7.748   24.782  0.414   1.00 22.00 ? 197 LEU A HB2  1 
ATOM   2599 H HB3  . LEU A 1 178 ? 7.651   26.093  1.308   1.00 22.00 ? 197 LEU A HB3  1 
ATOM   2600 H HG   . LEU A 1 178 ? 5.622   25.359  -0.525  1.00 25.10 ? 197 LEU A HG   1 
ATOM   2601 H HD11 . LEU A 1 178 ? 4.375   24.618  1.232   1.00 26.89 ? 197 LEU A HD11 1 
ATOM   2602 H HD12 . LEU A 1 178 ? 5.711   23.764  1.126   1.00 26.89 ? 197 LEU A HD12 1 
ATOM   2603 H HD13 . LEU A 1 178 ? 5.579   24.898  2.230   1.00 26.89 ? 197 LEU A HD13 1 
ATOM   2604 H HD21 . LEU A 1 178 ? 4.414   27.016  0.659   1.00 26.79 ? 197 LEU A HD21 1 
ATOM   2605 H HD22 . LEU A 1 178 ? 5.765   27.410  1.395   1.00 26.79 ? 197 LEU A HD22 1 
ATOM   2606 H HD23 . LEU A 1 178 ? 5.628   27.611  -0.175  1.00 26.79 ? 197 LEU A HD23 1 
ATOM   2607 N N    . TRP A 1 179 ? 10.491  25.860  -0.345  1.00 14.29 ? 198 TRP A N    1 
ATOM   2608 C CA   . TRP A 1 179 ? 11.803  25.952  0.274   1.00 14.35 ? 198 TRP A CA   1 
ATOM   2609 C C    . TRP A 1 179 ? 12.929  26.338  -0.671  1.00 14.09 ? 198 TRP A C    1 
ATOM   2610 O O    . TRP A 1 179 ? 13.985  26.768  -0.196  1.00 15.83 ? 198 TRP A O    1 
ATOM   2611 C CB   . TRP A 1 179 ? 12.183  24.585  0.850   1.00 14.20 ? 198 TRP A CB   1 
ATOM   2612 C CG   . TRP A 1 179 ? 11.234  24.001  1.838   1.00 13.74 ? 198 TRP A CG   1 
ATOM   2613 C CD1  . TRP A 1 179 ? 10.376  24.663  2.681   1.00 13.87 ? 198 TRP A CD1  1 
ATOM   2614 C CD2  . TRP A 1 179 ? 11.061  22.602  2.116   1.00 13.56 ? 198 TRP A CD2  1 
ATOM   2615 N NE1  . TRP A 1 179 ? 9.669   23.750  3.449   1.00 13.82 ? 198 TRP A NE1  1 
ATOM   2616 C CE2  . TRP A 1 179 ? 10.076  22.483  3.119   1.00 13.93 ? 198 TRP A CE2  1 
ATOM   2617 C CE3  . TRP A 1 179 ? 11.636  21.433  1.598   1.00 13.46 ? 198 TRP A CE3  1 
ATOM   2618 C CZ2  . TRP A 1 179 ? 9.673   21.244  3.622   1.00 13.66 ? 198 TRP A CZ2  1 
ATOM   2619 C CZ3  . TRP A 1 179 ? 11.236  20.212  2.099   1.00 13.58 ? 198 TRP A CZ3  1 
ATOM   2620 C CH2  . TRP A 1 179 ? 10.263  20.124  3.098   1.00 13.89 ? 198 TRP A CH2  1 
ATOM   2621 H H    . TRP A 1 179 ? 10.383  25.163  -0.838  1.00 17.15 ? 198 TRP A H    1 
ATOM   2622 H HA   . TRP A 1 179 ? 11.751  26.621  0.975   1.00 17.22 ? 198 TRP A HA   1 
ATOM   2623 H HB2  . TRP A 1 179 ? 12.253  23.956  0.115   1.00 17.05 ? 198 TRP A HB2  1 
ATOM   2624 H HB3  . TRP A 1 179 ? 13.041  24.673  1.295   1.00 17.05 ? 198 TRP A HB3  1 
ATOM   2625 H HD1  . TRP A 1 179 ? 10.283  25.587  2.730   1.00 16.65 ? 198 TRP A HD1  1 
ATOM   2626 H HE1  . TRP A 1 179 ? 9.072   23.946  4.036   1.00 16.59 ? 198 TRP A HE1  1 
ATOM   2627 H HE3  . TRP A 1 179 ? 12.279  21.480  0.927   1.00 16.16 ? 198 TRP A HE3  1 
ATOM   2628 H HZ2  . TRP A 1 179 ? 9.028   21.181  4.289   1.00 16.39 ? 198 TRP A HZ2  1 
ATOM   2629 H HZ3  . TRP A 1 179 ? 11.620  19.434  1.766   1.00 16.30 ? 198 TRP A HZ3  1 
ATOM   2630 H HH2  . TRP A 1 179 ? 10.010  19.287  3.414   1.00 16.68 ? 198 TRP A HH2  1 
ATOM   2631 N N    . GLY A 1 180 ? 12.760  26.151  -1.970  1.00 14.29 ? 199 GLY A N    1 
ATOM   2632 C CA   . GLY A 1 180 ? 13.873  26.173  -2.897  1.00 15.49 ? 199 GLY A CA   1 
ATOM   2633 C C    . GLY A 1 180 ? 14.543  24.812  -3.002  1.00 17.31 ? 199 GLY A C    1 
ATOM   2634 O O    . GLY A 1 180 ? 14.442  23.965  -2.121  1.00 16.98 ? 199 GLY A O    1 
ATOM   2635 H H    . GLY A 1 180 ? 11.998  26.007  -2.342  1.00 17.15 ? 199 GLY A H    1 
ATOM   2636 H HA2  . GLY A 1 180 ? 13.556  26.429  -3.777  1.00 18.59 ? 199 GLY A HA2  1 
ATOM   2637 H HA3  . GLY A 1 180 ? 14.531  26.819  -2.598  1.00 18.59 ? 199 GLY A HA3  1 
ATOM   2638 N N    . ASP A 1 181 ? 15.282  24.616  -4.094  1.00 18.94 ? 200 ASP A N    1 
ATOM   2639 C CA   . ASP A 1 181 ? 15.839  23.292  -4.363  1.00 19.97 ? 200 ASP A CA   1 
ATOM   2640 C C    . ASP A 1 181 ? 16.908  22.900  -3.340  1.00 20.24 ? 200 ASP A C    1 
ATOM   2641 O O    . ASP A 1 181 ? 16.969  21.739  -2.909  1.00 19.62 ? 200 ASP A O    1 
ATOM   2642 C CB   . ASP A 1 181 ? 16.407  23.257  -5.788  1.00 21.66 ? 200 ASP A CB   1 
ATOM   2643 C CG   . ASP A 1 181 ? 15.333  23.305  -6.850  1.00 23.97 ? 200 ASP A CG   1 
ATOM   2644 O OD1  . ASP A 1 181 ? 14.221  22.801  -6.625  1.00 24.46 ? 200 ASP A OD1  1 
ATOM   2645 O OD2  . ASP A 1 181 ? 15.620  23.834  -7.944  1.00 26.89 ? 200 ASP A OD2  1 
ATOM   2646 H H    . ASP A 1 181 ? 15.470  25.217  -4.680  1.00 22.73 ? 200 ASP A H    1 
ATOM   2647 H HA   . ASP A 1 181 ? 15.129  22.634  -4.299  1.00 23.97 ? 200 ASP A HA   1 
ATOM   2648 H HB2  . ASP A 1 181 ? 16.988  24.023  -5.915  1.00 26.00 ? 200 ASP A HB2  1 
ATOM   2649 H HB3  . ASP A 1 181 ? 16.909  22.436  -5.907  1.00 26.00 ? 200 ASP A HB3  1 
ATOM   2650 N N    . GLU A 1 182 ? 17.745  23.857  -2.925  1.00 21.61 ? 201 GLU A N    1 
ATOM   2651 C CA   . GLU A 1 182 ? 18.859  23.550  -2.031  1.00 23.35 ? 201 GLU A CA   1 
ATOM   2652 C C    . GLU A 1 182 ? 18.353  23.060  -0.676  1.00 20.51 ? 201 GLU A C    1 
ATOM   2653 O O    . GLU A 1 182 ? 18.781  22.008  -0.176  1.00 19.85 ? 201 GLU A O    1 
ATOM   2654 C CB   . GLU A 1 182 ? 19.739  24.793  -1.912  1.00 28.04 ? 201 GLU A CB   1 
ATOM   2655 C CG   . GLU A 1 182 ? 20.410  25.055  -0.585  1.00 33.24 ? 201 GLU A CG   1 
ATOM   2656 C CD   . GLU A 1 182 ? 21.496  26.126  -0.725  1.00 37.52 ? 201 GLU A CD   1 
ATOM   2657 O OE1  . GLU A 1 182 ? 21.413  26.918  -1.685  1.00 38.79 ? 201 GLU A OE1  1 
ATOM   2658 O OE2  . GLU A 1 182 ? 22.426  26.173  0.110   1.00 39.52 ? 201 GLU A OE2  1 
ATOM   2659 H H    . GLU A 1 182 ? 17.688  24.686  -3.146  1.00 25.93 ? 201 GLU A H    1 
ATOM   2660 H HA   . GLU A 1 182 ? 19.402  22.834  -2.395  1.00 28.03 ? 201 GLU A HA   1 
ATOM   2661 H HB2  . GLU A 1 182 ? 20.446  24.719  -2.572  1.00 33.66 ? 201 GLU A HB2  1 
ATOM   2662 H HB3  . GLU A 1 182 ? 19.187  25.566  -2.103  1.00 33.66 ? 201 GLU A HB3  1 
ATOM   2663 H HG2  . GLU A 1 182 ? 19.750  25.367  0.054   1.00 39.90 ? 201 GLU A HG2  1 
ATOM   2664 H HG3  . GLU A 1 182 ? 20.822  24.238  -0.264  1.00 39.90 ? 201 GLU A HG3  1 
ATOM   2665 N N    . LYS A 1 183 ? 17.400  23.781  -0.086  1.00 18.42 ? 202 LYS A N    1 
ATOM   2666 C CA   . LYS A 1 183 ? 16.836  23.336  1.184   1.00 17.02 ? 202 LYS A CA   1 
ATOM   2667 C C    . LYS A 1 183 ? 16.070  22.027  1.015   1.00 16.28 ? 202 LYS A C    1 
ATOM   2668 O O    . LYS A 1 183 ? 16.106  21.162  1.900   1.00 15.79 ? 202 LYS A O    1 
ATOM   2669 C CB   . LYS A 1 183 ? 15.931  24.425  1.764   1.00 17.79 ? 202 LYS A CB   1 
ATOM   2670 C CG   . LYS A 1 183 ? 15.186  24.064  3.056   1.00 18.78 ? 202 LYS A CG   1 
ATOM   2671 C CD   . LYS A 1 183 ? 16.095  23.758  4.245   1.00 20.88 ? 202 LYS A CD   1 
ATOM   2672 C CE   . LYS A 1 183 ? 16.343  24.943  5.147   1.00 21.92 ? 202 LYS A CE   1 
ATOM   2673 N NZ   . LYS A 1 183 ? 17.410  24.643  6.141   1.00 20.79 ? 202 LYS A NZ   1 
ATOM   2674 H H    . LYS A 1 183 ? 17.072  24.514  -0.393  1.00 22.11 ? 202 LYS A H    1 
ATOM   2675 H HA   . LYS A 1 183 ? 17.556  23.182  1.815   1.00 20.43 ? 202 LYS A HA   1 
ATOM   2676 H HB2  . LYS A 1 183 ? 16.478  25.203  1.956   1.00 21.35 ? 202 LYS A HB2  1 
ATOM   2677 H HB3  . LYS A 1 183 ? 15.260  24.648  1.099   1.00 21.35 ? 202 LYS A HB3  1 
ATOM   2678 H HG2  . LYS A 1 183 ? 14.619  24.810  3.306   1.00 22.54 ? 202 LYS A HG2  1 
ATOM   2679 H HG3  . LYS A 1 183 ? 14.645  23.276  2.892   1.00 22.54 ? 202 LYS A HG3  1 
ATOM   2680 H HD2  . LYS A 1 183 ? 15.684  23.061  4.780   1.00 25.07 ? 202 LYS A HD2  1 
ATOM   2681 H HD3  . LYS A 1 183 ? 16.954  23.457  3.911   1.00 25.07 ? 202 LYS A HD3  1 
ATOM   2682 H HE2  . LYS A 1 183 ? 16.625  25.702  4.613   1.00 26.31 ? 202 LYS A HE2  1 
ATOM   2683 H HE3  . LYS A 1 183 ? 15.528  25.160  5.627   1.00 26.31 ? 202 LYS A HE3  1 
ATOM   2684 H HZ1  . LYS A 1 183 ? 17.142  23.996  6.690   1.00 24.96 ? 202 LYS A HZ1  1 
ATOM   2685 H HZ2  . LYS A 1 183 ? 18.150  24.379  5.723   1.00 24.96 ? 202 LYS A HZ2  1 
ATOM   2686 H HZ3  . LYS A 1 183 ? 17.594  25.371  6.620   1.00 24.96 ? 202 LYS A HZ3  1 
ATOM   2687 N N    . PHE A 1 184 ? 15.357  21.859  -0.105  1.00 15.27 ? 203 PHE A N    1 
ATOM   2688 C CA   . PHE A 1 184 ? 14.662  20.595  -0.332  1.00 15.47 ? 203 PHE A CA   1 
ATOM   2689 C C    . PHE A 1 184 ? 15.635  19.422  -0.274  1.00 15.80 ? 203 PHE A C    1 
ATOM   2690 O O    . PHE A 1 184 ? 15.372  18.416  0.397   1.00 15.20 ? 203 PHE A O    1 
ATOM   2691 C CB   . PHE A 1 184 ? 13.925  20.620  -1.668  1.00 16.69 ? 203 PHE A CB   1 
ATOM   2692 C CG   . PHE A 1 184 ? 13.198  19.337  -1.980  1.00 15.72 ? 203 PHE A CG   1 
ATOM   2693 C CD1  . PHE A 1 184 ? 11.911  19.126  -1.514  1.00 16.20 ? 203 PHE A CD1  1 
ATOM   2694 C CD2  . PHE A 1 184 ? 13.793  18.350  -2.745  1.00 16.72 ? 203 PHE A CD2  1 
ATOM   2695 C CE1  . PHE A 1 184 ? 11.242  17.957  -1.799  1.00 16.78 ? 203 PHE A CE1  1 
ATOM   2696 C CE2  . PHE A 1 184 ? 13.123  17.177  -3.024  1.00 16.69 ? 203 PHE A CE2  1 
ATOM   2697 C CZ   . PHE A 1 184 ? 11.844  16.983  -2.565  1.00 16.64 ? 203 PHE A CZ   1 
ATOM   2698 H H    . PHE A 1 184 ? 15.265  22.444  -0.727  1.00 18.33 ? 203 PHE A H    1 
ATOM   2699 H HA   . PHE A 1 184 ? 13.998  20.477  0.366   1.00 18.57 ? 203 PHE A HA   1 
ATOM   2700 H HB2  . PHE A 1 184 ? 13.270  21.335  -1.651  1.00 20.03 ? 203 PHE A HB2  1 
ATOM   2701 H HB3  . PHE A 1 184 ? 14.568  20.776  -2.377  1.00 20.03 ? 203 PHE A HB3  1 
ATOM   2702 H HD1  . PHE A 1 184 ? 11.494  19.781  -1.003  1.00 19.45 ? 203 PHE A HD1  1 
ATOM   2703 H HD2  . PHE A 1 184 ? 14.654  18.478  -3.074  1.00 20.07 ? 203 PHE A HD2  1 
ATOM   2704 H HE1  . PHE A 1 184 ? 10.381  17.824  -1.473  1.00 20.14 ? 203 PHE A HE1  1 
ATOM   2705 H HE2  . PHE A 1 184 ? 13.540  16.514  -3.525  1.00 20.03 ? 203 PHE A HE2  1 
ATOM   2706 H HZ   . PHE A 1 184 ? 11.387  16.199  -2.769  1.00 19.97 ? 203 PHE A HZ   1 
ATOM   2707 N N    . GLU A 1 185 ? 16.768  19.528  -0.976  1.00 16.70 ? 204 GLU A N    1 
ATOM   2708 C CA   . GLU A 1 185 ? 17.714  18.416  -0.971  1.00 17.18 ? 204 GLU A CA   1 
ATOM   2709 C C    . GLU A 1 185 ? 18.289  18.204  0.423   1.00 15.60 ? 204 GLU A C    1 
ATOM   2710 O O    . GLU A 1 185 ? 18.484  17.061  0.853   1.00 15.72 ? 204 GLU A O    1 
ATOM   2711 C CB   . GLU A 1 185 ? 18.824  18.654  -1.989  1.00 19.84 ? 204 GLU A CB   1 
ATOM   2712 C CG   . GLU A 1 185 ? 18.324  18.762  -3.437  1.00 22.54 ? 204 GLU A CG   1 
ATOM   2713 C CD   . GLU A 1 185 ? 17.793  17.451  -4.043  1.00 24.58 ? 204 GLU A CD   1 
ATOM   2714 O OE1  . GLU A 1 185 ? 17.736  16.401  -3.354  1.00 25.24 ? 204 GLU A OE1  1 
ATOM   2715 O OE2  . GLU A 1 185 ? 17.399  17.480  -5.229  1.00 26.76 ? 204 GLU A OE2  1 
ATOM   2716 H H    . GLU A 1 185 ? 17.003  20.210  -1.446  1.00 20.04 ? 204 GLU A H    1 
ATOM   2717 H HA   . GLU A 1 185 ? 17.249  17.606  -1.234  1.00 20.62 ? 204 GLU A HA   1 
ATOM   2718 H HB2  . GLU A 1 185 ? 19.276  19.483  -1.769  1.00 23.82 ? 204 GLU A HB2  1 
ATOM   2719 H HB3  . GLU A 1 185 ? 19.449  17.914  -1.947  1.00 23.82 ? 204 GLU A HB3  1 
ATOM   2720 H HG2  . GLU A 1 185 ? 17.601  19.409  -3.464  1.00 27.05 ? 204 GLU A HG2  1 
ATOM   2721 H HG3  . GLU A 1 185 ? 19.059  19.063  -3.994  1.00 27.05 ? 204 GLU A HG3  1 
ATOM   2722 N N    . ALA A 1 186 ? 18.558  19.289  1.146   1.00 15.07 ? 205 ALA A N    1 
ATOM   2723 C CA   . ALA A 1 186 ? 19.095  19.147  2.490   1.00 14.79 ? 205 ALA A CA   1 
ATOM   2724 C C    . ALA A 1 186 ? 18.092  18.460  3.401   1.00 14.16 ? 205 ALA A C    1 
ATOM   2725 O O    . ALA A 1 186 ? 18.485  17.712  4.298   1.00 14.22 ? 205 ALA A O    1 
ATOM   2726 C CB   . ALA A 1 186 ? 19.482  20.507  3.061   1.00 15.03 ? 205 ALA A CB   1 
ATOM   2727 H H    . ALA A 1 186 ? 18.439  20.100  0.886   1.00 18.09 ? 205 ALA A H    1 
ATOM   2728 H HA   . ALA A 1 186 ? 19.902  18.610  2.451   1.00 17.76 ? 205 ALA A HA   1 
ATOM   2729 H HB1  . ALA A 1 186 ? 19.864  20.381  3.944   1.00 18.04 ? 205 ALA A HB1  1 
ATOM   2730 H HB2  . ALA A 1 186 ? 20.133  20.922  2.474   1.00 18.04 ? 205 ALA A HB2  1 
ATOM   2731 H HB3  . ALA A 1 186 ? 18.689  21.062  3.121   1.00 18.04 ? 205 ALA A HB3  1 
ATOM   2732 N N    . ILE A 1 187 ? 16.797  18.721  3.203   1.00 14.05 ? 206 ILE A N    1 
ATOM   2733 C CA   . ILE A 1 187 ? 15.781  18.055  4.014   1.00 13.16 ? 206 ILE A CA   1 
ATOM   2734 C C    . ILE A 1 187 ? 15.669  16.579  3.656   1.00 13.10 ? 206 ILE A C    1 
ATOM   2735 O O    . ILE A 1 187 ? 15.497  15.738  4.542   1.00 12.61 ? 206 ILE A O    1 
ATOM   2736 C CB   . ILE A 1 187 ? 14.462  18.845  3.945   1.00 14.10 ? 206 ILE A CB   1 
ATOM   2737 C CG1  . ILE A 1 187 ? 14.646  20.097  4.813   1.00 14.35 ? 206 ILE A CG1  1 
ATOM   2738 C CG2  . ILE A 1 187 ? 13.283  18.010  4.447   1.00 13.58 ? 206 ILE A CG2  1 
ATOM   2739 C CD1  . ILE A 1 187 ? 13.473  21.039  4.843   1.00 15.05 ? 206 ILE A CD1  1 
ATOM   2740 H H    . ILE A 1 187 ? 16.487  19.269  2.616   1.00 16.87 ? 206 ILE A H    1 
ATOM   2741 H HA   . ILE A 1 187 ? 16.051  18.061  4.945   1.00 15.80 ? 206 ILE A HA   1 
ATOM   2742 H HB   . ILE A 1 187 ? 14.264  19.082  3.025   1.00 16.92 ? 206 ILE A HB   1 
ATOM   2743 H HG12 . ILE A 1 187 ? 14.813  19.814  5.725   1.00 17.22 ? 206 ILE A HG12 1 
ATOM   2744 H HG13 . ILE A 1 187 ? 15.407  20.594  4.475   1.00 17.22 ? 206 ILE A HG13 1 
ATOM   2745 H HG21 . ILE A 1 187 ? 12.476  18.548  4.408   1.00 16.31 ? 206 ILE A HG21 1 
ATOM   2746 H HG22 . ILE A 1 187 ? 13.187  17.228  3.883   1.00 16.31 ? 206 ILE A HG22 1 
ATOM   2747 H HG23 . ILE A 1 187 ? 13.455  17.739  5.362   1.00 16.31 ? 206 ILE A HG23 1 
ATOM   2748 H HD11 . ILE A 1 187 ? 13.711  21.822  5.364   1.00 18.07 ? 206 ILE A HD11 1 
ATOM   2749 H HD12 . ILE A 1 187 ? 13.254  21.300  3.935   1.00 18.07 ? 206 ILE A HD12 1 
ATOM   2750 H HD13 . ILE A 1 187 ? 12.717  20.588  5.250   1.00 18.07 ? 206 ILE A HD13 1 
ATOM   2751 N N    . GLN A 1 188 ? 15.798  16.228  2.373   1.00 13.93 ? 207 GLN A N    1 
ATOM   2752 C CA   . GLN A 1 188 ? 15.785  14.807  2.028   1.00 13.99 ? 207 GLN A CA   1 
ATOM   2753 C C    . GLN A 1 188 ? 17.004  14.097  2.616   1.00 14.51 ? 207 GLN A C    1 
ATOM   2754 O O    . GLN A 1 188 ? 16.894  12.971  3.117   1.00 14.51 ? 207 GLN A O    1 
ATOM   2755 C CB   . GLN A 1 188 ? 15.742  14.599  0.519   1.00 14.30 ? 207 GLN A CB   1 
ATOM   2756 C CG   . GLN A 1 188 ? 14.592  15.315  -0.199  1.00 14.27 ? 207 GLN A CG   1 
ATOM   2757 C CD   . GLN A 1 188 ? 13.255  15.172  0.510   1.00 15.20 ? 207 GLN A CD   1 
ATOM   2758 O OE1  . GLN A 1 188 ? 12.807  14.064  0.779   1.00 15.87 ? 207 GLN A OE1  1 
ATOM   2759 N NE2  . GLN A 1 188 ? 12.615  16.289  0.810   1.00 15.47 ? 207 GLN A NE2  1 
ATOM   2760 H H    . GLN A 1 188 ? 15.889  16.771  1.712   1.00 16.73 ? 207 GLN A H    1 
ATOM   2761 H HA   . GLN A 1 188 ? 14.978  14.416  2.397   1.00 16.79 ? 207 GLN A HA   1 
ATOM   2762 H HB2  . GLN A 1 188 ? 16.571  14.927  0.139   1.00 17.16 ? 207 GLN A HB2  1 
ATOM   2763 H HB3  . GLN A 1 188 ? 15.649  13.649  0.342   1.00 17.16 ? 207 GLN A HB3  1 
ATOM   2764 H HG2  . GLN A 1 188 ? 14.798  16.261  -0.255  1.00 17.13 ? 207 GLN A HG2  1 
ATOM   2765 H HG3  . GLN A 1 188 ? 14.497  14.943  -1.089  1.00 17.13 ? 207 GLN A HG3  1 
ATOM   2766 H HE21 . GLN A 1 188 ? 12.958  17.050  0.604   1.00 18.57 ? 207 GLN A HE21 1 
ATOM   2767 H HE22 . GLN A 1 188 ? 11.855  16.254  1.211   1.00 18.57 ? 207 GLN A HE22 1 
ATOM   2768 N N    . GLN A 1 189 ? 18.173  14.743  2.584   1.00 15.04 ? 208 GLN A N    1 
ATOM   2769 C CA   . GLN A 1 189 ? 19.327  14.177  3.281   1.00 14.94 ? 208 GLN A CA   1 
ATOM   2770 C C    . GLN A 1 189 ? 19.064  14.100  4.781   1.00 13.98 ? 208 GLN A C    1 
ATOM   2771 O O    . GLN A 1 189 ? 19.462  13.135  5.447   1.00 14.41 ? 208 GLN A O    1 
ATOM   2772 C CB   . GLN A 1 189 ? 20.578  14.990  2.985   1.00 15.90 ? 208 GLN A CB   1 
ATOM   2773 C CG   . GLN A 1 189 ? 21.819  14.486  3.659   1.00 17.25 ? 208 GLN A CG   1 
ATOM   2774 C CD   . GLN A 1 189 ? 22.181  13.082  3.243   1.00 19.29 ? 208 GLN A CD   1 
ATOM   2775 O OE1  . GLN A 1 189 ? 22.192  12.749  2.058   1.00 22.71 ? 208 GLN A OE1  1 
ATOM   2776 N NE2  . GLN A 1 189 ? 22.497  12.253  4.216   1.00 19.57 ? 208 GLN A NE2  1 
ATOM   2777 H H    . GLN A 1 189 ? 18.319  15.487  2.178   1.00 18.05 ? 208 GLN A H    1 
ATOM   2778 H HA   . GLN A 1 189 ? 19.486  13.278  2.954   1.00 17.94 ? 208 GLN A HA   1 
ATOM   2779 H HB2  . GLN A 1 189 ? 20.737  14.975  2.028   1.00 19.08 ? 208 GLN A HB2  1 
ATOM   2780 H HB3  . GLN A 1 189 ? 20.432  15.902  3.283   1.00 19.08 ? 208 GLN A HB3  1 
ATOM   2781 H HG2  . GLN A 1 189 ? 22.561  15.068  3.430   1.00 20.71 ? 208 GLN A HG2  1 
ATOM   2782 H HG3  . GLN A 1 189 ? 21.679  14.488  4.619   1.00 20.71 ? 208 GLN A HG3  1 
ATOM   2783 H HE21 . GLN A 1 189 ? 22.488  12.524  5.032   1.00 23.49 ? 208 GLN A HE21 1 
ATOM   2784 H HE22 . GLN A 1 189 ? 22.712  11.440  4.036   1.00 23.49 ? 208 GLN A HE22 1 
ATOM   2785 N N    . GLY A 1 190 ? 18.381  15.103  5.326   1.00 13.81 ? 209 GLY A N    1 
ATOM   2786 C CA   . GLY A 1 190 ? 18.051  15.080  6.741   1.00 13.35 ? 209 GLY A CA   1 
ATOM   2787 C C    . GLY A 1 190 ? 17.155  13.926  7.140   1.00 12.61 ? 209 GLY A C    1 
ATOM   2788 O O    . GLY A 1 190 ? 17.237  13.440  8.274   1.00 13.54 ? 209 GLY A O    1 
ATOM   2789 H H    . GLY A 1 190 ? 18.102  15.798  4.903   1.00 16.58 ? 209 GLY A H    1 
ATOM   2790 H HA2  . GLY A 1 190 ? 18.871  15.015  7.255   1.00 16.03 ? 209 GLY A HA2  1 
ATOM   2791 H HA3  . GLY A 1 190 ? 17.598  15.905  6.973   1.00 16.03 ? 209 GLY A HA3  1 
ATOM   2792 N N    . LEU A 1 191 ? 16.292  13.472  6.230   1.00 12.76 ? 210 LEU A N    1 
ATOM   2793 C CA   . LEU A 1 191 ? 15.493  12.284  6.507   1.00 12.06 ? 210 LEU A CA   1 
ATOM   2794 C C    . LEU A 1 191 ? 16.384  11.055  6.623   1.00 12.48 ? 210 LEU A C    1 
ATOM   2795 O O    . LEU A 1 191 ? 16.246  10.267  7.565   1.00 12.36 ? 210 LEU A O    1 
ATOM   2796 C CB   . LEU A 1 191 ? 14.430  12.086  5.420   1.00 12.66 ? 210 LEU A CB   1 
ATOM   2797 C CG   . LEU A 1 191 ? 13.577  10.825  5.533   1.00 12.65 ? 210 LEU A CG   1 
ATOM   2798 C CD1  . LEU A 1 191 ? 12.854  10.766  6.866   1.00 13.21 ? 210 LEU A CD1  1 
ATOM   2799 C CD2  . LEU A 1 191 ? 12.609  10.746  4.376   1.00 14.28 ? 210 LEU A CD2  1 
ATOM   2800 H H    . LEU A 1 191 ? 16.153  13.828  5.459   1.00 15.31 ? 210 LEU A H    1 
ATOM   2801 H HA   . LEU A 1 191 ? 15.029  12.407  7.350   1.00 14.48 ? 210 LEU A HA   1 
ATOM   2802 H HB2  . LEU A 1 191 ? 13.826  12.844  5.448   1.00 15.20 ? 210 LEU A HB2  1 
ATOM   2803 H HB3  . LEU A 1 191 ? 14.880  12.052  4.562   1.00 15.20 ? 210 LEU A HB3  1 
ATOM   2804 H HG   . LEU A 1 191 ? 14.155  10.046  5.493   1.00 15.19 ? 210 LEU A HG   1 
ATOM   2805 H HD11 . LEU A 1 191 ? 12.256  10.002  6.867   1.00 15.85 ? 210 LEU A HD11 1 
ATOM   2806 H HD12 . LEU A 1 191 ? 13.509  10.675  7.576   1.00 15.85 ? 210 LEU A HD12 1 
ATOM   2807 H HD13 . LEU A 1 191 ? 12.347  11.584  6.986   1.00 15.85 ? 210 LEU A HD13 1 
ATOM   2808 H HD21 . LEU A 1 191 ? 12.117  9.913   4.432   1.00 17.14 ? 210 LEU A HD21 1 
ATOM   2809 H HD22 . LEU A 1 191 ? 11.996  11.497  4.426   1.00 17.14 ? 210 LEU A HD22 1 
ATOM   2810 H HD23 . LEU A 1 191 ? 13.108  10.781  3.545   1.00 17.14 ? 210 LEU A HD23 1 
ATOM   2811 N N    . GLN A 1 192 ? 17.308  10.874  5.675   1.00 12.03 ? 211 GLN A N    1 
ATOM   2812 C CA   . GLN A 1 192 ? 18.271  9.787   5.808   1.00 12.44 ? 211 GLN A CA   1 
ATOM   2813 C C    . GLN A 1 192 ? 18.994  9.867   7.149   1.00 12.05 ? 211 GLN A C    1 
ATOM   2814 O O    . GLN A 1 192 ? 19.143  8.862   7.854   1.00 12.84 ? 211 GLN A O    1 
ATOM   2815 C CB   . GLN A 1 192 ? 19.280  9.830   4.662   1.00 12.86 ? 211 GLN A CB   1 
ATOM   2816 C CG   . GLN A 1 192 ? 20.369  8.786   4.723   1.00 14.14 ? 211 GLN A CG   1 
ATOM   2817 C CD   . GLN A 1 192 ? 19.886  7.426   4.275   1.00 15.02 ? 211 GLN A CD   1 
ATOM   2818 O OE1  . GLN A 1 192 ? 19.149  7.314   3.280   1.00 17.39 ? 211 GLN A OE1  1 
ATOM   2819 N NE2  . GLN A 1 192 ? 20.313  6.380   4.968   1.00 15.77 ? 211 GLN A NE2  1 
ATOM   2820 H H    . GLN A 1 192 ? 17.393  11.354  4.966   1.00 14.44 ? 211 GLN A H    1 
ATOM   2821 H HA   . GLN A 1 192 ? 17.796  8.943   5.759   1.00 14.93 ? 211 GLN A HA   1 
ATOM   2822 H HB2  . GLN A 1 192 ? 18.802  9.701   3.828   1.00 15.43 ? 211 GLN A HB2  1 
ATOM   2823 H HB3  . GLN A 1 192 ? 19.712  10.699  4.667   1.00 15.43 ? 211 GLN A HB3  1 
ATOM   2824 H HG2  . GLN A 1 192 ? 21.099  9.054   4.143   1.00 16.98 ? 211 GLN A HG2  1 
ATOM   2825 H HG3  . GLN A 1 192 ? 20.684  8.708   5.637   1.00 16.98 ? 211 GLN A HG3  1 
ATOM   2826 H HE21 . GLN A 1 192 ? 20.839  6.494   5.639   1.00 18.93 ? 211 GLN A HE21 1 
ATOM   2827 H HE22 . GLN A 1 192 ? 20.063  5.587   4.748   1.00 18.93 ? 211 GLN A HE22 1 
ATOM   2828 N N    . ASP A 1 193 ? 19.474  11.060  7.501   1.00 12.21 ? 212 ASP A N    1 
ATOM   2829 C CA   . ASP A 1 193 ? 20.234  11.213  8.729   1.00 12.38 ? 212 ASP A CA   1 
ATOM   2830 C C    . ASP A 1 193 ? 19.374  10.974  9.969   1.00 11.47 ? 212 ASP A C    1 
ATOM   2831 O O    . ASP A 1 193 ? 19.839  10.359  10.930  1.00 12.59 ? 212 ASP A O    1 
ATOM   2832 C CB   . ASP A 1 193 ? 20.867  12.601  8.767   1.00 13.97 ? 212 ASP A CB   1 
ATOM   2833 C CG   . ASP A 1 193 ? 22.100  12.711  7.884   1.00 17.61 ? 212 ASP A CG   1 
ATOM   2834 O OD1  . ASP A 1 193 ? 22.780  11.696  7.726   1.00 22.07 ? 212 ASP A OD1  1 
ATOM   2835 O OD2  . ASP A 1 193 ? 22.359  13.788  7.335   1.00 18.54 ? 212 ASP A OD2  1 
ATOM   2836 H H    . ASP A 1 193 ? 19.372  11.784  7.049   1.00 14.66 ? 212 ASP A H    1 
ATOM   2837 H HA   . ASP A 1 193 ? 20.944  10.552  8.741   1.00 14.87 ? 212 ASP A HA   1 
ATOM   2838 H HB2  . ASP A 1 193 ? 20.218  13.253  8.458   1.00 16.77 ? 212 ASP A HB2  1 
ATOM   2839 H HB3  . ASP A 1 193 ? 21.131  12.803  9.678   1.00 16.77 ? 212 ASP A HB3  1 
ATOM   2840 N N    . ILE A 1 194 ? 18.117  11.448  9.986   1.00 11.07 ? 213 ILE A N    1 
ATOM   2841 C CA   . ILE A 1 194 ? 17.285  11.260  11.178  1.00 11.75 ? 213 ILE A CA   1 
ATOM   2842 C C    . ILE A 1 194 ? 16.974  9.783   11.400  1.00 11.35 ? 213 ILE A C    1 
ATOM   2843 O O    . ILE A 1 194 ? 16.912  9.324   12.547  1.00 11.79 ? 213 ILE A O    1 
ATOM   2844 C CB   . ILE A 1 194 ? 16.025  12.151  11.139  1.00 11.94 ? 213 ILE A CB   1 
ATOM   2845 C CG1  . ILE A 1 194 ? 15.584  12.490  12.565  1.00 11.85 ? 213 ILE A CG1  1 
ATOM   2846 C CG2  . ILE A 1 194 ? 14.878  11.496  10.386  1.00 12.29 ? 213 ILE A CG2  1 
ATOM   2847 C CD1  . ILE A 1 194 ? 14.417  13.471  12.607  1.00 12.50 ? 213 ILE A CD1  1 
ATOM   2848 H H    . ILE A 1 194 ? 17.736  11.869  9.339   1.00 13.29 ? 213 ILE A H    1 
ATOM   2849 H HA   . ILE A 1 194 ? 17.795  11.558  11.947  1.00 14.11 ? 213 ILE A HA   1 
ATOM   2850 H HB   . ILE A 1 194 ? 16.261  12.963  10.664  1.00 14.33 ? 213 ILE A HB   1 
ATOM   2851 H HG12 . ILE A 1 194 ? 15.307  11.675  13.011  1.00 14.23 ? 213 ILE A HG12 1 
ATOM   2852 H HG13 . ILE A 1 194 ? 16.330  12.891  13.039  1.00 14.23 ? 213 ILE A HG13 1 
ATOM   2853 H HG21 . ILE A 1 194 ? 14.196  12.162  10.207  1.00 14.75 ? 213 ILE A HG21 1 
ATOM   2854 H HG22 . ILE A 1 194 ? 15.215  11.134  9.552   1.00 14.75 ? 213 ILE A HG22 1 
ATOM   2855 H HG23 . ILE A 1 194 ? 14.509  10.783  10.931  1.00 14.75 ? 213 ILE A HG23 1 
ATOM   2856 H HD11 . ILE A 1 194 ? 14.225  13.694  13.532  1.00 15.01 ? 213 ILE A HD11 1 
ATOM   2857 H HD12 . ILE A 1 194 ? 14.659  14.272  12.117  1.00 15.01 ? 213 ILE A HD12 1 
ATOM   2858 H HD13 . ILE A 1 194 ? 13.640  13.056  12.200  1.00 15.01 ? 213 ILE A HD13 1 
ATOM   2859 N N    . ILE A 1 195 ? 16.781  9.020   10.323  1.00 11.04 ? 214 ILE A N    1 
ATOM   2860 C CA   . ILE A 1 195 ? 16.566  7.580   10.454  1.00 10.93 ? 214 ILE A CA   1 
ATOM   2861 C C    . ILE A 1 195 ? 17.808  6.904   11.030  1.00 10.84 ? 214 ILE A C    1 
ATOM   2862 O O    . ILE A 1 195 ? 17.716  6.094   11.958  1.00 11.00 ? 214 ILE A O    1 
ATOM   2863 C CB   . ILE A 1 195 ? 16.169  6.986   9.090   1.00 11.08 ? 214 ILE A CB   1 
ATOM   2864 C CG1  . ILE A 1 195 ? 14.799  7.521   8.683   1.00 11.60 ? 214 ILE A CG1  1 
ATOM   2865 C CG2  . ILE A 1 195 ? 16.168  5.467   9.137   1.00 12.65 ? 214 ILE A CG2  1 
ATOM   2866 C CD1  . ILE A 1 195 ? 14.500  7.304   7.196   1.00 12.89 ? 214 ILE A CD1  1 
ATOM   2867 H H    . ILE A 1 195 ? 16.771  9.308   9.513   1.00 13.25 ? 214 ILE A H    1 
ATOM   2868 H HA   . ILE A 1 195 ? 15.838  7.425   11.075  1.00 13.12 ? 214 ILE A HA   1 
ATOM   2869 H HB   . ILE A 1 195 ? 16.823  7.258   8.427   1.00 13.30 ? 214 ILE A HB   1 
ATOM   2870 H HG12 . ILE A 1 195 ? 14.116  7.063   9.197   1.00 13.92 ? 214 ILE A HG12 1 
ATOM   2871 H HG13 . ILE A 1 195 ? 14.766  8.474   8.861   1.00 13.92 ? 214 ILE A HG13 1 
ATOM   2872 H HG21 . ILE A 1 195 ? 15.904  5.124   8.269   1.00 15.19 ? 214 ILE A HG21 1 
ATOM   2873 H HG22 . ILE A 1 195 ? 17.060  5.157   9.358   1.00 15.19 ? 214 ILE A HG22 1 
ATOM   2874 H HG23 . ILE A 1 195 ? 15.539  5.172   9.814   1.00 15.19 ? 214 ILE A HG23 1 
ATOM   2875 H HD11 . ILE A 1 195 ? 13.668  7.751   6.973   1.00 15.47 ? 214 ILE A HD11 1 
ATOM   2876 H HD12 . ILE A 1 195 ? 15.225  7.675   6.670   1.00 15.47 ? 214 ILE A HD12 1 
ATOM   2877 H HD13 . ILE A 1 195 ? 14.420  6.353   7.025   1.00 15.47 ? 214 ILE A HD13 1 
ATOM   2878 N N    . GLN A 1 196 ? 18.989  7.233   10.491  1.00 10.92 ? 215 GLN A N    1 
ATOM   2879 C CA   . GLN A 1 196 ? 20.230  6.673   11.013  1.00 11.76 ? 215 GLN A CA   1 
ATOM   2880 C C    . GLN A 1 196 ? 20.413  7.025   12.484  1.00 12.15 ? 215 GLN A C    1 
ATOM   2881 O O    . GLN A 1 196 ? 20.781  6.172   13.298  1.00 11.62 ? 215 GLN A O    1 
ATOM   2882 C CB   . GLN A 1 196 ? 21.414  7.179   10.191  1.00 12.97 ? 215 GLN A CB   1 
ATOM   2883 C CG   . GLN A 1 196 ? 21.426  6.628   8.793   1.00 13.07 ? 215 GLN A CG   1 
ATOM   2884 C CD   . GLN A 1 196 ? 22.564  7.086   7.912   1.00 13.58 ? 215 GLN A CD   1 
ATOM   2885 O OE1  . GLN A 1 196 ? 22.552  6.813   6.707   1.00 14.42 ? 215 GLN A OE1  1 
ATOM   2886 N NE2  . GLN A 1 196 ? 23.550  7.753   8.494   1.00 13.79 ? 215 GLN A NE2  1 
ATOM   2887 H H    . GLN A 1 196 ? 19.094  7.774   9.830   1.00 13.12 ? 215 GLN A H    1 
ATOM   2888 H HA   . GLN A 1 196 ? 20.196  5.707   10.934  1.00 14.11 ? 215 GLN A HA   1 
ATOM   2889 H HB2  . GLN A 1 196 ? 21.368  8.146   10.133  1.00 15.57 ? 215 GLN A HB2  1 
ATOM   2890 H HB3  . GLN A 1 196 ? 22.238  6.912   10.627  1.00 15.57 ? 215 GLN A HB3  1 
ATOM   2891 H HG2  . GLN A 1 196 ? 21.478  5.661   8.849   1.00 15.70 ? 215 GLN A HG2  1 
ATOM   2892 H HG3  . GLN A 1 196 ? 20.601  6.891   8.356   1.00 15.70 ? 215 GLN A HG3  1 
ATOM   2893 H HE21 . GLN A 1 196 ? 23.524  7.909   9.339   1.00 16.56 ? 215 GLN A HE21 1 
ATOM   2894 H HE22 . GLN A 1 196 ? 24.216  8.031   8.026   1.00 16.56 ? 215 GLN A HE22 1 
ATOM   2895 N N    . GLU A 1 197 ? 20.218  8.295   12.830  1.00 12.34 ? 216 GLU A N    1 
ATOM   2896 C CA   . GLU A 1 197 ? 20.439  8.740   14.193  1.00 12.55 ? 216 GLU A CA   1 
ATOM   2897 C C    . GLU A 1 197 ? 19.411  8.139   15.143  1.00 12.19 ? 216 GLU A C    1 
ATOM   2898 O O    . GLU A 1 197 ? 19.732  7.878   16.307  1.00 12.70 ? 216 GLU A O    1 
ATOM   2899 C CB   . GLU A 1 197 ? 20.419  10.273  14.263  1.00 13.72 ? 216 GLU A CB   1 
ATOM   2900 C CG   . GLU A 1 197 ? 21.627  10.930  13.599  1.00 14.73 ? 216 GLU A CG   1 
ATOM   2901 C CD   . GLU A 1 197 ? 21.374  12.367  13.141  1.00 18.11 ? 216 GLU A CD   1 
ATOM   2902 O OE1  . GLU A 1 197 ? 20.555  13.022  13.767  1.00 22.38 ? 216 GLU A OE1  1 
ATOM   2903 O OE2  . GLU A 1 197 ? 22.037  12.819  12.197  1.00 18.72 ? 216 GLU A OE2  1 
ATOM   2904 H H    . GLU A 1 197 ? 19.958  8.915   12.293  1.00 14.81 ? 216 GLU A H    1 
ATOM   2905 H HA   . GLU A 1 197 ? 21.318  8.450   14.481  1.00 15.07 ? 216 GLU A HA   1 
ATOM   2906 H HB2  . GLU A 1 197 ? 19.621  10.596  13.815  1.00 16.47 ? 216 GLU A HB2  1 
ATOM   2907 H HB3  . GLU A 1 197 ? 20.408  10.543  15.195  1.00 16.47 ? 216 GLU A HB3  1 
ATOM   2908 H HG2  . GLU A 1 197 ? 22.361  10.948  14.234  1.00 17.69 ? 216 GLU A HG2  1 
ATOM   2909 H HG3  . GLU A 1 197 ? 21.876  10.411  12.819  1.00 17.69 ? 216 GLU A HG3  1 
ATOM   2910 N N    . THR A 1 198 ? 18.184  7.872   14.666  1.00 11.82 ? 217 THR A N    1 
ATOM   2911 C CA   . THR A 1 198 ? 17.212  7.179   15.499  1.00 11.97 ? 217 THR A CA   1 
ATOM   2912 C C    . THR A 1 198 ? 17.726  5.792   15.838  1.00 11.98 ? 217 THR A C    1 
ATOM   2913 O O    . THR A 1 198 ? 17.721  5.378   17.005  1.00 13.00 ? 217 THR A O    1 
ATOM   2914 C CB   . THR A 1 198 ? 15.870  7.092   14.763  1.00 12.15 ? 217 THR A CB   1 
ATOM   2915 O OG1  . THR A 1 198 ? 15.325  8.397   14.557  1.00 12.14 ? 217 THR A OG1  1 
ATOM   2916 C CG2  . THR A 1 198 ? 14.858  6.256   15.538  1.00 13.51 ? 217 THR A CG2  1 
ATOM   2917 H H    . THR A 1 198 ? 17.904  8.080   13.880  1.00 14.19 ? 217 THR A H    1 
ATOM   2918 H HA   . THR A 1 198 ? 17.071  7.673   16.322  1.00 14.37 ? 217 THR A HA   1 
ATOM   2919 H HB   . THR A 1 198 ? 16.028  6.666   13.906  1.00 14.59 ? 217 THR A HB   1 
ATOM   2920 H HG1  . THR A 1 198 ? 15.751  8.794   13.952  1.00 14.58 ? 217 THR A HG1  1 
ATOM   2921 H HG21 . THR A 1 198 ? 13.966  6.410   15.190  1.00 16.22 ? 217 THR A HG21 1 
ATOM   2922 H HG22 . THR A 1 198 ? 15.071  5.314   15.452  1.00 16.22 ? 217 THR A HG22 1 
ATOM   2923 H HG23 . THR A 1 198 ? 14.876  6.499   16.477  1.00 16.22 ? 217 THR A HG23 1 
ATOM   2924 N N    . ARG A 1 199 ? 18.166  5.050   14.818  1.00 11.11 ? 218 ARG A N    1 
ATOM   2925 C CA   . ARG A 1 199 ? 18.690  3.708   15.054  1.00 11.41 ? 218 ARG A CA   1 
ATOM   2926 C C    . ARG A 1 199 ? 19.861  3.734   16.032  1.00 11.80 ? 218 ARG A C    1 
ATOM   2927 O O    . ARG A 1 199 ? 19.922  2.917   16.960  1.00 14.04 ? 218 ARG A O    1 
ATOM   2928 C CB   . ARG A 1 199 ? 19.110  3.079   13.726  1.00 11.63 ? 218 ARG A CB   1 
ATOM   2929 C CG   . ARG A 1 199 ? 19.855  1.751   13.863  1.00 11.55 ? 218 ARG A CG   1 
ATOM   2930 C CD   . ARG A 1 199 ? 19.059  0.679   14.595  1.00 11.26 ? 218 ARG A CD   1 
ATOM   2931 N NE   . ARG A 1 199 ? 17.907  0.265   13.814  1.00 12.34 ? 218 ARG A NE   1 
ATOM   2932 C CZ   . ARG A 1 199 ? 16.856  -0.372  14.310  1.00 12.39 ? 218 ARG A CZ   1 
ATOM   2933 N NH1  . ARG A 1 199 ? 16.752  -0.629  15.597  1.00 12.23 ? 218 ARG A NH1  1 
ATOM   2934 N NH2  . ARG A 1 199 ? 15.885  -0.746  13.490  1.00 13.47 ? 218 ARG A NH2  1 
ATOM   2935 H H    . ARG A 1 199 ? 18.171  5.298   13.995  1.00 13.34 ? 218 ARG A H    1 
ATOM   2936 H HA   . ARG A 1 199 ? 17.989  3.161   15.443  1.00 13.70 ? 218 ARG A HA   1 
ATOM   2937 H HB2  . ARG A 1 199 ? 18.315  2.916   13.195  1.00 13.96 ? 218 ARG A HB2  1 
ATOM   2938 H HB3  . ARG A 1 199 ? 19.697  3.698   13.263  1.00 13.96 ? 218 ARG A HB3  1 
ATOM   2939 H HG2  . ARG A 1 199 ? 20.061  1.414   12.977  1.00 13.86 ? 218 ARG A HG2  1 
ATOM   2940 H HG3  . ARG A 1 199 ? 20.675  1.902   14.360  1.00 13.86 ? 218 ARG A HG3  1 
ATOM   2941 H HD2  . ARG A 1 199 ? 19.623  -0.096  14.745  1.00 13.52 ? 218 ARG A HD2  1 
ATOM   2942 H HD3  . ARG A 1 199 ? 18.745  1.031   15.442  1.00 13.52 ? 218 ARG A HD3  1 
ATOM   2943 H HE   . ARG A 1 199 ? 17.907  0.445   12.973  1.00 14.82 ? 218 ARG A HE   1 
ATOM   2944 H HH11 . ARG A 1 199 ? 17.375  -0.383  16.137  1.00 14.68 ? 218 ARG A HH11 1 
ATOM   2945 H HH12 . ARG A 1 199 ? 16.061  -1.044  15.898  1.00 14.68 ? 218 ARG A HH12 1 
ATOM   2946 H HH21 . ARG A 1 199 ? 15.942  -0.575  12.649  1.00 16.17 ? 218 ARG A HH21 1 
ATOM   2947 H HH22 . ARG A 1 199 ? 15.197  -1.160  13.799  1.00 16.17 ? 218 ARG A HH22 1 
ATOM   2948 N N    . GLN A 1 200 ? 20.797  4.674   15.845  1.00 12.35 ? 219 GLN A N    1 
ATOM   2949 C CA   . GLN A 1 200 ? 21.953  4.742   16.734  1.00 13.26 ? 219 GLN A CA   1 
ATOM   2950 C C    . GLN A 1 200 ? 21.529  5.010   18.171  1.00 14.74 ? 219 GLN A C    1 
ATOM   2951 O O    . GLN A 1 200 ? 22.088  4.432   19.110  1.00 16.81 ? 219 GLN A O    1 
ATOM   2952 C CB   . GLN A 1 200 ? 22.901  5.831   16.248  1.00 14.02 ? 219 GLN A CB   1 
ATOM   2953 C CG   . GLN A 1 200 ? 24.154  6.023   17.074  1.00 15.45 ? 219 GLN A CG   1 
ATOM   2954 C CD   . GLN A 1 200 ? 25.047  4.802   17.163  1.00 17.64 ? 219 GLN A CD   1 
ATOM   2955 O OE1  . GLN A 1 200 ? 25.180  4.043   16.209  1.00 17.64 ? 219 GLN A OE1  1 
ATOM   2956 N NE2  . GLN A 1 200 ? 25.693  4.627   18.311  1.00 20.48 ? 219 GLN A NE2  1 
ATOM   2957 H H    . GLN A 1 200 ? 20.783  5.269   15.224  1.00 14.83 ? 219 GLN A H    1 
ATOM   2958 H HA   . GLN A 1 200 ? 22.420  3.893   16.716  1.00 15.92 ? 219 GLN A HA   1 
ATOM   2959 H HB2  . GLN A 1 200 ? 23.181  5.610   15.346  1.00 16.84 ? 219 GLN A HB2  1 
ATOM   2960 H HB3  . GLN A 1 200 ? 22.423  6.675   16.249  1.00 16.84 ? 219 GLN A HB3  1 
ATOM   2961 H HG2  . GLN A 1 200 ? 24.677  6.738   16.680  1.00 18.55 ? 219 GLN A HG2  1 
ATOM   2962 H HG3  . GLN A 1 200 ? 23.894  6.261   17.978  1.00 18.55 ? 219 GLN A HG3  1 
ATOM   2963 H HE21 . GLN A 1 200 ? 25.591  5.191   18.952  1.00 24.58 ? 219 GLN A HE21 1 
ATOM   2964 H HE22 . GLN A 1 200 ? 26.212  3.949   18.413  1.00 24.58 ? 219 GLN A HE22 1 
ATOM   2965 N N    . LYS A 1 201 ? 20.535  5.876   18.365  1.00 14.85 ? 220 LYS A N    1 
ATOM   2966 C CA   . LYS A 1 201 ? 20.176  6.274   19.721  1.00 16.09 ? 220 LYS A CA   1 
ATOM   2967 C C    . LYS A 1 201 ? 19.290  5.248   20.405  1.00 16.18 ? 220 LYS A C    1 
ATOM   2968 O O    . LYS A 1 201 ? 19.387  5.078   21.625  1.00 18.65 ? 220 LYS A O    1 
ATOM   2969 C CB   . LYS A 1 201 ? 19.521  7.654   19.715  1.00 18.79 ? 220 LYS A CB   1 
ATOM   2970 C CG   . LYS A 1 201 ? 19.505  8.309   21.091  1.00 21.62 ? 220 LYS A CG   1 
ATOM   2971 C CD   . LYS A 1 201 ? 19.366  9.835   21.046  1.00 22.82 ? 220 LYS A CD   1 
ATOM   2972 C CE   . LYS A 1 201 ? 20.524  10.574  20.328  1.00 22.93 ? 220 LYS A CE   1 
ATOM   2973 N NZ   . LYS A 1 201 ? 20.097  11.980  19.981  1.00 21.57 ? 220 LYS A NZ   1 
ATOM   2974 H H    . LYS A 1 201 ? 20.065  6.239   17.743  1.00 17.83 ? 220 LYS A H    1 
ATOM   2975 H HA   . LYS A 1 201 ? 20.987  6.348   20.249  1.00 19.31 ? 220 LYS A HA   1 
ATOM   2976 H HB2  . LYS A 1 201 ? 20.012  8.234   19.112  1.00 22.55 ? 220 LYS A HB2  1 
ATOM   2977 H HB3  . LYS A 1 201 ? 18.603  7.565   19.415  1.00 22.55 ? 220 LYS A HB3  1 
ATOM   2978 H HG2  . LYS A 1 201 ? 18.755  7.959   21.596  1.00 25.95 ? 220 LYS A HG2  1 
ATOM   2979 H HG3  . LYS A 1 201 ? 20.337  8.102   21.546  1.00 25.95 ? 220 LYS A HG3  1 
ATOM   2980 H HD2  . LYS A 1 201 ? 18.545  10.056  20.578  1.00 27.39 ? 220 LYS A HD2  1 
ATOM   2981 H HD3  . LYS A 1 201 ? 19.328  10.169  21.956  1.00 27.39 ? 220 LYS A HD3  1 
ATOM   2982 H HE2  . LYS A 1 201 ? 21.296  10.618  20.912  1.00 27.53 ? 220 LYS A HE2  1 
ATOM   2983 H HE3  . LYS A 1 201 ? 20.753  10.107  19.509  1.00 27.53 ? 220 LYS A HE3  1 
ATOM   2984 H HZ1  . LYS A 1 201 ? 20.777  12.423  19.615  1.00 25.89 ? 220 LYS A HZ1  1 
ATOM   2985 H HZ2  . LYS A 1 201 ? 19.421  11.959  19.402  1.00 25.89 ? 220 LYS A HZ2  1 
ATOM   2986 H HZ3  . LYS A 1 201 ? 19.835  12.408  20.716  1.00 25.89 ? 220 LYS A HZ3  1 
ATOM   2987 N N    . ILE A 1 202 ? 18.441  4.533   19.660  1.00 14.24 ? 221 ILE A N    1 
ATOM   2988 C CA   . ILE A 1 202 ? 17.538  3.598   20.320  1.00 14.87 ? 221 ILE A CA   1 
ATOM   2989 C C    . ILE A 1 202 ? 18.106  2.191   20.444  1.00 15.05 ? 221 ILE A C    1 
ATOM   2990 O O    . ILE A 1 202 ? 17.628  1.422   21.287  1.00 15.94 ? 221 ILE A O    1 
ATOM   2991 C CB   . ILE A 1 202 ? 16.121  3.549   19.714  1.00 15.10 ? 221 ILE A CB   1 
ATOM   2992 C CG1  . ILE A 1 202 ? 16.090  2.889   18.335  1.00 13.92 ? 221 ILE A CG1  1 
ATOM   2993 C CG2  . ILE A 1 202 ? 15.502  4.918   19.678  1.00 16.40 ? 221 ILE A CG2  1 
ATOM   2994 C CD1  . ILE A 1 202 ? 14.663  2.770   17.753  1.00 15.11 ? 221 ILE A CD1  1 
ATOM   2995 H H    . ILE A 1 202 ? 18.373  4.573   18.804  1.00 17.09 ? 221 ILE A H    1 
ATOM   2996 H HA   . ILE A 1 202 ? 17.422  3.952   21.216  1.00 17.85 ? 221 ILE A HA   1 
ATOM   2997 H HB   . ILE A 1 202 ? 15.590  2.987   20.299  1.00 18.13 ? 221 ILE A HB   1 
ATOM   2998 H HG12 . ILE A 1 202 ? 16.620  3.420   17.720  1.00 16.71 ? 221 ILE A HG12 1 
ATOM   2999 H HG13 . ILE A 1 202 ? 16.459  1.995   18.406  1.00 16.71 ? 221 ILE A HG13 1 
ATOM   3000 H HG21 . ILE A 1 202 ? 14.546  4.829   19.538  1.00 19.68 ? 221 ILE A HG21 1 
ATOM   3001 H HG22 . ILE A 1 202 ? 15.673  5.364   20.522  1.00 19.68 ? 221 ILE A HG22 1 
ATOM   3002 H HG23 . ILE A 1 202 ? 15.897  5.424   18.950  1.00 19.68 ? 221 ILE A HG23 1 
ATOM   3003 H HD11 . ILE A 1 202 ? 14.677  2.154   17.004  1.00 18.14 ? 221 ILE A HD11 1 
ATOM   3004 H HD12 . ILE A 1 202 ? 14.067  2.438   18.443  1.00 18.14 ? 221 ILE A HD12 1 
ATOM   3005 H HD13 . ILE A 1 202 ? 14.369  3.646   17.455  1.00 18.14 ? 221 ILE A HD13 1 
ATOM   3006 N N    . GLY A 1 203 ? 19.081  1.829   19.619  1.00 14.87 ? 222 GLY A N    1 
ATOM   3007 C CA   . GLY A 1 203 ? 19.712  0.525   19.673  1.00 14.25 ? 222 GLY A CA   1 
ATOM   3008 C C    . GLY A 1 203 ? 19.145  -0.464  18.664  1.00 14.18 ? 222 GLY A C    1 
ATOM   3009 O O    . GLY A 1 203 ? 18.101  -0.254  18.035  1.00 14.97 ? 222 GLY A O    1 
ATOM   3010 H H    . GLY A 1 203 ? 19.400  2.338   19.003  1.00 17.85 ? 222 GLY A H    1 
ATOM   3011 H HA2  . GLY A 1 203 ? 20.661  0.624   19.498  1.00 17.10 ? 222 GLY A HA2  1 
ATOM   3012 H HA3  . GLY A 1 203 ? 19.592  0.152   20.561  1.00 17.10 ? 222 GLY A HA3  1 
ATOM   3013 N N    . ASP A 1 204 ? 19.858  -1.585  18.534  1.00 13.84 ? 223 ASP A N    1 
ATOM   3014 C CA   . ASP A 1 204 ? 19.537  -2.581  17.522  1.00 13.65 ? 223 ASP A CA   1 
ATOM   3015 C C    . ASP A 1 204 ? 18.387  -3.498  17.918  1.00 14.27 ? 223 ASP A C    1 
ATOM   3016 O O    . ASP A 1 204 ? 17.883  -4.240  17.063  1.00 16.78 ? 223 ASP A O    1 
ATOM   3017 C CB   . ASP A 1 204 ? 20.761  -3.434  17.224  1.00 14.19 ? 223 ASP A CB   1 
ATOM   3018 C CG   . ASP A 1 204 ? 21.878  -2.627  16.599  1.00 16.08 ? 223 ASP A CG   1 
ATOM   3019 O OD1  . ASP A 1 204 ? 21.568  -1.662  15.872  1.00 16.70 ? 223 ASP A OD1  1 
ATOM   3020 O OD2  . ASP A 1 204 ? 23.047  -2.970  16.832  1.00 19.85 ? 223 ASP A OD2  1 
ATOM   3021 H H    . ASP A 1 204 ? 20.535  -1.788  19.024  1.00 16.61 ? 223 ASP A H    1 
ATOM   3022 H HA   . ASP A 1 204 ? 19.281  -2.112  16.712  1.00 16.39 ? 223 ASP A HA   1 
ATOM   3023 H HB2  . ASP A 1 204 ? 21.091  -3.818  18.052  1.00 17.04 ? 223 ASP A HB2  1 
ATOM   3024 H HB3  . ASP A 1 204 ? 20.514  -4.140  16.607  1.00 17.04 ? 223 ASP A HB3  1 
ATOM   3025 N N    . ASP A 1 205 ? 17.965  -3.489  19.180  1.00 13.58 ? 224 ASP A N    1 
ATOM   3026 C CA   . ASP A 1 205 ? 16.902  -4.367  19.650  1.00 14.22 ? 224 ASP A CA   1 
ATOM   3027 C C    . ASP A 1 205 ? 15.548  -3.677  19.703  1.00 13.46 ? 224 ASP A C    1 
ATOM   3028 O O    . ASP A 1 205 ? 14.587  -4.257  20.221  1.00 14.60 ? 224 ASP A O    1 
ATOM   3029 C CB   . ASP A 1 205 ? 17.270  -4.991  20.999  1.00 16.37 ? 224 ASP A CB   1 
ATOM   3030 C CG   . ASP A 1 205 ? 17.411  -3.972  22.112  1.00 19.44 ? 224 ASP A CG   1 
ATOM   3031 O OD1  . ASP A 1 205 ? 17.362  -2.750  21.831  1.00 19.52 ? 224 ASP A OD1  1 
ATOM   3032 O OD2  . ASP A 1 205 ? 17.599  -4.411  23.276  1.00 23.34 ? 224 ASP A OD2  1 
ATOM   3033 H H    . ASP A 1 205 ? 18.286  -2.974  19.790  1.00 16.30 ? 224 ASP A H    1 
ATOM   3034 H HA   . ASP A 1 205 ? 16.815  -5.104  19.025  1.00 17.07 ? 224 ASP A HA   1 
ATOM   3035 H HB2  . ASP A 1 205 ? 16.575  -5.618  21.255  1.00 19.64 ? 224 ASP A HB2  1 
ATOM   3036 H HB3  . ASP A 1 205 ? 18.118  -5.455  20.910  1.00 19.64 ? 224 ASP A HB3  1 
ATOM   3037 N N    . LYS A 1 206 ? 15.441  -2.479  19.153  1.00 12.60 ? 225 LYS A N    1 
ATOM   3038 C CA   . LYS A 1 206 ? 14.189  -1.740  19.102  1.00 12.54 ? 225 LYS A CA   1 
ATOM   3039 C C    . LYS A 1 206 ? 13.689  -1.684  17.665  1.00 12.51 ? 225 LYS A C    1 
ATOM   3040 O O    . LYS A 1 206 ? 14.471  -1.742  16.710  1.00 13.85 ? 225 LYS A O    1 
ATOM   3041 C CB   . LYS A 1 206 ? 14.387  -0.332  19.643  1.00 13.21 ? 225 LYS A CB   1 
ATOM   3042 C CG   . LYS A 1 206 ? 14.914  -0.297  21.077  1.00 13.59 ? 225 LYS A CG   1 
ATOM   3043 C CD   . LYS A 1 206 ? 13.873  -0.842  22.076  1.00 14.35 ? 225 LYS A CD   1 
ATOM   3044 C CE   . LYS A 1 206 ? 14.395  -0.750  23.498  1.00 15.73 ? 225 LYS A CE   1 
ATOM   3045 N NZ   . LYS A 1 206 ? 13.365  -1.023  24.515  1.00 17.69 ? 225 LYS A NZ   1 
ATOM   3046 H H    . LYS A 1 206 ? 16.099  -2.059  18.793  1.00 15.13 ? 225 LYS A H    1 
ATOM   3047 H HA   . LYS A 1 206 ? 13.513  -2.181  19.639  1.00 15.05 ? 225 LYS A HA   1 
ATOM   3048 H HB2  . LYS A 1 206 ? 15.026  0.133   19.080  1.00 15.86 ? 225 LYS A HB2  1 
ATOM   3049 H HB3  . LYS A 1 206 ? 13.534  0.131   19.628  1.00 15.86 ? 225 LYS A HB3  1 
ATOM   3050 H HG2  . LYS A 1 206 ? 15.712  -0.845  21.139  1.00 16.31 ? 225 LYS A HG2  1 
ATOM   3051 H HG3  . LYS A 1 206 ? 15.120  0.618   21.321  1.00 16.31 ? 225 LYS A HG3  1 
ATOM   3052 H HD2  . LYS A 1 206 ? 13.058  -0.320  22.013  1.00 17.23 ? 225 LYS A HD2  1 
ATOM   3053 H HD3  . LYS A 1 206 ? 13.688  -1.773  21.876  1.00 17.23 ? 225 LYS A HD3  1 
ATOM   3054 H HE2  . LYS A 1 206 ? 15.107  -1.398  23.614  1.00 18.88 ? 225 LYS A HE2  1 
ATOM   3055 H HE3  . LYS A 1 206 ? 14.733  0.146   23.651  1.00 18.88 ? 225 LYS A HE3  1 
ATOM   3056 H HZ1  . LYS A 1 206 ? 13.042  -1.846  24.408  1.00 21.24 ? 225 LYS A HZ1  1 
ATOM   3057 H HZ2  . LYS A 1 206 ? 13.716  -0.955  25.330  1.00 21.24 ? 225 LYS A HZ2  1 
ATOM   3058 H HZ3  . LYS A 1 206 ? 12.698  -0.439  24.438  1.00 21.24 ? 225 LYS A HZ3  1 
ATOM   3059 N N    . LEU A 1 207 ? 12.370  -1.576  17.514  1.00 11.73 ? 226 LEU A N    1 
ATOM   3060 C CA   . LEU A 1 207 ? 11.750  -1.584  16.190  1.00 11.05 ? 226 LEU A CA   1 
ATOM   3061 C C    . LEU A 1 207 ? 11.610  -0.174  15.640  1.00 11.01 ? 226 LEU A C    1 
ATOM   3062 O O    . LEU A 1 207 ? 11.152  0.725   16.342  1.00 12.23 ? 226 LEU A O    1 
ATOM   3063 C CB   . LEU A 1 207 ? 10.374  -2.251  16.275  1.00 11.30 ? 226 LEU A CB   1 
ATOM   3064 C CG   . LEU A 1 207 ? 10.466  -3.771  16.486  1.00 11.67 ? 226 LEU A CG   1 
ATOM   3065 C CD1  . LEU A 1 207 ? 9.207   -4.335  17.070  1.00 12.57 ? 226 LEU A CD1  1 
ATOM   3066 C CD2  . LEU A 1 207 ? 10.809  -4.453  15.195  1.00 12.56 ? 226 LEU A CD2  1 
ATOM   3067 H H    . LEU A 1 207 ? 11.812  -1.498  18.164  1.00 14.08 ? 226 LEU A H    1 
ATOM   3068 H HA   . LEU A 1 207 ? 12.317  -2.077  15.577  1.00 13.27 ? 226 LEU A HA   1 
ATOM   3069 H HB2  . LEU A 1 207 ? 9.885   -1.872  17.022  1.00 13.57 ? 226 LEU A HB2  1 
ATOM   3070 H HB3  . LEU A 1 207 ? 9.894   -2.090  15.448  1.00 13.57 ? 226 LEU A HB3  1 
ATOM   3071 H HG   . LEU A 1 207 ? 11.172  -3.947  17.127  1.00 14.02 ? 226 LEU A HG   1 
ATOM   3072 H HD11 . LEU A 1 207 ? 9.338   -5.279  17.250  1.00 15.09 ? 226 LEU A HD11 1 
ATOM   3073 H HD12 . LEU A 1 207 ? 9.003   -3.866  17.894  1.00 15.09 ? 226 LEU A HD12 1 
ATOM   3074 H HD13 . LEU A 1 207 ? 8.484   -4.216  16.434  1.00 15.09 ? 226 LEU A HD13 1 
ATOM   3075 H HD21 . LEU A 1 207 ? 10.788  -5.413  15.331  1.00 15.07 ? 226 LEU A HD21 1 
ATOM   3076 H HD22 . LEU A 1 207 ? 10.158  -4.200  14.522  1.00 15.07 ? 226 LEU A HD22 1 
ATOM   3077 H HD23 . LEU A 1 207 ? 11.696  -4.177  14.918  1.00 15.07 ? 226 LEU A HD23 1 
ATOM   3078 N N    . ILE A 1 208 ? 11.952  -0.008  14.361  1.00 10.64 ? 227 ILE A N    1 
ATOM   3079 C CA   . ILE A 1 208 ? 11.653  1.207   13.616  1.00 10.84 ? 227 ILE A CA   1 
ATOM   3080 C C    . ILE A 1 208 ? 10.603  0.848   12.579  1.00 10.69 ? 227 ILE A C    1 
ATOM   3081 O O    . ILE A 1 208 ? 10.875  0.083   11.642  1.00 11.26 ? 227 ILE A O    1 
ATOM   3082 C CB   . ILE A 1 208 ? 12.890  1.852   12.973  1.00 11.86 ? 227 ILE A CB   1 
ATOM   3083 C CG1  . ILE A 1 208 ? 13.851  2.335   14.068  1.00 12.37 ? 227 ILE A CG1  1 
ATOM   3084 C CG2  . ILE A 1 208 ? 12.462  3.037   12.083  1.00 12.87 ? 227 ILE A CG2  1 
ATOM   3085 C CD1  . ILE A 1 208 ? 15.159  2.960   13.542  1.00 12.52 ? 227 ILE A CD1  1 
ATOM   3086 H H    . ILE A 1 208 ? 12.366  -0.602  13.897  1.00 12.78 ? 227 ILE A H    1 
ATOM   3087 H HA   . ILE A 1 208 ? 11.282  1.862   14.228  1.00 13.01 ? 227 ILE A HA   1 
ATOM   3088 H HB   . ILE A 1 208 ? 13.341  1.192   12.424  1.00 14.23 ? 227 ILE A HB   1 
ATOM   3089 H HG12 . ILE A 1 208 ? 13.399  3.008   14.601  1.00 14.85 ? 227 ILE A HG12 1 
ATOM   3090 H HG13 . ILE A 1 208 ? 14.091  1.577   14.623  1.00 14.85 ? 227 ILE A HG13 1 
ATOM   3091 H HG21 . ILE A 1 208 ? 13.255  3.469   11.729  1.00 15.45 ? 227 ILE A HG21 1 
ATOM   3092 H HG22 . ILE A 1 208 ? 11.914  2.704   11.355  1.00 15.45 ? 227 ILE A HG22 1 
ATOM   3093 H HG23 . ILE A 1 208 ? 11.954  3.667   12.618  1.00 15.45 ? 227 ILE A HG23 1 
ATOM   3094 H HD11 . ILE A 1 208 ? 15.754  3.122   14.290  1.00 15.04 ? 227 ILE A HD11 1 
ATOM   3095 H HD12 . ILE A 1 208 ? 15.573  2.346   12.916  1.00 15.04 ? 227 ILE A HD12 1 
ATOM   3096 H HD13 . ILE A 1 208 ? 14.952  3.797   13.097  1.00 15.04 ? 227 ILE A HD13 1 
ATOM   3097 N N    . VAL A 1 209 ? 9.402   1.376   12.772  1.00 10.56 ? 228 VAL A N    1 
ATOM   3098 C CA   . VAL A 1 209 ? 8.285   1.223   11.849  1.00 10.70 ? 228 VAL A CA   1 
ATOM   3099 C C    . VAL A 1 209 ? 8.123   2.577   11.180  1.00 10.68 ? 228 VAL A C    1 
ATOM   3100 O O    . VAL A 1 209 ? 8.275   3.602   11.845  1.00 11.68 ? 228 VAL A O    1 
ATOM   3101 C CB   . VAL A 1 209 ? 6.988   0.864   12.601  1.00 11.44 ? 228 VAL A CB   1 
ATOM   3102 C CG1  . VAL A 1 209 ? 5.857   0.546   11.631  1.00 11.19 ? 228 VAL A CG1  1 
ATOM   3103 C CG2  . VAL A 1 209 ? 7.206   -0.287  13.608  1.00 12.12 ? 228 VAL A CG2  1 
ATOM   3104 H H    . VAL A 1 209 ? 9.200   1.848   13.461  1.00 12.68 ? 228 VAL A H    1 
ATOM   3105 H HA   . VAL A 1 209 ? 8.464   0.526   11.198  1.00 12.84 ? 228 VAL A HA   1 
ATOM   3106 H HB   . VAL A 1 209 ? 6.721   1.642   13.116  1.00 13.73 ? 228 VAL A HB   1 
ATOM   3107 H HG11 . VAL A 1 209 ? 5.019   0.523   12.120  1.00 13.44 ? 228 VAL A HG11 1 
ATOM   3108 H HG12 . VAL A 1 209 ? 5.823   1.235   10.949  1.00 13.44 ? 228 VAL A HG12 1 
ATOM   3109 H HG13 . VAL A 1 209 ? 6.025   -0.317  11.222  1.00 13.44 ? 228 VAL A HG13 1 
ATOM   3110 H HG21 . VAL A 1 209 ? 6.353   -0.529  14.002  1.00 14.56 ? 228 VAL A HG21 1 
ATOM   3111 H HG22 . VAL A 1 209 ? 7.582   -1.049  13.140  1.00 14.56 ? 228 VAL A HG22 1 
ATOM   3112 H HG23 . VAL A 1 209 ? 7.818   0.010   14.300  1.00 14.56 ? 228 VAL A HG23 1 
ATOM   3113 N N    . TYR A 1 210 ? 7.827   2.600   9.879   1.00 10.55 ? 229 TYR A N    1 
ATOM   3114 C CA   . TYR A 1 210 ? 7.620   3.881   9.224   1.00 10.44 ? 229 TYR A CA   1 
ATOM   3115 C C    . TYR A 1 210 ? 6.465   3.822   8.242   1.00 10.26 ? 229 TYR A C    1 
ATOM   3116 O O    . TYR A 1 210 ? 6.061   2.758   7.785   1.00 11.26 ? 229 TYR A O    1 
ATOM   3117 C CB   . TYR A 1 210 ? 8.890   4.424   8.571   1.00 11.74 ? 229 TYR A CB   1 
ATOM   3118 C CG   . TYR A 1 210 ? 9.166   3.858   7.211   1.00 11.29 ? 229 TYR A CG   1 
ATOM   3119 C CD1  . TYR A 1 210 ? 9.815   2.644   7.051   1.00 12.53 ? 229 TYR A CD1  1 
ATOM   3120 C CD2  . TYR A 1 210 ? 8.765   4.529   6.068   1.00 11.97 ? 229 TYR A CD2  1 
ATOM   3121 C CE1  . TYR A 1 210 ? 10.054  2.127   5.801   1.00 13.98 ? 229 TYR A CE1  1 
ATOM   3122 C CE2  . TYR A 1 210 ? 9.012   4.023   4.818   1.00 13.34 ? 229 TYR A CE2  1 
ATOM   3123 C CZ   . TYR A 1 210 ? 9.634   2.821   4.686   1.00 14.63 ? 229 TYR A CZ   1 
ATOM   3124 O OH   . TYR A 1 210 ? 9.859   2.349   3.414   1.00 17.01 ? 229 TYR A OH   1 
ATOM   3125 H H    . TYR A 1 210 ? 7.744   1.907   9.377   1.00 12.67 ? 229 TYR A H    1 
ATOM   3126 H HA   . TYR A 1 210 ? 7.355   4.519   9.906   1.00 12.54 ? 229 TYR A HA   1 
ATOM   3127 H HB2  . TYR A 1 210 ? 8.805   5.386   8.478   1.00 14.10 ? 229 TYR A HB2  1 
ATOM   3128 H HB3  . TYR A 1 210 ? 9.647   4.212   9.139   1.00 14.10 ? 229 TYR A HB3  1 
ATOM   3129 H HD1  . TYR A 1 210 ? 10.092  2.171   7.802   1.00 15.04 ? 229 TYR A HD1  1 
ATOM   3130 H HD2  . TYR A 1 210 ? 8.318   5.340   6.150   1.00 14.37 ? 229 TYR A HD2  1 
ATOM   3131 H HE1  . TYR A 1 210 ? 10.497  1.315   5.707   1.00 16.78 ? 229 TYR A HE1  1 
ATOM   3132 H HE2  . TYR A 1 210 ? 8.755   4.501   4.063   1.00 16.02 ? 229 TYR A HE2  1 
ATOM   3133 H HH   . TYR A 1 210 ? 9.560   2.894   2.849   1.00 20.42 ? 229 TYR A HH   1 
ATOM   3134 N N    . ASN A 1 211 ? 5.941   5.000   7.924   1.00 10.34 ? 230 ASN A N    1 
ATOM   3135 C CA   . ASN A 1 211 ? 4.879   5.157   6.941   1.00 10.83 ? 230 ASN A CA   1 
ATOM   3136 C C    . ASN A 1 211 ? 5.442   5.959   5.768   1.00 11.47 ? 230 ASN A C    1 
ATOM   3137 O O    . ASN A 1 211 ? 5.663   7.171   5.894   1.00 12.04 ? 230 ASN A O    1 
ATOM   3138 C CB   . ASN A 1 211 ? 3.689   5.893   7.550   1.00 11.69 ? 230 ASN A CB   1 
ATOM   3139 C CG   . ASN A 1 211 ? 2.477   5.809   6.683   1.00 12.99 ? 230 ASN A CG   1 
ATOM   3140 O OD1  . ASN A 1 211 ? 2.471   5.066   5.711   1.00 14.83 ? 230 ASN A OD1  1 
ATOM   3141 N ND2  . ASN A 1 211 ? 1.437   6.569   7.011   1.00 13.99 ? 230 ASN A ND2  1 
ATOM   3142 H H    . ASN A 1 211 ? 6.192   5.743   8.276   1.00 12.41 ? 230 ASN A H    1 
ATOM   3143 H HA   . ASN A 1 211 ? 4.591   4.285   6.627   1.00 13.00 ? 230 ASN A HA   1 
ATOM   3144 H HB2  . ASN A 1 211 ? 3.475   5.497   8.410   1.00 14.03 ? 230 ASN A HB2  1 
ATOM   3145 H HB3  . ASN A 1 211 ? 3.917   6.829   7.664   1.00 14.03 ? 230 ASN A HB3  1 
ATOM   3146 H HD21 . ASN A 1 211 ? 0.721   6.547   6.534   1.00 16.79 ? 230 ASN A HD21 1 
ATOM   3147 H HD22 . ASN A 1 211 ? 1.479   7.082   7.700   1.00 16.79 ? 230 ASN A HD22 1 
ATOM   3148 N N    . GLY A 1 212 ? 5.663   5.300   4.627   1.00 11.40 ? 231 GLY A N    1 
ATOM   3149 C CA   . GLY A 1 212 ? 5.437   3.892   4.359   1.00 11.46 ? 231 GLY A CA   1 
ATOM   3150 C C    . GLY A 1 212 ? 5.440   3.565   2.883   1.00 12.20 ? 231 GLY A C    1 
ATOM   3151 O O    . GLY A 1 212 ? 5.893   4.355   2.064   1.00 14.27 ? 231 GLY A O    1 
ATOM   3152 H H    . GLY A 1 212 ? 5.975   5.694   3.929   1.00 13.69 ? 231 GLY A H    1 
ATOM   3153 H HA2  . GLY A 1 212 ? 6.134   3.370   4.787   1.00 13.75 ? 231 GLY A HA2  1 
ATOM   3154 H HA3  . GLY A 1 212 ? 4.578   3.632   4.726   1.00 13.75 ? 231 GLY A HA3  1 
ATOM   3155 N N    . ILE A 1 213 ? 4.965   2.367   2.564   1.00 11.86 ? 232 ILE A N    1 
ATOM   3156 C CA   . ILE A 1 213 ? 4.787   1.925   1.187   1.00 12.03 ? 232 ILE A CA   1 
ATOM   3157 C C    . ILE A 1 213 ? 3.526   2.581   0.661   1.00 12.49 ? 232 ILE A C    1 
ATOM   3158 O O    . ILE A 1 213 ? 2.493   2.580   1.342   1.00 12.91 ? 232 ILE A O    1 
ATOM   3159 C CB   . ILE A 1 213 ? 4.671   0.393   1.138   1.00 12.33 ? 232 ILE A CB   1 
ATOM   3160 C CG1  . ILE A 1 213 ? 6.012   -0.272  1.494   1.00 13.12 ? 232 ILE A CG1  1 
ATOM   3161 C CG2  . ILE A 1 213 ? 4.182   -0.117  -0.237  1.00 13.53 ? 232 ILE A CG2  1 
ATOM   3162 C CD1  . ILE A 1 213 ? 5.828   -1.696  1.958   1.00 13.53 ? 232 ILE A CD1  1 
ATOM   3163 H H    . ILE A 1 213 ? 4.733   1.774   3.143   1.00 14.24 ? 232 ILE A H    1 
ATOM   3164 H HA   . ILE A 1 213 ? 5.542   2.193   0.640   1.00 14.44 ? 232 ILE A HA   1 
ATOM   3165 H HB   . ILE A 1 213 ? 4.006   0.149   1.801   1.00 14.80 ? 232 ILE A HB   1 
ATOM   3166 H HG12 . ILE A 1 213 ? 6.582   -0.280  0.709   1.00 15.75 ? 232 ILE A HG12 1 
ATOM   3167 H HG13 . ILE A 1 213 ? 6.437   0.228   2.208   1.00 15.75 ? 232 ILE A HG13 1 
ATOM   3168 H HG21 . ILE A 1 213 ? 4.306   -1.078  -0.279  1.00 16.25 ? 232 ILE A HG21 1 
ATOM   3169 H HG22 . ILE A 1 213 ? 3.242   0.100   -0.338  1.00 16.25 ? 232 ILE A HG22 1 
ATOM   3170 H HG23 . ILE A 1 213 ? 4.698   0.314   -0.935  1.00 16.25 ? 232 ILE A HG23 1 
ATOM   3171 H HD11 . ILE A 1 213 ? 5.240   -1.703  2.729   1.00 16.24 ? 232 ILE A HD11 1 
ATOM   3172 H HD12 . ILE A 1 213 ? 5.436   -2.214  1.238   1.00 16.24 ? 232 ILE A HD12 1 
ATOM   3173 H HD13 . ILE A 1 213 ? 6.693   -2.064  2.198   1.00 16.24 ? 232 ILE A HD13 1 
ATOM   3174 N N    . ARG A 1 214 ? 3.605   3.146   -0.541  1.00 13.07 ? 233 ARG A N    1 
ATOM   3175 C CA   . ARG A 1 214 ? 2.491   3.907   -1.098  1.00 14.25 ? 233 ARG A CA   1 
ATOM   3176 C C    . ARG A 1 214 ? 2.492   3.771   -2.612  1.00 14.62 ? 233 ARG A C    1 
ATOM   3177 O O    . ARG A 1 214 ? 3.520   4.000   -3.256  1.00 15.33 ? 233 ARG A O    1 
ATOM   3178 C CB   . ARG A 1 214 ? 2.614   5.397   -0.719  1.00 15.80 ? 233 ARG A CB   1 
ATOM   3179 C CG   . ARG A 1 214 ? 1.539   6.327   -1.239  1.00 18.48 ? 233 ARG A CG   1 
ATOM   3180 C CD   . ARG A 1 214 ? 0.174   6.106   -0.617  1.00 19.12 ? 233 ARG A CD   1 
ATOM   3181 N NE   . ARG A 1 214 ? 0.218   6.028   0.839   1.00 18.25 ? 233 ARG A NE   1 
ATOM   3182 C CZ   . ARG A 1 214 ? 0.287   7.058   1.673   1.00 19.39 ? 233 ARG A CZ   1 
ATOM   3183 N NH1  . ARG A 1 214 ? 0.215   8.317   1.247   1.00 20.03 ? 233 ARG A NH1  1 
ATOM   3184 N NH2  . ARG A 1 214 ? 0.417   6.818   2.973   1.00 19.74 ? 233 ARG A NH2  1 
ATOM   3185 H H    . ARG A 1 214 ? 4.294   3.103   -1.053  1.00 15.70 ? 233 ARG A H    1 
ATOM   3186 H HA   . ARG A 1 214 ? 1.656   3.551   -0.757  1.00 17.10 ? 233 ARG A HA   1 
ATOM   3187 H HB2  . ARG A 1 214 ? 2.600   5.462   0.249   1.00 18.96 ? 233 ARG A HB2  1 
ATOM   3188 H HB3  . ARG A 1 214 ? 3.460   5.724   -1.061  1.00 18.96 ? 233 ARG A HB3  1 
ATOM   3189 H HG2  . ARG A 1 214 ? 1.802   7.241   -1.053  1.00 22.18 ? 233 ARG A HG2  1 
ATOM   3190 H HG3  . ARG A 1 214 ? 1.451   6.195   -2.196  1.00 22.18 ? 233 ARG A HG3  1 
ATOM   3191 H HD2  . ARG A 1 214 ? -0.406  6.844   -0.860  1.00 22.95 ? 233 ARG A HD2  1 
ATOM   3192 H HD3  . ARG A 1 214 ? -0.193  5.272   -0.950  1.00 22.95 ? 233 ARG A HD3  1 
ATOM   3193 H HE   . ARG A 1 214 ? 0.198   5.243   1.189   1.00 21.90 ? 233 ARG A HE   1 
ATOM   3194 H HH11 . ARG A 1 214 ? 0.121   8.482   0.408   1.00 24.04 ? 233 ARG A HH11 1 
ATOM   3195 H HH12 . ARG A 1 214 ? 0.263   8.965   1.810   1.00 24.04 ? 233 ARG A HH12 1 
ATOM   3196 H HH21 . ARG A 1 214 ? 0.455   6.008   3.259   1.00 23.69 ? 233 ARG A HH21 1 
ATOM   3197 H HH22 . ARG A 1 214 ? 0.463   7.473   3.529   1.00 23.69 ? 233 ARG A HH22 1 
ATOM   3198 N N    . SER A 1 215 ? 1.336   3.430   -3.177  1.00 14.62 ? 234 SER A N    1 
ATOM   3199 C CA   . SER A 1 215 ? 1.168   3.300   -4.619  1.00 14.57 ? 234 SER A CA   1 
ATOM   3200 C C    . SER A 1 215 ? 0.003   4.156   -5.072  1.00 16.01 ? 234 SER A C    1 
ATOM   3201 O O    . SER A 1 215 ? -1.144  3.871   -4.728  1.00 16.46 ? 234 SER A O    1 
ATOM   3202 C CB   . SER A 1 215 ? 0.932   1.839   -4.988  1.00 15.13 ? 234 SER A CB   1 
ATOM   3203 O OG   . SER A 1 215 ? 1.996   1.033   -4.546  1.00 16.00 ? 234 SER A OG   1 
ATOM   3204 H H    . SER A 1 215 ? 0.618   3.265   -2.733  1.00 17.55 ? 234 SER A H    1 
ATOM   3205 H HA   . SER A 1 215 ? 1.964   3.629   -5.065  1.00 17.49 ? 234 SER A HA   1 
ATOM   3206 H HB2  . SER A 1 215 ? 0.111   1.537   -4.569  1.00 18.17 ? 234 SER A HB2  1 
ATOM   3207 H HB3  . SER A 1 215 ? 0.859   1.765   -5.953  1.00 18.17 ? 234 SER A HB3  1 
ATOM   3208 H HG   . SER A 1 215 ? 1.862   0.234   -4.767  1.00 19.20 ? 234 SER A HG   1 
ATOM   3209 N N    . THR A 1 216 ? 0.286   5.176   -5.870  1.00 16.53 ? 235 THR A N    1 
ATOM   3210 C CA   . THR A 1 216 ? -0.739  6.007   -6.483  1.00 18.51 ? 235 THR A CA   1 
ATOM   3211 C C    . THR A 1 216 ? -0.392  6.162   -7.952  1.00 20.10 ? 235 THR A C    1 
ATOM   3212 O O    . THR A 1 216 ? 0.723   5.839   -8.375  1.00 21.40 ? 235 THR A O    1 
ATOM   3213 C CB   . THR A 1 216 ? -0.862  7.387   -5.820  1.00 19.70 ? 235 THR A CB   1 
ATOM   3214 O OG1  . THR A 1 216 ? 0.215   8.227   -6.237  1.00 21.39 ? 235 THR A OG1  1 
ATOM   3215 C CG2  . THR A 1 216 ? -0.863  7.272   -4.305  1.00 20.12 ? 235 THR A CG2  1 
ATOM   3216 H H    . THR A 1 216 ? 1.087   5.411   -6.076  1.00 19.84 ? 235 THR A H    1 
ATOM   3217 H HA   . THR A 1 216 ? -1.604  5.578   -6.382  1.00 22.22 ? 235 THR A HA   1 
ATOM   3218 H HB   . THR A 1 216 ? -1.703  7.790   -6.087  1.00 23.65 ? 235 THR A HB   1 
ATOM   3219 H HG1  . THR A 1 216 ? 0.942   7.933   -5.936  1.00 25.68 ? 235 THR A HG1  1 
ATOM   3220 H HG21 . THR A 1 216 ? -0.961  8.151   -3.906  1.00 24.14 ? 235 THR A HG21 1 
ATOM   3221 H HG22 . THR A 1 216 ? -1.599  6.710   -4.016  1.00 24.14 ? 235 THR A HG22 1 
ATOM   3222 H HG23 . THR A 1 216 ? -0.029  6.880   -4.002  1.00 24.14 ? 235 THR A HG23 1 
ATOM   3223 N N    . PRO A 1 217 ? -1.324  6.661   -8.768  1.00 22.86 ? 236 PRO A N    1 
ATOM   3224 C CA   . PRO A 1 217 ? -1.011  6.834   -10.198 1.00 25.18 ? 236 PRO A CA   1 
ATOM   3225 C C    . PRO A 1 217 ? 0.142   7.781   -10.457 1.00 29.13 ? 236 PRO A C    1 
ATOM   3226 O O    . PRO A 1 217 ? 0.834   7.626   -11.472 1.00 31.12 ? 236 PRO A O    1 
ATOM   3227 C CB   . PRO A 1 217 ? -2.327  7.362   -10.787 1.00 24.85 ? 236 PRO A CB   1 
ATOM   3228 C CG   . PRO A 1 217 ? -3.385  6.827   -9.858  1.00 24.81 ? 236 PRO A CG   1 
ATOM   3229 C CD   . PRO A 1 217 ? -2.751  6.914   -8.487  1.00 23.69 ? 236 PRO A CD   1 
ATOM   3230 H HA   . PRO A 1 217 ? -0.808  5.972   -10.595 1.00 30.23 ? 236 PRO A HA   1 
ATOM   3231 H HB2  . PRO A 1 217 ? -2.324  8.332   -10.793 1.00 29.82 ? 236 PRO A HB2  1 
ATOM   3232 H HB3  . PRO A 1 217 ? -2.449  7.025   -11.688 1.00 29.82 ? 236 PRO A HB3  1 
ATOM   3233 H HG2  . PRO A 1 217 ? -4.183  7.376   -9.909  1.00 29.78 ? 236 PRO A HG2  1 
ATOM   3234 H HG3  . PRO A 1 217 ? -3.598  5.909   -10.087 1.00 29.78 ? 236 PRO A HG3  1 
ATOM   3235 H HD2  . PRO A 1 217 ? -2.878  7.795   -8.102  1.00 28.44 ? 236 PRO A HD2  1 
ATOM   3236 H HD3  . PRO A 1 217 ? -3.113  6.238   -7.894  1.00 28.44 ? 236 PRO A HD3  1 
ATOM   3237 N N    . ASP A 1 218 ? 0.379   8.750   -9.572  1.00 31.07 ? 237 ASP A N    1 
ATOM   3238 C CA   . ASP A 1 218 ? 1.359   9.801   -9.821  1.00 34.64 ? 237 ASP A CA   1 
ATOM   3239 C C    . ASP A 1 218 ? 2.671   9.616   -9.074  1.00 35.42 ? 237 ASP A C    1 
ATOM   3240 O O    . ASP A 1 218 ? 3.707   10.103  -9.541  1.00 37.13 ? 237 ASP A O    1 
ATOM   3241 C CB   . ASP A 1 218 ? 0.773   11.154  -9.404  1.00 37.76 ? 237 ASP A CB   1 
ATOM   3242 C CG   . ASP A 1 218 ? -0.320  11.629  -10.333 1.00 40.55 ? 237 ASP A CG   1 
ATOM   3243 O OD1  . ASP A 1 218 ? -0.450  11.070  -11.442 1.00 41.33 ? 237 ASP A OD1  1 
ATOM   3244 O OD2  . ASP A 1 218 ? -1.061  12.559  -9.951  1.00 42.32 ? 237 ASP A OD2  1 
ATOM   3245 H H    . ASP A 1 218 ? -0.021  8.819   -8.814  1.00 37.29 ? 237 ASP A H    1 
ATOM   3246 H HA   . ASP A 1 218 ? 1.557   9.810   -10.770 1.00 41.57 ? 237 ASP A HA   1 
ATOM   3247 H HB2  . ASP A 1 218 ? 0.397   11.075  -8.513  1.00 45.32 ? 237 ASP A HB2  1 
ATOM   3248 H HB3  . ASP A 1 218 ? 1.480   11.819  -9.407  1.00 45.32 ? 237 ASP A HB3  1 
ATOM   3249 N N    . TRP A 1 219 ? 2.650   8.947   -7.925  1.00 33.70 ? 238 TRP A N    1 
ATOM   3250 C CA   . TRP A 1 219 ? 3.795   8.903   -7.029  1.00 32.23 ? 238 TRP A CA   1 
ATOM   3251 C C    . TRP A 1 219 ? 3.723   7.611   -6.239  1.00 30.15 ? 238 TRP A C    1 
ATOM   3252 O O    . TRP A 1 219 ? 2.667   7.282   -5.692  1.00 30.27 ? 238 TRP A O    1 
ATOM   3253 C CB   . TRP A 1 219 ? 3.763   10.083  -6.047  1.00 33.22 ? 238 TRP A CB   1 
ATOM   3254 C CG   . TRP A 1 219 ? 4.975   10.185  -5.167  1.00 33.60 ? 238 TRP A CG   1 
ATOM   3255 C CD1  . TRP A 1 219 ? 6.122   10.875  -5.433  1.00 34.23 ? 238 TRP A CD1  1 
ATOM   3256 C CD2  . TRP A 1 219 ? 5.158   9.586   -3.878  1.00 33.12 ? 238 TRP A CD2  1 
ATOM   3257 N NE1  . TRP A 1 219 ? 7.012   10.735  -4.395  1.00 34.44 ? 238 TRP A NE1  1 
ATOM   3258 C CE2  . TRP A 1 219 ? 6.444   9.950   -3.426  1.00 33.15 ? 238 TRP A CE2  1 
ATOM   3259 C CE3  . TRP A 1 219 ? 4.362   8.774   -3.062  1.00 32.10 ? 238 TRP A CE3  1 
ATOM   3260 C CZ2  . TRP A 1 219 ? 6.950   9.532   -2.192  1.00 32.07 ? 238 TRP A CZ2  1 
ATOM   3261 C CZ3  . TRP A 1 219 ? 4.861   8.364   -1.838  1.00 31.55 ? 238 TRP A CZ3  1 
ATOM   3262 C CH2  . TRP A 1 219 ? 6.144   8.742   -1.414  1.00 31.70 ? 238 TRP A CH2  1 
ATOM   3263 H H    . TRP A 1 219 ? 1.971   8.503   -7.639  1.00 40.45 ? 238 TRP A H    1 
ATOM   3264 H HA   . TRP A 1 219 ? 4.617   8.932   -7.543  1.00 38.69 ? 238 TRP A HA   1 
ATOM   3265 H HB2  . TRP A 1 219 ? 3.698   10.907  -6.555  1.00 39.87 ? 238 TRP A HB2  1 
ATOM   3266 H HB3  . TRP A 1 219 ? 2.989   9.986   -5.471  1.00 39.87 ? 238 TRP A HB3  1 
ATOM   3267 H HD1  . TRP A 1 219 ? 6.279   11.369  -6.205  1.00 41.08 ? 238 TRP A HD1  1 
ATOM   3268 H HE1  . TRP A 1 219 ? 7.797   11.083  -4.359  1.00 41.33 ? 238 TRP A HE1  1 
ATOM   3269 H HE3  . TRP A 1 219 ? 3.512   8.515   -3.337  1.00 38.52 ? 238 TRP A HE3  1 
ATOM   3270 H HZ2  . TRP A 1 219 ? 7.801   9.781   -1.910  1.00 38.49 ? 238 TRP A HZ2  1 
ATOM   3271 H HZ3  . TRP A 1 219 ? 4.337   7.828   -1.287  1.00 37.87 ? 238 TRP A HZ3  1 
ATOM   3272 H HH2  . TRP A 1 219 ? 6.455   8.449   -0.587  1.00 38.05 ? 238 TRP A HH2  1 
ATOM   3273 N N    . SER A 1 220 ? 4.842   6.896   -6.157  1.00 28.37 ? 239 SER A N    1 
ATOM   3274 C CA   . SER A 1 220 ? 4.872   5.645   -5.424  1.00 26.31 ? 239 SER A CA   1 
ATOM   3275 C C    . SER A 1 220 ? 6.199   5.519   -4.700  1.00 23.38 ? 239 SER A C    1 
ATOM   3276 O O    . SER A 1 220 ? 7.212   6.108   -5.098  1.00 25.43 ? 239 SER A O    1 
ATOM   3277 C CB   . SER A 1 220 ? 4.666   4.453   -6.356  1.00 27.69 ? 239 SER A CB   1 
ATOM   3278 O OG   . SER A 1 220 ? 3.406   4.571   -7.004  1.00 29.23 ? 239 SER A OG   1 
ATOM   3279 H H    . SER A 1 220 ? 5.590   7.118   -6.518  1.00 34.05 ? 239 SER A H    1 
ATOM   3280 H HA   . SER A 1 220 ? 4.167   5.637   -4.758  1.00 31.58 ? 239 SER A HA   1 
ATOM   3281 H HB2  . SER A 1 220 ? 5.370   4.440   -7.023  1.00 33.23 ? 239 SER A HB2  1 
ATOM   3282 H HB3  . SER A 1 220 ? 4.685   3.633   -5.838  1.00 33.23 ? 239 SER A HB3  1 
ATOM   3283 H HG   . SER A 1 220 ? 3.332   5.332   -7.351  1.00 35.09 ? 239 SER A HG   1 
ATOM   3284 N N    . ALA A 1 221 ? 6.169   4.734   -3.631  1.00 20.41 ? 240 ALA A N    1 
ATOM   3285 C CA   . ALA A 1 221 ? 7.336   4.468   -2.811  1.00 18.60 ? 240 ALA A CA   1 
ATOM   3286 C C    . ALA A 1 221 ? 7.254   3.038   -2.317  1.00 16.50 ? 240 ALA A C    1 
ATOM   3287 O O    . ALA A 1 221 ? 6.222   2.618   -1.795  1.00 16.27 ? 240 ALA A O    1 
ATOM   3288 C CB   . ALA A 1 221 ? 7.387   5.423   -1.612  1.00 20.57 ? 240 ALA A CB   1 
ATOM   3289 H H    . ALA A 1 221 ? 5.461   4.333   -3.353  1.00 24.49 ? 240 ALA A H    1 
ATOM   3290 H HA   . ALA A 1 221 ? 8.145   4.579   -3.335  1.00 22.32 ? 240 ALA A HA   1 
ATOM   3291 H HB1  . ALA A 1 221 ? 8.145   5.190   -1.054  1.00 24.69 ? 240 ALA A HB1  1 
ATOM   3292 H HB2  . ALA A 1 221 ? 7.482   6.332   -1.936  1.00 24.69 ? 240 ALA A HB2  1 
ATOM   3293 H HB3  . ALA A 1 221 ? 6.564   5.337   -1.105  1.00 24.69 ? 240 ALA A HB3  1 
ATOM   3294 N N    . GLY A 1 222 ? 8.334   2.288   -2.472  1.00 16.68 ? 241 GLY A N    1 
ATOM   3295 C CA   . GLY A 1 222 ? 8.454   0.983   -1.869  1.00 16.10 ? 241 GLY A CA   1 
ATOM   3296 C C    . GLY A 1 222 ? 9.235   1.029   -0.563  1.00 15.54 ? 241 GLY A C    1 
ATOM   3297 O O    . GLY A 1 222 ? 9.526   2.088   -0.006  1.00 16.52 ? 241 GLY A O    1 
ATOM   3298 H H    . GLY A 1 222 ? 9.022   2.523   -2.931  1.00 20.03 ? 241 GLY A H    1 
ATOM   3299 H HA2  . GLY A 1 222 ? 7.570   0.629   -1.686  1.00 19.33 ? 241 GLY A HA2  1 
ATOM   3300 H HA3  . GLY A 1 222 ? 8.913   0.385   -2.480  1.00 19.33 ? 241 GLY A HA3  1 
ATOM   3301 N N    . PHE A 1 223 ? 9.563   -0.155  -0.056  1.00 14.24 ? 242 PHE A N    1 
ATOM   3302 C CA   . PHE A 1 223 ? 10.312  -0.225  1.197   1.00 13.48 ? 242 PHE A CA   1 
ATOM   3303 C C    . PHE A 1 223 ? 11.681  0.420   1.005   1.00 14.47 ? 242 PHE A C    1 
ATOM   3304 O O    . PHE A 1 223 ? 12.387  0.108   0.051   1.00 17.59 ? 242 PHE A O    1 
ATOM   3305 C CB   . PHE A 1 223 ? 10.485  -1.687  1.630   1.00 13.76 ? 242 PHE A CB   1 
ATOM   3306 C CG   . PHE A 1 223 ? 10.672  -1.862  3.119   1.00 13.12 ? 242 PHE A CG   1 
ATOM   3307 C CD1  . PHE A 1 223 ? 11.818  -1.399  3.750   1.00 14.91 ? 242 PHE A CD1  1 
ATOM   3308 C CD2  . PHE A 1 223 ? 9.703   -2.444  3.886   1.00 13.68 ? 242 PHE A CD2  1 
ATOM   3309 C CE1  . PHE A 1 223 ? 11.983  -1.526  5.105   1.00 16.02 ? 242 PHE A CE1  1 
ATOM   3310 C CE2  . PHE A 1 223 ? 9.878   -2.594  5.239   1.00 15.08 ? 242 PHE A CE2  1 
ATOM   3311 C CZ   . PHE A 1 223 ? 11.004  -2.129  5.853   1.00 15.49 ? 242 PHE A CZ   1 
ATOM   3312 H H    . PHE A 1 223 ? 9.370   -0.915  -0.408  1.00 17.09 ? 242 PHE A H    1 
ATOM   3313 H HA   . PHE A 1 223 ? 9.828   0.244   1.895   1.00 16.18 ? 242 PHE A HA   1 
ATOM   3314 H HB2  . PHE A 1 223 ? 9.694   -2.185  1.370   1.00 16.52 ? 242 PHE A HB2  1 
ATOM   3315 H HB3  . PHE A 1 223 ? 11.268  -2.053  1.188   1.00 16.52 ? 242 PHE A HB3  1 
ATOM   3316 H HD1  . PHE A 1 223 ? 12.486  -0.996  3.244   1.00 17.90 ? 242 PHE A HD1  1 
ATOM   3317 H HD2  . PHE A 1 223 ? 8.917   -2.740  3.487   1.00 16.42 ? 242 PHE A HD2  1 
ATOM   3318 H HE1  . PHE A 1 223 ? 12.753  -1.204  5.514   1.00 19.23 ? 242 PHE A HE1  1 
ATOM   3319 H HE2  . PHE A 1 223 ? 9.221   -3.018  5.743   1.00 18.10 ? 242 PHE A HE2  1 
ATOM   3320 H HZ   . PHE A 1 223 ? 11.108  -2.220  6.772   1.00 18.59 ? 242 PHE A HZ   1 
ATOM   3321 N N    . ASP A 1 224 ? 12.062  1.316   1.912   1.00 14.67 ? 243 ASP A N    1 
ATOM   3322 C CA   . ASP A 1 224 ? 13.276  2.106   1.742   1.00 16.69 ? 243 ASP A CA   1 
ATOM   3323 C C    . ASP A 1 224 ? 14.014  2.143   3.079   1.00 14.91 ? 243 ASP A C    1 
ATOM   3324 O O    . ASP A 1 224 ? 13.478  1.773   4.127   1.00 14.91 ? 243 ASP A O    1 
ATOM   3325 C CB   . ASP A 1 224 ? 12.926  3.508   1.236   1.00 21.60 ? 243 ASP A CB   1 
ATOM   3326 C CG   . ASP A 1 224 ? 14.107  4.219   0.566   1.00 26.95 ? 243 ASP A CG   1 
ATOM   3327 O OD1  . ASP A 1 224 ? 15.241  3.694   0.579   1.00 28.00 ? 243 ASP A OD1  1 
ATOM   3328 O OD2  . ASP A 1 224 ? 13.872  5.307   -0.009  1.00 29.86 ? 243 ASP A OD2  1 
ATOM   3329 H H    . ASP A 1 224 ? 11.631  1.484   2.637   1.00 17.61 ? 243 ASP A H    1 
ATOM   3330 H HA   . ASP A 1 224 ? 13.873  1.697   1.096   1.00 20.04 ? 243 ASP A HA   1 
ATOM   3331 H HB2  . ASP A 1 224 ? 12.211  3.438   0.583   1.00 25.93 ? 243 ASP A HB2  1 
ATOM   3332 H HB3  . ASP A 1 224 ? 12.638  4.051   1.986   1.00 25.93 ? 243 ASP A HB3  1 
ATOM   3333 N N    . PHE A 1 225 ? 15.265  2.597   3.024   1.00 14.53 ? 244 PHE A N    1 
ATOM   3334 C CA   . PHE A 1 225 ? 16.106  2.767   4.206   1.00 14.20 ? 244 PHE A CA   1 
ATOM   3335 C C    . PHE A 1 225 ? 16.321  1.456   4.952   1.00 13.76 ? 244 PHE A C    1 
ATOM   3336 O O    . PHE A 1 225 ? 16.424  1.439   6.178   1.00 13.32 ? 244 PHE A O    1 
ATOM   3337 C CB   . PHE A 1 225 ? 15.532  3.827   5.141   1.00 15.08 ? 244 PHE A CB   1 
ATOM   3338 C CG   . PHE A 1 225 ? 15.176  5.119   4.457   1.00 15.86 ? 244 PHE A CG   1 
ATOM   3339 C CD1  . PHE A 1 225 ? 16.151  6.039   4.115   1.00 16.64 ? 244 PHE A CD1  1 
ATOM   3340 C CD2  . PHE A 1 225 ? 13.864  5.425   4.184   1.00 17.02 ? 244 PHE A CD2  1 
ATOM   3341 C CE1  . PHE A 1 225 ? 15.813  7.233   3.502   1.00 17.33 ? 244 PHE A CE1  1 
ATOM   3342 C CE2  . PHE A 1 225 ? 13.514  6.620   3.581   1.00 17.52 ? 244 PHE A CE2  1 
ATOM   3343 C CZ   . PHE A 1 225 ? 14.494  7.531   3.238   1.00 17.57 ? 244 PHE A CZ   1 
ATOM   3344 H H    . PHE A 1 225 ? 15.660  2.820   2.294   1.00 17.44 ? 244 PHE A H    1 
ATOM   3345 H HA   . PHE A 1 225 ? 16.979  3.063   3.904   1.00 17.04 ? 244 PHE A HA   1 
ATOM   3346 H HB2  . PHE A 1 225 ? 14.725  3.477   5.549   1.00 18.11 ? 244 PHE A HB2  1 
ATOM   3347 H HB3  . PHE A 1 225 ? 16.190  4.028   5.825   1.00 18.11 ? 244 PHE A HB3  1 
ATOM   3348 H HD1  . PHE A 1 225 ? 17.044  5.853   4.299   1.00 19.97 ? 244 PHE A HD1  1 
ATOM   3349 H HD2  . PHE A 1 225 ? 13.198  4.816   4.409   1.00 20.44 ? 244 PHE A HD2  1 
ATOM   3350 H HE1  . PHE A 1 225 ? 16.479  7.837   3.268   1.00 20.80 ? 244 PHE A HE1  1 
ATOM   3351 H HE2  . PHE A 1 225 ? 12.620  6.809   3.408   1.00 21.03 ? 244 PHE A HE2  1 
ATOM   3352 H HZ   . PHE A 1 225 ? 14.266  8.337   2.833   1.00 21.09 ? 244 PHE A HZ   1 
ATOM   3353 N N    . ALA A 1 226 ? 16.479  0.366   4.198   1.00 14.39 ? 245 ALA A N    1 
ATOM   3354 C CA   . ALA A 1 226 ? 16.389  -0.962  4.756   1.00 14.57 ? 245 ALA A CA   1 
ATOM   3355 C C    . ALA A 1 226 ? 17.562  -1.330  5.640   1.00 14.51 ? 245 ALA A C    1 
ATOM   3356 O O    . ALA A 1 226 ? 17.452  -2.287  6.402   1.00 14.36 ? 245 ALA A O    1 
ATOM   3357 C CB   . ALA A 1 226 ? 16.268  -1.990  3.618   1.00 16.12 ? 245 ALA A CB   1 
ATOM   3358 H H    . ALA A 1 226 ? 16.640  0.379   3.353   1.00 17.28 ? 245 ALA A H    1 
ATOM   3359 H HA   . ALA A 1 226 ? 15.592  -0.999  5.307   1.00 17.49 ? 245 ALA A HA   1 
ATOM   3360 H HB1  . ALA A 1 226 ? 16.271  -2.882  3.998   1.00 19.35 ? 245 ALA A HB1  1 
ATOM   3361 H HB2  . ALA A 1 226 ? 15.438  -1.836  3.140   1.00 19.35 ? 245 ALA A HB2  1 
ATOM   3362 H HB3  . ALA A 1 226 ? 17.021  -1.884  3.016   1.00 19.35 ? 245 ALA A HB3  1 
ATOM   3363 N N    . GLU A 1 227 ? 18.678  -0.615  5.561   1.00 14.97 ? 246 GLU A N    1 
ATOM   3364 C CA   . GLU A 1 227 ? 19.746  -0.889  6.513   1.00 15.21 ? 246 GLU A CA   1 
ATOM   3365 C C    . GLU A 1 227 ? 19.338  -0.503  7.922   1.00 14.46 ? 246 GLU A C    1 
ATOM   3366 O O    . GLU A 1 227 ? 19.956  -0.977  8.885   1.00 14.92 ? 246 GLU A O    1 
ATOM   3367 C CB   . GLU A 1 227 ? 21.009  -0.120  6.135   1.00 15.51 ? 246 GLU A CB   1 
ATOM   3368 C CG   . GLU A 1 227 ? 21.583  -0.492  4.778   1.00 18.22 ? 246 GLU A CG   1 
ATOM   3369 C CD   . GLU A 1 227 ? 20.950  0.269   3.624   1.00 23.01 ? 246 GLU A CD   1 
ATOM   3370 O OE1  . GLU A 1 227 ? 19.985  1.047   3.841   1.00 21.54 ? 246 GLU A OE1  1 
ATOM   3371 O OE2  . GLU A 1 227 ? 21.442  0.094   2.481   1.00 26.78 ? 246 GLU A OE2  1 
ATOM   3372 H H    . GLU A 1 227 ? 18.835  0.008   4.990   1.00 17.98 ? 246 GLU A H    1 
ATOM   3373 H HA   . GLU A 1 227 ? 19.952  -1.837  6.485   1.00 18.26 ? 246 GLU A HA   1 
ATOM   3374 H HB2  . GLU A 1 227 ? 20.801  0.827   6.117   1.00 18.62 ? 246 GLU A HB2  1 
ATOM   3375 H HB3  . GLU A 1 227 ? 21.691  -0.298  6.802   1.00 18.62 ? 246 GLU A HB3  1 
ATOM   3376 H HG2  . GLU A 1 227 ? 22.534  -0.298  4.776   1.00 21.87 ? 246 GLU A HG2  1 
ATOM   3377 H HG3  . GLU A 1 227 ? 21.438  -1.439  4.625   1.00 21.87 ? 246 GLU A HG3  1 
ATOM   3378 N N    . TYR A 1 228 ? 18.295  0.334   8.064   1.00 13.49 ? 247 TYR A N    1 
ATOM   3379 C CA   . TYR A 1 228 ? 17.917  0.908   9.351   1.00 13.47 ? 247 TYR A CA   1 
ATOM   3380 C C    . TYR A 1 228 ? 16.495  0.603   9.771   1.00 12.57 ? 247 TYR A C    1 
ATOM   3381 O O    . TYR A 1 228 ? 16.252  0.467   10.964  1.00 14.73 ? 247 TYR A O    1 
ATOM   3382 C CB   . TYR A 1 228 ? 18.131  2.445   9.326   1.00 13.54 ? 247 TYR A CB   1 
ATOM   3383 C CG   . TYR A 1 228 ? 19.527  2.754   8.845   1.00 13.48 ? 247 TYR A CG   1 
ATOM   3384 C CD1  . TYR A 1 228 ? 20.633  2.457   9.644   1.00 14.07 ? 247 TYR A CD1  1 
ATOM   3385 C CD2  . TYR A 1 228 ? 19.755  3.286   7.585   1.00 13.49 ? 247 TYR A CD2  1 
ATOM   3386 C CE1  . TYR A 1 228 ? 21.913  2.701   9.221   1.00 14.38 ? 247 TYR A CE1  1 
ATOM   3387 C CE2  . TYR A 1 228 ? 21.057  3.528   7.139   1.00 14.29 ? 247 TYR A CE2  1 
ATOM   3388 C CZ   . TYR A 1 228 ? 22.128  3.216   7.962   1.00 14.25 ? 247 TYR A CZ   1 
ATOM   3389 O OH   . TYR A 1 228 ? 23.424  3.441   7.577   1.00 16.24 ? 247 TYR A OH   1 
ATOM   3390 H H    . TYR A 1 228 ? 17.789  0.582   7.415   1.00 16.19 ? 247 TYR A H    1 
ATOM   3391 H HA   . TYR A 1 228 ? 18.494  0.541   10.039  1.00 16.17 ? 247 TYR A HA   1 
ATOM   3392 H HB2  . TYR A 1 228 ? 17.493  2.854   8.721   1.00 16.25 ? 247 TYR A HB2  1 
ATOM   3393 H HB3  . TYR A 1 228 ? 18.020  2.805   10.219  1.00 16.25 ? 247 TYR A HB3  1 
ATOM   3394 H HD1  . TYR A 1 228 ? 20.497  2.084   10.485  1.00 16.88 ? 247 TYR A HD1  1 
ATOM   3395 H HD2  . TYR A 1 228 ? 19.035  3.484   7.031   1.00 16.20 ? 247 TYR A HD2  1 
ATOM   3396 H HE1  . TYR A 1 228 ? 22.633  2.519   9.781   1.00 17.26 ? 247 TYR A HE1  1 
ATOM   3397 H HE2  . TYR A 1 228 ? 21.204  3.895   6.297   1.00 17.16 ? 247 TYR A HE2  1 
ATOM   3398 H HH   . TYR A 1 228 ? 23.472  3.481   6.740   1.00 19.49 ? 247 TYR A HH   1 
ATOM   3399 N N    . THR A 1 229 ? 15.541  0.545   8.847   1.00 12.63 ? 248 THR A N    1 
ATOM   3400 C CA   . THR A 1 229 ? 14.139  0.359   9.196   1.00 12.66 ? 248 THR A CA   1 
ATOM   3401 C C    . THR A 1 229 ? 13.795  -1.127  9.252   1.00 11.80 ? 248 THR A C    1 
ATOM   3402 O O    . THR A 1 229 ? 14.377  -1.944  8.544   1.00 13.10 ? 248 THR A O    1 
ATOM   3403 C CB   . THR A 1 229 ? 13.251  1.047   8.158   1.00 14.26 ? 248 THR A CB   1 
ATOM   3404 O OG1  . THR A 1 229 ? 13.603  0.595   6.850   1.00 15.21 ? 248 THR A OG1  1 
ATOM   3405 C CG2  . THR A 1 229 ? 13.387  2.584   8.220   1.00 14.69 ? 248 THR A CG2  1 
ATOM   3406 H H    . THR A 1 229 ? 15.683  0.612   8.002   1.00 15.16 ? 248 THR A H    1 
ATOM   3407 H HA   . THR A 1 229 ? 13.965  0.745   10.069  1.00 15.20 ? 248 THR A HA   1 
ATOM   3408 H HB   . THR A 1 229 ? 12.325  0.825   8.346   1.00 17.12 ? 248 THR A HB   1 
ATOM   3409 H HG1  . THR A 1 229 ? 14.230  1.063   6.543   1.00 18.26 ? 248 THR A HG1  1 
ATOM   3410 H HG21 . THR A 1 229 ? 12.733  2.999   7.635   1.00 17.63 ? 248 THR A HG21 1 
ATOM   3411 H HG22 . THR A 1 229 ? 13.239  2.894   9.127   1.00 17.63 ? 248 THR A HG22 1 
ATOM   3412 H HG23 . THR A 1 229 ? 14.275  2.850   7.937   1.00 17.63 ? 248 THR A HG23 1 
ATOM   3413 N N    . ASP A 1 230 ? 12.827  -1.469  10.112  1.00 10.75 ? 249 ASP A N    1 
ATOM   3414 C CA   . ASP A 1 230 ? 12.358  -2.842  10.262  1.00 10.80 ? 249 ASP A CA   1 
ATOM   3415 C C    . ASP A 1 230 ? 11.025  -3.096  9.589   1.00 11.69 ? 249 ASP A C    1 
ATOM   3416 O O    . ASP A 1 230 ? 10.810  -4.203  9.075   1.00 11.31 ? 249 ASP A O    1 
ATOM   3417 C CB   . ASP A 1 230 ? 12.203  -3.210  11.740  1.00 11.61 ? 249 ASP A CB   1 
ATOM   3418 C CG   . ASP A 1 230 ? 13.498  -3.083  12.505  1.00 12.12 ? 249 ASP A CG   1 
ATOM   3419 O OD1  . ASP A 1 230 ? 14.469  -3.775  12.109  1.00 13.19 ? 249 ASP A OD1  1 
ATOM   3420 O OD2  . ASP A 1 230 ? 13.555  -2.319  13.500  1.00 12.17 ? 249 ASP A OD2  1 
ATOM   3421 H H    . ASP A 1 230 ? 12.422  -0.911  10.625  1.00 12.91 ? 249 ASP A H    1 
ATOM   3422 H HA   . ASP A 1 230 ? 13.027  -3.425  9.871   1.00 12.97 ? 249 ASP A HA   1 
ATOM   3423 H HB2  . ASP A 1 230 ? 11.553  -2.616  12.148  1.00 13.94 ? 249 ASP A HB2  1 
ATOM   3424 H HB3  . ASP A 1 230 ? 11.901  -4.129  11.808  1.00 13.94 ? 249 ASP A HB3  1 
ATOM   3425 N N    . ALA A 1 231 ? 10.138  -2.102  9.574   1.00 11.44 ? 250 ALA A N    1 
ATOM   3426 C CA   . ALA A 1 231 ? 8.744   -2.340  9.222   1.00 11.15 ? 250 ALA A CA   1 
ATOM   3427 C C    . ALA A 1 231 ? 8.225   -1.139  8.459   1.00 10.59 ? 250 ALA A C    1 
ATOM   3428 O O    . ALA A 1 231 ? 8.551   0.008   8.786   1.00 11.14 ? 250 ALA A O    1 
ATOM   3429 C CB   . ALA A 1 231 ? 7.895   -2.498  10.479  1.00 11.98 ? 250 ALA A CB   1 
ATOM   3430 H H    . ALA A 1 231 ? 10.321  -1.284  9.765   1.00 13.73 ? 250 ALA A H    1 
ATOM   3431 H HA   . ALA A 1 231 ? 8.674   -3.135  8.672   1.00 13.39 ? 250 ALA A HA   1 
ATOM   3432 H HB1  . ALA A 1 231 ? 7.003   -2.781  10.224  1.00 14.38 ? 250 ALA A HB1  1 
ATOM   3433 H HB2  . ALA A 1 231 ? 8.301   -3.165  11.053  1.00 14.38 ? 250 ALA A HB2  1 
ATOM   3434 H HB3  . ALA A 1 231 ? 7.852   -1.646  10.941  1.00 14.38 ? 250 ALA A HB3  1 
ATOM   3435 N N    . ALA A 1 232 ? 7.387   -1.408  7.463   1.00 10.09 ? 251 ALA A N    1 
ATOM   3436 C CA   . ALA A 1 232 ? 6.708   -0.357  6.719   1.00 10.34 ? 251 ALA A CA   1 
ATOM   3437 C C    . ALA A 1 232 ? 5.218   -0.648  6.659   1.00 10.80 ? 251 ALA A C    1 
ATOM   3438 O O    . ALA A 1 232 ? 4.794   -1.792  6.482   1.00 11.23 ? 251 ALA A O    1 
ATOM   3439 C CB   . ALA A 1 232 ? 7.242   -0.220  5.283   1.00 11.05 ? 251 ALA A CB   1 
ATOM   3440 H H    . ALA A 1 232 ? 7.194   -2.203  7.197   1.00 12.11 ? 251 ALA A H    1 
ATOM   3441 H HA   . ALA A 1 232 ? 6.852   0.483   7.182   1.00 12.41 ? 251 ALA A HA   1 
ATOM   3442 H HB1  . ALA A 1 232 ? 6.836   0.557   4.868   1.00 13.26 ? 251 ALA A HB1  1 
ATOM   3443 H HB2  . ALA A 1 232 ? 8.206   -0.114  5.313   1.00 13.26 ? 251 ALA A HB2  1 
ATOM   3444 H HB3  . ALA A 1 232 ? 7.013   -1.019  4.784   1.00 13.26 ? 251 ALA A HB3  1 
ATOM   3445 N N    . MET A 1 233 ? 4.427   0.397   6.808   1.00 10.25 ? 252 MET A N    1 
ATOM   3446 C CA   . MET A 1 233 ? 2.990   0.316   6.643   1.00 9.91  ? 252 MET A CA   1 
ATOM   3447 C C    . MET A 1 233 ? 2.573   0.615   5.202   1.00 10.69 ? 252 MET A C    1 
ATOM   3448 O O    . MET A 1 233 ? 3.081   1.556   4.567   1.00 11.63 ? 252 MET A O    1 
ATOM   3449 C CB   . MET A 1 233 ? 2.329   1.394   7.495   1.00 11.39 ? 252 MET A CB   1 
ATOM   3450 C CG   . MET A 1 233 ? 0.829   1.408   7.452   1.00 13.90 ? 252 MET A CG   1 
ATOM   3451 S SD   . MET A 1 233 ? 0.032   2.480   8.648   1.00 15.11 ? 252 MET A SD   1 
ATOM   3452 C CE   . MET A 1 233 ? -0.330  1.288   9.980   1.00 18.01 ? 252 MET A CE   1 
ATOM   3453 H H    . MET A 1 233 ? 4.705   1.185   7.010   1.00 12.31 ? 252 MET A H    1 
ATOM   3454 H HA   . MET A 1 233 ? 2.712   -0.577  6.899   1.00 11.90 ? 252 MET A HA   1 
ATOM   3455 H HB2  . MET A 1 233 ? 2.592   1.258   8.419   1.00 13.68 ? 252 MET A HB2  1 
ATOM   3456 H HB3  . MET A 1 233 ? 2.636   2.260   7.186   1.00 13.68 ? 252 MET A HB3  1 
ATOM   3457 H HG2  . MET A 1 233 ? 0.551   1.703   6.570   1.00 16.68 ? 252 MET A HG2  1 
ATOM   3458 H HG3  . MET A 1 233 ? 0.510   0.506   7.615   1.00 16.68 ? 252 MET A HG3  1 
ATOM   3459 H HE1  . MET A 1 233 ? -0.778  1.751   10.705  1.00 21.62 ? 252 MET A HE1  1 
ATOM   3460 H HE2  . MET A 1 233 ? -0.903  0.588   9.631   1.00 21.62 ? 252 MET A HE2  1 
ATOM   3461 H HE3  . MET A 1 233 ? 0.504   0.906   10.297  1.00 21.62 ? 252 MET A HE3  1 
ATOM   3462 N N    . ILE A 1 234 ? 1.590   -0.153  4.739   1.00 10.53 ? 253 ILE A N    1 
ATOM   3463 C CA   . ILE A 1 234 ? 0.830   0.149   3.524   1.00 10.32 ? 253 ILE A CA   1 
ATOM   3464 C C    . ILE A 1 234 ? -0.477  0.750   4.028   1.00 10.55 ? 253 ILE A C    1 
ATOM   3465 O O    . ILE A 1 234 ? -1.444  0.038   4.289   1.00 11.79 ? 253 ILE A O    1 
ATOM   3466 C CB   . ILE A 1 234 ? 0.572   -1.086  2.650   1.00 11.18 ? 253 ILE A CB   1 
ATOM   3467 C CG1  . ILE A 1 234 ? 1.874   -1.821  2.328   1.00 11.83 ? 253 ILE A CG1  1 
ATOM   3468 C CG2  . ILE A 1 234 ? -0.187  -0.677  1.394   1.00 13.29 ? 253 ILE A CG2  1 
ATOM   3469 C CD1  . ILE A 1 234 ? 1.665   -3.180  1.705   1.00 12.66 ? 253 ILE A CD1  1 
ATOM   3470 H H    . ILE A 1 234 ? 1.334   -0.879  5.122   1.00 12.64 ? 253 ILE A H    1 
ATOM   3471 H HA   . ILE A 1 234 ? 1.324   0.792   2.990   1.00 12.39 ? 253 ILE A HA   1 
ATOM   3472 H HB   . ILE A 1 234 ? 0.021   -1.711  3.145   1.00 13.42 ? 253 ILE A HB   1 
ATOM   3473 H HG12 . ILE A 1 234 ? 2.389   -1.285  1.705   1.00 14.21 ? 253 ILE A HG12 1 
ATOM   3474 H HG13 . ILE A 1 234 ? 2.374   -1.945  3.150   1.00 14.21 ? 253 ILE A HG13 1 
ATOM   3475 H HG21 . ILE A 1 234 ? -0.389  -1.471  0.874   1.00 15.96 ? 253 ILE A HG21 1 
ATOM   3476 H HG22 . ILE A 1 234 ? -1.010  -0.233  1.652   1.00 15.96 ? 253 ILE A HG22 1 
ATOM   3477 H HG23 . ILE A 1 234 ? 0.365   -0.073  0.873   1.00 15.96 ? 253 ILE A HG23 1 
ATOM   3478 H HD11 . ILE A 1 234 ? 2.525   -3.617  1.604   1.00 15.20 ? 253 ILE A HD11 1 
ATOM   3479 H HD12 . ILE A 1 234 ? 1.092   -3.708  2.284   1.00 15.20 ? 253 ILE A HD12 1 
ATOM   3480 H HD13 . ILE A 1 234 ? 1.246   -3.069  0.837   1.00 15.20 ? 253 ILE A HD13 1 
ATOM   3481 N N    . GLU A 1 235 ? -0.481  2.074   4.231   1.00 10.90 ? 254 GLU A N    1 
ATOM   3482 C CA   . GLU A 1 235 ? -1.570  2.711   4.958   1.00 10.93 ? 254 GLU A CA   1 
ATOM   3483 C C    . GLU A 1 235 ? -2.848  2.787   4.141   1.00 11.22 ? 254 GLU A C    1 
ATOM   3484 O O    . GLU A 1 235 ? -3.949  2.786   4.709   1.00 12.09 ? 254 GLU A O    1 
ATOM   3485 C CB   . GLU A 1 235 ? -1.163  4.134   5.373   1.00 11.86 ? 254 GLU A CB   1 
ATOM   3486 C CG   . GLU A 1 235 ? -2.109  4.735   6.360   1.00 13.53 ? 254 GLU A CG   1 
ATOM   3487 C CD   . GLU A 1 235 ? -2.186  6.243   6.369   1.00 14.55 ? 254 GLU A CD   1 
ATOM   3488 O OE1  . GLU A 1 235 ? -1.221  6.921   5.901   1.00 14.23 ? 254 GLU A OE1  1 
ATOM   3489 O OE2  . GLU A 1 235 ? -3.229  6.773   6.867   1.00 15.71 ? 254 GLU A OE2  1 
ATOM   3490 H H    . GLU A 1 235 ? 0.131   2.614   3.959   1.00 13.08 ? 254 GLU A H    1 
ATOM   3491 H HA   . GLU A 1 235 ? -1.745  2.186   5.755   1.00 13.12 ? 254 GLU A HA   1 
ATOM   3492 H HB2  . GLU A 1 235 ? -0.282  4.106   5.779   1.00 14.24 ? 254 GLU A HB2  1 
ATOM   3493 H HB3  . GLU A 1 235 ? -1.148  4.701   4.586   1.00 14.24 ? 254 GLU A HB3  1 
ATOM   3494 H HG2  . GLU A 1 235 ? -3.001  4.404   6.167   1.00 16.24 ? 254 GLU A HG2  1 
ATOM   3495 H HG3  . GLU A 1 235 ? -1.838  4.457   7.249   1.00 16.24 ? 254 GLU A HG3  1 
ATOM   3496 N N    . HIS A 1 236 ? -2.725  2.918   2.824   1.00 12.41 ? 255 HIS A N    1 
ATOM   3497 C CA   . HIS A 1 236 ? -3.857  3.278   1.978   1.00 12.28 ? 255 HIS A CA   1 
ATOM   3498 C C    . HIS A 1 236 ? -4.380  2.115   1.156   1.00 13.11 ? 255 HIS A C    1 
ATOM   3499 O O    . HIS A 1 236 ? -5.041  2.343   0.142   1.00 13.86 ? 255 HIS A O    1 
ATOM   3500 C CB   . HIS A 1 236 ? -3.490  4.428   1.043   1.00 13.36 ? 255 HIS A CB   1 
ATOM   3501 C CG   . HIS A 1 236 ? -3.404  5.748   1.721   1.00 13.95 ? 255 HIS A CG   1 
ATOM   3502 N ND1  . HIS A 1 236 ? -3.193  6.920   1.026   1.00 14.33 ? 255 HIS A ND1  1 
ATOM   3503 C CD2  . HIS A 1 236 ? -3.517  6.093   3.025   1.00 14.59 ? 255 HIS A CD2  1 
ATOM   3504 C CE1  . HIS A 1 236 ? -3.159  7.931   1.872   1.00 14.79 ? 255 HIS A CE1  1 
ATOM   3505 N NE2  . HIS A 1 236 ? -3.371  7.460   3.090   1.00 15.96 ? 255 HIS A NE2  1 
ATOM   3506 H H    . HIS A 1 236 ? -1.989  2.803   2.394   1.00 14.90 ? 255 HIS A H    1 
ATOM   3507 H HA   . HIS A 1 236 ? -4.569  3.572   2.567   1.00 14.74 ? 255 HIS A HA   1 
ATOM   3508 H HB2  . HIS A 1 236 ? -2.625  4.243   0.645   1.00 16.04 ? 255 HIS A HB2  1 
ATOM   3509 H HB3  . HIS A 1 236 ? -4.166  4.494   0.351   1.00 16.04 ? 255 HIS A HB3  1 
ATOM   3510 H HD1  . HIS A 1 236 ? -3.098  6.982   0.173   1.00 17.20 ? 255 HIS A HD1  1 
ATOM   3511 H HD2  . HIS A 1 236 ? -3.665  5.517   3.739   1.00 17.52 ? 255 HIS A HD2  1 
ATOM   3512 H HE1  . HIS A 1 236 ? -3.013  8.822   1.650   1.00 17.75 ? 255 HIS A HE1  1 
ATOM   3513 N N    . PHE A 1 237 ? -4.137  0.871   1.577   1.00 13.24 ? 256 PHE A N    1 
ATOM   3514 C CA   . PHE A 1 237 ? -4.467  -0.247  0.715   1.00 12.63 ? 256 PHE A CA   1 
ATOM   3515 C C    . PHE A 1 237 ? -5.914  -0.186  0.231   1.00 12.64 ? 256 PHE A C    1 
ATOM   3516 O O    . PHE A 1 237 ? -6.851  -0.163  1.034   1.00 12.63 ? 256 PHE A O    1 
ATOM   3517 C CB   . PHE A 1 237 ? -4.226  -1.614  1.363   1.00 13.14 ? 256 PHE A CB   1 
ATOM   3518 C CG   . PHE A 1 237 ? -4.464  -2.705  0.384   1.00 13.73 ? 256 PHE A CG   1 
ATOM   3519 C CD1  . PHE A 1 237 ? -3.536  -2.948  -0.619  1.00 14.76 ? 256 PHE A CD1  1 
ATOM   3520 C CD2  . PHE A 1 237 ? -5.663  -3.384  0.349   1.00 14.36 ? 256 PHE A CD2  1 
ATOM   3521 C CE1  . PHE A 1 237 ? -3.781  -3.892  -1.595  1.00 14.86 ? 256 PHE A CE1  1 
ATOM   3522 C CE2  . PHE A 1 237 ? -5.918  -4.317  -0.634  1.00 15.47 ? 256 PHE A CE2  1 
ATOM   3523 C CZ   . PHE A 1 237 ? -4.987  -4.567  -1.615  1.00 14.98 ? 256 PHE A CZ   1 
ATOM   3524 H H    . PHE A 1 237 ? -3.792  0.662   2.337   1.00 15.90 ? 256 PHE A H    1 
ATOM   3525 H HA   . PHE A 1 237 ? -3.862  -0.176  -0.040  1.00 15.16 ? 256 PHE A HA   1 
ATOM   3526 H HB2  . PHE A 1 237 ? -3.308  -1.669  1.672   1.00 15.77 ? 256 PHE A HB2  1 
ATOM   3527 H HB3  . PHE A 1 237 ? -4.835  -1.730  2.110   1.00 15.77 ? 256 PHE A HB3  1 
ATOM   3528 H HD1  . PHE A 1 237 ? -2.740  -2.468  -0.633  1.00 17.72 ? 256 PHE A HD1  1 
ATOM   3529 H HD2  . PHE A 1 237 ? -6.307  -3.210  0.997   1.00 17.23 ? 256 PHE A HD2  1 
ATOM   3530 H HE1  . PHE A 1 237 ? -3.134  -4.074  -2.238  1.00 17.83 ? 256 PHE A HE1  1 
ATOM   3531 H HE2  . PHE A 1 237 ? -6.724  -4.780  -0.634  1.00 18.57 ? 256 PHE A HE2  1 
ATOM   3532 H HZ   . PHE A 1 237 ? -5.167  -5.184  -2.287  1.00 17.98 ? 256 PHE A HZ   1 
ATOM   3533 N N    . GLY A 1 238 ? -6.092  -0.252  -1.091  1.00 13.30 ? 257 GLY A N    1 
ATOM   3534 C CA   . GLY A 1 238 ? -7.403  -0.335  -1.707  1.00 13.13 ? 257 GLY A CA   1 
ATOM   3535 C C    . GLY A 1 238 ? -8.254  0.913   -1.652  1.00 13.13 ? 257 GLY A C    1 
ATOM   3536 O O    . GLY A 1 238 ? -9.404  0.875   -2.126  1.00 14.39 ? 257 GLY A O    1 
ATOM   3537 H H    . GLY A 1 238 ? -5.448  -0.249  -1.661  1.00 15.97 ? 257 GLY A H    1 
ATOM   3538 H HA2  . GLY A 1 238 ? -7.286  -0.564  -2.643  1.00 15.76 ? 257 GLY A HA2  1 
ATOM   3539 H HA3  . GLY A 1 238 ? -7.901  -1.044  -1.270  1.00 15.76 ? 257 GLY A HA3  1 
ATOM   3540 N N    . HIS A 1 239 ? -7.722  2.019   -1.140  1.00 13.09 ? 258 HIS A N    1 
ATOM   3541 C CA   . HIS A 1 239 ? -8.514  3.197   -0.812  1.00 13.96 ? 258 HIS A CA   1 
ATOM   3542 C C    . HIS A 1 239 ? -7.729  4.453   -1.146  1.00 14.45 ? 258 HIS A C    1 
ATOM   3543 O O    . HIS A 1 239 ? -6.593  4.405   -1.628  1.00 15.33 ? 258 HIS A O    1 
ATOM   3544 C CB   . HIS A 1 239 ? -8.956  3.137   0.654   1.00 14.98 ? 258 HIS A CB   1 
ATOM   3545 C CG   . HIS A 1 239 ? -10.130 2.241   0.861   1.00 14.96 ? 258 HIS A CG   1 
ATOM   3546 N ND1  . HIS A 1 239 ? -11.424 2.716   0.889   1.00 17.01 ? 258 HIS A ND1  1 
ATOM   3547 C CD2  . HIS A 1 239 ? -10.217 0.892   0.940   1.00 15.38 ? 258 HIS A CD2  1 
ATOM   3548 C CE1  . HIS A 1 239 ? -12.255 1.701   1.044   1.00 16.89 ? 258 HIS A CE1  1 
ATOM   3549 N NE2  . HIS A 1 239 ? -11.552 0.584   1.061   1.00 16.75 ? 258 HIS A NE2  1 
ATOM   3550 H H    . HIS A 1 239 ? -6.884  2.112   -0.970  1.00 15.72 ? 258 HIS A H    1 
ATOM   3551 H HA   . HIS A 1 239 ? -9.308  3.225   -1.370  1.00 16.76 ? 258 HIS A HA   1 
ATOM   3552 H HB2  . HIS A 1 239 ? -8.222  2.801   1.192   1.00 17.98 ? 258 HIS A HB2  1 
ATOM   3553 H HB3  . HIS A 1 239 ? -9.202  4.028   0.947   1.00 17.98 ? 258 HIS A HB3  1 
ATOM   3554 H HD2  . HIS A 1 239 ? -9.510  0.289   0.917   1.00 18.46 ? 258 HIS A HD2  1 
ATOM   3555 H HE1  . HIS A 1 239 ? -13.179 1.763   1.128   1.00 20.27 ? 258 HIS A HE1  1 
ATOM   3556 H HE2  . HIS A 1 239 ? -11.876 -0.209  1.135   1.00 20.11 ? 258 HIS A HE2  1 
ATOM   3557 N N    . PHE A 1 240 ? -8.366  5.595   -0.906  1.00 14.68 ? 259 PHE A N    1 
ATOM   3558 C CA   . PHE A 1 240 ? -7.778  6.914   -1.167  1.00 14.07 ? 259 PHE A CA   1 
ATOM   3559 C C    . PHE A 1 240 ? -7.397  6.979   -2.643  1.00 16.10 ? 259 PHE A C    1 
ATOM   3560 O O    . PHE A 1 240 ? -8.275  6.778   -3.492  1.00 18.51 ? 259 PHE A O    1 
ATOM   3561 C CB   . PHE A 1 240 ? -6.666  7.202   -0.152  1.00 14.69 ? 259 PHE A CB   1 
ATOM   3562 C CG   . PHE A 1 240 ? -7.094  7.094   1.264   1.00 14.99 ? 259 PHE A CG   1 
ATOM   3563 C CD1  . PHE A 1 240 ? -7.734  8.153   1.880   1.00 15.81 ? 259 PHE A CD1  1 
ATOM   3564 C CD2  . PHE A 1 240 ? -6.863  5.940   1.987   1.00 14.65 ? 259 PHE A CD2  1 
ATOM   3565 C CE1  . PHE A 1 240 ? -8.149  8.055   3.202   1.00 15.92 ? 259 PHE A CE1  1 
ATOM   3566 C CE2  . PHE A 1 240 ? -7.284  5.849   3.306   1.00 15.01 ? 259 PHE A CE2  1 
ATOM   3567 C CZ   . PHE A 1 240 ? -7.915  6.918   3.907   1.00 16.08 ? 259 PHE A CZ   1 
ATOM   3568 H H    . PHE A 1 240 ? -9.162  5.636   -0.583  1.00 17.63 ? 259 PHE A H    1 
ATOM   3569 H HA   . PHE A 1 240 ? -8.467  7.583   -1.027  1.00 16.89 ? 259 PHE A HA   1 
ATOM   3570 H HB2  . PHE A 1 240 ? -5.947  6.566   -0.292  1.00 17.64 ? 259 PHE A HB2  1 
ATOM   3571 H HB3  . PHE A 1 240 ? -6.342  8.105   -0.294  1.00 17.64 ? 259 PHE A HB3  1 
ATOM   3572 H HD1  . PHE A 1 240 ? -7.887  8.938   1.406   1.00 18.98 ? 259 PHE A HD1  1 
ATOM   3573 H HD2  . PHE A 1 240 ? -6.423  5.223   1.590   1.00 17.59 ? 259 PHE A HD2  1 
ATOM   3574 H HE1  . PHE A 1 240 ? -8.588  8.769   3.605   1.00 19.12 ? 259 PHE A HE1  1 
ATOM   3575 H HE2  . PHE A 1 240 ? -7.142  5.065   3.786   1.00 18.02 ? 259 PHE A HE2  1 
ATOM   3576 H HZ   . PHE A 1 240 ? -8.180  6.861   4.796   1.00 19.30 ? 259 PHE A HZ   1 
ATOM   3577 N N    . GLN A 1 241 ? -6.142  7.256   -2.989  1.00 16.97 ? 260 GLN A N    1 
ATOM   3578 C CA   . GLN A 1 241 ? -5.700  7.261   -4.375  1.00 19.07 ? 260 GLN A CA   1 
ATOM   3579 C C    . GLN A 1 241 ? -5.056  5.934   -4.777  1.00 18.03 ? 260 GLN A C    1 
ATOM   3580 O O    . GLN A 1 241 ? -4.377  5.866   -5.811  1.00 18.13 ? 260 GLN A O    1 
ATOM   3581 C CB   . GLN A 1 241 ? -4.749  8.427   -4.636  1.00 22.13 ? 260 GLN A CB   1 
ATOM   3582 C CG   . GLN A 1 241 ? -5.300  9.880   -4.404  1.00 26.68 ? 260 GLN A CG   1 
ATOM   3583 C CD   . GLN A 1 241 ? -5.840  10.146  -3.006  1.00 31.73 ? 260 GLN A CD   1 
ATOM   3584 O OE1  . GLN A 1 241 ? -5.076  10.454  -2.086  1.00 33.75 ? 260 GLN A OE1  1 
ATOM   3585 N NE2  . GLN A 1 241 ? -7.169  10.155  -2.864  1.00 33.88 ? 260 GLN A NE2  1 
ATOM   3586 H H    . GLN A 1 241 ? -5.520  7.446   -2.426  1.00 20.37 ? 260 GLN A H    1 
ATOM   3587 H HA   . GLN A 1 241 ? -6.474  7.396   -4.943  1.00 22.89 ? 260 GLN A HA   1 
ATOM   3588 H HB2  . GLN A 1 241 ? -3.982  8.322   -4.052  1.00 26.57 ? 260 GLN A HB2  1 
ATOM   3589 H HB3  . GLN A 1 241 ? -4.469  8.379   -5.563  1.00 26.57 ? 260 GLN A HB3  1 
ATOM   3590 H HG2  . GLN A 1 241 ? -4.580  10.510  -4.562  1.00 32.03 ? 260 GLN A HG2  1 
ATOM   3591 H HG3  . GLN A 1 241 ? -6.023  10.038  -5.030  1.00 32.03 ? 260 GLN A HG3  1 
ATOM   3592 H HE21 . GLN A 1 241 ? -7.675  10.014  -3.545  1.00 40.66 ? 260 GLN A HE21 1 
ATOM   3593 H HE22 . GLN A 1 241 ? -7.519  10.301  -2.092  1.00 40.66 ? 260 GLN A HE22 1 
ATOM   3594 N N    . SER A 1 242 ? -5.286  4.871   -4.003  1.00 16.33 ? 261 SER A N    1 
ATOM   3595 C CA   . SER A 1 242 ? -4.655  3.580   -4.222  1.00 15.34 ? 261 SER A CA   1 
ATOM   3596 C C    . SER A 1 242 ? -5.658  2.477   -4.525  1.00 15.20 ? 261 SER A C    1 
ATOM   3597 O O    . SER A 1 242 ? -5.326  1.296   -4.371  1.00 15.97 ? 261 SER A O    1 
ATOM   3598 C CB   . SER A 1 242 ? -3.813  3.183   -3.009  1.00 15.45 ? 261 SER A CB   1 
ATOM   3599 O OG   . SER A 1 242 ? -2.866  4.173   -2.679  1.00 14.98 ? 261 SER A OG   1 
ATOM   3600 H H    . SER A 1 242 ? -5.820  4.879   -3.328  1.00 19.61 ? 261 SER A H    1 
ATOM   3601 H HA   . SER A 1 242 ? -4.072  3.666   -4.993  1.00 18.41 ? 261 SER A HA   1 
ATOM   3602 H HB2  . SER A 1 242 ? -4.403  3.051   -2.250  1.00 18.55 ? 261 SER A HB2  1 
ATOM   3603 H HB3  . SER A 1 242 ? -3.344  2.359   -3.212  1.00 18.55 ? 261 SER A HB3  1 
ATOM   3604 H HG   . SER A 1 242 ? -2.376  4.334   -3.342  1.00 17.99 ? 261 SER A HG   1 
ATOM   3605 N N    . ALA A 1 243 ? -6.871  2.827   -4.967  1.00 15.83 ? 262 ALA A N    1 
ATOM   3606 C CA   . ALA A 1 243 ? -7.924  1.830   -5.148  1.00 16.31 ? 262 ALA A CA   1 
ATOM   3607 C C    . ALA A 1 243 ? -7.869  1.108   -6.490  1.00 17.13 ? 262 ALA A C    1 
ATOM   3608 O O    . ALA A 1 243 ? -8.542  0.088   -6.649  1.00 17.95 ? 262 ALA A O    1 
ATOM   3609 C CB   . ALA A 1 243 ? -9.306  2.472   -4.955  1.00 17.23 ? 262 ALA A CB   1 
ATOM   3610 H H    . ALA A 1 243 ? -7.105  3.630   -5.166  1.00 19.00 ? 262 ALA A H    1 
ATOM   3611 H HA   . ALA A 1 243 ? -7.815  1.154   -4.461  1.00 19.58 ? 262 ALA A HA   1 
ATOM   3612 H HB1  . ALA A 1 243 ? -9.985  1.781   -5.006  1.00 20.68 ? 262 ALA A HB1  1 
ATOM   3613 H HB2  . ALA A 1 243 ? -9.336  2.902   -4.086  1.00 20.68 ? 262 ALA A HB2  1 
ATOM   3614 H HB3  . ALA A 1 243 ? -9.449  3.129   -5.655  1.00 20.68 ? 262 ALA A HB3  1 
ATOM   3615 N N    . SER A 1 244 ? -7.072  1.573   -7.439  1.00 16.90 ? 263 SER A N    1 
ATOM   3616 C CA   . SER A 1 244 ? -7.054  0.938   -8.746  1.00 17.25 ? 263 SER A CA   1 
ATOM   3617 C C    . SER A 1 244 ? -6.393  -0.434  -8.665  1.00 17.22 ? 263 SER A C    1 
ATOM   3618 O O    . SER A 1 244 ? -5.571  -0.711  -7.792  1.00 17.11 ? 263 SER A O    1 
ATOM   3619 C CB   . SER A 1 244 ? -6.340  1.819   -9.770  1.00 17.86 ? 263 SER A CB   1 
ATOM   3620 O OG   . SER A 1 244 ? -4.948  1.824   -9.561  1.00 18.35 ? 263 SER A OG   1 
ATOM   3621 H H    . SER A 1 244 ? -6.540  2.243   -7.353  1.00 20.28 ? 263 SER A H    1 
ATOM   3622 H HA   . SER A 1 244 ? -7.965  0.814   -9.055  1.00 20.70 ? 263 SER A HA   1 
ATOM   3623 H HB2  . SER A 1 244 ? -6.522  1.478   -10.660 1.00 21.43 ? 263 SER A HB2  1 
ATOM   3624 H HB3  . SER A 1 244 ? -6.672  2.727   -9.689  1.00 21.43 ? 263 SER A HB3  1 
ATOM   3625 H HG   . SER A 1 244 ? -4.548  1.932   -10.291 1.00 22.02 ? 263 SER A HG   1 
ATOM   3626 N N    . LYS A 1 245 ? -6.758  -1.304  -9.615  1.00 18.53 ? 264 LYS A N    1 
ATOM   3627 C CA   . LYS A 1 245 ? -6.136  -2.623  -9.665  1.00 18.98 ? 264 LYS A CA   1 
ATOM   3628 C C    . LYS A 1 245 ? -4.626  -2.496  -9.809  1.00 18.40 ? 264 LYS A C    1 
ATOM   3629 O O    . LYS A 1 245 ? -3.870  -3.282  -9.221  1.00 17.72 ? 264 LYS A O    1 
ATOM   3630 C CB   . LYS A 1 245 ? -6.777  -3.463  -10.772 1.00 21.80 ? 264 LYS A CB   1 
ATOM   3631 C CG   . LYS A 1 245 ? -6.472  -2.999  -12.200 1.00 23.49 ? 264 LYS A CG   1 
ATOM   3632 C CD   . LYS A 1 245 ? -7.352  -3.708  -13.228 1.00 25.07 ? 264 LYS A CD   1 
ATOM   3633 C CE   . LYS A 1 245 ? -7.035  -3.241  -14.652 1.00 27.02 ? 264 LYS A CE   1 
ATOM   3634 N NZ   . LYS A 1 245 ? -7.594  -1.888  -14.947 1.00 28.67 ? 264 LYS A NZ   1 
ATOM   3635 H H    . LYS A 1 245 ? -7.348  -1.156  -10.223 1.00 22.24 ? 264 LYS A H    1 
ATOM   3636 H HA   . LYS A 1 245 ? -6.298  -3.103  -8.838  1.00 22.78 ? 264 LYS A HA   1 
ATOM   3637 H HB2  . LYS A 1 245 ? -6.458  -4.375  -10.689 1.00 26.17 ? 264 LYS A HB2  1 
ATOM   3638 H HB3  . LYS A 1 245 ? -7.740  -3.437  -10.658 1.00 26.17 ? 264 LYS A HB3  1 
ATOM   3639 H HG2  . LYS A 1 245 ? -6.635  -2.045  -12.268 1.00 28.19 ? 264 LYS A HG2  1 
ATOM   3640 H HG3  . LYS A 1 245 ? -5.545  -3.193  -12.408 1.00 28.19 ? 264 LYS A HG3  1 
ATOM   3641 H HD2  . LYS A 1 245 ? -7.197  -4.664  -13.179 1.00 30.09 ? 264 LYS A HD2  1 
ATOM   3642 H HD3  . LYS A 1 245 ? -8.284  -3.513  -13.043 1.00 30.09 ? 264 LYS A HD3  1 
ATOM   3643 H HE2  . LYS A 1 245 ? -6.073  -3.200  -14.766 1.00 32.44 ? 264 LYS A HE2  1 
ATOM   3644 H HE3  . LYS A 1 245 ? -7.418  -3.869  -15.285 1.00 32.44 ? 264 LYS A HE3  1 
ATOM   3645 H HZ1  . LYS A 1 245 ? -7.563  -1.730  -15.822 1.00 34.41 ? 264 LYS A HZ1  1 
ATOM   3646 H HZ2  . LYS A 1 245 ? -8.441  -1.843  -14.675 1.00 34.41 ? 264 LYS A HZ2  1 
ATOM   3647 H HZ3  . LYS A 1 245 ? -7.121  -1.264  -14.524 1.00 34.41 ? 264 LYS A HZ3  1 
ATOM   3648 N N    . GLU A 1 246 ? -4.165  -1.494  -10.564 1.00 19.15 ? 265 GLU A N    1 
ATOM   3649 C CA   . GLU A 1 246 ? -2.730  -1.314  -10.761 1.00 19.41 ? 265 GLU A CA   1 
ATOM   3650 C C    . GLU A 1 246 ? -2.027  -1.008  -9.443  1.00 17.55 ? 265 GLU A C    1 
ATOM   3651 O O    . GLU A 1 246 ? -0.976  -1.583  -9.132  1.00 17.47 ? 265 GLU A O    1 
ATOM   3652 C CB   . GLU A 1 246 ? -2.482  -0.190  -11.763 1.00 20.79 ? 265 GLU A CB   1 
ATOM   3653 C CG   . GLU A 1 246 ? -2.913  -0.503  -13.189 1.00 22.61 ? 265 GLU A CG   1 
ATOM   3654 C CD   . GLU A 1 246 ? -4.408  -0.298  -13.458 1.00 23.95 ? 265 GLU A CD   1 
ATOM   3655 O OE1  . GLU A 1 246 ? -5.112  0.246   -12.573 1.00 22.93 ? 265 GLU A OE1  1 
ATOM   3656 O OE2  . GLU A 1 246 ? -4.879  -0.677  -14.563 1.00 26.21 ? 265 GLU A OE2  1 
ATOM   3657 H H    . GLU A 1 246 ? -4.657  -0.913  -10.966 1.00 22.99 ? 265 GLU A H    1 
ATOM   3658 H HA   . GLU A 1 246 ? -2.360  -2.136  -11.121 1.00 23.30 ? 265 GLU A HA   1 
ATOM   3659 H HB2  . GLU A 1 246 ? -2.974  0.595   -11.474 1.00 24.96 ? 265 GLU A HB2  1 
ATOM   3660 H HB3  . GLU A 1 246 ? -1.531  0.003   -11.781 1.00 24.96 ? 265 GLU A HB3  1 
ATOM   3661 H HG2  . GLU A 1 246 ? -2.425  0.076   -13.795 1.00 27.13 ? 265 GLU A HG2  1 
ATOM   3662 H HG3  . GLU A 1 246 ? -2.706  -1.431  -13.378 1.00 27.13 ? 265 GLU A HG3  1 
ATOM   3663 N N    . THR A 1 247 ? -2.587  -0.094  -8.651  1.00 16.51 ? 266 THR A N    1 
ATOM   3664 C CA   . THR A 1 247 ? -1.929  0.267   -7.402  1.00 15.59 ? 266 THR A CA   1 
ATOM   3665 C C    . THR A 1 247 ? -2.097  -0.816  -6.347  1.00 14.77 ? 266 THR A C    1 
ATOM   3666 O O    . THR A 1 247 ? -1.182  -1.031  -5.547  1.00 15.07 ? 266 THR A O    1 
ATOM   3667 C CB   . THR A 1 247 ? -2.422  1.629   -6.896  1.00 16.37 ? 266 THR A CB   1 
ATOM   3668 O OG1  . THR A 1 247 ? -3.851  1.643   -6.817  1.00 16.19 ? 266 THR A OG1  1 
ATOM   3669 C CG2  . THR A 1 247 ? -1.969  2.734   -7.836  1.00 17.12 ? 266 THR A CG2  1 
ATOM   3670 H H    . THR A 1 247 ? -3.325  0.318   -8.810  1.00 19.82 ? 266 THR A H    1 
ATOM   3671 H HA   . THR A 1 247 ? -0.978  0.370   -7.564  1.00 18.71 ? 266 THR A HA   1 
ATOM   3672 H HB   . THR A 1 247 ? -2.053  1.791   -6.014  1.00 19.65 ? 266 THR A HB   1 
ATOM   3673 H HG1  . THR A 1 247 ? -4.182  1.645   -7.589  1.00 19.43 ? 266 THR A HG1  1 
ATOM   3674 H HG21 . THR A 1 247 ? -2.440  3.557   -7.631  1.00 20.55 ? 266 THR A HG21 1 
ATOM   3675 H HG22 . THR A 1 247 ? -1.016  2.883   -7.737  1.00 20.55 ? 266 THR A HG22 1 
ATOM   3676 H HG23 . THR A 1 247 ? -2.155  2.486   -8.755  1.00 20.55 ? 266 THR A HG23 1 
ATOM   3677 N N    . MET A 1 248 ? -3.239  -1.506  -6.322  1.00 14.65 ? 267 MET A N    1 
ATOM   3678 C CA   . MET A 1 248 ? -3.349  -2.639  -5.414  1.00 13.85 ? 267 MET A CA   1 
ATOM   3679 C C    . MET A 1 248 ? -2.322  -3.722  -5.707  1.00 14.56 ? 267 MET A C    1 
ATOM   3680 O O    . MET A 1 248 ? -1.714  -4.286  -4.784  1.00 14.36 ? 267 MET A O    1 
ATOM   3681 C CB   . MET A 1 248 ? -4.745  -3.226  -5.225  1.00 14.80 ? 267 MET A CB   1 
ATOM   3682 C CG   . MET A 1 248 ? -5.810  -2.239  -4.791  1.00 15.07 ? 267 MET A CG   1 
ATOM   3683 S SD   . MET A 1 248 ? -7.417  -3.018  -4.561  1.00 16.00 ? 267 MET A SD   1 
ATOM   3684 C CE   . MET A 1 248 ? -7.916  -3.165  -6.325  1.00 17.57 ? 267 MET A CE   1 
ATOM   3685 H H    . MET A 1 248 ? -3.934  -1.343  -6.802  1.00 17.59 ? 267 MET A H    1 
ATOM   3686 H HA   . MET A 1 248 ? -3.170  -2.243  -4.547  1.00 16.63 ? 267 MET A HA   1 
ATOM   3687 H HB2  . MET A 1 248 ? -5.032  -3.610  -6.068  1.00 17.77 ? 267 MET A HB2  1 
ATOM   3688 H HB3  . MET A 1 248 ? -4.696  -3.917  -4.545  1.00 17.77 ? 267 MET A HB3  1 
ATOM   3689 H HG2  . MET A 1 248 ? -5.546  -1.837  -3.949  1.00 18.09 ? 267 MET A HG2  1 
ATOM   3690 H HG3  . MET A 1 248 ? -5.902  -1.553  -5.471  1.00 18.09 ? 267 MET A HG3  1 
ATOM   3691 H HE1  . MET A 1 248 ? -8.793  -3.576  -6.372  1.00 21.09 ? 267 MET A HE1  1 
ATOM   3692 H HE2  . MET A 1 248 ? -7.944  -2.280  -6.720  1.00 21.09 ? 267 MET A HE2  1 
ATOM   3693 H HE3  . MET A 1 248 ? -7.267  -3.715  -6.792  1.00 21.09 ? 267 MET A HE3  1 
ATOM   3694 N N    . LEU A 1 249 ? -2.144  -4.059  -6.984  1.00 15.08 ? 268 LEU A N    1 
ATOM   3695 C CA   . LEU A 1 249 ? -1.160  -5.075  -7.320  1.00 16.18 ? 268 LEU A CA   1 
ATOM   3696 C C    . LEU A 1 249 ? 0.234   -4.627  -6.896  1.00 15.11 ? 268 LEU A C    1 
ATOM   3697 O O    . LEU A 1 249 ? 1.011   -5.420  -6.339  1.00 15.47 ? 268 LEU A O    1 
ATOM   3698 C CB   . LEU A 1 249 ? -1.190  -5.370  -8.815  1.00 17.09 ? 268 LEU A CB   1 
ATOM   3699 C CG   . LEU A 1 249 ? -0.226  -6.481  -9.234  1.00 17.70 ? 268 LEU A CG   1 
ATOM   3700 C CD1  . LEU A 1 249 ? -0.462  -7.799  -8.518  1.00 17.41 ? 268 LEU A CD1  1 
ATOM   3701 C CD2  . LEU A 1 249 ? -0.273  -6.680  -10.760 1.00 19.00 ? 268 LEU A CD2  1 
ATOM   3702 H H    . LEU A 1 249 ? -2.569  -3.723  -7.652  1.00 18.10 ? 268 LEU A H    1 
ATOM   3703 H HA   . LEU A 1 249 ? -1.381  -5.896  -6.853  1.00 19.42 ? 268 LEU A HA   1 
ATOM   3704 H HB2  . LEU A 1 249 ? -2.087  -5.645  -9.062  1.00 20.51 ? 268 LEU A HB2  1 
ATOM   3705 H HB3  . LEU A 1 249 ? -0.944  -4.565  -9.298  1.00 20.51 ? 268 LEU A HB3  1 
ATOM   3706 H HG   . LEU A 1 249 ? 0.663   -6.196  -8.970  1.00 21.25 ? 268 LEU A HG   1 
ATOM   3707 H HD11 . LEU A 1 249 ? 0.036   -8.498  -8.971  1.00 20.89 ? 268 LEU A HD11 1 
ATOM   3708 H HD12 . LEU A 1 249 ? -0.158  -7.719  -7.600  1.00 20.89 ? 268 LEU A HD12 1 
ATOM   3709 H HD13 . LEU A 1 249 ? -1.410  -8.003  -8.536  1.00 20.89 ? 268 LEU A HD13 1 
ATOM   3710 H HD21 . LEU A 1 249 ? 0.361   -7.371  -11.007 1.00 22.81 ? 268 LEU A HD21 1 
ATOM   3711 H HD22 . LEU A 1 249 ? -1.169  -6.947  -11.016 1.00 22.81 ? 268 LEU A HD22 1 
ATOM   3712 H HD23 . LEU A 1 249 ? -0.038  -5.845  -11.194 1.00 22.81 ? 268 LEU A HD23 1 
ATOM   3713 N N    A ARG A 1 250 ? 0.564   -3.350  -7.127  0.57 15.66 ? 269 ARG A N    1 
ATOM   3714 N N    B ARG A 1 250 ? 0.567   -3.353  -7.133  0.43 15.71 ? 269 ARG A N    1 
ATOM   3715 C CA   A ARG A 1 250 ? 1.875   -2.842  -6.726  0.57 15.12 ? 269 ARG A CA   1 
ATOM   3716 C CA   B ARG A 1 250 ? 1.876   -2.858  -6.717  0.43 15.47 ? 269 ARG A CA   1 
ATOM   3717 C C    A ARG A 1 250 ? 2.079   -2.958  -5.219  0.57 15.07 ? 269 ARG A C    1 
ATOM   3718 C C    B ARG A 1 250 ? 2.066   -3.008  -5.214  0.43 15.11 ? 269 ARG A C    1 
ATOM   3719 O O    A ARG A 1 250 ? 3.161   -3.339  -4.765  0.57 14.91 ? 269 ARG A O    1 
ATOM   3720 O O    B ARG A 1 250 ? 3.123   -3.454  -4.756  0.43 14.84 ? 269 ARG A O    1 
ATOM   3721 C CB   A ARG A 1 250 ? 2.064   -1.401  -7.205  0.57 16.16 ? 269 ARG A CB   1 
ATOM   3722 C CB   B ARG A 1 250 ? 2.087   -1.403  -7.138  0.43 16.59 ? 269 ARG A CB   1 
ATOM   3723 C CG   A ARG A 1 250 ? 2.313   -1.304  -8.710  0.57 17.13 ? 269 ARG A CG   1 
ATOM   3724 C CG   B ARG A 1 250 ? 3.557   -1.018  -7.075  0.43 17.63 ? 269 ARG A CG   1 
ATOM   3725 C CD   A ARG A 1 250 ? 3.336   -0.231  -9.079  0.57 18.73 ? 269 ARG A CD   1 
ATOM   3726 C CD   B ARG A 1 250 ? 3.825   0.469   -7.224  0.43 18.88 ? 269 ARG A CD   1 
ATOM   3727 N NE   A ARG A 1 250 ? 2.959   1.082   -8.581  0.57 18.80 ? 269 ARG A NE   1 
ATOM   3728 N NE   B ARG A 1 250 ? 4.154   1.088   -5.942  0.43 18.79 ? 269 ARG A NE   1 
ATOM   3729 C CZ   A ARG A 1 250 ? 2.046   1.877   -9.124  0.57 19.49 ? 269 ARG A CZ   1 
ATOM   3730 C CZ   B ARG A 1 250 ? 5.136   0.717   -5.128  0.43 20.16 ? 269 ARG A CZ   1 
ATOM   3731 N NH1  A ARG A 1 250 ? 1.432   1.562   -10.253 0.57 21.35 ? 269 ARG A NH1  1 
ATOM   3732 N NH1  B ARG A 1 250 ? 5.986   -0.265  -5.442  0.43 20.26 ? 269 ARG A NH1  1 
ATOM   3733 N NH2  A ARG A 1 250 ? 1.737   3.019   -8.513  0.57 17.38 ? 269 ARG A NH2  1 
ATOM   3734 N NH2  B ARG A 1 250 ? 5.260   1.333   -3.963  0.43 20.78 ? 269 ARG A NH2  1 
ATOM   3735 H H    A ARG A 1 250 ? 0.056   -2.770  -7.507  0.57 18.80 ? 269 ARG A H    1 
ATOM   3736 H H    B ARG A 1 250 ? 0.066   -2.773  -7.523  0.43 18.86 ? 269 ARG A H    1 
ATOM   3737 H HA   A ARG A 1 250 ? 2.560   -3.377  -7.156  0.57 18.15 ? 269 ARG A HA   1 
ATOM   3738 H HA   B ARG A 1 250 ? 2.550   -3.386  -7.173  0.43 18.57 ? 269 ARG A HA   1 
ATOM   3739 H HB2  A ARG A 1 250 ? 1.263   -0.893  -7.000  0.57 19.40 ? 269 ARG A HB2  1 
ATOM   3740 H HB2  B ARG A 1 250 ? 1.777   -1.284  -8.049  0.43 19.91 ? 269 ARG A HB2  1 
ATOM   3741 H HB3  A ARG A 1 250 ? 2.827   -1.014  -6.749  0.57 19.40 ? 269 ARG A HB3  1 
ATOM   3742 H HB3  B ARG A 1 250 ? 1.592   -0.821  -6.541  0.43 19.91 ? 269 ARG A HB3  1 
ATOM   3743 H HG2  A ARG A 1 250 ? 2.646   -2.156  -9.030  0.57 20.57 ? 269 ARG A HG2  1 
ATOM   3744 H HG2  B ARG A 1 250 ? 3.913   -1.294  -6.216  0.43 21.17 ? 269 ARG A HG2  1 
ATOM   3745 H HG3  A ARG A 1 250 ? 1.479   -1.085  -9.154  0.57 20.57 ? 269 ARG A HG3  1 
ATOM   3746 H HG3  B ARG A 1 250 ? 4.027   -1.472  -7.791  0.43 21.17 ? 269 ARG A HG3  1 
ATOM   3747 H HD2  A ARG A 1 250 ? 4.195   -0.465  -8.693  0.57 22.48 ? 269 ARG A HD2  1 
ATOM   3748 H HD2  B ARG A 1 250 ? 4.574   0.601   -7.827  0.43 22.66 ? 269 ARG A HD2  1 
ATOM   3749 H HD3  A ARG A 1 250 ? 3.409   -0.179  -10.044 0.57 22.48 ? 269 ARG A HD3  1 
ATOM   3750 H HD3  B ARG A 1 250 ? 3.033   0.904   -7.578  0.43 22.66 ? 269 ARG A HD3  1 
ATOM   3751 H HE   A ARG A 1 250 ? 3.362   1.367   -7.877  0.57 22.57 ? 269 ARG A HE   1 
ATOM   3752 H HE   B ARG A 1 250 ? 3.668   1.752   -5.692  0.43 22.56 ? 269 ARG A HE   1 
ATOM   3753 H HH11 A ARG A 1 250 ? 1.621   0.825   -10.654 0.57 25.63 ? 269 ARG A HH11 1 
ATOM   3754 H HH11 B ARG A 1 250 ? 5.907   -0.679  -6.192  0.43 24.32 ? 269 ARG A HH11 1 
ATOM   3755 H HH12 A ARG A 1 250 ? 0.843   2.093   -10.586 0.57 25.63 ? 269 ARG A HH12 1 
ATOM   3756 H HH12 B ARG A 1 250 ? 6.612   -0.483  -4.895  0.43 24.32 ? 269 ARG A HH12 1 
ATOM   3757 H HH21 A ARG A 1 250 ? 2.128   3.232   -7.777  0.57 20.86 ? 269 ARG A HH21 1 
ATOM   3758 H HH21 B ARG A 1 250 ? 4.712   1.959   -3.747  0.43 24.94 ? 269 ARG A HH21 1 
ATOM   3759 H HH22 A ARG A 1 250 ? 1.147   3.543   -8.854  0.57 20.86 ? 269 ARG A HH22 1 
ATOM   3760 H HH22 B ARG A 1 250 ? 5.890   1.107   -3.422  0.43 24.94 ? 269 ARG A HH22 1 
ATOM   3761 N N    . ASP A 1 251 ? 1.044   -2.670  -4.427  1.00 14.15 ? 270 ASP A N    1 
ATOM   3762 C CA   . ASP A 1 251 ? 1.170   -2.785  -2.976  1.00 13.51 ? 270 ASP A CA   1 
ATOM   3763 C C    . ASP A 1 251 ? 1.352   -4.234  -2.546  1.00 13.26 ? 270 ASP A C    1 
ATOM   3764 O O    . ASP A 1 251 ? 2.193   -4.527  -1.693  1.00 12.88 ? 270 ASP A O    1 
ATOM   3765 C CB   . ASP A 1 251 ? -0.065  -2.183  -2.298  1.00 14.18 ? 270 ASP A CB   1 
ATOM   3766 C CG   . ASP A 1 251 ? -0.044  -0.658  -2.228  1.00 13.99 ? 270 ASP A CG   1 
ATOM   3767 O OD1  . ASP A 1 251 ? 1.041   -0.034  -2.342  1.00 14.80 ? 270 ASP A OD1  1 
ATOM   3768 O OD2  . ASP A 1 251 ? -1.136  -0.079  -2.008  1.00 13.69 ? 270 ASP A OD2  1 
ATOM   3769 H H    . ASP A 1 251 ? 0.272   -2.411  -4.704  1.00 16.99 ? 270 ASP A H    1 
ATOM   3770 H HA   . ASP A 1 251 ? 1.951   -2.286  -2.692  1.00 16.21 ? 270 ASP A HA   1 
ATOM   3771 H HB2  . ASP A 1 251 ? -0.855  -2.446  -2.797  1.00 17.03 ? 270 ASP A HB2  1 
ATOM   3772 H HB3  . ASP A 1 251 ? -0.119  -2.521  -1.390  1.00 17.03 ? 270 ASP A HB3  1 
ATOM   3773 N N    . ILE A 1 252 ? 0.570   -5.152  -3.122  1.00 13.15 ? 271 ILE A N    1 
ATOM   3774 C CA   . ILE A 1 252 ? 0.675   -6.562  -2.751  1.00 13.32 ? 271 ILE A CA   1 
ATOM   3775 C C    . ILE A 1 252 ? 2.054   -7.108  -3.127  1.00 14.55 ? 271 ILE A C    1 
ATOM   3776 O O    . ILE A 1 252 ? 2.693   -7.825  -2.344  1.00 14.64 ? 271 ILE A O    1 
ATOM   3777 C CB   . ILE A 1 252 ? -0.463  -7.388  -3.394  1.00 13.61 ? 271 ILE A CB   1 
ATOM   3778 C CG1  . ILE A 1 252 ? -1.837  -6.965  -2.861  1.00 14.49 ? 271 ILE A CG1  1 
ATOM   3779 C CG2  . ILE A 1 252 ? -0.235  -8.896  -3.190  1.00 13.91 ? 271 ILE A CG2  1 
ATOM   3780 C CD1  . ILE A 1 252 ? -3.001  -7.396  -3.726  1.00 15.53 ? 271 ILE A CD1  1 
ATOM   3781 H H    . ILE A 1 252 ? -0.023  -4.986  -3.722  1.00 15.78 ? 271 ILE A H    1 
ATOM   3782 H HA   . ILE A 1 252 ? 0.576   -6.632  -1.788  1.00 15.99 ? 271 ILE A HA   1 
ATOM   3783 H HB   . ILE A 1 252 ? -0.449  -7.205  -4.347  1.00 16.34 ? 271 ILE A HB   1 
ATOM   3784 H HG12 . ILE A 1 252 ? -1.963  -7.358  -1.983  1.00 17.40 ? 271 ILE A HG12 1 
ATOM   3785 H HG13 . ILE A 1 252 ? -1.860  -5.998  -2.798  1.00 17.40 ? 271 ILE A HG13 1 
ATOM   3786 H HG21 . ILE A 1 252 ? -1.034  -9.375  -3.458  1.00 16.70 ? 271 ILE A HG21 1 
ATOM   3787 H HG22 . ILE A 1 252 ? 0.518   -9.177  -3.732  1.00 16.70 ? 271 ILE A HG22 1 
ATOM   3788 H HG23 . ILE A 1 252 ? -0.048  -9.062  -2.253  1.00 16.70 ? 271 ILE A HG23 1 
ATOM   3789 H HD11 . ILE A 1 252 ? -3.821  -7.041  -3.351  1.00 18.64 ? 271 ILE A HD11 1 
ATOM   3790 H HD12 . ILE A 1 252 ? -2.871  -7.052  -4.624  1.00 18.64 ? 271 ILE A HD12 1 
ATOM   3791 H HD13 . ILE A 1 252 ? -3.038  -8.365  -3.745  1.00 18.64 ? 271 ILE A HD13 1 
ATOM   3792 N N    . LEU A 1 253 ? 2.530   -6.780  -4.336  1.00 14.75 ? 272 LEU A N    1 
ATOM   3793 C CA   . LEU A 1 253 ? 3.832   -7.273  -4.772  1.00 14.14 ? 272 LEU A CA   1 
ATOM   3794 C C    . LEU A 1 253 ? 4.949   -6.701  -3.908  1.00 13.34 ? 272 LEU A C    1 
ATOM   3795 O O    . LEU A 1 253 ? 5.941   -7.392  -3.641  1.00 13.65 ? 272 LEU A O    1 
ATOM   3796 C CB   . LEU A 1 253 ? 4.067   -6.933  -6.247  1.00 15.11 ? 272 LEU A CB   1 
ATOM   3797 C CG   . LEU A 1 253 ? 3.220   -7.741  -7.216  1.00 16.21 ? 272 LEU A CG   1 
ATOM   3798 C CD1  . LEU A 1 253 ? 3.452   -7.278  -8.655  1.00 16.83 ? 272 LEU A CD1  1 
ATOM   3799 C CD2  . LEU A 1 253 ? 3.490   -9.234  -7.142  1.00 16.72 ? 272 LEU A CD2  1 
ATOM   3800 H H    . LEU A 1 253 ? 2.123   -6.284  -4.908  1.00 17.71 ? 272 LEU A H    1 
ATOM   3801 H HA   . LEU A 1 253 ? 3.847   -8.239  -4.692  1.00 16.97 ? 272 LEU A HA   1 
ATOM   3802 H HB2  . LEU A 1 253 ? 3.859   -5.995  -6.385  1.00 18.14 ? 272 LEU A HB2  1 
ATOM   3803 H HB3  . LEU A 1 253 ? 4.998   -7.101  -6.458  1.00 18.14 ? 272 LEU A HB3  1 
ATOM   3804 H HG   . LEU A 1 253 ? 2.296   -7.593  -6.960  1.00 19.46 ? 272 LEU A HG   1 
ATOM   3805 H HD11 . LEU A 1 253 ? 2.894   -7.804  -9.250  1.00 20.20 ? 272 LEU A HD11 1 
ATOM   3806 H HD12 . LEU A 1 253 ? 3.218   -6.339  -8.727  1.00 20.20 ? 272 LEU A HD12 1 
ATOM   3807 H HD13 . LEU A 1 253 ? 4.387   -7.404  -8.881  1.00 20.20 ? 272 LEU A HD13 1 
ATOM   3808 H HD21 . LEU A 1 253 ? 3.003   -9.679  -7.853  1.00 20.06 ? 272 LEU A HD21 1 
ATOM   3809 H HD22 . LEU A 1 253 ? 4.442   -9.389  -7.246  1.00 20.06 ? 272 LEU A HD22 1 
ATOM   3810 H HD23 . LEU A 1 253 ? 3.193   -9.566  -6.280  1.00 20.06 ? 272 LEU A HD23 1 
ATOM   3811 N N    . GLU A 1 254 ? 4.812   -5.455  -3.454  1.00 12.82 ? 273 GLU A N    1 
ATOM   3812 C CA   . GLU A 1 254 ? 5.849   -4.885  -2.597  1.00 13.25 ? 273 GLU A CA   1 
ATOM   3813 C C    . GLU A 1 254 ? 5.830   -5.513  -1.208  1.00 12.79 ? 273 GLU A C    1 
ATOM   3814 O O    . GLU A 1 254 ? 6.892   -5.730  -0.613  1.00 12.93 ? 273 GLU A O    1 
ATOM   3815 C CB   . GLU A 1 254 ? 5.746   -3.358  -2.552  1.00 14.20 ? 273 GLU A CB   1 
ATOM   3816 C CG   . GLU A 1 254 ? 6.803   -2.701  -1.687  1.00 14.97 ? 273 GLU A CG   1 
ATOM   3817 C CD   . GLU A 1 254 ? 8.245   -2.925  -2.153  1.00 16.54 ? 273 GLU A CD   1 
ATOM   3818 O OE1  . GLU A 1 254 ? 8.483   -3.469  -3.260  1.00 16.10 ? 273 GLU A OE1  1 
ATOM   3819 O OE2  . GLU A 1 254 ? 9.149   -2.515  -1.395  1.00 17.86 ? 273 GLU A OE2  1 
ATOM   3820 H H    . GLU A 1 254 ? 4.149   -4.935  -3.623  1.00 15.40 ? 273 GLU A H    1 
ATOM   3821 H HA   . GLU A 1 254 ? 6.717   -5.081  -2.983  1.00 15.90 ? 273 GLU A HA   1 
ATOM   3822 H HB2  . GLU A 1 254 ? 5.843   -3.012  -3.453  1.00 17.05 ? 273 GLU A HB2  1 
ATOM   3823 H HB3  . GLU A 1 254 ? 4.877   -3.115  -2.195  1.00 17.05 ? 273 GLU A HB3  1 
ATOM   3824 H HG2  . GLU A 1 254 ? 6.644   -1.744  -1.680  1.00 17.97 ? 273 GLU A HG2  1 
ATOM   3825 H HG3  . GLU A 1 254 ? 6.729   -3.056  -0.787  1.00 17.97 ? 273 GLU A HG3  1 
ATOM   3826 N N    . MET A 1 255 ? 4.643   -5.808  -0.669  1.00 12.26 ? 274 MET A N    1 
ATOM   3827 C CA   . MET A 1 255 ? 4.584   -6.623  0.543   1.00 12.34 ? 274 MET A CA   1 
ATOM   3828 C C    . MET A 1 255 ? 5.342   -7.922  0.364   1.00 11.94 ? 274 MET A C    1 
ATOM   3829 O O    . MET A 1 255 ? 6.168   -8.295  1.202   1.00 12.53 ? 274 MET A O    1 
ATOM   3830 C CB   . MET A 1 255 ? 3.148   -6.899  0.988   1.00 12.54 ? 274 MET A CB   1 
ATOM   3831 C CG   . MET A 1 255 ? 3.108   -7.688  2.282   1.00 12.76 ? 274 MET A CG   1 
ATOM   3832 S SD   . MET A 1 255 ? 1.439   -8.023  2.880   1.00 13.91 ? 274 MET A SD   1 
ATOM   3833 C CE   . MET A 1 255 ? 0.612   -8.719  1.459   1.00 14.05 ? 274 MET A CE   1 
ATOM   3834 H H    . MET A 1 255 ? 3.881   -5.556  -0.978  1.00 14.72 ? 274 MET A H    1 
ATOM   3835 H HA   . MET A 1 255 ? 4.993   -6.101  1.251   1.00 14.82 ? 274 MET A HA   1 
ATOM   3836 H HB2  . MET A 1 255 ? 2.689   -6.057  1.130   1.00 15.06 ? 274 MET A HB2  1 
ATOM   3837 H HB3  . MET A 1 255 ? 2.694   -7.413  0.303   1.00 15.06 ? 274 MET A HB3  1 
ATOM   3838 H HG2  . MET A 1 255 ? 3.548   -8.542  2.140   1.00 15.32 ? 274 MET A HG2  1 
ATOM   3839 H HG3  . MET A 1 255 ? 3.573   -7.186  2.969   1.00 15.32 ? 274 MET A HG3  1 
ATOM   3840 H HE1  . MET A 1 255 ? -0.291  -8.968  1.710   1.00 16.87 ? 274 MET A HE1  1 
ATOM   3841 H HE2  . MET A 1 255 ? 0.588   -8.055  0.752   1.00 16.87 ? 274 MET A HE2  1 
ATOM   3842 H HE3  . MET A 1 255 ? 1.101   -9.502  1.162   1.00 16.87 ? 274 MET A HE3  1 
ATOM   3843 N N    . GLN A 1 256 ? 5.021   -8.652  -0.700  1.00 12.42 ? 275 GLN A N    1 
ATOM   3844 C CA   . GLN A 1 256 ? 5.671   -9.933  -0.950  1.00 13.35 ? 275 GLN A CA   1 
ATOM   3845 C C    . GLN A 1 256 ? 7.180   -9.765  -1.019  1.00 13.49 ? 275 GLN A C    1 
ATOM   3846 O O    . GLN A 1 256 ? 7.932   -10.531 -0.395  1.00 14.48 ? 275 GLN A O    1 
ATOM   3847 C CB   . GLN A 1 256 ? 5.121   -10.540 -2.242  1.00 14.85 ? 275 GLN A CB   1 
ATOM   3848 C CG   . GLN A 1 256 ? 5.818   -11.842 -2.625  1.00 14.80 ? 275 GLN A CG   1 
ATOM   3849 C CD   . GLN A 1 256 ? 5.246   -12.474 -3.866  1.00 16.69 ? 275 GLN A CD   1 
ATOM   3850 O OE1  . GLN A 1 256 ? 4.832   -13.628 -3.832  1.00 17.24 ? 275 GLN A OE1  1 
ATOM   3851 N NE2  . GLN A 1 256 ? 5.250   -11.746 -4.958  1.00 16.54 ? 275 GLN A NE2  1 
ATOM   3852 H H    . GLN A 1 256 ? 4.435   -8.430  -1.289  1.00 14.91 ? 275 GLN A H    1 
ATOM   3853 H HA   . GLN A 1 256 ? 5.475   -10.545 -0.224  1.00 16.03 ? 275 GLN A HA   1 
ATOM   3854 H HB2  . GLN A 1 256 ? 4.177   -10.727 -2.125  1.00 17.83 ? 275 GLN A HB2  1 
ATOM   3855 H HB3  . GLN A 1 256 ? 5.246   -9.907  -2.966  1.00 17.83 ? 275 GLN A HB3  1 
ATOM   3856 H HG2  . GLN A 1 256 ? 6.757   -11.660 -2.788  1.00 17.76 ? 275 GLN A HG2  1 
ATOM   3857 H HG3  . GLN A 1 256 ? 5.725   -12.475 -1.897  1.00 17.76 ? 275 GLN A HG3  1 
ATOM   3858 H HE21 . GLN A 1 256 ? 5.569   -10.947 -4.942  1.00 19.86 ? 275 GLN A HE21 1 
ATOM   3859 H HE22 . GLN A 1 256 ? 4.933   -12.067 -5.690  1.00 19.86 ? 275 GLN A HE22 1 
ATOM   3860 N N    . ARG A 1 257 ? 7.643   -8.776  -1.788  1.00 13.01 ? 276 ARG A N    1 
ATOM   3861 C CA   . ARG A 1 257 ? 9.081   -8.595  -1.991  1.00 13.42 ? 276 ARG A CA   1 
ATOM   3862 C C    . ARG A 1 257 ? 9.787   -8.192  -0.702  1.00 13.50 ? 276 ARG A C    1 
ATOM   3863 O O    . ARG A 1 257 ? 10.800  -8.783  -0.324  1.00 13.77 ? 276 ARG A O    1 
ATOM   3864 C CB   . ARG A 1 257 ? 9.306   -7.530  -3.061  1.00 14.98 ? 276 ARG A CB   1 
ATOM   3865 C CG   . ARG A 1 257 ? 10.767  -7.411  -3.482  1.00 15.08 ? 276 ARG A CG   1 
ATOM   3866 C CD   . ARG A 1 257 ? 11.115  -6.064  -4.100  1.00 16.13 ? 276 ARG A CD   1 
ATOM   3867 N NE   . ARG A 1 257 ? 11.007  -4.992  -3.125  1.00 17.44 ? 276 ARG A NE   1 
ATOM   3868 C CZ   . ARG A 1 257 ? 11.874  -4.759  -2.149  1.00 18.00 ? 276 ARG A CZ   1 
ATOM   3869 N NH1  . ARG A 1 257 ? 12.990  -5.457  -2.025  1.00 19.17 ? 276 ARG A NH1  1 
ATOM   3870 N NH2  . ARG A 1 257 ? 11.605  -3.809  -1.260  1.00 18.87 ? 276 ARG A NH2  1 
ATOM   3871 H H    . ARG A 1 257 ? 7.151   -8.202  -2.198  1.00 15.62 ? 276 ARG A H    1 
ATOM   3872 H HA   . ARG A 1 257 ? 9.461   -9.436  -2.289  1.00 16.11 ? 276 ARG A HA   1 
ATOM   3873 H HB2  . ARG A 1 257 ? 8.785   -7.758  -3.847  1.00 17.98 ? 276 ARG A HB2  1 
ATOM   3874 H HB3  . ARG A 1 257 ? 9.023   -6.670  -2.713  1.00 17.98 ? 276 ARG A HB3  1 
ATOM   3875 H HG2  . ARG A 1 257 ? 11.329  -7.533  -2.701  1.00 18.10 ? 276 ARG A HG2  1 
ATOM   3876 H HG3  . ARG A 1 257 ? 10.961  -8.098  -4.140  1.00 18.10 ? 276 ARG A HG3  1 
ATOM   3877 H HD2  . ARG A 1 257 ? 12.026  -6.086  -4.430  1.00 19.37 ? 276 ARG A HD2  1 
ATOM   3878 H HD3  . ARG A 1 257 ? 10.502  -5.877  -4.829  1.00 19.37 ? 276 ARG A HD3  1 
ATOM   3879 H HE   . ARG A 1 257 ? 10.328  -4.467  -3.186  1.00 20.93 ? 276 ARG A HE   1 
ATOM   3880 H HH11 . ARG A 1 257 ? 13.170  -6.083  -2.586  1.00 23.01 ? 276 ARG A HH11 1 
ATOM   3881 H HH12 . ARG A 1 257 ? 13.535  -5.285  -1.382  1.00 23.01 ? 276 ARG A HH12 1 
ATOM   3882 H HH21 . ARG A 1 257 ? 10.877  -3.356  -1.323  1.00 22.65 ? 276 ARG A HH21 1 
ATOM   3883 H HH22 . ARG A 1 257 ? 12.159  -3.648  -0.623  1.00 22.65 ? 276 ARG A HH22 1 
ATOM   3884 N N    . ALA A 1 258 ? 9.266   -7.187  -0.007  1.00 12.90 ? 277 ALA A N    1 
ATOM   3885 C CA   . ALA A 1 258 ? 9.965   -6.701  1.175   1.00 13.13 ? 277 ALA A CA   1 
ATOM   3886 C C    . ALA A 1 258 ? 9.965   -7.733  2.290   1.00 12.14 ? 277 ALA A C    1 
ATOM   3887 O O    . ALA A 1 258 ? 10.966  -7.892  2.995   1.00 12.88 ? 277 ALA A O    1 
ATOM   3888 C CB   . ALA A 1 258 ? 9.337   -5.412  1.671   1.00 13.58 ? 277 ALA A CB   1 
ATOM   3889 H H    . ALA A 1 258 ? 8.531   -6.781  -0.193  1.00 15.49 ? 277 ALA A H    1 
ATOM   3890 H HA   . ALA A 1 258 ? 10.885  -6.520  0.923   1.00 15.76 ? 277 ALA A HA   1 
ATOM   3891 H HB1  . ALA A 1 258 ? 9.776   -5.143  2.493   1.00 16.31 ? 277 ALA A HB1  1 
ATOM   3892 H HB2  . ALA A 1 258 ? 9.449   -4.726  0.995   1.00 16.31 ? 277 ALA A HB2  1 
ATOM   3893 H HB3  . ALA A 1 258 ? 8.393   -5.564  1.835   1.00 16.31 ? 277 ALA A HB3  1 
ATOM   3894 N N    . ALA A 1 259 ? 8.864   -8.460  2.463   1.00 11.86 ? 278 ALA A N    1 
ATOM   3895 C CA   . ALA A 1 259 ? 8.840   -9.481  3.500   1.00 12.76 ? 278 ALA A CA   1 
ATOM   3896 C C    . ALA A 1 259 ? 9.705   -10.676 3.121   1.00 14.07 ? 278 ALA A C    1 
ATOM   3897 O O    . ALA A 1 259 ? 10.346  -11.279 3.991   1.00 15.53 ? 278 ALA A O    1 
ATOM   3898 C CB   . ALA A 1 259 ? 7.402   -9.893  3.783   1.00 12.85 ? 278 ALA A CB   1 
ATOM   3899 H H    . ALA A 1 259 ? 8.139   -8.383  2.006   1.00 14.24 ? 278 ALA A H    1 
ATOM   3900 H HA   . ALA A 1 259 ? 9.205   -9.115  4.320   1.00 15.32 ? 278 ALA A HA   1 
ATOM   3901 H HB1  . ALA A 1 259 ? 7.402   -10.611 4.436   1.00 15.43 ? 278 ALA A HB1  1 
ATOM   3902 H HB2  . ALA A 1 259 ? 6.918   -9.128  4.132   1.00 15.43 ? 278 ALA A HB2  1 
ATOM   3903 H HB3  . ALA A 1 259 ? 6.992   -10.196 2.958   1.00 15.43 ? 278 ALA A HB3  1 
ATOM   3904 N N    . LYS A 1 260 ? 9.766   -11.024 1.833   1.00 14.48 ? 279 LYS A N    1 
ATOM   3905 C CA   . LYS A 1 260 ? 10.688  -12.089 1.457   1.00 15.98 ? 279 LYS A CA   1 
ATOM   3906 C C    . LYS A 1 260 ? 12.138  -11.681 1.720   1.00 16.68 ? 279 LYS A C    1 
ATOM   3907 O O    . LYS A 1 260 ? 12.994  -12.542 1.971   1.00 18.32 ? 279 LYS A O    1 
ATOM   3908 C CB   . LYS A 1 260 ? 10.506  -12.460 -0.010  1.00 18.16 ? 279 LYS A CB   1 
ATOM   3909 C CG   . LYS A 1 260 ? 9.501   -13.551 -0.230  1.00 20.54 ? 279 LYS A CG   1 
ATOM   3910 C CD   . LYS A 1 260 ? 9.199   -13.745 -1.723  1.00 23.01 ? 279 LYS A CD   1 
ATOM   3911 C CE   . LYS A 1 260 ? 8.161   -14.820 -1.946  1.00 25.76 ? 279 LYS A CE   1 
ATOM   3912 N NZ   . LYS A 1 260 ? 8.567   -15.719 -3.055  1.00 28.32 ? 279 LYS A NZ   1 
ATOM   3913 H H    . LYS A 1 260 ? 9.308   -10.676 1.194   1.00 17.38 ? 279 LYS A H    1 
ATOM   3914 H HA   . LYS A 1 260 ? 10.487  -12.876 1.988   1.00 19.18 ? 279 LYS A HA   1 
ATOM   3915 H HB2  . LYS A 1 260 ? 10.205  -11.676 -0.496  1.00 21.80 ? 279 LYS A HB2  1 
ATOM   3916 H HB3  . LYS A 1 260 ? 11.357  -12.763 -0.364  1.00 21.80 ? 279 LYS A HB3  1 
ATOM   3917 H HG2  . LYS A 1 260 ? 9.850   -14.385 0.122   1.00 24.66 ? 279 LYS A HG2  1 
ATOM   3918 H HG3  . LYS A 1 260 ? 8.674   -13.321 0.221   1.00 24.66 ? 279 LYS A HG3  1 
ATOM   3919 H HD2  . LYS A 1 260 ? 8.862   -12.914 -2.093  1.00 27.62 ? 279 LYS A HD2  1 
ATOM   3920 H HD3  . LYS A 1 260 ? 10.012  -14.006 -2.184  1.00 27.62 ? 279 LYS A HD3  1 
ATOM   3921 H HE2  . LYS A 1 260 ? 8.065   -15.350 -1.139  1.00 30.92 ? 279 LYS A HE2  1 
ATOM   3922 H HE3  . LYS A 1 260 ? 7.313   -14.409 -2.176  1.00 30.92 ? 279 LYS A HE3  1 
ATOM   3923 H HZ1  . LYS A 1 260 ? 7.949   -16.348 -3.179  1.00 33.99 ? 279 LYS A HZ1  1 
ATOM   3924 H HZ2  . LYS A 1 260 ? 8.658   -15.252 -3.807  1.00 33.99 ? 279 LYS A HZ2  1 
ATOM   3925 H HZ3  . LYS A 1 260 ? 9.342   -16.110 -2.862  1.00 33.99 ? 279 LYS A HZ3  1 
ATOM   3926 N N    . ALA A 1 261 ? 12.425  -10.381 1.690   1.00 15.86 ? 280 ALA A N    1 
ATOM   3927 C CA   . ALA A 1 261 ? 13.760  -9.867  1.982   1.00 16.93 ? 280 ALA A CA   1 
ATOM   3928 C C    . ALA A 1 261 ? 14.009  -9.711  3.474   1.00 16.96 ? 280 ALA A C    1 
ATOM   3929 O O    . ALA A 1 261 ? 15.074  -9.214  3.861   1.00 19.59 ? 280 ALA A O    1 
ATOM   3930 C CB   . ALA A 1 261 ? 13.984  -8.526  1.288   1.00 18.29 ? 280 ALA A CB   1 
ATOM   3931 H H    . ALA A 1 261 ? 11.853  -9.767  1.499   1.00 19.04 ? 280 ALA A H    1 
ATOM   3932 H HA   . ALA A 1 261 ? 14.412  -10.491 1.627   1.00 20.32 ? 280 ALA A HA   1 
ATOM   3933 H HB1  . ALA A 1 261 ? 14.868  -8.197  1.516   1.00 21.96 ? 280 ALA A HB1  1 
ATOM   3934 H HB2  . ALA A 1 261 ? 13.915  -8.652  0.329   1.00 21.96 ? 280 ALA A HB2  1 
ATOM   3935 H HB3  . ALA A 1 261 ? 13.310  -7.898  1.589   1.00 21.96 ? 280 ALA A HB3  1 
ATOM   3936 N N    . GLY A 1 262 ? 13.049  -10.092 4.313   1.00 14.87 ? 281 GLY A N    1 
ATOM   3937 C CA   . GLY A 1 262 ? 13.250  -10.141 5.742   1.00 13.99 ? 281 GLY A CA   1 
ATOM   3938 C C    . GLY A 1 262 ? 12.607  -9.026  6.533   1.00 13.04 ? 281 GLY A C    1 
ATOM   3939 O O    . GLY A 1 262 ? 12.841  -8.943  7.744   1.00 14.85 ? 281 GLY A O    1 
ATOM   3940 H H    . GLY A 1 262 ? 12.260  -10.330 4.067   1.00 17.85 ? 281 GLY A H    1 
ATOM   3941 H HA2  . GLY A 1 262 ? 12.892  -10.980 6.074   1.00 16.79 ? 281 GLY A HA2  1 
ATOM   3942 H HA3  . GLY A 1 262 ? 14.204  -10.113 5.920   1.00 16.79 ? 281 GLY A HA3  1 
ATOM   3943 N N    . LYS A 1 263 ? 11.849  -8.146  5.894   1.00 12.44 ? 282 LYS A N    1 
ATOM   3944 C CA   . LYS A 1 263 ? 11.228  -7.024  6.594   1.00 11.70 ? 282 LYS A CA   1 
ATOM   3945 C C    . LYS A 1 263 ? 9.831   -7.366  7.109   1.00 11.62 ? 282 LYS A C    1 
ATOM   3946 O O    . LYS A 1 263 ? 9.190   -8.319  6.666   1.00 12.10 ? 282 LYS A O    1 
ATOM   3947 C CB   . LYS A 1 263 ? 11.131  -5.818  5.660   1.00 12.31 ? 282 LYS A CB   1 
ATOM   3948 C CG   . LYS A 1 263 ? 12.476  -5.292  5.194   1.00 14.83 ? 282 LYS A CG   1 
ATOM   3949 C CD   . LYS A 1 263 ? 13.396  -5.025  6.393   1.00 14.63 ? 282 LYS A CD   1 
ATOM   3950 C CE   . LYS A 1 263 ? 14.632  -4.252  6.000   1.00 14.88 ? 282 LYS A CE   1 
ATOM   3951 N NZ   . LYS A 1 263 ? 15.554  -4.175  7.154   1.00 15.93 ? 282 LYS A NZ   1 
ATOM   3952 H H    . LYS A 1 263 ? 11.676  -8.174  5.052   1.00 14.93 ? 282 LYS A H    1 
ATOM   3953 H HA   . LYS A 1 263 ? 11.778  -6.804  7.362   1.00 14.05 ? 282 LYS A HA   1 
ATOM   3954 H HB2  . LYS A 1 263 ? 10.625  -6.074  4.873   1.00 14.78 ? 282 LYS A HB2  1 
ATOM   3955 H HB3  . LYS A 1 263 ? 10.677  -5.099  6.126   1.00 14.78 ? 282 LYS A HB3  1 
ATOM   3956 H HG2  . LYS A 1 263 ? 12.900  -5.948  4.619   1.00 17.80 ? 282 LYS A HG2  1 
ATOM   3957 H HG3  . LYS A 1 263 ? 12.349  -4.460  4.711   1.00 17.80 ? 282 LYS A HG3  1 
ATOM   3958 H HD2  . LYS A 1 263 ? 12.913  -4.507  7.056   1.00 17.56 ? 282 LYS A HD2  1 
ATOM   3959 H HD3  . LYS A 1 263 ? 13.677  -5.872  6.774   1.00 17.56 ? 282 LYS A HD3  1 
ATOM   3960 H HE2  . LYS A 1 263 ? 15.083  -4.703  5.268   1.00 17.87 ? 282 LYS A HE2  1 
ATOM   3961 H HE3  . LYS A 1 263 ? 14.386  -3.352  5.734   1.00 17.87 ? 282 LYS A HE3  1 
ATOM   3962 H HZ1  . LYS A 1 263 ? 15.897  -4.979  7.324   1.00 19.12 ? 282 LYS A HZ1  1 
ATOM   3963 H HZ2  . LYS A 1 263 ? 16.218  -3.609  6.976   1.00 19.12 ? 282 LYS A HZ2  1 
ATOM   3964 H HZ3  . LYS A 1 263 ? 15.117  -3.890  7.875   1.00 19.12 ? 282 LYS A HZ3  1 
ATOM   3965 N N    . ILE A 1 264 ? 9.360   -6.536  8.039   1.00 11.03 ? 283 ILE A N    1 
ATOM   3966 C CA   . ILE A 1 264 ? 7.973   -6.538  8.486   1.00 10.52 ? 283 ILE A CA   1 
ATOM   3967 C C    . ILE A 1 264 ? 7.164   -5.627  7.574   1.00 10.26 ? 283 ILE A C    1 
ATOM   3968 O O    . ILE A 1 264 ? 7.606   -4.524  7.236   1.00 11.22 ? 283 ILE A O    1 
ATOM   3969 C CB   . ILE A 1 264 ? 7.899   -6.011  9.930   1.00 10.64 ? 283 ILE A CB   1 
ATOM   3970 C CG1  . ILE A 1 264 ? 8.600   -6.951  10.910  1.00 11.00 ? 283 ILE A CG1  1 
ATOM   3971 C CG2  . ILE A 1 264 ? 6.455   -5.808  10.383  1.00 11.24 ? 283 ILE A CG2  1 
ATOM   3972 C CD1  . ILE A 1 264 ? 8.953   -6.272  12.218  1.00 11.92 ? 283 ILE A CD1  1 
ATOM   3973 H H    . ILE A 1 264 ? 9.841   -5.944  8.436   1.00 13.24 ? 283 ILE A H    1 
ATOM   3974 H HA   . ILE A 1 264 ? 7.618   -7.439  8.438   1.00 12.64 ? 283 ILE A HA   1 
ATOM   3975 H HB   . ILE A 1 264 ? 8.355   -5.156  9.928   1.00 12.77 ? 283 ILE A HB   1 
ATOM   3976 H HG12 . ILE A 1 264 ? 8.014   -7.698  11.107  1.00 13.20 ? 283 ILE A HG12 1 
ATOM   3977 H HG13 . ILE A 1 264 ? 9.422   -7.272  10.506  1.00 13.20 ? 283 ILE A HG13 1 
ATOM   3978 H HG21 . ILE A 1 264 ? 6.443   -5.648  11.339  1.00 13.50 ? 283 ILE A HG21 1 
ATOM   3979 H HG22 . ILE A 1 264 ? 6.082   -5.043  9.916   1.00 13.50 ? 283 ILE A HG22 1 
ATOM   3980 H HG23 . ILE A 1 264 ? 5.943   -6.605  10.174  1.00 13.50 ? 283 ILE A HG23 1 
ATOM   3981 H HD11 . ILE A 1 264 ? 9.534   -6.856  12.730  1.00 14.31 ? 283 ILE A HD11 1 
ATOM   3982 H HD12 . ILE A 1 264 ? 9.409   -5.437  12.027  1.00 14.31 ? 283 ILE A HD12 1 
ATOM   3983 H HD13 . ILE A 1 264 ? 8.138   -6.098  12.713  1.00 14.31 ? 283 ILE A HD13 1 
ATOM   3984 N N    . VAL A 1 265 ? 5.960   -6.064  7.202   1.00 10.26 ? 284 VAL A N    1 
ATOM   3985 C CA   . VAL A 1 265 ? 5.038   -5.244  6.418   1.00 10.74 ? 284 VAL A CA   1 
ATOM   3986 C C    . VAL A 1 265 ? 3.696   -5.256  7.113   1.00 11.40 ? 284 VAL A C    1 
ATOM   3987 O O    . VAL A 1 265 ? 3.225   -6.320  7.521   1.00 10.70 ? 284 VAL A O    1 
ATOM   3988 C CB   . VAL A 1 265 ? 4.915   -5.717  4.958   1.00 11.70 ? 284 VAL A CB   1 
ATOM   3989 C CG1  . VAL A 1 265 ? 3.946   -4.833  4.198   1.00 12.12 ? 284 VAL A CG1  1 
ATOM   3990 C CG2  . VAL A 1 265 ? 6.293   -5.742  4.279   1.00 12.94 ? 284 VAL A CG2  1 
ATOM   3991 H H    . VAL A 1 265 ? 5.652   -6.844  7.395   1.00 12.32 ? 284 VAL A H    1 
ATOM   3992 H HA   . VAL A 1 265 ? 5.364   -4.331  6.396   1.00 12.90 ? 284 VAL A HA   1 
ATOM   3993 H HB   . VAL A 1 265 ? 4.566   -6.622  4.946   1.00 14.04 ? 284 VAL A HB   1 
ATOM   3994 H HG11 . VAL A 1 265 ? 4.164   -4.865  3.253   1.00 14.56 ? 284 VAL A HG11 1 
ATOM   3995 H HG12 . VAL A 1 265 ? 3.043   -5.158  4.340   1.00 14.56 ? 284 VAL A HG12 1 
ATOM   3996 H HG13 . VAL A 1 265 ? 4.025   -3.923  4.524   1.00 14.56 ? 284 VAL A HG13 1 
ATOM   3997 H HG21 . VAL A 1 265 ? 6.172   -5.875  3.326   1.00 15.54 ? 284 VAL A HG21 1 
ATOM   3998 H HG22 . VAL A 1 265 ? 6.740   -4.897  4.441   1.00 15.54 ? 284 VAL A HG22 1 
ATOM   3999 H HG23 . VAL A 1 265 ? 6.815   -6.470  4.651   1.00 15.54 ? 284 VAL A HG23 1 
ATOM   4000 N N    . VAL A 1 266 ? 3.106   -4.079  7.296   1.00 14.89 ? 285 VAL A N    1 
ATOM   4001 C CA   . VAL A 1 266 ? 1.817   -3.942  7.963   1.00 14.89 ? 285 VAL A CA   1 
ATOM   4002 C C    . VAL A 1 266 ? 0.875   -3.402  6.900   1.00 14.89 ? 285 VAL A C    1 
ATOM   4003 O O    . VAL A 1 266 ? 1.022   -2.258  6.449   1.00 14.89 ? 285 VAL A O    1 
ATOM   4004 C CB   . VAL A 1 266 ? 1.906   -2.989  9.156   1.00 14.89 ? 285 VAL A CB   1 
ATOM   4005 C CG1  . VAL A 1 266 ? 0.517   -2.736  9.762   1.00 14.89 ? 285 VAL A CG1  1 
ATOM   4006 C CG2  . VAL A 1 266 ? 2.867   -3.546  10.204  1.00 14.89 ? 285 VAL A CG2  1 
ATOM   4007 N N    . LEU A 1 267 ? -0.119  -4.204  6.518   1.00 11.42 ? 286 LEU A N    1 
ATOM   4008 C CA   . LEU A 1 267 ? -1.086  -3.801  5.505   1.00 11.56 ? 286 LEU A CA   1 
ATOM   4009 C C    . LEU A 1 267 ? -2.343  -3.298  6.209   1.00 11.36 ? 286 LEU A C    1 
ATOM   4010 O O    . LEU A 1 267 ? -2.994  -4.042  6.948   1.00 11.22 ? 286 LEU A O    1 
ATOM   4011 C CB   . LEU A 1 267 ? -1.414  -4.972  4.569   1.00 12.22 ? 286 LEU A CB   1 
ATOM   4012 C CG   . LEU A 1 267 ? -2.215  -4.611  3.321   1.00 12.51 ? 286 LEU A CG   1 
ATOM   4013 C CD1  . LEU A 1 267 ? -1.911  -5.526  2.172   1.00 13.56 ? 286 LEU A CD1  1 
ATOM   4014 C CD2  . LEU A 1 267 ? -3.698  -4.650  3.633   1.00 13.01 ? 286 LEU A CD2  1 
ATOM   4015 H H    . LEU A 1 267 ? -0.252  -4.992  6.836   1.00 13.72 ? 286 LEU A H    1 
ATOM   4016 H HA   . LEU A 1 267 ? -0.722  -3.080  4.968   1.00 13.88 ? 286 LEU A HA   1 
ATOM   4017 H HB2  . LEU A 1 267 ? -0.580  -5.368  4.272   1.00 14.67 ? 286 LEU A HB2  1 
ATOM   4018 H HB3  . LEU A 1 267 ? -1.933  -5.623  5.067   1.00 14.67 ? 286 LEU A HB3  1 
ATOM   4019 H HG   . LEU A 1 267 ? -1.964  -3.715  3.048   1.00 15.02 ? 286 LEU A HG   1 
ATOM   4020 H HD11 . LEU A 1 267 ? -2.434  -5.252  1.403   1.00 16.28 ? 286 LEU A HD11 1 
ATOM   4021 H HD12 . LEU A 1 267 ? -0.965  -5.470  1.966   1.00 16.28 ? 286 LEU A HD12 1 
ATOM   4022 H HD13 . LEU A 1 267 ? -2.142  -6.435  2.422   1.00 16.28 ? 286 LEU A HD13 1 
ATOM   4023 H HD21 . LEU A 1 267 ? -4.178  -4.956  2.847   1.00 15.62 ? 286 LEU A HD21 1 
ATOM   4024 H HD22 . LEU A 1 267 ? -3.850  -5.260  4.371   1.00 15.62 ? 286 LEU A HD22 1 
ATOM   4025 H HD23 . LEU A 1 267 ? -3.993  -3.758  3.875   1.00 15.62 ? 286 LEU A HD23 1 
ATOM   4026 N N    . LYS A 1 268 ? -2.659  -2.026  6.002   1.00 14.89 ? 287 LYS A N    1 
ATOM   4027 C CA   . LYS A 1 268 ? -3.807  -1.405  6.656   1.00 14.89 ? 287 LYS A CA   1 
ATOM   4028 C C    . LYS A 1 268 ? -5.010  -1.546  5.734   1.00 16.96 ? 287 LYS A C    1 
ATOM   4029 O O    . LYS A 1 268 ? -5.152  -0.819  4.748   1.00 16.82 ? 287 LYS A O    1 
ATOM   4030 C CB   . LYS A 1 268 ? -3.497  0.058   6.933   1.00 14.89 ? 287 LYS A CB   1 
ATOM   4031 C CG   . LYS A 1 268 ? -4.710  0.857   7.375   1.00 20.04 ? 287 LYS A CG   1 
ATOM   4032 C CD   . LYS A 1 268 ? -5.293  0.356   8.710   1.00 16.38 ? 287 LYS A CD   1 
ATOM   4033 C CE   . LYS A 1 268 ? -6.377  1.299   9.164   1.00 19.18 ? 287 LYS A CE   1 
ATOM   4034 N NZ   . LYS A 1 268 ? -7.680  1.026   8.453   1.00 14.89 ? 287 LYS A NZ   1 
ATOM   4035 N N    . GLY A 1 269 ? -5.870  -2.504  6.049   1.00 13.74 ? 288 GLY A N    1 
ATOM   4036 C CA   . GLY A 1 269 ? -7.117  -2.629  5.347   1.00 12.90 ? 288 GLY A CA   1 
ATOM   4037 C C    . GLY A 1 269 ? -8.185  -1.691  5.883   1.00 12.28 ? 288 GLY A C    1 
ATOM   4038 O O    . GLY A 1 269 ? -8.185  -1.304  7.053   1.00 12.53 ? 288 GLY A O    1 
ATOM   4039 H H    . GLY A 1 269 ? -5.748  -3.091  6.666   1.00 16.49 ? 288 GLY A H    1 
ATOM   4040 H HA2  . GLY A 1 269 ? -6.977  -2.427  4.408   1.00 15.48 ? 288 GLY A HA2  1 
ATOM   4041 H HA3  . GLY A 1 269 ? -7.441  -3.539  5.430   1.00 15.48 ? 288 GLY A HA3  1 
ATOM   4042 N N    . TRP A 1 270 ? -9.106  -1.327  4.991   1.00 11.36 ? 289 TRP A N    1 
ATOM   4043 C CA   . TRP A 1 270 ? -10.200 -0.411  5.288   1.00 11.64 ? 289 TRP A CA   1 
ATOM   4044 C C    . TRP A 1 270 ? -11.518 -1.161  5.141   1.00 11.40 ? 289 TRP A C    1 
ATOM   4045 O O    . TRP A 1 270 ? -11.707 -1.907  4.178   1.00 12.90 ? 289 TRP A O    1 
ATOM   4046 C CB   . TRP A 1 270 ? -10.130 0.819   4.349   1.00 12.44 ? 289 TRP A CB   1 
ATOM   4047 C CG   . TRP A 1 270 ? -8.911  1.604   4.653   1.00 11.37 ? 289 TRP A CG   1 
ATOM   4048 C CD1  . TRP A 1 270 ? -7.691  1.465   4.061   1.00 10.56 ? 289 TRP A CD1  1 
ATOM   4049 C CD2  . TRP A 1 270 ? -8.753  2.578   5.676   1.00 10.99 ? 289 TRP A CD2  1 
ATOM   4050 N NE1  . TRP A 1 270 ? -6.771  2.294   4.660   1.00 11.13 ? 289 TRP A NE1  1 
ATOM   4051 C CE2  . TRP A 1 270 ? -7.398  2.995   5.659   1.00 11.45 ? 289 TRP A CE2  1 
ATOM   4052 C CE3  . TRP A 1 270 ? -9.617  3.139   6.619   1.00 11.88 ? 289 TRP A CE3  1 
ATOM   4053 C CZ2  . TRP A 1 270 ? -6.904  3.961   6.537   1.00 11.90 ? 289 TRP A CZ2  1 
ATOM   4054 C CZ3  . TRP A 1 270 ? -9.118  4.078   7.486   1.00 12.27 ? 289 TRP A CZ3  1 
ATOM   4055 C CH2  . TRP A 1 270 ? -7.785  4.486   7.439   1.00 12.30 ? 289 TRP A CH2  1 
ATOM   4056 H H    . TRP A 1 270 ? -9.117  -1.610  4.179   1.00 13.64 ? 289 TRP A H    1 
ATOM   4057 H HA   . TRP A 1 270 ? -10.155 -0.083  6.200   1.00 13.98 ? 289 TRP A HA   1 
ATOM   4058 H HB2  . TRP A 1 270 ? -10.091 0.525   3.425   1.00 14.93 ? 289 TRP A HB2  1 
ATOM   4059 H HB3  . TRP A 1 270 ? -10.908 1.382   4.486   1.00 14.93 ? 289 TRP A HB3  1 
ATOM   4060 H HD1  . TRP A 1 270 ? -7.507  0.891   3.353   1.00 12.67 ? 289 TRP A HD1  1 
ATOM   4061 H HE1  . TRP A 1 270 ? -5.941  2.362   4.445   1.00 13.36 ? 289 TRP A HE1  1 
ATOM   4062 H HE3  . TRP A 1 270 ? -10.509 2.881   6.659   1.00 14.27 ? 289 TRP A HE3  1 
ATOM   4063 H HZ2  . TRP A 1 270 ? -6.015  4.235   6.509   1.00 14.28 ? 289 TRP A HZ2  1 
ATOM   4064 H HZ3  . TRP A 1 270 ? -9.683  4.452   8.123   1.00 14.73 ? 289 TRP A HZ3  1 
ATOM   4065 H HH2  . TRP A 1 270 ? -7.489  5.132   8.038   1.00 14.77 ? 289 TRP A HH2  1 
ATOM   4066 N N    . ALA A 1 271 ? -12.420 -0.949  6.101   1.00 11.44 ? 290 ALA A N    1 
ATOM   4067 C CA   . ALA A 1 271 ? -13.637 -1.740  6.230   1.00 12.56 ? 290 ALA A CA   1 
ATOM   4068 C C    . ALA A 1 271 ? -14.772 -1.257  5.346   1.00 13.13 ? 290 ALA A C    1 
ATOM   4069 O O    . ALA A 1 271 ? -15.925 -1.178  5.800   1.00 13.52 ? 290 ALA A O    1 
ATOM   4070 C CB   . ALA A 1 271 ? -14.056 -1.753  7.702   1.00 13.36 ? 290 ALA A CB   1 
ATOM   4071 H H    . ALA A 1 271 ? -12.346 -0.338  6.702   1.00 13.74 ? 290 ALA A H    1 
ATOM   4072 H HA   . ALA A 1 271 ? -13.452 -2.644  5.929   1.00 15.08 ? 290 ALA A HA   1 
ATOM   4073 H HB1  . ALA A 1 271 ? -14.830 -2.328  7.805   1.00 16.04 ? 290 ALA A HB1  1 
ATOM   4074 H HB2  . ALA A 1 271 ? -13.321 -2.089  8.237   1.00 16.04 ? 290 ALA A HB2  1 
ATOM   4075 H HB3  . ALA A 1 271 ? -14.278 -0.849  7.975   1.00 16.04 ? 290 ALA A HB3  1 
ATOM   4076 N N    . GLY A 1 272 ? -14.452 -0.976  4.076   1.00 13.13 ? 291 GLY A N    1 
ATOM   4077 C CA   . GLY A 1 272 ? -15.429 -0.539  3.090   1.00 13.70 ? 291 GLY A CA   1 
ATOM   4078 C C    . GLY A 1 272 ? -15.589 0.954   2.989   1.00 13.63 ? 291 GLY A C    1 
ATOM   4079 O O    . GLY A 1 272 ? -16.366 1.430   2.147   1.00 15.58 ? 291 GLY A O    1 
ATOM   4080 H H    . GLY A 1 272 ? -13.654 -1.034  3.761   1.00 15.76 ? 291 GLY A H    1 
ATOM   4081 H HA2  . GLY A 1 272 ? -15.161 -0.869  2.218   1.00 16.44 ? 291 GLY A HA2  1 
ATOM   4082 H HA3  . GLY A 1 272 ? -16.293 -0.916  3.319   1.00 16.44 ? 291 GLY A HA3  1 
ATOM   4083 N N    . PHE A 1 273 ? -14.897 1.699   3.832   1.00 13.07 ? 292 PHE A N    1 
ATOM   4084 C CA   . PHE A 1 273 ? -14.969 3.148   3.927   1.00 12.52 ? 292 PHE A CA   1 
ATOM   4085 C C    . PHE A 1 273 ? -13.852 3.575   4.858   1.00 12.12 ? 292 PHE A C    1 
ATOM   4086 O O    . PHE A 1 273 ? -13.233 2.746   5.538   1.00 11.72 ? 292 PHE A O    1 
ATOM   4087 C CB   . PHE A 1 273 ? -16.339 3.645   4.425   1.00 12.47 ? 292 PHE A CB   1 
ATOM   4088 C CG   . PHE A 1 273 ? -16.707 3.185   5.802   1.00 12.33 ? 292 PHE A CG   1 
ATOM   4089 C CD1  . PHE A 1 273 ? -17.192 1.908   6.019   1.00 12.07 ? 292 PHE A CD1  1 
ATOM   4090 C CD2  . PHE A 1 273 ? -16.604 4.040   6.880   1.00 12.03 ? 292 PHE A CD2  1 
ATOM   4091 C CE1  . PHE A 1 273 ? -17.524 1.483   7.288   1.00 12.69 ? 292 PHE A CE1  1 
ATOM   4092 C CE2  . PHE A 1 273 ? -16.943 3.617   8.158   1.00 12.59 ? 292 PHE A CE2  1 
ATOM   4093 C CZ   . PHE A 1 273 ? -17.406 2.337   8.362   1.00 12.91 ? 292 PHE A CZ   1 
ATOM   4094 H H    . PHE A 1 273 ? -14.341 1.368   4.399   1.00 15.69 ? 292 PHE A H    1 
ATOM   4095 H HA   . PHE A 1 273 ? -14.831 3.543   3.051   1.00 15.03 ? 292 PHE A HA   1 
ATOM   4096 H HB2  . PHE A 1 273 ? -16.331 4.615   4.433   1.00 14.97 ? 292 PHE A HB2  1 
ATOM   4097 H HB3  . PHE A 1 273 ? -17.024 3.324   3.817   1.00 14.97 ? 292 PHE A HB3  1 
ATOM   4098 H HD1  . PHE A 1 273 ? -17.297 1.328   5.299   1.00 14.49 ? 292 PHE A HD1  1 
ATOM   4099 H HD2  . PHE A 1 273 ? -16.304 4.910   6.748   1.00 14.44 ? 292 PHE A HD2  1 
ATOM   4100 H HE1  . PHE A 1 273 ? -17.830 0.614   7.420   1.00 15.23 ? 292 PHE A HE1  1 
ATOM   4101 H HE2  . PHE A 1 273 ? -16.857 4.199   8.878   1.00 15.12 ? 292 PHE A HE2  1 
ATOM   4102 H HZ   . PHE A 1 273 ? -17.637 2.052   9.217   1.00 15.50 ? 292 PHE A HZ   1 
ATOM   4103 N N    . THR A 1 274 ? -13.597 4.878   4.882   1.00 12.38 ? 293 THR A N    1 
ATOM   4104 C CA   . THR A 1 274 ? -12.543 5.423   5.713   1.00 12.73 ? 293 THR A CA   1 
ATOM   4105 C C    . THR A 1 274 ? -13.096 6.541   6.581   1.00 12.53 ? 293 THR A C    1 
ATOM   4106 O O    . THR A 1 274 ? -14.212 7.035   6.376   1.00 12.36 ? 293 THR A O    1 
ATOM   4107 C CB   . THR A 1 274 ? -11.372 5.996   4.903   1.00 13.16 ? 293 THR A CB   1 
ATOM   4108 O OG1  . THR A 1 274 ? -11.738 7.303   4.434   1.00 12.99 ? 293 THR A OG1  1 
ATOM   4109 C CG2  . THR A 1 274 ? -11.001 5.081   3.747   1.00 13.20 ? 293 THR A CG2  1 
ATOM   4110 H H    . THR A 1 274 ? -14.027 5.464   4.423   1.00 14.86 ? 293 THR A H    1 
ATOM   4111 H HA   . THR A 1 274 ? -12.218 4.696   6.267   1.00 15.28 ? 293 THR A HA   1 
ATOM   4112 H HB   . THR A 1 274 ? -10.580 6.065   5.459   1.00 15.80 ? 293 THR A HB   1 
ATOM   4113 H HG1  . THR A 1 274 ? -11.193 7.561   3.849   1.00 15.60 ? 293 THR A HG1  1 
ATOM   4114 H HG21 . THR A 1 274 ? -10.225 5.432   3.283   1.00 15.85 ? 293 THR A HG21 1 
ATOM   4115 H HG22 . THR A 1 274 ? -10.795 4.194   4.080   1.00 15.85 ? 293 THR A HG22 1 
ATOM   4116 H HG23 . THR A 1 274 ? -11.740 5.020   3.123   1.00 15.85 ? 293 THR A HG23 1 
ATOM   4117 N N    . PHE A 1 275 ? -12.249 7.000   7.509   1.00 12.91 ? 294 PHE A N    1 
ATOM   4118 C CA   . PHE A 1 275 ? -12.654 8.035   8.448   1.00 13.37 ? 294 PHE A CA   1 
ATOM   4119 C C    . PHE A 1 275 ? -12.894 9.397   7.813   1.00 12.77 ? 294 PHE A C    1 
ATOM   4120 O O    . PHE A 1 275 ? -13.430 10.277  8.497   1.00 14.22 ? 294 PHE A O    1 
ATOM   4121 C CB   . PHE A 1 275 ? -11.643 8.149   9.584   1.00 14.66 ? 294 PHE A CB   1 
ATOM   4122 C CG   . PHE A 1 275 ? -10.312 8.715   9.184   1.00 14.70 ? 294 PHE A CG   1 
ATOM   4123 C CD1  . PHE A 1 275 ? -9.349  7.916   8.599   1.00 15.76 ? 294 PHE A CD1  1 
ATOM   4124 C CD2  . PHE A 1 275 ? -10.019 10.048  9.413   1.00 15.94 ? 294 PHE A CD2  1 
ATOM   4125 C CE1  . PHE A 1 275 ? -8.111  8.428   8.258   1.00 15.86 ? 294 PHE A CE1  1 
ATOM   4126 C CE2  . PHE A 1 275 ? -8.793  10.562  9.075   1.00 16.41 ? 294 PHE A CE2  1 
ATOM   4127 C CZ   . PHE A 1 275 ? -7.836  9.751   8.490   1.00 16.24 ? 294 PHE A CZ   1 
ATOM   4128 H H    . PHE A 1 275 ? -11.440 6.725   7.611   1.00 15.50 ? 294 PHE A H    1 
ATOM   4129 H HA   . PHE A 1 275 ? -13.500 7.761   8.835   1.00 16.05 ? 294 PHE A HA   1 
ATOM   4130 H HB2  . PHE A 1 275 ? -12.013 8.728   10.269  1.00 17.60 ? 294 PHE A HB2  1 
ATOM   4131 H HB3  . PHE A 1 275 ? -11.486 7.263   9.948   1.00 17.60 ? 294 PHE A HB3  1 
ATOM   4132 H HD1  . PHE A 1 275 ? -9.536  7.020   8.433   1.00 18.91 ? 294 PHE A HD1  1 
ATOM   4133 H HD2  . PHE A 1 275 ? -10.659 10.601  9.799   1.00 19.13 ? 294 PHE A HD2  1 
ATOM   4134 H HE1  . PHE A 1 275 ? -7.468  7.878   7.872   1.00 19.04 ? 294 PHE A HE1  1 
ATOM   4135 H HE2  . PHE A 1 275 ? -8.605  11.458  9.240   1.00 19.70 ? 294 PHE A HE2  1 
ATOM   4136 H HZ   . PHE A 1 275 ? -7.008  10.103  8.255   1.00 19.50 ? 294 PHE A HZ   1 
ATOM   4137 N N    . ILE A 1 276 ? -12.526 9.599   6.541   1.00 12.78 ? 295 ILE A N    1 
ATOM   4138 C CA   . ILE A 1 276 ? -12.838 10.855  5.855   1.00 12.76 ? 295 ILE A CA   1 
ATOM   4139 C C    . ILE A 1 276 ? -14.078 10.752  4.966   1.00 12.19 ? 295 ILE A C    1 
ATOM   4140 O O    . ILE A 1 276 ? -14.493 11.755  4.354   1.00 13.18 ? 295 ILE A O    1 
ATOM   4141 C CB   . ILE A 1 276 ? -11.639 11.431  5.057   1.00 13.92 ? 295 ILE A CB   1 
ATOM   4142 C CG1  . ILE A 1 276 ? -11.262 10.561  3.862   1.00 13.93 ? 295 ILE A CG1  1 
ATOM   4143 C CG2  . ILE A 1 276 ? -10.438 11.639  5.977   1.00 14.19 ? 295 ILE A CG2  1 
ATOM   4144 C CD1  . ILE A 1 276 ? -10.287 11.198  2.949   1.00 14.47 ? 295 ILE A CD1  1 
ATOM   4145 H H    . ILE A 1 276 ? -12.099 9.028   6.060   1.00 15.34 ? 295 ILE A H    1 
ATOM   4146 H HA   . ILE A 1 276 ? -13.032 11.502  6.551   1.00 15.32 ? 295 ILE A HA   1 
ATOM   4147 H HB   . ILE A 1 276 ? -11.919 12.289  4.702   1.00 16.71 ? 295 ILE A HB   1 
ATOM   4148 H HG12 . ILE A 1 276 ? -10.869 9.736   4.188   1.00 16.72 ? 295 ILE A HG12 1 
ATOM   4149 H HG13 . ILE A 1 276 ? -12.064 10.367  3.351   1.00 16.72 ? 295 ILE A HG13 1 
ATOM   4150 H HG21 . ILE A 1 276 ? -9.738  12.095  5.484   1.00 17.03 ? 295 ILE A HG21 1 
ATOM   4151 H HG22 . ILE A 1 276 ? -10.711 12.176  6.737   1.00 17.03 ? 295 ILE A HG22 1 
ATOM   4152 H HG23 . ILE A 1 276 ? -10.119 10.774  6.280   1.00 17.03 ? 295 ILE A HG23 1 
ATOM   4153 H HD11 . ILE A 1 276 ? -10.169 10.633  2.169   1.00 17.37 ? 295 ILE A HD11 1 
ATOM   4154 H HD12 . ILE A 1 276 ? -10.626 12.066  2.681   1.00 17.37 ? 295 ILE A HD12 1 
ATOM   4155 H HD13 . ILE A 1 276 ? -9.442  11.302  3.413   1.00 17.37 ? 295 ILE A HD13 1 
ATOM   4156 N N    . ASP A 1 277 ? -14.706 9.586   4.897   1.00 12.53 ? 296 ASP A N    1 
ATOM   4157 C CA   . ASP A 1 277 ? -15.920 9.409   4.095   1.00 13.01 ? 296 ASP A CA   1 
ATOM   4158 C C    . ASP A 1 277 ? -17.107 9.828   4.961   1.00 12.72 ? 296 ASP A C    1 
ATOM   4159 O O    . ASP A 1 277 ? -17.565 9.064   5.820   1.00 13.11 ? 296 ASP A O    1 
ATOM   4160 C CB   . ASP A 1 277 ? -16.045 7.970   3.601   1.00 13.31 ? 296 ASP A CB   1 
ATOM   4161 C CG   . ASP A 1 277 ? -14.947 7.556   2.645   1.00 13.19 ? 296 ASP A CG   1 
ATOM   4162 O OD1  . ASP A 1 277 ? -14.419 8.402   1.875   1.00 13.79 ? 296 ASP A OD1  1 
ATOM   4163 O OD2  . ASP A 1 277 ? -14.609 6.337   2.659   1.00 13.29 ? 296 ASP A OD2  1 
ATOM   4164 H H    . ASP A 1 277 ? -14.451 8.875   5.306   1.00 15.04 ? 296 ASP A H    1 
ATOM   4165 H HA   . ASP A 1 277 ? -15.888 9.984   3.314   1.00 15.62 ? 296 ASP A HA   1 
ATOM   4166 H HB2  . ASP A 1 277 ? -16.013 7.374   4.365   1.00 15.98 ? 296 ASP A HB2  1 
ATOM   4167 H HB3  . ASP A 1 277 ? -16.892 7.871   3.138   1.00 15.98 ? 296 ASP A HB3  1 
ATOM   4168 N N    . ASP A 1 278 ? -17.641 11.027  4.704   1.00 13.81 ? 297 ASP A N    1 
ATOM   4169 C CA   . ASP A 1 278 ? -18.578 11.643  5.642   1.00 14.49 ? 297 ASP A CA   1 
ATOM   4170 C C    . ASP A 1 278 ? -19.885 10.864  5.768   1.00 14.58 ? 297 ASP A C    1 
ATOM   4171 O O    . ASP A 1 278 ? -20.323 10.547  6.885   1.00 14.92 ? 297 ASP A O    1 
ATOM   4172 C CB   . ASP A 1 278 ? -18.875 13.082  5.215   1.00 16.45 ? 297 ASP A CB   1 
ATOM   4173 C CG   . ASP A 1 278 ? -19.724 13.820  6.217   1.00 18.85 ? 297 ASP A CG   1 
ATOM   4174 O OD1  . ASP A 1 278 ? -19.312 13.949  7.378   1.00 20.81 ? 297 ASP A OD1  1 
ATOM   4175 O OD2  . ASP A 1 278 ? -20.814 14.274  5.823   1.00 20.79 ? 297 ASP A OD2  1 
ATOM   4176 H H    . ASP A 1 278 ? -17.479 11.497  4.002   1.00 16.58 ? 297 ASP A H    1 
ATOM   4177 H HA   . ASP A 1 278 ? -18.154 11.647  6.514   1.00 17.40 ? 297 ASP A HA   1 
ATOM   4178 H HB2  . ASP A 1 278 ? -18.038 13.563  5.119   1.00 19.74 ? 297 ASP A HB2  1 
ATOM   4179 H HB3  . ASP A 1 278 ? -19.349 13.070  4.369   1.00 19.74 ? 297 ASP A HB3  1 
ATOM   4180 N N    A GLN A 1 279 ? -20.538 10.561  4.640   0.56 14.62 ? 298 GLN A N    1 
ATOM   4181 N N    B GLN A 1 279 ? -20.544 10.565  4.648   0.44 14.97 ? 298 GLN A N    1 
ATOM   4182 C CA   A GLN A 1 279 ? -21.806 9.830   4.704   0.56 14.75 ? 298 GLN A CA   1 
ATOM   4183 C CA   B GLN A 1 279 ? -21.813 9.843   4.741   0.44 15.44 ? 298 GLN A CA   1 
ATOM   4184 C C    A GLN A 1 279 ? -21.623 8.488   5.400   0.56 13.78 ? 298 GLN A C    1 
ATOM   4185 C C    B GLN A 1 279 ? -21.623 8.486   5.414   0.44 14.12 ? 298 GLN A C    1 
ATOM   4186 O O    A GLN A 1 279 ? -22.440 8.090   6.238   0.56 14.33 ? 298 GLN A O    1 
ATOM   4187 O O    B GLN A 1 279 ? -22.435 8.075   6.250   0.44 14.47 ? 298 GLN A O    1 
ATOM   4188 C CB   A GLN A 1 279 ? -22.380 9.653   3.292   0.56 15.34 ? 298 GLN A CB   1 
ATOM   4189 C CB   B GLN A 1 279 ? -22.456 9.709   3.357   0.44 17.01 ? 298 GLN A CB   1 
ATOM   4190 C CG   A GLN A 1 279 ? -23.740 8.941   3.216   0.56 17.50 ? 298 GLN A CG   1 
ATOM   4191 C CG   B GLN A 1 279 ? -22.895 11.043  2.752   0.44 19.63 ? 298 GLN A CG   1 
ATOM   4192 C CD   A GLN A 1 279 ? -24.120 8.578   1.785   0.56 20.54 ? 298 GLN A CD   1 
ATOM   4193 C CD   B GLN A 1 279 ? -23.904 11.786  3.607   0.44 22.34 ? 298 GLN A CD   1 
ATOM   4194 O OE1  A GLN A 1 279 ? -23.713 7.538   1.263   0.56 22.65 ? 298 GLN A OE1  1 
ATOM   4195 O OE1  B GLN A 1 279 ? -24.859 11.202  4.127   0.44 22.67 ? 298 GLN A OE1  1 
ATOM   4196 N NE2  A GLN A 1 279 ? -24.911 9.428   1.153   0.56 21.75 ? 298 GLN A NE2  1 
ATOM   4197 N NE2  B GLN A 1 279 ? -23.674 13.079  3.789   0.44 24.49 ? 298 GLN A NE2  1 
ATOM   4198 H H    A GLN A 1 279 ? -20.275 10.762  3.846   0.56 17.55 ? 298 GLN A H    1 
ATOM   4199 H H    B GLN A 1 279 ? -20.288 10.761  3.850   0.44 17.97 ? 298 GLN A H    1 
ATOM   4200 H HA   A GLN A 1 279 ? -22.449 10.344  5.217   0.56 17.70 ? 298 GLN A HA   1 
ATOM   4201 H HA   B GLN A 1 279 ? -22.430 10.353  5.288   0.44 18.53 ? 298 GLN A HA   1 
ATOM   4202 H HB2  A GLN A 1 279 ? -22.491 10.531  2.895   0.56 18.42 ? 298 GLN A HB2  1 
ATOM   4203 H HB2  B GLN A 1 279 ? -21.813 9.306   2.752   0.44 20.42 ? 298 GLN A HB2  1 
ATOM   4204 H HB3  A GLN A 1 279 ? -21.751 9.131   2.770   0.56 18.42 ? 298 GLN A HB3  1 
ATOM   4205 H HB3  B GLN A 1 279 ? -23.241 9.144   3.431   0.44 20.42 ? 298 GLN A HB3  1 
ATOM   4206 H HG2  A GLN A 1 279 ? -23.700 8.123   3.736   0.56 21.01 ? 298 GLN A HG2  1 
ATOM   4207 H HG2  B GLN A 1 279 ? -22.116 11.613  2.648   0.44 23.57 ? 298 GLN A HG2  1 
ATOM   4208 H HG3  A GLN A 1 279 ? -24.426 9.527   3.572   0.56 21.01 ? 298 GLN A HG3  1 
ATOM   4209 H HG3  B GLN A 1 279 ? -23.302 10.877  1.887   0.44 23.57 ? 298 GLN A HG3  1 
ATOM   4210 H HE21 A GLN A 1 279 ? -25.183 10.141  1.551   0.56 26.11 ? 298 GLN A HE21 1 
ATOM   4211 H HE21 B GLN A 1 279 ? -22.985 13.448  3.430   0.44 29.40 ? 298 GLN A HE21 1 
ATOM   4212 H HE22 A GLN A 1 279 ? -25.154 9.269   0.344   0.56 26.11 ? 298 GLN A HE22 1 
ATOM   4213 H HE22 B GLN A 1 279 ? -24.215 13.549  4.266   0.44 29.40 ? 298 GLN A HE22 1 
ATOM   4214 N N    . ALA A 1 280 ? -20.535 7.791   5.090   1.00 13.21 ? 299 ALA A N    1 
ATOM   4215 C CA   . ALA A 1 280 ? -20.279 6.499   5.712   1.00 12.76 ? 299 ALA A CA   1 
ATOM   4216 C C    . ALA A 1 280 ? -20.011 6.626   7.207   1.00 12.14 ? 299 ALA A C    1 
ATOM   4217 O O    . ALA A 1 280 ? -20.482 5.788   7.998   1.00 12.39 ? 299 ALA A O    1 
ATOM   4218 C CB   . ALA A 1 280 ? -19.118 5.828   4.995   1.00 12.33 ? 299 ALA A CB   1 
ATOM   4219 H H    . ALA A 1 280 ? -19.937 8.044   4.527   1.00 15.86 ? 299 ALA A H    1 
ATOM   4220 H HA   . ALA A 1 280 ? -21.065 5.938   5.621   1.00 15.31 ? 299 ALA A HA   1 
ATOM   4221 H HB1  . ALA A 1 280 ? -18.943 4.970   5.411   1.00 14.80 ? 299 ALA A HB1  1 
ATOM   4222 H HB2  . ALA A 1 280 ? -19.354 5.701   4.062   1.00 14.80 ? 299 ALA A HB2  1 
ATOM   4223 H HB3  . ALA A 1 280 ? -18.334 6.395   5.063   1.00 14.80 ? 299 ALA A HB3  1 
ATOM   4224 N N    . MET A 1 281 ? -19.267 7.666   7.607   1.00 12.49 ? 300 MET A N    1 
ATOM   4225 C CA   . MET A 1 281 ? -18.968 7.894   9.016   1.00 13.44 ? 300 MET A CA   1 
ATOM   4226 C C    . MET A 1 281 ? -20.169 8.338   9.818   1.00 13.54 ? 300 MET A C    1 
ATOM   4227 O O    . MET A 1 281 ? -20.153 8.229   11.048  1.00 15.56 ? 300 MET A O    1 
ATOM   4228 C CB   . MET A 1 281 ? -17.806 8.862   9.203   1.00 13.47 ? 300 MET A CB   1 
ATOM   4229 C CG   . MET A 1 281 ? -16.457 8.330   8.750   1.00 13.79 ? 300 MET A CG   1 
ATOM   4230 S SD   . MET A 1 281 ? -15.942 6.940   9.808   1.00 15.02 ? 300 MET A SD   1 
ATOM   4231 C CE   . MET A 1 281 ? -15.708 7.769   11.344  1.00 17.07 ? 300 MET A CE   1 
ATOM   4232 H H    . MET A 1 281 ? -18.926 8.252   7.079   1.00 15.00 ? 300 MET A H    1 
ATOM   4233 H HA   . MET A 1 281 ? -18.668 7.046   9.377   1.00 16.13 ? 300 MET A HA   1 
ATOM   4234 H HB2  . MET A 1 281 ? -17.989 9.666   8.692   1.00 16.18 ? 300 MET A HB2  1 
ATOM   4235 H HB3  . MET A 1 281 ? -17.733 9.078   10.146  1.00 16.18 ? 300 MET A HB3  1 
ATOM   4236 H HG2  . MET A 1 281 ? -16.522 8.016   7.834   1.00 16.55 ? 300 MET A HG2  1 
ATOM   4237 H HG3  . MET A 1 281 ? -15.791 9.032   8.814   1.00 16.55 ? 300 MET A HG3  1 
ATOM   4238 H HE1  . MET A 1 281 ? -15.418 7.125   12.009  1.00 20.50 ? 300 MET A HE1  1 
ATOM   4239 H HE2  . MET A 1 281 ? -15.032 8.455   11.232  1.00 20.50 ? 300 MET A HE2  1 
ATOM   4240 H HE3  . MET A 1 281 ? -16.547 8.172   11.616  1.00 20.50 ? 300 MET A HE3  1 
ATOM   4241 N N    . ARG A 1 282 ? -21.224 8.801   9.161   1.00 13.48 ? 301 ARG A N    1 
ATOM   4242 C CA   . ARG A 1 282 ? -22.426 9.212   9.874   1.00 15.21 ? 301 ARG A CA   1 
ATOM   4243 C C    . ARG A 1 282 ? -23.371 8.045   10.137  1.00 14.98 ? 301 ARG A C    1 
ATOM   4244 O O    . ARG A 1 282 ? -24.328 8.207   10.887  1.00 16.15 ? 301 ARG A O    1 
ATOM   4245 C CB   . ARG A 1 282 ? -23.133 10.314  9.079   1.00 16.12 ? 301 ARG A CB   1 
ATOM   4246 C CG   . ARG A 1 282 ? -22.426 11.660  9.136   1.00 18.04 ? 301 ARG A CG   1 
ATOM   4247 C CD   . ARG A 1 282 ? -22.919 12.601  8.025   1.00 19.87 ? 301 ARG A CD   1 
ATOM   4248 N NE   . ARG A 1 282 ? -24.294 13.047  8.228   1.00 21.05 ? 301 ARG A NE   1 
ATOM   4249 C CZ   . ARG A 1 282 ? -24.659 14.024  9.046   1.00 23.49 ? 301 ARG A CZ   1 
ATOM   4250 N NH1  . ARG A 1 282 ? -23.767 14.712  9.738   1.00 25.14 ? 301 ARG A NH1  1 
ATOM   4251 N NH2  . ARG A 1 282 ? -25.949 14.334  9.159   1.00 24.31 ? 301 ARG A NH2  1 
ATOM   4252 H H    . ARG A 1 282 ? -21.268 8.887   8.307   1.00 16.19 ? 301 ARG A H    1 
ATOM   4253 H HA   . ARG A 1 282 ? -22.191 9.586   10.737  1.00 18.26 ? 301 ARG A HA   1 
ATOM   4254 H HB2  . ARG A 1 282 ? -23.183 10.044  8.149   1.00 19.34 ? 301 ARG A HB2  1 
ATOM   4255 H HB3  . ARG A 1 282 ? -24.026 10.433  9.438   1.00 19.34 ? 301 ARG A HB3  1 
ATOM   4256 H HG2  . ARG A 1 282 ? -22.603 12.080  9.992   1.00 21.66 ? 301 ARG A HG2  1 
ATOM   4257 H HG3  . ARG A 1 282 ? -21.472 11.527  9.022   1.00 21.66 ? 301 ARG A HG3  1 
ATOM   4258 H HD2  . ARG A 1 282 ? -22.350 13.387  8.001   1.00 23.86 ? 301 ARG A HD2  1 
ATOM   4259 H HD3  . ARG A 1 282 ? -22.878 12.136  7.175   1.00 23.86 ? 301 ARG A HD3  1 
ATOM   4260 H HE   . ARG A 1 282 ? -24.913 12.647  7.784   1.00 25.26 ? 301 ARG A HE   1 
ATOM   4261 H HH11 . ARG A 1 282 ? -22.930 14.529  9.663   1.00 30.18 ? 301 ARG A HH11 1 
ATOM   4262 H HH12 . ARG A 1 282 ? -24.024 15.342  10.264  1.00 30.18 ? 301 ARG A HH12 1 
ATOM   4263 H HH21 . ARG A 1 282 ? -26.536 13.901  8.703   1.00 29.18 ? 301 ARG A HH21 1 
ATOM   4264 H HH22 . ARG A 1 282 ? -26.196 14.966  9.687   1.00 29.18 ? 301 ARG A HH22 1 
ATOM   4265 N N    . LYS A 1 283 ? -23.122 6.873   9.558   1.00 14.05 ? 302 LYS A N    1 
ATOM   4266 C CA   . LYS A 1 283 ? -24.068 5.780   9.692   1.00 14.22 ? 302 LYS A CA   1 
ATOM   4267 C C    . LYS A 1 283 ? -24.063 5.243   11.123  1.00 13.85 ? 302 LYS A C    1 
ATOM   4268 O O    . LYS A 1 283 ? -23.020 5.213   11.790  1.00 14.36 ? 302 LYS A O    1 
ATOM   4269 C CB   . LYS A 1 283 ? -23.742 4.668   8.698   1.00 15.58 ? 302 LYS A CB   1 
ATOM   4270 C CG   . LYS A 1 283 ? -24.132 5.033   7.253   1.00 18.98 ? 302 LYS A CG   1 
ATOM   4271 C CD   . LYS A 1 283 ? -23.774 3.924   6.297   1.00 22.61 ? 302 LYS A CD   1 
ATOM   4272 C CE   . LYS A 1 283 ? -23.811 4.356   4.840   1.00 25.99 ? 302 LYS A CE   1 
ATOM   4273 N NZ   . LYS A 1 283 ? -23.802 3.149   3.943   1.00 28.44 ? 302 LYS A NZ   1 
ATOM   4274 H H    . LYS A 1 283 ? -22.423 6.691   9.091   1.00 16.86 ? 302 LYS A H    1 
ATOM   4275 H HA   . LYS A 1 283 ? -24.964 6.095   9.498   1.00 17.07 ? 302 LYS A HA   1 
ATOM   4276 H HB2  . LYS A 1 283 ? -22.788 4.495   8.718   1.00 18.70 ? 302 LYS A HB2  1 
ATOM   4277 H HB3  . LYS A 1 283 ? -24.229 3.867   8.948   1.00 18.70 ? 302 LYS A HB3  1 
ATOM   4278 H HG2  . LYS A 1 283 ? -25.089 5.182   7.205   1.00 22.78 ? 302 LYS A HG2  1 
ATOM   4279 H HG3  . LYS A 1 283 ? -23.657 5.835   6.983   1.00 22.78 ? 302 LYS A HG3  1 
ATOM   4280 H HD2  . LYS A 1 283 ? -22.876 3.616   6.494   1.00 27.14 ? 302 LYS A HD2  1 
ATOM   4281 H HD3  . LYS A 1 283 ? -24.406 3.196   6.408   1.00 27.14 ? 302 LYS A HD3  1 
ATOM   4282 H HE2  . LYS A 1 283 ? -24.620 4.864   4.670   1.00 31.19 ? 302 LYS A HE2  1 
ATOM   4283 H HE3  . LYS A 1 283 ? -23.032 4.898   4.640   1.00 31.19 ? 302 LYS A HE3  1 
ATOM   4284 H HZ1  . LYS A 1 283 ? -23.879 3.400   3.093   1.00 34.14 ? 302 LYS A HZ1  1 
ATOM   4285 H HZ2  . LYS A 1 283 ? -23.040 2.700   4.044   1.00 34.14 ? 302 LYS A HZ2  1 
ATOM   4286 H HZ3  . LYS A 1 283 ? -24.482 2.612   4.148   1.00 34.14 ? 302 LYS A HZ3  1 
ATOM   4287 N N    . PRO A 1 284 ? -25.213 4.762   11.605  1.00 13.80 ? 303 PRO A N    1 
ATOM   4288 C CA   . PRO A 1 284 ? -25.237 4.106   12.919  1.00 14.49 ? 303 PRO A CA   1 
ATOM   4289 C C    . PRO A 1 284 ? -24.201 3.001   12.994  1.00 14.13 ? 303 PRO A C    1 
ATOM   4290 O O    . PRO A 1 284 ? -23.921 2.326   12.007  1.00 13.79 ? 303 PRO A O    1 
ATOM   4291 C CB   . PRO A 1 284 ? -26.666 3.557   13.009  1.00 15.06 ? 303 PRO A CB   1 
ATOM   4292 C CG   . PRO A 1 284 ? -27.477 4.498   12.145  1.00 14.44 ? 303 PRO A CG   1 
ATOM   4293 C CD   . PRO A 1 284 ? -26.553 4.774   10.975  1.00 14.12 ? 303 PRO A CD   1 
ATOM   4294 H HA   . PRO A 1 284 ? -25.087 4.744   13.635  1.00 17.39 ? 303 PRO A HA   1 
ATOM   4295 H HB2  . PRO A 1 284 ? -26.698 2.651   12.665  1.00 18.08 ? 303 PRO A HB2  1 
ATOM   4296 H HB3  . PRO A 1 284 ? -26.973 3.574   13.929  1.00 18.08 ? 303 PRO A HB3  1 
ATOM   4297 H HG2  . PRO A 1 284 ? -28.297 4.068   11.855  1.00 17.34 ? 303 PRO A HG2  1 
ATOM   4298 H HG3  . PRO A 1 284 ? -27.684 5.311   12.632  1.00 17.34 ? 303 PRO A HG3  1 
ATOM   4299 H HD2  . PRO A 1 284 ? -26.627 4.078   10.303  1.00 16.95 ? 303 PRO A HD2  1 
ATOM   4300 H HD3  . PRO A 1 284 ? -26.743 5.639   10.580  1.00 16.95 ? 303 PRO A HD3  1 
ATOM   4301 N N    . LEU A 1 285 ? -23.675 2.793   14.202  1.00 14.25 ? 304 LEU A N    1 
ATOM   4302 C CA   . LEU A 1 285 ? -22.632 1.791   14.410  1.00 14.41 ? 304 LEU A CA   1 
ATOM   4303 C C    . LEU A 1 285 ? -23.039 0.411   13.907  1.00 14.00 ? 304 LEU A C    1 
ATOM   4304 O O    . LEU A 1 285 ? -22.225 -0.284  13.302  1.00 13.54 ? 304 LEU A O    1 
ATOM   4305 C CB   . LEU A 1 285 ? -22.255 1.719   15.885  1.00 15.45 ? 304 LEU A CB   1 
ATOM   4306 C CG   . LEU A 1 285 ? -21.222 0.658   16.253  1.00 16.38 ? 304 LEU A CG   1 
ATOM   4307 C CD1  . LEU A 1 285 ? -19.933 0.795   15.430  1.00 16.64 ? 304 LEU A CD1  1 
ATOM   4308 C CD2  . LEU A 1 285 ? -20.906 0.755   17.752  1.00 17.65 ? 304 LEU A CD2  1 
ATOM   4309 H H    . LEU A 1 285 ? -23.904 3.217   14.914  1.00 17.11 ? 304 LEU A H    1 
ATOM   4310 H HA   . LEU A 1 285 ? -21.853 2.069   13.905  1.00 17.30 ? 304 LEU A HA   1 
ATOM   4311 H HB2  . LEU A 1 285 ? -21.891 2.579   16.148  1.00 18.54 ? 304 LEU A HB2  1 
ATOM   4312 H HB3  . LEU A 1 285 ? -23.058 1.529   16.395  1.00 18.54 ? 304 LEU A HB3  1 
ATOM   4313 H HG   . LEU A 1 285 ? -21.592 -0.216  16.051  1.00 19.67 ? 304 LEU A HG   1 
ATOM   4314 H HD11 . LEU A 1 285 ? -19.291 0.135   15.737  1.00 19.98 ? 304 LEU A HD11 1 
ATOM   4315 H HD12 . LEU A 1 285 ? -20.138 0.646   14.494  1.00 19.98 ? 304 LEU A HD12 1 
ATOM   4316 H HD13 . LEU A 1 285 ? -19.573 1.688   15.551  1.00 19.98 ? 304 LEU A HD13 1 
ATOM   4317 H HD21 . LEU A 1 285 ? -20.181 0.147   17.962  1.00 21.18 ? 304 LEU A HD21 1 
ATOM   4318 H HD22 . LEU A 1 285 ? -20.646 1.665   17.962  1.00 21.18 ? 304 LEU A HD22 1 
ATOM   4319 H HD23 . LEU A 1 285 ? -21.698 0.512   18.258  1.00 21.18 ? 304 LEU A HD23 1 
ATOM   4320 N N    . THR A 1 286 ? -24.278 -0.027  14.163  1.00 15.39 ? 305 THR A N    1 
ATOM   4321 C CA   . THR A 1 286 ? -24.665 -1.355  13.700  1.00 15.95 ? 305 THR A CA   1 
ATOM   4322 C C    . THR A 1 286 ? -24.579 -1.460  12.183  1.00 15.11 ? 305 THR A C    1 
ATOM   4323 O O    . THR A 1 286 ? -24.187 -2.509  11.660  1.00 16.95 ? 305 THR A O    1 
ATOM   4324 C CB   . THR A 1 286 ? -26.049 -1.711  14.239  1.00 18.63 ? 305 THR A CB   1 
ATOM   4325 O OG1  . THR A 1 286 ? -25.934 -1.847  15.663  1.00 19.42 ? 305 THR A OG1  1 
ATOM   4326 C CG2  . THR A 1 286 ? -26.560 -3.020  13.672  1.00 20.36 ? 305 THR A CG2  1 
ATOM   4327 H H    . THR A 1 286 ? -24.885 0.410   14.587  1.00 18.47 ? 305 THR A H    1 
ATOM   4328 H HA   . THR A 1 286 ? -24.055 -2.021  14.055  1.00 19.15 ? 305 THR A HA   1 
ATOM   4329 H HB   . THR A 1 286 ? -26.684 -1.021  13.991  1.00 22.36 ? 305 THR A HB   1 
ATOM   4330 H HG1  . THR A 1 286 ? -25.412 -2.478  15.849  1.00 23.31 ? 305 THR A HG1  1 
ATOM   4331 H HG21 . THR A 1 286 ? -27.341 -3.314  14.166  1.00 24.43 ? 305 THR A HG21 1 
ATOM   4332 H HG22 . THR A 1 286 ? -26.801 -2.906  12.740  1.00 24.43 ? 305 THR A HG22 1 
ATOM   4333 H HG23 . THR A 1 286 ? -25.872 -3.701  13.738  1.00 24.43 ? 305 THR A HG23 1 
ATOM   4334 N N    . GLN A 1 287 ? -24.895 -0.370  11.460  1.00 14.36 ? 306 GLN A N    1 
ATOM   4335 C CA   . GLN A 1 287 ? -24.761 -0.392  10.010  1.00 14.10 ? 306 GLN A CA   1 
ATOM   4336 C C    . GLN A 1 287 ? -23.293 -0.357  9.592   1.00 13.24 ? 306 GLN A C    1 
ATOM   4337 O O    . GLN A 1 287 ? -22.898 -1.053  8.655   1.00 13.46 ? 306 GLN A O    1 
ATOM   4338 C CB   . GLN A 1 287 ? -25.550 0.761   9.400   1.00 15.50 ? 306 GLN A CB   1 
ATOM   4339 C CG   . GLN A 1 287 ? -25.438 0.842   7.889   1.00 17.39 ? 306 GLN A CG   1 
ATOM   4340 C CD   . GLN A 1 287 ? -26.008 -0.367  7.169   1.00 20.03 ? 306 GLN A CD   1 
ATOM   4341 O OE1  . GLN A 1 287 ? -26.750 -1.173  7.752   1.00 19.75 ? 306 GLN A OE1  1 
ATOM   4342 N NE2  . GLN A 1 287 ? -25.655 -0.504  5.891   1.00 21.02 ? 306 GLN A NE2  1 
ATOM   4343 H H    . GLN A 1 287 ? -25.182 0.372   11.786  1.00 17.24 ? 306 GLN A H    1 
ATOM   4344 H HA   . GLN A 1 287 ? -25.139 -1.215  9.663   1.00 16.93 ? 306 GLN A HA   1 
ATOM   4345 H HB2  . GLN A 1 287 ? -26.488 0.650   9.623   1.00 18.61 ? 306 GLN A HB2  1 
ATOM   4346 H HB3  . GLN A 1 287 ? -25.218 1.595   9.768   1.00 18.61 ? 306 GLN A HB3  1 
ATOM   4347 H HG2  . GLN A 1 287 ? -25.921 1.625   7.582   1.00 20.88 ? 306 GLN A HG2  1 
ATOM   4348 H HG3  . GLN A 1 287 ? -24.501 0.915   7.649   1.00 20.88 ? 306 GLN A HG3  1 
ATOM   4349 H HE21 . GLN A 1 287 ? -25.134 0.074   5.524   1.00 25.23 ? 306 GLN A HE21 1 
ATOM   4350 H HE22 . GLN A 1 287 ? -25.948 -1.170  5.433   1.00 25.23 ? 306 GLN A HE22 1 
ATOM   4351 N N    . LYS A 1 288 ? -22.460 0.413   10.293  1.00 13.00 ? 307 LYS A N    1 
ATOM   4352 C CA   . LYS A 1 288 ? -21.024 0.362   10.018  1.00 12.64 ? 307 LYS A CA   1 
ATOM   4353 C C    . LYS A 1 288 ? -20.503 -1.061  10.155  1.00 13.58 ? 307 LYS A C    1 
ATOM   4354 O O    . LYS A 1 288 ? -19.671 -1.509  9.361   1.00 13.71 ? 307 LYS A O    1 
ATOM   4355 C CB   . LYS A 1 288 ? -20.256 1.248   10.998  1.00 12.67 ? 307 LYS A CB   1 
ATOM   4356 C CG   . LYS A 1 288 ? -20.426 2.755   10.818  1.00 12.80 ? 307 LYS A CG   1 
ATOM   4357 C CD   . LYS A 1 288 ? -19.304 3.484   11.557  1.00 14.34 ? 307 LYS A CD   1 
ATOM   4358 C CE   . LYS A 1 288 ? -19.307 4.989   11.354  1.00 15.15 ? 307 LYS A CE   1 
ATOM   4359 N NZ   . LYS A 1 288 ? -20.349 5.646   12.204  1.00 15.15 ? 307 LYS A NZ   1 
ATOM   4360 H H    . LYS A 1 288 ? -22.693 0.958   10.916  1.00 15.61 ? 307 LYS A H    1 
ATOM   4361 H HA   . LYS A 1 288 ? -20.879 0.688   9.116   1.00 15.17 ? 307 LYS A HA   1 
ATOM   4362 H HB2  . LYS A 1 288 ? -20.551 1.032   11.896  1.00 15.21 ? 307 LYS A HB2  1 
ATOM   4363 H HB3  . LYS A 1 288 ? -19.310 1.053   10.904  1.00 15.21 ? 307 LYS A HB3  1 
ATOM   4364 H HG2  . LYS A 1 288 ? -20.379 2.981   9.876   1.00 15.37 ? 307 LYS A HG2  1 
ATOM   4365 H HG3  . LYS A 1 288 ? -21.278 3.037   11.185  1.00 15.37 ? 307 LYS A HG3  1 
ATOM   4366 H HD2  . LYS A 1 288 ? -19.396 3.315   12.507  1.00 17.21 ? 307 LYS A HD2  1 
ATOM   4367 H HD3  . LYS A 1 288 ? -18.452 3.146   11.241  1.00 17.21 ? 307 LYS A HD3  1 
ATOM   4368 H HE2  . LYS A 1 288 ? -18.440 5.348   11.599  1.00 18.18 ? 307 LYS A HE2  1 
ATOM   4369 H HE3  . LYS A 1 288 ? -19.499 5.189   10.425  1.00 18.18 ? 307 LYS A HE3  1 
ATOM   4370 H HZ1  . LYS A 1 288 ? -20.350 6.524   12.059  1.00 18.19 ? 307 LYS A HZ1  1 
ATOM   4371 H HZ2  . LYS A 1 288 ? -21.153 5.320   12.007  1.00 18.19 ? 307 LYS A HZ2  1 
ATOM   4372 H HZ3  . LYS A 1 288 ? -20.179 5.496   13.065  1.00 18.19 ? 307 LYS A HZ3  1 
ATOM   4373 N N    . ARG A 1 289 ? -20.969 -1.779  11.174  1.00 14.69 ? 308 ARG A N    1 
ATOM   4374 C CA   . ARG A 1 289 ? -20.521 -3.150  11.371  1.00 15.22 ? 308 ARG A CA   1 
ATOM   4375 C C    . ARG A 1 289 ? -20.990 -4.059  10.245  1.00 16.11 ? 308 ARG A C    1 
ATOM   4376 O O    . ARG A 1 289 ? -20.252 -4.965  9.833   1.00 16.73 ? 308 ARG A O    1 
ATOM   4377 C CB   . ARG A 1 289 ? -21.039 -3.671  12.710  1.00 16.24 ? 308 ARG A CB   1 
ATOM   4378 C CG   . ARG A 1 289 ? -20.353 -3.056  13.894  1.00 18.22 ? 308 ARG A CG   1 
ATOM   4379 C CD   . ARG A 1 289 ? -20.993 -3.484  15.185  1.00 19.97 ? 308 ARG A CD   1 
ATOM   4380 N NE   . ARG A 1 289 ? -20.144 -3.107  16.303  1.00 20.91 ? 308 ARG A NE   1 
ATOM   4381 C CZ   . ARG A 1 289 ? -20.558 -2.912  17.541  1.00 21.90 ? 308 ARG A CZ   1 
ATOM   4382 N NH1  . ARG A 1 289 ? -21.837 -3.025  17.867  1.00 22.21 ? 308 ARG A NH1  1 
ATOM   4383 N NH2  . ARG A 1 289 ? -19.667 -2.583  18.477  1.00 23.66 ? 308 ARG A NH2  1 
ATOM   4384 H H    . ARG A 1 289 ? -21.536 -1.499  11.756  1.00 17.63 ? 308 ARG A H    1 
ATOM   4385 H HA   . ARG A 1 289 ? -19.551 -3.161  11.383  1.00 18.27 ? 308 ARG A HA   1 
ATOM   4386 H HB2  . ARG A 1 289 ? -21.986 -3.473  12.778  1.00 19.49 ? 308 ARG A HB2  1 
ATOM   4387 H HB3  . ARG A 1 289 ? -20.898 -4.630  12.749  1.00 19.49 ? 308 ARG A HB3  1 
ATOM   4388 H HG2  . ARG A 1 289 ? -19.424 -3.335  13.907  1.00 21.88 ? 308 ARG A HG2  1 
ATOM   4389 H HG3  . ARG A 1 289 ? -20.408 -2.090  13.831  1.00 21.88 ? 308 ARG A HG3  1 
ATOM   4390 H HD2  . ARG A 1 289 ? -21.853 -3.047  15.285  1.00 23.97 ? 308 ARG A HD2  1 
ATOM   4391 H HD3  . ARG A 1 289 ? -21.108 -4.447  15.190  1.00 23.97 ? 308 ARG A HD3  1 
ATOM   4392 H HE   . ARG A 1 289 ? -19.305 -3.002  16.145  1.00 25.10 ? 308 ARG A HE   1 
ATOM   4393 H HH11 . ARG A 1 289 ? -22.417 -3.229  17.266  1.00 26.66 ? 308 ARG A HH11 1 
ATOM   4394 H HH12 . ARG A 1 289 ? -22.087 -2.895  18.679  1.00 26.66 ? 308 ARG A HH12 1 
ATOM   4395 H HH21 . ARG A 1 289 ? -18.836 -2.501  18.269  1.00 28.40 ? 308 ARG A HH21 1 
ATOM   4396 H HH22 . ARG A 1 289 ? -19.922 -2.454  19.288  1.00 28.40 ? 308 ARG A HH22 1 
ATOM   4397 N N    . ARG A 1 290 ? -22.217 -3.856  9.747   1.00 16.04 ? 309 ARG A N    1 
ATOM   4398 C CA   . ARG A 1 290 ? -22.667 -4.655  8.607   1.00 16.40 ? 309 ARG A CA   1 
ATOM   4399 C C    . ARG A 1 290 ? -21.798 -4.397  7.387   1.00 15.31 ? 309 ARG A C    1 
ATOM   4400 O O    . ARG A 1 290 ? -21.364 -5.339  6.711   1.00 16.25 ? 309 ARG A O    1 
ATOM   4401 C CB   . ARG A 1 290 ? -24.126 -4.348  8.275   1.00 19.05 ? 309 ARG A CB   1 
ATOM   4402 C CG   . ARG A 1 290 ? -25.127 -4.894  9.276   1.00 23.87 ? 309 ARG A CG   1 
ATOM   4403 C CD   . ARG A 1 290 ? -26.556 -4.538  8.873   1.00 27.48 ? 309 ARG A CD   1 
ATOM   4404 N NE   . ARG A 1 290 ? -27.540 -4.866  9.900   1.00 32.01 ? 309 ARG A NE   1 
ATOM   4405 C CZ   . ARG A 1 290 ? -28.259 -3.963  10.557  1.00 34.95 ? 309 ARG A CZ   1 
ATOM   4406 N NH1  . ARG A 1 290 ? -28.083 -2.663  10.365  1.00 36.47 ? 309 ARG A NH1  1 
ATOM   4407 N NH2  . ARG A 1 290 ? -29.170 -4.372  11.433  1.00 34.96 ? 309 ARG A NH2  1 
ATOM   4408 H H    . ARG A 1 290 ? -22.787 -3.283  10.042  1.00 19.25 ? 309 ARG A H    1 
ATOM   4409 H HA   . ARG A 1 290 ? -22.603 -5.592  8.848   1.00 19.68 ? 309 ARG A HA   1 
ATOM   4410 H HB2  . ARG A 1 290 ? -24.239 -3.386  8.242   1.00 22.87 ? 309 ARG A HB2  1 
ATOM   4411 H HB3  . ARG A 1 290 ? -24.334 -4.737  7.411   1.00 22.87 ? 309 ARG A HB3  1 
ATOM   4412 H HG2  . ARG A 1 290 ? -25.051 -5.860  9.314   1.00 28.65 ? 309 ARG A HG2  1 
ATOM   4413 H HG3  . ARG A 1 290 ? -24.950 -4.512  10.150  1.00 28.65 ? 309 ARG A HG3  1 
ATOM   4414 H HD2  . ARG A 1 290 ? -26.607 -3.584  8.705   1.00 32.99 ? 309 ARG A HD2  1 
ATOM   4415 H HD3  . ARG A 1 290 ? -26.788 -5.030  8.070   1.00 32.99 ? 309 ARG A HD3  1 
ATOM   4416 H HE   . ARG A 1 290 ? -27.663 -5.696  10.091  1.00 38.41 ? 309 ARG A HE   1 
ATOM   4417 H HH11 . ARG A 1 290 ? -27.493 -2.387  9.804   1.00 43.77 ? 309 ARG A HH11 1 
ATOM   4418 H HH12 . ARG A 1 290 ? -28.560 -2.096  10.801  1.00 43.77 ? 309 ARG A HH12 1 
ATOM   4419 H HH21 . ARG A 1 290 ? -29.289 -5.212  11.569  1.00 41.96 ? 309 ARG A HH21 1 
ATOM   4420 H HH22 . ARG A 1 290 ? -29.641 -3.795  11.864  1.00 41.96 ? 309 ARG A HH22 1 
ATOM   4421 N N    . VAL A 1 291 ? -21.499 -3.125  7.117   1.00 14.61 ? 310 VAL A N    1 
ATOM   4422 C CA   . VAL A 1 291 ? -20.613 -2.796  6.011   1.00 14.51 ? 310 VAL A CA   1 
ATOM   4423 C C    . VAL A 1 291 ? -19.241 -3.422  6.228   1.00 13.80 ? 310 VAL A C    1 
ATOM   4424 O O    . VAL A 1 291 ? -18.655 -4.001  5.303   1.00 13.75 ? 310 VAL A O    1 
ATOM   4425 C CB   . VAL A 1 291 ? -20.527 -1.269  5.833   1.00 14.16 ? 310 VAL A CB   1 
ATOM   4426 C CG1  . VAL A 1 291 ? -19.471 -0.935  4.792   1.00 14.61 ? 310 VAL A CG1  1 
ATOM   4427 C CG2  . VAL A 1 291 ? -21.870 -0.666  5.435   1.00 14.71 ? 310 VAL A CG2  1 
ATOM   4428 H H    . VAL A 1 291 ? -21.794 -2.446  7.554   1.00 17.53 ? 310 VAL A H    1 
ATOM   4429 H HA   . VAL A 1 291 ? -20.981 -3.169  5.194   1.00 17.41 ? 310 VAL A HA   1 
ATOM   4430 H HB   . VAL A 1 291 ? -20.279 -0.875  6.684   1.00 17.00 ? 310 VAL A HB   1 
ATOM   4431 H HG11 . VAL A 1 291 ? -19.520 0.011   4.585   1.00 17.54 ? 310 VAL A HG11 1 
ATOM   4432 H HG12 . VAL A 1 291 ? -18.596 -1.151  5.150   1.00 17.54 ? 310 VAL A HG12 1 
ATOM   4433 H HG13 . VAL A 1 291 ? -19.640 -1.457  3.993   1.00 17.54 ? 310 VAL A HG13 1 
ATOM   4434 H HG21 . VAL A 1 291 ? -21.789 0.300   5.412   1.00 17.65 ? 310 VAL A HG21 1 
ATOM   4435 H HG22 . VAL A 1 291 ? -22.118 -0.998  4.557   1.00 17.65 ? 310 VAL A HG22 1 
ATOM   4436 H HG23 . VAL A 1 291 ? -22.539 -0.927  6.087   1.00 17.65 ? 310 VAL A HG23 1 
ATOM   4437 N N    . ALA A 1 292 ? -18.709 -3.319  7.453   1.00 12.78 ? 311 ALA A N    1 
ATOM   4438 C CA   . ALA A 1 292 ? -17.391 -3.878  7.729   1.00 12.49 ? 311 ALA A CA   1 
ATOM   4439 C C    . ALA A 1 292 ? -17.370 -5.392  7.539   1.00 13.98 ? 311 ALA A C    1 
ATOM   4440 O O    . ALA A 1 292 ? -16.395 -5.939  7.018   1.00 13.94 ? 311 ALA A O    1 
ATOM   4441 C CB   . ALA A 1 292 ? -16.959 -3.489  9.142   1.00 13.01 ? 311 ALA A CB   1 
ATOM   4442 H H    . ALA A 1 292 ? -19.086 -2.937  8.125   1.00 15.34 ? 311 ALA A H    1 
ATOM   4443 H HA   . ALA A 1 292 ? -16.750 -3.504  7.104   1.00 15.00 ? 311 ALA A HA   1 
ATOM   4444 H HB1  . ALA A 1 292 ? -16.059 -3.817  9.298   1.00 15.61 ? 311 ALA A HB1  1 
ATOM   4445 H HB2  . ALA A 1 292 ? -16.978 -2.523  9.224   1.00 15.61 ? 311 ALA A HB2  1 
ATOM   4446 H HB3  . ALA A 1 292 ? -17.571 -3.887  9.781   1.00 15.61 ? 311 ALA A HB3  1 
ATOM   4447 N N    A LYS A 1 293 ? -18.427 -6.092  7.961   0.45 15.03 ? 312 LYS A N    1 
ATOM   4448 N N    B LYS A 1 293 ? -18.425 -6.092  7.958   0.55 14.48 ? 312 LYS A N    1 
ATOM   4449 C CA   A LYS A 1 293 ? -18.475 -7.538  7.749   0.45 16.56 ? 312 LYS A CA   1 
ATOM   4450 C CA   B LYS A 1 293 ? -18.456 -7.536  7.751   0.55 15.61 ? 312 LYS A CA   1 
ATOM   4451 C C    A LYS A 1 293 ? -18.459 -7.863  6.264   0.45 16.14 ? 312 LYS A C    1 
ATOM   4452 C C    B LYS A 1 293 ? -18.457 -7.867  6.264   0.55 15.63 ? 312 LYS A C    1 
ATOM   4453 O O    A LYS A 1 293 ? -17.717 -8.749  5.823   0.45 16.97 ? 312 LYS A O    1 
ATOM   4454 O O    B LYS A 1 293 ? -17.727 -8.762  5.821   0.55 16.66 ? 312 LYS A O    1 
ATOM   4455 C CB   A LYS A 1 293 ? -19.718 -8.126  8.422   0.45 18.52 ? 312 LYS A CB   1 
ATOM   4456 C CB   B LYS A 1 293 ? -19.685 -8.143  8.423   0.55 16.79 ? 312 LYS A CB   1 
ATOM   4457 C CG   A LYS A 1 293 ? -20.192 -9.486  7.895   0.45 20.70 ? 312 LYS A CG   1 
ATOM   4458 C CG   B LYS A 1 293 ? -19.578 -8.286  9.938   0.55 18.21 ? 312 LYS A CG   1 
ATOM   4459 C CD   A LYS A 1 293 ? -21.571 -9.820  8.469   0.45 22.32 ? 312 LYS A CD   1 
ATOM   4460 C CD   B LYS A 1 293 ? -20.780 -9.054  10.486  0.55 20.47 ? 312 LYS A CD   1 
ATOM   4461 C CE   A LYS A 1 293 ? -21.999 -11.234 8.127   0.45 23.33 ? 312 LYS A CE   1 
ATOM   4462 C CE   B LYS A 1 293 ? -20.982 -8.828  11.983  0.55 22.57 ? 312 LYS A CE   1 
ATOM   4463 N NZ   A LYS A 1 293 ? -21.294 -12.222 8.976   0.45 23.66 ? 312 LYS A NZ   1 
ATOM   4464 N NZ   B LYS A 1 293 ? -22.228 -9.483  12.483  0.55 24.85 ? 312 LYS A NZ   1 
ATOM   4465 H H    A LYS A 1 293 ? -19.113 -5.762  8.362   0.45 18.04 ? 312 LYS A H    1 
ATOM   4466 H H    B LYS A 1 293 ? -19.115 -5.763  8.353   0.55 17.39 ? 312 LYS A H    1 
ATOM   4467 H HA   A LYS A 1 293 ? -17.696 -7.947  8.158   0.45 19.88 ? 312 LYS A HA   1 
ATOM   4468 H HA   B LYS A 1 293 ? -17.668 -7.926  8.159   0.55 18.74 ? 312 LYS A HA   1 
ATOM   4469 H HB2  A LYS A 1 293 ? -19.526 -8.237  9.366   0.45 22.23 ? 312 LYS A HB2  1 
ATOM   4470 H HB2  B LYS A 1 293 ? -20.450 -7.577  8.237   0.55 20.16 ? 312 LYS A HB2  1 
ATOM   4471 H HB3  A LYS A 1 293 ? -20.450 -7.502  8.302   0.45 22.23 ? 312 LYS A HB3  1 
ATOM   4472 H HB3  B LYS A 1 293 ? -19.830 -9.029  8.056   0.55 20.16 ? 312 LYS A HB3  1 
ATOM   4473 H HG2  A LYS A 1 293 ? -20.256 -9.457  6.928   0.45 24.84 ? 312 LYS A HG2  1 
ATOM   4474 H HG2  B LYS A 1 293 ? -18.770 -8.773  10.163  0.55 21.86 ? 312 LYS A HG2  1 
ATOM   4475 H HG3  A LYS A 1 293 ? -19.567 -10.177 8.165   0.45 24.84 ? 312 LYS A HG3  1 
ATOM   4476 H HG3  B LYS A 1 293 ? -19.560 -7.406  10.347  0.55 21.86 ? 312 LYS A HG3  1 
ATOM   4477 H HD2  A LYS A 1 293 ? -21.545 -9.736  9.435   0.45 26.80 ? 312 LYS A HD2  1 
ATOM   4478 H HD2  B LYS A 1 293 ? -21.581 -8.761  10.026  0.55 24.57 ? 312 LYS A HD2  1 
ATOM   4479 H HD3  A LYS A 1 293 ? -22.228 -9.208  8.101   0.45 26.80 ? 312 LYS A HD3  1 
ATOM   4480 H HD3  B LYS A 1 293 ? -20.643 -10.004 10.341  0.55 24.57 ? 312 LYS A HD3  1 
ATOM   4481 H HE2  A LYS A 1 293 ? -22.953 -11.328 8.274   0.45 28.00 ? 312 LYS A HE2  1 
ATOM   4482 H HE2  B LYS A 1 293 ? -20.228 -9.201  12.467  0.55 27.09 ? 312 LYS A HE2  1 
ATOM   4483 H HE3  A LYS A 1 293 ? -21.786 -11.420 7.199   0.45 28.00 ? 312 LYS A HE3  1 
ATOM   4484 H HE3  B LYS A 1 293 ? -21.049 -7.876  12.156  0.55 27.09 ? 312 LYS A HE3  1 
ATOM   4485 H HZ1  A LYS A 1 293 ? -21.466 -12.063 9.835   0.45 28.40 ? 312 LYS A HZ1  1 
ATOM   4486 H HZ1  B LYS A 1 293 ? -22.201 -10.357 12.317  0.55 29.83 ? 312 LYS A HZ1  1 
ATOM   4487 H HZ2  A LYS A 1 293 ? -20.416 -12.167 8.843   0.45 28.40 ? 312 LYS A HZ2  1 
ATOM   4488 H HZ2  B LYS A 1 293 ? -22.939 -9.134  12.077  0.55 29.83 ? 312 LYS A HZ2  1 
ATOM   4489 H HZ3  A LYS A 1 293 ? -21.566 -13.045 8.775   0.45 28.40 ? 312 LYS A HZ3  1 
ATOM   4490 H HZ3  B LYS A 1 293 ? -22.306 -9.358  13.361  0.55 29.83 ? 312 LYS A HZ3  1 
ATOM   4491 N N    . ASP A 1 294 ? -19.260 -7.140  5.474   1.00 15.68 ? 313 ASP A N    1 
ATOM   4492 C CA   . ASP A 1 294 ? -19.361 -7.446  4.051   1.00 18.22 ? 313 ASP A CA   1 
ATOM   4493 C C    . ASP A 1 294 ? -18.081 -7.085  3.315   1.00 17.66 ? 313 ASP A C    1 
ATOM   4494 O O    . ASP A 1 294 ? -17.772 -7.671  2.271   1.00 19.71 ? 313 ASP A O    1 
ATOM   4495 C CB   . ASP A 1 294 ? -20.527 -6.689  3.405   1.00 20.99 ? 313 ASP A CB   1 
ATOM   4496 C CG   . ASP A 1 294 ? -21.881 -7.229  3.804   1.00 25.48 ? 313 ASP A CG   1 
ATOM   4497 O OD1  . ASP A 1 294 ? -21.950 -8.353  4.346   1.00 27.49 ? 313 ASP A OD1  1 
ATOM   4498 O OD2  . ASP A 1 294 ? -22.876 -6.512  3.562   1.00 27.06 ? 313 ASP A OD2  1 
ATOM   4499 H H    . ASP A 1 294 ? -19.744 -6.480  5.739   1.00 18.83 ? 313 ASP A H    1 
ATOM   4500 H HA   . ASP A 1 294 ? -19.529 -8.398  3.966   1.00 21.87 ? 313 ASP A HA   1 
ATOM   4501 H HB2  . ASP A 1 294 ? -20.486 -5.758  3.676   1.00 25.19 ? 313 ASP A HB2  1 
ATOM   4502 H HB3  . ASP A 1 294 ? -20.451 -6.758  2.441   1.00 25.19 ? 313 ASP A HB3  1 
ATOM   4503 N N    . SER A 1 295 ? -17.319 -6.140  3.846   1.00 15.42 ? 314 SER A N    1 
ATOM   4504 C CA   . SER A 1 295 ? -16.171 -5.585  3.155   1.00 14.42 ? 314 SER A CA   1 
ATOM   4505 C C    . SER A 1 295 ? -14.865 -6.285  3.512   1.00 12.91 ? 314 SER A C    1 
ATOM   4506 O O    . SER A 1 295 ? -13.821 -5.933  2.966   1.00 13.82 ? 314 SER A O    1 
ATOM   4507 C CB   . SER A 1 295 ? -16.058 -4.094  3.503   1.00 13.89 ? 314 SER A CB   1 
ATOM   4508 O OG   . SER A 1 295 ? -17.191 -3.361  3.077   1.00 15.32 ? 314 SER A OG   1 
ATOM   4509 H H    . SER A 1 295 ? -17.451 -5.797  4.624   1.00 18.51 ? 314 SER A H    1 
ATOM   4510 H HA   . SER A 1 295 ? -16.299 -5.678  2.198   1.00 17.32 ? 314 SER A HA   1 
ATOM   4511 H HB2  . SER A 1 295 ? -15.974 -4.005  4.465   1.00 16.68 ? 314 SER A HB2  1 
ATOM   4512 H HB3  . SER A 1 295 ? -15.271 -3.732  3.066   1.00 16.68 ? 314 SER A HB3  1 
ATOM   4513 H HG   . SER A 1 295 ? -17.860 -3.571  3.540   1.00 18.39 ? 314 SER A HG   1 
ATOM   4514 N N    . LEU A 1 296 ? -14.894 -7.278  4.395   1.00 12.95 ? 315 LEU A N    1 
ATOM   4515 C CA   . LEU A 1 296 ? -13.661 -7.879  4.894   1.00 12.64 ? 315 LEU A CA   1 
ATOM   4516 C C    . LEU A 1 296 ? -13.000 -8.801  3.884   1.00 13.54 ? 315 LEU A C    1 
ATOM   4517 O O    . LEU A 1 296 ? -11.768 -8.795  3.746   1.00 12.95 ? 315 LEU A O    1 
ATOM   4518 C CB   . LEU A 1 296 ? -13.952 -8.654  6.169   1.00 13.88 ? 315 LEU A CB   1 
ATOM   4519 C CG   . LEU A 1 296 ? -12.810 -9.548  6.694   1.00 13.71 ? 315 LEU A CG   1 
ATOM   4520 C CD1  . LEU A 1 296 ? -11.629 -8.660  7.064   1.00 13.66 ? 315 LEU A CD1  1 
ATOM   4521 C CD2  . LEU A 1 296 ? -13.285 -10.399 7.842   1.00 15.32 ? 315 LEU A CD2  1 
ATOM   4522 H H    . LEU A 1 296 ? -15.612 -7.621  4.721   1.00 15.54 ? 315 LEU A H    1 
ATOM   4523 H HA   . LEU A 1 296 ? -13.038 -7.160  5.085   1.00 15.18 ? 315 LEU A HA   1 
ATOM   4524 H HB2  . LEU A 1 296 ? -14.163 -8.016  6.869   1.00 16.67 ? 315 LEU A HB2  1 
ATOM   4525 H HB3  . LEU A 1 296 ? -14.715 -9.230  6.004   1.00 16.67 ? 315 LEU A HB3  1 
ATOM   4526 H HG   . LEU A 1 296 ? -12.514 -10.171 6.012   1.00 16.46 ? 315 LEU A HG   1 
ATOM   4527 H HD11 . LEU A 1 296 ? -10.906 -9.217  7.395   1.00 16.40 ? 315 LEU A HD11 1 
ATOM   4528 H HD12 . LEU A 1 296 ? -11.338 -8.176  6.275   1.00 16.40 ? 315 LEU A HD12 1 
ATOM   4529 H HD13 . LEU A 1 296 ? -11.906 -8.035  7.752   1.00 16.40 ? 315 LEU A HD13 1 
ATOM   4530 H HD21 . LEU A 1 296 ? -12.541 -10.928 8.172   1.00 18.40 ? 315 LEU A HD21 1 
ATOM   4531 H HD22 . LEU A 1 296 ? -13.618 -9.822  8.547   1.00 18.40 ? 315 LEU A HD22 1 
ATOM   4532 H HD23 . LEU A 1 296 ? -13.994 -10.984 7.531   1.00 18.40 ? 315 LEU A HD23 1 
ATOM   4533 N N    . LYS A 1 297 ? -13.787 -9.628  3.201   1.00 14.07 ? 316 LYS A N    1 
ATOM   4534 C CA   . LYS A 1 297 ? -13.194 -10.716 2.426   1.00 14.06 ? 316 LYS A CA   1 
ATOM   4535 C C    . LYS A 1 297 ? -12.215 -10.209 1.376   1.00 14.41 ? 316 LYS A C    1 
ATOM   4536 O O    . LYS A 1 297 ? -11.150 -10.805 1.176   1.00 14.51 ? 316 LYS A O    1 
ATOM   4537 C CB   . LYS A 1 297 ? -14.302 -11.539 1.764   1.00 17.42 ? 316 LYS A CB   1 
ATOM   4538 C CG   . LYS A 1 297 ? -13.787 -12.752 1.006   1.00 21.17 ? 316 LYS A CG   1 
ATOM   4539 C CD   . LYS A 1 297 ? -14.768 -13.930 0.985   1.00 25.96 ? 316 LYS A CD   1 
ATOM   4540 C CE   . LYS A 1 297 ? -16.189 -13.519 0.663   1.00 29.99 ? 316 LYS A CE   1 
ATOM   4541 N NZ   . LYS A 1 297 ? -16.329 -12.832 -0.669  1.00 32.59 ? 316 LYS A NZ   1 
ATOM   4542 H H    . LYS A 1 297 ? -14.645 -9.583  3.169   1.00 16.89 ? 316 LYS A H    1 
ATOM   4543 H HA   . LYS A 1 297 ? -12.699 -11.288 3.033   1.00 16.88 ? 316 LYS A HA   1 
ATOM   4544 H HB2  . LYS A 1 297 ? -14.910 -11.855 2.451   1.00 20.91 ? 316 LYS A HB2  1 
ATOM   4545 H HB3  . LYS A 1 297 ? -14.777 -10.975 1.134   1.00 20.91 ? 316 LYS A HB3  1 
ATOM   4546 H HG2  . LYS A 1 297 ? -13.615 -12.495 0.086   1.00 25.42 ? 316 LYS A HG2  1 
ATOM   4547 H HG3  . LYS A 1 297 ? -12.967 -13.057 1.424   1.00 25.42 ? 316 LYS A HG3  1 
ATOM   4548 H HD2  . LYS A 1 297 ? -14.482 -14.566 0.311   1.00 31.16 ? 316 LYS A HD2  1 
ATOM   4549 H HD3  . LYS A 1 297 ? -14.771 -14.352 1.859   1.00 31.16 ? 316 LYS A HD3  1 
ATOM   4550 H HE2  . LYS A 1 297 ? -16.748 -14.312 0.648   1.00 36.00 ? 316 LYS A HE2  1 
ATOM   4551 H HE3  . LYS A 1 297 ? -16.501 -12.906 1.347   1.00 36.00 ? 316 LYS A HE3  1 
ATOM   4552 H HZ1  . LYS A 1 297 ? -17.169 -12.562 -0.786  1.00 39.11 ? 316 LYS A HZ1  1 
ATOM   4553 H HZ2  . LYS A 1 297 ? -15.790 -12.124 -0.705  1.00 39.11 ? 316 LYS A HZ2  1 
ATOM   4554 H HZ3  . LYS A 1 297 ? -16.112 -13.393 -1.326  1.00 39.11 ? 316 LYS A HZ3  1 
ATOM   4555 N N    . PHE A 1 298 ? -12.555 -9.125  0.675   1.00 14.37 ? 317 PHE A N    1 
ATOM   4556 C CA   . PHE A 1 298 ? -11.669 -8.654  -0.390  1.00 14.36 ? 317 PHE A CA   1 
ATOM   4557 C C    . PHE A 1 298 ? -10.285 -8.248  0.125   1.00 13.11 ? 317 PHE A C    1 
ATOM   4558 O O    . PHE A 1 298 ? -9.282  -8.832  -0.320  1.00 13.65 ? 317 PHE A O    1 
ATOM   4559 C CB   . PHE A 1 298 ? -12.320 -7.553  -1.223  1.00 14.53 ? 317 PHE A CB   1 
ATOM   4560 C CG   . PHE A 1 298 ? -11.425 -7.049  -2.296  1.00 15.44 ? 317 PHE A CG   1 
ATOM   4561 C CD1  . PHE A 1 298 ? -11.143 -7.829  -3.408  1.00 15.80 ? 317 PHE A CD1  1 
ATOM   4562 C CD2  . PHE A 1 298 ? -10.777 -5.840  -2.145  1.00 15.95 ? 317 PHE A CD2  1 
ATOM   4563 C CE1  . PHE A 1 298 ? -10.274 -7.380  -4.382  1.00 16.74 ? 317 PHE A CE1  1 
ATOM   4564 C CE2  . PHE A 1 298 ? -9.912  -5.374  -3.127  1.00 16.88 ? 317 PHE A CE2  1 
ATOM   4565 C CZ   . PHE A 1 298 ? -9.659  -6.146  -4.242  1.00 16.84 ? 317 PHE A CZ   1 
ATOM   4566 H H    . PHE A 1 298 ? -13.270 -8.661  0.792   1.00 17.25 ? 317 PHE A H    1 
ATOM   4567 H HA   . PHE A 1 298 ? -11.553 -9.412  -0.984  1.00 17.24 ? 317 PHE A HA   1 
ATOM   4568 H HB2  . PHE A 1 298 ? -13.122 -7.904  -1.640  1.00 17.44 ? 317 PHE A HB2  1 
ATOM   4569 H HB3  . PHE A 1 298 ? -12.546 -6.809  -0.643  1.00 17.44 ? 317 PHE A HB3  1 
ATOM   4570 H HD1  . PHE A 1 298 ? -11.544 -8.663  -3.499  1.00 18.97 ? 317 PHE A HD1  1 
ATOM   4571 H HD2  . PHE A 1 298 ? -10.921 -5.333  -1.379  1.00 19.14 ? 317 PHE A HD2  1 
ATOM   4572 H HE1  . PHE A 1 298 ? -10.102 -7.905  -5.131  1.00 20.09 ? 317 PHE A HE1  1 
ATOM   4573 H HE2  . PHE A 1 298 ? -9.505  -4.543  -3.033  1.00 20.26 ? 317 PHE A HE2  1 
ATOM   4574 H HZ   . PHE A 1 298 ? -9.076  -5.839  -4.898  1.00 20.22 ? 317 PHE A HZ   1 
ATOM   4575 N N    . PRO A 1 299 ? -10.146 -7.284  1.035   1.00 12.60 ? 318 PRO A N    1 
ATOM   4576 C CA   . PRO A 1 299 ? -8.794  -6.933  1.505   1.00 12.86 ? 318 PRO A CA   1 
ATOM   4577 C C    . PRO A 1 299 ? -8.118  -8.068  2.254   1.00 12.78 ? 318 PRO A C    1 
ATOM   4578 O O    . PRO A 1 299 ? -6.888  -8.195  2.180   1.00 12.28 ? 318 PRO A O    1 
ATOM   4579 C CB   . PRO A 1 299 ? -9.025  -5.692  2.392   1.00 13.18 ? 318 PRO A CB   1 
ATOM   4580 C CG   . PRO A 1 299 ? -10.459 -5.786  2.820   1.00 13.19 ? 318 PRO A CG   1 
ATOM   4581 C CD   . PRO A 1 299 ? -11.185 -6.433  1.630   1.00 12.68 ? 318 PRO A CD   1 
ATOM   4582 H HA   . PRO A 1 299 ? -8.236  -6.667  0.758   1.00 15.44 ? 318 PRO A HA   1 
ATOM   4583 H HB2  . PRO A 1 299 ? -8.432  -5.718  3.159   1.00 15.82 ? 318 PRO A HB2  1 
ATOM   4584 H HB3  . PRO A 1 299 ? -8.868  -4.884  1.878   1.00 15.82 ? 318 PRO A HB3  1 
ATOM   4585 H HG2  . PRO A 1 299 ? -10.532 -6.338  3.613   1.00 15.83 ? 318 PRO A HG2  1 
ATOM   4586 H HG3  . PRO A 1 299 ? -10.809 -4.899  2.999   1.00 15.83 ? 318 PRO A HG3  1 
ATOM   4587 H HD2  . PRO A 1 299 ? -11.939 -6.965  1.931   1.00 15.22 ? 318 PRO A HD2  1 
ATOM   4588 H HD3  . PRO A 1 299 ? -11.486 -5.760  0.999   1.00 15.22 ? 318 PRO A HD3  1 
ATOM   4589 N N    . LEU A 1 300 ? -8.873  -8.887  2.993   1.00 11.89 ? 319 LEU A N    1 
ATOM   4590 C CA   . LEU A 1 300 ? -8.251  -10.020 3.670   1.00 12.24 ? 319 LEU A CA   1 
ATOM   4591 C C    . LEU A 1 300 ? -7.657  -10.990 2.663   1.00 12.30 ? 319 LEU A C    1 
ATOM   4592 O O    . LEU A 1 300 ? -6.550  -11.499 2.854   1.00 13.61 ? 319 LEU A O    1 
ATOM   4593 C CB   . LEU A 1 300 ? -9.264  -10.722 4.561   1.00 12.68 ? 319 LEU A CB   1 
ATOM   4594 C CG   . LEU A 1 300 ? -8.723  -11.963 5.253   1.00 13.18 ? 319 LEU A CG   1 
ATOM   4595 C CD1  . LEU A 1 300 ? -7.546  -11.657 6.157   1.00 13.23 ? 319 LEU A CD1  1 
ATOM   4596 C CD2  . LEU A 1 300 ? -9.831  -12.642 6.066   1.00 13.83 ? 319 LEU A CD2  1 
ATOM   4597 H H    . LEU A 1 300 ? -9.721  -8.808  3.114   1.00 14.27 ? 319 LEU A H    1 
ATOM   4598 H HA   . LEU A 1 300 ? -7.535  -9.695  4.237   1.00 14.69 ? 319 LEU A HA   1 
ATOM   4599 H HB2  . LEU A 1 300 ? -9.553  -10.102 5.249   1.00 15.22 ? 319 LEU A HB2  1 
ATOM   4600 H HB3  . LEU A 1 300 ? -10.021 -10.992 4.018   1.00 15.22 ? 319 LEU A HB3  1 
ATOM   4601 H HG   . LEU A 1 300 ? -8.407  -12.566 4.562   1.00 15.82 ? 319 LEU A HG   1 
ATOM   4602 H HD11 . LEU A 1 300 ? -7.232  -12.483 6.557   1.00 15.88 ? 319 LEU A HD11 1 
ATOM   4603 H HD12 . LEU A 1 300 ? -6.838  -11.255 5.630   1.00 15.88 ? 319 LEU A HD12 1 
ATOM   4604 H HD13 . LEU A 1 300 ? -7.832  -11.042 6.851   1.00 15.88 ? 319 LEU A HD13 1 
ATOM   4605 H HD21 . LEU A 1 300 ? -9.455  -13.399 6.542   1.00 16.60 ? 319 LEU A HD21 1 
ATOM   4606 H HD22 . LEU A 1 300 ? -10.196 -12.003 6.698   1.00 16.60 ? 319 LEU A HD22 1 
ATOM   4607 H HD23 . LEU A 1 300 ? -10.527 -12.944 5.461   1.00 16.60 ? 319 LEU A HD23 1 
ATOM   4608 N N    . ALA A 1 301 ? -8.394  -11.277 1.590   1.00 12.40 ? 320 ALA A N    1 
ATOM   4609 C CA   . ALA A 1 301 ? -7.865  -12.147 0.550   1.00 13.20 ? 320 ALA A CA   1 
ATOM   4610 C C    . ALA A 1 301 ? -6.649  -11.531 -0.138  1.00 12.76 ? 320 ALA A C    1 
ATOM   4611 O O    . ALA A 1 301 ? -5.700  -12.241 -0.472  1.00 14.04 ? 320 ALA A O    1 
ATOM   4612 C CB   . ALA A 1 301 ? -8.945  -12.461 -0.481  1.00 14.81 ? 320 ALA A CB   1 
ATOM   4613 H H    . ALA A 1 301 ? -9.190  -10.984 1.444   1.00 14.89 ? 320 ALA A H    1 
ATOM   4614 H HA   . ALA A 1 301 ? -7.588  -12.979 0.966   1.00 15.84 ? 320 ALA A HA   1 
ATOM   4615 H HB1  . ALA A 1 301 ? -8.579  -13.061 -1.149  1.00 17.77 ? 320 ALA A HB1  1 
ATOM   4616 H HB2  . ALA A 1 301 ? -9.695  -12.882 -0.034  1.00 17.77 ? 320 ALA A HB2  1 
ATOM   4617 H HB3  . ALA A 1 301 ? -9.231  -11.634 -0.900  1.00 17.77 ? 320 ALA A HB3  1 
ATOM   4618 N N    . CYS A 1 302 ? -6.673  -10.212 -0.392  1.00 12.62 ? 321 CYS A N    1 
ATOM   4619 C CA   . CYS A 1 302 ? -5.497  -9.552  -0.954  1.00 13.14 ? 321 CYS A CA   1 
ATOM   4620 C C    . CYS A 1 302 ? -4.296  -9.730  -0.037  1.00 12.55 ? 321 CYS A C    1 
ATOM   4621 O O    . CYS A 1 302 ? -3.193  -10.069 -0.486  1.00 13.21 ? 321 CYS A O    1 
ATOM   4622 C CB   . CYS A 1 302 ? -5.767  -8.054  -1.150  1.00 13.95 ? 321 CYS A CB   1 
ATOM   4623 S SG   . CYS A 1 302 ? -6.885  -7.671  -2.493  1.00 14.44 ? 321 CYS A SG   1 
ATOM   4624 H H    . CYS A 1 302 ? -7.344  -9.694  -0.249  1.00 15.15 ? 321 CYS A H    1 
ATOM   4625 H HA   . CYS A 1 302 ? -5.307  -9.948  -1.819  1.00 15.77 ? 321 CYS A HA   1 
ATOM   4626 H HB2  . CYS A 1 302 ? -6.156  -7.701  -0.334  1.00 16.74 ? 321 CYS A HB2  1 
ATOM   4627 H HB3  . CYS A 1 302 ? -4.924  -7.610  -1.334  1.00 16.74 ? 321 CYS A HB3  1 
ATOM   4628 H HG   . CYS A 1 302 ? -7.896  -8.302  -2.351  1.00 17.33 ? 321 CYS A HG   1 
ATOM   4629 N N    . PHE A 1 303 ? -4.501  -9.499  1.259   1.00 12.07 ? 322 PHE A N    1 
ATOM   4630 C CA   . PHE A 1 303 ? -3.427  -9.664  2.226   1.00 11.70 ? 322 PHE A CA   1 
ATOM   4631 C C    . PHE A 1 303 ? -2.909  -11.093 2.222   1.00 12.20 ? 322 PHE A C    1 
ATOM   4632 O O    . PHE A 1 303 ? -1.702  -11.322 2.123   1.00 12.24 ? 322 PHE A O    1 
ATOM   4633 C CB   . PHE A 1 303 ? -3.922  -9.270  3.618   1.00 11.54 ? 322 PHE A CB   1 
ATOM   4634 C CG   . PHE A 1 303 ? -2.945  -9.598  4.700   1.00 10.29 ? 322 PHE A CG   1 
ATOM   4635 C CD1  . PHE A 1 303 ? -1.831  -8.801  4.910   1.00 10.81 ? 322 PHE A CD1  1 
ATOM   4636 C CD2  . PHE A 1 303 ? -3.104  -10.736 5.475   1.00 11.69 ? 322 PHE A CD2  1 
ATOM   4637 C CE1  . PHE A 1 303 ? -0.916  -9.128  5.873   1.00 11.28 ? 322 PHE A CE1  1 
ATOM   4638 C CE2  . PHE A 1 303 ? -2.176  -11.068 6.461   1.00 11.23 ? 322 PHE A CE2  1 
ATOM   4639 C CZ   . PHE A 1 303 ? -1.084  -10.262 6.659   1.00 11.46 ? 322 PHE A CZ   1 
ATOM   4640 H H    . PHE A 1 303 ? -5.249  -9.248  1.600   1.00 14.49 ? 322 PHE A H    1 
ATOM   4641 H HA   . PHE A 1 303 ? -2.692  -9.077  1.988   1.00 14.05 ? 322 PHE A HA   1 
ATOM   4642 H HB2  . PHE A 1 303 ? -4.079  -8.313  3.637   1.00 13.86 ? 322 PHE A HB2  1 
ATOM   4643 H HB3  . PHE A 1 303 ? -4.746  -9.745  3.805   1.00 13.86 ? 322 PHE A HB3  1 
ATOM   4644 H HD1  . PHE A 1 303 ? -1.704  -8.038  4.394   1.00 12.98 ? 322 PHE A HD1  1 
ATOM   4645 H HD2  . PHE A 1 303 ? -3.840  -11.287 5.335   1.00 14.03 ? 322 PHE A HD2  1 
ATOM   4646 H HE1  . PHE A 1 303 ? -0.173  -8.585  6.003   1.00 13.55 ? 322 PHE A HE1  1 
ATOM   4647 H HE2  . PHE A 1 303 ? -2.296  -11.829 6.980   1.00 13.49 ? 322 PHE A HE2  1 
ATOM   4648 H HZ   . PHE A 1 303 ? -0.460  -10.472 7.316   1.00 13.76 ? 322 PHE A HZ   1 
ATOM   4649 N N    . LEU A 1 304 ? -3.813  -12.075 2.329   1.00 11.57 ? 323 LEU A N    1 
ATOM   4650 C CA   . LEU A 1 304 ? -3.365  -13.474 2.390   1.00 11.87 ? 323 LEU A CA   1 
ATOM   4651 C C    . LEU A 1 304 ? -2.738  -13.925 1.074   1.00 13.03 ? 323 LEU A C    1 
ATOM   4652 O O    . LEU A 1 304 ? -1.870  -14.805 1.065   1.00 13.70 ? 323 LEU A O    1 
ATOM   4653 C CB   . LEU A 1 304 ? -4.521  -14.403 2.770   1.00 12.84 ? 323 LEU A CB   1 
ATOM   4654 C CG   . LEU A 1 304 ? -5.040  -14.215 4.206   1.00 13.03 ? 323 LEU A CG   1 
ATOM   4655 C CD1  . LEU A 1 304 ? -6.271  -15.106 4.425   1.00 14.04 ? 323 LEU A CD1  1 
ATOM   4656 C CD2  . LEU A 1 304 ? -3.949  -14.488 5.253   1.00 13.56 ? 323 LEU A CD2  1 
ATOM   4657 H H    . LEU A 1 304 ? -4.665  -11.963 2.367   1.00 13.89 ? 323 LEU A H    1 
ATOM   4658 H HA   . LEU A 1 304 ? -2.694  -13.544 3.086   1.00 14.25 ? 323 LEU A HA   1 
ATOM   4659 H HB2  . LEU A 1 304 ? -5.261  -14.238 2.166   1.00 15.42 ? 323 LEU A HB2  1 
ATOM   4660 H HB3  . LEU A 1 304 ? -4.220  -15.321 2.684   1.00 15.42 ? 323 LEU A HB3  1 
ATOM   4661 H HG   . LEU A 1 304 ? -5.303  -13.290 4.330   1.00 15.65 ? 323 LEU A HG   1 
ATOM   4662 H HD11 . LEU A 1 304 ? -6.523  -15.071 5.361   1.00 16.85 ? 323 LEU A HD11 1 
ATOM   4663 H HD12 . LEU A 1 304 ? -7.000  -14.779 3.874   1.00 16.85 ? 323 LEU A HD12 1 
ATOM   4664 H HD13 . LEU A 1 304 ? -6.050  -16.017 4.175   1.00 16.85 ? 323 LEU A HD13 1 
ATOM   4665 H HD21 . LEU A 1 304 ? -4.352  -14.496 6.135   1.00 16.28 ? 323 LEU A HD21 1 
ATOM   4666 H HD22 . LEU A 1 304 ? -3.541  -15.349 5.068   1.00 16.28 ? 323 LEU A HD22 1 
ATOM   4667 H HD23 . LEU A 1 304 ? -3.279  -13.788 5.202   1.00 16.28 ? 323 LEU A HD23 1 
ATOM   4668 N N    . ALA A 1 305 ? -3.161  -13.340 -0.050  1.00 13.06 ? 324 ALA A N    1 
ATOM   4669 C CA   . ALA A 1 305 ? -2.565  -13.739 -1.321  1.00 14.01 ? 324 ALA A CA   1 
ATOM   4670 C C    . ALA A 1 305 ? -1.058  -13.515 -1.304  1.00 13.32 ? 324 ALA A C    1 
ATOM   4671 O O    . ALA A 1 305 ? -0.285  -14.382 -1.740  1.00 14.47 ? 324 ALA A O    1 
ATOM   4672 C CB   . ALA A 1 305 ? -3.220  -13.006 -2.492  1.00 15.11 ? 324 ALA A CB   1 
ATOM   4673 H H    . ALA A 1 305 ? -3.768  -12.733 -0.100  1.00 15.68 ? 324 ALA A H    1 
ATOM   4674 H HA   . ALA A 1 305 ? -2.732  -14.685 -1.457  1.00 16.82 ? 324 ALA A HA   1 
ATOM   4675 H HB1  . ALA A 1 305 ? -2.850  -13.345 -3.323  1.00 18.14 ? 324 ALA A HB1  1 
ATOM   4676 H HB2  . ALA A 1 305 ? -4.177  -13.164 -2.469  1.00 18.14 ? 324 ALA A HB2  1 
ATOM   4677 H HB3  . ALA A 1 305 ? -3.038  -12.057 -2.412  1.00 18.14 ? 324 ALA A HB3  1 
ATOM   4678 N N    . GLY A 1 306 ? -0.620  -12.368 -0.786  1.00 12.98 ? 325 GLY A N    1 
ATOM   4679 C CA   . GLY A 1 306 ? 0.777   -11.987 -0.850  1.00 12.97 ? 325 GLY A CA   1 
ATOM   4680 C C    . GLY A 1 306 ? 1.550   -12.132 0.442   1.00 12.96 ? 325 GLY A C    1 
ATOM   4681 O O    . GLY A 1 306 ? 2.758   -11.907 0.458   1.00 12.92 ? 325 GLY A O    1 
ATOM   4682 H H    . GLY A 1 306 ? -1.121  -11.792 -0.390  1.00 15.58 ? 325 GLY A H    1 
ATOM   4683 H HA2  . GLY A 1 306 ? 1.217   -12.536 -1.518  1.00 15.57 ? 325 GLY A HA2  1 
ATOM   4684 H HA3  . GLY A 1 306 ? 0.832   -11.057 -1.120  1.00 15.57 ? 325 GLY A HA3  1 
ATOM   4685 N N    . ALA A 1 307 ? 0.867   -12.442 1.543   1.00 12.26 ? 326 ALA A N    1 
ATOM   4686 C CA   . ALA A 1 307 ? 1.501   -12.376 2.858   1.00 12.64 ? 326 ALA A CA   1 
ATOM   4687 C C    . ALA A 1 307 ? 2.647   -13.356 3.000   1.00 13.02 ? 326 ALA A C    1 
ATOM   4688 O O    . ALA A 1 307 ? 2.607   -14.459 2.469   1.00 13.98 ? 326 ALA A O    1 
ATOM   4689 C CB   . ALA A 1 307 ? 0.480   -12.654 3.951   1.00 13.10 ? 326 ALA A CB   1 
ATOM   4690 H H    . ALA A 1 307 ? 0.044   -12.690 1.556   1.00 14.72 ? 326 ALA A H    1 
ATOM   4691 H HA   . ALA A 1 307 ? 1.861   -11.482 2.966   1.00 15.17 ? 326 ALA A HA   1 
ATOM   4692 H HB1  . ALA A 1 307 ? 0.939   -12.721 4.803   1.00 15.73 ? 326 ALA A HB1  1 
ATOM   4693 H HB2  . ALA A 1 307 ? -0.161  -11.926 3.977   1.00 15.73 ? 326 ALA A HB2  1 
ATOM   4694 H HB3  . ALA A 1 307 ? 0.025   -13.488 3.754   1.00 15.73 ? 326 ALA A HB3  1 
ATOM   4695 N N    . GLN A 1 308 ? 3.680   -12.931 3.722   1.00 12.83 ? 327 GLN A N    1 
ATOM   4696 C CA   . GLN A 1 308 ? 4.814   -13.764 4.061   1.00 12.83 ? 327 GLN A CA   1 
ATOM   4697 C C    . GLN A 1 308 ? 5.038   -13.666 5.563   1.00 12.72 ? 327 GLN A C    1 
ATOM   4698 O O    . GLN A 1 308 ? 4.306   -12.992 6.286   1.00 12.38 ? 327 GLN A O    1 
ATOM   4699 C CB   . GLN A 1 308 ? 6.085   -13.321 3.310   1.00 14.30 ? 327 GLN A CB   1 
ATOM   4700 C CG   . GLN A 1 308 ? 5.866   -12.973 1.865   1.00 15.12 ? 327 GLN A CG   1 
ATOM   4701 C CD   . GLN A 1 308 ? 5.670   -14.207 1.005   1.00 15.33 ? 327 GLN A CD   1 
ATOM   4702 O OE1  . GLN A 1 308 ? 6.351   -15.224 1.177   1.00 17.79 ? 327 GLN A OE1  1 
ATOM   4703 N NE2  . GLN A 1 308 ? 4.735   -14.122 0.072   1.00 15.72 ? 327 GLN A NE2  1 
ATOM   4704 H H    . GLN A 1 308 ? 3.743   -12.133 4.035   1.00 15.40 ? 327 GLN A H    1 
ATOM   4705 H HA   . GLN A 1 308 ? 4.620   -14.682 3.818   1.00 15.40 ? 327 GLN A HA   1 
ATOM   4706 H HB2  . GLN A 1 308 ? 6.445   -12.535 3.749   1.00 17.16 ? 327 GLN A HB2  1 
ATOM   4707 H HB3  . GLN A 1 308 ? 6.730   -14.045 3.342   1.00 17.16 ? 327 GLN A HB3  1 
ATOM   4708 H HG2  . GLN A 1 308 ? 5.072   -12.421 1.787   1.00 18.15 ? 327 GLN A HG2  1 
ATOM   4709 H HG3  . GLN A 1 308 ? 6.639   -12.492 1.532   1.00 18.15 ? 327 GLN A HG3  1 
ATOM   4710 H HE21 . GLN A 1 308 ? 4.281   -13.396 -0.017  1.00 18.87 ? 327 GLN A HE21 1 
ATOM   4711 H HE22 . GLN A 1 308 ? 4.580   -14.791 -0.445  1.00 18.87 ? 327 GLN A HE22 1 
ATOM   4712 N N    . GLU A 1 309 ? 6.060   -14.343 6.054   1.00 12.63 ? 328 GLU A N    1 
ATOM   4713 C CA   . GLU A 1 309 ? 6.395   -14.200 7.456   1.00 13.19 ? 328 GLU A CA   1 
ATOM   4714 C C    . GLU A 1 309 ? 6.588   -12.723 7.766   1.00 12.06 ? 328 GLU A C    1 
ATOM   4715 O O    . GLU A 1 309 ? 7.050   -11.943 6.930   1.00 13.13 ? 328 GLU A O    1 
ATOM   4716 C CB   . GLU A 1 309 ? 7.646   -15.005 7.771   1.00 17.31 ? 328 GLU A CB   1 
ATOM   4717 C CG   . GLU A 1 309 ? 7.991   -15.004 9.223   1.00 23.71 ? 328 GLU A CG   1 
ATOM   4718 C CD   . GLU A 1 309 ? 8.963   -16.109 9.602   1.00 28.36 ? 328 GLU A CD   1 
ATOM   4719 O OE1  . GLU A 1 309 ? 9.177   -17.032 8.785   1.00 30.61 ? 328 GLU A OE1  1 
ATOM   4720 O OE2  . GLU A 1 309 ? 9.480   -16.072 10.746  1.00 29.51 ? 328 GLU A OE2  1 
ATOM   4721 H H    . GLU A 1 309 ? 6.563   -14.879 5.608   1.00 15.16 ? 328 GLU A H    1 
ATOM   4722 H HA   . GLU A 1 309 ? 5.687   -14.543 8.023   1.00 15.83 ? 328 GLU A HA   1 
ATOM   4723 H HB2  . GLU A 1 309 ? 7.506   -15.925 7.497   1.00 20.77 ? 328 GLU A HB2  1 
ATOM   4724 H HB3  . GLU A 1 309 ? 8.395   -14.625 7.285   1.00 20.77 ? 328 GLU A HB3  1 
ATOM   4725 H HG2  . GLU A 1 309 ? 8.401   -14.155 9.449   1.00 28.46 ? 328 GLU A HG2  1 
ATOM   4726 H HG3  . GLU A 1 309 ? 7.180   -15.129 9.740   1.00 28.46 ? 328 GLU A HG3  1 
ATOM   4727 N N    . ASN A 1 310 ? 6.163   -12.331 8.960   1.00 11.14 ? 329 ASN A N    1 
ATOM   4728 C CA   . ASN A 1 310 ? 6.298   -10.960 9.454   1.00 10.83 ? 329 ASN A CA   1 
ATOM   4729 C C    . ASN A 1 310 ? 5.402   -9.952  8.737   1.00 10.87 ? 329 ASN A C    1 
ATOM   4730 O O    . ASN A 1 310 ? 5.672   -8.743  8.784   1.00 11.47 ? 329 ASN A O    1 
ATOM   4731 C CB   . ASN A 1 310 ? 7.757   -10.488 9.442   1.00 11.37 ? 329 ASN A CB   1 
ATOM   4732 C CG   . ASN A 1 310 ? 8.671   -11.443 10.169  1.00 11.79 ? 329 ASN A CG   1 
ATOM   4733 O OD1  . ASN A 1 310 ? 8.411   -11.807 11.312  1.00 12.35 ? 329 ASN A OD1  1 
ATOM   4734 N ND2  . ASN A 1 310 ? 9.715   -11.877 9.501   1.00 13.11 ? 329 ASN A ND2  1 
ATOM   4735 H H    . ASN A 1 310 ? 5.780   -12.857 9.522   1.00 13.38 ? 329 ASN A H    1 
ATOM   4736 H HA   . ASN A 1 310 ? 6.003   -10.967 10.378  1.00 13.01 ? 329 ASN A HA   1 
ATOM   4737 H HB2  . ASN A 1 310 ? 8.061   -10.417 8.524   1.00 13.66 ? 329 ASN A HB2  1 
ATOM   4738 H HB3  . ASN A 1 310 ? 7.815   -9.623  9.878   1.00 13.66 ? 329 ASN A HB3  1 
ATOM   4739 H HD21 . ASN A 1 310 ? 9.848   -11.616 8.693   1.00 15.74 ? 329 ASN A HD21 1 
ATOM   4740 H HD22 . ASN A 1 310 ? 10.266  -12.424 9.873   1.00 15.74 ? 329 ASN A HD22 1 
ATOM   4741 N N    . CYS A 1 311 ? 4.323   -10.425 8.113   1.00 10.78 ? 330 CYS A N    1 
ATOM   4742 C CA   . CYS A 1 311 ? 3.289   -9.568  7.547   1.00 10.56 ? 330 CYS A CA   1 
ATOM   4743 C C    . CYS A 1 311 ? 2.065   -9.567  8.449   1.00 10.87 ? 330 CYS A C    1 
ATOM   4744 O O    . CYS A 1 311 ? 1.642   -10.623 8.930   1.00 11.76 ? 330 CYS A O    1 
ATOM   4745 C CB   . CYS A 1 311 ? 2.904   -10.077 6.163   1.00 11.45 ? 330 CYS A CB   1 
ATOM   4746 S SG   . CYS A 1 311 ? 4.219   -9.810  4.959   1.00 12.53 ? 330 CYS A SG   1 
ATOM   4747 H H    . CYS A 1 311 ? 4.166   -11.263 8.004   1.00 12.94 ? 330 CYS A H    1 
ATOM   4748 H HA   . CYS A 1 311 ? 3.609   -8.655  7.478   1.00 12.68 ? 330 CYS A HA   1 
ATOM   4749 H HB2  . CYS A 1 311 ? 2.725   -11.029 6.212   1.00 13.75 ? 330 CYS A HB2  1 
ATOM   4750 H HB3  . CYS A 1 311 ? 2.113   -9.606  5.859   1.00 13.75 ? 330 CYS A HB3  1 
ATOM   4751 H HG   . CYS A 1 311 ? 3.825   -10.132 3.873   1.00 15.04 ? 330 CYS A HG   1 
ATOM   4752 N N    . TYR A 1 312 ? 1.503   -8.375  8.676   1.00 10.41 ? 331 TYR A N    1 
ATOM   4753 C CA   . TYR A 1 312 ? 0.389   -8.207  9.603   1.00 10.10 ? 331 TYR A CA   1 
ATOM   4754 C C    . TYR A 1 312 ? -0.737  -7.443  8.927   1.00 10.15 ? 331 TYR A C    1 
ATOM   4755 O O    . TYR A 1 312 ? -0.498  -6.506  8.162   1.00 11.12 ? 331 TYR A O    1 
ATOM   4756 C CB   . TYR A 1 312 ? 0.828   -7.428  10.857  1.00 10.53 ? 331 TYR A CB   1 
ATOM   4757 C CG   . TYR A 1 312 ? 1.849   -8.182  11.652  1.00 10.64 ? 331 TYR A CG   1 
ATOM   4758 C CD1  . TYR A 1 312 ? 3.194   -8.059  11.388  1.00 10.55 ? 331 TYR A CD1  1 
ATOM   4759 C CD2  . TYR A 1 312 ? 1.459   -9.055  12.639  1.00 11.64 ? 331 TYR A CD2  1 
ATOM   4760 C CE1  . TYR A 1 312 ? 4.144   -8.783  12.104  1.00 9.96  ? 331 TYR A CE1  1 
ATOM   4761 C CE2  . TYR A 1 312 ? 2.368   -9.774  13.359  1.00 11.96 ? 331 TYR A CE2  1 
ATOM   4762 C CZ   . TYR A 1 312 ? 3.723   -9.651  13.087  1.00 11.84 ? 331 TYR A CZ   1 
ATOM   4763 O OH   . TYR A 1 312 ? 4.613   -10.413 13.820  1.00 12.96 ? 331 TYR A OH   1 
ATOM   4764 H H    . TYR A 1 312 ? 1.755   -7.644  8.299   1.00 12.50 ? 331 TYR A H    1 
ATOM   4765 H HA   . TYR A 1 312 ? 0.059   -9.081  9.863   1.00 12.13 ? 331 TYR A HA   1 
ATOM   4766 H HB2  . TYR A 1 312 ? 1.218   -6.581  10.586  1.00 12.64 ? 331 TYR A HB2  1 
ATOM   4767 H HB3  . TYR A 1 312 ? 0.056   -7.272  11.423  1.00 12.64 ? 331 TYR A HB3  1 
ATOM   4768 H HD1  . TYR A 1 312 ? 3.474   -7.480  10.716  1.00 12.67 ? 331 TYR A HD1  1 
ATOM   4769 H HD2  . TYR A 1 312 ? 0.553   -9.159  12.821  1.00 13.97 ? 331 TYR A HD2  1 
ATOM   4770 H HE1  . TYR A 1 312 ? 5.050   -8.682  11.921  1.00 11.96 ? 331 TYR A HE1  1 
ATOM   4771 H HE2  . TYR A 1 312 ? 2.079   -10.347 14.032  1.00 14.35 ? 331 TYR A HE2  1 
ATOM   4772 H HH   . TYR A 1 312 ? 5.348   -10.464 13.417  1.00 15.56 ? 331 TYR A HH   1 
ATOM   4773 N N    . PHE A 1 313 ? -1.963  -7.822  9.262   1.00 10.10 ? 332 PHE A N    1 
ATOM   4774 C CA   . PHE A 1 313 ? -3.174  -7.188  8.762   1.00 10.32 ? 332 PHE A CA   1 
ATOM   4775 C C    . PHE A 1 313 ? -3.807  -6.349  9.861   1.00 10.31 ? 332 PHE A C    1 
ATOM   4776 O O    . PHE A 1 313 ? -3.884  -6.767  11.022  1.00 10.30 ? 332 PHE A O    1 
ATOM   4777 C CB   . PHE A 1 313 ? -4.148  -8.285  8.343   1.00 11.19 ? 332 PHE A CB   1 
ATOM   4778 C CG   . PHE A 1 313 ? -5.354  -7.828  7.552   1.00 10.73 ? 332 PHE A CG   1 
ATOM   4779 C CD1  . PHE A 1 313 ? -5.238  -7.081  6.392   1.00 11.10 ? 332 PHE A CD1  1 
ATOM   4780 C CD2  . PHE A 1 313 ? -6.616  -8.228  7.932   1.00 10.83 ? 332 PHE A CD2  1 
ATOM   4781 C CE1  . PHE A 1 313 ? -6.357  -6.728  5.653   1.00 12.07 ? 332 PHE A CE1  1 
ATOM   4782 C CE2  . PHE A 1 313 ? -7.740  -7.875  7.213   1.00 11.34 ? 332 PHE A CE2  1 
ATOM   4783 C CZ   . PHE A 1 313 ? -7.630  -7.143  6.070   1.00 12.21 ? 332 PHE A CZ   1 
ATOM   4784 H H    . PHE A 1 313 ? -2.126  -8.472  9.801   1.00 12.13 ? 332 PHE A H    1 
ATOM   4785 H HA   . PHE A 1 313 ? -2.979  -6.602  8.014   1.00 12.39 ? 332 PHE A HA   1 
ATOM   4786 H HB2  . PHE A 1 313 ? -3.669  -8.924  7.793   1.00 13.44 ? 332 PHE A HB2  1 
ATOM   4787 H HB3  . PHE A 1 313 ? -4.479  -8.720  9.145   1.00 13.44 ? 332 PHE A HB3  1 
ATOM   4788 H HD1  . PHE A 1 313 ? -4.396  -6.812  6.103   1.00 13.32 ? 332 PHE A HD1  1 
ATOM   4789 H HD2  . PHE A 1 313 ? -6.714  -8.751  8.695   1.00 13.00 ? 332 PHE A HD2  1 
ATOM   4790 H HE1  . PHE A 1 313 ? -6.264  -6.217  4.882   1.00 14.49 ? 332 PHE A HE1  1 
ATOM   4791 H HE2  . PHE A 1 313 ? -8.581  -8.139  7.512   1.00 13.61 ? 332 PHE A HE2  1 
ATOM   4792 H HZ   . PHE A 1 313 ? -8.385  -6.922  5.574   1.00 14.66 ? 332 PHE A HZ   1 
ATOM   4793 N N    . ILE A 1 314 ? -4.255  -5.152  9.481   1.00 11.23 ? 333 ILE A N    1 
ATOM   4794 C CA   . ILE A 1 314 ? -5.074  -4.294  10.337  1.00 11.22 ? 333 ILE A CA   1 
ATOM   4795 C C    . ILE A 1 314 ? -6.364  -4.027  9.584   1.00 11.01 ? 333 ILE A C    1 
ATOM   4796 O O    . ILE A 1 314 ? -6.337  -3.795  8.377   1.00 12.73 ? 333 ILE A O    1 
ATOM   4797 C CB   . ILE A 1 314 ? -4.328  -2.980  10.678  1.00 11.11 ? 333 ILE A CB   1 
ATOM   4798 C CG1  . ILE A 1 314 ? -2.980  -3.321  11.301  1.00 12.58 ? 333 ILE A CG1  1 
ATOM   4799 C CG2  . ILE A 1 314 ? -5.212  -2.091  11.565  1.00 12.40 ? 333 ILE A CG2  1 
ATOM   4800 C CD1  . ILE A 1 314 ? -2.258  -2.129  11.805  1.00 13.32 ? 333 ILE A CD1  1 
ATOM   4801 H H    . ILE A 1 314 ? -4.093  -4.806  8.710   1.00 13.48 ? 333 ILE A H    1 
ATOM   4802 H HA   . ILE A 1 314 ? -5.287  -4.734  11.174  1.00 13.47 ? 333 ILE A HA   1 
ATOM   4803 H HB   . ILE A 1 314 ? -4.149  -2.467  9.875   1.00 13.34 ? 333 ILE A HB   1 
ATOM   4804 H HG12 . ILE A 1 314 ? -3.121  -3.924  12.048  1.00 15.10 ? 333 ILE A HG12 1 
ATOM   4805 H HG13 . ILE A 1 314 ? -2.422  -3.749  10.632  1.00 15.10 ? 333 ILE A HG13 1 
ATOM   4806 H HG21 . ILE A 1 314 ? -4.811  -1.210  11.628  1.00 14.88 ? 333 ILE A HG21 1 
ATOM   4807 H HG22 . ILE A 1 314 ? -6.094  -2.025  11.167  1.00 14.88 ? 333 ILE A HG22 1 
ATOM   4808 H HG23 . ILE A 1 314 ? -5.275  -2.489  12.447  1.00 14.88 ? 333 ILE A HG23 1 
ATOM   4809 H HD11 . ILE A 1 314 ? -1.346  -2.380  12.022  1.00 15.99 ? 333 ILE A HD11 1 
ATOM   4810 H HD12 . ILE A 1 314 ? -2.257  -1.446  11.116  1.00 15.99 ? 333 ILE A HD12 1 
ATOM   4811 H HD13 . ILE A 1 314 ? -2.708  -1.799  12.598  1.00 15.99 ? 333 ILE A HD13 1 
ATOM   4812 N N    . TYR A 1 315 ? -7.499  -4.084  10.267  1.00 10.72 ? 334 TYR A N    1 
ATOM   4813 C CA   . TYR A 1 315 ? -8.776  -3.928  9.579   1.00 11.05 ? 334 TYR A CA   1 
ATOM   4814 C C    . TYR A 1 315 ? -9.783  -3.158  10.413  1.00 10.80 ? 334 TYR A C    1 
ATOM   4815 O O    . TYR A 1 315 ? -10.224 -3.628  11.458  1.00 12.51 ? 334 TYR A O    1 
ATOM   4816 C CB   . TYR A 1 315 ? -9.364  -5.294  9.209   1.00 11.39 ? 334 TYR A CB   1 
ATOM   4817 C CG   . TYR A 1 315 ? -10.642 -5.206  8.395   1.00 11.52 ? 334 TYR A CG   1 
ATOM   4818 C CD1  . TYR A 1 315 ? -10.607 -4.829  7.069   1.00 11.28 ? 334 TYR A CD1  1 
ATOM   4819 C CD2  . TYR A 1 315 ? -11.872 -5.468  8.972   1.00 11.93 ? 334 TYR A CD2  1 
ATOM   4820 C CE1  . TYR A 1 315 ? -11.766 -4.745  6.323   1.00 11.60 ? 334 TYR A CE1  1 
ATOM   4821 C CE2  . TYR A 1 315 ? -13.043 -5.378  8.235   1.00 12.08 ? 334 TYR A CE2  1 
ATOM   4822 C CZ   . TYR A 1 315 ? -12.979 -5.009  6.920   1.00 12.01 ? 334 TYR A CZ   1 
ATOM   4823 O OH   . TYR A 1 315 ? -14.116 -4.906  6.162   1.00 13.28 ? 334 TYR A OH   1 
ATOM   4824 H H    . TYR A 1 315 ? -7.556  -4.209  11.115  1.00 12.87 ? 334 TYR A H    1 
ATOM   4825 H HA   . TYR A 1 315 ? -8.609  -3.398  8.784   1.00 13.27 ? 334 TYR A HA   1 
ATOM   4826 H HB2  . TYR A 1 315 ? -8.711  -5.783  8.684   1.00 13.68 ? 334 TYR A HB2  1 
ATOM   4827 H HB3  . TYR A 1 315 ? -9.564  -5.780  10.024  1.00 13.68 ? 334 TYR A HB3  1 
ATOM   4828 H HD1  . TYR A 1 315 ? -9.790  -4.630  6.671   1.00 13.54 ? 334 TYR A HD1  1 
ATOM   4829 H HD2  . TYR A 1 315 ? -11.913 -5.710  9.869   1.00 14.32 ? 334 TYR A HD2  1 
ATOM   4830 H HE1  . TYR A 1 315 ? -11.728 -4.511  5.424   1.00 13.92 ? 334 TYR A HE1  1 
ATOM   4831 H HE2  . TYR A 1 315 ? -13.863 -5.565  8.632   1.00 14.50 ? 334 TYR A HE2  1 
ATOM   4832 H HH   . TYR A 1 315 ? -14.788 -4.831  6.660   1.00 15.94 ? 334 TYR A HH   1 
ATOM   4833 N N    . ASN A 1 316 ? -10.169 -1.985  9.914   1.00 10.68 ? 335 ASN A N    1 
ATOM   4834 C CA   . ASN A 1 316 ? -11.087 -1.082  10.602  1.00 10.55 ? 335 ASN A CA   1 
ATOM   4835 C C    . ASN A 1 316 ? -11.347 0.125   9.699   1.00 11.46 ? 335 ASN A C    1 
ATOM   4836 O O    . ASN A 1 316 ? -11.003 0.095   8.513   1.00 11.45 ? 335 ASN A O    1 
ATOM   4837 C CB   . ASN A 1 316 ? -10.475 -0.672  11.918  1.00 11.14 ? 335 ASN A CB   1 
ATOM   4838 C CG   . ASN A 1 316 ? -9.133  -0.032  11.712  1.00 11.12 ? 335 ASN A CG   1 
ATOM   4839 O OD1  . ASN A 1 316 ? -9.006  0.885   10.902  1.00 11.41 ? 335 ASN A OD1  1 
ATOM   4840 N ND2  . ASN A 1 316 ? -8.114  -0.550  12.376  1.00 11.25 ? 335 ASN A ND2  1 
ATOM   4841 H H    . ASN A 1 316 ? -9.904  -1.679  9.154   1.00 12.83 ? 335 ASN A H    1 
ATOM   4842 H HA   . ASN A 1 316 ? -11.937 -1.507  10.795  1.00 12.67 ? 335 ASN A HA   1 
ATOM   4843 H HB2  . ASN A 1 316 ? -11.056 -0.032  12.358  1.00 13.38 ? 335 ASN A HB2  1 
ATOM   4844 H HB3  . ASN A 1 316 ? -10.360 -1.455  12.478  1.00 13.38 ? 335 ASN A HB3  1 
ATOM   4845 H HD21 . ASN A 1 316 ? -7.328  -0.214  12.287  1.00 13.50 ? 335 ASN A HD21 1 
ATOM   4846 H HD22 . ASN A 1 316 ? -8.238  -1.223  12.896  1.00 13.50 ? 335 ASN A HD22 1 
ATOM   4847 N N    . TRP A 1 317 ? -11.989 1.172   10.226  1.00 10.64 ? 336 TRP A N    1 
ATOM   4848 C CA   . TRP A 1 317 ? -12.274 2.364   9.439   1.00 11.12 ? 336 TRP A CA   1 
ATOM   4849 C C    . TRP A 1 317 ? -11.610 3.628   9.987   1.00 11.29 ? 336 TRP A C    1 
ATOM   4850 O O    . TRP A 1 317 ? -12.006 4.730   9.610   1.00 11.95 ? 336 TRP A O    1 
ATOM   4851 C CB   . TRP A 1 317 ? -13.781 2.565   9.217   1.00 11.56 ? 336 TRP A CB   1 
ATOM   4852 C CG   . TRP A 1 317 ? -14.641 2.623   10.464  1.00 11.57 ? 336 TRP A CG   1 
ATOM   4853 C CD1  . TRP A 1 317 ? -14.953 3.745   11.184  1.00 12.43 ? 336 TRP A CD1  1 
ATOM   4854 C CD2  . TRP A 1 317 ? -15.337 1.532   11.104  1.00 11.78 ? 336 TRP A CD2  1 
ATOM   4855 N NE1  . TRP A 1 317 ? -15.796 3.422   12.228  1.00 12.85 ? 336 TRP A NE1  1 
ATOM   4856 C CE2  . TRP A 1 317 ? -16.044 2.078   12.200  1.00 12.09 ? 336 TRP A CE2  1 
ATOM   4857 C CE3  . TRP A 1 317 ? -15.452 0.159   10.846  1.00 12.31 ? 336 TRP A CE3  1 
ATOM   4858 C CZ2  . TRP A 1 317 ? -16.841 1.308   13.037  1.00 13.59 ? 336 TRP A CZ2  1 
ATOM   4859 C CZ3  . TRP A 1 317 ? -16.246 -0.607  11.693  1.00 13.04 ? 336 TRP A CZ3  1 
ATOM   4860 C CH2  . TRP A 1 317 ? -16.929 -0.033  12.770  1.00 13.69 ? 336 TRP A CH2  1 
ATOM   4861 H H    . TRP A 1 317 ? -12.268 1.211   11.039  1.00 12.78 ? 336 TRP A H    1 
ATOM   4862 H HA   . TRP A 1 317 ? -11.890 2.218   8.561   1.00 13.35 ? 336 TRP A HA   1 
ATOM   4863 H HB2  . TRP A 1 317 ? -13.907 3.402   8.743   1.00 13.88 ? 336 TRP A HB2  1 
ATOM   4864 H HB3  . TRP A 1 317 ? -14.108 1.827   8.679   1.00 13.88 ? 336 TRP A HB3  1 
ATOM   4865 H HD1  . TRP A 1 317 ? -14.642 4.601   10.996  1.00 14.92 ? 336 TRP A HD1  1 
ATOM   4866 H HE1  . TRP A 1 317 ? -16.113 3.977   12.803  1.00 15.43 ? 336 TRP A HE1  1 
ATOM   4867 H HE3  . TRP A 1 317 ? -15.008 -0.231  10.127  1.00 14.77 ? 336 TRP A HE3  1 
ATOM   4868 H HZ2  . TRP A 1 317 ? -17.298 1.689   13.752  1.00 16.32 ? 336 TRP A HZ2  1 
ATOM   4869 H HZ3  . TRP A 1 317 ? -16.325 -1.521  11.540  1.00 15.66 ? 336 TRP A HZ3  1 
ATOM   4870 H HH2  . TRP A 1 317 ? -17.453 -0.573  13.316  1.00 16.44 ? 336 TRP A HH2  1 
ATOM   4871 N N    . GLY A 1 318 ? -10.594 3.522   10.838  1.00 10.73 ? 337 GLY A N    1 
ATOM   4872 C CA   . GLY A 1 318 ? -9.916  4.726   11.279  1.00 10.49 ? 337 GLY A CA   1 
ATOM   4873 C C    . GLY A 1 318 ? -8.931  4.453   12.395  1.00 11.44 ? 337 GLY A C    1 
ATOM   4874 O O    . GLY A 1 318 ? -8.630  3.305   12.698  1.00 11.60 ? 337 GLY A O    1 
ATOM   4875 H H    . GLY A 1 318 ? -10.291 2.785   11.163  1.00 12.89 ? 337 GLY A H    1 
ATOM   4876 H HA2  . GLY A 1 318 ? -9.432  5.115   10.534  1.00 12.60 ? 337 GLY A HA2  1 
ATOM   4877 H HA3  . GLY A 1 318 ? -10.570 5.366   11.600  1.00 12.60 ? 337 GLY A HA3  1 
ATOM   4878 N N    . TYR A 1 319 ? -8.429  5.542   12.989  1.00 11.79 ? 338 TYR A N    1 
ATOM   4879 C CA   . TYR A 1 319 ? -7.332  5.484   13.939  1.00 11.42 ? 338 TYR A CA   1 
ATOM   4880 C C    . TYR A 1 319 ? -7.722  5.837   15.360  1.00 11.90 ? 338 TYR A C    1 
ATOM   4881 O O    . TYR A 1 319 ? -6.883  5.696   16.260  1.00 12.46 ? 338 TYR A O    1 
ATOM   4882 C CB   . TYR A 1 319 ? -6.188  6.396   13.485  1.00 11.33 ? 338 TYR A CB   1 
ATOM   4883 C CG   . TYR A 1 319 ? -5.639  5.981   12.126  1.00 12.05 ? 338 TYR A CG   1 
ATOM   4884 C CD1  . TYR A 1 319 ? -5.049  4.740   11.954  1.00 13.54 ? 338 TYR A CD1  1 
ATOM   4885 C CD2  . TYR A 1 319 ? -5.739  6.811   11.022  1.00 12.76 ? 338 TYR A CD2  1 
ATOM   4886 C CE1  . TYR A 1 319 ? -4.574  4.336   10.730  1.00 14.04 ? 338 TYR A CE1  1 
ATOM   4887 C CE2  . TYR A 1 319 ? -5.218  6.434   9.788   1.00 13.17 ? 338 TYR A CE2  1 
ATOM   4888 C CZ   . TYR A 1 319 ? -4.653  5.180   9.647   1.00 13.98 ? 338 TYR A CZ   1 
ATOM   4889 O OH   . TYR A 1 319 ? -4.154  4.770   8.439   1.00 15.27 ? 338 TYR A OH   1 
ATOM   4890 H H    . TYR A 1 319 ? -8.718  6.340   12.850  1.00 14.15 ? 338 TYR A H    1 
ATOM   4891 H HA   . TYR A 1 319 ? -6.998  4.573   13.956  1.00 13.71 ? 338 TYR A HA   1 
ATOM   4892 H HB2  . TYR A 1 319 ? -6.514  7.307   13.416  1.00 13.60 ? 338 TYR A HB2  1 
ATOM   4893 H HB3  . TYR A 1 319 ? -5.467  6.350   14.131  1.00 13.60 ? 338 TYR A HB3  1 
ATOM   4894 H HD1  . TYR A 1 319 ? -4.973  4.167   12.683  1.00 16.26 ? 338 TYR A HD1  1 
ATOM   4895 H HD2  . TYR A 1 319 ? -6.163  7.634   11.107  1.00 15.32 ? 338 TYR A HD2  1 
ATOM   4896 H HE1  . TYR A 1 319 ? -4.199  3.490   10.633  1.00 16.86 ? 338 TYR A HE1  1 
ATOM   4897 H HE2  . TYR A 1 319 ? -5.249  7.020   9.067   1.00 15.81 ? 338 TYR A HE2  1 
ATOM   4898 H HH   . TYR A 1 319 ? -4.225  5.388   7.874   1.00 18.33 ? 338 TYR A HH   1 
ATOM   4899 N N    . ARG A 1 320 ? -8.962  6.244   15.599  1.00 11.73 ? 339 ARG A N    1 
ATOM   4900 C CA   . ARG A 1 320 ? -9.496  6.325   16.954  1.00 12.75 ? 339 ARG A CA   1 
ATOM   4901 C C    . ARG A 1 320 ? -10.014 4.939   17.330  1.00 12.53 ? 339 ARG A C    1 
ATOM   4902 O O    . ARG A 1 320 ? -10.530 4.208   16.473  1.00 13.31 ? 339 ARG A O    1 
ATOM   4903 C CB   . ARG A 1 320 ? -10.613 7.372   17.020  1.00 15.39 ? 339 ARG A CB   1 
ATOM   4904 C CG   . ARG A 1 320 ? -10.105 8.783   16.735  1.00 18.73 ? 339 ARG A CG   1 
ATOM   4905 C CD   . ARG A 1 320 ? -11.251 9.811   16.736  1.00 25.04 ? 339 ARG A CD   1 
ATOM   4906 N NE   . ARG A 1 320 ? -10.768 11.193  16.724  1.00 31.68 ? 339 ARG A NE   1 
ATOM   4907 C CZ   . ARG A 1 320 ? -10.283 11.826  15.663  1.00 36.68 ? 339 ARG A CZ   1 
ATOM   4908 N NH1  . ARG A 1 320 ? -10.213 11.241  14.477  1.00 38.48 ? 339 ARG A NH1  1 
ATOM   4909 N NH2  . ARG A 1 320 ? -9.864  13.083  15.792  1.00 38.45 ? 339 ARG A NH2  1 
ATOM   4910 H H    . ARG A 1 320 ? -9.519  6.482   14.989  1.00 14.08 ? 339 ARG A H    1 
ATOM   4911 H HA   . ARG A 1 320 ? -8.819  6.596   17.594  1.00 15.30 ? 339 ARG A HA   1 
ATOM   4912 H HB2  . ARG A 1 320 ? -11.290 7.155   16.360  1.00 18.47 ? 339 ARG A HB2  1 
ATOM   4913 H HB3  . ARG A 1 320 ? -11.003 7.365   17.909  1.00 18.47 ? 339 ARG A HB3  1 
ATOM   4914 H HG2  . ARG A 1 320 ? -9.466  9.038   17.419  1.00 22.48 ? 339 ARG A HG2  1 
ATOM   4915 H HG3  . ARG A 1 320 ? -9.682  8.801   15.862  1.00 22.48 ? 339 ARG A HG3  1 
ATOM   4916 H HD2  . ARG A 1 320 ? -11.797 9.678   15.946  1.00 30.06 ? 339 ARG A HD2  1 
ATOM   4917 H HD3  . ARG A 1 320 ? -11.786 9.687   17.535  1.00 30.06 ? 339 ARG A HD3  1 
ATOM   4918 H HE   . ARG A 1 320 ? -10.802 11.630  17.464  1.00 38.02 ? 339 ARG A HE   1 
ATOM   4919 H HH11 . ARG A 1 320 ? -10.485 10.431  14.381  1.00 46.18 ? 339 ARG A HH11 1 
ATOM   4920 H HH12 . ARG A 1 320 ? -9.894  11.671  13.804  1.00 46.18 ? 339 ARG A HH12 1 
ATOM   4921 H HH21 . ARG A 1 320 ? -9.909  13.475  16.557  1.00 46.15 ? 339 ARG A HH21 1 
ATOM   4922 H HH22 . ARG A 1 320 ? -9.547  13.503  15.112  1.00 46.15 ? 339 ARG A HH22 1 
ATOM   4923 N N    . MET A 1 321 ? -9.867  4.581   18.615  1.00 12.73 ? 340 MET A N    1 
ATOM   4924 C CA   . MET A 1 321 ? -10.351 3.283   19.065  1.00 13.22 ? 340 MET A CA   1 
ATOM   4925 C C    . MET A 1 321 ? -11.719 2.908   18.521  1.00 12.72 ? 340 MET A C    1 
ATOM   4926 O O    . MET A 1 321 ? -11.945 1.766   18.098  1.00 12.79 ? 340 MET A O    1 
ATOM   4927 C CB   . MET A 1 321 ? -10.469 3.191   20.587  1.00 13.81 ? 340 MET A CB   1 
ATOM   4928 C CG   . MET A 1 321 ? -10.565 1.754   21.103  1.00 14.86 ? 340 MET A CG   1 
ATOM   4929 S SD   . MET A 1 321 ? -10.673 1.629   22.889  1.00 16.54 ? 340 MET A SD   1 
ATOM   4930 C CE   . MET A 1 321 ? -12.184 2.470   23.256  1.00 17.16 ? 340 MET A CE   1 
ATOM   4931 H H    . MET A 1 321 ? -9.499  5.064   19.225  1.00 15.28 ? 340 MET A H    1 
ATOM   4932 H HA   . MET A 1 321 ? -9.667  2.674   18.745  1.00 15.87 ? 340 MET A HA   1 
ATOM   4933 H HB2  . MET A 1 321 ? -9.686  3.600   20.987  1.00 16.58 ? 340 MET A HB2  1 
ATOM   4934 H HB3  . MET A 1 321 ? -11.270 3.663   20.867  1.00 16.58 ? 340 MET A HB3  1 
ATOM   4935 H HG2  . MET A 1 321 ? -11.360 1.341   20.729  1.00 17.83 ? 340 MET A HG2  1 
ATOM   4936 H HG3  . MET A 1 321 ? -9.775  1.268   20.820  1.00 17.83 ? 340 MET A HG3  1 
ATOM   4937 H HE1  . MET A 1 321 ? -12.325 2.461   24.215  1.00 20.60 ? 340 MET A HE1  1 
ATOM   4938 H HE2  . MET A 1 321 ? -12.122 3.385   22.939  1.00 20.60 ? 340 MET A HE2  1 
ATOM   4939 H HE3  . MET A 1 321 ? -12.915 2.015   22.810  1.00 20.60 ? 340 MET A HE3  1 
ATOM   4940 N N    . GLU A 1 322 ? -12.665 3.852   18.611  1.00 12.87 ? 341 GLU A N    1 
ATOM   4941 C CA   . GLU A 1 322 ? -14.044 3.578   18.260  1.00 13.67 ? 341 GLU A CA   1 
ATOM   4942 C C    . GLU A 1 322 ? -14.255 3.375   16.765  1.00 13.32 ? 341 GLU A C    1 
ATOM   4943 O O    . GLU A 1 322 ? -15.359 2.993   16.366  1.00 13.77 ? 341 GLU A O    1 
ATOM   4944 C CB   . GLU A 1 322 ? -14.979 4.674   18.746  1.00 16.83 ? 341 GLU A CB   1 
ATOM   4945 C CG   . GLU A 1 322 ? -14.772 6.100   18.209  1.00 20.86 ? 341 GLU A CG   1 
ATOM   4946 C CD   . GLU A 1 322 ? -13.667 6.893   18.873  1.00 23.38 ? 341 GLU A CD   1 
ATOM   4947 O OE1  . GLU A 1 322 ? -12.937 6.331   19.739  1.00 23.27 ? 341 GLU A OE1  1 
ATOM   4948 O OE2  . GLU A 1 322 ? -13.625 8.135   18.601  1.00 25.50 ? 341 GLU A OE2  1 
ATOM   4949 H H    . GLU A 1 322 ? -12.524 4.659   18.873  1.00 15.46 ? 341 GLU A H    1 
ATOM   4950 H HA   . GLU A 1 322 ? -14.293 2.761   18.721  1.00 16.42 ? 341 GLU A HA   1 
ATOM   4951 H HB2  . GLU A 1 322 ? -15.883 4.417   18.507  1.00 20.21 ? 341 GLU A HB2  1 
ATOM   4952 H HB3  . GLU A 1 322 ? -14.893 4.727   19.711  1.00 20.21 ? 341 GLU A HB3  1 
ATOM   4953 H HG2  . GLU A 1 322 ? -14.558 6.042   17.265  1.00 25.04 ? 341 GLU A HG2  1 
ATOM   4954 H HG3  . GLU A 1 322 ? -15.597 6.595   18.333  1.00 25.04 ? 341 GLU A HG3  1 
ATOM   4955 N N    . ASN A 1 323 ? -13.236 3.615   15.931  1.00 12.05 ? 342 ASN A N    1 
ATOM   4956 C CA   . ASN A 1 323 ? -13.396 3.491   14.490  1.00 11.90 ? 342 ASN A CA   1 
ATOM   4957 C C    . ASN A 1 323 ? -13.238 2.040   14.043  1.00 11.54 ? 342 ASN A C    1 
ATOM   4958 O O    . ASN A 1 323 ? -12.531 1.756   13.069  1.00 11.44 ? 342 ASN A O    1 
ATOM   4959 C CB   . ASN A 1 323 ? -12.402 4.370   13.719  1.00 12.73 ? 342 ASN A CB   1 
ATOM   4960 C CG   . ASN A 1 323 ? -12.522 5.869   13.996  1.00 11.63 ? 342 ASN A CG   1 
ATOM   4961 O OD1  . ASN A 1 323 ? -11.520 6.588   13.923  1.00 13.04 ? 342 ASN A OD1  1 
ATOM   4962 N ND2  . ASN A 1 323 ? -13.735 6.351   14.244  1.00 13.09 ? 342 ASN A ND2  1 
ATOM   4963 H H    . ASN A 1 323 ? -12.448 3.850   16.180  1.00 14.47 ? 342 ASN A H    1 
ATOM   4964 H HA   . ASN A 1 323 ? -14.291 3.796   14.274  1.00 14.28 ? 342 ASN A HA   1 
ATOM   4965 H HB2  . ASN A 1 323 ? -11.502 4.101   13.960  1.00 15.28 ? 342 ASN A HB2  1 
ATOM   4966 H HB3  . ASN A 1 323 ? -12.545 4.237   12.769  1.00 15.28 ? 342 ASN A HB3  1 
ATOM   4967 H HD21 . ASN A 1 323 ? -14.415 5.825   14.246  1.00 15.72 ? 342 ASN A HD21 1 
ATOM   4968 H HD22 . ASN A 1 323 ? -13.840 7.190   14.404  1.00 15.72 ? 342 ASN A HD22 1 
ATOM   4969 N N    . GLY A 1 324 ? -13.894 1.116   14.732  1.00 11.54 ? 343 GLY A N    1 
ATOM   4970 C CA   . GLY A 1 324 ? -13.870 -0.271  14.319  1.00 12.26 ? 343 GLY A CA   1 
ATOM   4971 C C    . GLY A 1 324 ? -12.670 -1.044  14.798  1.00 12.67 ? 343 GLY A C    1 
ATOM   4972 O O    . GLY A 1 324 ? -12.515 -2.216  14.443  1.00 12.73 ? 343 GLY A O    1 
ATOM   4973 H H    . GLY A 1 324 ? -14.357 1.270   15.440  1.00 13.86 ? 343 GLY A H    1 
ATOM   4974 H HA2  . GLY A 1 324 ? -14.664 -0.711  14.661  1.00 14.72 ? 343 GLY A HA2  1 
ATOM   4975 H HA3  . GLY A 1 324 ? -13.881 -0.308  13.350  1.00 14.72 ? 343 GLY A HA3  1 
ATOM   4976 N N    . CYS A 1 325 ? -11.821 -0.446  15.621  1.00 11.56 ? 344 CYS A N    1 
ATOM   4977 C CA   . CYS A 1 325 ? -10.506 -1.036  15.841  1.00 10.98 ? 344 CYS A CA   1 
ATOM   4978 C C    . CYS A 1 325 ? -10.556 -2.275  16.701  1.00 11.24 ? 344 CYS A C    1 
ATOM   4979 O O    . CYS A 1 325 ? -9.663  -3.116  16.593  1.00 12.31 ? 344 CYS A O    1 
ATOM   4980 C CB   . CYS A 1 325 ? -9.599  0.001   16.476  1.00 12.02 ? 344 CYS A CB   1 
ATOM   4981 S SG   . CYS A 1 325 ? -9.201  1.363   15.338  1.00 13.57 ? 344 CYS A SG   1 
ATOM   4982 H H    . CYS A 1 325 ? -11.976 0.281   16.054  1.00 13.87 ? 344 CYS A H    1 
ATOM   4983 H HA   . CYS A 1 325 ? -10.139 -1.302  14.984  1.00 13.19 ? 344 CYS A HA   1 
ATOM   4984 H HB2  . CYS A 1 325 ? -10.043 0.377   17.253  1.00 14.43 ? 344 CYS A HB2  1 
ATOM   4985 H HB3  . CYS A 1 325 ? -8.769  -0.424  16.741  1.00 14.43 ? 344 CYS A HB3  1 
ATOM   4986 H HG   . CYS A 1 325 ? -8.880  2.326   15.979  1.00 16.29 ? 344 CYS A HG   1 
ATOM   4987 N N    . LEU A 1 326 ? -11.561 -2.392  17.569  1.00 12.24 ? 345 LEU A N    1 
ATOM   4988 C CA   . LEU A 1 326 ? -11.708 -3.544  18.450  1.00 12.53 ? 345 LEU A CA   1 
ATOM   4989 C C    . LEU A 1 326 ? -12.847 -4.459  18.007  1.00 13.46 ? 345 LEU A C    1 
ATOM   4990 O O    . LEU A 1 326 ? -13.313 -5.296  18.790  1.00 14.58 ? 345 LEU A O    1 
ATOM   4991 C CB   . LEU A 1 326 ? -11.854 -3.132  19.918  1.00 13.80 ? 345 LEU A CB   1 
ATOM   4992 C CG   . LEU A 1 326 ? -10.741 -2.212  20.421  1.00 14.94 ? 345 LEU A CG   1 
ATOM   4993 C CD1  . LEU A 1 326 ? -10.903 -1.965  21.922  1.00 16.71 ? 345 LEU A CD1  1 
ATOM   4994 C CD2  . LEU A 1 326 ? -9.352  -2.736  20.159  1.00 14.37 ? 345 LEU A CD2  1 
ATOM   4995 H H    . LEU A 1 326 ? -12.180 -1.804  17.666  1.00 14.70 ? 345 LEU A H    1 
ATOM   4996 H HA   . LEU A 1 326 ? -10.887 -4.059  18.407  1.00 15.04 ? 345 LEU A HA   1 
ATOM   4997 H HB2  . LEU A 1 326 ? -12.696 -2.663  20.026  1.00 16.57 ? 345 LEU A HB2  1 
ATOM   4998 H HB3  . LEU A 1 326 ? -11.846 -3.931  20.467  1.00 16.57 ? 345 LEU A HB3  1 
ATOM   4999 H HG   . LEU A 1 326 ? -10.825 -1.383  19.925  1.00 17.94 ? 345 LEU A HG   1 
ATOM   5000 H HD11 . LEU A 1 326 ? -10.241 -1.316  22.208  1.00 20.06 ? 345 LEU A HD11 1 
ATOM   5001 H HD12 . LEU A 1 326 ? -11.795 -1.624  22.091  1.00 20.06 ? 345 LEU A HD12 1 
ATOM   5002 H HD13 . LEU A 1 326 ? -10.773 -2.801  22.396  1.00 20.06 ? 345 LEU A HD13 1 
ATOM   5003 H HD21 . LEU A 1 326 ? -8.710  -2.166  20.609  1.00 17.25 ? 345 LEU A HD21 1 
ATOM   5004 H HD22 . LEU A 1 326 ? -9.287  -3.642  20.500  1.00 17.25 ? 345 LEU A HD22 1 
ATOM   5005 H HD23 . LEU A 1 326 ? -9.188  -2.730  19.203  1.00 17.25 ? 345 LEU A HD23 1 
ATOM   5006 N N    . GLU A 1 327 ? -13.327 -4.294  16.777  1.00 12.84 ? 346 GLU A N    1 
ATOM   5007 C CA   . GLU A 1 327 ? -14.219 -5.284  16.194  1.00 12.95 ? 346 GLU A CA   1 
ATOM   5008 C C    . GLU A 1 327 ? -13.447 -6.566  15.923  1.00 13.76 ? 346 GLU A C    1 
ATOM   5009 O O    . GLU A 1 327 ? -12.230 -6.558  15.793  1.00 16.99 ? 346 GLU A O    1 
ATOM   5010 C CB   . GLU A 1 327 ? -14.824 -4.756  14.887  1.00 13.33 ? 346 GLU A CB   1 
ATOM   5011 C CG   . GLU A 1 327 ? -15.602 -3.465  15.044  1.00 14.60 ? 346 GLU A CG   1 
ATOM   5012 C CD   . GLU A 1 327 ? -16.881 -3.614  15.825  1.00 16.94 ? 346 GLU A CD   1 
ATOM   5013 O OE1  . GLU A 1 327 ? -17.541 -4.638  15.675  1.00 18.65 ? 346 GLU A OE1  1 
ATOM   5014 O OE2  . GLU A 1 327 ? -17.235 -2.683  16.573  1.00 18.10 ? 346 GLU A OE2  1 
ATOM   5015 H H    . GLU A 1 327 ? -13.152 -3.624  16.267  1.00 15.41 ? 346 GLU A H    1 
ATOM   5016 H HA   . GLU A 1 327 ? -14.948 -5.476  16.804  1.00 15.55 ? 346 GLU A HA   1 
ATOM   5017 H HB2  . GLU A 1 327 ? -14.107 -4.593  14.256  1.00 16.00 ? 346 GLU A HB2  1 
ATOM   5018 H HB3  . GLU A 1 327 ? -15.432 -5.425  14.534  1.00 16.00 ? 346 GLU A HB3  1 
ATOM   5019 H HG2  . GLU A 1 327 ? -15.046 -2.821  15.510  1.00 17.52 ? 346 GLU A HG2  1 
ATOM   5020 H HG3  . GLU A 1 327 ? -15.831 -3.130  14.164  1.00 17.52 ? 346 GLU A HG3  1 
ATOM   5021 N N    . TRP A 1 328 ? -14.163 -7.683  15.853  1.00 13.51 ? 347 TRP A N    1 
ATOM   5022 C CA   . TRP A 1 328 ? -13.541 -8.965  15.539  1.00 13.43 ? 347 TRP A CA   1 
ATOM   5023 C C    . TRP A 1 328 ? -14.426 -9.694  14.534  1.00 14.55 ? 347 TRP A C    1 
ATOM   5024 O O    . TRP A 1 328 ? -15.606 -9.366  14.359  1.00 15.70 ? 347 TRP A O    1 
ATOM   5025 C CB   . TRP A 1 328 ? -13.329 -9.823  16.789  1.00 13.97 ? 347 TRP A CB   1 
ATOM   5026 C CG   . TRP A 1 328 ? -12.241 -10.842 16.667  1.00 13.90 ? 347 TRP A CG   1 
ATOM   5027 C CD1  . TRP A 1 328 ? -12.396 -12.195 16.635  1.00 14.48 ? 347 TRP A CD1  1 
ATOM   5028 C CD2  . TRP A 1 328 ? -10.829 -10.601 16.567  1.00 13.51 ? 347 TRP A CD2  1 
ATOM   5029 N NE1  . TRP A 1 328 ? -11.184 -12.819 16.522  1.00 15.44 ? 347 TRP A NE1  1 
ATOM   5030 C CE2  . TRP A 1 328 ? -10.202 -11.861 16.482  1.00 14.60 ? 347 TRP A CE2  1 
ATOM   5031 C CE3  . TRP A 1 328 ? -10.042 -9.453  16.548  1.00 13.51 ? 347 TRP A CE3  1 
ATOM   5032 C CZ2  . TRP A 1 328 ? -8.822  -11.997 16.394  1.00 14.86 ? 347 TRP A CZ2  1 
ATOM   5033 C CZ3  . TRP A 1 328 ? -8.678  -9.594  16.465  1.00 14.11 ? 347 TRP A CZ3  1 
ATOM   5034 C CH2  . TRP A 1 328 ? -8.078  -10.854 16.375  1.00 15.23 ? 347 TRP A CH2  1 
ATOM   5035 H H    . TRP A 1 328 ? -15.012 -7.724  15.983  1.00 16.22 ? 347 TRP A H    1 
ATOM   5036 H HA   . TRP A 1 328 ? -12.670 -8.817  15.138  1.00 16.12 ? 347 TRP A HA   1 
ATOM   5037 H HB2  . TRP A 1 328 ? -13.100 -9.239  17.529  1.00 16.77 ? 347 TRP A HB2  1 
ATOM   5038 H HB3  . TRP A 1 328 ? -14.153 -10.297 16.982  1.00 16.77 ? 347 TRP A HB3  1 
ATOM   5039 H HD1  . TRP A 1 328 ? -13.215 -12.634 16.682  1.00 17.39 ? 347 TRP A HD1  1 
ATOM   5040 H HE1  . TRP A 1 328 ? -11.058 -13.669 16.484  1.00 18.54 ? 347 TRP A HE1  1 
ATOM   5041 H HE3  . TRP A 1 328 ? -10.430 -8.609  16.592  1.00 16.22 ? 347 TRP A HE3  1 
ATOM   5042 H HZ2  . TRP A 1 328 ? -8.421  -12.835 16.349  1.00 17.84 ? 347 TRP A HZ2  1 
ATOM   5043 H HZ3  . TRP A 1 328 ? -8.141  -8.835  16.469  1.00 16.94 ? 347 TRP A HZ3  1 
ATOM   5044 H HH2  . TRP A 1 328 ? -7.153  -10.914 16.300  1.00 18.28 ? 347 TRP A HH2  1 
ATOM   5045 N N    . TYR A 1 329 ? -13.834 -10.676 13.851  1.00 13.73 ? 348 TYR A N    1 
ATOM   5046 C CA   . TYR A 1 329 ? -14.466 -11.379 12.753  1.00 14.57 ? 348 TYR A CA   1 
ATOM   5047 C C    . TYR A 1 329 ? -14.061 -12.837 12.839  1.00 14.87 ? 348 TYR A C    1 
ATOM   5048 O O    . TYR A 1 329 ? -12.915 -13.141 13.193  1.00 15.20 ? 348 TYR A O    1 
ATOM   5049 C CB   . TYR A 1 329 ? -14.005 -10.784 11.412  1.00 14.69 ? 348 TYR A CB   1 
ATOM   5050 C CG   . TYR A 1 329 ? -14.238 -9.283  11.372  1.00 14.22 ? 348 TYR A CG   1 
ATOM   5051 C CD1  . TYR A 1 329 ? -13.298 -8.382  11.870  1.00 13.79 ? 348 TYR A CD1  1 
ATOM   5052 C CD2  . TYR A 1 329 ? -15.428 -8.773  10.894  1.00 14.74 ? 348 TYR A CD2  1 
ATOM   5053 C CE1  . TYR A 1 329 ? -13.553 -7.030  11.892  1.00 13.78 ? 348 TYR A CE1  1 
ATOM   5054 C CE2  . TYR A 1 329 ? -15.672 -7.419  10.878  1.00 14.29 ? 348 TYR A CE2  1 
ATOM   5055 C CZ   . TYR A 1 329 ? -14.735 -6.550  11.380  1.00 13.82 ? 348 TYR A CZ   1 
ATOM   5056 O OH   . TYR A 1 329 ? -15.041 -5.211  11.343  1.00 14.51 ? 348 TYR A OH   1 
ATOM   5057 H H    . TYR A 1 329 ? -13.038 -10.957 14.017  1.00 16.49 ? 348 TYR A H    1 
ATOM   5058 H HA   . TYR A 1 329 ? -15.433 -11.322 12.808  1.00 17.49 ? 348 TYR A HA   1 
ATOM   5059 H HB2  . TYR A 1 329 ? -13.057 -10.951 11.295  1.00 17.63 ? 348 TYR A HB2  1 
ATOM   5060 H HB3  . TYR A 1 329 ? -14.506 -11.192 10.689  1.00 17.63 ? 348 TYR A HB3  1 
ATOM   5061 H HD1  . TYR A 1 329 ? -12.486 -8.700  12.192  1.00 16.55 ? 348 TYR A HD1  1 
ATOM   5062 H HD2  . TYR A 1 329 ? -16.078 -9.356  10.576  1.00 17.70 ? 348 TYR A HD2  1 
ATOM   5063 H HE1  . TYR A 1 329 ? -12.927 -6.443  12.251  1.00 16.55 ? 348 TYR A HE1  1 
ATOM   5064 H HE2  . TYR A 1 329 ? -16.469 -7.093  10.528  1.00 17.16 ? 348 TYR A HE2  1 
ATOM   5065 H HH   . TYR A 1 329 ? -14.496 -4.778  11.813  1.00 17.42 ? 348 TYR A HH   1 
ATOM   5066 N N    . PRO A 1 330 ? -14.970 -13.760 12.526  1.00 15.15 ? 349 PRO A N    1 
ATOM   5067 C CA   . PRO A 1 330 ? -14.632 -15.187 12.687  1.00 15.61 ? 349 PRO A CA   1 
ATOM   5068 C C    . PRO A 1 330 ? -13.473 -15.612 11.810  1.00 14.71 ? 349 PRO A C    1 
ATOM   5069 O O    . PRO A 1 330 ? -12.767 -16.571 12.143  1.00 15.39 ? 349 PRO A O    1 
ATOM   5070 C CB   . PRO A 1 330 ? -15.939 -15.915 12.332  1.00 17.63 ? 349 PRO A CB   1 
ATOM   5071 C CG   . PRO A 1 330 ? -16.775 -14.913 11.621  1.00 18.96 ? 349 PRO A CG   1 
ATOM   5072 C CD   . PRO A 1 330 ? -16.374 -13.550 12.130  1.00 16.82 ? 349 PRO A CD   1 
ATOM   5073 H HA   . PRO A 1 330 ? -14.423 -15.383 13.613  1.00 18.74 ? 349 PRO A HA   1 
ATOM   5074 H HB2  . PRO A 1 330 ? -15.747 -16.673 11.757  1.00 21.16 ? 349 PRO A HB2  1 
ATOM   5075 H HB3  . PRO A 1 330 ? -16.377 -16.216 13.143  1.00 21.16 ? 349 PRO A HB3  1 
ATOM   5076 H HG2  . PRO A 1 330 ? -16.614 -14.979 10.667  1.00 22.76 ? 349 PRO A HG2  1 
ATOM   5077 H HG3  . PRO A 1 330 ? -17.711 -15.083 11.812  1.00 22.76 ? 349 PRO A HG3  1 
ATOM   5078 H HD2  . PRO A 1 330 ? -16.442 -12.882 11.430  1.00 20.19 ? 349 PRO A HD2  1 
ATOM   5079 H HD3  . PRO A 1 330 ? -16.915 -13.289 12.891  1.00 20.19 ? 349 PRO A HD3  1 
ATOM   5080 N N    . GLU A 1 331 ? -13.249 -14.905 10.697  1.00 14.82 ? 350 GLU A N    1 
ATOM   5081 C CA   . GLU A 1 331 ? -12.116 -15.211 9.830   1.00 14.05 ? 350 GLU A CA   1 
ATOM   5082 C C    . GLU A 1 331 ? -10.793 -15.126 10.577  1.00 13.84 ? 350 GLU A C    1 
ATOM   5083 O O    . GLU A 1 331 ? -9.832  -15.812 10.207  1.00 15.62 ? 350 GLU A O    1 
ATOM   5084 C CB   . GLU A 1 331 ? -12.069 -14.214 8.670   1.00 15.70 ? 350 GLU A CB   1 
ATOM   5085 C CG   . GLU A 1 331 ? -13.074 -14.471 7.566   1.00 17.20 ? 350 GLU A CG   1 
ATOM   5086 C CD   . GLU A 1 331 ? -14.491 -13.990 7.882   1.00 19.50 ? 350 GLU A CD   1 
ATOM   5087 O OE1  . GLU A 1 331 ? -14.734 -13.393 8.965   1.00 18.35 ? 350 GLU A OE1  1 
ATOM   5088 O OE2  . GLU A 1 331 ? -15.361 -14.227 7.006   1.00 22.26 ? 350 GLU A OE2  1 
ATOM   5089 H H    . GLU A 1 331 ? -13.735 -14.250 10.427  1.00 17.79 ? 350 GLU A H    1 
ATOM   5090 H HA   . GLU A 1 331 ? -12.234 -16.111 9.488   1.00 16.86 ? 350 GLU A HA   1 
ATOM   5091 H HB2  . GLU A 1 331 ? -12.243 -13.327 9.021   1.00 18.85 ? 350 GLU A HB2  1 
ATOM   5092 H HB3  . GLU A 1 331 ? -11.185 -14.247 8.273   1.00 18.85 ? 350 GLU A HB3  1 
ATOM   5093 H HG2  . GLU A 1 331 ? -12.779 -14.010 6.765   1.00 20.65 ? 350 GLU A HG2  1 
ATOM   5094 H HG3  . GLU A 1 331 ? -13.118 -15.426 7.402   1.00 20.65 ? 350 GLU A HG3  1 
ATOM   5095 N N    . PHE A 1 332 ? -10.723 -14.318 11.635  1.00 13.46 ? 351 PHE A N    1 
ATOM   5096 C CA   . PHE A 1 332 ? -9.487  -14.163 12.392  1.00 13.33 ? 351 PHE A CA   1 
ATOM   5097 C C    . PHE A 1 332 ? -9.281  -15.271 13.424  1.00 12.48 ? 351 PHE A C    1 
ATOM   5098 O O    . PHE A 1 332 ? -8.248  -15.281 14.105  1.00 12.87 ? 351 PHE A O    1 
ATOM   5099 C CB   . PHE A 1 332 ? -9.474  -12.811 13.098  1.00 13.24 ? 351 PHE A CB   1 
ATOM   5100 C CG   . PHE A 1 332 ? -9.486  -11.600 12.174  1.00 12.92 ? 351 PHE A CG   1 
ATOM   5101 C CD1  . PHE A 1 332 ? -9.303  -11.689 10.802  1.00 12.50 ? 351 PHE A CD1  1 
ATOM   5102 C CD2  . PHE A 1 332 ? -9.693  -10.348 12.712  1.00 13.49 ? 351 PHE A CD2  1 
ATOM   5103 C CE1  . PHE A 1 332 ? -9.322  -10.542 10.008  1.00 13.07 ? 351 PHE A CE1  1 
ATOM   5104 C CE2  . PHE A 1 332 ? -9.713  -9.212  11.937  1.00 12.55 ? 351 PHE A CE2  1 
ATOM   5105 C CZ   . PHE A 1 332 ? -9.520  -9.302  10.579  1.00 12.40 ? 351 PHE A CZ   1 
ATOM   5106 H H    . PHE A 1 332 ? -11.380 -13.850 11.932  1.00 16.15 ? 351 PHE A H    1 
ATOM   5107 H HA   . PHE A 1 332 ? -8.741  -14.187 11.772  1.00 16.01 ? 351 PHE A HA   1 
ATOM   5108 H HB2  . PHE A 1 332 ? -10.260 -12.753 13.663  1.00 15.89 ? 351 PHE A HB2  1 
ATOM   5109 H HB3  . PHE A 1 332 ? -8.671  -12.755 13.639  1.00 15.89 ? 351 PHE A HB3  1 
ATOM   5110 H HD1  . PHE A 1 332 ? -9.167  -12.521 10.409  1.00 15.01 ? 351 PHE A HD1  1 
ATOM   5111 H HD2  . PHE A 1 332 ? -9.824  -10.269 13.629  1.00 16.19 ? 351 PHE A HD2  1 
ATOM   5112 H HE1  . PHE A 1 332 ? -9.201  -10.614 9.089   1.00 15.70 ? 351 PHE A HE1  1 
ATOM   5113 H HE2  . PHE A 1 332 ? -9.856  -8.382  12.332  1.00 15.07 ? 351 PHE A HE2  1 
ATOM   5114 H HZ   . PHE A 1 332 ? -9.523  -8.536  10.051  1.00 14.88 ? 351 PHE A HZ   1 
ATOM   5115 N N    . ASP A 1 333 ? -10.253 -16.182 13.572  1.00 13.45 ? 352 ASP A N    1 
ATOM   5116 C CA   . ASP A 1 333 ? -10.159 -17.288 14.508  1.00 13.65 ? 352 ASP A CA   1 
ATOM   5117 C C    . ASP A 1 333 ? -9.949  -18.626 13.828  1.00 13.96 ? 352 ASP A C    1 
ATOM   5118 O O    . ASP A 1 333 ? -9.604  -19.601 14.504  1.00 15.83 ? 352 ASP A O    1 
ATOM   5119 C CB   . ASP A 1 333 ? -11.479 -17.406 15.289  1.00 14.65 ? 352 ASP A CB   1 
ATOM   5120 C CG   . ASP A 1 333 ? -11.745 -16.209 16.168  1.00 16.03 ? 352 ASP A CG   1 
ATOM   5121 O OD1  . ASP A 1 333 ? -10.766 -15.579 16.633  1.00 15.92 ? 352 ASP A OD1  1 
ATOM   5122 O OD2  . ASP A 1 333 ? -12.942 -15.874 16.366  1.00 17.48 ? 352 ASP A OD2  1 
ATOM   5123 H H    . ASP A 1 333 ? -10.989 -16.172 13.128  1.00 16.15 ? 352 ASP A H    1 
ATOM   5124 H HA   . ASP A 1 333 ? -9.425  -17.119 15.118  1.00 16.39 ? 352 ASP A HA   1 
ATOM   5125 H HB2  . ASP A 1 333 ? -12.213 -17.485 14.660  1.00 17.59 ? 352 ASP A HB2  1 
ATOM   5126 H HB3  . ASP A 1 333 ? -11.441 -18.192 15.856  1.00 17.59 ? 352 ASP A HB3  1 
ATOM   5127 N N    . LYS A 1 334 ? -10.186 -18.704 12.535  1.00 13.99 ? 353 LYS A N    1 
ATOM   5128 C CA   . LYS A 1 334 ? -10.139 -19.986 11.843  1.00 15.56 ? 353 LYS A CA   1 
ATOM   5129 C C    . LYS A 1 334 ? -8.691  -20.435 11.647  1.00 14.92 ? 353 LYS A C    1 
ATOM   5130 O O    . LYS A 1 334 ? -7.805  -19.606 11.418  1.00 14.87 ? 353 LYS A O    1 
ATOM   5131 C CB   . LYS A 1 334 ? -10.790 -19.821 10.472  1.00 18.03 ? 353 LYS A CB   1 
ATOM   5132 C CG   . LYS A 1 334 ? -12.272 -19.546 10.547  1.00 20.24 ? 353 LYS A CG   1 
ATOM   5133 C CD   . LYS A 1 334 ? -12.885 -19.519 9.171   1.00 23.17 ? 353 LYS A CD   1 
ATOM   5134 C CE   . LYS A 1 334 ? -14.236 -18.826 9.208   1.00 25.96 ? 353 LYS A CE   1 
ATOM   5135 N NZ   . LYS A 1 334 ? -15.263 -19.791 9.705   1.00 27.57 ? 353 LYS A NZ   1 
ATOM   5136 H H    . LYS A 1 334 ? -10.376 -18.034 12.030  1.00 16.80 ? 353 LYS A H    1 
ATOM   5137 H HA   . LYS A 1 334 ? -10.602 -20.663 12.361  1.00 18.67 ? 353 LYS A HA   1 
ATOM   5138 H HB2  . LYS A 1 334 ? -10.371 -19.076 10.013  1.00 21.65 ? 353 LYS A HB2  1 
ATOM   5139 H HB3  . LYS A 1 334 ? -10.664 -20.637 9.964   1.00 21.65 ? 353 LYS A HB3  1 
ATOM   5140 H HG2  . LYS A 1 334 ? -12.705 -20.244 11.062  1.00 24.29 ? 353 LYS A HG2  1 
ATOM   5141 H HG3  . LYS A 1 334 ? -12.420 -18.683 10.966  1.00 24.29 ? 353 LYS A HG3  1 
ATOM   5142 H HD2  . LYS A 1 334 ? -12.304 -19.033 8.565   1.00 27.81 ? 353 LYS A HD2  1 
ATOM   5143 H HD3  . LYS A 1 334 ? -13.011 -20.427 8.853   1.00 27.81 ? 353 LYS A HD3  1 
ATOM   5144 H HE2  . LYS A 1 334 ? -14.202 -18.065 9.809   1.00 31.15 ? 353 LYS A HE2  1 
ATOM   5145 H HE3  . LYS A 1 334 ? -14.483 -18.534 8.317   1.00 31.15 ? 353 LYS A HE3  1 
ATOM   5146 H HZ1  . LYS A 1 334 ? -15.044 -20.076 10.519  1.00 33.10 ? 353 LYS A HZ1  1 
ATOM   5147 H HZ2  . LYS A 1 334 ? -16.060 -19.396 9.741   1.00 33.10 ? 353 LYS A HZ2  1 
ATOM   5148 H HZ3  . LYS A 1 334 ? -15.312 -20.491 9.157   1.00 33.10 ? 353 LYS A HZ3  1 
ATOM   5149 N N    . PRO A 1 335 ? -8.419  -21.738 11.719  1.00 14.91 ? 354 PRO A N    1 
ATOM   5150 C CA   . PRO A 1 335 ? -7.077  -22.218 11.375  1.00 14.54 ? 354 PRO A CA   1 
ATOM   5151 C C    . PRO A 1 335 ? -6.664  -21.721 9.999   1.00 14.62 ? 354 PRO A C    1 
ATOM   5152 O O    . PRO A 1 335 ? -7.404  -21.830 9.021   1.00 15.40 ? 354 PRO A O    1 
ATOM   5153 C CB   . PRO A 1 335 ? -7.226  -23.745 11.408  1.00 15.81 ? 354 PRO A CB   1 
ATOM   5154 C CG   . PRO A 1 335 ? -8.318  -23.978 12.428  1.00 15.79 ? 354 PRO A CG   1 
ATOM   5155 C CD   . PRO A 1 335 ? -9.293  -22.847 12.152  1.00 14.64 ? 354 PRO A CD   1 
ATOM   5156 H HA   . PRO A 1 335 ? -6.426  -21.943 12.040  1.00 17.46 ? 354 PRO A HA   1 
ATOM   5157 H HB2  . PRO A 1 335 ? -7.485  -24.075 10.533  1.00 18.98 ? 354 PRO A HB2  1 
ATOM   5158 H HB3  . PRO A 1 335 ? -6.392  -24.157 11.684  1.00 18.98 ? 354 PRO A HB3  1 
ATOM   5159 H HG2  . PRO A 1 335 ? -8.732  -24.844 12.288  1.00 18.96 ? 354 PRO A HG2  1 
ATOM   5160 H HG3  . PRO A 1 335 ? -7.958  -23.924 13.327  1.00 18.96 ? 354 PRO A HG3  1 
ATOM   5161 H HD2  . PRO A 1 335 ? -9.915  -23.091 11.448  1.00 17.57 ? 354 PRO A HD2  1 
ATOM   5162 H HD3  . PRO A 1 335 ? -9.780  -22.608 12.956  1.00 17.57 ? 354 PRO A HD3  1 
ATOM   5163 N N    . LEU A 1 336 ? -5.460  -21.170 9.930   1.00 14.39 ? 355 LEU A N    1 
ATOM   5164 C CA   . LEU A 1 336 ? -4.851  -20.743 8.676   1.00 14.19 ? 355 LEU A CA   1 
ATOM   5165 C C    . LEU A 1 336 ? -3.672  -21.645 8.337   1.00 14.50 ? 355 LEU A C    1 
ATOM   5166 O O    . LEU A 1 336 ? -3.714  -22.410 7.357   1.00 15.58 ? 355 LEU A O    1 
ATOM   5167 C CB   . LEU A 1 336 ? -4.419  -19.274 8.771   1.00 14.43 ? 355 LEU A CB   1 
ATOM   5168 C CG   . LEU A 1 336 ? -3.701  -18.683 7.555   1.00 14.26 ? 355 LEU A CG   1 
ATOM   5169 C CD1  . LEU A 1 336 ? -4.587  -18.645 6.341   1.00 14.01 ? 355 LEU A CD1  1 
ATOM   5170 C CD2  . LEU A 1 336 ? -3.200  -17.264 7.905   1.00 14.21 ? 355 LEU A CD2  1 
ATOM   5171 H H    . LEU A 1 336 ? -4.960  -21.029 10.615  1.00 17.28 ? 355 LEU A H    1 
ATOM   5172 H HA   . LEU A 1 336 ? -5.498  -20.795 7.955   1.00 17.03 ? 355 LEU A HA   1 
ATOM   5173 H HB2  . LEU A 1 336 ? -5.213  -18.737 8.919   1.00 17.32 ? 355 LEU A HB2  1 
ATOM   5174 H HB3  . LEU A 1 336 ? -3.815  -19.188 9.525   1.00 17.32 ? 355 LEU A HB3  1 
ATOM   5175 H HG   . LEU A 1 336 ? -2.947  -19.249 7.329   1.00 17.12 ? 355 LEU A HG   1 
ATOM   5176 H HD11 . LEU A 1 336 ? -4.074  -18.315 5.586   1.00 16.82 ? 355 LEU A HD11 1 
ATOM   5177 H HD12 . LEU A 1 336 ? -4.908  -19.541 6.156   1.00 16.82 ? 355 LEU A HD12 1 
ATOM   5178 H HD13 . LEU A 1 336 ? -5.336  -18.054 6.515   1.00 16.82 ? 355 LEU A HD13 1 
ATOM   5179 H HD21 . LEU A 1 336 ? -2.687  -16.917 7.158   1.00 17.06 ? 355 LEU A HD21 1 
ATOM   5180 H HD22 . LEU A 1 336 ? -3.965  -16.692 8.074   1.00 17.06 ? 355 LEU A HD22 1 
ATOM   5181 H HD23 . LEU A 1 336 ? -2.642  -17.312 8.696   1.00 17.06 ? 355 LEU A HD23 1 
ATOM   5182 N N    . GLY A 1 337 ? -2.652  -21.646 9.186   1.00 14.33 ? 356 GLY A N    1 
ATOM   5183 C CA   . GLY A 1 337 ? -1.491  -22.485 8.984   1.00 15.04 ? 356 GLY A CA   1 
ATOM   5184 C C    . GLY A 1 337 ? -0.505  -21.889 7.997   1.00 15.38 ? 356 GLY A C    1 
ATOM   5185 O O    . GLY A 1 337 ? -0.757  -20.879 7.329   1.00 15.44 ? 356 GLY A O    1 
ATOM   5186 H H    . GLY A 1 337 ? -2.612  -21.161 9.895   1.00 17.21 ? 356 GLY A H    1 
ATOM   5187 H HA2  . GLY A 1 337 ? -1.035  -22.611 9.831   1.00 18.06 ? 356 GLY A HA2  1 
ATOM   5188 H HA3  . GLY A 1 337 ? -1.775  -23.349 8.647   1.00 18.06 ? 356 GLY A HA3  1 
ATOM   5189 N N    . LYS A 1 338 ? 0.650   -22.551 7.900   1.00 16.52 ? 357 LYS A N    1 
ATOM   5190 C CA   . LYS A 1 338 ? 1.716   -22.028 7.062   1.00 18.90 ? 357 LYS A CA   1 
ATOM   5191 C C    . LYS A 1 338 ? 1.309   -22.061 5.591   1.00 17.76 ? 357 LYS A C    1 
ATOM   5192 O O    . LYS A 1 338 ? 0.541   -22.932 5.164   1.00 17.93 ? 357 LYS A O    1 
ATOM   5193 C CB   . LYS A 1 338 ? 2.992   -22.848 7.220   1.00 22.87 ? 357 LYS A CB   1 
ATOM   5194 C CG   . LYS A 1 338 ? 3.459   -23.036 8.651   1.00 27.59 ? 357 LYS A CG   1 
ATOM   5195 C CD   . LYS A 1 338 ? 4.805   -23.761 8.695   1.00 30.58 ? 357 LYS A CD   1 
ATOM   5196 C CE   . LYS A 1 338 ? 5.101   -24.274 10.100  1.00 33.38 ? 357 LYS A CE   1 
ATOM   5197 N NZ   . LYS A 1 338 ? 6.563   -24.449 10.375  1.00 35.30 ? 357 LYS A NZ   1 
ATOM   5198 H H    . LYS A 1 338 ? 0.833   -23.289 8.302   1.00 19.83 ? 357 LYS A H    1 
ATOM   5199 H HA   . LYS A 1 338 ? 1.893   -21.113 7.329   1.00 22.69 ? 357 LYS A HA   1 
ATOM   5200 H HB2  . LYS A 1 338 ? 2.839   -23.730 6.845   1.00 27.45 ? 357 LYS A HB2  1 
ATOM   5201 H HB3  . LYS A 1 338 ? 3.706   -22.402 6.737   1.00 27.45 ? 357 LYS A HB3  1 
ATOM   5202 H HG2  . LYS A 1 338 ? 3.563   -22.169 9.074   1.00 33.11 ? 357 LYS A HG2  1 
ATOM   5203 H HG3  . LYS A 1 338 ? 2.808   -23.566 9.137   1.00 33.11 ? 357 LYS A HG3  1 
ATOM   5204 H HD2  . LYS A 1 338 ? 4.785   -24.518 8.089   1.00 36.70 ? 357 LYS A HD2  1 
ATOM   5205 H HD3  . LYS A 1 338 ? 5.512   -23.148 8.437   1.00 36.70 ? 357 LYS A HD3  1 
ATOM   5206 H HE2  . LYS A 1 338 ? 4.751   -23.640 10.746  1.00 40.06 ? 357 LYS A HE2  1 
ATOM   5207 H HE3  . LYS A 1 338 ? 4.672   -25.136 10.216  1.00 40.06 ? 357 LYS A HE3  1 
ATOM   5208 H HZ1  . LYS A 1 338 ? 6.681   -24.805 11.183  1.00 42.37 ? 357 LYS A HZ1  1 
ATOM   5209 H HZ2  . LYS A 1 338 ? 6.925   -24.988 9.767   1.00 42.37 ? 357 LYS A HZ2  1 
ATOM   5210 H HZ3  . LYS A 1 338 ? 6.975   -23.661 10.344  1.00 42.37 ? 357 LYS A HZ3  1 
ATOM   5211 N N    . PRO A 1 339 ? 1.812   -21.120 4.795   1.00 16.69 ? 358 PRO A N    1 
ATOM   5212 C CA   . PRO A 1 339 ? 1.668   -21.246 3.344   1.00 17.27 ? 358 PRO A CA   1 
ATOM   5213 C C    . PRO A 1 339 ? 2.262   -22.562 2.874   1.00 18.54 ? 358 PRO A C    1 
ATOM   5214 O O    . PRO A 1 339 ? 3.322   -22.989 3.338   1.00 19.44 ? 358 PRO A O    1 
ATOM   5215 C CB   . PRO A 1 339 ? 2.472   -20.067 2.783   1.00 17.96 ? 358 PRO A CB   1 
ATOM   5216 C CG   . PRO A 1 339 ? 2.657   -19.143 3.903   1.00 19.10 ? 358 PRO A CG   1 
ATOM   5217 C CD   . PRO A 1 339 ? 2.583   -19.930 5.177   1.00 17.91 ? 358 PRO A CD   1 
ATOM   5218 H HA   . PRO A 1 339 ? 0.738   -21.163 3.082   1.00 20.73 ? 358 PRO A HA   1 
ATOM   5219 H HB2  . PRO A 1 339 ? 3.327   -20.383 2.453   1.00 21.56 ? 358 PRO A HB2  1 
ATOM   5220 H HB3  . PRO A 1 339 ? 1.974   -19.644 2.066   1.00 21.56 ? 358 PRO A HB3  1 
ATOM   5221 H HG2  . PRO A 1 339 ? 3.525   -18.717 3.823   1.00 22.93 ? 358 PRO A HG2  1 
ATOM   5222 H HG3  . PRO A 1 339 ? 1.956   -18.473 3.881   1.00 22.93 ? 358 PRO A HG3  1 
ATOM   5223 H HD2  . PRO A 1 339 ? 3.469   -20.176 5.482   1.00 21.50 ? 358 PRO A HD2  1 
ATOM   5224 H HD3  . PRO A 1 339 ? 2.122   -19.427 5.867   1.00 21.50 ? 358 PRO A HD3  1 
ATOM   5225 N N    . VAL A 1 340 ? 1.592   -23.196 1.919   1.00 19.91 ? 359 VAL A N    1 
ATOM   5226 C CA   . VAL A 1 340 ? 2.117   -24.406 1.305   1.00 21.22 ? 359 VAL A CA   1 
ATOM   5227 C C    . VAL A 1 340 ? 2.510   -24.207 -0.144  1.00 22.35 ? 359 VAL A C    1 
ATOM   5228 O O    . VAL A 1 340 ? 2.905   -25.173 -0.813  1.00 25.26 ? 359 VAL A O    1 
ATOM   5229 C CB   . VAL A 1 340 ? 1.173   -25.604 1.486   1.00 24.21 ? 359 VAL A CB   1 
ATOM   5230 C CG1  . VAL A 1 340 ? 0.885   -25.842 2.960   1.00 25.89 ? 359 VAL A CG1  1 
ATOM   5231 C CG2  . VAL A 1 340 ? -0.099  -25.367 0.757   1.00 23.96 ? 359 VAL A CG2  1 
ATOM   5232 H H    . VAL A 1 340 ? 0.830   -22.943 1.611   1.00 23.90 ? 359 VAL A H    1 
ATOM   5233 H HA   . VAL A 1 340 ? 2.935   -24.641 1.770   1.00 25.47 ? 359 VAL A HA   1 
ATOM   5234 H HB   . VAL A 1 340 ? 1.601   -26.396 1.125   1.00 29.06 ? 359 VAL A HB   1 
ATOM   5235 H HG11 . VAL A 1 340 ? 0.290   -26.603 3.046   1.00 31.07 ? 359 VAL A HG11 1 
ATOM   5236 H HG12 . VAL A 1 340 ? 1.720   -26.022 3.420   1.00 31.07 ? 359 VAL A HG12 1 
ATOM   5237 H HG13 . VAL A 1 340 ? 0.466   -25.050 3.332   1.00 31.07 ? 359 VAL A HG13 1 
ATOM   5238 H HG21 . VAL A 1 340 ? -0.680  -26.135 0.875   1.00 28.76 ? 359 VAL A HG21 1 
ATOM   5239 H HG22 . VAL A 1 340 ? -0.525  -24.572 1.115   1.00 28.76 ? 359 VAL A HG22 1 
ATOM   5240 H HG23 . VAL A 1 340 ? 0.095   -25.242 -0.185  1.00 28.76 ? 359 VAL A HG23 1 
ATOM   5241 N N    . GLY A 1 341 ? 2.408   -22.988 -0.653  1.00 21.54 ? 360 GLY A N    1 
ATOM   5242 C CA   . GLY A 1 341 ? 2.933   -22.630 -1.955  1.00 20.64 ? 360 GLY A CA   1 
ATOM   5243 C C    . GLY A 1 341 ? 3.072   -21.126 -2.024  1.00 19.71 ? 360 GLY A C    1 
ATOM   5244 O O    . GLY A 1 341 ? 2.596   -20.392 -1.156  1.00 20.09 ? 360 GLY A O    1 
ATOM   5245 H H    . GLY A 1 341 ? 2.028   -22.331 -0.250  1.00 25.86 ? 360 GLY A H    1 
ATOM   5246 H HA2  . GLY A 1 341 ? 3.802   -23.040 -2.090  1.00 24.78 ? 360 GLY A HA2  1 
ATOM   5247 H HA3  . GLY A 1 341 ? 2.330   -22.929 -2.653  1.00 24.78 ? 360 GLY A HA3  1 
ATOM   5248 N N    . GLU A 1 342 ? 3.760   -20.678 -3.067  1.00 19.70 ? 361 GLU A N    1 
ATOM   5249 C CA   . GLU A 1 342 ? 3.931   -19.263 -3.314  1.00 19.69 ? 361 GLU A CA   1 
ATOM   5250 C C    . GLU A 1 342 ? 2.675   -18.684 -3.956  1.00 18.29 ? 361 GLU A C    1 
ATOM   5251 O O    . GLU A 1 342 ? 1.851   -19.398 -4.532  1.00 18.65 ? 361 GLU A O    1 
ATOM   5252 C CB   . GLU A 1 342 ? 5.110   -19.013 -4.247  1.00 21.58 ? 361 GLU A CB   1 
ATOM   5253 C CG   . GLU A 1 342 ? 6.433   -19.543 -3.733  1.00 23.94 ? 361 GLU A CG   1 
ATOM   5254 C CD   . GLU A 1 342 ? 6.941   -18.749 -2.552  1.00 26.73 ? 361 GLU A CD   1 
ATOM   5255 O OE1  . GLU A 1 342 ? 7.471   -19.368 -1.607  1.00 30.17 ? 361 GLU A OE1  1 
ATOM   5256 O OE2  . GLU A 1 342 ? 6.793   -17.509 -2.546  1.00 26.17 ? 361 GLU A OE2  1 
ATOM   5257 H H    . GLU A 1 342 ? 4.140   -21.182 -3.651  1.00 23.64 ? 361 GLU A H    1 
ATOM   5258 H HA   . GLU A 1 342 ? 4.100   -18.816 -2.470  1.00 23.63 ? 361 GLU A HA   1 
ATOM   5259 H HB2  . GLU A 1 342 ? 4.930   -19.446 -5.097  1.00 25.90 ? 361 GLU A HB2  1 
ATOM   5260 H HB3  . GLU A 1 342 ? 5.206   -18.057 -4.376  1.00 25.90 ? 361 GLU A HB3  1 
ATOM   5261 H HG2  . GLU A 1 342 ? 6.320   -20.465 -3.453  1.00 28.73 ? 361 GLU A HG2  1 
ATOM   5262 H HG3  . GLU A 1 342 ? 7.094   -19.491 -4.441  1.00 28.73 ? 361 GLU A HG3  1 
ATOM   5263 N N    . MET A 1 343 ? 2.541   -17.363 -3.867  1.00 17.62 ? 362 MET A N    1 
ATOM   5264 C CA   . MET A 1 343 ? 1.463   -16.682 -4.576  1.00 17.64 ? 362 MET A CA   1 
ATOM   5265 C C    . MET A 1 343 ? 1.596   -16.931 -6.067  1.00 18.47 ? 362 MET A C    1 
ATOM   5266 O O    . MET A 1 343 ? 2.691   -16.857 -6.634  1.00 19.49 ? 362 MET A O    1 
ATOM   5267 C CB   . MET A 1 343 ? 1.490   -15.186 -4.267  1.00 17.77 ? 362 MET A CB   1 
ATOM   5268 C CG   . MET A 1 343 ? 0.251   -14.441 -4.736  1.00 17.04 ? 362 MET A CG   1 
ATOM   5269 S SD   . MET A 1 343 ? 0.329   -12.648 -4.529  1.00 17.78 ? 362 MET A SD   1 
ATOM   5270 C CE   . MET A 1 343 ? 1.521   -12.207 -5.800  1.00 19.35 ? 362 MET A CE   1 
ATOM   5271 H H    . MET A 1 343 ? 3.055   -16.845 -3.411  1.00 21.15 ? 362 MET A H    1 
ATOM   5272 H HA   . MET A 1 343 ? 0.607   -17.021 -4.271  1.00 21.17 ? 362 MET A HA   1 
ATOM   5273 H HB2  . MET A 1 343 ? 1.561   -15.068 -3.307  1.00 21.33 ? 362 MET A HB2  1 
ATOM   5274 H HB3  . MET A 1 343 ? 2.258   -14.791 -4.708  1.00 21.33 ? 362 MET A HB3  1 
ATOM   5275 H HG2  . MET A 1 343 ? 0.121   -14.621 -5.680  1.00 20.45 ? 362 MET A HG2  1 
ATOM   5276 H HG3  . MET A 1 343 ? -0.512  -14.761 -4.229  1.00 20.45 ? 362 MET A HG3  1 
ATOM   5277 H HE1  . MET A 1 343 ? 1.635   -11.244 -5.806  1.00 23.23 ? 362 MET A HE1  1 
ATOM   5278 H HE2  . MET A 1 343 ? 2.367   -12.639 -5.603  1.00 23.23 ? 362 MET A HE2  1 
ATOM   5279 H HE3  . MET A 1 343 ? 1.190   -12.506 -6.661  1.00 23.23 ? 362 MET A HE3  1 
ATOM   5280 N N    . VAL A 1 344 ? 0.476   -17.261 -6.694  1.00 18.46 ? 363 VAL A N    1 
ATOM   5281 C CA   . VAL A 1 344 ? 0.399   -17.460 -8.135  1.00 19.81 ? 363 VAL A CA   1 
ATOM   5282 C C    . VAL A 1 344 ? -0.396  -16.303 -8.722  1.00 20.22 ? 363 VAL A C    1 
ATOM   5283 O O    . VAL A 1 344 ? -1.453  -15.932 -8.193  1.00 19.46 ? 363 VAL A O    1 
ATOM   5284 C CB   . VAL A 1 344 ? -0.263  -18.805 -8.469  1.00 22.01 ? 363 VAL A CB   1 
ATOM   5285 C CG1  . VAL A 1 344 ? -0.416  -18.958 -9.978  1.00 23.65 ? 363 VAL A CG1  1 
ATOM   5286 C CG2  . VAL A 1 344 ? 0.547   -19.942 -7.873  1.00 22.82 ? 363 VAL A CG2  1 
ATOM   5287 H H    . VAL A 1 344 ? -0.276  -17.378 -6.294  1.00 22.16 ? 363 VAL A H    1 
ATOM   5288 H HA   . VAL A 1 344 ? 1.290   -17.451 -8.518  1.00 23.77 ? 363 VAL A HA   1 
ATOM   5289 H HB   . VAL A 1 344 ? -1.152  -18.837 -8.081  1.00 26.42 ? 363 VAL A HB   1 
ATOM   5290 H HG11 . VAL A 1 344 ? -0.601  -19.888 -10.184 1.00 28.39 ? 363 VAL A HG11 1 
ATOM   5291 H HG12 . VAL A 1 344 ? -1.150  -18.401 -10.280 1.00 28.39 ? 363 VAL A HG12 1 
ATOM   5292 H HG13 . VAL A 1 344 ? 0.408   -18.681 -10.409 1.00 28.39 ? 363 VAL A HG13 1 
ATOM   5293 H HG21 . VAL A 1 344 ? 0.134   -20.785 -8.116  1.00 27.38 ? 363 VAL A HG21 1 
ATOM   5294 H HG22 . VAL A 1 344 ? 1.451   -19.904 -8.224  1.00 27.38 ? 363 VAL A HG22 1 
ATOM   5295 H HG23 . VAL A 1 344 ? 0.563   -19.847 -6.908  1.00 27.38 ? 363 VAL A HG23 1 
ATOM   5296 N N    . ARG A 1 345 ? 0.110   -15.727 -9.804  1.00 21.10 ? 364 ARG A N    1 
ATOM   5297 C CA   . ARG A 1 345 ? -0.565  -14.628 -10.471 1.00 22.05 ? 364 ARG A CA   1 
ATOM   5298 C C    . ARG A 1 345 ? -0.895  -14.995 -11.909 1.00 22.83 ? 364 ARG A C    1 
ATOM   5299 O O    . ARG A 1 345 ? -0.067  -15.568 -12.628 1.00 24.36 ? 364 ARG A O    1 
ATOM   5300 C CB   . ARG A 1 345 ? 0.295   -13.372 -10.481 1.00 24.11 ? 364 ARG A CB   1 
ATOM   5301 C CG   . ARG A 1 345 ? -0.375  -12.219 -11.183 1.00 26.55 ? 364 ARG A CG   1 
ATOM   5302 C CD   . ARG A 1 345 ? 0.148   -10.889 -10.687 1.00 29.35 ? 364 ARG A CD   1 
ATOM   5303 N NE   . ARG A 1 345 ? 1.372   -10.494 -11.370 1.00 31.63 ? 364 ARG A NE   1 
ATOM   5304 C CZ   . ARG A 1 345 ? 1.411   -9.924  -12.566 1.00 33.05 ? 364 ARG A CZ   1 
ATOM   5305 N NH1  . ARG A 1 345 ? 0.307   -9.670  -13.247 1.00 32.43 ? 364 ARG A NH1  1 
ATOM   5306 N NH2  . ARG A 1 345 ? 2.589   -9.600  -13.092 1.00 34.01 ? 364 ARG A NH2  1 
ATOM   5307 H H    . ARG A 1 345 ? 0.851   -15.959 -10.173 1.00 25.32 ? 364 ARG A H    1 
ATOM   5308 H HA   . ARG A 1 345 ? -1.392  -14.449 -9.996  1.00 26.47 ? 364 ARG A HA   1 
ATOM   5309 H HB2  . ARG A 1 345 ? 0.475   -13.104 -9.567  1.00 28.93 ? 364 ARG A HB2  1 
ATOM   5310 H HB3  . ARG A 1 345 ? 1.127   -13.562 -10.942 1.00 28.93 ? 364 ARG A HB3  1 
ATOM   5311 H HG2  . ARG A 1 345 ? -0.203  -12.278 -12.136 1.00 31.86 ? 364 ARG A HG2  1 
ATOM   5312 H HG3  . ARG A 1 345 ? -1.330  -12.252 -11.016 1.00 31.86 ? 364 ARG A HG3  1 
ATOM   5313 H HD2  . ARG A 1 345 ? -0.521  -10.204 -10.844 1.00 35.23 ? 364 ARG A HD2  1 
ATOM   5314 H HD3  . ARG A 1 345 ? 0.339   -10.955 -9.738  1.00 35.23 ? 364 ARG A HD3  1 
ATOM   5315 H HE   . ARG A 1 345 ? 2.119   -10.640 -10.971 1.00 37.96 ? 364 ARG A HE   1 
ATOM   5316 H HH11 . ARG A 1 345 ? -0.459  -9.876  -12.915 1.00 38.92 ? 364 ARG A HH11 1 
ATOM   5317 H HH12 . ARG A 1 345 ? 0.355   -9.300  -14.021 1.00 38.92 ? 364 ARG A HH12 1 
ATOM   5318 H HH21 . ARG A 1 345 ? 3.313   -9.761  -12.657 1.00 40.82 ? 364 ARG A HH21 1 
ATOM   5319 H HH22 . ARG A 1 345 ? 2.627   -9.230  -13.867 1.00 40.82 ? 364 ARG A HH22 1 
ATOM   5320 N N    . ASP A 1 346 ? -2.114  -14.650 -12.321 1.00 22.67 ? 365 ASP A N    1 
ATOM   5321 C CA   . ASP A 1 346 ? -2.577  -14.792 -13.706 1.00 24.99 ? 365 ASP A CA   1 
ATOM   5322 C C    . ASP A 1 346 ? -3.263  -13.462 -14.011 1.00 24.69 ? 365 ASP A C    1 
ATOM   5323 O O    . ASP A 1 346 ? -4.445  -13.274 -13.718 1.00 24.58 ? 365 ASP A O    1 
ATOM   5324 C CB   . ASP A 1 346 ? -3.515  -15.991 -13.845 1.00 28.00 ? 365 ASP A CB   1 
ATOM   5325 C CG   . ASP A 1 346 ? -4.149  -16.088 -15.216 1.00 31.42 ? 365 ASP A CG   1 
ATOM   5326 O OD1  . ASP A 1 346 ? -3.652  -15.437 -16.157 1.00 31.95 ? 365 ASP A OD1  1 
ATOM   5327 O OD2  . ASP A 1 346 ? -5.143  -16.832 -15.355 1.00 33.78 ? 365 ASP A OD2  1 
ATOM   5328 H H    . ASP A 1 346 ? -2.713  -14.319 -11.800 1.00 27.21 ? 365 ASP A H    1 
ATOM   5329 H HA   . ASP A 1 346 ? -1.843  -14.936 -14.323 1.00 29.99 ? 365 ASP A HA   1 
ATOM   5330 H HB2  . ASP A 1 346 ? -3.012  -16.805 -13.690 1.00 33.60 ? 365 ASP A HB2  1 
ATOM   5331 H HB3  . ASP A 1 346 ? -4.227  -15.912 -13.191 1.00 33.60 ? 365 ASP A HB3  1 
ATOM   5332 N N    . GLY A 1 347 ? -2.510  -12.516 -14.556 1.00 23.70 ? 366 GLY A N    1 
ATOM   5333 C CA   . GLY A 1 347 ? -3.056  -11.199 -14.795 1.00 24.06 ? 366 GLY A CA   1 
ATOM   5334 C C    . GLY A 1 347 ? -3.416  -10.478 -13.518 1.00 24.05 ? 366 GLY A C    1 
ATOM   5335 O O    . GLY A 1 347 ? -2.542  -10.215 -12.694 1.00 25.02 ? 366 GLY A O    1 
ATOM   5336 H H    . GLY A 1 347 ? -1.689  -12.615 -14.793 1.00 28.45 ? 366 GLY A H    1 
ATOM   5337 H HA2  . GLY A 1 347 ? -2.403  -10.664 -15.273 1.00 28.87 ? 366 GLY A HA2  1 
ATOM   5338 H HA3  . GLY A 1 347 ? -3.856  -11.278 -15.337 1.00 28.87 ? 366 GLY A HA3  1 
ATOM   5339 N N    . TRP A 1 348 ? -4.690  -10.135 -13.352 1.00 22.64 ? 367 TRP A N    1 
ATOM   5340 C CA   . TRP A 1 348 ? -5.171  -9.506  -12.132 1.00 21.28 ? 367 TRP A CA   1 
ATOM   5341 C C    . TRP A 1 348 ? -5.648  -10.505 -11.091 1.00 20.29 ? 367 TRP A C    1 
ATOM   5342 O O    . TRP A 1 348 ? -6.103  -10.092 -10.019 1.00 19.10 ? 367 TRP A O    1 
ATOM   5343 C CB   . TRP A 1 348 ? -6.289  -8.519  -12.459 1.00 22.15 ? 367 TRP A CB   1 
ATOM   5344 C CG   . TRP A 1 348 ? -5.833  -7.499  -13.444 1.00 22.68 ? 367 TRP A CG   1 
ATOM   5345 C CD1  . TRP A 1 348 ? -6.240  -7.366  -14.738 1.00 23.95 ? 367 TRP A CD1  1 
ATOM   5346 C CD2  . TRP A 1 348 ? -4.859  -6.467  -13.219 1.00 22.88 ? 367 TRP A CD2  1 
ATOM   5347 N NE1  . TRP A 1 348 ? -5.581  -6.318  -15.333 1.00 24.91 ? 367 TRP A NE1  1 
ATOM   5348 C CE2  . TRP A 1 348 ? -4.726  -5.753  -14.422 1.00 23.76 ? 367 TRP A CE2  1 
ATOM   5349 C CE3  . TRP A 1 348 ? -4.083  -6.087  -12.119 1.00 22.22 ? 367 TRP A CE3  1 
ATOM   5350 C CZ2  . TRP A 1 348 ? -3.852  -4.681  -14.559 1.00 24.31 ? 367 TRP A CZ2  1 
ATOM   5351 C CZ3  . TRP A 1 348 ? -3.219  -5.014  -12.251 1.00 22.54 ? 367 TRP A CZ3  1 
ATOM   5352 C CH2  . TRP A 1 348 ? -3.114  -4.321  -13.462 1.00 23.43 ? 367 TRP A CH2  1 
ATOM   5353 H H    . TRP A 1 348 ? -5.303  -10.260 -13.942 1.00 27.18 ? 367 TRP A H    1 
ATOM   5354 H HA   . TRP A 1 348 ? -4.441  -9.004  -11.735 1.00 25.54 ? 367 TRP A HA   1 
ATOM   5355 H HB2  . TRP A 1 348 ? -7.041  -8.999  -12.839 1.00 26.59 ? 367 TRP A HB2  1 
ATOM   5356 H HB3  . TRP A 1 348 ? -6.563  -8.062  -11.648 1.00 26.59 ? 367 TRP A HB3  1 
ATOM   5357 H HD1  . TRP A 1 348 ? -6.871  -7.906  -15.157 1.00 28.74 ? 367 TRP A HD1  1 
ATOM   5358 H HE1  . TRP A 1 348 ? -5.687  -6.059  -16.146 1.00 29.90 ? 367 TRP A HE1  1 
ATOM   5359 H HE3  . TRP A 1 348 ? -4.147  -6.546  -11.313 1.00 26.68 ? 367 TRP A HE3  1 
ATOM   5360 H HZ2  . TRP A 1 348 ? -3.772  -4.225  -15.365 1.00 29.18 ? 367 TRP A HZ2  1 
ATOM   5361 H HZ3  . TRP A 1 348 ? -2.702  -4.751  -11.525 1.00 27.06 ? 367 TRP A HZ3  1 
ATOM   5362 H HH2  . TRP A 1 348 ? -2.530  -3.599  -13.524 1.00 28.13 ? 367 TRP A HH2  1 
ATOM   5363 N N    . LYS A 1 349 ? -5.551  -11.795 -11.377 1.00 20.90 ? 368 LYS A N    1 
ATOM   5364 C CA   . LYS A 1 349 ? -5.995  -12.842 -10.471 1.00 21.55 ? 368 LYS A CA   1 
ATOM   5365 C C    . LYS A 1 349 ? -4.800  -13.355 -9.675  1.00 19.57 ? 368 LYS A C    1 
ATOM   5366 O O    . LYS A 1 349 ? -3.733  -13.626 -10.233 1.00 20.64 ? 368 LYS A O    1 
ATOM   5367 C CB   . LYS A 1 349 ? -6.607  -14.008 -11.250 1.00 24.49 ? 368 LYS A CB   1 
ATOM   5368 C CG   . LYS A 1 349 ? -7.967  -13.698 -11.866 1.00 28.32 ? 368 LYS A CG   1 
ATOM   5369 C CD   . LYS A 1 349 ? -8.285  -14.641 -13.022 1.00 32.18 ? 368 LYS A CD   1 
ATOM   5370 C CE   . LYS A 1 349 ? -8.402  -13.920 -14.381 1.00 35.45 ? 368 LYS A CE   1 
ATOM   5371 N NZ   . LYS A 1 349 ? -7.108  -13.649 -15.104 1.00 37.08 ? 368 LYS A NZ   1 
ATOM   5372 H H    . LYS A 1 349 ? -5.221  -12.098 -12.111 1.00 25.09 ? 368 LYS A H    1 
ATOM   5373 H HA   . LYS A 1 349 ? -6.663  -12.487 -9.864  1.00 25.86 ? 368 LYS A HA   1 
ATOM   5374 H HB2  . LYS A 1 349 ? -6.004  -14.250 -11.971 1.00 29.40 ? 368 LYS A HB2  1 
ATOM   5375 H HB3  . LYS A 1 349 ? -6.720  -14.759 -10.647 1.00 29.40 ? 368 LYS A HB3  1 
ATOM   5376 H HG2  . LYS A 1 349 ? -8.656  -13.799 -11.192 1.00 33.99 ? 368 LYS A HG2  1 
ATOM   5377 H HG3  . LYS A 1 349 ? -7.966  -12.789 -12.206 1.00 33.99 ? 368 LYS A HG3  1 
ATOM   5378 H HD2  . LYS A 1 349 ? -7.577  -15.299 -13.094 1.00 38.63 ? 368 LYS A HD2  1 
ATOM   5379 H HD3  . LYS A 1 349 ? -9.131  -15.081 -12.845 1.00 38.63 ? 368 LYS A HD3  1 
ATOM   5380 H HE2  . LYS A 1 349 ? -8.947  -14.467 -14.967 1.00 42.54 ? 368 LYS A HE2  1 
ATOM   5381 H HE3  . LYS A 1 349 ? -8.831  -13.063 -14.233 1.00 42.54 ? 368 LYS A HE3  1 
ATOM   5382 H HZ1  . LYS A 1 349 ? -7.271  -13.230 -15.872 1.00 44.51 ? 368 LYS A HZ1  1 
ATOM   5383 H HZ2  . LYS A 1 349 ? -6.580  -13.138 -14.603 1.00 44.51 ? 368 LYS A HZ2  1 
ATOM   5384 H HZ3  . LYS A 1 349 ? -6.689  -14.415 -15.277 1.00 44.51 ? 368 LYS A HZ3  1 
ATOM   5385 N N    . LEU A 1 350 ? -4.996  -13.521 -8.379  1.00 17.82 ? 369 LEU A N    1 
ATOM   5386 C CA   . LEU A 1 350 ? -3.968  -14.020 -7.480  1.00 16.85 ? 369 LEU A CA   1 
ATOM   5387 C C    . LEU A 1 350 ? -4.534  -15.194 -6.707  1.00 17.94 ? 369 LEU A C    1 
ATOM   5388 O O    . LEU A 1 350 ? -5.724  -15.225 -6.384  1.00 18.27 ? 369 LEU A O    1 
ATOM   5389 C CB   . LEU A 1 350 ? -3.523  -12.941 -6.475  1.00 17.61 ? 369 LEU A CB   1 
ATOM   5390 C CG   . LEU A 1 350 ? -3.178  -11.557 -7.025  1.00 18.67 ? 369 LEU A CG   1 
ATOM   5391 C CD1  . LEU A 1 350 ? -2.997  -10.559 -5.880  1.00 19.04 ? 369 LEU A CD1  1 
ATOM   5392 C CD2  . LEU A 1 350 ? -1.933  -11.631 -7.891  1.00 19.94 ? 369 LEU A CD2  1 
ATOM   5393 H H    . LEU A 1 350 ? -5.739  -13.346 -7.983  1.00 21.39 ? 369 LEU A H    1 
ATOM   5394 H HA   . LEU A 1 350 ? -3.195  -14.304 -7.993  1.00 20.23 ? 369 LEU A HA   1 
ATOM   5395 H HB2  . LEU A 1 350 ? -4.243  -12.817 -5.836  1.00 21.14 ? 369 LEU A HB2  1 
ATOM   5396 H HB3  . LEU A 1 350 ? -2.731  -13.268 -6.022  1.00 21.14 ? 369 LEU A HB3  1 
ATOM   5397 H HG   . LEU A 1 350 ? -3.906  -11.237 -7.581  1.00 22.40 ? 369 LEU A HG   1 
ATOM   5398 H HD11 . LEU A 1 350 ? -2.830  -9.678  -6.251  1.00 22.85 ? 369 LEU A HD11 1 
ATOM   5399 H HD12 . LEU A 1 350 ? -3.805  -10.544 -5.343  1.00 22.85 ? 369 LEU A HD12 1 
ATOM   5400 H HD13 . LEU A 1 350 ? -2.244  -10.836 -5.335  1.00 22.85 ? 369 LEU A HD13 1 
ATOM   5401 H HD21 . LEU A 1 350 ? -1.724  -10.743 -8.221  1.00 23.94 ? 369 LEU A HD21 1 
ATOM   5402 H HD22 . LEU A 1 350 ? -1.197  -11.968 -7.357  1.00 23.94 ? 369 LEU A HD22 1 
ATOM   5403 H HD23 . LEU A 1 350 ? -2.102  -12.229 -8.636  1.00 23.94 ? 369 LEU A HD23 1 
ATOM   5404 N N    . SER A 1 351 ? -3.675  -16.154 -6.385  1.00 17.44 ? 370 SER A N    1 
ATOM   5405 C CA   . SER A 1 351 ? -4.095  -17.258 -5.535  1.00 18.48 ? 370 SER A CA   1 
ATOM   5406 C C    . SER A 1 351 ? -2.972  -17.656 -4.592  1.00 17.17 ? 370 SER A C    1 
ATOM   5407 O O    . SER A 1 351 ? -1.787  -17.418 -4.850  1.00 16.95 ? 370 SER A O    1 
ATOM   5408 C CB   . SER A 1 351 ? -4.534  -18.487 -6.333  1.00 20.58 ? 370 SER A CB   1 
ATOM   5409 O OG   . SER A 1 351 ? -3.454  -19.025 -7.063  1.00 22.93 ? 370 SER A OG   1 
ATOM   5410 H H    . SER A 1 351 ? -2.855  -16.187 -6.642  1.00 20.94 ? 370 SER A H    1 
ATOM   5411 H HA   . SER A 1 351 ? -4.847  -16.947 -5.007  1.00 22.19 ? 370 SER A HA   1 
ATOM   5412 H HB2  . SER A 1 351 ? -4.866  -19.160 -5.719  1.00 24.71 ? 370 SER A HB2  1 
ATOM   5413 H HB3  . SER A 1 351 ? -5.234  -18.227 -6.952  1.00 24.71 ? 370 SER A HB3  1 
ATOM   5414 H HG   . SER A 1 351 ? -3.589  -19.840 -7.217  1.00 27.52 ? 370 SER A HG   1 
ATOM   5415 N N    . ARG A 1 352 ? -3.370  -18.258 -3.473  1.00 15.92 ? 371 ARG A N    1 
ATOM   5416 C CA   . ARG A 1 352 ? -2.415  -18.728 -2.479  1.00 15.61 ? 371 ARG A CA   1 
ATOM   5417 C C    . ARG A 1 352 ? -3.006  -19.908 -1.723  1.00 15.98 ? 371 ARG A C    1 
ATOM   5418 O O    . ARG A 1 352 ? -4.188  -19.901 -1.369  1.00 16.86 ? 371 ARG A O    1 
ATOM   5419 C CB   . ARG A 1 352 ? -2.051  -17.615 -1.498  1.00 16.65 ? 371 ARG A CB   1 
ATOM   5420 C CG   . ARG A 1 352 ? -0.859  -17.911 -0.620  1.00 15.51 ? 371 ARG A CG   1 
ATOM   5421 C CD   . ARG A 1 352 ? 0.445   -17.738 -1.393  1.00 15.77 ? 371 ARG A CD   1 
ATOM   5422 N NE   . ARG A 1 352 ? 1.604   -17.813 -0.515  1.00 15.49 ? 371 ARG A NE   1 
ATOM   5423 C CZ   . ARG A 1 352 ? 1.974   -16.843 0.310   1.00 15.21 ? 371 ARG A CZ   1 
ATOM   5424 N NH1  . ARG A 1 352 ? 1.307   -15.704 0.372   1.00 15.02 ? 371 ARG A NH1  1 
ATOM   5425 N NH2  . ARG A 1 352 ? 3.035   -17.020 1.096   1.00 16.13 ? 371 ARG A NH2  1 
ATOM   5426 H H    . ARG A 1 352 ? -4.193  -18.405 -3.268  1.00 19.11 ? 371 ARG A H    1 
ATOM   5427 H HA   . ARG A 1 352 ? -1.610  -19.031 -2.926  1.00 18.74 ? 371 ARG A HA   1 
ATOM   5428 H HB2  . ARG A 1 352 ? -1.848  -16.813 -2.004  1.00 19.99 ? 371 ARG A HB2  1 
ATOM   5429 H HB3  . ARG A 1 352 ? -2.810  -17.457 -0.915  1.00 19.99 ? 371 ARG A HB3  1 
ATOM   5430 H HG2  . ARG A 1 352 ? -0.853  -17.300 0.133   1.00 18.62 ? 371 ARG A HG2  1 
ATOM   5431 H HG3  . ARG A 1 352 ? -0.910  -18.827 -0.305  1.00 18.62 ? 371 ARG A HG3  1 
ATOM   5432 H HD2  . ARG A 1 352 ? 0.520   -18.442 -2.057  1.00 18.93 ? 371 ARG A HD2  1 
ATOM   5433 H HD3  . ARG A 1 352 ? 0.447   -16.871 -1.828  1.00 18.93 ? 371 ARG A HD3  1 
ATOM   5434 H HE   . ARG A 1 352 ? 2.078   -18.530 -0.533  1.00 18.59 ? 371 ARG A HE   1 
ATOM   5435 H HH11 . ARG A 1 352 ? 0.618   -15.582 -0.129  1.00 18.03 ? 371 ARG A HH11 1 
ATOM   5436 H HH12 . ARG A 1 352 ? 1.561   -15.086 0.913   1.00 18.03 ? 371 ARG A HH12 1 
ATOM   5437 H HH21 . ARG A 1 352 ? 3.474   -17.759 1.065   1.00 19.37 ? 371 ARG A HH21 1 
ATOM   5438 H HH22 . ARG A 1 352 ? 3.281   -16.396 1.633   1.00 19.37 ? 371 ARG A HH22 1 
ATOM   5439 N N    . GLU A 1 353 ? -2.177  -20.917 -1.489  1.00 16.56 ? 372 GLU A N    1 
ATOM   5440 C CA   . GLU A 1 353 ? -2.562  -22.094 -0.728  1.00 16.68 ? 372 GLU A CA   1 
ATOM   5441 C C    . GLU A 1 353 ? -1.891  -22.070 0.637   1.00 16.86 ? 372 GLU A C    1 
ATOM   5442 O O    . GLU A 1 353 ? -0.670  -21.905 0.731   1.00 17.03 ? 372 GLU A O    1 
ATOM   5443 C CB   . GLU A 1 353 ? -2.166  -23.365 -1.474  1.00 18.10 ? 372 GLU A CB   1 
ATOM   5444 C CG   . GLU A 1 353 ? -2.833  -23.532 -2.810  1.00 22.17 ? 372 GLU A CG   1 
ATOM   5445 C CD   . GLU A 1 353 ? -4.343  -23.547 -2.705  1.00 25.24 ? 372 GLU A CD   1 
ATOM   5446 O OE1  . GLU A 1 353 ? -4.854  -24.053 -1.692  1.00 24.56 ? 372 GLU A OE1  1 
ATOM   5447 O OE2  . GLU A 1 353 ? -5.017  -23.080 -3.653  1.00 28.30 ? 372 GLU A OE2  1 
ATOM   5448 H H    . GLU A 1 353 ? -1.364  -20.941 -1.768  1.00 19.88 ? 372 GLU A H    1 
ATOM   5449 H HA   . GLU A 1 353 ? -3.522  -22.090 -0.594  1.00 20.02 ? 372 GLU A HA   1 
ATOM   5450 H HB2  . GLU A 1 353 ? -1.208  -23.350 -1.624  1.00 21.72 ? 372 GLU A HB2  1 
ATOM   5451 H HB3  . GLU A 1 353 ? -2.404  -24.131 -0.929  1.00 21.72 ? 372 GLU A HB3  1 
ATOM   5452 H HG2  . GLU A 1 353 ? -2.578  -22.795 -3.386  1.00 26.61 ? 372 GLU A HG2  1 
ATOM   5453 H HG3  . GLU A 1 353 ? -2.550  -24.373 -3.203  1.00 26.61 ? 372 GLU A HG3  1 
ATOM   5454 N N    . TYR A 1 354 ? -2.693  -22.226 1.682   1.00 16.19 ? 373 TYR A N    1 
ATOM   5455 C CA   . TYR A 1 354 ? -2.246  -22.370 3.060   1.00 16.35 ? 373 TYR A CA   1 
ATOM   5456 C C    . TYR A 1 354 ? -2.597  -23.779 3.537   1.00 16.56 ? 373 TYR A C    1 
ATOM   5457 O O    . TYR A 1 354 ? -3.427  -24.484 2.952   1.00 17.84 ? 373 TYR A O    1 
ATOM   5458 C CB   . TYR A 1 354 ? -2.936  -21.340 3.958   1.00 15.75 ? 373 TYR A CB   1 
ATOM   5459 C CG   . TYR A 1 354 ? -2.418  -19.932 3.753   1.00 14.47 ? 373 TYR A CG   1 
ATOM   5460 C CD1  . TYR A 1 354 ? -2.937  -19.111 2.758   1.00 14.46 ? 373 TYR A CD1  1 
ATOM   5461 C CD2  . TYR A 1 354 ? -1.423  -19.397 4.584   1.00 14.24 ? 373 TYR A CD2  1 
ATOM   5462 C CE1  . TYR A 1 354 ? -2.454  -17.815 2.569   1.00 14.43 ? 373 TYR A CE1  1 
ATOM   5463 C CE2  . TYR A 1 354 ? -0.950  -18.116 4.404   1.00 14.63 ? 373 TYR A CE2  1 
ATOM   5464 C CZ   . TYR A 1 354 ? -1.475  -17.322 3.397   1.00 13.68 ? 373 TYR A CZ   1 
ATOM   5465 O OH   . TYR A 1 354 ? -0.987  -16.032 3.252   1.00 14.33 ? 373 TYR A OH   1 
ATOM   5466 H H    . TYR A 1 354 ? -3.550  -22.253 1.614   1.00 19.43 ? 373 TYR A H    1 
ATOM   5467 H HA   . TYR A 1 354 ? -1.288  -22.234 3.124   1.00 19.62 ? 373 TYR A HA   1 
ATOM   5468 H HB2  . TYR A 1 354 ? -3.887  -21.340 3.764   1.00 18.90 ? 373 TYR A HB2  1 
ATOM   5469 H HB3  . TYR A 1 354 ? -2.787  -21.581 4.886   1.00 18.90 ? 373 TYR A HB3  1 
ATOM   5470 H HD1  . TYR A 1 354 ? -3.617  -19.430 2.209   1.00 17.36 ? 373 TYR A HD1  1 
ATOM   5471 H HD2  . TYR A 1 354 ? -1.075  -19.919 5.271   1.00 17.10 ? 373 TYR A HD2  1 
ATOM   5472 H HE1  . TYR A 1 354 ? -2.794  -17.286 1.884   1.00 17.33 ? 373 TYR A HE1  1 
ATOM   5473 H HE2  . TYR A 1 354 ? -0.280  -17.785 4.958   1.00 17.57 ? 373 TYR A HE2  1 
ATOM   5474 H HH   . TYR A 1 354 ? -1.369  -15.651 2.608   1.00 17.20 ? 373 TYR A HH   1 
ATOM   5475 N N    . LYS A 1 355 ? -1.993  -24.183 4.649   1.00 16.60 ? 374 LYS A N    1 
ATOM   5476 C CA   . LYS A 1 355 ? -2.264  -25.519 5.165   1.00 17.63 ? 374 LYS A CA   1 
ATOM   5477 C C    . LYS A 1 355 ? -3.755  -25.741 5.366   1.00 17.13 ? 374 LYS A C    1 
ATOM   5478 O O    . LYS A 1 355 ? -4.270  -26.833 5.097   1.00 18.18 ? 374 LYS A O    1 
ATOM   5479 C CB   . LYS A 1 355 ? -1.506  -25.732 6.475   1.00 21.28 ? 374 LYS A CB   1 
ATOM   5480 C CG   . LYS A 1 355 ? -1.617  -27.160 7.017   1.00 25.79 ? 374 LYS A CG   1 
ATOM   5481 C CD   . LYS A 1 355 ? -0.355  -27.565 7.769   1.00 29.83 ? 374 LYS A CD   1 
ATOM   5482 C CE   . LYS A 1 355 ? -0.656  -28.319 9.053   1.00 31.94 ? 374 LYS A CE   1 
ATOM   5483 N NZ   . LYS A 1 355 ? 0.484   -28.238 10.019  1.00 33.68 ? 374 LYS A NZ   1 
ATOM   5484 H H    . LYS A 1 355 ? -1.437  -23.717 5.111   1.00 19.92 ? 374 LYS A H    1 
ATOM   5485 H HA   . LYS A 1 355 ? -1.950  -26.176 4.524   1.00 21.17 ? 374 LYS A HA   1 
ATOM   5486 H HB2  . LYS A 1 355 ? -0.566  -25.542 6.327   1.00 25.55 ? 374 LYS A HB2  1 
ATOM   5487 H HB3  . LYS A 1 355 ? -1.864  -25.130 7.145   1.00 25.55 ? 374 LYS A HB3  1 
ATOM   5488 H HG2  . LYS A 1 355 ? -2.368  -27.215 7.629   1.00 30.95 ? 374 LYS A HG2  1 
ATOM   5489 H HG3  . LYS A 1 355 ? -1.744  -27.776 6.279   1.00 30.95 ? 374 LYS A HG3  1 
ATOM   5490 H HD2  . LYS A 1 355 ? 0.182   -28.140 7.202   1.00 35.81 ? 374 LYS A HD2  1 
ATOM   5491 H HD3  . LYS A 1 355 ? 0.146   -26.767 8.000   1.00 35.81 ? 374 LYS A HD3  1 
ATOM   5492 H HE2  . LYS A 1 355 ? -1.441  -27.934 9.475   1.00 38.33 ? 374 LYS A HE2  1 
ATOM   5493 H HE3  . LYS A 1 355 ? -0.815  -29.253 8.847   1.00 38.33 ? 374 LYS A HE3  1 
ATOM   5494 H HZ1  . LYS A 1 355 ? 0.266   -28.644 10.781  1.00 40.42 ? 374 LYS A HZ1  1 
ATOM   5495 H HZ2  . LYS A 1 355 ? 1.203   -28.634 9.676   1.00 40.42 ? 374 LYS A HZ2  1 
ATOM   5496 H HZ3  . LYS A 1 355 ? 0.677   -27.387 10.191  1.00 40.42 ? 374 LYS A HZ3  1 
ATOM   5497 N N    . HIS A 1 356 ? -4.472  -24.711 5.827   1.00 16.58 ? 375 HIS A N    1 
ATOM   5498 C CA   . HIS A 1 356 ? -5.886  -24.859 6.141   1.00 17.39 ? 375 HIS A CA   1 
ATOM   5499 C C    . HIS A 1 356 ? -6.786  -23.906 5.362   1.00 17.31 ? 375 HIS A C    1 
ATOM   5500 O O    . HIS A 1 356 ? -7.920  -23.667 5.776   1.00 18.50 ? 375 HIS A O    1 
ATOM   5501 C CB   . HIS A 1 356 ? -6.117  -24.688 7.641   1.00 17.79 ? 375 HIS A CB   1 
ATOM   5502 C CG   . HIS A 1 356 ? -5.247  -25.554 8.496   1.00 18.57 ? 375 HIS A CG   1 
ATOM   5503 N ND1  . HIS A 1 356 ? -5.297  -26.930 8.466   1.00 21.05 ? 375 HIS A ND1  1 
ATOM   5504 C CD2  . HIS A 1 356 ? -4.317  -25.229 9.425   1.00 19.39 ? 375 HIS A CD2  1 
ATOM   5505 C CE1  . HIS A 1 356 ? -4.438  -27.414 9.347   1.00 20.60 ? 375 HIS A CE1  1 
ATOM   5506 N NE2  . HIS A 1 356 ? -3.822  -26.404 9.932   1.00 21.11 ? 375 HIS A NE2  1 
ATOM   5507 H H    . HIS A 1 356 ? -4.157  -23.923 5.965   1.00 19.91 ? 375 HIS A H    1 
ATOM   5508 H HA   . HIS A 1 356 ? -6.147  -25.758 5.886   1.00 20.88 ? 375 HIS A HA   1 
ATOM   5509 H HB2  . HIS A 1 356 ? -5.938  -23.765 7.879   1.00 21.35 ? 375 HIS A HB2  1 
ATOM   5510 H HB3  . HIS A 1 356 ? -7.040  -24.909 7.841   1.00 21.35 ? 375 HIS A HB3  1 
ATOM   5511 H HD1  . HIS A 1 356 ? -5.806  -27.400 7.956   1.00 25.26 ? 375 HIS A HD1  1 
ATOM   5512 H HD2  . HIS A 1 356 ? -4.062  -24.370 9.673   1.00 23.27 ? 375 HIS A HD2  1 
ATOM   5513 H HE1  . HIS A 1 356 ? -4.292  -28.315 9.525   1.00 24.73 ? 375 HIS A HE1  1 
ATOM   5514 N N    . ALA A 1 357 ? -6.324  -23.365 4.242   1.00 16.39 ? 376 ALA A N    1 
ATOM   5515 C CA   . ALA A 1 357 ? -7.166  -22.439 3.492   1.00 16.47 ? 376 ALA A CA   1 
ATOM   5516 C C    . ALA A 1 357 ? -6.668  -22.294 2.065   1.00 17.56 ? 376 ALA A C    1 
ATOM   5517 O O    . ALA A 1 357 ? -5.479  -22.426 1.797   1.00 17.98 ? 376 ALA A O    1 
ATOM   5518 C CB   . ALA A 1 357 ? -7.204  -21.053 4.156   1.00 18.30 ? 376 ALA A CB   1 
ATOM   5519 H H    . ALA A 1 357 ? -5.547  -23.513 3.903   1.00 19.68 ? 376 ALA A H    1 
ATOM   5520 H HA   . ALA A 1 357 ? -8.060  -22.813 3.458   1.00 19.77 ? 376 ALA A HA   1 
ATOM   5521 H HB1  . ALA A 1 357 ? -7.813  -20.483 3.662   1.00 21.96 ? 376 ALA A HB1  1 
ATOM   5522 H HB2  . ALA A 1 357 ? -7.509  -21.149 5.071   1.00 21.96 ? 376 ALA A HB2  1 
ATOM   5523 H HB3  . ALA A 1 357 ? -6.311  -20.673 4.143   1.00 21.96 ? 376 ALA A HB3  1 
ATOM   5524 N N    . SER A 1 358 ? -7.593  -21.975 1.163   1.00 17.99 ? 377 SER A N    1 
ATOM   5525 C CA   . SER A 1 358 ? -7.282  -21.652 -0.224  1.00 18.06 ? 377 SER A CA   1 
ATOM   5526 C C    . SER A 1 358 ? -7.837  -20.272 -0.518  1.00 17.69 ? 377 SER A C    1 
ATOM   5527 O O    . SER A 1 358 ? -9.020  -20.015 -0.264  1.00 18.80 ? 377 SER A O    1 
ATOM   5528 C CB   . SER A 1 358 ? -7.944  -22.641 -1.187  1.00 19.99 ? 377 SER A CB   1 
ATOM   5529 O OG   . SER A 1 358 ? -7.362  -23.931 -1.048  1.00 22.39 ? 377 SER A OG   1 
ATOM   5530 H H    . SER A 1 358 ? -8.434  -21.938 1.338   1.00 21.59 ? 377 SER A H    1 
ATOM   5531 H HA   . SER A 1 358 ? -6.320  -21.674 -0.353  1.00 21.68 ? 377 SER A HA   1 
ATOM   5532 H HB2  . SER A 1 358 ? -8.891  -22.695 -0.985  1.00 24.00 ? 377 SER A HB2  1 
ATOM   5533 H HB3  . SER A 1 358 ? -7.817  -22.331 -2.097  1.00 24.00 ? 377 SER A HB3  1 
ATOM   5534 H HG   . SER A 1 358 ? -6.554  -23.907 -1.275  1.00 26.88 ? 377 SER A HG   1 
ATOM   5535 N N    . VAL A 1 359 ? -6.983  -19.386 -1.031  1.00 16.48 ? 378 VAL A N    1 
ATOM   5536 C CA   . VAL A 1 359 ? -7.314  -17.984 -1.234  1.00 17.05 ? 378 VAL A CA   1 
ATOM   5537 C C    . VAL A 1 359 ? -7.285  -17.668 -2.717  1.00 17.35 ? 378 VAL A C    1 
ATOM   5538 O O    . VAL A 1 359 ? -6.335  -18.041 -3.416  1.00 17.10 ? 378 VAL A O    1 
ATOM   5539 C CB   . VAL A 1 359 ? -6.305  -17.099 -0.482  1.00 17.96 ? 378 VAL A CB   1 
ATOM   5540 C CG1  . VAL A 1 359 ? -6.566  -15.631 -0.740  1.00 18.07 ? 378 VAL A CG1  1 
ATOM   5541 C CG2  . VAL A 1 359 ? -6.357  -17.413 0.992   1.00 19.41 ? 378 VAL A CG2  1 
ATOM   5542 H H    . VAL A 1 359 ? -6.183  -19.584 -1.276  1.00 19.79 ? 378 VAL A H    1 
ATOM   5543 H HA   . VAL A 1 359 ? -8.215  -17.813 -0.919  1.00 20.47 ? 378 VAL A HA   1 
ATOM   5544 H HB   . VAL A 1 359 ? -5.411  -17.288 -0.807  1.00 21.55 ? 378 VAL A HB   1 
ATOM   5545 H HG11 . VAL A 1 359 ? -5.982  -15.102 -0.174  1.00 21.69 ? 378 VAL A HG11 1 
ATOM   5546 H HG12 . VAL A 1 359 ? -6.386  -15.437 -1.673  1.00 21.69 ? 378 VAL A HG12 1 
ATOM   5547 H HG13 . VAL A 1 359 ? -7.493  -15.434 -0.534  1.00 21.69 ? 378 VAL A HG13 1 
ATOM   5548 H HG21 . VAL A 1 359 ? -5.769  -16.804 1.466   1.00 23.30 ? 378 VAL A HG21 1 
ATOM   5549 H HG22 . VAL A 1 359 ? -7.268  -17.305 1.306   1.00 23.30 ? 378 VAL A HG22 1 
ATOM   5550 H HG23 . VAL A 1 359 ? -6.066  -18.328 1.130   1.00 23.30 ? 378 VAL A HG23 1 
ATOM   5551 N N    . ARG A 1 360 ? -8.313  -16.964 -3.184  1.00 18.72 ? 379 ARG A N    1 
ATOM   5552 C CA   . ARG A 1 360 ? -8.392  -16.477 -4.552  1.00 20.32 ? 379 ARG A CA   1 
ATOM   5553 C C    . ARG A 1 360 ? -8.895  -15.040 -4.536  1.00 18.92 ? 379 ARG A C    1 
ATOM   5554 O O    . ARG A 1 360 ? -9.851  -14.713 -3.825  1.00 18.29 ? 379 ARG A O    1 
ATOM   5555 C CB   . ARG A 1 360 ? -9.415  -17.285 -5.361  1.00 25.20 ? 379 ARG A CB   1 
ATOM   5556 C CG   . ARG A 1 360 ? -8.859  -18.507 -6.067  1.00 31.85 ? 379 ARG A CG   1 
ATOM   5557 C CD   . ARG A 1 360 ? -8.893  -19.762 -5.217  1.00 37.06 ? 379 ARG A CD   1 
ATOM   5558 N NE   . ARG A 1 360 ? -8.131  -20.827 -5.870  1.00 40.72 ? 379 ARG A NE   1 
ATOM   5559 C CZ   . ARG A 1 360 ? -6.977  -21.317 -5.440  1.00 43.11 ? 379 ARG A CZ   1 
ATOM   5560 N NH1  . ARG A 1 360 ? -6.450  -20.937 -4.285  1.00 42.60 ? 379 ARG A NH1  1 
ATOM   5561 N NH2  . ARG A 1 360 ? -6.333  -22.209 -6.189  1.00 44.70 ? 379 ARG A NH2  1 
ATOM   5562 H H    . ARG A 1 360 ? -8.998  -16.750 -2.709  1.00 22.47 ? 379 ARG A H    1 
ATOM   5563 H HA   . ARG A 1 360 ? -7.513  -16.528 -4.957  1.00 24.39 ? 379 ARG A HA   1 
ATOM   5564 H HB2  . ARG A 1 360 ? -10.110 -17.590 -4.757  1.00 30.25 ? 379 ARG A HB2  1 
ATOM   5565 H HB3  . ARG A 1 360 ? -9.796  -16.706 -6.039  1.00 30.25 ? 379 ARG A HB3  1 
ATOM   5566 H HG2  . ARG A 1 360 ? -9.385  -18.674 -6.865  1.00 38.23 ? 379 ARG A HG2  1 
ATOM   5567 H HG3  . ARG A 1 360 ? -7.935  -18.336 -6.309  1.00 38.23 ? 379 ARG A HG3  1 
ATOM   5568 H HD2  . ARG A 1 360 ? -8.497  -19.581 -4.351  1.00 44.48 ? 379 ARG A HD2  1 
ATOM   5569 H HD3  . ARG A 1 360 ? -9.810  -20.057 -5.107  1.00 44.48 ? 379 ARG A HD3  1 
ATOM   5570 H HE   . ARG A 1 360 ? -8.459  -21.162 -6.591  1.00 48.87 ? 379 ARG A HE   1 
ATOM   5571 H HH11 . ARG A 1 360 ? -6.858  -20.359 -3.795  1.00 51.13 ? 379 ARG A HH11 1 
ATOM   5572 H HH12 . ARG A 1 360 ? -5.700  -21.268 -4.025  1.00 51.13 ? 379 ARG A HH12 1 
ATOM   5573 H HH21 . ARG A 1 360 ? -6.667  -22.459 -6.941  1.00 53.64 ? 379 ARG A HH21 1 
ATOM   5574 H HH22 . ARG A 1 360 ? -5.584  -22.535 -5.921  1.00 53.64 ? 379 ARG A HH22 1 
ATOM   5575 N N    . VAL A 1 361 ? -8.272  -14.174 -5.321  1.00 17.83 ? 380 VAL A N    1 
ATOM   5576 C CA   . VAL A 1 361 ? -8.773  -12.809 -5.438  1.00 18.24 ? 380 VAL A CA   1 
ATOM   5577 C C    . VAL A 1 361 ? -8.551  -12.315 -6.857  1.00 18.80 ? 380 VAL A C    1 
ATOM   5578 O O    . VAL A 1 361 ? -7.583  -12.684 -7.523  1.00 20.01 ? 380 VAL A O    1 
ATOM   5579 C CB   . VAL A 1 361 ? -8.157  -11.859 -4.375  1.00 21.24 ? 380 VAL A CB   1 
ATOM   5580 C CG1  . VAL A 1 361 ? -6.658  -11.811 -4.500  1.00 22.34 ? 380 VAL A CG1  1 
ATOM   5581 C CG2  . VAL A 1 361 ? -8.745  -10.455 -4.495  1.00 22.11 ? 380 VAL A CG2  1 
ATOM   5582 H H    . VAL A 1 361 ? -7.571  -14.348 -5.788  1.00 21.40 ? 380 VAL A H    1 
ATOM   5583 H HA   . VAL A 1 361 ? -9.731  -12.809 -5.289  1.00 21.89 ? 380 VAL A HA   1 
ATOM   5584 H HB   . VAL A 1 361 ? -8.376  -12.206 -3.496  1.00 25.50 ? 380 VAL A HB   1 
ATOM   5585 H HG11 . VAL A 1 361 ? -6.300  -11.254 -3.790  1.00 26.81 ? 380 VAL A HG11 1 
ATOM   5586 H HG12 . VAL A 1 361 ? -6.306  -12.711 -4.423  1.00 26.81 ? 380 VAL A HG12 1 
ATOM   5587 H HG13 . VAL A 1 361 ? -6.425  -11.436 -5.363  1.00 26.81 ? 380 VAL A HG13 1 
ATOM   5588 H HG21 . VAL A 1 361 ? -8.505  -9.944  -3.706  1.00 26.53 ? 380 VAL A HG21 1 
ATOM   5589 H HG22 . VAL A 1 361 ? -8.385  -10.029 -5.288  1.00 26.53 ? 380 VAL A HG22 1 
ATOM   5590 H HG23 . VAL A 1 361 ? -9.710  -10.522 -4.564  1.00 26.53 ? 380 VAL A HG23 1 
ATOM   5591 N N    . ASP A 1 362 ? -9.483  -11.499 -7.326  1.00 18.12 ? 381 ASP A N    1 
ATOM   5592 C CA   . ASP A 1 362 ? -9.426  -10.883 -8.649  1.00 18.84 ? 381 ASP A CA   1 
ATOM   5593 C C    . ASP A 1 362 ? -9.437  -9.368  -8.450  1.00 17.96 ? 381 ASP A C    1 
ATOM   5594 O O    . ASP A 1 362 ? -10.448 -8.797  -8.033  1.00 17.77 ? 381 ASP A O    1 
ATOM   5595 C CB   . ASP A 1 362 ? -10.603 -11.362 -9.493  1.00 20.29 ? 381 ASP A CB   1 
ATOM   5596 C CG   . ASP A 1 362 ? -10.533 -10.882 -10.931 1.00 23.24 ? 381 ASP A CG   1 
ATOM   5597 O OD1  . ASP A 1 362 ? -10.050 -9.754  -11.179 1.00 22.75 ? 381 ASP A OD1  1 
ATOM   5598 O OD2  . ASP A 1 362 ? -11.007 -11.625 -11.817 1.00 26.24 ? 381 ASP A OD2  1 
ATOM   5599 H H    . ASP A 1 362 ? -10.185 -11.276 -6.882  1.00 21.75 ? 381 ASP A H    1 
ATOM   5600 H HA   . ASP A 1 362 ? -8.605  -11.117 -9.111  1.00 22.62 ? 381 ASP A HA   1 
ATOM   5601 H HB2  . ASP A 1 362 ? -10.612 -12.332 -9.501  1.00 24.35 ? 381 ASP A HB2  1 
ATOM   5602 H HB3  . ASP A 1 362 ? -11.427 -11.026 -9.105  1.00 24.35 ? 381 ASP A HB3  1 
ATOM   5603 N N    . LEU A 1 363 ? -8.291  -8.728  -8.689  1.00 17.82 ? 382 LEU A N    1 
ATOM   5604 C CA   . LEU A 1 363 ? -8.169  -7.295  -8.445  1.00 18.17 ? 382 LEU A CA   1 
ATOM   5605 C C    . LEU A 1 363 ? -8.988  -6.484  -9.436  1.00 19.47 ? 382 LEU A C    1 
ATOM   5606 O O    . LEU A 1 363 ? -9.325  -5.333  -9.146  1.00 19.51 ? 382 LEU A O    1 
ATOM   5607 C CB   . LEU A 1 363 ? -6.700  -6.893  -8.539  1.00 18.29 ? 382 LEU A CB   1 
ATOM   5608 C CG   . LEU A 1 363 ? -5.784  -7.554  -7.504  1.00 18.05 ? 382 LEU A CG   1 
ATOM   5609 C CD1  . LEU A 1 363 ? -4.355  -7.075  -7.739  1.00 17.98 ? 382 LEU A CD1  1 
ATOM   5610 C CD2  . LEU A 1 363 ? -6.217  -7.250  -6.086  1.00 17.90 ? 382 LEU A CD2  1 
ATOM   5611 H H    . LEU A 1 363 ? -7.576  -9.098  -8.991  1.00 21.39 ? 382 LEU A H    1 
ATOM   5612 H HA   . LEU A 1 363 ? -8.488  -7.090  -7.552  1.00 21.81 ? 382 LEU A HA   1 
ATOM   5613 H HB2  . LEU A 1 363 ? -6.370  -7.136  -9.418  1.00 21.95 ? 382 LEU A HB2  1 
ATOM   5614 H HB3  . LEU A 1 363 ? -6.636  -5.933  -8.415  1.00 21.95 ? 382 LEU A HB3  1 
ATOM   5615 H HG   . LEU A 1 363 ? -5.832  -8.517  -7.606  1.00 21.67 ? 382 LEU A HG   1 
ATOM   5616 H HD11 . LEU A 1 363 ? -3.758  -7.561  -7.149  1.00 21.59 ? 382 LEU A HD11 1 
ATOM   5617 H HD12 . LEU A 1 363 ? -4.114  -7.241  -8.663  1.00 21.59 ? 382 LEU A HD12 1 
ATOM   5618 H HD13 . LEU A 1 363 ? -4.305  -6.125  -7.549  1.00 21.59 ? 382 LEU A HD13 1 
ATOM   5619 H HD21 . LEU A 1 363 ? -5.529  -7.555  -5.474  1.00 21.48 ? 382 LEU A HD21 1 
ATOM   5620 H HD22 . LEU A 1 363 ? -6.341  -6.292  -5.992  1.00 21.48 ? 382 LEU A HD22 1 
ATOM   5621 H HD23 . LEU A 1 363 ? -7.050  -7.711  -5.905  1.00 21.48 ? 382 LEU A HD23 1 
ATOM   5622 N N    . GLU A 1 364 ? -9.345  -7.063  -10.585 1.00 19.87 ? 383 GLU A N    1 
ATOM   5623 C CA   . GLU A 1 364 ? -10.084 -6.310  -11.595 1.00 22.16 ? 383 GLU A CA   1 
ATOM   5624 C C    . GLU A 1 364 ? -11.569 -6.251  -11.267 1.00 21.74 ? 383 GLU A C    1 
ATOM   5625 O O    . GLU A 1 364 ? -12.196 -5.191  -11.406 1.00 21.33 ? 383 GLU A O    1 
ATOM   5626 C CB   . GLU A 1 364 ? -9.861  -6.937  -12.970 1.00 24.00 ? 383 GLU A CB   1 
ATOM   5627 C CG   . GLU A 1 364 ? -10.874 -6.486  -14.012 1.00 27.20 ? 383 GLU A CG   1 
ATOM   5628 C CD   . GLU A 1 364 ? -10.547 -6.967  -15.417 1.00 30.24 ? 383 GLU A CD   1 
ATOM   5629 O OE1  . GLU A 1 364 ? -9.865  -8.002  -15.566 1.00 29.38 ? 383 GLU A OE1  1 
ATOM   5630 O OE2  . GLU A 1 364 ? -10.997 -6.300  -16.369 1.00 32.80 ? 383 GLU A OE2  1 
ATOM   5631 H H    . GLU A 1 364 ? -9.174  -7.878  -10.800 1.00 23.84 ? 383 GLU A H    1 
ATOM   5632 H HA   . GLU A 1 364 ? -9.749  -5.400  -11.622 1.00 26.60 ? 383 GLU A HA   1 
ATOM   5633 H HB2  . GLU A 1 364 ? -8.978  -6.691  -13.287 1.00 28.81 ? 383 GLU A HB2  1 
ATOM   5634 H HB3  . GLU A 1 364 ? -9.927  -7.902  -12.889 1.00 28.81 ? 383 GLU A HB3  1 
ATOM   5635 H HG2  . GLU A 1 364 ? -11.747 -6.837  -13.773 1.00 32.65 ? 383 GLU A HG2  1 
ATOM   5636 H HG3  . GLU A 1 364 ? -10.898 -5.517  -14.027 1.00 32.65 ? 383 GLU A HG3  1 
ATOM   5637 N N    . SER A 1 365 ? -12.146 -7.373  -10.823 1.00 22.28 ? 384 SER A N    1 
ATOM   5638 C CA   . SER A 1 365 ? -13.559 -7.424  -10.465 1.00 21.76 ? 384 SER A CA   1 
ATOM   5639 C C    . SER A 1 365 ? -13.799 -7.172  -8.982  1.00 21.68 ? 384 SER A C    1 
ATOM   5640 O O    . SER A 1 365 ? -14.948 -6.986  -8.574  1.00 21.39 ? 384 SER A O    1 
ATOM   5641 C CB   . SER A 1 365 ? -14.148 -8.787  -10.838 1.00 22.51 ? 384 SER A CB   1 
ATOM   5642 O OG   . SER A 1 365 ? -13.444 -9.812  -10.159 1.00 21.75 ? 384 SER A OG   1 
ATOM   5643 H H    . SER A 1 365 ? -11.734 -8.120  -10.721 1.00 26.75 ? 384 SER A H    1 
ATOM   5644 H HA   . SER A 1 365 ? -14.032 -6.744  -10.969 1.00 26.12 ? 384 SER A HA   1 
ATOM   5645 H HB2  . SER A 1 365 ? -15.082 -8.814  -10.579 1.00 27.02 ? 384 SER A HB2  1 
ATOM   5646 H HB3  . SER A 1 365 ? -14.064 -8.921  -11.795 1.00 27.02 ? 384 SER A HB3  1 
ATOM   5647 H HG   . SER A 1 365 ? -13.639 -10.561 -10.487 1.00 26.11 ? 384 SER A HG   1 
ATOM   5648 N N    . LYS A 1 366 ? -12.742 -7.147  -8.179  1.00 21.86 ? 385 LYS A N    1 
ATOM   5649 C CA   . LYS A 1 366 ? -12.841 -6.990  -6.727  1.00 24.37 ? 385 LYS A CA   1 
ATOM   5650 C C    . LYS A 1 366 ? -13.604 -8.140  -6.089  1.00 24.10 ? 385 LYS A C    1 
ATOM   5651 O O    . LYS A 1 366 ? -14.279 -7.965  -5.070  1.00 25.20 ? 385 LYS A O    1 
ATOM   5652 C CB   . LYS A 1 366 ? -13.456 -5.650  -6.313  1.00 27.84 ? 385 LYS A CB   1 
ATOM   5653 C CG   . LYS A 1 366 ? -13.084 -4.462  -7.179  1.00 31.56 ? 385 LYS A CG   1 
ATOM   5654 C CD   . LYS A 1 366 ? -11.603 -4.113  -7.101  1.00 33.37 ? 385 LYS A CD   1 
ATOM   5655 C CE   . LYS A 1 366 ? -11.260 -2.870  -7.965  1.00 34.37 ? 385 LYS A CE   1 
ATOM   5656 N NZ   . LYS A 1 366 ? -10.937 -3.143  -9.413  1.00 34.17 ? 385 LYS A NZ   1 
ATOM   5657 H H    . LYS A 1 366 ? -11.932 -7.221  -8.456  1.00 26.24 ? 385 LYS A H    1 
ATOM   5658 H HA   . LYS A 1 366 ? -11.936 -7.001  -6.379  1.00 29.25 ? 385 LYS A HA   1 
ATOM   5659 H HB2  . LYS A 1 366 ? -14.422 -5.737  -6.343  1.00 33.42 ? 385 LYS A HB2  1 
ATOM   5660 H HB3  . LYS A 1 366 ? -13.168 -5.449  -5.409  1.00 33.42 ? 385 LYS A HB3  1 
ATOM   5661 H HG2  . LYS A 1 366 ? -13.295 -4.666  -8.103  1.00 37.88 ? 385 LYS A HG2  1 
ATOM   5662 H HG3  . LYS A 1 366 ? -13.590 -3.688  -6.887  1.00 37.88 ? 385 LYS A HG3  1 
ATOM   5663 H HD2  . LYS A 1 366 ? -11.368 -3.917  -6.180  1.00 40.05 ? 385 LYS A HD2  1 
ATOM   5664 H HD3  . LYS A 1 366 ? -11.080 -4.862  -7.425  1.00 40.05 ? 385 LYS A HD3  1 
ATOM   5665 H HE2  . LYS A 1 366 ? -12.022 -2.269  -7.949  1.00 41.25 ? 385 LYS A HE2  1 
ATOM   5666 H HE3  . LYS A 1 366 ? -10.486 -2.434  -7.576  1.00 41.25 ? 385 LYS A HE3  1 
ATOM   5667 H HZ1  . LYS A 1 366 ? -10.741 -2.382  -9.830  1.00 41.01 ? 385 LYS A HZ1  1 
ATOM   5668 H HZ2  . LYS A 1 366 ? -10.240 -3.693  -9.471  1.00 41.01 ? 385 LYS A HZ2  1 
ATOM   5669 H HZ3  . LYS A 1 366 ? -11.636 -3.520  -9.815  1.00 41.01 ? 385 LYS A HZ3  1 
ATOM   5670 N N    . GLU A 1 367 ? -13.511 -9.316  -6.691  1.00 24.89 ? 386 GLU A N    1 
ATOM   5671 C CA   . GLU A 1 367 ? -14.100 -10.528 -6.155  1.00 26.33 ? 386 GLU A CA   1 
ATOM   5672 C C    . GLU A 1 367 ? -13.032 -11.344 -5.438  1.00 23.63 ? 386 GLU A C    1 
ATOM   5673 O O    . GLU A 1 367 ? -11.844 -11.293 -5.768  1.00 23.37 ? 386 GLU A O    1 
ATOM   5674 C CB   . GLU A 1 367 ? -14.685 -11.379 -7.275  1.00 29.72 ? 386 GLU A CB   1 
ATOM   5675 C CG   . GLU A 1 367 ? -15.934 -10.796 -7.904  1.00 34.03 ? 386 GLU A CG   1 
ATOM   5676 C CD   . GLU A 1 367 ? -16.400 -11.626 -9.067  1.00 38.33 ? 386 GLU A CD   1 
ATOM   5677 O OE1  . GLU A 1 367 ? -15.623 -11.751 -10.041 1.00 39.81 ? 386 GLU A OE1  1 
ATOM   5678 O OE2  . GLU A 1 367 ? -17.526 -12.163 -9.004  1.00 40.49 ? 386 GLU A OE2  1 
ATOM   5679 H H    . GLU A 1 367 ? -13.097 -9.439  -7.435  1.00 29.88 ? 386 GLU A H    1 
ATOM   5680 H HA   . GLU A 1 367 ? -14.805 -10.297 -5.531  1.00 31.61 ? 386 GLU A HA   1 
ATOM   5681 H HB2  . GLU A 1 367 ? -14.019 -11.474 -7.974  1.00 35.67 ? 386 GLU A HB2  1 
ATOM   5682 H HB3  . GLU A 1 367 ? -14.915 -12.250 -6.915  1.00 35.67 ? 386 GLU A HB3  1 
ATOM   5683 H HG2  . GLU A 1 367 ? -16.644 -10.769 -7.244  1.00 40.84 ? 386 GLU A HG2  1 
ATOM   5684 H HG3  . GLU A 1 367 ? -15.745 -9.900  -8.225  1.00 40.84 ? 386 GLU A HG3  1 
ATOM   5685 N N    . ALA A 1 368 ? -13.464 -12.100 -4.440  1.00 21.32 ? 387 ALA A N    1 
ATOM   5686 C CA   . ALA A 1 368 ? -12.517 -12.870 -3.661  1.00 20.02 ? 387 ALA A CA   1 
ATOM   5687 C C    . ALA A 1 368 ? -13.223 -14.081 -3.092  1.00 20.44 ? 387 ALA A C    1 
ATOM   5688 O O    . ALA A 1 368 ? -14.442 -14.085 -2.913  1.00 20.82 ? 387 ALA A O    1 
ATOM   5689 C CB   . ALA A 1 368 ? -11.916 -12.045 -2.520  1.00 20.61 ? 387 ALA A CB   1 
ATOM   5690 H H    . ALA A 1 368 ? -14.287 -12.181 -4.201  1.00 25.59 ? 387 ALA A H    1 
ATOM   5691 H HA   . ALA A 1 368 ? -11.795 -13.167 -4.237  1.00 24.03 ? 387 ALA A HA   1 
ATOM   5692 H HB1  . ALA A 1 368 ? -11.284 -12.595 -2.032  1.00 24.74 ? 387 ALA A HB1  1 
ATOM   5693 H HB2  . ALA A 1 368 ? -11.464 -11.273 -2.893  1.00 24.74 ? 387 ALA A HB2  1 
ATOM   5694 H HB3  . ALA A 1 368 ? -12.630 -11.757 -1.929  1.00 24.74 ? 387 ALA A HB3  1 
ATOM   5695 N N    . GLU A 1 369 ? -12.443 -15.118 -2.827  1.00 21.03 ? 388 GLU A N    1 
ATOM   5696 C CA   . GLU A 1 369 ? -12.952 -16.329 -2.209  1.00 22.33 ? 388 GLU A CA   1 
ATOM   5697 C C    . GLU A 1 369 ? -11.882 -16.835 -1.262  1.00 19.70 ? 388 GLU A C    1 
ATOM   5698 O O    . GLU A 1 369 ? -10.697 -16.840 -1.603  1.00 19.37 ? 388 GLU A O    1 
ATOM   5699 C CB   . GLU A 1 369 ? -13.277 -17.375 -3.274  1.00 27.42 ? 388 GLU A CB   1 
ATOM   5700 C CG   . GLU A 1 369 ? -13.639 -18.735 -2.739  1.00 32.40 ? 388 GLU A CG   1 
ATOM   5701 C CD   . GLU A 1 369 ? -13.913 -19.724 -3.858  1.00 36.01 ? 388 GLU A CD   1 
ATOM   5702 O OE1  . GLU A 1 369 ? -12.943 -20.336 -4.360  1.00 37.00 ? 388 GLU A OE1  1 
ATOM   5703 O OE2  . GLU A 1 369 ? -15.089 -19.911 -4.227  1.00 37.84 ? 388 GLU A OE2  1 
ATOM   5704 H H    . GLU A 1 369 ? -11.601 -15.144 -3.000  1.00 25.24 ? 388 GLU A H    1 
ATOM   5705 H HA   . GLU A 1 369 ? -13.761 -16.156 -1.704  1.00 26.80 ? 388 GLU A HA   1 
ATOM   5706 H HB2  . GLU A 1 369 ? -14.031 -17.058 -3.796  1.00 32.91 ? 388 GLU A HB2  1 
ATOM   5707 H HB3  . GLU A 1 369 ? -12.501 -17.484 -3.845  1.00 32.91 ? 388 GLU A HB3  1 
ATOM   5708 H HG2  . GLU A 1 369 ? -12.905 -19.075 -2.205  1.00 38.88 ? 388 GLU A HG2  1 
ATOM   5709 H HG3  . GLU A 1 369 ? -14.439 -18.663 -2.194  1.00 38.88 ? 388 GLU A HG3  1 
ATOM   5710 N N    . ILE A 1 370 ? -12.294 -17.206 -0.060  1.00 18.95 ? 389 ILE A N    1 
ATOM   5711 C CA   . ILE A 1 370 ? -11.435 -17.890 0.896   1.00 19.09 ? 389 ILE A CA   1 
ATOM   5712 C C    . ILE A 1 370 ? -12.152 -19.163 1.309   1.00 20.21 ? 389 ILE A C    1 
ATOM   5713 O O    . ILE A 1 370 ? -13.244 -19.108 1.885   1.00 21.82 ? 389 ILE A O    1 
ATOM   5714 C CB   . ILE A 1 370 ? -11.095 -17.015 2.119   1.00 19.74 ? 389 ILE A CB   1 
ATOM   5715 C CG1  . ILE A 1 370 ? -10.471 -15.686 1.669   1.00 20.33 ? 389 ILE A CG1  1 
ATOM   5716 C CG2  . ILE A 1 370 ? -10.130 -17.774 3.042   1.00 20.67 ? 389 ILE A CG2  1 
ATOM   5717 C CD1  . ILE A 1 370 ? -10.221 -14.699 2.784   1.00 20.67 ? 389 ILE A CD1  1 
ATOM   5718 H H    . ILE A 1 370 ? -13.091 -17.068 0.234   1.00 22.75 ? 389 ILE A H    1 
ATOM   5719 H HA   . ILE A 1 370 ? -10.596 -18.130 0.472   1.00 22.91 ? 389 ILE A HA   1 
ATOM   5720 H HB   . ILE A 1 370 ? -11.912 -16.819 2.603   1.00 23.70 ? 389 ILE A HB   1 
ATOM   5721 H HG12 . ILE A 1 370 ? -9.618  -15.873 1.247   1.00 24.40 ? 389 ILE A HG12 1 
ATOM   5722 H HG13 . ILE A 1 370 ? -11.070 -15.264 1.033   1.00 24.40 ? 389 ILE A HG13 1 
ATOM   5723 H HG21 . ILE A 1 370 ? -9.870  -17.193 3.774   1.00 24.81 ? 389 ILE A HG21 1 
ATOM   5724 H HG22 . ILE A 1 370 ? -10.578 -18.562 3.388   1.00 24.81 ? 389 ILE A HG22 1 
ATOM   5725 H HG23 . ILE A 1 370 ? -9.347  -18.036 2.533   1.00 24.81 ? 389 ILE A HG23 1 
ATOM   5726 H HD11 . ILE A 1 370 ? -9.997  -13.837 2.399   1.00 24.81 ? 389 ILE A HD11 1 
ATOM   5727 H HD12 . ILE A 1 370 ? -11.023 -14.621 3.323   1.00 24.81 ? 389 ILE A HD12 1 
ATOM   5728 H HD13 . ILE A 1 370 ? -9.485  -15.018 3.330   1.00 24.81 ? 389 ILE A HD13 1 
ATOM   5729 N N    . ARG A 1 371 ? -11.567 -20.300 0.980   1.00 21.12 ? 390 ARG A N    1 
ATOM   5730 C CA   . ARG A 1 371 ? -12.127 -21.593 1.336   1.00 22.48 ? 390 ARG A CA   1 
ATOM   5731 C C    . ARG A 1 371 ? -11.348 -22.092 2.545   1.00 21.14 ? 390 ARG A C    1 
ATOM   5732 O O    . ARG A 1 371 ? -10.171 -22.454 2.428   1.00 22.82 ? 390 ARG A O    1 
ATOM   5733 C CB   . ARG A 1 371 ? -12.006 -22.580 0.178   1.00 26.47 ? 390 ARG A CB   1 
ATOM   5734 C CG   . ARG A 1 371 ? -12.980 -22.387 -0.954  1.00 32.46 ? 390 ARG A CG   1 
ATOM   5735 C CD   . ARG A 1 371 ? -12.460 -23.104 -2.203  1.00 38.32 ? 390 ARG A CD   1 
ATOM   5736 N NE   . ARG A 1 371 ? -13.432 -23.113 -3.285  1.00 43.73 ? 390 ARG A NE   1 
ATOM   5737 C CZ   . ARG A 1 371 ? -13.136 -22.947 -4.567  1.00 48.17 ? 390 ARG A CZ   1 
ATOM   5738 N NH1  . ARG A 1 371 ? -11.899 -22.684 -4.965  1.00 49.89 ? 390 ARG A NH1  1 
ATOM   5739 N NH2  . ARG A 1 371 ? -14.109 -23.030 -5.473  1.00 49.29 ? 390 ARG A NH2  1 
ATOM   5740 H H    . ARG A 1 371 ? -10.829 -20.351 0.541   1.00 25.36 ? 390 ARG A H    1 
ATOM   5741 H HA   . ARG A 1 371 ? -13.067 -21.502 1.557   1.00 26.99 ? 390 ARG A HA   1 
ATOM   5742 H HB2  . ARG A 1 371 ? -11.114 -22.503 -0.194  1.00 31.77 ? 390 ARG A HB2  1 
ATOM   5743 H HB3  . ARG A 1 371 ? -12.144 -23.475 0.527   1.00 31.77 ? 390 ARG A HB3  1 
ATOM   5744 H HG2  . ARG A 1 371 ? -13.842 -22.761 -0.713  1.00 38.95 ? 390 ARG A HG2  1 
ATOM   5745 H HG3  . ARG A 1 371 ? -13.071 -21.441 -1.151  1.00 38.95 ? 390 ARG A HG3  1 
ATOM   5746 H HD2  . ARG A 1 371 ? -11.662 -22.653 -2.519  1.00 45.99 ? 390 ARG A HD2  1 
ATOM   5747 H HD3  . ARG A 1 371 ? -12.253 -24.024 -1.977  1.00 45.99 ? 390 ARG A HD3  1 
ATOM   5748 H HE   . ARG A 1 371 ? -14.258 -23.235 -3.079  1.00 52.48 ? 390 ARG A HE   1 
ATOM   5749 H HH11 . ARG A 1 371 ? -11.266 -22.619 -4.386  1.00 59.88 ? 390 ARG A HH11 1 
ATOM   5750 H HH12 . ARG A 1 371 ? -11.729 -22.580 -5.802  1.00 59.88 ? 390 ARG A HH12 1 
ATOM   5751 H HH21 . ARG A 1 371 ? -14.917 -23.189 -5.223  1.00 59.15 ? 390 ARG A HH21 1 
ATOM   5752 H HH22 . ARG A 1 371 ? -13.930 -22.924 -6.307  1.00 59.15 ? 390 ARG A HH22 1 
ATOM   5753 N N    . TRP A 1 372 ? -11.998 -22.102 3.701   1.00 19.98 ? 391 TRP A N    1 
ATOM   5754 C CA   . TRP A 1 372 ? -11.377 -22.565 4.930   1.00 20.53 ? 391 TRP A CA   1 
ATOM   5755 C C    . TRP A 1 372 ? -11.586 -24.062 5.090   1.00 21.78 ? 391 TRP A C    1 
ATOM   5756 O O    . TRP A 1 372 ? -12.664 -24.585 4.803   1.00 22.44 ? 391 TRP A O    1 
ATOM   5757 C CB   . TRP A 1 372 ? -11.988 -21.855 6.133   1.00 19.30 ? 391 TRP A CB   1 
ATOM   5758 C CG   . TRP A 1 372 ? -11.876 -20.374 6.106   1.00 19.00 ? 391 TRP A CG   1 
ATOM   5759 C CD1  . TRP A 1 372 ? -12.834 -19.485 5.695   1.00 19.29 ? 391 TRP A CD1  1 
ATOM   5760 C CD2  . TRP A 1 372 ? -10.755 -19.592 6.518   1.00 17.80 ? 391 TRP A CD2  1 
ATOM   5761 N NE1  . TRP A 1 372 ? -12.369 -18.195 5.837   1.00 19.94 ? 391 TRP A NE1  1 
ATOM   5762 C CE2  . TRP A 1 372 ? -11.095 -18.241 6.335   1.00 18.31 ? 391 TRP A CE2  1 
ATOM   5763 C CE3  . TRP A 1 372 ? -9.496  -19.905 7.027   1.00 17.05 ? 391 TRP A CE3  1 
ATOM   5764 C CZ2  . TRP A 1 372 ? -10.218 -17.214 6.644   1.00 18.00 ? 391 TRP A CZ2  1 
ATOM   5765 C CZ3  . TRP A 1 372 ? -8.630  -18.889 7.328   1.00 17.14 ? 391 TRP A CZ3  1 
ATOM   5766 C CH2  . TRP A 1 372 ? -8.993  -17.562 7.147   1.00 17.89 ? 391 TRP A CH2  1 
ATOM   5767 H H    . TRP A 1 372 ? -12.812 -21.841 3.799   1.00 23.98 ? 391 TRP A H    1 
ATOM   5768 H HA   . TRP A 1 372 ? -10.426 -22.378 4.897   1.00 24.64 ? 391 TRP A HA   1 
ATOM   5769 H HB2  . TRP A 1 372 ? -12.932 -22.075 6.174   1.00 23.16 ? 391 TRP A HB2  1 
ATOM   5770 H HB3  . TRP A 1 372 ? -11.540 -22.166 6.935   1.00 23.16 ? 391 TRP A HB3  1 
ATOM   5771 H HD1  . TRP A 1 372 ? -13.673 -19.717 5.368   1.00 23.15 ? 391 TRP A HD1  1 
ATOM   5772 H HE1  . TRP A 1 372 ? -12.807 -17.480 5.645   1.00 23.93 ? 391 TRP A HE1  1 
ATOM   5773 H HE3  . TRP A 1 372 ? -9.247  -20.792 7.159   1.00 20.46 ? 391 TRP A HE3  1 
ATOM   5774 H HZ2  . TRP A 1 372 ? -10.452 -16.324 6.514   1.00 21.61 ? 391 TRP A HZ2  1 
ATOM   5775 H HZ3  . TRP A 1 372 ? -7.785  -19.091 7.660   1.00 20.58 ? 391 TRP A HZ3  1 
ATOM   5776 H HH2  . TRP A 1 372 ? -8.389  -16.892 7.373   1.00 21.48 ? 391 TRP A HH2  1 
ATOM   5777 N N    . ARG A 1 373 ? -10.565 -24.743 5.587   1.00 23.41 ? 392 ARG A N    1 
ATOM   5778 C CA   . ARG A 1 373 ? -10.623 -26.189 5.724   1.00 26.19 ? 392 ARG A CA   1 
ATOM   5779 C C    . ARG A 1 373 ? -9.849  -26.649 6.943   1.00 26.66 ? 392 ARG A C    1 
ATOM   5780 O O    . ARG A 1 373 ? -9.529  -25.851 7.833   1.00 26.19 ? 392 ARG A O    1 
ATOM   5781 C CB   . ARG A 1 373 ? -10.076 -26.823 4.443   1.00 29.88 ? 392 ARG A CB   1 
ATOM   5782 C CG   . ARG A 1 373 ? -8.621  -26.550 4.166   1.00 33.69 ? 392 ARG A CG   1 
ATOM   5783 C CD   . ARG A 1 373 ? -8.093  -27.408 3.012   1.00 37.19 ? 392 ARG A CD   1 
ATOM   5784 N NE   . ARG A 1 373 ? -6.960  -26.767 2.352   1.00 40.29 ? 392 ARG A NE   1 
ATOM   5785 C CZ   . ARG A 1 373 ? -7.042  -26.027 1.255   1.00 42.42 ? 392 ARG A CZ   1 
ATOM   5786 N NH1  . ARG A 1 373 ? -8.197  -25.829 0.637   1.00 42.88 ? 392 ARG A NH1  1 
ATOM   5787 N NH2  . ARG A 1 373 ? -5.936  -25.473 0.762   1.00 43.77 ? 392 ARG A NH2  1 
ATOM   5788 H H    . ARG A 1 373 ? -9.827  -24.390 5.852   1.00 28.10 ? 392 ARG A H    1 
ATOM   5789 H HA   . ARG A 1 373 ? -11.537 -26.487 5.849   1.00 31.44 ? 392 ARG A HA   1 
ATOM   5790 H HB2  . ARG A 1 373 ? -10.184 -27.784 4.506   1.00 35.87 ? 392 ARG A HB2  1 
ATOM   5791 H HB3  . ARG A 1 373 ? -10.584 -26.481 3.690   1.00 35.87 ? 392 ARG A HB3  1 
ATOM   5792 H HG2  . ARG A 1 373 ? -8.510  -25.617 3.926   1.00 40.44 ? 392 ARG A HG2  1 
ATOM   5793 H HG3  . ARG A 1 373 ? -8.100  -26.753 4.959   1.00 40.44 ? 392 ARG A HG3  1 
ATOM   5794 H HD2  . ARG A 1 373 ? -7.801  -28.267 3.357   1.00 44.64 ? 392 ARG A HD2  1 
ATOM   5795 H HD3  . ARG A 1 373 ? -8.797  -27.536 2.357   1.00 44.64 ? 392 ARG A HD3  1 
ATOM   5796 H HE   . ARG A 1 373 ? -6.181  -26.877 2.700   1.00 48.35 ? 392 ARG A HE   1 
ATOM   5797 H HH11 . ARG A 1 373 ? -8.916  -26.185 0.946   1.00 51.46 ? 392 ARG A HH11 1 
ATOM   5798 H HH12 . ARG A 1 373 ? -8.227  -25.346 -0.073  1.00 51.46 ? 392 ARG A HH12 1 
ATOM   5799 H HH21 . ARG A 1 373 ? -5.181  -25.597 1.154   1.00 52.53 ? 392 ARG A HH21 1 
ATOM   5800 H HH22 . ARG A 1 373 ? -5.977  -24.991 0.051   1.00 52.53 ? 392 ARG A HH22 1 
HETATM 5801 C C1   . EDO B 2 .   ? -0.991  7.008   9.848   0.94 25.24 ? 401 EDO A C1   1 
HETATM 5802 O O1   . EDO B 2 .   ? -0.705  8.304   9.280   0.94 23.08 ? 401 EDO A O1   1 
HETATM 5803 C C2   . EDO B 2 .   ? -1.954  7.251   11.003  0.94 23.96 ? 401 EDO A C2   1 
HETATM 5804 O O2   . EDO B 2 .   ? -1.348  8.217   11.892  0.94 23.73 ? 401 EDO A O2   1 
HETATM 5805 H H11  . EDO B 2 .   ? -0.074  6.533   10.204  0.94 30.30 ? 401 EDO A H11  1 
HETATM 5806 H H12  . EDO B 2 .   ? -1.442  6.351   9.101   0.94 30.30 ? 401 EDO A H12  1 
HETATM 5807 H HO1  . EDO B 2 .   ? -0.048  8.210   8.577   0.94 27.71 ? 401 EDO A HO1  1 
HETATM 5808 H H21  . EDO B 2 .   ? -2.149  6.318   11.535  0.94 28.75 ? 401 EDO A H21  1 
HETATM 5809 H H22  . EDO B 2 .   ? -2.907  7.628   10.627  0.94 28.75 ? 401 EDO A H22  1 
HETATM 5810 H HO2  . EDO B 2 .   ? -0.934  8.919   11.371  0.94 28.49 ? 401 EDO A HO2  1 
HETATM 5811 C C1   . EDO C 2 .   ? 15.211  -4.896  1.401   0.97 26.36 ? 402 EDO A C1   1 
HETATM 5812 O O1   . EDO C 2 .   ? 15.142  -5.423  0.072   0.97 30.36 ? 402 EDO A O1   1 
HETATM 5813 C C2   . EDO C 2 .   ? 13.845  -4.294  1.699   0.97 24.31 ? 402 EDO A C2   1 
HETATM 5814 O O2   . EDO C 2 .   ? 13.613  -3.247  0.745   0.97 23.59 ? 402 EDO A O2   1 
HETATM 5815 H H11  . EDO C 2 .   ? 15.991  -4.135  1.472   0.97 31.64 ? 402 EDO A H11  1 
HETATM 5816 H H12  . EDO C 2 .   ? 15.447  -5.687  2.116   0.97 31.64 ? 402 EDO A H12  1 
HETATM 5817 H HO1  . EDO C 2 .   ? 15.710  -4.902  -0.511  0.97 36.44 ? 402 EDO A HO1  1 
HETATM 5818 H H21  . EDO C 2 .   ? 13.819  -3.895  2.715   0.97 29.17 ? 402 EDO A H21  1 
HETATM 5819 H H22  . EDO C 2 .   ? 13.068  -5.058  1.619   0.97 29.17 ? 402 EDO A H22  1 
HETATM 5820 H HO2  . EDO C 2 .   ? 13.788  -3.578  -0.147  0.97 28.32 ? 402 EDO A HO2  1 
HETATM 5821 O O    . HOH D 3 .   ? 12.965  0.592   27.551  1.00 13.97 ? 501 HOH A O    1 
HETATM 5822 O O    . HOH D 3 .   ? -9.905  -5.827  16.018  1.00 25.20 ? 502 HOH A O    1 
HETATM 5823 O O    . HOH D 3 .   ? 10.051  13.081  -3.915  1.00 38.51 ? 503 HOH A O    1 
HETATM 5824 O O    . HOH D 3 .   ? 14.875  7.490   -0.693  1.00 35.99 ? 504 HOH A O    1 
HETATM 5825 O O    . HOH D 3 .   ? 8.963   4.139   1.414   1.00 23.07 ? 505 HOH A O    1 
HETATM 5826 O O    . HOH D 3 .   ? -10.995 7.049   21.250  1.00 26.11 ? 506 HOH A O    1 
HETATM 5827 O O    . HOH D 3 .   ? 9.216   18.069  28.786  1.00 25.22 ? 507 HOH A O    1 
HETATM 5828 O O    . HOH D 3 .   ? 17.037  -3.203  25.486  1.00 37.94 ? 508 HOH A O    1 
HETATM 5829 O O    . HOH D 3 .   ? -13.970 2.707   26.468  1.00 24.60 ? 509 HOH A O    1 
HETATM 5830 O O    . HOH D 3 .   ? -14.442 -14.760 18.153  1.00 26.23 ? 510 HOH A O    1 
HETATM 5831 O O    . HOH D 3 .   ? -13.848 -1.787  32.739  1.00 39.90 ? 511 HOH A O    1 
HETATM 5832 O O    . HOH D 3 .   ? 25.099  11.232  6.640   1.00 19.64 ? 512 HOH A O    1 
HETATM 5833 O O    . HOH D 3 .   ? -6.614  -7.449  33.651  1.00 18.05 ? 513 HOH A O    1 
HETATM 5834 O O    . HOH D 3 .   ? -0.855  2.456   -1.434  1.00 13.82 ? 514 HOH A O    1 
HETATM 5835 O O    . HOH D 3 .   ? -21.235 2.901   4.387   1.00 22.18 ? 515 HOH A O    1 
HETATM 5836 O O    . HOH D 3 .   ? -5.034  -13.046 16.835  1.00 27.78 ? 516 HOH A O    1 
HETATM 5837 O O    . HOH D 3 .   ? 12.162  -3.466  23.675  1.00 18.93 ? 517 HOH A O    1 
HETATM 5838 O O    . HOH D 3 .   ? -20.766 14.839  9.370   1.00 28.69 ? 518 HOH A O    1 
HETATM 5839 O O    . HOH D 3 .   ? 24.983  1.430   16.054  1.00 19.70 ? 519 HOH A O    1 
HETATM 5840 O O    . HOH D 3 .   ? 9.402   24.241  12.192  1.00 13.58 ? 520 HOH A O    1 
HETATM 5841 O O    . HOH D 3 .   ? 0.343   25.787  17.147  1.00 35.14 ? 521 HOH A O    1 
HETATM 5842 O O    . HOH D 3 .   ? -7.362  1.241   -13.508 1.00 36.22 ? 522 HOH A O    1 
HETATM 5843 O O    . HOH D 3 .   ? 17.624  19.754  -6.535  1.00 25.60 ? 523 HOH A O    1 
HETATM 5844 O O    . HOH D 3 .   ? -26.871 8.768   11.300  1.00 18.43 ? 524 HOH A O    1 
HETATM 5845 O O    . HOH D 3 .   ? 23.699  11.444  10.678  1.00 23.04 ? 525 HOH A O    1 
HETATM 5846 O O    . HOH D 3 .   ? 21.686  16.339  7.354   1.00 23.27 ? 526 HOH A O    1 
HETATM 5847 O O    . HOH D 3 .   ? -13.916 5.490   22.042  1.00 36.21 ? 527 HOH A O    1 
HETATM 5848 O O    . HOH D 3 .   ? 14.018  16.484  25.634  1.00 31.24 ? 528 HOH A O    1 
HETATM 5849 O O    . HOH D 3 .   ? -17.470 -15.674 7.686   1.00 43.96 ? 529 HOH A O    1 
HETATM 5850 O O    . HOH D 3 .   ? 7.194   -10.256 13.228  1.00 11.92 ? 530 HOH A O    1 
HETATM 5851 O O    . HOH D 3 .   ? -6.211  1.508   12.614  1.00 14.30 ? 531 HOH A O    1 
HETATM 5852 O O    . HOH D 3 .   ? -3.417  20.739  9.256   1.00 30.75 ? 532 HOH A O    1 
HETATM 5853 O O    . HOH D 3 .   ? -18.223 -2.603  0.751   1.00 35.93 ? 533 HOH A O    1 
HETATM 5854 O O    . HOH D 3 .   ? 9.402   -14.049 12.467  1.00 21.96 ? 534 HOH A O    1 
HETATM 5855 O O    . HOH D 3 .   ? -15.015 -17.388 15.666  1.00 32.73 ? 535 HOH A O    1 
HETATM 5856 O O    . HOH D 3 .   ? 1.494   4.075   3.443   1.00 12.44 ? 536 HOH A O    1 
HETATM 5857 O O    . HOH D 3 .   ? -14.299 14.388  4.746   1.00 23.44 ? 537 HOH A O    1 
HETATM 5858 O O    . HOH D 3 .   ? 15.447  26.051  9.734   1.00 25.18 ? 538 HOH A O    1 
HETATM 5859 O O    . HOH D 3 .   ? -12.022 -8.947  29.281  1.00 17.76 ? 539 HOH A O    1 
HETATM 5860 O O    . HOH D 3 .   ? 3.280   24.715  4.882   1.00 30.22 ? 540 HOH A O    1 
HETATM 5861 O O    . HOH D 3 .   ? -14.503 -1.861  28.166  1.00 27.18 ? 541 HOH A O    1 
HETATM 5862 O O    . HOH D 3 .   ? 7.007   -10.553 20.446  1.00 14.45 ? 542 HOH A O    1 
HETATM 5863 O O    . HOH D 3 .   ? 14.083  29.634  11.836  1.00 29.29 ? 543 HOH A O    1 
HETATM 5864 O O    . HOH D 3 .   ? 9.861   30.569  21.270  1.00 18.26 ? 544 HOH A O    1 
HETATM 5865 O O    . HOH D 3 .   ? -4.950  -15.282 21.008  1.00 21.91 ? 545 HOH A O    1 
HETATM 5866 O O    . HOH D 3 .   ? 3.368   23.776  15.704  1.00 13.85 ? 546 HOH A O    1 
HETATM 5867 O O    . HOH D 3 .   ? -15.918 -12.924 4.736   1.00 41.63 ? 547 HOH A O    1 
HETATM 5868 O O    . HOH D 3 .   ? 7.018   14.792  16.214  1.00 12.26 ? 548 HOH A O    1 
HETATM 5869 O O    . HOH D 3 .   ? -14.021 4.755   0.577   1.00 24.75 ? 549 HOH A O    1 
HETATM 5870 O O    . HOH D 3 .   ? 3.484   20.297  25.394  1.00 18.60 ? 550 HOH A O    1 
HETATM 5871 O O    . HOH D 3 .   ? -0.063  -21.070 -3.671  1.00 20.42 ? 551 HOH A O    1 
HETATM 5872 O O    . HOH D 3 .   ? 17.430  16.811  23.784  1.00 32.30 ? 552 HOH A O    1 
HETATM 5873 O O    . HOH D 3 .   ? 2.850   18.260  4.639   1.00 18.88 ? 553 HOH A O    1 
HETATM 5874 O O    . HOH D 3 .   ? 1.259   21.190  24.245  1.00 18.73 ? 554 HOH A O    1 
HETATM 5875 O O    . HOH D 3 .   ? 14.964  -5.245  9.914   1.00 14.34 ? 555 HOH A O    1 
HETATM 5876 O O    . HOH D 3 .   ? -5.826  -14.044 14.369  1.00 13.11 ? 556 HOH A O    1 
HETATM 5877 O O    . HOH D 3 .   ? 0.008   -12.752 -15.472 1.00 35.19 ? 557 HOH A O    1 
HETATM 5878 O O    . HOH D 3 .   ? 7.531   -7.141  24.675  1.00 22.97 ? 558 HOH A O    1 
HETATM 5879 O O    . HOH D 3 .   ? 21.331  21.193  -0.468  1.00 23.79 ? 559 HOH A O    1 
HETATM 5880 O O    . HOH D 3 .   ? -7.490  -16.960 11.024  1.00 14.45 ? 560 HOH A O    1 
HETATM 5881 O O    . HOH D 3 .   ? 18.053  -0.496  23.139  1.00 19.12 ? 561 HOH A O    1 
HETATM 5882 O O    . HOH D 3 .   ? -11.700 -8.483  26.688  1.00 15.39 ? 562 HOH A O    1 
HETATM 5883 O O    . HOH D 3 .   ? -12.244 -2.248  1.556   1.00 27.50 ? 563 HOH A O    1 
HETATM 5884 O O    . HOH D 3 .   ? -2.616  9.371   -1.842  1.00 29.31 ? 564 HOH A O    1 
HETATM 5885 O O    . HOH D 3 .   ? 11.220  -10.041 19.957  1.00 18.49 ? 565 HOH A O    1 
HETATM 5886 O O    . HOH D 3 .   ? 20.479  6.365   23.734  1.00 33.75 ? 566 HOH A O    1 
HETATM 5887 O O    . HOH D 3 .   ? -2.775  31.323  11.731  1.00 36.14 ? 567 HOH A O    1 
HETATM 5888 O O    . HOH D 3 .   ? 13.466  11.474  0.370   1.00 30.84 ? 568 HOH A O    1 
HETATM 5889 O O    . HOH D 3 .   ? -13.024 -3.532  12.018  1.00 14.04 ? 569 HOH A O    1 
HETATM 5890 O O    . HOH D 3 .   ? 4.926   -15.434 -6.059  1.00 24.76 ? 570 HOH A O    1 
HETATM 5891 O O    . HOH D 3 .   ? -16.580 -10.347 3.936   1.00 20.93 ? 571 HOH A O    1 
HETATM 5892 O O    . HOH D 3 .   ? 8.855   13.527  25.550  1.00 16.77 ? 572 HOH A O    1 
HETATM 5893 O O    . HOH D 3 .   ? 7.042   4.929   26.444  1.00 12.98 ? 573 HOH A O    1 
HETATM 5894 O O    . HOH D 3 .   ? -3.098  19.391  22.522  1.00 30.18 ? 574 HOH A O    1 
HETATM 5895 O O    . HOH D 3 .   ? -17.378 1.878   17.819  1.00 25.32 ? 575 HOH A O    1 
HETATM 5896 O O    . HOH D 3 .   ? 18.584  -4.084  14.433  1.00 19.45 ? 576 HOH A O    1 
HETATM 5897 O O    . HOH D 3 .   ? 8.519   30.068  -2.123  1.00 14.46 ? 577 HOH A O    1 
HETATM 5898 O O    . HOH D 3 .   ? -6.819  -10.938 -15.184 1.00 27.42 ? 578 HOH A O    1 
HETATM 5899 O O    . HOH D 3 .   ? 8.116   -0.975  32.418  1.00 34.44 ? 579 HOH A O    1 
HETATM 5900 O O    . HOH D 3 .   ? 9.970   -6.487  24.046  1.00 20.62 ? 580 HOH A O    1 
HETATM 5901 O O    . HOH D 3 .   ? 5.695   32.063  2.514   1.00 24.58 ? 581 HOH A O    1 
HETATM 5902 O O    . HOH D 3 .   ? -15.981 -0.279  16.878  1.00 17.33 ? 582 HOH A O    1 
HETATM 5903 O O    . HOH D 3 .   ? -11.440 7.957   30.860  1.00 22.35 ? 583 HOH A O    1 
HETATM 5904 O O    . HOH D 3 .   ? 1.100   10.348  7.373   1.00 24.48 ? 584 HOH A O    1 
HETATM 5905 O O    . HOH D 3 .   ? -12.601 -4.143  -15.890 1.00 24.37 ? 585 HOH A O    1 
HETATM 5906 O O    . HOH D 3 .   ? 22.118  19.889  6.929   1.00 27.01 ? 586 HOH A O    1 
HETATM 5907 O O    . HOH D 3 .   ? 2.874   7.406   32.437  1.00 17.00 ? 587 HOH A O    1 
HETATM 5908 O O    . HOH D 3 .   ? 1.107   22.353  16.689  1.00 18.11 ? 588 HOH A O    1 
HETATM 5909 O O    . HOH D 3 .   ? -24.173 -3.804  16.401  1.00 24.09 ? 589 HOH A O    1 
HETATM 5910 O O    . HOH D 3 .   ? 7.163   18.530  18.780  1.00 12.76 ? 590 HOH A O    1 
HETATM 5911 O O    . HOH D 3 .   ? 22.255  0.896   16.561  1.00 25.43 ? 591 HOH A O    1 
HETATM 5912 O O    . HOH D 3 .   ? -12.113 -3.111  -13.183 1.00 34.03 ? 592 HOH A O    1 
HETATM 5913 O O    . HOH D 3 .   ? -3.716  3.275   -11.530 1.00 31.99 ? 593 HOH A O    1 
HETATM 5914 O O    . HOH D 3 .   ? 19.002  5.165   1.588   1.00 33.48 ? 594 HOH A O    1 
HETATM 5915 O O    . HOH D 3 .   ? 0.398   11.746  33.499  1.00 31.89 ? 595 HOH A O    1 
HETATM 5916 O O    . HOH D 3 .   ? -15.018 -7.298  19.557  1.00 29.58 ? 596 HOH A O    1 
HETATM 5917 O O    . HOH D 3 .   ? -1.237  -15.047 13.749  1.00 13.83 ? 597 HOH A O    1 
HETATM 5918 O O    . HOH D 3 .   ? 4.947   12.374  -1.840  1.00 34.82 ? 598 HOH A O    1 
HETATM 5919 O O    . HOH D 3 .   ? 7.688   -4.579  -5.639  1.00 20.80 ? 599 HOH A O    1 
HETATM 5920 O O    . HOH D 3 .   ? 5.129   13.419  29.500  1.00 20.70 ? 600 HOH A O    1 
HETATM 5921 O O    . HOH D 3 .   ? 1.472   -24.101 15.097  1.00 36.00 ? 601 HOH A O    1 
HETATM 5922 O O    . HOH D 3 .   ? 0.054   1.377   33.646  1.00 19.20 ? 602 HOH A O    1 
HETATM 5923 O O    . HOH D 3 .   ? 7.171   6.788   2.172   1.00 20.53 ? 603 HOH A O    1 
HETATM 5924 O O    . HOH D 3 .   ? 13.974  27.302  4.097   1.00 35.21 ? 604 HOH A O    1 
HETATM 5925 O O    . HOH D 3 .   ? 6.858   -9.368  -5.322  1.00 18.08 ? 605 HOH A O    1 
HETATM 5926 O O    . HOH D 3 .   ? 8.312   -7.939  28.262  1.00 25.73 ? 606 HOH A O    1 
HETATM 5927 O O    . HOH D 3 .   ? -6.263  13.382  20.549  1.00 34.37 ? 607 HOH A O    1 
HETATM 5928 O O    . HOH D 3 .   ? 15.062  33.139  0.255   1.00 16.88 ? 608 HOH A O    1 
HETATM 5929 O O    . HOH D 3 .   ? 4.539   -15.896 -2.295  1.00 17.36 ? 609 HOH A O    1 
HETATM 5930 O O    . HOH D 3 .   ? 15.724  10.765  1.949   1.00 23.22 ? 610 HOH A O    1 
HETATM 5931 O O    . HOH D 3 .   ? -10.569 -1.084  -5.192  1.00 27.71 ? 611 HOH A O    1 
HETATM 5932 O O    . HOH D 3 .   ? 22.182  15.438  14.970  1.00 21.54 ? 612 HOH A O    1 
HETATM 5933 O O    . HOH D 3 .   ? -3.758  -0.443  -2.794  1.00 14.20 ? 613 HOH A O    1 
HETATM 5934 O O    . HOH D 3 .   ? 5.414   -3.259  -6.360  1.00 18.34 ? 614 HOH A O    1 
HETATM 5935 O O    . HOH D 3 .   ? 9.559   -14.143 21.074  1.00 32.36 ? 615 HOH A O    1 
HETATM 5936 O O    . HOH D 3 .   ? -9.166  -26.761 10.417  1.00 31.69 ? 616 HOH A O    1 
HETATM 5937 O O    . HOH D 3 .   ? -20.354 4.605   14.767  1.00 20.31 ? 617 HOH A O    1 
HETATM 5938 O O    . HOH D 3 .   ? -9.355  -10.300 -14.112 1.00 24.41 ? 618 HOH A O    1 
HETATM 5939 O O    . HOH D 3 .   ? 11.028  15.046  26.147  1.00 29.64 ? 619 HOH A O    1 
HETATM 5940 O O    . HOH D 3 .   ? 2.781   29.943  9.020   1.00 22.89 ? 620 HOH A O    1 
HETATM 5941 O O    . HOH D 3 .   ? 4.959   16.936  19.430  1.00 12.26 ? 621 HOH A O    1 
HETATM 5942 O O    . HOH D 3 .   ? 19.194  15.251  -1.299  1.00 26.94 ? 622 HOH A O    1 
HETATM 5943 O O    . HOH D 3 .   ? -2.394  -20.981 -5.413  1.00 25.93 ? 623 HOH A O    1 
HETATM 5944 O O    . HOH D 3 .   ? -8.484  -2.041  2.250   1.00 13.52 ? 624 HOH A O    1 
HETATM 5945 O O    . HOH D 3 .   ? 20.081  -0.599  11.627  1.00 20.72 ? 625 HOH A O    1 
HETATM 5946 O O    . HOH D 3 .   ? -11.740 7.711   1.687   1.00 14.08 ? 626 HOH A O    1 
HETATM 5947 O O    . HOH D 3 .   ? 19.439  3.764   3.947   1.00 24.93 ? 627 HOH A O    1 
HETATM 5948 O O    . HOH D 3 .   ? 3.886   17.657  1.993   1.00 20.64 ? 628 HOH A O    1 
HETATM 5949 O O    . HOH D 3 .   ? -7.917  -2.631  14.493  1.00 11.87 ? 629 HOH A O    1 
HETATM 5950 O O    . HOH D 3 .   ? 6.075   23.896  19.369  1.00 14.62 ? 630 HOH A O    1 
HETATM 5951 O O    . HOH D 3 .   ? 20.615  -2.624  13.449  1.00 18.64 ? 631 HOH A O    1 
HETATM 5952 O O    . HOH D 3 .   ? -13.603 -0.448  18.330  1.00 14.16 ? 632 HOH A O    1 
HETATM 5953 O O    . HOH D 3 .   ? -18.034 -9.660  13.046  1.00 33.25 ? 633 HOH A O    1 
HETATM 5954 O O    . HOH D 3 .   ? -14.432 -0.711  23.579  1.00 31.33 ? 634 HOH A O    1 
HETATM 5955 O O    . HOH D 3 .   ? -1.596  5.342   34.924  1.00 24.23 ? 635 HOH A O    1 
HETATM 5956 O O    . HOH D 3 .   ? -7.134  6.587   31.965  1.00 16.15 ? 636 HOH A O    1 
HETATM 5957 O O    . HOH D 3 .   ? 13.035  22.116  12.771  1.00 14.63 ? 637 HOH A O    1 
HETATM 5958 O O    . HOH D 3 .   ? 0.888   -22.317 12.061  1.00 26.99 ? 638 HOH A O    1 
HETATM 5959 O O    . HOH D 3 .   ? -13.292 10.721  11.242  1.00 31.80 ? 639 HOH A O    1 
HETATM 5960 O O    . HOH D 3 .   ? 10.167  -10.919 6.862   1.00 15.79 ? 640 HOH A O    1 
HETATM 5961 O O    . HOH D 3 .   ? 3.769   -11.404 -10.277 1.00 38.99 ? 641 HOH A O    1 
HETATM 5962 O O    . HOH D 3 .   ? 3.098   -15.106 21.071  1.00 31.14 ? 642 HOH A O    1 
HETATM 5963 O O    . HOH D 3 .   ? -6.938  -28.602 6.953   1.00 34.42 ? 643 HOH A O    1 
HETATM 5964 O O    . HOH D 3 .   ? 23.147  1.860   19.313  1.00 28.95 ? 644 HOH A O    1 
HETATM 5965 O O    . HOH D 3 .   ? -9.260  -19.346 17.260  1.00 19.78 ? 645 HOH A O    1 
HETATM 5966 O O    . HOH D 3 .   ? -3.560  6.783   -1.736  1.00 15.78 ? 646 HOH A O    1 
HETATM 5967 O O    . HOH D 3 .   ? -17.068 -11.864 8.895   1.00 24.96 ? 647 HOH A O    1 
HETATM 5968 O O    . HOH D 3 .   ? 12.376  24.700  -7.509  1.00 36.53 ? 648 HOH A O    1 
HETATM 5969 O O    . HOH D 3 .   ? 5.351   -8.313  31.840  1.00 38.60 ? 649 HOH A O    1 
HETATM 5970 O O    . HOH D 3 .   ? 5.122   -18.631 16.489  1.00 30.37 ? 650 HOH A O    1 
HETATM 5971 O O    . HOH D 3 .   ? 0.425   -2.844  -11.194 1.00 28.24 ? 651 HOH A O    1 
HETATM 5972 O O    . HOH D 3 .   ? -2.202  -16.881 15.598  1.00 14.92 ? 652 HOH A O    1 
HETATM 5973 O O    . HOH D 3 .   ? 11.770  -5.145  19.877  1.00 14.19 ? 653 HOH A O    1 
HETATM 5974 O O    . HOH D 3 .   ? -7.937  5.417   -5.911  1.00 21.63 ? 654 HOH A O    1 
HETATM 5975 O O    . HOH D 3 .   ? -5.671  9.112   20.400  1.00 19.55 ? 655 HOH A O    1 
HETATM 5976 O O    . HOH D 3 .   ? 19.738  19.159  20.314  1.00 20.54 ? 656 HOH A O    1 
HETATM 5977 O O    . HOH D 3 .   ? 5.872   25.748  27.964  1.00 17.18 ? 657 HOH A O    1 
HETATM 5978 O O    . HOH D 3 .   ? 11.765  -0.094  -2.673  1.00 34.66 ? 658 HOH A O    1 
HETATM 5979 O O    . HOH D 3 .   ? 23.740  3.564   4.795   1.00 23.17 ? 659 HOH A O    1 
HETATM 5980 O O    . HOH D 3 .   ? 12.701  -9.992  -1.992  1.00 19.27 ? 660 HOH A O    1 
HETATM 5981 O O    . HOH D 3 .   ? -2.973  0.655   34.374  1.00 36.40 ? 661 HOH A O    1 
HETATM 5982 O O    . HOH D 3 .   ? 7.871   26.202  11.037  1.00 13.70 ? 662 HOH A O    1 
HETATM 5983 O O    . HOH D 3 .   ? 14.830  -0.698  26.886  1.00 20.05 ? 663 HOH A O    1 
HETATM 5984 O O    . HOH D 3 .   ? -2.375  -5.188  32.992  1.00 17.13 ? 664 HOH A O    1 
HETATM 5985 O O    . HOH D 3 .   ? 21.120  17.909  5.246   1.00 18.86 ? 665 HOH A O    1 
HETATM 5986 O O    . HOH D 3 .   ? 16.705  26.488  -0.834  1.00 20.12 ? 666 HOH A O    1 
HETATM 5987 O O    . HOH D 3 .   ? -10.495 -1.707  -2.363  1.00 23.11 ? 667 HOH A O    1 
HETATM 5988 O O    . HOH D 3 .   ? -20.457 3.143   7.034   1.00 13.63 ? 668 HOH A O    1 
HETATM 5989 O O    . HOH D 3 .   ? 6.148   7.561   26.071  1.00 16.03 ? 669 HOH A O    1 
HETATM 5990 O O    . HOH D 3 .   ? 3.189   -20.481 15.465  1.00 35.34 ? 670 HOH A O    1 
HETATM 5991 O O    . HOH D 3 .   ? -25.186 8.635   6.623   1.00 16.06 ? 671 HOH A O    1 
HETATM 5992 O O    . HOH D 3 .   ? -3.704  -23.313 12.521  1.00 19.36 ? 672 HOH A O    1 
HETATM 5993 O O    . HOH D 3 .   ? -13.747 -4.085  0.819   1.00 23.11 ? 673 HOH A O    1 
HETATM 5994 O O    . HOH D 3 .   ? 4.121   -18.691 -8.255  1.00 32.39 ? 674 HOH A O    1 
HETATM 5995 O O    . HOH D 3 .   ? -6.100  -0.592  15.058  1.00 11.27 ? 675 HOH A O    1 
HETATM 5996 O O    . HOH D 3 .   ? 0.028   9.575   -1.290  1.00 33.34 ? 676 HOH A O    1 
HETATM 5997 O O    . HOH D 3 .   ? 19.849  23.731  5.009   1.00 27.40 ? 677 HOH A O    1 
HETATM 5998 O O    . HOH D 3 .   ? -9.894  -23.142 8.625   1.00 18.64 ? 678 HOH A O    1 
HETATM 5999 O O    . HOH D 3 .   ? 0.569   25.316  20.045  1.00 26.35 ? 679 HOH A O    1 
HETATM 6000 O O    . HOH D 3 .   ? 24.657  14.577  5.859   1.00 35.96 ? 680 HOH A O    1 
HETATM 6001 O O    . HOH D 3 .   ? -14.406 -12.412 19.766  1.00 28.46 ? 681 HOH A O    1 
HETATM 6002 O O    . HOH D 3 .   ? -11.979 2.015   -2.524  1.00 27.63 ? 682 HOH A O    1 
HETATM 6003 O O    . HOH D 3 .   ? 1.890   -13.015 15.541  1.00 25.74 ? 683 HOH A O    1 
HETATM 6004 O O    . HOH D 3 .   ? 22.162  -1.833  20.188  1.00 29.03 ? 684 HOH A O    1 
HETATM 6005 O O    . HOH D 3 .   ? 16.561  10.708  25.520  1.00 31.77 ? 685 HOH A O    1 
HETATM 6006 O O    . HOH D 3 .   ? 4.487   -3.959  32.727  1.00 26.68 ? 686 HOH A O    1 
HETATM 6007 O O    . HOH D 3 .   ? -0.316  3.031   1.169   1.00 13.42 ? 687 HOH A O    1 
HETATM 6008 O O    . HOH D 3 .   ? -6.790  0.513   32.982  1.00 40.12 ? 688 HOH A O    1 
HETATM 6009 O O    . HOH D 3 .   ? 11.455  -0.788  26.622  1.00 19.21 ? 689 HOH A O    1 
HETATM 6010 O O    . HOH D 3 .   ? -22.068 5.588   2.548   1.00 34.32 ? 690 HOH A O    1 
HETATM 6011 O O    . HOH D 3 .   ? 2.696   -16.551 -10.710 1.00 32.40 ? 691 HOH A O    1 
HETATM 6012 O O    . HOH D 3 .   ? -16.778 -7.603  17.023  1.00 31.54 ? 692 HOH A O    1 
HETATM 6013 O O    . HOH D 3 .   ? -5.063  14.773  22.586  1.00 32.19 ? 693 HOH A O    1 
HETATM 6014 O O    . HOH D 3 .   ? 10.404  -1.515  -4.116  1.00 28.57 ? 694 HOH A O    1 
HETATM 6015 O O    . HOH D 3 .   ? -19.174 8.373   2.627   1.00 16.62 ? 695 HOH A O    1 
HETATM 6016 O O    . HOH D 3 .   ? -17.660 -4.906  12.493  1.00 21.47 ? 696 HOH A O    1 
HETATM 6017 O O    . HOH D 3 .   ? 14.216  27.468  7.474   1.00 21.05 ? 697 HOH A O    1 
HETATM 6018 O O    . HOH D 3 .   ? 5.134   -18.968 0.775   1.00 26.72 ? 698 HOH A O    1 
HETATM 6019 O O    . HOH D 3 .   ? 5.289   33.244  9.832   1.00 20.98 ? 699 HOH A O    1 
HETATM 6020 O O    . HOH D 3 .   ? 9.514   10.853  25.013  1.00 15.50 ? 700 HOH A O    1 
HETATM 6021 O O    . HOH D 3 .   ? 4.608   -22.519 -5.126  1.00 37.02 ? 701 HOH A O    1 
HETATM 6022 O O    . HOH D 3 .   ? -5.497  4.098   -7.857  1.00 18.68 ? 702 HOH A O    1 
HETATM 6023 O O    . HOH D 3 .   ? 3.131   18.890  -0.287  1.00 32.39 ? 703 HOH A O    1 
HETATM 6024 O O    . HOH D 3 .   ? 0.214   -10.571 16.248  1.00 17.38 ? 704 HOH A O    1 
HETATM 6025 O O    . HOH D 3 .   ? 9.743   -5.762  27.524  1.00 33.32 ? 705 HOH A O    1 
HETATM 6026 O O    . HOH D 3 .   ? -11.134 5.580   -0.028  1.00 17.50 ? 706 HOH A O    1 
HETATM 6027 O O    . HOH D 3 .   ? 19.473  23.588  8.763   1.00 23.54 ? 707 HOH A O    1 
HETATM 6028 O O    . HOH D 3 .   ? -0.332  -18.182 -13.874 1.00 41.31 ? 708 HOH A O    1 
HETATM 6029 O O    . HOH D 3 .   ? -9.108  8.592   20.251  1.00 19.63 ? 709 HOH A O    1 
HETATM 6030 O O    . HOH D 3 .   ? 5.558   14.797  -5.313  1.00 29.57 ? 710 HOH A O    1 
HETATM 6031 O O    . HOH D 3 .   ? 15.518  27.000  -5.744  1.00 24.08 ? 711 HOH A O    1 
HETATM 6032 O O    . HOH D 3 .   ? 22.638  21.607  11.246  1.00 27.25 ? 712 HOH A O    1 
HETATM 6033 O O    . HOH D 3 .   ? 3.518   6.177   -9.430  1.00 37.43 ? 713 HOH A O    1 
HETATM 6034 O O    . HOH D 3 .   ? 13.861  31.951  14.469  1.00 30.20 ? 714 HOH A O    1 
HETATM 6035 O O    . HOH D 3 .   ? 13.786  14.846  -5.892  1.00 28.12 ? 715 HOH A O    1 
HETATM 6036 O O    . HOH D 3 .   ? 3.477   -20.358 12.458  1.00 24.16 ? 716 HOH A O    1 
HETATM 6037 O O    . HOH D 3 .   ? 3.909   12.883  16.835  1.00 12.27 ? 717 HOH A O    1 
HETATM 6038 O O    . HOH D 3 .   ? 13.430  -13.311 20.337  1.00 35.20 ? 718 HOH A O    1 
HETATM 6039 O O    . HOH D 3 .   ? -11.202 -1.125  33.506  1.00 21.94 ? 719 HOH A O    1 
HETATM 6040 O O    . HOH D 3 .   ? -10.389 12.795  24.967  1.00 30.96 ? 720 HOH A O    1 
HETATM 6041 O O    . HOH D 3 .   ? -15.393 -8.075  0.616   1.00 17.66 ? 721 HOH A O    1 
HETATM 6042 O O    . HOH D 3 .   ? 10.492  -2.978  28.003  1.00 33.68 ? 722 HOH A O    1 
HETATM 6043 O O    . HOH D 3 .   ? 9.633   7.483   -4.194  1.00 34.64 ? 723 HOH A O    1 
HETATM 6044 O O    . HOH D 3 .   ? -16.618 5.355   14.269  1.00 15.15 ? 724 HOH A O    1 
HETATM 6045 O O    . HOH D 3 .   ? -9.833  3.754   31.448  1.00 42.12 ? 725 HOH A O    1 
HETATM 6046 O O    . HOH D 3 .   ? 14.736  28.576  1.993   1.00 35.67 ? 726 HOH A O    1 
HETATM 6047 O O    . HOH D 3 .   ? 8.696   -14.458 15.045  1.00 19.19 ? 727 HOH A O    1 
HETATM 6048 O O    . HOH D 3 .   ? 21.694  15.395  23.582  1.00 35.03 ? 728 HOH A O    1 
HETATM 6049 O O    . HOH D 3 .   ? -1.689  19.638  16.990  1.00 22.38 ? 729 HOH A O    1 
HETATM 6050 O O    . HOH D 3 .   ? 16.386  -7.014  7.135   1.00 32.28 ? 730 HOH A O    1 
HETATM 6051 O O    . HOH D 3 .   ? 10.817  3.688   -3.273  1.00 34.17 ? 731 HOH A O    1 
HETATM 6052 O O    . HOH D 3 .   ? -7.865  14.202  25.236  1.00 25.99 ? 732 HOH A O    1 
HETATM 6053 O O    . HOH D 3 .   ? -15.262 -17.277 -0.018  1.00 25.78 ? 733 HOH A O    1 
HETATM 6054 O O    . HOH D 3 .   ? -1.454  27.708  10.146  1.00 31.83 ? 734 HOH A O    1 
HETATM 6055 O O    . HOH D 3 .   ? 10.310  -12.733 16.708  1.00 22.82 ? 735 HOH A O    1 
HETATM 6056 O O    . HOH D 3 .   ? -19.477 11.163  1.925   1.00 18.11 ? 736 HOH A O    1 
HETATM 6057 O O    . HOH D 3 .   ? -14.479 9.162   14.895  1.00 25.49 ? 737 HOH A O    1 
HETATM 6058 O O    . HOH D 3 .   ? -16.251 -11.396 -3.641  1.00 29.25 ? 738 HOH A O    1 
HETATM 6059 O O    . HOH D 3 .   ? 14.150  -7.918  -3.259  1.00 24.24 ? 739 HOH A O    1 
HETATM 6060 O O    . HOH D 3 .   ? 4.402   15.552  17.106  1.00 12.81 ? 740 HOH A O    1 
HETATM 6061 O O    . HOH D 3 .   ? 22.174  9.279   17.327  1.00 26.33 ? 741 HOH A O    1 
HETATM 6062 O O    . HOH D 3 .   ? 16.712  0.424   1.211   1.00 24.60 ? 742 HOH A O    1 
HETATM 6063 O O    . HOH D 3 .   ? 14.122  31.986  4.413   1.00 34.10 ? 743 HOH A O    1 
HETATM 6064 O O    . HOH D 3 .   ? -13.870 -2.612  -9.756  1.00 32.42 ? 744 HOH A O    1 
HETATM 6065 O O    . HOH D 3 .   ? -14.985 -21.783 3.608   1.00 29.00 ? 745 HOH A O    1 
HETATM 6066 O O    . HOH D 3 .   ? -15.854 -4.255  -9.449  1.00 41.94 ? 746 HOH A O    1 
HETATM 6067 O O    . HOH D 3 .   ? -2.731  -9.173  35.623  1.00 41.33 ? 747 HOH A O    1 
HETATM 6068 O O    . HOH D 3 .   ? 13.343  -8.573  21.719  1.00 39.68 ? 748 HOH A O    1 
HETATM 6069 O O    . HOH D 3 .   ? 0.547   11.031  2.513   1.00 46.99 ? 749 HOH A O    1 
HETATM 6070 O O    . HOH D 3 .   ? -9.480  -0.941  -10.865 1.00 28.46 ? 750 HOH A O    1 
HETATM 6071 O O    . HOH D 3 .   ? 7.600   -16.416 4.485   1.00 32.90 ? 751 HOH A O    1 
HETATM 6072 O O    . HOH D 3 .   ? 0.824   -24.590 10.128  1.00 28.49 ? 752 HOH A O    1 
HETATM 6073 O O    . HOH D 3 .   ? 4.676   -12.704 -7.778  1.00 25.65 ? 753 HOH A O    1 
HETATM 6074 O O    . HOH D 3 .   ? 23.597  9.569   3.311   1.00 36.45 ? 754 HOH A O    1 
HETATM 6075 O O    . HOH D 3 .   ? 16.199  -8.837  20.657  1.00 40.41 ? 755 HOH A O    1 
HETATM 6076 O O    . HOH D 3 .   ? 15.647  14.242  -3.866  1.00 32.50 ? 756 HOH A O    1 
HETATM 6077 O O    . HOH D 3 .   ? 17.744  25.459  10.463  1.00 32.56 ? 757 HOH A O    1 
HETATM 6078 O O    . HOH D 3 .   ? -1.491  22.342  16.012  1.00 31.60 ? 758 HOH A O    1 
HETATM 6079 O O    . HOH D 3 .   ? -0.110  17.488  25.859  1.00 33.96 ? 759 HOH A O    1 
HETATM 6080 O O    . HOH D 3 .   ? -15.510 -9.964  -1.364  1.00 40.90 ? 760 HOH A O    1 
HETATM 6081 O O    . HOH D 3 .   ? 7.165   8.061   -7.784  1.00 31.42 ? 761 HOH A O    1 
HETATM 6082 O O    . HOH D 3 .   ? 21.537  12.153  17.257  1.00 29.51 ? 762 HOH A O    1 
HETATM 6083 O O    . HOH D 3 .   ? 8.388   -13.689 -5.379  1.00 29.78 ? 763 HOH A O    1 
HETATM 6084 O O    . HOH D 3 .   ? 4.042   17.199  -5.165  1.00 36.12 ? 764 HOH A O    1 
HETATM 6085 O O    . HOH D 3 .   ? 24.065  14.970  13.134  1.00 31.61 ? 765 HOH A O    1 
HETATM 6086 O O    . HOH D 3 .   ? 3.319   27.628  5.602   1.00 37.13 ? 766 HOH A O    1 
HETATM 6087 O O    . HOH D 3 .   ? 27.045  2.101   19.504  1.00 35.81 ? 767 HOH A O    1 
HETATM 6088 O O    . HOH D 3 .   ? 20.450  25.300  15.190  1.00 28.57 ? 768 HOH A O    1 
HETATM 6089 O O    . HOH D 3 .   ? -8.819  11.509  -0.534  1.00 36.30 ? 769 HOH A O    1 
HETATM 6090 O O    . HOH D 3 .   ? 22.143  22.599  14.108  1.00 32.59 ? 770 HOH A O    1 
HETATM 6091 O O    . HOH D 3 .   ? -18.225 4.340   16.373  1.00 25.11 ? 771 HOH A O    1 
HETATM 6092 O O    . HOH D 3 .   ? -22.760 5.299   15.914  1.00 24.69 ? 772 HOH A O    1 
HETATM 6093 O O    . HOH D 3 .   ? 23.252  17.981  8.869   1.00 40.21 ? 773 HOH A O    1 
HETATM 6094 O O    . HOH D 3 .   ? -1.350  -12.952 26.982  1.00 31.76 ? 774 HOH A O    1 
HETATM 6095 O O    . HOH D 3 .   ? -18.903 -11.708 11.065  1.00 37.02 ? 775 HOH A O    1 
HETATM 6096 O O    . HOH D 3 .   ? -18.395 -10.797 1.744   1.00 37.89 ? 776 HOH A O    1 
HETATM 6097 O O    . HOH D 3 .   ? -9.721  -10.427 26.261  1.00 18.29 ? 777 HOH A O    1 
HETATM 6098 O O    . HOH D 3 .   ? -1.943  -12.599 15.394  1.00 21.64 ? 778 HOH A O    1 
HETATM 6099 O O    . HOH D 3 .   ? -18.198 7.444   13.893  1.00 24.38 ? 779 HOH A O    1 
HETATM 6100 O O    . HOH D 3 .   ? 13.003  -0.350  29.746  1.00 27.96 ? 780 HOH A O    1 
HETATM 6101 O O    . HOH D 3 .   ? -3.062  -22.948 17.044  1.00 24.01 ? 781 HOH A O    1 
HETATM 6102 O O    . HOH D 3 .   ? -19.579 2.438   2.358   1.00 36.32 ? 782 HOH A O    1 
HETATM 6103 O O    . HOH D 3 .   ? 29.080  4.607   18.799  1.00 34.39 ? 783 HOH A O    1 
HETATM 6104 O O    . HOH D 3 .   ? 3.296   25.998  22.214  1.00 32.07 ? 784 HOH A O    1 
HETATM 6105 O O    . HOH D 3 .   ? -28.199 0.354   12.003  1.00 24.02 ? 785 HOH A O    1 
HETATM 6106 O O    . HOH D 3 .   ? 3.005   26.162  17.102  1.00 18.44 ? 786 HOH A O    1 
HETATM 6107 O O    . HOH D 3 .   ? 21.888  18.526  0.720   1.00 28.78 ? 787 HOH A O    1 
HETATM 6108 O O    . HOH D 3 .   ? -4.086  -17.238 -10.016 1.00 36.56 ? 788 HOH A O    1 
HETATM 6109 O O    . HOH D 3 .   ? -23.940 7.437   14.401  1.00 34.55 ? 789 HOH A O    1 
HETATM 6110 O O    . HOH D 3 .   ? -7.098  9.038   18.144  1.00 39.50 ? 790 HOH A O    1 
HETATM 6111 O O    . HOH D 3 .   ? 19.824  24.322  2.505   1.00 29.09 ? 791 HOH A O    1 
HETATM 6112 O O    . HOH D 3 .   ? 3.845   13.890  -3.515  1.00 34.75 ? 792 HOH A O    1 
HETATM 6113 O O    . HOH D 3 .   ? 0.674   -1.203  34.638  1.00 33.88 ? 793 HOH A O    1 
HETATM 6114 O O    . HOH D 3 .   ? 8.333   9.032   26.702  1.00 17.60 ? 794 HOH A O    1 
HETATM 6115 O O    . HOH D 3 .   ? -16.466 -2.675  20.138  1.00 41.23 ? 795 HOH A O    1 
HETATM 6116 O O    . HOH D 3 .   ? 8.769   -11.201 -4.345  1.00 21.69 ? 796 HOH A O    1 
HETATM 6117 O O    . HOH D 3 .   ? 5.984   10.958  30.511  1.00 35.17 ? 797 HOH A O    1 
HETATM 6118 O O    . HOH D 3 .   ? 3.433   4.915   33.570  1.00 20.15 ? 798 HOH A O    1 
HETATM 6119 O O    . HOH D 3 .   ? 4.464   26.143  19.452  1.00 18.63 ? 799 HOH A O    1 
HETATM 6120 O O    . HOH D 3 .   ? 9.471   -10.217 24.035  1.00 36.58 ? 800 HOH A O    1 
HETATM 6121 O O    . HOH D 3 .   ? -1.319  -3.412  34.863  1.00 27.25 ? 801 HOH A O    1 
HETATM 6122 O O    . HOH D 3 .   ? -5.429  9.639   16.297  1.00 42.23 ? 802 HOH A O    1 
HETATM 6123 O O    . HOH D 3 .   ? -26.662 7.849   13.928  1.00 24.99 ? 803 HOH A O    1 
HETATM 6124 O O    . HOH D 3 .   ? 21.749  23.517  9.826   1.00 39.55 ? 804 HOH A O    1 
HETATM 6125 O O    . HOH D 3 .   ? -15.622 -6.208  -12.943 1.00 19.29 ? 805 HOH A O    1 
HETATM 6126 O O    . HOH D 3 .   ? 8.770   15.545  29.820  1.00 30.88 ? 806 HOH A O    1 
HETATM 6127 O O    . HOH D 3 .   ? -14.188 0.290   20.991  1.00 28.47 ? 807 HOH A O    1 
HETATM 6128 O O    . HOH D 3 .   ? -10.126 -3.008  0.163   1.00 18.83 ? 808 HOH A O    1 
HETATM 6129 O O    . HOH D 3 .   ? 21.935  22.264  5.494   1.00 32.65 ? 809 HOH A O    1 
HETATM 6130 O O    . HOH D 3 .   ? 7.958   13.316  28.305  1.00 23.54 ? 810 HOH A O    1 
HETATM 6131 O O    . HOH D 3 .   ? -15.560 -5.592  -0.735  1.00 25.87 ? 811 HOH A O    1 
HETATM 6132 O O    . HOH D 3 .   ? 18.265  19.158  22.613  1.00 36.79 ? 812 HOH A O    1 
HETATM 6133 O O    . HOH D 3 .   ? 7.248   -6.865  30.534  1.00 41.06 ? 813 HOH A O    1 
HETATM 6134 O O    . HOH D 3 .   ? -12.292 -23.354 9.697   1.00 27.50 ? 814 HOH A O    1 
HETATM 6135 O O    . HOH D 3 .   ? 1.420   8.673   34.311  1.00 34.06 ? 815 HOH A O    1 
HETATM 6136 O O    . HOH D 3 .   ? 13.032  27.175  -6.569  1.00 29.29 ? 816 HOH A O    1 
HETATM 6137 O O    . HOH D 3 .   ? 9.376   -11.479 21.515  1.00 18.91 ? 817 HOH A O    1 
HETATM 6138 O O    . HOH D 3 .   ? 17.303  -0.180  25.766  1.00 25.39 ? 818 HOH A O    1 
HETATM 6139 O O    . HOH D 3 .   ? -12.055 -19.574 18.209  1.00 29.54 ? 819 HOH A O    1 
HETATM 6140 O O    . HOH D 3 .   ? 11.566  -6.900  25.964  1.00 39.25 ? 820 HOH A O    1 
HETATM 6141 O O    . HOH D 3 .   ? -27.205 5.482   2.567   1.00 40.31 ? 821 HOH A O    1 
HETATM 6142 O O    . HOH D 3 .   ? -14.340 -1.579  -12.145 1.00 24.51 ? 822 HOH A O    1 
HETATM 6143 O O    . HOH D 3 .   ? 2.897   -4.275  -10.633 1.00 32.66 ? 823 HOH A O    1 
HETATM 6144 O O    . HOH D 3 .   ? -13.963 -8.222  25.290  1.00 26.14 ? 824 HOH A O    1 
HETATM 6145 O O    . HOH D 3 .   ? -13.208 -1.826  -2.177  1.00 38.90 ? 825 HOH A O    1 
HETATM 6146 O O    . HOH D 3 .   ? -23.903 -5.910  14.440  1.00 43.54 ? 826 HOH A O    1 
HETATM 6147 O O    . HOH D 3 .   ? -17.984 -14.412 3.426   1.00 40.44 ? 827 HOH A O    1 
HETATM 6148 O O    . HOH D 3 .   ? -6.289  5.868   34.438  1.00 22.16 ? 828 HOH A O    1 
HETATM 6149 O O    . HOH D 3 .   ? -5.563  -26.741 14.083  1.00 28.66 ? 829 HOH A O    1 
HETATM 6150 O O    . HOH D 3 .   ? 5.257   8.839   32.330  1.00 27.18 ? 830 HOH A O    1 
HETATM 6151 O O    . HOH D 3 .   ? 1.481   3.481   34.863  1.00 26.54 ? 831 HOH A O    1 
HETATM 6152 O O    . HOH D 3 .   ? 11.374  -11.016 -4.249  1.00 26.16 ? 832 HOH A O    1 
HETATM 6153 O O    . HOH D 3 .   ? 22.856  18.315  3.138   1.00 27.39 ? 833 HOH A O    1 
HETATM 6154 O O    . HOH D 3 .   ? 26.706  8.996   17.430  1.00 33.26 ? 834 HOH A O    1 
HETATM 6155 O O    . HOH D 3 .   ? -4.616  -24.349 14.974  1.00 22.89 ? 835 HOH A O    1 
HETATM 6156 O O    . HOH D 3 .   ? 7.160   7.512   33.485  1.00 39.14 ? 836 HOH A O    1 
HETATM 6157 O O    . HOH D 3 .   ? -5.069  -5.206  32.890  1.00 22.41 ? 837 HOH A O    1 
HETATM 6158 O O    . HOH D 3 .   ? 9.824   7.026   1.713   1.00 27.99 ? 838 HOH A O    1 
HETATM 6159 O O    . HOH D 3 .   ? 5.054   -3.892  -9.098  1.00 24.82 ? 839 HOH A O    1 
HETATM 6160 O O    . HOH D 3 .   ? 24.178  9.518   15.844  1.00 30.52 ? 840 HOH A O    1 
HETATM 6161 O O    . HOH D 3 .   ? 8.102   10.775  29.110  1.00 40.05 ? 841 HOH A O    1 
HETATM 6162 O O    . HOH D 3 .   ? 23.203  21.139  3.271   1.00 40.96 ? 842 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   . GLU A 18  ? 0.4560 0.5052 0.5363 0.0347  0.0019  0.0190  37  GLU A N   
2    C CA  . GLU A 18  ? 0.4307 0.4915 0.5281 0.0435  -0.0103 0.0065  37  GLU A CA  
3    C C   . GLU A 18  ? 0.3229 0.4309 0.4788 0.0777  -0.0323 0.0047  37  GLU A C   
4    O O   . GLU A 18  ? 0.2244 0.3940 0.4573 0.1035  -0.0482 -0.0107 37  GLU A O   
5    C CB  . GLU A 18  ? 0.4979 0.5348 0.5633 0.0003  -0.0225 0.0068  37  GLU A CB  
6    C CG  . GLU A 18  ? 0.5729 0.5682 0.5950 -0.0401 -0.0300 0.0102  37  GLU A CG  
7    C CD  . GLU A 18  ? 0.6229 0.5914 0.6231 -0.0683 -0.0382 0.0112  37  GLU A CD  
8    O OE1 . GLU A 18  ? 0.6255 0.5939 0.6280 -0.0656 -0.0472 0.0182  37  GLU A OE1 
9    O OE2 . GLU A 18  ? 0.6491 0.6064 0.6369 -0.0831 -0.0412 0.0107  37  GLU A OE2 
15   N N   . SER A 19  ? 0.2764 0.3957 0.4405 0.0859  -0.0339 0.0184  38  SER A N   
16   C CA  . SER A 19  ? 0.2312 0.3678 0.3933 0.0754  -0.0222 0.0276  38  SER A CA  
17   C C   . SER A 19  ? 0.1811 0.3124 0.3323 0.0594  -0.0196 0.0267  38  SER A C   
18   O O   . SER A 19  ? 0.1989 0.3050 0.3318 0.0668  -0.0192 0.0410  38  SER A O   
19   C CB  . SER A 19  ? 0.2606 0.3948 0.4116 0.0823  -0.0336 0.0426  38  SER A CB  
20   O OG  . SER A 19  ? 0.2498 0.4202 0.4245 0.0753  -0.0479 0.0456  38  SER A OG  
26   N N   . HIS A 20  ? 0.1356 0.2654 0.2788 0.0498  -0.0189 0.0230  39  HIS A N   
27   C CA  . HIS A 20  ? 0.1140 0.2399 0.2382 0.0077  -0.0122 0.0240  39  HIS A CA  
28   C C   . HIS A 20  ? 0.1147 0.1917 0.2018 0.0120  0.0065  0.0069  39  HIS A C   
29   O O   . HIS A 20  ? 0.1276 0.1795 0.1949 -0.0086 -0.0036 -0.0152 39  HIS A O   
30   C CB  . HIS A 20  ? 0.1088 0.2646 0.2497 -0.0175 -0.0235 0.0422  39  HIS A CB  
31   C CG  . HIS A 20  ? 0.1185 0.2849 0.2701 -0.0293 -0.0205 0.0593  39  HIS A CG  
32   N ND1 . HIS A 20  ? 0.1663 0.3142 0.2766 -0.0415 -0.0099 0.0672  39  HIS A ND1 
33   C CD2 . HIS A 20  ? 0.1349 0.3126 0.2836 -0.0419 -0.0346 0.0697  39  HIS A CD2 
34   C CE1 . HIS A 20  ? 0.1614 0.3248 0.2863 -0.0543 -0.0154 0.0738  39  HIS A CE1 
35   N NE2 . HIS A 20  ? 0.1415 0.3099 0.2805 -0.0492 -0.0450 0.0924  39  HIS A NE2 
43   N N   . TYR A 21  ? 0.1153 0.1743 0.1826 0.0094  0.0138  -0.0069 40  TYR A N   
44   C CA  . TYR A 21  ? 0.1216 0.1631 0.1700 0.0026  -0.0053 0.0069  40  TYR A CA  
45   C C   . TYR A 21  ? 0.1264 0.1679 0.1646 0.0051  -0.0081 0.0048  40  TYR A C   
46   O O   . TYR A 21  ? 0.1327 0.1724 0.1848 0.0108  -0.0031 0.0206  40  TYR A O   
47   C CB  . TYR A 21  ? 0.1303 0.1543 0.1740 0.0027  0.0001  0.0071  40  TYR A CB  
48   C CG  . TYR A 21  ? 0.1220 0.1480 0.1721 -0.0044 0.0087  0.0075  40  TYR A CG  
49   C CD1 . TYR A 21  ? 0.1340 0.1449 0.1707 -0.0177 0.0034  -0.0007 40  TYR A CD1 
50   C CD2 . TYR A 21  ? 0.1203 0.1614 0.1749 0.0098  0.0015  -0.0004 40  TYR A CD2 
51   C CE1 . TYR A 21  ? 0.1295 0.1480 0.1711 -0.0063 0.0131  -0.0131 40  TYR A CE1 
52   C CE2 . TYR A 21  ? 0.1376 0.1794 0.1793 0.0149  0.0084  -0.0053 40  TYR A CE2 
53   C CZ  . TYR A 21  ? 0.1128 0.1676 0.1731 0.0091  0.0248  -0.0035 40  TYR A CZ  
54   O OH  . TYR A 21  ? 0.1552 0.1899 0.1747 -0.0089 0.0225  -0.0131 40  TYR A OH  
64   N N   . PRO A 22  ? 0.1149 0.1564 0.1665 0.0176  -0.0019 0.0029  41  PRO A N   
65   C CA  . PRO A 22  ? 0.1217 0.1544 0.1648 0.0134  0.0053  0.0064  41  PRO A CA  
66   C C   . PRO A 22  ? 0.1217 0.1644 0.1565 -0.0026 -0.0047 0.0151  41  PRO A C   
67   O O   . PRO A 22  ? 0.1426 0.1659 0.1512 -0.0004 -0.0074 0.0043  41  PRO A O   
68   C CB  . PRO A 22  ? 0.1225 0.1638 0.1677 0.0192  0.0085  0.0131  41  PRO A CB  
69   C CG  . PRO A 22  ? 0.1459 0.1799 0.1694 0.0268  0.0047  0.0127  41  PRO A CG  
70   C CD  . PRO A 22  ? 0.1214 0.1659 0.1807 0.0186  0.0030  -0.0003 41  PRO A CD  
78   N N   . GLU A 23  ? 0.1421 0.1478 0.1426 0.0084  0.0012  0.0175  42  GLU A N   
79   C CA  . GLU A 23  ? 0.1437 0.1432 0.1611 -0.0093 -0.0092 0.0134  42  GLU A CA  
80   C C   . GLU A 23  ? 0.1521 0.1549 0.1686 0.0217  0.0028  0.0006  42  GLU A C   
81   O O   . GLU A 23  ? 0.1643 0.1841 0.1746 0.0292  0.0103  -0.0034 42  GLU A O   
82   C CB  . GLU A 23  ? 0.1688 0.1655 0.1869 -0.0214 -0.0206 0.0156  42  GLU A CB  
83   C CG  . GLU A 23  ? 0.2320 0.2041 0.2174 -0.0249 -0.0249 0.0336  42  GLU A CG  
84   C CD  . GLU A 23  ? 0.2663 0.2379 0.2492 -0.0494 0.0016  0.0713  42  GLU A CD  
85   O OE1 . GLU A 23  ? 0.3196 0.3152 0.2912 -0.0208 -0.0343 0.0422  42  GLU A OE1 
86   O OE2 . GLU A 23  ? 0.3035 0.2557 0.2406 -0.0297 -0.0228 0.0668  42  GLU A OE2 
93   N N   . PHE A 24  ? 0.1617 0.1651 0.1689 0.0070  -0.0029 -0.0117 43  PHE A N   
94   C CA  . PHE A 24  ? 0.1449 0.1598 0.1656 0.0173  0.0014  -0.0017 43  PHE A CA  
95   C C   . PHE A 24  ? 0.1665 0.1618 0.1807 0.0083  0.0001  0.0063  43  PHE A C   
96   O O   . PHE A 24  ? 0.1839 0.1796 0.2010 0.0027  -0.0351 -0.0053 43  PHE A O   
97   C CB  . PHE A 24  ? 0.1432 0.1672 0.1619 0.0207  0.0114  -0.0088 43  PHE A CB  
98   C CG  . PHE A 24  ? 0.1261 0.1564 0.1556 0.0290  -0.0005 -0.0043 43  PHE A CG  
99   C CD1 . PHE A 24  ? 0.1330 0.1553 0.1530 0.0121  0.0021  0.0002  43  PHE A CD1 
100  C CD2 . PHE A 24  ? 0.1790 0.1759 0.1519 0.0348  0.0023  -0.0085 43  PHE A CD2 
101  C CE1 . PHE A 24  ? 0.1496 0.1734 0.1566 0.0136  0.0209  0.0036  43  PHE A CE1 
102  C CE2 . PHE A 24  ? 0.1848 0.1630 0.1554 0.0154  -0.0158 -0.0196 43  PHE A CE2 
103  C CZ  . PHE A 24  ? 0.1590 0.1861 0.1581 0.0200  -0.0008 -0.0081 43  PHE A CZ  
113  N N   . SER A 25  ? 0.1592 0.1547 0.1684 -0.0096 -0.0045 0.0119  44  SER A N   
114  C CA  . SER A 25  ? 0.1912 0.1789 0.1674 -0.0118 -0.0161 0.0291  44  SER A CA  
115  C C   . SER A 25  ? 0.1830 0.1605 0.1718 -0.0081 -0.0170 0.0203  44  SER A C   
116  O O   . SER A 25  ? 0.1928 0.1552 0.1698 0.0053  -0.0116 0.0181  44  SER A O   
117  C CB  . SER A 25  ? 0.2401 0.2225 0.1725 -0.0517 -0.0077 0.0482  44  SER A CB  
118  O OG  . SER A 25  ? 0.2300 0.2685 0.1816 -0.0516 -0.0045 0.0550  44  SER A OG  
124  N N   . TRP A 26  ? 0.1796 0.1630 0.1872 0.0002  -0.0149 0.0061  45  TRP A N   
125  C CA  . TRP A 26  ? 0.1895 0.1529 0.1907 0.0056  0.0004  0.0077  45  TRP A CA  
126  C C   . TRP A 26  ? 0.1638 0.1614 0.1930 -0.0122 0.0085  0.0066  45  TRP A C   
127  O O   . TRP A 26  ? 0.1906 0.1647 0.1971 -0.0099 -0.0001 0.0185  45  TRP A O   
128  C CB  . TRP A 26  ? 0.1947 0.1597 0.2019 -0.0023 -0.0019 0.0062  45  TRP A CB  
129  C CG  . TRP A 26  ? 0.1781 0.1673 0.2008 -0.0119 0.0168  0.0023  45  TRP A CG  
130  C CD1 . TRP A 26  ? 0.2259 0.1532 0.2166 0.0118  0.0197  -0.0106 45  TRP A CD1 
131  C CD2 . TRP A 26  ? 0.1719 0.1637 0.1959 -0.0126 0.0165  0.0014  45  TRP A CD2 
132  N NE1 . TRP A 26  ? 0.2216 0.1770 0.2151 -0.0105 0.0343  -0.0355 45  TRP A NE1 
133  C CE2 . TRP A 26  ? 0.2054 0.1747 0.2060 -0.0180 0.0089  -0.0092 45  TRP A CE2 
134  C CE3 . TRP A 26  ? 0.1786 0.1716 0.1958 -0.0208 -0.0100 0.0141  45  TRP A CE3 
135  C CZ2 . TRP A 26  ? 0.2289 0.1904 0.2067 -0.0295 0.0088  -0.0004 45  TRP A CZ2 
136  C CZ3 . TRP A 26  ? 0.1957 0.1871 0.2014 -0.0365 -0.0281 0.0012  45  TRP A CZ3 
137  C CH2 . TRP A 26  ? 0.2415 0.1936 0.2039 -0.0382 -0.0171 -0.0048 45  TRP A CH2 
156  N N   . THR A 28  ? 0.1522 0.1788 0.1824 -0.0123 -0.0064 0.0095  47  THR A N   
157  C CA  . THR A 28  ? 0.1410 0.1610 0.1866 -0.0218 0.0044  0.0058  47  THR A CA  
158  C C   . THR A 28  ? 0.1345 0.1519 0.1817 -0.0090 0.0037  0.0130  47  THR A C   
159  O O   . THR A 28  ? 0.1382 0.1432 0.1894 -0.0008 0.0024  0.0002  47  THR A O   
160  C CB  . THR A 28  ? 0.1435 0.1527 0.1944 -0.0107 0.0061  0.0057  47  THR A CB  
161  O OG1 . THR A 28  ? 0.1541 0.1666 0.1948 -0.0301 0.0016  -0.0033 47  THR A OG1 
162  C CG2 . THR A 28  ? 0.1509 0.1647 0.2052 -0.0209 -0.0023 0.0162  47  THR A CG2 
170  N N   . VAL A 29  ? 0.1395 0.1373 0.1725 0.0033  0.0011  0.0105  48  VAL A N   
171  C CA  . VAL A 29  ? 0.1220 0.1419 0.1650 -0.0052 0.0055  -0.0011 48  VAL A CA  
172  C C   . VAL A 29  ? 0.1148 0.1565 0.1458 -0.0136 -0.0017 -0.0075 48  VAL A C   
173  O O   . VAL A 29  ? 0.1423 0.1528 0.1456 0.0033  -0.0095 0.0060  48  VAL A O   
174  C CB  . VAL A 29  ? 0.1394 0.1460 0.1750 -0.0136 -0.0157 0.0057  48  VAL A CB  
175  C CG1 . VAL A 29  ? 0.1501 0.1594 0.1901 -0.0090 -0.0210 0.0153  48  VAL A CG1 
176  C CG2 . VAL A 29  ? 0.1459 0.1534 0.1757 -0.0111 -0.0372 0.0008  48  VAL A CG2 
186  N N   . PRO A 30  ? 0.1054 0.1421 0.1358 0.0060  0.0053  0.0014  49  PRO A N   
187  C CA  . PRO A 30  ? 0.1091 0.1265 0.1502 -0.0157 0.0027  0.0083  49  PRO A CA  
188  C C   . PRO A 30  ? 0.1349 0.1322 0.1642 -0.0115 -0.0021 0.0137  49  PRO A C   
189  O O   . PRO A 30  ? 0.1470 0.1489 0.1590 -0.0034 -0.0002 0.0167  49  PRO A O   
190  C CB  . PRO A 30  ? 0.1504 0.1464 0.1557 -0.0056 -0.0093 0.0020  49  PRO A CB  
191  C CG  . PRO A 30  ? 0.1839 0.1712 0.1743 -0.0221 0.0019  0.0047  49  PRO A CG  
192  C CD  . PRO A 30  ? 0.1313 0.1508 0.1582 -0.0034 0.0051  -0.0049 49  PRO A CD  
200  N N   . ILE A 31  ? 0.1718 0.1319 0.1706 -0.0020 -0.0051 -0.0021 50  ILE A N   
201  C CA  . ILE A 31  ? 0.1885 0.1507 0.1853 -0.0032 0.0131  -0.0063 50  ILE A CA  
202  C C   . ILE A 31  ? 0.1698 0.1488 0.1695 0.0200  0.0016  -0.0025 50  ILE A C   
203  O O   . ILE A 31  ? 0.1773 0.1579 0.1829 0.0334  -0.0150 -0.0039 50  ILE A O   
204  C CB  . ILE A 31  ? 0.1874 0.1825 0.2221 -0.0041 0.0332  -0.0334 50  ILE A CB  
205  C CG1 . ILE A 31  ? 0.1977 0.1980 0.2383 -0.0223 0.0225  -0.0182 50  ILE A CG1 
206  C CG2 . ILE A 31  ? 0.1975 0.1966 0.2471 -0.0009 0.0425  -0.0273 50  ILE A CG2 
207  C CD1 . ILE A 31  ? 0.2098 0.2086 0.2299 -0.0463 -0.0023 -0.0169 50  ILE A CD1 
219  N N   . ALA A 32  ? 0.1197 0.1394 0.1602 -0.0086 -0.0041 -0.0032 51  ALA A N   
220  C CA  . ALA A 32  ? 0.1261 0.1478 0.1599 -0.0058 -0.0054 -0.0082 51  ALA A CA  
221  C C   . ALA A 32  ? 0.1391 0.1457 0.1461 -0.0010 0.0152  0.0015  51  ALA A C   
222  O O   . ALA A 32  ? 0.1496 0.1388 0.1537 -0.0080 0.0155  -0.0199 51  ALA A O   
223  C CB  . ALA A 32  ? 0.1202 0.1645 0.1652 -0.0027 0.0165  -0.0254 51  ALA A CB  
229  N N   . PHE A 33  ? 0.1134 0.1461 0.1270 0.0096  0.0076  0.0053  52  PHE A N   
230  C CA  . PHE A 33  ? 0.1019 0.1332 0.1297 0.0126  0.0170  -0.0037 52  PHE A CA  
231  C C   . PHE A 33  ? 0.1030 0.1394 0.1362 0.0073  0.0201  -0.0030 52  PHE A C   
232  O O   . PHE A 33  ? 0.1044 0.1449 0.1480 0.0056  0.0142  -0.0010 52  PHE A O   
233  C CB  . PHE A 33  ? 0.1440 0.1312 0.1367 0.0119  0.0130  -0.0023 52  PHE A CB  
234  C CG  . PHE A 33  ? 0.1346 0.1416 0.1405 0.0140  0.0227  0.0139  52  PHE A CG  
235  C CD1 . PHE A 33  ? 0.1380 0.1372 0.1430 0.0151  0.0175  0.0275  52  PHE A CD1 
236  C CD2 . PHE A 33  ? 0.1344 0.1456 0.1489 0.0154  0.0244  0.0198  52  PHE A CD2 
237  C CE1 . PHE A 33  ? 0.1433 0.1574 0.1564 0.0086  -0.0036 0.0183  52  PHE A CE1 
238  C CE2 . PHE A 33  ? 0.1391 0.1508 0.1610 0.0251  0.0107  0.0229  52  PHE A CE2 
239  C CZ  . PHE A 33  ? 0.1491 0.1568 0.1678 0.0166  0.0188  0.0182  52  PHE A CZ  
249  N N   . HIS A 34  ? 0.1211 0.1404 0.1365 -0.0096 0.0154  -0.0031 53  HIS A N   
250  C CA  . HIS A 34  ? 0.1187 0.1578 0.1379 0.0023  0.0251  0.0084  53  HIS A CA  
251  C C   . HIS A 34  ? 0.1127 0.1453 0.1395 0.0021  0.0035  -0.0005 53  HIS A C   
252  O O   . HIS A 34  ? 0.1333 0.1566 0.1365 0.0200  0.0032  0.0020  53  HIS A O   
253  C CB  . HIS A 34  ? 0.1142 0.1701 0.1491 0.0176  0.0219  0.0052  53  HIS A CB  
254  C CG  . HIS A 34  ? 0.1327 0.1807 0.1608 -0.0064 0.0157  0.0065  53  HIS A CG  
255  N ND1 . HIS A 34  ? 0.1955 0.1958 0.1758 -0.0247 0.0052  0.0067  53  HIS A ND1 
256  C CD2 . HIS A 34  ? 0.1510 0.1815 0.1855 -0.0185 0.0185  0.0120  53  HIS A CD2 
257  C CE1 . HIS A 34  ? 0.1884 0.1894 0.1767 -0.0135 0.0349  0.0188  53  HIS A CE1 
258  N NE2 . HIS A 34  ? 0.1707 0.1727 0.1866 -0.0253 0.0091  0.0146  53  HIS A NE2 
267  N N   . PHE A 35  ? 0.1157 0.1360 0.1296 0.0068  0.0046  -0.0026 54  PHE A N   
268  C CA  . PHE A 35  ? 0.1183 0.1339 0.1367 0.0110  0.0118  -0.0047 54  PHE A CA  
269  C C   . PHE A 35  ? 0.1041 0.1448 0.1433 0.0036  0.0225  -0.0013 54  PHE A C   
270  O O   . PHE A 35  ? 0.1162 0.1421 0.1445 0.0126  0.0081  0.0036  54  PHE A O   
271  C CB  . PHE A 35  ? 0.1007 0.1365 0.1366 0.0111  0.0282  0.0173  54  PHE A CB  
272  C CG  . PHE A 35  ? 0.1241 0.1383 0.1197 0.0049  0.0231  0.0093  54  PHE A CG  
273  C CD1 . PHE A 35  ? 0.2066 0.1576 0.1258 -0.0108 0.0397  0.0079  54  PHE A CD1 
274  C CD2 . PHE A 35  ? 0.1245 0.1476 0.1140 0.0195  0.0224  0.0099  54  PHE A CD2 
275  C CE1 . PHE A 35  ? 0.2424 0.1532 0.1365 -0.0040 0.0365  0.0103  54  PHE A CE1 
276  C CE2 . PHE A 35  ? 0.1547 0.1538 0.1145 0.0081  0.0366  0.0170  54  PHE A CE2 
277  C CZ  . PHE A 35  ? 0.2103 0.1560 0.1302 0.0010  0.0353  0.0294  54  PHE A CZ  
287  N N   . GLY A 36  ? 0.1290 0.1440 0.1369 0.0073  0.0231  -0.0071 55  GLY A N   
288  C CA  . GLY A 36  ? 0.1095 0.1646 0.1444 0.0134  0.0157  -0.0119 55  GLY A CA  
289  C C   . GLY A 36  ? 0.1117 0.1593 0.1482 0.0217  0.0245  -0.0121 55  GLY A C   
290  O O   . GLY A 36  ? 0.1063 0.1728 0.1650 0.0198  0.0151  -0.0080 55  GLY A O   
294  N N   . LYS A 37  ? 0.1309 0.1572 0.1552 0.0082  0.0262  -0.0063 56  LYS A N   
295  C CA  . LYS A 37  ? 0.1194 0.1636 0.1474 0.0052  0.0232  -0.0036 56  LYS A CA  
296  C C   . LYS A 37  ? 0.1275 0.1697 0.1676 0.0149  0.0315  -0.0074 56  LYS A C   
297  O O   . LYS A 37  ? 0.1510 0.1815 0.1552 -0.0117 0.0269  -0.0146 56  LYS A O   
298  C CB  . LYS A 37  ? 0.1348 0.1606 0.1428 -0.0060 0.0282  -0.0102 56  LYS A CB  
299  C CG  . LYS A 37  ? 0.1447 0.1601 0.1534 -0.0057 0.0414  0.0017  56  LYS A CG  
300  C CD  . LYS A 37  ? 0.1706 0.1651 0.1582 -0.0133 0.0604  0.0142  56  LYS A CD  
301  C CE  . LYS A 37  ? 0.1551 0.1727 0.1600 -0.0161 0.0632  0.0092  56  LYS A CE  
302  N NZ  . LYS A 37  ? 0.1700 0.1674 0.1719 -0.0111 0.0511  -0.0028 56  LYS A NZ  
316  N N   A SER A 38  ? 0.1559 0.1638 0.1812 0.0202  0.0259  -0.0087 57  SER A N   
317  N N   B SER A 38  ? 0.1503 0.1571 0.1706 0.0220  0.0217  -0.0178 57  SER A N   
318  C CA  A SER A 38  ? 0.1995 0.1788 0.1965 0.0214  0.0397  0.0016  57  SER A CA  
319  C CA  B SER A 38  ? 0.1819 0.1616 0.1753 0.0276  0.0306  -0.0171 57  SER A CA  
320  C C   A SER A 38  ? 0.1927 0.1801 0.1924 0.0231  0.0421  -0.0038 57  SER A C   
321  C C   B SER A 38  ? 0.1822 0.1727 0.1834 0.0265  0.0376  -0.0142 57  SER A C   
322  O O   A SER A 38  ? 0.2093 0.1869 0.1899 0.0312  0.0304  -0.0138 57  SER A O   
323  O O   B SER A 38  ? 0.1956 0.1790 0.1832 0.0334  0.0288  -0.0247 57  SER A O   
324  C CB  A SER A 38  ? 0.2387 0.1977 0.2106 0.0099  0.0421  0.0163  57  SER A CB  
325  C CB  B SER A 38  ? 0.1946 0.1620 0.1679 0.0246  0.0254  -0.0206 57  SER A CB  
326  O OG  A SER A 38  ? 0.2745 0.2266 0.2232 0.0242  0.0471  0.0235  57  SER A OG  
327  O OG  B SER A 38  ? 0.1911 0.1712 0.1579 0.0398  0.0245  -0.0289 57  SER A OG  
338  N N   . GLN A 39  ? 0.1618 0.1899 0.1853 0.0252  0.0594  -0.0055 58  GLN A N   
339  C CA  . GLN A 39  ? 0.1883 0.2228 0.1983 0.0086  0.0811  -0.0133 58  GLN A CA  
340  C C   . GLN A 39  ? 0.1795 0.1972 0.1882 0.0204  0.0526  -0.0158 58  GLN A C   
341  O O   . GLN A 39  ? 0.2213 0.1944 0.2023 0.0112  0.0553  -0.0173 58  GLN A O   
342  C CB  . GLN A 39  ? 0.2328 0.2802 0.2361 0.0103  0.0909  -0.0073 58  GLN A CB  
343  C CG  . GLN A 39  ? 0.2860 0.3202 0.2641 -0.0282 0.0559  -0.0022 58  GLN A CG  
344  C CD  . GLN A 39  ? 0.2902 0.3309 0.2757 -0.0463 0.0292  -0.0092 58  GLN A CD  
345  O OE1 . GLN A 39  ? 0.2218 0.3199 0.2684 -0.0589 0.0446  -0.0109 58  GLN A OE1 
346  N NE2 . GLN A 39  ? 0.3272 0.3443 0.2953 -0.0456 0.0326  -0.0146 58  GLN A NE2 
355  N N   . GLY A 40  ? 0.1763 0.1926 0.1712 0.0046  0.0299  -0.0180 59  GLY A N   
356  C CA  . GLY A 40  ? 0.1833 0.1729 0.1733 0.0013  0.0416  -0.0109 59  GLY A CA  
357  C C   . GLY A 40  ? 0.1582 0.1510 0.1564 0.0039  0.0393  -0.0093 59  GLY A C   
358  O O   . GLY A 40  ? 0.1730 0.1589 0.1577 -0.0022 0.0286  -0.0250 59  GLY A O   
362  N N   . LEU A 41  ? 0.1661 0.1513 0.1585 -0.0018 0.0346  -0.0111 60  LEU A N   
363  C CA  . LEU A 41  ? 0.1674 0.1429 0.1589 0.0048  0.0399  -0.0053 60  LEU A CA  
364  C C   . LEU A 41  ? 0.1660 0.1498 0.1631 0.0004  0.0383  -0.0086 60  LEU A C   
365  O O   . LEU A 41  ? 0.1656 0.1580 0.1769 -0.0065 0.0242  0.0052  60  LEU A O   
366  C CB  . LEU A 41  ? 0.1847 0.1599 0.1643 -0.0054 0.0395  -0.0006 60  LEU A CB  
367  C CG  . LEU A 41  ? 0.1887 0.1784 0.1641 -0.0204 0.0282  -0.0048 60  LEU A CG  
368  C CD1 . LEU A 41  ? 0.2169 0.2011 0.1605 -0.0285 0.0372  -0.0011 60  LEU A CD1 
369  C CD2 . LEU A 41  ? 0.1668 0.1933 0.1763 -0.0085 0.0169  -0.0162 60  LEU A CD2 
381  N N   . LEU A 42  ? 0.1397 0.1425 0.1533 -0.0092 0.0388  0.0050  61  LEU A N   
382  C CA  . LEU A 42  ? 0.1401 0.1612 0.1523 -0.0197 0.0293  -0.0006 61  LEU A CA  
383  C C   . LEU A 42  ? 0.1617 0.1665 0.1509 -0.0053 0.0277  -0.0076 61  LEU A C   
384  O O   . LEU A 42  ? 0.1707 0.1676 0.1491 -0.0225 0.0361  -0.0110 61  LEU A O   
385  C CB  . LEU A 42  ? 0.1424 0.1670 0.1496 -0.0184 0.0208  -0.0100 61  LEU A CB  
386  C CG  . LEU A 42  ? 0.1611 0.1773 0.1597 0.0053  0.0249  -0.0053 61  LEU A CG  
387  C CD1 . LEU A 42  ? 0.1757 0.1768 0.1653 0.0230  0.0151  -0.0073 61  LEU A CD1 
388  C CD2 . LEU A 42  ? 0.1770 0.2032 0.1736 0.0235  0.0300  0.0062  61  LEU A CD2 
400  N N   . THR A 43  ? 0.1527 0.1733 0.1468 -0.0070 0.0468  -0.0088 62  THR A N   
401  C CA  . THR A 43  ? 0.1494 0.1701 0.1471 -0.0103 0.0522  -0.0047 62  THR A CA  
402  C C   . THR A 43  ? 0.1732 0.1704 0.1525 -0.0133 0.0574  0.0099  62  THR A C   
403  O O   . THR A 43  ? 0.1722 0.1617 0.1639 -0.0009 0.0510  -0.0043 62  THR A O   
404  C CB  . THR A 43  ? 0.1615 0.1824 0.1663 -0.0175 0.0565  -0.0128 62  THR A CB  
405  O OG1 . THR A 43  ? 0.1866 0.1822 0.1731 -0.0148 0.0468  -0.0129 62  THR A OG1 
406  C CG2 . THR A 43  ? 0.1522 0.1907 0.1769 0.0044  0.0549  -0.0288 62  THR A CG2 
414  N N   . LYS A 44  ? 0.2018 0.1719 0.1520 -0.0095 0.0557  0.0133  63  LYS A N   
415  C CA  . LYS A 44  ? 0.2725 0.1943 0.1765 -0.0057 0.0583  0.0327  63  LYS A CA  
416  C C   . LYS A 44  ? 0.2338 0.1735 0.1831 -0.0057 0.0568  0.0269  63  LYS A C   
417  O O   . LYS A 44  ? 0.2217 0.1962 0.1816 -0.0278 0.0498  0.0358  63  LYS A O   
418  C CB  . LYS A 44  ? 0.3892 0.2548 0.2103 -0.0135 0.0851  0.0272  63  LYS A CB  
419  C CG  . LYS A 44  ? 0.4729 0.2997 0.2322 -0.0015 0.0901  0.0122  63  LYS A CG  
420  C CD  . LYS A 44  ? 0.5142 0.3367 0.2501 -0.0127 0.1100  0.0184  63  LYS A CD  
421  C CE  . LYS A 44  ? 0.5360 0.3644 0.2603 -0.0251 0.1342  0.0125  63  LYS A CE  
422  N NZ  . LYS A 44  ? 0.5494 0.3878 0.2880 -0.0350 0.1477  -0.0016 63  LYS A NZ  
436  N N   . GLU A 45  ? 0.2151 0.1609 0.2027 -0.0045 0.0512  0.0143  64  GLU A N   
437  C CA  . GLU A 45  ? 0.2141 0.1871 0.2138 -0.0217 0.0700  -0.0019 64  GLU A CA  
438  C C   . GLU A 45  ? 0.1865 0.1539 0.1811 -0.0242 0.0362  -0.0049 64  GLU A C   
439  O O   . GLU A 45  ? 0.1932 0.1545 0.1868 -0.0031 0.0383  -0.0033 64  GLU A O   
440  C CB  . GLU A 45  ? 0.2387 0.2230 0.2507 -0.0259 0.1036  0.0001  64  GLU A CB  
441  C CG  . GLU A 45  ? 0.2899 0.2442 0.2821 -0.0408 0.1278  -0.0003 64  GLU A CG  
442  C CD  . GLU A 45  ? 0.3360 0.2823 0.3127 -0.0532 0.1358  0.0114  64  GLU A CD  
443  O OE1 . GLU A 45  ? 0.3080 0.3065 0.3316 -0.0457 0.1448  0.0223  64  GLU A OE1 
444  O OE2 . GLU A 45  ? 0.4016 0.3118 0.3302 -0.0635 0.1275  0.0116  64  GLU A OE2 
451  N N   . GLU A 46  ? 0.1827 0.1329 0.1617 -0.0344 0.0383  0.0117  65  GLU A N   
452  C CA  . GLU A 46  ? 0.1780 0.1484 0.1522 0.0028  0.0290  0.0098  65  GLU A CA  
453  C C   . GLU A 46  ? 0.1873 0.1568 0.1616 -0.0063 0.0212  -0.0016 65  GLU A C   
454  O O   . GLU A 46  ? 0.1842 0.1482 0.1575 -0.0039 0.0061  -0.0043 65  GLU A O   
455  C CB  . GLU A 46  ? 0.1572 0.1442 0.1558 0.0054  0.0124  0.0031  65  GLU A CB  
456  C CG  . GLU A 46  ? 0.1596 0.1582 0.1705 0.0109  0.0180  0.0060  65  GLU A CG  
457  C CD  . GLU A 46  ? 0.1634 0.1792 0.1777 0.0055  0.0135  0.0081  65  GLU A CD  
458  O OE1 . GLU A 46  ? 0.1577 0.1663 0.1631 -0.0165 0.0327  -0.0034 65  GLU A OE1 
459  O OE2 . GLU A 46  ? 0.1660 0.2057 0.1985 0.0165  0.0109  0.0141  65  GLU A OE2 
466  N N   . ALA A 47  ? 0.1827 0.1654 0.1426 0.0002  0.0265  0.0034  66  ALA A N   
467  C CA  . ALA A 47  ? 0.1714 0.1563 0.1491 -0.0058 0.0171  0.0099  66  ALA A CA  
468  C C   . ALA A 47  ? 0.1765 0.1571 0.1601 -0.0024 0.0277  0.0084  66  ALA A C   
469  O O   . ALA A 47  ? 0.1762 0.1469 0.1680 -0.0049 0.0202  0.0062  66  ALA A O   
470  C CB  . ALA A 47  ? 0.1963 0.1602 0.1456 0.0065  0.0253  0.0141  66  ALA A CB  
476  N N   . GLU A 48  ? 0.1761 0.1340 0.1757 -0.0104 0.0358  0.0138  67  GLU A N   
477  C CA  . GLU A 48  ? 0.1863 0.1366 0.1748 -0.0086 0.0196  0.0133  67  GLU A CA  
478  C C   . GLU A 48  ? 0.1934 0.1388 0.1745 -0.0060 0.0093  0.0106  67  GLU A C   
479  O O   . GLU A 48  ? 0.1966 0.1503 0.1883 0.0073  -0.0127 0.0061  67  GLU A O   
480  C CB  . GLU A 48  ? 0.1741 0.1637 0.1736 -0.0138 0.0193  0.0065  67  GLU A CB  
481  C CG  . GLU A 48  ? 0.2041 0.1584 0.1790 -0.0268 -0.0061 0.0013  67  GLU A CG  
482  C CD  . GLU A 48  ? 0.2034 0.1768 0.1766 -0.0283 0.0044  -0.0032 67  GLU A CD  
483  O OE1 . GLU A 48  ? 0.2178 0.1929 0.1919 -0.0425 0.0174  0.0160  67  GLU A OE1 
484  O OE2 . GLU A 48  ? 0.1930 0.1896 0.1735 -0.0265 0.0279  -0.0040 67  GLU A OE2 
491  N N   . PHE A 49  ? 0.2041 0.1364 0.1702 -0.0097 0.0208  0.0035  68  PHE A N   
492  C CA  . PHE A 49  ? 0.1786 0.1332 0.1618 0.0036  0.0181  -0.0015 68  PHE A CA  
493  C C   . PHE A 49  ? 0.1629 0.1411 0.1692 -0.0020 0.0030  0.0080  68  PHE A C   
494  O O   . PHE A 49  ? 0.1964 0.1474 0.1809 -0.0021 0.0227  0.0083  68  PHE A O   
495  C CB  . PHE A 49  ? 0.1712 0.1652 0.1698 -0.0016 -0.0080 0.0105  68  PHE A CB  
496  C CG  . PHE A 49  ? 0.1663 0.1573 0.1631 0.0002  -0.0075 0.0164  68  PHE A CG  
497  C CD1 . PHE A 49  ? 0.1621 0.1658 0.1572 -0.0098 -0.0111 0.0237  68  PHE A CD1 
498  C CD2 . PHE A 49  ? 0.1646 0.1718 0.1654 0.0167  0.0183  0.0161  68  PHE A CD2 
499  C CE1 . PHE A 49  ? 0.1796 0.1676 0.1682 -0.0086 0.0030  0.0138  68  PHE A CE1 
500  C CE2 . PHE A 49  ? 0.1915 0.1703 0.1774 0.0218  0.0079  0.0049  68  PHE A CE2 
501  C CZ  . PHE A 49  ? 0.1755 0.1472 0.1546 0.0138  -0.0129 0.0040  68  PHE A CZ  
511  N N   . VAL A 50  ? 0.1658 0.1543 0.1756 -0.0045 -0.0041 0.0062  69  VAL A N   
512  C CA  . VAL A 50  ? 0.1850 0.1580 0.2013 -0.0095 0.0091  0.0308  69  VAL A CA  
513  C C   . VAL A 50  ? 0.1949 0.1629 0.1735 -0.0086 0.0079  0.0179  69  VAL A C   
514  O O   . VAL A 50  ? 0.1985 0.1783 0.1676 -0.0205 0.0080  0.0202  69  VAL A O   
515  C CB  . VAL A 50  ? 0.2224 0.1710 0.2635 -0.0092 0.0179  0.0672  69  VAL A CB  
516  C CG1 . VAL A 50  ? 0.2860 0.2084 0.2903 0.0248  0.0049  0.0550  69  VAL A CG1 
517  C CG2 . VAL A 50  ? 0.2158 0.1583 0.2841 0.0021  0.0176  0.0786  69  VAL A CG2 
527  N N   . ALA A 51  ? 0.1821 0.1666 0.1575 0.0120  0.0087  0.0155  70  ALA A N   
528  C CA  . ALA A 51  ? 0.1758 0.1542 0.1589 0.0046  -0.0043 0.0012  70  ALA A CA  
529  C C   . ALA A 51  ? 0.1522 0.1664 0.1705 0.0007  0.0172  0.0007  70  ALA A C   
530  O O   . ALA A 51  ? 0.1494 0.1757 0.1842 0.0088  0.0199  -0.0033 70  ALA A O   
531  C CB  . ALA A 51  ? 0.2130 0.1769 0.1631 0.0225  0.0111  -0.0147 70  ALA A CB  
537  N N   . THR A 52  ? 0.1412 0.1765 0.1891 -0.0099 0.0014  0.0062  71  THR A N   
538  C CA  . THR A 52  ? 0.1579 0.1873 0.1964 -0.0229 0.0242  0.0138  71  THR A CA  
539  C C   . THR A 52  ? 0.1583 0.1896 0.1873 -0.0187 0.0274  0.0042  71  THR A C   
540  O O   . THR A 52  ? 0.2301 0.2202 0.1966 0.0496  0.0105  0.0075  71  THR A O   
541  C CB  . THR A 52  ? 0.2085 0.1870 0.2173 -0.0043 0.0435  0.0312  71  THR A CB  
542  O OG1 . THR A 52  ? 0.2128 0.2094 0.2294 0.0072  0.0627  0.0476  71  THR A OG1 
543  C CG2 . THR A 52  ? 0.2639 0.1972 0.2376 -0.0067 0.0458  0.0267  71  THR A CG2 
551  N N   . ARG A 53  ? 0.1407 0.1759 0.1765 -0.0379 0.0451  0.0038  72  ARG A N   
552  C CA  . ARG A 53  ? 0.1411 0.1831 0.1703 -0.0346 0.0282  -0.0011 72  ARG A CA  
553  C C   . ARG A 53  ? 0.1510 0.1869 0.1565 -0.0334 0.0184  0.0076  72  ARG A C   
554  O O   . ARG A 53  ? 0.1525 0.2181 0.1526 -0.0453 0.0160  0.0035  72  ARG A O   
555  C CB  . ARG A 53  ? 0.1451 0.1824 0.1867 -0.0436 0.0233  -0.0034 72  ARG A CB  
556  C CG  . ARG A 53  ? 0.1445 0.1770 0.2093 -0.0372 0.0188  0.0125  72  ARG A CG  
557  C CD  . ARG A 53  ? 0.1513 0.1766 0.2157 -0.0119 0.0080  0.0176  72  ARG A CD  
558  N NE  . ARG A 53  ? 0.1506 0.1726 0.2223 0.0034  -0.0041 0.0214  72  ARG A NE  
559  C CZ  . ARG A 53  ? 0.1764 0.1680 0.2176 0.0081  0.0098  0.0400  72  ARG A CZ  
560  N NH1 . ARG A 53  ? 0.2070 0.1672 0.2292 -0.0151 0.0118  0.0404  72  ARG A NH1 
561  N NH2 . ARG A 53  ? 0.1857 0.2010 0.2226 0.0015  0.0194  0.0497  72  ARG A NH2 
575  N N   . SER A 54  ? 0.1227 0.1667 0.1384 -0.0155 0.0166  0.0073  73  SER A N   
576  C CA  . SER A 54  ? 0.1191 0.1578 0.1556 -0.0218 0.0143  0.0047  73  SER A CA  
577  C C   . SER A 54  ? 0.1276 0.1581 0.1555 -0.0096 0.0163  0.0179  73  SER A C   
578  O O   . SER A 54  ? 0.1307 0.1954 0.1611 0.0052  0.0145  0.0247  73  SER A O   
579  C CB  . SER A 54  ? 0.1373 0.1477 0.1675 -0.0127 0.0011  0.0104  73  SER A CB  
580  O OG  . SER A 54  ? 0.1546 0.1495 0.1717 0.0001  0.0058  0.0193  73  SER A OG  
586  N N   . ASN A 55  ? 0.1259 0.1409 0.1714 0.0004  0.0028  0.0082  74  ASN A N   
587  C CA  . ASN A 55  ? 0.1059 0.1271 0.1794 -0.0080 0.0223  0.0074  74  ASN A CA  
588  C C   . ASN A 55  ? 0.1218 0.1235 0.1792 0.0050  0.0171  0.0112  74  ASN A C   
589  O O   . ASN A 55  ? 0.1264 0.1408 0.1857 0.0040  0.0271  0.0183  74  ASN A O   
590  C CB  . ASN A 55  ? 0.1204 0.1204 0.1715 -0.0011 0.0246  -0.0003 74  ASN A CB  
591  C CG  . ASN A 55  ? 0.1364 0.1437 0.1687 0.0094  0.0229  0.0023  74  ASN A CG  
592  O OD1 . ASN A 55  ? 0.1888 0.1549 0.1925 0.0282  0.0438  0.0115  74  ASN A OD1 
593  N ND2 . ASN A 55  ? 0.1717 0.1640 0.1816 0.0122  0.0299  0.0105  74  ASN A ND2 
600  N N   . PHE A 56  ? 0.1115 0.1301 0.1690 -0.0095 0.0247  -0.0039 75  PHE A N   
601  C CA  . PHE A 56  ? 0.0924 0.1233 0.1530 -0.0090 0.0244  -0.0023 75  PHE A CA  
602  C C   . PHE A 56  ? 0.1010 0.1292 0.1544 -0.0030 0.0052  -0.0072 75  PHE A C   
603  O O   . PHE A 56  ? 0.1113 0.1440 0.1691 -0.0038 -0.0105 -0.0112 75  PHE A O   
604  C CB  . PHE A 56  ? 0.1215 0.1390 0.1528 0.0038  0.0250  0.0045  75  PHE A CB  
605  C CG  . PHE A 56  ? 0.1239 0.1340 0.1501 -0.0030 0.0096  -0.0069 75  PHE A CG  
606  C CD1 . PHE A 56  ? 0.1320 0.1383 0.1616 -0.0139 0.0298  0.0058  75  PHE A CD1 
607  C CD2 . PHE A 56  ? 0.1354 0.1469 0.1572 -0.0068 0.0286  -0.0194 75  PHE A CD2 
608  C CE1 . PHE A 56  ? 0.1488 0.1482 0.1537 -0.0046 0.0218  -0.0049 75  PHE A CE1 
609  C CE2 . PHE A 56  ? 0.1481 0.1529 0.1553 -0.0029 0.0373  -0.0024 75  PHE A CE2 
610  C CZ  . PHE A 56  ? 0.1405 0.1626 0.1588 -0.0223 0.0467  0.0006  75  PHE A CZ  
620  N N   . ILE A 57  ? 0.1173 0.1280 0.1472 -0.0007 0.0010  -0.0012 76  ILE A N   
621  C CA  . ILE A 57  ? 0.1137 0.1225 0.1400 0.0022  0.0140  0.0063  76  ILE A CA  
622  C C   . ILE A 57  ? 0.1003 0.1340 0.1472 0.0085  0.0096  0.0018  76  ILE A C   
623  O O   . ILE A 57  ? 0.1205 0.1400 0.1584 0.0082  -0.0111 0.0184  76  ILE A O   
624  C CB  . ILE A 57  ? 0.1140 0.1305 0.1430 0.0054  -0.0026 0.0000  76  ILE A CB  
625  C CG1 . ILE A 57  ? 0.1092 0.1532 0.1449 0.0060  0.0035  -0.0080 76  ILE A CG1 
626  C CG2 . ILE A 57  ? 0.1336 0.1280 0.1378 0.0170  0.0038  0.0117  76  ILE A CG2 
627  C CD1 . ILE A 57  ? 0.1274 0.1653 0.1465 0.0171  0.0081  -0.0041 76  ILE A CD1 
639  N N   A CYS A 58  ? 0.1157 0.1353 0.1543 0.0016  -0.0092 -0.0007 77  CYS A N   
640  N N   B CYS A 58  ? 0.1089 0.1193 0.1469 0.0064  0.0041  0.0020  77  CYS A N   
641  C CA  A CYS A 58  ? 0.1130 0.1380 0.1583 0.0005  0.0031  0.0055  77  CYS A CA  
642  C CA  B CYS A 58  ? 0.1078 0.1070 0.1443 0.0038  0.0132  0.0122  77  CYS A CA  
643  C C   A CYS A 58  ? 0.1246 0.1349 0.1654 -0.0027 0.0022  0.0002  77  CYS A C   
644  C C   B CYS A 58  ? 0.1237 0.1170 0.1562 0.0000  0.0074  0.0124  77  CYS A C   
645  O O   A CYS A 58  ? 0.1407 0.1260 0.1591 0.0139  -0.0011 -0.0188 77  CYS A O   
646  O O   B CYS A 58  ? 0.1239 0.1092 0.1497 0.0028  0.0101  0.0219  77  CYS A O   
647  C CB  A CYS A 58  ? 0.1087 0.1845 0.1653 0.0027  -0.0002 0.0105  77  CYS A CB  
648  C CB  B CYS A 58  ? 0.0985 0.1132 0.1355 0.0010  0.0190  0.0189  77  CYS A CB  
649  S SG  A CYS A 58  ? 0.1605 0.2480 0.1719 -0.0250 0.0037  0.0061  77  CYS A SG  
650  S SG  B CYS A 58  ? 0.1016 0.1246 0.1332 -0.0071 0.0237  0.0106  77  CYS A SG  
660  N N   . LEU A 59  ? 0.1426 0.1344 0.1657 0.0085  -0.0051 0.0017  78  LEU A N   
661  C CA  . LEU A 59  ? 0.1127 0.1381 0.1736 0.0068  0.0027  -0.0083 78  LEU A CA  
662  C C   . LEU A 59  ? 0.1048 0.1376 0.1684 0.0017  0.0386  -0.0029 78  LEU A C   
663  O O   . LEU A 59  ? 0.1254 0.1332 0.1866 -0.0014 0.0228  0.0144  78  LEU A O   
664  C CB  . LEU A 59  ? 0.1235 0.1368 0.1776 -0.0056 0.0189  0.0021  78  LEU A CB  
665  C CG  . LEU A 59  ? 0.1426 0.1398 0.1743 -0.0083 0.0234  0.0004  78  LEU A CG  
666  C CD1 . LEU A 59  ? 0.1378 0.1426 0.1692 0.0027  0.0198  -0.0037 78  LEU A CD1 
667  C CD2 . LEU A 59  ? 0.1566 0.1483 0.1613 -0.0017 0.0347  0.0006  78  LEU A CD2 
678  N N   . GLU A 60  ? 0.1062 0.1426 0.1633 0.0000  0.0244  0.0068  79  GLU A N   
679  C CA  . GLU A 60  ? 0.1155 0.1400 0.1497 0.0038  0.0152  0.0062  79  GLU A CA  
680  C C   . GLU A 60  ? 0.1246 0.1521 0.1554 -0.0034 0.0294  0.0046  79  GLU A C   
681  O O   . GLU A 60  ? 0.1510 0.1514 0.1556 -0.0070 0.0192  0.0096  79  GLU A O   
682  C CB  . GLU A 60  ? 0.1266 0.1506 0.1553 0.0041  0.0301  0.0105  79  GLU A CB  
683  C CG  . GLU A 60  ? 0.1957 0.1715 0.1574 -0.0008 0.0085  0.0064  79  GLU A CG  
684  C CD  . GLU A 60  ? 0.2453 0.1852 0.1647 0.0082  0.0310  -0.0045 79  GLU A CD  
685  O OE1 . GLU A 60  ? 0.2345 0.1912 0.1717 0.0167  0.0007  -0.0015 79  GLU A OE1 
686  O OE2 . GLU A 60  ? 0.3076 0.1972 0.1847 -0.0186 0.0215  -0.0182 79  GLU A OE2 
693  N N   . LYS A 61  ? 0.1416 0.1405 0.1572 -0.0051 0.0172  -0.0009 80  LYS A N   
694  C CA  . LYS A 61  ? 0.1572 0.1391 0.1591 -0.0038 0.0341  -0.0010 80  LYS A CA  
695  C C   . LYS A 61  ? 0.1645 0.1549 0.1640 -0.0023 0.0211  -0.0107 80  LYS A C   
696  O O   . LYS A 61  ? 0.1647 0.1554 0.1699 -0.0023 0.0107  -0.0058 80  LYS A O   
697  C CB  . LYS A 61  ? 0.2057 0.1589 0.1795 -0.0047 0.0262  0.0122  80  LYS A CB  
698  C CG  . LYS A 61  ? 0.2387 0.1946 0.2071 -0.0084 0.0131  0.0389  80  LYS A CG  
699  C CD  . LYS A 61  ? 0.2622 0.2092 0.2223 -0.0080 -0.0017 0.0443  80  LYS A CD  
700  C CE  . LYS A 61  ? 0.2998 0.2216 0.2575 -0.0212 0.0148  0.0599  80  LYS A CE  
701  N NZ  . LYS A 61  ? 0.3287 0.2473 0.2713 -0.0316 -0.0169 0.0589  80  LYS A NZ  
715  N N   . GLY A 62  ? 0.1580 0.1508 0.1531 -0.0075 0.0383  -0.0086 81  GLY A N   
716  C CA  . GLY A 62  ? 0.1539 0.1426 0.1606 -0.0024 0.0471  0.0028  81  GLY A CA  
717  C C   . GLY A 62  ? 0.1539 0.1380 0.1540 -0.0001 0.0370  -0.0038 81  GLY A C   
718  O O   . GLY A 62  ? 0.1672 0.1545 0.1662 -0.0014 0.0434  -0.0072 81  GLY A O   
722  N N   . HIS A 63  ? 0.1620 0.1419 0.1625 -0.0233 0.0480  0.0085  82  HIS A N   
723  C CA  . HIS A 63  ? 0.1372 0.1523 0.1483 -0.0176 0.0339  -0.0018 82  HIS A CA  
724  C C   . HIS A 63  ? 0.1413 0.1571 0.1486 -0.0124 0.0359  -0.0069 82  HIS A C   
725  O O   . HIS A 63  ? 0.1479 0.1675 0.1520 -0.0057 0.0177  -0.0042 82  HIS A O   
726  C CB  . HIS A 63  ? 0.1345 0.1581 0.1450 0.0002  0.0032  -0.0084 82  HIS A CB  
727  C CG  . HIS A 63  ? 0.1242 0.1488 0.1446 -0.0158 0.0190  -0.0162 82  HIS A CG  
728  N ND1 . HIS A 63  ? 0.1301 0.1543 0.1534 -0.0101 0.0300  -0.0167 82  HIS A ND1 
729  C CD2 . HIS A 63  ? 0.1271 0.1369 0.1536 -0.0207 0.0140  -0.0060 82  HIS A CD2 
730  C CE1 . HIS A 63  ? 0.1398 0.1534 0.1593 -0.0091 0.0259  -0.0120 82  HIS A CE1 
731  N NE2 . HIS A 63  ? 0.1209 0.1458 0.1530 -0.0278 0.0235  0.0053  82  HIS A NE2 
739  N N   . ALA A 64  ? 0.1470 0.1676 0.1610 -0.0020 0.0335  -0.0161 83  ALA A N   
740  C CA  . ALA A 64  ? 0.1553 0.1580 0.1441 0.0014  0.0366  -0.0193 83  ALA A CA  
741  C C   . ALA A 64  ? 0.1869 0.1635 0.1547 0.0077  0.0356  -0.0214 83  ALA A C   
742  O O   . ALA A 64  ? 0.2299 0.1655 0.1624 -0.0059 0.0295  -0.0185 83  ALA A O   
743  C CB  . ALA A 64  ? 0.1597 0.1680 0.1590 -0.0075 0.0313  -0.0163 83  ALA A CB  
749  N N   . THR A 65  ? 0.1800 0.1612 0.1558 -0.0084 0.0355  -0.0186 84  THR A N   
750  C CA  . THR A 65  ? 0.1800 0.1539 0.1601 -0.0147 0.0392  -0.0163 84  THR A CA  
751  C C   . THR A 65  ? 0.1957 0.1714 0.1731 -0.0033 0.0438  -0.0207 84  THR A C   
752  O O   . THR A 65  ? 0.2112 0.1949 0.1712 0.0011  0.0419  -0.0175 84  THR A O   
753  C CB  . THR A 65  ? 0.1912 0.1695 0.1742 -0.0109 0.0348  -0.0046 84  THR A CB  
754  O OG1 . THR A 65  ? 0.1966 0.1701 0.1765 -0.0286 0.0200  -0.0152 84  THR A OG1 
755  C CG2 . THR A 65  ? 0.1693 0.1810 0.1750 -0.0025 0.0233  -0.0182 84  THR A CG2 
763  N N   . ARG A 66  ? 0.2088 0.1835 0.1861 0.0128  0.0638  -0.0218 85  ARG A N   
764  C CA  . ARG A 66  ? 0.2384 0.1901 0.1951 0.0073  0.0763  -0.0291 85  ARG A CA  
765  C C   . ARG A 66  ? 0.2414 0.1968 0.1885 0.0004  0.0714  -0.0396 85  ARG A C   
766  O O   . ARG A 66  ? 0.2943 0.2268 0.1907 -0.0092 0.0656  -0.0452 85  ARG A O   
767  C CB  . ARG A 66  ? 0.2575 0.2204 0.2141 0.0351  0.0679  -0.0155 85  ARG A CB  
768  C CG  . ARG A 66  ? 0.2840 0.2443 0.2550 0.0507  0.0862  -0.0152 85  ARG A CG  
769  C CD  . ARG A 66  ? 0.3033 0.2631 0.2819 0.0607  0.1018  -0.0013 85  ARG A CD  
770  N NE  . ARG A 66  ? 0.3469 0.2969 0.3108 0.0684  0.1086  0.0022  85  ARG A NE  
771  C CZ  . ARG A 66  ? 0.4151 0.3108 0.3468 0.0679  0.1096  0.0107  85  ARG A CZ  
772  N NH1 . ARG A 66  ? 0.4548 0.3199 0.3641 0.0727  0.0990  0.0109  85  ARG A NH1 
773  N NH2 . ARG A 66  ? 0.4290 0.3248 0.3479 0.0586  0.1205  0.0243  85  ARG A NH2 
787  N N   . THR A 67  ? 0.1991 0.1835 0.1698 -0.0026 0.0711  -0.0355 86  THR A N   
788  C CA  . THR A 67  ? 0.1965 0.1935 0.1705 -0.0224 0.0875  -0.0406 86  THR A CA  
789  C C   . THR A 67  ? 0.2022 0.2038 0.1734 -0.0223 0.0713  -0.0481 86  THR A C   
790  O O   . THR A 67  ? 0.2379 0.2272 0.1852 -0.0184 0.0469  -0.0426 86  THR A O   
791  C CB  . THR A 67  ? 0.2263 0.1885 0.1715 -0.0432 0.0864  -0.0358 86  THR A CB  
792  O OG1 . THR A 67  ? 0.2431 0.1680 0.1653 -0.0355 0.0680  -0.0287 86  THR A OG1 
793  C CG2 . THR A 67  ? 0.2291 0.1929 0.1960 -0.0395 0.0826  -0.0448 86  THR A CG2 
801  N N   . HIS A 68  ? 0.1952 0.1798 0.1573 -0.0382 0.0666  -0.0341 87  HIS A N   
802  C CA  . HIS A 68  ? 0.1931 0.1735 0.1644 -0.0449 0.0445  -0.0366 87  HIS A CA  
803  C C   . HIS A 68  ? 0.2134 0.1819 0.1733 -0.0471 0.0397  -0.0358 87  HIS A C   
804  O O   . HIS A 68  ? 0.2272 0.1848 0.1799 -0.0489 0.0387  -0.0303 87  HIS A O   
805  C CB  . HIS A 68  ? 0.1774 0.1877 0.1623 -0.0271 0.0459  -0.0406 87  HIS A CB  
806  C CG  . HIS A 68  ? 0.1812 0.1852 0.1583 -0.0296 0.0368  -0.0178 87  HIS A CG  
807  N ND1 . HIS A 68  ? 0.2102 0.1806 0.1593 -0.0434 0.0301  -0.0137 87  HIS A ND1 
808  C CD2 . HIS A 68  ? 0.2019 0.1948 0.1586 -0.0213 0.0170  0.0018  87  HIS A CD2 
809  C CE1 . HIS A 68  ? 0.2215 0.1817 0.1588 -0.0324 0.0346  -0.0179 87  HIS A CE1 
810  N NE2 . HIS A 68  ? 0.2325 0.1819 0.1604 -0.0375 0.0231  -0.0020 87  HIS A NE2 
818  N N   . GLY A 69  ? 0.2039 0.1928 0.1741 -0.0215 0.0596  -0.0345 88  GLY A N   
819  C CA  . GLY A 69  ? 0.2054 0.1883 0.1807 -0.0378 0.0698  -0.0313 88  GLY A CA  
820  C C   . GLY A 69  ? 0.2250 0.2020 0.1845 -0.0122 0.0541  -0.0061 88  GLY A C   
821  O O   . GLY A 69  ? 0.2739 0.2582 0.2208 0.0312  0.0650  0.0172  88  GLY A O   
825  N N   . THR A 70  ? 0.1806 0.1714 0.1738 -0.0138 0.0445  -0.0145 89  THR A N   
826  C CA  . THR A 70  ? 0.1608 0.1545 0.1755 -0.0317 0.0295  -0.0078 89  THR A CA  
827  C C   . THR A 70  ? 0.1699 0.1503 0.1507 -0.0281 0.0218  -0.0003 89  THR A C   
828  O O   . THR A 70  ? 0.1778 0.1629 0.1458 -0.0152 0.0264  -0.0081 89  THR A O   
829  C CB  . THR A 70  ? 0.2080 0.1621 0.2027 -0.0264 0.0250  -0.0084 89  THR A CB  
830  O OG1 . THR A 70  ? 0.1984 0.1726 0.2095 -0.0185 0.0109  -0.0150 89  THR A OG1 
831  C CG2 . THR A 70  ? 0.2222 0.1650 0.2184 -0.0378 0.0516  -0.0105 89  THR A CG2 
839  N N   . THR A 71  ? 0.1673 0.1395 0.1359 -0.0154 0.0271  -0.0129 90  THR A N   
840  C CA  . THR A 71  ? 0.1629 0.1421 0.1375 -0.0307 0.0281  -0.0163 90  THR A CA  
841  C C   . THR A 71  ? 0.1823 0.1457 0.1448 -0.0444 0.0306  -0.0078 90  THR A C   
842  O O   . THR A 71  ? 0.1986 0.1405 0.1410 -0.0440 0.0241  0.0013  90  THR A O   
843  C CB  . THR A 71  ? 0.1662 0.1407 0.1521 -0.0076 0.0211  -0.0079 90  THR A CB  
844  O OG1 . THR A 71  ? 0.1576 0.1278 0.1698 -0.0074 0.0240  -0.0011 90  THR A OG1 
845  C CG2 . THR A 71  ? 0.1572 0.1514 0.1658 0.0048  0.0063  -0.0072 90  THR A CG2 
853  N N   . GLU A 72  ? 0.1638 0.1431 0.1469 -0.0246 0.0233  -0.0233 91  GLU A N   
854  C CA  . GLU A 72  ? 0.1462 0.1539 0.1493 -0.0171 0.0225  -0.0174 91  GLU A CA  
855  C C   . GLU A 72  ? 0.1598 0.1544 0.1435 -0.0176 0.0270  -0.0260 91  GLU A C   
856  O O   . GLU A 72  ? 0.1805 0.1507 0.1426 -0.0071 0.0232  -0.0165 91  GLU A O   
857  C CB  . GLU A 72  ? 0.1606 0.1735 0.1662 -0.0167 0.0142  -0.0078 91  GLU A CB  
858  C CG  . GLU A 72  ? 0.1814 0.1857 0.1758 -0.0239 0.0320  -0.0038 91  GLU A CG  
859  C CD  . GLU A 72  ? 0.1522 0.1660 0.1637 -0.0222 0.0282  -0.0161 91  GLU A CD  
860  O OE1 . GLU A 72  ? 0.1605 0.1558 0.1641 -0.0165 0.0169  -0.0148 91  GLU A OE1 
861  O OE2 . GLU A 72  ? 0.1635 0.1692 0.1625 -0.0085 0.0254  -0.0019 91  GLU A OE2 
868  N N   . ALA A 73  ? 0.1739 0.1674 0.1526 -0.0179 0.0354  -0.0105 92  ALA A N   
869  C CA  . ALA A 73  ? 0.1581 0.1707 0.1527 -0.0141 0.0307  -0.0082 92  ALA A CA  
870  C C   . ALA A 73  ? 0.1513 0.1569 0.1485 -0.0115 0.0234  -0.0098 92  ALA A C   
871  O O   . ALA A 73  ? 0.1657 0.1643 0.1554 -0.0213 0.0197  -0.0020 92  ALA A O   
872  C CB  . ALA A 73  ? 0.1849 0.1624 0.1692 -0.0283 0.0276  -0.0178 92  ALA A CB  
878  N N   . GLY A 74  ? 0.1541 0.1535 0.1465 -0.0011 0.0154  -0.0131 93  GLY A N   
879  C CA  . GLY A 74  ? 0.1697 0.1536 0.1467 -0.0109 0.0393  0.0044  93  GLY A CA  
880  C C   . GLY A 74  ? 0.1572 0.1499 0.1409 -0.0103 0.0257  0.0015  93  GLY A C   
881  O O   . GLY A 74  ? 0.1616 0.1530 0.1483 -0.0147 0.0211  0.0098  93  GLY A O   
885  N N   . ILE A 75  ? 0.1505 0.1523 0.1263 -0.0059 0.0336  -0.0032 94  ILE A N   
886  C CA  . ILE A 75  ? 0.1400 0.1578 0.1336 -0.0116 0.0302  -0.0064 94  ILE A CA  
887  C C   . ILE A 75  ? 0.1628 0.1497 0.1348 -0.0296 0.0190  -0.0010 94  ILE A C   
888  O O   . ILE A 75  ? 0.1731 0.1432 0.1427 -0.0193 0.0178  0.0102  94  ILE A O   
889  C CB  . ILE A 75  ? 0.1343 0.1555 0.1246 -0.0146 0.0155  0.0037  94  ILE A CB  
890  C CG1 . ILE A 75  ? 0.1492 0.1568 0.1249 -0.0242 0.0084  -0.0042 94  ILE A CG1 
891  C CG2 . ILE A 75  ? 0.1418 0.1694 0.1352 -0.0179 0.0269  0.0041  94  ILE A CG2 
892  C CD1 . ILE A 75  ? 0.1402 0.1732 0.1290 -0.0250 0.0145  -0.0179 94  ILE A CD1 
904  N N   . GLU A 76  ? 0.1584 0.1439 0.1337 -0.0221 0.0092  -0.0006 95  GLU A N   
905  C CA  . GLU A 76  ? 0.1620 0.1535 0.1349 -0.0101 0.0077  -0.0108 95  GLU A CA  
906  C C   . GLU A 76  ? 0.1533 0.1555 0.1262 -0.0006 0.0175  -0.0007 95  GLU A C   
907  O O   . GLU A 76  ? 0.1606 0.1645 0.1447 0.0010  0.0120  0.0031  95  GLU A O   
908  C CB  . GLU A 76  ? 0.1709 0.1729 0.1486 -0.0292 0.0166  -0.0062 95  GLU A CB  
909  C CG  . GLU A 76  ? 0.1501 0.1714 0.1333 -0.0336 0.0145  -0.0020 95  GLU A CG  
910  C CD  . GLU A 76  ? 0.1739 0.2022 0.1423 -0.0187 -0.0147 0.0081  95  GLU A CD  
911  O OE1 . GLU A 76  ? 0.1862 0.2186 0.1465 -0.0238 0.0078  0.0155  95  GLU A OE1 
912  O OE2 . GLU A 76  ? 0.2012 0.2012 0.1552 -0.0023 -0.0318 0.0033  95  GLU A OE2 
919  N N   . ALA A 77  ? 0.1547 0.1641 0.1191 -0.0239 0.0245  -0.0006 96  ALA A N   
920  C CA  . ALA A 77  ? 0.1450 0.1731 0.1286 -0.0343 0.0318  0.0103  96  ALA A CA  
921  C C   . ALA A 77  ? 0.1664 0.1690 0.1397 -0.0288 0.0192  0.0145  96  ALA A C   
922  O O   . ALA A 77  ? 0.1616 0.1584 0.1625 -0.0232 0.0159  0.0071  96  ALA A O   
923  C CB  . ALA A 77  ? 0.1618 0.1840 0.1469 -0.0261 0.0147  0.0040  96  ALA A CB  
929  N N   . GLU A 78  ? 0.1512 0.1593 0.1301 -0.0263 0.0334  0.0136  97  GLU A N   
930  C CA  . GLU A 78  ? 0.1405 0.1624 0.1479 -0.0222 0.0211  0.0060  97  GLU A CA  
931  C C   . GLU A 78  ? 0.1304 0.1556 0.1487 -0.0189 0.0242  0.0036  97  GLU A C   
932  O O   . GLU A 78  ? 0.1547 0.1634 0.1623 -0.0250 0.0130  0.0135  97  GLU A O   
933  C CB  . GLU A 78  ? 0.1386 0.1657 0.1586 -0.0159 0.0306  0.0002  97  GLU A CB  
934  C CG  . GLU A 78  ? 0.1466 0.1479 0.1569 -0.0273 0.0206  0.0102  97  GLU A CG  
935  C CD  . GLU A 78  ? 0.1622 0.1562 0.1660 -0.0158 0.0190  0.0246  97  GLU A CD  
936  O OE1 . GLU A 78  ? 0.1457 0.1676 0.1567 -0.0107 0.0332  0.0127  97  GLU A OE1 
937  O OE2 . GLU A 78  ? 0.1680 0.1706 0.2033 -0.0157 0.0253  0.0383  97  GLU A OE2 
944  N N   . ALA A 79  ? 0.1383 0.1479 0.1473 -0.0062 0.0286  -0.0015 98  ALA A N   
945  C CA  . ALA A 79  ? 0.1453 0.1515 0.1418 -0.0111 0.0231  -0.0112 98  ALA A CA  
946  C C   . ALA A 79  ? 0.1386 0.1363 0.1437 -0.0040 0.0207  -0.0017 98  ALA A C   
947  O O   . ALA A 79  ? 0.1723 0.1439 0.1561 -0.0207 0.0137  -0.0020 98  ALA A O   
948  C CB  . ALA A 79  ? 0.1651 0.1688 0.1459 0.0032  0.0014  0.0050  98  ALA A CB  
954  N N   . ARG A 80  ? 0.1638 0.1422 0.1456 -0.0159 0.0310  0.0054  99  ARG A N   
955  C CA  . ARG A 80  ? 0.1813 0.1702 0.1447 -0.0138 0.0206  0.0058  99  ARG A CA  
956  C C   . ARG A 80  ? 0.1777 0.1653 0.1586 -0.0098 0.0235  -0.0034 99  ARG A C   
957  O O   . ARG A 80  ? 0.2041 0.1725 0.1725 -0.0125 0.0231  0.0096  99  ARG A O   
958  C CB  . ARG A 80  ? 0.2156 0.2023 0.1434 -0.0325 0.0165  0.0253  99  ARG A CB  
959  C CG  . ARG A 80  ? 0.2290 0.2548 0.1590 -0.0532 0.0202  0.0118  99  ARG A CG  
960  C CD  . ARG A 80  ? 0.2502 0.2970 0.1778 -0.0875 0.0290  -0.0107 99  ARG A CD  
961  N NE  . ARG A 80  ? 0.3110 0.3487 0.2019 -0.1147 0.0081  -0.0191 99  ARG A NE  
962  C CZ  . ARG A 80  ? 0.4061 0.4268 0.2393 -0.1509 0.0206  -0.0168 99  ARG A CZ  
963  N NH1 . ARG A 80  ? 0.4696 0.4537 0.2566 -0.1412 0.0109  -0.0219 99  ARG A NH1 
964  N NH2 . ARG A 80  ? 0.4270 0.4662 0.2652 -0.1665 0.0011  -0.0227 99  ARG A NH2 
978  N N   . GLN A 81  ? 0.1681 0.1642 0.1626 -0.0278 0.0310  -0.0020 100 GLN A N   
979  C CA  . GLN A 81  ? 0.1754 0.1747 0.1746 -0.0333 0.0222  0.0002  100 GLN A CA  
980  C C   . GLN A 81  ? 0.1802 0.1636 0.1789 -0.0148 0.0187  0.0096  100 GLN A C   
981  O O   . GLN A 81  ? 0.1884 0.1608 0.1977 -0.0039 -0.0053 0.0073  100 GLN A O   
982  C CB  . GLN A 81  ? 0.2008 0.2330 0.2035 -0.0401 0.0216  -0.0250 100 GLN A CB  
983  C CG  . GLN A 81  ? 0.2492 0.2682 0.1870 -0.0007 0.0380  -0.0138 100 GLN A CG  
984  C CD  . GLN A 81  ? 0.2666 0.2858 0.1668 0.0373  0.0541  -0.0128 100 GLN A CD  
985  O OE1 . GLN A 81  ? 0.3084 0.3202 0.1830 0.0288  0.0172  0.0077  100 GLN A OE1 
986  N NE2 . GLN A 81  ? 0.2444 0.2577 0.1584 0.0334  0.0278  0.0079  100 GLN A NE2 
995  N N   . LEU A 82  ? 0.1778 0.1505 0.1626 -0.0306 0.0265  0.0116  101 LEU A N   
996  C CA  . LEU A 82  ? 0.1741 0.1572 0.1602 -0.0126 0.0272  0.0056  101 LEU A CA  
997  C C   . LEU A 82  ? 0.1805 0.1468 0.1636 -0.0032 0.0169  0.0029  101 LEU A C   
998  O O   . LEU A 82  ? 0.1898 0.1441 0.1647 -0.0001 0.0125  0.0180  101 LEU A O   
999  C CB  . LEU A 82  ? 0.1793 0.1427 0.1635 -0.0129 0.0185  0.0251  101 LEU A CB  
1000 C CG  . LEU A 82  ? 0.1790 0.1491 0.1627 -0.0185 0.0050  0.0290  101 LEU A CG  
1001 C CD1 . LEU A 82  ? 0.2242 0.1517 0.1620 -0.0205 0.0175  0.0299  101 LEU A CD1 
1002 C CD2 . LEU A 82  ? 0.1927 0.1759 0.1969 -0.0403 0.0034  0.0082  101 LEU A CD2 
1014 N N   . LYS A 83  ? 0.1735 0.1381 0.1819 -0.0053 0.0240  0.0042  102 LYS A N   
1015 C CA  . LYS A 83  ? 0.1702 0.1506 0.2069 -0.0090 0.0099  -0.0022 102 LYS A CA  
1016 C C   . LYS A 83  ? 0.1697 0.1754 0.2051 -0.0171 0.0137  -0.0021 102 LYS A C   
1017 O O   . LYS A 83  ? 0.1970 0.1791 0.2185 -0.0082 0.0192  -0.0027 102 LYS A O   
1018 C CB  . LYS A 83  ? 0.1860 0.1815 0.2469 0.0069  0.0203  -0.0050 102 LYS A CB  
1019 C CG  . LYS A 83  ? 0.2244 0.1848 0.2617 -0.0120 0.0160  -0.0094 102 LYS A CG  
1020 C CD  . LYS A 83  ? 0.3078 0.2263 0.2717 -0.0203 0.0032  -0.0171 102 LYS A CD  
1021 C CE  . LYS A 83  ? 0.3271 0.2226 0.2643 -0.0388 0.0155  -0.0149 102 LYS A CE  
1022 N NZ  . LYS A 83  ? 0.2681 0.2234 0.2473 -0.0464 0.0409  -0.0009 102 LYS A NZ  
1036 N N   . ASN A 84  ? 0.1700 0.1870 0.1882 -0.0139 0.0187  0.0085  103 ASN A N   
1037 C CA  . ASN A 84  ? 0.1937 0.2032 0.1844 -0.0059 0.0236  0.0194  103 ASN A CA  
1038 C C   . ASN A 84  ? 0.1824 0.1835 0.1790 -0.0214 0.0053  0.0336  103 ASN A C   
1039 O O   . ASN A 84  ? 0.2038 0.2070 0.1930 -0.0300 -0.0101 0.0409  103 ASN A O   
1040 C CB  . ASN A 84  ? 0.2516 0.2522 0.1918 0.0117  0.0137  0.0213  103 ASN A CB  
1041 C CG  . ASN A 84  ? 0.3255 0.3118 0.2327 0.0525  0.0100  0.0396  103 ASN A CG  
1042 O OD1 . ASN A 84  ? 0.3579 0.3475 0.2497 0.0706  -0.0030 0.0459  103 ASN A OD1 
1043 N ND2 . ASN A 84  ? 0.3561 0.3305 0.2502 0.0611  0.0128  0.0486  103 ASN A ND2 
1050 N N   . LEU A 85  ? 0.1410 0.1708 0.1675 -0.0133 0.0095  0.0225  104 LEU A N   
1051 C CA  . LEU A 85  ? 0.1494 0.1565 0.1668 -0.0057 0.0120  0.0286  104 LEU A CA  
1052 C C   . LEU A 85  ? 0.1558 0.1562 0.1724 -0.0035 0.0257  0.0285  104 LEU A C   
1053 O O   . LEU A 85  ? 0.1949 0.1727 0.1969 -0.0032 0.0493  0.0354  104 LEU A O   
1054 C CB  . LEU A 85  ? 0.1509 0.1801 0.1612 -0.0273 0.0246  0.0279  104 LEU A CB  
1055 C CG  . LEU A 85  ? 0.1615 0.1852 0.1746 -0.0122 0.0258  0.0182  104 LEU A CG  
1056 C CD1 . LEU A 85  ? 0.1558 0.1888 0.1855 0.0016  0.0233  0.0246  104 LEU A CD1 
1057 C CD2 . LEU A 85  ? 0.1835 0.1882 0.1811 0.0086  0.0321  0.0155  104 LEU A CD2 
1069 N N   . ASN A 86  ? 0.1604 0.1484 0.1599 -0.0025 0.0338  0.0221  105 ASN A N   
1070 C CA  . ASN A 86  ? 0.1509 0.1623 0.1739 -0.0170 0.0399  0.0158  105 ASN A CA  
1071 C C   . ASN A 86  ? 0.1475 0.1657 0.1738 -0.0107 0.0317  0.0248  105 ASN A C   
1072 O O   . ASN A 86  ? 0.1609 0.1675 0.1816 -0.0065 0.0460  0.0159  105 ASN A O   
1073 C CB  . ASN A 86  ? 0.1672 0.1576 0.1850 -0.0272 0.0499  0.0160  105 ASN A CB  
1074 C CG  . ASN A 86  ? 0.1806 0.1615 0.1899 -0.0094 0.0397  0.0199  105 ASN A CG  
1075 O OD1 . ASN A 86  ? 0.1598 0.1864 0.1997 0.0021  0.0472  0.0109  105 ASN A OD1 
1076 N ND2 . ASN A 86  ? 0.1906 0.1432 0.1698 0.0146  0.0262  0.0273  105 ASN A ND2 
1083 N N   . PRO A 87  ? 0.1376 0.1887 0.1904 0.0020  0.0109  0.0471  106 PRO A N   
1084 C CA  . PRO A 87  ? 0.1637 0.1937 0.2074 -0.0054 0.0181  0.0479  106 PRO A CA  
1085 C C   . PRO A 87  ? 0.1716 0.1981 0.2205 -0.0088 0.0361  0.0437  106 PRO A C   
1086 O O   . PRO A 87  ? 0.1871 0.2245 0.2527 -0.0244 0.0440  0.0212  106 PRO A O   
1087 C CB  . PRO A 87  ? 0.1944 0.2091 0.2229 -0.0005 0.0215  0.0530  106 PRO A CB  
1088 C CG  . PRO A 87  ? 0.2346 0.2462 0.2445 -0.0254 -0.0096 0.0642  106 PRO A CG  
1089 C CD  . PRO A 87  ? 0.1557 0.2163 0.2100 0.0023  0.0052  0.0608  106 PRO A CD  
1097 N N   . LYS A 88  ? 0.1778 0.1844 0.2063 0.0198  0.0585  0.0485  107 LYS A N   
1098 C CA  . LYS A 88  ? 0.1778 0.1874 0.2086 0.0264  0.0567  0.0448  107 LYS A CA  
1099 C C   . LYS A 88  ? 0.2028 0.1878 0.1936 0.0350  0.0663  0.0444  107 LYS A C   
1100 O O   . LYS A 88  ? 0.2086 0.1934 0.1997 0.0348  0.0603  0.0426  107 LYS A O   
1101 C CB  . LYS A 88  ? 0.2448 0.2144 0.2271 0.0376  0.0464  0.0479  107 LYS A CB  
1102 C CG  . LYS A 88  ? 0.3379 0.2312 0.2560 0.0353  0.0403  0.0605  107 LYS A CG  
1103 C CD  . LYS A 88  ? 0.3937 0.2553 0.2779 0.0519  0.0332  0.0719  107 LYS A CD  
1104 C CE  . LYS A 88  ? 0.4506 0.2813 0.2949 0.0528  0.0364  0.0809  107 LYS A CE  
1105 N NZ  . LYS A 88  ? 0.4948 0.3102 0.3098 0.0270  0.0545  0.0695  107 LYS A NZ  
1119 N N   . MET A 89  ? 0.2051 0.1750 0.1797 0.0211  0.0754  0.0481  108 MET A N   
1120 C CA  . MET A 89  ? 0.1904 0.1791 0.1859 0.0220  0.0514  0.0358  108 MET A CA  
1121 C C   . MET A 89  ? 0.1971 0.1682 0.1759 -0.0173 0.0331  0.0165  108 MET A C   
1122 O O   . MET A 89  ? 0.2695 0.1832 0.1804 -0.0383 0.0204  0.0094  108 MET A O   
1123 C CB  . MET A 89  ? 0.2057 0.2222 0.2014 0.0644  0.0421  0.0291  108 MET A CB  
1124 C CG  . MET A 89  ? 0.2621 0.2115 0.1987 0.0996  0.0383  0.0261  108 MET A CG  
1125 S SD  . MET A 89  ? 0.2213 0.2584 0.2352 -0.0113 0.0229  -0.0021 108 MET A SD  
1126 C CE  . MET A 89  ? 0.2561 0.2666 0.2221 -0.0070 -0.0019 0.0127  108 MET A CE  
1136 N N   . LYS A 90  ? 0.1312 0.1469 0.1556 -0.0040 0.0215  0.0114  109 LYS A N   
1137 C CA  . LYS A 90  ? 0.1229 0.1428 0.1473 -0.0013 0.0169  0.0159  109 LYS A CA  
1138 C C   . LYS A 90  ? 0.1232 0.1415 0.1426 -0.0031 0.0090  0.0123  109 LYS A C   
1139 O O   . LYS A 90  ? 0.1382 0.1399 0.1566 0.0169  0.0028  -0.0016 109 LYS A O   
1140 C CB  . LYS A 90  ? 0.1284 0.1478 0.1541 -0.0114 0.0198  0.0110  109 LYS A CB  
1141 C CG  . LYS A 90  ? 0.1415 0.1490 0.1710 -0.0144 0.0058  0.0013  109 LYS A CG  
1142 C CD  . LYS A 90  ? 0.1580 0.1389 0.1776 -0.0121 0.0104  0.0074  109 LYS A CD  
1143 C CE  . LYS A 90  ? 0.1533 0.1732 0.1988 0.0090  -0.0049 0.0081  109 LYS A CE  
1144 N NZ  . LYS A 90  ? 0.1693 0.1934 0.2052 0.0004  -0.0087 0.0214  109 LYS A NZ  
1158 N N   . VAL A 91  ? 0.1083 0.1368 0.1403 -0.0090 -0.0069 0.0179  110 VAL A N   
1159 C CA  . VAL A 91  ? 0.1235 0.1338 0.1296 0.0133  0.0147  0.0173  110 VAL A CA  
1160 C C   . VAL A 91  ? 0.1240 0.1452 0.1343 0.0015  0.0178  0.0111  110 VAL A C   
1161 O O   . VAL A 91  ? 0.1348 0.1435 0.1304 -0.0013 0.0013  0.0096  110 VAL A O   
1162 C CB  . VAL A 91  ? 0.1374 0.1423 0.1340 0.0009  0.0215  0.0128  110 VAL A CB  
1163 C CG1 . VAL A 91  ? 0.1528 0.1639 0.1386 0.0016  0.0010  0.0022  110 VAL A CG1 
1164 C CG2 . VAL A 91  ? 0.1578 0.1488 0.1424 0.0008  0.0192  0.0255  110 VAL A CG2 
1174 N N   . ILE A 92  ? 0.1188 0.1373 0.1308 -0.0014 0.0173  0.0066  111 ILE A N   
1175 C CA  . ILE A 92  ? 0.1241 0.1399 0.1320 -0.0040 0.0190  0.0075  111 ILE A CA  
1176 C C   . ILE A 92  ? 0.1008 0.1405 0.1350 -0.0013 0.0050  0.0104  111 ILE A C   
1177 O O   . ILE A 92  ? 0.1090 0.1502 0.1462 0.0003  -0.0018 0.0020  111 ILE A O   
1178 C CB  . ILE A 92  ? 0.1230 0.1460 0.1335 -0.0078 0.0074  0.0055  111 ILE A CB  
1179 C CG1 . ILE A 92  ? 0.1180 0.1550 0.1430 0.0029  0.0205  0.0122  111 ILE A CG1 
1180 C CG2 . ILE A 92  ? 0.1185 0.1438 0.1359 -0.0106 0.0197  0.0044  111 ILE A CG2 
1181 C CD1 . ILE A 92  ? 0.1362 0.1738 0.1602 0.0006  0.0149  0.0202  111 ILE A CD1 
1193 N N   . PHE A 93  ? 0.1098 0.1404 0.1446 -0.0120 0.0018  -0.0058 112 PHE A N   
1194 C CA  . PHE A 93  ? 0.1150 0.1306 0.1485 -0.0110 0.0251  -0.0146 112 PHE A CA  
1195 C C   . PHE A 93  ? 0.0855 0.1325 0.1323 -0.0230 0.0190  -0.0009 112 PHE A C   
1196 O O   . PHE A 93  ? 0.1243 0.1412 0.1379 -0.0009 0.0246  0.0014  112 PHE A O   
1197 C CB  . PHE A 93  ? 0.1354 0.1270 0.1488 -0.0211 0.0229  0.0014  112 PHE A CB  
1198 C CG  . PHE A 93  ? 0.1381 0.1258 0.1569 -0.0184 -0.0004 -0.0038 112 PHE A CG  
1199 C CD1 . PHE A 93  ? 0.1637 0.1358 0.1625 -0.0208 0.0249  -0.0192 112 PHE A CD1 
1200 C CD2 . PHE A 93  ? 0.1781 0.1379 0.1567 -0.0149 0.0207  0.0037  112 PHE A CD2 
1201 C CE1 . PHE A 93  ? 0.1623 0.1320 0.1705 -0.0108 0.0322  -0.0258 112 PHE A CE1 
1202 C CE2 . PHE A 93  ? 0.1827 0.1466 0.1587 -0.0202 0.0126  -0.0165 112 PHE A CE2 
1203 C CZ  . PHE A 93  ? 0.1718 0.1181 0.1573 -0.0065 0.0228  -0.0247 112 PHE A CZ  
1213 N N   . TYR A 94  ? 0.1220 0.1693 0.1307 0.0034  0.0207  0.0143  113 TYR A N   
1214 C CA  . TYR A 94  ? 0.1181 0.1632 0.1361 0.0108  0.0187  0.0140  113 TYR A CA  
1215 C C   . TYR A 94  ? 0.1423 0.1567 0.1416 -0.0015 0.0341  0.0164  113 TYR A C   
1216 O O   . TYR A 94  ? 0.1551 0.1664 0.1416 -0.0152 0.0322  0.0052  113 TYR A O   
1217 C CB  . TYR A 94  ? 0.1352 0.1666 0.1379 0.0196  0.0101  0.0278  113 TYR A CB  
1218 C CG  . TYR A 94  ? 0.1284 0.1678 0.1465 0.0063  0.0349  0.0415  113 TYR A CG  
1219 C CD1 . TYR A 94  ? 0.1379 0.1644 0.1530 0.0255  0.0208  0.0290  113 TYR A CD1 
1220 C CD2 . TYR A 94  ? 0.1189 0.1609 0.1706 -0.0081 0.0210  0.0378  113 TYR A CD2 
1221 C CE1 . TYR A 94  ? 0.1348 0.1484 0.1638 0.0352  0.0389  0.0250  113 TYR A CE1 
1222 C CE2 . TYR A 94  ? 0.1235 0.1550 0.1606 -0.0100 0.0138  0.0350  113 TYR A CE2 
1223 C CZ  . TYR A 94  ? 0.1301 0.1434 0.1551 0.0065  0.0259  0.0345  113 TYR A CZ  
1224 O OH  . TYR A 94  ? 0.1581 0.1400 0.1559 0.0052  0.0105  0.0212  113 TYR A OH  
1234 N N   . TRP A 95  ? 0.1374 0.1337 0.1434 0.0008  0.0364  0.0152  114 TRP A N   
1235 C CA  . TRP A 95  ? 0.1232 0.1384 0.1488 0.0007  0.0343  0.0098  114 TRP A CA  
1236 C C   . TRP A 95  ? 0.1295 0.1342 0.1685 0.0163  0.0380  0.0109  114 TRP A C   
1237 O O   . TRP A 95  ? 0.1503 0.1326 0.1802 0.0205  0.0575  0.0136  114 TRP A O   
1238 C CB  . TRP A 95  ? 0.1317 0.1585 0.1590 0.0114  0.0239  0.0028  114 TRP A CB  
1239 C CG  . TRP A 95  ? 0.1295 0.1550 0.1501 -0.0015 0.0291  0.0082  114 TRP A CG  
1240 C CD1 . TRP A 95  ? 0.1445 0.1488 0.1538 -0.0039 0.0311  0.0172  114 TRP A CD1 
1241 C CD2 . TRP A 95  ? 0.1310 0.1570 0.1477 0.0074  0.0464  0.0006  114 TRP A CD2 
1242 N NE1 . TRP A 95  ? 0.1518 0.1501 0.1486 0.0078  0.0150  -0.0117 114 TRP A NE1 
1243 C CE2 . TRP A 95  ? 0.1646 0.1419 0.1402 0.0275  0.0192  -0.0105 114 TRP A CE2 
1244 C CE3 . TRP A 95  ? 0.1426 0.1613 0.1440 0.0171  0.0291  0.0039  114 TRP A CE3 
1245 C CZ2 . TRP A 95  ? 0.1777 0.1428 0.1405 0.0224  0.0161  -0.0150 114 TRP A CZ2 
1246 C CZ3 . TRP A 95  ? 0.1756 0.1681 0.1477 0.0183  0.0312  -0.0032 114 TRP A CZ3 
1247 C CH2 . TRP A 95  ? 0.1766 0.1578 0.1554 0.0184  0.0257  -0.0068 114 TRP A CH2 
1258 N N   . ASN A 96  ? 0.1319 0.1387 0.1534 0.0255  0.0474  0.0240  115 ASN A N   
1259 C CA  . ASN A 96  ? 0.1354 0.1415 0.1430 0.0125  0.0323  0.0182  115 ASN A CA  
1260 C C   . ASN A 96  ? 0.1330 0.1438 0.1368 0.0198  0.0370  0.0112  115 ASN A C   
1261 O O   . ASN A 96  ? 0.1426 0.1564 0.1290 -0.0034 0.0217  0.0097  115 ASN A O   
1262 C CB  . ASN A 96  ? 0.1385 0.1305 0.1419 0.0102  0.0418  0.0212  115 ASN A CB  
1263 C CG  . ASN A 96  ? 0.1385 0.1377 0.1653 0.0183  0.0346  0.0176  115 ASN A CG  
1264 O OD1 . ASN A 96  ? 0.1400 0.1463 0.1695 0.0269  0.0271  0.0176  115 ASN A OD1 
1265 N ND2 . ASN A 96  ? 0.1660 0.1329 0.1702 -0.0050 0.0419  0.0058  115 ASN A ND2 
1272 N N   . THR A 97  ? 0.1360 0.1428 0.1461 0.0184  0.0212  0.0096  116 THR A N   
1273 C CA  . THR A 97  ? 0.1209 0.1395 0.1468 0.0074  0.0288  0.0074  116 THR A CA  
1274 C C   . THR A 97  ? 0.1201 0.1476 0.1592 0.0181  0.0436  0.0003  116 THR A C   
1275 O O   . THR A 97  ? 0.1383 0.1404 0.1818 0.0105  0.0393  -0.0019 116 THR A O   
1276 C CB  . THR A 97  ? 0.1174 0.1500 0.1452 -0.0033 0.0261  0.0167  116 THR A CB  
1277 O OG1 . THR A 97  ? 0.1518 0.1447 0.1468 -0.0034 0.0426  0.0139  116 THR A OG1 
1278 C CG2 . THR A 97  ? 0.1452 0.1515 0.1766 -0.0058 0.0412  0.0183  116 THR A CG2 
1286 N N   . PHE A 98  ? 0.1329 0.1481 0.1463 0.0321  0.0520  0.0100  117 PHE A N   
1287 C CA  . PHE A 98  ? 0.1322 0.1427 0.1579 0.0217  0.0310  0.0191  117 PHE A CA  
1288 C C   . PHE A 98  ? 0.1467 0.1473 0.1558 -0.0032 0.0376  0.0133  117 PHE A C   
1289 O O   . PHE A 98  ? 0.1668 0.1609 0.1596 -0.0046 0.0385  0.0046  117 PHE A O   
1290 C CB  . PHE A 98  ? 0.1645 0.1564 0.1565 0.0095  0.0149  0.0166  117 PHE A CB  
1291 C CG  . PHE A 98  ? 0.1768 0.1459 0.1447 -0.0114 0.0306  0.0087  117 PHE A CG  
1292 C CD1 . PHE A 98  ? 0.2011 0.1488 0.1522 -0.0113 0.0253  0.0294  117 PHE A CD1 
1293 C CD2 . PHE A 98  ? 0.2100 0.1530 0.1557 0.0005  0.0251  0.0153  117 PHE A CD2 
1294 C CE1 . PHE A 98  ? 0.1888 0.1593 0.1600 -0.0043 0.0348  0.0244  117 PHE A CE1 
1295 C CE2 . PHE A 98  ? 0.2199 0.1510 0.1603 0.0008  0.0322  0.0249  117 PHE A CE2 
1296 C CZ  . PHE A 98  ? 0.2090 0.1424 0.1664 -0.0046 0.0354  0.0221  117 PHE A CZ  
1306 N N   . LEU A 99  ? 0.1722 0.1478 0.1650 0.0200  0.0537  0.0173  118 LEU A N   
1307 C CA  . LEU A 99  ? 0.1635 0.1539 0.1553 0.0220  0.0539  0.0123  118 LEU A CA  
1308 C C   . LEU A 99  ? 0.1765 0.1488 0.1595 0.0321  0.0324  0.0075  118 LEU A C   
1309 O O   . LEU A 99  ? 0.1713 0.1507 0.1664 0.0187  0.0338  0.0098  118 LEU A O   
1310 C CB  . LEU A 99  ? 0.1813 0.1591 0.1464 0.0061  0.0267  0.0184  118 LEU A CB  
1311 C CG  . LEU A 99  ? 0.1933 0.1831 0.1446 0.0030  0.0198  -0.0033 118 LEU A CG  
1312 C CD1 . LEU A 99  ? 0.2209 0.2071 0.1566 -0.0059 0.0149  0.0067  118 LEU A CD1 
1313 C CD2 . LEU A 99  ? 0.2083 0.1932 0.1463 -0.0013 -0.0068 -0.0048 118 LEU A CD2 
1325 N N   . ASP A 100 ? 0.1950 0.1448 0.1610 0.0311  0.0296  0.0029  119 ASP A N   
1326 C CA  . ASP A 100 ? 0.1869 0.1490 0.1566 0.0066  0.0309  0.0052  119 ASP A CA  
1327 C C   . ASP A 100 ? 0.1652 0.1505 0.1701 0.0155  0.0277  0.0153  119 ASP A C   
1328 O O   . ASP A 100 ? 0.2046 0.1647 0.1875 0.0125  0.0404  -0.0046 119 ASP A O   
1329 C CB  . ASP A 100 ? 0.2017 0.1325 0.1630 -0.0016 0.0388  -0.0017 119 ASP A CB  
1330 C CG  . ASP A 100 ? 0.2340 0.1283 0.1585 0.0051  0.0420  0.0026  119 ASP A CG  
1331 O OD1 . ASP A 100 ? 0.2312 0.1429 0.1492 0.0069  0.0534  0.0083  119 ASP A OD1 
1332 O OD2 . ASP A 100 ? 0.2116 0.1327 0.1676 -0.0013 0.0261  -0.0053 119 ASP A OD2 
1337 N N   . TYR A 101 ? 0.1662 0.1437 0.1730 0.0249  0.0346  0.0092  120 TYR A N   
1338 C CA  . TYR A 101 ? 0.1678 0.1494 0.1756 0.0131  0.0239  0.0104  120 TYR A CA  
1339 C C   . TYR A 101 ? 0.1551 0.1611 0.1748 0.0147  0.0090  0.0039  120 TYR A C   
1340 O O   . TYR A 101 ? 0.1498 0.1618 0.1849 0.0197  0.0201  -0.0094 120 TYR A O   
1341 C CB  . TYR A 101 ? 0.1919 0.1649 0.1810 -0.0083 0.0210  -0.0036 120 TYR A CB  
1342 C CG  . TYR A 101 ? 0.1691 0.1759 0.1815 -0.0023 0.0091  -0.0063 120 TYR A CG  
1343 C CD1 . TYR A 101 ? 0.2016 0.2065 0.1885 0.0412  -0.0126 -0.0183 120 TYR A CD1 
1344 C CD2 . TYR A 101 ? 0.1686 0.2021 0.1881 0.0154  0.0052  -0.0015 120 TYR A CD2 
1345 C CE1 . TYR A 101 ? 0.2133 0.2222 0.1891 0.0528  -0.0129 -0.0252 120 TYR A CE1 
1346 C CE2 . TYR A 101 ? 0.1969 0.2168 0.1708 0.0092  0.0246  -0.0292 120 TYR A CE2 
1347 C CZ  . TYR A 101 ? 0.2073 0.2336 0.1666 0.0136  0.0114  -0.0256 120 TYR A CZ  
1348 O OH  . TYR A 101 ? 0.2439 0.2664 0.1860 -0.0024 -0.0133 -0.0363 120 TYR A OH  
1358 N N   . SER A 102 ? 0.1747 0.1627 0.1835 0.0194  0.0176  -0.0022 121 SER A N   
1359 C CA  . SER A 102 ? 0.1923 0.1750 0.1865 0.0413  0.0431  -0.0165 121 SER A CA  
1360 C C   . SER A 102 ? 0.2091 0.1727 0.1788 0.0225  0.0433  -0.0141 121 SER A C   
1361 O O   . SER A 102 ? 0.2614 0.1995 0.1899 -0.0130 0.0401  -0.0075 121 SER A O   
1362 C CB  . SER A 102 ? 0.2003 0.2075 0.2190 0.0571  0.0372  -0.0294 121 SER A CB  
1363 O OG  . SER A 102 ? 0.2158 0.2445 0.2421 0.0649  0.0236  -0.0277 121 SER A OG  
1369 N N   . MET A 103 ? 0.1628 0.1603 0.1778 0.0015  0.0348  -0.0128 122 MET A N   
1370 C CA  . MET A 103 ? 0.1645 0.1692 0.1811 -0.0009 0.0316  -0.0054 122 MET A CA  
1371 C C   . MET A 103 ? 0.1737 0.1529 0.1749 -0.0221 0.0379  -0.0108 122 MET A C   
1372 O O   . MET A 103 ? 0.1799 0.1558 0.1697 -0.0170 0.0293  -0.0210 122 MET A O   
1373 C CB  . MET A 103 ? 0.1995 0.1960 0.1951 -0.0168 0.0108  0.0015  122 MET A CB  
1374 C CG  . MET A 103 ? 0.2547 0.2017 0.2044 -0.0370 0.0105  0.0014  122 MET A CG  
1375 S SD  . MET A 103 ? 0.2475 0.1977 0.2001 -0.0295 0.0299  -0.0040 122 MET A SD  
1376 C CE  . MET A 103 ? 0.2942 0.2340 0.2255 -0.0045 -0.0010 0.0019  122 MET A CE  
1386 N N   . PHE A 104 ? 0.1610 0.1441 0.1783 -0.0340 0.0390  0.0036  123 PHE A N   
1387 C CA  . PHE A 104 ? 0.1588 0.1439 0.1710 -0.0120 0.0329  -0.0031 123 PHE A CA  
1388 C C   . PHE A 104 ? 0.1623 0.1473 0.1598 -0.0056 0.0333  0.0038  123 PHE A C   
1389 O O   . PHE A 104 ? 0.1888 0.1370 0.1564 -0.0187 0.0390  0.0146  123 PHE A O   
1390 C CB  . PHE A 104 ? 0.1622 0.1597 0.1522 0.0114  0.0270  0.0092  123 PHE A CB  
1391 C CG  . PHE A 104 ? 0.1467 0.1686 0.1342 0.0009  0.0276  0.0080  123 PHE A CG  
1392 C CD1 . PHE A 104 ? 0.1471 0.1757 0.1336 0.0063  0.0313  -0.0050 123 PHE A CD1 
1393 C CD2 . PHE A 104 ? 0.1644 0.1773 0.1316 0.0121  0.0274  0.0037  123 PHE A CD2 
1394 C CE1 . PHE A 104 ? 0.1608 0.1880 0.1250 0.0088  0.0470  -0.0036 123 PHE A CE1 
1395 C CE2 . PHE A 104 ? 0.1681 0.1847 0.1222 0.0050  0.0425  0.0052  123 PHE A CE2 
1396 C CZ  . PHE A 104 ? 0.1626 0.1876 0.1260 -0.0121 0.0424  -0.0005 123 PHE A CZ  
1406 N N   . ALA A 105 ? 0.1691 0.1481 0.1624 -0.0306 0.0488  -0.0037 124 ALA A N   
1407 C CA  . ALA A 105 ? 0.1966 0.1497 0.1816 -0.0093 0.0378  -0.0044 124 ALA A CA  
1408 C C   . ALA A 105 ? 0.1817 0.1375 0.1720 -0.0114 0.0384  0.0010  124 ALA A C   
1409 O O   . ALA A 105 ? 0.2033 0.1373 0.1826 -0.0116 0.0378  0.0091  124 ALA A O   
1410 C CB  . ALA A 105 ? 0.2169 0.1549 0.1778 -0.0403 0.0313  -0.0064 124 ALA A CB  
1416 N N   . ALA A 106 ? 0.1682 0.1331 0.1554 -0.0157 0.0486  -0.0145 125 ALA A N   
1417 C CA  . ALA A 106 ? 0.1734 0.1447 0.1611 -0.0163 0.0450  -0.0150 125 ALA A CA  
1418 C C   . ALA A 106 ? 0.1749 0.1456 0.1512 -0.0092 0.0310  -0.0179 125 ALA A C   
1419 O O   . ALA A 106 ? 0.1886 0.1509 0.1522 -0.0104 0.0287  -0.0119 125 ALA A O   
1420 C CB  . ALA A 106 ? 0.2103 0.1463 0.1703 -0.0094 0.0699  -0.0015 125 ALA A CB  
1426 N N   . HIS A 107 ? 0.1763 0.1379 0.1476 -0.0234 0.0427  -0.0098 126 HIS A N   
1427 C CA  . HIS A 107 ? 0.1789 0.1581 0.1589 -0.0173 0.0279  -0.0001 126 HIS A CA  
1428 C C   . HIS A 107 ? 0.2034 0.1509 0.1586 -0.0324 0.0186  -0.0025 126 HIS A C   
1429 O O   . HIS A 107 ? 0.2195 0.1350 0.1546 -0.0198 0.0202  -0.0096 126 HIS A O   
1430 C CB  . HIS A 107 ? 0.1600 0.1591 0.1593 -0.0285 0.0152  0.0075  126 HIS A CB  
1431 C CG  . HIS A 107 ? 0.1758 0.1674 0.1600 -0.0082 0.0211  -0.0005 126 HIS A CG  
1432 N ND1 . HIS A 107 ? 0.1851 0.1631 0.1528 0.0073  0.0344  0.0052  126 HIS A ND1 
1433 C CD2 . HIS A 107 ? 0.2035 0.1725 0.1702 -0.0066 0.0382  0.0062  126 HIS A CD2 
1434 C CE1 . HIS A 107 ? 0.1748 0.1778 0.1671 0.0085  0.0410  0.0093  126 HIS A CE1 
1435 N NE2 . HIS A 107 ? 0.2033 0.1786 0.1570 0.0001  0.0383  0.0116  126 HIS A NE2 
1443 N N   . LYS A 108 ? 0.2045 0.1443 0.1494 -0.0381 0.0118  -0.0185 127 LYS A N   
1444 C CA  . LYS A 108 ? 0.1902 0.1558 0.1593 -0.0286 0.0176  -0.0243 127 LYS A CA  
1445 C C   . LYS A 108 ? 0.2129 0.1639 0.1704 -0.0336 0.0187  -0.0207 127 LYS A C   
1446 O O   . LYS A 108 ? 0.2281 0.1770 0.1901 -0.0413 0.0069  -0.0391 127 LYS A O   
1447 C CB  . LYS A 108 ? 0.2012 0.1729 0.1548 0.0070  0.0161  -0.0223 127 LYS A CB  
1448 C CG  . LYS A 108 ? 0.2026 0.1973 0.1572 0.0095  -0.0006 -0.0421 127 LYS A CG  
1449 C CD  . LYS A 108 ? 0.1952 0.2049 0.1605 0.0289  0.0019  -0.0420 127 LYS A CD  
1450 C CE  . LYS A 108 ? 0.1966 0.2241 0.1716 0.0315  -0.0081 -0.0513 127 LYS A CE  
1451 N NZ  . LYS A 108 ? 0.2115 0.2179 0.1906 0.0354  -0.0183 -0.0664 127 LYS A NZ  
1465 N N   . GLU A 109 ? 0.1976 0.1642 0.1700 -0.0098 0.0203  -0.0109 128 GLU A N   
1466 C CA  . GLU A 109 ? 0.1953 0.1736 0.1652 -0.0321 0.0158  -0.0065 128 GLU A CA  
1467 C C   . GLU A 109 ? 0.2063 0.1546 0.1615 -0.0284 0.0355  -0.0111 128 GLU A C   
1468 O O   . GLU A 109 ? 0.2178 0.1595 0.1760 -0.0405 0.0362  -0.0172 128 GLU A O   
1469 C CB  . GLU A 109 ? 0.1871 0.1898 0.1651 -0.0367 -0.0103 0.0023  128 GLU A CB  
1470 C CG  . GLU A 109 ? 0.1904 0.1908 0.1657 -0.0049 0.0251  0.0008  128 GLU A CG  
1471 C CD  . GLU A 109 ? 0.2591 0.2367 0.1891 0.0304  0.0466  0.0179  128 GLU A CD  
1472 O OE1 . GLU A 109 ? 0.2798 0.2614 0.1794 0.0297  0.0758  0.0216  128 GLU A OE1 
1473 O OE2 . GLU A 109 ? 0.3034 0.2564 0.2304 0.0231  0.0528  0.0415  128 GLU A OE2 
1480 N N   . TYR A 110 ? 0.1877 0.1474 0.1504 -0.0374 0.0283  -0.0113 129 TYR A N   
1481 C CA  . TYR A 110 ? 0.1949 0.1550 0.1505 -0.0272 0.0205  -0.0024 129 TYR A CA  
1482 C C   . TYR A 110 ? 0.2192 0.1654 0.1556 -0.0195 0.0121  0.0063  129 TYR A C   
1483 O O   . TYR A 110 ? 0.2105 0.1419 0.1680 -0.0170 0.0122  0.0092  129 TYR A O   
1484 C CB  . TYR A 110 ? 0.1566 0.1519 0.1538 -0.0031 0.0259  -0.0041 129 TYR A CB  
1485 C CG  . TYR A 110 ? 0.1819 0.1532 0.1517 -0.0165 0.0259  0.0165  129 TYR A CG  
1486 C CD1 . TYR A 110 ? 0.1911 0.1482 0.1430 -0.0180 0.0289  -0.0006 129 TYR A CD1 
1487 C CD2 . TYR A 110 ? 0.1548 0.1539 0.1556 0.0100  0.0398  0.0186  129 TYR A CD2 
1488 C CE1 . TYR A 110 ? 0.2078 0.1568 0.1533 0.0057  0.0459  0.0119  129 TYR A CE1 
1489 C CE2 . TYR A 110 ? 0.1992 0.1574 0.1604 -0.0124 0.0464  0.0284  129 TYR A CE2 
1490 C CZ  . TYR A 110 ? 0.1929 0.1476 0.1455 -0.0036 0.0422  0.0226  129 TYR A CZ  
1491 O OH  . TYR A 110 ? 0.2044 0.1666 0.1499 -0.0061 0.0415  0.0303  129 TYR A OH  
1501 N N   . ALA A 111 ? 0.2137 0.1706 0.1578 -0.0136 0.0312  -0.0026 130 ALA A N   
1502 C CA  . ALA A 111 ? 0.1873 0.1743 0.1744 -0.0220 0.0213  -0.0108 130 ALA A CA  
1503 C C   . ALA A 111 ? 0.2057 0.1615 0.1839 -0.0236 0.0208  -0.0075 130 ALA A C   
1504 O O   . ALA A 111 ? 0.2415 0.1519 0.1914 -0.0143 0.0237  -0.0026 130 ALA A O   
1505 C CB  . ALA A 111 ? 0.1956 0.1792 0.1821 -0.0317 0.0296  -0.0038 130 ALA A CB  
1511 N N   . LYS A 112 ? 0.1835 0.1674 0.2009 -0.0162 0.0200  -0.0237 131 LYS A N   
1512 C CA  . LYS A 112 ? 0.2051 0.1709 0.2162 -0.0243 0.0148  -0.0242 131 LYS A CA  
1513 C C   . LYS A 112 ? 0.2021 0.1854 0.2359 -0.0400 0.0145  -0.0280 131 LYS A C   
1514 O O   . LYS A 112 ? 0.2047 0.2059 0.2562 -0.0466 0.0041  -0.0404 131 LYS A O   
1515 C CB  . LYS A 112 ? 0.2240 0.1676 0.2183 -0.0097 0.0201  -0.0158 131 LYS A CB  
1516 C CG  . LYS A 112 ? 0.2277 0.1632 0.2062 -0.0163 0.0193  -0.0095 131 LYS A CG  
1517 C CD  . LYS A 112 ? 0.2319 0.1627 0.2120 -0.0238 0.0188  -0.0074 131 LYS A CD  
1518 C CE  . LYS A 112 ? 0.2369 0.1585 0.2007 -0.0304 0.0232  0.0003  131 LYS A CE  
1519 N NZ  . LYS A 112 ? 0.2256 0.1457 0.2005 -0.0415 0.0171  0.0034  131 LYS A NZ  
1533 N N   . HIS A 113 ? 0.2077 0.1838 0.2346 -0.0160 0.0158  -0.0246 132 HIS A N   
1534 C CA  . HIS A 113 ? 0.2043 0.1773 0.2368 -0.0059 0.0215  -0.0232 132 HIS A CA  
1535 C C   . HIS A 113 ? 0.2331 0.1789 0.2409 -0.0069 0.0023  -0.0295 132 HIS A C   
1536 O O   . HIS A 113 ? 0.1695 0.1682 0.2352 -0.0083 0.0085  -0.0235 132 HIS A O   
1537 C CB  . HIS A 113 ? 0.2216 0.1960 0.2461 -0.0197 0.0289  -0.0177 132 HIS A CB  
1538 C CG  . HIS A 113 ? 0.2341 0.2209 0.2580 -0.0086 -0.0006 -0.0211 132 HIS A CG  
1539 N ND1 . HIS A 113 ? 0.2693 0.2396 0.2606 -0.0233 -0.0088 -0.0280 132 HIS A ND1 
1540 C CD2 . HIS A 113 ? 0.2455 0.2320 0.2642 -0.0144 0.0058  -0.0187 132 HIS A CD2 
1541 C CE1 . HIS A 113 ? 0.2943 0.2501 0.2728 -0.0139 -0.0070 -0.0211 132 HIS A CE1 
1542 N NE2 . HIS A 113 ? 0.3032 0.2489 0.2772 -0.0151 -0.0026 -0.0152 132 HIS A NE2 
1550 N N   . PRO A 114 ? 0.2286 0.1733 0.2517 0.0046  0.0109  -0.0307 133 PRO A N   
1551 C CA  . PRO A 114 ? 0.2576 0.1742 0.2515 0.0221  0.0226  -0.0188 133 PRO A CA  
1552 C C   . PRO A 114 ? 0.2473 0.1713 0.2498 0.0074  0.0288  -0.0067 133 PRO A C   
1553 O O   . PRO A 114 ? 0.2313 0.1626 0.2549 0.0026  0.0319  0.0012  133 PRO A O   
1554 C CB  . PRO A 114 ? 0.3047 0.1883 0.2643 0.0386  0.0182  -0.0306 133 PRO A CB  
1555 C CG  . PRO A 114 ? 0.3100 0.1844 0.2674 0.0252  -0.0034 -0.0329 133 PRO A CG  
1556 C CD  . PRO A 114 ? 0.2627 0.1749 0.2598 0.0241  0.0129  -0.0344 133 PRO A CD  
1564 N N   . GLN A 115 ? 0.2540 0.1755 0.2551 0.0222  0.0332  -0.0149 134 GLN A N   
1565 C CA  . GLN A 115 ? 0.2682 0.1968 0.2461 0.0093  0.0391  -0.0188 134 GLN A CA  
1566 C C   . GLN A 115 ? 0.2255 0.1915 0.2352 -0.0063 0.0629  -0.0046 134 GLN A C   
1567 O O   . GLN A 115 ? 0.2384 0.2254 0.2498 -0.0037 0.0734  0.0062  134 GLN A O   
1568 C CB  . GLN A 115 ? 0.3321 0.2435 0.2742 -0.0114 0.0319  -0.0436 134 GLN A CB  
1569 C CG  . GLN A 115 ? 0.4147 0.3007 0.2938 -0.0173 0.0385  -0.0368 134 GLN A CG  
1570 C CD  . GLN A 115 ? 0.4285 0.3175 0.2929 -0.0264 0.0294  -0.0316 134 GLN A CD  
1571 O OE1 . GLN A 115 ? 0.3540 0.2837 0.2716 -0.0273 0.0382  -0.0545 134 GLN A OE1 
1572 N NE2 . GLN A 115 ? 0.4388 0.3517 0.3021 -0.0255 0.0269  -0.0238 134 GLN A NE2 
1581 N N   . TRP A 116 ? 0.1815 0.1689 0.2228 -0.0137 0.0416  0.0115  135 TRP A N   
1582 C CA  . TRP A 116 ? 0.2009 0.1808 0.2087 0.0080  0.0377  0.0124  135 TRP A CA  
1583 C C   . TRP A 116 ? 0.1992 0.1731 0.1837 0.0132  0.0213  0.0056  135 TRP A C   
1584 O O   . TRP A 116 ? 0.1832 0.1788 0.1825 -0.0026 0.0454  0.0031  135 TRP A O   
1585 C CB  . TRP A 116 ? 0.2162 0.1741 0.2023 0.0184  0.0240  0.0159  135 TRP A CB  
1586 C CG  . TRP A 116 ? 0.2061 0.1854 0.2007 0.0023  0.0149  0.0048  135 TRP A CG  
1587 C CD1 . TRP A 116 ? 0.2308 0.1774 0.1989 -0.0014 0.0050  0.0166  135 TRP A CD1 
1588 C CD2 . TRP A 116 ? 0.1967 0.1712 0.2004 0.0001  0.0113  -0.0016 135 TRP A CD2 
1589 N NE1 . TRP A 116 ? 0.2269 0.1833 0.2025 -0.0111 -0.0099 0.0095  135 TRP A NE1 
1590 C CE2 . TRP A 116 ? 0.2271 0.1734 0.1989 -0.0114 0.0051  -0.0043 135 TRP A CE2 
1591 C CE3 . TRP A 116 ? 0.2113 0.1741 0.1987 -0.0155 -0.0007 -0.0041 135 TRP A CE3 
1592 C CZ2 . TRP A 116 ? 0.2260 0.1836 0.2097 -0.0032 -0.0068 -0.0130 135 TRP A CZ2 
1593 C CZ3 . TRP A 116 ? 0.2316 0.1898 0.2001 -0.0184 0.0116  -0.0058 135 TRP A CZ3 
1594 C CH2 . TRP A 116 ? 0.2508 0.1799 0.2038 -0.0056 0.0048  0.0004  135 TRP A CH2 
1605 N N   . TRP A 117 ? 0.2049 0.1523 0.1758 0.0067  0.0292  0.0004  136 TRP A N   
1606 C CA  . TRP A 117 ? 0.1630 0.1543 0.1711 0.0116  0.0398  0.0099  136 TRP A CA  
1607 C C   . TRP A 117 ? 0.1808 0.1712 0.1731 0.0205  0.0570  0.0144  136 TRP A C   
1608 O O   . TRP A 117 ? 0.2083 0.1968 0.1706 0.0082  0.0558  0.0205  136 TRP A O   
1609 C CB  . TRP A 117 ? 0.1743 0.1555 0.1727 0.0115  0.0360  0.0141  136 TRP A CB  
1610 C CG  . TRP A 117 ? 0.1890 0.1549 0.1746 0.0088  0.0361  0.0089  136 TRP A CG  
1611 C CD1 . TRP A 117 ? 0.1694 0.1606 0.1779 0.0036  0.0460  0.0104  136 TRP A CD1 
1612 C CD2 . TRP A 117 ? 0.1963 0.1444 0.1721 0.0118  0.0330  -0.0105 136 TRP A CD2 
1613 N NE1 . TRP A 117 ? 0.2035 0.1539 0.1784 0.0117  0.0341  -0.0073 136 TRP A NE1 
1614 C CE2 . TRP A 117 ? 0.2119 0.1483 0.1777 0.0310  0.0280  -0.0138 136 TRP A CE2 
1615 C CE3 . TRP A 117 ? 0.2499 0.1473 0.1814 0.0201  0.0322  -0.0070 136 TRP A CE3 
1616 C CZ2 . TRP A 117 ? 0.2584 0.1525 0.1946 0.0345  0.0357  -0.0178 136 TRP A CZ2 
1617 C CZ3 . TRP A 117 ? 0.2643 0.1559 0.1937 0.0132  0.0398  -0.0079 136 TRP A CZ3 
1618 C CH2 . TRP A 117 ? 0.2766 0.1804 0.1989 0.0274  0.0363  -0.0230 136 TRP A CH2 
1629 N N   . LEU A 118 ? 0.1999 0.1719 0.1552 0.0061  0.0321  0.0071  137 LEU A N   
1630 C CA  . LEU A 118 ? 0.2156 0.1693 0.1705 0.0144  0.0364  0.0141  137 LEU A CA  
1631 C C   . LEU A 118 ? 0.2148 0.1668 0.1790 0.0185  0.0366  0.0218  137 LEU A C   
1632 O O   . LEU A 118 ? 0.1853 0.1662 0.1811 0.0107  0.0623  0.0142  137 LEU A O   
1633 C CB  . LEU A 118 ? 0.2128 0.1712 0.1713 0.0134  0.0399  0.0127  137 LEU A CB  
1634 C CG  . LEU A 118 ? 0.2318 0.1797 0.1587 0.0157  0.0376  0.0150  137 LEU A CG  
1635 C CD1 . LEU A 118 ? 0.2415 0.2009 0.1643 0.0278  0.0650  0.0183  137 LEU A CD1 
1636 C CD2 . LEU A 118 ? 0.2532 0.1856 0.1578 0.0162  0.0260  -0.0008 137 LEU A CD2 
1648 N N   . ARG A 119 ? 0.2131 0.1541 0.1822 0.0272  0.0267  0.0402  138 ARG A N   
1649 C CA  . ARG A 119 ? 0.2070 0.1639 0.1830 0.0253  0.0140  0.0423  138 ARG A CA  
1650 C C   . ARG A 119 ? 0.2008 0.1635 0.1808 0.0186  0.0221  0.0325  138 ARG A C   
1651 O O   . ARG A 119 ? 0.2249 0.1771 0.1846 0.0351  0.0405  0.0476  138 ARG A O   
1652 C CB  . ARG A 119 ? 0.2394 0.1886 0.1902 0.0001  0.0105  0.0304  138 ARG A CB  
1653 C CG  . ARG A 119 ? 0.2367 0.2082 0.1791 0.0024  -0.0065 0.0360  138 ARG A CG  
1654 C CD  . ARG A 119 ? 0.2373 0.2416 0.1829 -0.0139 0.0045  0.0074  138 ARG A CD  
1655 N NE  . ARG A 119 ? 0.2137 0.2620 0.1865 -0.0218 -0.0037 -0.0125 138 ARG A NE  
1656 C CZ  . ARG A 119 ? 0.2003 0.2635 0.1789 0.0047  0.0079  -0.0241 138 ARG A CZ  
1657 N NH1 . ARG A 119 ? 0.1983 0.2465 0.1750 0.0028  0.0017  -0.0139 138 ARG A NH1 
1658 N NH2 . ARG A 119 ? 0.1978 0.2918 0.1878 0.0294  0.0267  -0.0213 138 ARG A NH2 
1672 N N   . THR A 120 ? 0.1815 0.1759 0.1736 0.0035  0.0063  0.0156  139 THR A N   
1673 C CA  . THR A 120 ? 0.1694 0.1590 0.1809 0.0010  0.0086  0.0184  139 THR A CA  
1674 C C   . THR A 120 ? 0.1711 0.1540 0.1849 -0.0020 -0.0089 0.0193  139 THR A C   
1675 O O   . THR A 120 ? 0.1761 0.1779 0.1834 -0.0040 -0.0114 0.0192  139 THR A O   
1676 C CB  . THR A 120 ? 0.1773 0.1886 0.2047 -0.0244 -0.0008 0.0075  139 THR A CB  
1677 O OG1 . THR A 120 ? 0.2060 0.1885 0.2110 0.0128  0.0086  0.0191  139 THR A OG1 
1678 C CG2 . THR A 120 ? 0.1764 0.2177 0.2102 -0.0358 0.0202  0.0000  139 THR A CG2 
1686 N N   . THR A 121 ? 0.1558 0.1561 0.1797 -0.0124 -0.0128 0.0194  140 THR A N   
1687 C CA  . THR A 121 ? 0.1503 0.1706 0.1874 -0.0108 0.0002  0.0295  140 THR A CA  
1688 C C   . THR A 121 ? 0.1831 0.1692 0.1872 -0.0269 0.0099  0.0277  140 THR A C   
1689 O O   . THR A 121 ? 0.2296 0.1813 0.1993 -0.0496 0.0069  0.0161  140 THR A O   
1690 C CB  . THR A 121 ? 0.1437 0.1723 0.1821 -0.0060 0.0066  0.0270  140 THR A CB  
1691 O OG1 . THR A 121 ? 0.1447 0.1835 0.1797 -0.0053 -0.0100 0.0269  140 THR A OG1 
1692 C CG2 . THR A 121 ? 0.1723 0.1736 0.1851 -0.0159 0.0129  0.0205  140 THR A CG2 
1700 N N   . THR A 122 ? 0.2048 0.1525 0.1957 -0.0115 0.0041  0.0329  141 THR A N   
1701 C CA  . THR A 122 ? 0.2577 0.1878 0.2165 -0.0023 -0.0060 0.0175  141 THR A CA  
1702 C C   . THR A 122 ? 0.2710 0.1794 0.2145 -0.0071 -0.0189 0.0155  141 THR A C   
1703 O O   . THR A 122 ? 0.3109 0.1862 0.2392 -0.0224 -0.0197 0.0122  141 THR A O   
1704 C CB  . THR A 122 ? 0.2650 0.2081 0.2369 0.0231  -0.0113 0.0241  141 THR A CB  
1705 O OG1 . THR A 122 ? 0.2575 0.2029 0.2657 0.0199  -0.0137 0.0073  141 THR A OG1 
1706 C CG2 . THR A 122 ? 0.2821 0.2213 0.2434 0.0251  -0.0324 0.0272  141 THR A CG2 
1714 N N   . GLY A 123 ? 0.2643 0.1800 0.1979 -0.0146 -0.0065 0.0211  142 GLY A N   
1715 C CA  . GLY A 123 ? 0.2391 0.1723 0.1904 -0.0234 -0.0167 0.0131  142 GLY A CA  
1716 C C   . GLY A 123 ? 0.2361 0.1861 0.1825 0.0162  -0.0174 0.0182  142 GLY A C   
1717 O O   . GLY A 123 ? 0.2803 0.1972 0.1667 0.0151  -0.0058 0.0234  142 GLY A O   
1721 N N   . GLU A 124 ? 0.2069 0.1772 0.2010 0.0149  -0.0100 0.0031  143 GLU A N   
1722 C CA  . GLU A 124 ? 0.2051 0.2052 0.2227 0.0584  0.0142  0.0142  143 GLU A CA  
1723 C C   . GLU A 124 ? 0.1788 0.1926 0.2103 0.0419  0.0270  0.0156  143 GLU A C   
1724 O O   . GLU A 124 ? 0.2055 0.1965 0.2183 0.0446  0.0465  0.0161  143 GLU A O   
1725 C CB  . GLU A 124 ? 0.2268 0.2499 0.2486 0.0801  0.0192  0.0101  143 GLU A CB  
1726 C CG  . GLU A 124 ? 0.2686 0.3146 0.2797 0.0872  0.0114  0.0030  143 GLU A CG  
1727 C CD  . GLU A 124 ? 0.3156 0.3795 0.3114 0.0620  0.0090  -0.0004 143 GLU A CD  
1728 O OE1 . GLU A 124 ? 0.3219 0.4044 0.3242 0.0341  -0.0204 -0.0080 143 GLU A OE1 
1729 O OE2 . GLU A 124 ? 0.3324 0.4043 0.3301 0.0687  0.0131  0.0080  143 GLU A OE2 
1736 N N   . LEU A 125 ? 0.1750 0.1901 0.2078 0.0306  0.0320  0.0040  144 LEU A N   
1737 C CA  . LEU A 125 ? 0.1968 0.1809 0.1978 0.0119  0.0278  -0.0045 144 LEU A CA  
1738 C C   . LEU A 125 ? 0.1782 0.1764 0.2072 0.0003  0.0189  -0.0062 144 LEU A C   
1739 O O   . LEU A 125 ? 0.1916 0.1840 0.2159 0.0160  0.0045  0.0053  144 LEU A O   
1740 C CB  . LEU A 125 ? 0.2066 0.1979 0.1928 0.0172  0.0408  -0.0054 144 LEU A CB  
1741 C CG  . LEU A 125 ? 0.2342 0.2156 0.1897 0.0045  0.0344  0.0067  144 LEU A CG  
1742 C CD1 . LEU A 125 ? 0.2406 0.2285 0.1860 0.0108  0.0385  -0.0019 144 LEU A CD1 
1743 C CD2 . LEU A 125 ? 0.2670 0.2373 0.1920 0.0039  0.0269  0.0145  144 LEU A CD2 
1755 N N   . ASP A 126 ? 0.1685 0.1644 0.1984 0.0036  0.0331  -0.0072 145 ASP A N   
1756 C CA  . ASP A 126 ? 0.1662 0.1632 0.1969 -0.0096 0.0232  0.0087  145 ASP A CA  
1757 C C   . ASP A 126 ? 0.1706 0.1721 0.1959 0.0041  0.0272  0.0101  145 ASP A C   
1758 O O   . ASP A 126 ? 0.1670 0.1829 0.1758 0.0172  0.0106  0.0090  145 ASP A O   
1759 C CB  . ASP A 126 ? 0.1868 0.1685 0.1982 -0.0193 0.0445  0.0145  145 ASP A CB  
1760 C CG  . ASP A 126 ? 0.2307 0.1791 0.2046 -0.0165 0.0492  -0.0024 145 ASP A CG  
1761 O OD1 . ASP A 126 ? 0.2045 0.1890 0.2128 -0.0028 0.0163  -0.0110 145 ASP A OD1 
1762 O OD2 . ASP A 126 ? 0.2703 0.1795 0.2134 -0.0007 0.0700  -0.0264 145 ASP A OD2 
1767 N N   . ARG A 127 ? 0.1552 0.1890 0.1829 -0.0131 0.0173  -0.0016 146 ARG A N   
1768 C CA  . ARG A 127 ? 0.1615 0.1924 0.2013 -0.0094 0.0233  -0.0011 146 ARG A CA  
1769 C C   . ARG A 127 ? 0.1835 0.2212 0.2137 -0.0152 0.0061  -0.0033 146 ARG A C   
1770 O O   . ARG A 127 ? 0.2136 0.2388 0.2148 0.0054  -0.0131 -0.0006 146 ARG A O   
1771 C CB  . ARG A 127 ? 0.1623 0.1914 0.2105 0.0180  0.0162  -0.0001 146 ARG A CB  
1772 C CG  . ARG A 127 ? 0.1765 0.1919 0.1889 0.0314  0.0164  -0.0218 146 ARG A CG  
1773 C CD  . ARG A 127 ? 0.1999 0.1987 0.1910 0.0545  0.0244  -0.0201 146 ARG A CD  
1774 N NE  . ARG A 127 ? 0.2160 0.1979 0.2003 0.0430  0.0395  -0.0206 146 ARG A NE  
1775 C CZ  . ARG A 127 ? 0.2116 0.2102 0.2016 0.0312  0.0242  -0.0398 146 ARG A CZ  
1776 N NH1 . ARG A 127 ? 0.2150 0.2129 0.2085 0.0254  0.0290  -0.0571 146 ARG A NH1 
1777 N NH2 . ARG A 127 ? 0.2504 0.2286 0.2221 0.0195  0.0102  -0.0419 146 ARG A NH2 
1791 N N   . LYS A 128 ? 0.2016 0.2259 0.2318 -0.0327 -0.0206 -0.0066 147 LYS A N   
1792 C CA  . LYS A 128 ? 0.2064 0.2687 0.2737 -0.0219 -0.0361 -0.0146 147 LYS A CA  
1793 C C   . LYS A 128 ? 0.2275 0.2995 0.2915 -0.0244 -0.0268 -0.0104 147 LYS A C   
1794 O O   . LYS A 128 ? 0.2404 0.3155 0.2743 -0.0181 -0.0097 -0.0046 147 LYS A O   
1795 C CB  . LYS A 128 ? 0.2331 0.2750 0.2932 -0.0111 -0.0229 -0.0216 147 LYS A CB  
1796 C CG  . LYS A 128 ? 0.2581 0.2917 0.3210 0.0088  -0.0065 -0.0357 147 LYS A CG  
1797 C CD  . LYS A 128 ? 0.2871 0.3074 0.3449 0.0126  0.0040  -0.0579 147 LYS A CD  
1798 C CE  . LYS A 128 ? 0.3125 0.3275 0.3734 0.0075  0.0112  -0.0504 147 LYS A CE  
1799 N NZ  . LYS A 128 ? 0.3226 0.3361 0.3849 -0.0143 0.0148  -0.0466 147 LYS A NZ  
1813 N N   . LYS A 129 ? 0.2499 0.3235 0.3134 -0.0308 -0.0485 -0.0012 148 LYS A N   
1814 C CA  . LYS A 129 ? 0.2775 0.3592 0.3502 -0.0092 -0.0538 -0.0044 148 LYS A CA  
1815 C C   . LYS A 129 ? 0.2659 0.3667 0.3538 0.0179  -0.0109 -0.0036 148 LYS A C   
1816 O O   . LYS A 129 ? 0.2746 0.3662 0.3643 0.0176  0.0104  0.0081  148 LYS A O   
1817 C CB  . LYS A 129 ? 0.3371 0.3787 0.3792 -0.0207 -0.0851 0.0053  148 LYS A CB  
1818 C CG  . LYS A 129 ? 0.4202 0.3996 0.4127 -0.0096 -0.0931 0.0198  148 LYS A CG  
1819 C CD  . LYS A 129 ? 0.4763 0.4137 0.4387 -0.0157 -0.1067 0.0340  148 LYS A CD  
1820 C CE  . LYS A 129 ? 0.5114 0.4219 0.4594 -0.0235 -0.1153 0.0481  148 LYS A CE  
1821 N NZ  . LYS A 129 ? 0.5325 0.4273 0.4716 -0.0236 -0.1218 0.0561  148 LYS A NZ  
1835 N N   . GLY A 130 ? 0.2307 0.3678 0.3330 0.0206  -0.0028 -0.0165 149 GLY A N   
1836 C CA  . GLY A 130 ? 0.2101 0.3592 0.3182 0.0228  0.0048  -0.0158 149 GLY A CA  
1837 C C   . GLY A 130 ? 0.2262 0.3476 0.3050 0.0230  0.0125  -0.0191 149 GLY A C   
1838 O O   . GLY A 130 ? 0.2287 0.3513 0.2980 0.0120  0.0277  -0.0260 149 GLY A O   
1842 N N   . GLN A 131 ? 0.2203 0.3153 0.2897 0.0145  0.0107  -0.0281 150 GLN A N   
1843 C CA  . GLN A 131 ? 0.2346 0.2838 0.2799 0.0290  0.0024  -0.0482 150 GLN A CA  
1844 C C   . GLN A 131 ? 0.2253 0.2642 0.2619 0.0204  0.0064  -0.0262 150 GLN A C   
1845 O O   . GLN A 131 ? 0.2528 0.2683 0.2733 0.0415  -0.0033 -0.0268 150 GLN A O   
1846 C CB  . GLN A 131 ? 0.2699 0.2785 0.2944 0.0565  0.0056  -0.0580 150 GLN A CB  
1847 C CG  . GLN A 131 ? 0.2806 0.2841 0.3130 0.0781  0.0145  -0.0718 150 GLN A CG  
1848 C CD  . GLN A 131 ? 0.3325 0.3022 0.3324 0.0715  0.0085  -0.0687 150 GLN A CD  
1849 O OE1 . GLN A 131 ? 0.3555 0.3039 0.3456 0.0651  0.0314  -0.0647 150 GLN A OE1 
1850 N NE2 . GLN A 131 ? 0.3210 0.3162 0.3346 0.0895  0.0009  -0.0685 150 GLN A NE2 
1859 N N   . LEU A 132 ? 0.1977 0.2346 0.2271 -0.0077 0.0096  -0.0141 151 LEU A N   
1860 C CA  . LEU A 132 ? 0.1952 0.1925 0.2059 -0.0159 0.0157  -0.0125 151 LEU A CA  
1861 C C   . LEU A 132 ? 0.1706 0.1766 0.1782 0.0087  0.0035  -0.0101 151 LEU A C   
1862 O O   . LEU A 132 ? 0.1892 0.1966 0.1798 -0.0228 0.0063  -0.0065 151 LEU A O   
1863 C CB  . LEU A 132 ? 0.1975 0.2093 0.2202 -0.0124 0.0184  -0.0237 151 LEU A CB  
1864 C CG  . LEU A 132 ? 0.2092 0.2168 0.2312 0.0108  0.0137  -0.0223 151 LEU A CG  
1865 C CD1 . LEU A 132 ? 0.2338 0.2364 0.2379 0.0299  0.0106  -0.0200 151 LEU A CD1 
1866 C CD2 . LEU A 132 ? 0.2040 0.2207 0.2349 -0.0287 0.0084  -0.0264 151 LEU A CD2 
1878 N N   . MET A 133 ? 0.1707 0.1677 0.1735 0.0161  0.0197  0.0026  152 MET A N   
1879 C CA  . MET A 133 ? 0.1433 0.1571 0.1653 0.0060  0.0265  -0.0115 152 MET A CA  
1880 C C   . MET A 133 ? 0.1687 0.1641 0.1572 0.0059  0.0270  -0.0003 152 MET A C   
1881 O O   . MET A 133 ? 0.1858 0.1639 0.1603 0.0122  0.0247  -0.0149 152 MET A O   
1882 C CB  . MET A 133 ? 0.1750 0.1784 0.1851 0.0016  0.0109  -0.0227 152 MET A CB  
1883 C CG  . MET A 133 ? 0.2167 0.1959 0.1980 -0.0080 -0.0174 -0.0220 152 MET A CG  
1884 S SD  . MET A 133 ? 0.1931 0.1717 0.1932 -0.0120 0.0109  -0.0027 152 MET A SD  
1885 C CE  . MET A 133 ? 0.2240 0.1776 0.1951 -0.0215 0.0296  0.0092  152 MET A CE  
1895 N N   . ARG A 134 ? 0.1625 0.1605 0.1419 0.0278  0.0201  0.0113  153 ARG A N   
1896 C CA  . ARG A 134 ? 0.1607 0.1592 0.1372 0.0204  0.0154  -0.0048 153 ARG A CA  
1897 C C   . ARG A 134 ? 0.1843 0.1469 0.1416 -0.0017 0.0220  0.0103  153 ARG A C   
1898 O O   . ARG A 134 ? 0.2046 0.1427 0.1759 0.0133  0.0106  0.0215  153 ARG A O   
1899 C CB  . ARG A 134 ? 0.1730 0.1703 0.1446 0.0154  0.0059  -0.0048 153 ARG A CB  
1900 C CG  . ARG A 134 ? 0.1784 0.1673 0.1448 0.0123  0.0015  -0.0012 153 ARG A CG  
1901 C CD  . ARG A 134 ? 0.1923 0.1797 0.1434 0.0146  0.0120  -0.0104 153 ARG A CD  
1902 N NE  . ARG A 134 ? 0.2154 0.1673 0.1345 0.0229  0.0101  -0.0073 153 ARG A NE  
1903 C CZ  . ARG A 134 ? 0.2479 0.1740 0.1477 0.0369  0.0088  -0.0078 153 ARG A CZ  
1904 N NH1 . ARG A 134 ? 0.2588 0.1690 0.1517 0.0349  0.0083  -0.0157 153 ARG A NH1 
1905 N NH2 . ARG A 134 ? 0.2517 0.1895 0.1420 0.0370  0.0187  -0.0071 153 ARG A NH2 
1919 N N   . TYR A 135 ? 0.1701 0.1267 0.1581 -0.0044 0.0062  0.0113  154 TYR A N   
1920 C CA  . TYR A 135 ? 0.1662 0.1454 0.1602 -0.0027 0.0200  0.0295  154 TYR A CA  
1921 C C   . TYR A 135 ? 0.1625 0.1532 0.1540 -0.0021 0.0131  0.0009  154 TYR A C   
1922 O O   . TYR A 135 ? 0.1857 0.1687 0.1548 0.0015  0.0241  0.0208  154 TYR A O   
1923 C CB  . TYR A 135 ? 0.1702 0.1347 0.1442 -0.0134 0.0093  0.0144  154 TYR A CB  
1924 C CG  . TYR A 135 ? 0.1666 0.1523 0.1314 0.0040  0.0272  0.0067  154 TYR A CG  
1925 C CD1 . TYR A 135 ? 0.1726 0.1519 0.1343 0.0092  0.0243  0.0106  154 TYR A CD1 
1926 C CD2 . TYR A 135 ? 0.1720 0.1579 0.1359 -0.0021 0.0201  0.0016  154 TYR A CD2 
1927 C CE1 . TYR A 135 ? 0.1881 0.1530 0.1308 0.0091  0.0229  0.0011  154 TYR A CE1 
1928 C CE2 . TYR A 135 ? 0.1587 0.1596 0.1398 -0.0145 0.0217  0.0077  154 TYR A CE2 
1929 C CZ  . TYR A 135 ? 0.1704 0.1517 0.1238 -0.0091 0.0335  0.0037  154 TYR A CZ  
1930 O OH  . TYR A 135 ? 0.1974 0.1476 0.1395 -0.0076 0.0389  0.0006  154 TYR A OH  
1940 N N   . ASP A 136 ? 0.1693 0.1440 0.1667 -0.0022 0.0318  0.0025  155 ASP A N   
1941 C CA  . ASP A 136 ? 0.1630 0.1446 0.1592 -0.0080 0.0424  0.0151  155 ASP A CA  
1942 C C   . ASP A 136 ? 0.1489 0.1447 0.1516 -0.0221 0.0397  0.0160  155 ASP A C   
1943 O O   . ASP A 136 ? 0.1879 0.1748 0.1548 -0.0223 0.0467  0.0142  155 ASP A O   
1944 C CB  . ASP A 136 ? 0.1704 0.1498 0.1820 -0.0177 0.0633  0.0145  155 ASP A CB  
1945 C CG  . ASP A 136 ? 0.1916 0.1616 0.2045 -0.0186 0.0679  0.0204  155 ASP A CG  
1946 O OD1 . ASP A 136 ? 0.1808 0.1642 0.1881 -0.0013 0.0534  0.0239  155 ASP A OD1 
1947 O OD2 . ASP A 136 ? 0.2199 0.1891 0.2370 -0.0394 0.0522  0.0202  155 ASP A OD2 
1952 N N   . LEU A 137 ? 0.1616 0.1268 0.1539 -0.0023 0.0164  0.0120  156 LEU A N   
1953 C CA  . LEU A 137 ? 0.1398 0.1447 0.1659 0.0070  0.0314  0.0133  156 LEU A CA  
1954 C C   . LEU A 137 ? 0.1492 0.1562 0.1697 0.0079  0.0282  0.0195  156 LEU A C   
1955 O O   . LEU A 137 ? 0.1465 0.1578 0.1851 0.0067  0.0300  0.0238  156 LEU A O   
1956 C CB  . LEU A 137 ? 0.1659 0.1582 0.1793 -0.0115 0.0262  0.0125  156 LEU A CB  
1957 C CG  . LEU A 137 ? 0.1888 0.1780 0.1993 -0.0185 0.0285  -0.0054 156 LEU A CG  
1958 C CD1 . LEU A 137 ? 0.1935 0.1784 0.2069 -0.0209 0.0323  -0.0056 156 LEU A CD1 
1959 C CD2 . LEU A 137 ? 0.2164 0.1986 0.2076 -0.0301 0.0152  0.0006  156 LEU A CD2 
1971 N N   . SER A 138 ? 0.1543 0.1764 0.1765 0.0000  0.0316  0.0280  157 SER A N   
1972 C CA  . SER A 138 ? 0.1424 0.1950 0.1814 -0.0029 0.0487  0.0247  157 SER A CA  
1973 C C   . SER A 138 ? 0.1331 0.1901 0.1991 0.0065  0.0291  0.0068  157 SER A C   
1974 O O   . SER A 138 ? 0.1621 0.1932 0.2231 -0.0115 0.0307  0.0010  157 SER A O   
1975 C CB  . SER A 138 ? 0.1707 0.2151 0.1932 0.0024  0.0302  0.0273  157 SER A CB  
1976 O OG  . SER A 138 ? 0.1825 0.2170 0.1983 0.0092  0.0492  0.0395  157 SER A OG  
1982 N N   . ASN A 139 ? 0.1608 0.1862 0.1927 -0.0177 0.0207  0.0057  158 ASN A N   
1983 C CA  . ASN A 139 ? 0.1596 0.1746 0.1977 -0.0118 0.0199  0.0034  158 ASN A CA  
1984 C C   . ASN A 139 ? 0.1697 0.1801 0.1976 -0.0254 0.0264  0.0133  158 ASN A C   
1985 O O   . ASN A 139 ? 0.1580 0.1753 0.2053 -0.0243 0.0239  0.0194  158 ASN A O   
1986 C CB  . ASN A 139 ? 0.1876 0.1635 0.2013 -0.0163 0.0245  0.0288  158 ASN A CB  
1987 C CG  . ASN A 139 ? 0.2127 0.1516 0.2061 -0.0264 0.0224  0.0262  158 ASN A CG  
1988 O OD1 . ASN A 139 ? 0.2042 0.1685 0.2137 -0.0169 0.0189  0.0193  158 ASN A OD1 
1989 N ND2 . ASN A 139 ? 0.2540 0.1549 0.2121 -0.0237 0.0360  0.0167  158 ASN A ND2 
1996 N N   . ALA A 140 ? 0.1784 0.1958 0.2096 -0.0120 0.0320  0.0042  159 ALA A N   
1997 C CA  . ALA A 140 ? 0.1481 0.1859 0.2141 -0.0254 0.0326  0.0047  159 ALA A CA  
1998 C C   . ALA A 140 ? 0.1608 0.1751 0.2171 -0.0344 0.0251  -0.0021 159 ALA A C   
1999 O O   . ALA A 140 ? 0.1772 0.1703 0.2288 -0.0336 0.0082  -0.0008 159 ALA A O   
2000 C CB  . ALA A 140 ? 0.1419 0.1943 0.2211 -0.0116 0.0366  0.0105  159 ALA A CB  
2006 N N   . GLU A 141 ? 0.1823 0.1820 0.2338 -0.0278 0.0214  -0.0068 160 GLU A N   
2007 C CA  . GLU A 141 ? 0.1843 0.1847 0.2447 -0.0549 0.0104  -0.0063 160 GLU A CA  
2008 C C   . GLU A 141 ? 0.1789 0.1867 0.2199 -0.0317 0.0049  0.0004  160 GLU A C   
2009 O O   . GLU A 141 ? 0.1751 0.1915 0.2061 -0.0158 0.0016  0.0003  160 GLU A O   
2010 C CB  . GLU A 141 ? 0.2076 0.2111 0.2916 -0.0856 -0.0122 -0.0255 160 GLU A CB  
2011 C CG  . GLU A 141 ? 0.2535 0.2582 0.3516 -0.0932 -0.0359 -0.0341 160 GLU A CG  
2012 C CD  . GLU A 141 ? 0.3074 0.2986 0.4065 -0.0983 -0.0493 -0.0471 160 GLU A CD  
2013 O OE1 . GLU A 141 ? 0.3298 0.3155 0.4298 -0.0933 -0.0578 -0.0391 160 GLU A OE1 
2014 O OE2 . GLU A 141 ? 0.3373 0.3163 0.4274 -0.0925 -0.0636 -0.0572 160 GLU A OE2 
2021 N N   . PHE A 142 ? 0.1439 0.1722 0.2051 -0.0217 0.0089  0.0079  161 PHE A N   
2022 C CA  . PHE A 142 ? 0.1636 0.1706 0.1954 -0.0021 0.0098  0.0147  161 PHE A CA  
2023 C C   . PHE A 142 ? 0.1526 0.1650 0.1905 -0.0006 0.0137  0.0179  161 PHE A C   
2024 O O   . PHE A 142 ? 0.1569 0.1874 0.1962 -0.0113 0.0116  0.0141  161 PHE A O   
2025 C CB  . PHE A 142 ? 0.1718 0.1665 0.1907 -0.0178 0.0146  0.0146  161 PHE A CB  
2026 C CG  . PHE A 142 ? 0.1353 0.1663 0.1749 -0.0149 0.0229  0.0170  161 PHE A CG  
2027 C CD1 . PHE A 142 ? 0.1659 0.1737 0.1811 0.0008  0.0158  0.0306  161 PHE A CD1 
2028 C CD2 . PHE A 142 ? 0.1542 0.1742 0.1840 0.0002  0.0250  0.0172  161 PHE A CD2 
2029 C CE1 . PHE A 142 ? 0.1515 0.1798 0.1772 0.0010  0.0072  0.0301  161 PHE A CE1 
2030 C CE2 . PHE A 142 ? 0.1508 0.1709 0.1830 -0.0049 0.0177  0.0197  161 PHE A CE2 
2031 C CZ  . PHE A 142 ? 0.1506 0.1643 0.1828 0.0010  0.0018  0.0277  161 PHE A CZ  
2041 N N   . ARG A 143 ? 0.1651 0.1563 0.1909 -0.0123 0.0184  0.0201  162 ARG A N   
2042 C CA  . ARG A 143 ? 0.1862 0.1579 0.1949 -0.0146 0.0115  0.0162  162 ARG A CA  
2043 C C   . ARG A 143 ? 0.1802 0.1746 0.1945 -0.0245 0.0240  0.0205  162 ARG A C   
2044 O O   . ARG A 143 ? 0.1628 0.1776 0.1944 -0.0438 0.0166  0.0300  162 ARG A O   
2045 C CB  . ARG A 143 ? 0.1667 0.1587 0.1972 -0.0197 0.0136  0.0159  162 ARG A CB  
2046 C CG  . ARG A 143 ? 0.1761 0.1737 0.2042 -0.0129 0.0238  0.0288  162 ARG A CG  
2047 C CD  . ARG A 143 ? 0.1933 0.1648 0.2054 -0.0096 0.0160  0.0217  162 ARG A CD  
2048 N NE  . ARG A 143 ? 0.1828 0.1845 0.2137 0.0163  0.0452  0.0200  162 ARG A NE  
2049 C CZ  . ARG A 143 ? 0.1275 0.2155 0.2232 0.0120  0.0384  0.0130  162 ARG A CZ  
2050 N NH1 . ARG A 143 ? 0.1821 0.2287 0.2340 -0.0102 0.0071  0.0201  162 ARG A NH1 
2051 N NH2 . ARG A 143 ? 0.1374 0.2651 0.2562 0.0173  0.0182  0.0071  162 ARG A NH2 
2065 N N   . ASN A 144 ? 0.1785 0.1798 0.1953 -0.0333 0.0136  0.0152  163 ASN A N   
2066 C CA  . ASN A 144 ? 0.1584 0.1925 0.2098 -0.0274 -0.0026 0.0091  163 ASN A CA  
2067 C C   . ASN A 144 ? 0.1814 0.1796 0.2050 -0.0444 0.0013  0.0100  163 ASN A C   
2068 O O   . ASN A 144 ? 0.1759 0.1851 0.2171 -0.0242 0.0018  0.0097  163 ASN A O   
2069 C CB  . ASN A 144 ? 0.1706 0.1907 0.2204 -0.0437 0.0057  -0.0047 163 ASN A CB  
2070 C CG  . ASN A 144 ? 0.2008 0.2121 0.2447 -0.0311 -0.0197 -0.0048 163 ASN A CG  
2071 O OD1 . ASN A 144 ? 0.2046 0.2123 0.2649 -0.0379 -0.0139 -0.0033 163 ASN A OD1 
2072 N ND2 . ASN A 144 ? 0.2511 0.2262 0.2501 -0.0310 -0.0375 -0.0164 163 ASN A ND2 
2079 N N   . TRP A 145 ? 0.1554 0.1536 0.1887 -0.0352 -0.0023 0.0137  164 TRP A N   
2080 C CA  . TRP A 145 ? 0.1545 0.1636 0.1810 -0.0205 0.0005  -0.0147 164 TRP A CA  
2081 C C   . TRP A 145 ? 0.1558 0.1573 0.1728 -0.0407 0.0095  0.0092  164 TRP A C   
2082 O O   . TRP A 145 ? 0.1645 0.1710 0.1782 -0.0341 -0.0007 0.0165  164 TRP A O   
2083 C CB  . TRP A 145 ? 0.1825 0.1727 0.1805 -0.0283 0.0124  -0.0096 164 TRP A CB  
2084 C CG  . TRP A 145 ? 0.1803 0.1733 0.1756 -0.0276 0.0240  -0.0122 164 TRP A CG  
2085 C CD1 . TRP A 145 ? 0.1958 0.1866 0.1729 -0.0345 0.0144  -0.0214 164 TRP A CD1 
2086 C CD2 . TRP A 145 ? 0.1570 0.1582 0.1715 -0.0190 0.0338  -0.0037 164 TRP A CD2 
2087 N NE1 . TRP A 145 ? 0.1916 0.1840 0.1694 -0.0205 0.0380  -0.0301 164 TRP A NE1 
2088 C CE2 . TRP A 145 ? 0.1856 0.1772 0.1726 -0.0173 0.0250  -0.0120 164 TRP A CE2 
2089 C CE3 . TRP A 145 ? 0.1898 0.1413 0.1848 -0.0260 0.0257  -0.0137 164 TRP A CE3 
2090 C CZ2 . TRP A 145 ? 0.1977 0.1695 0.1888 -0.0137 0.0246  -0.0142 164 TRP A CZ2 
2091 C CZ3 . TRP A 145 ? 0.1853 0.1400 0.1809 -0.0254 0.0136  -0.0082 164 TRP A CZ3 
2092 C CH2 . TRP A 145 ? 0.2022 0.1443 0.1942 -0.0420 0.0265  0.0057  164 TRP A CH2 
2103 N N   . TRP A 146 ? 0.1404 0.1593 0.1547 -0.0145 -0.0008 0.0038  165 TRP A N   
2104 C CA  . TRP A 146 ? 0.1511 0.1533 0.1498 -0.0096 0.0032  0.0055  165 TRP A CA  
2105 C C   . TRP A 146 ? 0.1266 0.1628 0.1683 -0.0192 0.0121  0.0094  165 TRP A C   
2106 O O   . TRP A 146 ? 0.1404 0.1529 0.1715 -0.0130 0.0207  0.0160  165 TRP A O   
2107 C CB  . TRP A 146 ? 0.1683 0.1410 0.1544 -0.0220 0.0230  0.0102  165 TRP A CB  
2108 C CG  . TRP A 146 ? 0.1631 0.1345 0.1554 -0.0080 0.0201  -0.0028 165 TRP A CG  
2109 C CD1 . TRP A 146 ? 0.1404 0.1199 0.1505 -0.0172 0.0177  0.0115  165 TRP A CD1 
2110 C CD2 . TRP A 146 ? 0.1574 0.1403 0.1535 -0.0052 0.0425  -0.0058 165 TRP A CD2 
2111 N NE1 . TRP A 146 ? 0.1425 0.1312 0.1527 -0.0032 0.0310  -0.0032 165 TRP A NE1 
2112 C CE2 . TRP A 146 ? 0.1438 0.1326 0.1413 0.0054  0.0219  -0.0100 165 TRP A CE2 
2113 C CE3 . TRP A 146 ? 0.1794 0.1535 0.1568 0.0042  0.0158  -0.0095 165 TRP A CE3 
2114 C CZ2 . TRP A 146 ? 0.1468 0.1506 0.1547 -0.0104 0.0360  -0.0181 165 TRP A CZ2 
2115 C CZ3 . TRP A 146 ? 0.1539 0.1451 0.1559 0.0157  0.0169  -0.0065 165 TRP A CZ3 
2116 C CH2 . TRP A 146 ? 0.1522 0.1421 0.1537 -0.0011 0.0299  -0.0156 165 TRP A CH2 
2127 N N   . THR A 147 ? 0.1336 0.1701 0.1822 -0.0086 0.0041  0.0154  166 THR A N   
2128 C CA  . THR A 147 ? 0.1575 0.1652 0.1905 -0.0115 -0.0004 0.0172  166 THR A CA  
2129 C C   . THR A 147 ? 0.1741 0.1622 0.1829 -0.0158 -0.0132 0.0167  166 THR A C   
2130 O O   . THR A 147 ? 0.1761 0.1696 0.1865 -0.0217 -0.0028 0.0230  166 THR A O   
2131 C CB  . THR A 147 ? 0.1558 0.1773 0.1942 -0.0117 0.0065  0.0073  166 THR A CB  
2132 O OG1 . THR A 147 ? 0.1276 0.2041 0.2051 -0.0136 0.0027  0.0121  166 THR A OG1 
2133 C CG2 . THR A 147 ? 0.1582 0.1915 0.1924 0.0168  0.0209  0.0073  166 THR A CG2 
2141 N N   . ASN A 148 ? 0.1740 0.1545 0.1743 -0.0295 -0.0114 0.0178  167 ASN A N   
2142 C CA  . ASN A 148 ? 0.1917 0.1886 0.1813 -0.0370 0.0002  0.0198  167 ASN A CA  
2143 C C   . ASN A 148 ? 0.1996 0.1872 0.1688 -0.0300 0.0064  0.0154  167 ASN A C   
2144 O O   . ASN A 148 ? 0.2145 0.2010 0.1686 -0.0247 0.0096  0.0147  167 ASN A O   
2145 C CB  . ASN A 148 ? 0.2259 0.2124 0.2093 -0.0469 -0.0159 0.0221  167 ASN A CB  
2146 C CG  . ASN A 148 ? 0.2613 0.2380 0.2438 -0.0464 -0.0181 0.0285  167 ASN A CG  
2147 O OD1 . ASN A 148 ? 0.2053 0.2630 0.2619 -0.0249 -0.0108 0.0353  167 ASN A OD1 
2148 N ND2 . ASN A 148 ? 0.3045 0.2602 0.2626 -0.0632 -0.0254 0.0352  167 ASN A ND2 
2155 N N   . VAL A 149 ? 0.2075 0.1825 0.1620 -0.0219 0.0025  0.0053  168 VAL A N   
2156 C CA  . VAL A 149 ? 0.2002 0.1717 0.1674 -0.0228 0.0019  0.0130  168 VAL A CA  
2157 C C   . VAL A 149 ? 0.1943 0.1641 0.1618 -0.0060 0.0145  0.0271  168 VAL A C   
2158 O O   . VAL A 149 ? 0.1998 0.1677 0.1720 0.0009  0.0188  0.0252  168 VAL A O   
2159 C CB  . VAL A 149 ? 0.1893 0.1626 0.1576 -0.0271 0.0106  0.0143  168 VAL A CB  
2160 C CG1 . VAL A 149 ? 0.2028 0.1647 0.1527 -0.0243 0.0098  0.0118  168 VAL A CG1 
2161 C CG2 . VAL A 149 ? 0.2113 0.1695 0.1594 -0.0361 0.0212  0.0036  168 VAL A CG2 
2171 N N   . ALA A 150 ? 0.1883 0.1556 0.1634 -0.0113 0.0020  0.0183  169 ALA A N   
2172 C CA  . ALA A 150 ? 0.1766 0.1634 0.1629 -0.0087 0.0032  0.0209  169 ALA A CA  
2173 C C   . ALA A 150 ? 0.1611 0.1657 0.1782 -0.0038 0.0017  0.0231  169 ALA A C   
2174 O O   . ALA A 150 ? 0.1505 0.1739 0.1809 -0.0054 0.0090  0.0117  169 ALA A O   
2175 C CB  . ALA A 150 ? 0.2117 0.1776 0.1579 0.0026  -0.0027 0.0109  169 ALA A CB  
2181 N N   . ALA A 151 ? 0.1761 0.1684 0.1978 -0.0059 -0.0106 0.0258  170 ALA A N   
2182 C CA  . ALA A 151 ? 0.1611 0.1645 0.2036 -0.0093 -0.0249 0.0331  170 ALA A CA  
2183 C C   . ALA A 151 ? 0.1478 0.1665 0.1968 -0.0206 -0.0292 0.0327  170 ALA A C   
2184 O O   . ALA A 151 ? 0.1602 0.1708 0.2203 -0.0092 -0.0187 0.0388  170 ALA A O   
2185 C CB  . ALA A 151 ? 0.1554 0.1849 0.2020 -0.0086 -0.0112 0.0351  170 ALA A CB  
2191 N N   . LYS A 152 ? 0.1624 0.1917 0.1889 -0.0165 -0.0154 0.0264  171 LYS A N   
2192 C CA  . LYS A 152 ? 0.1789 0.1879 0.1828 -0.0244 -0.0208 0.0164  171 LYS A CA  
2193 C C   . LYS A 152 ? 0.1663 0.1827 0.1643 -0.0220 -0.0090 0.0070  171 LYS A C   
2194 O O   . LYS A 152 ? 0.2011 0.1865 0.1608 -0.0243 -0.0093 0.0239  171 LYS A O   
2195 C CB  . LYS A 152 ? 0.2034 0.2080 0.2200 -0.0145 -0.0086 0.0066  171 LYS A CB  
2196 C CG  . LYS A 152 ? 0.2899 0.2245 0.2598 -0.0107 -0.0105 -0.0171 171 LYS A CG  
2197 C CD  . LYS A 152 ? 0.3756 0.2619 0.3123 0.0106  -0.0117 -0.0247 171 LYS A CD  
2198 C CE  . LYS A 152 ? 0.4494 0.3063 0.3562 0.0293  -0.0121 -0.0227 171 LYS A CE  
2199 N NZ  . LYS A 152 ? 0.5032 0.3278 0.3810 0.0314  -0.0246 -0.0155 171 LYS A NZ  
2213 N N   . ALA A 153 ? 0.1518 0.1772 0.1571 -0.0059 -0.0116 -0.0028 172 ALA A N   
2214 C CA  . ALA A 153 ? 0.1550 0.1830 0.1641 -0.0057 0.0030  0.0126  172 ALA A CA  
2215 C C   . ALA A 153 ? 0.1439 0.1868 0.1643 0.0020  -0.0003 -0.0063 172 ALA A C   
2216 O O   . ALA A 153 ? 0.1584 0.1863 0.1512 0.0084  0.0163  -0.0046 172 ALA A O   
2217 C CB  . ALA A 153 ? 0.1436 0.1867 0.1753 0.0018  -0.0080 0.0115  172 ALA A CB  
2223 N N   . VAL A 154 ? 0.1331 0.1969 0.1786 -0.0020 0.0044  -0.0137 173 VAL A N   
2224 C CA  . VAL A 154 ? 0.1470 0.2138 0.1954 0.0200  -0.0049 -0.0075 173 VAL A CA  
2225 C C   . VAL A 154 ? 0.1724 0.1983 0.2086 -0.0015 -0.0092 0.0047  173 VAL A C   
2226 O O   . VAL A 154 ? 0.1744 0.1989 0.2337 -0.0264 -0.0059 -0.0098 173 VAL A O   
2227 C CB  . VAL A 154 ? 0.1923 0.2731 0.1966 -0.0060 -0.0057 -0.0189 173 VAL A CB  
2228 C CG1 . VAL A 154 ? 0.1585 0.2670 0.1847 0.0015  -0.0024 -0.0269 173 VAL A CG1 
2229 C CG2 . VAL A 154 ? 0.2502 0.2958 0.1948 -0.0117 0.0102  -0.0118 173 VAL A CG2 
2239 N N   . VAL A 155 ? 0.1591 0.1918 0.2263 0.0014  -0.0102 0.0137  174 VAL A N   
2240 C CA  . VAL A 155 ? 0.1723 0.1986 0.2459 0.0081  -0.0064 0.0219  174 VAL A CA  
2241 C C   . VAL A 155 ? 0.1905 0.1961 0.2374 0.0035  -0.0320 0.0070  174 VAL A C   
2242 O O   . VAL A 155 ? 0.2428 0.2060 0.2376 -0.0026 -0.0434 0.0078  174 VAL A O   
2243 C CB  . VAL A 155 ? 0.1747 0.2180 0.2437 0.0017  -0.0126 0.0216  174 VAL A CB  
2244 C CG1 . VAL A 155 ? 0.1721 0.2407 0.2410 0.0225  -0.0227 0.0204  174 VAL A CG1 
2245 C CG2 . VAL A 155 ? 0.1801 0.2060 0.2541 -0.0038 -0.0151 0.0187  174 VAL A CG2 
2255 N N   . ASP A 156 ? 0.1916 0.2100 0.2419 0.0037  -0.0045 -0.0049 175 ASP A N   
2256 C CA  . ASP A 156 ? 0.2144 0.2374 0.2452 -0.0144 -0.0134 0.0062  175 ASP A CA  
2257 C C   . ASP A 156 ? 0.2144 0.2291 0.2074 -0.0025 -0.0038 0.0163  175 ASP A C   
2258 O O   . ASP A 156 ? 0.2485 0.2684 0.2048 -0.0129 0.0013  0.0264  175 ASP A O   
2259 C CB  . ASP A 156 ? 0.2374 0.2710 0.3057 -0.0420 -0.0078 -0.0043 175 ASP A CB  
2260 C CG  . ASP A 156 ? 0.3177 0.3241 0.3763 -0.0499 -0.0141 -0.0086 175 ASP A CG  
2261 O OD1 . ASP A 156 ? 0.3556 0.3617 0.4118 -0.0605 -0.0069 -0.0166 175 ASP A OD1 
2262 O OD2 . ASP A 156 ? 0.3681 0.3463 0.3964 -0.0652 -0.0190 -0.0002 175 ASP A OD2 
2267 N N   . GLY A 157 ? 0.2048 0.2040 0.1686 -0.0341 -0.0184 0.0013  176 GLY A N   
2268 C CA  . GLY A 157 ? 0.1972 0.1765 0.1778 -0.0243 -0.0109 -0.0090 176 GLY A CA  
2269 C C   . GLY A 157 ? 0.1797 0.1803 0.1780 -0.0067 -0.0056 -0.0072 176 GLY A C   
2270 O O   . GLY A 157 ? 0.1624 0.2112 0.2035 0.0038  0.0019  -0.0141 176 GLY A O   
2274 N N   . THR A 158 ? 0.1635 0.1857 0.1540 -0.0150 -0.0114 0.0014  177 THR A N   
2275 C CA  . THR A 158 ? 0.1715 0.1853 0.1508 -0.0151 0.0114  0.0079  177 THR A CA  
2276 C C   . THR A 158 ? 0.1767 0.1644 0.1484 -0.0239 0.0161  0.0099  177 THR A C   
2277 O O   . THR A 158 ? 0.2147 0.1592 0.1442 -0.0193 0.0155  0.0052  177 THR A O   
2278 C CB  . THR A 158 ? 0.1846 0.2035 0.1491 -0.0234 0.0135  0.0151  177 THR A CB  
2279 O OG1 . THR A 158 ? 0.2176 0.2303 0.1662 -0.0144 0.0255  0.0057  177 THR A OG1 
2280 C CG2 . THR A 158 ? 0.1829 0.2115 0.1498 -0.0302 0.0307  0.0104  177 THR A CG2 
2288 N N   . CYS A 159 ? 0.1747 0.1629 0.1499 -0.0194 0.0183  0.0056  178 CYS A N   
2289 C CA  . CYS A 159 ? 0.1284 0.1645 0.1425 0.0000  0.0312  0.0011  178 CYS A CA  
2290 C C   . CYS A 159 ? 0.1260 0.1640 0.1593 -0.0007 -0.0036 0.0083  178 CYS A C   
2291 O O   . CYS A 159 ? 0.1554 0.1736 0.1707 -0.0062 -0.0125 -0.0101 178 CYS A O   
2292 C CB  . CYS A 159 ? 0.1490 0.1638 0.1585 0.0179  0.0130  -0.0088 178 CYS A CB  
2293 S SG  . CYS A 159 ? 0.1477 0.1615 0.1622 -0.0010 0.0149  -0.0003 178 CYS A SG  
2299 N N   . ASP A 160 ? 0.1155 0.1591 0.1634 -0.0073 0.0012  0.0041  179 ASP A N   
2300 C CA  . ASP A 160 ? 0.1052 0.1497 0.1531 -0.0121 0.0016  -0.0011 179 ASP A CA  
2301 C C   . ASP A 160 ? 0.1230 0.1452 0.1463 -0.0006 0.0007  0.0018  179 ASP A C   
2302 O O   . ASP A 160 ? 0.1458 0.1560 0.1427 0.0249  0.0172  0.0116  179 ASP A O   
2303 C CB  . ASP A 160 ? 0.1180 0.1629 0.1550 0.0103  -0.0061 0.0123  179 ASP A CB  
2304 C CG  . ASP A 160 ? 0.1203 0.1784 0.1524 -0.0062 -0.0121 0.0230  179 ASP A CG  
2305 O OD1 . ASP A 160 ? 0.1473 0.1907 0.1933 0.0090  -0.0152 0.0372  179 ASP A OD1 
2306 O OD2 . ASP A 160 ? 0.1206 0.1934 0.1532 -0.0083 -0.0141 0.0244  179 ASP A OD2 
2311 N N   . GLY A 161 ? 0.1421 0.1426 0.1342 0.0111  0.0110  0.0065  180 GLY A N   
2312 C CA  . GLY A 161 ? 0.1218 0.1472 0.1374 0.0146  0.0181  0.0026  180 GLY A CA  
2313 C C   . GLY A 161 ? 0.1094 0.1409 0.1420 0.0134  0.0036  -0.0004 180 GLY A C   
2314 O O   . GLY A 161 ? 0.1269 0.1442 0.1430 0.0087  0.0022  0.0025  180 GLY A O   
2318 N N   . VAL A 162 ? 0.1226 0.1432 0.1370 0.0134  0.0078  0.0153  181 VAL A N   
2319 C CA  . VAL A 162 ? 0.1311 0.1463 0.1441 0.0066  0.0187  0.0147  181 VAL A CA  
2320 C C   . VAL A 162 ? 0.1443 0.1366 0.1356 -0.0023 0.0058  -0.0025 181 VAL A C   
2321 O O   . VAL A 162 ? 0.1345 0.1554 0.1497 0.0179  0.0039  0.0091  181 VAL A O   
2322 C CB  . VAL A 162 ? 0.1324 0.1450 0.1469 0.0009  0.0120  0.0069  181 VAL A CB  
2323 C CG1 . VAL A 162 ? 0.1511 0.1560 0.1602 -0.0036 0.0076  0.0072  181 VAL A CG1 
2324 C CG2 . VAL A 162 ? 0.1308 0.1619 0.1622 0.0021  0.0180  -0.0070 181 VAL A CG2 
2334 N N   . PHE A 163 ? 0.1151 0.1288 0.1248 -0.0083 0.0099  -0.0124 182 PHE A N   
2335 C CA  . PHE A 163 ? 0.1049 0.1356 0.1373 0.0065  0.0169  0.0050  182 PHE A CA  
2336 C C   . PHE A 163 ? 0.1291 0.1405 0.1380 -0.0065 0.0135  -0.0017 182 PHE A C   
2337 O O   . PHE A 163 ? 0.1415 0.1528 0.1516 -0.0170 0.0272  -0.0086 182 PHE A O   
2338 C CB  . PHE A 163 ? 0.0943 0.1449 0.1434 0.0061  0.0072  0.0145  182 PHE A CB  
2339 C CG  . PHE A 163 ? 0.1202 0.1488 0.1554 0.0084  0.0041  0.0091  182 PHE A CG  
2340 C CD1 . PHE A 163 ? 0.1438 0.1519 0.1605 -0.0049 0.0022  0.0176  182 PHE A CD1 
2341 C CD2 . PHE A 163 ? 0.1299 0.1476 0.1643 -0.0092 -0.0094 0.0088  182 PHE A CD2 
2342 C CE1 . PHE A 163 ? 0.1530 0.1544 0.1615 -0.0167 -0.0126 0.0258  182 PHE A CE1 
2343 C CE2 . PHE A 163 ? 0.1733 0.1540 0.1678 -0.0322 0.0161  -0.0017 182 PHE A CE2 
2344 C CZ  . PHE A 163 ? 0.1508 0.1758 0.1609 -0.0274 -0.0072 0.0206  182 PHE A CZ  
2354 N N   . MET A 164 ? 0.1380 0.1299 0.1329 -0.0095 0.0360  -0.0115 183 MET A N   
2355 C CA  . MET A 164 ? 0.1335 0.1486 0.1463 -0.0266 0.0267  0.0017  183 MET A CA  
2356 C C   . MET A 164 ? 0.1073 0.1285 0.1532 -0.0083 0.0199  -0.0053 183 MET A C   
2357 O O   . MET A 164 ? 0.1436 0.1355 0.1564 0.0068  0.0089  -0.0092 183 MET A O   
2358 C CB  . MET A 164 ? 0.1160 0.1424 0.1431 -0.0183 0.0174  0.0062  183 MET A CB  
2359 C CG  . MET A 164 ? 0.1488 0.1583 0.1733 -0.0325 -0.0106 0.0330  183 MET A CG  
2360 S SD  . MET A 164 ? 0.1384 0.1680 0.2037 -0.0196 -0.0100 0.0377  183 MET A SD  
2361 C CE  . MET A 164 ? 0.1654 0.1466 0.1883 -0.0227 0.0096  0.0290  183 MET A CE  
2371 N N   . ASP A 165 ? 0.1272 0.1351 0.1661 0.0067  0.0132  0.0042  184 ASP A N   
2372 C CA  . ASP A 165 ? 0.1263 0.1503 0.1664 0.0108  0.0117  0.0098  184 ASP A CA  
2373 C C   . ASP A 165 ? 0.1386 0.1613 0.1770 0.0009  0.0251  0.0115  184 ASP A C   
2374 O O   . ASP A 165 ? 0.1524 0.1687 0.1927 0.0071  0.0185  0.0287  184 ASP A O   
2375 C CB  . ASP A 165 ? 0.1280 0.1532 0.1779 -0.0020 0.0250  -0.0102 184 ASP A CB  
2376 C CG  . ASP A 165 ? 0.1361 0.1575 0.1732 0.0211  0.0338  0.0022  184 ASP A CG  
2377 O OD1 . ASP A 165 ? 0.1677 0.1740 0.1846 0.0105  0.0236  -0.0075 184 ASP A OD1 
2378 O OD2 . ASP A 165 ? 0.1478 0.1517 0.1907 0.0184  0.0386  0.0188  184 ASP A OD2 
2383 N N   . ALA A 166 ? 0.1481 0.1519 0.1744 0.0010  0.0174  -0.0026 185 ALA A N   
2384 C CA  . ALA A 166 ? 0.1599 0.1570 0.1677 0.0113  0.0110  0.0091  185 ALA A CA  
2385 C C   . ALA A 166 ? 0.1536 0.1445 0.1627 0.0130  0.0182  0.0142  185 ALA A C   
2386 O O   . ALA A 166 ? 0.1748 0.1526 0.1596 0.0153  0.0173  0.0063  185 ALA A O   
2387 C CB  . ALA A 166 ? 0.1870 0.1612 0.1605 0.0214  0.0238  0.0137  185 ALA A CB  
2393 N N   . PHE A 167 ? 0.1544 0.1461 0.1566 0.0156  0.0422  0.0057  186 PHE A N   
2394 C CA  . PHE A 167 ? 0.1496 0.1537 0.1485 0.0036  0.0308  0.0005  186 PHE A CA  
2395 C C   . PHE A 167 ? 0.1658 0.1698 0.1591 0.0006  0.0256  0.0048  186 PHE A C   
2396 O O   . PHE A 167 ? 0.1760 0.1804 0.1626 0.0008  0.0256  0.0009  186 PHE A O   
2397 C CB  . PHE A 167 ? 0.1661 0.1632 0.1509 0.0028  0.0405  -0.0056 186 PHE A CB  
2398 C CG  . PHE A 167 ? 0.1413 0.1663 0.1542 -0.0138 0.0451  -0.0064 186 PHE A CG  
2399 C CD1 . PHE A 167 ? 0.1493 0.1575 0.1610 0.0070  0.0191  0.0039  186 PHE A CD1 
2400 C CD2 . PHE A 167 ? 0.1617 0.1833 0.1629 -0.0098 0.0336  -0.0120 186 PHE A CD2 
2401 C CE1 . PHE A 167 ? 0.1244 0.1602 0.1541 0.0010  0.0291  -0.0009 186 PHE A CE1 
2402 C CE2 . PHE A 167 ? 0.1490 0.1787 0.1648 -0.0194 0.0168  0.0013  186 PHE A CE2 
2403 C CZ  . PHE A 167 ? 0.1415 0.1717 0.1570 -0.0185 0.0221  0.0042  186 PHE A CZ  
2413 N N   . PRO A 168 ? 0.1739 0.1735 0.1536 0.0055  0.0149  0.0207  187 PRO A N   
2414 C CA  . PRO A 168 ? 0.1798 0.1998 0.1637 -0.0041 0.0005  0.0295  187 PRO A CA  
2415 C C   . PRO A 168 ? 0.2041 0.1936 0.1570 -0.0028 0.0017  0.0326  187 PRO A C   
2416 O O   . PRO A 168 ? 0.2499 0.1943 0.1689 0.0041  -0.0015 0.0471  187 PRO A O   
2417 C CB  . PRO A 168 ? 0.1876 0.2091 0.1864 -0.0011 -0.0144 0.0229  187 PRO A CB  
2418 C CG  . PRO A 168 ? 0.2176 0.2013 0.1889 -0.0069 -0.0068 0.0208  187 PRO A CG  
2419 C CD  . PRO A 168 ? 0.1980 0.1831 0.1837 -0.0134 -0.0079 0.0267  187 PRO A CD  
2427 N N   A GLN A 169 ? 0.1928 0.1871 0.1573 -0.0011 0.0189  0.0294  188 GLN A N   
2428 N N   B GLN A 169 ? 0.2107 0.1993 0.1609 0.0077  0.0022  0.0307  188 GLN A N   
2429 C CA  A GLN A 169 ? 0.1646 0.1783 0.1578 -0.0017 0.0233  0.0216  188 GLN A CA  
2430 C CA  B GLN A 169 ? 0.2063 0.2036 0.1655 0.0215  -0.0063 0.0238  188 GLN A CA  
2431 C C   A GLN A 169 ? 0.1912 0.1680 0.1588 0.0156  0.0160  0.0309  188 GLN A C   
2432 C C   B GLN A 169 ? 0.2039 0.1804 0.1662 0.0178  -0.0023 0.0310  188 GLN A C   
2433 O O   A GLN A 169 ? 0.2054 0.1798 0.1533 0.0283  0.0195  0.0439  188 GLN A O   
2434 O O   B GLN A 169 ? 0.2098 0.1809 0.1699 0.0109  -0.0045 0.0388  188 GLN A O   
2435 C CB  A GLN A 169 ? 0.1523 0.1761 0.1686 0.0032  0.0320  0.0179  188 GLN A CB  
2436 C CB  B GLN A 169 ? 0.2197 0.2264 0.1746 0.0460  -0.0173 0.0181  188 GLN A CB  
2437 C CG  A GLN A 169 ? 0.1542 0.1796 0.1765 -0.0077 0.0202  0.0120  188 GLN A CG  
2438 C CG  B GLN A 169 ? 0.2345 0.2492 0.1864 0.0579  -0.0428 0.0035  188 GLN A CG  
2439 C CD  A GLN A 169 ? 0.1682 0.1890 0.1868 -0.0138 0.0339  0.0074  188 GLN A CD  
2440 C CD  B GLN A 169 ? 0.2714 0.2755 0.2075 0.0719  -0.0436 -0.0251 188 GLN A CD  
2441 O OE1 A GLN A 169 ? 0.1762 0.2027 0.1965 -0.0157 0.0327  0.0059  188 GLN A OE1 
2442 O OE1 B GLN A 169 ? 0.2512 0.2740 0.1989 0.1118  -0.0850 -0.0444 188 GLN A OE1 
2443 N NE2 A GLN A 169 ? 0.2238 0.1768 0.2009 -0.0036 0.0494  -0.0091 188 GLN A NE2 
2444 N NE2 B GLN A 169 ? 0.3030 0.2919 0.2202 0.0557  -0.0198 -0.0244 188 GLN A NE2 
2461 N N   . ILE A 170 ? 0.1805 0.1663 0.1601 0.0072  0.0112  0.0228  189 ILE A N   
2462 C CA  . ILE A 170 ? 0.1837 0.1555 0.1638 0.0136  0.0233  0.0181  189 ILE A CA  
2463 C C   . ILE A 170 ? 0.1810 0.1601 0.1770 0.0225  0.0285  0.0217  189 ILE A C   
2464 O O   . ILE A 170 ? 0.1873 0.1655 0.1833 0.0210  0.0375  0.0403  189 ILE A O   
2465 C CB  . ILE A 170 ? 0.1689 0.1529 0.1728 0.0044  0.0127  0.0053  189 ILE A CB  
2466 C CG1 . ILE A 170 ? 0.1769 0.1520 0.1784 -0.0075 0.0245  0.0169  189 ILE A CG1 
2467 C CG2 . ILE A 170 ? 0.1722 0.1726 0.1744 0.0103  0.0153  0.0007  189 ILE A CG2 
2468 C CD1 . ILE A 170 ? 0.1918 0.1607 0.1754 0.0082  0.0243  0.0207  189 ILE A CD1 
2480 N N   . ALA A 171 ? 0.2029 0.1795 0.1778 0.0153  0.0396  0.0008  190 ALA A N   
2481 C CA  . ALA A 171 ? 0.2272 0.2038 0.1851 0.0175  0.0446  0.0042  190 ALA A CA  
2482 C C   . ALA A 171 ? 0.2321 0.2165 0.1820 -0.0019 0.0425  0.0103  190 ALA A C   
2483 O O   . ALA A 171 ? 0.2743 0.2294 0.1911 -0.0088 0.0616  0.0086  190 ALA A O   
2484 C CB  . ALA A 171 ? 0.2542 0.2048 0.1979 0.0238  0.0408  -0.0068 190 ALA A CB  
2490 N N   . SER A 172 ? 0.2301 0.2344 0.1733 -0.0106 0.0206  0.0098  191 SER A N   
2491 C CA  . SER A 172 ? 0.2447 0.2438 0.1696 -0.0001 -0.0060 0.0114  191 SER A CA  
2492 C C   . SER A 172 ? 0.2755 0.2514 0.1686 -0.0066 0.0088  0.0049  191 SER A C   
2493 O O   . SER A 172 ? 0.2341 0.2282 0.1580 0.0061  0.0061  -0.0045 191 SER A O   
2494 C CB  . SER A 172 ? 0.2599 0.2685 0.1746 0.0044  -0.0261 0.0164  191 SER A CB  
2495 O OG  . SER A 172 ? 0.2888 0.3025 0.2003 0.0246  -0.0445 0.0139  191 SER A OG  
2501 N N   . GLN A 173 ? 0.3343 0.2676 0.1733 0.0017  0.0042  0.0011  192 GLN A N   
2502 C CA  . GLN A 173 ? 0.3551 0.2949 0.1745 -0.0086 0.0251  -0.0094 192 GLN A CA  
2503 C C   . GLN A 173 ? 0.3510 0.2913 0.1756 -0.0087 0.0101  0.0122  192 GLN A C   
2504 O O   . GLN A 173 ? 0.3563 0.3012 0.1789 -0.0343 0.0221  0.0056  192 GLN A O   
2505 C CB  . GLN A 173 ? 0.3914 0.3135 0.1760 -0.0113 0.0323  -0.0129 192 GLN A CB  
2506 C CG  . GLN A 173 ? 0.4387 0.3318 0.1847 -0.0031 0.0299  -0.0094 192 GLN A CG  
2507 C CD  . GLN A 173 ? 0.4455 0.3384 0.1973 0.0039  0.0346  -0.0091 192 GLN A CD  
2508 O OE1 . GLN A 173 ? 0.4526 0.3489 0.2095 0.0044  0.0333  -0.0045 192 GLN A OE1 
2509 N NE2 . GLN A 173 ? 0.4632 0.3454 0.2032 -0.0003 0.0376  -0.0196 192 GLN A NE2 
2518 N N   . ALA A 174 ? 0.3430 0.2905 0.1789 -0.0001 -0.0301 0.0272  193 ALA A N   
2519 C CA  . ALA A 174 ? 0.3192 0.2620 0.1858 -0.0166 -0.0242 0.0531  193 ALA A CA  
2520 C C   . ALA A 174 ? 0.2890 0.2345 0.1829 -0.0069 -0.0066 0.0576  193 ALA A C   
2521 O O   . ALA A 174 ? 0.2580 0.2483 0.1953 -0.0074 0.0144  0.0587  193 ALA A O   
2522 C CB  . ALA A 174 ? 0.3277 0.2720 0.1943 -0.0144 -0.0349 0.0589  193 ALA A CB  
2528 N N   . ASN A 175 ? 0.2534 0.1953 0.1616 0.0091  -0.0105 0.0481  194 ASN A N   
2529 C CA  . ASN A 175 ? 0.2348 0.1842 0.1563 0.0107  0.0240  0.0448  194 ASN A CA  
2530 C C   . ASN A 175 ? 0.2356 0.1811 0.1624 0.0057  0.0246  0.0377  194 ASN A C   
2531 O O   . ASN A 175 ? 0.2719 0.1744 0.1582 -0.0010 0.0217  0.0369  194 ASN A O   
2532 C CB  . ASN A 175 ? 0.2258 0.1759 0.1508 0.0175  0.0159  0.0415  194 ASN A CB  
2533 C CG  . ASN A 175 ? 0.2356 0.1647 0.1572 0.0164  0.0222  0.0145  194 ASN A CG  
2534 O OD1 . ASN A 175 ? 0.2333 0.1692 0.1563 0.0279  0.0393  0.0001  194 ASN A OD1 
2535 N ND2 . ASN A 175 ? 0.2510 0.1654 0.1592 0.0257  0.0271  0.0196  194 ASN A ND2 
2542 N N   . ARG A 176 ? 0.2491 0.1828 0.1688 0.0105  0.0210  0.0285  195 ARG A N   
2543 C CA  . ARG A 176 ? 0.2649 0.2058 0.1603 0.0071  0.0158  0.0362  195 ARG A CA  
2544 C C   . ARG A 176 ? 0.2803 0.2083 0.1689 -0.0148 0.0162  0.0437  195 ARG A C   
2545 O O   . ARG A 176 ? 0.3096 0.2310 0.1683 -0.0353 0.0162  0.0276  195 ARG A O   
2546 C CB  . ARG A 176 ? 0.2751 0.2374 0.1647 0.0135  0.0143  0.0296  195 ARG A CB  
2547 C CG  . ARG A 176 ? 0.2681 0.2607 0.1743 0.0318  0.0298  0.0016  195 ARG A CG  
2548 C CD  . ARG A 176 ? 0.3065 0.2782 0.1881 0.0454  0.0264  0.0011  195 ARG A CD  
2549 N NE  . ARG A 176 ? 0.3192 0.2963 0.2035 0.0436  0.0341  0.0001  195 ARG A NE  
2550 C CZ  . ARG A 176 ? 0.3229 0.2958 0.1939 0.0431  0.0445  0.0048  195 ARG A CZ  
2551 N NH1 . ARG A 176 ? 0.3095 0.2837 0.1896 0.0565  0.0553  0.0075  195 ARG A NH1 
2552 N NH2 . ARG A 176 ? 0.3345 0.2838 0.1805 0.0421  0.0491  -0.0047 195 ARG A NH2 
2566 N N   . LYS A 177 ? 0.2689 0.2088 0.1945 -0.0116 0.0019  0.0500  196 LYS A N   
2567 C CA  . LYS A 177 ? 0.2823 0.2025 0.2296 0.0078  -0.0196 0.0618  196 LYS A CA  
2568 C C   . LYS A 177 ? 0.2237 0.1894 0.2169 0.0083  -0.0086 0.0537  196 LYS A C   
2569 O O   . LYS A 177 ? 0.2236 0.1843 0.2110 0.0001  -0.0256 0.0527  196 LYS A O   
2570 C CB  . LYS A 177 ? 0.3660 0.2373 0.2831 0.0534  -0.0496 0.0528  196 LYS A CB  
2571 C CG  . LYS A 177 ? 0.4309 0.2895 0.3385 0.0538  -0.0680 0.0355  196 LYS A CG  
2572 C CD  . LYS A 177 ? 0.4807 0.3424 0.3821 0.0428  -0.0614 0.0319  196 LYS A CD  
2573 C CE  . LYS A 177 ? 0.4980 0.3651 0.4056 0.0268  -0.0664 0.0361  196 LYS A CE  
2574 N NZ  . LYS A 177 ? 0.4970 0.3608 0.4090 0.0171  -0.0907 0.0415  196 LYS A NZ  
2588 N N   . LEU A 178 ? 0.1891 0.2010 0.2065 0.0008  -0.0023 0.0425  197 LEU A N   
2589 C CA  . LEU A 178 ? 0.1801 0.2221 0.2011 0.0036  0.0322  0.0480  197 LEU A CA  
2590 C C   . LEU A 178 ? 0.1850 0.1979 0.1959 0.0025  0.0323  0.0374  197 LEU A C   
2591 O O   . LEU A 178 ? 0.1891 0.1825 0.2096 0.0015  0.0568  0.0221  197 LEU A O   
2592 C CB  . LEU A 178 ? 0.1985 0.2668 0.2310 -0.0233 0.0440  0.0490  197 LEU A CB  
2593 C CG  . LEU A 178 ? 0.2385 0.3099 0.2462 -0.0003 0.0546  0.0491  197 LEU A CG  
2594 C CD1 . LEU A 178 ? 0.2738 0.3249 0.2525 0.0004  0.0619  0.0544  197 LEU A CD1 
2595 C CD2 . LEU A 178 ? 0.2564 0.3288 0.2628 0.0222  0.0498  0.0329  197 LEU A CD2 
2607 N N   . TRP A 179 ? 0.1822 0.1859 0.1748 0.0315  0.0194  0.0339  198 TRP A N   
2608 C CA  . TRP A 179 ? 0.1938 0.1768 0.1745 0.0200  0.0250  0.0315  198 TRP A CA  
2609 C C   . TRP A 179 ? 0.1804 0.1707 0.1844 0.0032  0.0247  0.0554  198 TRP A C   
2610 O O   . TRP A 179 ? 0.2057 0.1915 0.2041 0.0083  0.0249  0.0553  198 TRP A O   
2611 C CB  . TRP A 179 ? 0.1989 0.1758 0.1648 0.0210  0.0215  0.0347  198 TRP A CB  
2612 C CG  . TRP A 179 ? 0.2008 0.1616 0.1598 0.0176  0.0371  0.0251  198 TRP A CG  
2613 C CD1 . TRP A 179 ? 0.2179 0.1484 0.1605 0.0224  0.0300  0.0123  198 TRP A CD1 
2614 C CD2 . TRP A 179 ? 0.2266 0.1434 0.1453 0.0207  0.0512  0.0240  198 TRP A CD2 
2615 N NE1 . TRP A 179 ? 0.2290 0.1387 0.1575 0.0197  0.0411  0.0070  198 TRP A NE1 
2616 C CE2 . TRP A 179 ? 0.2325 0.1465 0.1502 0.0317  0.0465  0.0087  198 TRP A CE2 
2617 C CE3 . TRP A 179 ? 0.2190 0.1475 0.1450 0.0217  0.0554  0.0244  198 TRP A CE3 
2618 C CZ2 . TRP A 179 ? 0.2245 0.1464 0.1479 0.0301  0.0581  0.0059  198 TRP A CZ2 
2619 C CZ3 . TRP A 179 ? 0.2220 0.1475 0.1464 0.0259  0.0403  0.0154  198 TRP A CZ3 
2620 C CH2 . TRP A 179 ? 0.2268 0.1581 0.1430 0.0188  0.0476  0.0120  198 TRP A CH2 
2631 N N   . GLY A 180 ? 0.1804 0.1739 0.1886 0.0319  0.0462  0.0512  199 GLY A N   
2632 C CA  . GLY A 180 ? 0.1891 0.1913 0.2081 0.0338  0.0598  0.0508  199 GLY A CA  
2633 C C   . GLY A 180 ? 0.2304 0.2023 0.2249 0.0438  0.0793  0.0548  199 GLY A C   
2634 O O   . GLY A 180 ? 0.2298 0.1944 0.2209 0.0534  0.0627  0.0617  199 GLY A O   
2638 N N   . ASP A 181 ? 0.2538 0.2307 0.2351 0.0522  0.0954  0.0595  200 ASP A N   
2639 C CA  . ASP A 181 ? 0.2787 0.2423 0.2379 0.0571  0.1021  0.0714  200 ASP A CA  
2640 C C   . ASP A 181 ? 0.2715 0.2391 0.2585 0.0510  0.0989  0.0729  200 ASP A C   
2641 O O   . ASP A 181 ? 0.2543 0.2336 0.2577 0.0791  0.1098  0.0526  200 ASP A O   
2642 C CB  . ASP A 181 ? 0.3227 0.2675 0.2329 0.0843  0.1047  0.0704  200 ASP A CB  
2643 C CG  . ASP A 181 ? 0.3747 0.3009 0.2350 0.0729  0.0983  0.0693  200 ASP A CG  
2644 O OD1 . ASP A 181 ? 0.3900 0.3122 0.2272 0.0712  0.0876  0.0743  200 ASP A OD1 
2645 O OD2 . ASP A 181 ? 0.4303 0.3389 0.2525 0.0621  0.0822  0.0666  200 ASP A OD2 
2650 N N   . GLU A 182 ? 0.2687 0.2595 0.2927 0.0546  0.0831  0.0779  201 GLU A N   
2651 C CA  . GLU A 182 ? 0.2928 0.2758 0.3187 0.0197  0.0790  0.0758  201 GLU A CA  
2652 C C   . GLU A 182 ? 0.2477 0.2394 0.2923 0.0290  0.0840  0.0697  201 GLU A C   
2653 O O   . GLU A 182 ? 0.2324 0.2287 0.2930 0.0414  0.0987  0.0652  201 GLU A O   
2654 C CB  . GLU A 182 ? 0.3659 0.3233 0.3763 -0.0209 0.0636  0.0743  201 GLU A CB  
2655 C CG  . GLU A 182 ? 0.4516 0.3734 0.4381 -0.0625 0.0633  0.0760  201 GLU A CG  
2656 C CD  . GLU A 182 ? 0.5155 0.4200 0.4901 -0.0844 0.0476  0.0722  201 GLU A CD  
2657 O OE1 . GLU A 182 ? 0.5348 0.4301 0.5090 -0.0985 0.0555  0.0752  201 GLU A OE1 
2658 O OE2 . GLU A 182 ? 0.5454 0.4434 0.5128 -0.0904 0.0391  0.0553  201 GLU A OE2 
2665 N N   . LYS A 183 ? 0.2053 0.2253 0.2693 0.0119  0.0847  0.0487  202 LYS A N   
2666 C CA  . LYS A 183 ? 0.1945 0.2031 0.2489 0.0176  0.0538  0.0273  202 LYS A CA  
2667 C C   . LYS A 183 ? 0.1994 0.1949 0.2242 0.0315  0.0609  0.0135  202 LYS A C   
2668 O O   . LYS A 183 ? 0.1918 0.1869 0.2212 0.0241  0.0597  0.0063  202 LYS A O   
2669 C CB  . LYS A 183 ? 0.1916 0.2149 0.2694 0.0153  0.0233  0.0021  202 LYS A CB  
2670 C CG  . LYS A 183 ? 0.2107 0.2287 0.2742 0.0426  -0.0108 -0.0028 202 LYS A CG  
2671 C CD  . LYS A 183 ? 0.2432 0.2634 0.2870 0.0349  -0.0143 0.0007  202 LYS A CD  
2672 C CE  . LYS A 183 ? 0.2653 0.2971 0.2705 0.0007  0.0001  0.0111  202 LYS A CE  
2673 N NZ  . LYS A 183 ? 0.2443 0.2969 0.2488 -0.0421 0.0185  0.0088  202 LYS A NZ  
2687 N N   . PHE A 184 ? 0.2043 0.1865 0.1894 0.0333  0.0653  0.0247  203 PHE A N   
2688 C CA  . PHE A 184 ? 0.2204 0.1954 0.1719 0.0468  0.0544  0.0303  203 PHE A CA  
2689 C C   . PHE A 184 ? 0.2216 0.1945 0.1842 0.0495  0.0696  0.0286  203 PHE A C   
2690 O O   . PHE A 184 ? 0.2053 0.1879 0.1844 0.0453  0.0462  0.0141  203 PHE A O   
2691 C CB  . PHE A 184 ? 0.2555 0.2123 0.1663 0.0468  0.0403  0.0166  203 PHE A CB  
2692 C CG  . PHE A 184 ? 0.2394 0.2065 0.1514 0.0678  0.0495  0.0117  203 PHE A CG  
2693 C CD1 . PHE A 184 ? 0.2501 0.2120 0.1535 0.0571  0.0551  0.0203  203 PHE A CD1 
2694 C CD2 . PHE A 184 ? 0.2619 0.2192 0.1543 0.0515  0.0355  -0.0058 203 PHE A CD2 
2695 C CE1 . PHE A 184 ? 0.2475 0.2368 0.1533 0.0428  0.0568  0.0018  203 PHE A CE1 
2696 C CE2 . PHE A 184 ? 0.2706 0.2231 0.1404 0.0499  0.0368  -0.0140 203 PHE A CE2 
2697 C CZ  . PHE A 184 ? 0.2608 0.2261 0.1453 0.0396  0.0299  -0.0058 203 PHE A CZ  
2707 N N   . GLU A 185 ? 0.2281 0.2011 0.2051 0.0623  0.0689  0.0312  204 GLU A N   
2708 C CA  . GLU A 185 ? 0.2387 0.2126 0.2013 0.0678  0.0742  0.0314  204 GLU A CA  
2709 C C   . GLU A 185 ? 0.2035 0.1968 0.1924 0.0507  0.0680  0.0255  204 GLU A C   
2710 O O   . GLU A 185 ? 0.1957 0.1958 0.2056 0.0496  0.0607  0.0209  204 GLU A O   
2711 C CB  . GLU A 185 ? 0.2615 0.2716 0.2207 0.0940  0.0738  0.0267  204 GLU A CB  
2712 C CG  . GLU A 185 ? 0.3270 0.3025 0.2269 0.0913  0.0609  0.0321  204 GLU A CG  
2713 C CD  . GLU A 185 ? 0.3705 0.3235 0.2399 0.0871  0.0535  0.0270  204 GLU A CD  
2714 O OE1 . GLU A 185 ? 0.3806 0.3319 0.2465 0.0751  0.0651  0.0164  204 GLU A OE1 
2715 O OE2 . GLU A 185 ? 0.4153 0.3446 0.2568 0.0769  0.0540  0.0271  204 GLU A OE2 
2722 N N   . ALA A 186 ? 0.1933 0.1855 0.1938 0.0255  0.0635  0.0362  205 ALA A N   
2723 C CA  . ALA A 186 ? 0.1880 0.1726 0.2014 0.0063  0.0562  0.0393  205 ALA A CA  
2724 C C   . ALA A 186 ? 0.1667 0.1719 0.1992 0.0115  0.0556  0.0321  205 ALA A C   
2725 O O   . ALA A 186 ? 0.1782 0.1682 0.1937 0.0055  0.0469  0.0425  205 ALA A O   
2726 C CB  . ALA A 186 ? 0.1826 0.1825 0.2058 0.0076  0.0582  0.0339  205 ALA A CB  
2732 N N   . ILE A 187 ? 0.1729 0.1730 0.1879 0.0211  0.0586  0.0193  206 ILE A N   
2733 C CA  . ILE A 187 ? 0.1740 0.1528 0.1732 0.0174  0.0488  0.0080  206 ILE A CA  
2734 C C   . ILE A 187 ? 0.1727 0.1619 0.1631 0.0260  0.0488  0.0110  206 ILE A C   
2735 O O   . ILE A 187 ? 0.1628 0.1650 0.1514 0.0128  0.0401  0.0248  206 ILE A O   
2736 C CB  . ILE A 187 ? 0.1889 0.1673 0.1793 0.0236  0.0409  0.0196  206 ILE A CB  
2737 C CG1 . ILE A 187 ? 0.1894 0.1744 0.1813 0.0341  0.0393  0.0282  206 ILE A CG1 
2738 C CG2 . ILE A 187 ? 0.1864 0.1576 0.1722 0.0143  0.0291  0.0096  206 ILE A CG2 
2739 C CD1 . ILE A 187 ? 0.1983 0.1751 0.1985 0.0365  0.0173  0.0205  206 ILE A CD1 
2751 N N   . GLN A 188 ? 0.1787 0.1737 0.1770 0.0272  0.0382  0.0112  207 GLN A N   
2752 C CA  . GLN A 188 ? 0.1866 0.1739 0.1711 0.0250  0.0409  0.0178  207 GLN A CA  
2753 C C   . GLN A 188 ? 0.1834 0.1780 0.1898 0.0323  0.0543  0.0058  207 GLN A C   
2754 O O   . GLN A 188 ? 0.1940 0.1771 0.1801 0.0344  0.0517  0.0167  207 GLN A O   
2755 C CB  . GLN A 188 ? 0.1867 0.1871 0.1694 0.0376  0.0373  -0.0067 207 GLN A CB  
2756 C CG  . GLN A 188 ? 0.1795 0.1925 0.1703 0.0279  0.0361  -0.0020 207 GLN A CG  
2757 C CD  . GLN A 188 ? 0.2105 0.1873 0.1797 0.0325  0.0290  0.0094  207 GLN A CD  
2758 O OE1 . GLN A 188 ? 0.2343 0.1701 0.1984 0.0379  0.0144  0.0139  207 GLN A OE1 
2759 N NE2 . GLN A 188 ? 0.2254 0.1901 0.1723 0.0332  0.0161  0.0125  207 GLN A NE2 
2768 N N   . GLN A 189 ? 0.1878 0.1829 0.2006 0.0323  0.0550  0.0138  208 GLN A N   
2769 C CA  . GLN A 189 ? 0.1840 0.1852 0.1985 0.0192  0.0659  0.0259  208 GLN A CA  
2770 C C   . GLN A 189 ? 0.1635 0.1715 0.1961 0.0245  0.0542  0.0236  208 GLN A C   
2771 O O   . GLN A 189 ? 0.1868 0.1590 0.2018 0.0259  0.0376  0.0310  208 GLN A O   
2772 C CB  . GLN A 189 ? 0.1878 0.1958 0.2204 0.0101  0.0580  0.0208  208 GLN A CB  
2773 C CG  . GLN A 189 ? 0.2017 0.2202 0.2336 0.0167  0.0705  0.0199  208 GLN A CG  
2774 C CD  . GLN A 189 ? 0.2327 0.2543 0.2457 0.0599  0.0807  0.0186  208 GLN A CD  
2775 O OE1 . GLN A 189 ? 0.3135 0.2804 0.2689 0.0712  0.0524  -0.0061 208 GLN A OE1 
2776 N NE2 . GLN A 189 ? 0.2253 0.2562 0.2620 0.0572  0.0740  0.0366  208 GLN A NE2 
2785 N N   . GLY A 190 ? 0.1694 0.1553 0.1999 0.0159  0.0404  0.0225  209 GLY A N   
2786 C CA  . GLY A 190 ? 0.1635 0.1511 0.1928 0.0026  0.0396  0.0077  209 GLY A CA  
2787 C C   . GLY A 190 ? 0.1361 0.1649 0.1781 0.0045  0.0311  0.0130  209 GLY A C   
2788 O O   . GLY A 190 ? 0.1520 0.1790 0.1833 0.0064  0.0243  0.0058  209 GLY A O   
2792 N N   . LEU A 191 ? 0.1394 0.1655 0.1798 0.0108  0.0336  0.0266  210 LEU A N   
2793 C CA  . LEU A 191 ? 0.1393 0.1560 0.1632 0.0137  0.0308  0.0107  210 LEU A CA  
2794 C C   . LEU A 191 ? 0.1482 0.1571 0.1689 0.0087  0.0272  0.0020  210 LEU A C   
2795 O O   . LEU A 191 ? 0.1463 0.1532 0.1702 0.0055  0.0205  0.0053  210 LEU A O   
2796 C CB  . LEU A 191 ? 0.1550 0.1638 0.1623 0.0099  0.0260  0.0141  210 LEU A CB  
2797 C CG  . LEU A 191 ? 0.1546 0.1609 0.1652 0.0118  0.0063  0.0216  210 LEU A CG  
2798 C CD1 . LEU A 191 ? 0.1658 0.1626 0.1734 -0.0004 0.0194  0.0037  210 LEU A CD1 
2799 C CD2 . LEU A 191 ? 0.1885 0.1720 0.1820 0.0239  -0.0244 0.0100  210 LEU A CD2 
2811 N N   . GLN A 192 ? 0.1348 0.1543 0.1681 0.0110  0.0329  -0.0005 211 GLN A N   
2812 C CA  . GLN A 192 ? 0.1486 0.1527 0.1713 0.0052  0.0365  0.0125  211 GLN A CA  
2813 C C   . GLN A 192 ? 0.1325 0.1498 0.1754 0.0014  0.0356  0.0189  211 GLN A C   
2814 O O   . GLN A 192 ? 0.1605 0.1559 0.1714 0.0224  0.0269  0.0143  211 GLN A O   
2815 C CB  . GLN A 192 ? 0.1441 0.1712 0.1732 0.0267  0.0205  0.0099  211 GLN A CB  
2816 C CG  . GLN A 192 ? 0.1853 0.1753 0.1768 0.0296  0.0296  0.0071  211 GLN A CG  
2817 C CD  . GLN A 192 ? 0.2043 0.1751 0.1914 0.0220  0.0172  0.0113  211 GLN A CD  
2818 O OE1 . GLN A 192 ? 0.2466 0.2046 0.2094 0.0164  -0.0157 0.0142  211 GLN A OE1 
2819 N NE2 . GLN A 192 ? 0.2240 0.1756 0.1996 0.0159  0.0273  0.0164  211 GLN A NE2 
2828 N N   . ASP A 193 ? 0.1348 0.1444 0.1848 0.0143  0.0378  0.0147  212 ASP A N   
2829 C CA  . ASP A 193 ? 0.1243 0.1524 0.1938 0.0138  0.0289  0.0047  212 ASP A CA  
2830 C C   . ASP A 193 ? 0.1152 0.1489 0.1717 0.0100  0.0260  0.0101  212 ASP A C   
2831 O O   . ASP A 193 ? 0.1413 0.1692 0.1678 0.0198  0.0035  0.0117  212 ASP A O   
2832 C CB  . ASP A 193 ? 0.1409 0.1642 0.2257 0.0012  0.0432  0.0032  212 ASP A CB  
2833 C CG  . ASP A 193 ? 0.2006 0.1946 0.2741 0.0094  0.0884  0.0153  212 ASP A CG  
2834 O OD1 . ASP A 193 ? 0.2696 0.2355 0.3336 0.0189  0.1211  0.0256  212 ASP A OD1 
2835 O OD2 . ASP A 193 ? 0.2115 0.2110 0.2819 -0.0040 0.0756  0.0228  212 ASP A OD2 
2840 N N   . ILE A 194 ? 0.1159 0.1401 0.1645 -0.0023 0.0212  0.0146  213 ILE A N   
2841 C CA  . ILE A 194 ? 0.1377 0.1482 0.1606 0.0092  0.0182  -0.0003 213 ILE A CA  
2842 C C   . ILE A 194 ? 0.1157 0.1548 0.1608 0.0046  0.0199  0.0058  213 ILE A C   
2843 O O   . ILE A 194 ? 0.1085 0.1761 0.1633 0.0029  0.0195  0.0144  213 ILE A O   
2844 C CB  . ILE A 194 ? 0.1401 0.1559 0.1576 -0.0051 0.0212  -0.0076 213 ILE A CB  
2845 C CG1 . ILE A 194 ? 0.1536 0.1483 0.1484 0.0028  0.0190  -0.0079 213 ILE A CG1 
2846 C CG2 . ILE A 194 ? 0.1433 0.1607 0.1629 0.0091  0.0132  -0.0161 213 ILE A CG2 
2847 C CD1 . ILE A 194 ? 0.1817 0.1517 0.1417 0.0120  0.0238  -0.0186 213 ILE A CD1 
2859 N N   . ILE A 195 ? 0.1215 0.1360 0.1618 0.0079  0.0110  0.0130  214 ILE A N   
2860 C CA  . ILE A 195 ? 0.1267 0.1315 0.1569 0.0211  0.0231  0.0132  214 ILE A CA  
2861 C C   . ILE A 195 ? 0.1037 0.1416 0.1665 0.0211  0.0336  0.0198  214 ILE A C   
2862 O O   . ILE A 195 ? 0.1129 0.1407 0.1643 0.0097  0.0186  0.0128  214 ILE A O   
2863 C CB  . ILE A 195 ? 0.1205 0.1398 0.1606 0.0221  0.0204  -0.0034 214 ILE A CB  
2864 C CG1 . ILE A 195 ? 0.1341 0.1433 0.1632 0.0087  0.0069  0.0060  214 ILE A CG1 
2865 C CG2 . ILE A 195 ? 0.1525 0.1587 0.1694 0.0141  0.0277  -0.0184 214 ILE A CG2 
2866 C CD1 . ILE A 195 ? 0.1631 0.1596 0.1670 -0.0102 -0.0089 0.0119  214 ILE A CD1 
2878 N N   . GLN A 196 ? 0.1053 0.1379 0.1718 0.0147  0.0230  0.0170  215 GLN A N   
2879 C CA  . GLN A 196 ? 0.1140 0.1551 0.1775 0.0225  0.0231  0.0164  215 GLN A CA  
2880 C C   . GLN A 196 ? 0.1379 0.1487 0.1751 0.0049  0.0109  0.0156  215 GLN A C   
2881 O O   . GLN A 196 ? 0.1278 0.1335 0.1803 0.0105  0.0154  0.0181  215 GLN A O   
2882 C CB  . GLN A 196 ? 0.1302 0.1626 0.1999 0.0158  0.0267  0.0134  215 GLN A CB  
2883 C CG  . GLN A 196 ? 0.1346 0.1686 0.1935 0.0103  0.0437  0.0088  215 GLN A CG  
2884 C CD  . GLN A 196 ? 0.1381 0.1821 0.1959 0.0072  0.0249  0.0120  215 GLN A CD  
2885 O OE1 . GLN A 196 ? 0.1443 0.2045 0.1991 0.0226  0.0109  -0.0020 215 GLN A OE1 
2886 N NE2 . GLN A 196 ? 0.1324 0.1911 0.2006 0.0284  0.0261  0.0293  215 GLN A NE2 
2895 N N   . GLU A 197 ? 0.1424 0.1472 0.1791 0.0000  0.0110  0.0151  216 GLU A N   
2896 C CA  . GLU A 197 ? 0.1332 0.1501 0.1936 -0.0040 -0.0040 -0.0032 216 GLU A CA  
2897 C C   . GLU A 197 ? 0.1423 0.1508 0.1699 0.0041  0.0015  0.0044  216 GLU A C   
2898 O O   . GLU A 197 ? 0.1562 0.1621 0.1645 0.0019  0.0002  0.0114  216 GLU A O   
2899 C CB  . GLU A 197 ? 0.1482 0.1541 0.2189 -0.0143 0.0003  0.0055  216 GLU A CB  
2900 C CG  . GLU A 197 ? 0.1398 0.1628 0.2572 -0.0093 0.0176  0.0131  216 GLU A CG  
2901 C CD  . GLU A 197 ? 0.1847 0.1842 0.3192 -0.0121 0.0490  0.0269  216 GLU A CD  
2902 O OE1 . GLU A 197 ? 0.2592 0.2029 0.3884 -0.0056 0.0967  0.0234  216 GLU A OE1 
2903 O OE2 . GLU A 197 ? 0.2235 0.1768 0.3109 -0.0278 0.0009  0.0516  216 GLU A OE2 
2910 N N   . THR A 198 ? 0.1408 0.1443 0.1640 -0.0086 0.0040  0.0095  217 THR A N   
2911 C CA  . THR A 198 ? 0.1360 0.1491 0.1696 -0.0026 0.0137  0.0080  217 THR A CA  
2912 C C   . THR A 198 ? 0.1423 0.1471 0.1655 0.0043  0.0187  0.0155  217 THR A C   
2913 O O   . THR A 198 ? 0.1629 0.1610 0.1702 0.0106  0.0057  0.0040  217 THR A O   
2914 C CB  . THR A 198 ? 0.1273 0.1550 0.1794 0.0128  0.0149  0.0148  217 THR A CB  
2915 O OG1 . THR A 198 ? 0.1248 0.1591 0.1775 0.0215  0.0170  0.0381  217 THR A OG1 
2916 C CG2 . THR A 198 ? 0.1531 0.1770 0.1833 -0.0120 -0.0006 0.0148  217 THR A CG2 
2924 N N   . ARG A 199 ? 0.1161 0.1477 0.1585 0.0156  0.0005  0.0171  218 ARG A N   
2925 C CA  . ARG A 199 ? 0.1299 0.1353 0.1685 0.0163  0.0020  -0.0002 218 ARG A CA  
2926 C C   . ARG A 199 ? 0.1217 0.1417 0.1848 -0.0040 0.0027  0.0203  218 ARG A C   
2927 O O   . ARG A 199 ? 0.1602 0.1633 0.2098 -0.0103 -0.0119 0.0241  218 ARG A O   
2928 C CB  . ARG A 199 ? 0.1294 0.1496 0.1627 0.0097  0.0009  -0.0017 218 ARG A CB  
2929 C CG  . ARG A 199 ? 0.1211 0.1461 0.1715 -0.0086 0.0010  0.0026  218 ARG A CG  
2930 C CD  . ARG A 199 ? 0.1149 0.1391 0.1739 0.0101  0.0024  0.0120  218 ARG A CD  
2931 N NE  . ARG A 199 ? 0.1508 0.1543 0.1639 -0.0233 0.0035  0.0087  218 ARG A NE  
2932 C CZ  . ARG A 199 ? 0.1429 0.1696 0.1580 -0.0071 0.0095  0.0052  218 ARG A CZ  
2933 N NH1 . ARG A 199 ? 0.1336 0.1722 0.1587 0.0030  -0.0062 0.0098  218 ARG A NH1 
2934 N NH2 . ARG A 199 ? 0.1817 0.1705 0.1598 -0.0337 0.0015  -0.0016 218 ARG A NH2 
2948 N N   . GLN A 200 ? 0.1393 0.1559 0.1740 -0.0144 -0.0106 0.0194  219 GLN A N   
2949 C CA  . GLN A 200 ? 0.1450 0.1755 0.1832 -0.0185 -0.0283 0.0172  219 GLN A CA  
2950 C C   . GLN A 200 ? 0.1649 0.2083 0.1868 -0.0351 -0.0384 0.0215  219 GLN A C   
2951 O O   . GLN A 200 ? 0.2075 0.2339 0.1973 -0.0402 -0.0441 0.0167  219 GLN A O   
2952 C CB  . GLN A 200 ? 0.1497 0.1854 0.1978 -0.0201 -0.0190 0.0165  219 GLN A CB  
2953 C CG  . GLN A 200 ? 0.1527 0.2134 0.2210 -0.0229 -0.0325 0.0124  219 GLN A CG  
2954 C CD  . GLN A 200 ? 0.1742 0.2621 0.2341 0.0060  -0.0460 0.0054  219 GLN A CD  
2955 O OE1 . GLN A 200 ? 0.1650 0.2656 0.2395 0.0100  -0.0400 0.0200  219 GLN A OE1 
2956 N NE2 . GLN A 200 ? 0.2183 0.3071 0.2526 0.0433  -0.0302 0.0014  219 GLN A NE2 
2965 N N   . LYS A 201 ? 0.1787 0.2128 0.1727 -0.0180 -0.0402 0.0067  220 LYS A N   
2966 C CA  . LYS A 201 ? 0.2256 0.2097 0.1759 -0.0281 -0.0247 -0.0017 220 LYS A CA  
2967 C C   . LYS A 201 ? 0.2375 0.2126 0.1646 -0.0353 0.0014  0.0011  220 LYS A C   
2968 O O   . LYS A 201 ? 0.2868 0.2426 0.1793 -0.0399 0.0043  0.0174  220 LYS A O   
2969 C CB  . LYS A 201 ? 0.2878 0.2260 0.1999 -0.0030 -0.0247 -0.0192 220 LYS A CB  
2970 C CG  . LYS A 201 ? 0.3260 0.2491 0.2464 0.0006  -0.0289 -0.0045 220 LYS A CG  
2971 C CD  . LYS A 201 ? 0.3400 0.2494 0.2776 0.0074  -0.0706 0.0159  220 LYS A CD  
2972 C CE  . LYS A 201 ? 0.3226 0.2513 0.2974 0.0167  -0.0915 0.0082  220 LYS A CE  
2973 N NZ  . LYS A 201 ? 0.2723 0.2392 0.3082 0.0035  -0.1023 0.0057  220 LYS A NZ  
2987 N N   . ILE A 202 ? 0.1845 0.1958 0.1606 -0.0358 -0.0120 0.0090  221 ILE A N   
2988 C CA  . ILE A 202 ? 0.1941 0.1998 0.1711 -0.0015 -0.0003 0.0270  221 ILE A CA  
2989 C C   . ILE A 202 ? 0.1830 0.1984 0.1904 -0.0312 -0.0158 0.0263  221 ILE A C   
2990 O O   . ILE A 202 ? 0.1750 0.2189 0.2118 -0.0311 -0.0107 0.0485  221 ILE A O   
2991 C CB  . ILE A 202 ? 0.1859 0.2108 0.1771 0.0011  0.0164  0.0201  221 ILE A CB  
2992 C CG1 . ILE A 202 ? 0.1548 0.1999 0.1741 0.0026  0.0080  0.0382  221 ILE A CG1 
2993 C CG2 . ILE A 202 ? 0.2058 0.2245 0.1927 0.0233  0.0255  0.0013  221 ILE A CG2 
2994 C CD1 . ILE A 202 ? 0.1698 0.2114 0.1931 0.0000  -0.0141 0.0428  221 ILE A CD1 
3006 N N   . GLY A 203 ? 0.1826 0.1909 0.1913 -0.0250 -0.0361 0.0345  222 GLY A N   
3007 C CA  . GLY A 203 ? 0.1742 0.1765 0.1906 -0.0119 -0.0311 0.0304  222 GLY A CA  
3008 C C   . GLY A 203 ? 0.1549 0.1793 0.2046 -0.0047 -0.0244 0.0351  222 GLY A C   
3009 O O   . GLY A 203 ? 0.1770 0.1833 0.2086 0.0265  -0.0283 0.0148  222 GLY A O   
3013 N N   . ASP A 204 ? 0.1214 0.1938 0.2106 -0.0112 0.0072  0.0348  223 ASP A N   
3014 C CA  . ASP A 204 ? 0.1125 0.1912 0.2150 0.0186  0.0063  0.0239  223 ASP A CA  
3015 C C   . ASP A 204 ? 0.1219 0.2087 0.2115 -0.0125 0.0050  0.0183  223 ASP A C   
3016 O O   . ASP A 204 ? 0.1704 0.2435 0.2236 -0.0565 0.0138  0.0161  223 ASP A O   
3017 C CB  . ASP A 204 ? 0.1126 0.2044 0.2223 0.0165  0.0195  0.0321  223 ASP A CB  
3018 C CG  . ASP A 204 ? 0.1264 0.2312 0.2533 0.0204  0.0257  0.0508  223 ASP A CG  
3019 O OD1 . ASP A 204 ? 0.1580 0.2393 0.2373 0.0196  0.0174  0.0412  223 ASP A OD1 
3020 O OD2 . ASP A 204 ? 0.1763 0.2825 0.2954 0.0200  0.0298  0.0702  223 ASP A OD2 
3025 N N   . ASP A 205 ? 0.1136 0.1977 0.2046 -0.0005 0.0109  0.0223  224 ASP A N   
3026 C CA  . ASP A 205 ? 0.1282 0.2031 0.2089 0.0000  0.0174  0.0312  224 ASP A CA  
3027 C C   . ASP A 205 ? 0.1259 0.1873 0.1984 -0.0140 0.0039  0.0220  224 ASP A C   
3028 O O   . ASP A 205 ? 0.1402 0.1951 0.2195 -0.0096 0.0247  0.0156  224 ASP A O   
3029 C CB  . ASP A 205 ? 0.1641 0.2335 0.2243 0.0014  -0.0035 0.0607  224 ASP A CB  
3030 C CG  . ASP A 205 ? 0.2334 0.2679 0.2373 0.0222  -0.0240 0.0702  224 ASP A CG  
3031 O OD1 . ASP A 205 ? 0.2341 0.2702 0.2374 -0.0023 -0.0360 0.0436  224 ASP A OD1 
3032 O OD2 . ASP A 205 ? 0.3257 0.3051 0.2559 0.0149  -0.0221 0.0653  224 ASP A OD2 
3037 N N   . LYS A 206 ? 0.1212 0.1837 0.1740 -0.0092 -0.0070 0.0183  225 LYS A N   
3038 C CA  . LYS A 206 ? 0.1292 0.1777 0.1695 -0.0046 -0.0087 0.0057  225 LYS A CA  
3039 C C   . LYS A 206 ? 0.1323 0.1824 0.1605 -0.0079 0.0083  0.0059  225 LYS A C   
3040 O O   . LYS A 206 ? 0.1282 0.2256 0.1726 0.0004  0.0173  0.0125  225 LYS A O   
3041 C CB  . LYS A 206 ? 0.1365 0.1931 0.1725 0.0185  -0.0089 -0.0031 225 LYS A CB  
3042 C CG  . LYS A 206 ? 0.1458 0.2068 0.1636 0.0059  -0.0067 -0.0083 225 LYS A CG  
3043 C CD  . LYS A 206 ? 0.1652 0.2203 0.1599 0.0073  -0.0036 -0.0181 225 LYS A CD  
3044 C CE  . LYS A 206 ? 0.1923 0.2352 0.1701 0.0097  0.0131  0.0047  225 LYS A CE  
3045 N NZ  . LYS A 206 ? 0.2512 0.2378 0.1832 0.0190  0.0235  0.0194  225 LYS A NZ  
3059 N N   . LEU A 207 ? 0.1282 0.1653 0.1522 0.0007  0.0098  0.0242  226 LEU A N   
3060 C CA  . LEU A 207 ? 0.1300 0.1398 0.1501 0.0017  0.0009  0.0090  226 LEU A CA  
3061 C C   . LEU A 207 ? 0.1270 0.1405 0.1509 0.0088  0.0136  0.0026  226 LEU A C   
3062 O O   . LEU A 207 ? 0.1532 0.1484 0.1630 0.0246  0.0375  0.0221  226 LEU A O   
3063 C CB  . LEU A 207 ? 0.1233 0.1507 0.1554 0.0034  -0.0087 0.0132  226 LEU A CB  
3064 C CG  . LEU A 207 ? 0.1221 0.1567 0.1647 -0.0069 -0.0064 0.0140  226 LEU A CG  
3065 C CD1 . LEU A 207 ? 0.1267 0.1588 0.1921 0.0056  0.0075  0.0249  226 LEU A CD1 
3066 C CD2 . LEU A 207 ? 0.1286 0.1690 0.1794 0.0073  -0.0128 0.0036  226 LEU A CD2 
3078 N N   . ILE A 208 ? 0.1231 0.1374 0.1439 0.0077  0.0073  0.0065  227 ILE A N   
3079 C CA  . ILE A 208 ? 0.1274 0.1399 0.1445 0.0052  0.0031  0.0029  227 ILE A CA  
3080 C C   . ILE A 208 ? 0.1143 0.1453 0.1464 0.0086  0.0140  -0.0062 227 ILE A C   
3081 O O   . ILE A 208 ? 0.1244 0.1516 0.1518 -0.0017 0.0148  0.0029  227 ILE A O   
3082 C CB  . ILE A 208 ? 0.1382 0.1617 0.1506 -0.0018 -0.0168 0.0138  227 ILE A CB  
3083 C CG1 . ILE A 208 ? 0.1326 0.1742 0.1630 -0.0129 -0.0182 -0.0078 227 ILE A CG1 
3084 C CG2 . ILE A 208 ? 0.1699 0.1604 0.1587 0.0091  -0.0286 0.0083  227 ILE A CG2 
3085 C CD1 . ILE A 208 ? 0.1372 0.1627 0.1760 -0.0231 -0.0013 0.0049  227 ILE A CD1 
3097 N N   . VAL A 209 ? 0.1013 0.1639 0.1362 0.0115  0.0049  0.0035  228 VAL A N   
3098 C CA  . VAL A 209 ? 0.1093 0.1621 0.1351 0.0181  -0.0098 0.0015  228 VAL A CA  
3099 C C   . VAL A 209 ? 0.1230 0.1490 0.1339 0.0056  0.0019  0.0026  228 VAL A C   
3100 O O   . VAL A 209 ? 0.1563 0.1409 0.1465 0.0150  0.0080  -0.0021 228 VAL A O   
3101 C CB  . VAL A 209 ? 0.1271 0.1659 0.1417 0.0014  0.0000  0.0010  228 VAL A CB  
3102 C CG1 . VAL A 209 ? 0.1179 0.1635 0.1438 -0.0002 0.0181  -0.0043 228 VAL A CG1 
3103 C CG2 . VAL A 209 ? 0.1530 0.1565 0.1512 0.0009  0.0051  0.0029  228 VAL A CG2 
3113 N N   . TYR A 210 ? 0.1203 0.1454 0.1352 -0.0013 -0.0106 0.0043  229 TYR A N   
3114 C CA  . TYR A 210 ? 0.1118 0.1415 0.1435 0.0056  -0.0065 0.0042  229 TYR A CA  
3115 C C   . TYR A 210 ? 0.1065 0.1416 0.1419 0.0057  0.0075  0.0091  229 TYR A C   
3116 O O   . TYR A 210 ? 0.1291 0.1517 0.1470 -0.0013 0.0044  0.0202  229 TYR A O   
3117 C CB  . TYR A 210 ? 0.1191 0.1623 0.1648 0.0076  0.0224  0.0035  229 TYR A CB  
3118 C CG  . TYR A 210 ? 0.0991 0.1671 0.1629 -0.0035 0.0047  -0.0055 229 TYR A CG  
3119 C CD1 . TYR A 210 ? 0.1300 0.1786 0.1675 0.0094  0.0172  -0.0023 229 TYR A CD1 
3120 C CD2 . TYR A 210 ? 0.1278 0.1664 0.1605 -0.0135 -0.0015 0.0051  229 TYR A CD2 
3121 C CE1 . TYR A 210 ? 0.1613 0.1971 0.1727 0.0038  0.0386  -0.0065 229 TYR A CE1 
3122 C CE2 . TYR A 210 ? 0.1533 0.1923 0.1614 0.0003  0.0053  0.0215  229 TYR A CE2 
3123 C CZ  . TYR A 210 ? 0.1860 0.2098 0.1601 0.0149  0.0441  -0.0096 229 TYR A CZ  
3124 O OH  . TYR A 210 ? 0.2493 0.2348 0.1623 0.0277  0.0455  -0.0225 229 TYR A OH  
3134 N N   . ASN A 211 ? 0.1088 0.1327 0.1514 0.0136  -0.0113 -0.0079 230 ASN A N   
3135 C CA  . ASN A 211 ? 0.1107 0.1489 0.1518 0.0155  0.0144  0.0036  230 ASN A CA  
3136 C C   . ASN A 211 ? 0.1446 0.1395 0.1515 0.0106  0.0018  0.0214  230 ASN A C   
3137 O O   . ASN A 211 ? 0.1566 0.1401 0.1609 0.0151  0.0183  0.0156  230 ASN A O   
3138 C CB  . ASN A 211 ? 0.1367 0.1415 0.1659 0.0148  0.0014  0.0029  230 ASN A CB  
3139 C CG  . ASN A 211 ? 0.1340 0.1742 0.1854 0.0289  -0.0042 -0.0044 230 ASN A CG  
3140 O OD1 . ASN A 211 ? 0.1362 0.2275 0.1998 0.0448  -0.0265 -0.0354 230 ASN A OD1 
3141 N ND2 . ASN A 211 ? 0.1483 0.1827 0.2005 0.0405  0.0072  -0.0139 230 ASN A ND2 
3148 N N   . GLY A 212 ? 0.1444 0.1432 0.1457 -0.0041 0.0002  0.0239  231 GLY A N   
3149 C CA  . GLY A 212 ? 0.1339 0.1571 0.1443 -0.0022 -0.0082 0.0186  231 GLY A CA  
3150 C C   . GLY A 212 ? 0.1543 0.1631 0.1461 -0.0060 0.0177  0.0158  231 GLY A C   
3151 O O   . GLY A 212 ? 0.2086 0.1874 0.1462 -0.0212 0.0255  0.0172  231 GLY A O   
3155 N N   . ILE A 213 ? 0.1490 0.1586 0.1429 -0.0025 0.0154  0.0212  232 ILE A N   
3156 C CA  . ILE A 213 ? 0.1421 0.1801 0.1347 0.0104  0.0288  0.0216  232 ILE A CA  
3157 C C   . ILE A 213 ? 0.1443 0.1950 0.1352 0.0104  0.0111  0.0013  232 ILE A C   
3158 O O   . ILE A 213 ? 0.1514 0.2039 0.1351 0.0081  0.0198  -0.0025 232 ILE A O   
3159 C CB  . ILE A 213 ? 0.1475 0.1838 0.1372 0.0176  0.0220  0.0068  232 ILE A CB  
3160 C CG1 . ILE A 213 ? 0.1508 0.1893 0.1582 0.0023  0.0251  0.0066  232 ILE A CG1 
3161 C CG2 . ILE A 213 ? 0.1768 0.1972 0.1402 0.0238  0.0048  -0.0073 232 ILE A CG2 
3162 C CD1 . ILE A 213 ? 0.1517 0.2019 0.1605 -0.0139 0.0119  0.0046  232 ILE A CD1 
3174 N N   . ARG A 214 ? 0.1474 0.1958 0.1535 0.0148  0.0204  0.0252  233 ARG A N   
3175 C CA  . ARG A 214 ? 0.1602 0.2138 0.1674 0.0281  0.0096  0.0312  233 ARG A CA  
3176 C C   . ARG A 214 ? 0.1558 0.2362 0.1635 0.0019  0.0004  0.0385  233 ARG A C   
3177 O O   . ARG A 214 ? 0.1592 0.2569 0.1666 -0.0224 0.0159  0.0318  233 ARG A O   
3178 C CB  . ARG A 214 ? 0.1929 0.2140 0.1933 0.0329  0.0069  0.0254  233 ARG A CB  
3179 C CG  . ARG A 214 ? 0.2417 0.2310 0.2295 0.0214  0.0135  0.0408  233 ARG A CG  
3180 C CD  . ARG A 214 ? 0.2435 0.2279 0.2550 0.0099  0.0238  0.0464  233 ARG A CD  
3181 N NE  . ARG A 214 ? 0.2193 0.2176 0.2564 0.0296  0.0452  0.0394  233 ARG A NE  
3182 C CZ  . ARG A 214 ? 0.2381 0.2211 0.2774 0.0260  0.0497  0.0482  233 ARG A CZ  
3183 N NH1 . ARG A 214 ? 0.2442 0.2216 0.2951 0.0160  0.0528  0.0552  233 ARG A NH1 
3184 N NH2 . ARG A 214 ? 0.2380 0.2242 0.2877 0.0602  0.0264  0.0450  233 ARG A NH2 
3198 N N   . SER A 215 ? 0.1699 0.2283 0.1572 0.0047  -0.0069 0.0352  234 SER A N   
3199 C CA  . SER A 215 ? 0.1655 0.2324 0.1555 0.0117  -0.0077 0.0379  234 SER A CA  
3200 C C   . SER A 215 ? 0.2001 0.2436 0.1645 0.0075  -0.0050 0.0460  234 SER A C   
3201 O O   . SER A 215 ? 0.2077 0.2472 0.1706 0.0024  -0.0194 0.0427  234 SER A O   
3202 C CB  . SER A 215 ? 0.1818 0.2354 0.1579 0.0258  -0.0095 0.0244  234 SER A CB  
3203 O OG  . SER A 215 ? 0.2087 0.2380 0.1611 0.0268  -0.0048 0.0206  234 SER A OG  
3209 N N   . THR A 216 ? 0.1995 0.2529 0.1756 -0.0023 0.0071  0.0639  235 THR A N   
3210 C CA  . THR A 216 ? 0.2337 0.2698 0.1999 0.0210  0.0021  0.0730  235 THR A CA  
3211 C C   . THR A 216 ? 0.2475 0.3061 0.2103 0.0445  0.0274  0.0943  235 THR A C   
3212 O O   . THR A 216 ? 0.2705 0.3263 0.2162 0.0552  0.0336  0.0963  235 THR A O   
3213 C CB  . THR A 216 ? 0.2494 0.2705 0.2287 0.0236  0.0137  0.0794  235 THR A CB  
3214 O OG1 . THR A 216 ? 0.2685 0.2824 0.2619 0.0124  0.0277  0.0929  235 THR A OG1 
3215 C CG2 . THR A 216 ? 0.2718 0.2716 0.2209 0.0231  0.0119  0.0761  235 THR A CG2 
3223 N N   . PRO A 217 ? 0.2900 0.3552 0.2233 0.0685  0.0220  0.1116  236 PRO A N   
3224 C CA  . PRO A 217 ? 0.3186 0.3944 0.2439 0.0751  0.0010  0.1414  236 PRO A CA  
3225 C C   . PRO A 217 ? 0.3800 0.4397 0.2872 0.0622  0.0200  0.1662  236 PRO A C   
3226 O O   . PRO A 217 ? 0.4204 0.4619 0.3002 0.0643  0.0523  0.1472  236 PRO A O   
3227 C CB  . PRO A 217 ? 0.3262 0.3854 0.2325 0.0856  -0.0190 0.1409  236 PRO A CB  
3228 C CG  . PRO A 217 ? 0.3223 0.3813 0.2390 0.0735  -0.0158 0.1193  236 PRO A CG  
3229 C CD  . PRO A 217 ? 0.3016 0.3697 0.2289 0.0663  -0.0023 0.1161  236 PRO A CD  
3237 N N   . ASP A 218 ? 0.3847 0.4674 0.3284 0.0481  0.0068  0.1847  237 ASP A N   
3238 C CA  . ASP A 218 ? 0.4261 0.5015 0.3886 0.0221  0.0061  0.1716  237 ASP A CA  
3239 C C   . ASP A 218 ? 0.4279 0.5123 0.4057 0.0055  0.0198  0.1745  237 ASP A C   
3240 O O   . ASP A 218 ? 0.4578 0.5271 0.4259 -0.0001 0.0181  0.1648  237 ASP A O   
3241 C CB  . ASP A 218 ? 0.4821 0.5266 0.4260 0.0188  -0.0008 0.1521  237 ASP A CB  
3242 C CG  . ASP A 218 ? 0.5381 0.5456 0.4568 0.0282  -0.0053 0.1319  237 ASP A CG  
3243 O OD1 . ASP A 218 ? 0.5534 0.5517 0.4653 0.0257  -0.0006 0.1339  237 ASP A OD1 
3244 O OD2 . ASP A 218 ? 0.5762 0.5550 0.4767 0.0343  -0.0124 0.1182  237 ASP A OD2 
3249 N N   . TRP A 219 ? 0.3812 0.4963 0.4031 0.0013  0.0218  0.1830  238 TRP A N   
3250 C CA  . TRP A 219 ? 0.3483 0.4738 0.4026 -0.0090 0.0236  0.1810  238 TRP A CA  
3251 C C   . TRP A 219 ? 0.2958 0.4685 0.3814 -0.0085 0.0279  0.1916  238 TRP A C   
3252 O O   . TRP A 219 ? 0.2769 0.4755 0.3975 -0.0075 0.0457  0.1909  238 TRP A O   
3253 C CB  . TRP A 219 ? 0.3853 0.4532 0.4236 -0.0187 0.0199  0.1629  238 TRP A CB  
3254 C CG  . TRP A 219 ? 0.4065 0.4323 0.4380 -0.0427 0.0332  0.1420  238 TRP A CG  
3255 C CD1 . TRP A 219 ? 0.4276 0.4295 0.4434 -0.0526 0.0284  0.1409  238 TRP A CD1 
3256 C CD2 . TRP A 219 ? 0.4019 0.4122 0.4443 -0.0486 0.0408  0.1313  238 TRP A CD2 
3257 N NE1 . TRP A 219 ? 0.4345 0.4269 0.4471 -0.0660 0.0363  0.1287  238 TRP A NE1 
3258 C CE2 . TRP A 219 ? 0.4073 0.4082 0.4441 -0.0641 0.0459  0.1321  238 TRP A CE2 
3259 C CE3 . TRP A 219 ? 0.3837 0.3902 0.4456 -0.0522 0.0489  0.1278  238 TRP A CE3 
3260 C CZ2 . TRP A 219 ? 0.3865 0.3872 0.4447 -0.0719 0.0503  0.1322  238 TRP A CZ2 
3261 C CZ3 . TRP A 219 ? 0.3754 0.3794 0.4441 -0.0640 0.0600  0.1259  238 TRP A CZ3 
3262 C CH2 . TRP A 219 ? 0.3836 0.3781 0.4428 -0.0642 0.0553  0.1309  238 TRP A CH2 
3273 N N   . SER A 220 ? 0.2808 0.4498 0.3472 -0.0085 0.0236  0.1880  239 SER A N   
3274 C CA  . SER A 220 ? 0.2561 0.4313 0.3124 -0.0144 0.0012  0.1660  239 SER A CA  
3275 C C   . SER A 220 ? 0.2172 0.3900 0.2811 -0.0307 0.0113  0.1403  239 SER A C   
3276 O O   . SER A 220 ? 0.2654 0.4090 0.2919 -0.0394 0.0077  0.1446  239 SER A O   
3277 C CB  . SER A 220 ? 0.2937 0.4444 0.3139 -0.0052 -0.0255 0.1540  239 SER A CB  
3278 O OG  . SER A 220 ? 0.3344 0.4626 0.3137 -0.0101 -0.0424 0.1386  239 SER A OG  
3284 N N   . ALA A 221 ? 0.1952 0.3405 0.2396 -0.0295 0.0149  0.1026  240 ALA A N   
3285 C CA  . ALA A 221 ? 0.2031 0.3011 0.2024 -0.0150 0.0185  0.0648  240 ALA A CA  
3286 C C   . ALA A 221 ? 0.1820 0.2639 0.1809 -0.0027 0.0210  0.0272  240 ALA A C   
3287 O O   . ALA A 221 ? 0.1834 0.2514 0.1834 0.0066  0.0557  0.0055  240 ALA A O   
3288 C CB  . ALA A 221 ? 0.2680 0.3151 0.1986 -0.0094 0.0022  0.0624  240 ALA A CB  
3294 N N   . GLY A 222 ? 0.1832 0.2665 0.1842 0.0058  0.0339  0.0231  241 GLY A N   
3295 C CA  . GLY A 222 ? 0.1761 0.2475 0.1882 0.0056  0.0212  0.0121  241 GLY A CA  
3296 C C   . GLY A 222 ? 0.1798 0.2300 0.1805 -0.0151 0.0165  -0.0049 241 GLY A C   
3297 O O   . GLY A 222 ? 0.2014 0.2189 0.2073 -0.0148 -0.0066 0.0019  241 GLY A O   
3301 N N   . PHE A 223 ? 0.1707 0.2071 0.1633 -0.0273 0.0125  -0.0040 242 PHE A N   
3302 C CA  . PHE A 223 ? 0.1499 0.2030 0.1592 -0.0288 0.0106  -0.0065 242 PHE A CA  
3303 C C   . PHE A 223 ? 0.1513 0.2202 0.1782 -0.0149 0.0270  -0.0099 242 PHE A C   
3304 O O   . PHE A 223 ? 0.1948 0.2684 0.2051 -0.0174 0.0499  -0.0270 242 PHE A O   
3305 C CB  . PHE A 223 ? 0.1667 0.1906 0.1657 -0.0148 0.0111  -0.0129 242 PHE A CB  
3306 C CG  . PHE A 223 ? 0.1519 0.1841 0.1626 -0.0208 0.0114  -0.0060 242 PHE A CG  
3307 C CD1 . PHE A 223 ? 0.2053 0.1894 0.1719 -0.0286 -0.0155 0.0101  242 PHE A CD1 
3308 C CD2 . PHE A 223 ? 0.1594 0.1932 0.1671 0.0182  0.0222  -0.0133 242 PHE A CD2 
3309 C CE1 . PHE A 223 ? 0.2467 0.1807 0.1814 -0.0184 -0.0170 -0.0296 242 PHE A CE1 
3310 C CE2 . PHE A 223 ? 0.2067 0.1889 0.1773 0.0457  0.0290  -0.0044 242 PHE A CE2 
3311 C CZ  . PHE A 223 ? 0.2399 0.1759 0.1726 0.0439  0.0057  -0.0324 242 PHE A CZ  
3321 N N   . ASP A 224 ? 0.1484 0.2297 0.1791 -0.0212 0.0056  0.0009  243 ASP A N   
3322 C CA  . ASP A 224 ? 0.2023 0.2352 0.1967 -0.0212 0.0058  0.0106  243 ASP A CA  
3323 C C   . ASP A 224 ? 0.1796 0.2125 0.1744 -0.0068 0.0215  0.0126  243 ASP A C   
3324 O O   . ASP A 224 ? 0.1842 0.2048 0.1776 -0.0180 0.0257  0.0302  243 ASP A O   
3325 C CB  . ASP A 224 ? 0.3097 0.2719 0.2392 -0.0210 -0.0001 0.0425  243 ASP A CB  
3326 C CG  . ASP A 224 ? 0.4325 0.3090 0.2825 0.0205  0.0092  0.0564  243 ASP A CG  
3327 O OD1 . ASP A 224 ? 0.4470 0.3199 0.2969 0.0239  0.0255  0.0489  243 ASP A OD1 
3328 O OD2 . ASP A 224 ? 0.4984 0.3285 0.3078 0.0443  0.0084  0.0624  243 ASP A OD2 
3333 N N   . PHE A 225 ? 0.1680 0.2073 0.1767 0.0006  0.0313  0.0019  244 PHE A N   
3334 C CA  . PHE A 225 ? 0.1608 0.2126 0.1660 0.0097  0.0325  0.0035  244 PHE A CA  
3335 C C   . PHE A 225 ? 0.1604 0.1995 0.1630 0.0020  0.0401  -0.0125 244 PHE A C   
3336 O O   . PHE A 225 ? 0.1476 0.1988 0.1595 0.0035  0.0223  -0.0077 244 PHE A O   
3337 C CB  . PHE A 225 ? 0.1757 0.2267 0.1707 0.0107  0.0247  0.0007  244 PHE A CB  
3338 C CG  . PHE A 225 ? 0.1884 0.2326 0.1817 0.0365  0.0292  0.0042  244 PHE A CG  
3339 C CD1 . PHE A 225 ? 0.2100 0.2331 0.1890 0.0359  0.0267  0.0130  244 PHE A CD1 
3340 C CD2 . PHE A 225 ? 0.2202 0.2444 0.1822 0.0645  0.0147  0.0075  244 PHE A CD2 
3341 C CE1 . PHE A 225 ? 0.2242 0.2399 0.1944 0.0410  0.0319  0.0155  244 PHE A CE1 
3342 C CE2 . PHE A 225 ? 0.2363 0.2424 0.1869 0.0748  0.0279  0.0152  244 PHE A CE2 
3343 C CZ  . PHE A 225 ? 0.2334 0.2483 0.1860 0.0560  0.0250  0.0091  244 PHE A CZ  
3353 N N   . ALA A 226 ? 0.1698 0.2008 0.1763 0.0147  0.0192  -0.0181 245 ALA A N   
3354 C CA  . ALA A 226 ? 0.1734 0.1959 0.1842 0.0085  0.0063  -0.0146 245 ALA A CA  
3355 C C   . ALA A 226 ? 0.1695 0.1905 0.1912 0.0055  -0.0013 -0.0052 245 ALA A C   
3356 O O   . ALA A 226 ? 0.1755 0.1756 0.1944 0.0049  -0.0148 -0.0079 245 ALA A O   
3357 C CB  . ALA A 226 ? 0.2229 0.2008 0.1887 0.0111  -0.0087 -0.0227 245 ALA A CB  
3363 N N   . GLU A 227 ? 0.1579 0.2010 0.2100 0.0108  0.0044  -0.0054 246 GLU A N   
3364 C CA  . GLU A 227 ? 0.1656 0.1997 0.2126 0.0039  0.0165  0.0155  246 GLU A CA  
3365 C C   . GLU A 227 ? 0.1541 0.1884 0.2069 0.0117  0.0158  0.0023  246 GLU A C   
3366 O O   . GLU A 227 ? 0.1705 0.1836 0.2127 -0.0018 0.0327  -0.0018 246 GLU A O   
3367 C CB  . GLU A 227 ? 0.1492 0.2273 0.2128 -0.0038 0.0271  0.0258  246 GLU A CB  
3368 C CG  . GLU A 227 ? 0.1995 0.2798 0.2129 0.0121  0.0451  0.0314  246 GLU A CG  
3369 C CD  . GLU A 227 ? 0.3028 0.3383 0.2333 0.0189  0.0418  0.0213  246 GLU A CD  
3370 O OE1 . GLU A 227 ? 0.2567 0.3217 0.2401 -0.0093 0.0575  0.0213  246 GLU A OE1 
3371 O OE2 . GLU A 227 ? 0.3899 0.3814 0.2465 0.0494  0.0326  0.0255  246 GLU A OE2 
3378 N N   . TYR A 228 ? 0.1269 0.1783 0.2072 0.0001  0.0298  -0.0009 247 TYR A N   
3379 C CA  . TYR A 228 ? 0.1429 0.1754 0.1934 0.0073  0.0067  0.0089  247 TYR A CA  
3380 C C   . TYR A 228 ? 0.1282 0.1720 0.1773 0.0230  0.0214  0.0271  247 TYR A C   
3381 O O   . TYR A 228 ? 0.1574 0.2274 0.1748 0.0450  0.0307  0.0432  247 TYR A O   
3382 C CB  . TYR A 228 ? 0.1457 0.1637 0.2051 0.0055  0.0080  0.0075  247 TYR A CB  
3383 C CG  . TYR A 228 ? 0.1365 0.1554 0.2202 -0.0026 -0.0105 0.0275  247 TYR A CG  
3384 C CD1 . TYR A 228 ? 0.1379 0.1641 0.2324 -0.0087 -0.0157 0.0294  247 TYR A CD1 
3385 C CD2 . TYR A 228 ? 0.1279 0.1606 0.2242 -0.0119 -0.0196 0.0407  247 TYR A CD2 
3386 C CE1 . TYR A 228 ? 0.1337 0.1682 0.2444 -0.0127 -0.0222 0.0365  247 TYR A CE1 
3387 C CE2 . TYR A 228 ? 0.1308 0.1740 0.2383 -0.0055 -0.0060 0.0397  247 TYR A CE2 
3388 C CZ  . TYR A 228 ? 0.1205 0.1718 0.2489 -0.0089 0.0008  0.0347  247 TYR A CZ  
3389 O OH  . TYR A 228 ? 0.1433 0.1943 0.2794 -0.0115 0.0076  0.0397  247 TYR A OH  
3399 N N   . THR A 229 ? 0.1244 0.1753 0.1801 -0.0045 0.0238  -0.0028 248 THR A N   
3400 C CA  . THR A 229 ? 0.1258 0.1649 0.1904 -0.0312 0.0222  -0.0102 248 THR A CA  
3401 C C   . THR A 229 ? 0.1089 0.1570 0.1826 -0.0028 0.0343  -0.0167 248 THR A C   
3402 O O   . THR A 229 ? 0.1334 0.1727 0.1916 -0.0119 0.0562  -0.0176 248 THR A O   
3403 C CB  . THR A 229 ? 0.1575 0.1714 0.2129 -0.0259 0.0330  -0.0002 248 THR A CB  
3404 O OG1 . THR A 229 ? 0.1505 0.1949 0.2327 -0.0088 0.0055  -0.0039 248 THR A OG1 
3405 C CG2 . THR A 229 ? 0.1740 0.1736 0.2105 -0.0327 0.0404  0.0185  248 THR A CG2 
3413 N N   . ASP A 230 ? 0.0916 0.1482 0.1688 -0.0032 0.0363  -0.0090 249 ASP A N   
3414 C CA  . ASP A 230 ? 0.1120 0.1482 0.1501 -0.0136 0.0130  -0.0217 249 ASP A CA  
3415 C C   . ASP A 230 ? 0.1354 0.1512 0.1578 -0.0026 0.0109  -0.0121 249 ASP A C   
3416 O O   . ASP A 230 ? 0.1396 0.1377 0.1523 0.0015  0.0147  -0.0214 249 ASP A O   
3417 C CB  . ASP A 230 ? 0.1246 0.1625 0.1541 0.0156  0.0068  -0.0175 249 ASP A CB  
3418 C CG  . ASP A 230 ? 0.1372 0.1589 0.1646 0.0060  0.0103  -0.0063 249 ASP A CG  
3419 O OD1 . ASP A 230 ? 0.1524 0.1722 0.1767 0.0060  0.0092  -0.0127 249 ASP A OD1 
3420 O OD2 . ASP A 230 ? 0.1368 0.1530 0.1725 0.0136  0.0079  -0.0015 249 ASP A OD2 
3425 N N   . ALA A 231 ? 0.1021 0.1638 0.1688 -0.0158 -0.0094 0.0100  250 ALA A N   
3426 C CA  . ALA A 231 ? 0.1155 0.1535 0.1546 -0.0122 -0.0065 0.0051  250 ALA A CA  
3427 C C   . ALA A 231 ? 0.1104 0.1470 0.1450 0.0047  0.0057  0.0057  250 ALA A C   
3428 O O   . ALA A 231 ? 0.1389 0.1491 0.1352 0.0002  0.0196  0.0079  250 ALA A O   
3429 C CB  . ALA A 231 ? 0.1410 0.1549 0.1593 0.0128  0.0105  0.0096  250 ALA A CB  
3435 N N   . ALA A 232 ? 0.1001 0.1394 0.1439 -0.0054 -0.0086 0.0009  251 ALA A N   
3436 C CA  . ALA A 232 ? 0.1072 0.1444 0.1413 0.0032  -0.0004 0.0083  251 ALA A CA  
3437 C C   . ALA A 232 ? 0.1229 0.1481 0.1393 0.0052  0.0049  0.0056  251 ALA A C   
3438 O O   . ALA A 232 ? 0.1361 0.1389 0.1518 0.0118  0.0101  0.0044  251 ALA A O   
3439 C CB  . ALA A 232 ? 0.1319 0.1448 0.1430 0.0232  0.0095  0.0159  251 ALA A CB  
3445 N N   . MET A 233 ? 0.1214 0.1396 0.1285 0.0083  -0.0053 0.0038  252 MET A N   
3446 C CA  . MET A 233 ? 0.0981 0.1542 0.1242 0.0011  0.0202  0.0115  252 MET A CA  
3447 C C   . MET A 233 ? 0.1130 0.1464 0.1467 0.0163  0.0061  0.0144  252 MET A C   
3448 O O   . MET A 233 ? 0.1243 0.1683 0.1494 -0.0032 -0.0006 0.0216  252 MET A O   
3449 C CB  . MET A 233 ? 0.1042 0.1820 0.1466 0.0083  0.0265  -0.0033 252 MET A CB  
3450 C CG  . MET A 233 ? 0.1393 0.2104 0.1784 0.0147  0.0291  -0.0069 252 MET A CG  
3451 S SD  . MET A 233 ? 0.1659 0.2247 0.1834 0.0277  0.0174  -0.0094 252 MET A SD  
3452 C CE  . MET A 233 ? 0.2403 0.2624 0.1815 -0.0028 0.0381  -0.0141 252 MET A CE  
3462 N N   . ILE A 234 ? 0.1214 0.1333 0.1453 0.0135  -0.0060 -0.0007 253 ILE A N   
3463 C CA  . ILE A 234 ? 0.1232 0.1385 0.1305 0.0006  -0.0091 0.0104  253 ILE A CA  
3464 C C   . ILE A 234 ? 0.1107 0.1474 0.1427 -0.0111 -0.0034 0.0088  253 ILE A C   
3465 O O   . ILE A 234 ? 0.1227 0.1785 0.1467 -0.0085 0.0089  0.0106  253 ILE A O   
3466 C CB  . ILE A 234 ? 0.1429 0.1553 0.1264 0.0044  0.0004  0.0026  253 ILE A CB  
3467 C CG1 . ILE A 234 ? 0.1599 0.1543 0.1354 -0.0052 -0.0041 -0.0102 253 ILE A CG1 
3468 C CG2 . ILE A 234 ? 0.1764 0.1888 0.1398 -0.0058 0.0064  -0.0031 253 ILE A CG2 
3469 C CD1 . ILE A 234 ? 0.1728 0.1653 0.1431 0.0020  -0.0009 -0.0169 253 ILE A CD1 
3481 N N   . GLU A 235 ? 0.1231 0.1453 0.1456 0.0067  -0.0015 0.0042  254 GLU A N   
3482 C CA  . GLU A 235 ? 0.1118 0.1560 0.1475 -0.0026 -0.0113 -0.0065 254 GLU A CA  
3483 C C   . GLU A 235 ? 0.1048 0.1606 0.1608 0.0153  -0.0026 0.0028  254 GLU A C   
3484 O O   . GLU A 235 ? 0.1165 0.1641 0.1788 0.0156  -0.0133 0.0142  254 GLU A O   
3485 C CB  . GLU A 235 ? 0.1177 0.1658 0.1672 0.0046  0.0005  -0.0147 254 GLU A CB  
3486 C CG  . GLU A 235 ? 0.1264 0.1971 0.1905 0.0294  0.0179  -0.0226 254 GLU A CG  
3487 C CD  . GLU A 235 ? 0.1253 0.2089 0.2186 0.0334  0.0096  -0.0199 254 GLU A CD  
3488 O OE1 . GLU A 235 ? 0.1366 0.1936 0.2105 0.0278  0.0006  -0.0126 254 GLU A OE1 
3489 O OE2 . GLU A 235 ? 0.1401 0.2262 0.2307 0.0328  0.0215  -0.0337 254 GLU A OE2 
3496 N N   . HIS A 236 ? 0.1414 0.1715 0.1584 0.0260  -0.0016 0.0072  255 HIS A N   
3497 C CA  . HIS A 236 ? 0.1385 0.1653 0.1629 0.0264  -0.0018 0.0211  255 HIS A CA  
3498 C C   . HIS A 236 ? 0.1651 0.1736 0.1593 0.0228  -0.0094 0.0253  255 HIS A C   
3499 O O   . HIS A 236 ? 0.1871 0.1752 0.1642 0.0036  -0.0216 0.0435  255 HIS A O   
3500 C CB  . HIS A 236 ? 0.1601 0.1696 0.1779 0.0135  0.0123  0.0121  255 HIS A CB  
3501 C CG  . HIS A 236 ? 0.1796 0.1679 0.1826 0.0128  -0.0068 0.0139  255 HIS A CG  
3502 N ND1 . HIS A 236 ? 0.1859 0.1690 0.1894 0.0006  -0.0071 0.0195  255 HIS A ND1 
3503 C CD2 . HIS A 236 ? 0.1800 0.1725 0.2020 0.0038  -0.0069 0.0171  255 HIS A CD2 
3504 C CE1 . HIS A 236 ? 0.1961 0.1505 0.2153 0.0041  -0.0158 0.0185  255 HIS A CE1 
3505 N NE2 . HIS A 236 ? 0.2194 0.1722 0.2150 0.0124  -0.0175 0.0169  255 HIS A NE2 
3513 N N   . PHE A 237 ? 0.1767 0.1686 0.1578 0.0146  -0.0068 0.0026  256 PHE A N   
3514 C CA  . PHE A 237 ? 0.1618 0.1673 0.1509 0.0168  -0.0130 0.0093  256 PHE A CA  
3515 C C   . PHE A 237 ? 0.1693 0.1625 0.1484 0.0105  -0.0038 0.0065  256 PHE A C   
3516 O O   . PHE A 237 ? 0.1700 0.1683 0.1415 0.0220  -0.0036 0.0163  256 PHE A O   
3517 C CB  . PHE A 237 ? 0.1694 0.1762 0.1535 0.0116  -0.0067 0.0020  256 PHE A CB  
3518 C CG  . PHE A 237 ? 0.1802 0.1789 0.1628 0.0132  -0.0035 0.0000  256 PHE A CG  
3519 C CD1 . PHE A 237 ? 0.2018 0.1891 0.1699 0.0263  -0.0064 0.0034  256 PHE A CD1 
3520 C CD2 . PHE A 237 ? 0.1902 0.1844 0.1707 0.0119  0.0198  0.0042  256 PHE A CD2 
3521 C CE1 . PHE A 237 ? 0.1956 0.1900 0.1788 0.0266  0.0157  -0.0026 256 PHE A CE1 
3522 C CE2 . PHE A 237 ? 0.2188 0.1827 0.1864 0.0174  0.0263  0.0018  256 PHE A CE2 
3523 C CZ  . PHE A 237 ? 0.2082 0.1799 0.1811 0.0032  0.0254  -0.0079 256 PHE A CZ  
3533 N N   . GLY A 238 ? 0.1738 0.1778 0.1538 0.0039  -0.0061 0.0048  257 GLY A N   
3534 C CA  . GLY A 238 ? 0.1626 0.1875 0.1487 0.0071  -0.0164 -0.0051 257 GLY A CA  
3535 C C   . GLY A 238 ? 0.1418 0.2053 0.1519 0.0153  -0.0306 -0.0056 257 GLY A C   
3536 O O   . GLY A 238 ? 0.1601 0.2178 0.1688 0.0092  -0.0270 -0.0070 257 GLY A O   
3540 N N   . HIS A 239 ? 0.1394 0.1980 0.1600 0.0160  -0.0202 0.0190  258 HIS A N   
3541 C CA  . HIS A 239 ? 0.1620 0.2063 0.1622 0.0282  -0.0090 0.0216  258 HIS A CA  
3542 C C   . HIS A 239 ? 0.1524 0.2161 0.1807 0.0135  -0.0155 0.0144  258 HIS A C   
3543 O O   . HIS A 239 ? 0.1727 0.2243 0.1855 0.0240  -0.0070 0.0385  258 HIS A O   
3544 C CB  . HIS A 239 ? 0.1870 0.2168 0.1652 0.0174  -0.0052 0.0119  258 HIS A CB  
3545 C CG  . HIS A 239 ? 0.1830 0.2155 0.1700 0.0128  0.0210  -0.0142 258 HIS A CG  
3546 N ND1 . HIS A 239 ? 0.2211 0.2330 0.1920 0.0124  0.0138  -0.0115 258 HIS A ND1 
3547 C CD2 . HIS A 239 ? 0.1993 0.2174 0.1675 -0.0019 0.0317  -0.0176 258 HIS A CD2 
3548 C CE1 . HIS A 239 ? 0.2152 0.2394 0.1870 -0.0109 0.0138  -0.0178 258 HIS A CE1 
3549 N NE2 . HIS A 239 ? 0.2248 0.2291 0.1825 -0.0052 0.0101  -0.0237 258 HIS A NE2 
3557 N N   . PHE A 240 ? 0.1559 0.2027 0.1994 0.0180  -0.0186 0.0231  259 PHE A N   
3558 C CA  . PHE A 240 ? 0.1403 0.1934 0.2007 0.0088  -0.0024 0.0135  259 PHE A CA  
3559 C C   . PHE A 240 ? 0.1805 0.2255 0.2056 0.0242  -0.0192 0.0175  259 PHE A C   
3560 O O   . PHE A 240 ? 0.2279 0.2683 0.2070 0.0255  -0.0270 0.0449  259 PHE A O   
3561 C CB  . PHE A 240 ? 0.1556 0.1933 0.2094 0.0147  0.0036  0.0134  259 PHE A CB  
3562 C CG  . PHE A 240 ? 0.1541 0.1962 0.2193 0.0161  0.0231  0.0252  259 PHE A CG  
3563 C CD1 . PHE A 240 ? 0.1774 0.2001 0.2232 0.0301  0.0196  0.0333  259 PHE A CD1 
3564 C CD2 . PHE A 240 ? 0.1322 0.2103 0.2141 0.0252  0.0094  0.0337  259 PHE A CD2 
3565 C CE1 . PHE A 240 ? 0.1636 0.2121 0.2294 0.0372  0.0186  0.0174  259 PHE A CE1 
3566 C CE2 . PHE A 240 ? 0.1377 0.2089 0.2238 0.0319  -0.0038 0.0330  259 PHE A CE2 
3567 C CZ  . PHE A 240 ? 0.1525 0.2253 0.2330 0.0153  0.0079  0.0212  259 PHE A CZ  
3577 N N   . GLN A 241 ? 0.1994 0.2384 0.2068 0.0457  -0.0113 0.0238  260 GLN A N   
3578 C CA  . GLN A 241 ? 0.2482 0.2448 0.2316 0.0431  -0.0019 0.0468  260 GLN A CA  
3579 C C   . GLN A 241 ? 0.2382 0.2368 0.2100 0.0288  0.0004  0.0450  260 GLN A C   
3580 O O   . GLN A 241 ? 0.2429 0.2366 0.2094 0.0162  0.0056  0.0425  260 GLN A O   
3581 C CB  . GLN A 241 ? 0.2942 0.2612 0.2855 0.0426  0.0090  0.0643  260 GLN A CB  
3582 C CG  . GLN A 241 ? 0.3777 0.2883 0.3479 0.0234  0.0159  0.0695  260 GLN A CG  
3583 C CD  . GLN A 241 ? 0.4435 0.3432 0.4190 -0.0062 0.0003  0.0581  260 GLN A CD  
3584 O OE1 . GLN A 241 ? 0.4725 0.3644 0.4456 -0.0047 -0.0024 0.0529  260 GLN A OE1 
3585 N NE2 . GLN A 241 ? 0.4715 0.3688 0.4468 -0.0151 -0.0135 0.0506  260 GLN A NE2 
3594 N N   . SER A 242 ? 0.2175 0.2192 0.1839 0.0278  0.0018  0.0409  261 SER A N   
3595 C CA  . SER A 242 ? 0.1910 0.2181 0.1737 0.0310  -0.0236 0.0146  261 SER A CA  
3596 C C   . SER A 242 ? 0.1872 0.2110 0.1795 0.0142  -0.0212 0.0234  261 SER A C   
3597 O O   . SER A 242 ? 0.2018 0.2026 0.2025 0.0221  -0.0574 0.0096  261 SER A O   
3598 C CB  . SER A 242 ? 0.1921 0.2095 0.1856 0.0268  -0.0140 0.0205  261 SER A CB  
3599 O OG  . SER A 242 ? 0.1962 0.1922 0.1810 0.0211  0.0023  0.0165  261 SER A OG  
3605 N N   . ALA A 243 ? 0.1943 0.2316 0.1755 0.0173  -0.0210 0.0188  262 ALA A N   
3606 C CA  . ALA A 243 ? 0.1917 0.2433 0.1848 0.0358  -0.0230 0.0113  262 ALA A CA  
3607 C C   . ALA A 243 ? 0.2203 0.2438 0.1866 0.0338  -0.0250 0.0142  262 ALA A C   
3608 O O   . ALA A 243 ? 0.2438 0.2472 0.1912 0.0299  -0.0256 0.0087  262 ALA A O   
3609 C CB  . ALA A 243 ? 0.1879 0.2640 0.2026 0.0486  -0.0356 0.0182  262 ALA A CB  
3615 N N   . SER A 244 ? 0.2238 0.2404 0.1778 0.0364  -0.0318 0.0089  263 SER A N   
3616 C CA  . SER A 244 ? 0.2391 0.2426 0.1736 0.0497  -0.0434 0.0113  263 SER A CA  
3617 C C   . SER A 244 ? 0.2474 0.2398 0.1673 0.0574  -0.0532 0.0107  263 SER A C   
3618 O O   . SER A 244 ? 0.2443 0.2400 0.1660 0.0466  -0.0352 0.0166  263 SER A O   
3619 C CB  . SER A 244 ? 0.2552 0.2526 0.1706 0.0670  -0.0530 0.0279  263 SER A CB  
3620 O OG  . SER A 244 ? 0.2606 0.2609 0.1755 0.0676  -0.0337 0.0340  263 SER A OG  
3626 N N   . LYS A 245 ? 0.2924 0.2384 0.1731 0.0558  -0.0679 0.0033  264 LYS A N   
3627 C CA  . LYS A 245 ? 0.3102 0.2441 0.1666 0.0598  -0.0658 0.0073  264 LYS A CA  
3628 C C   . LYS A 245 ? 0.2965 0.2481 0.1546 0.0420  -0.0510 0.0166  264 LYS A C   
3629 O O   . LYS A 245 ? 0.2742 0.2443 0.1548 0.0327  -0.0481 0.0048  264 LYS A O   
3630 C CB  . LYS A 245 ? 0.3737 0.2712 0.1834 0.0609  -0.0932 0.0173  264 LYS A CB  
3631 C CG  . LYS A 245 ? 0.4117 0.2860 0.1946 0.0542  -0.1139 0.0198  264 LYS A CG  
3632 C CD  . LYS A 245 ? 0.4445 0.3053 0.2028 0.0637  -0.1286 0.0235  264 LYS A CD  
3633 C CE  . LYS A 245 ? 0.4724 0.3287 0.2257 0.0603  -0.1252 0.0153  264 LYS A CE  
3634 N NZ  . LYS A 245 ? 0.4902 0.3547 0.2445 0.0588  -0.1379 0.0130  264 LYS A NZ  
3648 N N   . GLU A 246 ? 0.3137 0.2548 0.1591 0.0393  -0.0206 0.0204  265 GLU A N   
3649 C CA  . GLU A 246 ? 0.3165 0.2650 0.1560 0.0380  -0.0061 0.0276  265 GLU A CA  
3650 C C   . GLU A 246 ? 0.2691 0.2434 0.1542 0.0201  -0.0027 0.0273  265 GLU A C   
3651 O O   . GLU A 246 ? 0.2696 0.2304 0.1637 0.0292  0.0072  0.0208  265 GLU A O   
3652 C CB  . GLU A 246 ? 0.3519 0.2890 0.1492 0.0363  0.0052  0.0316  265 GLU A CB  
3653 C CG  . GLU A 246 ? 0.3950 0.3124 0.1514 0.0306  -0.0217 0.0203  265 GLU A CG  
3654 C CD  . GLU A 246 ? 0.4233 0.3246 0.1620 0.0508  -0.0408 0.0239  265 GLU A CD  
3655 O OE1 . GLU A 246 ? 0.4080 0.2983 0.1651 0.0441  -0.0512 0.0256  265 GLU A OE1 
3656 O OE2 . GLU A 246 ? 0.4721 0.3429 0.1809 0.0654  -0.0494 0.0268  265 GLU A OE2 
3663 N N   . THR A 247 ? 0.2356 0.2405 0.1511 0.0209  -0.0101 0.0189  266 THR A N   
3664 C CA  . THR A 247 ? 0.2215 0.2247 0.1460 0.0196  -0.0012 0.0240  266 THR A CA  
3665 C C   . THR A 247 ? 0.2103 0.2108 0.1400 0.0321  -0.0105 0.0223  266 THR A C   
3666 O O   . THR A 247 ? 0.2242 0.1961 0.1522 0.0491  -0.0198 0.0208  266 THR A O   
3667 C CB  . THR A 247 ? 0.2284 0.2334 0.1602 0.0186  0.0022  0.0229  266 THR A CB  
3668 O OG1 . THR A 247 ? 0.2211 0.2294 0.1645 0.0251  -0.0217 0.0187  266 THR A OG1 
3669 C CG2 . THR A 247 ? 0.2375 0.2450 0.1681 0.0173  0.0078  0.0247  266 THR A CG2 
3677 N N   . MET A 248 ? 0.2040 0.2123 0.1403 0.0247  -0.0043 0.0317  267 MET A N   
3678 C CA  . MET A 248 ? 0.1597 0.2060 0.1606 0.0458  -0.0121 0.0143  267 MET A CA  
3679 C C   . MET A 248 ? 0.1982 0.2096 0.1453 0.0426  -0.0121 -0.0098 267 MET A C   
3680 O O   . MET A 248 ? 0.1861 0.2200 0.1395 0.0279  -0.0285 -0.0027 267 MET A O   
3681 C CB  . MET A 248 ? 0.1845 0.2109 0.1671 0.0263  -0.0106 -0.0049 267 MET A CB  
3682 C CG  . MET A 248 ? 0.1845 0.2139 0.1743 0.0283  -0.0195 -0.0027 267 MET A CG  
3683 S SD  . MET A 248 ? 0.1868 0.2275 0.1936 0.0168  -0.0389 0.0002  267 MET A SD  
3684 C CE  . MET A 248 ? 0.2121 0.2497 0.2058 0.0141  -0.0317 -0.0061 267 MET A CE  
3694 N N   . LEU A 249 ? 0.2083 0.2202 0.1444 0.0445  -0.0039 -0.0178 268 LEU A N   
3695 C CA  . LEU A 249 ? 0.2297 0.2339 0.1510 0.0494  -0.0062 -0.0138 268 LEU A CA  
3696 C C   . LEU A 249 ? 0.2024 0.2289 0.1427 0.0537  -0.0096 0.0020  268 LEU A C   
3697 O O   . LEU A 249 ? 0.2103 0.2303 0.1473 0.0485  -0.0068 -0.0059 268 LEU A O   
3698 C CB  . LEU A 249 ? 0.2362 0.2586 0.1543 0.0338  -0.0076 -0.0205 268 LEU A CB  
3699 C CG  . LEU A 249 ? 0.2484 0.2760 0.1481 0.0310  0.0012  -0.0257 268 LEU A CG  
3700 C CD1 . LEU A 249 ? 0.2301 0.2735 0.1578 0.0252  -0.0174 -0.0273 268 LEU A CD1 
3701 C CD2 . LEU A 249 ? 0.2743 0.2956 0.1522 0.0351  0.0103  -0.0419 268 LEU A CD2 
3713 N N   A ARG A 250 ? 0.2120 0.2409 0.1422 0.0403  0.0128  0.0082  269 ARG A N   
3714 N N   B ARG A 250 ? 0.2089 0.2370 0.1509 0.0382  0.0039  0.0024  269 ARG A N   
3715 C CA  A ARG A 250 ? 0.1943 0.2405 0.1398 0.0288  0.0145  0.0242  269 ARG A CA  
3716 C CA  B ARG A 250 ? 0.1956 0.2357 0.1564 0.0232  0.0017  0.0094  269 ARG A CA  
3717 C C   A ARG A 250 ? 0.1974 0.2300 0.1450 0.0224  0.0139  0.0189  269 ARG A C   
3718 C C   B ARG A 250 ? 0.1955 0.2262 0.1525 0.0222  0.0075  0.0101  269 ARG A C   
3719 O O   A ARG A 250 ? 0.1860 0.2294 0.1512 0.0228  -0.0048 0.0213  269 ARG A O   
3720 O O   B ARG A 250 ? 0.1838 0.2232 0.1569 0.0256  -0.0056 0.0071  269 ARG A O   
3721 C CB  A ARG A 250 ? 0.2174 0.2600 0.1365 0.0231  0.0244  0.0451  269 ARG A CB  
3722 C CB  B ARG A 250 ? 0.2122 0.2504 0.1675 0.0091  0.0018  0.0150  269 ARG A CB  
3723 C CG  A ARG A 250 ? 0.2442 0.2697 0.1371 0.0098  0.0439  0.0563  269 ARG A CG  
3724 C CG  B ARG A 250 ? 0.2299 0.2590 0.1811 -0.0082 0.0112  0.0130  269 ARG A CG  
3725 C CD  A ARG A 250 ? 0.2659 0.2916 0.1542 0.0112  0.0494  0.0549  269 ARG A CD  
3726 C CD  B ARG A 250 ? 0.2505 0.2691 0.1975 0.0022  0.0194  0.0070  269 ARG A CD  
3727 N NE  A ARG A 250 ? 0.2655 0.2883 0.1606 0.0249  0.0538  0.0529  269 ARG A NE  
3728 N NE  B ARG A 250 ? 0.2340 0.2694 0.2106 0.0101  0.0234  0.0128  269 ARG A NE  
3729 C CZ  A ARG A 250 ? 0.2937 0.2896 0.1574 0.0299  0.0467  0.0661  269 ARG A CZ  
3730 C CZ  B ARG A 250 ? 0.2547 0.2735 0.2378 0.0085  0.0189  0.0173  269 ARG A CZ  
3731 N NH1 A ARG A 250 ? 0.3356 0.3015 0.1742 0.0326  0.0158  0.0617  269 ARG A NH1 
3732 N NH1 B ARG A 250 ? 0.2480 0.2656 0.2563 0.0036  -0.0111 0.0353  269 ARG A NH1 
3733 N NH2 A ARG A 250 ? 0.2469 0.2664 0.1469 0.0202  0.0681  0.0782  269 ARG A NH2 
3734 N NH2 B ARG A 250 ? 0.2791 0.2698 0.2407 0.0131  0.0212  0.0199  269 ARG A NH2 
3761 N N   . ASP A 251 ? 0.1783 0.2138 0.1458 0.0245  0.0140  0.0222  270 ASP A N   
3762 C CA  . ASP A 251 ? 0.1789 0.1928 0.1415 0.0199  0.0044  0.0101  270 ASP A CA  
3763 C C   . ASP A 251 ? 0.1746 0.1939 0.1354 0.0281  0.0041  -0.0109 270 ASP A C   
3764 O O   . ASP A 251 ? 0.1605 0.1873 0.1415 0.0102  -0.0101 0.0010  270 ASP A O   
3765 C CB  . ASP A 251 ? 0.1765 0.2060 0.1564 0.0207  0.0139  0.0081  270 ASP A CB  
3766 C CG  . ASP A 251 ? 0.1733 0.2000 0.1582 0.0271  0.0085  0.0174  270 ASP A CG  
3767 O OD1 . ASP A 251 ? 0.1979 0.2053 0.1591 0.0296  0.0063  0.0160  270 ASP A OD1 
3768 O OD2 . ASP A 251 ? 0.1701 0.1897 0.1605 0.0168  -0.0172 0.0092  270 ASP A OD2 
3773 N N   . ILE A 252 ? 0.1781 0.1859 0.1355 0.0261  -0.0121 -0.0102 271 ILE A N   
3774 C CA  . ILE A 252 ? 0.1809 0.1841 0.1409 0.0225  0.0023  -0.0139 271 ILE A CA  
3775 C C   . ILE A 252 ? 0.2127 0.1946 0.1455 0.0319  -0.0115 -0.0139 271 ILE A C   
3776 O O   . ILE A 252 ? 0.2058 0.2039 0.1467 0.0409  -0.0148 -0.0192 271 ILE A O   
3777 C CB  . ILE A 252 ? 0.1803 0.1901 0.1466 0.0252  -0.0027 -0.0132 271 ILE A CB  
3778 C CG1 . ILE A 252 ? 0.1857 0.2116 0.1533 0.0095  -0.0192 -0.0093 271 ILE A CG1 
3779 C CG2 . ILE A 252 ? 0.1905 0.1887 0.1492 0.0072  -0.0095 -0.0194 271 ILE A CG2 
3780 C CD1 . ILE A 252 ? 0.2171 0.2142 0.1588 -0.0071 -0.0210 -0.0070 271 ILE A CD1 
3792 N N   . LEU A 253 ? 0.2246 0.1990 0.1369 0.0323  0.0058  -0.0118 272 LEU A N   
3793 C CA  . LEU A 253 ? 0.1949 0.2069 0.1354 0.0266  0.0073  -0.0095 272 LEU A CA  
3794 C C   . LEU A 253 ? 0.1757 0.1933 0.1378 0.0329  0.0057  0.0007  272 LEU A C   
3795 O O   . LEU A 253 ? 0.1819 0.1854 0.1512 0.0466  0.0034  0.0065  272 LEU A O   
3796 C CB  . LEU A 253 ? 0.2014 0.2228 0.1499 0.0331  0.0090  -0.0111 272 LEU A CB  
3797 C CG  . LEU A 253 ? 0.2323 0.2272 0.1565 0.0360  -0.0058 -0.0181 272 LEU A CG  
3798 C CD1 . LEU A 253 ? 0.2477 0.2364 0.1553 0.0501  0.0206  -0.0065 272 LEU A CD1 
3799 C CD2 . LEU A 253 ? 0.2399 0.2284 0.1669 0.0377  -0.0141 -0.0268 272 LEU A CD2 
3811 N N   . GLU A 254 ? 0.1657 0.1834 0.1381 0.0058  0.0121  -0.0054 273 GLU A N   
3812 C CA  . GLU A 254 ? 0.1823 0.1859 0.1350 0.0011  0.0214  0.0015  273 GLU A CA  
3813 C C   . GLU A 254 ? 0.1590 0.1890 0.1380 0.0167  0.0226  0.0059  273 GLU A C   
3814 O O   . GLU A 254 ? 0.1625 0.1837 0.1450 0.0204  0.0242  0.0026  273 GLU A O   
3815 C CB  . GLU A 254 ? 0.1924 0.2005 0.1467 -0.0016 0.0320  -0.0059 273 GLU A CB  
3816 C CG  . GLU A 254 ? 0.1849 0.2191 0.1647 -0.0064 0.0264  -0.0117 273 GLU A CG  
3817 C CD  . GLU A 254 ? 0.1963 0.2371 0.1951 0.0008  0.0041  -0.0272 273 GLU A CD  
3818 O OE1 . GLU A 254 ? 0.1624 0.2501 0.1993 -0.0110 0.0106  -0.0394 273 GLU A OE1 
3819 O OE2 . GLU A 254 ? 0.2054 0.2505 0.2226 0.0293  -0.0117 -0.0346 273 GLU A OE2 
3826 N N   . MET A 255 ? 0.1565 0.1839 0.1253 0.0032  0.0181  0.0091  274 MET A N   
3827 C CA  . MET A 255 ? 0.1493 0.1834 0.1362 0.0065  0.0179  -0.0051 274 MET A CA  
3828 C C   . MET A 255 ? 0.1355 0.1783 0.1399 0.0165  0.0070  -0.0068 274 MET A C   
3829 O O   . MET A 255 ? 0.1443 0.1922 0.1396 0.0082  0.0072  -0.0057 274 MET A O   
3830 C CB  . MET A 255 ? 0.1461 0.1843 0.1463 0.0046  0.0140  -0.0064 274 MET A CB  
3831 C CG  . MET A 255 ? 0.1321 0.1876 0.1650 0.0129  0.0227  -0.0031 274 MET A CG  
3832 S SD  . MET A 255 ? 0.1717 0.1884 0.1686 0.0045  0.0103  0.0032  274 MET A SD  
3833 C CE  . MET A 255 ? 0.1622 0.1763 0.1954 0.0036  0.0065  0.0020  274 MET A CE  
3843 N N   . GLN A 256 ? 0.1511 0.1737 0.1471 0.0381  -0.0087 -0.0186 275 GLN A N   
3844 C CA  . GLN A 256 ? 0.1553 0.1910 0.1610 0.0349  0.0123  -0.0193 275 GLN A CA  
3845 C C   . GLN A 256 ? 0.1516 0.2012 0.1597 0.0335  0.0117  -0.0126 275 GLN A C   
3846 O O   . GLN A 256 ? 0.1684 0.2163 0.1655 0.0318  -0.0024 -0.0141 275 GLN A O   
3847 C CB  . GLN A 256 ? 0.1901 0.2061 0.1681 0.0223  -0.0074 -0.0212 275 GLN A CB  
3848 C CG  . GLN A 256 ? 0.2012 0.1987 0.1623 0.0015  -0.0225 -0.0192 275 GLN A CG  
3849 C CD  . GLN A 256 ? 0.2353 0.2231 0.1757 0.0137  -0.0140 -0.0259 275 GLN A CD  
3850 O OE1 . GLN A 256 ? 0.2549 0.2190 0.1811 -0.0046 -0.0260 -0.0281 275 GLN A OE1 
3851 N NE2 . GLN A 256 ? 0.2290 0.2314 0.1682 0.0250  -0.0233 -0.0273 275 GLN A NE2 
3860 N N   . ARG A 257 ? 0.1540 0.1940 0.1463 0.0334  0.0211  -0.0114 276 ARG A N   
3861 C CA  . ARG A 257 ? 0.1699 0.2042 0.1359 0.0336  0.0355  -0.0068 276 ARG A CA  
3862 C C   . ARG A 257 ? 0.1703 0.1929 0.1498 0.0283  0.0175  -0.0106 276 ARG A C   
3863 O O   . ARG A 257 ? 0.1723 0.1825 0.1685 0.0228  0.0143  -0.0154 276 ARG A O   
3864 C CB  . ARG A 257 ? 0.1975 0.2254 0.1461 0.0268  0.0380  -0.0029 276 ARG A CB  
3865 C CG  . ARG A 257 ? 0.1854 0.2391 0.1484 0.0427  0.0504  -0.0163 276 ARG A CG  
3866 C CD  . ARG A 257 ? 0.2002 0.2552 0.1576 0.0532  0.0522  -0.0081 276 ARG A CD  
3867 N NE  . ARG A 257 ? 0.2198 0.2685 0.1742 0.0362  0.0377  0.0039  276 ARG A NE  
3868 C CZ  . ARG A 257 ? 0.1948 0.2850 0.2043 0.0241  0.0375  -0.0061 276 ARG A CZ  
3869 N NH1 . ARG A 257 ? 0.2056 0.3078 0.2150 0.0167  0.0252  -0.0206 276 ARG A NH1 
3870 N NH2 . ARG A 257 ? 0.2166 0.2899 0.2104 0.0201  0.0416  -0.0065 276 ARG A NH2 
3884 N N   . ALA A 258 ? 0.1625 0.1926 0.1351 0.0307  0.0157  -0.0062 277 ALA A N   
3885 C CA  . ALA A 258 ? 0.1596 0.2009 0.1382 0.0296  0.0142  -0.0026 277 ALA A CA  
3886 C C   . ALA A 258 ? 0.1288 0.1934 0.1389 0.0311  0.0350  -0.0258 277 ALA A C   
3887 O O   . ALA A 258 ? 0.1384 0.2106 0.1403 0.0102  0.0093  -0.0169 277 ALA A O   
3888 C CB  . ALA A 258 ? 0.1750 0.1962 0.1449 0.0353  0.0093  0.0159  277 ALA A CB  
3894 N N   . ALA A 259 ? 0.1230 0.1922 0.1356 0.0114  0.0257  -0.0118 278 ALA A N   
3895 C CA  . ALA A 259 ? 0.1364 0.1997 0.1486 0.0246  0.0149  -0.0129 278 ALA A CA  
3896 C C   . ALA A 259 ? 0.1554 0.2185 0.1607 0.0374  0.0120  -0.0196 278 ALA A C   
3897 O O   . ALA A 259 ? 0.1815 0.2282 0.1805 0.0559  0.0143  -0.0086 278 ALA A O   
3898 C CB  . ALA A 259 ? 0.1372 0.1892 0.1618 0.0037  0.0238  -0.0149 278 ALA A CB  
3904 N N   . LYS A 260 ? 0.1626 0.2233 0.1641 0.0559  0.0209  -0.0266 279 LYS A N   
3905 C CA  . LYS A 260 ? 0.1930 0.2389 0.1750 0.0751  0.0320  -0.0370 279 LYS A CA  
3906 C C   . LYS A 260 ? 0.1924 0.2550 0.1864 0.0890  0.0281  -0.0310 279 LYS A C   
3907 O O   . LYS A 260 ? 0.2071 0.2779 0.2111 0.0792  0.0237  -0.0268 279 LYS A O   
3908 C CB  . LYS A 260 ? 0.2485 0.2555 0.1860 0.0928  0.0391  -0.0493 279 LYS A CB  
3909 C CG  . LYS A 260 ? 0.2963 0.2765 0.2078 0.0788  0.0306  -0.0497 279 LYS A CG  
3910 C CD  . LYS A 260 ? 0.3361 0.2989 0.2395 0.0481  0.0170  -0.0632 279 LYS A CD  
3911 C CE  . LYS A 260 ? 0.3884 0.3194 0.2709 0.0410  0.0144  -0.0742 279 LYS A CE  
3912 N NZ  . LYS A 260 ? 0.4315 0.3344 0.3102 0.0355  0.0194  -0.0765 279 LYS A NZ  
3926 N N   . ALA A 261 ? 0.1621 0.2609 0.1797 0.0584  0.0229  -0.0203 280 ALA A N   
3927 C CA  . ALA A 261 ? 0.1690 0.2764 0.1978 0.0500  0.0384  -0.0185 280 ALA A CA  
3928 C C   . ALA A 261 ? 0.1682 0.2767 0.1994 0.0274  0.0101  -0.0204 280 ALA A C   
3929 O O   . ALA A 261 ? 0.2035 0.3245 0.2163 -0.0050 -0.0005 -0.0058 280 ALA A O   
3930 C CB  . ALA A 261 ? 0.1905 0.2887 0.2159 0.0441  0.0500  -0.0223 280 ALA A CB  
3936 N N   . GLY A 262 ? 0.1536 0.2356 0.1759 0.0478  0.0156  -0.0303 281 GLY A N   
3937 C CA  . GLY A 262 ? 0.1495 0.2115 0.1704 0.0504  0.0072  -0.0251 281 GLY A CA  
3938 C C   . GLY A 262 ? 0.1281 0.1984 0.1692 0.0378  0.0233  -0.0150 281 GLY A C   
3939 O O   . GLY A 262 ? 0.1714 0.2070 0.1858 0.0415  -0.0097 -0.0166 281 GLY A O   
3943 N N   . LYS A 263 ? 0.1229 0.1926 0.1570 0.0284  0.0223  -0.0115 282 LYS A N   
3944 C CA  . LYS A 263 ? 0.1158 0.1592 0.1697 0.0176  0.0307  0.0063  282 LYS A CA  
3945 C C   . LYS A 263 ? 0.1178 0.1619 0.1617 0.0246  0.0151  -0.0060 282 LYS A C   
3946 O O   . LYS A 263 ? 0.1433 0.1556 0.1610 0.0179  0.0235  -0.0119 282 LYS A O   
3947 C CB  . LYS A 263 ? 0.1311 0.1696 0.1669 0.0131  0.0240  0.0105  282 LYS A CB  
3948 C CG  . LYS A 263 ? 0.1693 0.1939 0.2001 -0.0002 0.0210  0.0151  282 LYS A CG  
3949 C CD  . LYS A 263 ? 0.1678 0.1889 0.1992 -0.0009 0.0329  0.0188  282 LYS A CD  
3950 C CE  . LYS A 263 ? 0.1805 0.1828 0.2022 -0.0013 0.0468  -0.0222 282 LYS A CE  
3951 N NZ  . LYS A 263 ? 0.1953 0.1994 0.2104 -0.0023 0.0464  -0.0250 282 LYS A NZ  
3965 N N   . ILE A 264 ? 0.1097 0.1531 0.1561 0.0259  0.0225  -0.0057 283 ILE A N   
3966 C CA  . ILE A 264 ? 0.1073 0.1492 0.1433 0.0129  0.0329  0.0062  283 ILE A CA  
3967 C C   . ILE A 264 ? 0.1067 0.1451 0.1380 -0.0021 0.0193  -0.0003 283 ILE A C   
3968 O O   . ILE A 264 ? 0.1157 0.1606 0.1501 -0.0075 0.0035  0.0150  283 ILE A O   
3969 C CB  . ILE A 264 ? 0.1247 0.1478 0.1317 0.0104  0.0180  -0.0082 283 ILE A CB  
3970 C CG1 . ILE A 264 ? 0.1395 0.1587 0.1196 -0.0060 0.0044  0.0119  283 ILE A CG1 
3971 C CG2 . ILE A 264 ? 0.1408 0.1556 0.1308 -0.0068 0.0217  -0.0310 283 ILE A CG2 
3972 C CD1 . ILE A 264 ? 0.1533 0.1745 0.1252 0.0020  -0.0126 0.0094  283 ILE A CD1 
3984 N N   . VAL A 265 ? 0.1019 0.1471 0.1408 0.0037  0.0043  0.0021  284 VAL A N   
3985 C CA  . VAL A 265 ? 0.0988 0.1702 0.1392 -0.0239 -0.0002 0.0089  284 VAL A CA  
3986 C C   . VAL A 265 ? 0.1136 0.1684 0.1511 -0.0494 0.0332  0.0214  284 VAL A C   
3987 O O   . VAL A 265 ? 0.0978 0.1594 0.1495 -0.0005 0.0129  0.0145  284 VAL A O   
3988 C CB  . VAL A 265 ? 0.1200 0.1827 0.1418 -0.0011 -0.0086 0.0017  284 VAL A CB  
3989 C CG1 . VAL A 265 ? 0.1350 0.1770 0.1487 0.0025  -0.0109 0.0010  284 VAL A CG1 
3990 C CG2 . VAL A 265 ? 0.1393 0.2092 0.1434 0.0197  0.0009  -0.0075 284 VAL A CG2 
4007 N N   . LEU A 267 ? 0.1210 0.1509 0.1622 0.0737  0.0102  0.0127  286 LEU A N   
4008 C CA  . LEU A 267 ? 0.1177 0.1594 0.1623 0.0173  0.0103  -0.0012 286 LEU A CA  
4009 C C   . LEU A 267 ? 0.0933 0.1713 0.1668 -0.0332 0.0035  -0.0193 286 LEU A C   
4010 O O   . LEU A 267 ? 0.1141 0.1480 0.1642 -0.0001 0.0063  -0.0204 286 LEU A O   
4011 C CB  . LEU A 267 ? 0.1309 0.1576 0.1757 0.0211  -0.0031 0.0002  286 LEU A CB  
4012 C CG  . LEU A 267 ? 0.1343 0.1649 0.1760 0.0227  -0.0141 0.0066  286 LEU A CG  
4013 C CD1 . LEU A 267 ? 0.1844 0.1703 0.1606 0.0181  -0.0255 0.0138  286 LEU A CD1 
4014 C CD2 . LEU A 267 ? 0.1419 0.1771 0.1754 0.0327  -0.0350 0.0169  286 LEU A CD2 
4035 N N   . GLY A 269 ? 0.1329 0.1861 0.2029 0.0457  -0.0294 0.0241  288 GLY A N   
4036 C CA  . GLY A 269 ? 0.1219 0.1700 0.1982 0.0531  0.0004  0.0031  288 GLY A CA  
4037 C C   . GLY A 269 ? 0.1232 0.1593 0.1839 0.0302  0.0022  0.0033  288 GLY A C   
4038 O O   . GLY A 269 ? 0.1249 0.1728 0.1784 0.0115  -0.0128 -0.0094 288 GLY A O   
4042 N N   . TRP A 270 ? 0.1069 0.1516 0.1733 0.0200  -0.0132 -0.0006 289 TRP A N   
4043 C CA  . TRP A 270 ? 0.1021 0.1567 0.1837 0.0196  0.0004  0.0030  289 TRP A CA  
4044 C C   . TRP A 270 ? 0.0917 0.1589 0.1826 0.0104  0.0076  0.0071  289 TRP A C   
4045 O O   . TRP A 270 ? 0.1180 0.1805 0.1915 -0.0018 0.0117  -0.0040 289 TRP A O   
4046 C CB  . TRP A 270 ? 0.1266 0.1615 0.1844 0.0364  0.0005  0.0159  289 TRP A CB  
4047 C CG  . TRP A 270 ? 0.1124 0.1521 0.1675 0.0263  -0.0013 0.0215  289 TRP A CG  
4048 C CD1 . TRP A 270 ? 0.1069 0.1359 0.1583 0.0071  0.0089  0.0137  289 TRP A CD1 
4049 C CD2 . TRP A 270 ? 0.1072 0.1493 0.1610 0.0274  0.0158  0.0082  289 TRP A CD2 
4050 N NE1 . TRP A 270 ? 0.1238 0.1483 0.1507 -0.0020 0.0002  0.0008  289 TRP A NE1 
4051 C CE2 . TRP A 270 ? 0.1310 0.1453 0.1588 0.0171  0.0133  0.0059  289 TRP A CE2 
4052 C CE3 . TRP A 270 ? 0.1280 0.1579 0.1656 0.0120  0.0180  0.0065  289 TRP A CE3 
4053 C CZ2 . TRP A 270 ? 0.1254 0.1610 0.1657 0.0217  0.0104  0.0120  289 TRP A CZ2 
4054 C CZ3 . TRP A 270 ? 0.1350 0.1562 0.1751 0.0141  0.0173  -0.0137 289 TRP A CZ3 
4055 C CH2 . TRP A 270 ? 0.1388 0.1538 0.1748 0.0011  0.0102  -0.0042 289 TRP A CH2 
4066 N N   . ALA A 271 ? 0.1004 0.1509 0.1835 -0.0106 0.0177  0.0041  290 ALA A N   
4067 C CA  . ALA A 271 ? 0.1201 0.1686 0.1885 -0.0069 0.0096  0.0078  290 ALA A CA  
4068 C C   . ALA A 271 ? 0.1312 0.1713 0.1966 0.0133  0.0101  0.0042  290 ALA A C   
4069 O O   . ALA A 271 ? 0.1362 0.1716 0.2059 0.0074  0.0092  -0.0131 290 ALA A O   
4070 C CB  . ALA A 271 ? 0.1411 0.1746 0.1920 -0.0026 0.0225  0.0002  290 ALA A CB  
4076 N N   . GLY A 272 ? 0.1418 0.1621 0.1948 0.0037  -0.0018 0.0095  291 GLY A N   
4077 C CA  . GLY A 272 ? 0.1479 0.1751 0.1974 0.0075  -0.0285 0.0169  291 GLY A CA  
4078 C C   . GLY A 272 ? 0.1410 0.1825 0.1945 0.0238  -0.0288 0.0164  291 GLY A C   
4079 O O   . GLY A 272 ? 0.1970 0.1925 0.2024 0.0178  -0.0522 0.0037  291 GLY A O   
4083 N N   . PHE A 273 ? 0.1327 0.1735 0.1904 0.0114  -0.0083 0.0058  292 PHE A N   
4084 C CA  . PHE A 273 ? 0.1257 0.1695 0.1804 0.0002  -0.0033 0.0041  292 PHE A CA  
4085 C C   . PHE A 273 ? 0.1180 0.1600 0.1825 0.0173  0.0012  0.0185  292 PHE A C   
4086 O O   . PHE A 273 ? 0.1180 0.1472 0.1802 0.0133  0.0052  0.0191  292 PHE A O   
4087 C CB  . PHE A 273 ? 0.1263 0.1648 0.1827 -0.0089 -0.0098 0.0172  292 PHE A CB  
4088 C CG  . PHE A 273 ? 0.1275 0.1629 0.1780 -0.0126 0.0076  0.0137  292 PHE A CG  
4089 C CD1 . PHE A 273 ? 0.1195 0.1613 0.1777 -0.0184 0.0216  -0.0071 292 PHE A CD1 
4090 C CD2 . PHE A 273 ? 0.1206 0.1559 0.1806 -0.0023 0.0045  0.0275  292 PHE A CD2 
4091 C CE1 . PHE A 273 ? 0.1178 0.1663 0.1980 -0.0194 0.0224  -0.0015 292 PHE A CE1 
4092 C CE2 . PHE A 273 ? 0.1154 0.1769 0.1862 -0.0132 -0.0130 0.0110  292 PHE A CE2 
4093 C CZ  . PHE A 273 ? 0.1210 0.1805 0.1890 -0.0093 0.0115  0.0111  292 PHE A CZ  
4103 N N   . THR A 274 ? 0.1184 0.1584 0.1936 0.0051  -0.0132 0.0120  293 THR A N   
4104 C CA  . THR A 274 ? 0.1361 0.1611 0.1864 0.0066  -0.0227 0.0193  293 THR A CA  
4105 C C   . THR A 274 ? 0.1279 0.1656 0.1825 0.0094  -0.0186 0.0337  293 THR A C   
4106 O O   . THR A 274 ? 0.1213 0.1784 0.1698 -0.0103 -0.0029 0.0498  293 THR A O   
4107 C CB  . THR A 274 ? 0.1519 0.1607 0.1874 0.0016  -0.0031 0.0147  293 THR A CB  
4108 O OG1 . THR A 274 ? 0.1437 0.1580 0.1920 -0.0082 0.0030  0.0352  293 THR A OG1 
4109 C CG2 . THR A 274 ? 0.1504 0.1672 0.1841 -0.0092 -0.0031 0.0024  293 THR A CG2 
4117 N N   . PHE A 275 ? 0.1428 0.1614 0.1863 -0.0086 -0.0246 0.0351  294 PHE A N   
4118 C CA  . PHE A 275 ? 0.1557 0.1613 0.1909 -0.0069 -0.0196 0.0168  294 PHE A CA  
4119 C C   . PHE A 275 ? 0.1364 0.1580 0.1908 0.0058  0.0034  0.0165  294 PHE A C   
4120 O O   . PHE A 275 ? 0.1824 0.1641 0.1936 -0.0008 0.0178  0.0173  294 PHE A O   
4121 C CB  . PHE A 275 ? 0.1884 0.1674 0.2013 -0.0237 -0.0397 0.0196  294 PHE A CB  
4122 C CG  . PHE A 275 ? 0.1747 0.1687 0.2151 -0.0173 -0.0437 0.0146  294 PHE A CG  
4123 C CD1 . PHE A 275 ? 0.1741 0.1885 0.2360 -0.0236 -0.0424 0.0133  294 PHE A CD1 
4124 C CD2 . PHE A 275 ? 0.1938 0.1794 0.2324 -0.0195 -0.0352 0.0035  294 PHE A CD2 
4125 C CE1 . PHE A 275 ? 0.1765 0.1801 0.2461 -0.0255 -0.0511 0.0222  294 PHE A CE1 
4126 C CE2 . PHE A 275 ? 0.1983 0.1787 0.2466 -0.0194 -0.0387 0.0074  294 PHE A CE2 
4127 C CZ  . PHE A 275 ? 0.1918 0.1794 0.2460 -0.0078 -0.0473 0.0149  294 PHE A CZ  
4137 N N   . ILE A 276 ? 0.1436 0.1523 0.1895 -0.0026 0.0065  0.0349  295 ILE A N   
4138 C CA  . ILE A 276 ? 0.1376 0.1549 0.1924 -0.0062 -0.0069 0.0434  295 ILE A CA  
4139 C C   . ILE A 276 ? 0.1222 0.1493 0.1915 -0.0004 -0.0075 0.0214  295 ILE A C   
4140 O O   . ILE A 276 ? 0.1497 0.1554 0.1957 -0.0057 -0.0070 0.0281  295 ILE A O   
4141 C CB  . ILE A 276 ? 0.1557 0.1721 0.2012 -0.0191 -0.0032 0.0297  295 ILE A CB  
4142 C CG1 . ILE A 276 ? 0.1466 0.1838 0.1989 -0.0115 0.0141  0.0441  295 ILE A CG1 
4143 C CG2 . ILE A 276 ? 0.1367 0.1886 0.2137 -0.0323 -0.0037 0.0256  295 ILE A CG2 
4144 C CD1 . ILE A 276 ? 0.1539 0.1944 0.2015 -0.0083 0.0161  0.0358  295 ILE A CD1 
4156 N N   . ASP A 277 ? 0.1327 0.1579 0.1855 -0.0089 0.0018  0.0202  296 ASP A N   
4157 C CA  . ASP A 277 ? 0.1406 0.1688 0.1850 0.0109  0.0065  0.0229  296 ASP A CA  
4158 C C   . ASP A 277 ? 0.1356 0.1550 0.1926 0.0151  0.0076  0.0337  296 ASP A C   
4159 O O   . ASP A 277 ? 0.1481 0.1569 0.1933 0.0012  0.0063  0.0332  296 ASP A O   
4160 C CB  . ASP A 277 ? 0.1490 0.1713 0.1855 0.0265  0.0036  0.0203  296 ASP A CB  
4161 C CG  . ASP A 277 ? 0.1579 0.1623 0.1811 0.0257  0.0050  0.0364  296 ASP A CG  
4162 O OD1 . ASP A 277 ? 0.1680 0.1681 0.1879 0.0322  0.0283  0.0295  296 ASP A OD1 
4163 O OD2 . ASP A 277 ? 0.1592 0.1693 0.1764 0.0279  0.0121  0.0463  296 ASP A OD2 
4168 N N   . ASP A 278 ? 0.1473 0.1676 0.2097 0.0263  0.0197  0.0426  297 ASP A N   
4169 C CA  . ASP A 278 ? 0.1605 0.1670 0.2233 0.0365  0.0347  0.0371  297 ASP A CA  
4170 C C   . ASP A 278 ? 0.1555 0.1757 0.2230 0.0317  0.0175  0.0486  297 ASP A C   
4171 O O   . ASP A 278 ? 0.1555 0.1877 0.2235 0.0250  0.0316  0.0523  297 ASP A O   
4172 C CB  . ASP A 278 ? 0.1936 0.1779 0.2534 0.0314  0.0564  0.0279  297 ASP A CB  
4173 C CG  . ASP A 278 ? 0.2318 0.2065 0.2778 0.0120  0.0605  0.0320  297 ASP A CG  
4174 O OD1 . ASP A 278 ? 0.2658 0.2281 0.2967 0.0281  0.0541  0.0137  297 ASP A OD1 
4175 O OD2 . ASP A 278 ? 0.2541 0.2265 0.3091 0.0182  0.0752  0.0237  297 ASP A OD2 
4180 N N   A GLN A 279 ? 0.1476 0.1891 0.2187 0.0189  0.0199  0.0568  298 GLN A N   
4181 N N   B GLN A 279 ? 0.1580 0.1879 0.2229 0.0259  0.0069  0.0611  298 GLN A N   
4182 C CA  A GLN A 279 ? 0.1337 0.2079 0.2188 0.0067  0.0229  0.0412  298 GLN A CA  
4183 C CA  B GLN A 279 ? 0.1585 0.2043 0.2237 0.0180  -0.0016 0.0546  298 GLN A CA  
4184 C C   A GLN A 279 ? 0.1186 0.1944 0.2105 0.0097  0.0296  0.0404  298 GLN A C   
4185 C C   B GLN A 279 ? 0.1303 0.1928 0.2135 0.0154  0.0147  0.0451  298 GLN A C   
4186 O O   A GLN A 279 ? 0.1374 0.1903 0.2168 0.0014  0.0323  0.0428  298 GLN A O   
4187 O O   B GLN A 279 ? 0.1413 0.1907 0.2178 0.0072  0.0177  0.0437  298 GLN A O   
4188 C CB  A GLN A 279 ? 0.1311 0.2302 0.2217 0.0085  0.0311  0.0330  298 GLN A CB  
4189 C CB  B GLN A 279 ? 0.1890 0.2247 0.2327 0.0261  -0.0188 0.0588  298 GLN A CB  
4190 C CG  A GLN A 279 ? 0.1651 0.2664 0.2334 0.0193  0.0263  0.0114  298 GLN A CG  
4191 C CG  B GLN A 279 ? 0.2435 0.2559 0.2465 0.0303  -0.0382 0.0500  298 GLN A CG  
4192 C CD  A GLN A 279 ? 0.2212 0.3005 0.2586 0.0371  0.0202  -0.0084 298 GLN A CD  
4193 C CD  B GLN A 279 ? 0.3107 0.2807 0.2575 0.0232  -0.0523 0.0451  298 GLN A CD  
4194 O OE1 A GLN A 279 ? 0.2630 0.3231 0.2744 0.0395  0.0177  -0.0228 298 GLN A OE1 
4195 O OE1 B GLN A 279 ? 0.2974 0.3050 0.2591 0.0316  -0.0496 0.0318  298 GLN A OE1 
4196 N NE2 A GLN A 279 ? 0.2377 0.3206 0.2680 0.0500  0.0274  -0.0067 298 GLN A NE2 
4197 N NE2 B GLN A 279 ? 0.3715 0.2873 0.2718 0.0307  -0.0573 0.0338  298 GLN A NE2 
4214 N N   . ALA A 280 ? 0.1176 0.1740 0.2104 0.0164  0.0214  0.0356  299 ALA A N   
4215 C CA  . ALA A 280 ? 0.1186 0.1698 0.1962 0.0082  0.0059  0.0396  299 ALA A CA  
4216 C C   . ALA A 280 ? 0.1081 0.1625 0.1908 -0.0068 0.0106  0.0421  299 ALA A C   
4217 O O   . ALA A 280 ? 0.1230 0.1515 0.1960 -0.0134 0.0198  0.0265  299 ALA A O   
4218 C CB  . ALA A 280 ? 0.1176 0.1624 0.1883 0.0095  0.0177  0.0167  299 ALA A CB  
4224 N N   . MET A 281 ? 0.1275 0.1573 0.1899 -0.0033 0.0236  0.0397  300 MET A N   
4225 C CA  . MET A 281 ? 0.1612 0.1603 0.1891 -0.0177 0.0232  0.0292  300 MET A CA  
4226 C C   . MET A 281 ? 0.1640 0.1568 0.1936 -0.0073 0.0377  0.0189  300 MET A C   
4227 O O   . MET A 281 ? 0.1936 0.2005 0.1972 -0.0039 0.0440  0.0311  300 MET A O   
4228 C CB  . MET A 281 ? 0.1527 0.1648 0.1944 0.0025  0.0197  0.0305  300 MET A CB  
4229 C CG  . MET A 281 ? 0.1389 0.1827 0.2022 0.0054  -0.0139 0.0295  300 MET A CG  
4230 S SD  . MET A 281 ? 0.1745 0.1903 0.2057 0.0020  -0.0162 0.0419  300 MET A SD  
4231 C CE  . MET A 281 ? 0.2335 0.2059 0.2094 0.0069  0.0007  0.0531  300 MET A CE  
4241 N N   . ARG A 282 ? 0.1256 0.1717 0.2150 0.0223  0.0342  -0.0027 301 ARG A N   
4242 C CA  . ARG A 282 ? 0.1554 0.1881 0.2345 0.0229  0.0368  0.0028  301 ARG A CA  
4243 C C   . ARG A 282 ? 0.1534 0.1923 0.2234 0.0128  0.0293  0.0157  301 ARG A C   
4244 O O   . ARG A 282 ? 0.1942 0.1879 0.2315 0.0149  0.0556  0.0162  301 ARG A O   
4245 C CB  . ARG A 282 ? 0.1530 0.1968 0.2624 0.0154  0.0382  0.0021  301 ARG A CB  
4246 C CG  . ARG A 282 ? 0.1668 0.2183 0.3004 0.0071  0.0327  0.0045  301 ARG A CG  
4247 C CD  . ARG A 282 ? 0.1925 0.2311 0.3316 0.0097  0.0408  -0.0070 301 ARG A CD  
4248 N NE  . ARG A 282 ? 0.1963 0.2416 0.3618 -0.0007 0.0440  -0.0263 301 ARG A NE  
4249 C CZ  . ARG A 282 ? 0.2258 0.2750 0.3917 0.0292  0.0590  -0.0425 301 ARG A CZ  
4250 N NH1 . ARG A 282 ? 0.2763 0.2704 0.4087 0.0121  0.0529  -0.0454 301 ARG A NH1 
4251 N NH2 . ARG A 282 ? 0.2254 0.2927 0.4055 0.0502  0.0585  -0.0415 301 ARG A NH2 
4265 N N   . LYS A 283 ? 0.1242 0.1990 0.2104 0.0048  0.0281  0.0288  302 LYS A N   
4266 C CA  . LYS A 283 ? 0.1415 0.2016 0.1972 0.0031  0.0398  0.0111  302 LYS A CA  
4267 C C   . LYS A 283 ? 0.1245 0.1969 0.2048 0.0093  0.0168  0.0183  302 LYS A C   
4268 O O   . LYS A 283 ? 0.1214 0.2110 0.2134 0.0069  0.0111  0.0176  302 LYS A O   
4269 C CB  . LYS A 283 ? 0.1985 0.2128 0.1805 -0.0222 0.0552  0.0137  302 LYS A CB  
4270 C CG  . LYS A 283 ? 0.2834 0.2599 0.1778 -0.0452 0.0649  0.0045  302 LYS A CG  
4271 C CD  . LYS A 283 ? 0.3300 0.3199 0.2090 -0.0201 0.0556  -0.0192 302 LYS A CD  
4272 C CE  . LYS A 283 ? 0.3861 0.3643 0.2369 -0.0072 0.0266  -0.0493 302 LYS A CE  
4273 N NZ  . LYS A 283 ? 0.4273 0.4009 0.2526 0.0117  -0.0037 -0.0784 302 LYS A NZ  
4287 N N   . PRO A 284 ? 0.1165 0.1988 0.2089 0.0205  0.0131  0.0223  303 PRO A N   
4288 C CA  . PRO A 284 ? 0.1282 0.2088 0.2135 0.0164  0.0080  0.0223  303 PRO A CA  
4289 C C   . PRO A 284 ? 0.1207 0.2118 0.2044 0.0106  0.0201  0.0201  303 PRO A C   
4290 O O   . PRO A 284 ? 0.1223 0.2101 0.1918 0.0069  -0.0064 0.0085  303 PRO A O   
4291 C CB  . PRO A 284 ? 0.1384 0.2153 0.2186 0.0020  0.0200  0.0236  303 PRO A CB  
4292 C CG  . PRO A 284 ? 0.1289 0.2020 0.2178 0.0079  0.0239  0.0299  303 PRO A CG  
4293 C CD  . PRO A 284 ? 0.1193 0.2046 0.2127 0.0192  0.0191  0.0266  303 PRO A CD  
4301 N N   . LEU A 285 ? 0.1399 0.2001 0.2015 0.0201  0.0172  0.0408  304 LEU A N   
4302 C CA  . LEU A 285 ? 0.1430 0.2063 0.1982 0.0037  -0.0029 0.0495  304 LEU A CA  
4303 C C   . LEU A 285 ? 0.1254 0.2008 0.2057 -0.0101 0.0152  0.0531  304 LEU A C   
4304 O O   . LEU A 285 ? 0.1224 0.1827 0.2094 0.0103  0.0041  0.0400  304 LEU A O   
4305 C CB  . LEU A 285 ? 0.1720 0.2164 0.1986 -0.0165 -0.0239 0.0599  304 LEU A CB  
4306 C CG  . LEU A 285 ? 0.1845 0.2369 0.2010 -0.0023 -0.0120 0.0664  304 LEU A CG  
4307 C CD1 . LEU A 285 ? 0.1722 0.2478 0.2124 -0.0063 -0.0120 0.0471  304 LEU A CD1 
4308 C CD2 . LEU A 285 ? 0.1995 0.2615 0.2094 0.0142  -0.0117 0.0442  304 LEU A CD2 
4320 N N   . THR A 286 ? 0.1526 0.2025 0.2295 -0.0158 0.0221  0.0534  305 THR A N   
4321 C CA  . THR A 286 ? 0.1489 0.2145 0.2427 -0.0094 0.0364  0.0504  305 THR A CA  
4322 C C   . THR A 286 ? 0.1301 0.1967 0.2474 0.0151  0.0208  0.0337  305 THR A C   
4323 O O   . THR A 286 ? 0.1711 0.2033 0.2698 0.0090  0.0176  0.0263  305 THR A O   
4324 C CB  . THR A 286 ? 0.1889 0.2578 0.2611 -0.0085 0.0194  0.0493  305 THR A CB  
4325 O OG1 . THR A 286 ? 0.1869 0.2814 0.2695 0.0178  0.0196  0.0577  305 THR A OG1 
4326 C CG2 . THR A 286 ? 0.2215 0.2817 0.2703 -0.0239 0.0046  0.0488  305 THR A CG2 
4334 N N   . GLN A 287 ? 0.1149 0.1961 0.2345 0.0063  0.0157  0.0351  306 GLN A N   
4335 C CA  . GLN A 287 ? 0.1135 0.1943 0.2280 0.0097  0.0061  0.0211  306 GLN A CA  
4336 C C   . GLN A 287 ? 0.1156 0.1737 0.2138 0.0119  0.0048  0.0192  306 GLN A C   
4337 O O   . GLN A 287 ? 0.1199 0.1754 0.2159 0.0069  0.0186  0.0042  306 GLN A O   
4338 C CB  . GLN A 287 ? 0.1286 0.2237 0.2366 0.0251  -0.0029 0.0084  306 GLN A CB  
4339 C CG  . GLN A 287 ? 0.1494 0.2572 0.2542 0.0544  -0.0229 -0.0064 306 GLN A CG  
4340 C CD  . GLN A 287 ? 0.1959 0.2849 0.2802 0.0446  -0.0219 -0.0200 306 GLN A CD  
4341 O OE1 . GLN A 287 ? 0.1758 0.2765 0.2983 0.0114  -0.0337 -0.0337 306 GLN A OE1 
4342 N NE2 . GLN A 287 ? 0.2136 0.3010 0.2841 0.0553  -0.0450 -0.0191 306 GLN A NE2 
4351 N N   . LYS A 288 ? 0.1118 0.1736 0.2086 -0.0106 0.0028  0.0274  307 LYS A N   
4352 C CA  . LYS A 288 ? 0.0947 0.1848 0.2006 0.0039  0.0042  0.0324  307 LYS A CA  
4353 C C   . LYS A 288 ? 0.1142 0.1837 0.2180 -0.0025 0.0163  0.0339  307 LYS A C   
4354 O O   . LYS A 288 ? 0.1165 0.1905 0.2141 0.0080  0.0168  0.0344  307 LYS A O   
4355 C CB  . LYS A 288 ? 0.0939 0.1928 0.1948 -0.0036 0.0175  0.0234  307 LYS A CB  
4356 C CG  . LYS A 288 ? 0.1115 0.1822 0.1927 -0.0032 0.0188  0.0271  307 LYS A CG  
4357 C CD  . LYS A 288 ? 0.1592 0.1907 0.1949 0.0101  -0.0077 0.0079  307 LYS A CD  
4358 C CE  . LYS A 288 ? 0.1708 0.1969 0.2078 0.0047  0.0145  0.0170  307 LYS A CE  
4359 N NZ  . LYS A 288 ? 0.1760 0.1853 0.2145 0.0194  0.0094  0.0344  307 LYS A NZ  
4373 N N   . ARG A 289 ? 0.1405 0.1858 0.2317 0.0141  0.0349  0.0363  308 ARG A N   
4374 C CA  . ARG A 289 ? 0.1330 0.2018 0.2433 0.0374  0.0358  0.0487  308 ARG A CA  
4375 C C   . ARG A 289 ? 0.1563 0.1928 0.2629 0.0086  0.0462  0.0396  308 ARG A C   
4376 O O   . ARG A 289 ? 0.1759 0.1878 0.2720 0.0219  0.0495  0.0389  308 ARG A O   
4377 C CB  . ARG A 289 ? 0.1427 0.2289 0.2453 0.0307  0.0355  0.0635  308 ARG A CB  
4378 C CG  . ARG A 289 ? 0.1669 0.2756 0.2500 0.0421  0.0459  0.0605  308 ARG A CG  
4379 C CD  . ARG A 289 ? 0.1812 0.3196 0.2579 0.0322  0.0344  0.0719  308 ARG A CD  
4380 N NE  . ARG A 289 ? 0.1881 0.3472 0.2591 0.0412  0.0041  0.0885  308 ARG A NE  
4381 C CZ  . ARG A 289 ? 0.2089 0.3625 0.2606 0.0209  0.0076  0.0876  308 ARG A CZ  
4382 N NH1 . ARG A 289 ? 0.2011 0.3775 0.2653 0.0176  0.0360  0.0787  308 ARG A NH1 
4383 N NH2 . ARG A 289 ? 0.2652 0.3668 0.2669 0.0082  0.0029  0.0921  308 ARG A NH2 
4397 N N   . ARG A 290 ? 0.1474 0.1851 0.2768 0.0028  0.0320  0.0334  309 ARG A N   
4398 C CA  . ARG A 290 ? 0.1280 0.1959 0.2991 0.0010  0.0351  0.0144  309 ARG A CA  
4399 C C   . ARG A 290 ? 0.1218 0.1866 0.2731 -0.0036 0.0096  0.0209  309 ARG A C   
4400 O O   . ARG A 290 ? 0.1397 0.1938 0.2840 -0.0128 -0.0089 0.0160  309 ARG A O   
4401 C CB  . ARG A 290 ? 0.1227 0.2437 0.3574 0.0160  0.0645  0.0009  309 ARG A CB  
4402 C CG  . ARG A 290 ? 0.2038 0.2975 0.4055 0.0272  0.0800  -0.0082 309 ARG A CG  
4403 C CD  . ARG A 290 ? 0.2493 0.3477 0.4473 0.0353  0.0979  -0.0159 309 ARG A CD  
4404 N NE  . ARG A 290 ? 0.3360 0.3989 0.4812 0.0419  0.0943  -0.0250 309 ARG A NE  
4405 C CZ  . ARG A 290 ? 0.3911 0.4308 0.5061 0.0420  0.0897  -0.0326 309 ARG A CZ  
4406 N NH1 . ARG A 290 ? 0.4145 0.4555 0.5156 0.0394  0.0937  -0.0397 309 ARG A NH1 
4407 N NH2 . ARG A 290 ? 0.3825 0.4377 0.5083 0.0404  0.0916  -0.0286 309 ARG A NH2 
4421 N N   . VAL A 291 ? 0.1203 0.1941 0.2406 -0.0086 -0.0151 0.0236  310 VAL A N   
4422 C CA  . VAL A 291 ? 0.1339 0.1920 0.2253 0.0001  -0.0243 0.0338  310 VAL A CA  
4423 C C   . VAL A 291 ? 0.1331 0.1841 0.2071 0.0040  -0.0203 0.0235  310 VAL A C   
4424 O O   . VAL A 291 ? 0.1362 0.1853 0.2011 -0.0089 -0.0145 0.0002  310 VAL A O   
4425 C CB  . VAL A 291 ? 0.1229 0.1852 0.2299 0.0038  -0.0248 0.0370  310 VAL A CB  
4426 C CG1 . VAL A 291 ? 0.1293 0.1920 0.2338 0.0163  -0.0132 0.0400  310 VAL A CG1 
4427 C CG2 . VAL A 291 ? 0.1325 0.1968 0.2295 0.0228  -0.0198 0.0437  310 VAL A CG2 
4437 N N   . ALA A 292 ? 0.1020 0.1787 0.2048 0.0084  -0.0146 0.0077  311 ALA A N   
4438 C CA  . ALA A 292 ? 0.0980 0.1738 0.2029 0.0197  -0.0081 0.0102  311 ALA A CA  
4439 C C   . ALA A 292 ? 0.1281 0.1778 0.2254 0.0005  -0.0160 -0.0014 311 ALA A C   
4440 O O   . ALA A 292 ? 0.1313 0.1762 0.2223 0.0075  0.0123  -0.0047 311 ALA A O   
4441 C CB  . ALA A 292 ? 0.1273 0.1661 0.2008 0.0342  -0.0125 0.0129  311 ALA A CB  
4447 N N   A LYS A 293 ? 0.1464 0.1752 0.2495 0.0012  -0.0035 -0.0062 312 LYS A N   
4448 N N   B LYS A 293 ? 0.1298 0.1749 0.2455 0.0058  -0.0063 0.0011  312 LYS A N   
4449 C CA  A LYS A 293 ? 0.1679 0.1867 0.2747 -0.0073 -0.0070 -0.0060 312 LYS A CA  
4450 C CA  B LYS A 293 ? 0.1369 0.1882 0.2679 0.0002  -0.0151 0.0092  312 LYS A CA  
4451 C C   A LYS A 293 ? 0.1485 0.1877 0.2770 -0.0101 -0.0057 -0.0087 312 LYS A C   
4452 C C   B LYS A 293 ? 0.1332 0.1874 0.2733 -0.0058 -0.0085 0.0000  312 LYS A C   
4453 O O   A LYS A 293 ? 0.1681 0.2003 0.2764 -0.0003 -0.0025 -0.0107 312 LYS A O   
4454 O O   B LYS A 293 ? 0.1592 0.2013 0.2724 0.0050  -0.0055 -0.0025 312 LYS A O   
4455 C CB  A LYS A 293 ? 0.2099 0.1961 0.2977 -0.0116 0.0003  -0.0116 312 LYS A CB  
4456 C CB  B LYS A 293 ? 0.1511 0.2019 0.2851 0.0019  -0.0124 0.0165  312 LYS A CB  
4457 C CG  A LYS A 293 ? 0.2545 0.2163 0.3155 -0.0075 0.0016  -0.0085 312 LYS A CG  
4458 C CG  B LYS A 293 ? 0.1690 0.2287 0.2941 0.0125  -0.0158 0.0352  312 LYS A CG  
4459 C CD  A LYS A 293 ? 0.2905 0.2300 0.3277 -0.0185 0.0031  0.0010  312 LYS A CD  
4460 C CD  B LYS A 293 ? 0.2053 0.2632 0.3091 0.0123  -0.0159 0.0366  312 LYS A CD  
4461 C CE  A LYS A 293 ? 0.3121 0.2373 0.3370 -0.0183 0.0045  0.0072  312 LYS A CE  
4462 C CE  B LYS A 293 ? 0.2388 0.2933 0.3255 0.0062  -0.0058 0.0336  312 LYS A CE  
4463 N NZ  A LYS A 293 ? 0.3180 0.2377 0.3434 -0.0053 0.0060  0.0067  312 LYS A NZ  
4464 N NZ  B LYS A 293 ? 0.2977 0.3091 0.3375 0.0008  0.0082  0.0383  312 LYS A NZ  
4491 N N   . ASP A 294 ? 0.1304 0.1858 0.2797 -0.0177 -0.0233 -0.0165 313 ASP A N   
4492 C CA  . ASP A 294 ? 0.1762 0.2165 0.2995 0.0027  -0.0172 -0.0143 313 ASP A CA  
4493 C C   . ASP A 294 ? 0.1952 0.2026 0.2730 -0.0251 -0.0134 -0.0172 313 ASP A C   
4494 O O   . ASP A 294 ? 0.2342 0.2334 0.2814 -0.0552 -0.0149 -0.0337 313 ASP A O   
4495 C CB  . ASP A 294 ? 0.1915 0.2521 0.3538 0.0061  -0.0205 -0.0183 313 ASP A CB  
4496 C CG  . ASP A 294 ? 0.2721 0.2949 0.4010 0.0082  -0.0359 -0.0185 313 ASP A CG  
4497 O OD1 . ASP A 294 ? 0.3015 0.3212 0.4218 -0.0425 -0.0237 -0.0126 313 ASP A OD1 
4498 O OD2 . ASP A 294 ? 0.2923 0.3216 0.4144 0.0199  -0.0530 -0.0242 313 ASP A OD2 
4503 N N   . SER A 295 ? 0.1483 0.1901 0.2474 -0.0075 -0.0278 -0.0176 314 SER A N   
4504 C CA  . SER A 295 ? 0.1429 0.1815 0.2236 0.0046  -0.0174 0.0001  314 SER A CA  
4505 C C   . SER A 295 ? 0.1149 0.1705 0.2051 0.0183  -0.0173 0.0054  314 SER A C   
4506 O O   . SER A 295 ? 0.1215 0.1943 0.2093 0.0186  -0.0112 -0.0039 314 SER A O   
4507 C CB  . SER A 295 ? 0.1306 0.1773 0.2200 0.0238  -0.0175 0.0021  314 SER A CB  
4508 O OG  . SER A 295 ? 0.1593 0.1901 0.2328 0.0095  -0.0181 0.0190  314 SER A OG  
4514 N N   . LEU A 296 ? 0.1350 0.1540 0.2029 -0.0089 -0.0237 -0.0034 315 LEU A N   
4515 C CA  . LEU A 296 ? 0.1241 0.1638 0.1925 0.0002  -0.0188 -0.0028 315 LEU A CA  
4516 C C   . LEU A 296 ? 0.1388 0.1795 0.1962 -0.0090 -0.0255 0.0022  315 LEU A C   
4517 O O   . LEU A 296 ? 0.1282 0.1807 0.1832 -0.0068 -0.0291 0.0172  315 LEU A O   
4518 C CB  . LEU A 296 ? 0.1589 0.1725 0.1963 0.0128  -0.0219 0.0060  315 LEU A CB  
4519 C CG  . LEU A 296 ? 0.1603 0.1720 0.1888 0.0130  -0.0105 0.0141  315 LEU A CG  
4520 C CD1 . LEU A 296 ? 0.1638 0.1681 0.1871 0.0330  -0.0153 0.0029  315 LEU A CD1 
4521 C CD2 . LEU A 296 ? 0.1968 0.1978 0.1876 0.0058  -0.0083 0.0200  315 LEU A CD2 
4533 N N   . LYS A 297 ? 0.1588 0.1654 0.2105 0.0058  -0.0155 -0.0132 316 LYS A N   
4534 C CA  . LYS A 297 ? 0.1437 0.1753 0.2153 0.0016  -0.0089 -0.0289 316 LYS A CA  
4535 C C   . LYS A 297 ? 0.1682 0.1832 0.1960 0.0013  -0.0209 -0.0281 316 LYS A C   
4536 O O   . LYS A 297 ? 0.1700 0.1923 0.1889 0.0061  -0.0144 -0.0219 316 LYS A O   
4537 C CB  . LYS A 297 ? 0.1932 0.2170 0.2517 -0.0100 -0.0175 -0.0402 316 LYS A CB  
4538 C CG  . LYS A 297 ? 0.2476 0.2586 0.2983 -0.0020 -0.0162 -0.0487 316 LYS A CG  
4539 C CD  . LYS A 297 ? 0.3412 0.3095 0.3357 0.0051  -0.0178 -0.0376 316 LYS A CD  
4540 C CE  . LYS A 297 ? 0.4265 0.3556 0.3575 -0.0084 -0.0308 -0.0283 316 LYS A CE  
4541 N NZ  . LYS A 297 ? 0.4783 0.3825 0.3774 -0.0024 -0.0221 -0.0199 316 LYS A NZ  
4555 N N   . PHE A 298 ? 0.1747 0.1888 0.1826 -0.0043 -0.0173 0.0058  317 PHE A N   
4556 C CA  . PHE A 298 ? 0.1709 0.1936 0.1811 0.0045  -0.0474 0.0012  317 PHE A CA  
4557 C C   . PHE A 298 ? 0.1446 0.1812 0.1722 0.0048  -0.0460 0.0046  317 PHE A C   
4558 O O   . PHE A 298 ? 0.1549 0.1882 0.1756 0.0017  -0.0231 0.0089  317 PHE A O   
4559 C CB  . PHE A 298 ? 0.1830 0.1946 0.1745 -0.0024 -0.0594 -0.0199 317 PHE A CB  
4560 C CG  . PHE A 298 ? 0.2258 0.2029 0.1580 0.0166  -0.0624 -0.0106 317 PHE A CG  
4561 C CD1 . PHE A 298 ? 0.2264 0.2156 0.1584 0.0366  -0.0374 -0.0085 317 PHE A CD1 
4562 C CD2 . PHE A 298 ? 0.2438 0.1989 0.1631 0.0139  -0.0428 -0.0037 317 PHE A CD2 
4563 C CE1 . PHE A 298 ? 0.2478 0.2280 0.1600 0.0269  -0.0345 -0.0027 317 PHE A CE1 
4564 C CE2 . PHE A 298 ? 0.2557 0.2201 0.1655 0.0103  -0.0338 -0.0044 317 PHE A CE2 
4565 C CZ  . PHE A 298 ? 0.2463 0.2291 0.1646 0.0203  -0.0103 -0.0008 317 PHE A CZ  
4575 N N   . PRO A 299 ? 0.1358 0.1798 0.1630 0.0032  -0.0321 0.0071  318 PRO A N   
4576 C CA  . PRO A 299 ? 0.1563 0.1786 0.1539 0.0078  -0.0274 0.0035  318 PRO A CA  
4577 C C   . PRO A 299 ? 0.1652 0.1716 0.1488 -0.0083 -0.0157 0.0039  318 PRO A C   
4578 O O   . PRO A 299 ? 0.1567 0.1695 0.1405 0.0023  -0.0101 0.0018  318 PRO A O   
4579 C CB  . PRO A 299 ? 0.1549 0.1777 0.1682 0.0026  -0.0233 0.0016  318 PRO A CB  
4580 C CG  . PRO A 299 ? 0.1481 0.1827 0.1704 0.0308  -0.0319 0.0068  318 PRO A CG  
4581 C CD  . PRO A 299 ? 0.1344 0.1830 0.1645 0.0174  -0.0264 0.0077  318 PRO A CD  
4589 N N   . LEU A 300 ? 0.1448 0.1648 0.1422 -0.0001 -0.0187 0.0050  319 LEU A N   
4590 C CA  . LEU A 300 ? 0.1611 0.1569 0.1469 0.0057  -0.0082 0.0114  319 LEU A CA  
4591 C C   . LEU A 300 ? 0.1406 0.1678 0.1590 0.0016  -0.0128 0.0084  319 LEU A C   
4592 O O   . LEU A 300 ? 0.1465 0.1901 0.1805 -0.0020 -0.0162 -0.0116 319 LEU A O   
4593 C CB  . LEU A 300 ? 0.1537 0.1626 0.1655 0.0114  -0.0202 0.0082  319 LEU A CB  
4594 C CG  . LEU A 300 ? 0.1734 0.1714 0.1559 0.0154  -0.0213 0.0195  319 LEU A CG  
4595 C CD1 . LEU A 300 ? 0.1612 0.1856 0.1558 0.0276  -0.0377 0.0256  319 LEU A CD1 
4596 C CD2 . LEU A 300 ? 0.1981 0.1706 0.1567 0.0040  -0.0036 0.0059  319 LEU A CD2 
4608 N N   . ALA A 301 ? 0.1252 0.1798 0.1663 0.0030  -0.0227 -0.0050 320 ALA A N   
4609 C CA  . ALA A 301 ? 0.1533 0.1850 0.1631 -0.0003 -0.0127 -0.0098 320 ALA A CA  
4610 C C   . ALA A 301 ? 0.1548 0.1709 0.1590 -0.0034 -0.0132 -0.0142 320 ALA A C   
4611 O O   . ALA A 301 ? 0.1653 0.1925 0.1757 0.0091  -0.0206 -0.0213 320 ALA A O   
4612 C CB  . ALA A 301 ? 0.1910 0.1895 0.1821 0.0016  -0.0184 -0.0151 320 ALA A CB  
4618 N N   . CYS A 302 ? 0.1629 0.1609 0.1556 0.0139  -0.0077 0.0053  321 CYS A N   
4619 C CA  . CYS A 302 ? 0.1776 0.1806 0.1411 0.0129  -0.0175 0.0153  321 CYS A CA  
4620 C C   . CYS A 302 ? 0.1613 0.1728 0.1429 0.0221  -0.0086 -0.0039 321 CYS A C   
4621 O O   . CYS A 302 ? 0.1665 0.1824 0.1531 0.0211  -0.0078 -0.0043 321 CYS A O   
4622 C CB  . CYS A 302 ? 0.1747 0.1941 0.1611 0.0081  -0.0161 0.0181  321 CYS A CB  
4623 S SG  . CYS A 302 ? 0.1785 0.2117 0.1584 0.0106  -0.0348 0.0178  321 CYS A SG  
4629 N N   . PHE A 303 ? 0.1616 0.1619 0.1351 0.0157  -0.0060 -0.0064 322 PHE A N   
4630 C CA  . PHE A 303 ? 0.1634 0.1413 0.1399 0.0054  -0.0166 -0.0068 322 PHE A CA  
4631 C C   . PHE A 303 ? 0.1636 0.1550 0.1450 0.0095  -0.0218 -0.0144 322 PHE A C   
4632 O O   . PHE A 303 ? 0.1605 0.1710 0.1337 0.0145  -0.0232 -0.0115 322 PHE A O   
4633 C CB  . PHE A 303 ? 0.1612 0.1406 0.1366 0.0000  -0.0217 0.0053  322 PHE A CB  
4634 C CG  . PHE A 303 ? 0.1202 0.1449 0.1258 0.0261  -0.0187 -0.0096 322 PHE A CG  
4635 C CD1 . PHE A 303 ? 0.1323 0.1497 0.1288 0.0157  -0.0131 -0.0098 322 PHE A CD1 
4636 C CD2 . PHE A 303 ? 0.1515 0.1502 0.1424 0.0224  -0.0108 -0.0118 322 PHE A CD2 
4637 C CE1 . PHE A 303 ? 0.1386 0.1562 0.1340 0.0191  -0.0167 -0.0095 322 PHE A CE1 
4638 C CE2 . PHE A 303 ? 0.1437 0.1477 0.1355 0.0235  0.0025  0.0045  322 PHE A CE2 
4639 C CZ  . PHE A 303 ? 0.1413 0.1571 0.1371 0.0250  -0.0082 -0.0086 322 PHE A CZ  
4649 N N   . LEU A 304 ? 0.1555 0.1395 0.1447 0.0006  -0.0132 -0.0011 323 LEU A N   
4650 C CA  . LEU A 304 ? 0.1665 0.1385 0.1461 -0.0023 -0.0169 -0.0077 323 LEU A CA  
4651 C C   . LEU A 304 ? 0.1821 0.1477 0.1653 0.0046  -0.0111 -0.0141 323 LEU A C   
4652 O O   . LEU A 304 ? 0.1930 0.1566 0.1708 0.0225  -0.0120 -0.0270 323 LEU A O   
4653 C CB  . LEU A 304 ? 0.1914 0.1431 0.1534 0.0001  -0.0115 -0.0157 323 LEU A CB  
4654 C CG  . LEU A 304 ? 0.1752 0.1587 0.1613 0.0082  -0.0143 0.0075  323 LEU A CG  
4655 C CD1 . LEU A 304 ? 0.1911 0.1645 0.1778 -0.0041 -0.0210 0.0026  323 LEU A CD1 
4656 C CD2 . LEU A 304 ? 0.1897 0.1603 0.1653 0.0319  -0.0122 0.0084  323 LEU A CD2 
4668 N N   . ALA A 305 ? 0.1716 0.1613 0.1634 0.0087  -0.0106 -0.0037 324 ALA A N   
4669 C CA  . ALA A 305 ? 0.1913 0.1735 0.1675 0.0266  -0.0217 -0.0175 324 ALA A CA  
4670 C C   . ALA A 305 ? 0.1756 0.1669 0.1636 0.0126  -0.0191 -0.0221 324 ALA A C   
4671 O O   . ALA A 305 ? 0.1969 0.1753 0.1778 0.0244  -0.0130 -0.0220 324 ALA A O   
4672 C CB  . ALA A 305 ? 0.2114 0.1943 0.1684 0.0309  -0.0170 -0.0149 324 ALA A CB  
4678 N N   . GLY A 306 ? 0.1793 0.1623 0.1516 0.0082  -0.0043 -0.0141 325 GLY A N   
4679 C CA  . GLY A 306 ? 0.1719 0.1671 0.1538 0.0094  0.0022  -0.0116 325 GLY A CA  
4680 C C   . GLY A 306 ? 0.1625 0.1789 0.1511 0.0068  -0.0023 -0.0080 325 GLY A C   
4681 O O   . GLY A 306 ? 0.1625 0.1768 0.1516 0.0042  -0.0152 -0.0109 325 GLY A O   
4685 N N   . ALA A 307 ? 0.1456 0.1762 0.1441 0.0131  -0.0119 -0.0240 326 ALA A N   
4686 C CA  . ALA A 307 ? 0.1626 0.1678 0.1497 0.0161  -0.0196 -0.0269 326 ALA A CA  
4687 C C   . ALA A 307 ? 0.1638 0.1756 0.1552 0.0002  -0.0178 -0.0227 326 ALA A C   
4688 O O   . ALA A 307 ? 0.1797 0.1834 0.1682 0.0012  -0.0338 -0.0069 326 ALA A O   
4689 C CB  . ALA A 307 ? 0.1637 0.1786 0.1556 0.0183  -0.0045 -0.0277 326 ALA A CB  
4695 N N   . GLN A 308 ? 0.1499 0.1678 0.1697 0.0046  -0.0201 -0.0236 327 GLN A N   
4696 C CA  . GLN A 308 ? 0.1453 0.1748 0.1672 0.0105  -0.0041 -0.0229 327 GLN A CA  
4697 C C   . GLN A 308 ? 0.1500 0.1625 0.1707 0.0050  -0.0111 -0.0230 327 GLN A C   
4698 O O   . GLN A 308 ? 0.1435 0.1592 0.1676 0.0235  0.0010  -0.0170 327 GLN A O   
4699 C CB  . GLN A 308 ? 0.1707 0.2024 0.1700 0.0065  -0.0093 -0.0090 327 GLN A CB  
4700 C CG  . GLN A 308 ? 0.1911 0.2106 0.1727 0.0084  0.0171  -0.0103 327 GLN A CG  
4701 C CD  . GLN A 308 ? 0.1804 0.2122 0.1897 0.0356  0.0069  -0.0126 327 GLN A CD  
4702 O OE1 . GLN A 308 ? 0.2437 0.2252 0.2070 0.0624  -0.0124 -0.0181 327 GLN A OE1 
4703 N NE2 . GLN A 308 ? 0.1879 0.2195 0.1898 0.0389  -0.0138 -0.0071 327 GLN A NE2 
4712 N N   . GLU A 309 ? 0.1572 0.1565 0.1661 0.0244  -0.0231 -0.0391 328 GLU A N   
4713 C CA  . GLU A 309 ? 0.1682 0.1614 0.1715 0.0146  -0.0093 -0.0225 328 GLU A CA  
4714 C C   . GLU A 309 ? 0.1401 0.1529 0.1654 0.0050  0.0034  -0.0116 328 GLU A C   
4715 O O   . GLU A 309 ? 0.1644 0.1770 0.1574 -0.0182 0.0244  -0.0151 328 GLU A O   
4716 C CB  . GLU A 309 ? 0.2335 0.2147 0.2094 0.0299  -0.0089 -0.0273 328 GLU A CB  
4717 C CG  . GLU A 309 ? 0.3617 0.2718 0.2675 0.0393  -0.0106 -0.0289 328 GLU A CG  
4718 C CD  . GLU A 309 ? 0.4528 0.3219 0.3027 0.0546  -0.0263 -0.0293 328 GLU A CD  
4719 O OE1 . GLU A 309 ? 0.4820 0.3504 0.3305 0.0785  -0.0336 -0.0406 328 GLU A OE1 
4720 O OE2 . GLU A 309 ? 0.4853 0.3351 0.3010 0.0486  -0.0436 -0.0277 328 GLU A OE2 
4727 N N   . ASN A 310 ? 0.1430 0.1254 0.1550 0.0059  0.0102  -0.0113 329 ASN A N   
4728 C CA  . ASN A 310 ? 0.1131 0.1302 0.1683 -0.0042 0.0100  -0.0059 329 ASN A CA  
4729 C C   . ASN A 310 ? 0.1081 0.1408 0.1640 0.0038  0.0111  -0.0010 329 ASN A C   
4730 O O   . ASN A 310 ? 0.1277 0.1445 0.1636 0.0084  0.0142  0.0086  329 ASN A O   
4731 C CB  . ASN A 310 ? 0.1276 0.1416 0.1630 -0.0110 -0.0042 0.0040  329 ASN A CB  
4732 C CG  . ASN A 310 ? 0.1264 0.1605 0.1611 0.0182  -0.0078 -0.0108 329 ASN A CG  
4733 O OD1 . ASN A 310 ? 0.1438 0.1757 0.1497 0.0279  0.0033  -0.0145 329 ASN A OD1 
4734 N ND2 . ASN A 310 ? 0.1404 0.1865 0.1713 0.0270  0.0112  -0.0087 329 ASN A ND2 
4741 N N   . CYS A 311 ? 0.1075 0.1406 0.1614 0.0134  0.0131  -0.0176 330 CYS A N   
4742 C CA  . CYS A 311 ? 0.1199 0.1341 0.1473 0.0068  0.0029  0.0037  330 CYS A CA  
4743 C C   . CYS A 311 ? 0.1340 0.1303 0.1489 0.0099  -0.0079 0.0094  330 CYS A C   
4744 O O   . CYS A 311 ? 0.1292 0.1464 0.1714 0.0243  0.0048  0.0053  330 CYS A O   
4745 C CB  . CYS A 311 ? 0.1370 0.1544 0.1438 0.0078  0.0072  0.0124  330 CYS A CB  
4746 S SG  . CYS A 311 ? 0.1543 0.1699 0.1517 0.0041  0.0112  -0.0112 330 CYS A SG  
4752 N N   . TYR A 312 ? 0.1159 0.1273 0.1523 0.0114  0.0045  0.0058  331 TYR A N   
4753 C CA  . TYR A 312 ? 0.1199 0.1231 0.1409 0.0041  0.0002  0.0113  331 TYR A CA  
4754 C C   . TYR A 312 ? 0.1165 0.1338 0.1353 0.0057  0.0102  0.0134  331 TYR A C   
4755 O O   . TYR A 312 ? 0.1346 0.1448 0.1431 0.0012  0.0035  0.0138  331 TYR A O   
4756 C CB  . TYR A 312 ? 0.1279 0.1332 0.1390 0.0045  0.0012  0.0076  331 TYR A CB  
4757 C CG  . TYR A 312 ? 0.1094 0.1485 0.1464 0.0022  -0.0125 0.0103  331 TYR A CG  
4758 C CD1 . TYR A 312 ? 0.1014 0.1496 0.1501 -0.0050 -0.0034 0.0082  331 TYR A CD1 
4759 C CD2 . TYR A 312 ? 0.1114 0.1640 0.1667 0.0072  0.0082  0.0251  331 TYR A CD2 
4760 C CE1 . TYR A 312 ? 0.0927 0.1384 0.1476 0.0152  -0.0053 0.0028  331 TYR A CE1 
4761 C CE2 . TYR A 312 ? 0.1163 0.1643 0.1737 0.0195  -0.0010 0.0274  331 TYR A CE2 
4762 C CZ  . TYR A 312 ? 0.1174 0.1655 0.1670 0.0360  -0.0042 0.0144  331 TYR A CZ  
4763 O OH  . TYR A 312 ? 0.1379 0.1705 0.1840 0.0374  -0.0026 0.0177  331 TYR A OH  
4773 N N   . PHE A 313 ? 0.1085 0.1362 0.1391 0.0051  0.0213  0.0146  332 PHE A N   
4774 C CA  . PHE A 313 ? 0.1175 0.1288 0.1458 0.0147  0.0060  0.0080  332 PHE A CA  
4775 C C   . PHE A 313 ? 0.1170 0.1441 0.1307 0.0060  -0.0062 0.0085  332 PHE A C   
4776 O O   . PHE A 313 ? 0.1162 0.1455 0.1296 0.0046  -0.0037 0.0144  332 PHE A O   
4777 C CB  . PHE A 313 ? 0.1241 0.1389 0.1623 0.0068  -0.0073 -0.0152 332 PHE A CB  
4778 C CG  . PHE A 313 ? 0.1172 0.1429 0.1475 0.0095  -0.0067 0.0015  332 PHE A CG  
4779 C CD1 . PHE A 313 ? 0.1021 0.1697 0.1497 0.0074  -0.0144 0.0092  332 PHE A CD1 
4780 C CD2 . PHE A 313 ? 0.1191 0.1389 0.1536 -0.0061 -0.0052 0.0069  332 PHE A CD2 
4781 C CE1 . PHE A 313 ? 0.1292 0.1783 0.1511 -0.0009 -0.0212 -0.0006 332 PHE A CE1 
4782 C CE2 . PHE A 313 ? 0.1084 0.1598 0.1625 0.0019  -0.0028 0.0071  332 PHE A CE2 
4783 C CZ  . PHE A 313 ? 0.1266 0.1815 0.1559 0.0047  -0.0151 -0.0020 332 PHE A CZ  
4793 N N   . ILE A 314 ? 0.1216 0.1613 0.1438 0.0088  -0.0017 0.0151  333 ILE A N   
4794 C CA  . ILE A 314 ? 0.1263 0.1514 0.1486 0.0127  0.0165  0.0182  333 ILE A CA  
4795 C C   . ILE A 314 ? 0.1152 0.1617 0.1413 0.0306  0.0244  0.0223  333 ILE A C   
4796 O O   . ILE A 314 ? 0.1358 0.2092 0.1388 0.0237  0.0136  0.0279  333 ILE A O   
4797 C CB  . ILE A 314 ? 0.1001 0.1525 0.1695 0.0166  0.0219  0.0110  333 ILE A CB  
4798 C CG1 . ILE A 314 ? 0.1253 0.1762 0.1765 0.0176  0.0236  -0.0083 333 ILE A CG1 
4799 C CG2 . ILE A 314 ? 0.1214 0.1661 0.1835 -0.0003 0.0497  0.0116  333 ILE A CG2 
4800 C CD1 . ILE A 314 ? 0.1331 0.1913 0.1819 0.0092  0.0348  -0.0196 333 ILE A CD1 
4812 N N   . TYR A 315 ? 0.0993 0.1645 0.1435 0.0161  0.0062  0.0133  334 TYR A N   
4813 C CA  . TYR A 315 ? 0.1167 0.1435 0.1598 0.0154  -0.0114 0.0101  334 TYR A CA  
4814 C C   . TYR A 315 ? 0.1170 0.1317 0.1618 0.0264  -0.0005 0.0133  334 TYR A C   
4815 O O   . TYR A 315 ? 0.1449 0.1415 0.1889 0.0141  0.0172  0.0157  334 TYR A O   
4816 C CB  . TYR A 315 ? 0.1300 0.1377 0.1653 0.0167  -0.0175 -0.0006 334 TYR A CB  
4817 C CG  . TYR A 315 ? 0.1252 0.1467 0.1658 0.0092  -0.0077 -0.0031 334 TYR A CG  
4818 C CD1 . TYR A 315 ? 0.1152 0.1464 0.1669 0.0028  0.0004  -0.0015 334 TYR A CD1 
4819 C CD2 . TYR A 315 ? 0.1321 0.1525 0.1686 0.0051  -0.0037 0.0004  334 TYR A CD2 
4820 C CE1 . TYR A 315 ? 0.1107 0.1574 0.1725 0.0165  0.0188  0.0039  334 TYR A CE1 
4821 C CE2 . TYR A 315 ? 0.1225 0.1596 0.1769 -0.0020 0.0118  -0.0045 334 TYR A CE2 
4822 C CZ  . TYR A 315 ? 0.1160 0.1608 0.1795 0.0127  0.0069  -0.0038 334 TYR A CZ  
4823 O OH  . TYR A 315 ? 0.1244 0.1810 0.1992 0.0221  0.0013  -0.0099 334 TYR A OH  
4833 N N   . ASN A 316 ? 0.1219 0.1257 0.1583 0.0164  -0.0012 0.0181  335 ASN A N   
4834 C CA  . ASN A 316 ? 0.1155 0.1362 0.1493 0.0194  -0.0082 0.0159  335 ASN A CA  
4835 C C   . ASN A 316 ? 0.1300 0.1498 0.1556 0.0086  -0.0018 0.0034  335 ASN A C   
4836 O O   . ASN A 316 ? 0.1229 0.1542 0.1579 0.0134  -0.0048 -0.0008 335 ASN A O   
4837 C CB  . ASN A 316 ? 0.1309 0.1342 0.1583 -0.0049 -0.0121 0.0278  335 ASN A CB  
4838 C CG  . ASN A 316 ? 0.1225 0.1382 0.1617 0.0060  -0.0115 0.0206  335 ASN A CG  
4839 O OD1 . ASN A 316 ? 0.1469 0.1356 0.1509 0.0070  0.0064  0.0235  335 ASN A OD1 
4840 N ND2 . ASN A 316 ? 0.1212 0.1469 0.1592 0.0230  -0.0144 0.0076  335 ASN A ND2 
4847 N N   . TRP A 317 ? 0.1170 0.1321 0.1553 0.0041  0.0062  0.0167  336 TRP A N   
4848 C CA  . TRP A 317 ? 0.1205 0.1415 0.1604 0.0289  0.0012  0.0167  336 TRP A CA  
4849 C C   . TRP A 317 ? 0.1281 0.1465 0.1545 0.0321  -0.0148 0.0106  336 TRP A C   
4850 O O   . TRP A 317 ? 0.1331 0.1480 0.1730 0.0281  -0.0206 0.0212  336 TRP A O   
4851 C CB  . TRP A 317 ? 0.1292 0.1451 0.1651 0.0219  -0.0021 0.0044  336 TRP A CB  
4852 C CG  . TRP A 317 ? 0.1128 0.1637 0.1631 0.0175  -0.0105 0.0086  336 TRP A CG  
4853 C CD1 . TRP A 317 ? 0.1125 0.1890 0.1709 0.0201  0.0214  0.0115  336 TRP A CD1 
4854 C CD2 . TRP A 317 ? 0.1102 0.1707 0.1665 0.0118  -0.0017 0.0069  336 TRP A CD2 
4855 N NE1 . TRP A 317 ? 0.1252 0.1857 0.1773 0.0163  0.0006  0.0239  336 TRP A NE1 
4856 C CE2 . TRP A 317 ? 0.1125 0.1835 0.1633 0.0130  0.0023  0.0096  336 TRP A CE2 
4857 C CE3 . TRP A 317 ? 0.1357 0.1628 0.1691 -0.0073 -0.0115 0.0243  336 TRP A CE3 
4858 C CZ2 . TRP A 317 ? 0.1371 0.1999 0.1793 0.0110  -0.0078 0.0240  336 TRP A CZ2 
4859 C CZ3 . TRP A 317 ? 0.1504 0.1707 0.1745 0.0006  -0.0318 0.0081  336 TRP A CZ3 
4860 C CH2 . TRP A 317 ? 0.1446 0.1977 0.1780 -0.0088 -0.0272 0.0227  336 TRP A CH2 
4871 N N   . GLY A 318 ? 0.1046 0.1442 0.1590 0.0036  -0.0154 0.0155  337 GLY A N   
4872 C CA  . GLY A 318 ? 0.1132 0.1329 0.1526 -0.0001 -0.0116 0.0155  337 GLY A CA  
4873 C C   . GLY A 318 ? 0.1340 0.1366 0.1640 0.0098  -0.0080 -0.0006 337 GLY A C   
4874 O O   . GLY A 318 ? 0.1517 0.1232 0.1658 -0.0004 -0.0190 -0.0071 337 GLY A O   
4878 N N   . TYR A 319 ? 0.1372 0.1540 0.1566 -0.0092 -0.0114 -0.0015 338 TYR A N   
4879 C CA  . TYR A 319 ? 0.1475 0.1320 0.1543 -0.0011 -0.0216 0.0001  338 TYR A CA  
4880 C C   . TYR A 319 ? 0.1493 0.1413 0.1617 0.0052  -0.0045 0.0087  338 TYR A C   
4881 O O   . TYR A 319 ? 0.1524 0.1580 0.1630 0.0190  -0.0053 0.0038  338 TYR A O   
4882 C CB  . TYR A 319 ? 0.1297 0.1487 0.1519 -0.0133 -0.0034 0.0162  338 TYR A CB  
4883 C CG  . TYR A 319 ? 0.1245 0.1768 0.1565 -0.0132 0.0034  0.0030  338 TYR A CG  
4884 C CD1 . TYR A 319 ? 0.1532 0.1912 0.1702 -0.0158 0.0267  -0.0069 338 TYR A CD1 
4885 C CD2 . TYR A 319 ? 0.1224 0.1923 0.1701 0.0030  0.0097  0.0010  338 TYR A CD2 
4886 C CE1 . TYR A 319 ? 0.1583 0.2028 0.1724 0.0006  0.0217  0.0002  338 TYR A CE1 
4887 C CE2 . TYR A 319 ? 0.1267 0.2046 0.1691 -0.0036 0.0194  0.0078  338 TYR A CE2 
4888 C CZ  . TYR A 319 ? 0.1448 0.2126 0.1738 -0.0054 0.0178  -0.0063 338 TYR A CZ  
4889 O OH  . TYR A 319 ? 0.1769 0.2170 0.1864 -0.0044 0.0160  -0.0189 338 TYR A OH  
4899 N N   . ARG A 320 ? 0.1273 0.1594 0.1588 -0.0053 -0.0107 0.0145  339 ARG A N   
4900 C CA  . ARG A 320 ? 0.1426 0.1672 0.1744 0.0136  0.0043  0.0026  339 ARG A CA  
4901 C C   . ARG A 320 ? 0.1392 0.1728 0.1641 0.0217  -0.0001 -0.0008 339 ARG A C   
4902 O O   . ARG A 320 ? 0.1585 0.1890 0.1581 0.0069  0.0098  0.0049  339 ARG A O   
4903 C CB  . ARG A 320 ? 0.1894 0.1813 0.2140 0.0151  0.0163  0.0147  339 ARG A CB  
4904 C CG  . ARG A 320 ? 0.2483 0.2032 0.2600 0.0347  0.0174  0.0236  339 ARG A CG  
4905 C CD  . ARG A 320 ? 0.3674 0.2596 0.3245 0.0330  0.0178  0.0176  339 ARG A CD  
4906 N NE  . ARG A 320 ? 0.4994 0.3229 0.3815 0.0258  0.0279  0.0236  339 ARG A NE  
4907 C CZ  . ARG A 320 ? 0.6056 0.3658 0.4220 0.0253  0.0257  0.0101  339 ARG A CZ  
4908 N NH1 . ARG A 320 ? 0.6404 0.3862 0.4353 0.0308  0.0287  0.0037  339 ARG A NH1 
4909 N NH2 . ARG A 320 ? 0.6384 0.3820 0.4406 0.0151  0.0217  0.0067  339 ARG A NH2 
4923 N N   . MET A 321 ? 0.1589 0.1714 0.1534 -0.0034 0.0039  0.0050  340 MET A N   
4924 C CA  . MET A 321 ? 0.1692 0.1653 0.1679 -0.0054 0.0012  -0.0026 340 MET A CA  
4925 C C   . MET A 321 ? 0.1589 0.1594 0.1650 0.0091  0.0087  0.0043  340 MET A C   
4926 O O   . MET A 321 ? 0.1512 0.1608 0.1739 0.0012  -0.0049 0.0065  340 MET A O   
4927 C CB  . MET A 321 ? 0.1852 0.1639 0.1756 -0.0188 -0.0145 -0.0055 340 MET A CB  
4928 C CG  . MET A 321 ? 0.2090 0.1766 0.1788 -0.0211 -0.0175 0.0046  340 MET A CG  
4929 S SD  . MET A 321 ? 0.2555 0.1941 0.1788 -0.0247 -0.0166 0.0065  340 MET A SD  
4930 C CE  . MET A 321 ? 0.2682 0.1991 0.1850 -0.0084 -0.0057 0.0056  340 MET A CE  
4940 N N   . GLU A 322 ? 0.1551 0.1648 0.1693 0.0300  -0.0137 0.0051  341 GLU A N   
4941 C CA  . GLU A 322 ? 0.1506 0.1857 0.1832 0.0324  0.0133  0.0017  341 GLU A CA  
4942 C C   . GLU A 322 ? 0.1400 0.1942 0.1719 0.0210  0.0158  0.0129  341 GLU A C   
4943 O O   . GLU A 322 ? 0.1406 0.2059 0.1767 0.0233  0.0147  0.0081  341 GLU A O   
4944 C CB  . GLU A 322 ? 0.1962 0.2221 0.2213 0.0458  0.0145  -0.0097 341 GLU A CB  
4945 C CG  . GLU A 322 ? 0.2635 0.2563 0.2730 0.0446  0.0203  -0.0313 341 GLU A CG  
4946 C CD  . GLU A 322 ? 0.3163 0.2692 0.3030 0.0259  0.0171  -0.0333 341 GLU A CD  
4947 O OE1 . GLU A 322 ? 0.3048 0.2759 0.3035 0.0424  -0.0053 -0.0515 341 GLU A OE1 
4948 O OE2 . GLU A 322 ? 0.3531 0.2900 0.3259 0.0054  0.0242  -0.0323 341 GLU A OE2 
4955 N N   . ASN A 323 ? 0.1182 0.1828 0.1569 0.0190  0.0248  0.0136  342 ASN A N   
4956 C CA  . ASN A 323 ? 0.1266 0.1663 0.1591 0.0146  0.0097  -0.0013 342 ASN A CA  
4957 C C   . ASN A 323 ? 0.1219 0.1657 0.1510 0.0143  0.0036  0.0134  342 ASN A C   
4958 O O   . ASN A 323 ? 0.1302 0.1625 0.1420 0.0054  0.0100  0.0037  342 ASN A O   
4959 C CB  . ASN A 323 ? 0.1364 0.1715 0.1756 0.0135  -0.0055 0.0070  342 ASN A CB  
4960 C CG  . ASN A 323 ? 0.1147 0.1614 0.1658 0.0034  -0.0204 0.0128  342 ASN A CG  
4961 O OD1 . ASN A 323 ? 0.1472 0.1708 0.1773 0.0051  -0.0184 -0.0001 342 ASN A OD1 
4962 N ND2 . ASN A 323 ? 0.1674 0.1596 0.1705 0.0279  -0.0148 -0.0023 342 ASN A ND2 
4969 N N   . GLY A 324 ? 0.1147 0.1702 0.1537 0.0161  0.0194  0.0189  343 GLY A N   
4970 C CA  . GLY A 324 ? 0.1216 0.1761 0.1682 0.0132  0.0102  0.0097  343 GLY A CA  
4971 C C   . GLY A 324 ? 0.1403 0.1706 0.1703 0.0177  0.0031  0.0145  343 GLY A C   
4972 O O   . GLY A 324 ? 0.1424 0.1669 0.1743 0.0192  0.0024  0.0108  343 GLY A O   
4976 N N   . CYS A 325 ? 0.1236 0.1445 0.1711 0.0050  0.0003  0.0057  344 CYS A N   
4977 C CA  . CYS A 325 ? 0.1139 0.1465 0.1568 -0.0032 -0.0070 0.0266  344 CYS A CA  
4978 C C   . CYS A 325 ? 0.1159 0.1523 0.1590 -0.0050 0.0015  0.0168  344 CYS A C   
4979 O O   . CYS A 325 ? 0.1210 0.1753 0.1712 0.0145  0.0110  0.0276  344 CYS A O   
4980 C CB  . CYS A 325 ? 0.1075 0.1655 0.1836 -0.0104 0.0038  0.0240  344 CYS A CB  
4981 S SG  . CYS A 325 ? 0.1525 0.1733 0.1899 -0.0026 -0.0243 0.0213  344 CYS A SG  
4987 N N   . LEU A 326 ? 0.1365 0.1640 0.1646 -0.0050 0.0026  0.0157  345 LEU A N   
4988 C CA  . LEU A 326 ? 0.1432 0.1702 0.1627 0.0056  0.0127  0.0245  345 LEU A CA  
4989 C C   . LEU A 326 ? 0.1412 0.1785 0.1915 0.0036  0.0120  0.0383  345 LEU A C   
4990 O O   . LEU A 326 ? 0.1521 0.1916 0.2104 0.0027  0.0010  0.0528  345 LEU A O   
4991 C CB  . LEU A 326 ? 0.1783 0.1770 0.1692 0.0096  0.0149  0.0302  345 LEU A CB  
4992 C CG  . LEU A 326 ? 0.2150 0.1824 0.1704 -0.0026 -0.0015 0.0216  345 LEU A CG  
4993 C CD1 . LEU A 326 ? 0.2573 0.1985 0.1791 -0.0180 -0.0099 0.0120  345 LEU A CD1 
4994 C CD2 . LEU A 326 ? 0.1995 0.1757 0.1706 -0.0245 -0.0053 0.0213  345 LEU A CD2 
5006 N N   . GLU A 327 ? 0.1154 0.1657 0.2067 0.0054  0.0224  0.0228  346 GLU A N   
5007 C CA  . GLU A 327 ? 0.1184 0.1624 0.2112 -0.0130 0.0018  0.0252  346 GLU A CA  
5008 C C   . GLU A 327 ? 0.1147 0.1729 0.2352 -0.0109 0.0185  0.0209  346 GLU A C   
5009 O O   . GLU A 327 ? 0.1559 0.1922 0.2976 -0.0044 0.0187  -0.0037 346 GLU A O   
5010 C CB  . GLU A 327 ? 0.1297 0.1674 0.2095 0.0088  -0.0023 0.0202  346 GLU A CB  
5011 C CG  . GLU A 327 ? 0.1412 0.1819 0.2316 0.0094  -0.0045 0.0172  346 GLU A CG  
5012 C CD  . GLU A 327 ? 0.1611 0.2014 0.2810 -0.0114 0.0078  0.0043  346 GLU A CD  
5013 O OE1 . GLU A 327 ? 0.1424 0.2373 0.3288 -0.0159 0.0240  -0.0083 346 GLU A OE1 
5014 O OE2 . GLU A 327 ? 0.1922 0.2139 0.2818 -0.0250 0.0288  -0.0195 346 GLU A OE2 
5021 N N   . TRP A 328 ? 0.1276 0.1633 0.2224 -0.0008 0.0172  0.0305  347 TRP A N   
5022 C CA  . TRP A 328 ? 0.1337 0.1695 0.2070 0.0001  0.0147  0.0363  347 TRP A CA  
5023 C C   . TRP A 328 ? 0.1586 0.1679 0.2263 -0.0089 0.0107  0.0203  347 TRP A C   
5024 O O   . TRP A 328 ? 0.1759 0.1831 0.2377 -0.0030 0.0153  0.0045  347 TRP A O   
5025 C CB  . TRP A 328 ? 0.1595 0.1721 0.1991 0.0024  0.0213  0.0179  347 TRP A CB  
5026 C CG  . TRP A 328 ? 0.1551 0.1822 0.1908 0.0037  -0.0067 0.0139  347 TRP A CG  
5027 C CD1 . TRP A 328 ? 0.1730 0.1821 0.1951 -0.0012 -0.0085 0.0174  347 TRP A CD1 
5028 C CD2 . TRP A 328 ? 0.1650 0.1689 0.1796 0.0162  -0.0033 0.0055  347 TRP A CD2 
5029 N NE1 . TRP A 328 ? 0.2023 0.1853 0.1993 0.0167  -0.0175 0.0185  347 TRP A NE1 
5030 C CE2 . TRP A 328 ? 0.1802 0.1876 0.1869 0.0283  -0.0157 0.0038  347 TRP A CE2 
5031 C CE3 . TRP A 328 ? 0.1623 0.1805 0.1706 0.0164  0.0000  0.0156  347 TRP A CE3 
5032 C CZ2 . TRP A 328 ? 0.1910 0.1963 0.1775 0.0498  0.0004  -0.0011 347 TRP A CZ2 
5033 C CZ3 . TRP A 328 ? 0.1761 0.1779 0.1820 0.0042  -0.0010 0.0165  347 TRP A CZ3 
5034 C CH2 . TRP A 328 ? 0.1965 0.2045 0.1776 0.0362  0.0053  0.0094  347 TRP A CH2 
5045 N N   . TYR A 329 ? 0.1457 0.1653 0.2108 -0.0139 0.0040  0.0085  348 TYR A N   
5046 C CA  . TYR A 329 ? 0.1442 0.1857 0.2238 -0.0050 -0.0014 0.0080  348 TYR A CA  
5047 C C   . TYR A 329 ? 0.1590 0.1842 0.2219 0.0003  0.0039  0.0113  348 TYR A C   
5048 O O   . TYR A 329 ? 0.1792 0.1873 0.2112 -0.0203 0.0040  0.0107  348 TYR A O   
5049 C CB  . TYR A 329 ? 0.1513 0.1851 0.2216 0.0188  -0.0189 0.0092  348 TYR A CB  
5050 C CG  . TYR A 329 ? 0.1478 0.1748 0.2177 0.0211  -0.0119 0.0036  348 TYR A CG  
5051 C CD1 . TYR A 329 ? 0.1300 0.1812 0.2127 0.0204  0.0060  0.0043  348 TYR A CD1 
5052 C CD2 . TYR A 329 ? 0.1594 0.1775 0.2234 0.0237  -0.0290 0.0042  348 TYR A CD2 
5053 C CE1 . TYR A 329 ? 0.1278 0.1815 0.2144 0.0198  0.0082  0.0256  348 TYR A CE1 
5054 C CE2 . TYR A 329 ? 0.1527 0.1722 0.2182 0.0179  -0.0337 0.0201  348 TYR A CE2 
5055 C CZ  . TYR A 329 ? 0.1378 0.1701 0.2172 0.0302  -0.0235 0.0339  348 TYR A CZ  
5056 O OH  . TYR A 329 ? 0.1638 0.1719 0.2158 0.0311  -0.0117 0.0330  348 TYR A OH  
5066 N N   . PRO A 330 ? 0.1394 0.1859 0.2503 -0.0006 -0.0008 0.0230  349 PRO A N   
5067 C CA  . PRO A 330 ? 0.1646 0.1800 0.2486 -0.0260 0.0051  0.0059  349 PRO A CA  
5068 C C   . PRO A 330 ? 0.1500 0.1723 0.2368 -0.0077 -0.0149 0.0047  349 PRO A C   
5069 O O   . PRO A 330 ? 0.1666 0.1682 0.2502 -0.0086 -0.0176 -0.0029 349 PRO A O   
5070 C CB  . PRO A 330 ? 0.1977 0.1986 0.2734 -0.0180 -0.0087 0.0122  349 PRO A CB  
5071 C CG  . PRO A 330 ? 0.2237 0.2149 0.2818 -0.0238 -0.0326 0.0200  349 PRO A CG  
5072 C CD  . PRO A 330 ? 0.1675 0.2031 0.2683 0.0060  -0.0081 0.0247  349 PRO A CD  
5080 N N   . GLU A 331 ? 0.1595 0.1768 0.2267 -0.0198 -0.0141 0.0075  350 GLU A N   
5081 C CA  . GLU A 331 ? 0.1457 0.1712 0.2168 -0.0161 -0.0168 -0.0036 350 GLU A CA  
5082 C C   . GLU A 331 ? 0.1502 0.1834 0.1924 -0.0040 -0.0140 -0.0093 350 GLU A C   
5083 O O   . GLU A 331 ? 0.1804 0.2178 0.1952 0.0129  -0.0241 -0.0378 350 GLU A O   
5084 C CB  . GLU A 331 ? 0.1598 0.2106 0.2261 -0.0237 -0.0350 -0.0021 350 GLU A CB  
5085 C CG  . GLU A 331 ? 0.1805 0.2249 0.2482 -0.0544 -0.0582 -0.0127 350 GLU A CG  
5086 C CD  . GLU A 331 ? 0.2105 0.2532 0.2771 -0.0412 -0.0906 -0.0058 350 GLU A CD  
5087 O OE1 . GLU A 331 ? 0.1887 0.2253 0.2834 -0.0184 -0.0674 0.0114  350 GLU A OE1 
5088 O OE2 . GLU A 331 ? 0.2541 0.2906 0.3012 -0.0240 -0.1049 -0.0112 350 GLU A OE2 
5095 N N   . PHE A 332 ? 0.1528 0.1687 0.1898 0.0076  -0.0064 0.0118  351 PHE A N   
5096 C CA  . PHE A 332 ? 0.1586 0.1696 0.1784 -0.0073 -0.0041 0.0137  351 PHE A CA  
5097 C C   . PHE A 332 ? 0.1308 0.1618 0.1815 -0.0089 -0.0034 0.0167  351 PHE A C   
5098 O O   . PHE A 332 ? 0.1273 0.1772 0.1845 -0.0202 -0.0075 0.0214  351 PHE A O   
5099 C CB  . PHE A 332 ? 0.1654 0.1569 0.1808 0.0061  -0.0066 -0.0029 351 PHE A CB  
5100 C CG  . PHE A 332 ? 0.1457 0.1538 0.1916 -0.0069 -0.0132 -0.0046 351 PHE A CG  
5101 C CD1 . PHE A 332 ? 0.1549 0.1311 0.1891 -0.0183 -0.0063 -0.0163 351 PHE A CD1 
5102 C CD2 . PHE A 332 ? 0.1494 0.1644 0.1985 -0.0023 -0.0080 -0.0069 351 PHE A CD2 
5103 C CE1 . PHE A 332 ? 0.1627 0.1435 0.1906 0.0045  0.0001  -0.0102 351 PHE A CE1 
5104 C CE2 . PHE A 332 ? 0.1449 0.1322 0.1997 0.0017  -0.0033 -0.0264 351 PHE A CE2 
5105 C CZ  . PHE A 332 ? 0.1434 0.1431 0.1844 -0.0106 0.0004  0.0045  351 PHE A CZ  
5115 N N   . ASP A 333 ? 0.1702 0.1598 0.1812 -0.0256 -0.0014 0.0206  352 ASP A N   
5116 C CA  . ASP A 333 ? 0.1723 0.1551 0.1913 -0.0196 0.0115  0.0120  352 ASP A CA  
5117 C C   . ASP A 333 ? 0.1654 0.1542 0.2110 -0.0170 0.0037  0.0180  352 ASP A C   
5118 O O   . ASP A 333 ? 0.1884 0.1814 0.2317 -0.0058 -0.0053 0.0162  352 ASP A O   
5119 C CB  . ASP A 333 ? 0.1754 0.1813 0.1999 -0.0021 0.0072  0.0206  352 ASP A CB  
5120 C CG  . ASP A 333 ? 0.1875 0.1997 0.2220 0.0262  0.0152  0.0298  352 ASP A CG  
5121 O OD1 . ASP A 333 ? 0.2007 0.1953 0.2089 0.0269  0.0071  0.0246  352 ASP A OD1 
5122 O OD2 . ASP A 333 ? 0.2026 0.2149 0.2465 0.0267  0.0228  0.0472  352 ASP A OD2 
5127 N N   . LYS A 334 ? 0.1799 0.1431 0.2086 -0.0126 -0.0075 0.0181  353 LYS A N   
5128 C CA  . LYS A 334 ? 0.2047 0.1622 0.2241 -0.0165 -0.0096 -0.0036 353 LYS A CA  
5129 C C   . LYS A 334 ? 0.1976 0.1536 0.2156 -0.0186 -0.0139 0.0001  353 LYS A C   
5130 O O   . LYS A 334 ? 0.1883 0.1550 0.2217 -0.0215 -0.0101 0.0112  353 LYS A O   
5131 C CB  . LYS A 334 ? 0.2238 0.1989 0.2625 -0.0043 -0.0136 -0.0163 353 LYS A CB  
5132 C CG  . LYS A 334 ? 0.2514 0.2237 0.2939 0.0076  -0.0084 -0.0225 353 LYS A CG  
5133 C CD  . LYS A 334 ? 0.2880 0.2634 0.3289 0.0052  -0.0028 -0.0215 353 LYS A CD  
5134 C CE  . LYS A 334 ? 0.3323 0.2947 0.3592 -0.0175 0.0061  -0.0090 353 LYS A CE  
5135 N NZ  . LYS A 334 ? 0.3598 0.3101 0.3777 -0.0278 0.0077  0.0057  353 LYS A NZ  
5149 N N   . PRO A 335 ? 0.2013 0.1515 0.2138 -0.0147 -0.0228 0.0033  354 PRO A N   
5150 C CA  . PRO A 335 ? 0.1861 0.1583 0.2082 0.0088  -0.0069 -0.0014 354 PRO A CA  
5151 C C   . PRO A 335 ? 0.1888 0.1690 0.1978 0.0135  -0.0149 -0.0029 354 PRO A C   
5152 O O   . PRO A 335 ? 0.1734 0.1921 0.2197 -0.0054 -0.0226 0.0008  354 PRO A O   
5153 C CB  . PRO A 335 ? 0.2204 0.1599 0.2205 0.0342  0.0011  0.0040  354 PRO A CB  
5154 C CG  . PRO A 335 ? 0.2269 0.1553 0.2179 0.0128  0.0030  0.0003  354 PRO A CG  
5155 C CD  . PRO A 335 ? 0.2064 0.1386 0.2112 -0.0128 -0.0043 0.0032  354 PRO A CD  
5163 N N   . LEU A 336 ? 0.1908 0.1694 0.1867 -0.0032 -0.0093 0.0069  355 LEU A N   
5164 C CA  . LEU A 336 ? 0.1864 0.1706 0.1820 -0.0089 -0.0338 0.0071  355 LEU A CA  
5165 C C   . LEU A 336 ? 0.2061 0.1612 0.1835 -0.0057 -0.0289 -0.0116 355 LEU A C   
5166 O O   . LEU A 336 ? 0.2276 0.1805 0.1839 -0.0097 -0.0409 -0.0198 355 LEU A O   
5167 C CB  . LEU A 336 ? 0.1890 0.1685 0.1909 0.0099  -0.0240 0.0016  355 LEU A CB  
5168 C CG  . LEU A 336 ? 0.1927 0.1681 0.1811 -0.0048 -0.0397 -0.0146 355 LEU A CG  
5169 C CD1 . LEU A 336 ? 0.2015 0.1597 0.1713 0.0075  -0.0410 -0.0256 355 LEU A CD1 
5170 C CD2 . LEU A 336 ? 0.1965 0.1670 0.1765 -0.0237 -0.0554 -0.0197 355 LEU A CD2 
5182 N N   . GLY A 337 ? 0.1990 0.1586 0.1869 0.0079  -0.0159 0.0001  356 GLY A N   
5183 C CA  . GLY A 337 ? 0.2128 0.1686 0.1902 0.0283  -0.0210 -0.0004 356 GLY A CA  
5184 C C   . GLY A 337 ? 0.2048 0.1753 0.2044 0.0344  -0.0237 -0.0092 356 GLY A C   
5185 O O   . GLY A 337 ? 0.2107 0.1769 0.1990 0.0468  -0.0346 -0.0128 356 GLY A O   
5189 N N   . LYS A 338 ? 0.2142 0.1980 0.2154 0.0474  -0.0392 -0.0225 357 LYS A N   
5190 C CA  . LYS A 338 ? 0.2463 0.2415 0.2305 0.0424  -0.0455 -0.0063 357 LYS A CA  
5191 C C   . LYS A 338 ? 0.2378 0.2193 0.2178 0.0192  -0.0356 -0.0301 357 LYS A C   
5192 O O   . LYS A 338 ? 0.2465 0.2167 0.2182 0.0079  -0.0252 -0.0200 357 LYS A O   
5193 C CB  . LYS A 338 ? 0.2840 0.3137 0.2712 0.0647  -0.0557 -0.0015 357 LYS A CB  
5194 C CG  . LYS A 338 ? 0.3602 0.3684 0.3196 0.0745  -0.0784 0.0017  357 LYS A CG  
5195 C CD  . LYS A 338 ? 0.3998 0.4078 0.3543 0.0845  -0.0977 0.0138  357 LYS A CD  
5196 C CE  . LYS A 338 ? 0.4392 0.4454 0.3836 0.0880  -0.1044 0.0279  357 LYS A CE  
5197 N NZ  . LYS A 338 ? 0.4734 0.4632 0.4045 0.0804  -0.0993 0.0295  357 LYS A NZ  
5211 N N   . PRO A 339 ? 0.2166 0.2018 0.2158 0.0231  -0.0132 -0.0457 358 PRO A N   
5212 C CA  . PRO A 339 ? 0.2307 0.2040 0.2214 0.0365  -0.0260 -0.0463 358 PRO A CA  
5213 C C   . PRO A 339 ? 0.2452 0.2227 0.2366 0.0520  -0.0209 -0.0604 358 PRO A C   
5214 O O   . PRO A 339 ? 0.2362 0.2527 0.2499 0.0510  -0.0171 -0.0491 358 PRO A O   
5215 C CB  . PRO A 339 ? 0.2472 0.2075 0.2279 0.0176  -0.0250 -0.0403 358 PRO A CB  
5216 C CG  . PRO A 339 ? 0.2785 0.2173 0.2299 0.0001  -0.0094 -0.0354 358 PRO A CG  
5217 C CD  . PRO A 339 ? 0.2492 0.2108 0.2204 0.0066  -0.0114 -0.0363 358 PRO A CD  
5225 N N   . VAL A 340 ? 0.2866 0.2214 0.2487 0.0587  -0.0190 -0.0759 359 VAL A N   
5226 C CA  . VAL A 340 ? 0.3341 0.2123 0.2598 0.0852  -0.0093 -0.0798 359 VAL A CA  
5227 C C   . VAL A 340 ? 0.3820 0.2065 0.2606 0.0769  0.0042  -0.0730 359 VAL A C   
5228 O O   . VAL A 340 ? 0.4529 0.2264 0.2803 0.0794  0.0247  -0.0645 359 VAL A O   
5229 C CB  . VAL A 340 ? 0.3942 0.2425 0.2832 0.0711  -0.0075 -0.0895 359 VAL A CB  
5230 C CG1 . VAL A 340 ? 0.4239 0.2571 0.3026 0.0504  0.0032  -0.0703 359 VAL A CG1 
5231 C CG2 . VAL A 340 ? 0.3917 0.2300 0.2888 0.0942  -0.0255 -0.0972 359 VAL A CG2 
5241 N N   . GLY A 341 ? 0.3648 0.1977 0.2561 0.0752  0.0056  -0.0681 360 GLY A N   
5242 C CA  . GLY A 341 ? 0.3450 0.1885 0.2507 0.0760  -0.0018 -0.0764 360 GLY A CA  
5243 C C   . GLY A 341 ? 0.3047 0.1978 0.2467 0.0829  0.0056  -0.0605 360 GLY A C   
5244 O O   . GLY A 341 ? 0.3099 0.2023 0.2510 0.0776  0.0013  -0.0531 360 GLY A O   
5248 N N   . GLU A 342 ? 0.2959 0.2146 0.2379 0.0751  0.0192  -0.0377 361 GLU A N   
5249 C CA  . GLU A 342 ? 0.2843 0.2252 0.2386 0.0769  0.0044  -0.0248 361 GLU A CA  
5250 C C   . GLU A 342 ? 0.2696 0.2232 0.2020 0.0575  -0.0112 -0.0274 361 GLU A C   
5251 O O   . GLU A 342 ? 0.2882 0.2197 0.2008 0.0251  -0.0136 -0.0308 361 GLU A O   
5252 C CB  . GLU A 342 ? 0.2885 0.2424 0.2888 0.0871  -0.0027 -0.0277 361 GLU A CB  
5253 C CG  . GLU A 342 ? 0.3127 0.2650 0.3318 0.0873  -0.0252 -0.0213 361 GLU A CG  
5254 C CD  . GLU A 342 ? 0.3503 0.2932 0.3720 0.0777  -0.0600 -0.0028 361 GLU A CD  
5255 O OE1 . GLU A 342 ? 0.4324 0.3153 0.3986 0.0666  -0.0685 -0.0021 361 GLU A OE1 
5256 O OE2 . GLU A 342 ? 0.3174 0.2931 0.3838 0.0851  -0.0557 -0.0211 361 GLU A OE2 
5263 N N   . MET A 343 ? 0.2512 0.2254 0.1927 0.0606  -0.0208 -0.0213 362 MET A N   
5264 C CA  . MET A 343 ? 0.2652 0.2226 0.1823 0.0472  -0.0239 -0.0306 362 MET A CA  
5265 C C   . MET A 343 ? 0.2810 0.2393 0.1814 0.0403  -0.0106 -0.0401 362 MET A C   
5266 O O   . MET A 343 ? 0.3059 0.2458 0.1888 0.0260  -0.0014 -0.0374 362 MET A O   
5267 C CB  . MET A 343 ? 0.2634 0.2298 0.1822 0.0486  -0.0114 -0.0292 362 MET A CB  
5268 C CG  . MET A 343 ? 0.2403 0.2313 0.1758 0.0595  -0.0134 -0.0276 362 MET A CG  
5269 S SD  . MET A 343 ? 0.2690 0.2301 0.1764 0.0443  -0.0146 -0.0212 362 MET A SD  
5270 C CE  . MET A 343 ? 0.2935 0.2440 0.1977 0.0256  -0.0058 0.0114  362 MET A CE  
5280 N N   . VAL A 344 ? 0.2877 0.2446 0.1692 0.0565  -0.0288 -0.0516 363 VAL A N   
5281 C CA  . VAL A 344 ? 0.3223 0.2489 0.1813 0.0648  -0.0378 -0.0455 363 VAL A CA  
5282 C C   . VAL A 344 ? 0.3232 0.2534 0.1914 0.0741  -0.0273 -0.0402 363 VAL A C   
5283 O O   . VAL A 344 ? 0.3039 0.2374 0.1981 0.0439  -0.0095 -0.0380 363 VAL A O   
5284 C CB  . VAL A 344 ? 0.3780 0.2606 0.1977 0.0673  -0.0530 -0.0410 363 VAL A CB  
5285 C CG1 . VAL A 344 ? 0.4179 0.2739 0.2067 0.0548  -0.0527 -0.0547 363 VAL A CG1 
5286 C CG2 . VAL A 344 ? 0.3998 0.2623 0.2048 0.0737  -0.0481 -0.0284 363 VAL A CG2 
5296 N N   . ARG A 345 ? 0.3292 0.2773 0.1951 0.0852  -0.0193 -0.0448 364 ARG A N   
5297 C CA  . ARG A 345 ? 0.3528 0.2914 0.1936 0.0745  -0.0238 -0.0423 364 ARG A CA  
5298 C C   . ARG A 345 ? 0.3759 0.2972 0.1942 0.0705  -0.0187 -0.0453 364 ARG A C   
5299 O O   . ARG A 345 ? 0.3907 0.3202 0.2145 0.0710  -0.0075 -0.0344 364 ARG A O   
5300 C CB  . ARG A 345 ? 0.3884 0.3136 0.2139 0.0675  -0.0044 -0.0250 364 ARG A CB  
5301 C CG  . ARG A 345 ? 0.4318 0.3337 0.2432 0.0657  0.0048  -0.0209 364 ARG A CG  
5302 C CD  . ARG A 345 ? 0.4745 0.3660 0.2747 0.0584  0.0260  -0.0172 364 ARG A CD  
5303 N NE  . ARG A 345 ? 0.5090 0.3963 0.2965 0.0521  0.0392  -0.0066 364 ARG A NE  
5304 C CZ  . ARG A 345 ? 0.5250 0.4186 0.3123 0.0575  0.0410  0.0016  364 ARG A CZ  
5305 N NH1 . ARG A 345 ? 0.4990 0.4214 0.3117 0.0741  0.0326  0.0030  364 ARG A NH1 
5306 N NH2 . ARG A 345 ? 0.5323 0.4306 0.3292 0.0458  0.0448  0.0064  364 ARG A NH2 
5320 N N   . ASP A 346 ? 0.3750 0.2999 0.1864 0.0722  -0.0360 -0.0361 365 ASP A N   
5321 C CA  . ASP A 346 ? 0.4135 0.3266 0.2094 0.0805  -0.0570 -0.0282 365 ASP A CA  
5322 C C   . ASP A 346 ? 0.4147 0.3205 0.2028 0.0797  -0.0500 -0.0161 365 ASP A C   
5323 O O   . ASP A 346 ? 0.4203 0.3185 0.1950 0.0875  -0.0408 -0.0158 365 ASP A O   
5324 C CB  . ASP A 346 ? 0.4639 0.3634 0.2364 0.0724  -0.0745 -0.0377 365 ASP A CB  
5325 C CG  . ASP A 346 ? 0.5214 0.4015 0.2707 0.0602  -0.0781 -0.0354 365 ASP A CG  
5326 O OD1 . ASP A 346 ? 0.5367 0.4167 0.2604 0.0642  -0.0742 -0.0461 365 ASP A OD1 
5327 O OD2 . ASP A 346 ? 0.5591 0.4222 0.3023 0.0487  -0.0807 -0.0309 365 ASP A OD2 
5332 N N   . GLY A 347 ? 0.4008 0.3143 0.1856 0.0819  -0.0288 -0.0110 366 GLY A N   
5333 C CA  . GLY A 347 ? 0.4075 0.3199 0.1866 0.0839  -0.0288 -0.0104 366 GLY A CA  
5334 C C   . GLY A 347 ? 0.4021 0.3228 0.1889 0.0789  -0.0301 -0.0038 366 GLY A C   
5335 O O   . GLY A 347 ? 0.4145 0.3282 0.2078 0.0732  -0.0286 0.0000  366 GLY A O   
5339 N N   . TRP A 348 ? 0.3660 0.3137 0.1806 0.0696  -0.0238 -0.0046 367 TRP A N   
5340 C CA  . TRP A 348 ? 0.3417 0.2976 0.1693 0.0681  -0.0387 -0.0038 367 TRP A CA  
5341 C C   . TRP A 348 ? 0.3097 0.2929 0.1683 0.0574  -0.0395 -0.0016 367 TRP A C   
5342 O O   . TRP A 348 ? 0.2738 0.2889 0.1630 0.0424  -0.0534 0.0114  367 TRP A O   
5343 C CB  . TRP A 348 ? 0.3688 0.2958 0.1770 0.0550  -0.0456 -0.0031 367 TRP A CB  
5344 C CG  . TRP A 348 ? 0.4036 0.2885 0.1696 0.0458  -0.0597 0.0062  367 TRP A CG  
5345 C CD1 . TRP A 348 ? 0.4367 0.2960 0.1772 0.0288  -0.0620 0.0019  367 TRP A CD1 
5346 C CD2 . TRP A 348 ? 0.4076 0.2882 0.1735 0.0568  -0.0559 -0.0033 367 TRP A CD2 
5347 N NE1 . TRP A 348 ? 0.4558 0.3007 0.1900 0.0372  -0.0564 -0.0052 367 TRP A NE1 
5348 C CE2 . TRP A 348 ? 0.4285 0.2887 0.1854 0.0455  -0.0584 0.0012  367 TRP A CE2 
5349 C CE3 . TRP A 348 ? 0.3872 0.2797 0.1774 0.0732  -0.0504 -0.0135 367 TRP A CE3 
5350 C CZ2 . TRP A 348 ? 0.4263 0.2999 0.1976 0.0428  -0.0395 0.0018  367 TRP A CZ2 
5351 C CZ3 . TRP A 348 ? 0.3938 0.2835 0.1792 0.0624  -0.0455 -0.0136 367 TRP A CZ3 
5352 C CH2 . TRP A 348 ? 0.4126 0.2866 0.1912 0.0499  -0.0319 -0.0046 367 TRP A CH2 
5363 N N   . LYS A 349 ? 0.3241 0.2953 0.1748 0.0557  -0.0359 0.0016  368 LYS A N   
5364 C CA  . LYS A 349 ? 0.3250 0.3090 0.1846 0.0550  -0.0646 -0.0064 368 LYS A CA  
5365 C C   . LYS A 349 ? 0.2866 0.2782 0.1788 0.0487  -0.0554 -0.0210 368 LYS A C   
5366 O O   . LYS A 349 ? 0.2901 0.3087 0.1854 0.0481  -0.0480 -0.0103 368 LYS A O   
5367 C CB  . LYS A 349 ? 0.3594 0.3531 0.2181 0.0546  -0.0840 -0.0103 368 LYS A CB  
5368 C CG  . LYS A 349 ? 0.4268 0.3974 0.2518 0.0455  -0.0902 -0.0239 368 LYS A CG  
5369 C CD  . LYS A 349 ? 0.5057 0.4334 0.2837 0.0379  -0.0714 -0.0350 368 LYS A CD  
5370 C CE  . LYS A 349 ? 0.5739 0.4631 0.3098 0.0288  -0.0448 -0.0343 368 LYS A CE  
5371 N NZ  . LYS A 349 ? 0.6028 0.4787 0.3275 0.0217  -0.0337 -0.0331 368 LYS A NZ  
5385 N N   . LEU A 350 ? 0.2683 0.2416 0.1672 0.0360  -0.0517 -0.0428 369 LEU A N   
5386 C CA  . LEU A 350 ? 0.2559 0.2256 0.1587 0.0246  -0.0441 -0.0422 369 LEU A CA  
5387 C C   . LEU A 350 ? 0.2687 0.2302 0.1828 0.0298  -0.0393 -0.0329 369 LEU A C   
5388 O O   . LEU A 350 ? 0.2517 0.2460 0.1968 0.0363  -0.0135 -0.0114 369 LEU A O   
5389 C CB  . LEU A 350 ? 0.2776 0.2280 0.1637 0.0237  -0.0439 -0.0344 369 LEU A CB  
5390 C CG  . LEU A 350 ? 0.3025 0.2291 0.1775 0.0224  -0.0293 -0.0402 369 LEU A CG  
5391 C CD1 . LEU A 350 ? 0.2991 0.2370 0.1872 0.0160  -0.0390 -0.0382 369 LEU A CD1 
5392 C CD2 . LEU A 350 ? 0.3329 0.2326 0.1922 0.0159  -0.0251 -0.0429 369 LEU A CD2 
5404 N N   . SER A 351 ? 0.2639 0.2150 0.1839 0.0313  -0.0425 -0.0087 370 SER A N   
5405 C CA  . SER A 351 ? 0.2768 0.2254 0.2001 0.0233  -0.0582 -0.0211 370 SER A CA  
5406 C C   . SER A 351 ? 0.2481 0.2087 0.1956 0.0335  -0.0479 -0.0316 370 SER A C   
5407 O O   . SER A 351 ? 0.2507 0.2080 0.1854 0.0250  -0.0379 -0.0287 370 SER A O   
5408 C CB  . SER A 351 ? 0.3184 0.2438 0.2199 0.0142  -0.0655 -0.0429 370 SER A CB  
5409 O OG  . SER A 351 ? 0.3673 0.2626 0.2415 0.0122  -0.0601 -0.0636 370 SER A OG  
5415 N N   . ARG A 352 ? 0.2277 0.1924 0.1849 0.0292  -0.0349 -0.0324 371 ARG A N   
5416 C CA  . ARG A 352 ? 0.2168 0.1863 0.1902 0.0368  -0.0465 -0.0343 371 ARG A CA  
5417 C C   . ARG A 352 ? 0.2103 0.1916 0.2051 0.0310  -0.0430 -0.0358 371 ARG A C   
5418 O O   . ARG A 352 ? 0.2058 0.2040 0.2310 0.0218  -0.0668 -0.0357 371 ARG A O   
5419 C CB  . ARG A 352 ? 0.2512 0.2021 0.1796 0.0180  -0.0565 -0.0372 371 ARG A CB  
5420 C CG  . ARG A 352 ? 0.2317 0.1839 0.1736 0.0215  -0.0348 -0.0365 371 ARG A CG  
5421 C CD  . ARG A 352 ? 0.2366 0.1903 0.1723 0.0275  -0.0108 -0.0401 371 ARG A CD  
5422 N NE  . ARG A 352 ? 0.2191 0.1861 0.1831 0.0318  -0.0276 -0.0389 371 ARG A NE  
5423 C CZ  . ARG A 352 ? 0.2108 0.1887 0.1786 0.0279  -0.0305 -0.0396 371 ARG A CZ  
5424 N NH1 . ARG A 352 ? 0.2016 0.1882 0.1808 0.0296  -0.0033 -0.0284 371 ARG A NH1 
5425 N NH2 . ARG A 352 ? 0.2103 0.2088 0.1940 0.0084  -0.0352 -0.0346 371 ARG A NH2 
5439 N N   . GLU A 353 ? 0.2376 0.1874 0.2042 0.0311  -0.0361 -0.0201 372 GLU A N   
5440 C CA  . GLU A 353 ? 0.2478 0.1843 0.2015 0.0223  -0.0391 -0.0397 372 GLU A CA  
5441 C C   . GLU A 353 ? 0.2528 0.1870 0.2009 0.0160  -0.0515 -0.0373 372 GLU A C   
5442 O O   . GLU A 353 ? 0.2574 0.1884 0.2011 0.0211  -0.0491 -0.0301 372 GLU A O   
5443 C CB  . GLU A 353 ? 0.2772 0.1887 0.2218 0.0251  -0.0507 -0.0450 372 GLU A CB  
5444 C CG  . GLU A 353 ? 0.3401 0.2423 0.2599 0.0264  -0.0497 -0.0446 372 GLU A CG  
5445 C CD  . GLU A 353 ? 0.3782 0.2868 0.2939 0.0266  -0.0575 -0.0506 372 GLU A CD  
5446 O OE1 . GLU A 353 ? 0.3597 0.2776 0.2959 -0.0099 -0.0587 -0.0569 372 GLU A OE1 
5447 O OE2 . GLU A 353 ? 0.4215 0.3331 0.3207 0.0470  -0.0654 -0.0501 372 GLU A OE2 
5454 N N   . TYR A 354 ? 0.2430 0.1804 0.1917 0.0245  -0.0440 -0.0328 373 TYR A N   
5455 C CA  . TYR A 354 ? 0.2544 0.1720 0.1946 0.0262  -0.0458 -0.0330 373 TYR A CA  
5456 C C   . TYR A 354 ? 0.2586 0.1683 0.2022 0.0265  -0.0501 -0.0294 373 TYR A C   
5457 O O   . TYR A 354 ? 0.2997 0.1731 0.2052 0.0089  -0.0550 -0.0225 373 TYR A O   
5458 C CB  . TYR A 354 ? 0.2541 0.1565 0.1877 0.0249  -0.0391 -0.0327 373 TYR A CB  
5459 C CG  . TYR A 354 ? 0.2333 0.1444 0.1722 0.0200  -0.0343 -0.0266 373 TYR A CG  
5460 C CD1 . TYR A 354 ? 0.2327 0.1579 0.1589 0.0213  -0.0539 -0.0312 373 TYR A CD1 
5461 C CD2 . TYR A 354 ? 0.2219 0.1406 0.1786 0.0196  -0.0159 -0.0333 373 TYR A CD2 
5462 C CE1 . TYR A 354 ? 0.2164 0.1635 0.1685 0.0288  -0.0236 -0.0189 373 TYR A CE1 
5463 C CE2 . TYR A 354 ? 0.2324 0.1448 0.1788 0.0234  -0.0179 -0.0086 373 TYR A CE2 
5464 C CZ  . TYR A 354 ? 0.1947 0.1543 0.1706 0.0263  -0.0332 -0.0150 373 TYR A CZ  
5465 O OH  . TYR A 354 ? 0.2077 0.1675 0.1693 0.0225  -0.0308 -0.0128 373 TYR A OH  
5475 N N   . LYS A 355 ? 0.2553 0.1676 0.2078 0.0264  -0.0568 -0.0214 374 LYS A N   
5476 C CA  . LYS A 355 ? 0.2671 0.1726 0.2304 0.0385  -0.0617 -0.0132 374 LYS A CA  
5477 C C   . LYS A 355 ? 0.2683 0.1559 0.2265 0.0151  -0.0670 -0.0153 374 LYS A C   
5478 O O   . LYS A 355 ? 0.2830 0.1691 0.2385 -0.0111 -0.0593 -0.0267 374 LYS A O   
5479 C CB  . LYS A 355 ? 0.3135 0.2256 0.2695 0.0462  -0.0604 -0.0052 374 LYS A CB  
5480 C CG  . LYS A 355 ? 0.3833 0.2760 0.3206 0.0397  -0.0554 0.0094  374 LYS A CG  
5481 C CD  . LYS A 355 ? 0.4361 0.3340 0.3634 0.0325  -0.0361 0.0256  374 LYS A CD  
5482 C CE  . LYS A 355 ? 0.4535 0.3748 0.3851 0.0449  -0.0322 0.0286  374 LYS A CE  
5483 N NZ  . LYS A 355 ? 0.4759 0.4027 0.4011 0.0551  -0.0305 0.0298  374 LYS A NZ  
5497 N N   . HIS A 356 ? 0.2478 0.1524 0.2299 0.0053  -0.0685 -0.0132 375 HIS A N   
5498 C CA  . HIS A 356 ? 0.2560 0.1755 0.2293 -0.0002 -0.0691 -0.0103 375 HIS A CA  
5499 C C   . HIS A 356 ? 0.2627 0.1672 0.2276 0.0117  -0.0551 -0.0282 375 HIS A C   
5500 O O   . HIS A 356 ? 0.2710 0.1990 0.2330 0.0101  -0.0591 -0.0198 375 HIS A O   
5501 C CB  . HIS A 356 ? 0.2547 0.1822 0.2388 0.0028  -0.0678 -0.0024 375 HIS A CB  
5502 C CG  . HIS A 356 ? 0.2821 0.1748 0.2487 0.0065  -0.0684 0.0068  375 HIS A CG  
5503 N ND1 . HIS A 356 ? 0.3247 0.2025 0.2725 0.0069  -0.0617 0.0307  375 HIS A ND1 
5504 C CD2 . HIS A 356 ? 0.2873 0.1913 0.2581 -0.0111 -0.0758 0.0061  375 HIS A CD2 
5505 C CE1 . HIS A 356 ? 0.3179 0.1955 0.2694 0.0000  -0.0859 0.0315  375 HIS A CE1 
5506 N NE2 . HIS A 356 ? 0.3239 0.2143 0.2638 -0.0028 -0.0805 0.0189  375 HIS A NE2 
5514 N N   . ALA A 357 ? 0.2540 0.1542 0.2146 0.0090  -0.0549 -0.0319 376 ALA A N   
5515 C CA  . ALA A 357 ? 0.2461 0.1623 0.2175 0.0146  -0.0465 -0.0184 376 ALA A CA  
5516 C C   . ALA A 357 ? 0.2395 0.1905 0.2373 0.0118  -0.0585 -0.0108 376 ALA A C   
5517 O O   . ALA A 357 ? 0.2373 0.2008 0.2450 0.0255  -0.0462 -0.0169 376 ALA A O   
5518 C CB  . ALA A 357 ? 0.2890 0.1856 0.2205 0.0122  -0.0524 -0.0237 376 ALA A CB  
5524 N N   . SER A 358 ? 0.2435 0.1961 0.2438 0.0103  -0.0626 0.0028  377 SER A N   
5525 C CA  . SER A 358 ? 0.2454 0.1955 0.2452 0.0068  -0.0602 -0.0145 377 SER A CA  
5526 C C   . SER A 358 ? 0.2175 0.2070 0.2477 0.0108  -0.0588 0.0032  377 SER A C   
5527 O O   . SER A 358 ? 0.2243 0.2257 0.2643 0.0087  -0.0318 0.0113  377 SER A O   
5528 C CB  . SER A 358 ? 0.2934 0.2024 0.2639 -0.0075 -0.0662 -0.0279 377 SER A CB  
5529 O OG  . SER A 358 ? 0.3389 0.2336 0.2783 0.0067  -0.0399 -0.0284 377 SER A OG  
5535 N N   . VAL A 359 ? 0.2036 0.1944 0.2282 0.0160  -0.0564 0.0024  378 VAL A N   
5536 C CA  . VAL A 359 ? 0.2231 0.1982 0.2266 0.0105  -0.0474 -0.0185 378 VAL A CA  
5537 C C   . VAL A 359 ? 0.2276 0.1995 0.2322 0.0075  -0.0577 -0.0148 378 VAL A C   
5538 O O   . VAL A 359 ? 0.2196 0.2068 0.2235 0.0103  -0.0589 0.0027  378 VAL A O   
5539 C CB  . VAL A 359 ? 0.2438 0.2169 0.2215 0.0108  -0.0478 -0.0192 378 VAL A CB  
5540 C CG1 . VAL A 359 ? 0.2425 0.2139 0.2302 0.0112  -0.0414 -0.0128 378 VAL A CG1 
5541 C CG2 . VAL A 359 ? 0.2769 0.2358 0.2246 0.0291  -0.0446 -0.0156 378 VAL A CG2 
5551 N N   . ARG A 360 ? 0.2399 0.2203 0.2510 0.0170  -0.0579 -0.0085 379 ARG A N   
5552 C CA  . ARG A 360 ? 0.2830 0.2254 0.2638 0.0437  -0.0907 -0.0164 379 ARG A CA  
5553 C C   . ARG A 360 ? 0.2588 0.2193 0.2406 0.0264  -0.0652 -0.0037 379 ARG A C   
5554 O O   . ARG A 360 ? 0.2365 0.2096 0.2489 0.0181  -0.0450 0.0089  379 ARG A O   
5555 C CB  . ARG A 360 ? 0.3886 0.2522 0.3167 0.0612  -0.1098 -0.0524 379 ARG A CB  
5556 C CG  . ARG A 360 ? 0.5172 0.3140 0.3790 0.0625  -0.1154 -0.0768 379 ARG A CG  
5557 C CD  . ARG A 360 ? 0.6170 0.3648 0.4264 0.0634  -0.1260 -0.0953 379 ARG A CD  
5558 N NE  . ARG A 360 ? 0.6972 0.3897 0.4601 0.0653  -0.1340 -0.1101 379 ARG A NE  
5559 C CZ  . ARG A 360 ? 0.7564 0.4025 0.4792 0.0612  -0.1314 -0.1317 379 ARG A CZ  
5560 N NH1 . ARG A 360 ? 0.7623 0.3900 0.4664 0.0444  -0.1499 -0.1569 379 ARG A NH1 
5561 N NH2 . ARG A 360 ? 0.7859 0.4201 0.4924 0.0567  -0.1224 -0.1393 379 ARG A NH2 
5575 N N   . VAL A 361 ? 0.2266 0.2213 0.2294 0.0063  -0.0609 -0.0201 380 VAL A N   
5576 C CA  . VAL A 361 ? 0.2315 0.2322 0.2292 0.0078  -0.0711 -0.0120 380 VAL A CA  
5577 C C   . VAL A 361 ? 0.2482 0.2412 0.2249 0.0159  -0.0702 0.0062  380 VAL A C   
5578 O O   . VAL A 361 ? 0.2803 0.2613 0.2188 0.0659  -0.0476 0.0091  380 VAL A O   
5579 C CB  . VAL A 361 ? 0.2871 0.2563 0.2637 0.0054  -0.0582 -0.0266 380 VAL A CB  
5580 C CG1 . VAL A 361 ? 0.2925 0.2762 0.2800 0.0166  -0.0478 -0.0296 380 VAL A CG1 
5581 C CG2 . VAL A 361 ? 0.3139 0.2551 0.2709 -0.0052 -0.0640 -0.0404 380 VAL A CG2 
5591 N N   . ASP A 362 ? 0.2430 0.2321 0.2134 0.0185  -0.0994 0.0060  381 ASP A N   
5592 C CA  . ASP A 362 ? 0.2677 0.2421 0.2061 0.0318  -0.0990 -0.0023 381 ASP A CA  
5593 C C   . ASP A 362 ? 0.2505 0.2445 0.1873 0.0468  -0.0855 0.0051  381 ASP A C   
5594 O O   . ASP A 362 ? 0.2456 0.2403 0.1892 0.0329  -0.0756 0.0012  381 ASP A O   
5595 C CB  . ASP A 362 ? 0.2934 0.2544 0.2230 0.0384  -0.1424 -0.0172 381 ASP A CB  
5596 C CG  . ASP A 362 ? 0.3542 0.2787 0.2501 0.0456  -0.1446 -0.0339 381 ASP A CG  
5597 O OD1 . ASP A 362 ? 0.3395 0.2717 0.2531 0.0602  -0.1345 -0.0248 381 ASP A OD1 
5598 O OD2 . ASP A 362 ? 0.4291 0.2978 0.2699 0.0683  -0.1503 -0.0479 381 ASP A OD2 
5603 N N   . LEU A 363 ? 0.2603 0.2403 0.1762 0.0397  -0.0562 0.0035  382 LEU A N   
5604 C CA  . LEU A 363 ? 0.2610 0.2620 0.1675 0.0446  -0.0482 0.0089  382 LEU A CA  
5605 C C   . LEU A 363 ? 0.2833 0.2832 0.1732 0.0595  -0.0503 0.0037  382 LEU A C   
5606 O O   . LEU A 363 ? 0.2854 0.2877 0.1681 0.0581  -0.0260 0.0011  382 LEU A O   
5607 C CB  . LEU A 363 ? 0.2788 0.2622 0.1538 0.0233  -0.0286 0.0159  382 LEU A CB  
5608 C CG  . LEU A 363 ? 0.2615 0.2697 0.1547 0.0077  -0.0228 0.0188  382 LEU A CG  
5609 C CD1 . LEU A 363 ? 0.2499 0.2787 0.1547 0.0048  0.0016  0.0097  382 LEU A CD1 
5610 C CD2 . LEU A 363 ? 0.2415 0.2771 0.1614 0.0042  -0.0271 0.0032  382 LEU A CD2 
5622 N N   . GLU A 364 ? 0.3024 0.2844 0.1679 0.0906  -0.0663 0.0060  383 GLU A N   
5623 C CA  . GLU A 364 ? 0.3514 0.3071 0.1836 0.0904  -0.0723 0.0064  383 GLU A CA  
5624 C C   . GLU A 364 ? 0.3310 0.2908 0.2042 0.0694  -0.0820 0.0113  383 GLU A C   
5625 O O   . GLU A 364 ? 0.3099 0.2797 0.2210 0.0745  -0.0716 -0.0005 383 GLU A O   
5626 C CB  . GLU A 364 ? 0.4185 0.3264 0.1670 0.1186  -0.0725 0.0200  383 GLU A CB  
5627 C CG  . GLU A 364 ? 0.4987 0.3639 0.1711 0.1343  -0.0584 0.0251  383 GLU A CG  
5628 C CD  . GLU A 364 ? 0.5773 0.3904 0.1814 0.1424  -0.0452 0.0317  383 GLU A CD  
5629 O OE1 . GLU A 364 ? 0.5534 0.3862 0.1767 0.1425  -0.0438 0.0316  383 GLU A OE1 
5630 O OE2 . GLU A 364 ? 0.6343 0.4120 0.2000 0.1516  -0.0436 0.0347  383 GLU A OE2 
5637 N N   . SER A 365 ? 0.3336 0.2853 0.2277 0.0527  -0.1114 0.0127  384 SER A N   
5638 C CA  . SER A 365 ? 0.3086 0.2718 0.2463 0.0323  -0.1278 0.0270  384 SER A CA  
5639 C C   . SER A 365 ? 0.2831 0.2775 0.2631 0.0298  -0.0901 0.0253  384 SER A C   
5640 O O   . SER A 365 ? 0.2792 0.2681 0.2655 0.0448  -0.0871 0.0162  384 SER A O   
5641 C CB  . SER A 365 ? 0.3206 0.2706 0.2640 0.0096  -0.1387 0.0204  384 SER A CB  
5642 O OG  . SER A 365 ? 0.3054 0.2530 0.2682 -0.0045 -0.1498 0.0215  384 SER A OG  
5648 N N   . LYS A 366 ? 0.2668 0.2953 0.2684 0.0214  -0.0908 0.0237  385 LYS A N   
5649 C CA  . LYS A 366 ? 0.2921 0.3367 0.2972 0.0265  -0.0677 0.0273  385 LYS A CA  
5650 C C   . LYS A 366 ? 0.2500 0.3546 0.3112 -0.0039 -0.0722 0.0104  385 LYS A C   
5651 O O   . LYS A 366 ? 0.2794 0.3631 0.3151 -0.0429 -0.0651 -0.0171 385 LYS A O   
5652 C CB  . LYS A 366 ? 0.3515 0.3763 0.3302 0.0431  -0.0317 0.0314  385 LYS A CB  
5653 C CG  . LYS A 366 ? 0.4217 0.4192 0.3584 0.0284  -0.0232 0.0356  385 LYS A CG  
5654 C CD  . LYS A 366 ? 0.4547 0.4439 0.3692 0.0281  -0.0445 0.0428  385 LYS A CD  
5655 C CE  . LYS A 366 ? 0.4835 0.4530 0.3695 0.0359  -0.0548 0.0473  385 LYS A CE  
5656 N NZ  . LYS A 366 ? 0.4862 0.4508 0.3613 0.0413  -0.0618 0.0407  385 LYS A NZ  
5670 N N   . GLU A 367 ? 0.2643 0.3471 0.3344 0.0168  -0.0576 0.0363  386 GLU A N   
5671 C CA  . GLU A 367 ? 0.3010 0.3512 0.3484 0.0143  -0.0681 0.0582  386 GLU A CA  
5672 C C   . GLU A 367 ? 0.2713 0.3092 0.3174 0.0069  -0.0602 0.0385  386 GLU A C   
5673 O O   . GLU A 367 ? 0.2600 0.3082 0.3197 0.0176  -0.0359 0.0499  386 GLU A O   
5674 C CB  . GLU A 367 ? 0.3555 0.3877 0.3861 0.0120  -0.1116 0.0846  386 GLU A CB  
5675 C CG  . GLU A 367 ? 0.4266 0.4368 0.4296 0.0054  -0.1251 0.0906  386 GLU A CG  
5676 C CD  . GLU A 367 ? 0.5027 0.4807 0.4728 -0.0213 -0.1256 0.0854  386 GLU A CD  
5677 O OE1 . GLU A 367 ? 0.5405 0.4939 0.4781 -0.0345 -0.1456 0.0824  386 GLU A OE1 
5678 O OE2 . GLU A 367 ? 0.5365 0.5015 0.5006 -0.0285 -0.1036 0.0847  386 GLU A OE2 
5685 N N   . ALA A 368 ? 0.2464 0.2749 0.2886 0.0064  -0.0717 0.0122  387 ALA A N   
5686 C CA  . ALA A 368 ? 0.2363 0.2583 0.2662 0.0027  -0.0901 -0.0023 387 ALA A CA  
5687 C C   . ALA A 368 ? 0.2579 0.2552 0.2636 0.0094  -0.0880 -0.0158 387 ALA A C   
5688 O O   . ALA A 368 ? 0.2693 0.2552 0.2664 0.0134  -0.0927 -0.0085 387 ALA A O   
5689 C CB  . ALA A 368 ? 0.2647 0.2522 0.2660 -0.0022 -0.0729 -0.0166 387 ALA A CB  
5695 N N   . GLU A 369 ? 0.2628 0.2595 0.2765 0.0115  -0.0784 -0.0106 388 GLU A N   
5696 C CA  . GLU A 369 ? 0.2851 0.2677 0.2957 0.0060  -0.0694 -0.0142 388 GLU A CA  
5697 C C   . GLU A 369 ? 0.2266 0.2477 0.2743 0.0062  -0.0646 -0.0098 388 GLU A C   
5698 O O   . GLU A 369 ? 0.2229 0.2464 0.2666 0.0123  -0.0353 0.0048  388 GLU A O   
5699 C CB  . GLU A 369 ? 0.3916 0.3054 0.3448 -0.0031 -0.0759 -0.0336 388 GLU A CB  
5700 C CG  . GLU A 369 ? 0.4819 0.3627 0.3864 -0.0091 -0.0871 -0.0548 388 GLU A CG  
5701 C CD  . GLU A 369 ? 0.5360 0.4117 0.4203 -0.0134 -0.1007 -0.0761 388 GLU A CD  
5702 O OE1 . GLU A 369 ? 0.5538 0.4261 0.4259 -0.0091 -0.1019 -0.0845 388 GLU A OE1 
5703 O OE2 . GLU A 369 ? 0.5579 0.4409 0.4390 -0.0124 -0.1025 -0.0835 388 GLU A OE2 
5710 N N   . ILE A 370 ? 0.2098 0.2402 0.2702 -0.0036 -0.0481 -0.0121 389 ILE A N   
5711 C CA  . ILE A 370 ? 0.2271 0.2281 0.2701 -0.0045 -0.0505 -0.0067 389 ILE A CA  
5712 C C   . ILE A 370 ? 0.2317 0.2434 0.2929 -0.0073 -0.0466 -0.0060 389 ILE A C   
5713 O O   . ILE A 370 ? 0.2654 0.2546 0.3089 -0.0172 -0.0514 -0.0009 389 ILE A O   
5714 C CB  . ILE A 370 ? 0.2565 0.2346 0.2590 -0.0267 -0.0490 0.0030  389 ILE A CB  
5715 C CG1 . ILE A 370 ? 0.2718 0.2386 0.2622 -0.0381 -0.0532 -0.0002 389 ILE A CG1 
5716 C CG2 . ILE A 370 ? 0.2795 0.2509 0.2548 -0.0370 -0.0451 0.0041  389 ILE A CG2 
5717 C CD1 . ILE A 370 ? 0.2729 0.2429 0.2695 -0.0396 -0.0440 -0.0001 389 ILE A CD1 
5729 N N   . ARG A 371 ? 0.2565 0.2480 0.2980 -0.0209 -0.0471 0.0022  390 ARG A N   
5730 C CA  . ARG A 371 ? 0.2749 0.2646 0.3148 -0.0388 -0.0683 0.0008  390 ARG A CA  
5731 C C   . ARG A 371 ? 0.2581 0.2456 0.2994 -0.0471 -0.0687 0.0022  390 ARG A C   
5732 O O   . ARG A 371 ? 0.3005 0.2708 0.2958 -0.0252 -0.0581 0.0249  390 ARG A O   
5733 C CB  . ARG A 371 ? 0.3433 0.3151 0.3472 -0.0481 -0.1033 0.0021  390 ARG A CB  
5734 C CG  . ARG A 371 ? 0.4546 0.3827 0.3958 -0.0462 -0.1169 -0.0018 390 ARG A CG  
5735 C CD  . ARG A 371 ? 0.5731 0.4437 0.4393 -0.0527 -0.1234 -0.0033 390 ARG A CD  
5736 N NE  . ARG A 371 ? 0.6851 0.4961 0.4802 -0.0580 -0.1106 0.0007  390 ARG A NE  
5737 C CZ  . ARG A 371 ? 0.7784 0.5355 0.5163 -0.0604 -0.1076 -0.0003 390 ARG A CZ  
5738 N NH1 . ARG A 371 ? 0.8169 0.5465 0.5323 -0.0605 -0.1031 -0.0009 390 ARG A NH1 
5739 N NH2 . ARG A 371 ? 0.8006 0.5477 0.5243 -0.0648 -0.1122 -0.0032 390 ARG A NH2 
5753 N N   . TRP A 372 ? 0.2284 0.2418 0.2889 -0.0289 -0.0663 -0.0119 391 TRP A N   
5754 C CA  . TRP A 372 ? 0.2395 0.2551 0.2854 -0.0291 -0.0580 -0.0177 391 TRP A CA  
5755 C C   . TRP A 372 ? 0.2546 0.2627 0.3102 -0.0595 -0.0659 -0.0130 391 TRP A C   
5756 O O   . TRP A 372 ? 0.2534 0.2668 0.3323 -0.0549 -0.0622 0.0001  391 TRP A O   
5757 C CB  . TRP A 372 ? 0.2225 0.2480 0.2627 -0.0076 -0.0626 -0.0216 391 TRP A CB  
5758 C CG  . TRP A 372 ? 0.2305 0.2417 0.2497 0.0087  -0.0543 -0.0252 391 TRP A CG  
5759 C CD1 . TRP A 372 ? 0.2345 0.2389 0.2596 0.0057  -0.0573 -0.0256 391 TRP A CD1 
5760 C CD2 . TRP A 372 ? 0.2169 0.2323 0.2270 0.0145  -0.0444 -0.0267 391 TRP A CD2 
5761 N NE1 . TRP A 372 ? 0.2436 0.2521 0.2618 0.0118  -0.0568 -0.0333 391 TRP A NE1 
5762 C CE2 . TRP A 372 ? 0.2175 0.2436 0.2345 0.0115  -0.0520 -0.0266 391 TRP A CE2 
5763 C CE3 . TRP A 372 ? 0.2060 0.2300 0.2117 0.0017  -0.0330 -0.0297 391 TRP A CE3 
5764 C CZ2 . TRP A 372 ? 0.2268 0.2298 0.2274 0.0075  -0.0436 -0.0336 391 TRP A CZ2 
5765 C CZ3 . TRP A 372 ? 0.2122 0.2296 0.2095 0.0019  -0.0385 -0.0298 391 TRP A CZ3 
5766 C CH2 . TRP A 372 ? 0.2375 0.2245 0.2178 0.0013  -0.0352 -0.0255 391 TRP A CH2 
5777 N N   . ARG A 373 ? 0.3001 0.2618 0.3276 -0.0786 -0.0824 -0.0193 392 ARG A N   
5778 C CA  . ARG A 373 ? 0.3530 0.2886 0.3536 -0.0832 -0.0854 -0.0217 392 ARG A CA  
5779 C C   . ARG A 373 ? 0.3619 0.2999 0.3513 -0.0841 -0.1032 -0.0258 392 ARG A C   
5780 O O   . ARG A 373 ? 0.3559 0.2817 0.3576 -0.0883 -0.0970 -0.0156 392 ARG A O   
5781 C CB  . ARG A 373 ? 0.4344 0.3141 0.3869 -0.0704 -0.0616 -0.0247 392 ARG A CB  
5782 C CG  . ARG A 373 ? 0.5310 0.3353 0.4139 -0.0480 -0.0395 -0.0166 392 ARG A CG  
5783 C CD  . ARG A 373 ? 0.6297 0.3523 0.4311 -0.0404 -0.0237 -0.0082 392 ARG A CD  
5784 N NE  . ARG A 373 ? 0.7104 0.3663 0.4540 -0.0335 -0.0131 -0.0052 392 ARG A NE  
5785 C CZ  . ARG A 373 ? 0.7697 0.3696 0.4723 -0.0348 -0.0055 0.0080  392 ARG A CZ  
5786 N NH1 . ARG A 373 ? 0.7753 0.3708 0.4831 -0.0351 0.0011  0.0159  392 ARG A NH1 
5787 N NH2 . ARG A 373 ? 0.8123 0.3734 0.4772 -0.0265 -0.0074 0.0076  392 ARG A NH2 
# 
